data_9BBO
# 
_entry.id   9BBO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BBO         pdb_00009bbo 10.2210/pdb9bbo/pdb 
WWPDB D_1000283042 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BBO 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
_audit_author.name               'Tanner, J.J.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Visualization of transient states and molecular motions in the catalytic cycle of the proline catabolic bifunctional enzyme Proline Utilization A from kinetic crystallography and molecular dynamics simulations
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Buckley, D.B.'  1 ? 
primary 'Gamage, T.'     2 ? 
primary 'Campbell, A.C.' 3 ? 
primary 'Becker, D.F.'   4 ? 
primary 'Tanner, J.J.'   5 ? 
# 
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 'Trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase' 
131961.656 2    ? ? ? ? 
2 non-polymer syn 'GAMMA-L-GLUTAMIC ACID'                                                                                      
147.129    2    ? ? ? ? 
3 non-polymer syn 'SULFATE ION'                                                                                                
96.063     9    ? ? ? ? 
4 non-polymer syn 'TRIETHYLENE GLYCOL'                                                                                         
150.173    2    ? ? ? ? 
5 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                                                                                
785.550    2    ? ? ? ? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                                      
106.120    1    ? ? ? ? 
7 water       nat water                                                                                                        
18.015     1982 ? ? ? ? 
# 
_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       
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'GAMMA-L-GLUTAMIC ACID'       GGL 
3 'SULFATE ION'                 SO4 
4 'TRIETHYLENE GLYCOL'          PGE 
5 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
6 'DI(HYDROXYETHYL)ETHER'       PEG 
7 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    SER n 
1 2    MET n 
1 3    MET n 
1 4    SER n 
1 5    PRO n 
1 6    ASN n 
1 7    PRO n 
1 8    LEU n 
1 9    GLN n 
1 10   LYS n 
1 11   PRO n 
1 12   ALA n 
1 13   ILE n 
1 14   ASP n 
1 15   ALA n 
1 16   ALA n 
1 17   PRO n 
1 18   ALA n 
1 19   PRO n 
1 20   PHE n 
1 21   ALA n 
1 22   ASP n 
1 23   PHE n 
1 24   ALA n 
1 25   PRO n 
1 26   PRO n 
1 27   VAL n 
1 28   ARG n 
1 29   PRO n 
1 30   GLN n 
1 31   SER n 
1 32   THR n 
1 33   LEU n 
1 34   ARG n 
1 35   ARG n 
1 36   ALA n 
1 37   ILE n 
1 38   THR n 
1 39   ALA n 
1 40   ALA n 
1 41   TYR n 
1 42   ARG n 
1 43   ARG n 
1 44   PRO n 
1 45   GLU n 
1 46   THR n 
1 47   GLU n 
1 48   CYS n 
1 49   LEU n 
1 50   PRO n 
1 51   PRO n 
1 52   LEU n 
1 53   VAL n 
1 54   GLU n 
1 55   ALA n 
1 56   ALA n 
1 57   THR n 
1 58   GLN n 
1 59   SER n 
1 60   LYS n 
1 61   GLU n 
1 62   ILE n 
1 63   ARG n 
1 64   ASP n 
1 65   ALA n 
1 66   ALA n 
1 67   ALA n 
1 68   SER n 
1 69   THR n 
1 70   ALA n 
1 71   ARG n 
1 72   LYS n 
1 73   LEU n 
1 74   ILE n 
1 75   GLU n 
1 76   ALA n 
1 77   LEU n 
1 78   ARG n 
1 79   GLY n 
1 80   LYS n 
1 81   HIS n 
1 82   SER n 
1 83   GLY n 
1 84   SER n 
1 85   GLY n 
1 86   VAL n 
1 87   GLU n 
1 88   GLY n 
1 89   LEU n 
1 90   VAL n 
1 91   GLN n 
1 92   GLU n 
1 93   TYR n 
1 94   SER n 
1 95   LEU n 
1 96   SER n 
1 97   SER n 
1 98   GLN n 
1 99   GLU n 
1 100  GLY n 
1 101  VAL n 
1 102  ALA n 
1 103  LEU n 
1 104  MET n 
1 105  CYS n 
1 106  LEU n 
1 107  ALA n 
1 108  GLU n 
1 109  ALA n 
1 110  LEU n 
1 111  LEU n 
1 112  ARG n 
1 113  ILE n 
1 114  PRO n 
1 115  ASP n 
1 116  THR n 
1 117  ALA n 
1 118  THR n 
1 119  ARG n 
1 120  ASP n 
1 121  ALA n 
1 122  LEU n 
1 123  ILE n 
1 124  ARG n 
1 125  ASP n 
1 126  LYS n 
1 127  ILE n 
1 128  ALA n 
1 129  ASP n 
1 130  GLY n 
1 131  ASN n 
1 132  TRP n 
1 133  LYS n 
1 134  SER n 
1 135  HIS n 
1 136  LEU n 
1 137  GLY n 
1 138  GLY n 
1 139  SER n 
1 140  ARG n 
1 141  SER n 
1 142  LEU n 
1 143  PHE n 
1 144  VAL n 
1 145  ASN n 
1 146  ALA n 
1 147  ALA n 
1 148  THR n 
1 149  TRP n 
1 150  GLY n 
1 151  LEU n 
1 152  VAL n 
1 153  VAL n 
1 154  THR n 
1 155  GLY n 
1 156  LYS n 
1 157  LEU n 
1 158  THR n 
1 159  SER n 
1 160  THR n 
1 161  VAL n 
1 162  ASN n 
1 163  ASP n 
1 164  ARG n 
1 165  SER n 
1 166  LEU n 
1 167  ALA n 
1 168  ALA n 
1 169  ALA n 
1 170  LEU n 
1 171  THR n 
1 172  ARG n 
1 173  LEU n 
1 174  ILE n 
1 175  SER n 
1 176  ARG n 
1 177  CYS n 
1 178  GLY n 
1 179  GLU n 
1 180  PRO n 
1 181  VAL n 
1 182  ILE n 
1 183  ARG n 
1 184  ARG n 
1 185  GLY n 
1 186  VAL n 
1 187  ASP n 
1 188  MET n 
1 189  ALA n 
1 190  MET n 
1 191  ARG n 
1 192  MET n 
1 193  MET n 
1 194  GLY n 
1 195  GLU n 
1 196  GLN n 
1 197  PHE n 
1 198  VAL n 
1 199  THR n 
1 200  GLY n 
1 201  GLU n 
1 202  THR n 
1 203  ILE n 
1 204  ARG n 
1 205  GLU n 
1 206  ALA n 
1 207  LEU n 
1 208  LYS n 
1 209  ARG n 
1 210  SER n 
1 211  LYS n 
1 212  GLU n 
1 213  LEU n 
1 214  GLU n 
1 215  GLU n 
1 216  LYS n 
1 217  GLY n 
1 218  PHE n 
1 219  SER n 
1 220  TYR n 
1 221  SER n 
1 222  TYR n 
1 223  ASP n 
1 224  MET n 
1 225  LEU n 
1 226  GLY n 
1 227  GLU n 
1 228  ALA n 
1 229  ALA n 
1 230  THR n 
1 231  THR n 
1 232  ALA n 
1 233  ALA n 
1 234  ASP n 
1 235  ALA n 
1 236  GLU n 
1 237  ARG n 
1 238  TYR n 
1 239  TYR n 
1 240  ARG n 
1 241  ASP n 
1 242  TYR n 
1 243  GLU n 
1 244  SER n 
1 245  ALA n 
1 246  ILE n 
1 247  HIS n 
1 248  ALA n 
1 249  ILE n 
1 250  GLY n 
1 251  LYS n 
1 252  ALA n 
1 253  SER n 
1 254  ALA n 
1 255  GLY n 
1 256  ARG n 
1 257  GLY n 
1 258  ILE n 
1 259  TYR n 
1 260  GLU n 
1 261  GLY n 
1 262  PRO n 
1 263  GLY n 
1 264  ILE n 
1 265  SER n 
1 266  ILE n 
1 267  LYS n 
1 268  LEU n 
1 269  SER n 
1 270  ALA n 
1 271  LEU n 
1 272  HIS n 
1 273  PRO n 
1 274  ARG n 
1 275  TYR n 
1 276  SER n 
1 277  ARG n 
1 278  ALA n 
1 279  GLN n 
1 280  ALA n 
1 281  ALA n 
1 282  ARG n 
1 283  VAL n 
1 284  MET n 
1 285  GLY n 
1 286  GLU n 
1 287  LEU n 
1 288  LEU n 
1 289  PRO n 
1 290  ARG n 
1 291  VAL n 
1 292  LYS n 
1 293  ALA n 
1 294  LEU n 
1 295  ALA n 
1 296  LEU n 
1 297  LEU n 
1 298  ALA n 
1 299  LYS n 
1 300  ASN n 
1 301  TYR n 
1 302  ASP n 
1 303  ILE n 
1 304  GLY n 
1 305  LEU n 
1 306  ASN n 
1 307  ILE n 
1 308  ASP n 
1 309  ALA n 
1 310  GLU n 
1 311  GLU n 
1 312  ALA n 
1 313  ASP n 
1 314  ARG n 
1 315  LEU n 
1 316  GLU n 
1 317  LEU n 
1 318  SER n 
1 319  LEU n 
1 320  ASP n 
1 321  LEU n 
1 322  LEU n 
1 323  GLU n 
1 324  VAL n 
1 325  LEU n 
1 326  CYS n 
1 327  LEU n 
1 328  ASP n 
1 329  GLY n 
1 330  ASP n 
1 331  LEU n 
1 332  SER n 
1 333  GLY n 
1 334  TRP n 
1 335  ASN n 
1 336  GLY n 
1 337  MET n 
1 338  GLY n 
1 339  PHE n 
1 340  VAL n 
1 341  VAL n 
1 342  GLN n 
1 343  ALA n 
1 344  TYR n 
1 345  GLY n 
1 346  LYS n 
1 347  ARG n 
1 348  CYS n 
1 349  PRO n 
1 350  PHE n 
1 351  VAL n 
1 352  LEU n 
1 353  ASP n 
1 354  PHE n 
1 355  ILE n 
1 356  ILE n 
1 357  ASP n 
1 358  LEU n 
1 359  ALA n 
1 360  ARG n 
1 361  ARG n 
1 362  SER n 
1 363  GLY n 
1 364  ARG n 
1 365  ARG n 
1 366  ILE n 
1 367  MET n 
1 368  VAL n 
1 369  ARG n 
1 370  LEU n 
1 371  VAL n 
1 372  LYS n 
1 373  GLY n 
1 374  ALA n 
1 375  TYR n 
1 376  TRP n 
1 377  ASP n 
1 378  ALA n 
1 379  GLU n 
1 380  ILE n 
1 381  LYS n 
1 382  ARG n 
1 383  ALA n 
1 384  GLN n 
1 385  LEU n 
1 386  ASP n 
1 387  GLY n 
1 388  LEU n 
1 389  ALA n 
1 390  ASP n 
1 391  PHE n 
1 392  PRO n 
1 393  VAL n 
1 394  PHE n 
1 395  THR n 
1 396  ARG n 
1 397  LYS n 
1 398  ILE n 
1 399  HIS n 
1 400  THR n 
1 401  ASP n 
1 402  VAL n 
1 403  SER n 
1 404  TYR n 
1 405  ILE n 
1 406  ALA n 
1 407  CYS n 
1 408  ALA n 
1 409  ALA n 
1 410  LYS n 
1 411  LEU n 
1 412  LEU n 
1 413  ALA n 
1 414  ALA n 
1 415  THR n 
1 416  ASP n 
1 417  VAL n 
1 418  VAL n 
1 419  PHE n 
1 420  PRO n 
1 421  GLN n 
1 422  PHE n 
1 423  ALA n 
1 424  THR n 
1 425  HIS n 
1 426  ASN n 
1 427  ALA n 
1 428  GLN n 
1 429  THR n 
1 430  LEU n 
1 431  ALA n 
1 432  ALA n 
1 433  ILE n 
1 434  TYR n 
1 435  HIS n 
1 436  MET n 
1 437  ALA n 
1 438  GLY n 
1 439  LYS n 
1 440  ASP n 
1 441  PHE n 
1 442  HIS n 
1 443  VAL n 
1 444  GLY n 
1 445  LYS n 
1 446  TYR n 
1 447  GLU n 
1 448  PHE n 
1 449  GLN n 
1 450  CYS n 
1 451  LEU n 
1 452  HIS n 
1 453  GLY n 
1 454  MET n 
1 455  GLY n 
1 456  GLU n 
1 457  PRO n 
1 458  LEU n 
1 459  TYR n 
1 460  GLU n 
1 461  GLU n 
1 462  VAL n 
1 463  VAL n 
1 464  GLY n 
1 465  ARG n 
1 466  GLY n 
1 467  LYS n 
1 468  LEU n 
1 469  ASP n 
1 470  ARG n 
1 471  PRO n 
1 472  CYS n 
1 473  ARG n 
1 474  ILE n 
1 475  TYR n 
1 476  ALA n 
1 477  PRO n 
1 478  VAL n 
1 479  GLY n 
1 480  THR n 
1 481  HIS n 
1 482  GLU n 
1 483  THR n 
1 484  LEU n 
1 485  LEU n 
1 486  ALA n 
1 487  TYR n 
1 488  LEU n 
1 489  VAL n 
1 490  ARG n 
1 491  ARG n 
1 492  LEU n 
1 493  LEU n 
1 494  GLU n 
1 495  ASN n 
1 496  GLY n 
1 497  ALA n 
1 498  ASN n 
1 499  SER n 
1 500  SER n 
1 501  PHE n 
1 502  VAL n 
1 503  HIS n 
1 504  ARG n 
1 505  ILE n 
1 506  ASN n 
1 507  ASP n 
1 508  PRO n 
1 509  LYS n 
1 510  VAL n 
1 511  SER n 
1 512  ILE n 
1 513  ASP n 
1 514  GLU n 
1 515  LEU n 
1 516  ILE n 
1 517  ALA n 
1 518  ASP n 
1 519  PRO n 
1 520  VAL n 
1 521  GLU n 
1 522  VAL n 
1 523  VAL n 
1 524  ARG n 
1 525  ALA n 
1 526  MET n 
1 527  PRO n 
1 528  VAL n 
1 529  VAL n 
1 530  GLY n 
1 531  ALA n 
1 532  LYS n 
1 533  HIS n 
1 534  ASP n 
1 535  ARG n 
1 536  ILE n 
1 537  ALA n 
1 538  LEU n 
1 539  PRO n 
1 540  ALA n 
1 541  GLU n 
1 542  LEU n 
1 543  PHE n 
1 544  GLY n 
1 545  ASP n 
1 546  ALA n 
1 547  ARG n 
1 548  THR n 
1 549  ASN n 
1 550  SER n 
1 551  ALA n 
1 552  GLY n 
1 553  LEU n 
1 554  ASP n 
1 555  LEU n 
1 556  SER n 
1 557  ASN n 
1 558  GLU n 
1 559  GLU n 
1 560  THR n 
1 561  LEU n 
1 562  ALA n 
1 563  SER n 
1 564  LEU n 
1 565  THR n 
1 566  GLU n 
1 567  ALA n 
1 568  LEU n 
1 569  ARG n 
1 570  GLU n 
1 571  SER n 
1 572  ALA n 
1 573  ALA n 
1 574  MET n 
1 575  LYS n 
1 576  TRP n 
1 577  THR n 
1 578  ALA n 
1 579  LEU n 
1 580  PRO n 
1 581  GLN n 
1 582  LEU n 
1 583  ALA n 
1 584  THR n 
1 585  GLY n 
1 586  PRO n 
1 587  ALA n 
1 588  ALA n 
1 589  GLY n 
1 590  GLU n 
1 591  THR n 
1 592  ARG n 
1 593  THR n 
1 594  VAL n 
1 595  LEU n 
1 596  ASN n 
1 597  PRO n 
1 598  GLY n 
1 599  ASP n 
1 600  HIS n 
1 601  ARG n 
1 602  ASP n 
1 603  VAL n 
1 604  VAL n 
1 605  GLY n 
1 606  SER n 
1 607  VAL n 
1 608  THR n 
1 609  GLU n 
1 610  THR n 
1 611  SER n 
1 612  GLU n 
1 613  GLU n 
1 614  ASP n 
1 615  ALA n 
1 616  ARG n 
1 617  ARG n 
1 618  ALA n 
1 619  VAL n 
1 620  ARG n 
1 621  LEU n 
1 622  ALA n 
1 623  ALA n 
1 624  ASP n 
1 625  ALA n 
1 626  ALA n 
1 627  PRO n 
1 628  ASP n 
1 629  TRP n 
1 630  ALA n 
1 631  ALA n 
1 632  VAL n 
1 633  PRO n 
1 634  PRO n 
1 635  SER n 
1 636  GLU n 
1 637  ARG n 
1 638  ALA n 
1 639  ALA n 
1 640  CYS n 
1 641  LEU n 
1 642  ASP n 
1 643  ARG n 
1 644  ALA n 
1 645  ALA n 
1 646  GLU n 
1 647  LEU n 
1 648  MET n 
1 649  GLN n 
1 650  ALA n 
1 651  ARG n 
1 652  MET n 
1 653  PRO n 
1 654  THR n 
1 655  LEU n 
1 656  LEU n 
1 657  GLY n 
1 658  LEU n 
1 659  ILE n 
1 660  ILE n 
1 661  ARG n 
1 662  GLU n 
1 663  ALA n 
1 664  GLY n 
1 665  LYS n 
1 666  SER n 
1 667  ALA n 
1 668  LEU n 
1 669  ASN n 
1 670  ALA n 
1 671  ILE n 
1 672  ALA n 
1 673  GLU n 
1 674  VAL n 
1 675  ARG n 
1 676  GLU n 
1 677  ALA n 
1 678  ILE n 
1 679  ASP n 
1 680  PHE n 
1 681  LEU n 
1 682  ARG n 
1 683  TYR n 
1 684  TYR n 
1 685  ALA n 
1 686  GLU n 
1 687  GLN n 
1 688  THR n 
1 689  ARG n 
1 690  ARG n 
1 691  THR n 
1 692  LEU n 
1 693  GLY n 
1 694  PRO n 
1 695  GLY n 
1 696  HIS n 
1 697  GLY n 
1 698  PRO n 
1 699  LEU n 
1 700  GLY n 
1 701  PRO n 
1 702  ILE n 
1 703  VAL n 
1 704  CYS n 
1 705  ILE n 
1 706  SER n 
1 707  PRO n 
1 708  TRP n 
1 709  ASN n 
1 710  PHE n 
1 711  PRO n 
1 712  LEU n 
1 713  ALA n 
1 714  ILE n 
1 715  PHE n 
1 716  THR n 
1 717  GLY n 
1 718  GLN n 
1 719  ILE n 
1 720  ALA n 
1 721  ALA n 
1 722  ALA n 
1 723  LEU n 
1 724  VAL n 
1 725  ALA n 
1 726  GLY n 
1 727  ASN n 
1 728  PRO n 
1 729  VAL n 
1 730  LEU n 
1 731  ALA n 
1 732  LYS n 
1 733  PRO n 
1 734  ALA n 
1 735  GLU n 
1 736  GLU n 
1 737  THR n 
1 738  PRO n 
1 739  LEU n 
1 740  ILE n 
1 741  ALA n 
1 742  ALA n 
1 743  GLU n 
1 744  GLY n 
1 745  VAL n 
1 746  ARG n 
1 747  ILE n 
1 748  LEU n 
1 749  ARG n 
1 750  GLU n 
1 751  ALA n 
1 752  GLY n 
1 753  ILE n 
1 754  PRO n 
1 755  ALA n 
1 756  SER n 
1 757  ALA n 
1 758  LEU n 
1 759  GLN n 
1 760  LEU n 
1 761  LEU n 
1 762  PRO n 
1 763  GLY n 
1 764  ASP n 
1 765  GLY n 
1 766  ARG n 
1 767  VAL n 
1 768  GLY n 
1 769  ALA n 
1 770  ALA n 
1 771  LEU n 
1 772  VAL n 
1 773  ALA n 
1 774  ALA n 
1 775  ALA n 
1 776  GLU n 
1 777  THR n 
1 778  ALA n 
1 779  GLY n 
1 780  VAL n 
1 781  MET n 
1 782  PHE n 
1 783  THR n 
1 784  GLY n 
1 785  SER n 
1 786  THR n 
1 787  GLU n 
1 788  VAL n 
1 789  ALA n 
1 790  ARG n 
1 791  LEU n 
1 792  ILE n 
1 793  GLN n 
1 794  ALA n 
1 795  GLN n 
1 796  LEU n 
1 797  ALA n 
1 798  ASP n 
1 799  ARG n 
1 800  LEU n 
1 801  SER n 
1 802  PRO n 
1 803  ALA n 
1 804  GLY n 
1 805  ARG n 
1 806  PRO n 
1 807  ILE n 
1 808  PRO n 
1 809  LEU n 
1 810  ILE n 
1 811  ALA n 
1 812  GLU n 
1 813  THR n 
1 814  GLY n 
1 815  GLY n 
1 816  GLN n 
1 817  ASN n 
1 818  ALA n 
1 819  MET n 
1 820  ILE n 
1 821  VAL n 
1 822  ASP n 
1 823  SER n 
1 824  SER n 
1 825  ALA n 
1 826  LEU n 
1 827  ALA n 
1 828  GLU n 
1 829  GLN n 
1 830  VAL n 
1 831  VAL n 
1 832  GLY n 
1 833  ASP n 
1 834  VAL n 
1 835  ILE n 
1 836  THR n 
1 837  SER n 
1 838  ALA n 
1 839  PHE n 
1 840  ASP n 
1 841  SER n 
1 842  ALA n 
1 843  GLY n 
1 844  GLN n 
1 845  ARG n 
1 846  CYS n 
1 847  SER n 
1 848  ALA n 
1 849  LEU n 
1 850  ARG n 
1 851  VAL n 
1 852  LEU n 
1 853  CYS n 
1 854  LEU n 
1 855  GLN n 
1 856  GLU n 
1 857  ASP n 
1 858  VAL n 
1 859  ALA n 
1 860  ASP n 
1 861  ARG n 
1 862  ILE n 
1 863  LEU n 
1 864  THR n 
1 865  MET n 
1 866  LEU n 
1 867  LYS n 
1 868  GLY n 
1 869  ALA n 
1 870  LEU n 
1 871  HIS n 
1 872  GLU n 
1 873  LEU n 
1 874  HIS n 
1 875  ILE n 
1 876  GLY n 
1 877  ARG n 
1 878  THR n 
1 879  ASP n 
1 880  ARG n 
1 881  LEU n 
1 882  SER n 
1 883  VAL n 
1 884  ASP n 
1 885  VAL n 
1 886  GLY n 
1 887  PRO n 
1 888  VAL n 
1 889  ILE n 
1 890  THR n 
1 891  SER n 
1 892  GLU n 
1 893  ALA n 
1 894  LYS n 
1 895  ASP n 
1 896  ASN n 
1 897  ILE n 
1 898  GLU n 
1 899  LYS n 
1 900  HIS n 
1 901  ILE n 
1 902  GLU n 
1 903  ARG n 
1 904  MET n 
1 905  ARG n 
1 906  GLY n 
1 907  LEU n 
1 908  GLY n 
1 909  ARG n 
1 910  LYS n 
1 911  VAL n 
1 912  GLU n 
1 913  GLN n 
1 914  ILE n 
1 915  GLY n 
1 916  LEU n 
1 917  ALA n 
1 918  SER n 
1 919  GLU n 
1 920  THR n 
1 921  GLY n 
1 922  VAL n 
1 923  GLY n 
1 924  THR n 
1 925  PHE n 
1 926  VAL n 
1 927  PRO n 
1 928  PRO n 
1 929  THR n 
1 930  ILE n 
1 931  ILE n 
1 932  GLU n 
1 933  LEU n 
1 934  GLU n 
1 935  LYS n 
1 936  LEU n 
1 937  SER n 
1 938  ASP n 
1 939  LEU n 
1 940  GLN n 
1 941  ARG n 
1 942  GLU n 
1 943  VAL n 
1 944  PHE n 
1 945  GLY n 
1 946  PRO n 
1 947  VAL n 
1 948  LEU n 
1 949  HIS n 
1 950  VAL n 
1 951  ILE n 
1 952  ARG n 
1 953  TYR n 
1 954  ARG n 
1 955  ARG n 
1 956  ASP n 
1 957  ASP n 
1 958  LEU n 
1 959  ASP n 
1 960  ARG n 
1 961  LEU n 
1 962  VAL n 
1 963  ASP n 
1 964  ASP n 
1 965  VAL n 
1 966  ASN n 
1 967  ALA n 
1 968  THR n 
1 969  GLY n 
1 970  TYR n 
1 971  GLY n 
1 972  LEU n 
1 973  THR n 
1 974  PHE n 
1 975  GLY n 
1 976  LEU n 
1 977  HIS n 
1 978  THR n 
1 979  ARG n 
1 980  LEU n 
1 981  ASP n 
1 982  GLU n 
1 983  THR n 
1 984  ILE n 
1 985  ALA n 
1 986  HIS n 
1 987  VAL n 
1 988  THR n 
1 989  SER n 
1 990  ARG n 
1 991  ILE n 
1 992  LYS n 
1 993  ALA n 
1 994  GLY n 
1 995  ASN n 
1 996  LEU n 
1 997  TYR n 
1 998  ILE n 
1 999  ASN n 
1 1000 ARG n 
1 1001 ASN n 
1 1002 ILE n 
1 1003 ILE n 
1 1004 GLY n 
1 1005 ALA n 
1 1006 VAL n 
1 1007 VAL n 
1 1008 GLY n 
1 1009 VAL n 
1 1010 GLN n 
1 1011 PRO n 
1 1012 PHE n 
1 1013 GLY n 
1 1014 GLY n 
1 1015 ARG n 
1 1016 GLY n 
1 1017 LEU n 
1 1018 SER n 
1 1019 GLY n 
1 1020 THR n 
1 1021 GLY n 
1 1022 PRO n 
1 1023 LYS n 
1 1024 ALA n 
1 1025 GLY n 
1 1026 GLY n 
1 1027 PRO n 
1 1028 LEU n 
1 1029 TYR n 
1 1030 LEU n 
1 1031 GLY n 
1 1032 ARG n 
1 1033 LEU n 
1 1034 VAL n 
1 1035 THR n 
1 1036 THR n 
1 1037 ALA n 
1 1038 PRO n 
1 1039 VAL n 
1 1040 PRO n 
1 1041 PRO n 
1 1042 GLN n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
1 1046 VAL n 
1 1047 HIS n 
1 1048 THR n 
1 1049 ASP n 
1 1050 PRO n 
1 1051 VAL n 
1 1052 LEU n 
1 1053 LEU n 
1 1054 ASP n 
1 1055 PHE n 
1 1056 ALA n 
1 1057 LYS n 
1 1058 TRP n 
1 1059 LEU n 
1 1060 ASP n 
1 1061 GLY n 
1 1062 LYS n 
1 1063 GLY n 
1 1064 ALA n 
1 1065 ARG n 
1 1066 ALA n 
1 1067 GLU n 
1 1068 ALA n 
1 1069 GLU n 
1 1070 ALA n 
1 1071 ALA n 
1 1072 ARG n 
1 1073 ASN n 
1 1074 ALA n 
1 1075 GLY n 
1 1076 SER n 
1 1077 SER n 
1 1078 SER n 
1 1079 ALA n 
1 1080 LEU n 
1 1081 GLY n 
1 1082 LEU n 
1 1083 ASP n 
1 1084 LEU n 
1 1085 GLU n 
1 1086 LEU n 
1 1087 PRO n 
1 1088 GLY n 
1 1089 PRO n 
1 1090 VAL n 
1 1091 GLY n 
1 1092 GLU n 
1 1093 ARG n 
1 1094 ASN n 
1 1095 LEU n 
1 1096 TYR n 
1 1097 THR n 
1 1098 LEU n 
1 1099 HIS n 
1 1100 ALA n 
1 1101 ARG n 
1 1102 GLY n 
1 1103 ARG n 
1 1104 ILE n 
1 1105 LEU n 
1 1106 LEU n 
1 1107 VAL n 
1 1108 PRO n 
1 1109 ALA n 
1 1110 THR n 
1 1111 GLU n 
1 1112 SER n 
1 1113 GLY n 
1 1114 LEU n 
1 1115 TYR n 
1 1116 HIS n 
1 1117 GLN n 
1 1118 LEU n 
1 1119 ALA n 
1 1120 ALA n 
1 1121 ALA n 
1 1122 LEU n 
1 1123 ALA n 
1 1124 THR n 
1 1125 GLY n 
1 1126 ASN n 
1 1127 SER n 
1 1128 VAL n 
1 1129 ALA n 
1 1130 ILE n 
1 1131 ASP n 
1 1132 ALA n 
1 1133 ALA n 
1 1134 SER n 
1 1135 GLY n 
1 1136 LEU n 
1 1137 GLN n 
1 1138 ALA n 
1 1139 SER n 
1 1140 LEU n 
1 1141 LYS n 
1 1142 ASN n 
1 1143 LEU n 
1 1144 PRO n 
1 1145 GLN n 
1 1146 THR n 
1 1147 VAL n 
1 1148 GLY n 
1 1149 LEU n 
1 1150 ARG n 
1 1151 VAL n 
1 1152 SER n 
1 1153 TRP n 
1 1154 SER n 
1 1155 LYS n 
1 1156 ASP n 
1 1157 TRP n 
1 1158 ALA n 
1 1159 ALA n 
1 1160 ASP n 
1 1161 GLY n 
1 1162 PRO n 
1 1163 PHE n 
1 1164 ALA n 
1 1165 GLY n 
1 1166 ALA n 
1 1167 LEU n 
1 1168 VAL n 
1 1169 GLU n 
1 1170 GLY n 
1 1171 ASP n 
1 1172 ALA n 
1 1173 GLU n 
1 1174 ARG n 
1 1175 ILE n 
1 1176 ARG n 
1 1177 ALA n 
1 1178 VAL n 
1 1179 ASN n 
1 1180 LYS n 
1 1181 ALA n 
1 1182 ILE n 
1 1183 ALA n 
1 1184 ALA n 
1 1185 LEU n 
1 1186 PRO n 
1 1187 GLY n 
1 1188 PRO n 
1 1189 LEU n 
1 1190 LEU n 
1 1191 LEU n 
1 1192 VAL n 
1 1193 GLN n 
1 1194 ALA n 
1 1195 ALA n 
1 1196 SER n 
1 1197 SER n 
1 1198 GLY n 
1 1199 GLU n 
1 1200 ILE n 
1 1201 ALA n 
1 1202 ARG n 
1 1203 ASN n 
1 1204 PRO n 
1 1205 ASP n 
1 1206 ALA n 
1 1207 TYR n 
1 1208 CYS n 
1 1209 LEU n 
1 1210 ASN n 
1 1211 TRP n 
1 1212 LEU n 
1 1213 VAL n 
1 1214 GLU n 
1 1215 GLU n 
1 1216 VAL n 
1 1217 SER n 
1 1218 ALA n 
1 1219 SER n 
1 1220 ILE n 
1 1221 ASN n 
1 1222 THR n 
1 1223 ALA n 
1 1224 ALA n 
1 1225 ALA n 
1 1226 GLY n 
1 1227 GLY n 
1 1228 ASN n 
1 1229 ALA n 
1 1230 SER n 
1 1231 LEU n 
1 1232 MET n 
1 1233 ALA n 
1 1234 ILE n 
1 1235 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1235 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'putA, GHK55_27665' 
_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      'Sinorhizobium meliloti' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     382 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
FAD non-polymer                        . 'FLAVIN-ADENINE DINUCLEOTIDE' ?                 'C27 H33 N9 O15 P2' 785.550 
GGL 'L-gamma-peptide, C-delta linking' . 'GAMMA-L-GLUTAMIC ACID'       'L-GLUTAMIC ACID' 'C5 H9 N O4'        147.129 
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 
PEG non-polymer                        . 'DI(HYDROXYETHYL)ETHER'       ?                 'C4 H10 O3'         106.120 
PGE non-polymer                        . 'TRIETHYLENE GLYCOL'          ?                 'C6 H14 O4'         150.173 
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 
SO4 non-polymer                        . 'SULFATE ION'                 ?                 'O4 S -2'           96.063  
THR 'L-peptide linking'                y THREONINE                     ?                 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking'                y TRYPTOPHAN                    ?                 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking'                y TYROSINE                      ?                 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking'                y VALINE                        ?                 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    SER 1    -1   ?    ?   ?   A . n 
A 1 2    MET 2    0    ?    ?   ?   A . n 
A 1 3    MET 3    1    ?    ?   ?   A . n 
A 1 4    SER 4    2    ?    ?   ?   A . n 
A 1 5    PRO 5    3    ?    ?   ?   A . n 
A 1 6    ASN 6    4    ?    ?   ?   A . n 
A 1 7    PRO 7    5    ?    ?   ?   A . n 
A 1 8    LEU 8    6    ?    ?   ?   A . n 
A 1 9    GLN 9    7    ?    ?   ?   A . n 
A 1 10   LYS 10   8    ?    ?   ?   A . n 
A 1 11   PRO 11   9    ?    ?   ?   A . n 
A 1 12   ALA 12   10   ?    ?   ?   A . n 
A 1 13   ILE 13   11   ?    ?   ?   A . n 
A 1 14   ASP 14   12   ?    ?   ?   A . n 
A 1 15   ALA 15   13   ?    ?   ?   A . n 
A 1 16   ALA 16   14   ?    ?   ?   A . n 
A 1 17   PRO 17   15   15   PRO PRO A . n 
A 1 18   ALA 18   16   16   ALA ALA A . n 
A 1 19   PRO 19   17   17   PRO PRO A . n 
A 1 20   PHE 20   18   18   PHE PHE A . n 
A 1 21   ALA 21   19   19   ALA ALA A . n 
A 1 22   ASP 22   20   20   ASP ASP A . n 
A 1 23   PHE 23   21   21   PHE PHE A . n 
A 1 24   ALA 24   22   22   ALA ALA A . n 
A 1 25   PRO 25   23   23   PRO PRO A . n 
A 1 26   PRO 26   24   24   PRO PRO A . n 
A 1 27   VAL 27   25   25   VAL VAL A . n 
A 1 28   ARG 28   26   26   ARG ARG A . n 
A 1 29   PRO 29   27   27   PRO PRO A . n 
A 1 30   GLN 30   28   28   GLN GLN A . n 
A 1 31   SER 31   29   29   SER SER A . n 
A 1 32   THR 32   30   30   THR THR A . n 
A 1 33   LEU 33   31   31   LEU LEU A . n 
A 1 34   ARG 34   32   32   ARG ARG A . n 
A 1 35   ARG 35   33   33   ARG ARG A . n 
A 1 36   ALA 36   34   34   ALA ALA A . n 
A 1 37   ILE 37   35   35   ILE ILE A . n 
A 1 38   THR 38   36   36   THR THR A . n 
A 1 39   ALA 39   37   37   ALA ALA A . n 
A 1 40   ALA 40   38   38   ALA ALA A . n 
A 1 41   TYR 41   39   39   TYR TYR A . n 
A 1 42   ARG 42   40   40   ARG ARG A . n 
A 1 43   ARG 43   41   41   ARG ARG A . n 
A 1 44   PRO 44   42   42   PRO PRO A . n 
A 1 45   GLU 45   43   43   GLU GLU A . n 
A 1 46   THR 46   44   44   THR THR A . n 
A 1 47   GLU 47   45   45   GLU GLU A . n 
A 1 48   CYS 48   46   46   CYS CYS A . n 
A 1 49   LEU 49   47   47   LEU LEU A . n 
A 1 50   PRO 50   48   48   PRO PRO A . n 
A 1 51   PRO 51   49   49   PRO PRO A . n 
A 1 52   LEU 52   50   50   LEU LEU A . n 
A 1 53   VAL 53   51   51   VAL VAL A . n 
A 1 54   GLU 54   52   52   GLU GLU A . n 
A 1 55   ALA 55   53   53   ALA ALA A . n 
A 1 56   ALA 56   54   54   ALA ALA A . n 
A 1 57   THR 57   55   55   THR THR A . n 
A 1 58   GLN 58   56   56   GLN GLN A . n 
A 1 59   SER 59   57   57   SER SER A . n 
A 1 60   LYS 60   58   58   LYS LYS A . n 
A 1 61   GLU 61   59   59   GLU GLU A . n 
A 1 62   ILE 62   60   60   ILE ILE A . n 
A 1 63   ARG 63   61   61   ARG ARG A . n 
A 1 64   ASP 64   62   62   ASP ASP A . n 
A 1 65   ALA 65   63   63   ALA ALA A . n 
A 1 66   ALA 66   64   64   ALA ALA A . n 
A 1 67   ALA 67   65   65   ALA ALA A . n 
A 1 68   SER 68   66   66   SER SER A . n 
A 1 69   THR 69   67   67   THR THR A . n 
A 1 70   ALA 70   68   68   ALA ALA A . n 
A 1 71   ARG 71   69   69   ARG ARG A . n 
A 1 72   LYS 72   70   70   LYS LYS A . n 
A 1 73   LEU 73   71   71   LEU LEU A . n 
A 1 74   ILE 74   72   72   ILE ILE A . n 
A 1 75   GLU 75   73   73   GLU GLU A . n 
A 1 76   ALA 76   74   74   ALA ALA A . n 
A 1 77   LEU 77   75   75   LEU LEU A . n 
A 1 78   ARG 78   76   76   ARG ARG A . n 
A 1 79   GLY 79   77   77   GLY GLY A . n 
A 1 80   LYS 80   78   78   LYS LYS A . n 
A 1 81   HIS 81   79   79   HIS HIS A . n 
A 1 82   SER 82   80   80   SER SER A . n 
A 1 83   GLY 83   81   81   GLY GLY A . n 
A 1 84   SER 84   82   82   SER SER A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  135  GLY GLY A . n 
A 1 138  GLY 138  136  136  GLY GLY A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  492  GLU GLU A . n 
A 1 495  ASN 495  493  493  ASN ASN A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 1232 ILE ILE A . n 
A 1 1235 GLY 1235 1233 1233 GLY GLY A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   ?    ?   ?   B . n 
B 1 17   PRO 17   15   15   PRO PRO B . n 
B 1 18   ALA 18   16   16   ALA ALA B . n 
B 1 19   PRO 19   17   17   PRO PRO B . n 
B 1 20   PHE 20   18   18   PHE PHE B . n 
B 1 21   ALA 21   19   19   ALA ALA B . n 
B 1 22   ASP 22   20   20   ASP ASP B . n 
B 1 23   PHE 23   21   21   PHE PHE B . n 
B 1 24   ALA 24   22   22   ALA ALA B . n 
B 1 25   PRO 25   23   23   PRO PRO B . n 
B 1 26   PRO 26   24   24   PRO PRO B . n 
B 1 27   VAL 27   25   25   VAL VAL B . n 
B 1 28   ARG 28   26   26   ARG ARG B . n 
B 1 29   PRO 29   27   27   PRO PRO B . n 
B 1 30   GLN 30   28   28   GLN GLN B . n 
B 1 31   SER 31   29   29   SER SER B . n 
B 1 32   THR 32   30   30   THR THR B . n 
B 1 33   LEU 33   31   31   LEU LEU B . n 
B 1 34   ARG 34   32   32   ARG ARG B . n 
B 1 35   ARG 35   33   33   ARG ARG B . n 
B 1 36   ALA 36   34   34   ALA ALA B . n 
B 1 37   ILE 37   35   35   ILE ILE B . n 
B 1 38   THR 38   36   36   THR THR B . n 
B 1 39   ALA 39   37   37   ALA ALA B . n 
B 1 40   ALA 40   38   38   ALA ALA B . n 
B 1 41   TYR 41   39   39   TYR TYR B . n 
B 1 42   ARG 42   40   40   ARG ARG B . n 
B 1 43   ARG 43   41   41   ARG ARG B . n 
B 1 44   PRO 44   42   42   PRO PRO B . n 
B 1 45   GLU 45   43   43   GLU GLU B . n 
B 1 46   THR 46   44   44   THR THR B . n 
B 1 47   GLU 47   45   45   GLU GLU B . n 
B 1 48   CYS 48   46   46   CYS CYS B . n 
B 1 49   LEU 49   47   47   LEU LEU B . n 
B 1 50   PRO 50   48   48   PRO PRO B . n 
B 1 51   PRO 51   49   49   PRO PRO B . n 
B 1 52   LEU 52   50   50   LEU LEU B . n 
B 1 53   VAL 53   51   51   VAL VAL B . n 
B 1 54   GLU 54   52   52   GLU GLU B . n 
B 1 55   ALA 55   53   53   ALA ALA B . n 
B 1 56   ALA 56   54   54   ALA ALA B . n 
B 1 57   THR 57   55   55   THR THR B . n 
B 1 58   GLN 58   56   56   GLN GLN B . n 
B 1 59   SER 59   57   57   SER SER B . n 
B 1 60   LYS 60   58   58   LYS LYS B . n 
B 1 61   GLU 61   59   59   GLU GLU B . n 
B 1 62   ILE 62   60   60   ILE ILE B . n 
B 1 63   ARG 63   61   61   ARG ARG B . n 
B 1 64   ASP 64   62   62   ASP ASP B . n 
B 1 65   ALA 65   63   63   ALA ALA B . n 
B 1 66   ALA 66   64   64   ALA ALA B . n 
B 1 67   ALA 67   65   65   ALA ALA B . n 
B 1 68   SER 68   66   66   SER SER B . n 
B 1 69   THR 69   67   67   THR THR B . n 
B 1 70   ALA 70   68   68   ALA ALA B . n 
B 1 71   ARG 71   69   69   ARG ARG B . n 
B 1 72   LYS 72   70   70   LYS LYS B . n 
B 1 73   LEU 73   71   71   LEU LEU B . n 
B 1 74   ILE 74   72   72   ILE ILE B . n 
B 1 75   GLU 75   73   73   GLU GLU B . n 
B 1 76   ALA 76   74   74   ALA ALA B . n 
B 1 77   LEU 77   75   75   LEU LEU B . n 
B 1 78   ARG 78   76   76   ARG ARG B . n 
B 1 79   GLY 79   77   77   GLY GLY B . n 
B 1 80   LYS 80   78   78   LYS LYS B . n 
B 1 81   HIS 81   79   79   HIS HIS B . n 
B 1 82   SER 82   80   80   SER SER B . n 
B 1 83   GLY 83   81   81   GLY GLY B . n 
B 1 84   SER 84   82   82   SER SER B . n 
B 1 85   GLY 85   83   83   GLY GLY B . n 
B 1 86   VAL 86   84   84   VAL VAL B . n 
B 1 87   GLU 87   85   85   GLU GLU B . n 
B 1 88   GLY 88   86   86   GLY GLY B . n 
B 1 89   LEU 89   87   87   LEU LEU B . n 
B 1 90   VAL 90   88   88   VAL VAL B . n 
B 1 91   GLN 91   89   89   GLN GLN B . n 
B 1 92   GLU 92   90   90   GLU GLU B . n 
B 1 93   TYR 93   91   91   TYR TYR B . n 
B 1 94   SER 94   92   92   SER SER B . n 
B 1 95   LEU 95   93   93   LEU LEU B . n 
B 1 96   SER 96   94   94   SER SER B . n 
B 1 97   SER 97   95   95   SER SER B . n 
B 1 98   GLN 98   96   96   GLN GLN B . n 
B 1 99   GLU 99   97   97   GLU GLU B . n 
B 1 100  GLY 100  98   98   GLY GLY B . n 
B 1 101  VAL 101  99   99   VAL VAL B . n 
B 1 102  ALA 102  100  100  ALA ALA B . n 
B 1 103  LEU 103  101  101  LEU LEU B . n 
B 1 104  MET 104  102  102  MET MET B . n 
B 1 105  CYS 105  103  103  CYS CYS B . n 
B 1 106  LEU 106  104  104  LEU LEU B . n 
B 1 107  ALA 107  105  105  ALA ALA B . n 
B 1 108  GLU 108  106  106  GLU GLU B . n 
B 1 109  ALA 109  107  107  ALA ALA B . n 
B 1 110  LEU 110  108  108  LEU LEU B . n 
B 1 111  LEU 111  109  109  LEU LEU B . n 
B 1 112  ARG 112  110  110  ARG ARG B . n 
B 1 113  ILE 113  111  111  ILE ILE B . n 
B 1 114  PRO 114  112  112  PRO PRO B . n 
B 1 115  ASP 115  113  113  ASP ASP B . n 
B 1 116  THR 116  114  114  THR THR B . n 
B 1 117  ALA 117  115  115  ALA ALA B . n 
B 1 118  THR 118  116  116  THR THR B . n 
B 1 119  ARG 119  117  117  ARG ARG B . n 
B 1 120  ASP 120  118  118  ASP ASP B . n 
B 1 121  ALA 121  119  119  ALA ALA B . n 
B 1 122  LEU 122  120  120  LEU LEU B . n 
B 1 123  ILE 123  121  121  ILE ILE B . n 
B 1 124  ARG 124  122  122  ARG ARG B . n 
B 1 125  ASP 125  123  123  ASP ASP B . n 
B 1 126  LYS 126  124  124  LYS LYS B . n 
B 1 127  ILE 127  125  125  ILE ILE B . n 
B 1 128  ALA 128  126  126  ALA ALA B . n 
B 1 129  ASP 129  127  127  ASP ASP B . n 
B 1 130  GLY 130  128  ?    ?   ?   B . n 
B 1 131  ASN 131  129  129  ASN ASN B . n 
B 1 132  TRP 132  130  130  TRP TRP B . n 
B 1 133  LYS 133  131  131  LYS LYS B . n 
B 1 134  SER 134  132  132  SER SER B . n 
B 1 135  HIS 135  133  133  HIS HIS B . n 
B 1 136  LEU 136  134  134  LEU LEU B . n 
B 1 137  GLY 137  135  135  GLY GLY B . n 
B 1 138  GLY 138  136  136  GLY GLY B . n 
B 1 139  SER 139  137  137  SER SER B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  436  GLY GLY B . n 
B 1 439  LYS 439  437  437  LYS LYS B . n 
B 1 440  ASP 440  438  438  ASP ASP B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  492  GLU GLU B . n 
B 1 495  ASN 495  493  493  ASN ASN B . n 
B 1 496  GLY 496  494  494  GLY GLY B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 1223 ALA ALA B . n 
B 1 1226 GLY 1226 1224 1224 GLY GLY B . n 
B 1 1227 GLY 1227 1225 1225 GLY GLY B . n 
B 1 1228 ASN 1228 1226 1226 ASN ASN B . n 
B 1 1229 ALA 1229 1227 1227 ALA ALA B . n 
B 1 1230 SER 1230 1228 1228 SER SER B . n 
B 1 1231 LEU 1231 1229 1229 LEU LEU B . n 
B 1 1232 MET 1232 1230 1230 MET MET B . n 
B 1 1233 ALA 1233 1231 1231 ALA ALA B . n 
B 1 1234 ILE 1234 1232 1232 ILE ILE B . n 
B 1 1235 GLY 1235 1233 1233 GLY GLY B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GGL ? ? GGL ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GGL 1   1301 1    GGL GLX A . 
D 3 SO4 1   1302 2    SO4 SO4 A . 
E 3 SO4 1   1303 3    SO4 SO4 A . 
F 3 SO4 1   1304 4    SO4 SO4 A . 
G 3 SO4 1   1305 6    SO4 SO4 A . 
H 3 SO4 1   1306 9    SO4 SO4 A . 
I 4 PGE 1   1307 3    PGE PGE A . 
J 5 FAD 1   1308 1301 FAD FAD A . 
K 2 GGL 1   1301 2    GGL GLX B . 
L 3 SO4 1   1302 1    SO4 SO4 B . 
M 3 SO4 1   1303 5    SO4 SO4 B . 
N 3 SO4 1   1304 7    SO4 SO4 B . 
O 3 SO4 1   1305 8    SO4 SO4 B . 
P 6 PEG 1   1306 1    PEG PEG B . 
Q 4 PGE 1   1307 2    PGE PGE B . 
R 5 FAD 1   1308 1301 FAD FAD B . 
S 7 HOH 1   1401 1052 HOH HOH A . 
S 7 HOH 2   1402 1897 HOH HOH A . 
S 7 HOH 3   1403 2033 HOH HOH A . 
S 7 HOH 4   1404 2086 HOH HOH A . 
S 7 HOH 5   1405 1832 HOH HOH A . 
S 7 HOH 6   1406 994  HOH HOH A . 
S 7 HOH 7   1407 1587 HOH HOH A . 
S 7 HOH 8   1408 2020 HOH HOH A . 
S 7 HOH 9   1409 2047 HOH HOH A . 
S 7 HOH 10  1410 2073 HOH HOH A . 
S 7 HOH 11  1411 2022 HOH HOH A . 
S 7 HOH 12  1412 1657 HOH HOH A . 
S 7 HOH 13  1413 1896 HOH HOH A . 
S 7 HOH 14  1414 1791 HOH HOH A . 
S 7 HOH 15  1415 1460 HOH HOH A . 
S 7 HOH 16  1416 1826 HOH HOH A . 
S 7 HOH 17  1417 1960 HOH HOH A . 
S 7 HOH 18  1418 1358 HOH HOH A . 
S 7 HOH 19  1419 2077 HOH HOH A . 
S 7 HOH 20  1420 1926 HOH HOH A . 
S 7 HOH 21  1421 1911 HOH HOH A . 
S 7 HOH 22  1422 754  HOH HOH A . 
S 7 HOH 23  1423 2010 HOH HOH A . 
S 7 HOH 24  1424 1890 HOH HOH A . 
S 7 HOH 25  1425 1918 HOH HOH A . 
S 7 HOH 26  1426 624  HOH HOH A . 
S 7 HOH 27  1427 1665 HOH HOH A . 
S 7 HOH 28  1428 1653 HOH HOH A . 
S 7 HOH 29  1429 1678 HOH HOH A . 
S 7 HOH 30  1430 1637 HOH HOH A . 
S 7 HOH 31  1431 1670 HOH HOH A . 
S 7 HOH 32  1432 1971 HOH HOH A . 
S 7 HOH 33  1433 608  HOH HOH A . 
S 7 HOH 34  1434 1576 HOH HOH A . 
S 7 HOH 35  1435 1199 HOH HOH A . 
S 7 HOH 36  1436 3010 HOH HOH A . 
S 7 HOH 37  1437 2003 HOH HOH A . 
S 7 HOH 38  1438 959  HOH HOH A . 
S 7 HOH 39  1439 2013 HOH HOH A . 
S 7 HOH 40  1440 950  HOH HOH A . 
S 7 HOH 41  1441 1747 HOH HOH A . 
S 7 HOH 42  1442 1287 HOH HOH A . 
S 7 HOH 43  1443 2021 HOH HOH A . 
S 7 HOH 44  1444 1632 HOH HOH A . 
S 7 HOH 45  1445 1567 HOH HOH A . 
S 7 HOH 46  1446 1371 HOH HOH A . 
S 7 HOH 47  1447 1779 HOH HOH A . 
S 7 HOH 48  1448 602  HOH HOH A . 
S 7 HOH 49  1449 1970 HOH HOH A . 
S 7 HOH 50  1450 1956 HOH HOH A . 
S 7 HOH 51  1451 914  HOH HOH A . 
S 7 HOH 52  1452 1436 HOH HOH A . 
S 7 HOH 53  1453 1442 HOH HOH A . 
S 7 HOH 54  1454 1852 HOH HOH A . 
S 7 HOH 55  1455 2023 HOH HOH A . 
S 7 HOH 56  1456 847  HOH HOH A . 
S 7 HOH 57  1457 1906 HOH HOH A . 
S 7 HOH 58  1458 336  HOH HOH A . 
S 7 HOH 59  1459 702  HOH HOH A . 
S 7 HOH 60  1460 1476 HOH HOH A . 
S 7 HOH 61  1461 1355 HOH HOH A . 
S 7 HOH 62  1462 1907 HOH HOH A . 
S 7 HOH 63  1463 1408 HOH HOH A . 
S 7 HOH 64  1464 799  HOH HOH A . 
S 7 HOH 65  1465 1362 HOH HOH A . 
S 7 HOH 66  1466 1917 HOH HOH A . 
S 7 HOH 67  1467 1555 HOH HOH A . 
S 7 HOH 68  1468 373  HOH HOH A . 
S 7 HOH 69  1469 1032 HOH HOH A . 
S 7 HOH 70  1470 1715 HOH HOH A . 
S 7 HOH 71  1471 696  HOH HOH A . 
S 7 HOH 72  1472 1210 HOH HOH A . 
S 7 HOH 73  1473 285  HOH HOH A . 
S 7 HOH 74  1474 524  HOH HOH A . 
S 7 HOH 75  1475 359  HOH HOH A . 
S 7 HOH 76  1476 2061 HOH HOH A . 
S 7 HOH 77  1477 1475 HOH HOH A . 
S 7 HOH 78  1478 505  HOH HOH A . 
S 7 HOH 79  1479 740  HOH HOH A . 
S 7 HOH 80  1480 840  HOH HOH A . 
S 7 HOH 81  1481 3012 HOH HOH A . 
S 7 HOH 82  1482 224  HOH HOH A . 
S 7 HOH 83  1483 1735 HOH HOH A . 
S 7 HOH 84  1484 1708 HOH HOH A . 
S 7 HOH 85  1485 2052 HOH HOH A . 
S 7 HOH 86  1486 1478 HOH HOH A . 
S 7 HOH 87  1487 699  HOH HOH A . 
S 7 HOH 88  1488 1364 HOH HOH A . 
S 7 HOH 89  1489 861  HOH HOH A . 
S 7 HOH 90  1490 1973 HOH HOH A . 
S 7 HOH 91  1491 381  HOH HOH A . 
S 7 HOH 92  1492 742  HOH HOH A . 
S 7 HOH 93  1493 1489 HOH HOH A . 
S 7 HOH 94  1494 405  HOH HOH A . 
S 7 HOH 95  1495 1541 HOH HOH A . 
S 7 HOH 96  1496 586  HOH HOH A . 
S 7 HOH 97  1497 406  HOH HOH A . 
S 7 HOH 98  1498 596  HOH HOH A . 
S 7 HOH 99  1499 1648 HOH HOH A . 
S 7 HOH 100 1500 3009 HOH HOH A . 
S 7 HOH 101 1501 3023 HOH HOH A . 
S 7 HOH 102 1502 64   HOH HOH A . 
S 7 HOH 103 1503 1064 HOH HOH A . 
S 7 HOH 104 1504 1218 HOH HOH A . 
S 7 HOH 105 1505 1939 HOH HOH A . 
S 7 HOH 106 1506 1439 HOH HOH A . 
S 7 HOH 107 1507 1451 HOH HOH A . 
S 7 HOH 108 1508 1131 HOH HOH A . 
S 7 HOH 109 1509 1184 HOH HOH A . 
S 7 HOH 110 1510 1767 HOH HOH A . 
S 7 HOH 111 1511 1544 HOH HOH A . 
S 7 HOH 112 1512 1774 HOH HOH A . 
S 7 HOH 113 1513 440  HOH HOH A . 
S 7 HOH 114 1514 1776 HOH HOH A . 
S 7 HOH 115 1515 1437 HOH HOH A . 
S 7 HOH 116 1516 1105 HOH HOH A . 
S 7 HOH 117 1517 929  HOH HOH A . 
S 7 HOH 118 1518 404  HOH HOH A . 
S 7 HOH 119 1519 457  HOH HOH A . 
S 7 HOH 120 1520 940  HOH HOH A . 
S 7 HOH 121 1521 618  HOH HOH A . 
S 7 HOH 122 1522 587  HOH HOH A . 
S 7 HOH 123 1523 1730 HOH HOH A . 
S 7 HOH 124 1524 1927 HOH HOH A . 
S 7 HOH 125 1525 1441 HOH HOH A . 
S 7 HOH 126 1526 48   HOH HOH A . 
S 7 HOH 127 1527 997  HOH HOH A . 
S 7 HOH 128 1528 1381 HOH HOH A . 
S 7 HOH 129 1529 681  HOH HOH A . 
S 7 HOH 130 1530 1370 HOH HOH A . 
S 7 HOH 131 1531 927  HOH HOH A . 
S 7 HOH 132 1532 1025 HOH HOH A . 
S 7 HOH 133 1533 989  HOH HOH A . 
S 7 HOH 134 1534 1083 HOH HOH A . 
S 7 HOH 135 1535 1142 HOH HOH A . 
S 7 HOH 136 1536 1023 HOH HOH A . 
S 7 HOH 137 1537 279  HOH HOH A . 
S 7 HOH 138 1538 1606 HOH HOH A . 
S 7 HOH 139 1539 941  HOH HOH A . 
S 7 HOH 140 1540 1447 HOH HOH A . 
S 7 HOH 141 1541 1756 HOH HOH A . 
S 7 HOH 142 1542 700  HOH HOH A . 
S 7 HOH 143 1543 864  HOH HOH A . 
S 7 HOH 144 1544 1984 HOH HOH A . 
S 7 HOH 145 1545 1026 HOH HOH A . 
S 7 HOH 146 1546 24   HOH HOH A . 
S 7 HOH 147 1547 1369 HOH HOH A . 
S 7 HOH 148 1548 217  HOH HOH A . 
S 7 HOH 149 1549 2090 HOH HOH A . 
S 7 HOH 150 1550 720  HOH HOH A . 
S 7 HOH 151 1551 886  HOH HOH A . 
S 7 HOH 152 1552 419  HOH HOH A . 
S 7 HOH 153 1553 1171 HOH HOH A . 
S 7 HOH 154 1554 262  HOH HOH A . 
S 7 HOH 155 1555 697  HOH HOH A . 
S 7 HOH 156 1556 715  HOH HOH A . 
S 7 HOH 157 1557 1712 HOH HOH A . 
S 7 HOH 158 1558 118  HOH HOH A . 
S 7 HOH 159 1559 125  HOH HOH A . 
S 7 HOH 160 1560 247  HOH HOH A . 
S 7 HOH 161 1561 1915 HOH HOH A . 
S 7 HOH 162 1562 711  HOH HOH A . 
S 7 HOH 163 1563 1379 HOH HOH A . 
S 7 HOH 164 1564 1180 HOH HOH A . 
S 7 HOH 165 1565 383  HOH HOH A . 
S 7 HOH 166 1566 588  HOH HOH A . 
S 7 HOH 167 1567 879  HOH HOH A . 
S 7 HOH 168 1568 1134 HOH HOH A . 
S 7 HOH 169 1569 469  HOH HOH A . 
S 7 HOH 170 1570 255  HOH HOH A . 
S 7 HOH 171 1571 1856 HOH HOH A . 
S 7 HOH 172 1572 132  HOH HOH A . 
S 7 HOH 173 1573 139  HOH HOH A . 
S 7 HOH 174 1574 1099 HOH HOH A . 
S 7 HOH 175 1575 1985 HOH HOH A . 
S 7 HOH 176 1576 1031 HOH HOH A . 
S 7 HOH 177 1577 67   HOH HOH A . 
S 7 HOH 178 1578 1406 HOH HOH A . 
S 7 HOH 179 1579 397  HOH HOH A . 
S 7 HOH 180 1580 403  HOH HOH A . 
S 7 HOH 181 1581 169  HOH HOH A . 
S 7 HOH 182 1582 625  HOH HOH A . 
S 7 HOH 183 1583 321  HOH HOH A . 
S 7 HOH 184 1584 1095 HOH HOH A . 
S 7 HOH 185 1585 123  HOH HOH A . 
S 7 HOH 186 1586 122  HOH HOH A . 
S 7 HOH 187 1587 168  HOH HOH A . 
S 7 HOH 188 1588 671  HOH HOH A . 
S 7 HOH 189 1589 566  HOH HOH A . 
S 7 HOH 190 1590 1624 HOH HOH A . 
S 7 HOH 191 1591 154  HOH HOH A . 
S 7 HOH 192 1592 280  HOH HOH A . 
S 7 HOH 193 1593 722  HOH HOH A . 
S 7 HOH 194 1594 1790 HOH HOH A . 
S 7 HOH 195 1595 333  HOH HOH A . 
S 7 HOH 196 1596 719  HOH HOH A . 
S 7 HOH 197 1597 1640 HOH HOH A . 
S 7 HOH 198 1598 1417 HOH HOH A . 
S 7 HOH 199 1599 136  HOH HOH A . 
S 7 HOH 200 1600 1172 HOH HOH A . 
S 7 HOH 201 1601 537  HOH HOH A . 
S 7 HOH 202 1602 1752 HOH HOH A . 
S 7 HOH 203 1603 892  HOH HOH A . 
S 7 HOH 204 1604 257  HOH HOH A . 
S 7 HOH 205 1605 268  HOH HOH A . 
S 7 HOH 206 1606 386  HOH HOH A . 
S 7 HOH 207 1607 875  HOH HOH A . 
S 7 HOH 208 1608 348  HOH HOH A . 
S 7 HOH 209 1609 1892 HOH HOH A . 
S 7 HOH 210 1610 1029 HOH HOH A . 
S 7 HOH 211 1611 589  HOH HOH A . 
S 7 HOH 212 1612 752  HOH HOH A . 
S 7 HOH 213 1613 744  HOH HOH A . 
S 7 HOH 214 1614 576  HOH HOH A . 
S 7 HOH 215 1615 311  HOH HOH A . 
S 7 HOH 216 1616 614  HOH HOH A . 
S 7 HOH 217 1617 366  HOH HOH A . 
S 7 HOH 218 1618 7    HOH HOH A . 
S 7 HOH 219 1619 127  HOH HOH A . 
S 7 HOH 220 1620 1472 HOH HOH A . 
S 7 HOH 221 1621 434  HOH HOH A . 
S 7 HOH 222 1622 623  HOH HOH A . 
S 7 HOH 223 1623 265  HOH HOH A . 
S 7 HOH 224 1624 1698 HOH HOH A . 
S 7 HOH 225 1625 549  HOH HOH A . 
S 7 HOH 226 1626 2024 HOH HOH A . 
S 7 HOH 227 1627 349  HOH HOH A . 
S 7 HOH 228 1628 746  HOH HOH A . 
S 7 HOH 229 1629 356  HOH HOH A . 
S 7 HOH 230 1630 68   HOH HOH A . 
S 7 HOH 231 1631 1258 HOH HOH A . 
S 7 HOH 232 1632 615  HOH HOH A . 
S 7 HOH 233 1633 375  HOH HOH A . 
S 7 HOH 234 1634 616  HOH HOH A . 
S 7 HOH 235 1635 18   HOH HOH A . 
S 7 HOH 236 1636 12   HOH HOH A . 
S 7 HOH 237 1637 1527 HOH HOH A . 
S 7 HOH 238 1638 1916 HOH HOH A . 
S 7 HOH 239 1639 59   HOH HOH A . 
S 7 HOH 240 1640 1623 HOH HOH A . 
S 7 HOH 241 1641 369  HOH HOH A . 
S 7 HOH 242 1642 808  HOH HOH A . 
S 7 HOH 243 1643 101  HOH HOH A . 
S 7 HOH 244 1644 1410 HOH HOH A . 
S 7 HOH 245 1645 1404 HOH HOH A . 
S 7 HOH 246 1646 555  HOH HOH A . 
S 7 HOH 247 1647 1618 HOH HOH A . 
S 7 HOH 248 1648 284  HOH HOH A . 
S 7 HOH 249 1649 2042 HOH HOH A . 
S 7 HOH 250 1650 1505 HOH HOH A . 
S 7 HOH 251 1651 301  HOH HOH A . 
S 7 HOH 252 1652 908  HOH HOH A . 
S 7 HOH 253 1653 800  HOH HOH A . 
S 7 HOH 254 1654 289  HOH HOH A . 
S 7 HOH 255 1655 72   HOH HOH A . 
S 7 HOH 256 1656 736  HOH HOH A . 
S 7 HOH 257 1657 56   HOH HOH A . 
S 7 HOH 258 1658 541  HOH HOH A . 
S 7 HOH 259 1659 286  HOH HOH A . 
S 7 HOH 260 1660 16   HOH HOH A . 
S 7 HOH 261 1661 1101 HOH HOH A . 
S 7 HOH 262 1662 400  HOH HOH A . 
S 7 HOH 263 1663 1378 HOH HOH A . 
S 7 HOH 264 1664 842  HOH HOH A . 
S 7 HOH 265 1665 728  HOH HOH A . 
S 7 HOH 266 1666 14   HOH HOH A . 
S 7 HOH 267 1667 872  HOH HOH A . 
S 7 HOH 268 1668 105  HOH HOH A . 
S 7 HOH 269 1669 986  HOH HOH A . 
S 7 HOH 270 1670 704  HOH HOH A . 
S 7 HOH 271 1671 674  HOH HOH A . 
S 7 HOH 272 1672 408  HOH HOH A . 
S 7 HOH 273 1673 481  HOH HOH A . 
S 7 HOH 274 1674 115  HOH HOH A . 
S 7 HOH 275 1675 219  HOH HOH A . 
S 7 HOH 276 1676 622  HOH HOH A . 
S 7 HOH 277 1677 859  HOH HOH A . 
S 7 HOH 278 1678 474  HOH HOH A . 
S 7 HOH 279 1679 974  HOH HOH A . 
S 7 HOH 280 1680 165  HOH HOH A . 
S 7 HOH 281 1681 1466 HOH HOH A . 
S 7 HOH 282 1682 1773 HOH HOH A . 
S 7 HOH 283 1683 143  HOH HOH A . 
S 7 HOH 284 1684 70   HOH HOH A . 
S 7 HOH 285 1685 177  HOH HOH A . 
S 7 HOH 286 1686 304  HOH HOH A . 
S 7 HOH 287 1687 1081 HOH HOH A . 
S 7 HOH 288 1688 856  HOH HOH A . 
S 7 HOH 289 1689 782  HOH HOH A . 
S 7 HOH 290 1690 559  HOH HOH A . 
S 7 HOH 291 1691 147  HOH HOH A . 
S 7 HOH 292 1692 1414 HOH HOH A . 
S 7 HOH 293 1693 303  HOH HOH A . 
S 7 HOH 294 1694 237  HOH HOH A . 
S 7 HOH 295 1695 368  HOH HOH A . 
S 7 HOH 296 1696 167  HOH HOH A . 
S 7 HOH 297 1697 650  HOH HOH A . 
S 7 HOH 298 1698 786  HOH HOH A . 
S 7 HOH 299 1699 680  HOH HOH A . 
S 7 HOH 300 1700 171  HOH HOH A . 
S 7 HOH 301 1701 828  HOH HOH A . 
S 7 HOH 302 1702 106  HOH HOH A . 
S 7 HOH 303 1703 243  HOH HOH A . 
S 7 HOH 304 1704 461  HOH HOH A . 
S 7 HOH 305 1705 829  HOH HOH A . 
S 7 HOH 306 1706 426  HOH HOH A . 
S 7 HOH 307 1707 62   HOH HOH A . 
S 7 HOH 308 1708 630  HOH HOH A . 
S 7 HOH 309 1709 510  HOH HOH A . 
S 7 HOH 310 1710 75   HOH HOH A . 
S 7 HOH 311 1711 938  HOH HOH A . 
S 7 HOH 312 1712 947  HOH HOH A . 
S 7 HOH 313 1713 207  HOH HOH A . 
S 7 HOH 314 1714 1509 HOH HOH A . 
S 7 HOH 315 1715 1630 HOH HOH A . 
S 7 HOH 316 1716 1066 HOH HOH A . 
S 7 HOH 317 1717 1418 HOH HOH A . 
S 7 HOH 318 1718 1658 HOH HOH A . 
S 7 HOH 319 1719 46   HOH HOH A . 
S 7 HOH 320 1720 1693 HOH HOH A . 
S 7 HOH 321 1721 1513 HOH HOH A . 
S 7 HOH 322 1722 196  HOH HOH A . 
S 7 HOH 323 1723 313  HOH HOH A . 
S 7 HOH 324 1724 882  HOH HOH A . 
S 7 HOH 325 1725 992  HOH HOH A . 
S 7 HOH 326 1726 943  HOH HOH A . 
S 7 HOH 327 1727 192  HOH HOH A . 
S 7 HOH 328 1728 542  HOH HOH A . 
S 7 HOH 329 1729 833  HOH HOH A . 
S 7 HOH 330 1730 1005 HOH HOH A . 
S 7 HOH 331 1731 1457 HOH HOH A . 
S 7 HOH 332 1732 1096 HOH HOH A . 
S 7 HOH 333 1733 1380 HOH HOH A . 
S 7 HOH 334 1734 228  HOH HOH A . 
S 7 HOH 335 1735 26   HOH HOH A . 
S 7 HOH 336 1736 832  HOH HOH A . 
S 7 HOH 337 1737 1388 HOH HOH A . 
S 7 HOH 338 1738 344  HOH HOH A . 
S 7 HOH 339 1739 1068 HOH HOH A . 
S 7 HOH 340 1740 1748 HOH HOH A . 
S 7 HOH 341 1741 1387 HOH HOH A . 
S 7 HOH 342 1742 874  HOH HOH A . 
S 7 HOH 343 1743 1092 HOH HOH A . 
S 7 HOH 344 1744 300  HOH HOH A . 
S 7 HOH 345 1745 703  HOH HOH A . 
S 7 HOH 346 1746 306  HOH HOH A . 
S 7 HOH 347 1747 548  HOH HOH A . 
S 7 HOH 348 1748 701  HOH HOH A . 
S 7 HOH 349 1749 1483 HOH HOH A . 
S 7 HOH 350 1750 186  HOH HOH A . 
S 7 HOH 351 1751 233  HOH HOH A . 
S 7 HOH 352 1752 263  HOH HOH A . 
S 7 HOH 353 1753 493  HOH HOH A . 
S 7 HOH 354 1754 1390 HOH HOH A . 
S 7 HOH 355 1755 673  HOH HOH A . 
S 7 HOH 356 1756 51   HOH HOH A . 
S 7 HOH 357 1757 1424 HOH HOH A . 
S 7 HOH 358 1758 1549 HOH HOH A . 
S 7 HOH 359 1759 145  HOH HOH A . 
S 7 HOH 360 1760 1318 HOH HOH A . 
S 7 HOH 361 1761 69   HOH HOH A . 
S 7 HOH 362 1762 1393 HOH HOH A . 
S 7 HOH 363 1763 810  HOH HOH A . 
S 7 HOH 364 1764 245  HOH HOH A . 
S 7 HOH 365 1765 78   HOH HOH A . 
S 7 HOH 366 1766 584  HOH HOH A . 
S 7 HOH 367 1767 1517 HOH HOH A . 
S 7 HOH 368 1768 890  HOH HOH A . 
S 7 HOH 369 1769 299  HOH HOH A . 
S 7 HOH 370 1770 1062 HOH HOH A . 
S 7 HOH 371 1771 55   HOH HOH A . 
S 7 HOH 372 1772 1955 HOH HOH A . 
S 7 HOH 373 1773 1397 HOH HOH A . 
S 7 HOH 374 1774 277  HOH HOH A . 
S 7 HOH 375 1775 3018 HOH HOH A . 
S 7 HOH 376 1776 582  HOH HOH A . 
S 7 HOH 377 1777 446  HOH HOH A . 
S 7 HOH 378 1778 1058 HOH HOH A . 
S 7 HOH 379 1779 1024 HOH HOH A . 
S 7 HOH 380 1780 1595 HOH HOH A . 
S 7 HOH 381 1781 1733 HOH HOH A . 
S 7 HOH 382 1782 452  HOH HOH A . 
S 7 HOH 383 1783 1282 HOH HOH A . 
S 7 HOH 384 1784 1234 HOH HOH A . 
S 7 HOH 385 1785 412  HOH HOH A . 
S 7 HOH 386 1786 315  HOH HOH A . 
S 7 HOH 387 1787 1231 HOH HOH A . 
S 7 HOH 388 1788 1540 HOH HOH A . 
S 7 HOH 389 1789 107  HOH HOH A . 
S 7 HOH 390 1790 1103 HOH HOH A . 
S 7 HOH 391 1791 558  HOH HOH A . 
S 7 HOH 392 1792 11   HOH HOH A . 
S 7 HOH 393 1793 1429 HOH HOH A . 
S 7 HOH 394 1794 904  HOH HOH A . 
S 7 HOH 395 1795 66   HOH HOH A . 
S 7 HOH 396 1796 185  HOH HOH A . 
S 7 HOH 397 1797 1063 HOH HOH A . 
S 7 HOH 398 1798 1168 HOH HOH A . 
S 7 HOH 399 1799 684  HOH HOH A . 
S 7 HOH 400 1800 747  HOH HOH A . 
S 7 HOH 401 1801 90   HOH HOH A . 
S 7 HOH 402 1802 453  HOH HOH A . 
S 7 HOH 403 1803 76   HOH HOH A . 
S 7 HOH 404 1804 3004 HOH HOH A . 
S 7 HOH 405 1805 271  HOH HOH A . 
S 7 HOH 406 1806 96   HOH HOH A . 
S 7 HOH 407 1807 1260 HOH HOH A . 
S 7 HOH 408 1808 513  HOH HOH A . 
S 7 HOH 409 1809 335  HOH HOH A . 
S 7 HOH 410 1810 1456 HOH HOH A . 
S 7 HOH 411 1811 1061 HOH HOH A . 
S 7 HOH 412 1812 2065 HOH HOH A . 
S 7 HOH 413 1813 1461 HOH HOH A . 
S 7 HOH 414 1814 1627 HOH HOH A . 
S 7 HOH 415 1815 229  HOH HOH A . 
S 7 HOH 416 1816 1568 HOH HOH A . 
S 7 HOH 417 1817 866  HOH HOH A . 
S 7 HOH 418 1818 439  HOH HOH A . 
S 7 HOH 419 1819 1649 HOH HOH A . 
S 7 HOH 420 1820 1084 HOH HOH A . 
S 7 HOH 421 1821 1041 HOH HOH A . 
S 7 HOH 422 1822 35   HOH HOH A . 
S 7 HOH 423 1823 252  HOH HOH A . 
S 7 HOH 424 1824 1161 HOH HOH A . 
S 7 HOH 425 1825 205  HOH HOH A . 
S 7 HOH 426 1826 1759 HOH HOH A . 
S 7 HOH 427 1827 1202 HOH HOH A . 
S 7 HOH 428 1828 234  HOH HOH A . 
S 7 HOH 429 1829 896  HOH HOH A . 
S 7 HOH 430 1830 178  HOH HOH A . 
S 7 HOH 431 1831 668  HOH HOH A . 
S 7 HOH 432 1832 1165 HOH HOH A . 
S 7 HOH 433 1833 1238 HOH HOH A . 
S 7 HOH 434 1834 830  HOH HOH A . 
S 7 HOH 435 1835 1250 HOH HOH A . 
S 7 HOH 436 1836 819  HOH HOH A . 
S 7 HOH 437 1837 172  HOH HOH A . 
S 7 HOH 438 1838 19   HOH HOH A . 
S 7 HOH 439 1839 49   HOH HOH A . 
S 7 HOH 440 1840 2000 HOH HOH A . 
S 7 HOH 441 1841 710  HOH HOH A . 
S 7 HOH 442 1842 34   HOH HOH A . 
S 7 HOH 443 1843 133  HOH HOH A . 
S 7 HOH 444 1844 100  HOH HOH A . 
S 7 HOH 445 1845 1227 HOH HOH A . 
S 7 HOH 446 1846 355  HOH HOH A . 
S 7 HOH 447 1847 450  HOH HOH A . 
S 7 HOH 448 1848 1501 HOH HOH A . 
S 7 HOH 449 1849 9    HOH HOH A . 
S 7 HOH 450 1850 161  HOH HOH A . 
S 7 HOH 451 1851 496  HOH HOH A . 
S 7 HOH 452 1852 1738 HOH HOH A . 
S 7 HOH 453 1853 367  HOH HOH A . 
S 7 HOH 454 1854 835  HOH HOH A . 
S 7 HOH 455 1855 662  HOH HOH A . 
S 7 HOH 456 1856 565  HOH HOH A . 
S 7 HOH 457 1857 498  HOH HOH A . 
S 7 HOH 458 1858 855  HOH HOH A . 
S 7 HOH 459 1859 784  HOH HOH A . 
S 7 HOH 460 1860 339  HOH HOH A . 
S 7 HOH 461 1861 1195 HOH HOH A . 
S 7 HOH 462 1862 365  HOH HOH A . 
S 7 HOH 463 1863 1067 HOH HOH A . 
S 7 HOH 464 1864 1087 HOH HOH A . 
S 7 HOH 465 1865 1216 HOH HOH A . 
S 7 HOH 466 1866 254  HOH HOH A . 
S 7 HOH 467 1867 1656 HOH HOH A . 
S 7 HOH 468 1868 427  HOH HOH A . 
S 7 HOH 469 1869 1879 HOH HOH A . 
S 7 HOH 470 1870 200  HOH HOH A . 
S 7 HOH 471 1871 294  HOH HOH A . 
S 7 HOH 472 1872 274  HOH HOH A . 
S 7 HOH 473 1873 1170 HOH HOH A . 
S 7 HOH 474 1874 317  HOH HOH A . 
S 7 HOH 475 1875 291  HOH HOH A . 
S 7 HOH 476 1876 580  HOH HOH A . 
S 7 HOH 477 1877 595  HOH HOH A . 
S 7 HOH 478 1878 530  HOH HOH A . 
S 7 HOH 479 1879 1913 HOH HOH A . 
S 7 HOH 480 1880 126  HOH HOH A . 
S 7 HOH 481 1881 1065 HOH HOH A . 
S 7 HOH 482 1882 40   HOH HOH A . 
S 7 HOH 483 1883 975  HOH HOH A . 
S 7 HOH 484 1884 360  HOH HOH A . 
S 7 HOH 485 1885 1042 HOH HOH A . 
S 7 HOH 486 1886 1124 HOH HOH A . 
S 7 HOH 487 1887 460  HOH HOH A . 
S 7 HOH 488 1888 471  HOH HOH A . 
S 7 HOH 489 1889 1100 HOH HOH A . 
S 7 HOH 490 1890 2008 HOH HOH A . 
S 7 HOH 491 1891 1462 HOH HOH A . 
S 7 HOH 492 1892 1145 HOH HOH A . 
S 7 HOH 493 1893 180  HOH HOH A . 
S 7 HOH 494 1894 162  HOH HOH A . 
S 7 HOH 495 1895 951  HOH HOH A . 
S 7 HOH 496 1896 778  HOH HOH A . 
S 7 HOH 497 1897 490  HOH HOH A . 
S 7 HOH 498 1898 182  HOH HOH A . 
S 7 HOH 499 1899 164  HOH HOH A . 
S 7 HOH 500 1900 342  HOH HOH A . 
S 7 HOH 501 1901 319  HOH HOH A . 
S 7 HOH 502 1902 1178 HOH HOH A . 
S 7 HOH 503 1903 2050 HOH HOH A . 
S 7 HOH 504 1904 556  HOH HOH A . 
S 7 HOH 505 1905 862  HOH HOH A . 
S 7 HOH 506 1906 396  HOH HOH A . 
S 7 HOH 507 1907 1352 HOH HOH A . 
S 7 HOH 508 1908 362  HOH HOH A . 
S 7 HOH 509 1909 889  HOH HOH A . 
S 7 HOH 510 1910 431  HOH HOH A . 
S 7 HOH 511 1911 1118 HOH HOH A . 
S 7 HOH 512 1912 1117 HOH HOH A . 
S 7 HOH 513 1913 302  HOH HOH A . 
S 7 HOH 514 1914 1262 HOH HOH A . 
S 7 HOH 515 1915 357  HOH HOH A . 
S 7 HOH 516 1916 189  HOH HOH A . 
S 7 HOH 517 1917 525  HOH HOH A . 
S 7 HOH 518 1918 1237 HOH HOH A . 
S 7 HOH 519 1919 160  HOH HOH A . 
S 7 HOH 520 1920 592  HOH HOH A . 
S 7 HOH 521 1921 1643 HOH HOH A . 
S 7 HOH 522 1922 33   HOH HOH A . 
S 7 HOH 523 1923 1426 HOH HOH A . 
S 7 HOH 524 1924 836  HOH HOH A . 
S 7 HOH 525 1925 1997 HOH HOH A . 
S 7 HOH 526 1926 1157 HOH HOH A . 
S 7 HOH 527 1927 371  HOH HOH A . 
S 7 HOH 528 1928 922  HOH HOH A . 
S 7 HOH 529 1929 894  HOH HOH A . 
S 7 HOH 530 1930 347  HOH HOH A . 
S 7 HOH 531 1931 883  HOH HOH A . 
S 7 HOH 532 1932 964  HOH HOH A . 
S 7 HOH 533 1933 1044 HOH HOH A . 
S 7 HOH 534 1934 28   HOH HOH A . 
S 7 HOH 535 1935 179  HOH HOH A . 
S 7 HOH 536 1936 258  HOH HOH A . 
S 7 HOH 537 1937 1732 HOH HOH A . 
S 7 HOH 538 1938 341  HOH HOH A . 
S 7 HOH 539 1939 1177 HOH HOH A . 
S 7 HOH 540 1940 958  HOH HOH A . 
S 7 HOH 541 1941 1830 HOH HOH A . 
S 7 HOH 542 1942 248  HOH HOH A . 
S 7 HOH 543 1943 637  HOH HOH A . 
S 7 HOH 544 1944 236  HOH HOH A . 
S 7 HOH 545 1945 1669 HOH HOH A . 
S 7 HOH 546 1946 32   HOH HOH A . 
S 7 HOH 547 1947 690  HOH HOH A . 
S 7 HOH 548 1948 1477 HOH HOH A . 
S 7 HOH 549 1949 1493 HOH HOH A . 
S 7 HOH 550 1950 138  HOH HOH A . 
S 7 HOH 551 1951 1742 HOH HOH A . 
S 7 HOH 552 1952 724  HOH HOH A . 
S 7 HOH 553 1953 467  HOH HOH A . 
S 7 HOH 554 1954 2071 HOH HOH A . 
S 7 HOH 555 1955 135  HOH HOH A . 
S 7 HOH 556 1956 275  HOH HOH A . 
S 7 HOH 557 1957 152  HOH HOH A . 
S 7 HOH 558 1958 211  HOH HOH A . 
S 7 HOH 559 1959 731  HOH HOH A . 
S 7 HOH 560 1960 1389 HOH HOH A . 
S 7 HOH 561 1961 1089 HOH HOH A . 
S 7 HOH 562 1962 226  HOH HOH A . 
S 7 HOH 563 1963 1104 HOH HOH A . 
S 7 HOH 564 1964 985  HOH HOH A . 
S 7 HOH 565 1965 1734 HOH HOH A . 
S 7 HOH 566 1966 535  HOH HOH A . 
S 7 HOH 567 1967 2025 HOH HOH A . 
S 7 HOH 568 1968 639  HOH HOH A . 
S 7 HOH 569 1969 20   HOH HOH A . 
S 7 HOH 570 1970 1464 HOH HOH A . 
S 7 HOH 571 1971 1431 HOH HOH A . 
S 7 HOH 572 1972 1438 HOH HOH A . 
S 7 HOH 573 1973 83   HOH HOH A . 
S 7 HOH 574 1974 1224 HOH HOH A . 
S 7 HOH 575 1975 121  HOH HOH A . 
S 7 HOH 576 1976 354  HOH HOH A . 
S 7 HOH 577 1977 1646 HOH HOH A . 
S 7 HOH 578 1978 1492 HOH HOH A . 
S 7 HOH 579 1979 103  HOH HOH A . 
S 7 HOH 580 1980 1512 HOH HOH A . 
S 7 HOH 581 1981 488  HOH HOH A . 
S 7 HOH 582 1982 1187 HOH HOH A . 
S 7 HOH 583 1983 562  HOH HOH A . 
S 7 HOH 584 1984 651  HOH HOH A . 
S 7 HOH 585 1985 273  HOH HOH A . 
S 7 HOH 586 1986 2018 HOH HOH A . 
S 7 HOH 587 1987 421  HOH HOH A . 
S 7 HOH 588 1988 824  HOH HOH A . 
S 7 HOH 589 1989 159  HOH HOH A . 
S 7 HOH 590 1990 478  HOH HOH A . 
S 7 HOH 591 1991 1524 HOH HOH A . 
S 7 HOH 592 1992 134  HOH HOH A . 
S 7 HOH 593 1993 238  HOH HOH A . 
S 7 HOH 594 1994 93   HOH HOH A . 
S 7 HOH 595 1995 545  HOH HOH A . 
S 7 HOH 596 1996 415  HOH HOH A . 
S 7 HOH 597 1997 1525 HOH HOH A . 
S 7 HOH 598 1998 657  HOH HOH A . 
S 7 HOH 599 1999 87   HOH HOH A . 
S 7 HOH 600 2000 901  HOH HOH A . 
S 7 HOH 601 2001 130  HOH HOH A . 
S 7 HOH 602 2002 3013 HOH HOH A . 
S 7 HOH 603 2003 479  HOH HOH A . 
S 7 HOH 604 2004 267  HOH HOH A . 
S 7 HOH 605 2005 1078 HOH HOH A . 
S 7 HOH 606 2006 675  HOH HOH A . 
S 7 HOH 607 2007 937  HOH HOH A . 
S 7 HOH 608 2008 129  HOH HOH A . 
S 7 HOH 609 2009 763  HOH HOH A . 
S 7 HOH 610 2010 459  HOH HOH A . 
S 7 HOH 611 2011 644  HOH HOH A . 
S 7 HOH 612 2012 511  HOH HOH A . 
S 7 HOH 613 2013 1411 HOH HOH A . 
S 7 HOH 614 2014 174  HOH HOH A . 
S 7 HOH 615 2015 1749 HOH HOH A . 
S 7 HOH 616 2016 1571 HOH HOH A . 
S 7 HOH 617 2017 1114 HOH HOH A . 
S 7 HOH 618 2018 1499 HOH HOH A . 
S 7 HOH 619 2019 732  HOH HOH A . 
S 7 HOH 620 2020 380  HOH HOH A . 
S 7 HOH 621 2021 193  HOH HOH A . 
S 7 HOH 622 2022 436  HOH HOH A . 
S 7 HOH 623 2023 1085 HOH HOH A . 
S 7 HOH 624 2024 1762 HOH HOH A . 
S 7 HOH 625 2025 1664 HOH HOH A . 
S 7 HOH 626 2026 364  HOH HOH A . 
S 7 HOH 627 2027 382  HOH HOH A . 
S 7 HOH 628 2028 811  HOH HOH A . 
S 7 HOH 629 2029 878  HOH HOH A . 
S 7 HOH 630 2030 487  HOH HOH A . 
S 7 HOH 631 2031 641  HOH HOH A . 
S 7 HOH 632 2032 590  HOH HOH A . 
S 7 HOH 633 2033 573  HOH HOH A . 
S 7 HOH 634 2034 802  HOH HOH A . 
S 7 HOH 635 2035 522  HOH HOH A . 
S 7 HOH 636 2036 203  HOH HOH A . 
S 7 HOH 637 2037 1428 HOH HOH A . 
S 7 HOH 638 2038 1590 HOH HOH A . 
S 7 HOH 639 2039 270  HOH HOH A . 
S 7 HOH 640 2040 1191 HOH HOH A . 
S 7 HOH 641 2041 3006 HOH HOH A . 
S 7 HOH 642 2042 2001 HOH HOH A . 
S 7 HOH 643 2043 1521 HOH HOH A . 
S 7 HOH 644 2044 1580 HOH HOH A . 
S 7 HOH 645 2045 734  HOH HOH A . 
S 7 HOH 646 2046 1221 HOH HOH A . 
S 7 HOH 647 2047 1463 HOH HOH A . 
S 7 HOH 648 2048 632  HOH HOH A . 
S 7 HOH 649 2049 600  HOH HOH A . 
S 7 HOH 650 2050 574  HOH HOH A . 
S 7 HOH 651 2051 470  HOH HOH A . 
S 7 HOH 652 2052 1455 HOH HOH A . 
S 7 HOH 653 2053 569  HOH HOH A . 
S 7 HOH 654 2054 1737 HOH HOH A . 
S 7 HOH 655 2055 1982 HOH HOH A . 
S 7 HOH 656 2056 1391 HOH HOH A . 
S 7 HOH 657 2057 387  HOH HOH A . 
S 7 HOH 658 2058 873  HOH HOH A . 
S 7 HOH 659 2059 708  HOH HOH A . 
S 7 HOH 660 2060 1720 HOH HOH A . 
S 7 HOH 661 2061 1470 HOH HOH A . 
S 7 HOH 662 2062 578  HOH HOH A . 
S 7 HOH 663 2063 38   HOH HOH A . 
S 7 HOH 664 2064 603  HOH HOH A . 
S 7 HOH 665 2065 686  HOH HOH A . 
S 7 HOH 666 2066 1689 HOH HOH A . 
S 7 HOH 667 2067 1244 HOH HOH A . 
S 7 HOH 668 2068 611  HOH HOH A . 
S 7 HOH 669 2069 242  HOH HOH A . 
S 7 HOH 670 2070 557  HOH HOH A . 
S 7 HOH 671 2071 89   HOH HOH A . 
S 7 HOH 672 2072 761  HOH HOH A . 
S 7 HOH 673 2073 685  HOH HOH A . 
S 7 HOH 674 2074 1854 HOH HOH A . 
S 7 HOH 675 2075 1484 HOH HOH A . 
S 7 HOH 676 2076 621  HOH HOH A . 
S 7 HOH 677 2077 246  HOH HOH A . 
S 7 HOH 678 2078 290  HOH HOH A . 
S 7 HOH 679 2079 1538 HOH HOH A . 
S 7 HOH 680 2080 529  HOH HOH A . 
S 7 HOH 681 2081 787  HOH HOH A . 
S 7 HOH 682 2082 350  HOH HOH A . 
S 7 HOH 683 2083 1557 HOH HOH A . 
S 7 HOH 684 2084 1765 HOH HOH A . 
S 7 HOH 685 2085 887  HOH HOH A . 
S 7 HOH 686 2086 241  HOH HOH A . 
S 7 HOH 687 2087 1335 HOH HOH A . 
S 7 HOH 688 2088 334  HOH HOH A . 
S 7 HOH 689 2089 184  HOH HOH A . 
S 7 HOH 690 2090 1828 HOH HOH A . 
S 7 HOH 691 2091 417  HOH HOH A . 
S 7 HOH 692 2092 377  HOH HOH A . 
S 7 HOH 693 2093 483  HOH HOH A . 
S 7 HOH 694 2094 1421 HOH HOH A . 
S 7 HOH 695 2095 1633 HOH HOH A . 
S 7 HOH 696 2096 820  HOH HOH A . 
S 7 HOH 697 2097 465  HOH HOH A . 
S 7 HOH 698 2098 659  HOH HOH A . 
S 7 HOH 699 2099 1213 HOH HOH A . 
S 7 HOH 700 2100 1329 HOH HOH A . 
S 7 HOH 701 2101 1070 HOH HOH A . 
S 7 HOH 702 2102 1443 HOH HOH A . 
S 7 HOH 703 2103 925  HOH HOH A . 
S 7 HOH 704 2104 769  HOH HOH A . 
S 7 HOH 705 2105 260  HOH HOH A . 
S 7 HOH 706 2106 1485 HOH HOH A . 
S 7 HOH 707 2107 1625 HOH HOH A . 
S 7 HOH 708 2108 539  HOH HOH A . 
S 7 HOH 709 2109 1594 HOH HOH A . 
S 7 HOH 710 2110 1197 HOH HOH A . 
S 7 HOH 711 2111 1998 HOH HOH A . 
S 7 HOH 712 2112 1530 HOH HOH A . 
S 7 HOH 713 2113 2004 HOH HOH A . 
S 7 HOH 714 2114 707  HOH HOH A . 
S 7 HOH 715 2115 85   HOH HOH A . 
S 7 HOH 716 2116 1450 HOH HOH A . 
S 7 HOH 717 2117 2043 HOH HOH A . 
S 7 HOH 718 2118 725  HOH HOH A . 
S 7 HOH 719 2119 1192 HOH HOH A . 
S 7 HOH 720 2120 1626 HOH HOH A . 
S 7 HOH 721 2121 572  HOH HOH A . 
S 7 HOH 722 2122 36   HOH HOH A . 
S 7 HOH 723 2123 1297 HOH HOH A . 
S 7 HOH 724 2124 489  HOH HOH A . 
S 7 HOH 725 2125 295  HOH HOH A . 
S 7 HOH 726 2126 1736 HOH HOH A . 
S 7 HOH 727 2127 1827 HOH HOH A . 
S 7 HOH 728 2128 449  HOH HOH A . 
S 7 HOH 729 2129 781  HOH HOH A . 
S 7 HOH 730 2130 1651 HOH HOH A . 
S 7 HOH 731 2131 2091 HOH HOH A . 
S 7 HOH 732 2132 743  HOH HOH A . 
S 7 HOH 733 2133 957  HOH HOH A . 
S 7 HOH 734 2134 1235 HOH HOH A . 
S 7 HOH 735 2135 1019 HOH HOH A . 
S 7 HOH 736 2136 1140 HOH HOH A . 
S 7 HOH 737 2137 1941 HOH HOH A . 
S 7 HOH 738 2138 94   HOH HOH A . 
S 7 HOH 739 2139 1835 HOH HOH A . 
S 7 HOH 740 2140 2040 HOH HOH A . 
S 7 HOH 741 2141 638  HOH HOH A . 
S 7 HOH 742 2142 1714 HOH HOH A . 
S 7 HOH 743 2143 1636 HOH HOH A . 
S 7 HOH 744 2144 863  HOH HOH A . 
S 7 HOH 745 2145 1704 HOH HOH A . 
S 7 HOH 746 2146 1394 HOH HOH A . 
S 7 HOH 747 2147 962  HOH HOH A . 
S 7 HOH 748 2148 563  HOH HOH A . 
S 7 HOH 749 2149 553  HOH HOH A . 
S 7 HOH 750 2150 1930 HOH HOH A . 
S 7 HOH 751 2151 1677 HOH HOH A . 
S 7 HOH 752 2152 1780 HOH HOH A . 
S 7 HOH 753 2153 1249 HOH HOH A . 
S 7 HOH 754 2154 2041 HOH HOH A . 
S 7 HOH 755 2155 969  HOH HOH A . 
S 7 HOH 756 2156 394  HOH HOH A . 
S 7 HOH 757 2157 2063 HOH HOH A . 
S 7 HOH 758 2158 817  HOH HOH A . 
S 7 HOH 759 2159 1407 HOH HOH A . 
S 7 HOH 760 2160 780  HOH HOH A . 
S 7 HOH 761 2161 361  HOH HOH A . 
S 7 HOH 762 2162 1650 HOH HOH A . 
S 7 HOH 763 2163 486  HOH HOH A . 
S 7 HOH 764 2164 1223 HOH HOH A . 
S 7 HOH 765 2165 1775 HOH HOH A . 
S 7 HOH 766 2166 1957 HOH HOH A . 
S 7 HOH 767 2167 1445 HOH HOH A . 
S 7 HOH 768 2168 1629 HOH HOH A . 
S 7 HOH 769 2169 745  HOH HOH A . 
S 7 HOH 770 2170 1766 HOH HOH A . 
S 7 HOH 771 2171 846  HOH HOH A . 
S 7 HOH 772 2172 518  HOH HOH A . 
S 7 HOH 773 2173 1848 HOH HOH A . 
S 7 HOH 774 2174 695  HOH HOH A . 
S 7 HOH 775 2175 3015 HOH HOH A . 
S 7 HOH 776 2176 963  HOH HOH A . 
S 7 HOH 777 2177 1634 HOH HOH A . 
S 7 HOH 778 2178 485  HOH HOH A . 
S 7 HOH 779 2179 442  HOH HOH A . 
S 7 HOH 780 2180 1692 HOH HOH A . 
S 7 HOH 781 2181 1051 HOH HOH A . 
S 7 HOH 782 2182 965  HOH HOH A . 
S 7 HOH 783 2183 1721 HOH HOH A . 
S 7 HOH 784 2184 1271 HOH HOH A . 
S 7 HOH 785 2185 1691 HOH HOH A . 
S 7 HOH 786 2186 1239 HOH HOH A . 
S 7 HOH 787 2187 1229 HOH HOH A . 
S 7 HOH 788 2188 266  HOH HOH A . 
S 7 HOH 789 2189 926  HOH HOH A . 
S 7 HOH 790 2190 1597 HOH HOH A . 
S 7 HOH 791 2191 772  HOH HOH A . 
S 7 HOH 792 2192 932  HOH HOH A . 
S 7 HOH 793 2193 1274 HOH HOH A . 
S 7 HOH 794 2194 1257 HOH HOH A . 
S 7 HOH 795 2195 1769 HOH HOH A . 
S 7 HOH 796 2196 1996 HOH HOH A . 
S 7 HOH 797 2197 1914 HOH HOH A . 
S 7 HOH 798 2198 1240 HOH HOH A . 
S 7 HOH 799 2199 3022 HOH HOH A . 
S 7 HOH 800 2200 876  HOH HOH A . 
S 7 HOH 801 2201 1972 HOH HOH A . 
S 7 HOH 802 2202 3020 HOH HOH A . 
S 7 HOH 803 2203 1695 HOH HOH A . 
S 7 HOH 804 2204 839  HOH HOH A . 
S 7 HOH 805 2205 1851 HOH HOH A . 
S 7 HOH 806 2206 571  HOH HOH A . 
S 7 HOH 807 2207 1056 HOH HOH A . 
S 7 HOH 808 2208 1508 HOH HOH A . 
S 7 HOH 809 2209 1298 HOH HOH A . 
S 7 HOH 810 2210 1132 HOH HOH A . 
S 7 HOH 811 2211 1326 HOH HOH A . 
S 7 HOH 812 2212 916  HOH HOH A . 
S 7 HOH 813 2213 1943 HOH HOH A . 
S 7 HOH 814 2214 1889 HOH HOH A . 
S 7 HOH 815 2215 2078 HOH HOH A . 
S 7 HOH 816 2216 928  HOH HOH A . 
S 7 HOH 817 2217 1975 HOH HOH A . 
S 7 HOH 818 2218 2037 HOH HOH A . 
S 7 HOH 819 2219 464  HOH HOH A . 
S 7 HOH 820 2220 1847 HOH HOH A . 
S 7 HOH 821 2221 1226 HOH HOH A . 
S 7 HOH 822 2222 2087 HOH HOH A . 
S 7 HOH 823 2223 1152 HOH HOH A . 
S 7 HOH 824 2224 583  HOH HOH A . 
S 7 HOH 825 2225 1109 HOH HOH A . 
S 7 HOH 826 2226 1122 HOH HOH A . 
S 7 HOH 827 2227 691  HOH HOH A . 
S 7 HOH 828 2228 1331 HOH HOH A . 
S 7 HOH 829 2229 1983 HOH HOH A . 
S 7 HOH 830 2230 1116 HOH HOH A . 
S 7 HOH 831 2231 1753 HOH HOH A . 
S 7 HOH 832 2232 821  HOH HOH A . 
S 7 HOH 833 2233 751  HOH HOH A . 
S 7 HOH 834 2234 1900 HOH HOH A . 
S 7 HOH 835 2235 626  HOH HOH A . 
S 7 HOH 836 2236 1214 HOH HOH A . 
S 7 HOH 837 2237 3035 HOH HOH A . 
S 7 HOH 838 2238 709  HOH HOH A . 
S 7 HOH 839 2239 1942 HOH HOH A . 
S 7 HOH 840 2240 2015 HOH HOH A . 
S 7 HOH 841 2241 923  HOH HOH A . 
S 7 HOH 842 2242 466  HOH HOH A . 
S 7 HOH 843 2243 933  HOH HOH A . 
S 7 HOH 844 2244 2053 HOH HOH A . 
S 7 HOH 845 2245 1857 HOH HOH A . 
S 7 HOH 846 2246 435  HOH HOH A . 
S 7 HOH 847 2247 794  HOH HOH A . 
S 7 HOH 848 2248 240  HOH HOH A . 
S 7 HOH 849 2249 570  HOH HOH A . 
S 7 HOH 850 2250 1550 HOH HOH A . 
S 7 HOH 851 2251 445  HOH HOH A . 
S 7 HOH 852 2252 666  HOH HOH A . 
S 7 HOH 853 2253 329  HOH HOH A . 
S 7 HOH 854 2254 1552 HOH HOH A . 
S 7 HOH 855 2255 2054 HOH HOH A . 
S 7 HOH 856 2256 803  HOH HOH A . 
S 7 HOH 857 2257 149  HOH HOH A . 
S 7 HOH 858 2258 948  HOH HOH A . 
S 7 HOH 859 2259 1910 HOH HOH A . 
S 7 HOH 860 2260 1144 HOH HOH A . 
S 7 HOH 861 2261 512  HOH HOH A . 
S 7 HOH 862 2262 1859 HOH HOH A . 
S 7 HOH 863 2263 1891 HOH HOH A . 
S 7 HOH 864 2264 1805 HOH HOH A . 
S 7 HOH 865 2265 1309 HOH HOH A . 
S 7 HOH 866 2266 1855 HOH HOH A . 
S 7 HOH 867 2267 1974 HOH HOH A . 
S 7 HOH 868 2268 1212 HOH HOH A . 
S 7 HOH 869 2269 1514 HOH HOH A . 
S 7 HOH 870 2270 788  HOH HOH A . 
S 7 HOH 871 2271 2038 HOH HOH A . 
S 7 HOH 872 2272 528  HOH HOH A . 
S 7 HOH 873 2273 213  HOH HOH A . 
S 7 HOH 874 2274 652  HOH HOH A . 
S 7 HOH 875 2275 2005 HOH HOH A . 
S 7 HOH 876 2276 546  HOH HOH A . 
S 7 HOH 877 2277 1205 HOH HOH A . 
S 7 HOH 878 2278 1190 HOH HOH A . 
S 7 HOH 879 2279 664  HOH HOH A . 
S 7 HOH 880 2280 1789 HOH HOH A . 
S 7 HOH 881 2281 1293 HOH HOH A . 
S 7 HOH 882 2282 597  HOH HOH A . 
S 7 HOH 883 2283 526  HOH HOH A . 
S 7 HOH 884 2284 814  HOH HOH A . 
S 7 HOH 885 2285 682  HOH HOH A . 
S 7 HOH 886 2286 1110 HOH HOH A . 
S 7 HOH 887 2287 1261 HOH HOH A . 
S 7 HOH 888 2288 905  HOH HOH A . 
S 7 HOH 889 2289 2055 HOH HOH A . 
S 7 HOH 890 2290 1268 HOH HOH A . 
S 7 HOH 891 2291 1133 HOH HOH A . 
S 7 HOH 892 2292 977  HOH HOH A . 
S 7 HOH 893 2293 1992 HOH HOH A . 
S 7 HOH 894 2294 3005 HOH HOH A . 
S 7 HOH 895 2295 1663 HOH HOH A . 
S 7 HOH 896 2296 1435 HOH HOH A . 
S 7 HOH 897 2297 999  HOH HOH A . 
S 7 HOH 898 2298 1183 HOH HOH A . 
S 7 HOH 899 2299 1566 HOH HOH A . 
S 7 HOH 900 2300 1929 HOH HOH A . 
S 7 HOH 901 2301 1575 HOH HOH A . 
S 7 HOH 902 2302 677  HOH HOH A . 
S 7 HOH 903 2303 797  HOH HOH A . 
S 7 HOH 904 2304 1671 HOH HOH A . 
S 7 HOH 905 2305 1886 HOH HOH A . 
S 7 HOH 906 2306 2028 HOH HOH A . 
S 7 HOH 907 2307 1245 HOH HOH A . 
S 7 HOH 908 2308 1327 HOH HOH A . 
S 7 HOH 909 2309 692  HOH HOH A . 
S 7 HOH 910 2310 1130 HOH HOH A . 
S 7 HOH 911 2311 480  HOH HOH A . 
S 7 HOH 912 2312 1054 HOH HOH A . 
S 7 HOH 913 2313 1569 HOH HOH A . 
S 7 HOH 914 2314 1898 HOH HOH A . 
S 7 HOH 915 2315 477  HOH HOH A . 
S 7 HOH 916 2316 777  HOH HOH A . 
S 7 HOH 917 2317 1578 HOH HOH A . 
S 7 HOH 918 2318 218  HOH HOH A . 
S 7 HOH 919 2319 1344 HOH HOH A . 
S 7 HOH 920 2320 1551 HOH HOH A . 
S 7 HOH 921 2321 1831 HOH HOH A . 
S 7 HOH 922 2322 909  HOH HOH A . 
S 7 HOH 923 2323 1829 HOH HOH A . 
S 7 HOH 924 2324 973  HOH HOH A . 
S 7 HOH 925 2325 960  HOH HOH A . 
S 7 HOH 926 2326 3008 HOH HOH A . 
S 7 HOH 927 2327 1924 HOH HOH A . 
S 7 HOH 928 2328 1977 HOH HOH A . 
S 7 HOH 929 2329 1858 HOH HOH A . 
S 7 HOH 930 2330 1853 HOH HOH A . 
S 7 HOH 931 2331 640  HOH HOH A . 
S 7 HOH 932 2332 966  HOH HOH A . 
S 7 HOH 933 2333 2029 HOH HOH A . 
S 7 HOH 934 2334 1787 HOH HOH A . 
S 7 HOH 935 2335 1788 HOH HOH A . 
S 7 HOH 936 2336 1945 HOH HOH A . 
S 7 HOH 937 2337 2016 HOH HOH A . 
S 7 HOH 938 2338 1586 HOH HOH A . 
S 7 HOH 939 2339 717  HOH HOH A . 
S 7 HOH 940 2340 759  HOH HOH A . 
S 7 HOH 941 2341 2031 HOH HOH A . 
S 7 HOH 942 2342 1616 HOH HOH A . 
S 7 HOH 943 2343 1570 HOH HOH A . 
S 7 HOH 944 2344 1932 HOH HOH A . 
S 7 HOH 945 2345 2051 HOH HOH A . 
S 7 HOH 946 2346 1846 HOH HOH A . 
S 7 HOH 947 2347 1909 HOH HOH A . 
S 7 HOH 948 2348 636  HOH HOH A . 
S 7 HOH 949 2349 1086 HOH HOH A . 
S 7 HOH 950 2350 468  HOH HOH A . 
S 7 HOH 951 2351 903  HOH HOH A . 
S 7 HOH 952 2352 1301 HOH HOH A . 
S 7 HOH 953 2353 1043 HOH HOH A . 
S 7 HOH 954 2354 1607 HOH HOH A . 
S 7 HOH 955 2355 2044 HOH HOH A . 
S 7 HOH 956 2356 656  HOH HOH A . 
S 7 HOH 957 2357 2057 HOH HOH A . 
S 7 HOH 958 2358 1291 HOH HOH A . 
S 7 HOH 959 2359 813  HOH HOH A . 
S 7 HOH 960 2360 310  HOH HOH A . 
S 7 HOH 961 2361 1263 HOH HOH A . 
S 7 HOH 962 2362 1107 HOH HOH A . 
S 7 HOH 963 2363 919  HOH HOH A . 
S 7 HOH 964 2364 108  HOH HOH A . 
S 7 HOH 965 2365 1965 HOH HOH A . 
S 7 HOH 966 2366 729  HOH HOH A . 
S 7 HOH 967 2367 1800 HOH HOH A . 
S 7 HOH 968 2368 967  HOH HOH A . 
S 7 HOH 969 2369 1577 HOH HOH A . 
S 7 HOH 970 2370 1836 HOH HOH A . 
S 7 HOH 971 2371 1928 HOH HOH A . 
S 7 HOH 972 2372 917  HOH HOH A . 
S 7 HOH 973 2373 1522 HOH HOH A . 
S 7 HOH 974 2374 1893 HOH HOH A . 
S 7 HOH 975 2375 956  HOH HOH A . 
S 7 HOH 976 2376 1993 HOH HOH A . 
S 7 HOH 977 2377 1602 HOH HOH A . 
S 7 HOH 978 2378 1305 HOH HOH A . 
S 7 HOH 979 2379 1899 HOH HOH A . 
S 7 HOH 980 2380 1591 HOH HOH A . 
S 7 HOH 981 2381 949  HOH HOH A . 
S 7 HOH 982 2382 1908 HOH HOH A . 
S 7 HOH 983 2383 1289 HOH HOH A . 
S 7 HOH 984 2384 2002 HOH HOH A . 
S 7 HOH 985 2385 418  HOH HOH A . 
S 7 HOH 986 2386 1801 HOH HOH A . 
S 7 HOH 987 2387 1074 HOH HOH A . 
S 7 HOH 988 2388 2080 HOH HOH A . 
S 7 HOH 989 2389 790  HOH HOH A . 
S 7 HOH 990 2390 2069 HOH HOH A . 
S 7 HOH 991 2391 766  HOH HOH A . 
S 7 HOH 992 2392 2070 HOH HOH A . 
S 7 HOH 993 2393 924  HOH HOH A . 
S 7 HOH 994 2394 1952 HOH HOH A . 
S 7 HOH 995 2395 1003 HOH HOH A . 
T 7 HOH 1   1401 1925 HOH HOH B . 
T 7 HOH 2   1402 2088 HOH HOH B . 
T 7 HOH 3   1403 1865 HOH HOH B . 
T 7 HOH 4   1404 1839 HOH HOH B . 
T 7 HOH 5   1405 2007 HOH HOH B . 
T 7 HOH 6   1406 1860 HOH HOH B . 
T 7 HOH 7   1407 1833 HOH HOH B . 
T 7 HOH 8   1408 1621 HOH HOH B . 
T 7 HOH 9   1409 1978 HOH HOH B . 
T 7 HOH 10  1410 3007 HOH HOH B . 
T 7 HOH 11  1411 1904 HOH HOH B . 
T 7 HOH 12  1412 1919 HOH HOH B . 
T 7 HOH 13  1413 1940 HOH HOH B . 
T 7 HOH 14  1414 1870 HOH HOH B . 
T 7 HOH 15  1415 1966 HOH HOH B . 
T 7 HOH 16  1416 1813 HOH HOH B . 
T 7 HOH 17  1417 1873 HOH HOH B . 
T 7 HOH 18  1418 1454 HOH HOH B . 
T 7 HOH 19  1419 750  HOH HOH B . 
T 7 HOH 20  1420 1817 HOH HOH B . 
T 7 HOH 21  1421 1596 HOH HOH B . 
T 7 HOH 22  1422 1938 HOH HOH B . 
T 7 HOH 23  1423 1905 HOH HOH B . 
T 7 HOH 24  1424 2039 HOH HOH B . 
T 7 HOH 25  1425 3033 HOH HOH B . 
T 7 HOH 26  1426 1409 HOH HOH B . 
T 7 HOH 27  1427 1888 HOH HOH B . 
T 7 HOH 28  1428 1448 HOH HOH B . 
T 7 HOH 29  1429 1842 HOH HOH B . 
T 7 HOH 30  1430 1876 HOH HOH B . 
T 7 HOH 31  1431 1903 HOH HOH B . 
T 7 HOH 32  1432 823  HOH HOH B . 
T 7 HOH 33  1433 1467 HOH HOH B . 
T 7 HOH 34  1434 848  HOH HOH B . 
T 7 HOH 35  1435 1796 HOH HOH B . 
T 7 HOH 36  1436 1361 HOH HOH B . 
T 7 HOH 37  1437 1867 HOH HOH B . 
T 7 HOH 38  1438 649  HOH HOH B . 
T 7 HOH 39  1439 1093 HOH HOH B . 
T 7 HOH 40  1440 1882 HOH HOH B . 
T 7 HOH 41  1441 1901 HOH HOH B . 
T 7 HOH 42  1442 1794 HOH HOH B . 
T 7 HOH 43  1443 1200 HOH HOH B . 
T 7 HOH 44  1444 1845 HOH HOH B . 
T 7 HOH 45  1445 676  HOH HOH B . 
T 7 HOH 46  1446 1883 HOH HOH B . 
T 7 HOH 47  1447 1415 HOH HOH B . 
T 7 HOH 48  1448 906  HOH HOH B . 
T 7 HOH 49  1449 1933 HOH HOH B . 
T 7 HOH 50  1450 1967 HOH HOH B . 
T 7 HOH 51  1451 806  HOH HOH B . 
T 7 HOH 52  1452 1743 HOH HOH B . 
T 7 HOH 53  1453 1382 HOH HOH B . 
T 7 HOH 54  1454 296  HOH HOH B . 
T 7 HOH 55  1455 1519 HOH HOH B . 
T 7 HOH 56  1456 1895 HOH HOH B . 
T 7 HOH 57  1457 1368 HOH HOH B . 
T 7 HOH 58  1458 1115 HOH HOH B . 
T 7 HOH 59  1459 491  HOH HOH B . 
T 7 HOH 60  1460 1613 HOH HOH B . 
T 7 HOH 61  1461 1376 HOH HOH B . 
T 7 HOH 62  1462 591  HOH HOH B . 
T 7 HOH 63  1463 2079 HOH HOH B . 
T 7 HOH 64  1464 1511 HOH HOH B . 
T 7 HOH 65  1465 1802 HOH HOH B . 
T 7 HOH 66  1466 1868 HOH HOH B . 
T 7 HOH 67  1467 825  HOH HOH B . 
T 7 HOH 68  1468 981  HOH HOH B . 
T 7 HOH 69  1469 1528 HOH HOH B . 
T 7 HOH 70  1470 1357 HOH HOH B . 
T 7 HOH 71  1471 1936 HOH HOH B . 
T 7 HOH 72  1472 1028 HOH HOH B . 
T 7 HOH 73  1473 1682 HOH HOH B . 
T 7 HOH 74  1474 1593 HOH HOH B . 
T 7 HOH 75  1475 521  HOH HOH B . 
T 7 HOH 76  1476 441  HOH HOH B . 
T 7 HOH 77  1477 1164 HOH HOH B . 
T 7 HOH 78  1478 1033 HOH HOH B . 
T 7 HOH 79  1479 3021 HOH HOH B . 
T 7 HOH 80  1480 1356 HOH HOH B . 
T 7 HOH 81  1481 867  HOH HOH B . 
T 7 HOH 82  1482 1554 HOH HOH B . 
T 7 HOH 83  1483 791  HOH HOH B . 
T 7 HOH 84  1484 897  HOH HOH B . 
T 7 HOH 85  1485 508  HOH HOH B . 
T 7 HOH 86  1486 1777 HOH HOH B . 
T 7 HOH 87  1487 1112 HOH HOH B . 
T 7 HOH 88  1488 1359 HOH HOH B . 
T 7 HOH 89  1489 1605 HOH HOH B . 
T 7 HOH 90  1490 1878 HOH HOH B . 
T 7 HOH 91  1491 837  HOH HOH B . 
T 7 HOH 92  1492 430  HOH HOH B . 
T 7 HOH 93  1493 411  HOH HOH B . 
T 7 HOH 94  1494 1057 HOH HOH B . 
T 7 HOH 95  1495 1881 HOH HOH B . 
T 7 HOH 96  1496 1494 HOH HOH B . 
T 7 HOH 97  1497 10   HOH HOH B . 
T 7 HOH 98  1498 1401 HOH HOH B . 
T 7 HOH 99  1499 1446 HOH HOH B . 
T 7 HOH 100 1500 1990 HOH HOH B . 
T 7 HOH 101 1501 852  HOH HOH B . 
T 7 HOH 102 1502 2049 HOH HOH B . 
T 7 HOH 103 1503 1022 HOH HOH B . 
T 7 HOH 104 1504 2019 HOH HOH B . 
T 7 HOH 105 1505 2012 HOH HOH B . 
T 7 HOH 106 1506 920  HOH HOH B . 
T 7 HOH 107 1507 1150 HOH HOH B . 
T 7 HOH 108 1508 1638 HOH HOH B . 
T 7 HOH 109 1509 455  HOH HOH B . 
T 7 HOH 110 1510 29   HOH HOH B . 
T 7 HOH 111 1511 1366 HOH HOH B . 
T 7 HOH 112 1512 1810 HOH HOH B . 
T 7 HOH 113 1513 1515 HOH HOH B . 
T 7 HOH 114 1514 327  HOH HOH B . 
T 7 HOH 115 1515 5    HOH HOH B . 
T 7 HOH 116 1516 1412 HOH HOH B . 
T 7 HOH 117 1517 1038 HOH HOH B . 
T 7 HOH 118 1518 499  HOH HOH B . 
T 7 HOH 119 1519 1425 HOH HOH B . 
T 7 HOH 120 1520 1862 HOH HOH B . 
T 7 HOH 121 1521 869  HOH HOH B . 
T 7 HOH 122 1522 1138 HOH HOH B . 
T 7 HOH 123 1523 607  HOH HOH B . 
T 7 HOH 124 1524 1207 HOH HOH B . 
T 7 HOH 125 1525 598  HOH HOH B . 
T 7 HOH 126 1526 1383 HOH HOH B . 
T 7 HOH 127 1527 653  HOH HOH B . 
T 7 HOH 128 1528 531  HOH HOH B . 
T 7 HOH 129 1529 1396 HOH HOH B . 
T 7 HOH 130 1530 1040 HOH HOH B . 
T 7 HOH 131 1531 1030 HOH HOH B . 
T 7 HOH 132 1532 1573 HOH HOH B . 
T 7 HOH 133 1533 1741 HOH HOH B . 
T 7 HOH 134 1534 1059 HOH HOH B . 
T 7 HOH 135 1535 79   HOH HOH B . 
T 7 HOH 136 1536 433  HOH HOH B . 
T 7 HOH 137 1537 713  HOH HOH B . 
T 7 HOH 138 1538 448  HOH HOH B . 
T 7 HOH 139 1539 1562 HOH HOH B . 
T 7 HOH 140 1540 1091 HOH HOH B . 
T 7 HOH 141 1541 1201 HOH HOH B . 
T 7 HOH 142 1542 261  HOH HOH B . 
T 7 HOH 143 1543 1902 HOH HOH B . 
T 7 HOH 144 1544 712  HOH HOH B . 
T 7 HOH 145 1545 409  HOH HOH B . 
T 7 HOH 146 1546 756  HOH HOH B . 
T 7 HOH 147 1547 201  HOH HOH B . 
T 7 HOH 148 1548 1049 HOH HOH B . 
T 7 HOH 149 1549 560  HOH HOH B . 
T 7 HOH 150 1550 755  HOH HOH B . 
T 7 HOH 151 1551 899  HOH HOH B . 
T 7 HOH 152 1552 2009 HOH HOH B . 
T 7 HOH 153 1553 1645 HOH HOH B . 
T 7 HOH 154 1554 1072 HOH HOH B . 
T 7 HOH 155 1555 1377 HOH HOH B . 
T 7 HOH 156 1556 1198 HOH HOH B . 
T 7 HOH 157 1557 269  HOH HOH B . 
T 7 HOH 158 1558 1459 HOH HOH B . 
T 7 HOH 159 1559 601  HOH HOH B . 
T 7 HOH 160 1560 402  HOH HOH B . 
T 7 HOH 161 1561 1204 HOH HOH B . 
T 7 HOH 162 1562 253  HOH HOH B . 
T 7 HOH 163 1563 764  HOH HOH B . 
T 7 HOH 164 1564 860  HOH HOH B . 
T 7 HOH 165 1565 1770 HOH HOH B . 
T 7 HOH 166 1566 877  HOH HOH B . 
T 7 HOH 167 1567 604  HOH HOH B . 
T 7 HOH 168 1568 1343 HOH HOH B . 
T 7 HOH 169 1569 716  HOH HOH B . 
T 7 HOH 170 1570 1069 HOH HOH B . 
T 7 HOH 171 1571 1433 HOH HOH B . 
T 7 HOH 172 1572 970  HOH HOH B . 
T 7 HOH 173 1573 1533 HOH HOH B . 
T 7 HOH 174 1574 857  HOH HOH B . 
T 7 HOH 175 1575 308  HOH HOH B . 
T 7 HOH 176 1576 250  HOH HOH B . 
T 7 HOH 177 1577 1680 HOH HOH B . 
T 7 HOH 178 1578 1360 HOH HOH B . 
T 7 HOH 179 1579 1386 HOH HOH B . 
T 7 HOH 180 1580 1254 HOH HOH B . 
T 7 HOH 181 1581 77   HOH HOH B . 
T 7 HOH 182 1582 990  HOH HOH B . 
T 7 HOH 183 1583 1980 HOH HOH B . 
T 7 HOH 184 1584 43   HOH HOH B . 
T 7 HOH 185 1585 3019 HOH HOH B . 
T 7 HOH 186 1586 818  HOH HOH B . 
T 7 HOH 187 1587 422  HOH HOH B . 
T 7 HOH 188 1588 1701 HOH HOH B . 
T 7 HOH 189 1589 507  HOH HOH B . 
T 7 HOH 190 1590 137  HOH HOH B . 
T 7 HOH 191 1591 206  HOH HOH B . 
T 7 HOH 192 1592 113  HOH HOH B . 
T 7 HOH 193 1593 647  HOH HOH B . 
T 7 HOH 194 1594 53   HOH HOH B . 
T 7 HOH 195 1595 748  HOH HOH B . 
T 7 HOH 196 1596 1053 HOH HOH B . 
T 7 HOH 197 1597 2014 HOH HOH B . 
T 7 HOH 198 1598 1740 HOH HOH B . 
T 7 HOH 199 1599 45   HOH HOH B . 
T 7 HOH 200 1600 1374 HOH HOH B . 
T 7 HOH 201 1601 278  HOH HOH B . 
T 7 HOH 202 1602 1507 HOH HOH B . 
T 7 HOH 203 1603 1781 HOH HOH B . 
T 7 HOH 204 1604 1963 HOH HOH B . 
T 7 HOH 205 1605 119  HOH HOH B . 
T 7 HOH 206 1606 407  HOH HOH B . 
T 7 HOH 207 1607 1076 HOH HOH B . 
T 7 HOH 208 1608 251  HOH HOH B . 
T 7 HOH 209 1609 197  HOH HOH B . 
T 7 HOH 210 1610 880  HOH HOH B . 
T 7 HOH 211 1611 517  HOH HOH B . 
T 7 HOH 212 1612 1495 HOH HOH B . 
T 7 HOH 213 1613 843  HOH HOH B . 
T 7 HOH 214 1614 187  HOH HOH B . 
T 7 HOH 215 1615 845  HOH HOH B . 
T 7 HOH 216 1616 726  HOH HOH B . 
T 7 HOH 217 1617 850  HOH HOH B . 
T 7 HOH 218 1618 564  HOH HOH B . 
T 7 HOH 219 1619 413  HOH HOH B . 
T 7 HOH 220 1620 47   HOH HOH B . 
T 7 HOH 221 1621 844  HOH HOH B . 
T 7 HOH 222 1622 1148 HOH HOH B . 
T 7 HOH 223 1623 1050 HOH HOH B . 
T 7 HOH 224 1624 6    HOH HOH B . 
T 7 HOH 225 1625 1375 HOH HOH B . 
T 7 HOH 226 1626 110  HOH HOH B . 
T 7 HOH 227 1627 97   HOH HOH B . 
T 7 HOH 228 1628 552  HOH HOH B . 
T 7 HOH 229 1629 447  HOH HOH B . 
T 7 HOH 230 1630 1281 HOH HOH B . 
T 7 HOH 231 1631 2036 HOH HOH B . 
T 7 HOH 232 1632 519  HOH HOH B . 
T 7 HOH 233 1633 88   HOH HOH B . 
T 7 HOH 234 1634 854  HOH HOH B . 
T 7 HOH 235 1635 620  HOH HOH B . 
T 7 HOH 236 1636 765  HOH HOH B . 
T 7 HOH 237 1637 1167 HOH HOH B . 
T 7 HOH 238 1638 2056 HOH HOH B . 
T 7 HOH 239 1639 2084 HOH HOH B . 
T 7 HOH 240 1640 216  HOH HOH B . 
T 7 HOH 241 1641 190  HOH HOH B . 
T 7 HOH 242 1642 826  HOH HOH B . 
T 7 HOH 243 1643 322  HOH HOH B . 
T 7 HOH 244 1644 739  HOH HOH B . 
T 7 HOH 245 1645 1384 HOH HOH B . 
T 7 HOH 246 1646 1046 HOH HOH B . 
T 7 HOH 247 1647 91   HOH HOH B . 
T 7 HOH 248 1648 3014 HOH HOH B . 
T 7 HOH 249 1649 2046 HOH HOH B . 
T 7 HOH 250 1650 117  HOH HOH B . 
T 7 HOH 251 1651 323  HOH HOH B . 
T 7 HOH 252 1652 1277 HOH HOH B . 
T 7 HOH 253 1653 1372 HOH HOH B . 
T 7 HOH 254 1654 881  HOH HOH B . 
T 7 HOH 255 1655 98   HOH HOH B . 
T 7 HOH 256 1656 316  HOH HOH B . 
T 7 HOH 257 1657 456  HOH HOH B . 
T 7 HOH 258 1658 326  HOH HOH B . 
T 7 HOH 259 1659 1546 HOH HOH B . 
T 7 HOH 260 1660 1558 HOH HOH B . 
T 7 HOH 261 1661 952  HOH HOH B . 
T 7 HOH 262 1662 1660 HOH HOH B . 
T 7 HOH 263 1663 61   HOH HOH B . 
T 7 HOH 264 1664 30   HOH HOH B . 
T 7 HOH 265 1665 31   HOH HOH B . 
T 7 HOH 266 1666 1276 HOH HOH B . 
T 7 HOH 267 1667 1156 HOH HOH B . 
T 7 HOH 268 1668 599  HOH HOH B . 
T 7 HOH 269 1669 1    HOH HOH B . 
T 7 HOH 270 1670 331  HOH HOH B . 
T 7 HOH 271 1671 1255 HOH HOH B . 
T 7 HOH 272 1672 885  HOH HOH B . 
T 7 HOH 273 1673 309  HOH HOH B . 
T 7 HOH 274 1674 328  HOH HOH B . 
T 7 HOH 275 1675 1027 HOH HOH B . 
T 7 HOH 276 1676 338  HOH HOH B . 
T 7 HOH 277 1677 738  HOH HOH B . 
T 7 HOH 278 1678 1716 HOH HOH B . 
T 7 HOH 279 1679 231  HOH HOH B . 
T 7 HOH 280 1680 1760 HOH HOH B . 
T 7 HOH 281 1681 363  HOH HOH B . 
T 7 HOH 282 1682 1106 HOH HOH B . 
T 7 HOH 283 1683 1082 HOH HOH B . 
T 7 HOH 284 1684 1416 HOH HOH B . 
T 7 HOH 285 1685 1432 HOH HOH B . 
T 7 HOH 286 1686 1079 HOH HOH B . 
T 7 HOH 287 1687 1322 HOH HOH B . 
T 7 HOH 288 1688 1399 HOH HOH B . 
T 7 HOH 289 1689 99   HOH HOH B . 
T 7 HOH 290 1690 547  HOH HOH B . 
T 7 HOH 291 1691 141  HOH HOH B . 
T 7 HOH 292 1692 391  HOH HOH B . 
T 7 HOH 293 1693 1537 HOH HOH B . 
T 7 HOH 294 1694 181  HOH HOH B . 
T 7 HOH 295 1695 2072 HOH HOH B . 
T 7 HOH 296 1696 891  HOH HOH B . 
T 7 HOH 297 1697 155  HOH HOH B . 
T 7 HOH 298 1698 1139 HOH HOH B . 
T 7 HOH 299 1699 2058 HOH HOH B . 
T 7 HOH 300 1700 1739 HOH HOH B . 
T 7 HOH 301 1701 259  HOH HOH B . 
T 7 HOH 302 1702 645  HOH HOH B . 
T 7 HOH 303 1703 293  HOH HOH B . 
T 7 HOH 304 1704 698  HOH HOH B . 
T 7 HOH 305 1705 503  HOH HOH B . 
T 7 HOH 306 1706 723  HOH HOH B . 
T 7 HOH 307 1707 57   HOH HOH B . 
T 7 HOH 308 1708 1280 HOH HOH B . 
T 7 HOH 309 1709 1075 HOH HOH B . 
T 7 HOH 310 1710 500  HOH HOH B . 
T 7 HOH 311 1711 114  HOH HOH B . 
T 7 HOH 312 1712 230  HOH HOH B . 
T 7 HOH 313 1713 128  HOH HOH B . 
T 7 HOH 314 1714 86   HOH HOH B . 
T 7 HOH 315 1715 1363 HOH HOH B . 
T 7 HOH 316 1716 4    HOH HOH B . 
T 7 HOH 317 1717 1392 HOH HOH B . 
T 7 HOH 318 1718 516  HOH HOH B . 
T 7 HOH 319 1719 312  HOH HOH B . 
T 7 HOH 320 1720 1687 HOH HOH B . 
T 7 HOH 321 1721 898  HOH HOH B . 
T 7 HOH 322 1722 21   HOH HOH B . 
T 7 HOH 323 1723 148  HOH HOH B . 
T 7 HOH 324 1724 1768 HOH HOH B . 
T 7 HOH 325 1725 80   HOH HOH B . 
T 7 HOH 326 1726 1954 HOH HOH B . 
T 7 HOH 327 1727 1609 HOH HOH B . 
T 7 HOH 328 1728 798  HOH HOH B . 
T 7 HOH 329 1729 60   HOH HOH B . 
T 7 HOH 330 1730 1803 HOH HOH B . 
T 7 HOH 331 1731 432  HOH HOH B . 
T 7 HOH 332 1732 1126 HOH HOH B . 
T 7 HOH 333 1733 484  HOH HOH B . 
T 7 HOH 334 1734 163  HOH HOH B . 
T 7 HOH 335 1735 884  HOH HOH B . 
T 7 HOH 336 1736 131  HOH HOH B . 
T 7 HOH 337 1737 1471 HOH HOH B . 
T 7 HOH 338 1738 706  HOH HOH B . 
T 7 HOH 339 1739 672  HOH HOH B . 
T 7 HOH 340 1740 913  HOH HOH B . 
T 7 HOH 341 1741 318  HOH HOH B . 
T 7 HOH 342 1742 65   HOH HOH B . 
T 7 HOH 343 1743 1256 HOH HOH B . 
T 7 HOH 344 1744 757  HOH HOH B . 
T 7 HOH 345 1745 1746 HOH HOH B . 
T 7 HOH 346 1746 183  HOH HOH B . 
T 7 HOH 347 1747 388  HOH HOH B . 
T 7 HOH 348 1748 1694 HOH HOH B . 
T 7 HOH 349 1749 2062 HOH HOH B . 
T 7 HOH 350 1750 398  HOH HOH B . 
T 7 HOH 351 1751 619  HOH HOH B . 
T 7 HOH 352 1752 1427 HOH HOH B . 
T 7 HOH 353 1753 438  HOH HOH B . 
T 7 HOH 354 1754 372  HOH HOH B . 
T 7 HOH 355 1755 424  HOH HOH B . 
T 7 HOH 356 1756 1604 HOH HOH B . 
T 7 HOH 357 1757 544  HOH HOH B . 
T 7 HOH 358 1758 2034 HOH HOH B . 
T 7 HOH 359 1759 346  HOH HOH B . 
T 7 HOH 360 1760 54   HOH HOH B . 
T 7 HOH 361 1761 1160 HOH HOH B . 
T 7 HOH 362 1762 831  HOH HOH B . 
T 7 HOH 363 1763 942  HOH HOH B . 
T 7 HOH 364 1764 198  HOH HOH B . 
T 7 HOH 365 1765 801  HOH HOH B . 
T 7 HOH 366 1766 146  HOH HOH B . 
T 7 HOH 367 1767 222  HOH HOH B . 
T 7 HOH 368 1768 324  HOH HOH B . 
T 7 HOH 369 1769 2064 HOH HOH B . 
T 7 HOH 370 1770 2    HOH HOH B . 
T 7 HOH 371 1771 733  HOH HOH B . 
T 7 HOH 372 1772 58   HOH HOH B . 
T 7 HOH 373 1773 423  HOH HOH B . 
T 7 HOH 374 1774 74   HOH HOH B . 
T 7 HOH 375 1775 109  HOH HOH B . 
T 7 HOH 376 1776 202  HOH HOH B . 
T 7 HOH 377 1777 151  HOH HOH B . 
T 7 HOH 378 1778 593  HOH HOH B . 
T 7 HOH 379 1779 648  HOH HOH B . 
T 7 HOH 380 1780 605  HOH HOH B . 
T 7 HOH 381 1781 1248 HOH HOH B . 
T 7 HOH 382 1782 209  HOH HOH B . 
T 7 HOH 383 1783 384  HOH HOH B . 
T 7 HOH 384 1784 1194 HOH HOH B . 
T 7 HOH 385 1785 1143 HOH HOH B . 
T 7 HOH 386 1786 42   HOH HOH B . 
T 7 HOH 387 1787 1793 HOH HOH B . 
T 7 HOH 388 1788 194  HOH HOH B . 
T 7 HOH 389 1789 379  HOH HOH B . 
T 7 HOH 390 1790 551  HOH HOH B . 
T 7 HOH 391 1791 1635 HOH HOH B . 
T 7 HOH 392 1792 1465 HOH HOH B . 
T 7 HOH 393 1793 1542 HOH HOH B . 
T 7 HOH 394 1794 1610 HOH HOH B . 
T 7 HOH 395 1795 1151 HOH HOH B . 
T 7 HOH 396 1796 332  HOH HOH B . 
T 7 HOH 397 1797 215  HOH HOH B . 
T 7 HOH 398 1798 1405 HOH HOH B . 
T 7 HOH 399 1799 1690 HOH HOH B . 
T 7 HOH 400 1800 1490 HOH HOH B . 
T 7 HOH 401 1801 1497 HOH HOH B . 
T 7 HOH 402 1802 390  HOH HOH B . 
T 7 HOH 403 1803 1529 HOH HOH B . 
T 7 HOH 404 1804 1711 HOH HOH B . 
T 7 HOH 405 1805 1020 HOH HOH B . 
T 7 HOH 406 1806 1193 HOH HOH B . 
T 7 HOH 407 1807 515  HOH HOH B . 
T 7 HOH 408 1808 1048 HOH HOH B . 
T 7 HOH 409 1809 39   HOH HOH B . 
T 7 HOH 410 1810 297  HOH HOH B . 
T 7 HOH 411 1811 538  HOH HOH B . 
T 7 HOH 412 1812 220  HOH HOH B . 
T 7 HOH 413 1813 81   HOH HOH B . 
T 7 HOH 414 1814 144  HOH HOH B . 
T 7 HOH 415 1815 1536 HOH HOH B . 
T 7 HOH 416 1816 983  HOH HOH B . 
T 7 HOH 417 1817 353  HOH HOH B . 
T 7 HOH 418 1818 900  HOH HOH B . 
T 7 HOH 419 1819 492  HOH HOH B . 
T 7 HOH 420 1820 1313 HOH HOH B . 
T 7 HOH 421 1821 13   HOH HOH B . 
T 7 HOH 422 1822 536  HOH HOH B . 
T 7 HOH 423 1823 1510 HOH HOH B . 
T 7 HOH 424 1824 758  HOH HOH B . 
T 7 HOH 425 1825 805  HOH HOH B . 
T 7 HOH 426 1826 1488 HOH HOH B . 
T 7 HOH 427 1827 2093 HOH HOH B . 
T 7 HOH 428 1828 25   HOH HOH B . 
T 7 HOH 429 1829 393  HOH HOH B . 
T 7 HOH 430 1830 1102 HOH HOH B . 
T 7 HOH 431 1831 912  HOH HOH B . 
T 7 HOH 432 1832 235  HOH HOH B . 
T 7 HOH 433 1833 1055 HOH HOH B . 
T 7 HOH 434 1834 1545 HOH HOH B . 
T 7 HOH 435 1835 1699 HOH HOH B . 
T 7 HOH 436 1836 23   HOH HOH B . 
T 7 HOH 437 1837 1403 HOH HOH B . 
T 7 HOH 438 1838 1761 HOH HOH B . 
T 7 HOH 439 1839 895  HOH HOH B . 
T 7 HOH 440 1840 1872 HOH HOH B . 
T 7 HOH 441 1841 627  HOH HOH B . 
T 7 HOH 442 1842 853  HOH HOH B . 
T 7 HOH 443 1843 688  HOH HOH B . 
T 7 HOH 444 1844 1707 HOH HOH B . 
T 7 HOH 445 1845 1614 HOH HOH B . 
T 7 HOH 446 1846 111  HOH HOH B . 
T 7 HOH 447 1847 1639 HOH HOH B . 
T 7 HOH 448 1848 1729 HOH HOH B . 
T 7 HOH 449 1849 796  HOH HOH B . 
T 7 HOH 450 1850 429  HOH HOH B . 
T 7 HOH 451 1851 1034 HOH HOH B . 
T 7 HOH 452 1852 907  HOH HOH B . 
T 7 HOH 453 1853 494  HOH HOH B . 
T 7 HOH 454 1854 1581 HOH HOH B . 
T 7 HOH 455 1855 3    HOH HOH B . 
T 7 HOH 456 1856 1108 HOH HOH B . 
T 7 HOH 457 1857 416  HOH HOH B . 
T 7 HOH 458 1858 789  HOH HOH B . 
T 7 HOH 459 1859 376  HOH HOH B . 
T 7 HOH 460 1860 1482 HOH HOH B . 
T 7 HOH 461 1861 95   HOH HOH B . 
T 7 HOH 462 1862 1367 HOH HOH B . 
T 7 HOH 463 1863 1486 HOH HOH B . 
T 7 HOH 464 1864 504  HOH HOH B . 
T 7 HOH 465 1865 116  HOH HOH B . 
T 7 HOH 466 1866 705  HOH HOH B . 
T 7 HOH 467 1867 191  HOH HOH B . 
T 7 HOH 468 1868 212  HOH HOH B . 
T 7 HOH 469 1869 1430 HOH HOH B . 
T 7 HOH 470 1870 173  HOH HOH B . 
T 7 HOH 471 1871 1520 HOH HOH B . 
T 7 HOH 472 1872 1531 HOH HOH B . 
T 7 HOH 473 1873 918  HOH HOH B . 
T 7 HOH 474 1874 84   HOH HOH B . 
T 7 HOH 475 1875 753  HOH HOH B . 
T 7 HOH 476 1876 1398 HOH HOH B . 
T 7 HOH 477 1877 527  HOH HOH B . 
T 7 HOH 478 1878 870  HOH HOH B . 
T 7 HOH 479 1879 996  HOH HOH B . 
T 7 HOH 480 1880 858  HOH HOH B . 
T 7 HOH 481 1881 581  HOH HOH B . 
T 7 HOH 482 1882 476  HOH HOH B . 
T 7 HOH 483 1883 482  HOH HOH B . 
T 7 HOH 484 1884 102  HOH HOH B . 
T 7 HOH 485 1885 1179 HOH HOH B . 
T 7 HOH 486 1886 1060 HOH HOH B . 
T 7 HOH 487 1887 1783 HOH HOH B . 
T 7 HOH 488 1888 22   HOH HOH B . 
T 7 HOH 489 1889 2068 HOH HOH B . 
T 7 HOH 490 1890 1163 HOH HOH B . 
T 7 HOH 491 1891 1585 HOH HOH B . 
T 7 HOH 492 1892 2045 HOH HOH B . 
T 7 HOH 493 1893 378  HOH HOH B . 
T 7 HOH 494 1894 1113 HOH HOH B . 
T 7 HOH 495 1895 629  HOH HOH B . 
T 7 HOH 496 1896 1697 HOH HOH B . 
T 7 HOH 497 1897 1354 HOH HOH B . 
T 7 HOH 498 1898 509  HOH HOH B . 
T 7 HOH 499 1899 199  HOH HOH B . 
T 7 HOH 500 1900 340  HOH HOH B . 
T 7 HOH 501 1901 399  HOH HOH B . 
T 7 HOH 502 1902 1120 HOH HOH B . 
T 7 HOH 503 1903 223  HOH HOH B . 
T 7 HOH 504 1904 1506 HOH HOH B . 
T 7 HOH 505 1905 1612 HOH HOH B . 
T 7 HOH 506 1906 609  HOH HOH B . 
T 7 HOH 507 1907 1077 HOH HOH B . 
T 7 HOH 508 1908 1241 HOH HOH B . 
T 7 HOH 509 1909 501  HOH HOH B . 
T 7 HOH 510 1910 577  HOH HOH B . 
T 7 HOH 511 1911 902  HOH HOH B . 
T 7 HOH 512 1912 1615 HOH HOH B . 
T 7 HOH 513 1913 1233 HOH HOH B . 
T 7 HOH 514 1914 15   HOH HOH B . 
T 7 HOH 515 1915 1373 HOH HOH B . 
T 7 HOH 516 1916 282  HOH HOH B . 
T 7 HOH 517 1917 1400 HOH HOH B . 
T 7 HOH 518 1918 298  HOH HOH B . 
T 7 HOH 519 1919 1209 HOH HOH B . 
T 7 HOH 520 1920 1208 HOH HOH B . 
T 7 HOH 521 1921 1125 HOH HOH B . 
T 7 HOH 522 1922 425  HOH HOH B . 
T 7 HOH 523 1923 1498 HOH HOH B . 
T 7 HOH 524 1924 1047 HOH HOH B . 
T 7 HOH 525 1925 1088 HOH HOH B . 
T 7 HOH 526 1926 463  HOH HOH B . 
T 7 HOH 527 1927 2092 HOH HOH B . 
T 7 HOH 528 1928 888  HOH HOH B . 
T 7 HOH 529 1929 534  HOH HOH B . 
T 7 HOH 530 1930 1731 HOH HOH B . 
T 7 HOH 531 1931 71   HOH HOH B . 
T 7 HOH 532 1932 264  HOH HOH B . 
T 7 HOH 533 1933 17   HOH HOH B . 
T 7 HOH 534 1934 665  HOH HOH B . 
T 7 HOH 535 1935 663  HOH HOH B . 
T 7 HOH 536 1936 1667 HOH HOH B . 
T 7 HOH 537 1937 473  HOH HOH B . 
T 7 HOH 538 1938 1504 HOH HOH B . 
T 7 HOH 539 1939 1154 HOH HOH B . 
T 7 HOH 540 1940 157  HOH HOH B . 
T 7 HOH 541 1941 1784 HOH HOH B . 
T 7 HOH 542 1942 1444 HOH HOH B . 
T 7 HOH 543 1943 775  HOH HOH B . 
T 7 HOH 544 1944 939  HOH HOH B . 
T 7 HOH 545 1945 401  HOH HOH B . 
T 7 HOH 546 1946 1045 HOH HOH B . 
T 7 HOH 547 1947 8    HOH HOH B . 
T 7 HOH 548 1948 395  HOH HOH B . 
T 7 HOH 549 1949 770  HOH HOH B . 
T 7 HOH 550 1950 1473 HOH HOH B . 
T 7 HOH 551 1951 1474 HOH HOH B . 
T 7 HOH 552 1952 851  HOH HOH B . 
T 7 HOH 553 1953 2096 HOH HOH B . 
T 7 HOH 554 1954 41   HOH HOH B . 
T 7 HOH 555 1955 249  HOH HOH B . 
T 7 HOH 556 1956 1684 HOH HOH B . 
T 7 HOH 557 1957 256  HOH HOH B . 
T 7 HOH 558 1958 1215 HOH HOH B . 
T 7 HOH 559 1959 454  HOH HOH B . 
T 7 HOH 560 1960 170  HOH HOH B . 
T 7 HOH 561 1961 1809 HOH HOH B . 
T 7 HOH 562 1962 1563 HOH HOH B . 
T 7 HOH 563 1963 1806 HOH HOH B . 
T 7 HOH 564 1964 1319 HOH HOH B . 
T 7 HOH 565 1965 667  HOH HOH B . 
T 7 HOH 566 1966 1755 HOH HOH B . 
T 7 HOH 567 1967 871  HOH HOH B . 
T 7 HOH 568 1968 585  HOH HOH B . 
T 7 HOH 569 1969 239  HOH HOH B . 
T 7 HOH 570 1970 320  HOH HOH B . 
T 7 HOH 571 1971 628  HOH HOH B . 
T 7 HOH 572 1972 1419 HOH HOH B . 
T 7 HOH 573 1973 392  HOH HOH B . 
T 7 HOH 574 1974 188  HOH HOH B . 
T 7 HOH 575 1975 52   HOH HOH B . 
T 7 HOH 576 1976 1469 HOH HOH B . 
T 7 HOH 577 1977 208  HOH HOH B . 
T 7 HOH 578 1978 73   HOH HOH B . 
T 7 HOH 579 1979 2048 HOH HOH B . 
T 7 HOH 580 1980 276  HOH HOH B . 
T 7 HOH 581 1981 683  HOH HOH B . 
T 7 HOH 582 1982 1523 HOH HOH B . 
T 7 HOH 583 1983 443  HOH HOH B . 
T 7 HOH 584 1984 176  HOH HOH B . 
T 7 HOH 585 1985 893  HOH HOH B . 
T 7 HOH 586 1986 931  HOH HOH B . 
T 7 HOH 587 1987 1713 HOH HOH B . 
T 7 HOH 588 1988 112  HOH HOH B . 
T 7 HOH 589 1989 1920 HOH HOH B . 
T 7 HOH 590 1990 1458 HOH HOH B . 
T 7 HOH 591 1991 1561 HOH HOH B . 
T 7 HOH 592 1992 1073 HOH HOH B . 
T 7 HOH 593 1993 153  HOH HOH B . 
T 7 HOH 594 1994 1706 HOH HOH B . 
T 7 HOH 595 1995 124  HOH HOH B . 
T 7 HOH 596 1996 227  HOH HOH B . 
T 7 HOH 597 1997 1402 HOH HOH B . 
T 7 HOH 598 1998 50   HOH HOH B . 
T 7 HOH 599 1999 1365 HOH HOH B . 
T 7 HOH 600 2000 1620 HOH HOH B . 
T 7 HOH 601 2001 244  HOH HOH B . 
T 7 HOH 602 2002 1719 HOH HOH B . 
T 7 HOH 603 2003 1225 HOH HOH B . 
T 7 HOH 604 2004 351  HOH HOH B . 
T 7 HOH 605 2005 1385 HOH HOH B . 
T 7 HOH 606 2006 2011 HOH HOH B . 
T 7 HOH 607 2007 523  HOH HOH B . 
T 7 HOH 608 2008 1702 HOH HOH B . 
T 7 HOH 609 2009 1001 HOH HOH B . 
T 7 HOH 610 2010 92   HOH HOH B . 
T 7 HOH 611 2011 288  HOH HOH B . 
T 7 HOH 612 2012 1745 HOH HOH B . 
T 7 HOH 613 2013 150  HOH HOH B . 
T 7 HOH 614 2014 225  HOH HOH B . 
T 7 HOH 615 2015 1502 HOH HOH B . 
T 7 HOH 616 2016 506  HOH HOH B . 
T 7 HOH 617 2017 520  HOH HOH B . 
T 7 HOH 618 2018 554  HOH HOH B . 
T 7 HOH 619 2019 428  HOH HOH B . 
T 7 HOH 620 2020 158  HOH HOH B . 
T 7 HOH 621 2021 1727 HOH HOH B . 
T 7 HOH 622 2022 142  HOH HOH B . 
T 7 HOH 623 2023 1539 HOH HOH B . 
T 7 HOH 624 2024 2026 HOH HOH B . 
T 7 HOH 625 2025 330  HOH HOH B . 
T 7 HOH 626 2026 550  HOH HOH B . 
T 7 HOH 627 2027 495  HOH HOH B . 
T 7 HOH 628 2028 968  HOH HOH B . 
T 7 HOH 629 2029 1094 HOH HOH B . 
T 7 HOH 630 2030 865  HOH HOH B . 
T 7 HOH 631 2031 1141 HOH HOH B . 
T 7 HOH 632 2032 2066 HOH HOH B . 
T 7 HOH 633 2033 1129 HOH HOH B . 
T 7 HOH 634 2034 1153 HOH HOH B . 
T 7 HOH 635 2035 104  HOH HOH B . 
T 7 HOH 636 2036 783  HOH HOH B . 
T 7 HOH 637 2037 437  HOH HOH B . 
T 7 HOH 638 2038 642  HOH HOH B . 
T 7 HOH 639 2039 1121 HOH HOH B . 
T 7 HOH 640 2040 1090 HOH HOH B . 
T 7 HOH 641 2041 1644 HOH HOH B . 
T 7 HOH 642 2042 594  HOH HOH B . 
T 7 HOH 643 2043 1422 HOH HOH B . 
T 7 HOH 644 2044 1149 HOH HOH B . 
T 7 HOH 645 2045 687  HOH HOH B . 
T 7 HOH 646 2046 1189 HOH HOH B . 
T 7 HOH 647 2047 502  HOH HOH B . 
T 7 HOH 648 2048 210  HOH HOH B . 
T 7 HOH 649 2049 1871 HOH HOH B . 
T 7 HOH 650 2050 37   HOH HOH B . 
T 7 HOH 651 2051 82   HOH HOH B . 
T 7 HOH 652 2052 1724 HOH HOH B . 
T 7 HOH 653 2053 385  HOH HOH B . 
T 7 HOH 654 2054 1863 HOH HOH B . 
T 7 HOH 655 2055 292  HOH HOH B . 
T 7 HOH 656 2056 204  HOH HOH B . 
T 7 HOH 657 2057 1950 HOH HOH B . 
T 7 HOH 658 2058 953  HOH HOH B . 
T 7 HOH 659 2059 1311 HOH HOH B . 
T 7 HOH 660 2060 1532 HOH HOH B . 
T 7 HOH 661 2061 1166 HOH HOH B . 
T 7 HOH 662 2062 1111 HOH HOH B . 
T 7 HOH 663 2063 606  HOH HOH B . 
T 7 HOH 664 2064 631  HOH HOH B . 
T 7 HOH 665 2065 420  HOH HOH B . 
T 7 HOH 666 2066 514  HOH HOH B . 
T 7 HOH 667 2067 1995 HOH HOH B . 
T 7 HOH 668 2068 1353 HOH HOH B . 
T 7 HOH 669 2069 1440 HOH HOH B . 
T 7 HOH 670 2070 1123 HOH HOH B . 
T 7 HOH 671 2071 1175 HOH HOH B . 
T 7 HOH 672 2072 1243 HOH HOH B . 
T 7 HOH 673 2073 721  HOH HOH B . 
T 7 HOH 674 2074 532  HOH HOH B . 
T 7 HOH 675 2075 678  HOH HOH B . 
T 7 HOH 676 2076 156  HOH HOH B . 
T 7 HOH 677 2077 1480 HOH HOH B . 
T 7 HOH 678 2078 1039 HOH HOH B . 
T 7 HOH 679 2079 1158 HOH HOH B . 
T 7 HOH 680 2080 1273 HOH HOH B . 
T 7 HOH 681 2081 834  HOH HOH B . 
T 7 HOH 682 2082 44   HOH HOH B . 
T 7 HOH 683 2083 1877 HOH HOH B . 
T 7 HOH 684 2084 634  HOH HOH B . 
T 7 HOH 685 2085 1946 HOH HOH B . 
T 7 HOH 686 2086 1339 HOH HOH B . 
T 7 HOH 687 2087 1449 HOH HOH B . 
T 7 HOH 688 2088 451  HOH HOH B . 
T 7 HOH 689 2089 63   HOH HOH B . 
T 7 HOH 690 2090 370  HOH HOH B . 
T 7 HOH 691 2091 567  HOH HOH B . 
T 7 HOH 692 2092 272  HOH HOH B . 
T 7 HOH 693 2093 1922 HOH HOH B . 
T 7 HOH 694 2094 1242 HOH HOH B . 
T 7 HOH 695 2095 1710 HOH HOH B . 
T 7 HOH 696 2096 613  HOH HOH B . 
T 7 HOH 697 2097 1217 HOH HOH B . 
T 7 HOH 698 2098 809  HOH HOH B . 
T 7 HOH 699 2099 779  HOH HOH B . 
T 7 HOH 700 2100 1036 HOH HOH B . 
T 7 HOH 701 2101 730  HOH HOH B . 
T 7 HOH 702 2102 612  HOH HOH B . 
T 7 HOH 703 2103 1811 HOH HOH B . 
T 7 HOH 704 2104 669  HOH HOH B . 
T 7 HOH 705 2105 1912 HOH HOH B . 
T 7 HOH 706 2106 27   HOH HOH B . 
T 7 HOH 707 2107 921  HOH HOH B . 
T 7 HOH 708 2108 1434 HOH HOH B . 
T 7 HOH 709 2109 1452 HOH HOH B . 
T 7 HOH 710 2110 1279 HOH HOH B . 
T 7 HOH 711 2111 795  HOH HOH B . 
T 7 HOH 712 2112 1491 HOH HOH B . 
T 7 HOH 713 2113 1500 HOH HOH B . 
T 7 HOH 714 2114 374  HOH HOH B . 
T 7 HOH 715 2115 827  HOH HOH B . 
T 7 HOH 716 2116 281  HOH HOH B . 
T 7 HOH 717 2117 1487 HOH HOH B . 
T 7 HOH 718 2118 1608 HOH HOH B . 
T 7 HOH 719 2119 1196 HOH HOH B . 
T 7 HOH 720 2120 1935 HOH HOH B . 
T 7 HOH 721 2121 646  HOH HOH B . 
T 7 HOH 722 2122 1220 HOH HOH B . 
T 7 HOH 723 2123 1128 HOH HOH B . 
T 7 HOH 724 2124 1503 HOH HOH B . 
T 7 HOH 725 2125 1758 HOH HOH B . 
T 7 HOH 726 2126 3024 HOH HOH B . 
T 7 HOH 727 2127 971  HOH HOH B . 
T 7 HOH 728 2128 1278 HOH HOH B . 
T 7 HOH 729 2129 1959 HOH HOH B . 
T 7 HOH 730 2130 1518 HOH HOH B . 
T 7 HOH 731 2131 658  HOH HOH B . 
T 7 HOH 732 2132 1127 HOH HOH B . 
T 7 HOH 733 2133 287  HOH HOH B . 
T 7 HOH 734 2134 1726 HOH HOH B . 
T 7 HOH 735 2135 1999 HOH HOH B . 
T 7 HOH 736 2136 1547 HOH HOH B . 
T 7 HOH 737 2137 195  HOH HOH B . 
T 7 HOH 738 2138 1420 HOH HOH B . 
T 7 HOH 739 2139 462  HOH HOH B . 
T 7 HOH 740 2140 345  HOH HOH B . 
T 7 HOH 741 2141 2076 HOH HOH B . 
T 7 HOH 742 2142 1219 HOH HOH B . 
T 7 HOH 743 2143 1709 HOH HOH B . 
T 7 HOH 744 2144 1688 HOH HOH B . 
T 7 HOH 745 2145 2075 HOH HOH B . 
T 7 HOH 746 2146 936  HOH HOH B . 
T 7 HOH 747 2147 337  HOH HOH B . 
T 7 HOH 748 2148 1703 HOH HOH B . 
T 7 HOH 749 2149 617  HOH HOH B . 
T 7 HOH 750 2150 768  HOH HOH B . 
T 7 HOH 751 2151 1754 HOH HOH B . 
T 7 HOH 752 2152 1098 HOH HOH B . 
T 7 HOH 753 2153 961  HOH HOH B . 
T 7 HOH 754 2154 1979 HOH HOH B . 
T 7 HOH 755 2155 1772 HOH HOH B . 
T 7 HOH 756 2156 1232 HOH HOH B . 
T 7 HOH 757 2157 868  HOH HOH B . 
T 7 HOH 758 2158 804  HOH HOH B . 
T 7 HOH 759 2159 1182 HOH HOH B . 
T 7 HOH 760 2160 1838 HOH HOH B . 
T 7 HOH 761 2161 1921 HOH HOH B . 
T 7 HOH 762 2162 1718 HOH HOH B . 
T 7 HOH 763 2163 1923 HOH HOH B . 
T 7 HOH 764 2164 1696 HOH HOH B . 
T 7 HOH 765 2165 1725 HOH HOH B . 
T 7 HOH 766 2166 979  HOH HOH B . 
T 7 HOH 767 2167 1137 HOH HOH B . 
T 7 HOH 768 2168 1206 HOH HOH B . 
T 7 HOH 769 2169 1251 HOH HOH B . 
T 7 HOH 770 2170 838  HOH HOH B . 
T 7 HOH 771 2171 1169 HOH HOH B . 
T 7 HOH 772 2172 1931 HOH HOH B . 
T 7 HOH 773 2173 1589 HOH HOH B . 
T 7 HOH 774 2174 1560 HOH HOH B . 
T 7 HOH 775 2175 1272 HOH HOH B . 
T 7 HOH 776 2176 655  HOH HOH B . 
T 7 HOH 777 2177 1655 HOH HOH B . 
T 7 HOH 778 2178 643  HOH HOH B . 
T 7 HOH 779 2179 714  HOH HOH B . 
T 7 HOH 780 2180 1284 HOH HOH B . 
T 7 HOH 781 2181 1135 HOH HOH B . 
T 7 HOH 782 2182 976  HOH HOH B . 
T 7 HOH 783 2183 1617 HOH HOH B . 
T 7 HOH 784 2184 1155 HOH HOH B . 
T 7 HOH 785 2185 1786 HOH HOH B . 
T 7 HOH 786 2186 670  HOH HOH B . 
T 7 HOH 787 2187 1823 HOH HOH B . 
T 7 HOH 788 2188 1894 HOH HOH B . 
T 7 HOH 789 2189 1841 HOH HOH B . 
T 7 HOH 790 2190 1812 HOH HOH B . 
T 7 HOH 791 2191 1572 HOH HOH B . 
T 7 HOH 792 2192 793  HOH HOH B . 
T 7 HOH 793 2193 1834 HOH HOH B . 
T 7 HOH 794 2194 1516 HOH HOH B . 
T 7 HOH 795 2195 1807 HOH HOH B . 
T 7 HOH 796 2196 1659 HOH HOH B . 
T 7 HOH 797 2197 718  HOH HOH B . 
T 7 HOH 798 2198 930  HOH HOH B . 
T 7 HOH 799 2199 815  HOH HOH B . 
T 7 HOH 800 2200 1808 HOH HOH B . 
T 7 HOH 801 2201 1934 HOH HOH B . 
T 7 HOH 802 2202 1849 HOH HOH B . 
T 7 HOH 803 2203 1953 HOH HOH B . 
T 7 HOH 804 2204 1661 HOH HOH B . 
T 7 HOH 805 2205 1185 HOH HOH B . 
T 7 HOH 806 2206 1173 HOH HOH B . 
T 7 HOH 807 2207 314  HOH HOH B . 
T 7 HOH 808 2208 2089 HOH HOH B . 
T 7 HOH 809 2209 1037 HOH HOH B . 
T 7 HOH 810 2210 2081 HOH HOH B . 
T 7 HOH 811 2211 660  HOH HOH B . 
T 7 HOH 812 2212 1582 HOH HOH B . 
T 7 HOH 813 2213 1744 HOH HOH B . 
T 7 HOH 814 2214 1543 HOH HOH B . 
T 7 HOH 815 2215 774  HOH HOH B . 
T 7 HOH 816 2216 954  HOH HOH B . 
T 7 HOH 817 2217 993  HOH HOH B . 
T 7 HOH 818 2218 1162 HOH HOH B . 
T 7 HOH 819 2219 1795 HOH HOH B . 
T 7 HOH 820 2220 1798 HOH HOH B . 
T 7 HOH 821 2221 1619 HOH HOH B . 
T 7 HOH 822 2222 841  HOH HOH B . 
T 7 HOH 823 2223 3011 HOH HOH B . 
T 7 HOH 824 2224 561  HOH HOH B . 
T 7 HOH 825 2225 140  HOH HOH B . 
T 7 HOH 826 2226 1181 HOH HOH B . 
T 7 HOH 827 2227 849  HOH HOH B . 
T 7 HOH 828 2228 1958 HOH HOH B . 
T 7 HOH 829 2229 693  HOH HOH B . 
T 7 HOH 830 2230 934  HOH HOH B . 
T 7 HOH 831 2231 2030 HOH HOH B . 
T 7 HOH 832 2232 2074 HOH HOH B . 
T 7 HOH 833 2233 352  HOH HOH B . 
T 7 HOH 834 2234 1553 HOH HOH B . 
T 7 HOH 835 2235 982  HOH HOH B . 
T 7 HOH 836 2236 1583 HOH HOH B . 
T 7 HOH 837 2237 737  HOH HOH B . 
T 7 HOH 838 2238 633  HOH HOH B . 
T 7 HOH 839 2239 2059 HOH HOH B . 
T 7 HOH 840 2240 1662 HOH HOH B . 
T 7 HOH 841 2241 807  HOH HOH B . 
T 7 HOH 842 2242 1981 HOH HOH B . 
T 7 HOH 843 2243 1559 HOH HOH B . 
T 7 HOH 844 2244 1556 HOH HOH B . 
T 7 HOH 845 2245 1598 HOH HOH B . 
T 7 HOH 846 2246 1874 HOH HOH B . 
T 7 HOH 847 2247 762  HOH HOH B . 
T 7 HOH 848 2248 1887 HOH HOH B . 
T 7 HOH 849 2249 543  HOH HOH B . 
T 7 HOH 850 2250 1526 HOH HOH B . 
T 7 HOH 851 2251 1564 HOH HOH B . 
T 7 HOH 852 2252 980  HOH HOH B . 
T 7 HOH 853 2253 1866 HOH HOH B . 
T 7 HOH 854 2254 1797 HOH HOH B . 
T 7 HOH 855 2255 472  HOH HOH B . 
T 7 HOH 856 2256 2035 HOH HOH B . 
T 7 HOH 857 2257 2006 HOH HOH B . 
T 7 HOH 858 2258 1991 HOH HOH B . 
T 7 HOH 859 2259 2017 HOH HOH B . 
T 7 HOH 860 2260 1815 HOH HOH B . 
T 7 HOH 861 2261 1861 HOH HOH B . 
T 7 HOH 862 2262 2027 HOH HOH B . 
T 7 HOH 863 2263 1211 HOH HOH B . 
T 7 HOH 864 2264 760  HOH HOH B . 
T 7 HOH 865 2265 1869 HOH HOH B . 
T 7 HOH 866 2266 1011 HOH HOH B . 
T 7 HOH 867 2267 1228 HOH HOH B . 
T 7 HOH 868 2268 1948 HOH HOH B . 
T 7 HOH 869 2269 1481 HOH HOH B . 
T 7 HOH 870 2270 1964 HOH HOH B . 
T 7 HOH 871 2271 475  HOH HOH B . 
T 7 HOH 872 2272 1314 HOH HOH B . 
T 7 HOH 873 2273 1837 HOH HOH B . 
T 7 HOH 874 2274 1884 HOH HOH B . 
T 7 HOH 875 2275 1850 HOH HOH B . 
T 7 HOH 876 2276 1000 HOH HOH B . 
T 7 HOH 877 2277 910  HOH HOH B . 
T 7 HOH 878 2278 1961 HOH HOH B . 
T 7 HOH 879 2279 1146 HOH HOH B . 
T 7 HOH 880 2280 1864 HOH HOH B . 
T 7 HOH 881 2281 1097 HOH HOH B . 
T 7 HOH 882 2282 568  HOH HOH B . 
T 7 HOH 883 2283 1822 HOH HOH B . 
T 7 HOH 884 2284 358  HOH HOH B . 
T 7 HOH 885 2285 343  HOH HOH B . 
T 7 HOH 886 2286 1885 HOH HOH B . 
T 7 HOH 887 2287 1565 HOH HOH B . 
T 7 HOH 888 2288 679  HOH HOH B . 
T 7 HOH 889 2289 1592 HOH HOH B . 
T 7 HOH 890 2290 221  HOH HOH B . 
T 7 HOH 891 2291 579  HOH HOH B . 
T 7 HOH 892 2292 575  HOH HOH B . 
T 7 HOH 893 2293 3017 HOH HOH B . 
T 7 HOH 894 2294 1880 HOH HOH B . 
T 7 HOH 895 2295 1176 HOH HOH B . 
T 7 HOH 896 2296 1136 HOH HOH B . 
T 7 HOH 897 2297 1300 HOH HOH B . 
T 7 HOH 898 2298 214  HOH HOH B . 
T 7 HOH 899 2299 2082 HOH HOH B . 
T 7 HOH 900 2300 767  HOH HOH B . 
T 7 HOH 901 2301 972  HOH HOH B . 
T 7 HOH 902 2302 389  HOH HOH B . 
T 7 HOH 903 2303 1479 HOH HOH B . 
T 7 HOH 904 2304 533  HOH HOH B . 
T 7 HOH 905 2305 1321 HOH HOH B . 
T 7 HOH 906 2306 175  HOH HOH B . 
T 7 HOH 907 2307 911  HOH HOH B . 
T 7 HOH 908 2308 1574 HOH HOH B . 
T 7 HOH 909 2309 2067 HOH HOH B . 
T 7 HOH 910 2310 1968 HOH HOH B . 
T 7 HOH 911 2311 414  HOH HOH B . 
T 7 HOH 912 2312 1816 HOH HOH B . 
T 7 HOH 913 2313 1588 HOH HOH B . 
T 7 HOH 914 2314 1174 HOH HOH B . 
T 7 HOH 915 2315 1186 HOH HOH B . 
T 7 HOH 916 2316 1804 HOH HOH B . 
T 7 HOH 917 2317 749  HOH HOH B . 
T 7 HOH 918 2318 232  HOH HOH B . 
T 7 HOH 919 2319 3034 HOH HOH B . 
T 7 HOH 920 2320 2085 HOH HOH B . 
T 7 HOH 921 2321 1875 HOH HOH B . 
T 7 HOH 922 2322 1266 HOH HOH B . 
T 7 HOH 923 2323 1222 HOH HOH B . 
T 7 HOH 924 2324 1785 HOH HOH B . 
T 7 HOH 925 2325 1969 HOH HOH B . 
T 7 HOH 926 2326 1947 HOH HOH B . 
T 7 HOH 927 2327 1944 HOH HOH B . 
T 7 HOH 928 2328 955  HOH HOH B . 
T 7 HOH 929 2329 1423 HOH HOH B . 
T 7 HOH 930 2330 1818 HOH HOH B . 
T 7 HOH 931 2331 1310 HOH HOH B . 
T 7 HOH 932 2332 1303 HOH HOH B . 
T 7 HOH 933 2333 1159 HOH HOH B . 
T 7 HOH 934 2334 1611 HOH HOH B . 
T 7 HOH 935 2335 1792 HOH HOH B . 
T 7 HOH 936 2336 727  HOH HOH B . 
T 7 HOH 937 2337 1071 HOH HOH B . 
T 7 HOH 938 2338 2032 HOH HOH B . 
T 7 HOH 939 2339 1340 HOH HOH B . 
T 7 HOH 940 2340 1821 HOH HOH B . 
T 7 HOH 941 2341 1203 HOH HOH B . 
T 7 HOH 942 2342 1949 HOH HOH B . 
T 7 HOH 943 2343 458  HOH HOH B . 
T 7 HOH 944 2344 1825 HOH HOH B . 
T 7 HOH 945 2345 1600 HOH HOH B . 
T 7 HOH 946 2346 945  HOH HOH B . 
T 7 HOH 947 2347 2060 HOH HOH B . 
T 7 HOH 948 2348 1317 HOH HOH B . 
T 7 HOH 949 2349 1951 HOH HOH B . 
T 7 HOH 950 2350 2083 HOH HOH B . 
T 7 HOH 951 2351 935  HOH HOH B . 
T 7 HOH 952 2352 166  HOH HOH B . 
T 7 HOH 953 2353 1534 HOH HOH B . 
T 7 HOH 954 2354 1601 HOH HOH B . 
T 7 HOH 955 2355 1824 HOH HOH B . 
T 7 HOH 956 2356 1395 HOH HOH B . 
T 7 HOH 957 2357 984  HOH HOH B . 
T 7 HOH 958 2358 1666 HOH HOH B . 
T 7 HOH 959 2359 1819 HOH HOH B . 
T 7 HOH 960 2360 1253 HOH HOH B . 
T 7 HOH 961 2361 3003 HOH HOH B . 
T 7 HOH 962 2362 1989 HOH HOH B . 
T 7 HOH 963 2363 1962 HOH HOH B . 
T 7 HOH 964 2364 1304 HOH HOH B . 
T 7 HOH 965 2365 444  HOH HOH B . 
T 7 HOH 966 2366 1603 HOH HOH B . 
T 7 HOH 967 2367 1723 HOH HOH B . 
T 7 HOH 968 2368 1230 HOH HOH B . 
T 7 HOH 969 2369 1976 HOH HOH B . 
T 7 HOH 970 2370 307  HOH HOH B . 
T 7 HOH 971 2371 1348 HOH HOH B . 
T 7 HOH 972 2372 1988 HOH HOH B . 
T 7 HOH 973 2373 540  HOH HOH B . 
T 7 HOH 974 2374 1080 HOH HOH B . 
T 7 HOH 975 2375 283  HOH HOH B . 
T 7 HOH 976 2376 497  HOH HOH B . 
T 7 HOH 977 2377 1994 HOH HOH B . 
T 7 HOH 978 2378 1844 HOH HOH B . 
T 7 HOH 979 2379 1799 HOH HOH B . 
T 7 HOH 980 2380 1843 HOH HOH B . 
T 7 HOH 981 2381 1269 HOH HOH B . 
T 7 HOH 982 2382 1820 HOH HOH B . 
T 7 HOH 983 2383 1584 HOH HOH B . 
T 7 HOH 984 2384 1332 HOH HOH B . 
T 7 HOH 985 2385 1264 HOH HOH B . 
T 7 HOH 986 2386 1119 HOH HOH B . 
T 7 HOH 987 2387 3016 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
2   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
3   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
4   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
5   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
6   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
7   1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
8   1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
9   1 Y 1 A SER 80   ? OG  ? A SER 82   OG  
10  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
11  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
12  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
13  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
14  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
15  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
16  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
17  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
18  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
19  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
20  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
21  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
22  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
23  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
24  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
25  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
26  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
27  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
28  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
29  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
30  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
31  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
32  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
33  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
34  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
35  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
36  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
37  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
38  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
39  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
40  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
41  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
42  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
43  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
44  1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
45  1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
46  1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
47  1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
48  1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
49  1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
50  1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
51  1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
52  1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
53  1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
54  1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
55  1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
56  1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
57  1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
58  1 Y 1 A GLU 810  ? CG  ? A GLU 812  CG  
59  1 Y 1 A GLU 810  ? CD  ? A GLU 812  CD  
60  1 Y 1 A GLU 810  ? OE1 ? A GLU 812  OE1 
61  1 Y 1 A GLU 810  ? OE2 ? A GLU 812  OE2 
62  1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
63  1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
64  1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
65  1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
66  1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
67  1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
68  1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
69  1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
70  1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
71  1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
72  1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
73  1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
74  1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
75  1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
76  1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
77  1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
78  1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
79  1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
80  1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
81  1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
82  1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
83  1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
84  1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
85  1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
86  1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
87  1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
88  1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
89  1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
90  1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
91  1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
92  1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
93  1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
94  1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
95  1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
96  1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
97  1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
98  1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
99  1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
100 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
101 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
102 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
103 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
104 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
105 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
106 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
107 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
108 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
109 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
110 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
111 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
112 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
113 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
114 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
115 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
116 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
117 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
118 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
119 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
120 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
121 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
122 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
123 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
124 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
125 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
126 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
127 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
128 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
129 1 Y 1 B GLU 810  ? CG  ? B GLU 812  CG  
130 1 Y 1 B GLU 810  ? CD  ? B GLU 812  CD  
131 1 Y 1 B GLU 810  ? OE1 ? B GLU 812  OE1 
132 1 Y 1 B GLU 810  ? OE2 ? B GLU 812  OE2 
133 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
134 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
135 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
136 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
137 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
138 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
139 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
140 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
141 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
142 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
143 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
144 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
145 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
146 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
147 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
148 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
149 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
150 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
151 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
152 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
153 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
154 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
155 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
156 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
157 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
158 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
159 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
160 1 Y 1 B GLU 1171 ? CG  ? B GLU 1173 CG  
161 1 Y 1 B GLU 1171 ? CD  ? B GLU 1173 CD  
162 1 Y 1 B GLU 1171 ? OE1 ? B GLU 1173 OE1 
163 1 Y 1 B GLU 1171 ? OE2 ? B GLU 1173 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21rc1_5156: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                     2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.38 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BBO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.377 
_cell.length_a_esd                 ? 
_cell.length_b                     102.435 
_cell.length_b_esd                 ? 
_cell.length_c                     127.598 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BBO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BBO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.93 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M HEPES AT PH 7.5, 0.1 M AMMONIUM SULFATE, 0.1 M LITHIUM SULFATE MONOHYDRATE, 50 MM MGCL2, AND 25% (W/V) PEG 3350; crystal soaked in 325 mM L-glutamate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-07-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BBO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               102.43 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     386803 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.089 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       2347695 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.082 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           74652 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             19361 
_reflns_shell.percent_possible_obs                          95.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               0.911 
_reflns_shell.pdbx_Rpim_I_all                               0.459 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.627 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.783 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BBO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             51.77 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     386747 
_refine.ls_number_reflns_R_free                  19610 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.03 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1705 
_refine.ls_R_factor_R_free                       0.1908 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1694 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.15 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        18143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         198 
_refine_hist.number_atoms_solvent             1982 
_refine_hist.number_atoms_total               20323 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        51.77 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 18902 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.850  ? 25775 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.617 ? 7019  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 3004  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3367  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.52  . . 644 11910 95.00 . . . . 0.2703 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.52 1.54  . . 668 11915 95.00 . . . . 0.2563 . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 1.54 1.55  . . 668 11962 95.00 . . . . 0.2375 . . . . . . . . . . . 0.2622 
'X-RAY DIFFRACTION' 1.55 1.57  . . 613 11995 95.00 . . . . 0.2250 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 1.57 1.59  . . 652 11951 95.00 . . . . 0.2194 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.59 1.62  . . 639 12073 96.00 . . . . 0.2059 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 1.62 1.64  . . 633 12061 96.00 . . . . 0.1976 . . . . . . . . . . . 0.2236 
'X-RAY DIFFRACTION' 1.64 1.66  . . 635 12006 96.00 . . . . 0.1929 . . . . . . . . . . . 0.2124 
'X-RAY DIFFRACTION' 1.66 1.69  . . 626 12182 96.00 . . . . 0.1887 . . . . . . . . . . . 0.2267 
'X-RAY DIFFRACTION' 1.69 1.72  . . 615 12068 96.00 . . . . 0.1868 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 1.72 1.75  . . 621 12137 96.00 . . . . 0.1814 . . . . . . . . . . . 0.2135 
'X-RAY DIFFRACTION' 1.75 1.78  . . 627 12159 96.00 . . . . 0.1887 . . . . . . . . . . . 0.2218 
'X-RAY DIFFRACTION' 1.78 1.81  . . 635 12151 97.00 . . . . 0.1855 . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 1.81 1.85  . . 653 12197 97.00 . . . . 0.1892 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 1.85 1.89  . . 670 12142 97.00 . . . . 0.1875 . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 1.89 1.93  . . 704 12197 97.00 . . . . 0.1785 . . . . . . . . . . . 0.2064 
'X-RAY DIFFRACTION' 1.93 1.98  . . 648 12214 97.00 . . . . 0.1736 . . . . . . . . . . . 0.2079 
'X-RAY DIFFRACTION' 1.98 2.04  . . 659 12199 97.00 . . . . 0.1695 . . . . . . . . . . . 0.1995 
'X-RAY DIFFRACTION' 2.04 2.10  . . 674 12357 98.00 . . . . 0.1731 . . . . . . . . . . . 0.2054 
'X-RAY DIFFRACTION' 2.10 2.16  . . 645 12286 98.00 . . . . 0.1698 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 2.16 2.24  . . 653 12398 98.00 . . . . 0.1644 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 2.24 2.33  . . 661 12340 98.00 . . . . 0.1665 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 2.33 2.44  . . 665 12369 98.00 . . . . 0.1680 . . . . . . . . . . . 0.1905 
'X-RAY DIFFRACTION' 2.44 2.57  . . 668 12435 98.00 . . . . 0.1750 . . . . . . . . . . . 0.2103 
'X-RAY DIFFRACTION' 2.57 2.73  . . 707 12384 98.00 . . . . 0.1758 . . . . . . . . . . . 0.1896 
'X-RAY DIFFRACTION' 2.73 2.94  . . 683 12485 99.00 . . . . 0.1792 . . . . . . . . . . . 0.1982 
'X-RAY DIFFRACTION' 2.94 3.23  . . 645 12511 99.00 . . . . 0.1736 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 3.23 3.70  . . 641 12605 99.00 . . . . 0.1598 . . . . . . . . . . . 0.1776 
'X-RAY DIFFRACTION' 3.70 4.66  . . 647 12688 99.00 . . . . 0.1308 . . . . . . . . . . . 0.1384 
'X-RAY DIFFRACTION' 4.66 51.77 . . 711 12760 99.00 . . . . 0.1398 . . . . . . . . . . . 0.1507 
# 
_struct.entry_id                     9BBO 
_struct.title                        
'Proline utilization A complexed with the product L-glutamate in the aldehyde dehydrogenase active site' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BBO 
_struct_keywords.text            
;FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGNEASE, ALDEHYDE DEHYDROGENASE, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 6 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 7 ? 
T N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0AA90VXT3_RHIML 
_struct_ref.pdbx_db_accession          A0AA90VXT3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHS
GSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTSTVN
DRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDY
ESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLDLL
EVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDV
SYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHE
TLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEETLA
SLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAACLD
RAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIAAA
LVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRLSP
AGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDRLS
VDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDRLV
DDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVPPQ
HSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAAAL
ATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEIAR
NPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BBO A 3 ? 1235 ? A0AA90VXT3 1 ? 1233 ? 1 1233 
2 1 9BBO B 3 ? 1235 ? A0AA90VXT3 1 ? 1233 ? 1 1233 
# 
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 9BBO SER A 1 ? UNP A0AA90VXT3 ? ? 'expression tag' -1 1 
1 9BBO MET A 2 ? UNP A0AA90VXT3 ? ? 'expression tag' 0  2 
2 9BBO SER B 1 ? UNP A0AA90VXT3 ? ? 'expression tag' -1 3 
2 9BBO MET B 2 ? UNP A0AA90VXT3 ? ? 'expression tag' 0  4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? dimeric   2 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,S                     
2 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
3 1 B,K,L,M,N,O,P,Q,R,T                     
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 SER A 31   ? ALA A 40   ? SER A 29   ALA A 38   1 ? 10 
HELX_P HELX_P2   AA2 PRO A 44   ? THR A 57   ? PRO A 42   THR A 55   1 ? 14 
HELX_P HELX_P3   AA3 SER A 59   ? HIS A 81   ? SER A 57   HIS A 79   1 ? 23 
HELX_P HELX_P4   AA4 SER A 84   ? SER A 94   ? SER A 82   SER A 92   1 ? 11 
HELX_P HELX_P5   AA5 SER A 96   ? LEU A 111  ? SER A 94   LEU A 109  1 ? 16 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P8   AA8 ASN A 162  ? GLY A 178  ? ASN A 160  GLY A 176  1 ? 17 
HELX_P HELX_P9   AA9 GLY A 178  ? GLN A 196  ? GLY A 176  GLN A 194  1 ? 19 
HELX_P HELX_P10  AB1 THR A 202  ? GLU A 215  ? THR A 200  GLU A 213  1 ? 14 
HELX_P HELX_P11  AB2 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P12  AB3 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P13  AB4 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P14  AB5 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P15  AB6 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P16  AB7 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P17  AB8 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P18  AB9 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P19  AC1 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P20  AC2 TYR A 375  ? GLY A 387  ? TYR A 373  GLY A 385  1 ? 13 
HELX_P HELX_P21  AC3 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P22  AC4 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P23  AC5 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P24  AC6 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P25  AC7 TYR A 487  ? ALA A 497  ? TYR A 485  ALA A 495  1 ? 11 
HELX_P HELX_P26  AC8 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P27  AC9 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P28  AD1 ASP A 518  ? MET A 526  ? ASP A 516  MET A 524  1 ? 9  
HELX_P HELX_P29  AD2 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P30  AD3 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P31  AD4 SER A 611  ? ALA A 631  ? SER A 609  ALA A 629  1 ? 21 
HELX_P HELX_P32  AD5 PRO A 633  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P33  AD6 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
HELX_P HELX_P34  AD7 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P35  AD8 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P36  AD9 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P37  AE1 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P38  AE2 SER A 785  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
HELX_P HELX_P39  AE3 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P40  AE4 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P41  AE5 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P42  AE6 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P43  AE7 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P44  AE8 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P45  AE9 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P46  AF1 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P47  AF2 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P48  AF3 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P49  AF4 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P50  AF5 ASP A 1049 ? GLY A 1063 ? ASP A 1047 GLY A 1061 1 ? 15 
HELX_P HELX_P51  AF6 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P52  AF7 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P53  AF8 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P54  AF9 LEU A 1136 ? LEU A 1140 ? LEU A 1134 LEU A 1138 5 ? 5  
HELX_P HELX_P55  AG1 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P56  AG2 ASP A 1156 ? GLY A 1161 ? ASP A 1154 GLY A 1159 5 ? 6  
HELX_P HELX_P57  AG3 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P58  AG4 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P59  AG5 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P60  AG6 ALA A 1229 ? ILE A 1234 ? ALA A 1227 ILE A 1232 5 ? 6  
HELX_P HELX_P61  AG7 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P62  AG8 PRO B 44   ? ALA B 56   ? PRO B 42   ALA B 54   1 ? 13 
HELX_P HELX_P63  AG9 SER B 59   ? LYS B 80   ? SER B 57   LYS B 78   1 ? 22 
HELX_P HELX_P64  AH1 SER B 84   ? SER B 94   ? SER B 82   SER B 92   1 ? 11 
HELX_P HELX_P65  AH2 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P66  AH3 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P67  AH4 ASN B 131  ? HIS B 135  ? ASN B 129  HIS B 133  5 ? 5  
HELX_P HELX_P68  AH5 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P69  AH6 ASN B 162  ? GLN B 196  ? ASN B 160  GLN B 194  1 ? 35 
HELX_P HELX_P70  AH7 THR B 202  ? GLU B 215  ? THR B 200  GLU B 213  1 ? 14 
HELX_P HELX_P71  AH8 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P72  AH9 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P73  AI1 LYS B 267  ? LEU B 271  ? LYS B 265  LEU B 269  5 ? 5  
HELX_P HELX_P74  AI2 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P75  AI3 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P76  AI4 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P77  AI5 ARG B 314  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P78  AI6 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
HELX_P HELX_P79  AI7 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P80  AI8 TYR B 375  ? GLY B 387  ? TYR B 373  GLY B 385  1 ? 13 
HELX_P HELX_P81  AI9 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P82  AJ1 ASN B 426  ? GLY B 438  ? ASN B 424  GLY B 436  1 ? 13 
HELX_P HELX_P83  AJ2 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P84  AJ3 THR B 480  ? ALA B 486  ? THR B 478  ALA B 484  1 ? 7  
HELX_P HELX_P85  AJ4 TYR B 487  ? ALA B 497  ? TYR B 485  ALA B 495  1 ? 11 
HELX_P HELX_P86  AJ5 SER B 500  ? ASN B 506  ? SER B 498  ASN B 504  1 ? 7  
HELX_P HELX_P87  AJ6 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P88  AJ7 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P89  AJ8 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P90  AJ9 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P91  AK1 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P101 AL2 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P102 AL3 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P103 AL4 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P104 AL5 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P105 AL6 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P106 AL7 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P107 AL8 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P108 AL9 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P109 AM1 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P110 AM2 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P111 AM3 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P112 AM4 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P113 AM5 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P114 AM6 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P115 AM7 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P116 AM8 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P117 AM9 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P118 AN1 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P119 AN2 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P120 AN3 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P121 AN4 CYS B 1208 ? TRP B 1211 ? CYS B 1206 TRP B 1209 5 ? 4  
HELX_P HELX_P122 AN5 ALA B 1229 ? ILE B 1234 ? ALA B 1227 ILE B 1232 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 GLY 1021 A . ? GLY 1019 A PRO 1022 A ? PRO 1020 A 1 -2.16 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 2.98  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -3.57 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 4.59  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 3  ? 
AA3 ? 2  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
AA7 ? 9  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 5  ? 
AB2 ? 10 ? 
AB3 ? 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 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB2 1 2  ? anti-parallel 
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB2 5 6  ? parallel      
AB2 6 7  ? parallel      
AB2 7 8  ? parallel      
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  LEU A 305  ? ILE A 307  ? LEU A 303  ILE A 305  
AA1 4  MET A 337  ? GLN A 342  ? MET A 335  GLN A 340  
AA1 5  ILE A 366  ? VAL A 371  ? ILE A 364  VAL A 369  
AA1 6  VAL A 418  ? ALA A 423  ? VAL A 416  ALA A 421  
AA1 7  GLU A 447  ? LEU A 451  ? GLU A 445  LEU A 449  
AA1 8  CYS A 472  ? PRO A 477  ? CYS A 470  PRO A 475  
AA1 9  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? GLU A 609  ? ASP A 597  GLU A 607  
AA2 3  GLU A 590  ? ASN A 596  ? GLU A 588  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? GLU B 1085 ? ASP B 1081 GLU B 1083 
AB3 1  VAL B 1151 ? SER B 1154 ? VAL B 1149 SER B 1152 
AB3 2  SER B 1127 ? ASP B 1131 ? SER B 1125 ASP B 1129 
AB3 3  ARG B 1103 ? VAL B 1107 ? ARG B 1101 VAL B 1105 
AB3 4  GLY B 1165 ? GLU B 1169 ? GLY B 1163 GLU B 1167 
AB3 5  VAL B 1192 ? ALA B 1195 ? VAL B 1190 ALA B 1193 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N TYR A 222  ? N TYR A 220  O SER A 265  ? O SER A 263  
AA1 2 3  N ILE A 266  ? N ILE A 264  O ASN A 306  ? O ASN A 304  
AA1 3 4  N LEU A 305  ? N LEU A 303  O GLY A 338  ? O GLY A 336  
AA1 4 5  N PHE A 339  ? N PHE A 337  O MET A 367  ? O MET A 365  
AA1 5 6  N VAL A 368  ? N VAL A 366  O GLN A 421  ? O GLN A 419  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O VAL A 607  ? O VAL A 605  N ARG A 592  ? N ARG A 590  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O TYR A 1096 ? O TYR A 1094 N LEU A 1084 ? N LEU A 1082 
AA6 1 2  O SER A 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O VAL B 607  ? O VAL B 605  N ARG B 592  ? N ARG B 590  
AA9 1 2  N LEU B 582  ? N LEU B 580  O GLY B 585  ? O GLY B 583  
AB1 1 2  O GLN B 759  ? O GLN B 757  N ALA B 731  ? N ALA B 729  
AB1 2 3  O LYS B 732  ? O LYS B 730  N CYS B 704  ? N CYS B 702  
AB1 3 4  N ILE B 705  ? N ILE B 703  O MET B 781  ? O MET B 779  
AB1 4 5  N PHE B 782  ? N PHE B 780  O ILE B 810  ? O ILE B 808  
AB2 1 2  N GLU B 912  ? N GLU B 910  O ILE B 930  ? O ILE B 928  
AB2 2 3  N ILE B 931  ? N ILE B 929  O LEU B 948  ? O LEU B 946  
AB2 3 4  O HIS B 949  ? O HIS B 947  N LEU B 852  ? N LEU B 850  
AB2 4 5  O CYS B 853  ? O CYS B 851  N MET B 819  ? N MET B 817  
AB2 5 6  N ILE B 820  ? N ILE B 818  O HIS B 977  ? O HIS B 975  
AB2 6 7  N PHE B 974  ? N PHE B 972  O TYR B 997  ? O TYR B 995  
AB2 7 8  N LEU B 996  ? N LEU B 994  O SER B 1217 ? O SER B 1215 
AB2 8 9  O ALA B 1218 ? O ALA B 1216 N LEU B 1095 ? N LEU B 1093 
AB2 9 10 O TYR B 1096 ? O TYR B 1094 N LEU B 1084 ? N LEU B 1082 
AB3 1 2  O SER B 1154 ? O SER B 1152 N ILE B 1130 ? N ILE B 1128 
AB3 2 3  O ALA B 1129 ? O ALA B 1127 N LEU B 1106 ? N LEU B 1104 
AB3 3 4  N VAL B 1107 ? N VAL B 1105 O LEU B 1167 ? O LEU B 1165 
AB3 4 5  N VAL B 1168 ? N VAL B 1166 O GLN B 1193 ? O GLN B 1191 
# 
_pdbx_entry_details.entry_id                   9BBO 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 22   ? ? -157.07 58.51   
2  1 LYS A 124  ? ? -130.79 -47.57  
3  1 GLU A 308  ? ? -120.36 -133.92 
4  1 MET A 452  ? ? -156.04 -49.92  
5  1 VAL A 460  ? ? -120.08 -51.99  
6  1 LYS A 465  ? ? -123.93 -125.08 
7  1 ASP A 597  ? ? -172.15 96.42   
8  1 THR A 689  ? ? -130.78 -46.47  
9  1 HIS A 694  ? ? -104.74 75.82   
10 1 THR A 811  ? A -140.36 35.76   
11 1 THR A 811  ? B -121.75 -160.48 
12 1 GLN A 842  ? ? -91.67  36.14   
13 1 LEU A 970  ? ? -100.51 -88.18  
14 1 ALA B 22   ? ? -156.29 59.41   
15 1 LYS B 124  ? ? -128.88 -52.95  
16 1 SER B 132  ? ? -98.09  40.88   
17 1 HIS B 133  ? ? -155.76 -24.54  
18 1 LEU B 134  ? ? -131.10 -40.48  
19 1 GLU B 308  ? ? -120.81 -133.85 
20 1 MET B 452  ? ? -153.23 -48.83  
21 1 VAL B 460  ? ? -126.81 -50.30  
22 1 LYS B 465  ? ? -118.05 -123.09 
23 1 ASP B 597  ? ? -171.34 96.98   
24 1 HIS B 694  ? ? -103.72 79.07   
25 1 GLN B 842  ? ? -92.02  43.31   
26 1 LEU B 970  ? ? -98.10  -87.05  
27 1 VAL B 1007 ? ? -120.19 -50.02  
28 1 GLN B 1008 ? ? -119.05 78.98   
29 1 ASP B 1154 ? ? -160.84 90.11   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.8637 66.0768 93.8122 0.1280 ? 0.0184 ? 0.0219  ? 0.0852 ? 0.0165  ? 0.1032 ? 0.6666 ? -0.0400 
? 0.2098 ? 0.1451 ? -0.0283 ? 0.2358 ? -0.0397 ? -0.0990 ? 0.0002  ? 0.0527 ? 0.0454 ? 0.0320  ? -0.0227 ? -0.0387 ? -0.0058 ? 
2 'X-RAY DIFFRACTION' ? refined 5.4637   31.2296 92.7031 0.0940 ? 0.0081 ? -0.0114 ? 0.1075 ? -0.0165 ? 0.1038 ? 0.2052 ? -0.0056 
? 0.0749 ? 0.3191 ? -0.0256 ? 0.4949 ? 0.0213  ? -0.0250 ? -0.0154 ? 0.0722 ? 0.0212 ? -0.0195 ? 0.0857  ? -0.0355 ? -0.0378 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2394 ? 5.88 . 
2 1 O ? A HOH 2395 ? 5.88 . 
3 1 O ? B HOH 2386 ? 5.81 . 
4 1 O ? B HOH 2387 ? 5.89 . 
# 
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 SER -1  ? A SER 1   
2  1 Y 1 A MET 0   ? A MET 2   
3  1 Y 1 A MET 1   ? A MET 3   
4  1 Y 1 A SER 2   ? A SER 4   
5  1 Y 1 A PRO 3   ? A PRO 5   
6  1 Y 1 A ASN 4   ? A ASN 6   
7  1 Y 1 A PRO 5   ? A PRO 7   
8  1 Y 1 A LEU 6   ? A LEU 8   
9  1 Y 1 A GLN 7   ? A GLN 9   
10 1 Y 1 A LYS 8   ? A LYS 10  
11 1 Y 1 A PRO 9   ? A PRO 11  
12 1 Y 1 A ALA 10  ? A ALA 12  
13 1 Y 1 A ILE 11  ? A ILE 13  
14 1 Y 1 A ASP 12  ? A ASP 14  
15 1 Y 1 A ALA 13  ? A ALA 15  
16 1 Y 1 A ALA 14  ? A ALA 16  
17 1 Y 1 B SER -1  ? B SER 1   
18 1 Y 1 B MET 0   ? B MET 2   
19 1 Y 1 B MET 1   ? B MET 3   
20 1 Y 1 B SER 2   ? B SER 4   
21 1 Y 1 B PRO 3   ? B PRO 5   
22 1 Y 1 B ASN 4   ? B ASN 6   
23 1 Y 1 B PRO 5   ? B PRO 7   
24 1 Y 1 B LEU 6   ? B LEU 8   
25 1 Y 1 B GLN 7   ? B GLN 9   
26 1 Y 1 B LYS 8   ? B LYS 10  
27 1 Y 1 B PRO 9   ? B PRO 11  
28 1 Y 1 B ALA 10  ? B ALA 12  
29 1 Y 1 B ILE 11  ? B ILE 13  
30 1 Y 1 B ASP 12  ? B ASP 14  
31 1 Y 1 B ALA 13  ? B ALA 15  
32 1 Y 1 B ALA 14  ? B ALA 16  
33 1 Y 1 B GLY 128 ? B GLY 130 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GGL N      N N N 174 
GGL CA     C N S 175 
GGL C      C N N 176 
GGL O      O N N 177 
GGL CB     C N N 178 
GGL CG     C N N 179 
GGL CD     C N N 180 
GGL OE1    O N N 181 
GGL OE2    O N N 182 
GGL OXT    O N N 183 
GGL H      H N N 184 
GGL H2     H N N 185 
GGL HA     H N N 186 
GGL HB2    H N N 187 
GGL HB3    H N N 188 
GGL HG2    H N N 189 
GGL HG3    H N N 190 
GGL HE2    H N N 191 
GGL HXT    H N N 192 
GLN N      N N N 193 
GLN CA     C N S 194 
GLN C      C N N 195 
GLN O      O N N 196 
GLN CB     C N N 197 
GLN CG     C N N 198 
GLN CD     C N N 199 
GLN OE1    O N N 200 
GLN NE2    N N N 201 
GLN OXT    O N N 202 
GLN H      H N N 203 
GLN H2     H N N 204 
GLN HA     H N N 205 
GLN HB2    H N N 206 
GLN HB3    H N N 207 
GLN HG2    H N N 208 
GLN HG3    H N N 209 
GLN HE21   H N N 210 
GLN HE22   H N N 211 
GLN HXT    H N N 212 
GLU N      N N N 213 
GLU CA     C N S 214 
GLU C      C N N 215 
GLU O      O N N 216 
GLU CB     C N N 217 
GLU CG     C N N 218 
GLU CD     C N N 219 
GLU OE1    O N N 220 
GLU OE2    O N N 221 
GLU OXT    O N N 222 
GLU H      H N N 223 
GLU H2     H N N 224 
GLU HA     H N N 225 
GLU HB2    H N N 226 
GLU HB3    H N N 227 
GLU HG2    H N N 228 
GLU HG3    H N N 229 
GLU HE2    H N N 230 
GLU HXT    H N N 231 
GLY N      N N N 232 
GLY CA     C N N 233 
GLY C      C N N 234 
GLY O      O N N 235 
GLY OXT    O N N 236 
GLY H      H N N 237 
GLY H2     H N N 238 
GLY HA2    H N N 239 
GLY HA3    H N N 240 
GLY HXT    H N N 241 
HIS N      N N N 242 
HIS CA     C N S 243 
HIS C      C N N 244 
HIS O      O N N 245 
HIS CB     C N N 246 
HIS CG     C Y N 247 
HIS ND1    N Y N 248 
HIS CD2    C Y N 249 
HIS CE1    C Y N 250 
HIS NE2    N Y N 251 
HIS OXT    O N N 252 
HIS H      H N N 253 
HIS H2     H N N 254 
HIS HA     H N N 255 
HIS HB2    H N N 256 
HIS HB3    H N N 257 
HIS HD1    H N N 258 
HIS HD2    H N N 259 
HIS HE1    H N N 260 
HIS HE2    H N N 261 
HIS HXT    H N N 262 
HOH O      O N N 263 
HOH H1     H N N 264 
HOH H2     H N N 265 
ILE N      N N N 266 
ILE CA     C N S 267 
ILE C      C N N 268 
ILE O      O N N 269 
ILE CB     C N S 270 
ILE CG1    C N N 271 
ILE CG2    C N N 272 
ILE CD1    C N N 273 
ILE OXT    O N N 274 
ILE H      H N N 275 
ILE H2     H N N 276 
ILE HA     H N N 277 
ILE HB     H N N 278 
ILE HG12   H N N 279 
ILE HG13   H N N 280 
ILE HG21   H N N 281 
ILE HG22   H N N 282 
ILE HG23   H N N 283 
ILE HD11   H N N 284 
ILE HD12   H N N 285 
ILE HD13   H N N 286 
ILE HXT    H N N 287 
LEU N      N N N 288 
LEU CA     C N S 289 
LEU C      C N N 290 
LEU O      O N N 291 
LEU CB     C N N 292 
LEU CG     C N N 293 
LEU CD1    C N N 294 
LEU CD2    C N N 295 
LEU OXT    O N N 296 
LEU H      H N N 297 
LEU H2     H N N 298 
LEU HA     H N N 299 
LEU HB2    H N N 300 
LEU HB3    H N N 301 
LEU HG     H N N 302 
LEU HD11   H N N 303 
LEU HD12   H N N 304 
LEU HD13   H N N 305 
LEU HD21   H N N 306 
LEU HD22   H N N 307 
LEU HD23   H N N 308 
LEU HXT    H N N 309 
LYS N      N N N 310 
LYS CA     C N S 311 
LYS C      C N N 312 
LYS O      O N N 313 
LYS CB     C N N 314 
LYS CG     C N N 315 
LYS CD     C N N 316 
LYS CE     C N N 317 
LYS NZ     N N N 318 
LYS OXT    O N N 319 
LYS H      H N N 320 
LYS H2     H N N 321 
LYS HA     H N N 322 
LYS HB2    H N N 323 
LYS HB3    H N N 324 
LYS HG2    H N N 325 
LYS HG3    H N N 326 
LYS HD2    H N N 327 
LYS HD3    H N N 328 
LYS HE2    H N N 329 
LYS HE3    H N N 330 
LYS HZ1    H N N 331 
LYS HZ2    H N N 332 
LYS HZ3    H N N 333 
LYS HXT    H N N 334 
MET N      N N N 335 
MET CA     C N S 336 
MET C      C N N 337 
MET O      O N N 338 
MET CB     C N N 339 
MET CG     C N N 340 
MET SD     S N N 341 
MET CE     C N N 342 
MET OXT    O N N 343 
MET H      H N N 344 
MET H2     H N N 345 
MET HA     H N N 346 
MET HB2    H N N 347 
MET HB3    H N N 348 
MET HG2    H N N 349 
MET HG3    H N N 350 
MET HE1    H N N 351 
MET HE2    H N N 352 
MET HE3    H N N 353 
MET HXT    H N N 354 
PEG C1     C N N 355 
PEG O1     O N N 356 
PEG C2     C N N 357 
PEG O2     O N N 358 
PEG C3     C N N 359 
PEG C4     C N N 360 
PEG O4     O N N 361 
PEG H11    H N N 362 
PEG H12    H N N 363 
PEG HO1    H N N 364 
PEG H21    H N N 365 
PEG H22    H N N 366 
PEG H31    H N N 367 
PEG H32    H N N 368 
PEG H41    H N N 369 
PEG H42    H N N 370 
PEG HO4    H N N 371 
PGE C1     C N N 372 
PGE O1     O N N 373 
PGE C2     C N N 374 
PGE O2     O N N 375 
PGE C3     C N N 376 
PGE C4     C N N 377 
PGE O4     O N N 378 
PGE C6     C N N 379 
PGE C5     C N N 380 
PGE O3     O N N 381 
PGE H1     H N N 382 
PGE H12    H N N 383 
PGE HO1    H N N 384 
PGE H2     H N N 385 
PGE H22    H N N 386 
PGE H3     H N N 387 
PGE H32    H N N 388 
PGE H4     H N N 389 
PGE H42    H N N 390 
PGE HO4    H N N 391 
PGE H6     H N N 392 
PGE H62    H N N 393 
PGE H5     H N N 394 
PGE H52    H N N 395 
PHE N      N N N 396 
PHE CA     C N S 397 
PHE C      C N N 398 
PHE O      O N N 399 
PHE CB     C N N 400 
PHE CG     C Y N 401 
PHE CD1    C Y N 402 
PHE CD2    C Y N 403 
PHE CE1    C Y N 404 
PHE CE2    C Y N 405 
PHE CZ     C Y N 406 
PHE OXT    O N N 407 
PHE H      H N N 408 
PHE H2     H N N 409 
PHE HA     H N N 410 
PHE HB2    H N N 411 
PHE HB3    H N N 412 
PHE HD1    H N N 413 
PHE HD2    H N N 414 
PHE HE1    H N N 415 
PHE HE2    H N N 416 
PHE HZ     H N N 417 
PHE HXT    H N N 418 
PRO N      N N N 419 
PRO CA     C N S 420 
PRO C      C N N 421 
PRO O      O N N 422 
PRO CB     C N N 423 
PRO CG     C N N 424 
PRO CD     C N N 425 
PRO OXT    O N N 426 
PRO H      H N N 427 
PRO HA     H N N 428 
PRO HB2    H N N 429 
PRO HB3    H N N 430 
PRO HG2    H N N 431 
PRO HG3    H N N 432 
PRO HD2    H N N 433 
PRO HD3    H N N 434 
PRO HXT    H N N 435 
SER N      N N N 436 
SER CA     C N S 437 
SER C      C N N 438 
SER O      O N N 439 
SER CB     C N N 440 
SER OG     O N N 441 
SER OXT    O N N 442 
SER H      H N N 443 
SER H2     H N N 444 
SER HA     H N N 445 
SER HB2    H N N 446 
SER HB3    H N N 447 
SER HG     H N N 448 
SER HXT    H N N 449 
SO4 S      S N N 450 
SO4 O1     O N N 451 
SO4 O2     O N N 452 
SO4 O3     O N N 453 
SO4 O4     O N N 454 
THR N      N N N 455 
THR CA     C N S 456 
THR C      C N N 457 
THR O      O N N 458 
THR CB     C N R 459 
THR OG1    O N N 460 
THR CG2    C N N 461 
THR OXT    O N N 462 
THR H      H N N 463 
THR H2     H N N 464 
THR HA     H N N 465 
THR HB     H N N 466 
THR HG1    H N N 467 
THR HG21   H N N 468 
THR HG22   H N N 469 
THR HG23   H N N 470 
THR HXT    H N N 471 
TRP N      N N N 472 
TRP CA     C N S 473 
TRP C      C N N 474 
TRP O      O N N 475 
TRP CB     C N N 476 
TRP CG     C Y N 477 
TRP CD1    C Y N 478 
TRP CD2    C Y N 479 
TRP NE1    N Y N 480 
TRP CE2    C Y N 481 
TRP CE3    C Y N 482 
TRP CZ2    C Y N 483 
TRP CZ3    C Y N 484 
TRP CH2    C Y N 485 
TRP OXT    O N N 486 
TRP H      H N N 487 
TRP H2     H N N 488 
TRP HA     H N N 489 
TRP HB2    H N N 490 
TRP HB3    H N N 491 
TRP HD1    H N N 492 
TRP HE1    H N N 493 
TRP HE3    H N N 494 
TRP HZ2    H N N 495 
TRP HZ3    H N N 496 
TRP HH2    H N N 497 
TRP HXT    H N N 498 
TYR N      N N N 499 
TYR CA     C N S 500 
TYR C      C N N 501 
TYR O      O N N 502 
TYR CB     C N N 503 
TYR CG     C Y N 504 
TYR CD1    C Y N 505 
TYR CD2    C Y N 506 
TYR CE1    C Y N 507 
TYR CE2    C Y N 508 
TYR CZ     C Y N 509 
TYR OH     O N N 510 
TYR OXT    O N N 511 
TYR H      H N N 512 
TYR H2     H N N 513 
TYR HA     H N N 514 
TYR HB2    H N N 515 
TYR HB3    H N N 516 
TYR HD1    H N N 517 
TYR HD2    H N N 518 
TYR HE1    H N N 519 
TYR HE2    H N N 520 
TYR HH     H N N 521 
TYR HXT    H N N 522 
VAL N      N N N 523 
VAL CA     C N S 524 
VAL C      C N N 525 
VAL O      O N N 526 
VAL CB     C N N 527 
VAL CG1    C N N 528 
VAL CG2    C N N 529 
VAL OXT    O N N 530 
VAL H      H N N 531 
VAL H2     H N N 532 
VAL HA     H N N 533 
VAL HB     H N N 534 
VAL HG11   H N N 535 
VAL HG12   H N N 536 
VAL HG13   H N N 537 
VAL HG21   H N N 538 
VAL HG22   H N N 539 
VAL HG23   H N N 540 
VAL HXT    H N N 541 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GGL N     CA     sing N N 174 
GGL N     H      sing N N 175 
GGL N     H2     sing N N 176 
GGL CA    C      sing N N 177 
GGL CA    CB     sing N N 178 
GGL CA    HA     sing N N 179 
GGL C     O      doub N N 180 
GGL C     OXT    sing N N 181 
GGL CB    CG     sing N N 182 
GGL CB    HB2    sing N N 183 
GGL CB    HB3    sing N N 184 
GGL CG    CD     sing N N 185 
GGL CG    HG2    sing N N 186 
GGL CG    HG3    sing N N 187 
GGL CD    OE1    doub N N 188 
GGL CD    OE2    sing N N 189 
GGL OE2   HE2    sing N N 190 
GGL OXT   HXT    sing N N 191 
GLN N     CA     sing N N 192 
GLN N     H      sing N N 193 
GLN N     H2     sing N N 194 
GLN CA    C      sing N N 195 
GLN CA    CB     sing N N 196 
GLN CA    HA     sing N N 197 
GLN C     O      doub N N 198 
GLN C     OXT    sing N N 199 
GLN CB    CG     sing N N 200 
GLN CB    HB2    sing N N 201 
GLN CB    HB3    sing N N 202 
GLN CG    CD     sing N N 203 
GLN CG    HG2    sing N N 204 
GLN CG    HG3    sing N N 205 
GLN CD    OE1    doub N N 206 
GLN CD    NE2    sing N N 207 
GLN NE2   HE21   sing N N 208 
GLN NE2   HE22   sing N N 209 
GLN OXT   HXT    sing N N 210 
GLU N     CA     sing N N 211 
GLU N     H      sing N N 212 
GLU N     H2     sing N N 213 
GLU CA    C      sing N N 214 
GLU CA    CB     sing N N 215 
GLU CA    HA     sing N N 216 
GLU C     O      doub N N 217 
GLU C     OXT    sing N N 218 
GLU CB    CG     sing N N 219 
GLU CB    HB2    sing N N 220 
GLU CB    HB3    sing N N 221 
GLU CG    CD     sing N N 222 
GLU CG    HG2    sing N N 223 
GLU CG    HG3    sing N N 224 
GLU CD    OE1    doub N N 225 
GLU CD    OE2    sing N N 226 
GLU OE2   HE2    sing N N 227 
GLU OXT   HXT    sing N N 228 
GLY N     CA     sing N N 229 
GLY N     H      sing N N 230 
GLY N     H2     sing N N 231 
GLY CA    C      sing N N 232 
GLY CA    HA2    sing N N 233 
GLY CA    HA3    sing N N 234 
GLY C     O      doub N N 235 
GLY C     OXT    sing N N 236 
GLY OXT   HXT    sing N N 237 
HIS N     CA     sing N N 238 
HIS N     H      sing N N 239 
HIS N     H2     sing N N 240 
HIS CA    C      sing N N 241 
HIS CA    CB     sing N N 242 
HIS CA    HA     sing N N 243 
HIS C     O      doub N N 244 
HIS C     OXT    sing N N 245 
HIS CB    CG     sing N N 246 
HIS CB    HB2    sing N N 247 
HIS CB    HB3    sing N N 248 
HIS CG    ND1    sing Y N 249 
HIS CG    CD2    doub Y N 250 
HIS ND1   CE1    doub Y N 251 
HIS ND1   HD1    sing N N 252 
HIS CD2   NE2    sing Y N 253 
HIS CD2   HD2    sing N N 254 
HIS CE1   NE2    sing Y N 255 
HIS CE1   HE1    sing N N 256 
HIS NE2   HE2    sing N N 257 
HIS OXT   HXT    sing N N 258 
HOH O     H1     sing N N 259 
HOH O     H2     sing N N 260 
ILE N     CA     sing N N 261 
ILE N     H      sing N N 262 
ILE N     H2     sing N N 263 
ILE CA    C      sing N N 264 
ILE CA    CB     sing N N 265 
ILE CA    HA     sing N N 266 
ILE C     O      doub N N 267 
ILE C     OXT    sing N N 268 
ILE CB    CG1    sing N N 269 
ILE CB    CG2    sing N N 270 
ILE CB    HB     sing N N 271 
ILE CG1   CD1    sing N N 272 
ILE CG1   HG12   sing N N 273 
ILE CG1   HG13   sing N N 274 
ILE CG2   HG21   sing N N 275 
ILE CG2   HG22   sing N N 276 
ILE CG2   HG23   sing N N 277 
ILE CD1   HD11   sing N N 278 
ILE CD1   HD12   sing N N 279 
ILE CD1   HD13   sing N N 280 
ILE OXT   HXT    sing N N 281 
LEU N     CA     sing N N 282 
LEU N     H      sing N N 283 
LEU N     H2     sing N N 284 
LEU CA    C      sing N N 285 
LEU CA    CB     sing N N 286 
LEU CA    HA     sing N N 287 
LEU C     O      doub N N 288 
LEU C     OXT    sing N N 289 
LEU CB    CG     sing N N 290 
LEU CB    HB2    sing N N 291 
LEU CB    HB3    sing N N 292 
LEU CG    CD1    sing N N 293 
LEU CG    CD2    sing N N 294 
LEU CG    HG     sing N N 295 
LEU CD1   HD11   sing N N 296 
LEU CD1   HD12   sing N N 297 
LEU CD1   HD13   sing N N 298 
LEU CD2   HD21   sing N N 299 
LEU CD2   HD22   sing N N 300 
LEU CD2   HD23   sing N N 301 
LEU OXT   HXT    sing N N 302 
LYS N     CA     sing N N 303 
LYS N     H      sing N N 304 
LYS N     H2     sing N N 305 
LYS CA    C      sing N N 306 
LYS CA    CB     sing N N 307 
LYS CA    HA     sing N N 308 
LYS C     O      doub N N 309 
LYS C     OXT    sing N N 310 
LYS CB    CG     sing N N 311 
LYS CB    HB2    sing N N 312 
LYS CB    HB3    sing N N 313 
LYS CG    CD     sing N N 314 
LYS CG    HG2    sing N N 315 
LYS CG    HG3    sing N N 316 
LYS CD    CE     sing N N 317 
LYS CD    HD2    sing N N 318 
LYS CD    HD3    sing N N 319 
LYS CE    NZ     sing N N 320 
LYS CE    HE2    sing N N 321 
LYS CE    HE3    sing N N 322 
LYS NZ    HZ1    sing N N 323 
LYS NZ    HZ2    sing N N 324 
LYS NZ    HZ3    sing N N 325 
LYS OXT   HXT    sing N N 326 
MET N     CA     sing N N 327 
MET N     H      sing N N 328 
MET N     H2     sing N N 329 
MET CA    C      sing N N 330 
MET CA    CB     sing N N 331 
MET CA    HA     sing N N 332 
MET C     O      doub N N 333 
MET C     OXT    sing N N 334 
MET CB    CG     sing N N 335 
MET CB    HB2    sing N N 336 
MET CB    HB3    sing N N 337 
MET CG    SD     sing N N 338 
MET CG    HG2    sing N N 339 
MET CG    HG3    sing N N 340 
MET SD    CE     sing N N 341 
MET CE    HE1    sing N N 342 
MET CE    HE2    sing N N 343 
MET CE    HE3    sing N N 344 
MET OXT   HXT    sing N N 345 
PEG C1    O1     sing N N 346 
PEG C1    C2     sing N N 347 
PEG C1    H11    sing N N 348 
PEG C1    H12    sing N N 349 
PEG O1    HO1    sing N N 350 
PEG C2    O2     sing N N 351 
PEG C2    H21    sing N N 352 
PEG C2    H22    sing N N 353 
PEG O2    C3     sing N N 354 
PEG C3    C4     sing N N 355 
PEG C3    H31    sing N N 356 
PEG C3    H32    sing N N 357 
PEG C4    O4     sing N N 358 
PEG C4    H41    sing N N 359 
PEG C4    H42    sing N N 360 
PEG O4    HO4    sing N N 361 
PGE C1    O1     sing N N 362 
PGE C1    C2     sing N N 363 
PGE C1    H1     sing N N 364 
PGE C1    H12    sing N N 365 
PGE O1    HO1    sing N N 366 
PGE C2    O2     sing N N 367 
PGE C2    H2     sing N N 368 
PGE C2    H22    sing N N 369 
PGE O2    C3     sing N N 370 
PGE C3    C4     sing N N 371 
PGE C3    H3     sing N N 372 
PGE C3    H32    sing N N 373 
PGE C4    O3     sing N N 374 
PGE C4    H4     sing N N 375 
PGE C4    H42    sing N N 376 
PGE O4    C6     sing N N 377 
PGE O4    HO4    sing N N 378 
PGE C6    C5     sing N N 379 
PGE C6    H6     sing N N 380 
PGE C6    H62    sing N N 381 
PGE C5    O3     sing N N 382 
PGE C5    H5     sing N N 383 
PGE C5    H52    sing N N 384 
PHE N     CA     sing N N 385 
PHE N     H      sing N N 386 
PHE N     H2     sing N N 387 
PHE CA    C      sing N N 388 
PHE CA    CB     sing N N 389 
PHE CA    HA     sing N N 390 
PHE C     O      doub N N 391 
PHE C     OXT    sing N N 392 
PHE CB    CG     sing N N 393 
PHE CB    HB2    sing N N 394 
PHE CB    HB3    sing N N 395 
PHE CG    CD1    doub Y N 396 
PHE CG    CD2    sing Y N 397 
PHE CD1   CE1    sing Y N 398 
PHE CD1   HD1    sing N N 399 
PHE CD2   CE2    doub Y N 400 
PHE CD2   HD2    sing N N 401 
PHE CE1   CZ     doub Y N 402 
PHE CE1   HE1    sing N N 403 
PHE CE2   CZ     sing Y N 404 
PHE CE2   HE2    sing N N 405 
PHE CZ    HZ     sing N N 406 
PHE OXT   HXT    sing N N 407 
PRO N     CA     sing N N 408 
PRO N     CD     sing N N 409 
PRO N     H      sing N N 410 
PRO CA    C      sing N N 411 
PRO CA    CB     sing N N 412 
PRO CA    HA     sing N N 413 
PRO C     O      doub N N 414 
PRO C     OXT    sing N N 415 
PRO CB    CG     sing N N 416 
PRO CB    HB2    sing N N 417 
PRO CB    HB3    sing N N 418 
PRO CG    CD     sing N N 419 
PRO CG    HG2    sing N N 420 
PRO CG    HG3    sing N N 421 
PRO CD    HD2    sing N N 422 
PRO CD    HD3    sing N N 423 
PRO OXT   HXT    sing N N 424 
SER N     CA     sing N N 425 
SER N     H      sing N N 426 
SER N     H2     sing N N 427 
SER CA    C      sing N N 428 
SER CA    CB     sing N N 429 
SER CA    HA     sing N N 430 
SER C     O      doub N N 431 
SER C     OXT    sing N N 432 
SER CB    OG     sing N N 433 
SER CB    HB2    sing N N 434 
SER CB    HB3    sing N N 435 
SER OG    HG     sing N N 436 
SER OXT   HXT    sing N N 437 
SO4 S     O1     doub N N 438 
SO4 S     O2     doub N N 439 
SO4 S     O3     sing N N 440 
SO4 S     O4     sing N N 441 
THR N     CA     sing N N 442 
THR N     H      sing N N 443 
THR N     H2     sing N N 444 
THR CA    C      sing N N 445 
THR CA    CB     sing N N 446 
THR CA    HA     sing N N 447 
THR C     O      doub N N 448 
THR C     OXT    sing N N 449 
THR CB    OG1    sing N N 450 
THR CB    CG2    sing N N 451 
THR CB    HB     sing N N 452 
THR OG1   HG1    sing N N 453 
THR CG2   HG21   sing N N 454 
THR CG2   HG22   sing N N 455 
THR CG2   HG23   sing N N 456 
THR OXT   HXT    sing N N 457 
TRP N     CA     sing N N 458 
TRP N     H      sing N N 459 
TRP N     H2     sing N N 460 
TRP CA    C      sing N N 461 
TRP CA    CB     sing N N 462 
TRP CA    HA     sing N N 463 
TRP C     O      doub N N 464 
TRP C     OXT    sing N N 465 
TRP CB    CG     sing N N 466 
TRP CB    HB2    sing N N 467 
TRP CB    HB3    sing N N 468 
TRP CG    CD1    doub Y N 469 
TRP CG    CD2    sing Y N 470 
TRP CD1   NE1    sing Y N 471 
TRP CD1   HD1    sing N N 472 
TRP CD2   CE2    doub Y N 473 
TRP CD2   CE3    sing Y N 474 
TRP NE1   CE2    sing Y N 475 
TRP NE1   HE1    sing N N 476 
TRP CE2   CZ2    sing Y N 477 
TRP CE3   CZ3    doub Y N 478 
TRP CE3   HE3    sing N N 479 
TRP CZ2   CH2    doub Y N 480 
TRP CZ2   HZ2    sing N N 481 
TRP CZ3   CH2    sing Y N 482 
TRP CZ3   HZ3    sing N N 483 
TRP CH2   HH2    sing N N 484 
TRP OXT   HXT    sing N N 485 
TYR N     CA     sing N N 486 
TYR N     H      sing N N 487 
TYR N     H2     sing N N 488 
TYR CA    C      sing N N 489 
TYR CA    CB     sing N N 490 
TYR CA    HA     sing N N 491 
TYR C     O      doub N N 492 
TYR C     OXT    sing N N 493 
TYR CB    CG     sing N N 494 
TYR CB    HB2    sing N N 495 
TYR CB    HB3    sing N N 496 
TYR CG    CD1    doub Y N 497 
TYR CG    CD2    sing Y N 498 
TYR CD1   CE1    sing Y N 499 
TYR CD1   HD1    sing N N 500 
TYR CD2   CE2    doub Y N 501 
TYR CD2   HD2    sing N N 502 
TYR CE1   CZ     doub Y N 503 
TYR CE1   HE1    sing N N 504 
TYR CE2   CZ     sing Y N 505 
TYR CE2   HE2    sing N N 506 
TYR CZ    OH     sing N N 507 
TYR OH    HH     sing N N 508 
TYR OXT   HXT    sing N N 509 
VAL N     CA     sing N N 510 
VAL N     H      sing N N 511 
VAL N     H2     sing N N 512 
VAL CA    C      sing N N 513 
VAL CA    CB     sing N N 514 
VAL CA    HA     sing N N 515 
VAL C     O      doub N N 516 
VAL C     OXT    sing N N 517 
VAL CB    CG1    sing N N 518 
VAL CB    CG2    sing N N 519 
VAL CB    HB     sing N N 520 
VAL CG1   HG11   sing N N 521 
VAL CG1   HG12   sing N N 522 
VAL CG1   HG13   sing N N 523 
VAL CG2   HG21   sing N N 524 
VAL CG2   HG22   sing N N 525 
VAL CG2   HG23   sing N N 526 
VAL OXT   HXT    sing N N 527 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01GM065546 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5KF6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BBO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009864 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002899 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009762 
_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]   0.008169 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N     . PRO A 1 17   ? -48.988 90.791  104.257 1.00 43.30 ?  15   PRO A N     1 
ATOM   2     C CA    . PRO A 1 17   ? -49.470 89.410  104.131 1.00 37.48 ?  15   PRO A CA    1 
ATOM   3     C C     . PRO A 1 17   ? -49.076 88.551  105.331 1.00 36.21 ?  15   PRO A C     1 
ATOM   4     O O     . PRO A 1 17   ? -47.913 88.582  105.751 1.00 34.41 ?  15   PRO A O     1 
ATOM   5     C CB    . PRO A 1 17   ? -48.786 88.910  102.854 1.00 41.31 ?  15   PRO A CB    1 
ATOM   6     C CG    . PRO A 1 17   ? -48.434 90.146  102.096 1.00 39.59 ?  15   PRO A CG    1 
ATOM   7     C CD    . PRO A 1 17   ? -48.117 91.176  103.134 1.00 38.45 ?  15   PRO A CD    1 
ATOM   8     N N     . ALA A 1 18   ? -50.033 87.794  105.866 1.00 32.56 ?  16   ALA A N     1 
ATOM   9     C CA    . ALA A 1 18   ? -49.772 86.999  107.057 1.00 32.54 ?  16   ALA A CA    1 
ATOM   10    C C     . ALA A 1 18   ? -48.685 85.966  106.765 1.00 31.16 ?  16   ALA A C     1 
ATOM   11    O O     . ALA A 1 18   ? -48.642 85.405  105.663 1.00 30.48 ?  16   ALA A O     1 
ATOM   12    C CB    . ALA A 1 18   ? -51.051 86.306  107.530 1.00 33.93 ?  16   ALA A CB    1 
ATOM   13    N N     . PRO A 1 19   ? -47.782 85.709  107.710 1.00 28.61 ?  17   PRO A N     1 
ATOM   14    C CA    . PRO A 1 19   ? -46.703 84.747  107.450 1.00 29.00 ?  17   PRO A CA    1 
ATOM   15    C C     . PRO A 1 19   ? -47.265 83.357  107.199 1.00 27.74 ?  17   PRO A C     1 
ATOM   16    O O     . PRO A 1 19   ? -48.091 82.850  107.966 1.00 27.76 ?  17   PRO A O     1 
ATOM   17    C CB    . PRO A 1 19   ? -45.856 84.805  108.729 1.00 27.30 ?  17   PRO A CB    1 
ATOM   18    C CG    . PRO A 1 19   ? -46.174 86.132  109.338 1.00 32.40 ?  17   PRO A CG    1 
ATOM   19    C CD    . PRO A 1 19   ? -47.623 86.381  109.011 1.00 28.34 ?  17   PRO A CD    1 
ATOM   20    N N     . PHE A 1 20   ? -46.833 82.766  106.086 1.00 26.77 ?  18   PHE A N     1 
ATOM   21    C CA    . PHE A 1 20   ? -47.097 81.387  105.693 1.00 25.01 ?  18   PHE A CA    1 
ATOM   22    C C     . PHE A 1 20   ? -48.561 81.119  105.384 1.00 25.01 ?  18   PHE A C     1 
ATOM   23    O O     . PHE A 1 20   ? -48.954 79.956  105.281 1.00 26.80 ?  18   PHE A O     1 
ATOM   24    C CB    . PHE A 1 20   ? -46.606 80.403  106.759 1.00 24.00 ?  18   PHE A CB    1 
ATOM   25    C CG    . PHE A 1 20   ? -45.135 80.520  107.057 1.00 22.81 ?  18   PHE A CG    1 
ATOM   26    C CD1   . PHE A 1 20   ? -44.193 80.049  106.157 1.00 22.33 ?  18   PHE A CD1   1 
ATOM   27    C CD2   . PHE A 1 20   ? -44.697 81.103  108.234 1.00 23.12 ?  18   PHE A CD2   1 
ATOM   28    C CE1   . PHE A 1 20   ? -42.842 80.159  106.434 1.00 23.30 ?  18   PHE A CE1   1 
ATOM   29    C CE2   . PHE A 1 20   ? -43.354 81.208  108.521 1.00 25.70 ?  18   PHE A CE2   1 
ATOM   30    C CZ    . PHE A 1 20   ? -42.424 80.740  107.625 1.00 22.03 ?  18   PHE A CZ    1 
ATOM   31    N N     . ALA A 1 21   ? -49.378 82.160  105.220 1.00 26.83 ?  19   ALA A N     1 
ATOM   32    C CA    . ALA A 1 21   ? -50.781 81.948  104.882 1.00 28.75 ?  19   ALA A CA    1 
ATOM   33    C C     . ALA A 1 21   ? -50.963 81.376  103.481 1.00 30.80 ?  19   ALA A C     1 
ATOM   34    O O     . ALA A 1 21   ? -52.048 80.879  103.162 1.00 33.08 ?  19   ALA A O     1 
ATOM   35    C CB    . ALA A 1 21   ? -51.554 83.259  105.012 1.00 30.77 ?  19   ALA A CB    1 
ATOM   36    N N     . ASP A 1 22   ? -49.938 81.433  102.638 1.00 25.13 ?  20   ASP A N     1 
ATOM   37    C CA    . ASP A 1 22   ? -50.024 80.926  101.276 1.00 30.69 ?  20   ASP A CA    1 
ATOM   38    C C     . ASP A 1 22   ? -48.821 80.057  100.961 1.00 24.88 ?  20   ASP A C     1 
ATOM   39    O O     . ASP A 1 22   ? -48.305 80.058  99.839  1.00 23.52 ?  20   ASP A O     1 
ATOM   40    C CB    . ASP A 1 22   ? -50.137 82.070  100.272 1.00 32.96 ?  20   ASP A CB    1 
ATOM   41    C CG    . ASP A 1 22   ? -51.510 82.715  100.276 1.00 42.71 ?  20   ASP A CG    1 
ATOM   42    O OD1   . ASP A 1 22   ? -52.517 81.976  100.363 1.00 46.76 ?  20   ASP A OD1   1 
ATOM   43    O OD2   . ASP A 1 22   ? -51.580 83.960  100.193 1.00 46.68 ?  20   ASP A OD2   1 
ATOM   44    N N     . PHE A 1 23   ? -48.349 79.305  101.959 1.00 19.89 ?  21   PHE A N     1 
ATOM   45    C CA    . PHE A 1 23   ? -47.078 78.603  101.808 1.00 18.94 ?  21   PHE A CA    1 
ATOM   46    C C     . PHE A 1 23   ? -47.127 77.587  100.669 1.00 17.01 ?  21   PHE A C     1 
ATOM   47    O O     . PHE A 1 23   ? -46.276 77.602  99.769  1.00 17.41 ?  21   PHE A O     1 
ATOM   48    C CB    . PHE A 1 23   ? -46.685 77.918  103.118 1.00 18.95 ?  21   PHE A CB    1 
ATOM   49    C CG    . PHE A 1 23   ? -45.452 77.070  102.997 1.00 18.15 ?  21   PHE A CG    1 
ATOM   50    C CD1   . PHE A 1 23   ? -44.234 77.652  102.706 1.00 18.46 ?  21   PHE A CD1   1 
ATOM   51    C CD2   . PHE A 1 23   ? -45.518 75.696  103.163 1.00 20.33 ?  21   PHE A CD2   1 
ATOM   52    C CE1   . PHE A 1 23   ? -43.095 76.883  102.578 1.00 19.00 ?  21   PHE A CE1   1 
ATOM   53    C CE2   . PHE A 1 23   ? -44.384 74.917  103.040 1.00 20.41 ?  21   PHE A CE2   1 
ATOM   54    C CZ    . PHE A 1 23   ? -43.171 75.513  102.742 1.00 18.81 ?  21   PHE A CZ    1 
ATOM   55    N N     . ALA A 1 24   ? -48.081 76.657  100.721 1.00 18.82 ?  22   ALA A N     1 
ATOM   56    C CA    . ALA A 1 24   ? -48.135 75.616  99.699  1.00 18.77 ?  22   ALA A CA    1 
ATOM   57    C C     . ALA A 1 24   ? -49.528 75.013  99.572  1.00 18.49 ?  22   ALA A C     1 
ATOM   58    O O     . ALA A 1 24   ? -49.689 73.795  99.711  1.00 17.93 ?  22   ALA A O     1 
ATOM   59    C CB    . ALA A 1 24   ? -47.130 74.510  100.015 1.00 22.65 ?  22   ALA A CB    1 
ATOM   60    N N     . PRO A 1 25   ? -50.546 75.811  99.275  1.00 21.00 ?  23   PRO A N     1 
ATOM   61    C CA    . PRO A 1 25   ? -51.902 75.269  99.173  1.00 19.18 ?  23   PRO A CA    1 
ATOM   62    C C     . PRO A 1 25   ? -51.997 74.294  98.014  1.00 18.60 ?  23   PRO A C     1 
ATOM   63    O O     . PRO A 1 25   ? -51.421 74.534  96.943  1.00 20.83 ?  23   PRO A O     1 
ATOM   64    C CB    . PRO A 1 25   ? -52.759 76.518  98.926  1.00 20.47 ?  23   PRO A CB    1 
ATOM   65    C CG    . PRO A 1 25   ? -51.829 77.445  98.217  1.00 22.12 ?  23   PRO A CG    1 
ATOM   66    C CD    . PRO A 1 25   ? -50.479 77.217  98.846  1.00 19.77 ?  23   PRO A CD    1 
ATOM   67    N N     . PRO A 1 26   ? -52.690 73.174  98.197  1.00 19.42 ?  24   PRO A N     1 
ATOM   68    C CA    . PRO A 1 26   ? -52.799 72.192  97.115  1.00 19.40 ?  24   PRO A CA    1 
ATOM   69    C C     . PRO A 1 26   ? -53.647 72.717  95.966  1.00 22.08 ?  24   PRO A C     1 
ATOM   70    O O     . PRO A 1 26   ? -54.442 73.649  96.113  1.00 20.50 ?  24   PRO A O     1 
ATOM   71    C CB    . PRO A 1 26   ? -53.464 70.988  97.791  1.00 20.21 ?  24   PRO A CB    1 
ATOM   72    C CG    . PRO A 1 26   ? -54.233 71.585  98.925  1.00 22.16 ?  24   PRO A CG    1 
ATOM   73    C CD    . PRO A 1 26   ? -53.426 72.762  99.405  1.00 23.07 ?  24   PRO A CD    1 
ATOM   74    N N     . VAL A 1 27   ? -53.446 72.093  94.799  1.00 18.69 ?  25   VAL A N     1 
ATOM   75    C CA    . VAL A 1 27   ? -54.193 72.456  93.593  1.00 21.23 ?  25   VAL A CA    1 
ATOM   76    C C     . VAL A 1 27   ? -55.691 72.329  93.827  1.00 20.96 ?  25   VAL A C     1 
ATOM   77    O O     . VAL A 1 27   ? -56.479 73.162  93.361  1.00 24.49 ?  25   VAL A O     1 
ATOM   78    C CB    . VAL A 1 27   ? -53.732 71.584  92.409  1.00 21.13 ?  25   VAL A CB    1 
ATOM   79    C CG1   . VAL A 1 27   ? -54.683 71.733  91.218  1.00 23.82 ?  25   VAL A CG1   1 
ATOM   80    C CG2   . VAL A 1 27   ? -52.318 71.945  92.010  1.00 21.26 ?  25   VAL A CG2   1 
ATOM   81    N N     . ARG A 1 28   ? -56.105 71.296  94.548  1.00 25.40 ?  26   ARG A N     1 
ATOM   82    C CA    . ARG A 1 28   ? -57.504 71.066  94.874  1.00 22.74 ?  26   ARG A CA    1 
ATOM   83    C C     . ARG A 1 28   ? -57.561 70.388  96.231  1.00 27.67 ?  26   ARG A C     1 
ATOM   84    O O     . ARG A 1 28   ? -56.566 69.805  96.680  1.00 23.90 ?  26   ARG A O     1 
ATOM   85    C CB    . ARG A 1 28   ? -58.189 70.201  93.807  1.00 26.01 ?  26   ARG A CB    1 
ATOM   86    C CG    . ARG A 1 28   ? -57.695 68.752  93.772  1.00 24.08 ?  26   ARG A CG    1 
ATOM   87    C CD    . ARG A 1 28   ? -58.294 67.966  92.598  1.00 27.89 ?  26   ARG A CD    1 
ATOM   88    N NE    . ARG A 1 28   ? -57.612 68.267  91.340  1.00 27.46 ?  26   ARG A NE    1 
ATOM   89    C CZ    . ARG A 1 28   ? -58.042 69.143  90.442  1.00 29.76 ?  26   ARG A CZ    1 
ATOM   90    N NH1   . ARG A 1 28   ? -59.190 69.783  90.593  1.00 31.86 ?  26   ARG A NH1   1 
ATOM   91    N NH2   . ARG A 1 28   ? -57.295 69.391  89.371  1.00 29.57 ?  26   ARG A NH2   1 
ATOM   92    N N     . PRO A 1 29   ? -58.696 70.457  96.925  1.00 24.57 ?  27   PRO A N     1 
ATOM   93    C CA    . PRO A 1 29   ? -58.819 69.674  98.156  1.00 24.83 ?  27   PRO A CA    1 
ATOM   94    C C     . PRO A 1 29   ? -58.631 68.198  97.842  1.00 22.79 ?  27   PRO A C     1 
ATOM   95    O O     . PRO A 1 29   ? -59.077 67.700  96.806  1.00 25.93 ?  27   PRO A O     1 
ATOM   96    C CB    . PRO A 1 29   ? -60.239 69.989  98.644  1.00 27.40 ?  27   PRO A CB    1 
ATOM   97    C CG    . PRO A 1 29   ? -60.531 71.334  98.072  1.00 28.77 ?  27   PRO A CG    1 
ATOM   98    C CD    . PRO A 1 29   ? -59.858 71.344  96.722  1.00 26.85 ?  27   PRO A CD    1 
ATOM   99    N N     . GLN A 1 30   ? -57.948 67.501  98.739  1.00 25.61 ?  28   GLN A N     1 
ATOM   100   C CA    . GLN A 1 30   ? -57.579 66.116  98.486  1.00 24.70 ?  28   GLN A CA    1 
ATOM   101   C C     . GLN A 1 30   ? -58.748 65.194  98.829  1.00 22.78 ?  28   GLN A C     1 
ATOM   102   O O     . GLN A 1 30   ? -59.178 65.130  99.988  1.00 25.41 ?  28   GLN A O     1 
ATOM   103   C CB    . GLN A 1 30   ? -56.332 65.762  99.295  1.00 23.41 ?  28   GLN A CB    1 
ATOM   104   C CG    . GLN A 1 30   ? -55.154 66.722  99.047  1.00 19.76 ?  28   GLN A CG    1 
ATOM   105   C CD    . GLN A 1 30   ? -54.570 66.577  97.646  1.00 20.46 ?  28   GLN A CD    1 
ATOM   106   O OE1   . GLN A 1 30   ? -53.836 65.632  97.372  1.00 20.86 ?  28   GLN A OE1   1 
ATOM   107   N NE2   . GLN A 1 30   ? -54.898 67.515  96.752  1.00 20.72 ?  28   GLN A NE2   1 
ATOM   108   N N     . SER A 1 31   ? -59.258 64.480  97.823  1.00 21.78 ?  29   SER A N     1 
ATOM   109   C CA    . SER A 1 31   ? -60.327 63.512  98.048  1.00 21.11 ?  29   SER A CA    1 
ATOM   110   C C     . SER A 1 31   ? -59.823 62.332  98.873  1.00 21.65 ?  29   SER A C     1 
ATOM   111   O O     . SER A 1 31   ? -58.622 62.158  99.097  1.00 22.58 ?  29   SER A O     1 
ATOM   112   C CB    . SER A 1 31   ? -60.860 62.978  96.725  1.00 20.32 ?  29   SER A CB    1 
ATOM   113   O OG    . SER A 1 31   ? -59.864 62.155  96.120  1.00 19.49 ?  29   SER A OG    1 
ATOM   114   N N     . THR A 1 32   ? -60.770 61.496  99.315  1.00 20.47 ?  30   THR A N     1 
ATOM   115   C CA    . THR A 1 32   ? -60.405 60.272  100.021 1.00 20.73 ?  30   THR A CA    1 
ATOM   116   C C     . THR A 1 32   ? -59.467 59.414  99.181  1.00 20.90 ?  30   THR A C     1 
ATOM   117   O O     . THR A 1 32   ? -58.468 58.888  99.693  1.00 20.74 ?  30   THR A O     1 
ATOM   118   C CB    . THR A 1 32   ? -61.668 59.494  100.401 1.00 21.55 ?  30   THR A CB    1 
ATOM   119   O OG1   . THR A 1 32   ? -62.489 60.319  101.234 1.00 28.71 ?  30   THR A OG1   1 
ATOM   120   C CG2   . THR A 1 32   ? -61.317 58.229  101.146 1.00 24.98 ?  30   THR A CG2   1 
ATOM   121   N N     . LEU A 1 33   ? -59.762 59.275  97.886  1.00 20.03 ?  31   LEU A N     1 
ATOM   122   C CA    . LEU A 1 33   ? -58.893 58.491  97.016  1.00 18.09 ?  31   LEU A CA    1 
ATOM   123   C C     . LEU A 1 33   ? -57.523 59.136  96.875  1.00 20.79 ?  31   LEU A C     1 
ATOM   124   O O     . LEU A 1 33   ? -56.505 58.438  96.882  1.00 17.99 ?  31   LEU A O     1 
ATOM   125   C CB    . LEU A 1 33   ? -59.546 58.324  95.651  1.00 19.17 ?  31   LEU A CB    1 
ATOM   126   C CG    . LEU A 1 33   ? -60.697 57.327  95.664  1.00 20.31 ?  31   LEU A CG    1 
ATOM   127   C CD1   . LEU A 1 33   ? -61.526 57.449  94.407  1.00 22.17 ?  31   LEU A CD1   1 
ATOM   128   C CD2   . LEU A 1 33   ? -60.148 55.912  95.833  1.00 24.24 ?  31   LEU A CD2   1 
ATOM   129   N N     . ARG A 1 34   ? -57.471 60.463  96.749  1.00 16.46 ?  32   ARG A N     1 
ATOM   130   C CA    . ARG A 1 34   ? -56.166 61.113  96.641  1.00 15.79 ?  32   ARG A CA    1 
ATOM   131   C C     . ARG A 1 34   ? -55.371 60.966  97.934  1.00 17.02 ?  32   ARG A C     1 
ATOM   132   O O     . ARG A 1 34   ? -54.152 60.780  97.894  1.00 18.85 ?  32   ARG A O     1 
ATOM   133   C CB    . ARG A 1 34   ? -56.329 62.587  96.272  1.00 19.30 ?  32   ARG A CB    1 
ATOM   134   C CG    . ARG A 1 34   ? -56.743 62.816  94.826  1.00 18.19 ?  32   ARG A CG    1 
ATOM   135   C CD    . ARG A 1 34   ? -55.595 62.576  93.824  1.00 18.77 ?  32   ARG A CD    1 
ATOM   136   N NE    . ARG A 1 34   ? -54.463 63.486  93.985  1.00 19.66 ?  32   ARG A NE    1 
ATOM   137   C CZ    . ARG A 1 34   ? -54.341 64.649  93.355  1.00 20.71 ?  32   ARG A CZ    1 
ATOM   138   N NH1   . ARG A 1 34   ? -55.293 65.106  92.552  1.00 20.71 ?  32   ARG A NH1   1 
ATOM   139   N NH2   . ARG A 1 34   ? -53.235 65.370  93.528  1.00 22.46 ?  32   ARG A NH2   1 
ATOM   140   N N     . ARG A 1 35   ? -56.043 61.015  99.093  1.00 17.21 ?  33   ARG A N     1 
ATOM   141   C CA    . ARG A 1 35   ? -55.315 60.884  100.351 1.00 18.55 ?  33   ARG A CA    1 
ATOM   142   C C     . ARG A 1 35   ? -54.751 59.482  100.537 1.00 17.43 ?  33   ARG A C     1 
ATOM   143   O O     . ARG A 1 35   ? -53.685 59.323  101.142 1.00 18.36 ?  33   ARG A O     1 
ATOM   144   C CB    . ARG A 1 35   ? -56.223 61.264  101.522 1.00 20.65 ?  33   ARG A CB    1 
ATOM   145   C CG    . ARG A 1 35   ? -56.513 62.752  101.544 1.00 21.45 ?  33   ARG A CG    1 
ATOM   146   C CD    . ARG A 1 35   ? -57.575 63.149  102.571 1.00 26.51 ?  33   ARG A CD    1 
ATOM   147   N NE    . ARG A 1 35   ? -57.781 64.591  102.501 1.00 31.99 ?  33   ARG A NE    1 
ATOM   148   C CZ    . ARG A 1 35   ? -57.049 65.483  103.155 1.00 36.69 ?  33   ARG A CZ    1 
ATOM   149   N NH1   . ARG A 1 35   ? -56.112 65.113  104.014 1.00 41.84 ?  33   ARG A NH1   1 
ATOM   150   N NH2   . ARG A 1 35   ? -57.259 66.780  102.940 1.00 40.07 ?  33   ARG A NH2   1 
ATOM   151   N N     . ALA A 1 36   ? -55.443 58.457  100.028 1.00 17.01 ?  34   ALA A N     1 
ATOM   152   C CA    . ALA A 1 36   ? -54.906 57.100  100.119 1.00 19.41 ?  34   ALA A CA    1 
ATOM   153   C C     . ALA A 1 36   ? -53.634 56.949  99.299  1.00 19.79 ?  34   ALA A C     1 
ATOM   154   O O     . ALA A 1 36   ? -52.742 56.177  99.670  1.00 18.98 ?  34   ALA A O     1 
ATOM   155   C CB    . ALA A 1 36   ? -55.949 56.080  99.657  1.00 20.38 ?  34   ALA A CB    1 
ATOM   156   N N     . ILE A 1 37   ? -53.541 57.668  98.182  1.00 15.11 ?  35   ILE A N     1 
ATOM   157   C CA    . ILE A 1 37   ? -52.301 57.694  97.411  1.00 15.60 ?  35   ILE A CA    1 
ATOM   158   C C     . ILE A 1 37   ? -51.176 58.288  98.246  1.00 16.86 ?  35   ILE A C     1 
ATOM   159   O O     . ILE A 1 37   ? -50.121 57.673  98.434  1.00 16.39 ?  35   ILE A O     1 
ATOM   160   C CB    . ILE A 1 37   ? -52.504 58.479  96.106  1.00 14.36 ?  35   ILE A CB    1 
ATOM   161   C CG1   . ILE A 1 37   ? -53.480 57.752  95.193  1.00 14.49 ?  35   ILE A CG1   1 
ATOM   162   C CG2   . ILE A 1 37   ? -51.169 58.673  95.389  1.00 14.76 ?  35   ILE A CG2   1 
ATOM   163   C CD1   . ILE A 1 37   ? -53.933 58.623  94.025  1.00 15.87 ?  35   ILE A CD1   1 
ATOM   164   N N     . THR A 1 38   ? -51.390 59.494  98.769  1.00 17.39 ?  36   THR A N     1 
ATOM   165   C CA    . THR A 1 38   ? -50.325 60.168  99.501  1.00 16.71 ?  36   THR A CA    1 
ATOM   166   C C     . THR A 1 38   ? -49.904 59.358  100.713 1.00 17.25 ?  36   THR A C     1 
ATOM   167   O O     . THR A 1 38   ? -48.717 59.306  101.048 1.00 15.82 ?  36   THR A O     1 
ATOM   168   C CB    . THR A 1 38   ? -50.782 61.554  99.931  1.00 15.09 ?  36   THR A CB    1 
ATOM   169   O OG1   . THR A 1 38   ? -51.292 62.256  98.800  1.00 16.48 ?  36   THR A OG1   1 
ATOM   170   C CG2   . THR A 1 38   ? -49.649 62.341  100.550 1.00 18.10 ?  36   THR A CG2   1 
ATOM   171   N N     . ALA A 1 39   ? -50.863 58.688  101.357 1.00 17.12 ?  37   ALA A N     1 
ATOM   172   C CA    . ALA A 1 39   ? -50.553 57.900  102.544 1.00 18.42 ?  37   ALA A CA    1 
ATOM   173   C C     . ALA A 1 39   ? -49.588 56.754  102.257 1.00 20.18 ?  37   ALA A C     1 
ATOM   174   O O     . ALA A 1 39   ? -48.883 56.311  103.170 1.00 19.95 ?  37   ALA A O     1 
ATOM   175   C CB    . ALA A 1 39   ? -51.844 57.348  103.160 1.00 19.38 ?  37   ALA A CB    1 
ATOM   176   N N     . ALA A 1 40   ? -49.526 56.279  101.016 1.00 17.71 ?  38   ALA A N     1 
ATOM   177   C CA    . ALA A 1 40   ? -48.681 55.145  100.661 1.00 17.94 ?  38   ALA A CA    1 
ATOM   178   C C     . ALA A 1 40   ? -47.309 55.549  100.139 1.00 16.44 ?  38   ALA A C     1 
ATOM   179   O O     . ALA A 1 40   ? -46.511 54.663  99.841  1.00 16.72 ?  38   ALA A O     1 
ATOM   180   C CB    . ALA A 1 40   ? -49.376 54.279  99.608  1.00 17.23 ?  38   ALA A CB    1 
ATOM   181   N N     . TYR A 1 41   ? -47.025 56.853  100.033 1.00 15.36 ?  39   TYR A N     1 
ATOM   182   C CA    . TYR A 1 41   ? -45.840 57.352  99.327  1.00 14.68 ?  39   TYR A CA    1 
ATOM   183   C C     . TYR A 1 41   ? -44.571 56.599  99.724  1.00 15.70 ?  39   TYR A C     1 
ATOM   184   O O     . TYR A 1 41   ? -43.826 56.101  98.867  1.00 15.77 ?  39   TYR A O     1 
ATOM   185   C CB    . TYR A 1 41   ? -45.705 58.856  99.606  1.00 14.90 ?  39   TYR A CB    1 
ATOM   186   C CG    . TYR A 1 41   ? -44.955 59.716  98.591  1.00 13.87 ?  39   TYR A CG    1 
ATOM   187   C CD1   . TYR A 1 41   ? -43.860 59.238  97.886  1.00 15.79 ?  39   TYR A CD1   1 
ATOM   188   C CD2   . TYR A 1 41   ? -45.335 61.049  98.381  1.00 14.41 ?  39   TYR A CD2   1 
ATOM   189   C CE1   . TYR A 1 41   ? -43.167 60.053  96.993  1.00 14.63 ?  39   TYR A CE1   1 
ATOM   190   C CE2   . TYR A 1 41   ? -44.651 61.866  97.488  1.00 14.35 ?  39   TYR A CE2   1 
ATOM   191   C CZ    . TYR A 1 41   ? -43.564 61.363  96.804  1.00 13.53 ?  39   TYR A CZ    1 
ATOM   192   O OH    . TYR A 1 41   ? -42.886 62.172  95.926  1.00 15.34 ?  39   TYR A OH    1 
ATOM   193   N N     . ARG A 1 42   ? -44.308 56.500  101.021 1.00 17.34 ?  40   ARG A N     1 
ATOM   194   C CA    . ARG A 1 42   ? -43.089 55.855  101.499 1.00 17.30 ?  40   ARG A CA    1 
ATOM   195   C C     . ARG A 1 42   ? -43.414 54.780  102.520 1.00 17.74 ?  40   ARG A C     1 
ATOM   196   O O     . ARG A 1 42   ? -42.666 54.553  103.481 1.00 21.20 ?  40   ARG A O     1 
ATOM   197   C CB    . ARG A 1 42   ? -42.117 56.891  102.060 1.00 19.40 ?  40   ARG A CB    1 
ATOM   198   C CG    . ARG A 1 42   ? -41.562 57.788  100.949 1.00 17.97 ?  40   ARG A CG    1 
ATOM   199   C CD    . ARG A 1 42   ? -40.775 58.964  101.451 1.00 21.39 ?  40   ARG A CD    1 
ATOM   200   N NE    . ARG A 1 42   ? -40.773 59.994  100.419 1.00 19.21 ?  40   ARG A NE    1 
ATOM   201   C CZ    . ARG A 1 42   ? -39.967 60.000  99.368  1.00 17.17 ?  40   ARG A CZ    1 
ATOM   202   N NH1   . ARG A 1 42   ? -39.001 59.098  99.228  1.00 17.74 ?  40   ARG A NH1   1 
ATOM   203   N NH2   . ARG A 1 42   ? -40.129 60.932  98.433  1.00 16.25 ?  40   ARG A NH2   1 
ATOM   204   N N     . ARG A 1 43   ? -44.526 54.093  102.308 1.00 17.64 ?  41   ARG A N     1 
ATOM   205   C CA    . ARG A 1 43   ? -44.952 53.033  103.212 1.00 17.21 ?  41   ARG A CA    1 
ATOM   206   C C     . ARG A 1 43   ? -43.893 51.936  103.280 1.00 19.59 ?  41   ARG A C     1 
ATOM   207   O O     . ARG A 1 43   ? -43.334 51.554  102.244 1.00 19.28 ?  41   ARG A O     1 
ATOM   208   C CB    . ARG A 1 43   ? -46.280 52.456  102.722 1.00 18.49 ?  41   ARG A CB    1 
ATOM   209   C CG    . ARG A 1 43   ? -46.772 51.234  103.471 1.00 18.40 ?  41   ARG A CG    1 
ATOM   210   C CD    . ARG A 1 43   ? -48.211 50.977  103.102 1.00 21.77 ?  41   ARG A CD    1 
ATOM   211   N NE    . ARG A 1 43   ? -49.051 52.123  103.445 1.00 22.04 ?  41   ARG A NE    1 
ATOM   212   C CZ    . ARG A 1 43   ? -50.191 52.435  102.843 1.00 21.05 ?  41   ARG A CZ    1 
ATOM   213   N NH1   . ARG A 1 43   ? -50.674 51.702  101.853 1.00 20.74 ?  41   ARG A NH1   1 
ATOM   214   N NH2   . ARG A 1 43   ? -50.870 53.501  103.256 1.00 19.37 ?  41   ARG A NH2   1 
ATOM   215   N N     . PRO A 1 44   ? -43.585 51.416  104.470 1.00 19.59 ?  42   PRO A N     1 
ATOM   216   C CA    . PRO A 1 44   ? -42.578 50.355  104.572 1.00 19.79 ?  42   PRO A CA    1 
ATOM   217   C C     . PRO A 1 44   ? -42.871 49.209  103.616 1.00 19.01 ?  42   PRO A C     1 
ATOM   218   O O     . PRO A 1 44   ? -44.020 48.835  103.389 1.00 20.24 ?  42   PRO A O     1 
ATOM   219   C CB    . PRO A 1 44   ? -42.682 49.913  106.035 1.00 22.12 ?  42   PRO A CB    1 
ATOM   220   C CG    . PRO A 1 44   ? -43.127 51.135  106.740 1.00 21.96 ?  42   PRO A CG    1 
ATOM   221   C CD    . PRO A 1 44   ? -44.080 51.827  105.795 1.00 21.75 ?  42   PRO A CD    1 
ATOM   222   N N     . GLU A 1 45   ? -41.798 48.672  103.027 1.00 21.65 ?  43   GLU A N     1 
ATOM   223   C CA    . GLU A 1 45   ? -41.937 47.598  102.052 1.00 21.37 ?  43   GLU A CA    1 
ATOM   224   C C     . GLU A 1 45   ? -42.641 46.369  102.635 1.00 22.04 ?  43   GLU A C     1 
ATOM   225   O O     . GLU A 1 45   ? -43.414 45.703  101.934 1.00 22.01 ?  43   GLU A O     1 
ATOM   226   C CB    . GLU A 1 45   ? -40.548 47.250  101.503 1.00 23.19 ?  43   GLU A CB    1 
ATOM   227   C CG    . GLU A 1 45   ? -40.561 46.824  100.057 1.00 22.00 ?  43   GLU A CG    1 
ATOM   228   C CD    . GLU A 1 45   ? -39.222 47.010  99.334  1.00 18.34 ?  43   GLU A CD    1 
ATOM   229   O OE1   . GLU A 1 45   ? -38.298 47.701  99.839  1.00 19.31 ?  43   GLU A OE1   1 
ATOM   230   O OE2   . GLU A 1 45   ? -39.108 46.429  98.249  1.00 18.32 ?  43   GLU A OE2   1 
ATOM   231   N N     . THR A 1 46   ? -42.405 46.048  103.915 1.00 23.57 ?  44   THR A N     1 
ATOM   232   C CA    . THR A 1 46   ? -43.081 44.896  104.516 1.00 25.41 ?  44   THR A CA    1 
ATOM   233   C C     . THR A 1 46   ? -44.586 45.101  104.657 1.00 26.55 ?  44   THR A C     1 
ATOM   234   O O     . THR A 1 46   ? -45.322 44.115  104.773 1.00 29.10 ?  44   THR A O     1 
ATOM   235   C CB    . THR A 1 46   ? -42.495 44.578  105.890 1.00 24.57 ?  44   THR A CB    1 
ATOM   236   O OG1   . THR A 1 46   ? -42.499 45.765  106.692 1.00 25.01 ?  44   THR A OG1   1 
ATOM   237   C CG2   . THR A 1 46   ? -41.069 44.046  105.762 1.00 23.08 ?  44   THR A CG2   1 
ATOM   238   N N     . GLU A 1 47   ? -45.055 46.350  104.667 1.00 23.14 ?  45   GLU A N     1 
ATOM   239   C CA    . GLU A 1 47   ? -46.487 46.620  104.709 1.00 21.92 ?  45   GLU A CA    1 
ATOM   240   C C     . GLU A 1 47   ? -47.116 46.610  103.320 1.00 24.54 ?  45   GLU A C     1 
ATOM   241   O O     . GLU A 1 47   ? -48.304 46.295  103.180 1.00 24.25 ?  45   GLU A O     1 
ATOM   242   C CB    . GLU A 1 47   ? -46.743 47.967  105.386 1.00 24.48 ?  45   GLU A CB    1 
ATOM   243   C CG    . GLU A 1 47   ? -46.210 48.085  106.808 1.00 32.93 ?  45   GLU A CG    1 
ATOM   244   C CD    . GLU A 1 47   ? -46.508 49.448  107.410 1.00 32.72 ?  45   GLU A CD    1 
ATOM   245   O OE1   . GLU A 1 47   ? -47.398 50.144  106.877 1.00 34.88 ?  45   GLU A OE1   1 
ATOM   246   O OE2   . GLU A 1 47   ? -45.852 49.824  108.409 1.00 45.68 ?  45   GLU A OE2   1 
ATOM   247   N N     . CYS A 1 48   ? -46.338 46.943  102.285 1.00 20.89 ?  46   CYS A N     1 
ATOM   248   C CA    . CYS A 1 48   ? -46.899 47.032  100.939 1.00 20.53 ?  46   CYS A CA    1 
ATOM   249   C C     . CYS A 1 48   ? -47.167 45.657  100.346 1.00 16.78 ?  46   CYS A C     1 
ATOM   250   O O     . CYS A 1 48   ? -48.146 45.472  99.618  1.00 19.27 ?  46   CYS A O     1 
ATOM   251   C CB    . CYS A 1 48   ? -45.948 47.797  100.011 1.00 20.22 ?  46   CYS A CB    1 
ATOM   252   S SG    . CYS A 1 48   ? -45.671 49.535  100.399 1.00 21.61 ?  46   CYS A SG    1 
ATOM   253   N N     . LEU A 1 49   ? -46.282 44.690  100.601 1.00 21.63 ?  47   LEU A N     1 
ATOM   254   C CA    . LEU A 1 49   ? -46.325 43.452  99.829  1.00 22.41 ?  47   LEU A CA    1 
ATOM   255   C C     . LEU A 1 49   ? -47.500 42.518  100.139 1.00 21.69 ?  47   LEU A C     1 
ATOM   256   O O     . LEU A 1 49   ? -48.069 41.958  99.194  1.00 24.45 ?  47   LEU A O     1 
ATOM   257   C CB    . LEU A 1 49   ? -44.999 42.695  99.988  1.00 22.70 ?  47   LEU A CB    1 
ATOM   258   C CG    . LEU A 1 49   ? -43.978 42.929  98.862  1.00 23.08 ?  47   LEU A CG    1 
ATOM   259   C CD1   . LEU A 1 49   ? -44.522 42.437  97.533  1.00 23.84 ?  47   LEU A CD1   1 
ATOM   260   C CD2   . LEU A 1 49   ? -43.575 44.396  98.770  1.00 23.10 ?  47   LEU A CD2   1 
ATOM   261   N N     . PRO A 1 50   ? -47.900 42.301  101.397 1.00 24.10 ?  48   PRO A N     1 
ATOM   262   C CA    . PRO A 1 50   ? -48.958 41.302  101.671 1.00 27.28 ?  48   PRO A CA    1 
ATOM   263   C C     . PRO A 1 50   ? -50.228 41.541  100.864 1.00 24.72 ?  48   PRO A C     1 
ATOM   264   O O     . PRO A 1 50   ? -50.745 40.588  100.258 1.00 24.30 ?  48   PRO A O     1 
ATOM   265   C CB    . PRO A 1 50   ? -49.197 41.443  103.184 1.00 24.96 ?  48   PRO A CB    1 
ATOM   266   C CG    . PRO A 1 50   ? -47.853 41.803  103.708 1.00 25.24 ?  48   PRO A CG    1 
ATOM   267   C CD    . PRO A 1 50   ? -47.259 42.748  102.650 1.00 22.83 ?  48   PRO A CD    1 
ATOM   268   N N     . PRO A 1 51   ? -50.769 42.772  100.800 1.00 22.83 ?  49   PRO A N     1 
ATOM   269   C CA    . PRO A 1 51   ? -51.981 42.952  99.979  1.00 25.56 ?  49   PRO A CA    1 
ATOM   270   C C     . PRO A 1 51   ? -51.730 42.750  98.492  1.00 22.85 ?  49   PRO A C     1 
ATOM   271   O O     . PRO A 1 51   ? -52.649 42.353  97.767  1.00 27.08 ?  49   PRO A O     1 
ATOM   272   C CB    . PRO A 1 51   ? -52.427 44.391  100.294 1.00 24.61 ?  49   PRO A CB    1 
ATOM   273   C CG    . PRO A 1 51   ? -51.211 45.066  100.783 1.00 27.81 ?  49   PRO A CG    1 
ATOM   274   C CD    . PRO A 1 51   ? -50.424 44.017  101.515 1.00 23.32 ?  49   PRO A CD    1 
ATOM   275   N N     . LEU A 1 52   ? -50.511 43.012  98.012  1.00 23.70 ?  50   LEU A N     1 
ATOM   276   C CA    . LEU A 1 52   ? -50.201 42.736  96.613  1.00 23.12 ?  50   LEU A CA    1 
ATOM   277   C C     . LEU A 1 52   ? -50.141 41.234  96.348  1.00 22.45 ?  50   LEU A C     1 
ATOM   278   O O     . LEU A 1 52   ? -50.669 40.756  95.338  1.00 22.89 ?  50   LEU A O     1 
ATOM   279   C CB    . LEU A 1 52   ? -48.884 43.410  96.224  1.00 20.71 ?  50   LEU A CB    1 
ATOM   280   C CG    . LEU A 1 52   ? -48.839 44.943  96.330  1.00 20.61 ?  50   LEU A CG    1 
ATOM   281   C CD1   . LEU A 1 52   ? -47.428 45.470  96.070  1.00 20.55 ?  50   LEU A CD1   1 
ATOM   282   C CD2   . LEU A 1 52   ? -49.824 45.577  95.358  1.00 20.53 ?  50   LEU A CD2   1 
ATOM   283   N N     . VAL A 1 53   ? -49.513 40.474  97.253  1.00 24.77 ?  51   VAL A N     1 
ATOM   284   C CA    . VAL A 1 53   ? -49.482 39.020  97.106  1.00 28.05 ?  51   VAL A CA    1 
ATOM   285   C C     . VAL A 1 53   ? -50.899 38.459  97.059  1.00 22.64 ?  51   VAL A C     1 
ATOM   286   O O     . VAL A 1 53   ? -51.221 37.611  96.215  1.00 26.64 ?  51   VAL A O     1 
ATOM   287   C CB    . VAL A 1 53   ? -48.662 38.378  98.240  1.00 25.94 ?  51   VAL A CB    1 
ATOM   288   C CG1   . VAL A 1 53   ? -48.794 36.852  98.194  1.00 29.63 ?  51   VAL A CG1   1 
ATOM   289   C CG2   . VAL A 1 53   ? -47.201 38.785  98.135  1.00 25.61 ?  51   VAL A CG2   1 
ATOM   290   N N     . GLU A 1 54   ? -51.770 38.928  97.957  1.00 25.20 ?  52   GLU A N     1 
ATOM   291   C CA    . GLU A 1 54   ? -53.150 38.449  97.947  1.00 27.97 ?  52   GLU A CA    1 
ATOM   292   C C     . GLU A 1 54   ? -53.831 38.780  96.625  1.00 29.47 ?  52   GLU A C     1 
ATOM   293   O O     . GLU A 1 54   ? -54.450 37.915  95.998  1.00 28.27 ?  52   GLU A O     1 
ATOM   294   C CB    . GLU A 1 54   ? -53.925 39.036  99.128  1.00 30.38 ?  52   GLU A CB    1 
ATOM   295   N N     . ALA A 1 55   ? -53.678 40.025  96.153  1.00 25.54 ?  53   ALA A N     1 
ATOM   296   C CA    . ALA A 1 55   ? -54.338 40.434  94.919  1.00 26.38 ?  53   ALA A CA    1 
ATOM   297   C C     . ALA A 1 55   ? -53.788 39.703  93.697  1.00 24.67 ?  53   ALA A C     1 
ATOM   298   O O     . ALA A 1 55   ? -54.523 39.493  92.728  1.00 27.88 ?  53   ALA A O     1 
ATOM   299   C CB    . ALA A 1 55   ? -54.208 41.947  94.742  1.00 24.44 ?  53   ALA A CB    1 
ATOM   300   N N     . ALA A 1 56   ? -52.516 39.300  93.727  1.00 26.46 ?  54   ALA A N     1 
ATOM   301   C CA    . ALA A 1 56   ? -51.870 38.652  92.591  1.00 27.91 ?  54   ALA A CA    1 
ATOM   302   C C     . ALA A 1 56   ? -52.027 37.136  92.581  1.00 30.91 ?  54   ALA A C     1 
ATOM   303   O O     . ALA A 1 56   ? -51.558 36.488  91.639  1.00 28.91 ?  54   ALA A O     1 
ATOM   304   C CB    . ALA A 1 56   ? -50.375 38.998  92.561  1.00 24.18 ?  54   ALA A CB    1 
ATOM   305   N N     . THR A 1 57   ? -52.669 36.555  93.589  1.00 30.68 ?  55   THR A N     1 
ATOM   306   C CA    . THR A 1 57   ? -52.769 35.105  93.667  1.00 32.70 ?  55   THR A CA    1 
ATOM   307   C C     . THR A 1 57   ? -53.689 34.569  92.574  1.00 30.10 ?  55   THR A C     1 
ATOM   308   O O     . THR A 1 57   ? -54.735 35.153  92.278  1.00 32.94 ?  55   THR A O     1 
ATOM   309   C CB    . THR A 1 57   ? -53.268 34.699  95.054  1.00 33.50 ?  55   THR A CB    1 
ATOM   310   O OG1   . THR A 1 57   ? -52.281 35.068  96.029  1.00 31.60 ?  55   THR A OG1   1 
ATOM   311   C CG2   . THR A 1 57   ? -53.523 33.192  95.137  1.00 34.07 ?  55   THR A CG2   1 
ATOM   312   N N     . GLN A 1 58   ? -53.275 33.463  91.949  1.00 33.02 ?  56   GLN A N     1 
ATOM   313   C CA    . GLN A 1 58   ? -54.098 32.746  90.985  1.00 29.22 ?  56   GLN A CA    1 
ATOM   314   C C     . GLN A 1 58   ? -54.133 31.268  91.363  1.00 34.69 ?  56   GLN A C     1 
ATOM   315   O O     . GLN A 1 58   ? -53.311 30.791  92.149  1.00 35.20 ?  56   GLN A O     1 
ATOM   316   C CB    . GLN A 1 58   ? -53.582 32.921  89.545  1.00 33.02 ?  56   GLN A CB    1 
ATOM   317   C CG    . GLN A 1 58   ? -53.413 34.381  89.124  1.00 32.90 ?  56   GLN A CG    1 
ATOM   318   C CD    . GLN A 1 58   ? -53.402 34.580  87.616  1.00 27.57 ?  56   GLN A CD    1 
ATOM   319   O OE1   . GLN A 1 58   ? -54.431 34.444  86.950  1.00 30.65 ?  56   GLN A OE1   1 
ATOM   320   N NE2   . GLN A 1 58   ? -52.235 34.917  87.070  1.00 31.19 ?  56   GLN A NE2   1 
ATOM   321   N N     . SER A 1 59   ? -55.099 30.550  90.792  1.00 32.48 ?  57   SER A N     1 
ATOM   322   C CA    . SER A 1 59   ? -55.274 29.139  91.115  1.00 34.12 ?  57   SER A CA    1 
ATOM   323   C C     . SER A 1 59   ? -54.059 28.329  90.671  1.00 38.78 ?  57   SER A C     1 
ATOM   324   O O     . SER A 1 59   ? -53.260 28.761  89.834  1.00 34.94 ?  57   SER A O     1 
ATOM   325   C CB    . SER A 1 59   ? -56.537 28.588  90.456  1.00 34.50 ?  57   SER A CB    1 
ATOM   326   O OG    . SER A 1 59   ? -56.455 28.647  89.041  1.00 38.86 ?  57   SER A OG    1 
ATOM   327   N N     . LYS A 1 60   ? -53.921 27.133  91.253  1.00 34.75 ?  58   LYS A N     1 
ATOM   328   C CA    . LYS A 1 60   ? -52.830 26.251  90.853  1.00 34.87 ?  58   LYS A CA    1 
ATOM   329   C C     . LYS A 1 60   ? -52.928 25.897  89.377  1.00 35.55 ?  58   LYS A C     1 
ATOM   330   O O     . LYS A 1 60   ? -51.910 25.828  88.679  1.00 34.56 ?  58   LYS A O     1 
ATOM   331   C CB    . LYS A 1 60   ? -52.831 24.982  91.708  1.00 39.11 ?  58   LYS A CB    1 
ATOM   332   C CG    . LYS A 1 60   ? -51.702 24.008  91.373  1.00 40.76 ?  58   LYS A CG    1 
ATOM   333   C CD    . LYS A 1 60   ? -50.346 24.705  91.399  1.00 43.46 ?  58   LYS A CD    1 
ATOM   334   C CE    . LYS A 1 60   ? -49.199 23.718  91.580  1.00 43.06 ?  58   LYS A CE    1 
ATOM   335   N NZ    . LYS A 1 60   ? -49.018 22.823  90.402  1.00 44.76 ?  58   LYS A NZ    1 
ATOM   336   N N     . GLU A 1 61   ? -54.149 25.678  88.883  1.00 33.53 ?  59   GLU A N     1 
ATOM   337   C CA    . GLU A 1 61   ? -54.330 25.343  87.474  1.00 34.06 ?  59   GLU A CA    1 
ATOM   338   C C     . GLU A 1 61   ? -53.861 26.475  86.567  1.00 37.46 ?  59   GLU A C     1 
ATOM   339   O O     . GLU A 1 61   ? -53.201 26.229  85.550  1.00 33.93 ?  59   GLU A O     1 
ATOM   340   C CB    . GLU A 1 61   ? -55.795 25.005  87.200  1.00 38.18 ?  59   GLU A CB    1 
ATOM   341   N N     . ILE A 1 62   ? -54.194 27.723  86.910  1.00 32.78 ?  60   ILE A N     1 
ATOM   342   C CA    . ILE A 1 62   ? -53.777 28.847  86.073  1.00 32.54 ?  60   ILE A CA    1 
ATOM   343   C C     . ILE A 1 62   ? -52.263 29.024  86.120  1.00 32.63 ?  60   ILE A C     1 
ATOM   344   O O     . ILE A 1 62   ? -51.624 29.287  85.093  1.00 31.15 ?  60   ILE A O     1 
ATOM   345   C CB    . ILE A 1 62   ? -54.515 30.132  86.485  1.00 31.19 ?  60   ILE A CB    1 
ATOM   346   C CG1   . ILE A 1 62   ? -55.944 30.102  85.946  1.00 35.16 ?  60   ILE A CG1   1 
ATOM   347   C CG2   . ILE A 1 62   ? -53.785 31.371  85.966  1.00 31.64 ?  60   ILE A CG2   1 
ATOM   348   C CD1   . ILE A 1 62   ? -56.689 31.384  86.138  1.00 34.00 ?  60   ILE A CD1   1 
ATOM   349   N N     . ARG A 1 63   ? -51.664 28.877  87.303  1.00 30.70 ?  61   ARG A N     1 
ATOM   350   C CA    . ARG A 1 63   ? -50.218 29.024  87.423  1.00 30.90 ?  61   ARG A CA    1 
ATOM   351   C C     . ARG A 1 63   ? -49.483 27.992  86.577  1.00 33.72 ?  61   ARG A C     1 
ATOM   352   O O     . ARG A 1 63   ? -48.495 28.318  85.906  1.00 30.34 ?  61   ARG A O     1 
ATOM   353   C CB    . ARG A 1 63   ? -49.806 28.928  88.890  1.00 31.56 ?  61   ARG A CB    1 
ATOM   354   C CG    . ARG A 1 63   ? -50.309 30.111  89.702  1.00 37.84 ?  61   ARG A CG    1 
ATOM   355   C CD    . ARG A 1 63   ? -49.752 30.146  91.111  1.00 40.19 ?  61   ARG A CD    1 
ATOM   356   N NE    . ARG A 1 63   ? -50.458 29.237  92.004  1.00 39.95 ?  61   ARG A NE    1 
ATOM   357   C CZ    . ARG A 1 63   ? -49.938 28.122  92.497  1.00 46.37 ?  61   ARG A CZ    1 
ATOM   358   N NH1   . ARG A 1 63   ? -48.700 27.754  92.211  1.00 46.70 ?  61   ARG A NH1   1 
ATOM   359   N NH2   . ARG A 1 63   ? -50.675 27.364  93.304  1.00 44.64 ?  61   ARG A NH2   1 
ATOM   360   N N     . ASP A 1 64   ? -49.952 26.742  86.585  1.00 32.46 ?  62   ASP A N     1 
ATOM   361   C CA    . ASP A 1 64   ? -49.351 25.737  85.714  1.00 31.81 ?  62   ASP A CA    1 
ATOM   362   C C     . ASP A 1 64   ? -49.534 26.105  84.246  1.00 31.10 ?  62   ASP A C     1 
ATOM   363   O O     . ASP A 1 64   ? -48.597 25.985  83.447  1.00 31.27 ?  62   ASP A O     1 
ATOM   364   C CB    . ASP A 1 64   ? -49.951 24.360  86.013  1.00 32.29 ?  62   ASP A CB    1 
ATOM   365   C CG    . ASP A 1 64   ? -49.567 23.841  87.385  1.00 35.31 ?  62   ASP A CG    1 
ATOM   366   O OD1   . ASP A 1 64   ? -48.680 24.438  88.028  1.00 38.34 ?  62   ASP A OD1   1 
ATOM   367   O OD2   . ASP A 1 64   ? -50.152 22.824  87.824  1.00 42.77 ?  62   ASP A OD2   1 
ATOM   368   N N     . ALA A 1 65   ? -50.731 26.568  83.873  1.00 30.09 ?  63   ALA A N     1 
ATOM   369   C CA    . ALA A 1 65   ? -50.958 26.990  82.495  1.00 30.48 ?  63   ALA A CA    1 
ATOM   370   C C     . ALA A 1 65   ? -50.088 28.185  82.139  1.00 30.45 ?  63   ALA A C     1 
ATOM   371   O O     . ALA A 1 65   ? -49.581 28.279  81.017  1.00 31.15 ?  63   ALA A O     1 
ATOM   372   C CB    . ALA A 1 65   ? -52.435 27.326  82.277  1.00 29.51 ?  63   ALA A CB    1 
ATOM   373   N N     . ALA A 1 66   ? -49.904 29.107  83.086  1.00 26.53 ?  64   ALA A N     1 
ATOM   374   C CA    . ALA A 1 66   ? -49.095 30.289  82.811  1.00 30.56 ?  64   ALA A CA    1 
ATOM   375   C C     . ALA A 1 66   ? -47.626 29.922  82.661  1.00 33.05 ?  64   ALA A C     1 
ATOM   376   O O     . ALA A 1 66   ? -46.948 30.419  81.753  1.00 29.26 ?  64   ALA A O     1 
ATOM   377   C CB    . ALA A 1 66   ? -49.280 31.328  83.915  1.00 29.52 ?  64   ALA A CB    1 
ATOM   378   N N     . ALA A 1 67   ? -47.121 29.050  83.537  1.00 29.68 ?  65   ALA A N     1 
ATOM   379   C CA    . ALA A 1 67   ? -45.740 28.606  83.407  1.00 28.17 ?  65   ALA A CA    1 
ATOM   380   C C     . ALA A 1 67   ? -45.528 27.888  82.080  1.00 29.50 ?  65   ALA A C     1 
ATOM   381   O O     . ALA A 1 67   ? -44.491 28.059  81.429  1.00 28.20 ?  65   ALA A O     1 
ATOM   382   C CB    . ALA A 1 67   ? -45.362 27.704  84.582  1.00 31.44 ?  65   ALA A CB    1 
ATOM   383   N N     . SER A 1 68   ? -46.510 27.091  81.653  1.00 30.41 ?  66   SER A N     1 
ATOM   384   C CA    . SER A 1 68   ? -46.400 26.409  80.369  1.00 31.70 ?  66   SER A CA    1 
ATOM   385   C C     . SER A 1 68   ? -46.331 27.406  79.217  1.00 30.69 ?  66   SER A C     1 
ATOM   386   O O     . SER A 1 68   ? -45.504 27.261  78.308  1.00 31.52 ?  66   SER A O     1 
ATOM   387   C CB    . SER A 1 68   ? -47.578 25.451  80.185  1.00 33.84 ?  66   SER A CB    1 
ATOM   388   O OG    . SER A 1 68   ? -47.509 24.804  78.926  1.00 40.74 ?  66   SER A OG    1 
ATOM   389   N N     . THR A 1 69   ? -47.198 28.424  79.235  1.00 30.57 ?  67   THR A N     1 
ATOM   390   C CA    . THR A 1 69   ? -47.164 29.440  78.187  1.00 29.13 ?  67   THR A CA    1 
ATOM   391   C C     . THR A 1 69   ? -45.856 30.222  78.214  1.00 28.14 ?  67   THR A C     1 
ATOM   392   O O     . THR A 1 69   ? -45.281 30.513  77.159  1.00 28.42 ?  67   THR A O     1 
ATOM   393   C CB    . THR A 1 69   ? -48.353 30.386  78.338  1.00 26.91 ?  67   THR A CB    1 
ATOM   394   O OG1   . THR A 1 69   ? -49.563 29.658  78.105  1.00 27.44 ?  67   THR A OG1   1 
ATOM   395   C CG2   . THR A 1 69   ? -48.256 31.563  77.355  1.00 26.44 ?  67   THR A CG2   1 
ATOM   396   N N     . ALA A 1 70   ? -45.373 30.569  79.411  1.00 25.14 ?  68   ALA A N     1 
ATOM   397   C CA    . ALA A 1 70   ? -44.108 31.291  79.517  1.00 26.08 ?  68   ALA A CA    1 
ATOM   398   C C     . ALA A 1 70   ? -42.955 30.453  78.987  1.00 27.86 ?  68   ALA A C     1 
ATOM   399   O O     . ALA A 1 70   ? -42.081 30.964  78.280  1.00 27.03 ?  68   ALA A O     1 
ATOM   400   C CB    . ALA A 1 70   ? -43.847 31.701  80.966  1.00 25.87 ?  68   ALA A CB    1 
ATOM   401   N N     . ARG A 1 71   ? -42.937 29.158  79.315  1.00 28.21 ?  69   ARG A N     1 
ATOM   402   C CA    . ARG A 1 71   ? -41.890 28.288  78.789  1.00 29.90 ?  69   ARG A CA    1 
ATOM   403   C C     . ARG A 1 71   ? -41.915 28.270  77.264  1.00 28.17 ?  69   ARG A C     1 
ATOM   404   O O     . ARG A 1 71   ? -40.869 28.399  76.614  1.00 30.57 ?  69   ARG A O     1 
ATOM   405   C CB    . ARG A 1 71   ? -42.045 26.876  79.356  1.00 29.54 ?  69   ARG A CB    1 
ATOM   406   C CG    . ARG A 1 71   ? -41.148 25.863  78.698  1.00 33.19 ?  69   ARG A CG    1 
ATOM   407   C CD    . ARG A 1 71   ? -41.208 24.520  79.413  1.00 30.78 ?  69   ARG A CD    1 
ATOM   408   N NE    . ARG A 1 71   ? -40.408 24.519  80.631  1.00 36.19 ?  69   ARG A NE    1 
ATOM   409   C CZ    . ARG A 1 71   ? -39.083 24.455  80.652  1.00 35.52 ?  69   ARG A CZ    1 
ATOM   410   N NH1   . ARG A 1 71   ? -38.373 24.420  79.533  1.00 37.54 ?  69   ARG A NH1   1 
ATOM   411   N NH2   . ARG A 1 71   ? -38.453 24.429  81.824  1.00 39.15 ?  69   ARG A NH2   1 
ATOM   412   N N     . LYS A 1 72   ? -43.111 28.155  76.677  1.00 26.62 ?  70   LYS A N     1 
ATOM   413   C CA    . LYS A 1 72   ? -43.225 28.123  75.222  1.00 28.32 ?  70   LYS A CA    1 
ATOM   414   C C     . LYS A 1 72   ? -42.687 29.405  74.595  1.00 31.38 ?  70   LYS A C     1 
ATOM   415   O O     . LYS A 1 72   ? -41.952 29.357  73.601  1.00 28.16 ?  70   LYS A O     1 
ATOM   416   C CB    . LYS A 1 72   ? -44.679 27.898  74.809  1.00 31.09 ?  70   LYS A CB    1 
ATOM   417   C CG    . LYS A 1 72   ? -44.904 27.939  73.298  1.00 29.59 ?  70   LYS A CG    1 
ATOM   418   C CD    . LYS A 1 72   ? -46.302 27.480  72.930  1.00 33.44 ?  70   LYS A CD    1 
ATOM   419   C CE    . LYS A 1 72   ? -46.439 27.254  71.430  1.00 35.88 ?  70   LYS A CE    1 
ATOM   420   N NZ    . LYS A 1 72   ? -47.770 26.687  71.063  1.00 52.92 ?  70   LYS A NZ    1 
ATOM   421   N N     . LEU A 1 73   ? -43.041 30.562  75.161  1.00 27.91 ?  71   LEU A N     1 
ATOM   422   C CA    . LEU A 1 73   ? -42.542 31.827  74.627  1.00 26.57 ?  71   LEU A CA    1 
ATOM   423   C C     . LEU A 1 73   ? -41.025 31.913  74.733  1.00 27.48 ?  71   LEU A C     1 
ATOM   424   O O     . LEU A 1 73   ? -40.358 32.369  73.799  1.00 26.03 ?  71   LEU A O     1 
ATOM   425   C CB    . LEU A 1 73   ? -43.192 33.002  75.360  1.00 28.34 ?  71   LEU A CB    1 
ATOM   426   C CG    . LEU A 1 73   ? -44.703 33.197  75.202  1.00 28.50 ?  71   LEU A CG    1 
ATOM   427   C CD1   . LEU A 1 73   ? -45.220 34.199  76.220  1.00 25.86 ?  71   LEU A CD1   1 
ATOM   428   C CD2   . LEU A 1 73   ? -45.050 33.654  73.800  1.00 24.99 ?  71   LEU A CD2   1 
ATOM   429   N N     . ILE A 1 74   ? -40.463 31.472  75.863  1.00 24.09 ?  72   ILE A N     1 
ATOM   430   C CA    . ILE A 1 74   ? -39.026 31.594  76.090  1.00 24.17 ?  72   ILE A CA    1 
ATOM   431   C C     . ILE A 1 74   ? -38.251 30.631  75.199  1.00 30.50 ?  72   ILE A C     1 
ATOM   432   O O     . ILE A 1 74   ? -37.181 30.969  74.680  1.00 27.88 ?  72   ILE A O     1 
ATOM   433   C CB    . ILE A 1 74   ? -38.713 31.384  77.582  1.00 30.23 ?  72   ILE A CB    1 
ATOM   434   C CG1   . ILE A 1 74   ? -39.244 32.575  78.394  1.00 29.32 ?  72   ILE A CG1   1 
ATOM   435   C CG2   . ILE A 1 74   ? -37.219 31.192  77.800  1.00 29.26 ?  72   ILE A CG2   1 
ATOM   436   C CD1   . ILE A 1 74   ? -39.396 32.301  79.870  1.00 28.77 ?  72   ILE A CD1   1 
ATOM   437   N N     . GLU A 1 75   ? -38.771 29.416  75.007  1.00 30.80 ?  73   GLU A N     1 
ATOM   438   C CA    . GLU A 1 75   ? -38.133 28.490  74.077  1.00 32.41 ?  73   GLU A CA    1 
ATOM   439   C C     . GLU A 1 75   ? -38.111 29.061  72.662  1.00 30.00 ?  73   GLU A C     1 
ATOM   440   O O     . GLU A 1 75   ? -37.127 28.892  71.933  1.00 32.11 ?  73   GLU A O     1 
ATOM   441   C CB    . GLU A 1 75   ? -38.843 27.134  74.118  1.00 30.69 ?  73   GLU A CB    1 
ATOM   442   C CG    . GLU A 1 75   ? -38.555 26.349  75.390  1.00 34.13 ?  73   GLU A CG    1 
ATOM   443   C CD    . GLU A 1 75   ? -39.401 25.095  75.542  1.00 39.51 ?  73   GLU A CD    1 
ATOM   444   O OE1   . GLU A 1 75   ? -40.442 24.978  74.856  1.00 37.65 ?  73   GLU A OE1   1 
ATOM   445   O OE2   . GLU A 1 75   ? -39.023 24.227  76.359  1.00 41.29 ?  73   GLU A OE2   1 
ATOM   446   N N     . ALA A 1 76   ? -39.173 29.767  72.268  1.00 31.89 ?  74   ALA A N     1 
ATOM   447   C CA    . ALA A 1 76   ? -39.182 30.412  70.957  1.00 31.00 ?  74   ALA A CA    1 
ATOM   448   C C     . ALA A 1 76   ? -38.164 31.546  70.888  1.00 28.99 ?  74   ALA A C     1 
ATOM   449   O O     . ALA A 1 76   ? -37.471 31.701  69.875  1.00 32.23 ?  74   ALA A O     1 
ATOM   450   C CB    . ALA A 1 76   ? -40.583 30.929  70.633  1.00 32.43 ?  74   ALA A CB    1 
ATOM   451   N N     . LEU A 1 77   ? -38.064 32.352  71.949  1.00 28.89 ?  75   LEU A N     1 
ATOM   452   C CA    . LEU A 1 77   ? -37.109 33.457  71.958  1.00 29.01 ?  75   LEU A CA    1 
ATOM   453   C C     . LEU A 1 77   ? -35.676 32.957  71.844  1.00 35.26 ?  75   LEU A C     1 
ATOM   454   O O     . LEU A 1 77   ? -34.878 33.502  71.074  1.00 35.90 ?  75   LEU A O     1 
ATOM   455   C CB    . LEU A 1 77   ? -37.271 34.285  73.230  1.00 29.88 ?  75   LEU A CB    1 
ATOM   456   C CG    . LEU A 1 77   ? -38.478 35.215  73.234  1.00 32.34 ?  75   LEU A CG    1 
ATOM   457   C CD1   . LEU A 1 77   ? -38.661 35.832  74.600  1.00 29.05 ?  75   LEU A CD1   1 
ATOM   458   C CD2   . LEU A 1 77   ? -38.272 36.288  72.187  1.00 29.35 ?  75   LEU A CD2   1 
ATOM   459   N N     . ARG A 1 78   ? -35.328 31.926  72.612  1.00 32.95 ?  76   ARG A N     1 
ATOM   460   C CA    . ARG A 1 78   ? -33.966 31.414  72.580  1.00 31.58 ?  76   ARG A CA    1 
ATOM   461   C C     . ARG A 1 78   ? -33.675 30.620  71.318  1.00 34.37 ?  76   ARG A C     1 
ATOM   462   O O     . ARG A 1 78   ? -32.506 30.500  70.938  1.00 36.12 ?  76   ARG A O     1 
ATOM   463   C CB    . ARG A 1 78   ? -33.701 30.565  73.822  1.00 29.58 ?  76   ARG A CB    1 
ATOM   464   C CG    . ARG A 1 78   ? -33.521 31.408  75.068  1.00 34.85 ?  76   ARG A CG    1 
ATOM   465   C CD    . ARG A 1 78   ? -33.194 30.577  76.282  1.00 28.59 ?  76   ARG A CD    1 
ATOM   466   N NE    . ARG A 1 78   ? -32.626 31.399  77.340  1.00 30.92 ?  76   ARG A NE    1 
ATOM   467   C CZ    . ARG A 1 78   ? -32.250 30.941  78.525  1.00 27.97 ?  76   ARG A CZ    1 
ATOM   468   N NH1   . ARG A 1 78   ? -32.406 29.669  78.855  1.00 31.45 ?  76   ARG A NH1   1 
ATOM   469   N NH2   . ARG A 1 78   ? -31.694 31.778  79.397  1.00 29.16 ?  76   ARG A NH2   1 
ATOM   470   N N     . GLY A 1 79   ? -34.707 30.102  70.649  1.00 33.07 ?  77   GLY A N     1 
ATOM   471   C CA    . GLY A 1 79   ? -34.492 29.312  69.453  1.00 39.18 ?  77   GLY A CA    1 
ATOM   472   C C     . GLY A 1 79   ? -34.255 30.117  68.195  1.00 38.39 ?  77   GLY A C     1 
ATOM   473   O O     . GLY A 1 79   ? -33.634 29.607  67.258  1.00 43.64 ?  77   GLY A O     1 
ATOM   474   N N     . LYS A 1 80   ? -34.745 31.354  68.141  1.00 40.59 ?  78   LYS A N     1 
ATOM   475   C CA    . LYS A 1 80   ? -34.545 32.204  66.976  1.00 43.80 ?  78   LYS A CA    1 
ATOM   476   C C     . LYS A 1 80   ? -33.538 33.315  67.224  1.00 43.54 ?  78   LYS A C     1 
ATOM   477   O O     . LYS A 1 80   ? -33.281 34.115  66.317  1.00 49.54 ?  78   LYS A O     1 
ATOM   478   C CB    . LYS A 1 80   ? -35.881 32.802  66.512  1.00 38.30 ?  78   LYS A CB    1 
ATOM   479   C CG    . LYS A 1 80   ? -36.524 33.771  67.488  1.00 37.96 ?  78   LYS A CG    1 
ATOM   480   C CD    . LYS A 1 80   ? -37.932 34.127  67.033  1.00 37.87 ?  78   LYS A CD    1 
ATOM   481   C CE    . LYS A 1 80   ? -38.640 34.991  68.058  1.00 34.75 ?  78   LYS A CE    1 
ATOM   482   N NZ    . LYS A 1 80   ? -40.026 35.340  67.623  1.00 27.14 ?  78   LYS A NZ    1 
ATOM   483   N N     . HIS A 1 81   ? -32.954 33.381  68.417  1.00 42.02 ?  79   HIS A N     1 
ATOM   484   C CA    . HIS A 1 81   ? -32.006 34.442  68.724  1.00 50.47 ?  79   HIS A CA    1 
ATOM   485   C C     . HIS A 1 81   ? -30.692 34.212  67.987  1.00 53.76 ?  79   HIS A C     1 
ATOM   486   O O     . HIS A 1 81   ? -30.108 33.125  68.059  1.00 54.10 ?  79   HIS A O     1 
ATOM   487   C CB    . HIS A 1 81   ? -31.759 34.519  70.229  1.00 50.68 ?  79   HIS A CB    1 
ATOM   488   C CG    . HIS A 1 81   ? -30.850 35.641  70.631  1.00 57.81 ?  79   HIS A CG    1 
ATOM   489   N ND1   . HIS A 1 81   ? -29.822 35.481  71.537  1.00 59.62 ?  79   HIS A ND1   1 
ATOM   490   C CD2   . HIS A 1 81   ? -30.814 36.939  70.247  1.00 58.43 ?  79   HIS A CD2   1 
ATOM   491   C CE1   . HIS A 1 81   ? -29.191 36.631  71.692  1.00 57.25 ?  79   HIS A CE1   1 
ATOM   492   N NE2   . HIS A 1 81   ? -29.773 37.533  70.922  1.00 61.75 ?  79   HIS A NE2   1 
ATOM   493   N N     . SER A 1 82   ? -30.233 35.237  67.278  1.00 54.95 ?  80   SER A N     1 
ATOM   494   C CA    . SER A 1 82   ? -28.942 35.234  66.606  1.00 53.35 ?  80   SER A CA    1 
ATOM   495   C C     . SER A 1 82   ? -28.029 36.275  67.243  1.00 56.11 ?  80   SER A C     1 
ATOM   496   O O     . SER A 1 82   ? -28.445 37.073  68.088  1.00 55.87 ?  80   SER A O     1 
ATOM   497   C CB    . SER A 1 82   ? -29.105 35.510  65.105  1.00 50.81 ?  80   SER A CB    1 
ATOM   498   N N     . GLY A 1 83   ? -26.765 36.255  66.833  1.00 52.40 ?  81   GLY A N     1 
ATOM   499   C CA    . GLY A 1 83   ? -25.831 37.259  67.309  1.00 52.19 ?  81   GLY A CA    1 
ATOM   500   C C     . GLY A 1 83   ? -26.153 38.626  66.728  1.00 47.93 ?  81   GLY A C     1 
ATOM   501   O O     . GLY A 1 83   ? -26.571 38.755  65.575  1.00 47.24 ?  81   GLY A O     1 
ATOM   502   N N     . SER A 1 84   ? -25.958 39.660  67.544  1.00 45.18 ?  82   SER A N     1 
ATOM   503   C CA    . SER A 1 84   ? -26.263 41.013  67.110  1.00 42.35 ?  82   SER A CA    1 
ATOM   504   C C     . SER A 1 84   ? -25.293 41.457  66.015  1.00 37.89 ?  82   SER A C     1 
ATOM   505   O O     . SER A 1 84   ? -24.292 40.796  65.716  1.00 34.01 ?  82   SER A O     1 
ATOM   506   C CB    . SER A 1 84   ? -26.205 41.986  68.288  1.00 38.91 ?  82   SER A CB    1 
ATOM   507   O OG    . SER A 1 84   ? -24.865 42.211  68.691  1.00 38.68 ?  82   SER A OG    1 
ATOM   508   N N     . GLY A 1 85   ? -25.611 42.601  65.407  1.00 34.26 ?  83   GLY A N     1 
ATOM   509   C CA    . GLY A 1 85   ? -24.728 43.160  64.402  1.00 31.15 ?  83   GLY A CA    1 
ATOM   510   C C     . GLY A 1 85   ? -23.392 43.583  64.981  1.00 25.49 ?  83   GLY A C     1 
ATOM   511   O O     . GLY A 1 85   ? -22.343 43.334  64.382  1.00 25.36 ?  83   GLY A O     1 
ATOM   512   N N     . VAL A 1 86   ? -23.410 44.231  66.152  1.00 29.29 ?  84   VAL A N     1 
ATOM   513   C CA    . VAL A 1 86   ? -22.167 44.700  66.760  1.00 25.03 ?  84   VAL A CA    1 
ATOM   514   C C     . VAL A 1 86   ? -21.277 43.521  67.127  1.00 27.65 ?  84   VAL A C     1 
ATOM   515   O O     . VAL A 1 86   ? -20.058 43.559  66.917  1.00 24.94 ?  84   VAL A O     1 
ATOM   516   C CB    . VAL A 1 86   ? -22.461 45.589  67.982  1.00 27.58 ?  84   VAL A CB    1 
ATOM   517   C CG1   . VAL A 1 86   ? -21.194 45.794  68.810  1.00 25.94 ?  84   VAL A CG1   1 
ATOM   518   C CG2   . VAL A 1 86   ? -22.995 46.931  67.533  1.00 29.37 ?  84   VAL A CG2   1 
ATOM   519   N N     . GLU A 1 87   ? -21.871 42.451  67.664  1.00 28.98 ?  85   GLU A N     1 
ATOM   520   C CA    . GLU A 1 87   ? -21.098 41.257  67.994  1.00 29.74 ?  85   GLU A CA    1 
ATOM   521   C C     . GLU A 1 87   ? -20.461 40.645  66.756  1.00 28.13 ?  85   GLU A C     1 
ATOM   522   O O     . GLU A 1 87   ? -19.312 40.190  66.802  1.00 27.85 ?  85   GLU A O     1 
ATOM   523   C CB    . GLU A 1 87   ? -21.987 40.227  68.694  1.00 37.05 ?  85   GLU A CB    1 
ATOM   524   C CG    . GLU A 1 87   ? -22.377 40.596  70.117  1.00 41.46 ?  85   GLU A CG    1 
ATOM   525   C CD    . GLU A 1 87   ? -23.493 39.718  70.661  1.00 49.51 ?  85   GLU A CD    1 
ATOM   526   O OE1   . GLU A 1 87   ? -23.958 38.819  69.927  1.00 49.26 ?  85   GLU A OE1   1 
ATOM   527   O OE2   . GLU A 1 87   ? -23.907 39.932  71.820  1.00 54.97 ?  85   GLU A OE2   1 
ATOM   528   N N     . GLY A 1 88   ? -21.192 40.608  65.641  1.00 27.84 ?  86   GLY A N     1 
ATOM   529   C CA    . GLY A 1 88   ? -20.618 40.067  64.424  1.00 26.47 ?  86   GLY A CA    1 
ATOM   530   C C     . GLY A 1 88   ? -19.487 40.917  63.887  1.00 26.00 ?  86   GLY A C     1 
ATOM   531   O O     . GLY A 1 88   ? -18.547 40.399  63.276  1.00 28.04 ?  86   GLY A O     1 
ATOM   532   N N     . LEU A 1 89   ? -19.567 42.230  64.102  1.00 25.35 ?  87   LEU A N     1 
ATOM   533   C CA    . LEU A 1 89   ? -18.503 43.128  63.673  1.00 25.50 ?  87   LEU A CA    1 
ATOM   534   C C     . LEU A 1 89   ? -17.261 42.932  64.531  1.00 22.23 ?  87   LEU A C     1 
ATOM   535   O O     . LEU A 1 89   ? -16.144 42.799  64.016  1.00 22.44 ?  87   LEU A O     1 
ATOM   536   C CB    . LEU A 1 89   ? -19.009 44.567  63.749  1.00 25.39 ?  87   LEU A CB    1 
ATOM   537   C CG    . LEU A 1 89   ? -18.119 45.723  63.331  1.00 30.64 ?  87   LEU A CG    1 
ATOM   538   C CD1   . LEU A 1 89   ? -17.673 45.503  61.924  1.00 32.88 ?  87   LEU A CD1   1 
ATOM   539   C CD2   . LEU A 1 89   ? -18.903 47.029  63.460  1.00 29.02 ?  87   LEU A CD2   1 
ATOM   540   N N     . VAL A 1 90   ? -17.451 42.893  65.849  1.00 23.26 ?  88   VAL A N     1 
ATOM   541   C CA    . VAL A 1 90   ? -16.359 42.593  66.765  1.00 22.06 ?  88   VAL A CA    1 
ATOM   542   C C     . VAL A 1 90   ? -15.705 41.263  66.405  1.00 25.01 ?  88   VAL A C     1 
ATOM   543   O O     . VAL A 1 90   ? -14.472 41.144  66.387  1.00 24.26 ?  88   VAL A O     1 
ATOM   544   C CB    . VAL A 1 90   ? -16.889 42.614  68.209  1.00 20.50 ?  88   VAL A CB    1 
ATOM   545   C CG1   . VAL A 1 90   ? -15.861 42.038  69.168  1.00 22.51 ?  88   VAL A CG1   1 
ATOM   546   C CG2   . VAL A 1 90   ? -17.285 44.040  68.594  1.00 21.11 ?  88   VAL A CG2   1 
ATOM   547   N N     . GLN A 1 91   ? -16.514 40.254  66.070  1.00 23.88 ?  89   GLN A N     1 
ATOM   548   C CA    . GLN A 1 91   ? -15.955 38.954  65.702  1.00 29.14 ?  89   GLN A CA    1 
ATOM   549   C C     . GLN A 1 91   ? -15.171 39.032  64.399  1.00 26.31 ?  89   GLN A C     1 
ATOM   550   O O     . GLN A 1 91   ? -14.041 38.532  64.313  1.00 28.00 ?  89   GLN A O     1 
ATOM   551   C CB    . GLN A 1 91   ? -17.068 37.909  65.592  1.00 30.97 ?  89   GLN A CB    1 
ATOM   552   N N     . GLU A 1 92   ? -15.749 39.658  63.369  1.00 26.72 ?  90   GLU A N     1 
ATOM   553   C CA    . GLU A 1 92   ? -15.117 39.637  62.053  1.00 26.97 ?  90   GLU A CA    1 
ATOM   554   C C     . GLU A 1 92   ? -13.730 40.262  62.089  1.00 27.42 ?  90   GLU A C     1 
ATOM   555   O O     . GLU A 1 92   ? -12.787 39.732  61.491  1.00 25.18 ?  90   GLU A O     1 
ATOM   556   C CB    . GLU A 1 92   ? -16.001 40.348  61.024  1.00 27.44 ?  90   GLU A CB    1 
ATOM   557   C CG    . GLU A 1 92   ? -15.434 40.333  59.607  1.00 30.22 ?  90   GLU A CG    1 
ATOM   558   C CD    . GLU A 1 92   ? -16.349 41.004  58.588  1.00 34.63 ?  90   GLU A CD    1 
ATOM   559   O OE1   . GLU A 1 92   ? -17.454 41.451  58.965  1.00 32.67 ?  90   GLU A OE1   1 
ATOM   560   O OE2   . GLU A 1 92   ? -15.956 41.086  57.405  1.00 34.47 ?  90   GLU A OE2   1 
ATOM   561   N N     . TYR A 1 93   ? -13.574 41.371  62.811  1.00 25.64 ?  91   TYR A N     1 
ATOM   562   C CA    . TYR A 1 93   ? -12.320 42.112  62.815  1.00 21.88 ?  91   TYR A CA    1 
ATOM   563   C C     . TYR A 1 93   ? -11.499 41.897  64.085  1.00 23.99 ?  91   TYR A C     1 
ATOM   564   O O     . TYR A 1 93   ? -10.519 42.619  64.301  1.00 22.60 ?  91   TYR A O     1 
ATOM   565   C CB    . TYR A 1 93   ? -12.598 43.601  62.588  1.00 22.84 ?  91   TYR A CB    1 
ATOM   566   C CG    . TYR A 1 93   ? -13.104 43.872  61.183  1.00 22.22 ?  91   TYR A CG    1 
ATOM   567   C CD1   . TYR A 1 93   ? -12.208 44.021  60.130  1.00 21.57 ?  91   TYR A CD1   1 
ATOM   568   C CD2   . TYR A 1 93   ? -14.465 43.951  60.902  1.00 24.98 ?  91   TYR A CD2   1 
ATOM   569   C CE1   . TYR A 1 93   ? -12.651 44.242  58.834  1.00 24.50 ?  91   TYR A CE1   1 
ATOM   570   C CE2   . TYR A 1 93   ? -14.917 44.179  59.598  1.00 25.85 ?  91   TYR A CE2   1 
ATOM   571   C CZ    . TYR A 1 93   ? -13.998 44.329  58.577  1.00 25.83 ?  91   TYR A CZ    1 
ATOM   572   O OH    . TYR A 1 93   ? -14.414 44.556  57.285  1.00 27.08 ?  91   TYR A OH    1 
ATOM   573   N N     . SER A 1 94   ? -11.867 40.915  64.912  1.00 21.68 ?  92   SER A N     1 
ATOM   574   C CA    . SER A 1 94   ? -11.134 40.562  66.133  1.00 22.20 ?  92   SER A CA    1 
ATOM   575   C C     . SER A 1 94   ? -10.927 41.780  67.024  1.00 20.06 ?  92   SER A C     1 
ATOM   576   O O     . SER A 1 94   ? -9.827  42.034  67.530  1.00 19.21 ?  92   SER A O     1 
ATOM   577   C CB    . SER A 1 94   ? -9.790  39.906  65.809  1.00 21.63 ?  92   SER A CB    1 
ATOM   578   O OG    . SER A 1 94   ? -9.970  38.796  64.941  1.00 27.39 ?  92   SER A OG    1 
ATOM   579   N N     . LEU A 1 95   ? -11.995 42.548  67.205  1.00 18.15 ?  93   LEU A N     1 
ATOM   580   C CA    . LEU A 1 95   ? -11.906 43.776  67.982  1.00 18.13 ?  93   LEU A CA    1 
ATOM   581   C C     . LEU A 1 95   ? -11.918 43.477  69.471  1.00 16.00 ?  93   LEU A C     1 
ATOM   582   O O     . LEU A 1 95   ? -12.686 42.637  69.944  1.00 19.41 ?  93   LEU A O     1 
ATOM   583   C CB    . LEU A 1 95   ? -13.073 44.715  67.663  1.00 17.68 ?  93   LEU A CB    1 
ATOM   584   C CG    . LEU A 1 95   ? -13.189 45.125  66.199  1.00 16.54 ?  93   LEU A CG    1 
ATOM   585   C CD1   . LEU A 1 95   ? -14.323 46.143  66.072  1.00 20.16 ?  93   LEU A CD1   1 
ATOM   586   C CD2   . LEU A 1 95   ? -11.888 45.683  65.673  1.00 20.69 ?  93   LEU A CD2   1 
ATOM   587   N N     . SER A 1 96   ? -11.076 44.185  70.216  1.00 14.22 ?  94   SER A N     1 
ATOM   588   C CA    . SER A 1 96   ? -11.270 44.259  71.654  1.00 14.05 ?  94   SER A CA    1 
ATOM   589   C C     . SER A 1 96   ? -12.517 45.086  71.981  1.00 15.74 ?  94   SER A C     1 
ATOM   590   O O     . SER A 1 96   ? -13.089 45.765  71.124  1.00 14.11 ?  94   SER A O     1 
ATOM   591   C CB    . SER A 1 96   ? -10.058 44.900  72.312  1.00 16.55 ?  94   SER A CB    1 
ATOM   592   O OG    . SER A 1 96   ? -10.030 46.273  71.955  1.00 14.42 ?  94   SER A OG    1 
ATOM   593   N N     . SER A 1 97   ? -12.934 45.036  73.248  1.00 15.26 ?  95   SER A N     1 
ATOM   594   C CA    . SER A 1 97   ? -14.061 45.858  73.675  1.00 14.47 ?  95   SER A CA    1 
ATOM   595   C C     . SER A 1 97   ? -13.794 47.337  73.423  1.00 14.03 ?  95   SER A C     1 
ATOM   596   O O     . SER A 1 97   ? -14.655 48.053  72.896  1.00 12.66 ?  95   SER A O     1 
ATOM   597   C CB    . SER A 1 97   ? -14.368 45.620  75.154  1.00 17.44 ?  95   SER A CB    1 
ATOM   598   O OG    . SER A 1 97   ? -14.939 44.339  75.318  1.00 23.83 ?  95   SER A OG    1 
ATOM   599   N N     . GLN A 1 98   ? -12.618 47.824  73.813  1.00 11.98 ?  96   GLN A N     1 
ATOM   600   C CA    . GLN A 1 98   ? -12.345 49.241  73.621  1.00 11.67 ?  96   GLN A CA    1 
ATOM   601   C C     . GLN A 1 98   ? -12.292 49.592  72.137  1.00 10.67 ?  96   GLN A C     1 
ATOM   602   O O     . GLN A 1 98   ? -12.714 50.687  71.743  1.00 10.90 ?  96   GLN A O     1 
ATOM   603   C CB    . GLN A 1 98   ? -11.047 49.635  74.331  1.00 11.85 ?  96   GLN A CB    1 
ATOM   604   C CG    . GLN A 1 98   ? -11.202 49.728  75.868  1.00 12.42 ?  96   GLN A CG    1 
ATOM   605   C CD    . GLN A 1 98   ? -12.118 50.851  76.297  1.00 14.25 ?  96   GLN A CD    1 
ATOM   606   O OE1   . GLN A 1 98   ? -13.337 50.689  76.361  1.00 16.02 ?  96   GLN A OE1   1 
ATOM   607   N NE2   . GLN A 1 98   ? -11.533 51.992  76.633  1.00 15.42 ?  96   GLN A NE2   1 
ATOM   608   N N     . GLU A 1 99   ? -11.770 48.684  71.304  1.00 12.54 ?  97   GLU A N     1 
ATOM   609   C CA    . GLU A 1 99   ? -11.790 48.931  69.863  1.00 11.35 ?  97   GLU A CA    1 
ATOM   610   C C     . GLU A 1 99   ? -13.210 49.005  69.337  1.00 13.95 ?  97   GLU A C     1 
ATOM   611   O O     . GLU A 1 99   ? -13.519 49.863  68.500  1.00 12.70 ?  97   GLU A O     1 
ATOM   612   C CB    . GLU A 1 99   ? -10.995 47.859  69.119  1.00 13.24 ?  97   GLU A CB    1 
ATOM   613   C CG    . GLU A 1 99   ? -9.495  48.005  69.344  1.00 13.44 ?  97   GLU A CG    1 
ATOM   614   C CD    . GLU A 1 99   ? -8.693  46.815  68.860  1.00 14.93 ?  97   GLU A CD    1 
ATOM   615   O OE1   . GLU A 1 99   ? -9.300  45.809  68.431  1.00 15.95 ?  97   GLU A OE1   1 
ATOM   616   O OE2   . GLU A 1 99   ? -7.446  46.885  68.932  1.00 15.20 ?  97   GLU A OE2   1 
ATOM   617   N N     . GLY A 1 100  ? -14.092 48.116  69.801  1.00 12.77 ?  98   GLY A N     1 
ATOM   618   C CA    . GLY A 1 100  ? -15.476 48.184  69.355  1.00 13.20 ?  98   GLY A CA    1 
ATOM   619   C C     . GLY A 1 100  ? -16.136 49.494  69.748  1.00 11.46 ?  98   GLY A C     1 
ATOM   620   O O     . GLY A 1 100  ? -16.827 50.127  68.944  1.00 12.31 ?  98   GLY A O     1 
ATOM   621   N N     . VAL A 1 101  ? -15.924 49.922  70.994  1.00 11.40 ?  99   VAL A N     1 
ATOM   622   C CA    . VAL A 1 101  ? -16.480 51.193  71.451  1.00 11.91 ?  99   VAL A CA    1 
ATOM   623   C C     . VAL A 1 101  ? -15.925 52.339  70.618  1.00 10.70 ?  99   VAL A C     1 
ATOM   624   O O     . VAL A 1 101  ? -16.677 53.177  70.111  1.00 12.31 ?  99   VAL A O     1 
ATOM   625   C CB    . VAL A 1 101  ? -16.194 51.393  72.945  1.00 11.63 ?  99   VAL A CB    1 
ATOM   626   C CG1   . VAL A 1 101  ? -16.631 52.794  73.382  1.00 12.90 ?  99   VAL A CG1   1 
ATOM   627   C CG2   . VAL A 1 101  ? -16.929 50.334  73.753  1.00 13.63 ?  99   VAL A CG2   1 
ATOM   628   N N     . ALA A 1 102  ? -14.598 52.365  70.432  1.00 12.06 ?  100  ALA A N     1 
ATOM   629   C CA    . ALA A 1 102  ? -13.975 53.448  69.673  1.00 11.93 ?  100  ALA A CA    1 
ATOM   630   C C     . ALA A 1 102  ? -14.496 53.500  68.245  1.00 11.92 ?  100  ALA A C     1 
ATOM   631   O O     . ALA A 1 102  ? -14.712 54.587  67.701  1.00 11.71 ?  100  ALA A O     1 
ATOM   632   C CB    . ALA A 1 102  ? -12.450 53.286  69.671  1.00 11.43 ?  100  ALA A CB    1 
ATOM   633   N N     . LEU A 1 103  ? -14.660 52.334  67.618  1.00 11.38 ?  101  LEU A N     1 
ATOM   634   C CA    . LEU A 1 103  ? -15.171 52.279  66.253  1.00 11.24 ?  101  LEU A CA    1 
ATOM   635   C C     . LEU A 1 103  ? -16.564 52.871  66.176  1.00 12.41 ?  101  LEU A C     1 
ATOM   636   O O     . LEU A 1 103  ? -16.870 53.633  65.251  1.00 14.48 ?  101  LEU A O     1 
ATOM   637   C CB    . LEU A 1 103  ? -15.173 50.838  65.742  1.00 14.34 ?  101  LEU A CB    1 
ATOM   638   C CG    . LEU A 1 103  ? -15.783 50.650  64.351  1.00 12.52 ?  101  LEU A CG    1 
ATOM   639   C CD1   . LEU A 1 103  ? -14.969 51.421  63.313  1.00 16.05 ?  101  LEU A CD1   1 
ATOM   640   C CD2   . LEU A 1 103  ? -15.812 49.166  64.055  1.00 15.11 ?  101  LEU A CD2   1 
ATOM   641   N N     . MET A 1 104  ? -17.430 52.523  67.131  1.00 11.36 ?  102  MET A N     1 
ATOM   642   C CA    . MET A 1 104  ? -18.786 53.069  67.081  1.00 14.32 ?  102  MET A CA    1 
ATOM   643   C C     . MET A 1 104  ? -18.790 54.567  67.340  1.00 14.77 ?  102  MET A C     1 
ATOM   644   O O     . MET A 1 104  ? -19.602 55.282  66.746  1.00 14.90 ?  102  MET A O     1 
ATOM   645   C CB    . MET A 1 104  ? -19.703 52.345  68.070  1.00 13.65 ?  102  MET A CB    1 
ATOM   646   C CG    . MET A 1 104  ? -19.837 50.859  67.769  1.00 14.41 ?  102  MET A CG    1 
ATOM   647   S SD    . MET A 1 104  ? -20.314 50.450  66.062  1.00 20.84 ?  102  MET A SD    1 
ATOM   648   C CE    . MET A 1 104  ? -21.992 51.058  66.042  1.00 22.69 ?  102  MET A CE    1 
ATOM   649   N N     . CYS A 1 105  ? -17.889 55.065  68.197  1.00 13.18 ?  103  CYS A N     1 
ATOM   650   C CA    . CYS A 1 105  ? -17.762 56.510  68.375  1.00 12.73 ?  103  CYS A CA    1 
ATOM   651   C C     . CYS A 1 105  ? -17.316 57.190  67.086  1.00 15.12 ?  103  CYS A C     1 
ATOM   652   O O     . CYS A 1 105  ? -17.828 58.260  66.733  1.00 16.81 ?  103  CYS A O     1 
ATOM   653   C CB    . CYS A 1 105  ? -16.766 56.823  69.491  1.00 13.61 ?  103  CYS A CB    1 
ATOM   654   S SG    . CYS A 1 105  ? -17.343 56.372  71.118  1.00 14.79 ?  103  CYS A SG    1 
ATOM   655   N N     . LEU A 1 106  ? -16.336 56.609  66.385  1.00 13.48 ?  104  LEU A N     1 
ATOM   656   C CA    . LEU A 1 106  ? -15.919 57.166  65.104  1.00 16.86 ?  104  LEU A CA    1 
ATOM   657   C C     . LEU A 1 106  ? -17.071 57.168  64.121  1.00 16.57 ?  104  LEU A C     1 
ATOM   658   O O     . LEU A 1 106  ? -17.305 58.162  63.426  1.00 17.91 ?  104  LEU A O     1 
ATOM   659   C CB    . LEU A 1 106  ? -14.752 56.366  64.532  1.00 14.39 ?  104  LEU A CB    1 
ATOM   660   C CG    . LEU A 1 106  ? -14.367 56.750  63.097  1.00 16.22 ?  104  LEU A CG    1 
ATOM   661   C CD1   . LEU A 1 106  ? -13.823 58.178  63.069  1.00 19.68 ?  104  LEU A CD1   1 
ATOM   662   C CD2   . LEU A 1 106  ? -13.360 55.752  62.528  1.00 17.46 ?  104  LEU A CD2   1 
ATOM   663   N N     . ALA A 1 107  ? -17.798 56.050  64.038  1.00 13.90 ?  105  ALA A N     1 
ATOM   664   C CA    . ALA A 1 107  ? -18.935 55.981  63.127  1.00 16.01 ?  105  ALA A CA    1 
ATOM   665   C C     . ALA A 1 107  ? -19.961 57.060  63.454  1.00 18.69 ?  105  ALA A C     1 
ATOM   666   O O     . ALA A 1 107  ? -20.485 57.721  62.550  1.00 18.22 ?  105  ALA A O     1 
ATOM   667   C CB    . ALA A 1 107  ? -19.574 54.592  63.191  1.00 16.18 ?  105  ALA A CB    1 
ATOM   668   N N     . GLU A 1 108  ? -20.265 57.244  64.738  1.00 16.40 ?  106  GLU A N     1 
ATOM   669   C CA    . GLU A 1 108  ? -21.173 58.313  65.151  1.00 17.52 ?  106  GLU A CA    1 
ATOM   670   C C     . GLU A 1 108  ? -20.697 59.669  64.649  1.00 19.51 ?  106  GLU A C     1 
ATOM   671   O O     . GLU A 1 108  ? -21.489 60.456  64.113  1.00 21.74 ?  106  GLU A O     1 
ATOM   672   C CB    . GLU A 1 108  ? -21.291 58.322  66.675  1.00 16.71 ?  106  GLU A CB    1 
ATOM   673   C CG    . GLU A 1 108  ? -22.176 59.441  67.252  1.00 17.37 ?  106  GLU A CG    1 
ATOM   674   C CD    . GLU A 1 108  ? -21.893 59.743  68.714  1.00 21.94 ?  106  GLU A CD    1 
ATOM   675   O OE1   . GLU A 1 108  ? -21.398 58.843  69.430  1.00 18.67 ?  106  GLU A OE1   1 
ATOM   676   O OE2   . GLU A 1 108  ? -22.162 60.892  69.138  1.00 20.92 ?  106  GLU A OE2   1 
ATOM   677   N N     . ALA A 1 109  ? -19.401 59.958  64.815  1.00 19.30 ?  107  ALA A N     1 
ATOM   678   C CA    . ALA A 1 109  ? -18.848 61.238  64.381  1.00 20.84 ?  107  ALA A CA    1 
ATOM   679   C C     . ALA A 1 109  ? -18.918 61.396  62.867  1.00 23.05 ?  107  ALA A C     1 
ATOM   680   O O     . ALA A 1 109  ? -19.259 62.477  62.370  1.00 25.21 ?  107  ALA A O     1 
ATOM   681   C CB    . ALA A 1 109  ? -17.407 61.372  64.867  1.00 21.02 ?  107  ALA A CB    1 
ATOM   682   N N     . LEU A 1 110  ? -18.600 60.336  62.113  1.00 19.61 ?  108  LEU A N     1 
ATOM   683   C CA    . LEU A 1 110  ? -18.696 60.411  60.658  1.00 21.11 ?  108  LEU A CA    1 
ATOM   684   C C     . LEU A 1 110  ? -20.130 60.654  60.201  1.00 23.25 ?  108  LEU A C     1 
ATOM   685   O O     . LEU A 1 110  ? -20.349 61.325  59.187  1.00 26.40 ?  108  LEU A O     1 
ATOM   686   C CB    . LEU A 1 110  ? -18.144 59.136  60.023  1.00 20.52 ?  108  LEU A CB    1 
ATOM   687   C CG    . LEU A 1 110  ? -16.622 59.034  60.094  1.00 23.22 ?  108  LEU A CG    1 
ATOM   688   C CD1   . LEU A 1 110  ? -16.193 57.608  59.829  1.00 20.86 ?  108  LEU A CD1   1 
ATOM   689   C CD2   . LEU A 1 110  ? -16.016 59.980  59.062  1.00 23.64 ?  108  LEU A CD2   1 
ATOM   690   N N     . LEU A 1 111  ? -21.115 60.138  60.939  1.00 22.28 ?  109  LEU A N     1 
ATOM   691   C CA    . LEU A 1 111  ? -22.512 60.378  60.599  1.00 23.00 ?  109  LEU A CA    1 
ATOM   692   C C     . LEU A 1 111  ? -22.972 61.787  60.963  1.00 26.50 ?  109  LEU A C     1 
ATOM   693   O O     . LEU A 1 111  ? -24.075 62.182  60.564  1.00 29.14 ?  109  LEU A O     1 
ATOM   694   C CB    . LEU A 1 111  ? -23.400 59.325  61.280  1.00 21.01 ?  109  LEU A CB    1 
ATOM   695   C CG    . LEU A 1 111  ? -23.180 57.900  60.739  1.00 20.02 ?  109  LEU A CG    1 
ATOM   696   C CD1   . LEU A 1 111  ? -23.851 56.847  61.614  1.00 21.96 ?  109  LEU A CD1   1 
ATOM   697   C CD2   . LEU A 1 111  ? -23.639 57.773  59.289  1.00 21.58 ?  109  LEU A CD2   1 
ATOM   698   N N     . ARG A 1 112  ? -22.165 62.556  61.698  1.00 25.28 ?  110  ARG A N     1 
ATOM   699   C CA    . ARG A 1 112  ? -22.460 63.973  61.881  1.00 27.30 ?  110  ARG A CA    1 
ATOM   700   C C     . ARG A 1 112  ? -22.138 64.784  60.634  1.00 31.50 ?  110  ARG A C     1 
ATOM   701   O O     . ARG A 1 112  ? -22.529 65.954  60.557  1.00 34.79 ?  110  ARG A O     1 
ATOM   702   C CB    . ARG A 1 112  ? -21.699 64.529  63.092  1.00 28.15 ?  110  ARG A CB    1 
ATOM   703   C CG    . ARG A 1 112  ? -22.084 63.877  64.422  1.00 24.78 ?  110  ARG A CG    1 
ATOM   704   C CD    . ARG A 1 112  ? -21.111 64.226  65.556  1.00 28.38 ?  110  ARG A CD    1 
ATOM   705   N NE    . ARG A 1 112  ? -21.202 65.620  65.980  1.00 29.98 ?  110  ARG A NE    1 
ATOM   706   C CZ    . ARG A 1 112  ? -22.022 66.074  66.921  1.00 32.40 ?  110  ARG A CZ    1 
ATOM   707   N NH1   . ARG A 1 112  ? -22.856 65.270  67.560  1.00 31.11 ?  110  ARG A NH1   1 
ATOM   708   N NH2   . ARG A 1 112  ? -22.008 67.369  67.225  1.00 33.01 ?  110  ARG A NH2   1 
ATOM   709   N N     . ILE A 1 113  ? -21.439 64.191  59.667  1.00 28.79 ?  111  ILE A N     1 
ATOM   710   C CA    . ILE A 1 113  ? -21.202 64.790  58.355  1.00 34.04 ?  111  ILE A CA    1 
ATOM   711   C C     . ILE A 1 113  ? -22.424 64.514  57.484  1.00 35.40 ?  111  ILE A C     1 
ATOM   712   O O     . ILE A 1 113  ? -22.671 63.353  57.128  1.00 34.26 ?  111  ILE A O     1 
ATOM   713   C CB    . ILE A 1 113  ? -19.923 64.238  57.712  1.00 32.66 ?  111  ILE A CB    1 
ATOM   714   C CG1   . ILE A 1 113  ? -18.716 64.537  58.598  1.00 31.92 ?  111  ILE A CG1   1 
ATOM   715   C CG2   . ILE A 1 113  ? -19.725 64.819  56.322  1.00 34.15 ?  111  ILE A CG2   1 
ATOM   716   C CD1   . ILE A 1 113  ? -17.417 64.005  58.047  1.00 33.31 ?  111  ILE A CD1   1 
ATOM   717   N N     . PRO A 1 114  ? -23.198 65.535  57.104  1.00 42.75 ?  112  PRO A N     1 
ATOM   718   C CA    . PRO A 1 114  ? -24.513 65.257  56.492  1.00 44.31 ?  112  PRO A CA    1 
ATOM   719   C C     . PRO A 1 114  ? -24.433 64.703  55.080  1.00 42.05 ?  112  PRO A C     1 
ATOM   720   O O     . PRO A 1 114  ? -25.241 63.837  54.719  1.00 42.57 ?  112  PRO A O     1 
ATOM   721   C CB    . PRO A 1 114  ? -25.215 66.626  56.523  1.00 42.05 ?  112  PRO A CB    1 
ATOM   722   C CG    . PRO A 1 114  ? -24.363 67.510  57.401  1.00 46.77 ?  112  PRO A CG    1 
ATOM   723   C CD    . PRO A 1 114  ? -22.969 66.975  57.302  1.00 42.81 ?  112  PRO A CD    1 
ATOM   724   N N     . ASP A 1 115  ? -23.490 65.171  54.267  1.00 40.52 ?  113  ASP A N     1 
ATOM   725   C CA    . ASP A 1 115  ? -23.421 64.744  52.876  1.00 43.55 ?  113  ASP A CA    1 
ATOM   726   C C     . ASP A 1 115  ? -22.694 63.410  52.759  1.00 39.62 ?  113  ASP A C     1 
ATOM   727   O O     . ASP A 1 115  ? -21.571 63.260  53.252  1.00 40.62 ?  113  ASP A O     1 
ATOM   728   C CB    . ASP A 1 115  ? -22.720 65.800  52.025  1.00 45.65 ?  113  ASP A CB    1 
ATOM   729   C CG    . ASP A 1 115  ? -22.503 65.340  50.600  1.00 43.74 ?  113  ASP A CG    1 
ATOM   730   O OD1   . ASP A 1 115  ? -23.494 64.963  49.938  1.00 47.83 ?  113  ASP A OD1   1 
ATOM   731   O OD2   . ASP A 1 115  ? -21.342 65.355  50.139  1.00 43.89 ?  113  ASP A OD2   1 
ATOM   732   N N     . THR A 1 116  ? -23.327 62.451  52.077  1.00 40.36 ?  114  THR A N     1 
ATOM   733   C CA    . THR A 1 116  ? -22.775 61.100  52.003  1.00 39.47 ?  114  THR A CA    1 
ATOM   734   C C     . THR A 1 116  ? -21.445 61.073  51.255  1.00 41.87 ?  114  THR A C     1 
ATOM   735   O O     . THR A 1 116  ? -20.463 60.493  51.738  1.00 38.73 ?  114  THR A O     1 
ATOM   736   C CB    . THR A 1 116  ? -23.783 60.158  51.342  1.00 42.13 ?  114  THR A CB    1 
ATOM   737   O OG1   . THR A 1 116  ? -25.000 60.153  52.098  1.00 41.01 ?  114  THR A OG1   1 
ATOM   738   C CG2   . THR A 1 116  ? -23.227 58.743  51.277  1.00 43.27 ?  114  THR A CG2   1 
ATOM   739   N N     . ALA A 1 117  ? -21.391 61.690  50.071  1.00 40.69 ?  115  ALA A N     1 
ATOM   740   C CA    . ALA A 1 117  ? -20.166 61.650  49.276  1.00 37.41 ?  115  ALA A CA    1 
ATOM   741   C C     . ALA A 1 117  ? -18.998 62.287  50.018  1.00 34.36 ?  115  ALA A C     1 
ATOM   742   O O     . ALA A 1 117  ? -17.869 61.789  49.952  1.00 39.70 ?  115  ALA A O     1 
ATOM   743   C CB    . ALA A 1 117  ? -20.387 62.343  47.932  1.00 42.39 ?  115  ALA A CB    1 
ATOM   744   N N     . THR A 1 118  ? -19.248 63.390  50.725  1.00 37.29 ?  116  THR A N     1 
ATOM   745   C CA    . THR A 1 118  ? -18.190 64.025  51.506  1.00 38.47 ?  116  THR A CA    1 
ATOM   746   C C     . THR A 1 118  ? -17.669 63.080  52.581  1.00 34.42 ?  116  THR A C     1 
ATOM   747   O O     . THR A 1 118  ? -16.455 62.905  52.740  1.00 33.41 ?  116  THR A O     1 
ATOM   748   C CB    . THR A 1 118  ? -18.709 65.316  52.142  1.00 34.75 ?  116  THR A CB    1 
ATOM   749   O OG1   . THR A 1 118  ? -19.016 66.270  51.118  1.00 42.43 ?  116  THR A OG1   1 
ATOM   750   C CG2   . THR A 1 118  ? -17.670 65.903  53.080  1.00 38.49 ?  116  THR A CG2   1 
ATOM   751   N N     . ARG A 1 119  ? -18.586 62.459  53.324  1.00 35.16 ?  117  ARG A N     1 
ATOM   752   C CA    . ARG A 1 119  ? -18.209 61.500  54.358  1.00 32.95 ?  117  ARG A CA    1 
ATOM   753   C C     . ARG A 1 119  ? -17.365 60.368  53.782  1.00 34.42 ?  117  ARG A C     1 
ATOM   754   O O     . ARG A 1 119  ? -16.305 60.028  54.322  1.00 30.16 ?  117  ARG A O     1 
ATOM   755   C CB    . ARG A 1 119  ? -19.469 60.947  55.020  1.00 31.47 ?  117  ARG A CB    1 
ATOM   756   C CG    . ARG A 1 119  ? -19.217 60.021  56.193  1.00 29.72 ?  117  ARG A CG    1 
ATOM   757   C CD    . ARG A 1 119  ? -20.491 59.270  56.521  1.00 25.51 ?  117  ARG A CD    1 
ATOM   758   N NE    . ARG A 1 119  ? -21.608 60.181  56.729  1.00 28.14 ?  117  ARG A NE    1 
ATOM   759   C CZ    . ARG A 1 119  ? -22.843 59.968  56.298  1.00 30.56 ?  117  ARG A CZ    1 
ATOM   760   N NH1   . ARG A 1 119  ? -23.156 58.891  55.594  1.00 30.00 ?  117  ARG A NH1   1 
ATOM   761   N NH2   . ARG A 1 119  ? -23.789 60.864  56.570  1.00 34.21 ?  117  ARG A NH2   1 
ATOM   762   N N     . ASP A 1 120  ? -17.822 59.776  52.674  1.00 33.91 ?  118  ASP A N     1 
ATOM   763   C CA    . ASP A 1 120  ? -17.102 58.656  52.078  1.00 36.10 ?  118  ASP A CA    1 
ATOM   764   C C     . ASP A 1 120  ? -15.731 59.071  51.570  1.00 36.06 ?  118  ASP A C     1 
ATOM   765   O O     . ASP A 1 120  ? -14.791 58.268  51.604  1.00 33.45 ?  118  ASP A O     1 
ATOM   766   C CB    . ASP A 1 120  ? -17.920 58.045  50.941  1.00 35.90 ?  118  ASP A CB    1 
ATOM   767   C CG    . ASP A 1 120  ? -19.264 57.530  51.405  1.00 38.33 ?  118  ASP A CG    1 
ATOM   768   O OD1   . ASP A 1 120  ? -19.418 57.276  52.621  1.00 37.72 ?  118  ASP A OD1   1 
ATOM   769   O OD2   . ASP A 1 120  ? -20.167 57.374  50.558  1.00 41.84 ?  118  ASP A OD2   1 
ATOM   770   N N     . ALA A 1 121  ? -15.598 60.309  51.085  1.00 34.05 ?  119  ALA A N     1 
ATOM   771   C CA    . ALA A 1 121  ? -14.290 60.791  50.660  1.00 37.42 ?  119  ALA A CA    1 
ATOM   772   C C     . ALA A 1 121  ? -13.358 60.953  51.851  1.00 36.40 ?  119  ALA A C     1 
ATOM   773   O O     . ALA A 1 121  ? -12.172 60.612  51.771  1.00 36.20 ?  119  ALA A O     1 
ATOM   774   C CB    . ALA A 1 121  ? -14.434 62.113  49.905  1.00 36.46 ?  119  ALA A CB    1 
ATOM   775   N N     . LEU A 1 122  ? -13.879 61.464  52.970  1.00 35.24 ?  120  LEU A N     1 
ATOM   776   C CA    . LEU A 1 122  ? -13.053 61.614  54.162  1.00 31.97 ?  120  LEU A CA    1 
ATOM   777   C C     . LEU A 1 122  ? -12.561 60.260  54.658  1.00 36.04 ?  120  LEU A C     1 
ATOM   778   O O     . LEU A 1 122  ? -11.394 60.117  55.042  1.00 34.07 ?  120  LEU A O     1 
ATOM   779   C CB    . LEU A 1 122  ? -13.835 62.340  55.255  1.00 32.15 ?  120  LEU A CB    1 
ATOM   780   C CG    . LEU A 1 122  ? -13.012 62.751  56.475  1.00 33.63 ?  120  LEU A CG    1 
ATOM   781   C CD1   . LEU A 1 122  ? -11.990 63.811  56.085  1.00 39.19 ?  120  LEU A CD1   1 
ATOM   782   C CD2   . LEU A 1 122  ? -13.900 63.243  57.607  1.00 35.18 ?  120  LEU A CD2   1 
ATOM   783   N N     . ILE A 1 123  ? -13.434 59.250  54.640  1.00 32.63 ?  121  ILE A N     1 
ATOM   784   C CA    . ILE A 1 123  ? -13.038 57.914  55.076  1.00 30.83 ?  121  ILE A CA    1 
ATOM   785   C C     . ILE A 1 123  ? -11.932 57.365  54.182  1.00 34.98 ?  121  ILE A C     1 
ATOM   786   O O     . ILE A 1 123  ? -10.888 56.903  54.663  1.00 31.66 ?  121  ILE A O     1 
ATOM   787   C CB    . ILE A 1 123  ? -14.254 56.973  55.096  1.00 30.09 ?  121  ILE A CB    1 
ATOM   788   C CG1   . ILE A 1 123  ? -15.223 57.361  56.218  1.00 28.31 ?  121  ILE A CG1   1 
ATOM   789   C CG2   . ILE A 1 123  ? -13.791 55.524  55.222  1.00 30.04 ?  121  ILE A CG2   1 
ATOM   790   C CD1   . ILE A 1 123  ? -16.594 56.737  56.073  1.00 29.19 ?  121  ILE A CD1   1 
ATOM   791   N N     . ARG A 1 124  ? -12.144 57.409  52.864  1.00 31.88 ?  122  ARG A N     1 
ATOM   792   C CA    . ARG A 1 124  ? -11.202 56.772  51.946  1.00 39.95 ?  122  ARG A CA    1 
ATOM   793   C C     . ARG A 1 124  ? -9.878  57.522  51.893  1.00 40.02 ?  122  ARG A C     1 
ATOM   794   O O     . ARG A 1 124  ? -8.811  56.902  51.812  1.00 43.72 ?  122  ARG A O     1 
ATOM   795   C CB    . ARG A 1 124  ? -11.813 56.670  50.548  1.00 37.97 ?  122  ARG A CB    1 
ATOM   796   N N     . ASP A 1 125  ? -9.921  58.853  51.956  1.00 41.18 ?  123  ASP A N     1 
ATOM   797   C CA    . ASP A 1 125  ? -8.746  59.661  51.660  1.00 45.50 ?  123  ASP A CA    1 
ATOM   798   C C     . ASP A 1 125  ? -8.034  60.198  52.892  1.00 46.01 ?  123  ASP A C     1 
ATOM   799   O O     . ASP A 1 125  ? -6.878  60.618  52.779  1.00 50.28 ?  123  ASP A O     1 
ATOM   800   C CB    . ASP A 1 125  ? -9.131  60.840  50.753  1.00 49.74 ?  123  ASP A CB    1 
ATOM   801   C CG    . ASP A 1 125  ? -9.733  60.392  49.427  1.00 51.11 ?  123  ASP A CG    1 
ATOM   802   O OD1   . ASP A 1 125  ? -9.314  59.338  48.901  1.00 52.20 ?  123  ASP A OD1   1 
ATOM   803   O OD2   . ASP A 1 125  ? -10.627 61.097  48.909  1.00 54.03 ?  123  ASP A OD2   1 
ATOM   804   N N     . LYS A 1 126  ? -8.673  60.193  54.062  1.00 40.31 ?  124  LYS A N     1 
ATOM   805   C CA    . LYS A 1 126  ? -8.046  60.808  55.227  1.00 42.31 ?  124  LYS A CA    1 
ATOM   806   C C     . LYS A 1 126  ? -8.069  59.898  56.452  1.00 41.07 ?  124  LYS A C     1 
ATOM   807   O O     . LYS A 1 126  ? -7.044  59.736  57.124  1.00 47.11 ?  124  LYS A O     1 
ATOM   808   C CB    . LYS A 1 126  ? -8.729  62.140  55.546  1.00 42.95 ?  124  LYS A CB    1 
ATOM   809   N N     . ILE A 1 127  ? -9.228  59.308  56.755  1.00 38.76 ?  125  ILE A N     1 
ATOM   810   C CA    . ILE A 1 127  ? -9.372  58.527  57.984  1.00 33.43 ?  125  ILE A CA    1 
ATOM   811   C C     . ILE A 1 127  ? -8.604  57.213  57.878  1.00 38.69 ?  125  ILE A C     1 
ATOM   812   O O     . ILE A 1 127  ? -7.842  56.845  58.781  1.00 35.10 ?  125  ILE A O     1 
ATOM   813   C CB    . ILE A 1 127  ? -10.862 58.279  58.293  1.00 29.30 ?  125  ILE A CB    1 
ATOM   814   C CG1   . ILE A 1 127  ? -11.660 59.584  58.253  1.00 35.68 ?  125  ILE A CG1   1 
ATOM   815   C CG2   . ILE A 1 127  ? -11.021 57.631  59.664  1.00 29.34 ?  125  ILE A CG2   1 
ATOM   816   C CD1   . ILE A 1 127  ? -11.211 60.602  59.267  1.00 38.77 ?  125  ILE A CD1   1 
ATOM   817   N N     . ALA A 1 128  ? -8.792  56.489  56.772  1.00 29.71 ?  126  ALA A N     1 
ATOM   818   C CA    . ALA A 1 128  ? -8.260  55.135  56.670  1.00 34.52 ?  126  ALA A CA    1 
ATOM   819   C C     . ALA A 1 128  ? -6.747  55.139  56.530  1.00 42.30 ?  126  ALA A C     1 
ATOM   820   O O     . ALA A 1 128  ? -6.068  54.276  57.093  1.00 37.34 ?  126  ALA A O     1 
ATOM   821   C CB    . ALA A 1 128  ? -8.892  54.406  55.486  1.00 32.44 ?  126  ALA A CB    1 
ATOM   822   N N     . ASP A 1 129  ? -6.207  56.097  55.775  1.00 53.84 ?  127  ASP A N     1 
ATOM   823   C CA    . ASP A 1 129  ? -4.796  56.102  55.414  1.00 58.10 ?  127  ASP A CA    1 
ATOM   824   C C     . ASP A 1 129  ? -3.893  56.595  56.534  1.00 59.23 ?  127  ASP A C     1 
ATOM   825   O O     . ASP A 1 129  ? -2.667  56.488  56.411  1.00 65.01 ?  127  ASP A O     1 
ATOM   826   C CB    . ASP A 1 129  ? -4.579  56.959  54.163  1.00 58.24 ?  127  ASP A CB    1 
ATOM   827   N N     . GLY A 1 130  ? -4.452  57.128  57.614  1.00 52.75 ?  128  GLY A N     1 
ATOM   828   C CA    . GLY A 1 130  ? -3.612  57.519  58.723  1.00 59.30 ?  128  GLY A CA    1 
ATOM   829   C C     . GLY A 1 130  ? -4.334  58.112  59.910  1.00 56.90 ?  128  GLY A C     1 
ATOM   830   O O     . GLY A 1 130  ? -5.244  57.500  60.481  1.00 53.34 ?  128  GLY A O     1 
ATOM   831   N N     . ASN A 1 131  ? -3.918  59.316  60.287  1.00 63.29 ?  129  ASN A N     1 
ATOM   832   C CA    . ASN A 1 131  ? -4.392  59.944  61.512  1.00 60.67 ?  129  ASN A CA    1 
ATOM   833   C C     . ASN A 1 131  ? -5.820  60.440  61.340  1.00 58.17 ?  129  ASN A C     1 
ATOM   834   O O     . ASN A 1 131  ? -6.088  61.340  60.536  1.00 61.73 ?  129  ASN A O     1 
ATOM   835   C CB    . ASN A 1 131  ? -3.468  61.095  61.894  1.00 65.13 ?  129  ASN A CB    1 
ATOM   836   C CG    . ASN A 1 131  ? -3.019  61.895  60.691  1.00 70.43 ?  129  ASN A CG    1 
ATOM   837   O OD1   . ASN A 1 131  ? -2.004  61.581  60.068  1.00 76.24 ?  129  ASN A OD1   1 
ATOM   838   N ND2   . ASN A 1 131  ? -3.783  62.925  60.345  1.00 69.74 ?  129  ASN A ND2   1 
ATOM   839   N N     . TRP A 1 132  ? -6.736  59.839  62.095  1.00 50.06 ?  130  TRP A N     1 
ATOM   840   C CA    . TRP A 1 132  ? -8.092  60.357  62.204  1.00 43.10 ?  130  TRP A CA    1 
ATOM   841   C C     . TRP A 1 132  ? -8.147  61.654  62.996  1.00 41.69 ?  130  TRP A C     1 
ATOM   842   O O     . TRP A 1 132  ? -9.112  62.412  62.854  1.00 42.34 ?  130  TRP A O     1 
ATOM   843   C CB    . TRP A 1 132  ? -8.979  59.311  62.876  1.00 36.59 ?  130  TRP A CB    1 
ATOM   844   C CG    . TRP A 1 132  ? -8.403  58.828  64.188  1.00 32.32 ?  130  TRP A CG    1 
ATOM   845   C CD1   . TRP A 1 132  ? -7.534  57.788  64.372  1.00 30.93 ?  130  TRP A CD1   1 
ATOM   846   C CD2   . TRP A 1 132  ? -8.648  59.379  65.482  1.00 26.84 ?  130  TRP A CD2   1 
ATOM   847   N NE1   . TRP A 1 132  ? -7.232  57.653  65.708  1.00 27.08 ?  130  TRP A NE1   1 
ATOM   848   C CE2   . TRP A 1 132  ? -7.898  58.622  66.410  1.00 26.85 ?  130  TRP A CE2   1 
ATOM   849   C CE3   . TRP A 1 132  ? -9.426  60.440  65.951  1.00 30.23 ?  130  TRP A CE3   1 
ATOM   850   C CZ2   . TRP A 1 132  ? -7.916  58.886  67.772  1.00 23.42 ?  130  TRP A CZ2   1 
ATOM   851   C CZ3   . TRP A 1 132  ? -9.441  60.704  67.306  1.00 26.25 ?  130  TRP A CZ3   1 
ATOM   852   C CH2   . TRP A 1 132  ? -8.690  59.929  68.204  1.00 25.30 ?  130  TRP A CH2   1 
ATOM   853   N N     . LYS A 1 133  ? -7.137  61.912  63.833  1.00 45.74 ?  131  LYS A N     1 
ATOM   854   C CA    . LYS A 1 133  ? -7.199  63.036  64.763  1.00 49.54 ?  131  LYS A CA    1 
ATOM   855   C C     . LYS A 1 133  ? -7.200  64.370  64.025  1.00 56.19 ?  131  LYS A C     1 
ATOM   856   O O     . LYS A 1 133  ? -7.926  65.296  64.408  1.00 58.83 ?  131  LYS A O     1 
ATOM   857   C CB    . LYS A 1 133  ? -6.030  62.960  65.749  1.00 45.03 ?  131  LYS A CB    1 
ATOM   858   C CG    . LYS A 1 133  ? -5.835  61.576  66.375  1.00 45.62 ?  131  LYS A CG    1 
ATOM   859   C CD    . LYS A 1 133  ? -4.844  61.587  67.540  1.00 42.90 ?  131  LYS A CD    1 
ATOM   860   C CE    . LYS A 1 133  ? -4.751  60.203  68.187  1.00 37.69 ?  131  LYS A CE    1 
ATOM   861   N NZ    . LYS A 1 133  ? -4.109  60.208  69.534  1.00 31.35 ?  131  LYS A NZ    1 
ATOM   862   N N     . SER A 1 134  ? -6.409  64.483  62.956  1.00 57.97 ?  132  SER A N     1 
ATOM   863   C CA    . SER A 1 134  ? -6.315  65.743  62.227  1.00 56.38 ?  132  SER A CA    1 
ATOM   864   C C     . SER A 1 134  ? -7.605  66.101  61.498  1.00 56.23 ?  132  SER A C     1 
ATOM   865   O O     . SER A 1 134  ? -7.772  67.258  61.098  1.00 55.20 ?  132  SER A O     1 
ATOM   866   C CB    . SER A 1 134  ? -5.158  65.684  61.229  1.00 56.76 ?  132  SER A CB    1 
ATOM   867   N N     . HIS A 1 135  ? -8.523  65.147  61.322  1.00 55.05 ?  133  HIS A N     1 
ATOM   868   C CA    . HIS A 1 135  ? -9.703  65.369  60.499  1.00 54.48 ?  133  HIS A CA    1 
ATOM   869   C C     . HIS A 1 135  ? -11.013 65.353  61.271  1.00 55.77 ?  133  HIS A C     1 
ATOM   870   O O     . HIS A 1 135  ? -12.027 65.814  60.737  1.00 54.64 ?  133  HIS A O     1 
ATOM   871   C CB    . HIS A 1 135  ? -9.774  64.319  59.380  1.00 53.04 ?  133  HIS A CB    1 
ATOM   872   C CG    . HIS A 1 135  ? -8.556  64.292  58.510  1.00 55.52 ?  133  HIS A CG    1 
ATOM   873   N ND1   . HIS A 1 135  ? -7.485  63.458  58.752  1.00 54.85 ?  133  HIS A ND1   1 
ATOM   874   C CD2   . HIS A 1 135  ? -8.229  65.014  57.412  1.00 55.41 ?  133  HIS A CD2   1 
ATOM   875   C CE1   . HIS A 1 135  ? -6.556  63.659  57.836  1.00 55.76 ?  133  HIS A CE1   1 
ATOM   876   N NE2   . HIS A 1 135  ? -6.983  64.598  57.010  1.00 58.17 ?  133  HIS A NE2   1 
ATOM   877   N N     . LEU A 1 136  ? -11.021 64.840  62.498  1.00 51.51 ?  134  LEU A N     1 
ATOM   878   C CA    . LEU A 1 136  ? -12.233 64.791  63.301  1.00 51.61 ?  134  LEU A CA    1 
ATOM   879   C C     . LEU A 1 136  ? -11.856 64.945  64.766  1.00 51.72 ?  134  LEU A C     1 
ATOM   880   O O     . LEU A 1 136  ? -10.688 64.829  65.146  1.00 51.14 ?  134  LEU A O     1 
ATOM   881   C CB    . LEU A 1 136  ? -13.009 63.483  63.085  1.00 45.20 ?  134  LEU A CB    1 
ATOM   882   C CG    . LEU A 1 136  ? -13.732 63.254  61.757  1.00 46.30 ?  134  LEU A CG    1 
ATOM   883   C CD1   . LEU A 1 136  ? -14.239 61.830  61.679  1.00 41.06 ?  134  LEU A CD1   1 
ATOM   884   C CD2   . LEU A 1 136  ? -14.875 64.234  61.594  1.00 47.43 ?  134  LEU A CD2   1 
ATOM   885   N N     . GLY A 1 137  ? -12.866 65.206  65.591  1.00 46.93 ?  135  GLY A N     1 
ATOM   886   C CA    . GLY A 1 137  ? -12.655 65.215  67.024  1.00 42.04 ?  135  GLY A CA    1 
ATOM   887   C C     . GLY A 1 137  ? -11.870 66.391  67.557  1.00 44.74 ?  135  GLY A C     1 
ATOM   888   O O     . GLY A 1 137  ? -11.214 66.263  68.596  1.00 45.69 ?  135  GLY A O     1 
ATOM   889   N N     . GLY A 1 138  ? -11.925 67.539  66.883  1.00 43.52 ?  136  GLY A N     1 
ATOM   890   C CA    . GLY A 1 138  ? -11.228 68.725  67.349  1.00 45.39 ?  136  GLY A CA    1 
ATOM   891   C C     . GLY A 1 138  ? -11.866 69.361  68.571  1.00 40.63 ?  136  GLY A C     1 
ATOM   892   O O     . GLY A 1 138  ? -11.498 69.051  69.710  1.00 42.53 ?  136  GLY A O     1 
ATOM   893   N N     . SER A 1 139  ? -12.834 70.255  68.347  1.00 31.46 ?  137  SER A N     1 
ATOM   894   C CA    . SER A 1 139  ? -13.521 70.908  69.458  1.00 25.52 ?  137  SER A CA    1 
ATOM   895   C C     . SER A 1 139  ? -14.332 69.935  70.294  1.00 26.70 ?  137  SER A C     1 
ATOM   896   O O     . SER A 1 139  ? -14.577 70.208  71.474  1.00 29.06 ?  137  SER A O     1 
ATOM   897   C CB    . SER A 1 139  ? -14.446 72.009  68.942  1.00 31.65 ?  137  SER A CB    1 
ATOM   898   O OG    . SER A 1 139  ? -13.704 73.090  68.402  1.00 32.82 ?  137  SER A OG    1 
ATOM   899   N N     . ARG A 1 140  ? -14.762 68.820  69.714  1.00 21.99 ?  138  ARG A N     1 
ATOM   900   C CA    . ARG A 1 140  ? -15.583 67.839  70.413  1.00 21.73 ?  138  ARG A CA    1 
ATOM   901   C C     . ARG A 1 140  ? -14.874 66.498  70.330  1.00 22.58 ?  138  ARG A C     1 
ATOM   902   O O     . ARG A 1 140  ? -14.558 66.034  69.232  1.00 22.12 ?  138  ARG A O     1 
ATOM   903   C CB    . ARG A 1 140  ? -16.984 67.770  69.792  1.00 25.08 ?  138  ARG A CB    1 
ATOM   904   C CG    . ARG A 1 140  ? -17.869 66.613  70.236  1.00 27.21 ?  138  ARG A CG    1 
ATOM   905   C CD    . ARG A 1 140  ? -19.078 66.522  69.320  1.00 30.10 ?  138  ARG A CD    1 
ATOM   906   N NE    . ARG A 1 140  ? -20.035 65.485  69.698  1.00 29.04 ?  138  ARG A NE    1 
ATOM   907   C CZ    . ARG A 1 140  ? -20.001 64.232  69.258  1.00 29.65 ?  138  ARG A CZ    1 
ATOM   908   N NH1   . ARG A 1 140  ? -19.004 63.786  68.506  1.00 28.35 ?  138  ARG A NH1   1 
ATOM   909   N NH2   . ARG A 1 140  ? -20.993 63.405  69.583  1.00 31.22 ?  138  ARG A NH2   1 
ATOM   910   N N     . SER A 1 141  ? -14.591 65.897  71.484  1.00 19.68 ?  139  SER A N     1 
ATOM   911   C CA    . SER A 1 141  ? -13.999 64.568  71.498  1.00 16.68 ?  139  SER A CA    1 
ATOM   912   C C     . SER A 1 141  ? -14.849 63.606  70.681  1.00 16.43 ?  139  SER A C     1 
ATOM   913   O O     . SER A 1 141  ? -16.080 63.662  70.704  1.00 17.34 ?  139  SER A O     1 
ATOM   914   C CB    . SER A 1 141  ? -13.891 64.052  72.936  1.00 17.45 ?  139  SER A CB    1 
ATOM   915   O OG    . SER A 1 141  ? -13.505 62.683  72.976  1.00 15.77 ?  139  SER A OG    1 
ATOM   916   N N     . LEU A 1 142  ? -14.189 62.715  69.946  1.00 15.96 ?  140  LEU A N     1 
ATOM   917   C CA    A LEU A 1 142  ? -14.933 61.648  69.287  0.50 16.22 ?  140  LEU A CA    1 
ATOM   918   C CA    B LEU A 1 142  ? -14.918 61.643  69.288  0.50 16.23 ?  140  LEU A CA    1 
ATOM   919   C C     . LEU A 1 142  ? -15.711 60.802  70.276  1.00 17.21 ?  140  LEU A C     1 
ATOM   920   O O     . LEU A 1 142  ? -16.700 60.173  69.896  1.00 15.89 ?  140  LEU A O     1 
ATOM   921   C CB    A LEU A 1 142  ? -13.996 60.719  68.517  0.50 16.71 ?  140  LEU A CB    1 
ATOM   922   C CB    B LEU A 1 142  ? -13.931 60.749  68.548  0.50 16.71 ?  140  LEU A CB    1 
ATOM   923   C CG    A LEU A 1 142  ? -13.282 61.213  67.271  0.50 20.00 ?  140  LEU A CG    1 
ATOM   924   C CG    B LEU A 1 142  ? -14.237 60.368  67.112  0.50 17.81 ?  140  LEU A CG    1 
ATOM   925   C CD1   A LEU A 1 142  ? -12.713 60.013  66.530  0.50 21.51 ?  140  LEU A CD1   1 
ATOM   926   C CD1   B LEU A 1 142  ? -14.091 61.571  66.205  0.50 22.40 ?  140  LEU A CD1   1 
ATOM   927   C CD2   A LEU A 1 142  ? -14.234 61.983  66.390  0.50 23.06 ?  140  LEU A CD2   1 
ATOM   928   C CD2   B LEU A 1 142  ? -13.290 59.266  66.710  0.50 18.38 ?  140  LEU A CD2   1 
ATOM   929   N N     . PHE A 1 143  ? -15.286 60.774  71.530  1.00 13.29 ?  141  PHE A N     1 
ATOM   930   C CA    . PHE A 1 143  ? -15.739 59.772  72.476  1.00 14.12 ?  141  PHE A CA    1 
ATOM   931   C C     . PHE A 1 143  ? -16.730 60.315  73.503  1.00 14.72 ?  141  PHE A C     1 
ATOM   932   O O     . PHE A 1 143  ? -16.926 59.689  74.542  1.00 15.41 ?  141  PHE A O     1 
ATOM   933   C CB    . PHE A 1 143  ? -14.500 59.170  73.146  1.00 13.15 ?  141  PHE A CB    1 
ATOM   934   C CG    . PHE A 1 143  ? -13.459 58.722  72.153  1.00 12.83 ?  141  PHE A CG    1 
ATOM   935   C CD1   . PHE A 1 143  ? -13.752 57.698  71.256  1.00 13.11 ?  141  PHE A CD1   1 
ATOM   936   C CD2   . PHE A 1 143  ? -12.209 59.345  72.078  1.00 13.72 ?  141  PHE A CD2   1 
ATOM   937   C CE1   . PHE A 1 143  ? -12.818 57.276  70.318  1.00 13.51 ?  141  PHE A CE1   1 
ATOM   938   C CE2   . PHE A 1 143  ? -11.278 58.930  71.141  1.00 13.46 ?  141  PHE A CE2   1 
ATOM   939   C CZ    . PHE A 1 143  ? -11.578 57.904  70.252  1.00 12.63 ?  141  PHE A CZ    1 
ATOM   940   N N     . VAL A 1 144  ? -17.398 61.434  73.196  1.00 14.40 ?  142  VAL A N     1 
ATOM   941   C CA    A VAL A 1 144  ? -18.343 62.060  74.123  0.50 15.84 ?  142  VAL A CA    1 
ATOM   942   C CA    B VAL A 1 144  ? -18.302 62.042  74.167  0.50 15.85 ?  142  VAL A CA    1 
ATOM   943   C C     . VAL A 1 144  ? -19.405 61.071  74.584  1.00 16.67 ?  142  VAL A C     1 
ATOM   944   O O     . VAL A 1 144  ? -19.823 61.068  75.748  1.00 16.39 ?  142  VAL A O     1 
ATOM   945   C CB    A VAL A 1 144  ? -18.987 63.295  73.462  0.50 15.77 ?  142  VAL A CB    1 
ATOM   946   C CB    B VAL A 1 144  ? -18.884 63.356  73.615  0.50 15.89 ?  142  VAL A CB    1 
ATOM   947   C CG1   A VAL A 1 144  ? -20.215 63.759  74.243  0.50 16.91 ?  142  VAL A CG1   1 
ATOM   948   C CG1   B VAL A 1 144  ? -17.791 64.397  73.453  0.50 17.56 ?  142  VAL A CG1   1 
ATOM   949   C CG2   A VAL A 1 144  ? -17.977 64.422  73.346  0.50 17.50 ?  142  VAL A CG2   1 
ATOM   950   C CG2   B VAL A 1 144  ? -19.561 63.106  72.316  0.50 18.33 ?  142  VAL A CG2   1 
ATOM   951   N N     . ASN A 1 145  ? -19.885 60.227  73.668  1.00 15.59 ?  143  ASN A N     1 
ATOM   952   C CA    . ASN A 1 145  ? -20.951 59.288  74.001  1.00 14.85 ?  143  ASN A CA    1 
ATOM   953   C C     . ASN A 1 145  ? -20.445 57.866  74.201  1.00 15.34 ?  143  ASN A C     1 
ATOM   954   O O     . ASN A 1 145  ? -21.221 56.908  74.073  1.00 15.03 ?  143  ASN A O     1 
ATOM   955   C CB    . ASN A 1 145  ? -22.031 59.317  72.922  1.00 14.47 ?  143  ASN A CB    1 
ATOM   956   C CG    . ASN A 1 145  ? -22.820 60.598  72.950  1.00 18.87 ?  143  ASN A CG    1 
ATOM   957   O OD1   . ASN A 1 145  ? -23.309 61.008  74.006  1.00 19.88 ?  143  ASN A OD1   1 
ATOM   958   N ND2   . ASN A 1 145  ? -22.936 61.248  71.811  1.00 19.93 ?  143  ASN A ND2   1 
ATOM   959   N N     . ALA A 1 146  ? -19.159 57.705  74.532  1.00 13.77 ?  144  ALA A N     1 
ATOM   960   C CA    . ALA A 1 146  ? -18.622 56.360  74.661  1.00 14.45 ?  144  ALA A CA    1 
ATOM   961   C C     . ALA A 1 146  ? -19.233 55.569  75.816  1.00 14.49 ?  144  ALA A C     1 
ATOM   962   O O     . ALA A 1 146  ? -19.194 54.339  75.772  1.00 15.69 ?  144  ALA A O     1 
ATOM   963   C CB    . ALA A 1 146  ? -17.090 56.411  74.813  1.00 14.76 ?  144  ALA A CB    1 
ATOM   964   N N     . ALA A 1 147  ? -19.813 56.217  76.839  1.00 13.02 ?  145  ALA A N     1 
ATOM   965   C CA    . ALA A 1 147  ? -20.475 55.424  77.872  1.00 17.02 ?  145  ALA A CA    1 
ATOM   966   C C     . ALA A 1 147  ? -21.680 54.705  77.290  1.00 16.82 ?  145  ALA A C     1 
ATOM   967   O O     . ALA A 1 147  ? -21.971 53.561  77.654  1.00 18.12 ?  145  ALA A O     1 
ATOM   968   C CB    . ALA A 1 147  ? -20.889 56.299  79.065  1.00 17.72 ?  145  ALA A CB    1 
ATOM   969   N N     . THR A 1 148  ? -22.371 55.352  76.356  1.00 14.64 ?  146  THR A N     1 
ATOM   970   C CA    . THR A 1 148  ? -23.503 54.718  75.693  1.00 15.01 ?  146  THR A CA    1 
ATOM   971   C C     . THR A 1 148  ? -23.041 53.571  74.808  1.00 13.65 ?  146  THR A C     1 
ATOM   972   O O     . THR A 1 148  ? -23.558 52.451  74.896  1.00 15.68 ?  146  THR A O     1 
ATOM   973   C CB    . THR A 1 148  ? -24.260 55.770  74.891  1.00 18.57 ?  146  THR A CB    1 
ATOM   974   O OG1   . THR A 1 148  ? -24.626 56.832  75.774  1.00 18.78 ?  146  THR A OG1   1 
ATOM   975   C CG2   . THR A 1 148  ? -25.514 55.180  74.262  1.00 21.86 ?  146  THR A CG2   1 
ATOM   976   N N     . TRP A 1 149  ? -22.041 53.822  73.960  1.00 14.38 ?  147  TRP A N     1 
ATOM   977   C CA    . TRP A 1 149  ? -21.555 52.741  73.106  1.00 15.73 ?  147  TRP A CA    1 
ATOM   978   C C     . TRP A 1 149  ? -20.903 51.635  73.922  1.00 13.56 ?  147  TRP A C     1 
ATOM   979   O O     . TRP A 1 149  ? -20.929 50.478  73.511  1.00 14.95 ?  147  TRP A O     1 
ATOM   980   C CB    . TRP A 1 149  ? -20.578 53.279  72.057  1.00 13.93 ?  147  TRP A CB    1 
ATOM   981   C CG    . TRP A 1 149  ? -21.245 54.189  71.064  1.00 14.28 ?  147  TRP A CG    1 
ATOM   982   C CD1   . TRP A 1 149  ? -21.026 55.523  70.903  1.00 15.70 ?  147  TRP A CD1   1 
ATOM   983   C CD2   . TRP A 1 149  ? -22.253 53.823  70.114  1.00 14.58 ?  147  TRP A CD2   1 
ATOM   984   N NE1   . TRP A 1 149  ? -21.832 56.018  69.893  1.00 15.96 ?  147  TRP A NE1   1 
ATOM   985   C CE2   . TRP A 1 149  ? -22.591 54.990  69.395  1.00 16.11 ?  147  TRP A CE2   1 
ATOM   986   C CE3   . TRP A 1 149  ? -22.898 52.623  69.802  1.00 15.62 ?  147  TRP A CE3   1 
ATOM   987   C CZ2   . TRP A 1 149  ? -23.556 54.994  68.382  1.00 15.36 ?  147  TRP A CZ2   1 
ATOM   988   C CZ3   . TRP A 1 149  ? -23.850 52.618  68.776  1.00 20.57 ?  147  TRP A CZ3   1 
ATOM   989   C CH2   . TRP A 1 149  ? -24.173 53.805  68.087  1.00 21.81 ?  147  TRP A CH2   1 
ATOM   990   N N     . GLY A 1 150  ? -20.325 51.971  75.078  1.00 14.08 ?  148  GLY A N     1 
ATOM   991   C CA    . GLY A 1 150  ? -19.842 50.934  75.974  1.00 15.18 ?  148  GLY A CA    1 
ATOM   992   C C     . GLY A 1 150  ? -20.949 49.993  76.414  1.00 15.74 ?  148  GLY A C     1 
ATOM   993   O O     . GLY A 1 150  ? -20.749 48.779  76.485  1.00 16.91 ?  148  GLY A O     1 
ATOM   994   N N     . LEU A 1 151  ? -22.136 50.540  76.716  1.00 17.39 ?  149  LEU A N     1 
ATOM   995   C CA    . LEU A 1 151  ? -23.272 49.674  77.038  1.00 19.35 ?  149  LEU A CA    1 
ATOM   996   C C     . LEU A 1 151  ? -23.652 48.796  75.854  1.00 17.78 ?  149  LEU A C     1 
ATOM   997   O O     . LEU A 1 151  ? -23.945 47.604  76.020  1.00 21.58 ?  149  LEU A O     1 
ATOM   998   C CB    . LEU A 1 151  ? -24.475 50.516  77.462  1.00 19.48 ?  149  LEU A CB    1 
ATOM   999   C CG    . LEU A 1 151  ? -24.621 50.767  78.954  1.00 24.20 ?  149  LEU A CG    1 
ATOM   1000  C CD1   . LEU A 1 151  ? -25.739 51.759  79.203  1.00 24.54 ?  149  LEU A CD1   1 
ATOM   1001  C CD2   . LEU A 1 151  ? -24.893 49.464  79.697  1.00 20.37 ?  149  LEU A CD2   1 
ATOM   1002  N N     . VAL A 1 152  ? -23.672 49.372  74.650  1.00 17.36 ?  150  VAL A N     1 
ATOM   1003  C CA    . VAL A 1 152  ? -24.042 48.609  73.457  1.00 18.95 ?  150  VAL A CA    1 
ATOM   1004  C C     . VAL A 1 152  ? -23.060 47.473  73.208  1.00 21.74 ?  150  VAL A C     1 
ATOM   1005  O O     . VAL A 1 152  ? -23.459 46.351  72.877  1.00 22.17 ?  150  VAL A O     1 
ATOM   1006  C CB    . VAL A 1 152  ? -24.135 49.544  72.237  1.00 21.13 ?  150  VAL A CB    1 
ATOM   1007  C CG1   . VAL A 1 152  ? -24.321 48.750  70.956  1.00 23.12 ?  150  VAL A CG1   1 
ATOM   1008  C CG2   . VAL A 1 152  ? -25.257 50.544  72.426  1.00 23.82 ?  150  VAL A CG2   1 
ATOM   1009  N N     . VAL A 1 153  ? -21.762 47.743  73.357  1.00 18.25 ?  151  VAL A N     1 
ATOM   1010  C CA    . VAL A 1 153  ? -20.737 46.768  72.997  1.00 20.05 ?  151  VAL A CA    1 
ATOM   1011  C C     . VAL A 1 153  ? -20.536 45.732  74.097  1.00 18.81 ?  151  VAL A C     1 
ATOM   1012  O O     . VAL A 1 153  ? -20.420 44.530  73.814  1.00 22.98 ?  151  VAL A O     1 
ATOM   1013  C CB    . VAL A 1 153  ? -19.423 47.506  72.676  1.00 17.18 ?  151  VAL A CB    1 
ATOM   1014  C CG1   . VAL A 1 153  ? -18.262 46.519  72.536  1.00 20.17 ?  151  VAL A CG1   1 
ATOM   1015  C CG2   . VAL A 1 153  ? -19.575 48.342  71.418  1.00 18.08 ?  151  VAL A CG2   1 
ATOM   1016  N N     . THR A 1 154  ? -20.487 46.171  75.362  1.00 18.17 ?  152  THR A N     1 
ATOM   1017  C CA    . THR A 1 154  ? -20.082 45.307  76.465  1.00 21.19 ?  152  THR A CA    1 
ATOM   1018  C C     . THR A 1 154  ? -21.212 44.929  77.403  1.00 21.78 ?  152  THR A C     1 
ATOM   1019  O O     . THR A 1 154  ? -21.033 44.013  78.213  1.00 23.69 ?  152  THR A O     1 
ATOM   1020  C CB    . THR A 1 154  ? -18.982 45.969  77.314  1.00 21.53 ?  152  THR A CB    1 
ATOM   1021  O OG1   . THR A 1 154  ? -19.548 47.004  78.135  1.00 21.48 ?  152  THR A OG1   1 
ATOM   1022  C CG2   . THR A 1 154  ? -17.898 46.576  76.438  1.00 24.13 ?  152  THR A CG2   1 
ATOM   1023  N N     . GLY A 1 155  ? -22.341 45.627  77.344  1.00 19.57 ?  153  GLY A N     1 
ATOM   1024  C CA    . GLY A 1 155  ? -23.394 45.449  78.325  1.00 19.50 ?  153  GLY A CA    1 
ATOM   1025  C C     . GLY A 1 155  ? -23.106 46.057  79.678  1.00 23.84 ?  153  GLY A C     1 
ATOM   1026  O O     . GLY A 1 155  ? -23.947 45.944  80.581  1.00 23.88 ?  153  GLY A O     1 
ATOM   1027  N N     . LYS A 1 156  ? -21.956 46.697  79.852  1.00 20.53 ?  154  LYS A N     1 
ATOM   1028  C CA    . LYS A 1 156  ? -21.574 47.288  81.124  1.00 22.19 ?  154  LYS A CA    1 
ATOM   1029  C C     . LYS A 1 156  ? -21.532 48.803  80.997  1.00 21.14 ?  154  LYS A C     1 
ATOM   1030  O O     . LYS A 1 156  ? -21.112 49.343  79.967  1.00 19.04 ?  154  LYS A O     1 
ATOM   1031  C CB    . LYS A 1 156  ? -20.215 46.762  81.595  1.00 27.79 ?  154  LYS A CB    1 
ATOM   1032  N N     . LEU A 1 157  ? -21.974 49.483  82.050  1.00 18.92 ?  155  LEU A N     1 
ATOM   1033  C CA    . LEU A 1 157  ? -21.952 50.934  82.118  1.00 18.59 ?  155  LEU A CA    1 
ATOM   1034  C C     . LEU A 1 157  ? -20.696 51.386  82.852  1.00 18.30 ?  155  LEU A C     1 
ATOM   1035  O O     . LEU A 1 157  ? -20.441 50.959  83.986  1.00 23.79 ?  155  LEU A O     1 
ATOM   1036  C CB    . LEU A 1 157  ? -23.200 51.457  82.823  1.00 19.63 ?  155  LEU A CB    1 
ATOM   1037  C CG    . LEU A 1 157  ? -23.247 52.965  83.025  1.00 18.81 ?  155  LEU A CG    1 
ATOM   1038  C CD1   . LEU A 1 157  ? -23.218 53.721  81.697  1.00 19.99 ?  155  LEU A CD1   1 
ATOM   1039  C CD2   . LEU A 1 157  ? -24.484 53.315  83.830  1.00 20.46 ?  155  LEU A CD2   1 
ATOM   1040  N N     . THR A 1 158  ? -19.903 52.224  82.190  1.00 20.35 ?  156  THR A N     1 
ATOM   1041  C CA    . THR A 1 158  ? -18.783 52.939  82.789  1.00 22.71 ?  156  THR A CA    1 
ATOM   1042  C C     . THR A 1 158  ? -19.093 54.429  82.695  1.00 23.38 ?  156  THR A C     1 
ATOM   1043  O O     . THR A 1 158  ? -19.226 54.958  81.587  1.00 23.18 ?  156  THR A O     1 
ATOM   1044  C CB    . THR A 1 158  ? -17.476 52.588  82.064  1.00 24.31 ?  156  THR A CB    1 
ATOM   1045  O OG1   . THR A 1 158  ? -17.294 51.161  82.070  1.00 26.36 ?  156  THR A OG1   1 
ATOM   1046  C CG2   . THR A 1 158  ? -16.286 53.254  82.736  1.00 24.76 ?  156  THR A CG2   1 
ATOM   1047  N N     . SER A 1 159  ? -19.210 55.101  83.855  1.00 21.19 ?  157  SER A N     1 
ATOM   1048  C CA    . SER A 1 159  ? -19.788 56.446  83.921  1.00 18.91 ?  157  SER A CA    1 
ATOM   1049  C C     . SER A 1 159  ? -18.956 57.505  83.199  1.00 22.50 ?  157  SER A C     1 
ATOM   1050  O O     . SER A 1 159  ? -19.520 58.462  82.663  1.00 22.06 ?  157  SER A O     1 
ATOM   1051  C CB    . SER A 1 159  ? -19.987 56.864  85.377  1.00 25.60 ?  157  SER A CB    1 
ATOM   1052  O OG    . SER A 1 159  ? -18.755 56.887  86.074  1.00 24.29 ?  157  SER A OG    1 
ATOM   1053  N N     . THR A 1 160  ? -17.633 57.398  83.214  1.00 20.07 ?  158  THR A N     1 
ATOM   1054  C CA    . THR A 1 160  ? -16.798 58.339  82.481  1.00 18.84 ?  158  THR A CA    1 
ATOM   1055  C C     . THR A 1 160  ? -16.016 57.576  81.421  1.00 17.27 ?  158  THR A C     1 
ATOM   1056  O O     . THR A 1 160  ? -15.919 56.349  81.448  1.00 18.09 ?  158  THR A O     1 
ATOM   1057  C CB    . THR A 1 160  ? -15.857 59.114  83.417  1.00 19.44 ?  158  THR A CB    1 
ATOM   1058  O OG1   . THR A 1 160  ? -14.986 58.196  84.081  1.00 21.94 ?  158  THR A OG1   1 
ATOM   1059  C CG2   . THR A 1 160  ? -16.646 59.884  84.449  1.00 24.15 ?  158  THR A CG2   1 
ATOM   1060  N N     . VAL A 1 161  ? -15.446 58.337  80.494  1.00 13.40 ?  159  VAL A N     1 
ATOM   1061  C CA    . VAL A 1 161  ? -14.883 57.819  79.249  1.00 14.10 ?  159  VAL A CA    1 
ATOM   1062  C C     . VAL A 1 161  ? -13.363 57.844  79.357  1.00 12.76 ?  159  VAL A C     1 
ATOM   1063  O O     . VAL A 1 161  ? -12.772 58.908  79.571  1.00 12.15 ?  159  VAL A O     1 
ATOM   1064  C CB    . VAL A 1 161  ? -15.352 58.670  78.059  1.00 15.96 ?  159  VAL A CB    1 
ATOM   1065  C CG1   . VAL A 1 161  ? -14.651 58.269  76.785  1.00 16.85 ?  159  VAL A CG1   1 
ATOM   1066  C CG2   . VAL A 1 161  ? -16.882 58.612  77.908  1.00 18.49 ?  159  VAL A CG2   1 
ATOM   1067  N N     . ASN A 1 162  ? -12.711 56.692  79.166  1.00 12.38 ?  160  ASN A N     1 
ATOM   1068  C CA    . ASN A 1 162  ? -11.247 56.722  79.101  1.00 11.98 ?  160  ASN A CA    1 
ATOM   1069  C C     . ASN A 1 162  ? -10.870 57.069  77.671  1.00 11.79 ?  160  ASN A C     1 
ATOM   1070  O O     . ASN A 1 162  ? -10.666 56.191  76.820  1.00 11.57 ?  160  ASN A O     1 
ATOM   1071  C CB    . ASN A 1 162  ? -10.626 55.403  79.533  1.00 14.11 ?  160  ASN A CB    1 
ATOM   1072  C CG    . ASN A 1 162  ? -9.096  55.474  79.576  1.00 14.20 ?  160  ASN A CG    1 
ATOM   1073  O OD1   . ASN A 1 162  ? -8.490  56.296  78.897  1.00 13.32 ?  160  ASN A OD1   1 
ATOM   1074  N ND2   . ASN A 1 162  ? -8.481  54.623  80.384  1.00 16.91 ?  160  ASN A ND2   1 
ATOM   1075  N N     . ASP A 1 163  ? -10.787 58.376  77.392  1.00 10.95 ?  161  ASP A N     1 
ATOM   1076  C CA    . ASP A 1 163  ? -10.600 58.806  76.019  1.00 11.47 ?  161  ASP A CA    1 
ATOM   1077  C C     . ASP A 1 163  ? -9.190  58.545  75.509  1.00 10.48 ?  161  ASP A C     1 
ATOM   1078  O O     . ASP A 1 163  ? -8.999  58.440  74.296  1.00 12.39 ?  161  ASP A O     1 
ATOM   1079  C CB    . ASP A 1 163  ? -10.986 60.291  75.834  1.00 13.40 ?  161  ASP A CB    1 
ATOM   1080  C CG    . ASP A 1 163  ? -10.394 61.243  76.890  1.00 15.64 ?  161  ASP A CG    1 
ATOM   1081  O OD1   . ASP A 1 163  ? -10.230 60.865  78.086  1.00 13.28 ?  161  ASP A OD1   1 
ATOM   1082  O OD2   . ASP A 1 163  ? -10.136 62.414  76.487  1.00 15.68 ?  161  ASP A OD2   1 
ATOM   1083  N N     . ARG A 1 164  ? -8.209  58.373  76.399  1.00 11.65 ?  162  ARG A N     1 
ATOM   1084  C CA    . ARG A 1 164  ? -6.882  58.008  75.912  1.00 9.93  ?  162  ARG A CA    1 
ATOM   1085  C C     . ARG A 1 164  ? -6.831  56.545  75.494  1.00 11.21 ?  162  ARG A C     1 
ATOM   1086  O O     . ARG A 1 164  ? -6.191  56.201  74.488  1.00 12.03 ?  162  ARG A O     1 
ATOM   1087  C CB    . ARG A 1 164  ? -5.830  58.298  76.986  1.00 12.35 ?  162  ARG A CB    1 
ATOM   1088  C CG    . ARG A 1 164  ? -5.669  59.782  77.320  1.00 14.51 ?  162  ARG A CG    1 
ATOM   1089  C CD    . ARG A 1 164  ? -5.616  60.695  76.083  1.00 24.70 ?  162  ARG A CD    1 
ATOM   1090  N NE    . ARG A 1 164  ? -4.757  60.244  74.993  1.00 24.27 ?  162  ARG A NE    1 
ATOM   1091  C CZ    . ARG A 1 164  ? -4.966  60.530  73.711  1.00 26.61 ?  162  ARG A CZ    1 
ATOM   1092  N NH1   . ARG A 1 164  ? -6.011  61.246  73.321  1.00 31.77 ?  162  ARG A NH1   1 
ATOM   1093  N NH2   . ARG A 1 164  ? -4.118  60.075  72.797  1.00 22.62 ?  162  ARG A NH2   1 
ATOM   1094  N N     . SER A 1 165  ? -7.511  55.674  76.251  1.00 10.86 ?  163  SER A N     1 
ATOM   1095  C CA    . SER A 1 165  ? -7.623  54.272  75.858  1.00 11.17 ?  163  SER A CA    1 
ATOM   1096  C C     . SER A 1 165  ? -8.369  54.126  74.539  1.00 9.75  ?  163  SER A C     1 
ATOM   1097  O O     . SER A 1 165  ? -7.978  53.330  73.678  1.00 10.07 ?  163  SER A O     1 
ATOM   1098  C CB    . SER A 1 165  ? -8.347  53.485  76.956  1.00 11.07 ?  163  SER A CB    1 
ATOM   1099  O OG    . SER A 1 165  ? -8.632  52.166  76.543  1.00 12.53 ?  163  SER A OG    1 
ATOM   1100  N N     . LEU A 1 166  ? -9.466  54.876  74.376  1.00 12.06 ?  164  LEU A N     1 
ATOM   1101  C CA    . LEU A 1 166  ? -10.219 54.786  73.134  1.00 10.46 ?  164  LEU A CA    1 
ATOM   1102  C C     . LEU A 1 166  ? -9.435  55.350  71.948  1.00 10.02 ?  164  LEU A C     1 
ATOM   1103  O O     . LEU A 1 166  ? -9.525  54.817  70.843  1.00 10.26 ?  164  LEU A O     1 
ATOM   1104  C CB    . LEU A 1 166  ? -11.565 55.497  73.294  1.00 10.40 ?  164  LEU A CB    1 
ATOM   1105  C CG    . LEU A 1 166  ? -12.466 54.773  74.288  1.00 11.04 ?  164  LEU A CG    1 
ATOM   1106  C CD1   . LEU A 1 166  ? -13.607 55.670  74.648  1.00 12.82 ?  164  LEU A CD1   1 
ATOM   1107  C CD2   . LEU A 1 166  ? -12.975 53.477  73.682  1.00 11.83 ?  164  LEU A CD2   1 
ATOM   1108  N N     . ALA A 1 167  ? -8.667  56.429  72.164  1.00 10.16 ?  165  ALA A N     1 
ATOM   1109  C CA    . ALA A 1 167  ? -7.868  56.955  71.062  1.00 11.56 ?  165  ALA A CA    1 
ATOM   1110  C C     . ALA A 1 167  ? -6.817  55.944  70.634  1.00 11.88 ?  165  ALA A C     1 
ATOM   1111  O O     . ALA A 1 167  ? -6.579  55.756  69.441  1.00 12.90 ?  165  ALA A O     1 
ATOM   1112  C CB    . ALA A 1 167  ? -7.217  58.277  71.456  1.00 12.40 ?  165  ALA A CB    1 
ATOM   1113  N N     . ALA A 1 168  ? -6.148  55.312  71.604  1.00 11.00 ?  166  ALA A N     1 
ATOM   1114  C CA    . ALA A 1 168  ? -5.172  54.280  71.266  1.00 11.70 ?  166  ALA A CA    1 
ATOM   1115  C C     . ALA A 1 168  ? -5.832  53.122  70.527  1.00 11.29 ?  166  ALA A C     1 
ATOM   1116  O O     . ALA A 1 168  ? -5.298  52.613  69.529  1.00 11.88 ?  166  ALA A O     1 
ATOM   1117  C CB    . ALA A 1 168  ? -4.503  53.801  72.553  1.00 11.05 ?  166  ALA A CB    1 
ATOM   1118  N N     . ALA A 1 169  ? -7.013  52.710  70.992  1.00 10.91 ?  167  ALA A N     1 
ATOM   1119  C CA    . ALA A 1 169  ? -7.713  51.602  70.355  1.00 11.10 ?  167  ALA A CA    1 
ATOM   1120  C C     . ALA A 1 169  ? -8.138  51.943  68.932  1.00 11.33 ?  167  ALA A C     1 
ATOM   1121  O O     . ALA A 1 169  ? -8.099  51.085  68.047  1.00 12.01 ?  167  ALA A O     1 
ATOM   1122  C CB    . ALA A 1 169  ? -8.932  51.209  71.193  1.00 11.14 ?  167  ALA A CB    1 
ATOM   1123  N N     . LEU A 1 170  ? -8.576  53.180  68.701  1.00 11.12 ?  168  LEU A N     1 
ATOM   1124  C CA    . LEU A 1 170  ? -9.014  53.554  67.360  1.00 11.35 ?  168  LEU A CA    1 
ATOM   1125  C C     . LEU A 1 170  ? -7.839  53.612  66.398  1.00 12.51 ?  168  LEU A C     1 
ATOM   1126  O O     . LEU A 1 170  ? -7.935  53.124  65.264  1.00 13.38 ?  168  LEU A O     1 
ATOM   1127  C CB    . LEU A 1 170  ? -9.743  54.897  67.431  1.00 11.45 ?  168  LEU A CB    1 
ATOM   1128  C CG    . LEU A 1 170  ? -10.336 55.365  66.105  1.00 12.92 ?  168  LEU A CG    1 
ATOM   1129  C CD1   . LEU A 1 170  ? -11.328 54.340  65.615  1.00 13.58 ?  168  LEU A CD1   1 
ATOM   1130  C CD2   . LEU A 1 170  ? -11.007 56.700  66.287  1.00 14.97 ?  168  LEU A CD2   1 
ATOM   1131  N N     . THR A 1 171  ? -6.716  54.190  66.844  1.00 12.84 ?  169  THR A N     1 
ATOM   1132  C CA    . THR A 1 171  ? -5.500  54.170  66.032  1.00 13.32 ?  169  THR A CA    1 
ATOM   1133  C C     . THR A 1 171  ? -5.088  52.742  65.712  1.00 14.35 ?  169  THR A C     1 
ATOM   1134  O O     . THR A 1 171  ? -4.750  52.412  64.569  1.00 13.79 ?  169  THR A O     1 
ATOM   1135  C CB    . THR A 1 171  ? -4.370  54.879  66.761  1.00 14.24 ?  169  THR A CB    1 
ATOM   1136  O OG1   . THR A 1 171  ? -4.721  56.259  66.946  1.00 17.39 ?  169  THR A OG1   1 
ATOM   1137  C CG2   . THR A 1 171  ? -3.046  54.741  65.991  1.00 14.07 ?  169  THR A CG2   1 
ATOM   1138  N N     . ARG A 1 172  ? -5.122  51.877  66.725  1.00 12.37 ?  170  ARG A N     1 
ATOM   1139  C CA    . ARG A 1 172  ? -4.711  50.494  66.512  1.00 12.99 ?  170  ARG A CA    1 
ATOM   1140  C C     . ARG A 1 172  ? -5.617  49.789  65.507  1.00 13.04 ?  170  ARG A C     1 
ATOM   1141  O O     . ARG A 1 172  ? -5.128  49.127  64.576  1.00 13.55 ?  170  ARG A O     1 
ATOM   1142  C CB    . ARG A 1 172  ? -4.699  49.755  67.851  1.00 12.49 ?  170  ARG A CB    1 
ATOM   1143  C CG    . ARG A 1 172  ? -3.982  48.407  67.796  1.00 12.91 ?  170  ARG A CG    1 
ATOM   1144  C CD    . ARG A 1 172  ? -4.196  47.608  69.098  1.00 13.00 ?  170  ARG A CD    1 
ATOM   1145  N NE    . ARG A 1 172  ? -3.932  48.397  70.293  1.00 12.26 ?  170  ARG A NE    1 
ATOM   1146  C CZ    . ARG A 1 172  ? -4.865  48.850  71.128  1.00 11.95 ?  170  ARG A CZ    1 
ATOM   1147  N NH1   . ARG A 1 172  ? -6.152  48.589  70.938  1.00 12.69 ?  170  ARG A NH1   1 
ATOM   1148  N NH2   . ARG A 1 172  ? -4.496  49.558  72.192  1.00 13.12 ?  170  ARG A NH2   1 
ATOM   1149  N N     . LEU A 1 173  ? -6.949  49.934  65.655  1.00 13.07 ?  171  LEU A N     1 
ATOM   1150  C CA    . LEU A 1 173  ? -7.824  49.173  64.774  1.00 13.33 ?  171  LEU A CA    1 
ATOM   1151  C C     . LEU A 1 173  ? -7.789  49.718  63.350  1.00 13.43 ?  171  LEU A C     1 
ATOM   1152  O O     . LEU A 1 173  ? -7.844  48.945  62.392  1.00 14.64 ?  171  LEU A O     1 
ATOM   1153  C CB    . LEU A 1 173  ? -9.265  49.149  65.313  1.00 14.52 ?  171  LEU A CB    1 
ATOM   1154  C CG    . LEU A 1 173  ? -10.131 50.405  65.272  1.00 13.05 ?  171  LEU A CG    1 
ATOM   1155  C CD1   . LEU A 1 173  ? -10.938 50.473  63.974  1.00 17.40 ?  171  LEU A CD1   1 
ATOM   1156  C CD2   . LEU A 1 173  ? -11.096 50.413  66.432  1.00 15.45 ?  171  LEU A CD2   1 
ATOM   1157  N N     . ILE A 1 174  ? -7.650  51.036  63.189  1.00 13.22 ?  172  ILE A N     1 
ATOM   1158  C CA    . ILE A 1 174  ? -7.583  51.584  61.834  1.00 14.41 ?  172  ILE A CA    1 
ATOM   1159  C C     . ILE A 1 174  ? -6.272  51.182  61.165  1.00 15.36 ?  172  ILE A C     1 
ATOM   1160  O O     . ILE A 1 174  ? -6.255  50.798  59.987  1.00 16.60 ?  172  ILE A O     1 
ATOM   1161  C CB    . ILE A 1 174  ? -7.766  53.111  61.864  1.00 13.27 ?  172  ILE A CB    1 
ATOM   1162  C CG1   . ILE A 1 174  ? -9.204  53.475  62.231  1.00 16.25 ?  172  ILE A CG1   1 
ATOM   1163  C CG2   . ILE A 1 174  ? -7.405  53.712  60.472  1.00 16.27 ?  172  ILE A CG2   1 
ATOM   1164  C CD1   . ILE A 1 174  ? -9.378  54.958  62.472  1.00 17.21 ?  172  ILE A CD1   1 
ATOM   1165  N N     . SER A 1 175  ? -5.156  51.251  61.904  1.00 14.78 ?  173  SER A N     1 
ATOM   1166  C CA    . SER A 1 175  ? -3.873  50.870  61.319  1.00 14.49 ?  173  SER A CA    1 
ATOM   1167  C C     . SER A 1 175  ? -3.810  49.391  61.014  1.00 14.92 ?  173  SER A C     1 
ATOM   1168  O O     . SER A 1 175  ? -3.067  48.990  60.107  1.00 18.20 ?  173  SER A O     1 
ATOM   1169  C CB    . SER A 1 175  ? -2.735  51.240  62.254  1.00 17.41 ?  173  SER A CB    1 
ATOM   1170  O OG    . SER A 1 175  ? -2.617  52.642  62.365  1.00 22.63 ?  173  SER A OG    1 
ATOM   1171  N N     . ARG A 1 176  ? -4.597  48.578  61.721  1.00 15.40 ?  174  ARG A N     1 
ATOM   1172  C CA    . ARG A 1 176  ? -4.607  47.142  61.481  1.00 15.15 ?  174  ARG A CA    1 
ATOM   1173  C C     . ARG A 1 176  ? -5.540  46.767  60.336  1.00 18.86 ?  174  ARG A C     1 
ATOM   1174  O O     . ARG A 1 176  ? -5.170  45.958  59.484  1.00 20.22 ?  174  ARG A O     1 
ATOM   1175  C CB    . ARG A 1 176  ? -5.013  46.422  62.785  1.00 17.01 ?  174  ARG A CB    1 
ATOM   1176  C CG    . ARG A 1 176  ? -4.855  44.891  62.730  1.00 18.60 ?  174  ARG A CG    1 
ATOM   1177  C CD    . ARG A 1 176  ? -5.096  44.298  64.114  1.00 19.14 ?  174  ARG A CD    1 
ATOM   1178  N NE    . ARG A 1 176  ? -6.511  44.298  64.458  1.00 17.30 ?  174  ARG A NE    1 
ATOM   1179  C CZ    . ARG A 1 176  ? -7.086  44.966  65.457  1.00 17.48 ?  174  ARG A CZ    1 
ATOM   1180  N NH1   . ARG A 1 176  ? -6.387  45.714  66.321  1.00 15.57 ?  174  ARG A NH1   1 
ATOM   1181  N NH2   . ARG A 1 176  ? -8.407  44.886  65.601  1.00 21.77 ?  174  ARG A NH2   1 
ATOM   1182  N N     . CYS A 1 177  ? -6.746  47.351  60.300  1.00 17.53 ?  175  CYS A N     1 
ATOM   1183  C CA    . CYS A 1 177  ? -7.814  46.879  59.435  1.00 20.82 ?  175  CYS A CA    1 
ATOM   1184  C C     . CYS A 1 177  ? -8.254  47.867  58.370  1.00 20.04 ?  175  CYS A C     1 
ATOM   1185  O O     . CYS A 1 177  ? -8.924  47.450  57.419  1.00 22.51 ?  175  CYS A O     1 
ATOM   1186  C CB    . CYS A 1 177  ? -9.040  46.491  60.273  1.00 20.76 ?  175  CYS A CB    1 
ATOM   1187  S SG    . CYS A 1 177  ? -8.663  45.211  61.527  1.00 24.54 ?  175  CYS A SG    1 
ATOM   1188  N N     . GLY A 1 178  ? -7.961  49.155  58.522  1.00 20.43 ?  176  GLY A N     1 
ATOM   1189  C CA    . GLY A 1 178  ? -8.181  50.073  57.410  1.00 20.31 ?  176  GLY A CA    1 
ATOM   1190  C C     . GLY A 1 178  ? -9.634  50.429  57.117  1.00 19.72 ?  176  GLY A C     1 
ATOM   1191  O O     . GLY A 1 178  ? -10.536 50.282  57.937  1.00 19.28 ?  176  GLY A O     1 
ATOM   1192  N N     . GLU A 1 179  ? -9.831  50.940  55.906  1.00 20.13 ?  177  GLU A N     1 
ATOM   1193  C CA    . GLU A 1 179  ? -11.155 51.366  55.462  1.00 19.23 ?  177  GLU A CA    1 
ATOM   1194  C C     . GLU A 1 179  ? -12.244 50.311  55.625  1.00 17.19 ?  177  GLU A C     1 
ATOM   1195  O O     . GLU A 1 179  ? -13.358 50.685  56.029  1.00 20.15 ?  177  GLU A O     1 
ATOM   1196  C CB    . GLU A 1 179  ? -11.078 51.830  53.996  1.00 22.89 ?  177  GLU A CB    1 
ATOM   1197  C CG    . GLU A 1 179  ? -12.358 52.499  53.478  1.00 26.43 ?  177  GLU A CG    1 
ATOM   1198  C CD    . GLU A 1 179  ? -13.321 51.528  52.822  1.00 33.60 ?  177  GLU A CD    1 
ATOM   1199  O OE1   . GLU A 1 179  ? -12.912 50.380  52.532  1.00 39.09 ?  177  GLU A OE1   1 
ATOM   1200  O OE2   . GLU A 1 179  ? -14.488 51.917  52.581  1.00 39.72 ?  177  GLU A OE2   1 
ATOM   1201  N N     . PRO A 1 180  ? -12.026 49.024  55.334  1.00 17.49 ?  178  PRO A N     1 
ATOM   1202  C CA    . PRO A 1 180  ? -13.133 48.067  55.483  1.00 21.43 ?  178  PRO A CA    1 
ATOM   1203  C C     . PRO A 1 180  ? -13.769 48.057  56.861  1.00 20.18 ?  178  PRO A C     1 
ATOM   1204  O O     . PRO A 1 180  ? -14.994 47.939  56.962  1.00 21.47 ?  178  PRO A O     1 
ATOM   1205  C CB    . PRO A 1 180  ? -12.470 46.729  55.149  1.00 20.82 ?  178  PRO A CB    1 
ATOM   1206  C CG    . PRO A 1 180  ? -11.444 47.094  54.135  1.00 20.29 ?  178  PRO A CG    1 
ATOM   1207  C CD    . PRO A 1 180  ? -10.867 48.387  54.679  1.00 20.55 ?  178  PRO A CD    1 
ATOM   1208  N N     . VAL A 1 181  ? -12.991 48.191  57.932  1.00 17.78 ?  179  VAL A N     1 
ATOM   1209  C CA    . VAL A 1 181  ? -13.628 48.170  59.244  1.00 16.43 ?  179  VAL A CA    1 
ATOM   1210  C C     . VAL A 1 181  ? -14.357 49.484  59.515  1.00 18.24 ?  179  VAL A C     1 
ATOM   1211  O O     . VAL A 1 181  ? -15.392 49.493  60.195  1.00 17.78 ?  179  VAL A O     1 
ATOM   1212  C CB    . VAL A 1 181  ? -12.607 47.829  60.355  1.00 15.19 ?  179  VAL A CB    1 
ATOM   1213  C CG1   . VAL A 1 181  ? -11.619 48.973  60.625  1.00 16.69 ?  179  VAL A CG1   1 
ATOM   1214  C CG2   . VAL A 1 181  ? -13.333 47.439  61.642  1.00 18.01 ?  179  VAL A CG2   1 
ATOM   1215  N N     . ILE A 1 182  ? -13.837 50.609  59.009  1.00 16.74 ?  180  ILE A N     1 
ATOM   1216  C CA    . ILE A 1 182  ? -14.529 51.886  59.167  1.00 16.11 ?  180  ILE A CA    1 
ATOM   1217  C C     . ILE A 1 182  ? -15.857 51.840  58.436  1.00 18.66 ?  180  ILE A C     1 
ATOM   1218  O O     . ILE A 1 182  ? -16.886 52.286  58.952  1.00 18.28 ?  180  ILE A O     1 
ATOM   1219  C CB    . ILE A 1 182  ? -13.652 53.048  58.662  1.00 16.22 ?  180  ILE A CB    1 
ATOM   1220  C CG1   . ILE A 1 182  ? -12.316 53.088  59.412  1.00 18.15 ?  180  ILE A CG1   1 
ATOM   1221  C CG2   . ILE A 1 182  ? -14.393 54.383  58.802  1.00 20.66 ?  180  ILE A CG2   1 
ATOM   1222  C CD1   . ILE A 1 182  ? -11.306 54.047  58.814  1.00 20.78 ?  180  ILE A CD1   1 
ATOM   1223  N N     . ARG A 1 183  ? -15.849 51.292  57.223  1.00 19.25 ?  181  ARG A N     1 
ATOM   1224  C CA    . ARG A 1 183  ? -17.077 51.156  56.449  1.00 22.00 ?  181  ARG A CA    1 
ATOM   1225  C C     . ARG A 1 183  ? -18.123 50.355  57.210  1.00 21.26 ?  181  ARG A C     1 
ATOM   1226  O O     . ARG A 1 183  ? -19.293 50.753  57.300  1.00 21.88 ?  181  ARG A O     1 
ATOM   1227  C CB    . ARG A 1 183  ? -16.754 50.487  55.113  1.00 23.81 ?  181  ARG A CB    1 
ATOM   1228  C CG    . ARG A 1 183  ? -17.935 50.336  54.168  1.00 28.40 ?  181  ARG A CG    1 
ATOM   1229  C CD    . ARG A 1 183  ? -18.235 51.662  53.500  1.00 33.08 ?  181  ARG A CD    1 
ATOM   1230  N NE    . ARG A 1 183  ? -19.342 52.355  54.139  1.00 29.84 ?  181  ARG A NE    1 
ATOM   1231  C CZ    . ARG A 1 183  ? -19.496 53.671  54.140  1.00 31.41 ?  181  ARG A CZ    1 
ATOM   1232  N NH1   . ARG A 1 183  ? -18.603 54.471  53.577  1.00 33.58 ?  181  ARG A NH1   1 
ATOM   1233  N NH2   . ARG A 1 183  ? -20.561 54.199  54.736  1.00 30.35 ?  181  ARG A NH2   1 
ATOM   1234  N N     . ARG A 1 184  ? -17.719 49.208  57.756  1.00 19.71 ?  182  ARG A N     1 
ATOM   1235  C CA    . ARG A 1 184  ? -18.669 48.376  58.484  1.00 21.56 ?  182  ARG A CA    1 
ATOM   1236  C C     . ARG A 1 184  ? -19.176 49.078  59.739  1.00 20.24 ?  182  ARG A C     1 
ATOM   1237  O O     . ARG A 1 184  ? -20.363 48.967  60.078  1.00 19.54 ?  182  ARG A O     1 
ATOM   1238  C CB    . ARG A 1 184  ? -18.023 47.037  58.823  1.00 23.34 ?  182  ARG A CB    1 
ATOM   1239  C CG    . ARG A 1 184  ? -17.925 46.099  57.637  1.00 26.52 ?  182  ARG A CG    1 
ATOM   1240  C CD    . ARG A 1 184  ? -19.133 45.160  57.563  1.00 28.34 ?  182  ARG A CD    1 
ATOM   1241  N NE    . ARG A 1 184  ? -18.983 44.004  58.440  1.00 31.51 ?  182  ARG A NE    1 
ATOM   1242  C CZ    . ARG A 1 184  ? -19.772 43.727  59.470  1.00 28.87 ?  182  ARG A CZ    1 
ATOM   1243  N NH1   . ARG A 1 184  ? -20.798 44.501  59.785  1.00 26.67 ?  182  ARG A NH1   1 
ATOM   1244  N NH2   . ARG A 1 184  ? -19.532 42.637  60.194  1.00 31.36 ?  182  ARG A NH2   1 
ATOM   1245  N N     . GLY A 1 185  ? -18.299 49.810  60.438  1.00 17.89 ?  183  GLY A N     1 
ATOM   1246  C CA    . GLY A 1 185  ? -18.742 50.555  61.610  1.00 15.38 ?  183  GLY A CA    1 
ATOM   1247  C C     . GLY A 1 185  ? -19.760 51.628  61.269  1.00 19.38 ?  183  GLY A C     1 
ATOM   1248  O O     . GLY A 1 185  ? -20.777 51.767  61.949  1.00 17.55 ?  183  GLY A O     1 
ATOM   1249  N N     . VAL A 1 186  ? -19.508 52.382  60.196  1.00 19.14 ?  184  VAL A N     1 
ATOM   1250  C CA    . VAL A 1 186  ? -20.428 53.445  59.789  1.00 17.27 ?  184  VAL A CA    1 
ATOM   1251  C C     . VAL A 1 186  ? -21.787 52.862  59.421  1.00 19.19 ?  184  VAL A C     1 
ATOM   1252  O O     . VAL A 1 186  ? -22.836 53.374  59.837  1.00 18.44 ?  184  VAL A O     1 
ATOM   1253  C CB    . VAL A 1 186  ? -19.830 54.242  58.615  1.00 17.29 ?  184  VAL A CB    1 
ATOM   1254  C CG1   . VAL A 1 186  ? -20.930 55.129  57.969  1.00 20.23 ?  184  VAL A CG1   1 
ATOM   1255  C CG2   . VAL A 1 186  ? -18.674 55.082  59.080  1.00 19.58 ?  184  VAL A CG2   1 
ATOM   1256  N N     . ASP A 1 187  ? -21.789 51.783  58.640  1.00 17.19 ?  185  ASP A N     1 
ATOM   1257  C CA    . ASP A 1 187  ? -23.049 51.175  58.226  1.00 21.05 ?  185  ASP A CA    1 
ATOM   1258  C C     . ASP A 1 187  ? -23.807 50.615  59.421  1.00 22.06 ?  185  ASP A C     1 
ATOM   1259  O O     . ASP A 1 187  ? -25.036 50.718  59.481  1.00 22.73 ?  185  ASP A O     1 
ATOM   1260  C CB    . ASP A 1 187  ? -22.790 50.089  57.181  1.00 23.32 ?  185  ASP A CB    1 
ATOM   1261  C CG    . ASP A 1 187  ? -22.328 50.662  55.834  1.00 26.12 ?  185  ASP A CG    1 
ATOM   1262  O OD1   . ASP A 1 187  ? -22.405 51.896  55.643  1.00 29.42 ?  185  ASP A OD1   1 
ATOM   1263  O OD2   . ASP A 1 187  ? -21.886 49.883  54.970  1.00 27.45 ?  185  ASP A OD2   1 
ATOM   1264  N N     . MET A 1 188  ? -23.086 50.056  60.398  1.00 20.61 ?  186  MET A N     1 
ATOM   1265  C CA    . MET A 1 188  ? -23.736 49.519  61.593  1.00 18.90 ?  186  MET A CA    1 
ATOM   1266  C C     . MET A 1 188  ? -24.352 50.627  62.433  1.00 20.70 ?  186  MET A C     1 
ATOM   1267  O O     . MET A 1 188  ? -25.507 50.524  62.872  1.00 21.19 ?  186  MET A O     1 
ATOM   1268  C CB    . MET A 1 188  ? -22.722 48.729  62.420  1.00 23.70 ?  186  MET A CB    1 
ATOM   1269  C CG    . MET A 1 188  ? -23.306 48.073  63.662  1.00 27.25 ?  186  MET A CG    1 
ATOM   1270  S SD    . MET A 1 188  ? -24.532 46.833  63.223  1.00 33.21 ?  186  MET A SD    1 
ATOM   1271  C CE    . MET A 1 188  ? -23.521 45.734  62.219  1.00 30.66 ?  186  MET A CE    1 
ATOM   1272  N N     . ALA A 1 189  ? -23.589 51.691  62.686  1.00 19.23 ?  187  ALA A N     1 
ATOM   1273  C CA    . ALA A 1 189  ? -24.122 52.801  63.469  1.00 18.37 ?  187  ALA A CA    1 
ATOM   1274  C C     . ALA A 1 189  ? -25.299 53.449  62.760  1.00 17.83 ?  187  ALA A C     1 
ATOM   1275  O O     . ALA A 1 189  ? -26.265 53.871  63.409  1.00 19.46 ?  187  ALA A O     1 
ATOM   1276  C CB    . ALA A 1 189  ? -23.033 53.835  63.742  1.00 19.86 ?  187  ALA A CB    1 
ATOM   1277  N N     . MET A 1 190  ? -25.228 53.551  61.427  1.00 17.91 ?  188  MET A N     1 
ATOM   1278  C CA    . MET A 1 190  ? -26.336 54.126  60.668  1.00 19.57 ?  188  MET A CA    1 
ATOM   1279  C C     . MET A 1 190  ? -27.615 53.324  60.878  1.00 20.02 ?  188  MET A C     1 
ATOM   1280  O O     . MET A 1 190  ? -28.683 53.891  61.141  1.00 21.94 ?  188  MET A O     1 
ATOM   1281  C CB    . MET A 1 190  ? -25.982 54.186  59.183  1.00 24.32 ?  188  MET A CB    1 
ATOM   1282  C CG    . MET A 1 190  ? -26.935 55.029  58.368  1.00 25.07 ?  188  MET A CG    1 
ATOM   1283  S SD    . MET A 1 190  ? -26.557 55.003  56.605  1.00 34.34 ?  188  MET A SD    1 
ATOM   1284  C CE    . MET A 1 190  ? -24.780 55.240  56.604  1.00 26.46 ?  188  MET A CE    1 
ATOM   1285  N N     . ARG A 1 191  ? -27.518 51.994  60.782  1.00 18.52 ?  189  ARG A N     1 
ATOM   1286  C CA    . ARG A 1 191  ? -28.680 51.141  61.002  1.00 22.55 ?  189  ARG A CA    1 
ATOM   1287  C C     . ARG A 1 191  ? -29.188 51.268  62.431  1.00 22.60 ?  189  ARG A C     1 
ATOM   1288  O O     . ARG A 1 191  ? -30.389 51.450  62.666  1.00 21.35 ?  189  ARG A O     1 
ATOM   1289  C CB    . ARG A 1 191  ? -28.325 49.685  60.680  1.00 23.04 ?  189  ARG A CB    1 
ATOM   1290  C CG    . ARG A 1 191  ? -29.486 48.710  60.802  1.00 30.65 ?  189  ARG A CG    1 
ATOM   1291  C CD    . ARG A 1 191  ? -29.013 47.321  61.261  1.00 35.20 ?  189  ARG A CD    1 
ATOM   1292  N NE    . ARG A 1 191  ? -27.855 46.833  60.521  1.00 45.20 ?  189  ARG A NE    1 
ATOM   1293  C CZ    . ARG A 1 191  ? -27.202 45.711  60.803  1.00 51.66 ?  189  ARG A CZ    1 
ATOM   1294  N NH1   . ARG A 1 191  ? -27.574 44.925  61.803  1.00 52.01 ?  189  ARG A NH1   1 
ATOM   1295  N NH2   . ARG A 1 191  ? -26.146 45.370  60.067  1.00 48.13 ?  189  ARG A NH2   1 
ATOM   1296  N N     . MET A 1 192  ? -28.285 51.178  63.411  1.00 18.72 ?  190  MET A N     1 
ATOM   1297  C CA    . MET A 1 192  ? -28.732 51.200  64.802  1.00 18.23 ?  190  MET A CA    1 
ATOM   1298  C C     . MET A 1 192  ? -29.383 52.527  65.151  1.00 20.90 ?  190  MET A C     1 
ATOM   1299  O O     . MET A 1 192  ? -30.438 52.560  65.793  1.00 19.14 ?  190  MET A O     1 
ATOM   1300  C CB    . MET A 1 192  ? -27.558 50.923  65.739  1.00 20.11 ?  190  MET A CB    1 
ATOM   1301  C CG    . MET A 1 192  ? -26.972 49.543  65.539  1.00 21.18 ?  190  MET A CG    1 
ATOM   1302  S SD    . MET A 1 192  ? -25.670 49.175  66.724  1.00 28.56 ?  190  MET A SD    1 
ATOM   1303  C CE    . MET A 1 192  ? -26.639 49.009  68.219  1.00 28.24 ?  190  MET A CE    1 
ATOM   1304  N N     . MET A 1 193  ? -28.765 53.634  64.751  1.00 19.89 ?  191  MET A N     1 
ATOM   1305  C CA    . MET A 1 193  ? -29.288 54.929  65.145  1.00 19.60 ?  191  MET A CA    1 
ATOM   1306  C C     . MET A 1 193  ? -30.443 55.396  64.271  1.00 17.95 ?  191  MET A C     1 
ATOM   1307  O O     . MET A 1 193  ? -31.141 56.338  64.660  1.00 21.86 ?  191  MET A O     1 
ATOM   1308  C CB    . MET A 1 193  ? -28.165 55.964  65.136  1.00 19.80 ?  191  MET A CB    1 
ATOM   1309  C CG    . MET A 1 193  ? -27.183 55.752  66.267  1.00 22.71 ?  191  MET A CG    1 
ATOM   1310  S SD    . MET A 1 193  ? -26.100 57.178  66.495  1.00 33.53 ?  191  MET A SD    1 
ATOM   1311  C CE    . MET A 1 193  ? -25.054 56.926  65.112  1.00 24.84 ?  191  MET A CE    1 
ATOM   1312  N N     . GLY A 1 194  ? -30.678 54.762  63.131  1.00 20.01 ?  192  GLY A N     1 
ATOM   1313  C CA    . GLY A 1 194  ? -31.782 55.179  62.285  1.00 18.57 ?  192  GLY A CA    1 
ATOM   1314  C C     . GLY A 1 194  ? -32.964 54.233  62.300  1.00 22.33 ?  192  GLY A C     1 
ATOM   1315  O O     . GLY A 1 194  ? -34.074 54.635  61.934  1.00 22.62 ?  192  GLY A O     1 
ATOM   1316  N N     . GLU A 1 195  ? -32.745 52.986  62.724  1.00 19.98 ?  193  GLU A N     1 
ATOM   1317  C CA    . GLU A 1 195  ? -33.748 51.931  62.592  1.00 19.10 ?  193  GLU A CA    1 
ATOM   1318  C C     . GLU A 1 195  ? -33.976 51.092  63.836  1.00 19.59 ?  193  GLU A C     1 
ATOM   1319  O O     . GLU A 1 195  ? -35.000 50.405  63.893  1.00 19.09 ?  193  GLU A O     1 
ATOM   1320  C CB    . GLU A 1 195  ? -33.370 50.968  61.458  1.00 24.43 ?  193  GLU A CB    1 
ATOM   1321  C CG    . GLU A 1 195  ? -33.159 51.609  60.114  1.00 27.64 ?  193  GLU A CG    1 
ATOM   1322  C CD    . GLU A 1 195  ? -32.534 50.641  59.133  1.00 30.82 ?  193  GLU A CD    1 
ATOM   1323  O OE1   . GLU A 1 195  ? -32.992 49.480  59.066  1.00 35.39 ?  193  GLU A OE1   1 
ATOM   1324  O OE2   . GLU A 1 195  ? -31.561 51.031  58.455  1.00 39.13 ?  193  GLU A OE2   1 
ATOM   1325  N N     . GLN A 1 196  ? -33.064 51.086  64.811  1.00 18.84 ?  194  GLN A N     1 
ATOM   1326  C CA    . GLN A 1 196  ? -33.198 50.252  65.998  1.00 20.95 ?  194  GLN A CA    1 
ATOM   1327  C C     . GLN A 1 196  ? -33.497 51.075  67.244  1.00 22.05 ?  194  GLN A C     1 
ATOM   1328  O O     . GLN A 1 196  ? -34.489 50.826  67.937  1.00 21.44 ?  194  GLN A O     1 
ATOM   1329  C CB    . GLN A 1 196  ? -31.925 49.418  66.207  1.00 23.30 ?  194  GLN A CB    1 
ATOM   1330  C CG    . GLN A 1 196  ? -31.994 48.574  67.465  1.00 30.67 ?  194  GLN A CG    1 
ATOM   1331  C CD    . GLN A 1 196  ? -30.720 47.805  67.731  1.00 30.08 ?  194  GLN A CD    1 
ATOM   1332  O OE1   . GLN A 1 196  ? -29.967 47.481  66.809  1.00 31.19 ?  194  GLN A OE1   1 
ATOM   1333  N NE2   . GLN A 1 196  ? -30.469 47.505  69.001  1.00 34.52 ?  194  GLN A NE2   1 
ATOM   1334  N N     . PHE A 1 197  ? -32.648 52.049  67.559  1.00 19.86 ?  195  PHE A N     1 
ATOM   1335  C CA    . PHE A 1 197  ? -32.907 52.893  68.713  1.00 18.94 ?  195  PHE A CA    1 
ATOM   1336  C C     . PHE A 1 197  ? -34.070 53.829  68.469  1.00 20.31 ?  195  PHE A C     1 
ATOM   1337  O O     . PHE A 1 197  ? -34.654 54.341  69.430  1.00 19.70 ?  195  PHE A O     1 
ATOM   1338  C CB    . PHE A 1 197  ? -31.663 53.691  69.062  1.00 21.40 ?  195  PHE A CB    1 
ATOM   1339  C CG    . PHE A 1 197  ? -30.519 52.838  69.516  1.00 23.75 ?  195  PHE A CG    1 
ATOM   1340  C CD1   . PHE A 1 197  ? -30.738 51.773  70.369  1.00 23.00 ?  195  PHE A CD1   1 
ATOM   1341  C CD2   . PHE A 1 197  ? -29.230 53.095  69.077  1.00 27.05 ?  195  PHE A CD2   1 
ATOM   1342  C CE1   . PHE A 1 197  ? -29.689 50.978  70.792  1.00 28.76 ?  195  PHE A CE1   1 
ATOM   1343  C CE2   . PHE A 1 197  ? -28.176 52.301  69.496  1.00 25.69 ?  195  PHE A CE2   1 
ATOM   1344  C CZ    . PHE A 1 197  ? -28.412 51.244  70.348  1.00 24.67 ?  195  PHE A CZ    1 
ATOM   1345  N N     . VAL A 1 198  ? -34.403 54.071  67.204  1.00 17.10 ?  196  VAL A N     1 
ATOM   1346  C CA    . VAL A 1 198  ? -35.606 54.796  66.830  1.00 15.59 ?  196  VAL A CA    1 
ATOM   1347  C C     . VAL A 1 198  ? -36.288 54.029  65.715  1.00 17.01 ?  196  VAL A C     1 
ATOM   1348  O O     . VAL A 1 198  ? -35.660 53.282  64.962  1.00 18.96 ?  196  VAL A O     1 
ATOM   1349  C CB    . VAL A 1 198  ? -35.338 56.254  66.379  1.00 16.25 ?  196  VAL A CB    1 
ATOM   1350  C CG1   . VAL A 1 198  ? -34.709 57.066  67.501  1.00 17.61 ?  196  VAL A CG1   1 
ATOM   1351  C CG2   . VAL A 1 198  ? -34.482 56.303  65.109  1.00 18.69 ?  196  VAL A CG2   1 
ATOM   1352  N N     . THR A 1 199  ? -37.598 54.225  65.618  1.00 15.51 ?  197  THR A N     1 
ATOM   1353  C CA    . THR A 1 199  ? -38.329 53.708  64.473  1.00 16.45 ?  197  THR A CA    1 
ATOM   1354  C C     . THR A 1 199  ? -38.012 54.520  63.231  1.00 17.68 ?  197  THR A C     1 
ATOM   1355  O O     . THR A 1 199  ? -37.928 53.969  62.131  1.00 21.58 ?  197  THR A O     1 
ATOM   1356  C CB    . THR A 1 199  ? -39.826 53.729  64.773  1.00 17.07 ?  197  THR A CB    1 
ATOM   1357  O OG1   . THR A 1 199  ? -40.051 53.026  65.998  1.00 19.29 ?  197  THR A OG1   1 
ATOM   1358  C CG2   . THR A 1 199  ? -40.609 53.055  63.667  1.00 20.64 ?  197  THR A CG2   1 
ATOM   1359  N N     . GLY A 1 200  ? -37.801 55.818  63.399  1.00 17.89 ?  198  GLY A N     1 
ATOM   1360  C CA    . GLY A 1 200  ? -37.364 56.672  62.314  1.00 18.23 ?  198  GLY A CA    1 
ATOM   1361  C C     . GLY A 1 200  ? -36.824 57.970  62.866  1.00 16.41 ?  198  GLY A C     1 
ATOM   1362  O O     . GLY A 1 200  ? -37.049 58.318  64.032  1.00 16.11 ?  198  GLY A O     1 
ATOM   1363  N N     . GLU A 1 201  ? -36.077 58.675  62.014  1.00 18.30 ?  199  GLU A N     1 
ATOM   1364  C CA    . GLU A 1 201  ? -35.508 59.966  62.390  1.00 18.24 ?  199  GLU A CA    1 
ATOM   1365  C C     . GLU A 1 201  ? -36.586 61.029  62.535  1.00 19.21 ?  199  GLU A C     1 
ATOM   1366  O O     . GLU A 1 201  ? -36.489 61.902  63.405  1.00 18.61 ?  199  GLU A O     1 
ATOM   1367  C CB    . GLU A 1 201  ? -34.482 60.405  61.342  1.00 22.29 ?  199  GLU A CB    1 
ATOM   1368  C CG    . GLU A 1 201  ? -33.905 61.801  61.576  1.00 25.33 ?  199  GLU A CG    1 
ATOM   1369  C CD    . GLU A 1 201  ? -32.902 62.215  60.499  1.00 32.03 ?  199  GLU A CD    1 
ATOM   1370  O OE1   . GLU A 1 201  ? -32.880 61.583  59.420  1.00 34.54 ?  199  GLU A OE1   1 
ATOM   1371  O OE2   . GLU A 1 201  ? -32.135 63.173  60.744  1.00 39.42 ?  199  GLU A OE2   1 
ATOM   1372  N N     . THR A 1 202  ? -37.628 60.937  61.716  1.00 16.46 ?  200  THR A N     1 
ATOM   1373  C CA    . THR A 1 202  ? -38.748 61.862  61.686  1.00 17.21 ?  200  THR A CA    1 
ATOM   1374  C C     . THR A 1 202  ? -40.039 61.072  61.794  1.00 15.44 ?  200  THR A C     1 
ATOM   1375  O O     . THR A 1 202  ? -40.074 59.869  61.525  1.00 16.82 ?  200  THR A O     1 
ATOM   1376  C CB    . THR A 1 202  ? -38.792 62.650  60.386  1.00 17.62 ?  200  THR A CB    1 
ATOM   1377  O OG1   . THR A 1 202  ? -39.012 61.731  59.304  1.00 20.24 ?  200  THR A OG1   1 
ATOM   1378  C CG2   . THR A 1 202  ? -37.469 63.388  60.164  1.00 19.55 ?  200  THR A CG2   1 
ATOM   1379  N N     . ILE A 1 203  ? -41.124 61.770  62.134  1.00 14.83 ?  201  ILE A N     1 
ATOM   1380  C CA    . ILE A 1 203  ? -42.395 61.067  62.272  1.00 15.25 ?  201  ILE A CA    1 
ATOM   1381  C C     . ILE A 1 203  ? -42.841 60.492  60.926  1.00 16.42 ?  201  ILE A C     1 
ATOM   1382  O O     . ILE A 1 203  ? -43.383 59.385  60.867  1.00 17.74 ?  201  ILE A O     1 
ATOM   1383  C CB    . ILE A 1 203  ? -43.455 61.995  62.908  1.00 16.24 ?  201  ILE A CB    1 
ATOM   1384  C CG1   . ILE A 1 203  ? -44.740 61.223  63.250  1.00 14.60 ?  201  ILE A CG1   1 
ATOM   1385  C CG2   . ILE A 1 203  ? -43.762 63.198  62.023  1.00 19.16 ?  201  ILE A CG2   1 
ATOM   1386  C CD1   . ILE A 1 203  ? -44.516 60.052  64.193  1.00 15.30 ?  201  ILE A CD1   1 
ATOM   1387  N N     . ARG A 1 204  ? -42.550 61.183  59.820  1.00 17.97 ?  202  ARG A N     1 
ATOM   1388  C CA    . ARG A 1 204  ? -42.922 60.647  58.509  1.00 18.18 ?  202  ARG A CA    1 
ATOM   1389  C C     . ARG A 1 204  ? -42.178 59.359  58.194  1.00 18.70 ?  202  ARG A C     1 
ATOM   1390  O O     . ARG A 1 204  ? -42.772 58.401  57.690  1.00 19.23 ?  202  ARG A O     1 
ATOM   1391  C CB    . ARG A 1 204  ? -42.664 61.687  57.432  1.00 22.65 ?  202  ARG A CB    1 
ATOM   1392  C CG    . ARG A 1 204  ? -43.823 62.632  57.268  1.00 26.48 ?  202  ARG A CG    1 
ATOM   1393  C CD    . ARG A 1 204  ? -43.429 63.869  56.490  1.00 31.65 ?  202  ARG A CD    1 
ATOM   1394  N NE    . ARG A 1 204  ? -44.541 64.808  56.442  1.00 32.52 ?  202  ARG A NE    1 
ATOM   1395  C CZ    . ARG A 1 204  ? -44.950 65.536  57.473  1.00 33.35 ?  202  ARG A CZ    1 
ATOM   1396  N NH1   . ARG A 1 204  ? -44.353 65.460  58.659  1.00 24.60 ?  202  ARG A NH1   1 
ATOM   1397  N NH2   . ARG A 1 204  ? -45.984 66.361  57.310  1.00 29.33 ?  202  ARG A NH2   1 
ATOM   1398  N N     . GLU A 1 205  ? -40.875 59.320  58.483  1.00 17.15 ?  203  GLU A N     1 
ATOM   1399  C CA    . GLU A 1 205  ? -40.106 58.098  58.297  1.00 19.15 ?  203  GLU A CA    1 
ATOM   1400  C C     . GLU A 1 205  ? -40.616 56.994  59.204  1.00 18.88 ?  203  GLU A C     1 
ATOM   1401  O O     . GLU A 1 205  ? -40.745 55.841  58.774  1.00 19.65 ?  203  GLU A O     1 
ATOM   1402  C CB    . GLU A 1 205  ? -38.635 58.381  58.576  1.00 20.71 ?  203  GLU A CB    1 
ATOM   1403  C CG    . GLU A 1 205  ? -37.671 57.328  58.109  1.00 25.53 ?  203  GLU A CG    1 
ATOM   1404  C CD    . GLU A 1 205  ? -36.235 57.795  58.271  1.00 31.53 ?  203  GLU A CD    1 
ATOM   1405  O OE1   . GLU A 1 205  ? -35.709 57.725  59.403  1.00 26.72 ?  203  GLU A OE1   1 
ATOM   1406  O OE2   . GLU A 1 205  ? -35.646 58.269  57.272  1.00 37.91 ?  203  GLU A OE2   1 
ATOM   1407  N N     . ALA A 1 206  ? -40.917 57.333  60.464  1.00 15.98 ?  204  ALA A N     1 
ATOM   1408  C CA    . ALA A 1 206  ? -41.395 56.332  61.409  1.00 17.37 ?  204  ALA A CA    1 
ATOM   1409  C C     . ALA A 1 206  ? -42.721 55.753  60.955  1.00 17.15 ?  204  ALA A C     1 
ATOM   1410  O O     . ALA A 1 206  ? -42.920 54.536  61.009  1.00 16.65 ?  204  ALA A O     1 
ATOM   1411  C CB    . ALA A 1 206  ? -41.535 56.939  62.806  1.00 17.82 ?  204  ALA A CB    1 
ATOM   1412  N N     . LEU A 1 207  ? -43.632 56.613  60.498  1.00 16.19 ?  205  LEU A N     1 
ATOM   1413  C CA    . LEU A 1 207  ? -44.930 56.134  60.028  1.00 16.07 ?  205  LEU A CA    1 
ATOM   1414  C C     . LEU A 1 207  ? -44.776 55.192  58.840  1.00 19.81 ?  205  LEU A C     1 
ATOM   1415  O O     . LEU A 1 207  ? -45.445 54.151  58.774  1.00 21.54 ?  205  LEU A O     1 
ATOM   1416  C CB    . LEU A 1 207  ? -45.826 57.320  59.666  1.00 17.60 ?  205  LEU A CB    1 
ATOM   1417  C CG    . LEU A 1 207  ? -46.352 58.106  60.866  1.00 17.44 ?  205  LEU A CG    1 
ATOM   1418  C CD1   . LEU A 1 207  ? -46.925 59.442  60.436  1.00 16.73 ?  205  LEU A CD1   1 
ATOM   1419  C CD2   . LEU A 1 207  ? -47.393 57.272  61.596  1.00 16.03 ?  205  LEU A CD2   1 
ATOM   1420  N N     . LYS A 1 208  ? -43.890 55.535  57.896  1.00 20.33 ?  206  LYS A N     1 
ATOM   1421  C CA    . LYS A 1 208  ? -43.686 54.691  56.721  1.00 21.67 ?  206  LYS A CA    1 
ATOM   1422  C C     . LYS A 1 208  ? -43.235 53.292  57.121  1.00 21.83 ?  206  LYS A C     1 
ATOM   1423  O O     . LYS A 1 208  ? -43.703 52.293  56.558  1.00 25.50 ?  206  LYS A O     1 
ATOM   1424  C CB    . LYS A 1 208  ? -42.661 55.351  55.794  1.00 23.83 ?  206  LYS A CB    1 
ATOM   1425  C CG    . LYS A 1 208  ? -42.348 54.572  54.530  1.00 30.90 ?  206  LYS A CG    1 
ATOM   1426  C CD    . LYS A 1 208  ? -41.122 55.163  53.830  1.00 34.28 ?  206  LYS A CD    1 
ATOM   1427  C CE    . LYS A 1 208  ? -40.720 54.350  52.601  1.00 41.88 ?  206  LYS A CE    1 
ATOM   1428  N NZ    . LYS A 1 208  ? -41.825 54.263  51.601  1.00 43.38 ?  206  LYS A NZ    1 
ATOM   1429  N N     . ARG A 1 209  ? -42.360 53.199  58.118  1.00 20.91 ?  207  ARG A N     1 
ATOM   1430  C CA    . ARG A 1 209  ? -41.816 51.926  58.567  1.00 20.41 ?  207  ARG A CA    1 
ATOM   1431  C C     . ARG A 1 209  ? -42.752 51.166  59.496  1.00 22.19 ?  207  ARG A C     1 
ATOM   1432  O O     . ARG A 1 209  ? -42.441 50.029  59.868  1.00 26.07 ?  207  ARG A O     1 
ATOM   1433  C CB    . ARG A 1 209  ? -40.477 52.166  59.250  1.00 22.74 ?  207  ARG A CB    1 
ATOM   1434  C CG    . ARG A 1 209  ? -39.447 52.747  58.289  1.00 23.01 ?  207  ARG A CG    1 
ATOM   1435  C CD    . ARG A 1 209  ? -38.178 53.091  59.010  1.00 23.58 ?  207  ARG A CD    1 
ATOM   1436  N NE    . ARG A 1 209  ? -37.160 53.600  58.101  1.00 27.75 ?  207  ARG A NE    1 
ATOM   1437  C CZ    . ARG A 1 209  ? -36.002 54.108  58.498  1.00 31.48 ?  207  ARG A CZ    1 
ATOM   1438  N NH1   . ARG A 1 209  ? -35.696 54.206  59.781  1.00 28.97 ?  207  ARG A NH1   1 
ATOM   1439  N NH2   . ARG A 1 209  ? -35.129 54.529  57.585  1.00 34.40 ?  207  ARG A NH2   1 
ATOM   1440  N N     . SER A 1 210  ? -43.895 51.746  59.851  1.00 19.30 ?  208  SER A N     1 
ATOM   1441  C CA    . SER A 1 210  ? -44.818 51.103  60.772  1.00 21.52 ?  208  SER A CA    1 
ATOM   1442  C C     . SER A 1 210  ? -45.828 50.205  60.076  1.00 23.12 ?  208  SER A C     1 
ATOM   1443  O O     . SER A 1 210  ? -46.436 49.353  60.735  1.00 23.39 ?  208  SER A O     1 
ATOM   1444  C CB    . SER A 1 210  ? -45.559 52.166  61.588  1.00 19.61 ?  208  SER A CB    1 
ATOM   1445  O OG    . SER A 1 210  ? -44.651 52.879  62.411  1.00 20.00 ?  208  SER A OG    1 
ATOM   1446  N N     . LYS A 1 211  ? -46.006 50.360  58.763  1.00 24.58 ?  209  LYS A N     1 
ATOM   1447  C CA    . LYS A 1 211  ? -47.062 49.642  58.058  1.00 26.25 ?  209  LYS A CA    1 
ATOM   1448  C C     . LYS A 1 211  ? -46.842 48.134  58.079  1.00 25.20 ?  209  LYS A C     1 
ATOM   1449  O O     . LYS A 1 211  ? -47.813 47.373  58.144  1.00 26.25 ?  209  LYS A O     1 
ATOM   1450  C CB    . LYS A 1 211  ? -47.162 50.160  56.624  1.00 24.51 ?  209  LYS A CB    1 
ATOM   1451  C CG    . LYS A 1 211  ? -47.473 51.662  56.558  1.00 27.56 ?  209  LYS A CG    1 
ATOM   1452  C CD    . LYS A 1 211  ? -47.579 52.160  55.123  1.00 32.81 ?  209  LYS A CD    1 
ATOM   1453  N N     . GLU A 1 212  ? -45.583 47.692  58.069  1.00 24.09 ?  210  GLU A N     1 
ATOM   1454  C CA    . GLU A 1 212  ? -45.285 46.263  58.005  1.00 28.77 ?  210  GLU A CA    1 
ATOM   1455  C C     . GLU A 1 212  ? -45.885 45.515  59.189  1.00 27.36 ?  210  GLU A C     1 
ATOM   1456  O O     . GLU A 1 212  ? -46.593 44.516  59.013  1.00 30.96 ?  210  GLU A O     1 
ATOM   1457  C CB    . GLU A 1 212  ? -43.773 46.047  57.947  1.00 30.29 ?  210  GLU A CB    1 
ATOM   1458  C CG    . GLU A 1 212  ? -43.364 44.587  57.806  1.00 38.36 ?  210  GLU A CG    1 
ATOM   1459  C CD    . GLU A 1 212  ? -41.884 44.428  57.502  1.00 46.62 ?  210  GLU A CD    1 
ATOM   1460  O OE1   . GLU A 1 212  ? -41.315 45.326  56.846  1.00 45.75 ?  210  GLU A OE1   1 
ATOM   1461  O OE2   . GLU A 1 212  ? -41.289 43.411  57.919  1.00 54.66 ?  210  GLU A OE2   1 
ATOM   1462  N N     . LEU A 1 213  ? -45.616 45.985  60.410  1.00 25.07 ?  211  LEU A N     1 
ATOM   1463  C CA    . LEU A 1 213  ? -46.132 45.291  61.582  1.00 23.83 ?  211  LEU A CA    1 
ATOM   1464  C C     . LEU A 1 213  ? -47.586 45.627  61.874  1.00 23.63 ?  211  LEU A C     1 
ATOM   1465  O O     . LEU A 1 213  ? -48.281 44.812  62.490  1.00 24.58 ?  211  LEU A O     1 
ATOM   1466  C CB    . LEU A 1 213  ? -45.263 45.593  62.802  1.00 22.66 ?  211  LEU A CB    1 
ATOM   1467  C CG    . LEU A 1 213  ? -43.883 44.929  62.714  1.00 25.56 ?  211  LEU A CG    1 
ATOM   1468  C CD1   . LEU A 1 213  ? -43.014 45.257  63.915  1.00 24.71 ?  211  LEU A CD1   1 
ATOM   1469  C CD2   . LEU A 1 213  ? -44.026 43.420  62.550  1.00 30.16 ?  211  LEU A CD2   1 
ATOM   1470  N N     . GLU A 1 214  ? -48.081 46.782  61.424  1.00 22.52 ?  212  GLU A N     1 
ATOM   1471  C CA    . GLU A 1 214  ? -49.509 47.044  61.564  1.00 21.09 ?  212  GLU A CA    1 
ATOM   1472  C C     . GLU A 1 214  ? -50.338 46.036  60.781  1.00 26.42 ?  212  GLU A C     1 
ATOM   1473  O O     . GLU A 1 214  ? -51.396 45.602  61.246  1.00 25.67 ?  212  GLU A O     1 
ATOM   1474  C CB    . GLU A 1 214  ? -49.831 48.466  61.118  1.00 21.16 ?  212  GLU A CB    1 
ATOM   1475  C CG    . GLU A 1 214  ? -49.352 49.506  62.119  1.00 20.48 ?  212  GLU A CG    1 
ATOM   1476  C CD    . GLU A 1 214  ? -49.769 50.906  61.732  1.00 25.08 ?  212  GLU A CD    1 
ATOM   1477  O OE1   . GLU A 1 214  ? -50.052 51.152  60.537  1.00 25.13 ?  212  GLU A OE1   1 
ATOM   1478  O OE2   . GLU A 1 214  ? -49.811 51.769  62.628  1.00 22.30 ?  212  GLU A OE2   1 
ATOM   1479  N N     . GLU A 1 215  ? -49.867 45.642  59.596  1.00 25.96 ?  213  GLU A N     1 
ATOM   1480  C CA    . GLU A 1 215  ? -50.577 44.639  58.811  1.00 27.51 ?  213  GLU A CA    1 
ATOM   1481  C C     . GLU A 1 215  ? -50.567 43.270  59.476  1.00 31.64 ?  213  GLU A C     1 
ATOM   1482  O O     . GLU A 1 215  ? -51.381 42.414  59.114  1.00 36.43 ?  213  GLU A O     1 
ATOM   1483  C CB    . GLU A 1 215  ? -49.967 44.548  57.413  1.00 34.32 ?  213  GLU A CB    1 
ATOM   1484  C CG    . GLU A 1 215  ? -50.175 45.805  56.590  1.00 39.19 ?  213  GLU A CG    1 
ATOM   1485  C CD    . GLU A 1 215  ? -49.308 45.849  55.350  1.00 48.78 ?  213  GLU A CD    1 
ATOM   1486  O OE1   . GLU A 1 215  ? -48.689 44.814  55.008  1.00 52.55 ?  213  GLU A OE1   1 
ATOM   1487  O OE2   . GLU A 1 215  ? -49.243 46.928  54.722  1.00 46.18 ?  213  GLU A OE2   1 
ATOM   1488  N N     . LYS A 1 216  ? -49.677 43.050  60.437  1.00 28.31 ?  214  LYS A N     1 
ATOM   1489  C CA    . LYS A 1 216  ? -49.618 41.808  61.193  1.00 31.55 ?  214  LYS A CA    1 
ATOM   1490  C C     . LYS A 1 216  ? -50.418 41.863  62.489  1.00 33.87 ?  214  LYS A C     1 
ATOM   1491  O O     . LYS A 1 216  ? -50.498 40.851  63.194  1.00 35.88 ?  214  LYS A O     1 
ATOM   1492  C CB    . LYS A 1 216  ? -48.165 41.454  61.510  1.00 27.55 ?  214  LYS A CB    1 
ATOM   1493  C CG    . LYS A 1 216  ? -47.330 41.081  60.301  1.00 36.22 ?  214  LYS A CG    1 
ATOM   1494  C CD    . LYS A 1 216  ? -45.879 40.834  60.704  1.00 39.72 ?  214  LYS A CD    1 
ATOM   1495  C CE    . LYS A 1 216  ? -45.131 40.026  59.651  1.00 44.66 ?  214  LYS A CE    1 
ATOM   1496  N NZ    . LYS A 1 216  ? -45.272 40.598  58.282  1.00 49.27 ?  214  LYS A NZ    1 
ATOM   1497  N N     . GLY A 1 217  ? -51.005 43.012  62.822  1.00 27.92 ?  215  GLY A N     1 
ATOM   1498  C CA    . GLY A 1 217  ? -51.821 43.151  64.012  1.00 25.80 ?  215  GLY A CA    1 
ATOM   1499  C C     . GLY A 1 217  ? -51.203 43.972  65.123  1.00 23.13 ?  215  GLY A C     1 
ATOM   1500  O O     . GLY A 1 217  ? -51.816 44.089  66.189  1.00 25.84 ?  215  GLY A O     1 
ATOM   1501  N N     . PHE A 1 218  ? -50.006 44.515  64.929  1.00 21.38 ?  216  PHE A N     1 
ATOM   1502  C CA    . PHE A 1 218  ? -49.453 45.449  65.894  1.00 18.95 ?  216  PHE A CA    1 
ATOM   1503  C C     . PHE A 1 218  ? -50.081 46.827  65.702  1.00 19.47 ?  216  PHE A C     1 
ATOM   1504  O O     . PHE A 1 218  ? -50.641 47.143  64.651  1.00 20.35 ?  216  PHE A O     1 
ATOM   1505  C CB    . PHE A 1 218  ? -47.929 45.563  65.748  1.00 19.12 ?  216  PHE A CB    1 
ATOM   1506  C CG    . PHE A 1 218  ? -47.165 44.360  66.227  1.00 24.04 ?  216  PHE A CG    1 
ATOM   1507  C CD1   . PHE A 1 218  ? -46.980 43.263  65.398  1.00 23.93 ?  216  PHE A CD1   1 
ATOM   1508  C CD2   . PHE A 1 218  ? -46.603 44.340  67.493  1.00 21.26 ?  216  PHE A CD2   1 
ATOM   1509  C CE1   . PHE A 1 218  ? -46.272 42.160  65.828  1.00 23.47 ?  216  PHE A CE1   1 
ATOM   1510  C CE2   . PHE A 1 218  ? -45.888 43.234  67.937  1.00 23.78 ?  216  PHE A CE2   1 
ATOM   1511  C CZ    . PHE A 1 218  ? -45.717 42.145  67.097  1.00 23.58 ?  216  PHE A CZ    1 
ATOM   1512  N N     . SER A 1 219  ? -49.975 47.652  66.739  1.00 18.16 ?  217  SER A N     1 
ATOM   1513  C CA    . SER A 1 219  ? -50.301 49.071  66.666  1.00 15.94 ?  217  SER A CA    1 
ATOM   1514  C C     . SER A 1 219  ? -49.087 49.846  67.168  1.00 15.70 ?  217  SER A C     1 
ATOM   1515  O O     . SER A 1 219  ? -48.095 49.250  67.592  1.00 15.89 ?  217  SER A O     1 
ATOM   1516  C CB    . SER A 1 219  ? -51.558 49.411  67.476  1.00 17.11 ?  217  SER A CB    1 
ATOM   1517  O OG    . SER A 1 219  ? -51.372 49.111  68.839  1.00 20.56 ?  217  SER A OG    1 
ATOM   1518  N N     . TYR A 1 220  ? -49.160 51.182  67.126  1.00 14.84 ?  218  TYR A N     1 
ATOM   1519  C CA    . TYR A 1 220  ? -48.022 52.025  67.480  1.00 14.04 ?  218  TYR A CA    1 
ATOM   1520  C C     . TYR A 1 220  ? -48.426 53.177  68.394  1.00 15.36 ?  218  TYR A C     1 
ATOM   1521  O O     . TYR A 1 220  ? -49.551 53.677  68.333  1.00 15.79 ?  218  TYR A O     1 
ATOM   1522  C CB    . TYR A 1 220  ? -47.359 52.592  66.215  1.00 14.16 ?  218  TYR A CB    1 
ATOM   1523  C CG    . TYR A 1 220  ? -46.429 51.602  65.554  1.00 14.13 ?  218  TYR A CG    1 
ATOM   1524  C CD1   . TYR A 1 220  ? -46.912 50.628  64.681  1.00 17.68 ?  218  TYR A CD1   1 
ATOM   1525  C CD2   . TYR A 1 220  ? -45.071 51.636  65.820  1.00 16.28 ?  218  TYR A CD2   1 
ATOM   1526  C CE1   . TYR A 1 220  ? -46.041 49.704  64.089  1.00 18.40 ?  218  TYR A CE1   1 
ATOM   1527  C CE2   . TYR A 1 220  ? -44.205 50.735  65.236  1.00 18.54 ?  218  TYR A CE2   1 
ATOM   1528  C CZ    . TYR A 1 220  ? -44.691 49.775  64.377  1.00 17.61 ?  218  TYR A CZ    1 
ATOM   1529  O OH    . TYR A 1 220  ? -43.795 48.886  63.821  1.00 20.57 ?  218  TYR A OH    1 
ATOM   1530  N N     . SER A 1 221  ? -47.489 53.583  69.256  1.00 13.63 ?  219  SER A N     1 
ATOM   1531  C CA    . SER A 1 221  ? -47.553 54.849  69.988  1.00 13.64 ?  219  SER A CA    1 
ATOM   1532  C C     . SER A 1 221  ? -46.199 55.519  69.845  1.00 16.56 ?  219  SER A C     1 
ATOM   1533  O O     . SER A 1 221  ? -45.186 54.950  70.255  1.00 16.97 ?  219  SER A O     1 
ATOM   1534  C CB    . SER A 1 221  ? -47.871 54.641  71.472  1.00 17.91 ?  219  SER A CB    1 
ATOM   1535  O OG    . SER A 1 221  ? -47.961 55.889  72.164  1.00 17.75 ?  219  SER A OG    1 
ATOM   1536  N N     . TYR A 1 222  ? -46.165 56.704  69.250  1.00 11.91 ?  220  TYR A N     1 
ATOM   1537  C CA    . TYR A 1 222  ? -44.880 57.326  68.932  1.00 12.38 ?  220  TYR A CA    1 
ATOM   1538  C C     . TYR A 1 222  ? -44.377 58.182  70.088  1.00 13.85 ?  220  TYR A C     1 
ATOM   1539  O O     . TYR A 1 222  ? -45.112 59.011  70.632  1.00 14.96 ?  220  TYR A O     1 
ATOM   1540  C CB    . TYR A 1 222  ? -44.989 58.141  67.639  1.00 13.37 ?  220  TYR A CB    1 
ATOM   1541  C CG    . TYR A 1 222  ? -45.322 57.234  66.489  1.00 12.05 ?  220  TYR A CG    1 
ATOM   1542  C CD1   . TYR A 1 222  ? -44.336 56.473  65.876  1.00 13.88 ?  220  TYR A CD1   1 
ATOM   1543  C CD2   . TYR A 1 222  ? -46.637 57.084  66.058  1.00 13.58 ?  220  TYR A CD2   1 
ATOM   1544  C CE1   . TYR A 1 222  ? -44.653 55.598  64.840  1.00 15.37 ?  220  TYR A CE1   1 
ATOM   1545  C CE2   . TYR A 1 222  ? -46.958 56.226  65.026  1.00 15.31 ?  220  TYR A CE2   1 
ATOM   1546  C CZ    . TYR A 1 222  ? -45.961 55.485  64.422  1.00 14.09 ?  220  TYR A CZ    1 
ATOM   1547  O OH    . TYR A 1 222  ? -46.288 54.619  63.410  1.00 16.75 ?  220  TYR A OH    1 
ATOM   1548  N N     . ASP A 1 223  ? -43.112 57.967  70.443  1.00 15.68 ?  221  ASP A N     1 
ATOM   1549  C CA    . ASP A 1 223  ? -42.401 58.649  71.521  1.00 17.27 ?  221  ASP A CA    1 
ATOM   1550  C C     . ASP A 1 223  ? -41.465 59.666  70.872  1.00 20.68 ?  221  ASP A C     1 
ATOM   1551  O O     . ASP A 1 223  ? -40.459 59.292  70.256  1.00 16.75 ?  221  ASP A O     1 
ATOM   1552  C CB    . ASP A 1 223  ? -41.650 57.605  72.348  1.00 18.68 ?  221  ASP A CB    1 
ATOM   1553  C CG    . ASP A 1 223  ? -40.661 58.204  73.346  1.00 21.83 ?  221  ASP A CG    1 
ATOM   1554  O OD1   . ASP A 1 223  ? -40.741 59.406  73.657  1.00 23.41 ?  221  ASP A OD1   1 
ATOM   1555  O OD2   . ASP A 1 223  ? -39.794 57.437  73.810  1.00 25.65 ?  221  ASP A OD2   1 
ATOM   1556  N N     . MET A 1 224  ? -41.792 60.947  70.997  1.00 20.38 ?  222  MET A N     1 
ATOM   1557  C CA    . MET A 1 224  ? -41.005 61.975  70.332  1.00 20.65 ?  222  MET A CA    1 
ATOM   1558  C C     . MET A 1 224  ? -39.727 62.357  71.100  1.00 20.97 ?  222  MET A C     1 
ATOM   1559  O O     . MET A 1 224  ? -39.016 63.278  70.677  1.00 25.79 ?  222  MET A O     1 
ATOM   1560  C CB    . MET A 1 224  ? -41.886 63.198  70.060  1.00 24.73 ?  222  MET A CB    1 
ATOM   1561  C CG    . MET A 1 224  ? -43.169 62.847  69.268  1.00 23.15 ?  222  MET A CG    1 
ATOM   1562  S SD    . MET A 1 224  ? -42.872 61.965  67.707  1.00 25.57 ?  222  MET A SD    1 
ATOM   1563  C CE    . MET A 1 224  ? -41.864 63.145  66.868  1.00 20.00 ?  222  MET A CE    1 
ATOM   1564  N N     . LEU A 1 225  ? -39.409 61.652  72.185  1.00 25.31 ?  223  LEU A N     1 
ATOM   1565  C CA    . LEU A 1 225  ? -38.101 61.661  72.839  1.00 22.27 ?  223  LEU A CA    1 
ATOM   1566  C C     . LEU A 1 225  ? -37.767 62.970  73.550  1.00 29.10 ?  223  LEU A C     1 
ATOM   1567  O O     . LEU A 1 225  ? -36.661 63.101  74.092  1.00 29.20 ?  223  LEU A O     1 
ATOM   1568  C CB    . LEU A 1 225  ? -36.982 61.316  71.846  1.00 20.57 ?  223  LEU A CB    1 
ATOM   1569  C CG    . LEU A 1 225  ? -36.862 59.832  71.465  1.00 18.21 ?  223  LEU A CG    1 
ATOM   1570  C CD1   . LEU A 1 225  ? -35.659 59.557  70.560  1.00 22.54 ?  223  LEU A CD1   1 
ATOM   1571  C CD2   . LEU A 1 225  ? -36.787 58.975  72.710  1.00 19.12 ?  223  LEU A CD2   1 
ATOM   1572  N N     . GLY A 1 226  ? -38.687 63.928  73.600  1.00 26.12 ?  224  GLY A N     1 
ATOM   1573  C CA    . GLY A 1 226  ? -38.432 65.146  74.348  1.00 27.02 ?  224  GLY A CA    1 
ATOM   1574  C C     . GLY A 1 226  ? -38.691 64.965  75.833  1.00 22.35 ?  224  GLY A C     1 
ATOM   1575  O O     . GLY A 1 226  ? -39.586 64.230  76.253  1.00 22.84 ?  224  GLY A O     1 
ATOM   1576  N N     . GLU A 1 227  ? -37.867 65.629  76.639  1.00 18.67 ?  225  GLU A N     1 
ATOM   1577  C CA    . GLU A 1 227  ? -38.105 65.663  78.073  1.00 18.83 ?  225  GLU A CA    1 
ATOM   1578  C C     . GLU A 1 227  ? -37.249 66.747  78.698  1.00 21.32 ?  225  GLU A C     1 
ATOM   1579  O O     . GLU A 1 227  ? -36.292 67.241  78.092  1.00 19.04 ?  225  GLU A O     1 
ATOM   1580  C CB    . GLU A 1 227  ? -37.810 64.317  78.730  1.00 20.62 ?  225  GLU A CB    1 
ATOM   1581  C CG    . GLU A 1 227  ? -36.353 63.897  78.694  1.00 19.06 ?  225  GLU A CG    1 
ATOM   1582  C CD    . GLU A 1 227  ? -36.187 62.491  79.226  1.00 26.28 ?  225  GLU A CD    1 
ATOM   1583  O OE1   . GLU A 1 227  ? -36.408 61.532  78.455  1.00 25.19 ?  225  GLU A OE1   1 
ATOM   1584  O OE2   . GLU A 1 227  ? -35.858 62.343  80.417  1.00 25.81 ?  225  GLU A OE2   1 
ATOM   1585  N N     . ALA A 1 228  ? -37.621 67.111  79.926  1.00 18.83 ?  226  ALA A N     1 
ATOM   1586  C CA    . ALA A 1 228  ? -36.810 67.978  80.775  1.00 19.55 ?  226  ALA A CA    1 
ATOM   1587  C C     . ALA A 1 228  ? -36.473 69.301  80.072  1.00 17.58 ?  226  ALA A C     1 
ATOM   1588  O O     . ALA A 1 228  ? -35.311 69.683  79.927  1.00 20.01 ?  226  ALA A O     1 
ATOM   1589  C CB    . ALA A 1 228  ? -35.540 67.249  81.227  1.00 21.26 ?  226  ALA A CB    1 
ATOM   1590  N N     . ALA A 1 229  ? -37.519 70.014  79.649  1.00 13.96 ?  227  ALA A N     1 
ATOM   1591  C CA    . ALA A 1 229  ? -37.326 71.372  79.151  1.00 13.41 ?  227  ALA A CA    1 
ATOM   1592  C C     . ALA A 1 229  ? -36.598 72.214  80.193  1.00 16.33 ?  227  ALA A C     1 
ATOM   1593  O O     . ALA A 1 229  ? -36.922 72.168  81.383  1.00 14.80 ?  227  ALA A O     1 
ATOM   1594  C CB    . ALA A 1 229  ? -38.672 72.019  78.822  1.00 14.89 ?  227  ALA A CB    1 
ATOM   1595  N N     . THR A 1 230  ? -35.617 72.995  79.733  1.00 14.21 ?  228  THR A N     1 
ATOM   1596  C CA    . THR A 1 230  ? -34.840 73.875  80.603  1.00 15.79 ?  228  THR A CA    1 
ATOM   1597  C C     . THR A 1 230  ? -35.251 75.336  80.478  1.00 13.99 ?  228  THR A C     1 
ATOM   1598  O O     . THR A 1 230  ? -35.080 76.106  81.431  1.00 13.65 ?  228  THR A O     1 
ATOM   1599  C CB    . THR A 1 230  ? -33.346 73.734  80.270  1.00 16.05 ?  228  THR A CB    1 
ATOM   1600  O OG1   . THR A 1 230  ? -32.977 72.345  80.333  1.00 23.81 ?  228  THR A OG1   1 
ATOM   1601  C CG2   . THR A 1 230  ? -32.494 74.499  81.248  1.00 21.39 ?  228  THR A CG2   1 
ATOM   1602  N N     . THR A 1 231  ? -35.796 75.736  79.324  1.00 13.97 ?  229  THR A N     1 
ATOM   1603  C CA    . THR A 1 231  ? -36.182 77.110  79.053  1.00 13.34 ?  229  THR A CA    1 
ATOM   1604  C C     . THR A 1 231  ? -37.573 77.126  78.448  1.00 13.18 ?  229  THR A C     1 
ATOM   1605  O O     . THR A 1 231  ? -38.079 76.102  77.981  1.00 13.57 ?  229  THR A O     1 
ATOM   1606  C CB    . THR A 1 231  ? -35.234 77.791  78.069  1.00 14.27 ?  229  THR A CB    1 
ATOM   1607  O OG1   . THR A 1 231  ? -35.431 77.188  76.785  1.00 15.57 ?  229  THR A OG1   1 
ATOM   1608  C CG2   . THR A 1 231  ? -33.768 77.595  78.476  1.00 14.72 ?  229  THR A CG2   1 
ATOM   1609  N N     . ALA A 1 232  ? -38.172 78.316  78.445  1.00 12.99 ?  230  ALA A N     1 
ATOM   1610  C CA    . ALA A 1 232  ? -39.454 78.493  77.773  1.00 12.95 ?  230  ALA A CA    1 
ATOM   1611  C C     . ALA A 1 232  ? -39.343 78.137  76.299  1.00 16.18 ?  230  ALA A C     1 
ATOM   1612  O O     . ALA A 1 232  ? -40.247 77.504  75.735  1.00 16.59 ?  230  ALA A O     1 
ATOM   1613  C CB    . ALA A 1 232  ? -39.950 79.924  77.956  1.00 14.59 ?  230  ALA A CB    1 
ATOM   1614  N N     . ALA A 1 233  ? -38.232 78.509  75.658  1.00 15.09 ?  231  ALA A N     1 
ATOM   1615  C CA    . ALA A 1 233  ? -38.083 78.204  74.235  1.00 16.35 ?  231  ALA A CA    1 
ATOM   1616  C C     . ALA A 1 233  ? -38.002 76.705  73.990  1.00 15.64 ?  231  ALA A C     1 
ATOM   1617  O O     . ALA A 1 233  ? -38.548 76.212  72.993  1.00 17.52 ?  231  ALA A O     1 
ATOM   1618  C CB    . ALA A 1 233  ? -36.854 78.911  73.660  1.00 19.68 ?  231  ALA A CB    1 
ATOM   1619  N N     . ASP A 1 234  ? -37.325 75.958  74.874  1.00 15.45 ?  232  ASP A N     1 
ATOM   1620  C CA    . ASP A 1 234  ? -37.292 74.501  74.764  1.00 16.35 ?  232  ASP A CA    1 
ATOM   1621  C C     . ASP A 1 234  ? -38.697 73.943  74.821  1.00 15.73 ?  232  ASP A C     1 
ATOM   1622  O O     . ASP A 1 234  ? -39.059 73.041  74.061  1.00 17.36 ?  232  ASP A O     1 
ATOM   1623  C CB    . ASP A 1 234  ? -36.510 73.860  75.918  1.00 22.45 ?  232  ASP A CB    1 
ATOM   1624  C CG    . ASP A 1 234  ? -35.020 73.996  75.808  1.00 29.42 ?  232  ASP A CG    1 
ATOM   1625  O OD1   . ASP A 1 234  ? -34.489 74.244  74.709  1.00 26.43 ?  232  ASP A OD1   1 
ATOM   1626  O OD2   . ASP A 1 234  ? -34.375 73.804  76.871  1.00 29.37 ?  232  ASP A OD2   1 
ATOM   1627  N N     . ALA A 1 235  ? -39.472 74.406  75.797  1.00 14.04 ?  233  ALA A N     1 
ATOM   1628  C CA    . ALA A 1 235  ? -40.806 73.863  75.987  1.00 13.20 ?  233  ALA A CA    1 
ATOM   1629  C C     . ALA A 1 235  ? -41.668 74.154  74.777  1.00 16.82 ?  233  ALA A C     1 
ATOM   1630  O O     . ALA A 1 235  ? -42.465 73.308  74.354  1.00 15.42 ?  233  ALA A O     1 
ATOM   1631  C CB    . ALA A 1 235  ? -41.429 74.447  77.258  1.00 15.02 ?  233  ALA A CB    1 
ATOM   1632  N N     . GLU A 1 236  ? -41.516 75.346  74.207  1.00 15.69 ?  234  GLU A N     1 
ATOM   1633  C CA    . GLU A 1 236  ? -42.272 75.690  73.012  1.00 13.11 ?  234  GLU A CA    1 
ATOM   1634  C C     . GLU A 1 236  ? -41.833 74.838  71.823  1.00 15.59 ?  234  GLU A C     1 
ATOM   1635  O O     . GLU A 1 236  ? -42.667 74.448  70.994  1.00 15.28 ?  234  GLU A O     1 
ATOM   1636  C CB    . GLU A 1 236  ? -42.119 77.190  72.724  1.00 16.20 ?  234  GLU A CB    1 
ATOM   1637  C CG    . GLU A 1 236  ? -42.965 77.692  71.571  1.00 21.36 ?  234  GLU A CG    1 
ATOM   1638  C CD    . GLU A 1 236  ? -44.474 77.482  71.768  1.00 30.51 ?  234  GLU A CD    1 
ATOM   1639  O OE1   . GLU A 1 236  ? -44.937 77.318  72.923  1.00 30.75 ?  234  GLU A OE1   1 
ATOM   1640  O OE2   . GLU A 1 236  ? -45.205 77.486  70.750  1.00 28.43 ?  234  GLU A OE2   1 
ATOM   1641  N N     . ARG A 1 237  ? -40.537 74.528  71.727  1.00 15.18 ?  235  ARG A N     1 
ATOM   1642  C CA    . ARG A 1 237  ? -40.052 73.626  70.684  1.00 16.42 ?  235  ARG A CA    1 
ATOM   1643  C C     . ARG A 1 237  ? -40.662 72.237  70.829  1.00 18.64 ?  235  ARG A C     1 
ATOM   1644  O O     . ARG A 1 237  ? -41.136 71.651  69.851  1.00 15.51 ?  235  ARG A O     1 
ATOM   1645  C CB    . ARG A 1 237  ? -38.516 73.554  70.707  1.00 19.02 ?  235  ARG A CB    1 
ATOM   1646  C CG    . ARG A 1 237  ? -37.930 72.475  69.804  1.00 25.26 ?  235  ARG A CG    1 
ATOM   1647  C CD    . ARG A 1 237  ? -36.414 72.619  69.665  1.00 30.73 ?  235  ARG A CD    1 
ATOM   1648  N NE    . ARG A 1 237  ? -35.741 72.523  70.956  1.00 30.25 ?  235  ARG A NE    1 
ATOM   1649  C CZ    . ARG A 1 237  ? -35.304 71.393  71.494  1.00 33.20 ?  235  ARG A CZ    1 
ATOM   1650  N NH1   . ARG A 1 237  ? -35.449 70.230  70.877  1.00 37.05 ?  235  ARG A NH1   1 
ATOM   1651  N NH2   . ARG A 1 237  ? -34.699 71.431  72.679  1.00 38.08 ?  235  ARG A NH2   1 
ATOM   1652  N N     . TYR A 1 238  ? -40.667 71.687  72.043  1.00 14.94 ?  236  TYR A N     1 
ATOM   1653  C CA    . TYR A 1 238  ? -41.266 70.374  72.227  1.00 12.87 ?  236  TYR A CA    1 
ATOM   1654  C C     . TYR A 1 238  ? -42.761 70.415  71.941  1.00 13.02 ?  236  TYR A C     1 
ATOM   1655  O O     . TYR A 1 238  ? -43.309 69.468  71.364  1.00 15.30 ?  236  TYR A O     1 
ATOM   1656  C CB    . TYR A 1 238  ? -41.004 69.864  73.644  1.00 14.44 ?  236  TYR A CB    1 
ATOM   1657  C CG    . TYR A 1 238  ? -39.573 69.473  73.910  1.00 16.25 ?  236  TYR A CG    1 
ATOM   1658  C CD1   . TYR A 1 238  ? -38.855 68.705  73.008  1.00 19.90 ?  236  TYR A CD1   1 
ATOM   1659  C CD2   . TYR A 1 238  ? -38.946 69.866  75.081  1.00 16.18 ?  236  TYR A CD2   1 
ATOM   1660  C CE1   . TYR A 1 238  ? -37.539 68.341  73.259  1.00 21.77 ?  236  TYR A CE1   1 
ATOM   1661  C CE2   . TYR A 1 238  ? -37.636 69.499  75.349  1.00 19.04 ?  236  TYR A CE2   1 
ATOM   1662  C CZ    . TYR A 1 238  ? -36.940 68.742  74.438  1.00 20.93 ?  236  TYR A CZ    1 
ATOM   1663  O OH    . TYR A 1 238  ? -35.638 68.387  74.712  1.00 24.88 ?  236  TYR A OH    1 
ATOM   1664  N N     . TYR A 1 239  ? -43.432 71.515  72.307  1.00 14.86 ?  237  TYR A N     1 
ATOM   1665  C CA    . TYR A 1 239  ? -44.856 71.645  72.017  1.00 13.68 ?  237  TYR A CA    1 
ATOM   1666  C C     . TYR A 1 239  ? -45.119 71.592  70.519  1.00 15.71 ?  237  TYR A C     1 
ATOM   1667  O O     . TYR A 1 239  ? -45.982 70.834  70.054  1.00 13.48 ?  237  TYR A O     1 
ATOM   1668  C CB    . TYR A 1 239  ? -45.430 72.941  72.591  1.00 15.27 ?  237  TYR A CB    1 
ATOM   1669  C CG    . TYR A 1 239  ? -46.890 73.077  72.234  1.00 15.84 ?  237  TYR A CG    1 
ATOM   1670  C CD1   . TYR A 1 239  ? -47.289 73.652  71.031  1.00 17.06 ?  237  TYR A CD1   1 
ATOM   1671  C CD2   . TYR A 1 239  ? -47.871 72.561  73.059  1.00 15.88 ?  237  TYR A CD2   1 
ATOM   1672  C CE1   . TYR A 1 239  ? -48.622 73.730  70.677  1.00 21.85 ?  237  TYR A CE1   1 
ATOM   1673  C CE2   . TYR A 1 239  ? -49.203 72.656  72.723  1.00 17.25 ?  237  TYR A CE2   1 
ATOM   1674  C CZ    . TYR A 1 239  ? -49.570 73.226  71.533  1.00 20.47 ?  237  TYR A CZ    1 
ATOM   1675  O OH    . TYR A 1 239  ? -50.899 73.315  71.190  1.00 24.55 ?  237  TYR A OH    1 
ATOM   1676  N N     . ARG A 1 240  ? -44.432 72.438  69.745  1.00 13.83 ?  238  ARG A N     1 
ATOM   1677  C CA    . ARG A 1 240  ? -44.757 72.457  68.322  1.00 12.71 ?  238  ARG A CA    1 
ATOM   1678  C C     . ARG A 1 240  ? -44.333 71.150  67.658  1.00 12.27 ?  238  ARG A C     1 
ATOM   1679  O O     . ARG A 1 240  ? -44.939 70.742  66.657  1.00 15.67 ?  238  ARG A O     1 
ATOM   1680  C CB    . ARG A 1 240  ? -44.137 73.679  67.631  1.00 19.43 ?  238  ARG A CB    1 
ATOM   1681  C CG    . ARG A 1 240  ? -42.663 73.642  67.553  1.00 16.24 ?  238  ARG A CG    1 
ATOM   1682  C CD    . ARG A 1 240  ? -42.101 74.766  66.651  1.00 15.17 ?  238  ARG A CD    1 
ATOM   1683  N NE    . ARG A 1 240  ? -40.663 74.892  66.861  1.00 19.14 ?  238  ARG A NE    1 
ATOM   1684  C CZ    . ARG A 1 240  ? -40.107 75.674  67.781  1.00 22.21 ?  238  ARG A CZ    1 
ATOM   1685  N NH1   . ARG A 1 240  ? -40.831 76.501  68.522  1.00 19.67 ?  238  ARG A NH1   1 
ATOM   1686  N NH2   . ARG A 1 240  ? -38.787 75.634  67.954  1.00 25.44 ?  238  ARG A NH2   1 
ATOM   1687  N N     . ASP A 1 241  ? -43.344 70.448  68.222  1.00 13.85 ?  239  ASP A N     1 
ATOM   1688  C CA    . ASP A 1 241  ? -42.992 69.121  67.723  1.00 13.54 ?  239  ASP A CA    1 
ATOM   1689  C C     . ASP A 1 241  ? -44.107 68.109  67.994  1.00 16.25 ?  239  ASP A C     1 
ATOM   1690  O O     . ASP A 1 241  ? -44.451 67.310  67.116  1.00 16.54 ?  239  ASP A O     1 
ATOM   1691  C CB    . ASP A 1 241  ? -41.675 68.652  68.337  1.00 18.29 ?  239  ASP A CB    1 
ATOM   1692  C CG    . ASP A 1 241  ? -40.477 69.485  67.873  1.00 23.88 ?  239  ASP A CG    1 
ATOM   1693  O OD1   . ASP A 1 241  ? -40.631 70.328  66.952  1.00 29.80 ?  239  ASP A OD1   1 
ATOM   1694  O OD2   . ASP A 1 241  ? -39.377 69.308  68.445  1.00 32.07 ?  239  ASP A OD2   1 
ATOM   1695  N N     . TYR A 1 242  ? -44.689 68.124  69.197  1.00 14.47 ?  240  TYR A N     1 
ATOM   1696  C CA    . TYR A 1 242  ? -45.830 67.246  69.458  1.00 14.02 ?  240  TYR A CA    1 
ATOM   1697  C C     . TYR A 1 242  ? -47.009 67.586  68.555  1.00 12.35 ?  240  TYR A C     1 
ATOM   1698  O O     . TYR A 1 242  ? -47.693 66.686  68.048  1.00 12.82 ?  240  TYR A O     1 
ATOM   1699  C CB    . TYR A 1 242  ? -46.273 67.353  70.914  1.00 12.89 ?  240  TYR A CB    1 
ATOM   1700  C CG    . TYR A 1 242  ? -45.395 66.708  71.957  1.00 11.69 ?  240  TYR A CG    1 
ATOM   1701  C CD1   . TYR A 1 242  ? -44.868 65.436  71.786  1.00 14.76 ?  240  TYR A CD1   1 
ATOM   1702  C CD2   . TYR A 1 242  ? -45.164 67.359  73.161  1.00 13.38 ?  240  TYR A CD2   1 
ATOM   1703  C CE1   . TYR A 1 242  ? -44.087 64.849  72.782  1.00 16.45 ?  240  TYR A CE1   1 
ATOM   1704  C CE2   . TYR A 1 242  ? -44.398 66.786  74.149  1.00 12.99 ?  240  TYR A CE2   1 
ATOM   1705  C CZ    . TYR A 1 242  ? -43.867 65.544  73.958  1.00 11.60 ?  240  TYR A CZ    1 
ATOM   1706  O OH    . TYR A 1 242  ? -43.101 64.987  74.961  1.00 13.48 ?  240  TYR A OH    1 
ATOM   1707  N N     . GLU A 1 243  ? -47.281 68.880  68.367  1.00 12.08 ?  241  GLU A N     1 
ATOM   1708  C CA    . GLU A 1 243  ? -48.408 69.282  67.532  1.00 11.28 ?  241  GLU A CA    1 
ATOM   1709  C C     . GLU A 1 243  ? -48.216 68.794  66.104  1.00 13.35 ?  241  GLU A C     1 
ATOM   1710  O O     . GLU A 1 243  ? -49.133 68.220  65.505  1.00 13.57 ?  241  GLU A O     1 
ATOM   1711  C CB    . GLU A 1 243  ? -48.580 70.802  67.580  1.00 14.50 ?  241  GLU A CB    1 
ATOM   1712  C CG    . GLU A 1 243  ? -49.748 71.364  66.795  1.00 15.78 ?  241  GLU A CG    1 
ATOM   1713  C CD    . GLU A 1 243  ? -49.676 72.888  66.646  1.00 21.02 ?  241  GLU A CD    1 
ATOM   1714  O OE1   . GLU A 1 243  ? -48.556 73.464  66.724  1.00 27.95 ?  241  GLU A OE1   1 
ATOM   1715  O OE2   . GLU A 1 243  ? -50.725 73.517  66.415  1.00 19.21 ?  241  GLU A OE2   1 
ATOM   1716  N N     . SER A 1 244  ? -47.010 68.968  65.554  1.00 13.63 ?  242  SER A N     1 
ATOM   1717  C CA    . SER A 1 244  ? -46.789 68.510  64.185  1.00 13.70 ?  242  SER A CA    1 
ATOM   1718  C C     . SER A 1 244  ? -46.868 66.986  64.093  1.00 14.78 ?  242  SER A C     1 
ATOM   1719  O O     . SER A 1 244  ? -47.382 66.448  63.107  1.00 16.27 ?  242  SER A O     1 
ATOM   1720  C CB    . SER A 1 244  ? -45.442 69.025  63.665  1.00 16.60 ?  242  SER A CB    1 
ATOM   1721  O OG    . SER A 1 244  ? -44.353 68.484  64.386  1.00 21.42 ?  242  SER A OG    1 
ATOM   1722  N N     . ALA A 1 245  ? -46.387 66.269  65.115  1.00 12.88 ?  243  ALA A N     1 
ATOM   1723  C CA    . ALA A 1 245  ? -46.473 64.815  65.082  1.00 11.71 ?  243  ALA A CA    1 
ATOM   1724  C C     . ALA A 1 245  ? -47.929 64.340  65.157  1.00 11.45 ?  243  ALA A C     1 
ATOM   1725  O O     . ALA A 1 245  ? -48.300 63.365  64.497  1.00 12.65 ?  243  ALA A O     1 
ATOM   1726  C CB    . ALA A 1 245  ? -45.642 64.210  66.217  1.00 13.49 ?  243  ALA A CB    1 
ATOM   1727  N N     . ILE A 1 246  ? -48.759 64.986  65.986  1.00 11.99 ?  244  ILE A N     1 
ATOM   1728  C CA    . ILE A 1 246  ? -50.167 64.597  66.048  1.00 11.62 ?  244  ILE A CA    1 
ATOM   1729  C C     . ILE A 1 246  ? -50.834 64.732  64.684  1.00 12.98 ?  244  ILE A C     1 
ATOM   1730  O O     . ILE A 1 246  ? -51.582 63.848  64.266  1.00 12.57 ?  244  ILE A O     1 
ATOM   1731  C CB    . ILE A 1 246  ? -50.900 65.404  67.132  1.00 10.54 ?  244  ILE A CB    1 
ATOM   1732  C CG1   . ILE A 1 246  ? -50.435 64.928  68.502  1.00 12.90 ?  244  ILE A CG1   1 
ATOM   1733  C CG2   . ILE A 1 246  ? -52.428 65.225  67.005  1.00 13.28 ?  244  ILE A CG2   1 
ATOM   1734  C CD1   . ILE A 1 246  ? -50.879 65.837  69.640  1.00 12.24 ?  244  ILE A CD1   1 
ATOM   1735  N N     . HIS A 1 247  ? -50.569 65.823  63.960  1.00 12.46 ?  245  HIS A N     1 
ATOM   1736  C CA    . HIS A 1 247  ? -51.116 65.937  62.610  1.00 12.60 ?  245  HIS A CA    1 
ATOM   1737  C C     . HIS A 1 247  ? -50.662 64.778  61.727  1.00 12.87 ?  245  HIS A C     1 
ATOM   1738  O O     . HIS A 1 247  ? -51.473 64.172  61.019  1.00 13.92 ?  245  HIS A O     1 
ATOM   1739  C CB    . HIS A 1 247  ? -50.715 67.271  61.975  1.00 13.99 ?  245  HIS A CB    1 
ATOM   1740  C CG    . HIS A 1 247  ? -51.457 68.449  62.519  1.00 14.18 ?  245  HIS A CG    1 
ATOM   1741  N ND1   . HIS A 1 247  ? -52.810 68.624  62.339  1.00 15.81 ?  245  HIS A ND1   1 
ATOM   1742  C CD2   . HIS A 1 247  ? -51.023 69.537  63.203  1.00 17.29 ?  245  HIS A CD2   1 
ATOM   1743  C CE1   . HIS A 1 247  ? -53.185 69.759  62.906  1.00 19.94 ?  245  HIS A CE1   1 
ATOM   1744  N NE2   . HIS A 1 247  ? -52.120 70.324  63.448  1.00 18.20 ?  245  HIS A NE2   1 
ATOM   1745  N N     . ALA A 1 248  ? -49.362 64.465  61.734  1.00 14.19 ?  246  ALA A N     1 
ATOM   1746  C CA    . ALA A 1 248  ? -48.882 63.387  60.877  1.00 13.94 ?  246  ALA A CA    1 
ATOM   1747  C C     . ALA A 1 248  ? -49.497 62.047  61.268  1.00 14.44 ?  246  ALA A C     1 
ATOM   1748  O O     . ALA A 1 248  ? -49.910 61.268  60.399  1.00 15.03 ?  246  ALA A O     1 
ATOM   1749  C CB    . ALA A 1 248  ? -47.354 63.312  60.935  1.00 14.53 ?  246  ALA A CB    1 
ATOM   1750  N N     . ILE A 1 249  ? -49.560 61.760  62.575  1.00 12.92 ?  247  ILE A N     1 
ATOM   1751  C CA    . ILE A 1 249  ? -50.117 60.498  63.049  1.00 12.54 ?  247  ILE A CA    1 
ATOM   1752  C C     . ILE A 1 249  ? -51.609 60.429  62.754  1.00 13.64 ?  247  ILE A C     1 
ATOM   1753  O O     . ILE A 1 249  ? -52.136 59.376  62.370  1.00 12.60 ?  247  ILE A O     1 
ATOM   1754  C CB    . ILE A 1 249  ? -49.828 60.333  64.551  1.00 12.33 ?  247  ILE A CB    1 
ATOM   1755  C CG1   . ILE A 1 249  ? -48.314 60.265  64.785  1.00 11.98 ?  247  ILE A CG1   1 
ATOM   1756  C CG2   . ILE A 1 249  ? -50.539 59.092  65.115  1.00 14.15 ?  247  ILE A CG2   1 
ATOM   1757  C CD1   . ILE A 1 249  ? -47.915 60.506  66.263  1.00 13.71 ?  247  ILE A CD1   1 
ATOM   1758  N N     . GLY A 1 250  ? -52.315 61.543  62.937  1.00 12.33 ?  248  GLY A N     1 
ATOM   1759  C CA    . GLY A 1 250  ? -53.747 61.543  62.687  1.00 12.92 ?  248  GLY A CA    1 
ATOM   1760  C C     . GLY A 1 250  ? -54.084 61.410  61.214  1.00 13.79 ?  248  GLY A C     1 
ATOM   1761  O O     . GLY A 1 250  ? -55.032 60.713  60.849  1.00 14.63 ?  248  GLY A O     1 
ATOM   1762  N N     . LYS A 1 251  ? -53.323 62.086  60.349  1.00 13.77 ?  249  LYS A N     1 
ATOM   1763  C CA    . LYS A 1 251  ? -53.511 61.886  58.915  1.00 14.35 ?  249  LYS A CA    1 
ATOM   1764  C C     . LYS A 1 251  ? -53.318 60.426  58.536  1.00 14.97 ?  249  LYS A C     1 
ATOM   1765  O O     . LYS A 1 251  ? -54.071 59.882  57.714  1.00 17.17 ?  249  LYS A O     1 
ATOM   1766  C CB    . LYS A 1 251  ? -52.527 62.745  58.126  1.00 14.63 ?  249  LYS A CB    1 
ATOM   1767  C CG    . LYS A 1 251  ? -52.781 64.221  58.144  1.00 17.18 ?  249  LYS A CG    1 
ATOM   1768  C CD    . LYS A 1 251  ? -51.523 64.904  57.631  1.00 18.04 ?  249  LYS A CD    1 
ATOM   1769  C CE    . LYS A 1 251  ? -51.656 66.407  57.613  1.00 19.85 ?  249  LYS A CE    1 
ATOM   1770  N NZ    . LYS A 1 251  ? -50.416 66.975  56.971  1.00 19.07 ?  249  LYS A NZ    1 
ATOM   1771  N N     . ALA A 1 252  ? -52.291 59.786  59.107  1.00 15.82 ?  250  ALA A N     1 
ATOM   1772  C CA    . ALA A 1 252  ? -51.999 58.389  58.806  1.00 14.83 ?  250  ALA A CA    1 
ATOM   1773  C C     . ALA A 1 252  ? -53.030 57.458  59.421  1.00 17.28 ?  250  ALA A C     1 
ATOM   1774  O O     . ALA A 1 252  ? -53.385 56.435  58.822  1.00 18.38 ?  250  ALA A O     1 
ATOM   1775  C CB    . ALA A 1 252  ? -50.600 58.026  59.317  1.00 16.70 ?  250  ALA A CB    1 
ATOM   1776  N N     . SER A 1 253  ? -53.502 57.772  60.628  1.00 14.27 ?  251  SER A N     1 
ATOM   1777  C CA    . SER A 1 253  ? -54.508 56.919  61.250  1.00 16.03 ?  251  SER A CA    1 
ATOM   1778  C C     . SER A 1 253  ? -55.717 56.764  60.346  1.00 16.72 ?  251  SER A C     1 
ATOM   1779  O O     . SER A 1 253  ? -56.272 55.667  60.222  1.00 16.80 ?  251  SER A O     1 
ATOM   1780  C CB    . SER A 1 253  ? -54.930 57.501  62.592  1.00 14.53 ?  251  SER A CB    1 
ATOM   1781  O OG    . SER A 1 253  ? -55.950 56.689  63.147  1.00 16.25 ?  251  SER A OG    1 
ATOM   1782  N N     . ALA A 1 254  ? -56.139 57.859  59.725  1.00 16.56 ?  252  ALA A N     1 
ATOM   1783  C CA    . ALA A 1 254  ? -57.186 57.849  58.710  1.00 18.36 ?  252  ALA A CA    1 
ATOM   1784  C C     . ALA A 1 254  ? -58.453 57.173  59.220  1.00 19.70 ?  252  ALA A C     1 
ATOM   1785  O O     . ALA A 1 254  ? -59.055 56.334  58.546  1.00 20.58 ?  252  ALA A O     1 
ATOM   1786  C CB    . ALA A 1 254  ? -56.679 57.187  57.427  1.00 17.52 ?  252  ALA A CB    1 
ATOM   1787  N N     . GLY A 1 255  ? -58.857 57.541  60.434  1.00 16.15 ?  253  GLY A N     1 
ATOM   1788  C CA    . GLY A 1 255  ? -60.104 57.043  60.981  1.00 19.05 ?  253  GLY A CA    1 
ATOM   1789  C C     . GLY A 1 255  ? -60.072 55.648  61.570  1.00 20.18 ?  253  GLY A C     1 
ATOM   1790  O O     . GLY A 1 255  ? -61.140 55.103  61.871  1.00 20.22 ?  253  GLY A O     1 
ATOM   1791  N N     . ARG A 1 256  ? -58.893 55.060  61.779  1.00 16.57 ?  254  ARG A N     1 
ATOM   1792  C CA    . ARG A 1 256  ? -58.821 53.728  62.368  1.00 17.81 ?  254  ARG A CA    1 
ATOM   1793  C C     . ARG A 1 256  ? -59.205 53.713  63.838  1.00 18.01 ?  254  ARG A C     1 
ATOM   1794  O O     . ARG A 1 256  ? -59.481 52.636  64.378  1.00 18.80 ?  254  ARG A O     1 
ATOM   1795  C CB    . ARG A 1 256  ? -57.418 53.139  62.201  1.00 16.76 ?  254  ARG A CB    1 
ATOM   1796  C CG    . ARG A 1 256  ? -57.188 52.487  60.836  1.00 20.25 ?  254  ARG A CG    1 
ATOM   1797  C CD    . ARG A 1 256  ? -55.765 51.988  60.692  1.00 18.66 ?  254  ARG A CD    1 
ATOM   1798  N NE    . ARG A 1 256  ? -54.821 53.085  60.486  1.00 17.53 ?  254  ARG A NE    1 
ATOM   1799  C CZ    . ARG A 1 256  ? -53.503 52.939  60.459  1.00 19.24 ?  254  ARG A CZ    1 
ATOM   1800  N NH1   . ARG A 1 256  ? -52.930 51.776  60.731  1.00 21.19 ?  254  ARG A NH1   1 
ATOM   1801  N NH2   . ARG A 1 256  ? -52.737 53.984  60.153  1.00 19.86 ?  254  ARG A NH2   1 
ATOM   1802  N N     . GLY A 1 257  ? -59.210 54.865  64.504  1.00 17.41 ?  255  GLY A N     1 
ATOM   1803  C CA    . GLY A 1 257  ? -59.610 54.897  65.895  1.00 17.66 ?  255  GLY A CA    1 
ATOM   1804  C C     . GLY A 1 257  ? -58.457 54.653  66.845  1.00 15.53 ?  255  GLY A C     1 
ATOM   1805  O O     . GLY A 1 257  ? -57.310 54.405  66.458  1.00 16.66 ?  255  GLY A O     1 
ATOM   1806  N N     . ILE A 1 258  ? -58.786 54.694  68.135  1.00 14.40 ?  256  ILE A N     1 
ATOM   1807  C CA    . ILE A 1 258  ? -57.741 54.728  69.149  1.00 14.01 ?  256  ILE A CA    1 
ATOM   1808  C C     . ILE A 1 258  ? -57.150 53.362  69.464  1.00 15.33 ?  256  ILE A C     1 
ATOM   1809  O O     . ILE A 1 258  ? -56.059 53.300  70.049  1.00 15.82 ?  256  ILE A O     1 
ATOM   1810  C CB    . ILE A 1 258  ? -58.255 55.384  70.439  1.00 14.21 ?  256  ILE A CB    1 
ATOM   1811  C CG1   . ILE A 1 258  ? -59.367 54.537  71.074  1.00 14.25 ?  256  ILE A CG1   1 
ATOM   1812  C CG2   . ILE A 1 258  ? -58.693 56.833  70.171  1.00 14.99 ?  256  ILE A CG2   1 
ATOM   1813  C CD1   . ILE A 1 258  ? -59.907 55.146  72.361  1.00 14.76 ?  256  ILE A CD1   1 
ATOM   1814  N N     . TYR A 1 259  ? -57.819 52.262  69.100  1.00 16.49 ?  257  TYR A N     1 
ATOM   1815  C CA    . TYR A 1 259  ? -57.277 50.933  69.378  1.00 14.33 ?  257  TYR A CA    1 
ATOM   1816  C C     . TYR A 1 259  ? -56.508 50.351  68.203  1.00 18.71 ?  257  TYR A C     1 
ATOM   1817  O O     . TYR A 1 259  ? -55.362 49.924  68.372  1.00 19.49 ?  257  TYR A O     1 
ATOM   1818  C CB    . TYR A 1 259  ? -58.399 49.974  69.801  1.00 16.65 ?  257  TYR A CB    1 
ATOM   1819  C CG    . TYR A 1 259  ? -59.216 50.543  70.936  1.00 15.67 ?  257  TYR A CG    1 
ATOM   1820  C CD1   . TYR A 1 259  ? -58.635 50.800  72.168  1.00 15.57 ?  257  TYR A CD1   1 
ATOM   1821  C CD2   . TYR A 1 259  ? -60.562 50.859  70.765  1.00 18.34 ?  257  TYR A CD2   1 
ATOM   1822  C CE1   . TYR A 1 259  ? -59.359 51.351  73.205  1.00 18.96 ?  257  TYR A CE1   1 
ATOM   1823  C CE2   . TYR A 1 259  ? -61.296 51.406  71.797  1.00 17.54 ?  257  TYR A CE2   1 
ATOM   1824  C CZ    . TYR A 1 259  ? -60.690 51.646  73.018  1.00 18.46 ?  257  TYR A CZ    1 
ATOM   1825  O OH    . TYR A 1 259  ? -61.419 52.208  74.040  1.00 18.71 ?  257  TYR A OH    1 
ATOM   1826  N N     . GLU A 1 260  ? -57.106 50.337  67.012  1.00 15.23 ?  258  GLU A N     1 
ATOM   1827  C CA    . GLU A 1 260  ? -56.383 49.836  65.847  1.00 20.50 ?  258  GLU A CA    1 
ATOM   1828  C C     . GLU A 1 260  ? -55.328 50.831  65.383  1.00 19.31 ?  258  GLU A C     1 
ATOM   1829  O O     . GLU A 1 260  ? -54.236 50.432  64.955  1.00 22.31 ?  258  GLU A O     1 
ATOM   1830  C CB    . GLU A 1 260  ? -57.343 49.516  64.700  1.00 23.51 ?  258  GLU A CB    1 
ATOM   1831  C CG    . GLU A 1 260  ? -56.597 48.928  63.505  1.00 27.55 ?  258  GLU A CG    1 
ATOM   1832  C CD    . GLU A 1 260  ? -57.419 48.831  62.232  1.00 32.46 ?  258  GLU A CD    1 
ATOM   1833  O OE1   . GLU A 1 260  ? -58.669 48.901  62.293  1.00 32.65 ?  258  GLU A OE1   1 
ATOM   1834  O OE2   . GLU A 1 260  ? -56.792 48.675  61.161  1.00 28.38 ?  258  GLU A OE2   1 
ATOM   1835  N N     . GLY A 1 261  ? -55.626 52.124  65.473  1.00 16.32 ?  259  GLY A N     1 
ATOM   1836  C CA    . GLY A 1 261  ? -54.785 53.136  64.882  1.00 15.67 ?  259  GLY A CA    1 
ATOM   1837  C C     . GLY A 1 261  ? -53.720 53.633  65.835  1.00 16.47 ?  259  GLY A C     1 
ATOM   1838  O O     . GLY A 1 261  ? -53.758 53.379  67.044  1.00 15.69 ?  259  GLY A O     1 
ATOM   1839  N N     . PRO A 1 262  ? -52.746 54.354  65.290  1.00 14.12 ?  260  PRO A N     1 
ATOM   1840  C CA    . PRO A 1 262  ? -51.608 54.815  66.090  1.00 13.82 ?  260  PRO A CA    1 
ATOM   1841  C C     . PRO A 1 262  ? -51.977 55.978  66.995  1.00 14.52 ?  260  PRO A C     1 
ATOM   1842  O O     . PRO A 1 262  ? -52.977 56.664  66.802  1.00 15.68 ?  260  PRO A O     1 
ATOM   1843  C CB    . PRO A 1 262  ? -50.594 55.255  65.027  1.00 14.64 ?  260  PRO A CB    1 
ATOM   1844  C CG    . PRO A 1 262  ? -51.458 55.647  63.845  1.00 16.66 ?  260  PRO A CG    1 
ATOM   1845  C CD    . PRO A 1 262  ? -52.607 54.693  63.864  1.00 15.66 ?  260  PRO A CD    1 
ATOM   1846  N N     . GLY A 1 263  ? -51.134 56.187  68.002  1.00 12.08 ?  261  GLY A N     1 
ATOM   1847  C CA    . GLY A 1 263  ? -51.275 57.334  68.870  1.00 13.76 ?  261  GLY A CA    1 
ATOM   1848  C C     . GLY A 1 263  ? -49.938 57.955  69.209  1.00 12.32 ?  261  GLY A C     1 
ATOM   1849  O O     . GLY A 1 263  ? -48.916 57.606  68.602  1.00 12.88 ?  261  GLY A O     1 
ATOM   1850  N N     . ILE A 1 264  ? -49.939 58.892  70.149  1.00 12.95 ?  262  ILE A N     1 
ATOM   1851  C CA    . ILE A 1 264  ? -48.718 59.577  70.551  1.00 10.76 ?  262  ILE A CA    1 
ATOM   1852  C C     . ILE A 1 264  ? -48.553 59.483  72.064  1.00 13.11 ?  262  ILE A C     1 
ATOM   1853  O O     . ILE A 1 264  ? -49.531 59.361  72.809  1.00 12.88 ?  262  ILE A O     1 
ATOM   1854  C CB    . ILE A 1 264  ? -48.728 61.053  70.085  1.00 11.80 ?  262  ILE A CB    1 
ATOM   1855  C CG1   . ILE A 1 264  ? -47.311 61.641  70.118  1.00 12.97 ?  262  ILE A CG1   1 
ATOM   1856  C CG2   . ILE A 1 264  ? -49.732 61.904  70.918  1.00 12.49 ?  262  ILE A CG2   1 
ATOM   1857  C CD1   . ILE A 1 264  ? -47.249 63.064  69.567  1.00 15.19 ?  262  ILE A CD1   1 
ATOM   1858  N N     . SER A 1 265  ? -47.300 59.541  72.510  1.00 10.96 ?  263  SER A N     1 
ATOM   1859  C CA    . SER A 1 265  ? -46.946 59.631  73.916  1.00 10.99 ?  263  SER A CA    1 
ATOM   1860  C C     . SER A 1 265  ? -46.207 60.939  74.153  1.00 14.47 ?  263  SER A C     1 
ATOM   1861  O O     . SER A 1 265  ? -45.408 61.370  73.310  1.00 15.79 ?  263  SER A O     1 
ATOM   1862  C CB    . SER A 1 265  ? -46.069 58.452  74.370  1.00 14.06 ?  263  SER A CB    1 
ATOM   1863  O OG    . SER A 1 265  ? -46.827 57.250  74.380  1.00 16.25 ?  263  SER A OG    1 
ATOM   1864  N N     . ILE A 1 266  ? -46.491 61.579  75.287  1.00 12.09 ?  264  ILE A N     1 
ATOM   1865  C CA    . ILE A 1 266  ? -45.882 62.856  75.638  1.00 11.20 ?  264  ILE A CA    1 
ATOM   1866  C C     . ILE A 1 266  ? -45.325 62.759  77.048  1.00 12.85 ?  264  ILE A C     1 
ATOM   1867  O O     . ILE A 1 266  ? -45.760 61.943  77.861  1.00 12.18 ?  264  ILE A O     1 
ATOM   1868  C CB    . ILE A 1 266  ? -46.865 64.044  75.554  1.00 12.75 ?  264  ILE A CB    1 
ATOM   1869  C CG1   . ILE A 1 266  ? -47.961 63.939  76.620  1.00 13.99 ?  264  ILE A CG1   1 
ATOM   1870  C CG2   . ILE A 1 266  ? -47.474 64.146  74.147  1.00 13.86 ?  264  ILE A CG2   1 
ATOM   1871  C CD1   . ILE A 1 266  ? -48.789 65.220  76.753  1.00 16.88 ?  264  ILE A CD1   1 
ATOM   1872  N N     . LYS A 1 267  ? -44.356 63.617  77.334  1.00 11.90 ?  265  LYS A N     1 
ATOM   1873  C CA    . LYS A 1 267  ? -43.822 63.774  78.680  1.00 10.93 ?  265  LYS A CA    1 
ATOM   1874  C C     . LYS A 1 267  ? -44.131 65.182  79.165  1.00 12.49 ?  265  LYS A C     1 
ATOM   1875  O O     . LYS A 1 267  ? -43.808 66.157  78.482  1.00 12.31 ?  265  LYS A O     1 
ATOM   1876  C CB    . LYS A 1 267  ? -42.306 63.513  78.708  1.00 13.89 ?  265  LYS A CB    1 
ATOM   1877  C CG    . LYS A 1 267  ? -41.958 62.025  78.760  1.00 17.80 ?  265  LYS A CG    1 
ATOM   1878  C CD    . LYS A 1 267  ? -40.449 61.830  78.780  1.00 18.26 ?  265  LYS A CD    1 
ATOM   1879  C CE    . LYS A 1 267  ? -40.071 60.370  78.975  1.00 22.81 ?  265  LYS A CE    1 
ATOM   1880  N NZ    . LYS A 1 267  ? -40.632 59.492  77.902  1.00 24.36 ?  265  LYS A NZ    1 
ATOM   1881  N N     . LEU A 1 268  ? -44.783 65.297  80.328  1.00 10.67 ?  266  LEU A N     1 
ATOM   1882  C CA    . LEU A 1 268  ? -45.119 66.632  80.820  1.00 10.53 ?  266  LEU A CA    1 
ATOM   1883  C C     . LEU A 1 268  ? -43.868 67.471  81.075  1.00 12.20 ?  266  LEU A C     1 
ATOM   1884  O O     . LEU A 1 268  ? -43.904 68.694  80.904  1.00 11.58 ?  266  LEU A O     1 
ATOM   1885  C CB    . LEU A 1 268  ? -45.988 66.531  82.083  1.00 12.14 ?  266  LEU A CB    1 
ATOM   1886  C CG    . LEU A 1 268  ? -47.323 65.808  81.852  1.00 12.91 ?  266  LEU A CG    1 
ATOM   1887  C CD1   . LEU A 1 268  ? -48.141 65.711  83.131  1.00 14.74 ?  266  LEU A CD1   1 
ATOM   1888  C CD2   . LEU A 1 268  ? -48.109 66.523  80.750  1.00 13.74 ?  266  LEU A CD2   1 
ATOM   1889  N N     . SER A 1 269  ? -42.748 66.848  81.444  1.00 11.75 ?  267  SER A N     1 
ATOM   1890  C CA    . SER A 1 269  ? -41.541 67.640  81.680  1.00 11.46 ?  267  SER A CA    1 
ATOM   1891  C C     . SER A 1 269  ? -41.031 68.311  80.412  1.00 13.46 ?  267  SER A C     1 
ATOM   1892  O O     . SER A 1 269  ? -40.231 69.248  80.509  1.00 12.32 ?  267  SER A O     1 
ATOM   1893  C CB    . SER A 1 269  ? -40.428 66.781  82.288  1.00 12.21 ?  267  SER A CB    1 
ATOM   1894  O OG    . SER A 1 269  ? -39.924 65.846  81.350  1.00 13.39 ?  267  SER A OG    1 
ATOM   1895  N N     . ALA A 1 270  ? -41.461 67.850  79.231  1.00 10.42 ?  268  ALA A N     1 
ATOM   1896  C CA    . ALA A 1 270  ? -41.059 68.505  77.991  1.00 11.31 ?  268  ALA A CA    1 
ATOM   1897  C C     . ALA A 1 270  ? -41.815 69.798  77.760  1.00 12.62 ?  268  ALA A C     1 
ATOM   1898  O O     . ALA A 1 270  ? -41.354 70.644  76.992  1.00 12.68 ?  268  ALA A O     1 
ATOM   1899  C CB    . ALA A 1 270  ? -41.304 67.575  76.802  1.00 12.47 ?  268  ALA A CB    1 
ATOM   1900  N N     . LEU A 1 271  ? -42.965 69.966  78.403  1.00 11.20 ?  269  LEU A N     1 
ATOM   1901  C CA    . LEU A 1 271  ? -43.892 71.022  78.037  1.00 12.65 ?  269  LEU A CA    1 
ATOM   1902  C C     . LEU A 1 271  ? -43.837 72.217  78.974  1.00 11.71 ?  269  LEU A C     1 
ATOM   1903  O O     . LEU A 1 271  ? -44.536 73.204  78.738  1.00 12.90 ?  269  LEU A O     1 
ATOM   1904  C CB    . LEU A 1 271  ? -45.319 70.464  77.972  1.00 12.87 ?  269  LEU A CB    1 
ATOM   1905  C CG    . LEU A 1 271  ? -45.557 69.530  76.785  1.00 15.22 ?  269  LEU A CG    1 
ATOM   1906  C CD1   . LEU A 1 271  ? -46.979 68.956  76.869  1.00 15.53 ?  269  LEU A CD1   1 
ATOM   1907  C CD2   . LEU A 1 271  ? -45.367 70.303  75.499  1.00 15.18 ?  269  LEU A CD2   1 
ATOM   1908  N N     . HIS A 1 272  ? -42.998 72.168  80.009  1.00 11.84 ?  270  HIS A N     1 
ATOM   1909  C CA    . HIS A 1 272  ? -42.836 73.326  80.878  1.00 13.89 ?  270  HIS A CA    1 
ATOM   1910  C C     . HIS A 1 272  ? -41.484 73.234  81.564  1.00 14.02 ?  270  HIS A C     1 
ATOM   1911  O O     . HIS A 1 272  ? -41.115 72.156  82.037  1.00 13.50 ?  270  HIS A O     1 
ATOM   1912  C CB    . HIS A 1 272  ? -43.950 73.409  81.924  1.00 14.09 ?  270  HIS A CB    1 
ATOM   1913  C CG    . HIS A 1 272  ? -44.075 74.764  82.534  1.00 16.39 ?  270  HIS A CG    1 
ATOM   1914  N ND1   . HIS A 1 272  ? -43.164 75.258  83.446  1.00 16.08 ?  270  HIS A ND1   1 
ATOM   1915  C CD2   . HIS A 1 272  ? -44.979 75.749  82.332  1.00 17.96 ?  270  HIS A CD2   1 
ATOM   1916  C CE1   . HIS A 1 272  ? -43.507 76.490  83.781  1.00 18.27 ?  270  HIS A CE1   1 
ATOM   1917  N NE2   . HIS A 1 272  ? -44.604 76.813  83.117  1.00 19.26 ?  270  HIS A NE2   1 
ATOM   1918  N N     . PRO A 1 273  ? -40.718 74.330  81.635  1.00 12.36 ?  271  PRO A N     1 
ATOM   1919  C CA    . PRO A 1 273  ? -39.396 74.261  82.278  1.00 13.36 ?  271  PRO A CA    1 
ATOM   1920  C C     . PRO A 1 273  ? -39.449 74.172  83.790  1.00 13.63 ?  271  PRO A C     1 
ATOM   1921  O O     . PRO A 1 273  ? -38.421 73.855  84.404  1.00 14.26 ?  271  PRO A O     1 
ATOM   1922  C CB    . PRO A 1 273  ? -38.722 75.559  81.830  1.00 13.37 ?  271  PRO A CB    1 
ATOM   1923  C CG    . PRO A 1 273  ? -39.856 76.513  81.635  1.00 15.74 ?  271  PRO A CG    1 
ATOM   1924  C CD    . PRO A 1 273  ? -40.987 75.653  81.056  1.00 12.73 ?  271  PRO A CD    1 
ATOM   1925  N N     . ARG A 1 274  ? -40.606 74.385  84.415  1.00 11.30 ?  272  ARG A N     1 
ATOM   1926  C CA    . ARG A 1 274  ? -40.707 74.302  85.879  1.00 11.71 ?  272  ARG A CA    1 
ATOM   1927  C C     . ARG A 1 274  ? -41.827 73.342  86.275  1.00 13.56 ?  272  ARG A C     1 
ATOM   1928  O O     . ARG A 1 274  ? -42.736 73.679  87.038  1.00 14.89 ?  272  ARG A O     1 
ATOM   1929  C CB    . ARG A 1 274  ? -40.938 75.673  86.508  1.00 12.70 ?  272  ARG A CB    1 
ATOM   1930  C CG    . ARG A 1 274  ? -39.826 76.687  86.291  1.00 14.30 ?  272  ARG A CG    1 
ATOM   1931  C CD    . ARG A 1 274  ? -38.454 76.203  86.816  1.00 13.41 ?  272  ARG A CD    1 
ATOM   1932  N NE    . ARG A 1 274  ? -38.489 75.760  88.211  1.00 14.67 ?  272  ARG A NE    1 
ATOM   1933  C CZ    . ARG A 1 274  ? -38.457 76.587  89.251  1.00 15.19 ?  272  ARG A CZ    1 
ATOM   1934  N NH1   . ARG A 1 274  ? -38.409 77.898  89.083  1.00 14.90 ?  272  ARG A NH1   1 
ATOM   1935  N NH2   . ARG A 1 274  ? -38.479 76.089  90.486  1.00 17.50 ?  272  ARG A NH2   1 
ATOM   1936  N N     . TYR A 1 275  ? -41.748 72.120  85.762  1.00 13.85 ?  273  TYR A N     1 
ATOM   1937  C CA    . TYR A 1 275  ? -42.753 71.095  86.055  1.00 12.10 ?  273  TYR A CA    1 
ATOM   1938  C C     . TYR A 1 275  ? -42.388 70.446  87.383  1.00 12.46 ?  273  TYR A C     1 
ATOM   1939  O O     . TYR A 1 275  ? -41.591 69.511  87.450  1.00 13.66 ?  273  TYR A O     1 
ATOM   1940  C CB    . TYR A 1 275  ? -42.819 70.082  84.910  1.00 13.02 ?  273  TYR A CB    1 
ATOM   1941  C CG    . TYR A 1 275  ? -43.772 68.945  85.170  1.00 11.58 ?  273  TYR A CG    1 
ATOM   1942  C CD1   . TYR A 1 275  ? -45.083 69.191  85.562  1.00 12.41 ?  273  TYR A CD1   1 
ATOM   1943  C CD2   . TYR A 1 275  ? -43.363 67.634  85.007  1.00 11.98 ?  273  TYR A CD2   1 
ATOM   1944  C CE1   . TYR A 1 275  ? -45.954 68.138  85.839  1.00 13.90 ?  273  TYR A CE1   1 
ATOM   1945  C CE2   . TYR A 1 275  ? -44.220 66.575  85.263  1.00 12.34 ?  273  TYR A CE2   1 
ATOM   1946  C CZ    . TYR A 1 275  ? -45.503 66.834  85.693  1.00 13.78 ?  273  TYR A CZ    1 
ATOM   1947  O OH    . TYR A 1 275  ? -46.353 65.780  85.931  1.00 15.61 ?  273  TYR A OH    1 
ATOM   1948  N N     . SER A 1 276  ? -42.990 70.954  88.459  1.00 13.38 ?  274  SER A N     1 
ATOM   1949  C CA    . SER A 1 276  ? -42.705 70.476  89.807  1.00 11.67 ?  274  SER A CA    1 
ATOM   1950  C C     . SER A 1 276  ? -43.830 70.910  90.731  1.00 12.13 ?  274  SER A C     1 
ATOM   1951  O O     . SER A 1 276  ? -44.534 71.894  90.475  1.00 13.79 ?  274  SER A O     1 
ATOM   1952  C CB    . SER A 1 276  ? -41.368 70.999  90.331  1.00 19.04 ?  274  SER A CB    1 
ATOM   1953  O OG    . SER A 1 276  ? -41.455 72.381  90.603  1.00 21.23 ?  274  SER A OG    1 
ATOM   1954  N N     . ARG A 1 277  ? -43.967 70.167  91.834  1.00 12.70 ?  275  ARG A N     1 
ATOM   1955  C CA    . ARG A 1 277  ? -44.969 70.518  92.842  1.00 12.93 ?  275  ARG A CA    1 
ATOM   1956  C C     . ARG A 1 277  ? -44.741 71.925  93.389  1.00 13.45 ?  275  ARG A C     1 
ATOM   1957  O O     . ARG A 1 277  ? -45.702 72.632  93.704  1.00 12.95 ?  275  ARG A O     1 
ATOM   1958  C CB    . ARG A 1 277  ? -44.969 69.492  93.981  1.00 14.56 ?  275  ARG A CB    1 
ATOM   1959  C CG    . ARG A 1 277  ? -45.881 69.830  95.195  1.00 14.50 ?  275  ARG A CG    1 
ATOM   1960  C CD    . ARG A 1 277  ? -47.339 70.085  94.798  1.00 15.83 ?  275  ARG A CD    1 
ATOM   1961  N NE    . ARG A 1 277  ? -48.169 70.396  95.965  1.00 13.78 ?  275  ARG A NE    1 
ATOM   1962  C CZ    . ARG A 1 277  ? -48.341 71.617  96.458  1.00 15.26 ?  275  ARG A CZ    1 
ATOM   1963  N NH1   . ARG A 1 277  ? -47.743 72.671  95.918  1.00 16.52 ?  275  ARG A NH1   1 
ATOM   1964  N NH2   . ARG A 1 277  ? -49.162 71.794  97.494  1.00 16.73 ?  275  ARG A NH2   1 
ATOM   1965  N N     . ALA A 1 278  ? -43.477 72.334  93.544  1.00 15.93 ?  276  ALA A N     1 
ATOM   1966  C CA    . ALA A 1 278  ? -43.197 73.662  94.078  1.00 15.53 ?  276  ALA A CA    1 
ATOM   1967  C C     . ALA A 1 278  ? -43.756 74.753  93.185  1.00 16.29 ?  276  ALA A C     1 
ATOM   1968  O O     . ALA A 1 278  ? -44.076 75.849  93.664  1.00 17.53 ?  276  ALA A O     1 
ATOM   1969  C CB    . ALA A 1 278  ? -41.691 73.852  94.271  1.00 16.31 ?  276  ALA A CB    1 
ATOM   1970  N N     . GLN A 1 279  ? -43.887 74.470  91.889  1.00 14.00 ?  277  GLN A N     1 
ATOM   1971  C CA    . GLN A 1 279  ? -44.418 75.410  90.915  1.00 13.71 ?  277  GLN A CA    1 
ATOM   1972  C C     . GLN A 1 279  ? -45.795 74.984  90.424  1.00 15.78 ?  277  GLN A C     1 
ATOM   1973  O O     . GLN A 1 279  ? -46.160 75.263  89.281  1.00 14.72 ?  277  GLN A O     1 
ATOM   1974  C CB    . GLN A 1 279  ? -43.453 75.543  89.738  1.00 14.79 ?  277  GLN A CB    1 
ATOM   1975  C CG    . GLN A 1 279  ? -42.038 75.962  90.146  1.00 15.51 ?  277  GLN A CG    1 
ATOM   1976  C CD    . GLN A 1 279  ? -41.999 77.382  90.661  1.00 18.12 ?  277  GLN A CD    1 
ATOM   1977  O OE1   . GLN A 1 279  ? -42.538 78.288  90.040  1.00 25.77 ?  277  GLN A OE1   1 
ATOM   1978  N NE2   . GLN A 1 279  ? -41.358 77.586  91.801  1.00 16.83 ?  277  GLN A NE2   1 
ATOM   1979  N N     . ALA A 1 280  ? -46.583 74.352  91.295  1.00 14.19 ?  278  ALA A N     1 
ATOM   1980  C CA    . ALA A 1 280  ? -47.858 73.777  90.865  1.00 14.93 ?  278  ALA A CA    1 
ATOM   1981  C C     . ALA A 1 280  ? -48.786 74.816  90.246  1.00 15.37 ?  278  ALA A C     1 
ATOM   1982  O O     . ALA A 1 280  ? -49.507 74.508  89.291  1.00 16.16 ?  278  ALA A O     1 
ATOM   1983  C CB    . ALA A 1 280  ? -48.562 73.095  92.036  1.00 16.46 ?  278  ALA A CB    1 
ATOM   1984  N N     . ALA A 1 281  ? -48.826 76.036  90.793  1.00 14.37 ?  279  ALA A N     1 
ATOM   1985  C CA    . ALA A 1 281  ? -49.707 77.050  90.217  1.00 16.74 ?  279  ALA A CA    1 
ATOM   1986  C C     . ALA A 1 281  ? -49.314 77.372  88.780  1.00 16.03 ?  279  ALA A C     1 
ATOM   1987  O O     . ALA A 1 281  ? -50.182 77.542  87.914  1.00 17.60 ?  279  ALA A O     1 
ATOM   1988  C CB    . ALA A 1 281  ? -49.706 78.322  91.066  1.00 19.74 ?  279  ALA A CB    1 
ATOM   1989  N N     . ARG A 1 282  ? -48.015 77.465  88.499  1.00 13.86 ?  280  ARG A N     1 
ATOM   1990  C CA    . ARG A 1 282  ? -47.597 77.705  87.119  1.00 14.08 ?  280  ARG A CA    1 
ATOM   1991  C C     . ARG A 1 282  ? -47.908 76.503  86.237  1.00 15.26 ?  280  ARG A C     1 
ATOM   1992  O O     . ARG A 1 282  ? -48.259 76.660  85.059  1.00 15.71 ?  280  ARG A O     1 
ATOM   1993  C CB    . ARG A 1 282  ? -46.098 78.017  87.048  1.00 15.98 ?  280  ARG A CB    1 
ATOM   1994  C CG    . ARG A 1 282  ? -45.693 79.353  87.637  1.00 17.65 ?  280  ARG A CG    1 
ATOM   1995  C CD    . ARG A 1 282  ? -44.260 79.662  87.232  1.00 16.71 ?  280  ARG A CD    1 
ATOM   1996  N NE    . ARG A 1 282  ? -44.152 79.817  85.788  1.00 15.66 ?  280  ARG A NE    1 
ATOM   1997  C CZ    . ARG A 1 282  ? -43.009 79.837  85.120  1.00 15.29 ?  280  ARG A CZ    1 
ATOM   1998  N NH1   . ARG A 1 282  ? -41.844 79.685  85.737  1.00 16.43 ?  280  ARG A NH1   1 
ATOM   1999  N NH2   . ARG A 1 282  ? -43.034 79.985  83.797  1.00 18.62 ?  280  ARG A NH2   1 
ATOM   2000  N N     . VAL A 1 283  ? -47.764 75.292  86.775  1.00 13.25 ?  281  VAL A N     1 
ATOM   2001  C CA    . VAL A 1 283  ? -48.077 74.097  86.000  1.00 13.09 ?  281  VAL A CA    1 
ATOM   2002  C C     . VAL A 1 283  ? -49.540 74.103  85.578  1.00 15.34 ?  281  VAL A C     1 
ATOM   2003  O O     . VAL A 1 283  ? -49.867 73.893  84.405  1.00 14.19 ?  281  VAL A O     1 
ATOM   2004  C CB    . VAL A 1 283  ? -47.724 72.836  86.803  1.00 13.91 ?  281  VAL A CB    1 
ATOM   2005  C CG1   . VAL A 1 283  ? -48.304 71.590  86.125  1.00 16.56 ?  281  VAL A CG1   1 
ATOM   2006  C CG2   . VAL A 1 283  ? -46.213 72.727  86.946  1.00 13.93 ?  281  VAL A CG2   1 
ATOM   2007  N N     . MET A 1 284  ? -50.443 74.358  86.524  1.00 14.50 ?  282  MET A N     1 
ATOM   2008  C CA    . MET A 1 284  ? -51.864 74.335  86.184  1.00 14.50 ?  282  MET A CA    1 
ATOM   2009  C C     . MET A 1 284  ? -52.235 75.492  85.265  1.00 18.49 ?  282  MET A C     1 
ATOM   2010  O O     . MET A 1 284  ? -53.139 75.356  84.433  1.00 18.63 ?  282  MET A O     1 
ATOM   2011  C CB    . MET A 1 284  ? -52.708 74.360  87.462  1.00 15.33 ?  282  MET A CB    1 
ATOM   2012  C CG    . MET A 1 284  ? -52.457 73.172  88.389  1.00 15.74 ?  282  MET A CG    1 
ATOM   2013  S SD    . MET A 1 284  ? -52.664 71.555  87.599  1.00 18.73 ?  282  MET A SD    1 
ATOM   2014  C CE    . MET A 1 284  ? -54.432 71.547  87.257  1.00 19.85 ?  282  MET A CE    1 
ATOM   2015  N N     . GLY A 1 285  ? -51.549 76.624  85.382  1.00 14.35 ?  283  GLY A N     1 
ATOM   2016  C CA    . GLY A 1 285  ? -51.916 77.798  84.613  1.00 15.49 ?  283  GLY A CA    1 
ATOM   2017  C C     . GLY A 1 285  ? -51.321 77.822  83.225  1.00 17.43 ?  283  GLY A C     1 
ATOM   2018  O O     . GLY A 1 285  ? -51.930 78.359  82.296  1.00 18.17 ?  283  GLY A O     1 
ATOM   2019  N N     . GLU A 1 286  ? -50.149 77.223  83.062  1.00 13.98 ?  284  GLU A N     1 
ATOM   2020  C CA    . GLU A 1 286  ? -49.367 77.331  81.837  1.00 14.93 ?  284  GLU A CA    1 
ATOM   2021  C C     . GLU A 1 286  ? -49.173 76.006  81.126  1.00 16.34 ?  284  GLU A C     1 
ATOM   2022  O O     . GLU A 1 286  ? -49.217 75.965  79.895  1.00 18.56 ?  284  GLU A O     1 
ATOM   2023  C CB    . GLU A 1 286  ? -47.977 77.923  82.144  1.00 16.35 ?  284  GLU A CB    1 
ATOM   2024  C CG    . GLU A 1 286  ? -48.036 79.268  82.833  1.00 15.74 ?  284  GLU A CG    1 
ATOM   2025  C CD    . GLU A 1 286  ? -46.691 79.735  83.349  1.00 16.64 ?  284  GLU A CD    1 
ATOM   2026  O OE1   . GLU A 1 286  ? -45.662 79.367  82.750  1.00 18.79 ?  284  GLU A OE1   1 
ATOM   2027  O OE2   . GLU A 1 286  ? -46.670 80.481  84.356  1.00 21.48 ?  284  GLU A OE2   1 
ATOM   2028  N N     . LEU A 1 287  ? -48.926 74.921  81.863  1.00 13.10 ?  285  LEU A N     1 
ATOM   2029  C CA    . LEU A 1 287  ? -48.710 73.618  81.242  1.00 13.94 ?  285  LEU A CA    1 
ATOM   2030  C C     . LEU A 1 287  ? -50.038 72.990  80.835  1.00 16.32 ?  285  LEU A C     1 
ATOM   2031  O O     . LEU A 1 287  ? -50.172 72.481  79.719  1.00 14.79 ?  285  LEU A O     1 
ATOM   2032  C CB    . LEU A 1 287  ? -47.958 72.690  82.201  1.00 14.70 ?  285  LEU A CB    1 
ATOM   2033  C CG    . LEU A 1 287  ? -47.083 71.576  81.625  1.00 21.01 ?  285  LEU A CG    1 
ATOM   2034  C CD1   . LEU A 1 287  ? -46.335 70.867  82.740  1.00 18.03 ?  285  LEU A CD1   1 
ATOM   2035  C CD2   . LEU A 1 287  ? -47.855 70.560  80.824  1.00 20.44 ?  285  LEU A CD2   1 
ATOM   2036  N N     . LEU A 1 288  ? -51.023 73.012  81.729  1.00 13.74 ?  286  LEU A N     1 
ATOM   2037  C CA    . LEU A 1 288  ? -52.324 72.412  81.429  1.00 15.63 ?  286  LEU A CA    1 
ATOM   2038  C C     . LEU A 1 288  ? -52.941 72.894  80.116  1.00 16.20 ?  286  LEU A C     1 
ATOM   2039  O O     . LEU A 1 288  ? -53.365 72.042  79.321  1.00 14.97 ?  286  LEU A O     1 
ATOM   2040  C CB    . LEU A 1 288  ? -53.281 72.646  82.605  1.00 17.53 ?  286  LEU A CB    1 
ATOM   2041  C CG    . LEU A 1 288  ? -54.733 72.258  82.305  1.00 21.52 ?  286  LEU A CG    1 
ATOM   2042  C CD1   . LEU A 1 288  ? -54.852 70.739  82.112  1.00 18.89 ?  286  LEU A CD1   1 
ATOM   2043  C CD2   . LEU A 1 288  ? -55.660 72.755  83.404  1.00 25.53 ?  286  LEU A CD2   1 
ATOM   2044  N N     . PRO A 1 289  ? -53.011 74.194  79.811  1.00 15.50 ?  287  PRO A N     1 
ATOM   2045  C CA    . PRO A 1 289  ? -53.605 74.589  78.522  1.00 15.80 ?  287  PRO A CA    1 
ATOM   2046  C C     . PRO A 1 289  ? -52.878 74.005  77.327  1.00 14.39 ?  287  PRO A C     1 
ATOM   2047  O O     . PRO A 1 289  ? -53.499 73.755  76.280  1.00 14.86 ?  287  PRO A O     1 
ATOM   2048  C CB    . PRO A 1 289  ? -53.508 76.120  78.547  1.00 18.36 ?  287  PRO A CB    1 
ATOM   2049  C CG    . PRO A 1 289  ? -53.504 76.465  80.005  1.00 21.03 ?  287  PRO A CG    1 
ATOM   2050  C CD    . PRO A 1 289  ? -52.718 75.367  80.659  1.00 16.75 ?  287  PRO A CD    1 
ATOM   2051  N N     . ARG A 1 290  ? -51.567 73.796  77.433  1.00 13.02 ?  288  ARG A N     1 
ATOM   2052  C CA    . ARG A 1 290  ? -50.827 73.195  76.330  1.00 12.54 ?  288  ARG A CA    1 
ATOM   2053  C C     . ARG A 1 290  ? -51.228 71.745  76.123  1.00 13.47 ?  288  ARG A C     1 
ATOM   2054  O O     . ARG A 1 290  ? -51.423 71.309  74.978  1.00 12.83 ?  288  ARG A O     1 
ATOM   2055  C CB    . ARG A 1 290  ? -49.315 73.316  76.568  1.00 15.74 ?  288  ARG A CB    1 
ATOM   2056  C CG    . ARG A 1 290  ? -48.848 74.753  76.503  1.00 16.56 ?  288  ARG A CG    1 
ATOM   2057  C CD    . ARG A 1 290  ? -47.453 74.919  77.071  1.00 18.89 ?  288  ARG A CD    1 
ATOM   2058  N NE    . ARG A 1 290  ? -47.151 76.339  77.245  1.00 22.31 ?  288  ARG A NE    1 
ATOM   2059  C CZ    . ARG A 1 290  ? -46.199 76.812  78.039  1.00 22.35 ?  288  ARG A CZ    1 
ATOM   2060  N NH1   . ARG A 1 290  ? -45.415 76.004  78.738  1.00 20.64 ?  288  ARG A NH1   1 
ATOM   2061  N NH2   . ARG A 1 290  ? -46.044 78.131  78.153  1.00 23.70 ?  288  ARG A NH2   1 
ATOM   2062  N N     . VAL A 1 291  ? -51.327 70.971  77.214  1.00 13.29 ?  289  VAL A N     1 
ATOM   2063  C CA    . VAL A 1 291  ? -51.779 69.590  77.083  1.00 12.72 ?  289  VAL A CA    1 
ATOM   2064  C C     . VAL A 1 291  ? -53.192 69.562  76.528  1.00 12.87 ?  289  VAL A C     1 
ATOM   2065  O O     . VAL A 1 291  ? -53.522 68.717  75.686  1.00 13.42 ?  289  VAL A O     1 
ATOM   2066  C CB    . VAL A 1 291  ? -51.686 68.834  78.421  1.00 15.36 ?  289  VAL A CB    1 
ATOM   2067  C CG1   . VAL A 1 291  ? -52.094 67.378  78.211  1.00 16.36 ?  289  VAL A CG1   1 
ATOM   2068  C CG2   . VAL A 1 291  ? -50.291 68.904  78.946  1.00 16.61 ?  289  VAL A CG2   1 
ATOM   2069  N N     . LYS A 1 292  ? -54.049 70.472  76.999  1.00 11.84 ?  290  LYS A N     1 
ATOM   2070  C CA    . LYS A 1 292  ? -55.422 70.501  76.498  1.00 11.73 ?  290  LYS A CA    1 
ATOM   2071  C C     . LYS A 1 292  ? -55.452 70.741  75.000  1.00 15.27 ?  290  LYS A C     1 
ATOM   2072  O O     . LYS A 1 292  ? -56.205 70.077  74.274  1.00 12.16 ?  290  LYS A O     1 
ATOM   2073  C CB    . LYS A 1 292  ? -56.249 71.563  77.212  1.00 13.21 ?  290  LYS A CB    1 
ATOM   2074  C CG    . LYS A 1 292  ? -57.683 71.593  76.695  1.00 14.77 ?  290  LYS A CG    1 
ATOM   2075  C CD    . LYS A 1 292  ? -58.547 72.675  77.318  1.00 16.84 ?  290  LYS A CD    1 
ATOM   2076  C CE    . LYS A 1 292  ? -59.932 72.670  76.692  1.00 15.06 ?  290  LYS A CE    1 
ATOM   2077  N NZ    . LYS A 1 292  ? -60.846 73.601  77.413  1.00 17.41 ?  290  LYS A NZ    1 
ATOM   2078  N N     . ALA A 1 293  ? -54.625 71.670  74.508  1.00 13.72 ?  291  ALA A N     1 
ATOM   2079  C CA    . ALA A 1 293  ? -54.616 71.941  73.076  1.00 11.56 ?  291  ALA A CA    1 
ATOM   2080  C C     . ALA A 1 293  ? -54.150 70.725  72.279  1.00 12.75 ?  291  ALA A C     1 
ATOM   2081  O O     . ALA A 1 293  ? -54.696 70.436  71.209  1.00 14.31 ?  291  ALA A O     1 
ATOM   2082  C CB    . ALA A 1 293  ? -53.740 73.161  72.763  1.00 13.29 ?  291  ALA A CB    1 
ATOM   2083  N N     . LEU A 1 294  ? -53.137 70.006  72.769  1.00 11.41 ?  292  LEU A N     1 
ATOM   2084  C CA    . LEU A 1 294  ? -52.700 68.791  72.085  1.00 12.84 ?  292  LEU A CA    1 
ATOM   2085  C C     . LEU A 1 294  ? -53.790 67.723  72.128  1.00 11.76 ?  292  LEU A C     1 
ATOM   2086  O O     . LEU A 1 294  ? -54.033 67.027  71.131  1.00 12.87 ?  292  LEU A O     1 
ATOM   2087  C CB    . LEU A 1 294  ? -51.410 68.263  72.716  1.00 12.54 ?  292  LEU A CB    1 
ATOM   2088  C CG    . LEU A 1 294  ? -50.164 69.148  72.576  1.00 11.37 ?  292  LEU A CG    1 
ATOM   2089  C CD1   . LEU A 1 294  ? -49.021 68.534  73.355  1.00 13.30 ?  292  LEU A CD1   1 
ATOM   2090  C CD2   . LEU A 1 294  ? -49.750 69.364  71.111  1.00 11.96 ?  292  LEU A CD2   1 
ATOM   2091  N N     . ALA A 1 295  ? -54.456 67.586  73.275  1.00 12.60 ?  293  ALA A N     1 
ATOM   2092  C CA    . ALA A 1 295  ? -55.535 66.610  73.399  1.00 11.79 ?  293  ALA A CA    1 
ATOM   2093  C C     . ALA A 1 295  ? -56.705 66.944  72.483  1.00 13.42 ?  293  ALA A C     1 
ATOM   2094  O O     . ALA A 1 295  ? -57.335 66.037  71.923  1.00 12.53 ?  293  ALA A O     1 
ATOM   2095  C CB    . ALA A 1 295  ? -55.995 66.529  74.854  1.00 12.25 ?  293  ALA A CB    1 
ATOM   2096  N N     . LEU A 1 296  ? -57.036 68.228  72.338  1.00 11.09 ?  294  LEU A N     1 
ATOM   2097  C CA    . LEU A 1 296  ? -58.102 68.598  71.403  1.00 11.33 ?  294  LEU A CA    1 
ATOM   2098  C C     . LEU A 1 296  ? -57.765 68.168  69.984  1.00 13.42 ?  294  LEU A C     1 
ATOM   2099  O O     . LEU A 1 296  ? -58.647 67.741  69.231  1.00 13.92 ?  294  LEU A O     1 
ATOM   2100  C CB    . LEU A 1 296  ? -58.365 70.105  71.442  1.00 12.51 ?  294  LEU A CB    1 
ATOM   2101  C CG    . LEU A 1 296  ? -59.069 70.610  72.698  1.00 13.72 ?  294  LEU A CG    1 
ATOM   2102  C CD1   . LEU A 1 296  ? -58.980 72.125  72.782  1.00 17.68 ?  294  LEU A CD1   1 
ATOM   2103  C CD2   . LEU A 1 296  ? -60.543 70.173  72.738  1.00 18.83 ?  294  LEU A CD2   1 
ATOM   2104  N N     . LEU A 1 297  ? -56.493 68.295  69.598  1.00 12.97 ?  295  LEU A N     1 
ATOM   2105  C CA    A LEU A 1 297  ? -56.080 67.839  68.277  0.60 13.73 ?  295  LEU A CA    1 
ATOM   2106  C CA    B LEU A 1 297  ? -56.028 67.831  68.294  0.40 13.77 ?  295  LEU A CA    1 
ATOM   2107  C C     . LEU A 1 297  ? -56.157 66.320  68.166  1.00 12.87 ?  295  LEU A C     1 
ATOM   2108  O O     . LEU A 1 297  ? -56.642 65.794  67.155  1.00 13.64 ?  295  LEU A O     1 
ATOM   2109  C CB    A LEU A 1 297  ? -54.667 68.336  67.967  0.60 15.27 ?  295  LEU A CB    1 
ATOM   2110  C CB    B LEU A 1 297  ? -54.569 68.243  68.120  0.40 15.16 ?  295  LEU A CB    1 
ATOM   2111  C CG    A LEU A 1 297  ? -54.339 68.346  66.477  0.60 14.58 ?  295  LEU A CG    1 
ATOM   2112  C CG    B LEU A 1 297  ? -54.239 69.338  67.128  0.40 17.13 ?  295  LEU A CG    1 
ATOM   2113  C CD1   A LEU A 1 297  ? -55.302 69.281  65.723  0.60 18.10 ?  295  LEU A CD1   1 
ATOM   2114  C CD1   B LEU A 1 297  ? -52.809 69.753  67.355  0.40 17.07 ?  295  LEU A CD1   1 
ATOM   2115  C CD2   A LEU A 1 297  ? -52.891 68.777  66.263  0.60 19.10 ?  295  LEU A CD2   1 
ATOM   2116  C CD2   B LEU A 1 297  ? -54.417 68.756  65.747  0.40 17.79 ?  295  LEU A CD2   1 
ATOM   2117  N N     . ALA A 1 298  ? -55.679 65.600  69.182  1.00 11.20 ?  296  ALA A N     1 
ATOM   2118  C CA    . ALA A 1 298  ? -55.793 64.148  69.178  1.00 12.06 ?  296  ALA A CA    1 
ATOM   2119  C C     . ALA A 1 298  ? -57.250 63.731  69.086  1.00 13.78 ?  296  ALA A C     1 
ATOM   2120  O O     . ALA A 1 298  ? -57.582 62.778  68.376  1.00 14.11 ?  296  ALA A O     1 
ATOM   2121  C CB    . ALA A 1 298  ? -55.127 63.557  70.426  1.00 12.81 ?  296  ALA A CB    1 
ATOM   2122  N N     . LYS A 1 299  ? -58.134 64.442  69.794  1.00 12.69 ?  297  LYS A N     1 
ATOM   2123  C CA    A LYS A 1 299  ? -59.561 64.142  69.710  0.50 12.27 ?  297  LYS A CA    1 
ATOM   2124  C CA    B LYS A 1 299  ? -59.560 64.143  69.711  0.50 12.27 ?  297  LYS A CA    1 
ATOM   2125  C C     . LYS A 1 299  ? -60.079 64.291  68.285  1.00 14.33 ?  297  LYS A C     1 
ATOM   2126  O O     . LYS A 1 299  ? -60.856 63.454  67.812  1.00 14.19 ?  297  LYS A O     1 
ATOM   2127  C CB    A LYS A 1 299  ? -60.352 65.048  70.658  0.50 12.27 ?  297  LYS A CB    1 
ATOM   2128  C CB    B LYS A 1 299  ? -60.336 65.052  70.666  0.50 12.26 ?  297  LYS A CB    1 
ATOM   2129  C CG    A LYS A 1 299  ? -61.860 65.091  70.375  0.50 14.80 ?  297  LYS A CG    1 
ATOM   2130  C CG    B LYS A 1 299  ? -61.843 65.097  70.437  0.50 14.81 ?  297  LYS A CG    1 
ATOM   2131  C CD    A LYS A 1 299  ? -62.584 66.014  71.339  0.50 15.98 ?  297  LYS A CD    1 
ATOM   2132  C CD    B LYS A 1 299  ? -62.524 65.829  71.576  0.50 15.92 ?  297  LYS A CD    1 
ATOM   2133  C CE    A LYS A 1 299  ? -63.995 66.301  70.850  0.50 16.81 ?  297  LYS A CE    1 
ATOM   2134  C CE    B LYS A 1 299  ? -63.954 66.161  71.221  0.50 17.08 ?  297  LYS A CE    1 
ATOM   2135  N NZ    A LYS A 1 299  ? -64.774 67.125  71.814  0.50 17.18 ?  297  LYS A NZ    1 
ATOM   2136  N NZ    B LYS A 1 299  ? -64.012 67.136  70.106  0.50 17.72 ?  297  LYS A NZ    1 
ATOM   2137  N N     . ASN A 1 300  ? -59.659 65.350  67.578  1.00 14.31 ?  298  ASN A N     1 
ATOM   2138  C CA    . ASN A 1 300  ? -60.235 65.567  66.251  1.00 12.69 ?  298  ASN A CA    1 
ATOM   2139  C C     . ASN A 1 300  ? -59.842 64.459  65.288  1.00 13.31 ?  298  ASN A C     1 
ATOM   2140  O O     . ASN A 1 300  ? -60.654 64.047  64.449  1.00 17.15 ?  298  ASN A O     1 
ATOM   2141  C CB    . ASN A 1 300  ? -59.837 66.918  65.656  1.00 15.29 ?  298  ASN A CB    1 
ATOM   2142  C CG    . ASN A 1 300  ? -60.656 67.230  64.397  1.00 21.68 ?  298  ASN A CG    1 
ATOM   2143  O OD1   . ASN A 1 300  ? -61.825 67.624  64.486  1.00 30.70 ?  298  ASN A OD1   1 
ATOM   2144  N ND2   . ASN A 1 300  ? -60.070 66.998  63.229  1.00 21.28 ?  298  ASN A ND2   1 
ATOM   2145  N N     . TYR A 1 301  ? -58.612 63.955  65.394  1.00 13.26 ?  299  TYR A N     1 
ATOM   2146  C CA    . TYR A 1 301  ? -58.176 62.822  64.587  1.00 14.04 ?  299  TYR A CA    1 
ATOM   2147  C C     . TYR A 1 301  ? -58.574 61.468  65.174  1.00 15.02 ?  299  TYR A C     1 
ATOM   2148  O O     . TYR A 1 301  ? -58.398 60.444  64.503  1.00 15.95 ?  299  TYR A O     1 
ATOM   2149  C CB    . TYR A 1 301  ? -56.659 62.854  64.415  1.00 12.96 ?  299  TYR A CB    1 
ATOM   2150  C CG    . TYR A 1 301  ? -56.122 63.933  63.516  1.00 12.20 ?  299  TYR A CG    1 
ATOM   2151  C CD1   . TYR A 1 301  ? -56.288 63.865  62.139  1.00 14.49 ?  299  TYR A CD1   1 
ATOM   2152  C CD2   . TYR A 1 301  ? -55.368 64.978  64.039  1.00 13.53 ?  299  TYR A CD2   1 
ATOM   2153  C CE1   . TYR A 1 301  ? -55.745 64.842  61.308  1.00 13.07 ?  299  TYR A CE1   1 
ATOM   2154  C CE2   . TYR A 1 301  ? -54.820 65.955  63.225  1.00 13.45 ?  299  TYR A CE2   1 
ATOM   2155  C CZ    . TYR A 1 301  ? -55.016 65.884  61.853  1.00 14.48 ?  299  TYR A CZ    1 
ATOM   2156  O OH    . TYR A 1 301  ? -54.472 66.857  61.030  1.00 14.98 ?  299  TYR A OH    1 
ATOM   2157  N N     . ASP A 1 302  ? -59.105 61.444  66.393  1.00 12.32 ?  300  ASP A N     1 
ATOM   2158  C CA    . ASP A 1 302  ? -59.440 60.224  67.138  1.00 13.74 ?  300  ASP A CA    1 
ATOM   2159  C C     . ASP A 1 302  ? -58.244 59.278  67.261  1.00 13.72 ?  300  ASP A C     1 
ATOM   2160  O O     . ASP A 1 302  ? -58.304 58.107  66.886  1.00 14.29 ?  300  ASP A O     1 
ATOM   2161  C CB    . ASP A 1 302  ? -60.640 59.497  66.520  1.00 12.95 ?  300  ASP A CB    1 
ATOM   2162  C CG    . ASP A 1 302  ? -61.315 58.565  67.515  1.00 18.72 ?  300  ASP A CG    1 
ATOM   2163  O OD1   . ASP A 1 302  ? -61.258 58.848  68.739  1.00 18.19 ?  300  ASP A OD1   1 
ATOM   2164  O OD2   . ASP A 1 302  ? -61.895 57.543  67.081  1.00 17.94 ?  300  ASP A OD2   1 
ATOM   2165  N N     . ILE A 1 303  ? -57.149 59.805  67.816  1.00 11.97 ?  301  ILE A N     1 
ATOM   2166  C CA    . ILE A 1 303  ? -55.967 59.006  68.134  1.00 11.59 ?  301  ILE A CA    1 
ATOM   2167  C C     . ILE A 1 303  ? -55.721 59.035  69.639  1.00 12.35 ?  301  ILE A C     1 
ATOM   2168  O O     . ILE A 1 303  ? -56.233 59.889  70.367  1.00 12.32 ?  301  ILE A O     1 
ATOM   2169  C CB    . ILE A 1 303  ? -54.701 59.481  67.384  1.00 12.89 ?  301  ILE A CB    1 
ATOM   2170  C CG1   . ILE A 1 303  ? -54.215 60.831  67.922  1.00 12.38 ?  301  ILE A CG1   1 
ATOM   2171  C CG2   . ILE A 1 303  ? -54.985 59.548  65.899  1.00 14.16 ?  301  ILE A CG2   1 
ATOM   2172  C CD1   . ILE A 1 303  ? -52.838 61.217  67.396  1.00 15.77 ?  301  ILE A CD1   1 
ATOM   2173  N N     . GLY A 1 304  ? -54.933 58.072  70.100  1.00 13.18 ?  302  GLY A N     1 
ATOM   2174  C CA    . GLY A 1 304  ? -54.533 58.062  71.496  1.00 12.04 ?  302  GLY A CA    1 
ATOM   2175  C C     . GLY A 1 304  ? -53.502 59.136  71.799  1.00 12.27 ?  302  GLY A C     1 
ATOM   2176  O O     . GLY A 1 304  ? -52.638 59.473  70.978  1.00 13.05 ?  302  GLY A O     1 
ATOM   2177  N N     . LEU A 1 305  ? -53.596 59.685  73.008  1.00 10.90 ?  303  LEU A N     1 
ATOM   2178  C CA    . LEU A 1 305  ? -52.596 60.608  73.546  1.00 11.12 ?  303  LEU A CA    1 
ATOM   2179  C C     . LEU A 1 305  ? -52.265 60.169  74.965  1.00 12.57 ?  303  LEU A C     1 
ATOM   2180  O O     . LEU A 1 305  ? -53.098 60.301  75.869  1.00 12.20 ?  303  LEU A O     1 
ATOM   2181  C CB    . LEU A 1 305  ? -53.096 62.055  73.516  1.00 12.73 ?  303  LEU A CB    1 
ATOM   2182  C CG    . LEU A 1 305  ? -52.053 63.100  73.947  1.00 14.98 ?  303  LEU A CG    1 
ATOM   2183  C CD1   . LEU A 1 305  ? -52.255 64.408  73.207  1.00 18.82 ?  303  LEU A CD1   1 
ATOM   2184  C CD2   . LEU A 1 305  ? -52.119 63.363  75.434  1.00 20.67 ?  303  LEU A CD2   1 
ATOM   2185  N N     . ASN A 1 306  ? -51.048 59.670  75.169  1.00 12.40 ?  304  ASN A N     1 
ATOM   2186  C CA    . ASN A 1 306  ? -50.639 59.061  76.431  1.00 11.40 ?  304  ASN A CA    1 
ATOM   2187  C C     . ASN A 1 306  ? -49.685 59.981  77.181  1.00 13.00 ?  304  ASN A C     1 
ATOM   2188  O O     . ASN A 1 306  ? -48.733 60.504  76.589  1.00 13.19 ?  304  ASN A O     1 
ATOM   2189  C CB    . ASN A 1 306  ? -49.952 57.721  76.169  1.00 13.40 ?  304  ASN A CB    1 
ATOM   2190  C CG    . ASN A 1 306  ? -49.328 57.143  77.418  1.00 13.71 ?  304  ASN A CG    1 
ATOM   2191  O OD1   . ASN A 1 306  ? -48.122 57.303  77.667  1.00 16.66 ?  304  ASN A OD1   1 
ATOM   2192  N ND2   . ASN A 1 306  ? -50.140 56.505  78.225  1.00 12.50 ?  304  ASN A ND2   1 
ATOM   2193  N N     . ILE A 1 307  ? -49.919 60.146  78.478  1.00 12.04 ?  305  ILE A N     1 
ATOM   2194  C CA    . ILE A 1 307  ? -49.013 60.880  79.360  1.00 12.08 ?  305  ILE A CA    1 
ATOM   2195  C C     . ILE A 1 307  ? -48.049 59.891  80.014  1.00 11.67 ?  305  ILE A C     1 
ATOM   2196  O O     . ILE A 1 307  ? -48.441 59.078  80.867  1.00 12.09 ?  305  ILE A O     1 
ATOM   2197  C CB    . ILE A 1 307  ? -49.782 61.683  80.415  1.00 12.63 ?  305  ILE A CB    1 
ATOM   2198  C CG1   . ILE A 1 307  ? -50.662 62.731  79.733  1.00 14.12 ?  305  ILE A CG1   1 
ATOM   2199  C CG2   . ILE A 1 307  ? -48.800 62.331  81.427  1.00 14.94 ?  305  ILE A CG2   1 
ATOM   2200  C CD1   . ILE A 1 307  ? -51.665 63.359  80.680  1.00 17.06 ?  305  ILE A CD1   1 
ATOM   2201  N N     . ASP A 1 308  ? -46.773 59.966  79.622  1.00 11.73 ?  306  ASP A N     1 
ATOM   2202  C CA    . ASP A 1 308  ? -45.747 59.102  80.190  1.00 11.76 ?  306  ASP A CA    1 
ATOM   2203  C C     . ASP A 1 308  ? -45.517 59.439  81.664  1.00 11.08 ?  306  ASP A C     1 
ATOM   2204  O O     . ASP A 1 308  ? -45.710 60.580  82.096  1.00 12.13 ?  306  ASP A O     1 
ATOM   2205  C CB    . ASP A 1 308  ? -44.430 59.278  79.428  1.00 12.37 ?  306  ASP A CB    1 
ATOM   2206  C CG    . ASP A 1 308  ? -44.412 58.574  78.075  1.00 16.20 ?  306  ASP A CG    1 
ATOM   2207  O OD1   . ASP A 1 308  ? -45.382 57.877  77.711  1.00 16.20 ?  306  ASP A OD1   1 
ATOM   2208  O OD2   . ASP A 1 308  ? -43.382 58.718  77.370  1.00 18.37 ?  306  ASP A OD2   1 
ATOM   2209  N N     . ALA A 1 309  ? -45.084 58.435  82.437  1.00 11.08 ?  307  ALA A N     1 
ATOM   2210  C CA    . ALA A 1 309  ? -44.791 58.614  83.854  1.00 10.65 ?  307  ALA A CA    1 
ATOM   2211  C C     . ALA A 1 309  ? -43.298 58.845  84.060  1.00 12.38 ?  307  ALA A C     1 
ATOM   2212  O O     . ALA A 1 309  ? -42.456 58.176  83.450  1.00 12.78 ?  307  ALA A O     1 
ATOM   2213  C CB    . ALA A 1 309  ? -45.271 57.409  84.674  1.00 10.98 ?  307  ALA A CB    1 
ATOM   2214  N N     . GLU A 1 310  ? -42.982 59.796  84.933  1.00 12.13 ?  308  GLU A N     1 
ATOM   2215  C CA    . GLU A 1 310  ? -41.595 60.199  85.146  1.00 12.63 ?  308  GLU A CA    1 
ATOM   2216  C C     . GLU A 1 310  ? -41.183 59.983  86.601  1.00 11.80 ?  308  GLU A C     1 
ATOM   2217  O O     . GLU A 1 310  ? -41.450 58.914  87.172  1.00 12.02 ?  308  GLU A O     1 
ATOM   2218  C CB    . GLU A 1 310  ? -41.421 61.653  84.689  1.00 12.20 ?  308  GLU A CB    1 
ATOM   2219  C CG    . GLU A 1 310  ? -41.758 61.803  83.172  1.00 13.81 ?  308  GLU A CG    1 
ATOM   2220  C CD    . GLU A 1 310  ? -41.490 63.192  82.606  1.00 13.09 ?  308  GLU A CD    1 
ATOM   2221  O OE1   . GLU A 1 310  ? -40.304 63.506  82.342  1.00 16.23 ?  308  GLU A OE1   1 
ATOM   2222  O OE2   . GLU A 1 310  ? -42.478 63.948  82.417  1.00 13.50 ?  308  GLU A OE2   1 
ATOM   2223  N N     . GLU A 1 311  ? -40.528 60.965  87.210  1.00 11.84 ?  309  GLU A N     1 
ATOM   2224  C CA    . GLU A 1 311  ? -40.002 60.759  88.554  1.00 13.81 ?  309  GLU A CA    1 
ATOM   2225  C C     . GLU A 1 311  ? -41.137 60.681  89.577  1.00 10.82 ?  309  GLU A C     1 
ATOM   2226  O O     . GLU A 1 311  ? -42.247 61.188  89.368  1.00 12.36 ?  309  GLU A O     1 
ATOM   2227  C CB    . GLU A 1 311  ? -39.037 61.884  88.933  1.00 12.95 ?  309  GLU A CB    1 
ATOM   2228  C CG    . GLU A 1 311  ? -37.766 61.974  88.061  1.00 14.80 ?  309  GLU A CG    1 
ATOM   2229  C CD    . GLU A 1 311  ? -37.931 62.857  86.830  1.00 16.47 ?  309  GLU A CD    1 
ATOM   2230  O OE1   . GLU A 1 311  ? -39.062 63.202  86.462  1.00 14.91 ?  309  GLU A OE1   1 
ATOM   2231  O OE2   . GLU A 1 311  ? -36.901 63.222  86.218  1.00 21.51 ?  309  GLU A OE2   1 
ATOM   2232  N N     . ALA A 1 312  ? -40.844 60.026  90.707  1.00 12.17 ?  310  ALA A N     1 
ATOM   2233  C CA    . ALA A 1 312  ? -41.875 59.815  91.722  1.00 10.00 ?  310  ALA A CA    1 
ATOM   2234  C C     . ALA A 1 312  ? -42.436 61.130  92.259  1.00 12.18 ?  310  ALA A C     1 
ATOM   2235  O O     . ALA A 1 312  ? -43.623 61.195  92.618  1.00 13.18 ?  310  ALA A O     1 
ATOM   2236  C CB    . ALA A 1 312  ? -41.302 58.962  92.868  1.00 13.77 ?  310  ALA A CB    1 
ATOM   2237  N N     . ASP A 1 313  ? -41.622 62.187  92.328  1.00 13.33 ?  311  ASP A N     1 
ATOM   2238  C CA    . ASP A 1 313  ? -42.141 63.447  92.857  1.00 12.90 ?  311  ASP A CA    1 
ATOM   2239  C C     . ASP A 1 313  ? -43.007 64.214  91.864  1.00 12.34 ?  311  ASP A C     1 
ATOM   2240  O O     . ASP A 1 313  ? -43.480 65.308  92.204  1.00 15.26 ?  311  ASP A O     1 
ATOM   2241  C CB    . ASP A 1 313  ? -41.013 64.350  93.402  1.00 12.59 ?  311  ASP A CB    1 
ATOM   2242  C CG    . ASP A 1 313  ? -40.038 64.830  92.349  1.00 17.93 ?  311  ASP A CG    1 
ATOM   2243  O OD1   . ASP A 1 313  ? -40.217 64.533  91.155  1.00 15.07 ?  311  ASP A OD1   1 
ATOM   2244  O OD2   . ASP A 1 313  ? -39.068 65.523  92.743  1.00 21.99 ?  311  ASP A OD2   1 
ATOM   2245  N N     . ARG A 1 314  ? -43.255 63.656  90.680  1.00 11.60 ?  312  ARG A N     1 
ATOM   2246  C CA    . ARG A 1 314  ? -44.184 64.240  89.722  1.00 11.44 ?  312  ARG A CA    1 
ATOM   2247  C C     . ARG A 1 314  ? -45.482 63.455  89.592  1.00 11.83 ?  312  ARG A C     1 
ATOM   2248  O O     . ARG A 1 314  ? -46.404 63.929  88.923  1.00 13.20 ?  312  ARG A O     1 
ATOM   2249  C CB    . ARG A 1 314  ? -43.501 64.367  88.353  1.00 13.24 ?  312  ARG A CB    1 
ATOM   2250  C CG    . ARG A 1 314  ? -42.483 65.484  88.359  1.00 13.73 ?  312  ARG A CG    1 
ATOM   2251  C CD    . ARG A 1 314  ? -41.462 65.346  87.248  1.00 15.20 ?  312  ARG A CD    1 
ATOM   2252  N NE    . ARG A 1 314  ? -40.877 66.652  86.980  1.00 15.24 ?  312  ARG A NE    1 
ATOM   2253  C CZ    . ARG A 1 314  ? -39.888 66.854  86.124  1.00 13.15 ?  312  ARG A CZ    1 
ATOM   2254  N NH1   . ARG A 1 314  ? -39.296 65.845  85.512  1.00 14.74 ?  312  ARG A NH1   1 
ATOM   2255  N NH2   . ARG A 1 314  ? -39.489 68.099  85.878  1.00 15.71 ?  312  ARG A NH2   1 
ATOM   2256  N N     . LEU A 1 315  ? -45.589 62.286  90.226  1.00 12.80 ?  313  LEU A N     1 
ATOM   2257  C CA    . LEU A 1 315  ? -46.768 61.442  90.056  1.00 12.34 ?  313  LEU A CA    1 
ATOM   2258  C C     . LEU A 1 315  ? -48.042 62.173  90.461  1.00 13.23 ?  313  LEU A C     1 
ATOM   2259  O O     . LEU A 1 315  ? -48.978 62.314  89.666  1.00 12.49 ?  313  LEU A O     1 
ATOM   2260  C CB    . LEU A 1 315  ? -46.614 60.179  90.892  1.00 12.11 ?  313  LEU A CB    1 
ATOM   2261  C CG    . LEU A 1 315  ? -47.424 58.944  90.487  1.00 14.04 ?  313  LEU A CG    1 
ATOM   2262  C CD1   . LEU A 1 315  ? -47.004 57.794  91.386  1.00 15.52 ?  313  LEU A CD1   1 
ATOM   2263  C CD2   . LEU A 1 315  ? -48.941 59.119  90.547  1.00 17.07 ?  313  LEU A CD2   1 
ATOM   2264  N N     . GLU A 1 316  ? -48.110 62.619  91.709  1.00 13.84 ?  314  GLU A N     1 
ATOM   2265  C CA    . GLU A 1 316  ? -49.376 63.172  92.170  1.00 12.99 ?  314  GLU A CA    1 
ATOM   2266  C C     . GLU A 1 316  ? -49.710 64.493  91.472  1.00 13.19 ?  314  GLU A C     1 
ATOM   2267  O O     . GLU A 1 316  ? -50.883 64.753  91.166  1.00 14.89 ?  314  GLU A O     1 
ATOM   2268  C CB    . GLU A 1 316  ? -49.358 63.293  93.693  1.00 13.87 ?  314  GLU A CB    1 
ATOM   2269  C CG    . GLU A 1 316  ? -49.422 61.906  94.343  1.00 15.17 ?  314  GLU A CG    1 
ATOM   2270  C CD    . GLU A 1 316  ? -49.401 61.937  95.851  1.00 15.83 ?  314  GLU A CD    1 
ATOM   2271  O OE1   . GLU A 1 316  ? -50.116 62.761  96.436  1.00 18.16 ?  314  GLU A OE1   1 
ATOM   2272  O OE2   . GLU A 1 316  ? -48.659 61.132  96.452  1.00 17.58 ?  314  GLU A OE2   1 
ATOM   2273  N N     . LEU A 1 317  ? -48.703 65.312  91.158  1.00 14.06 ?  315  LEU A N     1 
ATOM   2274  C CA    . LEU A 1 317  ? -48.952 66.521  90.373  1.00 14.27 ?  315  LEU A CA    1 
ATOM   2275  C C     . LEU A 1 317  ? -49.594 66.186  89.029  1.00 13.51 ?  315  LEU A C     1 
ATOM   2276  O O     . LEU A 1 317  ? -50.555 66.851  88.599  1.00 13.90 ?  315  LEU A O     1 
ATOM   2277  C CB    . LEU A 1 317  ? -47.642 67.276  90.167  1.00 16.05 ?  315  LEU A CB    1 
ATOM   2278  C CG    . LEU A 1 317  ? -47.722 68.533  89.301  1.00 16.64 ?  315  LEU A CG    1 
ATOM   2279  C CD1   . LEU A 1 317  ? -48.686 69.567  89.890  1.00 18.59 ?  315  LEU A CD1   1 
ATOM   2280  C CD2   . LEU A 1 317  ? -46.330 69.098  89.186  1.00 20.88 ?  315  LEU A CD2   1 
ATOM   2281  N N     . SER A 1 318  ? -49.091 65.139  88.360  1.00 12.82 ?  316  SER A N     1 
ATOM   2282  C CA    . SER A 1 318  ? -49.656 64.765  87.065  1.00 12.11 ?  316  SER A CA    1 
ATOM   2283  C C     . SER A 1 318  ? -51.121 64.355  87.188  1.00 14.79 ?  316  SER A C     1 
ATOM   2284  O O     . SER A 1 318  ? -51.895 64.558  86.241  1.00 13.23 ?  316  SER A O     1 
ATOM   2285  C CB    . SER A 1 318  ? -48.833 63.644  86.418  1.00 12.48 ?  316  SER A CB    1 
ATOM   2286  O OG    . SER A 1 318  ? -49.040 62.397  87.049  1.00 13.10 ?  316  SER A OG    1 
ATOM   2287  N N     . LEU A 1 319  ? -51.534 63.824  88.353  1.00 13.31 ?  317  LEU A N     1 
ATOM   2288  C CA    . LEU A 1 319  ? -52.937 63.447  88.551  1.00 13.36 ?  317  LEU A CA    1 
ATOM   2289  C C     . LEU A 1 319  ? -53.853 64.660  88.505  1.00 15.59 ?  317  LEU A C     1 
ATOM   2290  O O     . LEU A 1 319  ? -55.002 64.553  88.060  1.00 14.94 ?  317  LEU A O     1 
ATOM   2291  C CB    . LEU A 1 319  ? -53.125 62.709  89.880  1.00 14.60 ?  317  LEU A CB    1 
ATOM   2292  C CG    . LEU A 1 319  ? -52.390 61.371  89.971  1.00 16.87 ?  317  LEU A CG    1 
ATOM   2293  C CD1   . LEU A 1 319  ? -52.593 60.765  91.367  1.00 16.07 ?  317  LEU A CD1   1 
ATOM   2294  C CD2   . LEU A 1 319  ? -52.871 60.414  88.893  1.00 15.43 ?  317  LEU A CD2   1 
ATOM   2295  N N     . ASP A 1 320  ? -53.369 65.829  88.938  1.00 14.23 ?  318  ASP A N     1 
ATOM   2296  C CA    . ASP A 1 320  ? -54.208 67.019  88.862  1.00 16.27 ?  318  ASP A CA    1 
ATOM   2297  C C     . ASP A 1 320  ? -54.443 67.439  87.423  1.00 17.26 ?  318  ASP A C     1 
ATOM   2298  O O     . ASP A 1 320  ? -55.526 67.936  87.095  1.00 16.95 ?  318  ASP A O     1 
ATOM   2299  C CB    . ASP A 1 320  ? -53.587 68.155  89.664  1.00 16.28 ?  318  ASP A CB    1 
ATOM   2300  C CG    . ASP A 1 320  ? -53.767 67.960  91.151  1.00 19.53 ?  318  ASP A CG    1 
ATOM   2301  O OD1   . ASP A 1 320  ? -54.934 67.815  91.577  1.00 21.15 ?  318  ASP A OD1   1 
ATOM   2302  O OD2   . ASP A 1 320  ? -52.751 67.902  91.874  1.00 22.81 ?  318  ASP A OD2   1 
ATOM   2303  N N     . LEU A 1 321  ? -53.454 67.244  86.548  1.00 13.80 ?  319  LEU A N     1 
ATOM   2304  C CA    . LEU A 1 321  ? -53.692 67.513  85.134  1.00 14.16 ?  319  LEU A CA    1 
ATOM   2305  C C     . LEU A 1 321  ? -54.643 66.487  84.535  1.00 14.64 ?  319  LEU A C     1 
ATOM   2306  O O     . LEU A 1 321  ? -55.566 66.849  83.793  1.00 14.45 ?  319  LEU A O     1 
ATOM   2307  C CB    . LEU A 1 321  ? -52.367 67.533  84.376  1.00 15.19 ?  319  LEU A CB    1 
ATOM   2308  C CG    . LEU A 1 321  ? -51.537 68.803  84.567  1.00 18.51 ?  319  LEU A CG    1 
ATOM   2309  C CD1   . LEU A 1 321  ? -50.630 68.671  85.765  1.00 20.47 ?  319  LEU A CD1   1 
ATOM   2310  C CD2   . LEU A 1 321  ? -50.729 69.076  83.296  1.00 20.38 ?  319  LEU A CD2   1 
ATOM   2311  N N     . LEU A 1 322  ? -54.447 65.203  84.854  1.00 14.31 ?  320  LEU A N     1 
ATOM   2312  C CA    . LEU A 1 322  ? -55.341 64.169  84.345  1.00 13.94 ?  320  LEU A CA    1 
ATOM   2313  C C     . LEU A 1 322  ? -56.777 64.447  84.759  1.00 14.11 ?  320  LEU A C     1 
ATOM   2314  O O     . LEU A 1 322  ? -57.696 64.325  83.945  1.00 15.05 ?  320  LEU A O     1 
ATOM   2315  C CB    . LEU A 1 322  ? -54.891 62.792  84.846  1.00 13.09 ?  320  LEU A CB    1 
ATOM   2316  C CG    . LEU A 1 322  ? -55.740 61.620  84.348  1.00 15.05 ?  320  LEU A CG    1 
ATOM   2317  C CD1   . LEU A 1 322  ? -55.584 61.462  82.843  1.00 15.66 ?  320  LEU A CD1   1 
ATOM   2318  C CD2   . LEU A 1 322  ? -55.389 60.321  85.093  1.00 13.92 ?  320  LEU A CD2   1 
ATOM   2319  N N     . GLU A 1 323  ? -56.987 64.838  86.016  1.00 14.03 ?  321  GLU A N     1 
ATOM   2320  C CA    . GLU A 1 323  ? -58.341 65.104  86.498  1.00 15.20 ?  321  GLU A CA    1 
ATOM   2321  C C     . GLU A 1 323  ? -59.003 66.230  85.705  1.00 15.98 ?  321  GLU A C     1 
ATOM   2322  O O     . GLU A 1 323  ? -60.134 66.082  85.225  1.00 17.05 ?  321  GLU A O     1 
ATOM   2323  C CB    . GLU A 1 323  ? -58.306 65.438  87.992  1.00 16.59 ?  321  GLU A CB    1 
ATOM   2324  C CG    . GLU A 1 323  ? -59.606 66.033  88.551  1.00 22.32 ?  321  GLU A CG    1 
ATOM   2325  C CD    . GLU A 1 323  ? -60.314 65.116  89.513  1.00 23.81 ?  321  GLU A CD    1 
ATOM   2326  O OE1   . GLU A 1 323  ? -59.668 64.212  90.069  1.00 29.98 ?  321  GLU A OE1   1 
ATOM   2327  O OE2   . GLU A 1 323  ? -61.533 65.306  89.720  1.00 26.23 ?  321  GLU A OE2   1 
ATOM   2328  N N     . VAL A 1 324  ? -58.321 67.374  85.564  1.00 13.37 ?  322  VAL A N     1 
ATOM   2329  C CA    . VAL A 1 324  ? -58.932 68.504  84.870  1.00 14.09 ?  322  VAL A CA    1 
ATOM   2330  C C     . VAL A 1 324  ? -59.238 68.137  83.425  1.00 14.02 ?  322  VAL A C     1 
ATOM   2331  O O     . VAL A 1 324  ? -60.315 68.458  82.904  1.00 16.66 ?  322  VAL A O     1 
ATOM   2332  C CB    . VAL A 1 324  ? -58.035 69.752  84.943  1.00 18.15 ?  322  VAL A CB    1 
ATOM   2333  C CG1   . VAL A 1 324  ? -58.657 70.880  84.132  1.00 18.75 ?  322  VAL A CG1   1 
ATOM   2334  C CG2   . VAL A 1 324  ? -57.852 70.193  86.367  1.00 19.49 ?  322  VAL A CG2   1 
ATOM   2335  N N     . LEU A 1 325  ? -58.308 67.451  82.757  1.00 12.74 ?  323  LEU A N     1 
ATOM   2336  C CA    . LEU A 1 325  ? -58.527 67.089  81.358  1.00 13.55 ?  323  LEU A CA    1 
ATOM   2337  C C     . LEU A 1 325  ? -59.717 66.151  81.206  1.00 13.97 ?  323  LEU A C     1 
ATOM   2338  O O     . LEU A 1 325  ? -60.540 66.323  80.296  1.00 13.81 ?  323  LEU A O     1 
ATOM   2339  C CB    . LEU A 1 325  ? -57.275 66.446  80.779  1.00 13.27 ?  323  LEU A CB    1 
ATOM   2340  C CG    . LEU A 1 325  ? -56.057 67.362  80.648  1.00 15.40 ?  323  LEU A CG    1 
ATOM   2341  C CD1   . LEU A 1 325  ? -54.808 66.525  80.511  1.00 16.16 ?  323  LEU A CD1   1 
ATOM   2342  C CD2   . LEU A 1 325  ? -56.217 68.248  79.439  1.00 16.11 ?  323  LEU A CD2   1 
ATOM   2343  N N     . CYS A 1 326  ? -59.831 65.156  82.087  1.00 12.98 ?  324  CYS A N     1 
ATOM   2344  C CA    . CYS A 1 326  ? -60.926 64.201  81.941  1.00 12.38 ?  324  CYS A CA    1 
ATOM   2345  C C     . CYS A 1 326  ? -62.275 64.811  82.283  1.00 14.18 ?  324  CYS A C     1 
ATOM   2346  O O     . CYS A 1 326  ? -63.304 64.276  81.850  1.00 14.53 ?  324  CYS A O     1 
ATOM   2347  C CB    . CYS A 1 326  ? -60.675 62.964  82.803  1.00 13.25 ?  324  CYS A CB    1 
ATOM   2348  S SG    . CYS A 1 326  ? -59.335 61.935  82.158  1.00 16.98 ?  324  CYS A SG    1 
ATOM   2349  N N     . LEU A 1 327  ? -62.305 65.904  83.044  1.00 13.58 ?  325  LEU A N     1 
ATOM   2350  C CA    . LEU A 1 327  ? -63.555 66.558  83.403  1.00 14.07 ?  325  LEU A CA    1 
ATOM   2351  C C     . LEU A 1 327  ? -63.890 67.720  82.478  1.00 14.59 ?  325  LEU A C     1 
ATOM   2352  O O     . LEU A 1 327  ? -64.968 68.318  82.612  1.00 15.45 ?  325  LEU A O     1 
ATOM   2353  C CB    . LEU A 1 327  ? -63.506 67.034  84.864  1.00 15.18 ?  325  LEU A CB    1 
ATOM   2354  C CG    . LEU A 1 327  ? -63.338 65.946  85.932  1.00 18.27 ?  325  LEU A CG    1 
ATOM   2355  C CD1   . LEU A 1 327  ? -63.242 66.567  87.328  1.00 23.31 ?  325  LEU A CD1   1 
ATOM   2356  C CD2   . LEU A 1 327  ? -64.477 64.962  85.874  1.00 21.72 ?  325  LEU A CD2   1 
ATOM   2357  N N     . ASP A 1 328  ? -63.001 68.036  81.534  1.00 14.74 ?  326  ASP A N     1 
ATOM   2358  C CA    . ASP A 1 328  ? -63.192 69.166  80.636  1.00 14.66 ?  326  ASP A CA    1 
ATOM   2359  C C     . ASP A 1 328  ? -64.146 68.789  79.508  1.00 14.86 ?  326  ASP A C     1 
ATOM   2360  O O     . ASP A 1 328  ? -63.822 67.945  78.664  1.00 14.37 ?  326  ASP A O     1 
ATOM   2361  C CB    . ASP A 1 328  ? -61.840 69.597  80.081  1.00 14.49 ?  326  ASP A CB    1 
ATOM   2362  C CG    . ASP A 1 328  ? -61.900 70.914  79.357  1.00 17.88 ?  326  ASP A CG    1 
ATOM   2363  O OD1   . ASP A 1 328  ? -62.842 71.148  78.572  1.00 18.82 ?  326  ASP A OD1   1 
ATOM   2364  O OD2   . ASP A 1 328  ? -60.985 71.729  79.573  1.00 20.32 ?  326  ASP A OD2   1 
ATOM   2365  N N     . GLY A 1 329  ? -65.304 69.442  79.475  1.00 15.07 ?  327  GLY A N     1 
ATOM   2366  C CA    . GLY A 1 329  ? -66.301 69.126  78.462  1.00 15.81 ?  327  GLY A CA    1 
ATOM   2367  C C     . GLY A 1 329  ? -65.829 69.292  77.028  1.00 17.33 ?  327  GLY A C     1 
ATOM   2368  O O     . GLY A 1 329  ? -66.354 68.642  76.125  1.00 15.31 ?  327  GLY A O     1 
ATOM   2369  N N     . ASP A 1 330  ? -64.840 70.156  76.782  1.00 14.63 ?  328  ASP A N     1 
ATOM   2370  C CA    . ASP A 1 330  ? -64.366 70.324  75.408  1.00 14.40 ?  328  ASP A CA    1 
ATOM   2371  C C     . ASP A 1 330  ? -63.735 69.056  74.842  1.00 13.80 ?  328  ASP A C     1 
ATOM   2372  O O     . ASP A 1 330  ? -63.585 68.944  73.623  1.00 15.69 ?  328  ASP A O     1 
ATOM   2373  C CB    . ASP A 1 330  ? -63.320 71.442  75.304  1.00 15.51 ?  328  ASP A CB    1 
ATOM   2374  C CG    . ASP A 1 330  ? -63.901 72.820  75.512  1.00 21.24 ?  328  ASP A CG    1 
ATOM   2375  O OD1   . ASP A 1 330  ? -65.102 73.018  75.241  1.00 21.63 ?  328  ASP A OD1   1 
ATOM   2376  O OD2   . ASP A 1 330  ? -63.137 73.714  75.933  1.00 19.40 ?  328  ASP A OD2   1 
ATOM   2377  N N     . LEU A 1 331  ? -63.325 68.117  75.694  1.00 12.84 ?  329  LEU A N     1 
ATOM   2378  C CA    . LEU A 1 331  ? -62.705 66.881  75.247  1.00 12.40 ?  329  LEU A CA    1 
ATOM   2379  C C     . LEU A 1 331  ? -63.675 65.711  75.244  1.00 14.15 ?  329  LEU A C     1 
ATOM   2380  O O     . LEU A 1 331  ? -63.255 64.574  75.000  1.00 14.49 ?  329  LEU A O     1 
ATOM   2381  C CB    . LEU A 1 331  ? -61.495 66.554  76.126  1.00 14.16 ?  329  LEU A CB    1 
ATOM   2382  C CG    . LEU A 1 331  ? -60.300 67.486  75.921  1.00 12.52 ?  329  LEU A CG    1 
ATOM   2383  C CD1   . LEU A 1 331  ? -59.273 67.282  77.018  1.00 13.30 ?  329  LEU A CD1   1 
ATOM   2384  C CD2   . LEU A 1 331  ? -59.641 67.180  74.588  1.00 14.34 ?  329  LEU A CD2   1 
ATOM   2385  N N     . SER A 1 332  ? -64.956 65.955  75.515  1.00 15.13 ?  330  SER A N     1 
ATOM   2386  C CA    . SER A 1 332  ? -65.893 64.845  75.623  1.00 16.19 ?  330  SER A CA    1 
ATOM   2387  C C     . SER A 1 332  ? -66.092 64.176  74.265  1.00 15.37 ?  330  SER A C     1 
ATOM   2388  O O     . SER A 1 332  ? -65.979 64.804  73.211  1.00 16.76 ?  330  SER A O     1 
ATOM   2389  C CB    . SER A 1 332  ? -67.229 65.325  76.185  1.00 17.77 ?  330  SER A CB    1 
ATOM   2390  O OG    . SER A 1 332  ? -67.937 66.094  75.248  1.00 21.29 ?  330  SER A OG    1 
ATOM   2391  N N     . GLY A 1 333  ? -66.395 62.879  74.309  1.00 13.86 ?  331  GLY A N     1 
ATOM   2392  C CA    . GLY A 1 333  ? -66.619 62.085  73.121  1.00 15.48 ?  331  GLY A CA    1 
ATOM   2393  C C     . GLY A 1 333  ? -65.398 61.344  72.635  1.00 17.46 ?  331  GLY A C     1 
ATOM   2394  O O     . GLY A 1 333  ? -65.500 60.568  71.675  1.00 21.23 ?  331  GLY A O     1 
ATOM   2395  N N     . TRP A 1 334  ? -64.256 61.560  73.270  1.00 15.26 ?  332  TRP A N     1 
ATOM   2396  C CA    . TRP A 1 334  ? -62.983 60.982  72.881  1.00 13.87 ?  332  TRP A CA    1 
ATOM   2397  C C     . TRP A 1 334  ? -62.452 60.160  74.042  1.00 13.03 ?  332  TRP A C     1 
ATOM   2398  O O     . TRP A 1 334  ? -62.384 60.656  75.166  1.00 14.20 ?  332  TRP A O     1 
ATOM   2399  C CB    . TRP A 1 334  ? -62.014 62.106  72.522  1.00 13.64 ?  332  TRP A CB    1 
ATOM   2400  C CG    . TRP A 1 334  ? -60.583 61.740  72.330  1.00 13.46 ?  332  TRP A CG    1 
ATOM   2401  C CD1   . TRP A 1 334  ? -60.048 60.988  71.324  1.00 12.03 ?  332  TRP A CD1   1 
ATOM   2402  C CD2   . TRP A 1 334  ? -59.493 62.208  73.114  1.00 11.77 ?  332  TRP A CD2   1 
ATOM   2403  N NE1   . TRP A 1 334  ? -58.674 60.927  71.458  1.00 12.64 ?  332  TRP A NE1   1 
ATOM   2404  C CE2   . TRP A 1 334  ? -58.310 61.676  72.548  1.00 12.24 ?  332  TRP A CE2   1 
ATOM   2405  C CE3   . TRP A 1 334  ? -59.396 63.003  74.262  1.00 14.10 ?  332  TRP A CE3   1 
ATOM   2406  C CZ2   . TRP A 1 334  ? -57.050 61.921  73.087  1.00 12.84 ?  332  TRP A CZ2   1 
ATOM   2407  C CZ3   . TRP A 1 334  ? -58.140 63.251  74.795  1.00 12.24 ?  332  TRP A CZ3   1 
ATOM   2408  C CH2   . TRP A 1 334  ? -56.980 62.717  74.204  1.00 13.78 ?  332  TRP A CH2   1 
ATOM   2409  N N     . ASN A 1 335  ? -62.079 58.906  73.772  1.00 13.07 ?  333  ASN A N     1 
ATOM   2410  C CA    . ASN A 1 335  ? -61.557 57.994  74.786  1.00 13.34 ?  333  ASN A CA    1 
ATOM   2411  C C     . ASN A 1 335  ? -60.062 57.761  74.641  1.00 12.21 ?  333  ASN A C     1 
ATOM   2412  O O     . ASN A 1 335  ? -59.535 56.776  75.183  1.00 13.95 ?  333  ASN A O     1 
ATOM   2413  C CB    . ASN A 1 335  ? -62.284 56.646  74.727  1.00 13.00 ?  333  ASN A CB    1 
ATOM   2414  C CG    . ASN A 1 335  ? -63.635 56.681  75.401  1.00 15.77 ?  333  ASN A CG    1 
ATOM   2415  O OD1   . ASN A 1 335  ? -63.887 57.484  76.303  1.00 15.28 ?  333  ASN A OD1   1 
ATOM   2416  N ND2   . ASN A 1 335  ? -64.526 55.792  74.959  1.00 18.14 ?  333  ASN A ND2   1 
ATOM   2417  N N     . GLY A 1 336  ? -59.370 58.629  73.895  1.00 13.57 ?  334  GLY A N     1 
ATOM   2418  C CA    . GLY A 1 336  ? -57.962 58.416  73.618  1.00 12.96 ?  334  GLY A CA    1 
ATOM   2419  C C     . GLY A 1 336  ? -56.984 58.897  74.674  1.00 12.19 ?  334  GLY A C     1 
ATOM   2420  O O     . GLY A 1 336  ? -55.793 58.615  74.545  1.00 12.61 ?  334  GLY A O     1 
ATOM   2421  N N     . MET A 1 337  ? -57.427 59.619  75.703  1.00 12.66 ?  335  MET A N     1 
ATOM   2422  C CA    A MET A 1 337  ? -56.508 60.047  76.751  0.52 12.07 ?  335  MET A CA    1 
ATOM   2423  C CA    B MET A 1 337  ? -56.500 60.046  76.744  0.48 12.08 ?  335  MET A CA    1 
ATOM   2424  C C     . MET A 1 337  ? -55.955 58.842  77.504  1.00 12.12 ?  335  MET A C     1 
ATOM   2425  O O     . MET A 1 337  ? -56.721 57.984  77.974  1.00 13.23 ?  335  MET A O     1 
ATOM   2426  C CB    A MET A 1 337  ? -57.213 61.001  77.714  0.52 14.66 ?  335  MET A CB    1 
ATOM   2427  C CB    B MET A 1 337  ? -57.169 61.024  77.706  0.48 14.65 ?  335  MET A CB    1 
ATOM   2428  C CG    A MET A 1 337  ? -56.285 61.650  78.712  0.52 16.66 ?  335  MET A CG    1 
ATOM   2429  C CG    B MET A 1 337  ? -56.294 61.392  78.897  0.48 16.87 ?  335  MET A CG    1 
ATOM   2430  S SD    A MET A 1 337  ? -55.287 62.931  77.950  0.52 17.90 ?  335  MET A SD    1 
ATOM   2431  S SD    B MET A 1 337  ? -56.378 63.152  79.259  0.48 17.26 ?  335  MET A SD    1 
ATOM   2432  C CE    A MET A 1 337  ? -56.469 64.255  77.724  0.52 19.65 ?  335  MET A CE    1 
ATOM   2433  C CE    B MET A 1 337  ? -55.734 63.796  77.713  0.48 14.04 ?  335  MET A CE    1 
ATOM   2434  N N     . GLY A 1 338  ? -54.618 58.781  77.617  1.00 12.28 ?  336  GLY A N     1 
ATOM   2435  C CA    . GLY A 1 338  ? -53.952 57.690  78.296  1.00 13.16 ?  336  GLY A CA    1 
ATOM   2436  C C     . GLY A 1 338  ? -52.981 58.185  79.354  1.00 11.60 ?  336  GLY A C     1 
ATOM   2437  O O     . GLY A 1 338  ? -52.576 59.346  79.368  1.00 12.44 ?  336  GLY A O     1 
ATOM   2438  N N     . PHE A 1 339  ? -52.635 57.274  80.266  1.00 10.92 ?  337  PHE A N     1 
ATOM   2439  C CA    . PHE A 1 339  ? -51.856 57.632  81.447  1.00 11.43 ?  337  PHE A CA    1 
ATOM   2440  C C     . PHE A 1 339  ? -51.079 56.419  81.941  1.00 13.19 ?  337  PHE A C     1 
ATOM   2441  O O     . PHE A 1 339  ? -51.650 55.334  82.095  1.00 12.41 ?  337  PHE A O     1 
ATOM   2442  C CB    . PHE A 1 339  ? -52.804 58.158  82.532  1.00 11.54 ?  337  PHE A CB    1 
ATOM   2443  C CG    . PHE A 1 339  ? -52.124 58.835  83.691  1.00 11.87 ?  337  PHE A CG    1 
ATOM   2444  C CD1   . PHE A 1 339  ? -51.828 60.197  83.644  1.00 12.83 ?  337  PHE A CD1   1 
ATOM   2445  C CD2   . PHE A 1 339  ? -51.802 58.116  84.836  1.00 11.89 ?  337  PHE A CD2   1 
ATOM   2446  C CE1   . PHE A 1 339  ? -51.227 60.829  84.739  1.00 14.12 ?  337  PHE A CE1   1 
ATOM   2447  C CE2   . PHE A 1 339  ? -51.199 58.739  85.927  1.00 14.03 ?  337  PHE A CE2   1 
ATOM   2448  C CZ    . PHE A 1 339  ? -50.913 60.098  85.870  1.00 14.92 ?  337  PHE A CZ    1 
ATOM   2449  N N     . VAL A 1 340  ? -49.772 56.598  82.184  1.00 12.04 ?  338  VAL A N     1 
ATOM   2450  C CA    . VAL A 1 340  ? -48.906 55.525  82.663  1.00 10.63 ?  338  VAL A CA    1 
ATOM   2451  C C     . VAL A 1 340  ? -48.916 55.473  84.182  1.00 11.32 ?  338  VAL A C     1 
ATOM   2452  O O     . VAL A 1 340  ? -48.900 56.514  84.844  1.00 12.44 ?  338  VAL A O     1 
ATOM   2453  C CB    . VAL A 1 340  ? -47.471 55.745  82.154  1.00 10.68 ?  338  VAL A CB    1 
ATOM   2454  C CG1   . VAL A 1 340  ? -46.547 54.655  82.691  1.00 12.67 ?  338  VAL A CG1   1 
ATOM   2455  C CG2   . VAL A 1 340  ? -47.473 55.810  80.637  1.00 13.00 ?  338  VAL A CG2   1 
ATOM   2456  N N     . VAL A 1 341  ? -48.929 54.265  84.741  1.00 12.31 ?  339  VAL A N     1 
ATOM   2457  C CA    A VAL A 1 341  ? -48.699 54.057  86.167  0.56 11.64 ?  339  VAL A CA    1 
ATOM   2458  C CA    B VAL A 1 341  ? -48.684 54.071  86.167  0.44 11.65 ?  339  VAL A CA    1 
ATOM   2459  C C     . VAL A 1 341  ? -47.565 53.054  86.328  1.00 11.80 ?  339  VAL A C     1 
ATOM   2460  O O     . VAL A 1 341  ? -47.514 52.044  85.614  1.00 13.30 ?  339  VAL A O     1 
ATOM   2461  C CB    A VAL A 1 341  ? -49.964 53.569  86.901  0.56 12.99 ?  339  VAL A CB    1 
ATOM   2462  C CB    B VAL A 1 341  ? -49.947 53.636  86.945  0.44 13.02 ?  339  VAL A CB    1 
ATOM   2463  C CG1   A VAL A 1 341  ? -49.788 53.772  88.394  0.56 14.93 ?  339  VAL A CG1   1 
ATOM   2464  C CG1   B VAL A 1 341  ? -51.017 54.714  86.861  0.44 14.60 ?  339  VAL A CG1   1 
ATOM   2465  C CG2   A VAL A 1 341  ? -51.190 54.312  86.399  0.56 14.97 ?  339  VAL A CG2   1 
ATOM   2466  C CG2   B VAL A 1 341  ? -50.464 52.294  86.466  0.44 13.29 ?  339  VAL A CG2   1 
ATOM   2467  N N     . GLN A 1 342  ? -46.652 53.336  87.262  1.00 11.56 ?  340  GLN A N     1 
ATOM   2468  C CA    . GLN A 1 342  ? -45.436 52.551  87.453  1.00 13.54 ?  340  GLN A CA    1 
ATOM   2469  C C     . GLN A 1 342  ? -45.605 51.572  88.610  1.00 13.04 ?  340  GLN A C     1 
ATOM   2470  O O     . GLN A 1 342  ? -45.747 51.982  89.768  1.00 14.90 ?  340  GLN A O     1 
ATOM   2471  C CB    . GLN A 1 342  ? -44.249 53.479  87.711  1.00 11.63 ?  340  GLN A CB    1 
ATOM   2472  C CG    . GLN A 1 342  ? -43.953 54.461  86.553  1.00 11.17 ?  340  GLN A CG    1 
ATOM   2473  C CD    . GLN A 1 342  ? -43.365 55.773  87.034  1.00 12.22 ?  340  GLN A CD    1 
ATOM   2474  O OE1   . GLN A 1 342  ? -43.870 56.376  87.987  1.00 13.05 ?  340  GLN A OE1   1 
ATOM   2475  N NE2   . GLN A 1 342  ? -42.312 56.245  86.353  1.00 11.75 ?  340  GLN A NE2   1 
ATOM   2476  N N     . ALA A 1 343  ? -45.534 50.277  88.296  1.00 12.54 ?  341  ALA A N     1 
ATOM   2477  C CA    . ALA A 1 343  ? -45.731 49.236  89.303  1.00 14.61 ?  341  ALA A CA    1 
ATOM   2478  C C     . ALA A 1 343  ? -44.582 49.135  90.300  1.00 15.27 ?  341  ALA A C     1 
ATOM   2479  O O     . ALA A 1 343  ? -44.760 48.526  91.361  1.00 15.26 ?  341  ALA A O     1 
ATOM   2480  C CB    . ALA A 1 343  ? -45.923 47.889  88.618  1.00 16.76 ?  341  ALA A CB    1 
ATOM   2481  N N     . TYR A 1 344  ? -43.399 49.681  89.990  1.00 14.21 ?  342  TYR A N     1 
ATOM   2482  C CA    . TYR A 1 344  ? -42.366 49.678  91.024  1.00 14.20 ?  342  TYR A CA    1 
ATOM   2483  C C     . TYR A 1 344  ? -42.651 50.682  92.128  1.00 15.39 ?  342  TYR A C     1 
ATOM   2484  O O     . TYR A 1 344  ? -41.909 50.716  93.114  1.00 15.80 ?  342  TYR A O     1 
ATOM   2485  C CB    . TYR A 1 344  ? -40.953 49.903  90.431  1.00 13.79 ?  342  TYR A CB    1 
ATOM   2486  C CG    . TYR A 1 344  ? -40.518 51.262  89.875  1.00 12.87 ?  342  TYR A CG    1 
ATOM   2487  C CD1   . TYR A 1 344  ? -41.372 52.363  89.783  1.00 13.69 ?  342  TYR A CD1   1 
ATOM   2488  C CD2   . TYR A 1 344  ? -39.216 51.414  89.419  1.00 12.95 ?  342  TYR A CD2   1 
ATOM   2489  C CE1   . TYR A 1 344  ? -40.919 53.578  89.248  1.00 13.52 ?  342  TYR A CE1   1 
ATOM   2490  C CE2   . TYR A 1 344  ? -38.760 52.603  88.900  1.00 12.82 ?  342  TYR A CE2   1 
ATOM   2491  C CZ    . TYR A 1 344  ? -39.608 53.685  88.819  1.00 11.58 ?  342  TYR A CZ    1 
ATOM   2492  O OH    . TYR A 1 344  ? -39.139 54.866  88.304  1.00 11.66 ?  342  TYR A OH    1 
ATOM   2493  N N     . GLY A 1 345  ? -43.716 51.467  92.002  1.00 12.81 ?  343  GLY A N     1 
ATOM   2494  C CA    . GLY A 1 345  ? -44.040 52.497  92.974  1.00 13.24 ?  343  GLY A CA    1 
ATOM   2495  C C     . GLY A 1 345  ? -45.055 52.006  93.993  1.00 13.55 ?  343  GLY A C     1 
ATOM   2496  O O     . GLY A 1 345  ? -46.014 51.304  93.655  1.00 14.70 ?  343  GLY A O     1 
ATOM   2497  N N     . LYS A 1 346  ? -44.830 52.397  95.249  1.00 13.56 ?  344  LYS A N     1 
ATOM   2498  C CA    . LYS A 1 346  ? -45.670 51.915  96.340  1.00 14.29 ?  344  LYS A CA    1 
ATOM   2499  C C     . LYS A 1 346  ? -47.096 52.441  96.258  1.00 15.19 ?  344  LYS A C     1 
ATOM   2500  O O     . LYS A 1 346  ? -48.001 51.836  96.840  1.00 16.42 ?  344  LYS A O     1 
ATOM   2501  C CB    . LYS A 1 346  ? -45.043 52.297  97.680  1.00 14.28 ?  344  LYS A CB    1 
ATOM   2502  C CG    . LYS A 1 346  ? -43.703 51.617  97.933  1.00 15.59 ?  344  LYS A CG    1 
ATOM   2503  C CD    . LYS A 1 346  ? -43.018 52.166  99.161  1.00 17.28 ?  344  LYS A CD    1 
ATOM   2504  C CE    . LYS A 1 346  ? -41.780 51.359  99.491  1.00 19.13 ?  344  LYS A CE    1 
ATOM   2505  N NZ    . LYS A 1 346  ? -41.023 51.941  100.639 1.00 19.66 ?  344  LYS A NZ    1 
ATOM   2506  N N     . ARG A 1 347  ? -47.319 53.542  95.546  1.00 15.08 ?  345  ARG A N     1 
ATOM   2507  C CA    . ARG A 1 347  ? -48.653 54.116  95.419  1.00 13.84 ?  345  ARG A CA    1 
ATOM   2508  C C     . ARG A 1 347  ? -49.471 53.506  94.280  1.00 15.35 ?  345  ARG A C     1 
ATOM   2509  O O     . ARG A 1 347  ? -50.667 53.803  94.171  1.00 16.17 ?  345  ARG A O     1 
ATOM   2510  C CB    . ARG A 1 347  ? -48.537 55.638  95.225  1.00 14.02 ?  345  ARG A CB    1 
ATOM   2511  C CG    . ARG A 1 347  ? -47.998 56.350  96.464  1.00 16.05 ?  345  ARG A CG    1 
ATOM   2512  C CD    . ARG A 1 347  ? -47.579 57.766  96.167  1.00 12.14 ?  345  ARG A CD    1 
ATOM   2513  N NE    . ARG A 1 347  ? -46.350 57.809  95.374  1.00 13.85 ?  345  ARG A NE    1 
ATOM   2514  C CZ    . ARG A 1 347  ? -45.864 58.896  94.790  1.00 13.73 ?  345  ARG A CZ    1 
ATOM   2515  N NH1   . ARG A 1 347  ? -46.452 60.076  94.918  1.00 14.12 ?  345  ARG A NH1   1 
ATOM   2516  N NH2   . ARG A 1 347  ? -44.767 58.797  94.040  1.00 13.83 ?  345  ARG A NH2   1 
ATOM   2517  N N     . CYS A 1 348  ? -48.874 52.648  93.454  1.00 14.97 ?  346  CYS A N     1 
ATOM   2518  C CA    . CYS A 1 348  ? -49.505 52.204  92.208  1.00 15.13 ?  346  CYS A CA    1 
ATOM   2519  C C     . CYS A 1 348  ? -50.938 51.690  92.360  1.00 16.85 ?  346  CYS A C     1 
ATOM   2520  O O     . CYS A 1 348  ? -51.814 52.164  91.616  1.00 15.12 ?  346  CYS A O     1 
ATOM   2521  C CB    . CYS A 1 348  ? -48.613 51.147  91.541  1.00 16.88 ?  346  CYS A CB    1 
ATOM   2522  S SG    . CYS A 1 348  ? -49.102 50.817  89.828  1.00 19.90 ?  346  CYS A SG    1 
ATOM   2523  N N     . PRO A 1 349  ? -51.255 50.744  93.253  1.00 16.79 ?  347  PRO A N     1 
ATOM   2524  C CA    . PRO A 1 349  ? -52.656 50.288  93.327  1.00 14.92 ?  347  PRO A CA    1 
ATOM   2525  C C     . PRO A 1 349  ? -53.615 51.399  93.708  1.00 14.95 ?  347  PRO A C     1 
ATOM   2526  O O     . PRO A 1 349  ? -54.765 51.406  93.251  1.00 17.42 ?  347  PRO A O     1 
ATOM   2527  C CB    . PRO A 1 349  ? -52.622 49.177  94.389  1.00 19.36 ?  347  PRO A CB    1 
ATOM   2528  C CG    . PRO A 1 349  ? -51.395 49.431  95.178  1.00 19.13 ?  347  PRO A CG    1 
ATOM   2529  C CD    . PRO A 1 349  ? -50.404 50.081  94.262  1.00 16.55 ?  347  PRO A CD    1 
ATOM   2530  N N     . PHE A 1 350  ? -53.165 52.350  94.524  1.00 16.77 ?  348  PHE A N     1 
ATOM   2531  C CA    . PHE A 1 350  ? -54.027 53.435  94.972  1.00 17.29 ?  348  PHE A CA    1 
ATOM   2532  C C     . PHE A 1 350  ? -54.216 54.469  93.874  1.00 15.70 ?  348  PHE A C     1 
ATOM   2533  O O     . PHE A 1 350  ? -55.298 55.054  93.736  1.00 16.48 ?  348  PHE A O     1 
ATOM   2534  C CB    . PHE A 1 350  ? -53.438 54.055  96.237  1.00 18.47 ?  348  PHE A CB    1 
ATOM   2535  C CG    . PHE A 1 350  ? -53.094 53.036  97.278  1.00 17.43 ?  348  PHE A CG    1 
ATOM   2536  C CD1   . PHE A 1 350  ? -54.096 52.462  98.044  1.00 19.07 ?  348  PHE A CD1   1 
ATOM   2537  C CD2   . PHE A 1 350  ? -51.791 52.614  97.463  1.00 18.62 ?  348  PHE A CD2   1 
ATOM   2538  C CE1   . PHE A 1 350  ? -53.798 51.502  98.995  1.00 21.58 ?  348  PHE A CE1   1 
ATOM   2539  C CE2   . PHE A 1 350  ? -51.488 51.639  98.415  1.00 18.71 ?  348  PHE A CE2   1 
ATOM   2540  C CZ    . PHE A 1 350  ? -52.488 51.096  99.180  1.00 20.22 ?  348  PHE A CZ    1 
ATOM   2541  N N     . VAL A 1 351  ? -53.171 54.693  93.080  1.00 14.68 ?  349  VAL A N     1 
ATOM   2542  C CA    . VAL A 1 351  ? -53.303 55.530  91.892  1.00 13.01 ?  349  VAL A CA    1 
ATOM   2543  C C     . VAL A 1 351  ? -54.317 54.923  90.935  1.00 14.79 ?  349  VAL A C     1 
ATOM   2544  O O     . VAL A 1 351  ? -55.157 55.631  90.360  1.00 14.10 ?  349  VAL A O     1 
ATOM   2545  C CB    . VAL A 1 351  ? -51.927 55.710  91.219  1.00 14.57 ?  349  VAL A CB    1 
ATOM   2546  C CG1   . VAL A 1 351  ? -52.070 56.493  89.912  1.00 14.18 ?  349  VAL A CG1   1 
ATOM   2547  C CG2   . VAL A 1 351  ? -50.964 56.427  92.173  1.00 15.39 ?  349  VAL A CG2   1 
ATOM   2548  N N     . LEU A 1 352  ? -54.259 53.598  90.749  1.00 16.04 ?  350  LEU A N     1 
ATOM   2549  C CA    . LEU A 1 352  ? -55.222 52.933  89.879  1.00 15.92 ?  350  LEU A CA    1 
ATOM   2550  C C     . LEU A 1 352  ? -56.644 53.081  90.414  1.00 14.63 ?  350  LEU A C     1 
ATOM   2551  O O     . LEU A 1 352  ? -57.576 53.317  89.638  1.00 17.38 ?  350  LEU A O     1 
ATOM   2552  C CB    . LEU A 1 352  ? -54.851 51.452  89.715  1.00 15.95 ?  350  LEU A CB    1 
ATOM   2553  C CG    . LEU A 1 352  ? -53.603 51.215  88.856  1.00 15.13 ?  350  LEU A CG    1 
ATOM   2554  C CD1   . LEU A 1 352  ? -53.216 49.748  88.878  1.00 18.21 ?  350  LEU A CD1   1 
ATOM   2555  C CD2   . LEU A 1 352  ? -53.849 51.659  87.424  1.00 17.98 ?  350  LEU A CD2   1 
ATOM   2556  N N     . ASP A 1 353  ? -56.834 52.937  91.735  1.00 16.59 ?  351  ASP A N     1 
ATOM   2557  C CA    . ASP A 1 353  ? -58.158 53.183  92.314  1.00 16.40 ?  351  ASP A CA    1 
ATOM   2558  C C     . ASP A 1 353  ? -58.651 54.579  91.951  1.00 14.80 ?  351  ASP A C     1 
ATOM   2559  O O     . ASP A 1 353  ? -59.824 54.773  91.598  1.00 18.44 ?  351  ASP A O     1 
ATOM   2560  C CB    . ASP A 1 353  ? -58.124 53.033  93.837  1.00 17.16 ?  351  ASP A CB    1 
ATOM   2561  C CG    . ASP A 1 353  ? -57.976 51.598  94.295  1.00 20.08 ?  351  ASP A CG    1 
ATOM   2562  O OD1   . ASP A 1 353  ? -58.239 50.664  93.510  1.00 21.20 ?  351  ASP A OD1   1 
ATOM   2563  O OD2   . ASP A 1 353  ? -57.585 51.419  95.463  1.00 24.39 ?  351  ASP A OD2   1 
ATOM   2564  N N     . PHE A 1 354  ? -57.772 55.574  92.066  1.00 15.84 ?  352  PHE A N     1 
ATOM   2565  C CA    . PHE A 1 354  ? -58.156 56.936  91.720  1.00 15.73 ?  352  PHE A CA    1 
ATOM   2566  C C     . PHE A 1 354  ? -58.512 57.054  90.240  1.00 16.14 ?  352  PHE A C     1 
ATOM   2567  O O     . PHE A 1 354  ? -59.510 57.692  89.887  1.00 16.57 ?  352  PHE A O     1 
ATOM   2568  C CB    . PHE A 1 354  ? -57.030 57.903  92.100  1.00 15.06 ?  352  PHE A CB    1 
ATOM   2569  C CG    . PHE A 1 354  ? -57.197 59.275  91.539  1.00 14.40 ?  352  PHE A CG    1 
ATOM   2570  C CD1   . PHE A 1 354  ? -57.938 60.227  92.218  1.00 18.34 ?  352  PHE A CD1   1 
ATOM   2571  C CD2   . PHE A 1 354  ? -56.598 59.622  90.330  1.00 16.24 ?  352  PHE A CD2   1 
ATOM   2572  C CE1   . PHE A 1 354  ? -58.108 61.501  91.682  1.00 19.78 ?  352  PHE A CE1   1 
ATOM   2573  C CE2   . PHE A 1 354  ? -56.758 60.890  89.799  1.00 17.86 ?  352  PHE A CE2   1 
ATOM   2574  C CZ    . PHE A 1 354  ? -57.511 61.828  90.480  1.00 17.35 ?  352  PHE A CZ    1 
ATOM   2575  N N     . ILE A 1 355  ? -57.685 56.473  89.355  1.00 15.01 ?  353  ILE A N     1 
ATOM   2576  C CA    . ILE A 1 355  ? -57.914 56.582  87.913  1.00 14.98 ?  353  ILE A CA    1 
ATOM   2577  C C     . ILE A 1 355  ? -59.203 55.880  87.510  1.00 14.80 ?  353  ILE A C     1 
ATOM   2578  O O     . ILE A 1 355  ? -59.980 56.401  86.704  1.00 16.24 ?  353  ILE A O     1 
ATOM   2579  C CB    . ILE A 1 355  ? -56.712 56.023  87.134  1.00 14.19 ?  353  ILE A CB    1 
ATOM   2580  C CG1   . ILE A 1 355  ? -55.495 56.917  87.350  1.00 15.57 ?  353  ILE A CG1   1 
ATOM   2581  C CG2   . ILE A 1 355  ? -57.030 55.933  85.646  1.00 14.82 ?  353  ILE A CG2   1 
ATOM   2582  C CD1   . ILE A 1 355  ? -54.233 56.341  86.752  1.00 16.12 ?  353  ILE A CD1   1 
ATOM   2583  N N     . ILE A 1 356  ? -59.444 54.678  88.045  1.00 15.66 ?  354  ILE A N     1 
ATOM   2584  C CA    . ILE A 1 356  ? -60.662 53.946  87.701  1.00 15.30 ?  354  ILE A CA    1 
ATOM   2585  C C     . ILE A 1 356  ? -61.893 54.735  88.133  1.00 15.82 ?  354  ILE A C     1 
ATOM   2586  O O     . ILE A 1 356  ? -62.879 54.833  87.391  1.00 16.89 ?  354  ILE A O     1 
ATOM   2587  C CB    . ILE A 1 356  ? -60.620 52.535  88.323  1.00 17.66 ?  354  ILE A CB    1 
ATOM   2588  C CG1   . ILE A 1 356  ? -59.569 51.672  87.620  1.00 18.18 ?  354  ILE A CG1   1 
ATOM   2589  C CG2   . ILE A 1 356  ? -61.981 51.867  88.226  1.00 17.82 ?  354  ILE A CG2   1 
ATOM   2590  C CD1   . ILE A 1 356  ? -59.169 50.440  88.407  1.00 20.60 ?  354  ILE A CD1   1 
ATOM   2591  N N     . ASP A 1 357  ? -61.842 55.342  89.321  1.00 15.34 ?  355  ASP A N     1 
ATOM   2592  C CA    . ASP A 1 357  ? -62.952 56.177  89.769  1.00 16.54 ?  355  ASP A CA    1 
ATOM   2593  C C     . ASP A 1 357  ? -63.111 57.422  88.894  1.00 16.65 ?  355  ASP A C     1 
ATOM   2594  O O     . ASP A 1 357  ? -64.242 57.843  88.597  1.00 16.26 ?  355  ASP A O     1 
ATOM   2595  C CB    . ASP A 1 357  ? -62.747 56.579  91.224  1.00 17.94 ?  355  ASP A CB    1 
ATOM   2596  C CG    . ASP A 1 357  ? -63.794 57.565  91.692  1.00 17.07 ?  355  ASP A CG    1 
ATOM   2597  O OD1   . ASP A 1 357  ? -64.933 57.125  91.965  1.00 23.69 ?  355  ASP A OD1   1 
ATOM   2598  O OD2   . ASP A 1 357  ? -63.484 58.777  91.769  1.00 18.20 ?  355  ASP A OD2   1 
ATOM   2599  N N     . LEU A 1 358  ? -61.996 58.039  88.488  1.00 14.33 ?  356  LEU A N     1 
ATOM   2600  C CA    . LEU A 1 358  ? -62.078 59.189  87.590  1.00 14.49 ?  356  LEU A CA    1 
ATOM   2601  C C     . LEU A 1 358  ? -62.708 58.802  86.256  1.00 13.67 ?  356  LEU A C     1 
ATOM   2602  O O     . LEU A 1 358  ? -63.519 59.552  85.700  1.00 16.56 ?  356  LEU A O     1 
ATOM   2603  C CB    . LEU A 1 358  ? -60.682 59.784  87.382  1.00 13.22 ?  356  LEU A CB    1 
ATOM   2604  C CG    . LEU A 1 358  ? -60.567 60.922  86.361  1.00 14.12 ?  356  LEU A CG    1 
ATOM   2605  C CD1   . LEU A 1 358  ? -61.384 62.133  86.804  1.00 16.58 ?  356  LEU A CD1   1 
ATOM   2606  C CD2   . LEU A 1 358  ? -59.089 61.295  86.170  1.00 15.21 ?  356  LEU A CD2   1 
ATOM   2607  N N     . ALA A 1 359  ? -62.355 57.621  85.739  1.00 15.77 ?  357  ALA A N     1 
ATOM   2608  C CA    . ALA A 1 359  ? -62.964 57.128  84.509  1.00 15.58 ?  357  ALA A CA    1 
ATOM   2609  C C     . ALA A 1 359  ? -64.467 56.936  84.679  1.00 15.86 ?  357  ALA A C     1 
ATOM   2610  O O     . ALA A 1 359  ? -65.243 57.256  83.772  1.00 16.66 ?  357  ALA A O     1 
ATOM   2611  C CB    . ALA A 1 359  ? -62.290 55.818  84.086  1.00 17.89 ?  357  ALA A CB    1 
ATOM   2612  N N     . ARG A 1 360  ? -64.896 56.428  85.839  1.00 15.88 ?  358  ARG A N     1 
ATOM   2613  C CA    . ARG A 1 360  ? -66.326 56.282  86.111  1.00 17.02 ?  358  ARG A CA    1 
ATOM   2614  C C     . ARG A 1 360  ? -67.022 57.641  86.163  1.00 19.13 ?  358  ARG A C     1 
ATOM   2615  O O     . ARG A 1 360  ? -68.061 57.849  85.519  1.00 20.07 ?  358  ARG A O     1 
ATOM   2616  C CB    . ARG A 1 360  ? -66.544 55.513  87.417  1.00 19.25 ?  358  ARG A CB    1 
ATOM   2617  C CG    . ARG A 1 360  ? -66.260 54.027  87.310  1.00 25.18 ?  358  ARG A CG    1 
ATOM   2618  C CD    . ARG A 1 360  ? -66.786 53.249  88.523  1.00 24.61 ?  358  ARG A CD    1 
ATOM   2619  N NE    . ARG A 1 360  ? -65.956 52.081  88.792  1.00 28.57 ?  358  ARG A NE    1 
ATOM   2620  C CZ    . ARG A 1 360  ? -66.109 50.906  88.198  1.00 34.19 ?  358  ARG A CZ    1 
ATOM   2621  N NH1   . ARG A 1 360  ? -67.078 50.698  87.319  1.00 35.64 ?  358  ARG A NH1   1 
ATOM   2622  N NH2   . ARG A 1 360  ? -65.268 49.917  88.493  1.00 34.35 ?  358  ARG A NH2   1 
ATOM   2623  N N     . ARG A 1 361  ? -66.450 58.590  86.909  1.00 17.11 ?  359  ARG A N     1 
ATOM   2624  C CA    . ARG A 1 361  ? -67.062 59.915  87.044  1.00 19.07 ?  359  ARG A CA    1 
ATOM   2625  C C     . ARG A 1 361  ? -67.160 60.636  85.704  1.00 15.74 ?  359  ARG A C     1 
ATOM   2626  O O     . ARG A 1 361  ? -68.193 61.248  85.382  1.00 20.07 ?  359  ARG A O     1 
ATOM   2627  C CB    . ARG A 1 361  ? -66.250 60.768  88.024  1.00 20.78 ?  359  ARG A CB    1 
ATOM   2628  C CG    . ARG A 1 361  ? -66.372 60.350  89.472  1.00 21.54 ?  359  ARG A CG    1 
ATOM   2629  C CD    . ARG A 1 361  ? -65.637 61.336  90.364  1.00 23.70 ?  359  ARG A CD    1 
ATOM   2630  N NE    . ARG A 1 361  ? -64.181 61.210  90.333  1.00 20.74 ?  359  ARG A NE    1 
ATOM   2631  C CZ    . ARG A 1 361  ? -63.338 62.206  90.091  1.00 19.89 ?  359  ARG A CZ    1 
ATOM   2632  N NH1   . ARG A 1 361  ? -63.766 63.407  89.742  1.00 21.48 ?  359  ARG A NH1   1 
ATOM   2633  N NH2   . ARG A 1 361  ? -62.029 62.000  90.229  1.00 20.93 ?  359  ARG A NH2   1 
ATOM   2634  N N     . SER A 1 362  ? -66.072 60.621  84.932  1.00 15.22 ?  360  SER A N     1 
ATOM   2635  C CA    . SER A 1 362  ? -65.994 61.366  83.689  1.00 16.19 ?  360  SER A CA    1 
ATOM   2636  C C     . SER A 1 362  ? -66.664 60.652  82.535  1.00 16.25 ?  360  SER A C     1 
ATOM   2637  O O     . SER A 1 362  ? -66.995 61.298  81.538  1.00 18.32 ?  360  SER A O     1 
ATOM   2638  C CB    . SER A 1 362  ? -64.527 61.606  83.325  1.00 16.00 ?  360  SER A CB    1 
ATOM   2639  O OG    . SER A 1 362  ? -63.889 60.372  83.030  1.00 16.03 ?  360  SER A OG    1 
ATOM   2640  N N     . GLY A 1 363  ? -66.850 59.341  82.642  1.00 16.83 ?  361  GLY A N     1 
ATOM   2641  C CA    . GLY A 1 363  ? -67.356 58.589  81.518  1.00 17.21 ?  361  GLY A CA    1 
ATOM   2642  C C     . GLY A 1 363  ? -66.356 58.385  80.406  1.00 17.72 ?  361  GLY A C     1 
ATOM   2643  O O     . GLY A 1 363  ? -66.749 57.951  79.322  1.00 19.53 ?  361  GLY A O     1 
ATOM   2644  N N     . ARG A 1 364  ? -65.084 58.700  80.642  1.00 18.10 ?  362  ARG A N     1 
ATOM   2645  C CA    . ARG A 1 364  ? -64.007 58.490  79.678  1.00 16.97 ?  362  ARG A CA    1 
ATOM   2646  C C     . ARG A 1 364  ? -63.324 57.168  79.974  1.00 17.84 ?  362  ARG A C     1 
ATOM   2647  O O     . ARG A 1 364  ? -62.943 56.906  81.119  1.00 19.09 ?  362  ARG A O     1 
ATOM   2648  C CB    . ARG A 1 364  ? -62.956 59.595  79.751  1.00 17.34 ?  362  ARG A CB    1 
ATOM   2649  C CG    . ARG A 1 364  ? -63.505 61.005  79.876  1.00 23.10 ?  362  ARG A CG    1 
ATOM   2650  C CD    . ARG A 1 364  ? -63.354 61.790  78.606  1.00 18.97 ?  362  ARG A CD    1 
ATOM   2651  N NE    . ARG A 1 364  ? -64.144 63.009  78.694  1.00 16.53 ?  362  ARG A NE    1 
ATOM   2652  C CZ    . ARG A 1 364  ? -63.648 64.235  78.795  1.00 14.24 ?  362  ARG A CZ    1 
ATOM   2653  N NH1   . ARG A 1 364  ? -62.337 64.461  78.769  1.00 14.26 ?  362  ARG A NH1   1 
ATOM   2654  N NH2   . ARG A 1 364  ? -64.489 65.262  78.923  1.00 13.98 ?  362  ARG A NH2   1 
ATOM   2655  N N     . ARG A 1 365  ? -63.114 56.363  78.938  1.00 16.75 ?  363  ARG A N     1 
ATOM   2656  C CA    . ARG A 1 365  ? -62.467 55.065  79.112  1.00 15.11 ?  363  ARG A CA    1 
ATOM   2657  C C     . ARG A 1 365  ? -60.952 55.272  79.053  1.00 14.96 ?  363  ARG A C     1 
ATOM   2658  O O     . ARG A 1 365  ? -60.312 55.119  78.013  1.00 17.44 ?  363  ARG A O     1 
ATOM   2659  C CB    . ARG A 1 365  ? -62.951 54.079  78.058  1.00 15.50 ?  363  ARG A CB    1 
ATOM   2660  C CG    . ARG A 1 365  ? -62.445 52.670  78.310  1.00 17.88 ?  363  ARG A CG    1 
ATOM   2661  C CD    . ARG A 1 365  ? -63.344 51.598  77.729  1.00 23.14 ?  363  ARG A CD    1 
ATOM   2662  N NE    . ARG A 1 365  ? -62.822 50.279  78.070  1.00 19.99 ?  363  ARG A NE    1 
ATOM   2663  C CZ    . ARG A 1 365  ? -62.118 49.520  77.244  1.00 18.68 ?  363  ARG A CZ    1 
ATOM   2664  N NH1   . ARG A 1 365  ? -61.943 49.857  75.978  1.00 21.01 ?  363  ARG A NH1   1 
ATOM   2665  N NH2   . ARG A 1 365  ? -61.558 48.407  77.705  1.00 20.07 ?  363  ARG A NH2   1 
ATOM   2666  N N     . ILE A 1 366  ? -60.373 55.635  80.198  1.00 13.16 ?  364  ILE A N     1 
ATOM   2667  C CA    . ILE A 1 366  ? -58.970 56.041  80.235  1.00 13.32 ?  364  ILE A CA    1 
ATOM   2668  C C     . ILE A 1 366  ? -58.085 54.874  79.832  1.00 14.79 ?  364  ILE A C     1 
ATOM   2669  O O     . ILE A 1 366  ? -58.259 53.746  80.310  1.00 13.99 ?  364  ILE A O     1 
ATOM   2670  C CB    . ILE A 1 366  ? -58.602 56.579  81.629  1.00 12.98 ?  364  ILE A CB    1 
ATOM   2671  C CG1   . ILE A 1 366  ? -59.466 57.799  81.972  1.00 15.21 ?  364  ILE A CG1   1 
ATOM   2672  C CG2   . ILE A 1 366  ? -57.113 56.939  81.684  1.00 15.30 ?  364  ILE A CG2   1 
ATOM   2673  C CD1   . ILE A 1 366  ? -59.331 58.291  83.411  1.00 16.72 ?  364  ILE A CD1   1 
ATOM   2674  N N     . MET A 1 367  ? -57.139 55.143  78.942  1.00 13.78 ?  365  MET A N     1 
ATOM   2675  C CA    . MET A 1 367  ? -56.165 54.144  78.519  1.00 13.56 ?  365  MET A CA    1 
ATOM   2676  C C     . MET A 1 367  ? -55.063 54.121  79.564  1.00 15.33 ?  365  MET A C     1 
ATOM   2677  O O     . MET A 1 367  ? -54.389 55.132  79.763  1.00 16.81 ?  365  MET A O     1 
ATOM   2678  C CB    . MET A 1 367  ? -55.615 54.492  77.134  1.00 13.29 ?  365  MET A CB    1 
ATOM   2679  C CG    . MET A 1 367  ? -56.718 54.742  76.106  1.00 16.07 ?  365  MET A CG    1 
ATOM   2680  S SD    . MET A 1 367  ? -56.159 55.127  74.424  1.00 16.51 ?  365  MET A SD    1 
ATOM   2681  C CE    . MET A 1 367  ? -55.938 53.498  73.683  1.00 16.75 ?  365  MET A CE    1 
ATOM   2682  N N     . VAL A 1 368  ? -54.905 53.005  80.269  1.00 13.19 ?  366  VAL A N     1 
ATOM   2683  C CA    . VAL A 1 368  ? -53.970 52.942  81.390  1.00 11.94 ?  366  VAL A CA    1 
ATOM   2684  C C     . VAL A 1 368  ? -52.820 52.030  81.002  1.00 12.44 ?  366  VAL A C     1 
ATOM   2685  O O     . VAL A 1 368  ? -53.002 50.810  80.892  1.00 14.42 ?  366  VAL A O     1 
ATOM   2686  C CB    . VAL A 1 368  ? -54.640 52.440  82.677  1.00 12.95 ?  366  VAL A CB    1 
ATOM   2687  C CG1   . VAL A 1 368  ? -53.624 52.454  83.823  1.00 14.82 ?  366  VAL A CG1   1 
ATOM   2688  C CG2   . VAL A 1 368  ? -55.857 53.292  82.982  1.00 16.50 ?  366  VAL A CG2   1 
ATOM   2689  N N     . ARG A 1 369  ? -51.626 52.604  80.824  1.00 11.93 ?  367  ARG A N     1 
ATOM   2690  C CA    . ARG A 1 369  ? -50.446 51.809  80.521  1.00 11.86 ?  367  ARG A CA    1 
ATOM   2691  C C     . ARG A 1 369  ? -49.773 51.457  81.836  1.00 13.91 ?  367  ARG A C     1 
ATOM   2692  O O     . ARG A 1 369  ? -49.286 52.337  82.549  1.00 14.82 ?  367  ARG A O     1 
ATOM   2693  C CB    . ARG A 1 369  ? -49.476 52.550  79.606  1.00 14.35 ?  367  ARG A CB    1 
ATOM   2694  C CG    . ARG A 1 369  ? -48.252 51.689  79.288  1.00 13.79 ?  367  ARG A CG    1 
ATOM   2695  C CD    . ARG A 1 369  ? -47.084 52.509  78.752  1.00 13.98 ?  367  ARG A CD    1 
ATOM   2696  N NE    . ARG A 1 369  ? -47.405 53.160  77.494  1.00 13.60 ?  367  ARG A NE    1 
ATOM   2697  C CZ    . ARG A 1 369  ? -46.808 54.258  77.050  1.00 15.15 ?  367  ARG A CZ    1 
ATOM   2698  N NH1   . ARG A 1 369  ? -45.877 54.884  77.763  1.00 15.56 ?  367  ARG A NH1   1 
ATOM   2699  N NH2   . ARG A 1 369  ? -47.170 54.757  75.873  1.00 15.25 ?  367  ARG A NH2   1 
ATOM   2700  N N     . LEU A 1 370  ? -49.764 50.172  82.158  1.00 13.18 ?  368  LEU A N     1 
ATOM   2701  C CA    . LEU A 1 370  ? -49.063 49.679  83.330  1.00 12.24 ?  368  LEU A CA    1 
ATOM   2702  C C     . LEU A 1 370  ? -47.638 49.309  82.924  1.00 13.86 ?  368  LEU A C     1 
ATOM   2703  O O     . LEU A 1 370  ? -47.445 48.448  82.061  1.00 12.79 ?  368  LEU A O     1 
ATOM   2704  C CB    . LEU A 1 370  ? -49.816 48.484  83.920  1.00 14.28 ?  368  LEU A CB    1 
ATOM   2705  C CG    . LEU A 1 370  ? -49.263 47.895  85.213  1.00 15.47 ?  368  LEU A CG    1 
ATOM   2706  C CD1   . LEU A 1 370  ? -49.438 48.886  86.357  1.00 17.14 ?  368  LEU A CD1   1 
ATOM   2707  C CD2   . LEU A 1 370  ? -49.937 46.559  85.553  1.00 17.14 ?  368  LEU A CD2   1 
ATOM   2708  N N     . VAL A 1 371  ? -46.654 49.957  83.549  1.00 12.36 ?  369  VAL A N     1 
ATOM   2709  C CA    . VAL A 1 371  ? -45.236 49.695  83.318  1.00 12.34 ?  369  VAL A CA    1 
ATOM   2710  C C     . VAL A 1 371  ? -44.615 49.330  84.661  1.00 12.98 ?  369  VAL A C     1 
ATOM   2711  O O     . VAL A 1 371  ? -45.207 49.555  85.711  1.00 14.15 ?  369  VAL A O     1 
ATOM   2712  C CB    . VAL A 1 371  ? -44.488 50.908  82.713  1.00 13.09 ?  369  VAL A CB    1 
ATOM   2713  C CG1   . VAL A 1 371  ? -45.151 51.410  81.433  1.00 12.94 ?  369  VAL A CG1   1 
ATOM   2714  C CG2   . VAL A 1 371  ? -44.380 52.045  83.734  1.00 12.61 ?  369  VAL A CG2   1 
ATOM   2715  N N     . LYS A 1 372  ? -43.377 48.817  84.634  1.00 13.10 ?  370  LYS A N     1 
ATOM   2716  C CA    . LYS A 1 372  ? -42.721 48.623  85.926  1.00 12.50 ?  370  LYS A CA    1 
ATOM   2717  C C     . LYS A 1 372  ? -42.079 49.922  86.418  1.00 13.64 ?  370  LYS A C     1 
ATOM   2718  O O     . LYS A 1 372  ? -42.377 50.377  87.526  1.00 17.19 ?  370  LYS A O     1 
ATOM   2719  C CB    . LYS A 1 372  ? -41.742 47.443  85.857  1.00 15.65 ?  370  LYS A CB    1 
ATOM   2720  C CG    . LYS A 1 372  ? -42.539 46.129  85.764  1.00 15.25 ?  370  LYS A CG    1 
ATOM   2721  C CD    . LYS A 1 372  ? -41.701 44.858  85.700  1.00 14.49 ?  370  LYS A CD    1 
ATOM   2722  C CE    . LYS A 1 372  ? -42.625 43.671  85.399  1.00 15.68 ?  370  LYS A CE    1 
ATOM   2723  N NZ    . LYS A 1 372  ? -41.869 42.416  85.101  1.00 17.10 ?  370  LYS A NZ    1 
ATOM   2724  N N     . GLY A 1 373  ? -41.238 50.564  85.604  1.00 13.47 ?  371  GLY A N     1 
ATOM   2725  C CA    . GLY A 1 373  ? -40.733 51.888  85.932  1.00 12.52 ?  371  GLY A CA    1 
ATOM   2726  C C     . GLY A 1 373  ? -39.297 52.108  85.485  1.00 12.45 ?  371  GLY A C     1 
ATOM   2727  O O     . GLY A 1 373  ? -38.482 51.185  85.587  1.00 13.85 ?  371  GLY A O     1 
ATOM   2728  N N     . ALA A 1 374  ? -38.957 53.306  85.003  1.00 11.11 ?  372  ALA A N     1 
ATOM   2729  C CA    . ALA A 1 374  ? -37.687 53.500  84.303  1.00 12.09 ?  372  ALA A CA    1 
ATOM   2730  C C     . ALA A 1 374  ? -36.625 54.232  85.113  1.00 13.63 ?  372  ALA A C     1 
ATOM   2731  O O     . ALA A 1 374  ? -35.501 54.386  84.617  1.00 14.85 ?  372  ALA A O     1 
ATOM   2732  C CB    . ALA A 1 374  ? -37.916 54.262  82.989  1.00 13.90 ?  372  ALA A CB    1 
ATOM   2733  N N     . TYR A 1 375  ? -36.928 54.689  86.328  1.00 12.33 ?  373  TYR A N     1 
ATOM   2734  C CA    . TYR A 1 375  ? -36.056 55.609  87.054  1.00 11.46 ?  373  TYR A CA    1 
ATOM   2735  C C     . TYR A 1 375  ? -35.574 55.024  88.379  1.00 11.12 ?  373  TYR A C     1 
ATOM   2736  O O     . TYR A 1 375  ? -35.281 55.776  89.314  1.00 12.20 ?  373  TYR A O     1 
ATOM   2737  C CB    . TYR A 1 375  ? -36.760 56.948  87.312  1.00 12.93 ?  373  TYR A CB    1 
ATOM   2738  C CG    . TYR A 1 375  ? -37.346 57.596  86.077  1.00 11.43 ?  373  TYR A CG    1 
ATOM   2739  C CD1   . TYR A 1 375  ? -38.563 57.171  85.545  1.00 12.59 ?  373  TYR A CD1   1 
ATOM   2740  C CD2   . TYR A 1 375  ? -36.675 58.635  85.441  1.00 14.19 ?  373  TYR A CD2   1 
ATOM   2741  C CE1   . TYR A 1 375  ? -39.089 57.756  84.411  1.00 14.13 ?  373  TYR A CE1   1 
ATOM   2742  C CE2   . TYR A 1 375  ? -37.204 59.233  84.313  1.00 15.14 ?  373  TYR A CE2   1 
ATOM   2743  C CZ    . TYR A 1 375  ? -38.397 58.780  83.795  1.00 17.71 ?  373  TYR A CZ    1 
ATOM   2744  O OH    . TYR A 1 375  ? -38.906 59.384  82.664  1.00 17.99 ?  373  TYR A OH    1 
ATOM   2745  N N     . TRP A 1 376  ? -35.446 53.698  88.464  1.00 10.70 ?  374  TRP A N     1 
ATOM   2746  C CA    . TRP A 1 376  ? -35.263 53.064  89.767  1.00 12.47 ?  374  TRP A CA    1 
ATOM   2747  C C     . TRP A 1 376  ? -34.010 53.568  90.476  1.00 12.30 ?  374  TRP A C     1 
ATOM   2748  O O     . TRP A 1 376  ? -34.077 54.012  91.629  1.00 12.63 ?  374  TRP A O     1 
ATOM   2749  C CB    . TRP A 1 376  ? -35.224 51.544  89.629  1.00 11.76 ?  374  TRP A CB    1 
ATOM   2750  C CG    . TRP A 1 376  ? -35.060 50.869  90.958  1.00 12.41 ?  374  TRP A CG    1 
ATOM   2751  C CD1   . TRP A 1 376  ? -36.024 50.676  91.905  1.00 14.52 ?  374  TRP A CD1   1 
ATOM   2752  C CD2   . TRP A 1 376  ? -33.854 50.301  91.498  1.00 14.93 ?  374  TRP A CD2   1 
ATOM   2753  N NE1   . TRP A 1 376  ? -35.501 50.023  92.994  1.00 15.27 ?  374  TRP A NE1   1 
ATOM   2754  C CE2   . TRP A 1 376  ? -34.168 49.784  92.772  1.00 15.61 ?  374  TRP A CE2   1 
ATOM   2755  C CE3   . TRP A 1 376  ? -32.545 50.182  91.029  1.00 16.66 ?  374  TRP A CE3   1 
ATOM   2756  C CZ2   . TRP A 1 376  ? -33.224 49.154  93.579  1.00 18.87 ?  374  TRP A CZ2   1 
ATOM   2757  C CZ3   . TRP A 1 376  ? -31.610 49.549  91.831  1.00 16.67 ?  374  TRP A CZ3   1 
ATOM   2758  C CH2   . TRP A 1 376  ? -31.953 49.046  93.092  1.00 16.97 ?  374  TRP A CH2   1 
ATOM   2759  N N     . ASP A 1 377  ? -32.849 53.506  89.811  1.00 13.29 ?  375  ASP A N     1 
ATOM   2760  C CA    . ASP A 1 377  ? -31.641 53.843  90.558  1.00 12.80 ?  375  ASP A CA    1 
ATOM   2761  C C     . ASP A 1 377  ? -31.610 55.321  90.926  1.00 12.55 ?  375  ASP A C     1 
ATOM   2762  O O     . ASP A 1 377  ? -31.037 55.681  91.959  1.00 13.67 ?  375  ASP A O     1 
ATOM   2763  C CB    . ASP A 1 377  ? -30.367 53.395  89.804  1.00 18.24 ?  375  ASP A CB    1 
ATOM   2764  C CG    . ASP A 1 377  ? -30.220 53.989  88.414  1.00 22.79 ?  375  ASP A CG    1 
ATOM   2765  O OD1   . ASP A 1 377  ? -30.754 55.075  88.134  1.00 24.85 ?  375  ASP A OD1   1 
ATOM   2766  O OD2   . ASP A 1 377  ? -29.523 53.343  87.587  1.00 20.82 ?  375  ASP A OD2   1 
ATOM   2767  N N     . ALA A 1 378  ? -32.255 56.185  90.133  1.00 11.71 ?  376  ALA A N     1 
ATOM   2768  C CA    . ALA A 1 378  ? -32.321 57.596  90.491  1.00 10.26 ?  376  ALA A CA    1 
ATOM   2769  C C     . ALA A 1 378  ? -33.223 57.818  91.694  1.00 12.34 ?  376  ALA A C     1 
ATOM   2770  O O     . ALA A 1 378  ? -32.971 58.733  92.494  1.00 12.44 ?  376  ALA A O     1 
ATOM   2771  C CB    . ALA A 1 378  ? -32.822 58.428  89.305  1.00 13.68 ?  376  ALA A CB    1 
ATOM   2772  N N     . GLU A 1 379  ? -34.288 57.021  91.817  1.00 13.12 ?  377  GLU A N     1 
ATOM   2773  C CA    . GLU A 1 379  ? -35.157 57.153  92.981  1.00 11.26 ?  377  GLU A CA    1 
ATOM   2774  C C     . GLU A 1 379  ? -34.437 56.727  94.251  1.00 12.36 ?  377  GLU A C     1 
ATOM   2775  O O     . GLU A 1 379  ? -34.653 57.320  95.309  1.00 14.10 ?  377  GLU A O     1 
ATOM   2776  C CB    . GLU A 1 379  ? -36.437 56.337  92.816  1.00 13.27 ?  377  GLU A CB    1 
ATOM   2777  C CG    . GLU A 1 379  ? -37.345 56.738  91.628  1.00 13.16 ?  377  GLU A CG    1 
ATOM   2778  C CD    . GLU A 1 379  ? -37.940 58.150  91.708  1.00 13.88 ?  377  GLU A CD    1 
ATOM   2779  O OE1   . GLU A 1 379  ? -37.815 58.853  92.741  1.00 14.22 ?  377  GLU A OE1   1 
ATOM   2780  O OE2   . GLU A 1 379  ? -38.546 58.562  90.694  1.00 14.73 ?  377  GLU A OE2   1 
ATOM   2781  N N     . ILE A 1 380  ? -33.578 55.703  94.170  1.00 12.05 ?  378  ILE A N     1 
ATOM   2782  C CA    . ILE A 1 380  ? -32.822 55.297  95.358  1.00 13.14 ?  378  ILE A CA    1 
ATOM   2783  C C     . ILE A 1 380  ? -31.892 56.423  95.786  1.00 13.15 ?  378  ILE A C     1 
ATOM   2784  O O     . ILE A 1 380  ? -31.828 56.799  96.968  1.00 13.04 ?  378  ILE A O     1 
ATOM   2785  C CB    . ILE A 1 380  ? -32.041 53.996  95.086  1.00 12.78 ?  378  ILE A CB    1 
ATOM   2786  C CG1   . ILE A 1 380  ? -32.973 52.851  94.673  1.00 13.67 ?  378  ILE A CG1   1 
ATOM   2787  C CG2   . ILE A 1 380  ? -31.176 53.577  96.302  1.00 13.15 ?  378  ILE A CG2   1 
ATOM   2788  C CD1   . ILE A 1 380  ? -34.091 52.508  95.678  1.00 14.04 ?  378  ILE A CD1   1 
ATOM   2789  N N     . LYS A 1 381  ? -31.151 56.979  94.825  1.00 12.42 ?  379  LYS A N     1 
ATOM   2790  C CA    . LYS A 1 381  ? -30.215 58.051  95.137  1.00 11.80 ?  379  LYS A CA    1 
ATOM   2791  C C     . LYS A 1 381  ? -30.927 59.259  95.732  1.00 12.63 ?  379  LYS A C     1 
ATOM   2792  O O     . LYS A 1 381  ? -30.486 59.812  96.747  1.00 12.06 ?  379  LYS A O     1 
ATOM   2793  C CB    . LYS A 1 381  ? -29.421 58.450  93.890  1.00 12.85 ?  379  LYS A CB    1 
ATOM   2794  C CG    . LYS A 1 381  ? -28.422 59.565  94.163  1.00 12.21 ?  379  LYS A CG    1 
ATOM   2795  C CD    . LYS A 1 381  ? -27.525 59.823  92.953  1.00 11.71 ?  379  LYS A CD    1 
ATOM   2796  C CE    . LYS A 1 381  ? -26.520 60.919  93.247  1.00 12.40 ?  379  LYS A CE    1 
ATOM   2797  N NZ    . LYS A 1 381  ? -25.653 61.218  92.026  1.00 11.90 ?  379  LYS A NZ    1 
ATOM   2798  N N     . ARG A 1 382  ? -32.049 59.671  95.136  1.00 11.84 ?  380  ARG A N     1 
ATOM   2799  C CA    A ARG A 1 382  ? -32.733 60.876  95.597  0.49 13.25 ?  380  ARG A CA    1 
ATOM   2800  C CA    B ARG A 1 382  ? -32.714 60.884  95.600  0.51 13.24 ?  380  ARG A CA    1 
ATOM   2801  C C     . ARG A 1 382  ? -33.235 60.729  97.030  1.00 12.68 ?  380  ARG A C     1 
ATOM   2802  O O     . ARG A 1 382  ? -33.096 61.653  97.843  1.00 14.03 ?  380  ARG A O     1 
ATOM   2803  C CB    A ARG A 1 382  ? -33.897 61.209  94.664  0.49 16.08 ?  380  ARG A CB    1 
ATOM   2804  C CB    B ARG A 1 382  ? -33.836 61.261  94.625  0.51 16.07 ?  380  ARG A CB    1 
ATOM   2805  C CG    A ARG A 1 382  ? -34.716 62.404  95.123  0.49 18.89 ?  380  ARG A CG    1 
ATOM   2806  C CG    B ARG A 1 382  ? -34.553 62.587  94.912  0.51 19.47 ?  380  ARG A CG    1 
ATOM   2807  C CD    A ARG A 1 382  ? -35.672 62.837  94.032  0.49 19.70 ?  380  ARG A CD    1 
ATOM   2808  C CD    B ARG A 1 382  ? -33.634 63.693  95.433  0.51 20.54 ?  380  ARG A CD    1 
ATOM   2809  N NE    A ARG A 1 382  ? -35.057 62.683  92.720  0.49 24.54 ?  380  ARG A NE    1 
ATOM   2810  N NE    B ARG A 1 382  ? -32.607 64.140  94.503  0.51 24.83 ?  380  ARG A NE    1 
ATOM   2811  C CZ    A ARG A 1 382  ? -35.672 62.923  91.570  0.49 23.01 ?  380  ARG A CZ    1 
ATOM   2812  C CZ    B ARG A 1 382  ? -31.672 65.029  94.812  0.51 24.30 ?  380  ARG A CZ    1 
ATOM   2813  N NH1   A ARG A 1 382  ? -36.914 63.372  91.535  0.49 18.11 ?  380  ARG A NH1   1 
ATOM   2814  N NH1   B ARG A 1 382  ? -31.627 65.600  96.008  0.51 20.28 ?  380  ARG A NH1   1 
ATOM   2815  N NH2   A ARG A 1 382  ? -35.025 62.700  90.430  0.49 28.17 ?  380  ARG A NH2   1 
ATOM   2816  N NH2   B ARG A 1 382  ? -30.756 65.348  93.905  0.51 25.82 ?  380  ARG A NH2   1 
ATOM   2817  N N     . ALA A 1 383  ? -33.821 59.574  97.364  1.00 11.85 ?  381  ALA A N     1 
ATOM   2818  C CA    . ALA A 1 383  ? -34.324 59.380  98.723  1.00 12.19 ?  381  ALA A CA    1 
ATOM   2819  C C     . ALA A 1 383  ? -33.182 59.394  99.726  1.00 12.32 ?  381  ALA A C     1 
ATOM   2820  O O     . ALA A 1 383  ? -33.322 59.928  100.832 1.00 14.79 ?  381  ALA A O     1 
ATOM   2821  C CB    . ALA A 1 383  ? -35.106 58.072  98.815  1.00 15.55 ?  381  ALA A CB    1 
ATOM   2822  N N     . GLN A 1 384  ? -32.033 58.826  99.352  1.00 12.93 ?  382  GLN A N     1 
ATOM   2823  C CA    . GLN A 1 384  ? -30.898 58.837  100.272 1.00 13.10 ?  382  GLN A CA    1 
ATOM   2824  C C     . GLN A 1 384  ? -30.365 60.250  100.474 1.00 12.98 ?  382  GLN A C     1 
ATOM   2825  O O     . GLN A 1 384  ? -30.125 60.673  101.613 1.00 14.90 ?  382  GLN A O     1 
ATOM   2826  C CB    . GLN A 1 384  ? -29.798 57.905  99.759  1.00 12.72 ?  382  GLN A CB    1 
ATOM   2827  C CG    . GLN A 1 384  ? -30.164 56.437  99.885  1.00 13.14 ?  382  GLN A CG    1 
ATOM   2828  C CD    . GLN A 1 384  ? -29.055 55.512  99.449  1.00 13.99 ?  382  GLN A CD    1 
ATOM   2829  O OE1   . GLN A 1 384  ? -28.178 55.917  98.698  1.00 15.53 ?  382  GLN A OE1   1 
ATOM   2830  N NE2   . GLN A 1 384  ? -29.096 54.265  99.895  1.00 15.04 ?  382  GLN A NE2   1 
ATOM   2831  N N     . LEU A 1 385  ? -30.187 61.006  99.381  1.00 12.52 ?  383  LEU A N     1 
ATOM   2832  C CA    . LEU A 1 385  ? -29.703 62.378  99.500  1.00 13.79 ?  383  LEU A CA    1 
ATOM   2833  C C     . LEU A 1 385  ? -30.615 63.217  100.383 1.00 14.08 ?  383  LEU A C     1 
ATOM   2834  O O     . LEU A 1 385  ? -30.142 64.046  101.171 1.00 15.67 ?  383  LEU A O     1 
ATOM   2835  C CB    . LEU A 1 385  ? -29.594 63.023  98.119  1.00 14.37 ?  383  LEU A CB    1 
ATOM   2836  C CG    . LEU A 1 385  ? -28.462 62.545  97.218  1.00 16.68 ?  383  LEU A CG    1 
ATOM   2837  C CD1   . LEU A 1 385  ? -28.632 63.187  95.868  1.00 16.86 ?  383  LEU A CD1   1 
ATOM   2838  C CD2   . LEU A 1 385  ? -27.150 62.942  97.817  1.00 18.39 ?  383  LEU A CD2   1 
ATOM   2839  N N     . ASP A 1 386  ? -31.927 63.035  100.246 1.00 14.90 ?  384  ASP A N     1 
ATOM   2840  C CA    . ASP A 1 386  ? -32.877 63.888  100.938 1.00 14.21 ?  384  ASP A CA    1 
ATOM   2841  C C     . ASP A 1 386  ? -33.192 63.396  102.344 1.00 15.67 ?  384  ASP A C     1 
ATOM   2842  O O     . ASP A 1 386  ? -33.966 64.049  103.047 1.00 16.36 ?  384  ASP A O     1 
ATOM   2843  C CB    . ASP A 1 386  ? -34.165 64.008  100.117 1.00 17.28 ?  384  ASP A CB    1 
ATOM   2844  C CG    . ASP A 1 386  ? -33.992 64.867  98.877  1.00 20.53 ?  384  ASP A CG    1 
ATOM   2845  O OD1   . ASP A 1 386  ? -32.921 65.496  98.697  1.00 23.24 ?  384  ASP A OD1   1 
ATOM   2846  O OD2   . ASP A 1 386  ? -34.941 64.899  98.062  1.00 19.66 ?  384  ASP A OD2   1 
ATOM   2847  N N     . GLY A 1 387  ? -32.596 62.284  102.773 1.00 14.59 ?  385  GLY A N     1 
ATOM   2848  C CA    . GLY A 1 387  ? -32.786 61.782  104.134 1.00 14.47 ?  385  GLY A CA    1 
ATOM   2849  C C     . GLY A 1 387  ? -34.221 61.451  104.476 1.00 18.26 ?  385  GLY A C     1 
ATOM   2850  O O     . GLY A 1 387  ? -34.669 61.728  105.596 1.00 18.32 ?  385  GLY A O     1 
ATOM   2851  N N     . LEU A 1 388  ? -34.949 60.853  103.546 1.00 16.83 ?  386  LEU A N     1 
ATOM   2852  C CA    . LEU A 1 388  ? -36.367 60.600  103.746 1.00 16.81 ?  386  LEU A CA    1 
ATOM   2853  C C     . LEU A 1 388  ? -36.596 59.242  104.406 1.00 17.83 ?  386  LEU A C     1 
ATOM   2854  O O     . LEU A 1 388  ? -35.691 58.417  104.546 1.00 18.27 ?  386  LEU A O     1 
ATOM   2855  C CB    . LEU A 1 388  ? -37.108 60.721  102.412 1.00 17.00 ?  386  LEU A CB    1 
ATOM   2856  C CG    . LEU A 1 388  ? -36.966 62.124  101.814 1.00 17.10 ?  386  LEU A CG    1 
ATOM   2857  C CD1   . LEU A 1 388  ? -37.726 62.252  100.493 1.00 18.76 ?  386  LEU A CD1   1 
ATOM   2858  C CD2   . LEU A 1 388  ? -37.419 63.210  102.785 1.00 19.55 ?  386  LEU A CD2   1 
ATOM   2859  N N     . ALA A 1 389  ? -37.834 59.030  104.870 1.00 19.55 ?  387  ALA A N     1 
ATOM   2860  C CA    . ALA A 1 389  ? -38.097 57.895  105.749 1.00 20.21 ?  387  ALA A CA    1 
ATOM   2861  C C     . ALA A 1 389  ? -37.903 56.563  105.040 1.00 22.04 ?  387  ALA A C     1 
ATOM   2862  O O     . ALA A 1 389  ? -37.471 55.585  105.654 1.00 24.63 ?  387  ALA A O     1 
ATOM   2863  C CB    . ALA A 1 389  ? -39.517 57.995  106.309 1.00 25.81 ?  387  ALA A CB    1 
ATOM   2864  N N     . ASP A 1 390  ? -38.203 56.510  103.748 1.00 17.20 ?  388  ASP A N     1 
ATOM   2865  C CA    . ASP A 1 390  ? -38.144 55.268  102.995 1.00 16.60 ?  388  ASP A CA    1 
ATOM   2866  C C     . ASP A 1 390  ? -38.143 55.656  101.524 1.00 16.45 ?  388  ASP A C     1 
ATOM   2867  O O     . ASP A 1 390  ? -38.191 56.838  101.184 1.00 16.43 ?  388  ASP A O     1 
ATOM   2868  C CB    . ASP A 1 390  ? -39.330 54.361  103.360 1.00 18.93 ?  388  ASP A CB    1 
ATOM   2869  C CG    . ASP A 1 390  ? -39.026 52.876  103.214 1.00 21.43 ?  388  ASP A CG    1 
ATOM   2870  O OD1   . ASP A 1 390  ? -38.427 52.452  102.199 1.00 20.25 ?  388  ASP A OD1   1 
ATOM   2871  O OD2   . ASP A 1 390  ? -39.390 52.118  104.152 1.00 22.47 ?  388  ASP A OD2   1 
ATOM   2872  N N     . PHE A 1 391  ? -38.103 54.666  100.672 1.00 16.40 ?  389  PHE A N     1 
ATOM   2873  C CA    . PHE A 1 391  ? -38.117 54.888  99.235  1.00 15.35 ?  389  PHE A CA    1 
ATOM   2874  C C     . PHE A 1 391  ? -39.549 54.948  98.721  1.00 14.65 ?  389  PHE A C     1 
ATOM   2875  O O     . PHE A 1 391  ? -40.467 54.385  99.333  1.00 14.72 ?  389  PHE A O     1 
ATOM   2876  C CB    . PHE A 1 391  ? -37.344 53.776  98.532  1.00 15.75 ?  389  PHE A CB    1 
ATOM   2877  C CG    . PHE A 1 391  ? -35.931 53.673  99.012  1.00 13.76 ?  389  PHE A CG    1 
ATOM   2878  C CD1   . PHE A 1 391  ? -34.997 54.586  98.579  1.00 13.62 ?  389  PHE A CD1   1 
ATOM   2879  C CD2   . PHE A 1 391  ? -35.552 52.707  99.932  1.00 15.08 ?  389  PHE A CD2   1 
ATOM   2880  C CE1   . PHE A 1 391  ? -33.678 54.544  99.034  1.00 15.19 ?  389  PHE A CE1   1 
ATOM   2881  C CE2   . PHE A 1 391  ? -34.243 52.654  100.392 1.00 15.18 ?  389  PHE A CE2   1 
ATOM   2882  C CZ    . PHE A 1 391  ? -33.305 53.575  99.938  1.00 13.45 ?  389  PHE A CZ    1 
ATOM   2883  N N     . PRO A 1 392  ? -39.781 55.663  97.621  1.00 13.89 ?  390  PRO A N     1 
ATOM   2884  C CA    . PRO A 1 392  ? -41.098 55.628  96.977  1.00 15.12 ?  390  PRO A CA    1 
ATOM   2885  C C     . PRO A 1 392  ? -41.256 54.487  95.982  1.00 13.26 ?  390  PRO A C     1 
ATOM   2886  O O     . PRO A 1 392  ? -42.284 54.407  95.293  1.00 14.86 ?  390  PRO A O     1 
ATOM   2887  C CB    . PRO A 1 392  ? -41.142 56.986  96.266  1.00 13.60 ?  390  PRO A CB    1 
ATOM   2888  C CG    . PRO A 1 392  ? -39.712 57.184  95.798  1.00 11.82 ?  390  PRO A CG    1 
ATOM   2889  C CD    . PRO A 1 392  ? -38.859 56.600  96.945  1.00 12.47 ?  390  PRO A CD    1 
ATOM   2890  N N     . VAL A 1 393  ? -40.249 53.618  95.886  1.00 12.95 ?  391  VAL A N     1 
ATOM   2891  C CA    . VAL A 1 393  ? -40.247 52.463  95.004  1.00 13.35 ?  391  VAL A CA    1 
ATOM   2892  C C     . VAL A 1 393  ? -39.794 51.253  95.807  1.00 14.63 ?  391  VAL A C     1 
ATOM   2893  O O     . VAL A 1 393  ? -39.176 51.379  96.865  1.00 15.50 ?  391  VAL A O     1 
ATOM   2894  C CB    . VAL A 1 393  ? -39.312 52.666  93.788  1.00 13.56 ?  391  VAL A CB    1 
ATOM   2895  C CG1   . VAL A 1 393  ? -39.833 53.780  92.882  1.00 15.69 ?  391  VAL A CG1   1 
ATOM   2896  C CG2   . VAL A 1 393  ? -37.913 53.005  94.272  1.00 14.58 ?  391  VAL A CG2   1 
ATOM   2897  N N     . PHE A 1 394  ? -40.114 50.070  95.287  1.00 14.11 ?  392  PHE A N     1 
ATOM   2898  C CA    . PHE A 1 394  ? -39.611 48.845  95.883  1.00 14.51 ?  392  PHE A CA    1 
ATOM   2899  C C     . PHE A 1 394  ? -38.101 48.760  95.684  1.00 14.12 ?  392  PHE A C     1 
ATOM   2900  O O     . PHE A 1 394  ? -37.518 49.461  94.845  1.00 16.22 ?  392  PHE A O     1 
ATOM   2901  C CB    . PHE A 1 394  ? -40.335 47.638  95.288  1.00 15.37 ?  392  PHE A CB    1 
ATOM   2902  C CG    . PHE A 1 394  ? -41.824 47.672  95.540  1.00 14.50 ?  392  PHE A CG    1 
ATOM   2903  C CD1   . PHE A 1 394  ? -42.308 47.591  96.842  1.00 18.67 ?  392  PHE A CD1   1 
ATOM   2904  C CD2   . PHE A 1 394  ? -42.723 47.843  94.499  1.00 17.41 ?  392  PHE A CD2   1 
ATOM   2905  C CE1   . PHE A 1 394  ? -43.665 47.667  97.109  1.00 18.37 ?  392  PHE A CE1   1 
ATOM   2906  C CE2   . PHE A 1 394  ? -44.096 47.908  94.751  1.00 15.95 ?  392  PHE A CE2   1 
ATOM   2907  C CZ    . PHE A 1 394  ? -44.567 47.814  96.065  1.00 18.42 ?  392  PHE A CZ    1 
ATOM   2908  N N     . THR A 1 395  ? -37.454 47.930  96.516  1.00 15.94 ?  393  THR A N     1 
ATOM   2909  C CA    . THR A 1 395  ? -36.010 47.734  96.425  1.00 15.50 ?  393  THR A CA    1 
ATOM   2910  C C     . THR A 1 395  ? -35.613 46.332  95.989  1.00 17.83 ?  393  THR A C     1 
ATOM   2911  O O     . THR A 1 395  ? -34.425 46.104  95.722  1.00 16.48 ?  393  THR A O     1 
ATOM   2912  C CB    . THR A 1 395  ? -35.319 48.048  97.764  1.00 16.16 ?  393  THR A CB    1 
ATOM   2913  O OG1   . THR A 1 395  ? -35.829 47.187  98.785  1.00 18.20 ?  393  THR A OG1   1 
ATOM   2914  C CG2   . THR A 1 395  ? -35.530 49.497  98.163  1.00 19.19 ?  393  THR A CG2   1 
ATOM   2915  N N     . ARG A 1 396  ? -36.550 45.389  95.920  1.00 17.13 ?  394  ARG A N     1 
ATOM   2916  C CA    . ARG A 1 396  ? -36.295 44.084  95.322  1.00 18.06 ?  394  ARG A CA    1 
ATOM   2917  C C     . ARG A 1 396  ? -37.099 43.963  94.040  1.00 16.87 ?  394  ARG A C     1 
ATOM   2918  O O     . ARG A 1 396  ? -38.291 44.293  94.013  1.00 17.38 ?  394  ARG A O     1 
ATOM   2919  C CB    . ARG A 1 396  ? -36.653 42.936  96.266  1.00 18.80 ?  394  ARG A CB    1 
ATOM   2920  C CG    . ARG A 1 396  ? -35.837 42.895  97.535  1.00 20.19 ?  394  ARG A CG    1 
ATOM   2921  C CD    . ARG A 1 396  ? -36.196 41.667  98.368  1.00 22.59 ?  394  ARG A CD    1 
ATOM   2922  N NE    . ARG A 1 396  ? -35.589 41.743  99.689  1.00 25.04 ?  394  ARG A NE    1 
ATOM   2923  C CZ    . ARG A 1 396  ? -34.813 40.808  100.220 1.00 28.40 ?  394  ARG A CZ    1 
ATOM   2924  N NH1   . ARG A 1 396  ? -34.551 39.680  99.579  1.00 30.34 ?  394  ARG A NH1   1 
ATOM   2925  N NH2   . ARG A 1 396  ? -34.285 41.013  101.426 1.00 27.09 ?  394  ARG A NH2   1 
ATOM   2926  N N     . LYS A 1 397  ? -36.437 43.507  92.977  1.00 17.35 ?  395  LYS A N     1 
ATOM   2927  C CA    . LYS A 1 397  ? -37.087 43.417  91.676  1.00 17.88 ?  395  LYS A CA    1 
ATOM   2928  C C     . LYS A 1 397  ? -38.325 42.525  91.729  1.00 19.39 ?  395  LYS A C     1 
ATOM   2929  O O     . LYS A 1 397  ? -39.340 42.817  91.084  1.00 18.57 ?  395  LYS A O     1 
ATOM   2930  C CB    . LYS A 1 397  ? -36.074 42.923  90.641  1.00 19.75 ?  395  LYS A CB    1 
ATOM   2931  C CG    . LYS A 1 397  ? -36.431 43.239  89.210  1.00 23.49 ?  395  LYS A CG    1 
ATOM   2932  C CD    . LYS A 1 397  ? -37.126 42.073  88.572  1.00 21.49 ?  395  LYS A CD    1 
ATOM   2933  C CE    . LYS A 1 397  ? -37.546 42.388  87.145  1.00 22.67 ?  395  LYS A CE    1 
ATOM   2934  N NZ    . LYS A 1 397  ? -38.240 41.212  86.574  1.00 22.94 ?  395  LYS A NZ    1 
ATOM   2935  N N     . ILE A 1 398  ? -38.273 41.442  92.513  1.00 18.12 ?  396  ILE A N     1 
ATOM   2936  C CA    . ILE A 1 398  ? -39.418 40.543  92.582  1.00 18.51 ?  396  ILE A CA    1 
ATOM   2937  C C     . ILE A 1 398  ? -40.624 41.238  93.212  1.00 17.05 ?  396  ILE A C     1 
ATOM   2938  O O     . ILE A 1 398  ? -41.771 40.890  92.907  1.00 19.26 ?  396  ILE A O     1 
ATOM   2939  C CB    . ILE A 1 398  ? -39.026 39.254  93.335  1.00 20.92 ?  396  ILE A CB    1 
ATOM   2940  C CG1   . ILE A 1 398  ? -40.032 38.150  93.047  1.00 26.23 ?  396  ILE A CG1   1 
ATOM   2941  C CG2   . ILE A 1 398  ? -38.887 39.521  94.814  1.00 23.65 ?  396  ILE A CG2   1 
ATOM   2942  C CD1   . ILE A 1 398  ? -39.651 36.823  93.656  1.00 28.85 ?  396  ILE A CD1   1 
ATOM   2943  N N     . HIS A 1 399  ? -40.395 42.232  94.080  1.00 18.98 ?  397  HIS A N     1 
ATOM   2944  C CA    . HIS A 1 399  ? -41.516 43.000  94.618  1.00 18.08 ?  397  HIS A CA    1 
ATOM   2945  C C     . HIS A 1 399  ? -42.226 43.782  93.516  1.00 17.07 ?  397  HIS A C     1 
ATOM   2946  O O     . HIS A 1 399  ? -43.458 43.846  93.487  1.00 17.50 ?  397  HIS A O     1 
ATOM   2947  C CB    . HIS A 1 399  ? -41.035 43.937  95.728  1.00 18.05 ?  397  HIS A CB    1 
ATOM   2948  C CG    . HIS A 1 399  ? -40.519 43.219  96.941  1.00 17.48 ?  397  HIS A CG    1 
ATOM   2949  N ND1   . HIS A 1 399  ? -39.838 43.861  97.952  1.00 18.01 ?  397  HIS A ND1   1 
ATOM   2950  C CD2   . HIS A 1 399  ? -40.591 41.916  97.302  1.00 21.86 ?  397  HIS A CD2   1 
ATOM   2951  C CE1   . HIS A 1 399  ? -39.508 42.981  98.884  1.00 19.48 ?  397  HIS A CE1   1 
ATOM   2952  N NE2   . HIS A 1 399  ? -39.953 41.794  98.515  1.00 21.24 ?  397  HIS A NE2   1 
ATOM   2953  N N     . THR A 1 400  ? -41.463 44.381  92.598  1.00 15.40 ?  398  THR A N     1 
ATOM   2954  C CA    . THR A 1 400  ? -42.083 45.077  91.474  1.00 15.14 ?  398  THR A CA    1 
ATOM   2955  C C     . THR A 1 400  ? -42.880 44.117  90.597  1.00 16.45 ?  398  THR A C     1 
ATOM   2956  O O     . THR A 1 400  ? -43.959 44.467  90.097  1.00 16.01 ?  398  THR A O     1 
ATOM   2957  C CB    . THR A 1 400  ? -40.998 45.796  90.671  1.00 13.36 ?  398  THR A CB    1 
ATOM   2958  O OG1   . THR A 1 400  ? -40.456 46.851  91.475  1.00 15.71 ?  398  THR A OG1   1 
ATOM   2959  C CG2   . THR A 1 400  ? -41.562 46.379  89.378  1.00 14.33 ?  398  THR A CG2   1 
ATOM   2960  N N     . ASP A 1 401  ? -42.376 42.894  90.407  1.00 16.54 ?  399  ASP A N     1 
ATOM   2961  C CA    . ASP A 1 401  ? -43.105 41.921  89.602  1.00 16.82 ?  399  ASP A CA    1 
ATOM   2962  C C     . ASP A 1 401  ? -44.444 41.569  90.242  1.00 18.12 ?  399  ASP A C     1 
ATOM   2963  O O     . ASP A 1 401  ? -45.471 41.514  89.559  1.00 17.95 ?  399  ASP A O     1 
ATOM   2964  C CB    . ASP A 1 401  ? -42.256 40.664  89.396  1.00 17.40 ?  399  ASP A CB    1 
ATOM   2965  C CG    . ASP A 1 401  ? -41.062 40.909  88.486  1.00 19.84 ?  399  ASP A CG    1 
ATOM   2966  O OD1   . ASP A 1 401  ? -41.105 41.872  87.684  1.00 22.17 ?  399  ASP A OD1   1 
ATOM   2967  O OD2   . ASP A 1 401  ? -40.074 40.150  88.580  1.00 24.16 ?  399  ASP A OD2   1 
ATOM   2968  N N     . VAL A 1 402  ? -44.447 41.313  91.554  1.00 17.43 ?  400  VAL A N     1 
ATOM   2969  C CA    . VAL A 1 402  ? -45.704 41.015  92.239  1.00 19.39 ?  400  VAL A CA    1 
ATOM   2970  C C     . VAL A 1 402  ? -46.647 42.212  92.180  1.00 17.53 ?  400  VAL A C     1 
ATOM   2971  O O     . VAL A 1 402  ? -47.854 42.061  91.936  1.00 17.66 ?  400  VAL A O     1 
ATOM   2972  C CB    . VAL A 1 402  ? -45.434 40.590  93.691  1.00 20.45 ?  400  VAL A CB    1 
ATOM   2973  C CG1   . VAL A 1 402  ? -46.764 40.388  94.431  1.00 17.48 ?  400  VAL A CG1   1 
ATOM   2974  C CG2   . VAL A 1 402  ? -44.601 39.323  93.722  1.00 23.67 ?  400  VAL A CG2   1 
ATOM   2975  N N     . SER A 1 403  ? -46.116 43.416  92.415  1.00 17.62 ?  401  SER A N     1 
ATOM   2976  C CA    . SER A 1 403  ? -46.922 44.630  92.297  1.00 17.47 ?  401  SER A CA    1 
ATOM   2977  C C     . SER A 1 403  ? -47.569 44.723  90.918  1.00 19.36 ?  401  SER A C     1 
ATOM   2978  O O     . SER A 1 403  ? -48.771 45.003  90.790  1.00 16.92 ?  401  SER A O     1 
ATOM   2979  C CB    . SER A 1 403  ? -46.047 45.857  92.570  1.00 16.25 ?  401  SER A CB    1 
ATOM   2980  O OG    . SER A 1 403  ? -46.778 47.063  92.397  1.00 16.79 ?  401  SER A OG    1 
ATOM   2981  N N     . TYR A 1 404  ? -46.782 44.476  89.868  1.00 16.17 ?  402  TYR A N     1 
ATOM   2982  C CA    . TYR A 1 404  ? -47.309 44.528  88.508  1.00 16.16 ?  402  TYR A CA    1 
ATOM   2983  C C     . TYR A 1 404  ? -48.488 43.574  88.326  1.00 17.64 ?  402  TYR A C     1 
ATOM   2984  O O     . TYR A 1 404  ? -49.543 43.961  87.806  1.00 16.46 ?  402  TYR A O     1 
ATOM   2985  C CB    . TYR A 1 404  ? -46.181 44.222  87.522  1.00 16.75 ?  402  TYR A CB    1 
ATOM   2986  C CG    . TYR A 1 404  ? -46.487 44.569  86.085  1.00 15.99 ?  402  TYR A CG    1 
ATOM   2987  C CD1   . TYR A 1 404  ? -47.267 43.733  85.305  1.00 16.50 ?  402  TYR A CD1   1 
ATOM   2988  C CD2   . TYR A 1 404  ? -45.986 45.723  85.502  1.00 14.31 ?  402  TYR A CD2   1 
ATOM   2989  C CE1   . TYR A 1 404  ? -47.555 44.031  83.992  1.00 16.09 ?  402  TYR A CE1   1 
ATOM   2990  C CE2   . TYR A 1 404  ? -46.266 46.022  84.167  1.00 15.61 ?  402  TYR A CE2   1 
ATOM   2991  C CZ    . TYR A 1 404  ? -47.038 45.170  83.424  1.00 15.66 ?  402  TYR A CZ    1 
ATOM   2992  O OH    . TYR A 1 404  ? -47.334 45.451  82.111  1.00 16.92 ?  402  TYR A OH    1 
ATOM   2993  N N     . ILE A 1 405  ? -48.338 42.322  88.765  1.00 17.33 ?  403  ILE A N     1 
ATOM   2994  C CA    . ILE A 1 405  ? -49.400 41.346  88.558  1.00 18.97 ?  403  ILE A CA    1 
ATOM   2995  C C     . ILE A 1 405  ? -50.618 41.688  89.410  1.00 18.11 ?  403  ILE A C     1 
ATOM   2996  O O     . ILE A 1 405  ? -51.760 41.572  88.948  1.00 20.04 ?  403  ILE A O     1 
ATOM   2997  C CB    . ILE A 1 405  ? -48.858 39.933  88.824  1.00 18.27 ?  403  ILE A CB    1 
ATOM   2998  C CG1   . ILE A 1 405  ? -47.792 39.619  87.766  1.00 21.53 ?  403  ILE A CG1   1 
ATOM   2999  C CG2   . ILE A 1 405  ? -49.987 38.918  88.810  1.00 23.91 ?  403  ILE A CG2   1 
ATOM   3000  C CD1   . ILE A 1 405  ? -46.866 38.476  88.124  1.00 25.34 ?  403  ILE A CD1   1 
ATOM   3001  N N     . ALA A 1 406  ? -50.399 42.191  90.632  1.00 18.73 ?  404  ALA A N     1 
ATOM   3002  C CA    . ALA A 1 406  ? -51.525 42.611  91.473  1.00 18.86 ?  404  ALA A CA    1 
ATOM   3003  C C     . ALA A 1 406  ? -52.300 43.756  90.835  1.00 18.88 ?  404  ALA A C     1 
ATOM   3004  O O     . ALA A 1 406  ? -53.538 43.785  90.876  1.00 21.68 ?  404  ALA A O     1 
ATOM   3005  C CB    . ALA A 1 406  ? -51.027 43.026  92.857  1.00 20.31 ?  404  ALA A CB    1 
ATOM   3006  N N     . CYS A 1 407  ? -51.587 44.718  90.255  1.00 18.03 ?  405  CYS A N     1 
ATOM   3007  C CA    . CYS A 1 407  ? -52.254 45.842  89.609  1.00 17.11 ?  405  CYS A CA    1 
ATOM   3008  C C     . CYS A 1 407  ? -52.941 45.425  88.312  1.00 17.11 ?  405  CYS A C     1 
ATOM   3009  O O     . CYS A 1 407  ? -53.984 45.983  87.959  1.00 17.63 ?  405  CYS A O     1 
ATOM   3010  C CB    . CYS A 1 407  ? -51.229 46.945  89.384  1.00 18.62 ?  405  CYS A CB    1 
ATOM   3011  S SG    . CYS A 1 407  ? -50.711 47.713  90.949  1.00 23.08 ?  405  CYS A SG    1 
ATOM   3012  N N     . ALA A 1 408  ? -52.404 44.419  87.617  1.00 17.90 ?  406  ALA A N     1 
ATOM   3013  C CA    . ALA A 1 408  ? -53.080 43.887  86.438  1.00 17.92 ?  406  ALA A CA    1 
ATOM   3014  C C     . ALA A 1 408  ? -54.414 43.253  86.808  1.00 19.71 ?  406  ALA A C     1 
ATOM   3015  O O     . ALA A 1 408  ? -55.399 43.395  86.076  1.00 19.62 ?  406  ALA A O     1 
ATOM   3016  C CB    . ALA A 1 408  ? -52.181 42.869  85.731  1.00 19.71 ?  406  ALA A CB    1 
ATOM   3017  N N     . ALA A 1 409  ? -54.462 42.544  87.937  1.00 20.47 ?  407  ALA A N     1 
ATOM   3018  C CA    . ALA A 1 409  ? -55.726 41.984  88.405  1.00 19.70 ?  407  ALA A CA    1 
ATOM   3019  C C     . ALA A 1 409  ? -56.749 43.084  88.658  1.00 21.87 ?  407  ALA A C     1 
ATOM   3020  O O     . ALA A 1 409  ? -57.928 42.945  88.298  1.00 21.99 ?  407  ALA A O     1 
ATOM   3021  C CB    . ALA A 1 409  ? -55.494 41.149  89.668  1.00 21.55 ?  407  ALA A CB    1 
ATOM   3022  N N     . LYS A 1 410  ? -56.313 44.194  89.260  1.00 18.63 ?  408  LYS A N     1 
ATOM   3023  C CA    . LYS A 1 410  ? -57.218 45.319  89.472  1.00 18.44 ?  408  LYS A CA    1 
ATOM   3024  C C     . LYS A 1 410  ? -57.705 45.889  88.144  1.00 20.41 ?  408  LYS A C     1 
ATOM   3025  O O     . LYS A 1 410  ? -58.905 46.147  87.968  1.00 20.74 ?  408  LYS A O     1 
ATOM   3026  C CB    . LYS A 1 410  ? -56.517 46.390  90.310  1.00 20.05 ?  408  LYS A CB    1 
ATOM   3027  C CG    . LYS A 1 410  ? -57.355 47.619  90.639  1.00 20.47 ?  408  LYS A CG    1 
ATOM   3028  C CD    . LYS A 1 410  ? -56.549 48.637  91.442  1.00 22.45 ?  408  LYS A CD    1 
ATOM   3029  C CE    . LYS A 1 410  ? -56.114 48.114  92.797  1.00 22.66 ?  408  LYS A CE    1 
ATOM   3030  N NZ    . LYS A 1 410  ? -57.253 48.059  93.765  1.00 23.77 ?  408  LYS A NZ    1 
ATOM   3031  N N     . LEU A 1 411  ? -56.792 46.067  87.181  1.00 15.94 ?  409  LEU A N     1 
ATOM   3032  C CA    . LEU A 1 411  ? -57.195 46.630  85.894  1.00 16.14 ?  409  LEU A CA    1 
ATOM   3033  C C     . LEU A 1 411  ? -58.102 45.675  85.119  1.00 17.75 ?  409  LEU A C     1 
ATOM   3034  O O     . LEU A 1 411  ? -59.058 46.113  84.465  1.00 18.51 ?  409  LEU A O     1 
ATOM   3035  C CB    . LEU A 1 411  ? -55.953 46.984  85.070  1.00 16.04 ?  409  LEU A CB    1 
ATOM   3036  C CG    . LEU A 1 411  ? -55.235 48.267  85.473  1.00 16.22 ?  409  LEU A CG    1 
ATOM   3037  C CD1   . LEU A 1 411  ? -53.841 48.301  84.873  1.00 17.60 ?  409  LEU A CD1   1 
ATOM   3038  C CD2   . LEU A 1 411  ? -56.020 49.486  84.998  1.00 16.87 ?  409  LEU A CD2   1 
ATOM   3039  N N     . LEU A 1 412  ? -57.820 44.369  85.172  1.00 20.49 ?  410  LEU A N     1 
ATOM   3040  C CA    . LEU A 1 412  ? -58.636 43.413  84.432  1.00 20.49 ?  410  LEU A CA    1 
ATOM   3041  C C     . LEU A 1 412  ? -60.052 43.305  84.983  1.00 19.38 ?  410  LEU A C     1 
ATOM   3042  O O     . LEU A 1 412  ? -60.950 42.871  84.253  1.00 24.61 ?  410  LEU A O     1 
ATOM   3043  C CB    . LEU A 1 412  ? -57.968 42.037  84.430  1.00 22.00 ?  410  LEU A CB    1 
ATOM   3044  C CG    . LEU A 1 412  ? -56.754 41.957  83.500  1.00 21.98 ?  410  LEU A CG    1 
ATOM   3045  C CD1   . LEU A 1 412  ? -56.050 40.624  83.649  1.00 27.55 ?  410  LEU A CD1   1 
ATOM   3046  C CD2   . LEU A 1 412  ? -57.188 42.166  82.069  1.00 21.22 ?  410  LEU A CD2   1 
ATOM   3047  N N     . ALA A 1 413  ? -60.273 43.684  86.242  1.00 18.61 ?  411  ALA A N     1 
ATOM   3048  C CA    . ALA A 1 413  ? -61.616 43.726  86.809  1.00 20.50 ?  411  ALA A CA    1 
ATOM   3049  C C     . ALA A 1 413  ? -62.392 44.972  86.411  1.00 20.86 ?  411  ALA A C     1 
ATOM   3050  O O     . ALA A 1 413  ? -63.556 45.096  86.792  1.00 25.20 ?  411  ALA A O     1 
ATOM   3051  C CB    . ALA A 1 413  ? -61.548 43.645  88.340  1.00 24.28 ?  411  ALA A CB    1 
ATOM   3052  N N     . ALA A 1 414  ? -61.785 45.898  85.655  1.00 19.88 ?  412  ALA A N     1 
ATOM   3053  C CA    . ALA A 1 414  ? -62.405 47.182  85.346  1.00 21.42 ?  412  ALA A CA    1 
ATOM   3054  C C     . ALA A 1 414  ? -62.335 47.511  83.858  1.00 20.00 ?  412  ALA A C     1 
ATOM   3055  O O     . ALA A 1 414  ? -62.372 48.687  83.484  1.00 19.14 ?  412  ALA A O     1 
ATOM   3056  C CB    . ALA A 1 414  ? -61.754 48.303  86.161  1.00 20.95 ?  412  ALA A CB    1 
ATOM   3057  N N     . THR A 1 415  ? -62.262 46.490  82.991  1.00 19.57 ?  413  THR A N     1 
ATOM   3058  C CA    . THR A 1 415  ? -62.149 46.748  81.559  1.00 19.91 ?  413  THR A CA    1 
ATOM   3059  C C     . THR A 1 415  ? -63.387 47.413  80.970  1.00 19.34 ?  413  THR A C     1 
ATOM   3060  O O     . THR A 1 415  ? -63.323 47.890  79.830  1.00 20.71 ?  413  THR A O     1 
ATOM   3061  C CB    . THR A 1 415  ? -61.839 45.457  80.791  1.00 19.54 ?  413  THR A CB    1 
ATOM   3062  O OG1   . THR A 1 415  ? -62.906 44.509  80.983  1.00 23.82 ?  413  THR A OG1   1 
ATOM   3063  C CG2   . THR A 1 415  ? -60.538 44.844  81.286  1.00 21.31 ?  413  THR A CG2   1 
ATOM   3064  N N     . ASP A 1 416  ? -64.507 47.470  81.703  1.00 22.92 ?  414  ASP A N     1 
ATOM   3065  C CA    . ASP A 1 416  ? -65.622 48.242  81.180  1.00 21.02 ?  414  ASP A CA    1 
ATOM   3066  C C     . ASP A 1 416  ? -65.403 49.745  81.297  1.00 22.86 ?  414  ASP A C     1 
ATOM   3067  O O     . ASP A 1 416  ? -65.972 50.495  80.499  1.00 27.99 ?  414  ASP A O     1 
ATOM   3068  C CB    . ASP A 1 416  ? -66.935 47.831  81.864  1.00 26.20 ?  414  ASP A CB    1 
ATOM   3069  C CG    . ASP A 1 416  ? -66.882 47.944  83.372  1.00 33.48 ?  414  ASP A CG    1 
ATOM   3070  O OD1   . ASP A 1 416  ? -65.782 47.836  83.954  1.00 30.07 ?  414  ASP A OD1   1 
ATOM   3071  O OD2   . ASP A 1 416  ? -67.962 48.127  83.984  1.00 43.37 ?  414  ASP A OD2   1 
ATOM   3072  N N     . VAL A 1 417  ? -64.566 50.209  82.226  1.00 19.90 ?  415  VAL A N     1 
ATOM   3073  C CA    . VAL A 1 417  ? -64.384 51.643  82.412  1.00 22.31 ?  415  VAL A CA    1 
ATOM   3074  C C     . VAL A 1 417  ? -62.979 52.137  82.081  1.00 21.53 ?  415  VAL A C     1 
ATOM   3075  O O     . VAL A 1 417  ? -62.802 53.353  81.928  1.00 20.92 ?  415  VAL A O     1 
ATOM   3076  C CB    . VAL A 1 417  ? -64.771 52.092  83.834  1.00 24.22 ?  415  VAL A CB    1 
ATOM   3077  C CG1   . VAL A 1 417  ? -66.211 51.691  84.138  1.00 30.45 ?  415  VAL A CG1   1 
ATOM   3078  C CG2   . VAL A 1 417  ? -63.807 51.541  84.844  1.00 22.62 ?  415  VAL A CG2   1 
ATOM   3079  N N     . VAL A 1 418  ? -61.976 51.258  81.989  1.00 17.45 ?  416  VAL A N     1 
ATOM   3080  C CA    . VAL A 1 418  ? -60.644 51.644  81.535  1.00 18.15 ?  416  VAL A CA    1 
ATOM   3081  C C     . VAL A 1 418  ? -60.158 50.624  80.521  1.00 17.84 ?  416  VAL A C     1 
ATOM   3082  O O     . VAL A 1 418  ? -60.663 49.503  80.440  1.00 17.26 ?  416  VAL A O     1 
ATOM   3083  C CB    . VAL A 1 418  ? -59.614 51.779  82.684  1.00 14.41 ?  416  VAL A CB    1 
ATOM   3084  C CG1   . VAL A 1 418  ? -60.043 52.870  83.662  1.00 17.49 ?  416  VAL A CG1   1 
ATOM   3085  C CG2   . VAL A 1 418  ? -59.400 50.456  83.407  1.00 18.02 ?  416  VAL A CG2   1 
ATOM   3086  N N     . PHE A 1 419  ? -59.155 51.033  79.743  1.00 14.23 ?  417  PHE A N     1 
ATOM   3087  C CA    . PHE A 1 419  ? -58.516 50.182  78.743  1.00 16.45 ?  417  PHE A CA    1 
ATOM   3088  C C     . PHE A 1 419  ? -57.115 49.829  79.233  1.00 13.78 ?  417  PHE A C     1 
ATOM   3089  O O     . PHE A 1 419  ? -56.189 50.647  79.090  1.00 15.22 ?  417  PHE A O     1 
ATOM   3090  C CB    . PHE A 1 419  ? -58.452 50.902  77.391  1.00 15.66 ?  417  PHE A CB    1 
ATOM   3091  C CG    . PHE A 1 419  ? -57.726 50.133  76.315  1.00 15.78 ?  417  PHE A CG    1 
ATOM   3092  C CD1   . PHE A 1 419  ? -58.168 48.874  75.922  1.00 18.50 ?  417  PHE A CD1   1 
ATOM   3093  C CD2   . PHE A 1 419  ? -56.634 50.680  75.673  1.00 15.73 ?  417  PHE A CD2   1 
ATOM   3094  C CE1   . PHE A 1 419  ? -57.522 48.165  74.930  1.00 17.15 ?  417  PHE A CE1   1 
ATOM   3095  C CE2   . PHE A 1 419  ? -55.975 49.980  74.676  1.00 14.30 ?  417  PHE A CE2   1 
ATOM   3096  C CZ    . PHE A 1 419  ? -56.418 48.724  74.292  1.00 15.91 ?  417  PHE A CZ    1 
ATOM   3097  N N     . PRO A 1 420  ? -56.902 48.642  79.810  1.00 14.42 ?  418  PRO A N     1 
ATOM   3098  C CA    . PRO A 1 420  ? -55.564 48.294  80.316  1.00 13.90 ?  418  PRO A CA    1 
ATOM   3099  C C     . PRO A 1 420  ? -54.582 48.004  79.191  1.00 13.92 ?  418  PRO A C     1 
ATOM   3100  O O     . PRO A 1 420  ? -54.914 47.337  78.206  1.00 16.80 ?  418  PRO A O     1 
ATOM   3101  C CB    . PRO A 1 420  ? -55.815 47.036  81.160  1.00 14.22 ?  418  PRO A CB    1 
ATOM   3102  C CG    . PRO A 1 420  ? -57.289 47.027  81.419  1.00 16.81 ?  418  PRO A CG    1 
ATOM   3103  C CD    . PRO A 1 420  ? -57.898 47.618  80.184  1.00 15.54 ?  418  PRO A CD    1 
ATOM   3104  N N     . GLN A 1 421  ? -53.358 48.509  79.359  1.00 14.12 ?  419  GLN A N     1 
ATOM   3105  C CA    . GLN A 1 421  ? -52.275 48.340  78.396  1.00 14.44 ?  419  GLN A CA    1 
ATOM   3106  C C     . GLN A 1 421  ? -51.069 47.828  79.168  1.00 13.37 ?  419  GLN A C     1 
ATOM   3107  O O     . GLN A 1 421  ? -50.462 48.573  79.941  1.00 14.48 ?  419  GLN A O     1 
ATOM   3108  C CB    . GLN A 1 421  ? -51.971 49.657  77.690  1.00 12.78 ?  419  GLN A CB    1 
ATOM   3109  C CG    . GLN A 1 421  ? -53.203 50.273  77.009  1.00 14.35 ?  419  GLN A CG    1 
ATOM   3110  C CD    . GLN A 1 421  ? -52.976 51.728  76.626  1.00 12.80 ?  419  GLN A CD    1 
ATOM   3111  O OE1   . GLN A 1 421  ? -52.737 52.570  77.500  1.00 15.52 ?  419  GLN A OE1   1 
ATOM   3112  N NE2   . GLN A 1 421  ? -53.073 52.040  75.329  1.00 14.35 ?  419  GLN A NE2   1 
ATOM   3113  N N     . PHE A 1 422  ? -50.722 46.561  78.967  1.00 14.33 ?  420  PHE A N     1 
ATOM   3114  C CA    . PHE A 1 422  ? -49.717 45.892  79.793  1.00 14.48 ?  420  PHE A CA    1 
ATOM   3115  C C     . PHE A 1 422  ? -48.365 45.951  79.079  1.00 15.09 ?  420  PHE A C     1 
ATOM   3116  O O     . PHE A 1 422  ? -48.062 45.115  78.227  1.00 15.41 ?  420  PHE A O     1 
ATOM   3117  C CB    . PHE A 1 422  ? -50.166 44.470  80.101  1.00 15.87 ?  420  PHE A CB    1 
ATOM   3118  C CG    . PHE A 1 422  ? -51.453 44.417  80.881  1.00 16.99 ?  420  PHE A CG    1 
ATOM   3119  C CD1   . PHE A 1 422  ? -51.510 44.922  82.171  1.00 19.49 ?  420  PHE A CD1   1 
ATOM   3120  C CD2   . PHE A 1 422  ? -52.603 43.886  80.318  1.00 18.69 ?  420  PHE A CD2   1 
ATOM   3121  C CE1   . PHE A 1 422  ? -52.695 44.885  82.894  1.00 16.21 ?  420  PHE A CE1   1 
ATOM   3122  C CE2   . PHE A 1 422  ? -53.784 43.847  81.043  1.00 17.62 ?  420  PHE A CE2   1 
ATOM   3123  C CZ    . PHE A 1 422  ? -53.822 44.353  82.328  1.00 19.90 ?  420  PHE A CZ    1 
ATOM   3124  N N     . ALA A 1 423  ? -47.556 46.946  79.443  1.00 14.47 ?  421  ALA A N     1 
ATOM   3125  C CA    . ALA A 1 423  ? -46.248 47.175  78.833  1.00 12.62 ?  421  ALA A CA    1 
ATOM   3126  C C     . ALA A 1 423  ? -45.207 46.339  79.565  1.00 14.30 ?  421  ALA A C     1 
ATOM   3127  O O     . ALA A 1 423  ? -44.869 46.638  80.715  1.00 16.89 ?  421  ALA A O     1 
ATOM   3128  C CB    . ALA A 1 423  ? -45.896 48.660  78.904  1.00 13.28 ?  421  ALA A CB    1 
ATOM   3129  N N     . THR A 1 424  ? -44.679 45.306  78.903  1.00 13.93 ?  422  THR A N     1 
ATOM   3130  C CA    . THR A 1 424  ? -43.629 44.494  79.515  1.00 15.05 ?  422  THR A CA    1 
ATOM   3131  C C     . THR A 1 424  ? -42.940 43.651  78.447  1.00 15.65 ?  422  THR A C     1 
ATOM   3132  O O     . THR A 1 424  ? -43.560 43.237  77.460  1.00 16.47 ?  422  THR A O     1 
ATOM   3133  C CB    . THR A 1 424  ? -44.162 43.588  80.635  1.00 16.49 ?  422  THR A CB    1 
ATOM   3134  O OG1   . THR A 1 424  ? -43.059 42.900  81.253  1.00 16.33 ?  422  THR A OG1   1 
ATOM   3135  C CG2   . THR A 1 424  ? -45.125 42.562  80.091  1.00 19.81 ?  422  THR A CG2   1 
ATOM   3136  N N     . HIS A 1 425  ? -41.640 43.417  78.654  1.00 16.45 ?  423  HIS A N     1 
ATOM   3137  C CA    . HIS A 1 425  ? -40.867 42.469  77.856  1.00 16.20 ?  423  HIS A CA    1 
ATOM   3138  C C     . HIS A 1 425  ? -40.654 41.136  78.560  1.00 17.82 ?  423  HIS A C     1 
ATOM   3139  O O     . HIS A 1 425  ? -39.973 40.262  78.016  1.00 20.09 ?  423  HIS A O     1 
ATOM   3140  C CB    . HIS A 1 425  ? -39.515 43.074  77.489  1.00 15.47 ?  423  HIS A CB    1 
ATOM   3141  C CG    . HIS A 1 425  ? -39.638 44.329  76.696  1.00 15.92 ?  423  HIS A CG    1 
ATOM   3142  N ND1   . HIS A 1 425  ? -38.937 45.474  77.001  1.00 17.50 ?  423  HIS A ND1   1 
ATOM   3143  C CD2   . HIS A 1 425  ? -40.412 44.630  75.628  1.00 18.30 ?  423  HIS A CD2   1 
ATOM   3144  C CE1   . HIS A 1 425  ? -39.268 46.426  76.144  1.00 16.94 ?  423  HIS A CE1   1 
ATOM   3145  N NE2   . HIS A 1 425  ? -40.161 45.936  75.301  1.00 16.41 ?  423  HIS A NE2   1 
ATOM   3146  N N     . ASN A 1 426  ? -41.215 40.967  79.751  1.00 16.11 ?  424  ASN A N     1 
ATOM   3147  C CA    . ASN A 1 426  ? -41.003 39.776  80.572  1.00 19.29 ?  424  ASN A CA    1 
ATOM   3148  C C     . ASN A 1 426  ? -42.058 38.717  80.239  1.00 21.68 ?  424  ASN A C     1 
ATOM   3149  O O     . ASN A 1 426  ? -43.252 38.916  80.494  1.00 19.24 ?  424  ASN A O     1 
ATOM   3150  C CB    . ASN A 1 426  ? -41.064 40.193  82.044  1.00 19.13 ?  424  ASN A CB    1 
ATOM   3151  C CG    . ASN A 1 426  ? -40.720 39.067  83.008  1.00 20.53 ?  424  ASN A CG    1 
ATOM   3152  O OD1   . ASN A 1 426  ? -41.169 37.936  82.852  1.00 22.75 ?  424  ASN A OD1   1 
ATOM   3153  N ND2   . ASN A 1 426  ? -39.944 39.393  84.033  1.00 20.17 ?  424  ASN A ND2   1 
ATOM   3154  N N     . ALA A 1 427  ? -41.617 37.576  79.689  1.00 19.01 ?  425  ALA A N     1 
ATOM   3155  C CA    . ALA A 1 427  ? -42.559 36.554  79.240  1.00 19.29 ?  425  ALA A CA    1 
ATOM   3156  C C     . ALA A 1 427  ? -43.318 35.923  80.401  1.00 20.52 ?  425  ALA A C     1 
ATOM   3157  O O     . ALA A 1 427  ? -44.452 35.464  80.216  1.00 21.77 ?  425  ALA A O     1 
ATOM   3158  C CB    . ALA A 1 427  ? -41.829 35.471  78.441  1.00 22.00 ?  425  ALA A CB    1 
ATOM   3159  N N     . GLN A 1 428  ? -42.715 35.882  81.590  1.00 20.86 ?  426  GLN A N     1 
ATOM   3160  C CA    . GLN A 1 428  ? -43.426 35.362  82.755  1.00 21.73 ?  426  GLN A CA    1 
ATOM   3161  C C     . GLN A 1 428  ? -44.559 36.298  83.150  1.00 21.21 ?  426  GLN A C     1 
ATOM   3162  O O     . GLN A 1 428  ? -45.692 35.856  83.375  1.00 21.41 ?  426  GLN A O     1 
ATOM   3163  C CB    . GLN A 1 428  ? -42.453 35.159  83.920  1.00 23.81 ?  426  GLN A CB    1 
ATOM   3164  C CG    . GLN A 1 428  ? -42.974 34.228  85.020  1.00 26.55 ?  426  GLN A CG    1 
ATOM   3165  C CD    . GLN A 1 428  ? -44.008 34.881  85.918  1.00 29.64 ?  426  GLN A CD    1 
ATOM   3166  O OE1   . GLN A 1 428  ? -43.905 36.071  86.243  1.00 26.91 ?  426  GLN A OE1   1 
ATOM   3167  N NE2   . GLN A 1 428  ? -45.020 34.110  86.318  1.00 28.14 ?  426  GLN A NE2   1 
ATOM   3168  N N     . THR A 1 429  ? -44.266 37.602  83.230  1.00 20.03 ?  427  THR A N     1 
ATOM   3169  C CA    . THR A 1 429  ? -45.304 38.591  83.504  1.00 20.10 ?  427  THR A CA    1 
ATOM   3170  C C     . THR A 1 429  ? -46.420 38.510  82.472  1.00 21.29 ?  427  THR A C     1 
ATOM   3171  O O     . THR A 1 429  ? -47.610 38.480  82.820  1.00 19.51 ?  427  THR A O     1 
ATOM   3172  C CB    . THR A 1 429  ? -44.686 39.990  83.508  1.00 19.79 ?  427  THR A CB    1 
ATOM   3173  O OG1   . THR A 1 429  ? -43.560 40.019  84.390  1.00 20.37 ?  427  THR A OG1   1 
ATOM   3174  C CG2   . THR A 1 429  ? -45.704 41.005  83.975  1.00 22.02 ?  427  THR A CG2   1 
ATOM   3175  N N     . LEU A 1 430  ? -46.043 38.464  81.190  1.00 19.25 ?  428  LEU A N     1 
ATOM   3176  C CA    . LEU A 1 430  ? -47.006 38.363  80.098  1.00 19.64 ?  428  LEU A CA    1 
ATOM   3177  C C     . LEU A 1 430  ? -47.909 37.147  80.265  1.00 21.55 ?  428  LEU A C     1 
ATOM   3178  O O     . LEU A 1 430  ? -49.138 37.261  80.200  1.00 22.38 ?  428  LEU A O     1 
ATOM   3179  C CB    . LEU A 1 430  ? -46.251 38.303  78.765  1.00 19.32 ?  428  LEU A CB    1 
ATOM   3180  C CG    . LEU A 1 430  ? -46.950 38.496  77.415  1.00 24.36 ?  428  LEU A CG    1 
ATOM   3181  C CD1   . LEU A 1 430  ? -45.884 38.695  76.350  1.00 26.51 ?  428  LEU A CD1   1 
ATOM   3182  C CD2   . LEU A 1 430  ? -47.831 37.324  77.040  1.00 23.95 ?  428  LEU A CD2   1 
ATOM   3183  N N     . ALA A 1 431  ? -47.313 35.968  80.468  1.00 21.17 ?  429  ALA A N     1 
ATOM   3184  C CA    . ALA A 1 431  ? -48.105 34.743  80.574  1.00 22.61 ?  429  ALA A CA    1 
ATOM   3185  C C     . ALA A 1 431  ? -49.076 34.802  81.744  1.00 23.74 ?  429  ALA A C     1 
ATOM   3186  O O     . ALA A 1 431  ? -50.230 34.363  81.625  1.00 23.41 ?  429  ALA A O     1 
ATOM   3187  C CB    . ALA A 1 431  ? -47.182 33.532  80.719  1.00 21.98 ?  429  ALA A CB    1 
ATOM   3188  N N     . ALA A 1 432  ? -48.624 35.328  82.885  1.00 23.65 ?  430  ALA A N     1 
ATOM   3189  C CA    . ALA A 1 432  ? -49.487 35.396  84.060  1.00 24.52 ?  430  ALA A CA    1 
ATOM   3190  C C     . ALA A 1 432  ? -50.735 36.216  83.774  1.00 26.09 ?  430  ALA A C     1 
ATOM   3191  O O     . ALA A 1 432  ? -51.849 35.829  84.151  1.00 24.67 ?  430  ALA A O     1 
ATOM   3192  C CB    . ALA A 1 432  ? -48.712 35.977  85.243  1.00 24.82 ?  430  ALA A CB    1 
ATOM   3193  N N     . ILE A 1 433  ? -50.572 37.331  83.065  1.00 23.74 ?  431  ILE A N     1 
ATOM   3194  C CA    . ILE A 1 433  ? -51.682 38.223  82.759  1.00 23.90 ?  431  ILE A CA    1 
ATOM   3195  C C     . ILE A 1 433  ? -52.560 37.653  81.653  1.00 23.39 ?  431  ILE A C     1 
ATOM   3196  O O     . ILE A 1 433  ? -53.793 37.767  81.701  1.00 24.17 ?  431  ILE A O     1 
ATOM   3197  C CB    . ILE A 1 433  ? -51.113 39.603  82.394  1.00 24.31 ?  431  ILE A CB    1 
ATOM   3198  C CG1   . ILE A 1 433  ? -50.444 40.201  83.626  1.00 22.36 ?  431  ILE A CG1   1 
ATOM   3199  C CG2   . ILE A 1 433  ? -52.181 40.511  81.818  1.00 23.67 ?  431  ILE A CG2   1 
ATOM   3200  C CD1   . ILE A 1 433  ? -49.717 41.472  83.341  1.00 22.42 ?  431  ILE A CD1   1 
ATOM   3201  N N     . TYR A 1 434  ? -51.946 37.037  80.642  1.00 23.54 ?  432  TYR A N     1 
ATOM   3202  C CA    . TYR A 1 434  ? -52.715 36.389  79.587  1.00 23.54 ?  432  TYR A CA    1 
ATOM   3203  C C     . TYR A 1 434  ? -53.689 35.363  80.161  1.00 24.30 ?  432  TYR A C     1 
ATOM   3204  O O     . TYR A 1 434  ? -54.865 35.330  79.777  1.00 26.99 ?  432  TYR A O     1 
ATOM   3205  C CB    . TYR A 1 434  ? -51.754 35.751  78.582  1.00 25.64 ?  432  TYR A CB    1 
ATOM   3206  C CG    . TYR A 1 434  ? -52.399 34.820  77.594  1.00 25.37 ?  432  TYR A CG    1 
ATOM   3207  C CD1   . TYR A 1 434  ? -53.194 35.303  76.565  1.00 24.94 ?  432  TYR A CD1   1 
ATOM   3208  C CD2   . TYR A 1 434  ? -52.202 33.447  77.684  1.00 26.81 ?  432  TYR A CD2   1 
ATOM   3209  C CE1   . TYR A 1 434  ? -53.788 34.437  75.656  1.00 28.60 ?  432  TYR A CE1   1 
ATOM   3210  C CE2   . TYR A 1 434  ? -52.780 32.580  76.786  1.00 29.82 ?  432  TYR A CE2   1 
ATOM   3211  C CZ    . TYR A 1 434  ? -53.572 33.075  75.776  1.00 34.67 ?  432  TYR A CZ    1 
ATOM   3212  O OH    . TYR A 1 434  ? -54.149 32.200  74.884  1.00 37.98 ?  432  TYR A OH    1 
ATOM   3213  N N     . HIS A 1 435  ? -53.237 34.540  81.105  1.00 25.00 ?  433  HIS A N     1 
ATOM   3214  C CA    . HIS A 1 435  ? -54.165 33.563  81.674  1.00 25.68 ?  433  HIS A CA    1 
ATOM   3215  C C     . HIS A 1 435  ? -55.097 34.193  82.704  1.00 27.58 ?  433  HIS A C     1 
ATOM   3216  O O     . HIS A 1 435  ? -56.244 33.747  82.851  1.00 27.62 ?  433  HIS A O     1 
ATOM   3217  C CB    . HIS A 1 435  ? -53.386 32.394  82.272  1.00 27.58 ?  433  HIS A CB    1 
ATOM   3218  C CG    . HIS A 1 435  ? -52.761 31.516  81.233  1.00 30.32 ?  433  HIS A CG    1 
ATOM   3219  N ND1   . HIS A 1 435  ? -53.461 30.525  80.580  1.00 28.49 ?  433  HIS A ND1   1 
ATOM   3220  C CD2   . HIS A 1 435  ? -51.512 31.501  80.712  1.00 28.16 ?  433  HIS A CD2   1 
ATOM   3221  C CE1   . HIS A 1 435  ? -52.666 29.928  79.710  1.00 30.64 ?  433  HIS A CE1   1 
ATOM   3222  N NE2   . HIS A 1 435  ? -51.477 30.499  79.771  1.00 29.76 ?  433  HIS A NE2   1 
ATOM   3223  N N     . MET A 1 436  ? -54.636 35.236  83.397  1.00 26.12 ?  434  MET A N     1 
ATOM   3224  C CA    . MET A 1 436  ? -55.500 35.941  84.337  1.00 26.55 ?  434  MET A CA    1 
ATOM   3225  C C     . MET A 1 436  ? -56.700 36.560  83.630  1.00 29.12 ?  434  MET A C     1 
ATOM   3226  O O     . MET A 1 436  ? -57.813 36.567  84.173  1.00 27.88 ?  434  MET A O     1 
ATOM   3227  C CB    . MET A 1 436  ? -54.696 37.012  85.070  1.00 26.25 ?  434  MET A CB    1 
ATOM   3228  C CG    . MET A 1 436  ? -55.514 37.826  86.042  1.00 28.42 ?  434  MET A CG    1 
ATOM   3229  S SD    . MET A 1 436  ? -54.575 39.207  86.714  1.00 30.10 ?  434  MET A SD    1 
ATOM   3230  C CE    . MET A 1 436  ? -53.410 38.337  87.762  1.00 29.32 ?  434  MET A CE    1 
ATOM   3231  N N     . ALA A 1 437  ? -56.498 37.074  82.413  1.00 24.91 ?  435  ALA A N     1 
ATOM   3232  C CA    . ALA A 1 437  ? -57.578 37.727  81.678  1.00 28.42 ?  435  ALA A CA    1 
ATOM   3233  C C     . ALA A 1 437  ? -58.628 36.745  81.171  1.00 32.15 ?  435  ALA A C     1 
ATOM   3234  O O     . ALA A 1 437  ? -59.745 37.164  80.840  1.00 30.20 ?  435  ALA A O     1 
ATOM   3235  C CB    . ALA A 1 437  ? -57.006 38.525  80.506  1.00 28.65 ?  435  ALA A CB    1 
ATOM   3236  N N     . GLY A 1 438  ? -58.298 35.463  81.086  1.00 32.55 ?  436  GLY A N     1 
ATOM   3237  C CA    . GLY A 1 438  ? -59.284 34.469  80.726  1.00 34.54 ?  436  GLY A CA    1 
ATOM   3238  C C     . GLY A 1 438  ? -59.518 34.364  79.230  1.00 37.17 ?  436  GLY A C     1 
ATOM   3239  O O     . GLY A 1 438  ? -58.802 34.932  78.400  1.00 34.94 ?  436  GLY A O     1 
ATOM   3240  N N     . LYS A 1 439  ? -60.588 33.639  78.898  1.00 38.75 ?  437  LYS A N     1 
ATOM   3241  C CA    . LYS A 1 439  ? -60.851 33.185  77.537  1.00 41.76 ?  437  LYS A CA    1 
ATOM   3242  C C     . LYS A 1 439  ? -61.559 34.211  76.663  1.00 38.45 ?  437  LYS A C     1 
ATOM   3243  O O     . LYS A 1 439  ? -61.359 34.208  75.443  1.00 38.30 ?  437  LYS A O     1 
ATOM   3244  C CB    . LYS A 1 439  ? -61.693 31.906  77.577  1.00 41.63 ?  437  LYS A CB    1 
ATOM   3245  N N     . ASP A 1 440  ? -62.389 35.077  77.238  1.00 37.12 ?  438  ASP A N     1 
ATOM   3246  C CA    . ASP A 1 440  ? -63.156 36.026  76.439  1.00 39.43 ?  438  ASP A CA    1 
ATOM   3247  C C     . ASP A 1 440  ? -62.272 37.212  76.082  1.00 37.45 ?  438  ASP A C     1 
ATOM   3248  O O     . ASP A 1 440  ? -61.747 37.891  76.973  1.00 36.58 ?  438  ASP A O     1 
ATOM   3249  C CB    . ASP A 1 440  ? -64.400 36.493  77.193  1.00 39.93 ?  438  ASP A CB    1 
ATOM   3250  C CG    . ASP A 1 440  ? -65.367 35.359  77.484  1.00 47.02 ?  438  ASP A CG    1 
ATOM   3251  O OD1   . ASP A 1 440  ? -65.404 34.394  76.693  1.00 47.93 ?  438  ASP A OD1   1 
ATOM   3252  O OD2   . ASP A 1 440  ? -66.084 35.434  78.505  1.00 46.62 ?  438  ASP A OD2   1 
ATOM   3253  N N     . PHE A 1 441  ? -62.103 37.464  74.788  1.00 32.66 ?  439  PHE A N     1 
ATOM   3254  C CA    . PHE A 1 441  ? -61.318 38.609  74.361  1.00 30.21 ?  439  PHE A CA    1 
ATOM   3255  C C     . PHE A 1 441  ? -61.916 39.226  73.109  1.00 33.97 ?  439  PHE A C     1 
ATOM   3256  O O     . PHE A 1 441  ? -62.469 38.531  72.254  1.00 32.35 ?  439  PHE A O     1 
ATOM   3257  C CB    . PHE A 1 441  ? -59.854 38.252  74.086  1.00 30.99 ?  439  PHE A CB    1 
ATOM   3258  C CG    . PHE A 1 441  ? -59.022 39.446  73.750  1.00 25.20 ?  439  PHE A CG    1 
ATOM   3259  C CD1   . PHE A 1 441  ? -58.563 40.274  74.759  1.00 28.93 ?  439  PHE A CD1   1 
ATOM   3260  C CD2   . PHE A 1 441  ? -58.747 39.780  72.435  1.00 26.28 ?  439  PHE A CD2   1 
ATOM   3261  C CE1   . PHE A 1 441  ? -57.824 41.398  74.468  1.00 26.03 ?  439  PHE A CE1   1 
ATOM   3262  C CE2   . PHE A 1 441  ? -58.004 40.914  72.136  1.00 28.03 ?  439  PHE A CE2   1 
ATOM   3263  C CZ    . PHE A 1 441  ? -57.544 41.718  73.163  1.00 23.07 ?  439  PHE A CZ    1 
ATOM   3264  N N     . HIS A 1 442  ? -61.786 40.547  73.012  1.00 27.38 ?  440  HIS A N     1 
ATOM   3265  C CA    . HIS A 1 442  ? -62.093 41.290  71.797  1.00 28.92 ?  440  HIS A CA    1 
ATOM   3266  C C     . HIS A 1 442  ? -61.149 42.478  71.739  1.00 28.25 ?  440  HIS A C     1 
ATOM   3267  O O     . HIS A 1 442  ? -60.725 42.988  72.777  1.00 24.76 ?  440  HIS A O     1 
ATOM   3268  C CB    . HIS A 1 442  ? -63.551 41.762  71.762  1.00 32.04 ?  440  HIS A CB    1 
ATOM   3269  C CG    . HIS A 1 442  ? -63.936 42.627  72.921  1.00 28.41 ?  440  HIS A CG    1 
ATOM   3270  N ND1   . HIS A 1 442  ? -63.876 44.005  72.878  1.00 31.21 ?  440  HIS A ND1   1 
ATOM   3271  C CD2   . HIS A 1 442  ? -64.386 42.309  74.158  1.00 27.07 ?  440  HIS A CD2   1 
ATOM   3272  C CE1   . HIS A 1 442  ? -64.276 44.497  74.037  1.00 27.93 ?  440  HIS A CE1   1 
ATOM   3273  N NE2   . HIS A 1 442  ? -64.591 43.489  74.832  1.00 31.11 ?  440  HIS A NE2   1 
ATOM   3274  N N     . VAL A 1 443  ? -60.802 42.907  70.522  1.00 27.92 ?  441  VAL A N     1 
ATOM   3275  C CA    . VAL A 1 443  ? -59.939 44.075  70.392  1.00 30.40 ?  441  VAL A CA    1 
ATOM   3276  C C     . VAL A 1 443  ? -60.642 45.268  71.017  1.00 28.15 ?  441  VAL A C     1 
ATOM   3277  O O     . VAL A 1 443  ? -61.819 45.534  70.739  1.00 28.90 ?  441  VAL A O     1 
ATOM   3278  C CB    . VAL A 1 443  ? -59.569 44.325  68.923  1.00 30.43 ?  441  VAL A CB    1 
ATOM   3279  C CG1   . VAL A 1 443  ? -59.022 45.736  68.743  1.00 30.37 ?  441  VAL A CG1   1 
ATOM   3280  C CG2   . VAL A 1 443  ? -58.530 43.311  68.471  1.00 31.18 ?  441  VAL A CG2   1 
ATOM   3281  N N     . GLY A 1 444  ? -59.932 45.967  71.898  1.00 24.51 ?  442  GLY A N     1 
ATOM   3282  C CA    . GLY A 1 444  ? -60.510 47.013  72.715  1.00 19.43 ?  442  GLY A CA    1 
ATOM   3283  C C     . GLY A 1 444  ? -60.685 46.634  74.167  1.00 18.52 ?  442  GLY A C     1 
ATOM   3284  O O     . GLY A 1 444  ? -60.931 47.520  74.994  1.00 20.10 ?  442  GLY A O     1 
ATOM   3285  N N     . LYS A 1 445  ? -60.546 45.357  74.516  1.00 20.15 ?  443  LYS A N     1 
ATOM   3286  C CA    . LYS A 1 445  ? -60.708 44.970  75.912  1.00 19.79 ?  443  LYS A CA    1 
ATOM   3287  C C     . LYS A 1 445  ? -59.461 45.315  76.712  1.00 18.61 ?  443  LYS A C     1 
ATOM   3288  O O     . LYS A 1 445  ? -59.540 45.988  77.747  1.00 20.38 ?  443  LYS A O     1 
ATOM   3289  C CB    . LYS A 1 445  ? -61.018 43.479  76.023  1.00 23.76 ?  443  LYS A CB    1 
ATOM   3290  C CG    . LYS A 1 445  ? -61.401 43.071  77.432  1.00 23.60 ?  443  LYS A CG    1 
ATOM   3291  C CD    . LYS A 1 445  ? -62.073 41.716  77.457  1.00 27.87 ?  443  LYS A CD    1 
ATOM   3292  C CE    . LYS A 1 445  ? -62.720 41.455  78.811  1.00 32.32 ?  443  LYS A CE    1 
ATOM   3293  N NZ    . LYS A 1 445  ? -63.243 40.055  78.905  1.00 37.02 ?  443  LYS A NZ    1 
ATOM   3294  N N     . TYR A 1 446  ? -58.301 44.866  76.233  1.00 18.87 ?  444  TYR A N     1 
ATOM   3295  C CA    . TYR A 1 446  ? -57.003 45.277  76.753  1.00 16.96 ?  444  TYR A CA    1 
ATOM   3296  C C     . TYR A 1 446  ? -55.985 44.987  75.660  1.00 18.57 ?  444  TYR A C     1 
ATOM   3297  O O     . TYR A 1 446  ? -56.313 44.397  74.631  1.00 18.31 ?  444  TYR A O     1 
ATOM   3298  C CB    . TYR A 1 446  ? -56.656 44.551  78.058  1.00 19.04 ?  444  TYR A CB    1 
ATOM   3299  C CG    . TYR A 1 446  ? -56.432 43.071  77.897  1.00 21.46 ?  444  TYR A CG    1 
ATOM   3300  C CD1   . TYR A 1 446  ? -57.498 42.186  77.990  1.00 27.94 ?  444  TYR A CD1   1 
ATOM   3301  C CD2   . TYR A 1 446  ? -55.164 42.554  77.648  1.00 25.02 ?  444  TYR A CD2   1 
ATOM   3302  C CE1   . TYR A 1 446  ? -57.312 40.835  77.843  1.00 28.28 ?  444  TYR A CE1   1 
ATOM   3303  C CE2   . TYR A 1 446  ? -54.972 41.185  77.500  1.00 30.46 ?  444  TYR A CE2   1 
ATOM   3304  C CZ    . TYR A 1 446  ? -56.057 40.339  77.595  1.00 31.91 ?  444  TYR A CZ    1 
ATOM   3305  O OH    . TYR A 1 446  ? -55.900 38.976  77.454  1.00 42.21 ?  444  TYR A OH    1 
ATOM   3306  N N     . GLU A 1 447  ? -54.744 45.412  75.885  1.00 16.13 ?  445  GLU A N     1 
ATOM   3307  C CA    . GLU A 1 447  ? -53.668 45.093  74.954  1.00 16.03 ?  445  GLU A CA    1 
ATOM   3308  C C     . GLU A 1 447  ? -52.378 44.958  75.741  1.00 16.56 ?  445  GLU A C     1 
ATOM   3309  O O     . GLU A 1 447  ? -52.296 45.356  76.903  1.00 16.74 ?  445  GLU A O     1 
ATOM   3310  C CB    . GLU A 1 447  ? -53.511 46.156  73.857  1.00 14.91 ?  445  GLU A CB    1 
ATOM   3311  C CG    . GLU A 1 447  ? -53.065 47.509  74.401  1.00 16.01 ?  445  GLU A CG    1 
ATOM   3312  C CD    . GLU A 1 447  ? -52.976 48.614  73.358  1.00 15.89 ?  445  GLU A CD    1 
ATOM   3313  O OE1   . GLU A 1 447  ? -53.513 48.461  72.240  1.00 18.20 ?  445  GLU A OE1   1 
ATOM   3314  O OE2   . GLU A 1 447  ? -52.362 49.658  73.681  1.00 15.62 ?  445  GLU A OE2   1 
ATOM   3315  N N     . PHE A 1 448  ? -51.369 44.381  75.098  1.00 17.69 ?  446  PHE A N     1 
ATOM   3316  C CA    . PHE A 1 448  ? -50.004 44.445  75.590  1.00 17.18 ?  446  PHE A CA    1 
ATOM   3317  C C     . PHE A 1 448  ? -49.275 45.575  74.868  1.00 14.39 ?  446  PHE A C     1 
ATOM   3318  O O     . PHE A 1 448  ? -49.763 46.121  73.877  1.00 16.35 ?  446  PHE A O     1 
ATOM   3319  C CB    . PHE A 1 448  ? -49.278 43.113  75.377  1.00 17.63 ?  446  PHE A CB    1 
ATOM   3320  C CG    . PHE A 1 448  ? -49.873 41.966  76.142  1.00 18.40 ?  446  PHE A CG    1 
ATOM   3321  C CD1   . PHE A 1 448  ? -49.531 41.750  77.468  1.00 18.64 ?  446  PHE A CD1   1 
ATOM   3322  C CD2   . PHE A 1 448  ? -50.768 41.102  75.537  1.00 20.72 ?  446  PHE A CD2   1 
ATOM   3323  C CE1   . PHE A 1 448  ? -50.076 40.691  78.184  1.00 22.51 ?  446  PHE A CE1   1 
ATOM   3324  C CE2   . PHE A 1 448  ? -51.323 40.042  76.242  1.00 24.90 ?  446  PHE A CE2   1 
ATOM   3325  C CZ    . PHE A 1 448  ? -50.978 39.836  77.568  1.00 22.14 ?  446  PHE A CZ    1 
ATOM   3326  N N     . GLN A 1 449  ? -48.111 45.947  75.395  1.00 14.87 ?  447  GLN A N     1 
ATOM   3327  C CA    . GLN A 1 449  ? -47.259 46.934  74.742  1.00 14.88 ?  447  GLN A CA    1 
ATOM   3328  C C     . GLN A 1 449  ? -45.803 46.536  74.896  1.00 16.34 ?  447  GLN A C     1 
ATOM   3329  O O     . GLN A 1 449  ? -45.430 45.823  75.829  1.00 15.23 ?  447  GLN A O     1 
ATOM   3330  C CB    . GLN A 1 449  ? -47.436 48.350  75.313  1.00 13.78 ?  447  GLN A CB    1 
ATOM   3331  C CG    . GLN A 1 449  ? -48.850 48.847  75.239  1.00 15.29 ?  447  GLN A CG    1 
ATOM   3332  C CD    . GLN A 1 449  ? -48.944 50.341  75.434  1.00 14.66 ?  447  GLN A CD    1 
ATOM   3333  O OE1   . GLN A 1 449  ? -48.018 50.971  75.948  1.00 16.52 ?  447  GLN A OE1   1 
ATOM   3334  N NE2   . GLN A 1 449  ? -50.069 50.921  75.022  1.00 14.73 ?  447  GLN A NE2   1 
ATOM   3335  N N     . CYS A 1 450  ? -44.979 47.026  73.974  1.00 13.98 ?  448  CYS A N     1 
ATOM   3336  C CA    . CYS A 1 450  ? -43.553 46.729  74.003  1.00 14.19 ?  448  CYS A CA    1 
ATOM   3337  C C     . CYS A 1 450  ? -42.800 47.872  73.345  1.00 15.17 ?  448  CYS A C     1 
ATOM   3338  O O     . CYS A 1 450  ? -43.389 48.754  72.714  1.00 15.54 ?  448  CYS A O     1 
ATOM   3339  C CB    . CYS A 1 450  ? -43.231 45.404  73.304  1.00 15.54 ?  448  CYS A CB    1 
ATOM   3340  S SG    . CYS A 1 450  ? -43.321 45.454  71.482  1.00 18.29 ?  448  CYS A SG    1 
ATOM   3341  N N     . LEU A 1 451  ? -41.477 47.828  73.479  1.00 14.20 ?  449  LEU A N     1 
ATOM   3342  C CA    . LEU A 1 451  ? -40.602 48.843  72.916  1.00 14.16 ?  449  LEU A CA    1 
ATOM   3343  C C     . LEU A 1 451  ? -40.118 48.437  71.530  1.00 14.04 ?  449  LEU A C     1 
ATOM   3344  O O     . LEU A 1 451  ? -39.758 47.277  71.300  1.00 16.25 ?  449  LEU A O     1 
ATOM   3345  C CB    . LEU A 1 451  ? -39.411 49.067  73.847  1.00 15.38 ?  449  LEU A CB    1 
ATOM   3346  C CG    . LEU A 1 451  ? -38.307 49.988  73.332  1.00 16.16 ?  449  LEU A CG    1 
ATOM   3347  C CD1   . LEU A 1 451  ? -38.780 51.445  73.258  1.00 17.41 ?  449  LEU A CD1   1 
ATOM   3348  C CD2   . LEU A 1 451  ? -37.105 49.868  74.257  1.00 18.16 ?  449  LEU A CD2   1 
ATOM   3349  N N     . HIS A 1 452  ? -40.145 49.391  70.600  1.00 13.86 ?  450  HIS A N     1 
ATOM   3350  C CA    . HIS A 1 452  ? -39.565 49.172  69.279  1.00 15.63 ?  450  HIS A CA    1 
ATOM   3351  C C     . HIS A 1 452  ? -38.129 48.669  69.372  1.00 18.03 ?  450  HIS A C     1 
ATOM   3352  O O     . HIS A 1 452  ? -37.333 49.159  70.176  1.00 17.74 ?  450  HIS A O     1 
ATOM   3353  C CB    . HIS A 1 452  ? -39.593 50.473  68.470  1.00 16.61 ?  450  HIS A CB    1 
ATOM   3354  C CG    . HIS A 1 452  ? -38.808 50.388  67.198  1.00 14.10 ?  450  HIS A CG    1 
ATOM   3355  N ND1   . HIS A 1 452  ? -39.341 49.904  66.022  1.00 17.48 ?  450  HIS A ND1   1 
ATOM   3356  C CD2   . HIS A 1 452  ? -37.511 50.681  66.937  1.00 17.73 ?  450  HIS A CD2   1 
ATOM   3357  C CE1   . HIS A 1 452  ? -38.409 49.925  65.084  1.00 20.71 ?  450  HIS A CE1   1 
ATOM   3358  N NE2   . HIS A 1 452  ? -37.290 50.384  65.617  1.00 18.44 ?  450  HIS A NE2   1 
ATOM   3359  N N     . GLY A 1 453  ? -37.794 47.718  68.504  1.00 21.26 ?  451  GLY A N     1 
ATOM   3360  C CA    . GLY A 1 453  ? -36.431 47.214  68.465  1.00 21.98 ?  451  GLY A CA    1 
ATOM   3361  C C     . GLY A 1 453  ? -36.010 46.494  69.727  1.00 25.42 ?  451  GLY A C     1 
ATOM   3362  O O     . GLY A 1 453  ? -34.825 46.491  70.067  1.00 29.39 ?  451  GLY A O     1 
ATOM   3363  N N     . MET A 1 454  ? -36.955 45.882  70.432  1.00 20.18 ?  452  MET A N     1 
ATOM   3364  C CA    . MET A 1 454  ? -36.657 45.195  71.679  1.00 20.67 ?  452  MET A CA    1 
ATOM   3365  C C     . MET A 1 454  ? -37.707 44.130  71.961  1.00 20.71 ?  452  MET A C     1 
ATOM   3366  O O     . MET A 1 454  ? -37.367 42.977  72.239  1.00 22.13 ?  452  MET A O     1 
ATOM   3367  C CB    . MET A 1 454  ? -36.594 46.182  72.842  1.00 19.81 ?  452  MET A CB    1 
ATOM   3368  C CG    . MET A 1 454  ? -36.487 45.520  74.194  1.00 21.82 ?  452  MET A CG    1 
ATOM   3369  S SD    . MET A 1 454  ? -34.933 44.635  74.399  1.00 26.87 ?  452  MET A SD    1 
ATOM   3370  C CE    . MET A 1 454  ? -33.777 45.986  74.195  1.00 26.07 ?  452  MET A CE    1 
ATOM   3371  N N     . GLY A 1 455  ? -38.984 44.500  71.882  1.00 19.56 ?  453  GLY A N     1 
ATOM   3372  C CA    . GLY A 1 455  ? -40.043 43.571  72.215  1.00 18.75 ?  453  GLY A CA    1 
ATOM   3373  C C     . GLY A 1 455  ? -40.625 42.756  71.080  1.00 21.12 ?  453  GLY A C     1 
ATOM   3374  O O     . GLY A 1 455  ? -41.406 41.836  71.341  1.00 20.94 ?  453  GLY A O     1 
ATOM   3375  N N     . GLU A 1 456  ? -40.271 43.055  69.828  1.00 20.81 ?  454  GLU A N     1 
ATOM   3376  C CA    . GLU A 1 456  ? -40.865 42.325  68.709  1.00 23.49 ?  454  GLU A CA    1 
ATOM   3377  C C     . GLU A 1 456  ? -40.595 40.826  68.737  1.00 25.56 ?  454  GLU A C     1 
ATOM   3378  O O     . GLU A 1 456  ? -41.510 40.064  68.380  1.00 25.86 ?  454  GLU A O     1 
ATOM   3379  C CB    . GLU A 1 456  ? -40.390 42.908  67.373  1.00 25.39 ?  454  GLU A CB    1 
ATOM   3380  C CG    . GLU A 1 456  ? -40.852 44.326  67.123  1.00 26.64 ?  454  GLU A CG    1 
ATOM   3381  C CD    . GLU A 1 456  ? -39.822 45.341  67.553  1.00 28.21 ?  454  GLU A CD    1 
ATOM   3382  O OE1   . GLU A 1 456  ? -38.975 45.009  68.421  1.00 24.91 ?  454  GLU A OE1   1 
ATOM   3383  O OE2   . GLU A 1 456  ? -39.850 46.466  67.005  1.00 27.45 ?  454  GLU A OE2   1 
ATOM   3384  N N     . PRO A 1 457  ? -39.402 40.336  69.103  1.00 24.56 ?  455  PRO A N     1 
ATOM   3385  C CA    . PRO A 1 457  ? -39.221 38.875  69.147  1.00 27.77 ?  455  PRO A CA    1 
ATOM   3386  C C     . PRO A 1 457  ? -40.212 38.181  70.066  1.00 27.42 ?  455  PRO A C     1 
ATOM   3387  O O     . PRO A 1 457  ? -40.742 37.117  69.713  1.00 28.12 ?  455  PRO A O     1 
ATOM   3388  C CB    . PRO A 1 457  ? -37.770 38.722  69.623  1.00 23.40 ?  455  PRO A CB    1 
ATOM   3389  C CG    . PRO A 1 457  ? -37.095 39.970  69.146  1.00 24.82 ?  455  PRO A CG    1 
ATOM   3390  C CD    . PRO A 1 457  ? -38.126 41.047  69.315  1.00 22.08 ?  455  PRO A CD    1 
ATOM   3391  N N     . LEU A 1 458  ? -40.501 38.775  71.226  1.00 23.14 ?  456  LEU A N     1 
ATOM   3392  C CA    . LEU A 1 458  ? -41.489 38.195  72.126  1.00 21.28 ?  456  LEU A CA    1 
ATOM   3393  C C     . LEU A 1 458  ? -42.895 38.327  71.556  1.00 22.74 ?  456  LEU A C     1 
ATOM   3394  O O     . LEU A 1 458  ? -43.653 37.354  71.514  1.00 23.52 ?  456  LEU A O     1 
ATOM   3395  C CB    . LEU A 1 458  ? -41.399 38.863  73.497  1.00 22.44 ?  456  LEU A CB    1 
ATOM   3396  C CG    . LEU A 1 458  ? -42.488 38.485  74.504  1.00 20.50 ?  456  LEU A CG    1 
ATOM   3397  C CD1   . LEU A 1 458  ? -42.478 36.989  74.770  1.00 21.82 ?  456  LEU A CD1   1 
ATOM   3398  C CD2   . LEU A 1 458  ? -42.258 39.265  75.789  1.00 22.98 ?  456  LEU A CD2   1 
ATOM   3399  N N     . TYR A 1 459  ? -43.266 39.522  71.101  1.00 21.11 ?  457  TYR A N     1 
ATOM   3400  C CA    . TYR A 1 459  ? -44.668 39.714  70.759  1.00 20.55 ?  457  TYR A CA    1 
ATOM   3401  C C     . TYR A 1 459  ? -45.044 39.159  69.392  1.00 22.48 ?  457  TYR A C     1 
ATOM   3402  O O     . TYR A 1 459  ? -46.239 39.006  69.117  1.00 24.09 ?  457  TYR A O     1 
ATOM   3403  C CB    . TYR A 1 459  ? -45.026 41.194  70.911  1.00 22.12 ?  457  TYR A CB    1 
ATOM   3404  C CG    . TYR A 1 459  ? -45.250 41.488  72.374  1.00 17.90 ?  457  TYR A CG    1 
ATOM   3405  C CD1   . TYR A 1 459  ? -46.445 41.142  72.984  1.00 18.96 ?  457  TYR A CD1   1 
ATOM   3406  C CD2   . TYR A 1 459  ? -44.247 42.047  73.161  1.00 18.78 ?  457  TYR A CD2   1 
ATOM   3407  C CE1   . TYR A 1 459  ? -46.656 41.371  74.316  1.00 19.69 ?  457  TYR A CE1   1 
ATOM   3408  C CE2   . TYR A 1 459  ? -44.450 42.289  74.509  1.00 17.72 ?  457  TYR A CE2   1 
ATOM   3409  C CZ    . TYR A 1 459  ? -45.659 41.939  75.082  1.00 19.47 ?  457  TYR A CZ    1 
ATOM   3410  O OH    . TYR A 1 459  ? -45.856 42.171  76.427  1.00 20.52 ?  457  TYR A OH    1 
ATOM   3411  N N     . GLU A 1 460  ? -44.068 38.803  68.554  1.00 23.94 ?  458  GLU A N     1 
ATOM   3412  C CA    . GLU A 1 460  ? -44.379 38.004  67.374  1.00 25.36 ?  458  GLU A CA    1 
ATOM   3413  C C     . GLU A 1 460  ? -44.776 36.577  67.729  1.00 27.47 ?  458  GLU A C     1 
ATOM   3414  O O     . GLU A 1 460  ? -45.283 35.856  66.864  1.00 28.96 ?  458  GLU A O     1 
ATOM   3415  C CB    . GLU A 1 460  ? -43.191 38.003  66.416  1.00 27.89 ?  458  GLU A CB    1 
ATOM   3416  C CG    . GLU A 1 460  ? -43.066 39.326  65.679  1.00 33.31 ?  458  GLU A CG    1 
ATOM   3417  C CD    . GLU A 1 460  ? -41.964 39.327  64.648  1.00 42.94 ?  458  GLU A CD    1 
ATOM   3418  O OE1   . GLU A 1 460  ? -41.039 38.489  64.759  1.00 43.16 ?  458  GLU A OE1   1 
ATOM   3419  O OE2   . GLU A 1 460  ? -42.032 40.169  63.725  1.00 47.52 ?  458  GLU A OE2   1 
ATOM   3420  N N     . GLU A 1 461  ? -44.564 36.159  68.972  1.00 24.83 ?  459  GLU A N     1 
ATOM   3421  C CA    . GLU A 1 461  ? -45.121 34.915  69.488  1.00 28.64 ?  459  GLU A CA    1 
ATOM   3422  C C     . GLU A 1 461  ? -46.454 35.125  70.199  1.00 27.72 ?  459  GLU A C     1 
ATOM   3423  O O     . GLU A 1 461  ? -46.992 34.175  70.781  1.00 28.29 ?  459  GLU A O     1 
ATOM   3424  C CB    . GLU A 1 461  ? -44.117 34.251  70.433  1.00 26.46 ?  459  GLU A CB    1 
ATOM   3425  C CG    . GLU A 1 461  ? -42.729 34.092  69.845  1.00 30.11 ?  459  GLU A CG    1 
ATOM   3426  C CD    . GLU A 1 461  ? -42.701 33.136  68.661  1.00 32.81 ?  459  GLU A CD    1 
ATOM   3427  O OE1   . GLU A 1 461  ? -43.565 32.234  68.598  1.00 34.90 ?  459  GLU A OE1   1 
ATOM   3428  O OE2   . GLU A 1 461  ? -41.818 33.289  67.790  1.00 34.95 ?  459  GLU A OE2   1 
ATOM   3429  N N     . VAL A 1 462  ? -47.001 36.346  70.151  1.00 26.87 ?  460  VAL A N     1 
ATOM   3430  C CA    . VAL A 1 462  ? -48.222 36.716  70.857  1.00 24.46 ?  460  VAL A CA    1 
ATOM   3431  C C     . VAL A 1 462  ? -49.304 37.180  69.888  1.00 26.49 ?  460  VAL A C     1 
ATOM   3432  O O     . VAL A 1 462  ? -50.437 36.681  69.915  1.00 27.37 ?  460  VAL A O     1 
ATOM   3433  C CB    . VAL A 1 462  ? -47.944 37.805  71.922  1.00 23.77 ?  460  VAL A CB    1 
ATOM   3434  C CG1   . VAL A 1 462  ? -49.233 38.264  72.570  1.00 24.15 ?  460  VAL A CG1   1 
ATOM   3435  C CG2   . VAL A 1 462  ? -46.967 37.289  72.973  1.00 24.85 ?  460  VAL A CG2   1 
ATOM   3436  N N     . VAL A 1 463  ? -48.967 38.135  69.014  1.00 26.21 ?  461  VAL A N     1 
ATOM   3437  C CA    . VAL A 1 463  ? -49.937 38.726  68.099  1.00 24.44 ?  461  VAL A CA    1 
ATOM   3438  C C     . VAL A 1 463  ? -50.318 37.727  67.014  1.00 28.86 ?  461  VAL A C     1 
ATOM   3439  O O     . VAL A 1 463  ? -49.465 37.012  66.475  1.00 32.72 ?  461  VAL A O     1 
ATOM   3440  C CB    . VAL A 1 463  ? -49.356 40.013  67.489  1.00 25.14 ?  461  VAL A CB    1 
ATOM   3441  C CG1   . VAL A 1 463  ? -50.302 40.604  66.461  1.00 29.30 ?  461  VAL A CG1   1 
ATOM   3442  C CG2   . VAL A 1 463  ? -49.060 41.018  68.587  1.00 22.13 ?  461  VAL A CG2   1 
ATOM   3443  N N     . GLY A 1 464  ? -51.596 37.680  66.686  1.00 30.49 ?  462  GLY A N     1 
ATOM   3444  C CA    . GLY A 1 464  ? -52.034 36.901  65.547  1.00 31.76 ?  462  GLY A CA    1 
ATOM   3445  C C     . GLY A 1 464  ? -52.780 35.647  65.962  1.00 35.11 ?  462  GLY A C     1 
ATOM   3446  O O     . GLY A 1 464  ? -52.565 35.089  67.047  1.00 29.46 ?  462  GLY A O     1 
ATOM   3447  N N     . ARG A 1 465  ? -53.667 35.188  65.072  1.00 32.83 ?  463  ARG A N     1 
ATOM   3448  C CA    . ARG A 1 465  ? -54.508 34.034  65.376  1.00 34.43 ?  463  ARG A CA    1 
ATOM   3449  C C     . ARG A 1 465  ? -53.683 32.769  65.573  1.00 35.76 ?  463  ARG A C     1 
ATOM   3450  O O     . ARG A 1 465  ? -54.086 31.878  66.332  1.00 40.01 ?  463  ARG A O     1 
ATOM   3451  C CB    . ARG A 1 465  ? -55.543 33.836  64.265  1.00 33.08 ?  463  ARG A CB    1 
ATOM   3452  N N     . GLY A 1 466  ? -52.531 32.671  64.910  1.00 34.99 ?  464  GLY A N     1 
ATOM   3453  C CA    . GLY A 1 466  ? -51.656 31.529  65.070  1.00 33.54 ?  464  GLY A CA    1 
ATOM   3454  C C     . GLY A 1 466  ? -50.812 31.532  66.320  1.00 36.75 ?  464  GLY A C     1 
ATOM   3455  O O     . GLY A 1 466  ? -50.010 30.616  66.521  1.00 36.71 ?  464  GLY A O     1 
ATOM   3456  N N     . LYS A 1 467  ? -50.968 32.549  67.175  1.00 33.69 ?  465  LYS A N     1 
ATOM   3457  C CA    . LYS A 1 467  ? -50.186 32.663  68.401  1.00 31.16 ?  465  LYS A CA    1 
ATOM   3458  C C     . LYS A 1 467  ? -51.174 32.759  69.556  1.00 33.60 ?  465  LYS A C     1 
ATOM   3459  O O     . LYS A 1 467  ? -52.033 31.892  69.687  1.00 34.97 ?  465  LYS A O     1 
ATOM   3460  C CB    . LYS A 1 467  ? -49.210 33.825  68.316  1.00 28.30 ?  465  LYS A CB    1 
ATOM   3461  C CG    . LYS A 1 467  ? -48.198 33.707  67.192  1.00 30.30 ?  465  LYS A CG    1 
ATOM   3462  C CD    . LYS A 1 467  ? -47.284 32.505  67.408  1.00 30.27 ?  465  LYS A CD    1 
ATOM   3463  C CE    . LYS A 1 467  ? -46.159 32.487  66.392  1.00 34.69 ?  465  LYS A CE    1 
ATOM   3464  N NZ    . LYS A 1 467  ? -45.250 31.329  66.596  1.00 35.36 ?  465  LYS A NZ    1 
ATOM   3465  N N     . LEU A 1 468  ? -51.082 33.796  70.390  1.00 27.42 ?  466  LEU A N     1 
ATOM   3466  C CA    . LEU A 1 468  ? -52.024 33.999  71.480  1.00 28.23 ?  466  LEU A CA    1 
ATOM   3467  C C     . LEU A 1 468  ? -53.201 34.885  71.092  1.00 27.47 ?  466  LEU A C     1 
ATOM   3468  O O     . LEU A 1 468  ? -54.143 35.014  71.881  1.00 27.65 ?  466  LEU A O     1 
ATOM   3469  C CB    . LEU A 1 468  ? -51.305 34.599  72.695  1.00 28.63 ?  466  LEU A CB    1 
ATOM   3470  C CG    . LEU A 1 468  ? -50.152 33.765  73.262  1.00 27.30 ?  466  LEU A CG    1 
ATOM   3471  C CD1   . LEU A 1 468  ? -49.598 34.367  74.543  1.00 28.71 ?  466  LEU A CD1   1 
ATOM   3472  C CD2   . LEU A 1 468  ? -50.596 32.325  73.487  1.00 32.85 ?  466  LEU A CD2   1 
ATOM   3473  N N     . ASP A 1 469  ? -53.158 35.503  69.908  1.00 27.67 ?  467  ASP A N     1 
ATOM   3474  C CA    . ASP A 1 469  ? -54.247 36.335  69.397  1.00 28.58 ?  467  ASP A CA    1 
ATOM   3475  C C     . ASP A 1 469  ? -54.575 37.478  70.355  1.00 27.33 ?  467  ASP A C     1 
ATOM   3476  O O     . ASP A 1 469  ? -55.740 37.769  70.631  1.00 26.48 ?  467  ASP A O     1 
ATOM   3477  C CB    . ASP A 1 469  ? -55.495 35.499  69.099  1.00 28.54 ?  467  ASP A CB    1 
ATOM   3478  C CG    . ASP A 1 469  ? -56.462 36.215  68.186  1.00 34.13 ?  467  ASP A CG    1 
ATOM   3479  O OD1   . ASP A 1 469  ? -56.008 37.076  67.400  1.00 36.22 ?  467  ASP A OD1   1 
ATOM   3480  O OD2   . ASP A 1 469  ? -57.677 35.931  68.267  1.00 35.15 ?  467  ASP A OD2   1 
ATOM   3481  N N     . ARG A 1 470  ? -53.528 38.119  70.878  1.00 25.59 ?  468  ARG A N     1 
ATOM   3482  C CA    . ARG A 1 470  ? -53.646 39.337  71.656  1.00 24.82 ?  468  ARG A CA    1 
ATOM   3483  C C     . ARG A 1 470  ? -52.825 40.444  71.006  1.00 21.72 ?  468  ARG A C     1 
ATOM   3484  O O     . ARG A 1 470  ? -51.707 40.194  70.538  1.00 23.97 ?  468  ARG A O     1 
ATOM   3485  C CB    . ARG A 1 470  ? -53.174 39.128  73.101  1.00 23.19 ?  468  ARG A CB    1 
ATOM   3486  C CG    . ARG A 1 470  ? -53.931 38.042  73.851  1.00 24.76 ?  468  ARG A CG    1 
ATOM   3487  C CD    . ARG A 1 470  ? -55.383 38.434  74.065  1.00 26.94 ?  468  ARG A CD    1 
ATOM   3488  N NE    . ARG A 1 470  ? -56.131 37.363  74.716  1.00 29.87 ?  468  ARG A NE    1 
ATOM   3489  C CZ    . ARG A 1 470  ? -56.852 36.453  74.074  1.00 31.22 ?  468  ARG A CZ    1 
ATOM   3490  N NH1   . ARG A 1 470  ? -56.961 36.462  72.755  1.00 28.08 ?  468  ARG A NH1   1 
ATOM   3491  N NH2   . ARG A 1 470  ? -57.484 35.516  74.774  1.00 30.92 ?  468  ARG A NH2   1 
ATOM   3492  N N     . PRO A 1 471  ? -53.346 41.664  70.956  1.00 20.65 ?  469  PRO A N     1 
ATOM   3493  C CA    . PRO A 1 471  ? -52.643 42.753  70.274  1.00 19.21 ?  469  PRO A CA    1 
ATOM   3494  C C     . PRO A 1 471  ? -51.533 43.343  71.124  1.00 21.41 ?  469  PRO A C     1 
ATOM   3495  O O     . PRO A 1 471  ? -51.511 43.238  72.350  1.00 19.49 ?  469  PRO A O     1 
ATOM   3496  C CB    . PRO A 1 471  ? -53.747 43.790  70.044  1.00 22.58 ?  469  PRO A CB    1 
ATOM   3497  C CG    . PRO A 1 471  ? -54.681 43.562  71.182  1.00 22.52 ?  469  PRO A CG    1 
ATOM   3498  C CD    . PRO A 1 471  ? -54.702 42.062  71.368  1.00 22.89 ?  469  PRO A CD    1 
ATOM   3499  N N     . CYS A 1 472  ? -50.613 44.005  70.435  1.00 18.52 ?  470  CYS A N     1 
ATOM   3500  C CA    . CYS A 1 472  ? -49.484 44.651  71.083  1.00 17.30 ?  470  CYS A CA    1 
ATOM   3501  C C     . CYS A 1 472  ? -49.264 45.995  70.420  1.00 17.76 ?  470  CYS A C     1 
ATOM   3502  O O     . CYS A 1 472  ? -49.172 46.067  69.191  1.00 18.75 ?  470  CYS A O     1 
ATOM   3503  C CB    . CYS A 1 472  ? -48.222 43.795  70.970  1.00 18.50 ?  470  CYS A CB    1 
ATOM   3504  S SG    . CYS A 1 472  ? -46.804 44.529  71.791  1.00 19.83 ?  470  CYS A SG    1 
ATOM   3505  N N     . ARG A 1 473  ? -49.166 47.043  71.227  1.00 16.72 ?  471  ARG A N     1 
ATOM   3506  C CA    . ARG A 1 473  ? -48.821 48.373  70.746  1.00 16.02 ?  471  ARG A CA    1 
ATOM   3507  C C     . ARG A 1 473  ? -47.329 48.612  70.943  1.00 15.71 ?  471  ARG A C     1 
ATOM   3508  O O     . ARG A 1 473  ? -46.807 48.448  72.053  1.00 16.48 ?  471  ARG A O     1 
ATOM   3509  C CB    . ARG A 1 473  ? -49.631 49.449  71.472  1.00 15.50 ?  471  ARG A CB    1 
ATOM   3510  C CG    . ARG A 1 473  ? -49.452 50.836  70.860  1.00 15.28 ?  471  ARG A CG    1 
ATOM   3511  C CD    . ARG A 1 473  ? -50.370 51.867  71.491  1.00 14.98 ?  471  ARG A CD    1 
ATOM   3512  N NE    . ARG A 1 473  ? -51.738 51.366  71.509  1.00 14.82 ?  471  ARG A NE    1 
ATOM   3513  C CZ    . ARG A 1 473  ? -52.615 51.511  70.523  1.00 16.49 ?  471  ARG A CZ    1 
ATOM   3514  N NH1   . ARG A 1 473  ? -52.356 52.271  69.471  1.00 16.39 ?  471  ARG A NH1   1 
ATOM   3515  N NH2   . ARG A 1 473  ? -53.774 50.859  70.587  1.00 16.02 ?  471  ARG A NH2   1 
ATOM   3516  N N     . ILE A 1 474  ? -46.657 49.006  69.867  1.00 16.54 ?  472  ILE A N     1 
ATOM   3517  C CA    . ILE A 1 474  ? -45.222 49.261  69.872  1.00 15.38 ?  472  ILE A CA    1 
ATOM   3518  C C     . ILE A 1 474  ? -44.974 50.723  70.211  1.00 15.42 ?  472  ILE A C     1 
ATOM   3519  O O     . ILE A 1 474  ? -45.432 51.629  69.501  1.00 14.86 ?  472  ILE A O     1 
ATOM   3520  C CB    . ILE A 1 474  ? -44.590 48.899  68.523  1.00 16.63 ?  472  ILE A CB    1 
ATOM   3521  C CG1   . ILE A 1 474  ? -44.753 47.405  68.244  1.00 19.81 ?  472  ILE A CG1   1 
ATOM   3522  C CG2   . ILE A 1 474  ? -43.108 49.273  68.522  1.00 15.78 ?  472  ILE A CG2   1 
ATOM   3523  C CD1   . ILE A 1 474  ? -44.388 47.023  66.818  1.00 21.25 ?  472  ILE A CD1   1 
ATOM   3524  N N     . TYR A 1 475  ? -44.228 50.948  71.287  1.00 14.16 ?  473  TYR A N     1 
ATOM   3525  C CA    . TYR A 1 475  ? -43.766 52.269  71.698  1.00 14.19 ?  473  TYR A CA    1 
ATOM   3526  C C     . TYR A 1 475  ? -42.547 52.617  70.855  1.00 14.85 ?  473  TYR A C     1 
ATOM   3527  O O     . TYR A 1 475  ? -41.493 51.979  70.986  1.00 15.53 ?  473  TYR A O     1 
ATOM   3528  C CB    . TYR A 1 475  ? -43.451 52.214  73.189  1.00 15.50 ?  473  TYR A CB    1 
ATOM   3529  C CG    . TYR A 1 475  ? -43.115 53.472  73.962  1.00 16.47 ?  473  TYR A CG    1 
ATOM   3530  C CD1   . TYR A 1 475  ? -44.051 54.480  74.179  1.00 16.72 ?  473  TYR A CD1   1 
ATOM   3531  C CD2   . TYR A 1 475  ? -41.885 53.586  74.588  1.00 24.51 ?  473  TYR A CD2   1 
ATOM   3532  C CE1   . TYR A 1 475  ? -43.730 55.609  74.944  1.00 16.13 ?  473  TYR A CE1   1 
ATOM   3533  C CE2   . TYR A 1 475  ? -41.564 54.691  75.347  1.00 27.38 ?  473  TYR A CE2   1 
ATOM   3534  C CZ    . TYR A 1 475  ? -42.488 55.692  75.528  1.00 22.76 ?  473  TYR A CZ    1 
ATOM   3535  O OH    . TYR A 1 475  ? -42.139 56.792  76.284  1.00 26.39 ?  473  TYR A OH    1 
ATOM   3536  N N     . ALA A 1 476  ? -42.701 53.603  69.973  1.00 13.02 ?  474  ALA A N     1 
ATOM   3537  C CA    . ALA A 1 476  ? -41.794 53.818  68.846  1.00 13.45 ?  474  ALA A CA    1 
ATOM   3538  C C     . ALA A 1 476  ? -41.074 55.144  69.006  1.00 13.47 ?  474  ALA A C     1 
ATOM   3539  O O     . ALA A 1 476  ? -41.662 56.209  68.750  1.00 13.65 ?  474  ALA A O     1 
ATOM   3540  C CB    . ALA A 1 476  ? -42.568 53.779  67.524  1.00 16.38 ?  474  ALA A CB    1 
ATOM   3541  N N     . PRO A 1 477  ? -39.810 55.140  69.437  1.00 14.41 ?  475  PRO A N     1 
ATOM   3542  C CA    . PRO A 1 477  ? -39.075 56.401  69.541  1.00 12.75 ?  475  PRO A CA    1 
ATOM   3543  C C     . PRO A 1 477  ? -38.845 56.999  68.163  1.00 14.33 ?  475  PRO A C     1 
ATOM   3544  O O     . PRO A 1 477  ? -38.657 56.287  67.174  1.00 15.10 ?  475  PRO A O     1 
ATOM   3545  C CB    . PRO A 1 477  ? -37.749 55.993  70.202  1.00 14.31 ?  475  PRO A CB    1 
ATOM   3546  C CG    . PRO A 1 477  ? -37.999 54.601  70.774  1.00 16.51 ?  475  PRO A CG    1 
ATOM   3547  C CD    . PRO A 1 477  ? -38.983 53.984  69.827  1.00 15.10 ?  475  PRO A CD    1 
ATOM   3548  N N     . VAL A 1 478  ? -38.866 58.326  68.103  1.00 12.95 ?  476  VAL A N     1 
ATOM   3549  C CA    . VAL A 1 478  ? -38.721 59.063  66.857  1.00 13.76 ?  476  VAL A CA    1 
ATOM   3550  C C     . VAL A 1 478  ? -37.794 60.238  67.137  1.00 13.61 ?  476  VAL A C     1 
ATOM   3551  O O     . VAL A 1 478  ? -38.063 61.032  68.045  1.00 16.18 ?  476  VAL A O     1 
ATOM   3552  C CB    . VAL A 1 478  ? -40.076 59.579  66.346  1.00 15.15 ?  476  VAL A CB    1 
ATOM   3553  C CG1   . VAL A 1 478  ? -39.865 60.362  65.034  1.00 16.21 ?  476  VAL A CG1   1 
ATOM   3554  C CG2   . VAL A 1 478  ? -41.055 58.418  66.167  1.00 15.86 ?  476  VAL A CG2   1 
ATOM   3555  N N     . GLY A 1 479  ? -36.710 60.357  66.375  1.00 16.04 ?  477  GLY A N     1 
ATOM   3556  C CA    . GLY A 1 479  ? -35.826 61.483  66.610  1.00 16.49 ?  477  GLY A CA    1 
ATOM   3557  C C     . GLY A 1 479  ? -34.483 61.326  65.940  1.00 17.40 ?  477  GLY A C     1 
ATOM   3558  O O     . GLY A 1 479  ? -34.108 60.246  65.460  1.00 17.23 ?  477  GLY A O     1 
ATOM   3559  N N     . THR A 1 480  ? -33.766 62.445  65.911  1.00 18.59 ?  478  THR A N     1 
ATOM   3560  C CA    . THR A 1 480  ? -32.431 62.516  65.353  1.00 16.82 ?  478  THR A CA    1 
ATOM   3561  C C     . THR A 1 480  ? -31.429 61.832  66.275  1.00 20.13 ?  478  THR A C     1 
ATOM   3562  O O     . THR A 1 480  ? -31.727 61.490  67.418  1.00 19.06 ?  478  THR A O     1 
ATOM   3563  C CB    . THR A 1 480  ? -32.008 63.969  65.174  1.00 20.26 ?  478  THR A CB    1 
ATOM   3564  O OG1   . THR A 1 480  ? -32.019 64.607  66.462  1.00 22.02 ?  478  THR A OG1   1 
ATOM   3565  C CG2   . THR A 1 480  ? -32.947 64.700  64.228  1.00 24.58 ?  478  THR A CG2   1 
ATOM   3566  N N     . HIS A 1 481  ? -30.201 61.682  65.770  1.00 21.54 ?  479  HIS A N     1 
ATOM   3567  C CA    . HIS A 1 481  ? -29.131 61.109  66.585  1.00 20.92 ?  479  HIS A CA    1 
ATOM   3568  C C     . HIS A 1 481  ? -28.964 61.863  67.899  1.00 25.70 ?  479  HIS A C     1 
ATOM   3569  O O     . HIS A 1 481  ? -28.852 61.252  68.971  1.00 22.90 ?  479  HIS A O     1 
ATOM   3570  C CB    . HIS A 1 481  ? -27.816 61.119  65.805  1.00 21.66 ?  479  HIS A CB    1 
ATOM   3571  C CG    . HIS A 1 481  ? -27.807 60.210  64.623  1.00 24.30 ?  479  HIS A CG    1 
ATOM   3572  N ND1   . HIS A 1 481  ? -26.673 59.985  63.872  1.00 23.94 ?  479  HIS A ND1   1 
ATOM   3573  C CD2   . HIS A 1 481  ? -28.787 59.464  64.059  1.00 23.62 ?  479  HIS A CD2   1 
ATOM   3574  C CE1   . HIS A 1 481  ? -26.953 59.137  62.900  1.00 27.14 ?  479  HIS A CE1   1 
ATOM   3575  N NE2   . HIS A 1 481  ? -28.229 58.805  62.990  1.00 24.78 ?  479  HIS A NE2   1 
ATOM   3576  N N     . GLU A 1 482  ? -28.950 63.197  67.835  1.00 26.42 ?  480  GLU A N     1 
ATOM   3577  C CA    . GLU A 1 482  ? -28.749 63.997  69.039  1.00 26.40 ?  480  GLU A CA    1 
ATOM   3578  C C     . GLU A 1 482  ? -29.839 63.726  70.065  1.00 26.94 ?  480  GLU A C     1 
ATOM   3579  O O     . GLU A 1 482  ? -29.563 63.565  71.259  1.00 26.64 ?  480  GLU A O     1 
ATOM   3580  C CB    . GLU A 1 482  ? -28.714 65.486  68.690  1.00 28.18 ?  480  GLU A CB    1 
ATOM   3581  C CG    . GLU A 1 482  ? -28.477 66.372  69.910  1.00 28.12 ?  480  GLU A CG    1 
ATOM   3582  C CD    . GLU A 1 482  ? -28.725 67.849  69.640  1.00 48.15 ?  480  GLU A CD    1 
ATOM   3583  O OE1   . GLU A 1 482  ? -28.770 68.251  68.456  1.00 52.18 ?  480  GLU A OE1   1 
ATOM   3584  O OE2   . GLU A 1 482  ? -28.879 68.610  70.621  1.00 50.93 ?  480  GLU A OE2   1 
ATOM   3585  N N     . THR A 1 483  ? -31.089 63.676  69.610  1.00 22.88 ?  481  THR A N     1 
ATOM   3586  C CA    . THR A 1 483  ? -32.206 63.490  70.521  1.00 22.99 ?  481  THR A CA    1 
ATOM   3587  C C     . THR A 1 483  ? -32.199 62.093  71.121  1.00 24.08 ?  481  THR A C     1 
ATOM   3588  O O     . THR A 1 483  ? -32.501 61.919  72.304  1.00 23.12 ?  481  THR A O     1 
ATOM   3589  C CB    . THR A 1 483  ? -33.516 63.748  69.778  1.00 24.88 ?  481  THR A CB    1 
ATOM   3590  O OG1   . THR A 1 483  ? -33.500 65.078  69.245  1.00 26.76 ?  481  THR A OG1   1 
ATOM   3591  C CG2   . THR A 1 483  ? -34.694 63.605  70.708  1.00 28.26 ?  481  THR A CG2   1 
ATOM   3592  N N     . LEU A 1 484  ? -31.872 61.078  70.322  1.00 20.15 ?  482  LEU A N     1 
ATOM   3593  C CA    . LEU A 1 484  ? -31.938 59.726  70.858  1.00 22.05 ?  482  LEU A CA    1 
ATOM   3594  C C     . LEU A 1 484  ? -30.775 59.438  71.796  1.00 22.15 ?  482  LEU A C     1 
ATOM   3595  O O     . LEU A 1 484  ? -30.922 58.640  72.727  1.00 24.41 ?  482  LEU A O     1 
ATOM   3596  C CB    . LEU A 1 484  ? -32.004 58.705  69.720  1.00 22.37 ?  482  LEU A CB    1 
ATOM   3597  C CG    . LEU A 1 484  ? -30.757 58.393  68.891  1.00 22.47 ?  482  LEU A CG    1 
ATOM   3598  C CD1   . LEU A 1 484  ? -29.997 57.224  69.498  1.00 23.04 ?  482  LEU A CD1   1 
ATOM   3599  C CD2   . LEU A 1 484  ? -31.131 58.087  67.448  1.00 25.26 ?  482  LEU A CD2   1 
ATOM   3600  N N     . LEU A 1 485  ? -29.623 60.079  71.589  1.00 21.65 ?  483  LEU A N     1 
ATOM   3601  C CA    . LEU A 1 485  ? -28.477 59.798  72.452  1.00 20.02 ?  483  LEU A CA    1 
ATOM   3602  C C     . LEU A 1 485  ? -28.609 60.426  73.837  1.00 20.62 ?  483  LEU A C     1 
ATOM   3603  O O     . LEU A 1 485  ? -27.946 59.963  74.770  1.00 22.65 ?  483  LEU A O     1 
ATOM   3604  C CB    . LEU A 1 485  ? -27.186 60.276  71.781  1.00 21.82 ?  483  LEU A CB    1 
ATOM   3605  C CG    . LEU A 1 485  ? -26.703 59.437  70.594  1.00 22.38 ?  483  LEU A CG    1 
ATOM   3606  C CD1   . LEU A 1 485  ? -25.623 60.184  69.828  1.00 26.66 ?  483  LEU A CD1   1 
ATOM   3607  C CD2   . LEU A 1 485  ? -26.213 58.073  71.029  1.00 23.48 ?  483  LEU A CD2   1 
ATOM   3608  N N     . ALA A 1 486  ? -29.475 61.431  74.000  1.00 20.75 ?  484  ALA A N     1 
ATOM   3609  C CA    . ALA A 1 486  ? -29.523 62.193  75.246  1.00 23.66 ?  484  ALA A CA    1 
ATOM   3610  C C     . ALA A 1 486  ? -29.799 61.301  76.454  1.00 24.27 ?  484  ALA A C     1 
ATOM   3611  O O     . ALA A 1 486  ? -29.108 61.398  77.477  1.00 26.17 ?  484  ALA A O     1 
ATOM   3612  C CB    . ALA A 1 486  ? -30.577 63.297  75.140  1.00 23.71 ?  484  ALA A CB    1 
ATOM   3613  N N     . TYR A 1 487  ? -30.807 60.424  76.364  1.00 24.21 ?  485  TYR A N     1 
ATOM   3614  C CA    . TYR A 1 487  ? -31.170 59.566  77.491  1.00 22.38 ?  485  TYR A CA    1 
ATOM   3615  C C     . TYR A 1 487  ? -31.211 58.094  77.084  1.00 23.20 ?  485  TYR A C     1 
ATOM   3616  O O     . TYR A 1 487  ? -31.979 57.304  77.645  1.00 24.24 ?  485  TYR A O     1 
ATOM   3617  C CB    . TYR A 1 487  ? -32.500 60.011  78.111  1.00 23.65 ?  485  TYR A CB    1 
ATOM   3618  C CG    . TYR A 1 487  ? -32.469 61.459  78.552  1.00 26.21 ?  485  TYR A CG    1 
ATOM   3619  C CD1   . TYR A 1 487  ? -31.944 61.818  79.798  1.00 25.16 ?  485  TYR A CD1   1 
ATOM   3620  C CD2   . TYR A 1 487  ? -32.931 62.472  77.718  1.00 24.28 ?  485  TYR A CD2   1 
ATOM   3621  C CE1   . TYR A 1 487  ? -31.889 63.149  80.195  1.00 28.79 ?  485  TYR A CE1   1 
ATOM   3622  C CE2   . TYR A 1 487  ? -32.879 63.800  78.108  1.00 30.47 ?  485  TYR A CE2   1 
ATOM   3623  C CZ    . TYR A 1 487  ? -32.363 64.135  79.346  1.00 32.47 ?  485  TYR A CZ    1 
ATOM   3624  O OH    . TYR A 1 487  ? -32.319 65.461  79.732  1.00 35.68 ?  485  TYR A OH    1 
ATOM   3625  N N     . LEU A 1 488  ? -30.363 57.700  76.125  1.00 21.20 ?  486  LEU A N     1 
ATOM   3626  C CA    . LEU A 1 488  ? -30.333 56.306  75.691  1.00 21.09 ?  486  LEU A CA    1 
ATOM   3627  C C     . LEU A 1 488  ? -29.806 55.376  76.783  1.00 18.93 ?  486  LEU A C     1 
ATOM   3628  O O     . LEU A 1 488  ? -30.186 54.198  76.829  1.00 20.48 ?  486  LEU A O     1 
ATOM   3629  C CB    . LEU A 1 488  ? -29.492 56.167  74.417  1.00 21.27 ?  486  LEU A CB    1 
ATOM   3630  C CG    . LEU A 1 488  ? -29.481 54.773  73.772  1.00 24.17 ?  486  LEU A CG    1 
ATOM   3631  C CD1   . LEU A 1 488  ? -30.899 54.288  73.510  1.00 26.80 ?  486  LEU A CD1   1 
ATOM   3632  C CD2   . LEU A 1 488  ? -28.690 54.754  72.477  1.00 20.31 ?  486  LEU A CD2   1 
ATOM   3633  N N     . VAL A 1 489  ? -28.936 55.876  77.666  1.00 21.35 ?  487  VAL A N     1 
ATOM   3634  C CA    . VAL A 1 489  ? -28.422 55.033  78.743  1.00 19.28 ?  487  VAL A CA    1 
ATOM   3635  C C     . VAL A 1 489  ? -29.562 54.549  79.631  1.00 18.72 ?  487  VAL A C     1 
ATOM   3636  O O     . VAL A 1 489  ? -29.649 53.362  79.964  1.00 19.71 ?  487  VAL A O     1 
ATOM   3637  C CB    . VAL A 1 489  ? -27.344 55.779  79.549  1.00 17.28 ?  487  VAL A CB    1 
ATOM   3638  C CG1   . VAL A 1 489  ? -27.105 55.075  80.871  1.00 18.49 ?  487  VAL A CG1   1 
ATOM   3639  C CG2   . VAL A 1 489  ? -26.036 55.829  78.749  1.00 19.08 ?  487  VAL A CG2   1 
ATOM   3640  N N     . ARG A 1 490  ? -30.456 55.461  80.034  1.00 20.38 ?  488  ARG A N     1 
ATOM   3641  C CA    . ARG A 1 490  ? -31.597 55.053  80.854  1.00 19.23 ?  488  ARG A CA    1 
ATOM   3642  C C     . ARG A 1 490  ? -32.435 53.989  80.151  1.00 19.28 ?  488  ARG A C     1 
ATOM   3643  O O     . ARG A 1 490  ? -32.890 53.024  80.783  1.00 20.94 ?  488  ARG A O     1 
ATOM   3644  C CB    . ARG A 1 490  ? -32.460 56.270  81.199  1.00 21.54 ?  488  ARG A CB    1 
ATOM   3645  C CG    . ARG A 1 490  ? -33.643 55.937  82.115  1.00 22.32 ?  488  ARG A CG    1 
ATOM   3646  C CD    . ARG A 1 490  ? -34.527 57.163  82.389  1.00 26.22 ?  488  ARG A CD    1 
ATOM   3647  N NE    . ARG A 1 490  ? -35.274 57.559  81.198  1.00 25.82 ?  488  ARG A NE    1 
ATOM   3648  C CZ    . ARG A 1 490  ? -35.385 58.803  80.749  1.00 24.49 ?  488  ARG A CZ    1 
ATOM   3649  N NH1   . ARG A 1 490  ? -34.821 59.821  81.378  1.00 24.89 ?  488  ARG A NH1   1 
ATOM   3650  N NH2   . ARG A 1 490  ? -36.089 59.031  79.642  1.00 25.36 ?  488  ARG A NH2   1 
ATOM   3651  N N     . ARG A 1 491  ? -32.628 54.134  78.838  1.00 20.49 ?  489  ARG A N     1 
ATOM   3652  C CA    . ARG A 1 491  ? -33.428 53.166  78.094  1.00 21.71 ?  489  ARG A CA    1 
ATOM   3653  C C     . ARG A 1 491  ? -32.730 51.818  78.009  1.00 24.95 ?  489  ARG A C     1 
ATOM   3654  O O     . ARG A 1 491  ? -33.382 50.771  78.088  1.00 24.41 ?  489  ARG A O     1 
ATOM   3655  C CB    . ARG A 1 491  ? -33.719 53.687  76.691  1.00 26.14 ?  489  ARG A CB    1 
ATOM   3656  C CG    . ARG A 1 491  ? -34.515 52.695  75.853  1.00 30.30 ?  489  ARG A CG    1 
ATOM   3657  C CD    . ARG A 1 491  ? -35.975 53.089  75.826  1.00 30.14 ?  489  ARG A CD    1 
ATOM   3658  N NE    . ARG A 1 491  ? -36.157 54.219  74.927  1.00 36.59 ?  489  ARG A NE    1 
ATOM   3659  C CZ    . ARG A 1 491  ? -37.265 54.938  74.822  1.00 32.24 ?  489  ARG A CZ    1 
ATOM   3660  N NH1   . ARG A 1 491  ? -38.322 54.700  75.585  1.00 35.12 ?  489  ARG A NH1   1 
ATOM   3661  N NH2   . ARG A 1 491  ? -37.311 55.922  73.931  1.00 25.43 ?  489  ARG A NH2   1 
ATOM   3662  N N     . LEU A 1 492  ? -31.405 51.822  77.844  1.00 21.40 ?  490  LEU A N     1 
ATOM   3663  C CA    . LEU A 1 492  ? -30.684 50.555  77.766  1.00 21.85 ?  490  LEU A CA    1 
ATOM   3664  C C     . LEU A 1 492  ? -30.754 49.805  79.091  1.00 25.21 ?  490  LEU A C     1 
ATOM   3665  O O     . LEU A 1 492  ? -30.876 48.573  79.114  1.00 23.89 ?  490  LEU A O     1 
ATOM   3666  C CB    . LEU A 1 492  ? -29.232 50.799  77.345  1.00 22.39 ?  490  LEU A CB    1 
ATOM   3667  C CG    . LEU A 1 492  ? -29.096 51.288  75.900  1.00 22.09 ?  490  LEU A CG    1 
ATOM   3668  C CD1   . LEU A 1 492  ? -27.668 51.793  75.597  1.00 25.68 ?  490  LEU A CD1   1 
ATOM   3669  C CD2   . LEU A 1 492  ? -29.502 50.198  74.920  1.00 25.51 ?  490  LEU A CD2   1 
ATOM   3670  N N     . LEU A 1 493  ? -30.702 50.531  80.206  1.00 21.42 ?  491  LEU A N     1 
ATOM   3671  C CA    . LEU A 1 493  ? -30.729 49.883  81.510  1.00 23.12 ?  491  LEU A CA    1 
ATOM   3672  C C     . LEU A 1 493  ? -32.081 49.253  81.823  1.00 22.55 ?  491  LEU A C     1 
ATOM   3673  O O     . LEU A 1 493  ? -32.144 48.358  82.676  1.00 23.74 ?  491  LEU A O     1 
ATOM   3674  C CB    . LEU A 1 493  ? -30.356 50.891  82.597  1.00 20.81 ?  491  LEU A CB    1 
ATOM   3675  C CG    . LEU A 1 493  ? -28.893 50.905  83.044  1.00 26.13 ?  491  LEU A CG    1 
ATOM   3676  C CD1   . LEU A 1 493  ? -27.978 50.908  81.844  1.00 27.76 ?  491  LEU A CD1   1 
ATOM   3677  C CD2   . LEU A 1 493  ? -28.617 52.107  83.937  1.00 25.90 ?  491  LEU A CD2   1 
ATOM   3678  N N     . GLU A 1 494  ? -33.155 49.685  81.144  1.00 21.94 ?  492  GLU A N     1 
ATOM   3679  C CA    . GLU A 1 494  ? -34.469 49.087  81.377  1.00 23.07 ?  492  GLU A CA    1 
ATOM   3680  C C     . GLU A 1 494  ? -34.422 47.585  81.151  1.00 23.91 ?  492  GLU A C     1 
ATOM   3681  O O     . GLU A 1 494  ? -34.950 46.805  81.955  1.00 25.08 ?  492  GLU A O     1 
ATOM   3682  C CB    . GLU A 1 494  ? -35.523 49.714  80.458  1.00 22.31 ?  492  GLU A CB    1 
ATOM   3683  C CG    . GLU A 1 494  ? -35.883 51.183  80.754  1.00 22.11 ?  492  GLU A CG    1 
ATOM   3684  C CD    . GLU A 1 494  ? -36.741 51.798  79.657  1.00 24.90 ?  492  GLU A CD    1 
ATOM   3685  O OE1   . GLU A 1 494  ? -37.297 51.036  78.833  1.00 28.44 ?  492  GLU A OE1   1 
ATOM   3686  O OE2   . GLU A 1 494  ? -36.865 53.042  79.607  1.00 31.29 ?  492  GLU A OE2   1 
ATOM   3687  N N     . ASN A 1 495  ? -33.767 47.160  80.073  1.00 22.06 ?  493  ASN A N     1 
ATOM   3688  C CA    . ASN A 1 495  ? -33.725 45.760  79.689  1.00 20.13 ?  493  ASN A CA    1 
ATOM   3689  C C     . ASN A 1 495  ? -32.323 45.170  79.782  1.00 23.72 ?  493  ASN A C     1 
ATOM   3690  O O     . ASN A 1 495  ? -32.131 44.013  79.394  1.00 25.28 ?  493  ASN A O     1 
ATOM   3691  C CB    . ASN A 1 495  ? -34.291 45.603  78.273  1.00 23.29 ?  493  ASN A CB    1 
ATOM   3692  C CG    . ASN A 1 495  ? -35.735 46.104  78.165  1.00 21.55 ?  493  ASN A CG    1 
ATOM   3693  O OD1   . ASN A 1 495  ? -36.664 45.486  78.709  1.00 22.27 ?  493  ASN A OD1   1 
ATOM   3694  N ND2   . ASN A 1 495  ? -35.929 47.229  77.466  1.00 19.96 ?  493  ASN A ND2   1 
ATOM   3695  N N     . GLY A 1 496  ? -31.356 45.918  80.321  1.00 24.93 ?  494  GLY A N     1 
ATOM   3696  C CA    . GLY A 1 496  ? -29.967 45.480  80.316  1.00 26.92 ?  494  GLY A CA    1 
ATOM   3697  C C     . GLY A 1 496  ? -29.296 45.283  81.665  1.00 28.55 ?  494  GLY A C     1 
ATOM   3698  O O     . GLY A 1 496  ? -28.094 45.003  81.718  1.00 28.74 ?  494  GLY A O     1 
ATOM   3699  N N     . ALA A 1 497  ? -30.042 45.418  82.762  1.00 26.54 ?  495  ALA A N     1 
ATOM   3700  C CA    . ALA A 1 497  ? -29.467 45.160  84.076  1.00 26.96 ?  495  ALA A CA    1 
ATOM   3701  C C     . ALA A 1 497  ? -29.477 43.660  84.382  1.00 27.48 ?  495  ALA A C     1 
ATOM   3702  O O     . ALA A 1 497  ? -30.157 42.865  83.724  1.00 24.60 ?  495  ALA A O     1 
ATOM   3703  C CB    . ALA A 1 497  ? -30.221 45.937  85.156  1.00 25.57 ?  495  ALA A CB    1 
ATOM   3704  N N     . ASN A 1 498  ? -28.728 43.277  85.424  1.00 29.62 ?  496  ASN A N     1 
ATOM   3705  C CA    . ASN A 1 498  ? -28.597 41.860  85.768  1.00 28.97 ?  496  ASN A CA    1 
ATOM   3706  C C     . ASN A 1 498  ? -29.948 41.216  86.047  1.00 30.04 ?  496  ASN A C     1 
ATOM   3707  O O     . ASN A 1 498  ? -30.154 40.033  85.748  1.00 27.79 ?  496  ASN A O     1 
ATOM   3708  C CB    . ASN A 1 498  ? -27.689 41.688  86.984  1.00 30.35 ?  496  ASN A CB    1 
ATOM   3709  C CG    . ASN A 1 498  ? -26.218 41.712  86.625  1.00 40.50 ?  496  ASN A CG    1 
ATOM   3710  O OD1   . ASN A 1 498  ? -25.851 41.633  85.450  1.00 42.47 ?  496  ASN A OD1   1 
ATOM   3711  N ND2   . ASN A 1 498  ? -25.363 41.804  87.641  1.00 38.36 ?  496  ASN A ND2   1 
ATOM   3712  N N     . SER A 1 499  ? -30.871 41.967  86.644  1.00 25.03 ?  497  SER A N     1 
ATOM   3713  C CA    . SER A 1 499  ? -32.189 41.443  86.968  1.00 27.14 ?  497  SER A CA    1 
ATOM   3714  C C     . SER A 1 499  ? -33.184 41.559  85.818  1.00 22.55 ?  497  SER A C     1 
ATOM   3715  O O     . SER A 1 499  ? -34.300 41.045  85.941  1.00 26.55 ?  497  SER A O     1 
ATOM   3716  C CB    . SER A 1 499  ? -32.749 42.164  88.202  1.00 28.37 ?  497  SER A CB    1 
ATOM   3717  O OG    . SER A 1 499  ? -32.572 43.567  88.085  1.00 34.00 ?  497  SER A OG    1 
ATOM   3718  N N     . SER A 1 500  ? -32.818 42.225  84.724  1.00 22.37 ?  498  SER A N     1 
ATOM   3719  C CA    . SER A 1 500  ? -33.738 42.420  83.611  1.00 23.52 ?  498  SER A CA    1 
ATOM   3720  C C     . SER A 1 500  ? -33.999 41.109  82.881  1.00 23.68 ?  498  SER A C     1 
ATOM   3721  O O     . SER A 1 500  ? -33.077 40.331  82.627  1.00 25.09 ?  498  SER A O     1 
ATOM   3722  C CB    . SER A 1 500  ? -33.176 43.444  82.622  1.00 22.11 ?  498  SER A CB    1 
ATOM   3723  O OG    . SER A 1 500  ? -33.018 44.720  83.217  1.00 24.57 ?  498  SER A OG    1 
ATOM   3724  N N     . PHE A 1 501  ? -35.268 40.885  82.521  1.00 20.17 ?  499  PHE A N     1 
ATOM   3725  C CA    . PHE A 1 501  ? -35.641 39.686  81.776  1.00 20.56 ?  499  PHE A CA    1 
ATOM   3726  C C     . PHE A 1 501  ? -34.825 39.544  80.498  1.00 23.89 ?  499  PHE A C     1 
ATOM   3727  O O     . PHE A 1 501  ? -34.321 38.458  80.189  1.00 24.34 ?  499  PHE A O     1 
ATOM   3728  C CB    . PHE A 1 501  ? -37.134 39.714  81.440  1.00 20.11 ?  499  PHE A CB    1 
ATOM   3729  C CG    . PHE A 1 501  ? -37.575 38.561  80.592  1.00 22.32 ?  499  PHE A CG    1 
ATOM   3730  C CD1   . PHE A 1 501  ? -37.935 37.362  81.173  1.00 23.28 ?  499  PHE A CD1   1 
ATOM   3731  C CD2   . PHE A 1 501  ? -37.628 38.677  79.212  1.00 22.94 ?  499  PHE A CD2   1 
ATOM   3732  C CE1   . PHE A 1 501  ? -38.336 36.295  80.398  1.00 25.89 ?  499  PHE A CE1   1 
ATOM   3733  C CE2   . PHE A 1 501  ? -38.029 37.614  78.429  1.00 24.10 ?  499  PHE A CE2   1 
ATOM   3734  C CZ    . PHE A 1 501  ? -38.387 36.420  79.024  1.00 25.94 ?  499  PHE A CZ    1 
ATOM   3735  N N     . VAL A 1 502  ? -34.712 40.625  79.721  1.00 21.21 ?  500  VAL A N     1 
ATOM   3736  C CA    . VAL A 1 502  ? -34.045 40.524  78.428  1.00 26.05 ?  500  VAL A CA    1 
ATOM   3737  C C     . VAL A 1 502  ? -32.589 40.118  78.613  1.00 26.59 ?  500  VAL A C     1 
ATOM   3738  O O     . VAL A 1 502  ? -32.055 39.302  77.851  1.00 28.25 ?  500  VAL A O     1 
ATOM   3739  C CB    . VAL A 1 502  ? -34.181 41.846  77.648  1.00 22.31 ?  500  VAL A CB    1 
ATOM   3740  C CG1   . VAL A 1 502  ? -33.311 41.825  76.407  1.00 27.10 ?  500  VAL A CG1   1 
ATOM   3741  C CG2   . VAL A 1 502  ? -35.634 42.073  77.248  1.00 23.12 ?  500  VAL A CG2   1 
ATOM   3742  N N     . HIS A 1 503  ? -31.933 40.655  79.643  1.00 23.94 ?  501  HIS A N     1 
ATOM   3743  C CA    . HIS A 1 503  ? -30.553 40.275  79.925  1.00 26.74 ?  501  HIS A CA    1 
ATOM   3744  C C     . HIS A 1 503  ? -30.463 38.812  80.339  1.00 27.61 ?  501  HIS A C     1 
ATOM   3745  O O     . HIS A 1 503  ? -29.573 38.086  79.884  1.00 27.27 ?  501  HIS A O     1 
ATOM   3746  C CB    . HIS A 1 503  ? -29.976 41.188  81.010  1.00 24.48 ?  501  HIS A CB    1 
ATOM   3747  C CG    . HIS A 1 503  ? -28.523 40.950  81.293  1.00 31.81 ?  501  HIS A CG    1 
ATOM   3748  N ND1   . HIS A 1 503  ? -28.086 40.123  82.306  1.00 33.13 ?  501  HIS A ND1   1 
ATOM   3749  C CD2   . HIS A 1 503  ? -27.409 41.435  80.696  1.00 34.10 ?  501  HIS A CD2   1 
ATOM   3750  C CE1   . HIS A 1 503  ? -26.764 40.107  82.319  1.00 35.43 ?  501  HIS A CE1   1 
ATOM   3751  N NE2   . HIS A 1 503  ? -26.329 40.891  81.349  1.00 36.72 ?  501  HIS A NE2   1 
ATOM   3752  N N     . ARG A 1 504  ? -31.391 38.356  81.182  1.00 24.87 ?  502  ARG A N     1 
ATOM   3753  C CA    . ARG A 1 504  ? -31.340 36.987  81.678  1.00 25.47 ?  502  ARG A CA    1 
ATOM   3754  C C     . ARG A 1 504  ? -31.645 35.976  80.579  1.00 29.44 ?  502  ARG A C     1 
ATOM   3755  O O     . ARG A 1 504  ? -31.052 34.891  80.549  1.00 27.31 ?  502  ARG A O     1 
ATOM   3756  C CB    . ARG A 1 504  ? -32.307 36.830  82.849  1.00 25.49 ?  502  ARG A CB    1 
ATOM   3757  C CG    . ARG A 1 504  ? -31.879 37.619  84.073  1.00 30.03 ?  502  ARG A CG    1 
ATOM   3758  C CD    . ARG A 1 504  ? -33.018 37.811  85.052  1.00 29.40 ?  502  ARG A CD    1 
ATOM   3759  N NE    . ARG A 1 504  ? -33.681 36.553  85.375  1.00 33.83 ?  502  ARG A NE    1 
ATOM   3760  C CZ    . ARG A 1 504  ? -33.188 35.630  86.189  1.00 32.18 ?  502  ARG A CZ    1 
ATOM   3761  N NH1   . ARG A 1 504  ? -31.993 35.759  86.740  1.00 35.92 ?  502  ARG A NH1   1 
ATOM   3762  N NH2   . ARG A 1 504  ? -33.916 34.549  86.458  1.00 38.35 ?  502  ARG A NH2   1 
ATOM   3763  N N     . ILE A 1 505  ? -32.563 36.297  79.664  1.00 26.69 ?  503  ILE A N     1 
ATOM   3764  C CA    . ILE A 1 505  ? -32.855 35.318  78.623  1.00 31.19 ?  503  ILE A CA    1 
ATOM   3765  C C     . ILE A 1 505  ? -31.664 35.150  77.682  1.00 33.71 ?  503  ILE A C     1 
ATOM   3766  O O     . ILE A 1 505  ? -31.500 34.081  77.079  1.00 31.18 ?  503  ILE A O     1 
ATOM   3767  C CB    . ILE A 1 505  ? -34.149 35.680  77.867  1.00 31.47 ?  503  ILE A CB    1 
ATOM   3768  C CG1   . ILE A 1 505  ? -34.749 34.415  77.257  1.00 37.31 ?  503  ILE A CG1   1 
ATOM   3769  C CG2   . ILE A 1 505  ? -33.893 36.728  76.796  1.00 35.18 ?  503  ILE A CG2   1 
ATOM   3770  C CD1   . ILE A 1 505  ? -36.115 34.605  76.688  1.00 31.93 ?  503  ILE A CD1   1 
ATOM   3771  N N     . ASN A 1 506  ? -30.802 36.161  77.574  1.00 29.78 ?  504  ASN A N     1 
ATOM   3772  C CA    . ASN A 1 506  ? -29.568 36.063  76.805  1.00 32.23 ?  504  ASN A CA    1 
ATOM   3773  C C     . ASN A 1 506  ? -28.412 35.491  77.616  1.00 35.34 ?  504  ASN A C     1 
ATOM   3774  O O     . ASN A 1 506  ? -27.311 35.333  77.075  1.00 40.21 ?  504  ASN A O     1 
ATOM   3775  C CB    . ASN A 1 506  ? -29.176 37.435  76.246  1.00 36.18 ?  504  ASN A CB    1 
ATOM   3776  C CG    . ASN A 1 506  ? -30.094 37.894  75.128  1.00 41.51 ?  504  ASN A CG    1 
ATOM   3777  O OD1   . ASN A 1 506  ? -30.775 37.084  74.499  1.00 46.33 ?  504  ASN A OD1   1 
ATOM   3778  N ND2   . ASN A 1 506  ? -30.113 39.197  74.871  1.00 42.89 ?  504  ASN A ND2   1 
ATOM   3779  N N     . ASP A 1 507  ? -28.631 35.182  78.893  1.00 34.16 ?  505  ASP A N     1 
ATOM   3780  C CA    . ASP A 1 507  ? -27.611 34.555  79.721  1.00 36.35 ?  505  ASP A CA    1 
ATOM   3781  C C     . ASP A 1 507  ? -27.758 33.041  79.622  1.00 36.56 ?  505  ASP A C     1 
ATOM   3782  O O     . ASP A 1 507  ? -28.735 32.491  80.152  1.00 34.95 ?  505  ASP A O     1 
ATOM   3783  C CB    . ASP A 1 507  ? -27.745 35.011  81.167  1.00 34.38 ?  505  ASP A CB    1 
ATOM   3784  C CG    . ASP A 1 507  ? -26.594 34.543  82.048  1.00 39.66 ?  505  ASP A CG    1 
ATOM   3785  O OD1   . ASP A 1 507  ? -25.975 33.498  81.752  1.00 41.69 ?  505  ASP A OD1   1 
ATOM   3786  O OD2   . ASP A 1 507  ? -26.311 35.228  83.049  1.00 37.15 ?  505  ASP A OD2   1 
ATOM   3787  N N     . PRO A 1 508  ? -26.823 32.330  78.987  1.00 39.35 ?  506  PRO A N     1 
ATOM   3788  C CA    . PRO A 1 508  ? -26.953 30.865  78.896  1.00 41.54 ?  506  PRO A CA    1 
ATOM   3789  C C     . PRO A 1 508  ? -26.920 30.169  80.246  1.00 38.00 ?  506  PRO A C     1 
ATOM   3790  O O     . PRO A 1 508  ? -27.386 29.027  80.346  1.00 44.53 ?  506  PRO A O     1 
ATOM   3791  C CB    . PRO A 1 508  ? -25.754 30.453  78.027  1.00 44.20 ?  506  PRO A CB    1 
ATOM   3792  C CG    . PRO A 1 508  ? -25.300 31.719  77.346  1.00 48.97 ?  506  PRO A CG    1 
ATOM   3793  C CD    . PRO A 1 508  ? -25.619 32.828  78.302  1.00 43.06 ?  506  PRO A CD    1 
ATOM   3794  N N     . LYS A 1 509  ? -26.389 30.815  81.284  1.00 37.49 ?  507  LYS A N     1 
ATOM   3795  C CA    . LYS A 1 509  ? -26.375 30.241  82.625  1.00 39.73 ?  507  LYS A CA    1 
ATOM   3796  C C     . LYS A 1 509  ? -27.698 30.414  83.366  1.00 41.06 ?  507  LYS A C     1 
ATOM   3797  O O     . LYS A 1 509  ? -27.808 29.967  84.513  1.00 42.93 ?  507  LYS A O     1 
ATOM   3798  C CB    . LYS A 1 509  ? -25.239 30.855  83.449  1.00 43.77 ?  507  LYS A CB    1 
ATOM   3799  N N     . VAL A 1 510  ? -28.693 31.051  82.754  1.00 38.61 ?  508  VAL A N     1 
ATOM   3800  C CA    . VAL A 1 510  ? -30.025 31.180  83.334  1.00 37.30 ?  508  VAL A CA    1 
ATOM   3801  C C     . VAL A 1 510  ? -30.930 30.157  82.659  1.00 33.10 ?  508  VAL A C     1 
ATOM   3802  O O     . VAL A 1 510  ? -31.106 30.183  81.436  1.00 34.05 ?  508  VAL A O     1 
ATOM   3803  C CB    . VAL A 1 510  ? -30.575 32.607  83.177  1.00 32.36 ?  508  VAL A CB    1 
ATOM   3804  C CG1   . VAL A 1 510  ? -32.014 32.681  83.685  1.00 31.89 ?  508  VAL A CG1   1 
ATOM   3805  C CG2   . VAL A 1 510  ? -29.699 33.602  83.921  1.00 33.32 ?  508  VAL A CG2   1 
ATOM   3806  N N     . SER A 1 511  ? -31.489 29.244  83.448  1.00 35.05 ?  509  SER A N     1 
ATOM   3807  C CA    . SER A 1 511  ? -32.337 28.200  82.896  1.00 33.65 ?  509  SER A CA    1 
ATOM   3808  C C     . SER A 1 511  ? -33.752 28.722  82.675  1.00 33.64 ?  509  SER A C     1 
ATOM   3809  O O     . SER A 1 511  ? -34.168 29.736  83.245  1.00 31.06 ?  509  SER A O     1 
ATOM   3810  C CB    . SER A 1 511  ? -32.377 26.981  83.820  1.00 36.40 ?  509  SER A CB    1 
ATOM   3811  O OG    . SER A 1 511  ? -33.114 27.269  84.995  1.00 35.90 ?  509  SER A OG    1 
ATOM   3812  N N     . ILE A 1 512  ? -34.495 28.010  81.826  1.00 31.68 ?  510  ILE A N     1 
ATOM   3813  C CA    . ILE A 1 512  ? -35.883 28.381  81.572  1.00 30.79 ?  510  ILE A CA    1 
ATOM   3814  C C     . ILE A 1 512  ? -36.714 28.220  82.838  1.00 36.51 ?  510  ILE A C     1 
ATOM   3815  O O     . ILE A 1 512  ? -37.616 29.022  83.111  1.00 31.83 ?  510  ILE A O     1 
ATOM   3816  C CB    . ILE A 1 512  ? -36.448 27.559  80.399  1.00 30.88 ?  510  ILE A CB    1 
ATOM   3817  C CG1   . ILE A 1 512  ? -35.637 27.840  79.134  1.00 31.41 ?  510  ILE A CG1   1 
ATOM   3818  C CG2   . ILE A 1 512  ? -37.932 27.848  80.182  1.00 32.15 ?  510  ILE A CG2   1 
ATOM   3819  C CD1   . ILE A 1 512  ? -36.254 27.293  77.879  1.00 34.78 ?  510  ILE A CD1   1 
ATOM   3820  N N     . ASP A 1 513  ? -36.415 27.192  83.641  1.00 34.03 ?  511  ASP A N     1 
ATOM   3821  C CA    . ASP A 1 513  ? -37.125 27.021  84.904  1.00 34.52 ?  511  ASP A CA    1 
ATOM   3822  C C     . ASP A 1 513  ? -36.962 28.245  85.792  1.00 34.74 ?  511  ASP A C     1 
ATOM   3823  O O     . ASP A 1 513  ? -37.927 28.695  86.422  1.00 33.24 ?  511  ASP A O     1 
ATOM   3824  C CB    . ASP A 1 513  ? -36.636 25.764  85.627  1.00 39.16 ?  511  ASP A CB    1 
ATOM   3825  C CG    . ASP A 1 513  ? -37.276 24.493  85.092  1.00 42.81 ?  511  ASP A CG    1 
ATOM   3826  O OD1   . ASP A 1 513  ? -38.336 24.579  84.432  1.00 42.87 ?  511  ASP A OD1   1 
ATOM   3827  O OD2   . ASP A 1 513  ? -36.719 23.402  85.342  1.00 45.41 ?  511  ASP A OD2   1 
ATOM   3828  N N     . GLU A 1 514  ? -35.751 28.807  85.843  1.00 32.26 ?  512  GLU A N     1 
ATOM   3829  C CA    . GLU A 1 514  ? -35.527 30.025  86.611  1.00 34.31 ?  512  GLU A CA    1 
ATOM   3830  C C     . GLU A 1 514  ? -36.310 31.202  86.037  1.00 29.84 ?  512  GLU A C     1 
ATOM   3831  O O     . GLU A 1 514  ? -36.742 32.084  86.788  1.00 35.30 ?  512  GLU A O     1 
ATOM   3832  C CB    . GLU A 1 514  ? -34.028 30.349  86.661  1.00 36.38 ?  512  GLU A CB    1 
ATOM   3833  C CG    . GLU A 1 514  ? -33.198 29.327  87.446  1.00 39.55 ?  512  GLU A CG    1 
ATOM   3834  C CD    . GLU A 1 514  ? -31.689 29.507  87.281  1.00 44.25 ?  512  GLU A CD    1 
ATOM   3835  O OE1   . GLU A 1 514  ? -31.255 30.179  86.323  1.00 45.85 ?  512  GLU A OE1   1 
ATOM   3836  O OE2   . GLU A 1 514  ? -30.931 28.967  88.116  1.00 55.17 ?  512  GLU A OE2   1 
ATOM   3837  N N     . LEU A 1 515  ? -36.505 31.231  84.717  1.00 31.17 ?  513  LEU A N     1 
ATOM   3838  C CA    . LEU A 1 515  ? -37.180 32.366  84.092  1.00 29.83 ?  513  LEU A CA    1 
ATOM   3839  C C     . LEU A 1 515  ? -38.688 32.309  84.279  1.00 30.09 ?  513  LEU A C     1 
ATOM   3840  O O     . LEU A 1 515  ? -39.345 33.356  84.300  1.00 27.05 ?  513  LEU A O     1 
ATOM   3841  C CB    . LEU A 1 515  ? -36.841 32.432  82.601  1.00 29.97 ?  513  LEU A CB    1 
ATOM   3842  C CG    . LEU A 1 515  ? -35.422 32.888  82.246  1.00 27.36 ?  513  LEU A CG    1 
ATOM   3843  C CD1   . LEU A 1 515  ? -35.143 32.609  80.780  1.00 31.74 ?  513  LEU A CD1   1 
ATOM   3844  C CD2   . LEU A 1 515  ? -35.230 34.372  82.550  1.00 28.84 ?  513  LEU A CD2   1 
ATOM   3845  N N     . ILE A 1 516  ? -39.254 31.112  84.414  1.00 28.88 ?  514  ILE A N     1 
ATOM   3846  C CA    . ILE A 1 516  ? -40.694 30.969  84.583  1.00 28.63 ?  514  ILE A CA    1 
ATOM   3847  C C     . ILE A 1 516  ? -41.081 30.865  86.052  1.00 31.23 ?  514  ILE A C     1 
ATOM   3848  O O     . ILE A 1 516  ? -42.260 30.646  86.361  1.00 31.84 ?  514  ILE A O     1 
ATOM   3849  C CB    . ILE A 1 516  ? -41.239 29.774  83.784  1.00 30.28 ?  514  ILE A CB    1 
ATOM   3850  C CG1   . ILE A 1 516  ? -40.701 28.462  84.364  1.00 32.26 ?  514  ILE A CG1   1 
ATOM   3851  C CG2   . ILE A 1 516  ? -40.877 29.916  82.313  1.00 30.45 ?  514  ILE A CG2   1 
ATOM   3852  C CD1   . ILE A 1 516  ? -41.228 27.231  83.683  1.00 31.81 ?  514  ILE A CD1   1 
ATOM   3853  N N     . ALA A 1 517  ? -40.116 31.013  86.960  1.00 28.67 ?  515  ALA A N     1 
ATOM   3854  C CA    . ALA A 1 517  ? -40.410 31.096  88.382  1.00 29.55 ?  515  ALA A CA    1 
ATOM   3855  C C     . ALA A 1 517  ? -41.482 32.143  88.649  1.00 32.44 ?  515  ALA A C     1 
ATOM   3856  O O     . ALA A 1 517  ? -41.464 33.232  88.072  1.00 31.84 ?  515  ALA A O     1 
ATOM   3857  C CB    . ALA A 1 517  ? -39.140 31.444  89.162  1.00 32.25 ?  515  ALA A CB    1 
ATOM   3858  N N     . ASP A 1 518  ? -42.404 31.808  89.551  1.00 32.92 ?  516  ASP A N     1 
ATOM   3859  C CA    . ASP A 1 518  ? -43.543 32.661  89.857  1.00 29.11 ?  516  ASP A CA    1 
ATOM   3860  C C     . ASP A 1 518  ? -43.167 33.652  90.952  1.00 29.60 ?  516  ASP A C     1 
ATOM   3861  O O     . ASP A 1 518  ? -42.985 33.240  92.108  1.00 28.53 ?  516  ASP A O     1 
ATOM   3862  C CB    . ASP A 1 518  ? -44.728 31.806  90.289  1.00 30.48 ?  516  ASP A CB    1 
ATOM   3863  C CG    . ASP A 1 518  ? -45.983 32.618  90.540  1.00 30.70 ?  516  ASP A CG    1 
ATOM   3864  O OD1   . ASP A 1 518  ? -45.970 33.856  90.346  1.00 29.75 ?  516  ASP A OD1   1 
ATOM   3865  O OD2   . ASP A 1 518  ? -46.992 31.997  90.930  1.00 35.77 ?  516  ASP A OD2   1 
ATOM   3866  N N     . PRO A 1 519  ? -43.061 34.950  90.656  1.00 25.30 ?  517  PRO A N     1 
ATOM   3867  C CA    . PRO A 1 519  ? -42.691 35.907  91.712  1.00 27.67 ?  517  PRO A CA    1 
ATOM   3868  C C     . PRO A 1 519  ? -43.668 35.925  92.870  1.00 25.58 ?  517  PRO A C     1 
ATOM   3869  O O     . PRO A 1 519  ? -43.259 36.177  94.011  1.00 27.67 ?  517  PRO A O     1 
ATOM   3870  C CB    . PRO A 1 519  ? -42.676 37.262  90.979  1.00 26.31 ?  517  PRO A CB    1 
ATOM   3871  C CG    . PRO A 1 519  ? -42.672 36.936  89.526  1.00 32.13 ?  517  PRO A CG    1 
ATOM   3872  C CD    . PRO A 1 519  ? -43.343 35.612  89.372  1.00 27.08 ?  517  PRO A CD    1 
ATOM   3873  N N     . VAL A 1 520  ? -44.953 35.691  92.598  1.00 28.64 ?  518  VAL A N     1 
ATOM   3874  C CA    . VAL A 1 520  ? -45.969 35.755  93.644  1.00 25.93 ?  518  VAL A CA    1 
ATOM   3875  C C     . VAL A 1 520  ? -45.719 34.669  94.683  1.00 28.56 ?  518  VAL A C     1 
ATOM   3876  O O     . VAL A 1 520  ? -45.703 34.932  95.890  1.00 28.14 ?  518  VAL A O     1 
ATOM   3877  C CB    . VAL A 1 520  ? -47.376 35.641  93.031  1.00 30.28 ?  518  VAL A CB    1 
ATOM   3878  C CG1   . VAL A 1 520  ? -48.440 35.772  94.110  1.00 33.16 ?  518  VAL A CG1   1 
ATOM   3879  C CG2   . VAL A 1 520  ? -47.575 36.702  91.955  1.00 29.27 ?  518  VAL A CG2   1 
ATOM   3880  N N     . GLU A 1 521  ? -45.491 33.436  94.226  1.00 30.42 ?  519  GLU A N     1 
ATOM   3881  C CA    . GLU A 1 521  ? -45.261 32.345  95.170  1.00 33.21 ?  519  GLU A CA    1 
ATOM   3882  C C     . GLU A 1 521  ? -43.904 32.457  95.854  1.00 33.17 ?  519  GLU A C     1 
ATOM   3883  O O     . GLU A 1 521  ? -43.773 32.084  97.027  1.00 33.85 ?  519  GLU A O     1 
ATOM   3884  C CB    . GLU A 1 521  ? -45.397 30.998  94.464  1.00 33.43 ?  519  GLU A CB    1 
ATOM   3885  C CG    . GLU A 1 521  ? -46.831 30.643  94.116  1.00 34.15 ?  519  GLU A CG    1 
ATOM   3886  C CD    . GLU A 1 521  ? -47.778 30.857  95.282  1.00 43.75 ?  519  GLU A CD    1 
ATOM   3887  O OE1   . GLU A 1 521  ? -47.407 30.513  96.428  1.00 46.67 ?  519  GLU A OE1   1 
ATOM   3888  O OE2   . GLU A 1 521  ? -48.891 31.378  95.056  1.00 43.73 ?  519  GLU A OE2   1 
ATOM   3889  N N     . VAL A 1 522  ? -42.891 32.972  95.152  1.00 32.24 ?  520  VAL A N     1 
ATOM   3890  C CA    . VAL A 1 522  ? -41.573 33.130  95.759  1.00 28.51 ?  520  VAL A CA    1 
ATOM   3891  C C     . VAL A 1 522  ? -41.614 34.169  96.876  1.00 34.66 ?  520  VAL A C     1 
ATOM   3892  O O     . VAL A 1 522  ? -41.022 33.975  97.945  1.00 34.49 ?  520  VAL A O     1 
ATOM   3893  C CB    . VAL A 1 522  ? -40.529 33.487  94.684  1.00 32.59 ?  520  VAL A CB    1 
ATOM   3894  C CG1   . VAL A 1 522  ? -39.174 33.771  95.321  1.00 29.62 ?  520  VAL A CG1   1 
ATOM   3895  C CG2   . VAL A 1 522  ? -40.418 32.361  93.670  1.00 35.70 ?  520  VAL A CG2   1 
ATOM   3896  N N     . VAL A 1 523  ? -42.312 35.285  96.651  1.00 29.71 ?  521  VAL A N     1 
ATOM   3897  C CA    . VAL A 1 523  ? -42.435 36.296  97.695  1.00 30.81 ?  521  VAL A CA    1 
ATOM   3898  C C     . VAL A 1 523  ? -43.238 35.757  98.874  1.00 32.62 ?  521  VAL A C     1 
ATOM   3899  O O     . VAL A 1 523  ? -42.904 36.016  100.036 1.00 32.39 ?  521  VAL A O     1 
ATOM   3900  C CB    . VAL A 1 523  ? -43.057 37.583  97.122  1.00 26.02 ?  521  VAL A CB    1 
ATOM   3901  C CG1   . VAL A 1 523  ? -43.461 38.522  98.248  1.00 28.81 ?  521  VAL A CG1   1 
ATOM   3902  C CG2   . VAL A 1 523  ? -42.056 38.278  96.195  1.00 26.95 ?  521  VAL A CG2   1 
ATOM   3903  N N     . ARG A 1 524  ? -44.300 34.995  98.598  1.00 30.85 ?  522  ARG A N     1 
ATOM   3904  C CA    . ARG A 1 524  ? -45.138 34.479  99.678  1.00 34.99 ?  522  ARG A CA    1 
ATOM   3905  C C     . ARG A 1 524  ? -44.337 33.600  100.631 1.00 37.00 ?  522  ARG A C     1 
ATOM   3906  O O     . ARG A 1 524  ? -44.553 33.633  101.849 1.00 39.95 ?  522  ARG A O     1 
ATOM   3907  C CB    . ARG A 1 524  ? -46.317 33.698  99.102  1.00 34.49 ?  522  ARG A CB    1 
ATOM   3908  C CG    . ARG A 1 524  ? -47.361 33.311  100.150 1.00 35.15 ?  522  ARG A CG    1 
ATOM   3909  C CD    . ARG A 1 524  ? -48.233 32.173  99.670  1.00 41.80 ?  522  ARG A CD    1 
ATOM   3910  N NE    . ARG A 1 524  ? -48.746 32.402  98.325  1.00 41.17 ?  522  ARG A NE    1 
ATOM   3911  C CZ    . ARG A 1 524  ? -49.817 33.130  98.045  1.00 39.77 ?  522  ARG A CZ    1 
ATOM   3912  N NH1   . ARG A 1 524  ? -50.502 33.746  98.996  1.00 37.79 ?  522  ARG A NH1   1 
ATOM   3913  N NH2   . ARG A 1 524  ? -50.212 33.244  96.779  1.00 40.05 ?  522  ARG A NH2   1 
ATOM   3914  N N     . ALA A 1 525  ? -43.389 32.827  100.098 1.00 36.78 ?  523  ALA A N     1 
ATOM   3915  C CA    . ALA A 1 525  ? -42.647 31.853  100.886 1.00 35.98 ?  523  ALA A CA    1 
ATOM   3916  C C     . ALA A 1 525  ? -41.441 32.444  101.604 1.00 37.25 ?  523  ALA A C     1 
ATOM   3917  O O     . ALA A 1 525  ? -40.807 31.735  102.395 1.00 40.86 ?  523  ALA A O     1 
ATOM   3918  C CB    . ALA A 1 525  ? -42.195 30.694  99.990  1.00 32.54 ?  523  ALA A CB    1 
ATOM   3919  N N     . MET A 1 526  ? -41.097 33.704  101.348 1.00 35.64 ?  524  MET A N     1 
ATOM   3920  C CA    A MET A 1 526  ? -39.991 34.325  102.057 0.55 37.47 ?  524  MET A CA    1 
ATOM   3921  C CA    B MET A 1 526  ? -39.989 34.325  102.056 0.45 37.48 ?  524  MET A CA    1 
ATOM   3922  C C     . MET A 1 526  ? -40.287 34.364  103.555 1.00 39.19 ?  524  MET A C     1 
ATOM   3923  O O     . MET A 1 526  ? -41.450 34.442  103.965 1.00 39.15 ?  524  MET A O     1 
ATOM   3924  C CB    A MET A 1 526  ? -39.743 35.737  101.533 0.55 38.67 ?  524  MET A CB    1 
ATOM   3925  C CB    B MET A 1 526  ? -39.732 35.737  101.523 0.45 38.65 ?  524  MET A CB    1 
ATOM   3926  C CG    A MET A 1 526  ? -39.217 35.774  100.113 0.55 37.15 ?  524  MET A CG    1 
ATOM   3927  C CG    B MET A 1 526  ? -38.823 35.783  100.293 0.45 37.32 ?  524  MET A CG    1 
ATOM   3928  S SD    A MET A 1 526  ? -37.694 34.829  99.946  0.55 40.77 ?  524  MET A SD    1 
ATOM   3929  S SD    B MET A 1 526  ? -38.829 37.351  99.383  0.45 38.09 ?  524  MET A SD    1 
ATOM   3930  C CE    A MET A 1 526  ? -36.629 35.692  101.103 0.55 38.94 ?  524  MET A CE    1 
ATOM   3931  C CE    B MET A 1 526  ? -38.277 38.510  100.634 0.45 34.62 ?  524  MET A CE    1 
ATOM   3932  N N     . PRO A 1 527  ? -39.252 34.288  104.399 1.00 42.82 ?  525  PRO A N     1 
ATOM   3933  C CA    . PRO A 1 527  ? -39.502 34.334  105.852 1.00 42.75 ?  525  PRO A CA    1 
ATOM   3934  C C     . PRO A 1 527  ? -40.158 35.629  106.288 1.00 43.75 ?  525  PRO A C     1 
ATOM   3935  O O     . PRO A 1 527  ? -41.173 35.605  107.000 1.00 40.02 ?  525  PRO A O     1 
ATOM   3936  C CB    . PRO A 1 527  ? -38.098 34.165  106.449 1.00 40.46 ?  525  PRO A CB    1 
ATOM   3937  C CG    . PRO A 1 527  ? -37.318 33.481  105.384 1.00 41.84 ?  525  PRO A CG    1 
ATOM   3938  C CD    . PRO A 1 527  ? -37.837 34.029  104.093 1.00 40.75 ?  525  PRO A CD    1 
ATOM   3939  N N     . VAL A 1 528  ? -39.604 36.763  105.872 1.00 42.28 ?  526  VAL A N     1 
ATOM   3940  C CA    . VAL A 1 528  ? -40.196 38.075  106.093 1.00 36.51 ?  526  VAL A CA    1 
ATOM   3941  C C     . VAL A 1 528  ? -40.702 38.566  104.744 1.00 32.62 ?  526  VAL A C     1 
ATOM   3942  O O     . VAL A 1 528  ? -39.906 38.947  103.876 1.00 35.52 ?  526  VAL A O     1 
ATOM   3943  C CB    . VAL A 1 528  ? -39.192 39.063  106.698 1.00 38.94 ?  526  VAL A CB    1 
ATOM   3944  C CG1   . VAL A 1 528  ? -39.883 40.380  107.037 1.00 37.71 ?  526  VAL A CG1   1 
ATOM   3945  C CG2   . VAL A 1 528  ? -38.526 38.465  107.929 1.00 42.57 ?  526  VAL A CG2   1 
ATOM   3946  N N     . VAL A 1 529  ? -42.023 38.557  104.560 1.00 31.36 ?  527  VAL A N     1 
ATOM   3947  C CA    . VAL A 1 529  ? -42.599 39.000  103.296 1.00 31.22 ?  527  VAL A CA    1 
ATOM   3948  C C     . VAL A 1 529  ? -42.339 40.491  103.114 1.00 29.97 ?  527  VAL A C     1 
ATOM   3949  O O     . VAL A 1 529  ? -42.619 41.305  104.004 1.00 28.20 ?  527  VAL A O     1 
ATOM   3950  C CB    . VAL A 1 529  ? -44.102 38.681  103.243 1.00 29.38 ?  527  VAL A CB    1 
ATOM   3951  C CG1   . VAL A 1 529  ? -44.719 39.225  101.961 1.00 31.93 ?  527  VAL A CG1   1 
ATOM   3952  C CG2   . VAL A 1 529  ? -44.323 37.182  103.336 1.00 35.42 ?  527  VAL A CG2   1 
ATOM   3953  N N     . GLY A 1 530  ? -41.782 40.856  101.959 1.00 26.44 ?  528  GLY A N     1 
ATOM   3954  C CA    . GLY A 1 530  ? -41.597 42.257  101.637 1.00 26.05 ?  528  GLY A CA    1 
ATOM   3955  C C     . GLY A 1 530  ? -40.389 42.931  102.246 1.00 24.49 ?  528  GLY A C     1 
ATOM   3956  O O     . GLY A 1 530  ? -40.333 44.164  102.270 1.00 23.39 ?  528  GLY A O     1 
ATOM   3957  N N     . ALA A 1 531  ? -39.406 42.172  102.733 1.00 22.07 ?  529  ALA A N     1 
ATOM   3958  C CA    . ALA A 1 531  ? -38.219 42.786  103.317 1.00 23.82 ?  529  ALA A CA    1 
ATOM   3959  C C     . ALA A 1 531  ? -37.455 43.633  102.302 1.00 19.19 ?  529  ALA A C     1 
ATOM   3960  O O     . ALA A 1 531  ? -37.296 43.252  101.140 1.00 24.72 ?  529  ALA A O     1 
ATOM   3961  C CB    . ALA A 1 531  ? -37.290 41.709  103.873 1.00 26.13 ?  529  ALA A CB    1 
ATOM   3962  N N     . LYS A 1 532  ? -36.953 44.776  102.770 1.00 20.61 ?  530  LYS A N     1 
ATOM   3963  C CA    . LYS A 1 532  ? -36.055 45.617  101.984 1.00 17.94 ?  530  LYS A CA    1 
ATOM   3964  C C     . LYS A 1 532  ? -34.854 44.814  101.498 1.00 21.51 ?  530  LYS A C     1 
ATOM   3965  O O     . LYS A 1 532  ? -34.391 43.884  102.159 1.00 20.82 ?  530  LYS A O     1 
ATOM   3966  C CB    . LYS A 1 532  ? -35.583 46.799  102.843 1.00 22.98 ?  530  LYS A CB    1 
ATOM   3967  C CG    . LYS A 1 532  ? -34.585 47.749  102.201 1.00 26.18 ?  530  LYS A CG    1 
ATOM   3968  C CD    . LYS A 1 532  ? -34.041 48.741  103.223 1.00 22.32 ?  530  LYS A CD    1 
ATOM   3969  C CE    . LYS A 1 532  ? -33.251 48.044  104.329 1.00 21.72 ?  530  LYS A CE    1 
ATOM   3970  N NZ    . LYS A 1 532  ? -31.951 47.531  103.813 1.00 23.48 ?  530  LYS A NZ    1 
ATOM   3971  N N     . HIS A 1 533  ? -34.352 45.171  100.324 1.00 19.22 ?  531  HIS A N     1 
ATOM   3972  C CA    . HIS A 1 533  ? -33.123 44.568  99.826  1.00 20.01 ?  531  HIS A CA    1 
ATOM   3973  C C     . HIS A 1 533  ? -31.987 44.737  100.834 1.00 19.93 ?  531  HIS A C     1 
ATOM   3974  O O     . HIS A 1 533  ? -31.755 45.834  101.350 1.00 21.61 ?  531  HIS A O     1 
ATOM   3975  C CB    . HIS A 1 533  ? -32.746 45.210  98.490  1.00 19.27 ?  531  HIS A CB    1 
ATOM   3976  C CG    . HIS A 1 533  ? -31.769 44.408  97.695  1.00 21.60 ?  531  HIS A CG    1 
ATOM   3977  N ND1   . HIS A 1 533  ? -30.469 44.197  98.106  1.00 22.38 ?  531  HIS A ND1   1 
ATOM   3978  C CD2   . HIS A 1 533  ? -31.912 43.727  96.534  1.00 26.37 ?  531  HIS A CD2   1 
ATOM   3979  C CE1   . HIS A 1 533  ? -29.846 43.444  97.217  1.00 28.73 ?  531  HIS A CE1   1 
ATOM   3980  N NE2   . HIS A 1 533  ? -30.701 43.141  96.257  1.00 29.78 ?  531  HIS A NE2   1 
ATOM   3981  N N     . ASP A 1 534  ? -31.267 43.638  101.099 1.00 21.30 ?  532  ASP A N     1 
ATOM   3982  C CA    . ASP A 1 534  ? -30.175 43.668  102.072 1.00 25.10 ?  532  ASP A CA    1 
ATOM   3983  C C     . ASP A 1 534  ? -29.079 44.667  101.716 1.00 26.61 ?  532  ASP A C     1 
ATOM   3984  O O     . ASP A 1 534  ? -28.387 45.165  102.612 1.00 26.89 ?  532  ASP A O     1 
ATOM   3985  C CB    . ASP A 1 534  ? -29.553 42.277  102.215 1.00 28.02 ?  532  ASP A CB    1 
ATOM   3986  C CG    . ASP A 1 534  ? -30.455 41.309  102.936 1.00 40.36 ?  532  ASP A CG    1 
ATOM   3987  O OD1   . ASP A 1 534  ? -31.329 41.775  103.701 1.00 44.21 ?  532  ASP A OD1   1 
ATOM   3988  O OD2   . ASP A 1 534  ? -30.288 40.086  102.744 1.00 48.49 ?  532  ASP A OD2   1 
ATOM   3989  N N     . ARG A 1 535  ? -28.880 44.956  100.433 1.00 20.82 ?  533  ARG A N     1 
ATOM   3990  C CA    . ARG A 1 535  ? -27.729 45.741  100.008 1.00 22.50 ?  533  ARG A CA    1 
ATOM   3991  C C     . ARG A 1 535  ? -28.064 47.197  99.694  1.00 21.36 ?  533  ARG A C     1 
ATOM   3992  O O     . ARG A 1 535  ? -27.210 47.913  99.159  1.00 23.30 ?  533  ARG A O     1 
ATOM   3993  C CB    . ARG A 1 535  ? -27.059 45.078  98.801  1.00 25.65 ?  533  ARG A CB    1 
ATOM   3994  C CG    . ARG A 1 535  ? -26.206 43.870  99.177  1.00 33.91 ?  533  ARG A CG    1 
ATOM   3995  C CD    . ARG A 1 535  ? -26.159 42.828  98.062  1.00 39.17 ?  533  ARG A CD    1 
ATOM   3996  N NE    . ARG A 1 535  ? -25.748 43.394  96.782  1.00 47.16 ?  533  ARG A NE    1 
ATOM   3997  C CZ    . ARG A 1 535  ? -24.488 43.526  96.387  1.00 52.26 ?  533  ARG A CZ    1 
ATOM   3998  N NH1   . ARG A 1 535  ? -23.479 43.142  97.152  1.00 55.25 ?  533  ARG A NH1   1 
ATOM   3999  N NH2   . ARG A 1 535  ? -24.235 44.058  95.193  1.00 49.45 ?  533  ARG A NH2   1 
ATOM   4000  N N     . ILE A 1 536  ? -29.263 47.660  100.038 1.00 20.60 ?  534  ILE A N     1 
ATOM   4001  C CA    . ILE A 1 536  ? -29.659 49.050  99.844  1.00 20.44 ?  534  ILE A CA    1 
ATOM   4002  C C     . ILE A 1 536  ? -29.966 49.653  101.208 1.00 20.95 ?  534  ILE A C     1 
ATOM   4003  O O     . ILE A 1 536  ? -30.847 49.161  101.923 1.00 21.70 ?  534  ILE A O     1 
ATOM   4004  C CB    . ILE A 1 536  ? -30.869 49.165  98.911  1.00 19.46 ?  534  ILE A CB    1 
ATOM   4005  C CG1   . ILE A 1 536  ? -30.526 48.564  97.555  1.00 25.08 ?  534  ILE A CG1   1 
ATOM   4006  C CG2   . ILE A 1 536  ? -31.316 50.618  98.795  1.00 20.39 ?  534  ILE A CG2   1 
ATOM   4007  C CD1   . ILE A 1 536  ? -31.679 48.568  96.615  1.00 24.07 ?  534  ILE A CD1   1 
ATOM   4008  N N     . ALA A 1 537  ? -29.248 50.713  101.565 1.00 17.94 ?  535  ALA A N     1 
ATOM   4009  C CA    . ALA A 1 537  ? -29.412 51.324  102.876 1.00 18.88 ?  535  ALA A CA    1 
ATOM   4010  C C     . ALA A 1 537  ? -30.610 52.263  102.875 1.00 17.34 ?  535  ALA A C     1 
ATOM   4011  O O     . ALA A 1 537  ? -30.765 53.077  101.963 1.00 16.83 ?  535  ALA A O     1 
ATOM   4012  C CB    . ALA A 1 537  ? -28.151 52.089  103.269 1.00 19.05 ?  535  ALA A CB    1 
ATOM   4013  N N     . LEU A 1 538  ? -31.463 52.142  103.892 1.00 18.13 ?  536  LEU A N     1 
ATOM   4014  C CA    . LEU A 1 538  ? -32.431 53.201  104.141 1.00 16.42 ?  536  LEU A CA    1 
ATOM   4015  C C     . LEU A 1 538  ? -31.678 54.510  104.364 1.00 16.08 ?  536  LEU A C     1 
ATOM   4016  O O     . LEU A 1 538  ? -30.550 54.500  104.861 1.00 17.81 ?  536  LEU A O     1 
ATOM   4017  C CB    . LEU A 1 538  ? -33.292 52.879  105.363 1.00 17.75 ?  536  LEU A CB    1 
ATOM   4018  C CG    . LEU A 1 538  ? -34.316 51.759  105.209 1.00 20.39 ?  536  LEU A CG    1 
ATOM   4019  C CD1   . LEU A 1 538  ? -34.914 51.399  106.557 1.00 22.02 ?  536  LEU A CD1   1 
ATOM   4020  C CD2   . LEU A 1 538  ? -35.412 52.175  104.232 1.00 21.60 ?  536  LEU A CD2   1 
ATOM   4021  N N     . PRO A 1 539  ? -32.256 55.649  103.974 1.00 15.81 ?  537  PRO A N     1 
ATOM   4022  C CA    . PRO A 1 539  ? -31.540 56.920  104.170 1.00 15.36 ?  537  PRO A CA    1 
ATOM   4023  C C     . PRO A 1 539  ? -31.051 57.122  105.601 1.00 18.66 ?  537  PRO A C     1 
ATOM   4024  O O     . PRO A 1 539  ? -29.922 57.589  105.783 1.00 18.63 ?  537  PRO A O     1 
ATOM   4025  C CB    . PRO A 1 539  ? -32.572 57.971  103.730 1.00 15.60 ?  537  PRO A CB    1 
ATOM   4026  C CG    . PRO A 1 539  ? -33.381 57.249  102.682 1.00 16.54 ?  537  PRO A CG    1 
ATOM   4027  C CD    . PRO A 1 539  ? -33.494 55.820  103.194 1.00 16.64 ?  537  PRO A CD    1 
ATOM   4028  N N     . ALA A 1 540  ? -31.834 56.735  106.616 1.00 16.75 ?  538  ALA A N     1 
ATOM   4029  C CA    . ALA A 1 540  ? -31.386 56.917  107.994 1.00 19.34 ?  538  ALA A CA    1 
ATOM   4030  C C     . ALA A 1 540  ? -30.148 56.096  108.326 1.00 21.65 ?  538  ALA A C     1 
ATOM   4031  O O     . ALA A 1 540  ? -29.424 56.445  109.269 1.00 22.83 ?  538  ALA A O     1 
ATOM   4032  C CB    . ALA A 1 540  ? -32.501 56.555  108.977 1.00 22.45 ?  538  ALA A CB    1 
ATOM   4033  N N     . GLU A 1 541  ? -29.885 55.020  107.586 1.00 19.06 ?  539  GLU A N     1 
ATOM   4034  C CA    . GLU A 1 541  ? -28.809 54.089  107.903 1.00 22.04 ?  539  GLU A CA    1 
ATOM   4035  C C     . GLU A 1 541  ? -27.612 54.222  106.966 1.00 19.04 ?  539  GLU A C     1 
ATOM   4036  O O     . GLU A 1 541  ? -26.772 53.317  106.905 1.00 20.09 ?  539  GLU A O     1 
ATOM   4037  C CB    . GLU A 1 541  ? -29.355 52.659  107.906 1.00 22.89 ?  539  GLU A CB    1 
ATOM   4038  C CG    . GLU A 1 541  ? -30.494 52.494  108.922 1.00 24.38 ?  539  GLU A CG    1 
ATOM   4039  C CD    . GLU A 1 541  ? -31.187 51.142  108.862 1.00 33.99 ?  539  GLU A CD    1 
ATOM   4040  O OE1   . GLU A 1 541  ? -30.610 50.187  108.306 1.00 38.26 ?  539  GLU A OE1   1 
ATOM   4041  O OE2   . GLU A 1 541  ? -32.315 51.034  109.386 1.00 38.18 ?  539  GLU A OE2   1 
ATOM   4042  N N     . LEU A 1 542  ? -27.501 55.357  106.258 1.00 18.69 ?  540  LEU A N     1 
ATOM   4043  C CA    . LEU A 1 542  ? -26.417 55.571  105.303 1.00 20.65 ?  540  LEU A CA    1 
ATOM   4044  C C     . LEU A 1 542  ? -25.037 55.367  105.909 1.00 19.57 ?  540  LEU A C     1 
ATOM   4045  O O     . LEU A 1 542  ? -24.107 54.943  105.214 1.00 20.92 ?  540  LEU A O     1 
ATOM   4046  C CB    . LEU A 1 542  ? -26.492 56.991  104.749 1.00 21.20 ?  540  LEU A CB    1 
ATOM   4047  C CG    . LEU A 1 542  ? -27.110 57.271  103.386 1.00 24.64 ?  540  LEU A CG    1 
ATOM   4048  C CD1   . LEU A 1 542  ? -26.594 58.614  102.884 1.00 18.29 ?  540  LEU A CD1   1 
ATOM   4049  C CD2   . LEU A 1 542  ? -26.846 56.162  102.385 1.00 22.24 ?  540  LEU A CD2   1 
ATOM   4050  N N     . PHE A 1 543  ? -24.871 55.700  107.184 1.00 17.84 ?  541  PHE A N     1 
ATOM   4051  C CA    . PHE A 1 543  ? -23.570 55.647  107.830 1.00 19.70 ?  541  PHE A CA    1 
ATOM   4052  C C     . PHE A 1 543  ? -23.446 54.465  108.776 1.00 20.49 ?  541  PHE A C     1 
ATOM   4053  O O     . PHE A 1 543  ? -22.477 54.390  109.541 1.00 21.85 ?  541  PHE A O     1 
ATOM   4054  C CB    . PHE A 1 543  ? -23.308 56.972  108.541 1.00 19.46 ?  541  PHE A CB    1 
ATOM   4055  C CG    . PHE A 1 543  ? -23.558 58.166  107.656 1.00 16.35 ?  541  PHE A CG    1 
ATOM   4056  C CD1   . PHE A 1 543  ? -22.887 58.293  106.445 1.00 18.86 ?  541  PHE A CD1   1 
ATOM   4057  C CD2   . PHE A 1 543  ? -24.463 59.150  108.025 1.00 17.99 ?  541  PHE A CD2   1 
ATOM   4058  C CE1   . PHE A 1 543  ? -23.121 59.364  105.618 1.00 19.75 ?  541  PHE A CE1   1 
ATOM   4059  C CE2   . PHE A 1 543  ? -24.699 60.234  107.196 1.00 19.15 ?  541  PHE A CE2   1 
ATOM   4060  C CZ    . PHE A 1 543  ? -24.026 60.341  105.994 1.00 18.57 ?  541  PHE A CZ    1 
ATOM   4061  N N     . GLY A 1 544  ? -24.398 53.538  108.728 1.00 18.40 ?  542  GLY A N     1 
ATOM   4062  C CA    . GLY A 1 544  ? -24.296 52.317  109.515 1.00 20.61 ?  542  GLY A CA    1 
ATOM   4063  C C     . GLY A 1 544  ? -24.173 52.599  110.999 1.00 21.84 ?  542  GLY A C     1 
ATOM   4064  O O     . GLY A 1 544  ? -24.882 53.440  111.564 1.00 22.28 ?  542  GLY A O     1 
ATOM   4065  N N     . ASP A 1 545  ? -23.236 51.894  111.639 1.00 24.75 ?  543  ASP A N     1 
ATOM   4066  C CA    . ASP A 1 545  ? -23.044 51.966  113.082 1.00 28.25 ?  543  ASP A CA    1 
ATOM   4067  C C     . ASP A 1 545  ? -22.378 53.253  113.539 1.00 25.57 ?  543  ASP A C     1 
ATOM   4068  O O     . ASP A 1 545  ? -22.387 53.533  114.744 1.00 28.44 ?  543  ASP A O     1 
ATOM   4069  C CB    . ASP A 1 545  ? -22.202 50.780  113.555 1.00 28.26 ?  543  ASP A CB    1 
ATOM   4070  C CG    . ASP A 1 545  ? -22.949 49.468  113.464 1.00 38.39 ?  543  ASP A CG    1 
ATOM   4071  O OD1   . ASP A 1 545  ? -24.196 49.490  113.558 1.00 42.80 ?  543  ASP A OD1   1 
ATOM   4072  O OD2   . ASP A 1 545  ? -22.291 48.416  113.306 1.00 52.47 ?  543  ASP A OD2   1 
ATOM   4073  N N     . ALA A 1 546  ? -21.804 54.031  112.625 1.00 23.65 ?  544  ALA A N     1 
ATOM   4074  C CA    . ALA A 1 546  ? -21.041 55.207  113.027 1.00 23.67 ?  544  ALA A CA    1 
ATOM   4075  C C     . ALA A 1 546  ? -21.951 56.288  113.592 1.00 24.42 ?  544  ALA A C     1 
ATOM   4076  O O     . ALA A 1 546  ? -21.669 56.860  114.649 1.00 23.57 ?  544  ALA A O     1 
ATOM   4077  C CB    . ALA A 1 546  ? -20.236 55.744  111.846 1.00 23.30 ?  544  ALA A CB    1 
ATOM   4078  N N     . ARG A 1 547  ? -23.053 56.577  112.907 1.00 20.14 ?  545  ARG A N     1 
ATOM   4079  C CA    A ARG A 1 547  ? -23.979 57.589  113.389 0.58 21.85 ?  545  ARG A CA    1 
ATOM   4080  C CA    B ARG A 1 547  ? -23.943 57.655  113.324 0.42 21.85 ?  545  ARG A CA    1 
ATOM   4081  C C     . ARG A 1 547  ? -25.267 57.493  112.596 1.00 19.24 ?  545  ARG A C     1 
ATOM   4082  O O     . ARG A 1 547  ? -25.330 56.857  111.541 1.00 18.82 ?  545  ARG A O     1 
ATOM   4083  C CB    A ARG A 1 547  ? -23.396 58.998  113.277 0.58 23.61 ?  545  ARG A CB    1 
ATOM   4084  C CB    B ARG A 1 547  ? -23.338 59.037  113.032 0.42 22.75 ?  545  ARG A CB    1 
ATOM   4085  C CG    A ARG A 1 547  ? -22.911 59.343  111.913 0.58 22.75 ?  545  ARG A CG    1 
ATOM   4086  C CG    B ARG A 1 547  ? -23.172 59.359  111.557 0.42 23.14 ?  545  ARG A CG    1 
ATOM   4087  C CD    A ARG A 1 547  ? -22.318 60.732  111.916 0.58 24.28 ?  545  ARG A CD    1 
ATOM   4088  C CD    B ARG A 1 547  ? -22.683 60.797  111.338 0.42 22.04 ?  545  ARG A CD    1 
ATOM   4089  N NE    A ARG A 1 547  ? -21.606 60.998  110.679 0.58 20.52 ?  545  ARG A NE    1 
ATOM   4090  N NE    B ARG A 1 547  ? -22.536 61.117  109.923 0.42 23.53 ?  545  ARG A NE    1 
ATOM   4091  C CZ    A ARG A 1 547  ? -22.088 61.696  109.656 0.58 19.88 ?  545  ARG A CZ    1 
ATOM   4092  C CZ    B ARG A 1 547  ? -21.492 60.746  109.196 0.42 16.27 ?  545  ARG A CZ    1 
ATOM   4093  N NH1   A ARG A 1 547  ? -23.281 62.265  109.706 0.58 18.52 ?  545  ARG A NH1   1 
ATOM   4094  N NH1   B ARG A 1 547  ? -20.497 60.058  109.728 0.42 18.96 ?  545  ARG A NH1   1 
ATOM   4095  N NH2   A ARG A 1 547  ? -21.348 61.834  108.567 0.58 21.92 ?  545  ARG A NH2   1 
ATOM   4096  N NH2   B ARG A 1 547  ? -21.450 61.065  107.903 0.42 17.90 ?  545  ARG A NH2   1 
ATOM   4097  N N     . THR A 1 548  ? -26.302 58.116  113.146 1.00 18.82 ?  546  THR A N     1 
ATOM   4098  C CA    . THR A 1 548  ? -27.617 58.141  112.528 1.00 18.49 ?  546  THR A CA    1 
ATOM   4099  C C     . THR A 1 548  ? -27.705 59.356  111.621 1.00 17.30 ?  546  THR A C     1 
ATOM   4100  O O     . THR A 1 548  ? -27.417 60.480  112.047 1.00 16.04 ?  546  THR A O     1 
ATOM   4101  C CB    . THR A 1 548  ? -28.717 58.204  113.588 1.00 17.19 ?  546  THR A CB    1 
ATOM   4102  O OG1   . THR A 1 548  ? -28.622 57.066  114.459 1.00 23.25 ?  546  THR A OG1   1 
ATOM   4103  C CG2   . THR A 1 548  ? -30.077 58.224  112.943 1.00 20.18 ?  546  THR A CG2   1 
ATOM   4104  N N     . ASN A 1 549  ? -28.077 59.120  110.362 1.00 15.25 ?  547  ASN A N     1 
ATOM   4105  C CA    . ASN A 1 549  ? -28.266 60.213  109.422 1.00 14.25 ?  547  ASN A CA    1 
ATOM   4106  C C     . ASN A 1 549  ? -29.397 61.112  109.899 1.00 14.68 ?  547  ASN A C     1 
ATOM   4107  O O     . ASN A 1 549  ? -30.380 60.644  110.480 1.00 17.55 ?  547  ASN A O     1 
ATOM   4108  C CB    . ASN A 1 549  ? -28.558 59.645  108.024 1.00 15.74 ?  547  ASN A CB    1 
ATOM   4109  C CG    . ASN A 1 549  ? -28.362 60.662  106.919 1.00 15.54 ?  547  ASN A CG    1 
ATOM   4110  O OD1   . ASN A 1 549  ? -27.849 61.765  107.141 1.00 14.69 ?  547  ASN A OD1   1 
ATOM   4111  N ND2   . ASN A 1 549  ? -28.748 60.285  105.687 1.00 15.97 ?  547  ASN A ND2   1 
ATOM   4112  N N     . SER A 1 550  ? -29.242 62.414  109.682 1.00 14.89 ?  548  SER A N     1 
ATOM   4113  C CA    . SER A 1 550  ? -30.364 63.321  109.895 1.00 15.11 ?  548  SER A CA    1 
ATOM   4114  C C     . SER A 1 550  ? -31.480 63.013  108.905 1.00 17.49 ?  548  SER A C     1 
ATOM   4115  O O     . SER A 1 550  ? -31.248 62.492  107.810 1.00 16.01 ?  548  SER A O     1 
ATOM   4116  C CB    . SER A 1 550  ? -29.920 64.768  109.731 1.00 14.98 ?  548  SER A CB    1 
ATOM   4117  O OG    . SER A 1 550  ? -29.385 64.965  108.425 1.00 15.61 ?  548  SER A OG    1 
ATOM   4118  N N     . ALA A 1 551  ? -32.702 63.348  109.291 1.00 15.96 ?  549  ALA A N     1 
ATOM   4119  C CA    . ALA A 1 551  ? -33.858 63.150  108.426 1.00 17.58 ?  549  ALA A CA    1 
ATOM   4120  C C     . ALA A 1 551  ? -34.336 64.481  107.872 1.00 16.68 ?  549  ALA A C     1 
ATOM   4121  O O     . ALA A 1 551  ? -34.339 65.497  108.571 1.00 16.58 ?  549  ALA A O     1 
ATOM   4122  C CB    . ALA A 1 551  ? -35.002 62.468  109.176 1.00 18.94 ?  549  ALA A CB    1 
ATOM   4123  N N     . GLY A 1 552  ? -34.744 64.470  106.609 1.00 15.51 ?  550  GLY A N     1 
ATOM   4124  C CA    . GLY A 1 552  ? -35.317 65.627  105.971 1.00 17.77 ?  550  GLY A CA    1 
ATOM   4125  C C     . GLY A 1 552  ? -36.827 65.553  105.921 1.00 17.34 ?  550  GLY A C     1 
ATOM   4126  O O     . GLY A 1 552  ? -37.471 64.832  106.691 1.00 20.01 ?  550  GLY A O     1 
ATOM   4127  N N     . LEU A 1 553  ? -37.403 66.319  104.994 1.00 18.50 ?  551  LEU A N     1 
ATOM   4128  C CA    . LEU A 1 553  ? -38.843 66.397  104.812 1.00 17.03 ?  551  LEU A CA    1 
ATOM   4129  C C     . LEU A 1 553  ? -39.127 66.405  103.322 1.00 18.35 ?  551  LEU A C     1 
ATOM   4130  O O     . LEU A 1 553  ? -38.371 67.000  102.549 1.00 20.02 ?  551  LEU A O     1 
ATOM   4131  C CB    . LEU A 1 553  ? -39.433 67.653  105.463 1.00 19.19 ?  551  LEU A CB    1 
ATOM   4132  C CG    . LEU A 1 553  ? -39.361 67.712  106.984 1.00 19.49 ?  551  LEU A CG    1 
ATOM   4133  C CD1   . LEU A 1 553  ? -39.828 69.069  107.487 1.00 23.72 ?  551  LEU A CD1   1 
ATOM   4134  C CD2   . LEU A 1 553  ? -40.228 66.615  107.573 1.00 21.71 ?  551  LEU A CD2   1 
ATOM   4135  N N     . ASP A 1 554  ? -40.207 65.741  102.920 1.00 16.80 ?  552  ASP A N     1 
ATOM   4136  C CA    . ASP A 1 554  ? -40.551 65.617  101.499 1.00 15.99 ?  552  ASP A CA    1 
ATOM   4137  C C     . ASP A 1 554  ? -41.518 66.734  101.121 1.00 15.95 ?  552  ASP A C     1 
ATOM   4138  O O     . ASP A 1 554  ? -42.708 66.669  101.432 1.00 17.08 ?  552  ASP A O     1 
ATOM   4139  C CB    . ASP A 1 554  ? -41.159 64.249  101.213 1.00 18.06 ?  552  ASP A CB    1 
ATOM   4140  C CG    . ASP A 1 554  ? -41.459 64.041  99.742  1.00 19.28 ?  552  ASP A CG    1 
ATOM   4141  O OD1   . ASP A 1 554  ? -41.182 64.956  98.922  1.00 18.59 ?  552  ASP A OD1   1 
ATOM   4142  O OD2   . ASP A 1 554  ? -41.950 62.948  99.399  1.00 19.29 ?  552  ASP A OD2   1 
ATOM   4143  N N     . LEU A 1 555  ? -41.016 67.742  100.413 1.00 15.84 ?  553  LEU A N     1 
ATOM   4144  C CA    . LEU A 1 555  ? -41.867 68.866  100.037 1.00 15.02 ?  553  LEU A CA    1 
ATOM   4145  C C     . LEU A 1 555  ? -42.721 68.572  98.809  1.00 16.17 ?  553  LEU A C     1 
ATOM   4146  O O     . LEU A 1 555  ? -43.357 69.494  98.283  1.00 17.62 ?  553  LEU A O     1 
ATOM   4147  C CB    . LEU A 1 555  ? -41.030 70.121  99.810  1.00 14.03 ?  553  LEU A CB    1 
ATOM   4148  C CG    . LEU A 1 555  ? -40.229 70.548  101.042 1.00 16.56 ?  553  LEU A CG    1 
ATOM   4149  C CD1   . LEU A 1 555  ? -39.463 71.830  100.761 1.00 22.35 ?  553  LEU A CD1   1 
ATOM   4150  C CD2   . LEU A 1 555  ? -41.130 70.718  102.257 1.00 19.57 ?  553  LEU A CD2   1 
ATOM   4151  N N     . SER A 1 556  ? -42.764 67.320  98.354  1.00 16.18 ?  554  SER A N     1 
ATOM   4152  C CA    . SER A 1 556  ? -43.752 66.894  97.370  1.00 14.79 ?  554  SER A CA    1 
ATOM   4153  C C     . SER A 1 556  ? -44.902 66.124  98.003  1.00 16.49 ?  554  SER A C     1 
ATOM   4154  O O     . SER A 1 556  ? -45.829 65.720  97.295  1.00 17.15 ?  554  SER A O     1 
ATOM   4155  C CB    . SER A 1 556  ? -43.101 66.034  96.276  1.00 16.43 ?  554  SER A CB    1 
ATOM   4156  O OG    . SER A 1 556  ? -42.812 64.714  96.746  1.00 17.50 ?  554  SER A OG    1 
ATOM   4157  N N     . ASN A 1 557  ? -44.870 65.920  99.315  1.00 16.44 ?  555  ASN A N     1 
ATOM   4158  C CA    . ASN A 1 557  ? -45.874 65.144  100.027 1.00 15.28 ?  555  ASN A CA    1 
ATOM   4159  C C     . ASN A 1 557  ? -46.916 66.106  100.596 1.00 15.83 ?  555  ASN A C     1 
ATOM   4160  O O     . ASN A 1 557  ? -46.580 66.970  101.412 1.00 15.34 ?  555  ASN A O     1 
ATOM   4161  C CB    . ASN A 1 557  ? -45.203 64.331  101.139 1.00 17.18 ?  555  ASN A CB    1 
ATOM   4162  C CG    . ASN A 1 557  ? -46.172 63.449  101.897 1.00 16.62 ?  555  ASN A CG    1 
ATOM   4163  O OD1   . ASN A 1 557  ? -47.188 63.910  102.403 1.00 18.97 ?  555  ASN A OD1   1 
ATOM   4164  N ND2   . ASN A 1 557  ? -45.844 62.166  101.998 1.00 19.33 ?  555  ASN A ND2   1 
ATOM   4165  N N     . GLU A 1 558  ? -48.178 65.951  100.176 1.00 17.07 ?  556  GLU A N     1 
ATOM   4166  C CA    . GLU A 1 558  ? -49.213 66.881  100.630 1.00 17.07 ?  556  GLU A CA    1 
ATOM   4167  C C     . GLU A 1 558  ? -49.438 66.823  102.134 1.00 17.92 ?  556  GLU A C     1 
ATOM   4168  O O     . GLU A 1 558  ? -49.768 67.846  102.739 1.00 19.16 ?  556  GLU A O     1 
ATOM   4169  C CB    . GLU A 1 558  ? -50.550 66.636  99.922  1.00 19.55 ?  556  GLU A CB    1 
ATOM   4170  C CG    . GLU A 1 558  ? -50.572 66.938  98.424  1.00 18.24 ?  556  GLU A CG    1 
ATOM   4171  C CD    . GLU A 1 558  ? -50.337 68.402  98.045  1.00 18.49 ?  556  GLU A CD    1 
ATOM   4172  O OE1   . GLU A 1 558  ? -50.392 69.330  98.888  1.00 18.94 ?  556  GLU A OE1   1 
ATOM   4173  O OE2   . GLU A 1 558  ? -50.111 68.625  96.838  1.00 17.56 ?  556  GLU A OE2   1 
ATOM   4174  N N     . GLU A 1 559  ? -49.307 65.646  102.753 1.00 15.81 ?  557  GLU A N     1 
ATOM   4175  C CA    . GLU A 1 559  ? -49.429 65.584  104.207 1.00 17.46 ?  557  GLU A CA    1 
ATOM   4176  C C     . GLU A 1 559  ? -48.337 66.420  104.857 1.00 18.17 ?  557  GLU A C     1 
ATOM   4177  O O     . GLU A 1 559  ? -48.598 67.193  105.789 1.00 21.39 ?  557  GLU A O     1 
ATOM   4178  C CB    . GLU A 1 559  ? -49.351 64.138  104.696 1.00 23.20 ?  557  GLU A CB    1 
ATOM   4179  C CG    . GLU A 1 559  ? -50.472 63.216  104.253 1.00 24.22 ?  557  GLU A CG    1 
ATOM   4180  C CD    . GLU A 1 559  ? -50.208 61.767  104.658 1.00 31.21 ?  557  GLU A CD    1 
ATOM   4181  O OE1   . GLU A 1 559  ? -49.215 61.515  105.380 1.00 40.35 ?  557  GLU A OE1   1 
ATOM   4182  O OE2   . GLU A 1 559  ? -50.980 60.875  104.258 1.00 29.89 ?  557  GLU A OE2   1 
ATOM   4183  N N     . THR A 1 560  ? -47.104 66.283  104.364 1.00 16.96 ?  558  THR A N     1 
ATOM   4184  C CA    . THR A 1 560  ? -45.997 67.072  104.891 1.00 18.19 ?  558  THR A CA    1 
ATOM   4185  C C     . THR A 1 560  ? -46.217 68.559  104.672 1.00 18.64 ?  558  THR A C     1 
ATOM   4186  O O     . THR A 1 560  ? -45.978 69.367  105.572 1.00 18.24 ?  558  THR A O     1 
ATOM   4187  C CB    . THR A 1 560  ? -44.693 66.637  104.230 1.00 17.48 ?  558  THR A CB    1 
ATOM   4188  O OG1   . THR A 1 560  ? -44.479 65.247  104.485 1.00 19.94 ?  558  THR A OG1   1 
ATOM   4189  C CG2   . THR A 1 560  ? -43.522 67.448  104.759 1.00 19.39 ?  558  THR A CG2   1 
ATOM   4190  N N     . LEU A 1 561  ? -46.661 68.946  103.476 1.00 16.86 ?  559  LEU A N     1 
ATOM   4191  C CA    . LEU A 1 561  ? -46.878 70.363  103.217 1.00 15.60 ?  559  LEU A CA    1 
ATOM   4192  C C     . LEU A 1 561  ? -47.956 70.927  104.127 1.00 19.74 ?  559  LEU A C     1 
ATOM   4193  O O     . LEU A 1 561  ? -47.851 72.068  104.587 1.00 19.37 ?  559  LEU A O     1 
ATOM   4194  C CB    . LEU A 1 561  ? -47.247 70.583  101.747 1.00 16.01 ?  559  LEU A CB    1 
ATOM   4195  C CG    . LEU A 1 561  ? -46.077 70.304  100.805 1.00 16.77 ?  559  LEU A CG    1 
ATOM   4196  C CD1   . LEU A 1 561  ? -46.556 70.395  99.372  1.00 16.11 ?  559  LEU A CD1   1 
ATOM   4197  C CD2   . LEU A 1 561  ? -44.937 71.282  101.050 1.00 16.04 ?  559  LEU A CD2   1 
ATOM   4198  N N     . ALA A 1 562  ? -48.997 70.143  104.406 1.00 17.74 ?  560  ALA A N     1 
ATOM   4199  C CA    . ALA A 1 562  ? -50.085 70.654  105.231 1.00 19.49 ?  560  ALA A CA    1 
ATOM   4200  C C     . ALA A 1 562  ? -49.644 70.795  106.679 1.00 20.40 ?  560  ALA A C     1 
ATOM   4201  O O     . ALA A 1 562  ? -49.983 71.783  107.342 1.00 21.61 ?  560  ALA A O     1 
ATOM   4202  C CB    . ALA A 1 562  ? -51.312 69.747  105.114 1.00 20.88 ?  560  ALA A CB    1 
ATOM   4203  N N     . SER A 1 563  ? -48.887 69.821  107.189 1.00 20.44 ?  561  SER A N     1 
ATOM   4204  C CA    . SER A 1 563  ? -48.441 69.918  108.574 1.00 23.15 ?  561  SER A CA    1 
ATOM   4205  C C     . SER A 1 563  ? -47.371 70.993  108.725 1.00 20.06 ?  561  SER A C     1 
ATOM   4206  O O     . SER A 1 563  ? -47.355 71.725  109.722 1.00 23.32 ?  561  SER A O     1 
ATOM   4207  C CB    . SER A 1 563  ? -47.948 68.552  109.062 1.00 23.37 ?  561  SER A CB    1 
ATOM   4208  O OG    . SER A 1 563  ? -46.744 68.181  108.441 1.00 29.38 ?  561  SER A OG    1 
ATOM   4209  N N     . LEU A 1 564  ? -46.483 71.118  107.731 1.00 21.65 ?  562  LEU A N     1 
ATOM   4210  C CA    A LEU A 1 564  ? -45.498 72.191  107.758 0.51 20.33 ?  562  LEU A CA    1 
ATOM   4211  C CA    B LEU A 1 564  ? -45.498 72.197  107.742 0.49 20.33 ?  562  LEU A CA    1 
ATOM   4212  C C     . LEU A 1 564  ? -46.171 73.560  107.722 1.00 20.26 ?  562  LEU A C     1 
ATOM   4213  O O     . LEU A 1 564  ? -45.773 74.473  108.455 1.00 20.90 ?  562  LEU A O     1 
ATOM   4214  C CB    A LEU A 1 564  ? -44.525 72.023  106.588 0.51 21.21 ?  562  LEU A CB    1 
ATOM   4215  C CB    B LEU A 1 564  ? -44.556 72.068  106.543 0.49 21.22 ?  562  LEU A CB    1 
ATOM   4216  C CG    A LEU A 1 564  ? -43.264 72.875  106.596 0.51 19.93 ?  562  LEU A CG    1 
ATOM   4217  C CG    B LEU A 1 564  ? -43.229 71.361  106.768 0.49 20.14 ?  562  LEU A CG    1 
ATOM   4218  C CD1   A LEU A 1 564  ? -42.512 72.680  107.897 0.51 21.43 ?  562  LEU A CD1   1 
ATOM   4219  C CD1   B LEU A 1 564  ? -42.418 71.350  105.489 0.49 19.08 ?  562  LEU A CD1   1 
ATOM   4220  C CD2   A LEU A 1 564  ? -42.386 72.516  105.406 0.51 17.72 ?  562  LEU A CD2   1 
ATOM   4221  C CD2   B LEU A 1 564  ? -42.461 72.046  107.884 0.49 22.00 ?  562  LEU A CD2   1 
ATOM   4222  N N     . THR A 1 565  ? -47.195 73.720  106.880 1.00 19.47 ?  563  THR A N     1 
ATOM   4223  C CA    . THR A 1 565  ? -47.910 74.989  106.833 1.00 20.91 ?  563  THR A CA    1 
ATOM   4224  C C     . THR A 1 565  ? -48.346 75.406  108.229 1.00 21.12 ?  563  THR A C     1 
ATOM   4225  O O     . THR A 1 565  ? -48.148 76.557  108.633 1.00 23.27 ?  563  THR A O     1 
ATOM   4226  C CB    . THR A 1 565  ? -49.125 74.889  105.907 1.00 18.59 ?  563  THR A CB    1 
ATOM   4227  O OG1   . THR A 1 565  ? -48.681 74.735  104.549 1.00 20.52 ?  563  THR A OG1   1 
ATOM   4228  C CG2   . THR A 1 565  ? -49.966 76.152  106.006 1.00 21.99 ?  563  THR A CG2   1 
ATOM   4229  N N     . GLU A 1 566  ? -48.882 74.461  109.004 1.00 22.49 ?  564  GLU A N     1 
ATOM   4230  C CA    . GLU A 1 566  ? -49.380 74.805  110.330 1.00 22.95 ?  564  GLU A CA    1 
ATOM   4231  C C     . GLU A 1 566  ? -48.235 75.095  111.290 1.00 22.97 ?  564  GLU A C     1 
ATOM   4232  O O     . GLU A 1 566  ? -48.305 76.043  112.081 1.00 23.14 ?  564  GLU A O     1 
ATOM   4233  C CB    . GLU A 1 566  ? -50.272 73.682  110.864 1.00 26.56 ?  564  GLU A CB    1 
ATOM   4234  C CG    . GLU A 1 566  ? -51.530 73.459  110.022 1.00 27.05 ?  564  GLU A CG    1 
ATOM   4235  C CD    . GLU A 1 566  ? -52.328 74.738  109.821 1.00 39.14 ?  564  GLU A CD    1 
ATOM   4236  O OE1   . GLU A 1 566  ? -52.559 75.459  110.819 1.00 41.33 ?  564  GLU A OE1   1 
ATOM   4237  O OE2   . GLU A 1 566  ? -52.710 75.029  108.661 1.00 38.46 ?  564  GLU A OE2   1 
ATOM   4238  N N     . ALA A 1 567  ? -47.164 74.305  111.224 1.00 21.83 ?  565  ALA A N     1 
ATOM   4239  C CA    . ALA A 1 567  ? -46.044 74.525  112.131 1.00 21.67 ?  565  ALA A CA    1 
ATOM   4240  C C     . ALA A 1 567  ? -45.333 75.834  111.817 1.00 21.44 ?  565  ALA A C     1 
ATOM   4241  O O     . ALA A 1 567  ? -44.876 76.534  112.730 1.00 23.31 ?  565  ALA A O     1 
ATOM   4242  C CB    . ALA A 1 567  ? -45.075 73.347  112.066 1.00 22.98 ?  565  ALA A CB    1 
ATOM   4243  N N     . LEU A 1 568  ? -45.224 76.181  110.533 1.00 20.45 ?  566  LEU A N     1 
ATOM   4244  C CA    . LEU A 1 568  ? -44.607 77.451  110.165 1.00 20.13 ?  566  LEU A CA    1 
ATOM   4245  C C     . LEU A 1 568  ? -45.445 78.627  110.658 1.00 21.62 ?  566  LEU A C     1 
ATOM   4246  O O     . LEU A 1 568  ? -44.911 79.580  111.241 1.00 21.95 ?  566  LEU A O     1 
ATOM   4247  C CB    . LEU A 1 568  ? -44.402 77.516  108.646 1.00 19.98 ?  566  LEU A CB    1 
ATOM   4248  C CG    . LEU A 1 568  ? -43.415 76.487  108.080 1.00 21.54 ?  566  LEU A CG    1 
ATOM   4249  C CD1   . LEU A 1 568  ? -43.400 76.525  106.552 1.00 20.83 ?  566  LEU A CD1   1 
ATOM   4250  C CD2   . LEU A 1 568  ? -42.021 76.714  108.637 1.00 22.50 ?  566  LEU A CD2   1 
ATOM   4251  N N     . ARG A 1 569  ? -46.764 78.575  110.436 1.00 21.41 ?  567  ARG A N     1 
ATOM   4252  C CA    . ARG A 1 569  ? -47.651 79.623  110.939 1.00 22.34 ?  567  ARG A CA    1 
ATOM   4253  C C     . ARG A 1 569  ? -47.515 79.781  112.442 1.00 25.75 ?  567  ARG A C     1 
ATOM   4254  O O     . ARG A 1 569  ? -47.451 80.904  112.955 1.00 25.65 ?  567  ARG A O     1 
ATOM   4255  C CB    . ARG A 1 569  ? -49.103 79.305  110.588 1.00 28.29 ?  567  ARG A CB    1 
ATOM   4256  C CG    . ARG A 1 569  ? -49.450 79.524  109.140 1.00 30.01 ?  567  ARG A CG    1 
ATOM   4257  C CD    . ARG A 1 569  ? -50.914 79.195  108.884 1.00 38.81 ?  567  ARG A CD    1 
ATOM   4258  N NE    . ARG A 1 569  ? -51.198 79.111  107.457 1.00 37.43 ?  567  ARG A NE    1 
ATOM   4259  C CZ    . ARG A 1 569  ? -52.348 78.686  106.950 1.00 41.27 ?  567  ARG A CZ    1 
ATOM   4260  N NH1   . ARG A 1 569  ? -53.334 78.276  107.729 1.00 46.67 ?  567  ARG A NH1   1 
ATOM   4261  N NH2   . ARG A 1 569  ? -52.509 78.671  105.628 1.00 40.91 ?  567  ARG A NH2   1 
ATOM   4262  N N     . GLU A 1 570  ? -47.468 78.661  113.162 1.00 23.26 ?  568  GLU A N     1 
ATOM   4263  C CA    . GLU A 1 570  ? -47.327 78.723  114.608 1.00 25.47 ?  568  GLU A CA    1 
ATOM   4264  C C     . GLU A 1 570  ? -45.979 79.298  115.018 1.00 27.64 ?  568  GLU A C     1 
ATOM   4265  O O     . GLU A 1 570  ? -45.900 80.019  116.019 1.00 28.95 ?  568  GLU A O     1 
ATOM   4266  C CB    . GLU A 1 570  ? -47.542 77.332  115.200 1.00 27.93 ?  568  GLU A CB    1 
ATOM   4267  C CG    . GLU A 1 570  ? -48.996 76.879  115.118 1.00 35.28 ?  568  GLU A CG    1 
ATOM   4268  C CD    . GLU A 1 570  ? -49.154 75.379  115.268 1.00 42.08 ?  568  GLU A CD    1 
ATOM   4269  O OE1   . GLU A 1 570  ? -48.134 74.662  115.173 1.00 43.09 ?  568  GLU A OE1   1 
ATOM   4270  O OE2   . GLU A 1 570  ? -50.299 74.919  115.477 1.00 48.04 ?  568  GLU A OE2   1 
ATOM   4271  N N     . SER A 1 571  ? -44.917 79.013  114.252 1.00 25.48 ?  569  SER A N     1 
ATOM   4272  C CA    . SER A 1 571  ? -43.610 79.580  114.575 1.00 26.24 ?  569  SER A CA    1 
ATOM   4273  C C     . SER A 1 571  ? -43.614 81.096  114.443 1.00 24.82 ?  569  SER A C     1 
ATOM   4274  O O     . SER A 1 571  ? -42.885 81.777  115.168 1.00 27.44 ?  569  SER A O     1 
ATOM   4275  C CB    . SER A 1 571  ? -42.526 78.974  113.677 1.00 24.82 ?  569  SER A CB    1 
ATOM   4276  O OG    . SER A 1 571  ? -42.511 79.591  112.400 1.00 27.20 ?  569  SER A OG    1 
ATOM   4277  N N     . ALA A 1 572  ? -44.418 81.643  113.529 1.00 26.43 ?  570  ALA A N     1 
ATOM   4278  C CA    . ALA A 1 572  ? -44.438 83.085  113.317 1.00 25.42 ?  570  ALA A CA    1 
ATOM   4279  C C     . ALA A 1 572  ? -45.230 83.821  114.387 1.00 29.33 ?  570  ALA A C     1 
ATOM   4280  O O     . ALA A 1 572  ? -45.081 85.040  114.526 1.00 30.66 ?  570  ALA A O     1 
ATOM   4281  C CB    . ALA A 1 572  ? -45.006 83.405  111.932 1.00 28.57 ?  570  ALA A CB    1 
ATOM   4282  N N     . ALA A 1 573  ? -46.049 83.109  115.150 1.00 27.87 ?  571  ALA A N     1 
ATOM   4283  C CA    . ALA A 1 573  ? -46.811 83.679  116.251 1.00 30.27 ?  571  ALA A CA    1 
ATOM   4284  C C     . ALA A 1 573  ? -46.032 83.699  117.560 1.00 33.63 ?  571  ALA A C     1 
ATOM   4285  O O     . ALA A 1 573  ? -46.568 84.152  118.577 1.00 38.94 ?  571  ALA A O     1 
ATOM   4286  C CB    . ALA A 1 573  ? -48.114 82.898  116.435 1.00 31.09 ?  571  ALA A CB    1 
ATOM   4287  N N     . MET A 1 574  ? -44.791 83.223  117.560 1.00 29.37 ?  572  MET A N     1 
ATOM   4288  C CA    . MET A 1 574  ? -43.998 83.130  118.775 1.00 31.30 ?  572  MET A CA    1 
ATOM   4289  C C     . MET A 1 574  ? -43.181 84.396  118.984 1.00 32.59 ?  572  MET A C     1 
ATOM   4290  O O     . MET A 1 574  ? -42.777 85.062  118.026 1.00 29.29 ?  572  MET A O     1 
ATOM   4291  C CB    . MET A 1 574  ? -43.065 81.922  118.719 1.00 31.61 ?  572  MET A CB    1 
ATOM   4292  C CG    . MET A 1 574  ? -43.781 80.597  118.811 1.00 32.81 ?  572  MET A CG    1 
ATOM   4293  S SD    . MET A 1 574  ? -42.700 79.227  118.410 1.00 38.88 ?  572  MET A SD    1 
ATOM   4294  C CE    . MET A 1 574  ? -43.781 77.843  118.768 1.00 44.93 ?  572  MET A CE    1 
ATOM   4295  N N     . LYS A 1 575  ? -42.925 84.709  120.258 1.00 31.99 ?  573  LYS A N     1 
ATOM   4296  C CA    . LYS A 1 575  ? -42.123 85.873  120.645 1.00 32.43 ?  573  LYS A CA    1 
ATOM   4297  C C     . LYS A 1 575  ? -40.677 85.431  120.853 1.00 30.80 ?  573  LYS A C     1 
ATOM   4298  O O     . LYS A 1 575  ? -40.215 85.183  121.971 1.00 34.91 ?  573  LYS A O     1 
ATOM   4299  C CB    . LYS A 1 575  ? -42.695 86.532  121.896 1.00 35.67 ?  573  LYS A CB    1 
ATOM   4300  C CG    . LYS A 1 575  ? -44.117 87.043  121.728 1.00 40.32 ?  573  LYS A CG    1 
ATOM   4301  C CD    . LYS A 1 575  ? -44.210 88.039  120.582 1.00 41.58 ?  573  LYS A CD    1 
ATOM   4302  N N     . TRP A 1 576  ? -39.952 85.349  119.743 1.00 29.35 ?  574  TRP A N     1 
ATOM   4303  C CA    . TRP A 1 576  ? -38.556 84.934  119.768 1.00 26.87 ?  574  TRP A CA    1 
ATOM   4304  C C     . TRP A 1 576  ? -37.672 86.024  120.361 1.00 22.69 ?  574  TRP A C     1 
ATOM   4305  O O     . TRP A 1 576  ? -37.823 87.206  120.041 1.00 27.31 ?  574  TRP A O     1 
ATOM   4306  C CB    . TRP A 1 576  ? -38.086 84.621  118.355 1.00 26.76 ?  574  TRP A CB    1 
ATOM   4307  C CG    . TRP A 1 576  ? -38.797 83.495  117.692 1.00 22.71 ?  574  TRP A CG    1 
ATOM   4308  C CD1   . TRP A 1 576  ? -39.754 83.585  116.716 1.00 27.01 ?  574  TRP A CD1   1 
ATOM   4309  C CD2   . TRP A 1 576  ? -38.594 82.099  117.929 1.00 21.66 ?  574  TRP A CD2   1 
ATOM   4310  N NE1   . TRP A 1 576  ? -40.153 82.328  116.334 1.00 25.81 ?  574  TRP A NE1   1 
ATOM   4311  C CE2   . TRP A 1 576  ? -39.460 81.398  117.063 1.00 24.44 ?  574  TRP A CE2   1 
ATOM   4312  C CE3   . TRP A 1 576  ? -37.756 81.372  118.781 1.00 22.62 ?  574  TRP A CE3   1 
ATOM   4313  C CZ2   . TRP A 1 576  ? -39.518 80.006  117.029 1.00 27.03 ?  574  TRP A CZ2   1 
ATOM   4314  C CZ3   . TRP A 1 576  ? -37.814 79.988  118.748 1.00 25.55 ?  574  TRP A CZ3   1 
ATOM   4315  C CH2   . TRP A 1 576  ? -38.692 79.318  117.879 1.00 27.66 ?  574  TRP A CH2   1 
ATOM   4316  N N     . THR A 1 577  ? -36.750 85.632  121.240 1.00 23.39 ?  575  THR A N     1 
ATOM   4317  C CA    . THR A 1 577  ? -35.818 86.592  121.813 1.00 24.65 ?  575  THR A CA    1 
ATOM   4318  C C     . THR A 1 577  ? -34.423 85.989  121.877 1.00 25.97 ?  575  THR A C     1 
ATOM   4319  O O     . THR A 1 577  ? -34.242 84.768  121.838 1.00 24.62 ?  575  THR A O     1 
ATOM   4320  C CB    . THR A 1 577  ? -36.222 87.056  123.225 1.00 24.10 ?  575  THR A CB    1 
ATOM   4321  O OG1   . THR A 1 577  ? -36.033 85.985  124.162 1.00 29.32 ?  575  THR A OG1   1 
ATOM   4322  C CG2   . THR A 1 577  ? -37.677 87.540  123.268 1.00 29.48 ?  575  THR A CG2   1 
ATOM   4323  N N     . ALA A 1 578  ? -33.434 86.874  121.971 1.00 24.96 ?  576  ALA A N     1 
ATOM   4324  C CA    . ALA A 1 578  ? -32.041 86.496  122.177 1.00 23.23 ?  576  ALA A CA    1 
ATOM   4325  C C     . ALA A 1 578  ? -31.465 87.450  123.206 1.00 26.30 ?  576  ALA A C     1 
ATOM   4326  O O     . ALA A 1 578  ? -31.613 88.668  123.072 1.00 26.39 ?  576  ALA A O     1 
ATOM   4327  C CB    . ALA A 1 578  ? -31.227 86.561  120.878 1.00 24.40 ?  576  ALA A CB    1 
ATOM   4328  N N     . LEU A 1 579  ? -30.826 86.898  124.227 1.00 25.54 ?  577  LEU A N     1 
ATOM   4329  C CA    . LEU A 1 579  ? -30.318 87.656  125.358 1.00 27.45 ?  577  LEU A CA    1 
ATOM   4330  C C     . LEU A 1 579  ? -28.860 87.311  125.587 1.00 26.83 ?  577  LEU A C     1 
ATOM   4331  O O     . LEU A 1 579  ? -28.400 86.236  125.188 1.00 25.46 ?  577  LEU A O     1 
ATOM   4332  C CB    . LEU A 1 579  ? -31.118 87.342  126.630 1.00 29.50 ?  577  LEU A CB    1 
ATOM   4333  C CG    . LEU A 1 579  ? -32.631 87.481  126.537 1.00 31.33 ?  577  LEU A CG    1 
ATOM   4334  C CD1   . LEU A 1 579  ? -33.249 87.089  127.863 1.00 38.59 ?  577  LEU A CD1   1 
ATOM   4335  C CD2   . LEU A 1 579  ? -32.991 88.904  126.168 1.00 35.55 ?  577  LEU A CD2   1 
ATOM   4336  N N     . PRO A 1 580  ? -28.098 88.201  126.230 1.00 27.52 ?  578  PRO A N     1 
ATOM   4337  C CA    . PRO A 1 580  ? -26.768 87.801  126.695 1.00 26.04 ?  578  PRO A CA    1 
ATOM   4338  C C     . PRO A 1 580  ? -26.927 86.794  127.816 1.00 31.12 ?  578  PRO A C     1 
ATOM   4339  O O     . PRO A 1 580  ? -27.332 87.161  128.923 1.00 31.03 ?  578  PRO A O     1 
ATOM   4340  C CB    . PRO A 1 580  ? -26.139 89.114  127.184 1.00 28.52 ?  578  PRO A CB    1 
ATOM   4341  C CG    . PRO A 1 580  ? -27.060 90.212  126.704 1.00 28.29 ?  578  PRO A CG    1 
ATOM   4342  C CD    . PRO A 1 580  ? -28.409 89.592  126.596 1.00 26.14 ?  578  PRO A CD    1 
ATOM   4343  N N     . GLN A 1 581  ? -26.671 85.523  127.525 1.00 24.76 ?  579  GLN A N     1 
ATOM   4344  C CA    . GLN A 1 581  ? -26.872 84.429  128.473 1.00 27.53 ?  579  GLN A CA    1 
ATOM   4345  C C     . GLN A 1 581  ? -25.524 84.098  129.092 1.00 27.53 ?  579  GLN A C     1 
ATOM   4346  O O     . GLN A 1 581  ? -24.773 83.273  128.578 1.00 26.77 ?  579  GLN A O     1 
ATOM   4347  C CB    . GLN A 1 581  ? -27.480 83.215  127.777 1.00 26.19 ?  579  GLN A CB    1 
ATOM   4348  C CG    . GLN A 1 581  ? -28.844 83.467  127.164 1.00 24.42 ?  579  GLN A CG    1 
ATOM   4349  C CD    . GLN A 1 581  ? -29.947 83.622  128.205 1.00 30.77 ?  579  GLN A CD    1 
ATOM   4350  O OE1   . GLN A 1 581  ? -29.712 83.503  129.413 1.00 32.71 ?  579  GLN A OE1   1 
ATOM   4351  N NE2   . GLN A 1 581  ? -31.162 83.888  127.736 1.00 30.71 ?  579  GLN A NE2   1 
ATOM   4352  N N     . LEU A 1 582  ? -25.220 84.750  130.210 1.00 27.18 ?  580  LEU A N     1 
ATOM   4353  C CA    . LEU A 1 582  ? -23.974 84.512  130.910 1.00 27.77 ?  580  LEU A CA    1 
ATOM   4354  C C     . LEU A 1 582  ? -24.103 83.288  131.821 1.00 30.54 ?  580  LEU A C     1 
ATOM   4355  O O     . LEU A 1 582  ? -25.188 82.727  132.009 1.00 28.82 ?  580  LEU A O     1 
ATOM   4356  C CB    . LEU A 1 582  ? -23.574 85.762  131.693 1.00 27.79 ?  580  LEU A CB    1 
ATOM   4357  C CG    . LEU A 1 582  ? -22.745 86.810  130.933 1.00 37.90 ?  580  LEU A CG    1 
ATOM   4358  C CD1   . LEU A 1 582  ? -23.469 87.363  129.713 1.00 34.34 ?  580  LEU A CD1   1 
ATOM   4359  C CD2   . LEU A 1 582  ? -22.343 87.945  131.859 1.00 36.87 ?  580  LEU A CD2   1 
ATOM   4360  N N     . ALA A 1 583  ? -22.968 82.859  132.377 1.00 27.78 ?  581  ALA A N     1 
ATOM   4361  C CA    . ALA A 1 583  ? -22.985 81.723  133.294 1.00 30.22 ?  581  ALA A CA    1 
ATOM   4362  C C     . ALA A 1 583  ? -23.884 81.993  134.489 1.00 32.23 ?  581  ALA A C     1 
ATOM   4363  O O     . ALA A 1 583  ? -24.535 81.076  134.998 1.00 38.97 ?  581  ALA A O     1 
ATOM   4364  C CB    . ALA A 1 583  ? -21.571 81.404  133.774 1.00 29.72 ?  581  ALA A CB    1 
ATOM   4365  N N     . THR A 1 584  ? -23.946 83.251  134.924 1.00 29.25 ?  582  THR A N     1 
ATOM   4366  C CA    . THR A 1 584  ? -24.702 83.689  136.091 1.00 33.46 ?  582  THR A CA    1 
ATOM   4367  C C     . THR A 1 584  ? -26.178 83.902  135.797 1.00 31.43 ?  582  THR A C     1 
ATOM   4368  O O     . THR A 1 584  ? -26.956 84.100  136.738 1.00 34.85 ?  582  THR A O     1 
ATOM   4369  C CB    . THR A 1 584  ? -24.108 84.996  136.622 1.00 36.88 ?  582  THR A CB    1 
ATOM   4370  O OG1   . THR A 1 584  ? -23.994 85.940  135.548 1.00 35.87 ?  582  THR A OG1   1 
ATOM   4371  C CG2   . THR A 1 584  ? -22.734 84.764  137.246 1.00 37.43 ?  582  THR A CG2   1 
ATOM   4372  N N     . GLY A 1 585  ? -26.572 83.880  134.523 1.00 33.42 ?  583  GLY A N     1 
ATOM   4373  C CA    . GLY A 1 585  ? -27.930 84.154  134.119 1.00 32.93 ?  583  GLY A CA    1 
ATOM   4374  C C     . GLY A 1 585  ? -27.977 85.166  132.991 1.00 33.91 ?  583  GLY A C     1 
ATOM   4375  O O     . GLY A 1 585  ? -26.942 85.650  132.519 1.00 34.40 ?  583  GLY A O     1 
ATOM   4376  N N     . PRO A 1 586  ? -29.184 85.500  132.532 1.00 28.93 ?  584  PRO A N     1 
ATOM   4377  C CA    . PRO A 1 586  ? -29.322 86.524  131.491 1.00 29.79 ?  584  PRO A CA    1 
ATOM   4378  C C     . PRO A 1 586  ? -28.855 87.879  131.993 1.00 36.05 ?  584  PRO A C     1 
ATOM   4379  O O     . PRO A 1 586  ? -28.959 88.196  133.180 1.00 35.18 ?  584  PRO A O     1 
ATOM   4380  C CB    . PRO A 1 586  ? -30.827 86.537  131.193 1.00 37.38 ?  584  PRO A CB    1 
ATOM   4381  C CG    . PRO A 1 586  ? -31.408 85.363  131.939 1.00 38.31 ?  584  PRO A CG    1 
ATOM   4382  C CD    . PRO A 1 586  ? -30.489 85.075  133.064 1.00 35.72 ?  584  PRO A CD    1 
ATOM   4383  N N     . ALA A 1 587  ? -28.357 88.693  131.067 1.00 32.19 ?  585  ALA A N     1 
ATOM   4384  C CA    . ALA A 1 587  ? -27.833 90.013  131.384 1.00 35.52 ?  585  ALA A CA    1 
ATOM   4385  C C     . ALA A 1 587  ? -28.661 91.085  130.689 1.00 36.86 ?  585  ALA A C     1 
ATOM   4386  O O     . ALA A 1 587  ? -29.287 90.838  129.655 1.00 35.30 ?  585  ALA A O     1 
ATOM   4387  C CB    . ALA A 1 587  ? -26.362 90.147  130.975 1.00 34.90 ?  585  ALA A CB    1 
ATOM   4388  N N     . ALA A 1 588  ? -28.674 92.279  131.278 1.00 35.38 ?  586  ALA A N     1 
ATOM   4389  C CA    . ALA A 1 588  ? -29.364 93.405  130.671 1.00 36.41 ?  586  ALA A CA    1 
ATOM   4390  C C     . ALA A 1 588  ? -28.500 94.044  129.586 1.00 34.84 ?  586  ALA A C     1 
ATOM   4391  O O     . ALA A 1 588  ? -27.276 93.894  129.560 1.00 37.89 ?  586  ALA A O     1 
ATOM   4392  C CB    . ALA A 1 588  ? -29.728 94.448  131.729 1.00 36.42 ?  586  ALA A CB    1 
ATOM   4393  N N     . GLY A 1 589  ? -29.156 94.768  128.687 1.00 35.04 ?  587  GLY A N     1 
ATOM   4394  C CA    . GLY A 1 589  ? -28.439 95.431  127.613 1.00 33.34 ?  587  GLY A CA    1 
ATOM   4395  C C     . GLY A 1 589  ? -29.383 96.222  126.732 1.00 35.05 ?  587  GLY A C     1 
ATOM   4396  O O     . GLY A 1 589  ? -30.570 96.370  127.033 1.00 39.49 ?  587  GLY A O     1 
ATOM   4397  N N     . GLU A 1 590  ? -28.830 96.738  125.634 1.00 34.84 ?  588  GLU A N     1 
ATOM   4398  C CA    . GLU A 1 590  ? -29.621 97.465  124.648 1.00 36.46 ?  588  GLU A CA    1 
ATOM   4399  C C     . GLU A 1 590  ? -30.428 96.479  123.812 1.00 32.89 ?  588  GLU A C     1 
ATOM   4400  O O     . GLU A 1 590  ? -29.876 95.521  123.260 1.00 34.93 ?  588  GLU A O     1 
ATOM   4401  C CB    . GLU A 1 590  ? -28.720 98.310  123.748 1.00 38.30 ?  588  GLU A CB    1 
ATOM   4402  N N     . THR A 1 591  ? -31.733 96.718  123.721 1.00 33.26 ?  589  THR A N     1 
ATOM   4403  C CA    . THR A 1 591  ? -32.669 95.813  123.068 1.00 34.24 ?  589  THR A CA    1 
ATOM   4404  C C     . THR A 1 591  ? -33.193 96.445  121.784 1.00 30.33 ?  589  THR A C     1 
ATOM   4405  O O     . THR A 1 591  ? -33.584 97.616  121.781 1.00 36.15 ?  589  THR A O     1 
ATOM   4406  C CB    . THR A 1 591  ? -33.831 95.478  124.012 1.00 32.65 ?  589  THR A CB    1 
ATOM   4407  O OG1   . THR A 1 591  ? -33.333 94.795  125.173 1.00 32.00 ?  589  THR A OG1   1 
ATOM   4408  C CG2   . THR A 1 591  ? -34.838 94.603  123.323 1.00 34.97 ?  589  THR A CG2   1 
ATOM   4409  N N     . ARG A 1 592  ? -33.197 95.672  120.694 1.00 30.90 ?  590  ARG A N     1 
ATOM   4410  C CA    . ARG A 1 592  ? -33.759 96.131  119.432 1.00 32.33 ?  590  ARG A CA    1 
ATOM   4411  C C     . ARG A 1 592  ? -34.429 94.956  118.732 1.00 30.53 ?  590  ARG A C     1 
ATOM   4412  O O     . ARG A 1 592  ? -34.216 93.797  119.090 1.00 30.25 ?  590  ARG A O     1 
ATOM   4413  C CB    . ARG A 1 592  ? -32.693 96.758  118.526 1.00 35.60 ?  590  ARG A CB    1 
ATOM   4414  C CG    . ARG A 1 592  ? -31.559 95.821  118.156 1.00 35.42 ?  590  ARG A CG    1 
ATOM   4415  C CD    . ARG A 1 592  ? -30.914 96.226  116.830 1.00 43.43 ?  590  ARG A CD    1 
ATOM   4416  N NE    . ARG A 1 592  ? -29.881 95.285  116.411 1.00 45.15 ?  590  ARG A NE    1 
ATOM   4417  C CZ    . ARG A 1 592  ? -30.094 94.220  115.648 1.00 41.93 ?  590  ARG A CZ    1 
ATOM   4418  N NH1   . ARG A 1 592  ? -31.298 93.933  115.178 1.00 37.53 ?  590  ARG A NH1   1 
ATOM   4419  N NH2   . ARG A 1 592  ? -29.073 93.420  115.354 1.00 39.85 ?  590  ARG A NH2   1 
ATOM   4420  N N     . THR A 1 593  ? -35.257 95.268  117.739 1.00 29.51 ?  591  THR A N     1 
ATOM   4421  C CA    . THR A 1 593  ? -36.009 94.238  117.039 1.00 27.24 ?  591  THR A CA    1 
ATOM   4422  C C     . THR A 1 593  ? -35.192 93.628  115.902 1.00 30.78 ?  591  THR A C     1 
ATOM   4423  O O     . THR A 1 593  ? -34.216 94.207  115.412 1.00 30.62 ?  591  THR A O     1 
ATOM   4424  C CB    . THR A 1 593  ? -37.318 94.790  116.477 1.00 35.18 ?  591  THR A CB    1 
ATOM   4425  O OG1   . THR A 1 593  ? -37.034 95.823  115.521 1.00 34.61 ?  591  THR A OG1   1 
ATOM   4426  C CG2   . THR A 1 593  ? -38.179 95.345  117.596 1.00 35.25 ?  591  THR A CG2   1 
ATOM   4427  N N     . VAL A 1 594  ? -35.620 92.441  115.482 1.00 24.39 ?  592  VAL A N     1 
ATOM   4428  C CA    . VAL A 1 594  ? -35.009 91.703  114.382 1.00 27.02 ?  592  VAL A CA    1 
ATOM   4429  C C     . VAL A 1 594  ? -36.049 91.607  113.278 1.00 26.94 ?  592  VAL A C     1 
ATOM   4430  O O     . VAL A 1 594  ? -37.155 91.098  113.504 1.00 27.49 ?  592  VAL A O     1 
ATOM   4431  C CB    . VAL A 1 594  ? -34.540 90.309  114.823 1.00 24.58 ?  592  VAL A CB    1 
ATOM   4432  C CG1   . VAL A 1 594  ? -33.904 89.563  113.665 1.00 22.50 ?  592  VAL A CG1   1 
ATOM   4433  C CG2   . VAL A 1 594  ? -33.553 90.423  115.984 1.00 26.36 ?  592  VAL A CG2   1 
ATOM   4434  N N     . LEU A 1 595  ? -35.704 92.098  112.091 1.00 25.97 ?  593  LEU A N     1 
ATOM   4435  C CA    . LEU A 1 595  ? -36.641 92.204  110.983 1.00 26.89 ?  593  LEU A CA    1 
ATOM   4436  C C     . LEU A 1 595  ? -36.401 91.116  109.941 1.00 24.10 ?  593  LEU A C     1 
ATOM   4437  O O     . LEU A 1 595  ? -35.272 90.664  109.733 1.00 26.53 ?  593  LEU A O     1 
ATOM   4438  C CB    . LEU A 1 595  ? -36.531 93.579  110.323 1.00 25.90 ?  593  LEU A CB    1 
ATOM   4439  C CG    . LEU A 1 595  ? -36.710 94.736  111.303 1.00 29.84 ?  593  LEU A CG    1 
ATOM   4440  C CD1   . LEU A 1 595  ? -36.581 96.075  110.595 1.00 27.88 ?  593  LEU A CD1   1 
ATOM   4441  C CD2   . LEU A 1 595  ? -38.048 94.616  112.006 1.00 27.84 ?  593  LEU A CD2   1 
ATOM   4442  N N     . ASN A 1 596  ? -37.482 90.710  109.283 1.00 25.27 ?  594  ASN A N     1 
ATOM   4443  C CA    . ASN A 1 596  ? -37.421 89.760  108.171 1.00 24.45 ?  594  ASN A CA    1 
ATOM   4444  C C     . ASN A 1 596  ? -36.733 90.405  106.970 1.00 20.28 ?  594  ASN A C     1 
ATOM   4445  O O     . ASN A 1 596  ? -37.216 91.432  106.474 1.00 22.61 ?  594  ASN A O     1 
ATOM   4446  C CB    . ASN A 1 596  ? -38.856 89.338  107.823 1.00 23.71 ?  594  ASN A CB    1 
ATOM   4447  C CG    . ASN A 1 596  ? -38.936 88.234  106.773 1.00 24.56 ?  594  ASN A CG    1 
ATOM   4448  O OD1   . ASN A 1 596  ? -38.060 88.078  105.916 1.00 21.98 ?  594  ASN A OD1   1 
ATOM   4449  N ND2   . ASN A 1 596  ? -40.016 87.462  106.834 1.00 26.34 ?  594  ASN A ND2   1 
ATOM   4450  N N     . PRO A 1 597  ? -35.621 89.861  106.470 1.00 21.08 ?  595  PRO A N     1 
ATOM   4451  C CA    . PRO A 1 597  ? -34.966 90.492  105.311 1.00 20.27 ?  595  PRO A CA    1 
ATOM   4452  C C     . PRO A 1 597  ? -35.839 90.548  104.069 1.00 22.07 ?  595  PRO A C     1 
ATOM   4453  O O     . PRO A 1 597  ? -35.608 91.410  103.211 1.00 20.92 ?  595  PRO A O     1 
ATOM   4454  C CB    . PRO A 1 597  ? -33.714 89.629  105.085 1.00 21.55 ?  595  PRO A CB    1 
ATOM   4455  C CG    . PRO A 1 597  ? -33.917 88.402  105.883 1.00 25.52 ?  595  PRO A CG    1 
ATOM   4456  C CD    . PRO A 1 597  ? -34.848 88.721  106.995 1.00 18.62 ?  595  PRO A CD    1 
ATOM   4457  N N     . GLY A 1 598  ? -36.851 89.688  103.960 1.00 20.30 ?  596  GLY A N     1 
ATOM   4458  C CA    . GLY A 1 598  ? -37.728 89.720  102.805 1.00 19.75 ?  596  GLY A CA    1 
ATOM   4459  C C     . GLY A 1 598  ? -38.903 90.663  102.920 1.00 23.61 ?  596  GLY A C     1 
ATOM   4460  O O     . GLY A 1 598  ? -39.635 90.852  101.942 1.00 23.67 ?  596  GLY A O     1 
ATOM   4461  N N     . ASP A 1 599  ? -39.090 91.262  104.093 1.00 21.99 ?  597  ASP A N     1 
ATOM   4462  C CA    . ASP A 1 599  ? -40.196 92.169  104.368 1.00 23.56 ?  597  ASP A CA    1 
ATOM   4463  C C     . ASP A 1 599  ? -39.963 92.797  105.734 1.00 24.23 ?  597  ASP A C     1 
ATOM   4464  O O     . ASP A 1 599  ? -40.301 92.200  106.764 1.00 23.98 ?  597  ASP A O     1 
ATOM   4465  C CB    . ASP A 1 599  ? -41.528 91.423  104.334 1.00 23.08 ?  597  ASP A CB    1 
ATOM   4466  C CG    . ASP A 1 599  ? -42.729 92.353  104.377 1.00 27.44 ?  597  ASP A CG    1 
ATOM   4467  O OD1   . ASP A 1 599  ? -42.595 93.499  104.855 1.00 27.46 ?  597  ASP A OD1   1 
ATOM   4468  O OD2   . ASP A 1 599  ? -43.808 91.924  103.918 1.00 30.62 ?  597  ASP A OD2   1 
ATOM   4469  N N     . HIS A 1 600  ? -39.384 94.001  105.749 1.00 24.65 ?  598  HIS A N     1 
ATOM   4470  C CA    . HIS A 1 600  ? -38.976 94.637  106.998 1.00 22.86 ?  598  HIS A CA    1 
ATOM   4471  C C     . HIS A 1 600  ? -40.150 94.978  107.909 1.00 27.68 ?  598  HIS A C     1 
ATOM   4472  O O     . HIS A 1 600  ? -39.927 95.373  109.060 1.00 29.72 ?  598  HIS A O     1 
ATOM   4473  C CB    . HIS A 1 600  ? -38.167 95.896  106.700 1.00 25.16 ?  598  HIS A CB    1 
ATOM   4474  C CG    . HIS A 1 600  ? -36.779 95.617  106.223 1.00 27.64 ?  598  HIS A CG    1 
ATOM   4475  N ND1   . HIS A 1 600  ? -35.894 96.615  105.877 1.00 28.19 ?  598  HIS A ND1   1 
ATOM   4476  C CD2   . HIS A 1 600  ? -36.119 94.447  106.039 1.00 25.48 ?  598  HIS A CD2   1 
ATOM   4477  C CE1   . HIS A 1 600  ? -34.750 96.073  105.495 1.00 29.80 ?  598  HIS A CE1   1 
ATOM   4478  N NE2   . HIS A 1 600  ? -34.859 94.759  105.586 1.00 27.10 ?  598  HIS A NE2   1 
ATOM   4479  N N     . ARG A 1 601  ? -41.382 94.831  107.423 1.00 26.52 ?  599  ARG A N     1 
ATOM   4480  C CA    . ARG A 1 601  ? -42.560 95.020  108.259 1.00 28.29 ?  599  ARG A CA    1 
ATOM   4481  C C     . ARG A 1 601  ? -42.785 93.845  109.201 1.00 31.01 ?  599  ARG A C     1 
ATOM   4482  O O     . ARG A 1 601  ? -43.516 93.983  110.189 1.00 31.05 ?  599  ARG A O     1 
ATOM   4483  C CB    . ARG A 1 601  ? -43.790 95.218  107.372 1.00 26.69 ?  599  ARG A CB    1 
ATOM   4484  C CG    . ARG A 1 601  ? -43.639 96.310  106.336 1.00 30.35 ?  599  ARG A CG    1 
ATOM   4485  C CD    . ARG A 1 601  ? -44.813 96.313  105.383 1.00 28.09 ?  599  ARG A CD    1 
ATOM   4486  N NE    . ARG A 1 601  ? -44.874 95.077  104.611 1.00 27.96 ?  599  ARG A NE    1 
ATOM   4487  C CZ    . ARG A 1 601  ? -45.760 94.835  103.656 1.00 30.68 ?  599  ARG A CZ    1 
ATOM   4488  N NH1   . ARG A 1 601  ? -46.684 95.725  103.328 1.00 32.41 ?  599  ARG A NH1   1 
ATOM   4489  N NH2   . ARG A 1 601  ? -45.719 93.671  103.013 1.00 28.17 ?  599  ARG A NH2   1 
ATOM   4490  N N     . ASP A 1 602  ? -42.180 92.698  108.909 1.00 26.77 ?  600  ASP A N     1 
ATOM   4491  C CA    . ASP A 1 602  ? -42.365 91.478  109.687 1.00 29.28 ?  600  ASP A CA    1 
ATOM   4492  C C     . ASP A 1 602  ? -41.304 91.462  110.778 1.00 31.18 ?  600  ASP A C     1 
ATOM   4493  O O     . ASP A 1 602  ? -40.139 91.151  110.523 1.00 29.51 ?  600  ASP A O     1 
ATOM   4494  C CB    . ASP A 1 602  ? -42.265 90.257  108.780 1.00 28.09 ?  600  ASP A CB    1 
ATOM   4495  C CG    . ASP A 1 602  ? -42.461 88.955  109.520 1.00 30.82 ?  600  ASP A CG    1 
ATOM   4496  O OD1   . ASP A 1 602  ? -43.048 88.977  110.615 1.00 33.23 ?  600  ASP A OD1   1 
ATOM   4497  O OD2   . ASP A 1 602  ? -42.015 87.905  109.000 1.00 30.88 ?  600  ASP A OD2   1 
ATOM   4498  N N     . VAL A 1 603  ? -41.702 91.817  111.995 1.00 29.80 ?  601  VAL A N     1 
ATOM   4499  C CA    . VAL A 1 603  ? -40.812 91.739  113.148 1.00 24.72 ?  601  VAL A CA    1 
ATOM   4500  C C     . VAL A 1 603  ? -40.744 90.283  113.596 1.00 28.66 ?  601  VAL A C     1 
ATOM   4501  O O     . VAL A 1 603  ? -41.762 89.691  113.970 1.00 32.56 ?  601  VAL A O     1 
ATOM   4502  C CB    . VAL A 1 603  ? -41.294 92.656  114.284 1.00 28.17 ?  601  VAL A CB    1 
ATOM   4503  C CG1   . VAL A 1 603  ? -40.329 92.615  115.467 1.00 26.93 ?  601  VAL A CG1   1 
ATOM   4504  C CG2   . VAL A 1 603  ? -41.447 94.077  113.777 1.00 31.84 ?  601  VAL A CG2   1 
ATOM   4505  N N     . VAL A 1 604  ? -39.550 89.694  113.532 1.00 24.95 ?  602  VAL A N     1 
ATOM   4506  C CA    . VAL A 1 604  ? -39.393 88.289  113.898 1.00 23.22 ?  602  VAL A CA    1 
ATOM   4507  C C     . VAL A 1 604  ? -39.153 88.126  115.398 1.00 26.23 ?  602  VAL A C     1 
ATOM   4508  O O     . VAL A 1 604  ? -39.616 87.150  116.001 1.00 24.32 ?  602  VAL A O     1 
ATOM   4509  C CB    . VAL A 1 604  ? -38.254 87.655  113.080 1.00 23.80 ?  602  VAL A CB    1 
ATOM   4510  C CG1   . VAL A 1 604  ? -38.150 86.161  113.378 1.00 21.96 ?  602  VAL A CG1   1 
ATOM   4511  C CG2   . VAL A 1 604  ? -38.477 87.895  111.586 1.00 27.49 ?  602  VAL A CG2   1 
ATOM   4512  N N     . GLY A 1 605  ? -38.456 89.064  116.022 1.00 24.85 ?  603  GLY A N     1 
ATOM   4513  C CA    . GLY A 1 605  ? -38.210 88.947  117.442 1.00 23.94 ?  603  GLY A CA    1 
ATOM   4514  C C     . GLY A 1 605  ? -37.413 90.121  117.954 1.00 25.91 ?  603  GLY A C     1 
ATOM   4515  O O     . GLY A 1 605  ? -37.289 91.152  117.292 1.00 27.10 ?  603  GLY A O     1 
ATOM   4516  N N     . SER A 1 606  ? -36.868 89.943  119.149 1.00 25.48 ?  604  SER A N     1 
ATOM   4517  C CA    A SER A 1 606  ? -36.126 90.993  119.829 0.53 27.05 ?  604  SER A CA    1 
ATOM   4518  C CA    B SER A 1 606  ? -36.130 90.990  119.831 0.47 27.04 ?  604  SER A CA    1 
ATOM   4519  C C     . SER A 1 606  ? -34.796 90.445  120.315 1.00 26.92 ?  604  SER A C     1 
ATOM   4520  O O     . SER A 1 606  ? -34.718 89.309  120.791 1.00 29.66 ?  604  SER A O     1 
ATOM   4521  C CB    A SER A 1 606  ? -36.916 91.561  121.011 0.53 28.61 ?  604  SER A CB    1 
ATOM   4522  C CB    B SER A 1 606  ? -36.933 91.532  121.006 0.47 28.61 ?  604  SER A CB    1 
ATOM   4523  O OG    A SER A 1 606  ? -38.170 92.063  120.587 0.53 29.41 ?  604  SER A OG    1 
ATOM   4524  O OG    B SER A 1 606  ? -36.286 92.646  121.571 0.47 29.81 ?  604  SER A OG    1 
ATOM   4525  N N     . VAL A 1 607  ? -33.749 91.255  120.194 1.00 23.67 ?  605  VAL A N     1 
ATOM   4526  C CA    . VAL A 1 607  ? -32.416 90.874  120.643 1.00 24.99 ?  605  VAL A CA    1 
ATOM   4527  C C     . VAL A 1 607  ? -31.926 91.910  121.644 1.00 27.47 ?  605  VAL A C     1 
ATOM   4528  O O     . VAL A 1 607  ? -32.040 93.118  121.409 1.00 26.87 ?  605  VAL A O     1 
ATOM   4529  C CB    . VAL A 1 607  ? -31.428 90.723  119.466 1.00 27.35 ?  605  VAL A CB    1 
ATOM   4530  C CG1   . VAL A 1 607  ? -31.379 91.991  118.614 1.00 24.03 ?  605  VAL A CG1   1 
ATOM   4531  C CG2   . VAL A 1 607  ? -30.051 90.374  119.994 1.00 24.40 ?  605  VAL A CG2   1 
ATOM   4532  N N     . THR A 1 608  ? -31.407 91.433  122.770 1.00 26.20 ?  606  THR A N     1 
ATOM   4533  C CA    . THR A 1 608  ? -30.688 92.256  123.731 1.00 28.11 ?  606  THR A CA    1 
ATOM   4534  C C     . THR A 1 608  ? -29.201 91.996  123.545 1.00 30.30 ?  606  THR A C     1 
ATOM   4535  O O     . THR A 1 608  ? -28.744 90.859  123.705 1.00 27.30 ?  606  THR A O     1 
ATOM   4536  C CB    . THR A 1 608  ? -31.116 91.924  125.158 1.00 29.80 ?  606  THR A CB    1 
ATOM   4537  O OG1   . THR A 1 608  ? -32.516 92.191  125.301 1.00 31.13 ?  606  THR A OG1   1 
ATOM   4538  C CG2   . THR A 1 608  ? -30.327 92.759  126.162 1.00 33.06 ?  606  THR A CG2   1 
ATOM   4539  N N     . GLU A 1 609  ? -28.450 93.036  123.213 1.00 29.57 ?  607  GLU A N     1 
ATOM   4540  C CA    . GLU A 1 609  ? -27.055 92.863  122.844 1.00 31.43 ?  607  GLU A CA    1 
ATOM   4541  C C     . GLU A 1 609  ? -26.125 93.073  124.039 1.00 30.94 ?  607  GLU A C     1 
ATOM   4542  O O     . GLU A 1 609  ? -26.479 93.699  125.043 1.00 30.60 ?  607  GLU A O     1 
ATOM   4543  C CB    . GLU A 1 609  ? -26.708 93.792  121.674 1.00 34.87 ?  607  GLU A CB    1 
ATOM   4544  C CG    . GLU A 1 609  ? -27.398 93.319  120.381 1.00 37.42 ?  607  GLU A CG    1 
ATOM   4545  C CD    . GLU A 1 609  ? -27.199 94.240  119.187 1.00 41.09 ?  607  GLU A CD    1 
ATOM   4546  O OE1   . GLU A 1 609  ? -27.110 95.472  119.386 1.00 42.89 ?  607  GLU A OE1   1 
ATOM   4547  O OE2   . GLU A 1 609  ? -27.142 93.721  118.043 1.00 39.88 ?  607  GLU A OE2   1 
ATOM   4548  N N     . THR A 1 610  ? -24.932 92.500  123.924 1.00 30.48 ?  608  THR A N     1 
ATOM   4549  C CA    . THR A 1 610  ? -23.979 92.398  125.022 1.00 29.29 ?  608  THR A CA    1 
ATOM   4550  C C     . THR A 1 610  ? -23.103 93.639  125.097 1.00 29.96 ?  608  THR A C     1 
ATOM   4551  O O     . THR A 1 610  ? -22.601 94.117  124.078 1.00 32.09 ?  608  THR A O     1 
ATOM   4552  C CB    . THR A 1 610  ? -23.080 91.167  124.835 1.00 31.09 ?  608  THR A CB    1 
ATOM   4553  O OG1   . THR A 1 610  ? -23.874 90.021  124.502 1.00 28.14 ?  608  THR A OG1   1 
ATOM   4554  C CG2   . THR A 1 610  ? -22.270 90.874  126.092 1.00 28.75 ?  608  THR A CG2   1 
ATOM   4555  N N     . SER A 1 611  ? -22.906 94.149  126.312 1.00 31.28 ?  609  SER A N     1 
ATOM   4556  C CA    . SER A 1 611  ? -21.914 95.193  126.521 1.00 34.14 ?  609  SER A CA    1 
ATOM   4557  C C     . SER A 1 611  ? -20.510 94.603  126.460 1.00 33.45 ?  609  SER A C     1 
ATOM   4558  O O     . SER A 1 611  ? -20.303 93.409  126.706 1.00 33.65 ?  609  SER A O     1 
ATOM   4559  C CB    . SER A 1 611  ? -22.123 95.876  127.870 1.00 32.93 ?  609  SER A CB    1 
ATOM   4560  O OG    . SER A 1 611  ? -21.732 95.015  128.925 1.00 36.46 ?  609  SER A OG    1 
ATOM   4561  N N     . GLU A 1 612  ? -19.536 95.451  126.122 1.00 35.01 ?  610  GLU A N     1 
ATOM   4562  C CA    . GLU A 1 612  ? -18.154 94.981  126.108 1.00 36.14 ?  610  GLU A CA    1 
ATOM   4563  C C     . GLU A 1 612  ? -17.720 94.513  127.490 1.00 35.39 ?  610  GLU A C     1 
ATOM   4564  O O     . GLU A 1 612  ? -16.923 93.574  127.607 1.00 36.23 ?  610  GLU A O     1 
ATOM   4565  C CB    . GLU A 1 612  ? -17.220 96.079  125.601 1.00 39.36 ?  610  GLU A CB    1 
ATOM   4566  C CG    . GLU A 1 612  ? -17.299 96.322  124.103 1.00 41.14 ?  610  GLU A CG    1 
ATOM   4567  C CD    . GLU A 1 612  ? -16.444 97.494  123.659 1.00 48.45 ?  610  GLU A CD    1 
ATOM   4568  O OE1   . GLU A 1 612  ? -15.864 98.176  124.533 1.00 55.94 ?  610  GLU A OE1   1 
ATOM   4569  O OE2   . GLU A 1 612  ? -16.353 97.735  122.436 1.00 54.07 ?  610  GLU A OE2   1 
ATOM   4570  N N     . GLU A 1 613  ? -18.251 95.139  128.541 1.00 36.00 ?  611  GLU A N     1 
ATOM   4571  C CA    . GLU A 1 613  ? -17.910 94.731  129.898 1.00 35.03 ?  611  GLU A CA    1 
ATOM   4572  C C     . GLU A 1 613  ? -18.432 93.332  130.201 1.00 32.16 ?  611  GLU A C     1 
ATOM   4573  O O     . GLU A 1 613  ? -17.718 92.515  130.791 1.00 32.46 ?  611  GLU A O     1 
ATOM   4574  C CB    . GLU A 1 613  ? -18.463 95.750  130.894 1.00 36.92 ?  611  GLU A CB    1 
ATOM   4575  C CG    . GLU A 1 613  ? -18.193 95.431  132.355 1.00 40.47 ?  611  GLU A CG    1 
ATOM   4576  C CD    . GLU A 1 613  ? -18.743 96.504  133.283 1.00 52.79 ?  611  GLU A CD    1 
ATOM   4577  O OE1   . GLU A 1 613  ? -18.096 97.564  133.416 1.00 54.24 ?  611  GLU A OE1   1 
ATOM   4578  O OE2   . GLU A 1 613  ? -19.832 96.296  133.861 1.00 49.33 ?  611  GLU A OE2   1 
ATOM   4579  N N     . ASP A 1 614  ? -19.668 93.029  129.792 1.00 32.91 ?  612  ASP A N     1 
ATOM   4580  C CA    . ASP A 1 614  ? -20.214 91.697  130.046 1.00 31.33 ?  612  ASP A CA    1 
ATOM   4581  C C     . ASP A 1 614  ? -19.560 90.641  129.166 1.00 31.74 ?  612  ASP A C     1 
ATOM   4582  O O     . ASP A 1 614  ? -19.488 89.470  129.554 1.00 27.92 ?  612  ASP A O     1 
ATOM   4583  C CB    . ASP A 1 614  ? -21.726 91.694  129.843 1.00 30.76 ?  612  ASP A CB    1 
ATOM   4584  C CG    . ASP A 1 614  ? -22.473 92.293  131.025 1.00 35.09 ?  612  ASP A CG    1 
ATOM   4585  O OD1   . ASP A 1 614  ? -21.851 92.489  132.093 1.00 35.42 ?  612  ASP A OD1   1 
ATOM   4586  O OD2   . ASP A 1 614  ? -23.682 92.566  130.880 1.00 38.85 ?  612  ASP A OD2   1 
ATOM   4587  N N     . ALA A 1 615  ? -19.076 91.028  127.988 1.00 26.02 ?  613  ALA A N     1 
ATOM   4588  C CA    . ALA A 1 615  ? -18.315 90.081  127.182 1.00 29.52 ?  613  ALA A CA    1 
ATOM   4589  C C     . ALA A 1 615  ? -17.019 89.698  127.882 1.00 27.36 ?  613  ALA A C     1 
ATOM   4590  O O     . ALA A 1 615  ? -16.664 88.516  127.941 1.00 28.18 ?  613  ALA A O     1 
ATOM   4591  C CB    . ALA A 1 615  ? -18.035 90.665  125.799 1.00 29.42 ?  613  ALA A CB    1 
ATOM   4592  N N     . ARG A 1 616  ? -16.316 90.681  128.451 1.00 30.23 ?  614  ARG A N     1 
ATOM   4593  C CA    . ARG A 1 616  ? -15.117 90.366  129.222 1.00 32.19 ?  614  ARG A CA    1 
ATOM   4594  C C     . ARG A 1 616  ? -15.455 89.553  130.466 1.00 28.29 ?  614  ARG A C     1 
ATOM   4595  O O     . ARG A 1 616  ? -14.726 88.614  130.809 1.00 28.96 ?  614  ARG A O     1 
ATOM   4596  C CB    . ARG A 1 616  ? -14.373 91.653  129.580 1.00 32.05 ?  614  ARG A CB    1 
ATOM   4597  C CG    . ARG A 1 616  ? -13.616 92.226  128.386 1.00 40.73 ?  614  ARG A CG    1 
ATOM   4598  C CD    . ARG A 1 616  ? -12.714 93.383  128.766 1.00 45.59 ?  614  ARG A CD    1 
ATOM   4599  N NE    . ARG A 1 616  ? -13.468 94.614  128.962 1.00 47.61 ?  614  ARG A NE    1 
ATOM   4600  C CZ    . ARG A 1 616  ? -13.775 95.465  127.991 1.00 51.16 ?  614  ARG A CZ    1 
ATOM   4601  N NH1   . ARG A 1 616  ? -13.403 95.251  126.738 1.00 49.62 ?  614  ARG A NH1   1 
ATOM   4602  N NH2   . ARG A 1 616  ? -14.476 96.557  128.285 1.00 48.68 ?  614  ARG A NH2   1 
ATOM   4603  N N     . ARG A 1 617  ? -16.571 89.875  131.133 1.00 28.07 ?  615  ARG A N     1 
ATOM   4604  C CA    . ARG A 1 617  ? -17.012 89.073  132.274 1.00 32.20 ?  615  ARG A CA    1 
ATOM   4605  C C     . ARG A 1 617  ? -17.252 87.625  131.871 1.00 26.56 ?  615  ARG A C     1 
ATOM   4606  O O     . ARG A 1 617  ? -16.875 86.699  132.599 1.00 27.17 ?  615  ARG A O     1 
ATOM   4607  C CB    . ARG A 1 617  ? -18.292 89.654  132.883 1.00 33.02 ?  615  ARG A CB    1 
ATOM   4608  C CG    . ARG A 1 617  ? -18.127 90.958  133.643 1.00 40.35 ?  615  ARG A CG    1 
ATOM   4609  C CD    . ARG A 1 617  ? -19.125 91.076  134.799 1.00 45.44 ?  615  ARG A CD    1 
ATOM   4610  N NE    . ARG A 1 617  ? -20.511 91.219  134.363 1.00 48.54 ?  615  ARG A NE    1 
ATOM   4611  C CZ    . ARG A 1 617  ? -21.466 90.318  134.563 1.00 46.34 ?  615  ARG A CZ    1 
ATOM   4612  N NH1   . ARG A 1 617  ? -21.212 89.157  135.147 1.00 47.88 ?  615  ARG A NH1   1 
ATOM   4613  N NH2   . ARG A 1 617  ? -22.711 90.597  134.187 1.00 41.40 ?  615  ARG A NH2   1 
ATOM   4614  N N     . ALA A 1 618  ? -17.887 87.410  130.715 1.00 27.94 ?  616  ALA A N     1 
ATOM   4615  C CA    . ALA A 1 618  ? -18.218 86.053  130.293 1.00 27.09 ?  616  ALA A CA    1 
ATOM   4616  C C     . ALA A 1 618  ? -16.967 85.207  130.097 1.00 24.34 ?  616  ALA A C     1 
ATOM   4617  O O     . ALA A 1 618  ? -16.951 84.021  130.450 1.00 25.57 ?  616  ALA A O     1 
ATOM   4618  C CB    . ALA A 1 618  ? -19.054 86.090  129.014 1.00 25.02 ?  616  ALA A CB    1 
ATOM   4619  N N     . VAL A 1 619  ? -15.907 85.787  129.527 1.00 23.74 ?  617  VAL A N     1 
ATOM   4620  C CA    . VAL A 1 619  ? -14.667 85.030  129.376 1.00 27.33 ?  617  VAL A CA    1 
ATOM   4621  C C     . VAL A 1 619  ? -14.112 84.637  130.740 1.00 24.21 ?  617  VAL A C     1 
ATOM   4622  O O     . VAL A 1 619  ? -13.682 83.493  130.941 1.00 26.17 ?  617  VAL A O     1 
ATOM   4623  C CB    . VAL A 1 619  ? -13.642 85.823  128.545 1.00 27.53 ?  617  VAL A CB    1 
ATOM   4624  C CG1   . VAL A 1 619  ? -12.361 85.015  128.382 1.00 27.53 ?  617  VAL A CG1   1 
ATOM   4625  C CG2   . VAL A 1 619  ? -14.219 86.162  127.170 1.00 24.66 ?  617  VAL A CG2   1 
ATOM   4626  N N     . ARG A 1 620  ? -14.138 85.561  131.708 1.00 28.00 ?  618  ARG A N     1 
ATOM   4627  C CA    . ARG A 1 620  ? -13.655 85.220  133.045 1.00 28.12 ?  618  ARG A CA    1 
ATOM   4628  C C     . ARG A 1 620  ? -14.482 84.099  133.657 1.00 27.24 ?  618  ARG A C     1 
ATOM   4629  O O     . ARG A 1 620  ? -13.927 83.169  134.255 1.00 29.03 ?  618  ARG A O     1 
ATOM   4630  C CB    . ARG A 1 620  ? -13.660 86.450  133.953 1.00 32.67 ?  618  ARG A CB    1 
ATOM   4631  C CG    . ARG A 1 620  ? -12.598 87.484  133.610 1.00 36.53 ?  618  ARG A CG    1 
ATOM   4632  C CD    . ARG A 1 620  ? -12.445 88.531  134.714 1.00 43.79 ?  618  ARG A CD    1 
ATOM   4633  N NE    . ARG A 1 620  ? -13.631 89.372  134.847 1.00 51.16 ?  618  ARG A NE    1 
ATOM   4634  C CZ    . ARG A 1 620  ? -13.857 90.466  134.130 1.00 46.53 ?  618  ARG A CZ    1 
ATOM   4635  N NH1   . ARG A 1 620  ? -12.993 90.889  133.222 1.00 48.34 ?  618  ARG A NH1   1 
ATOM   4636  N NH2   . ARG A 1 620  ? -14.976 91.154  134.333 1.00 48.37 ?  618  ARG A NH2   1 
ATOM   4637  N N     . LEU A 1 621  ? -15.811 84.159  133.504 1.00 25.61 ?  619  LEU A N     1 
ATOM   4638  C CA    . LEU A 1 621  ? -16.666 83.093  134.017 1.00 28.00 ?  619  LEU A CA    1 
ATOM   4639  C C     . LEU A 1 621  ? -16.374 81.762  133.333 1.00 25.89 ?  619  LEU A C     1 
ATOM   4640  O O     . LEU A 1 621  ? -16.376 80.710  133.984 1.00 29.59 ?  619  LEU A O     1 
ATOM   4641  C CB    . LEU A 1 621  ? -18.138 83.465  133.837 1.00 26.16 ?  619  LEU A CB    1 
ATOM   4642  C CG    . LEU A 1 621  ? -18.634 84.661  134.640 1.00 27.91 ?  619  LEU A CG    1 
ATOM   4643  C CD1   . LEU A 1 621  ? -20.021 85.089  134.180 1.00 27.30 ?  619  LEU A CD1   1 
ATOM   4644  C CD2   . LEU A 1 621  ? -18.654 84.293  136.117 1.00 29.76 ?  619  LEU A CD2   1 
ATOM   4645  N N     . ALA A 1 622  ? -16.128 81.785  132.017 1.00 26.03 ?  620  ALA A N     1 
ATOM   4646  C CA    . ALA A 1 622  ? -15.799 80.553  131.302 1.00 24.26 ?  620  ALA A CA    1 
ATOM   4647  C C     . ALA A 1 622  ? -14.470 79.977  131.778 1.00 23.23 ?  620  ALA A C     1 
ATOM   4648  O O     . ALA A 1 622  ? -14.316 78.755  131.889 1.00 24.93 ?  620  ALA A O     1 
ATOM   4649  C CB    . ALA A 1 622  ? -15.752 80.806  129.793 1.00 23.74 ?  620  ALA A CB    1 
ATOM   4650  N N     . ALA A 1 623  ? -13.488 80.840  132.033 1.00 24.99 ?  621  ALA A N     1 
ATOM   4651  C CA    . ALA A 1 623  ? -12.219 80.354  132.551 1.00 28.01 ?  621  ALA A CA    1 
ATOM   4652  C C     . ALA A 1 623  ? -12.400 79.725  133.928 1.00 28.65 ?  621  ALA A C     1 
ATOM   4653  O O     . ALA A 1 623  ? -11.826 78.667  134.211 1.00 25.45 ?  621  ALA A O     1 
ATOM   4654  C CB    . ALA A 1 623  ? -11.201 81.493  132.594 1.00 28.35 ?  621  ALA A CB    1 
ATOM   4655  N N     . ASP A 1 624  ? -13.218 80.348  134.784 1.00 27.72 ?  622  ASP A N     1 
ATOM   4656  C CA    . ASP A 1 624  ? -13.495 79.795  136.110 1.00 34.43 ?  622  ASP A CA    1 
ATOM   4657  C C     . ASP A 1 624  ? -14.123 78.412  136.018 1.00 33.14 ?  622  ASP A C     1 
ATOM   4658  O O     . ASP A 1 624  ? -13.813 77.522  136.821 1.00 35.86 ?  622  ASP A O     1 
ATOM   4659  C CB    . ASP A 1 624  ? -14.433 80.722  136.884 1.00 32.55 ?  622  ASP A CB    1 
ATOM   4660  C CG    . ASP A 1 624  ? -13.754 81.988  137.354 1.00 43.57 ?  622  ASP A CG    1 
ATOM   4661  O OD1   . ASP A 1 624  ? -12.513 82.082  137.241 1.00 45.86 ?  622  ASP A OD1   1 
ATOM   4662  O OD2   . ASP A 1 624  ? -14.471 82.891  137.844 1.00 53.12 ?  622  ASP A OD2   1 
ATOM   4663  N N     . ALA A 1 625  ? -15.016 78.222  135.057 1.00 34.42 ?  623  ALA A N     1 
ATOM   4664  C CA    . ALA A 1 625  ? -15.782 76.995  134.907 1.00 38.12 ?  623  ALA A CA    1 
ATOM   4665  C C     . ALA A 1 625  ? -15.108 75.966  134.017 1.00 31.35 ?  623  ALA A C     1 
ATOM   4666  O O     . ALA A 1 625  ? -15.666 74.881  133.822 1.00 34.37 ?  623  ALA A O     1 
ATOM   4667  C CB    . ALA A 1 625  ? -17.162 77.316  134.337 1.00 41.94 ?  623  ALA A CB    1 
ATOM   4668  N N     . ALA A 1 626  ? -13.940 76.277  133.456 1.00 28.34 ?  624  ALA A N     1 
ATOM   4669  C CA    . ALA A 1 626  ? -13.315 75.350  132.515 1.00 28.81 ?  624  ALA A CA    1 
ATOM   4670  C C     . ALA A 1 626  ? -12.964 74.007  133.145 1.00 31.57 ?  624  ALA A C     1 
ATOM   4671  O O     . ALA A 1 626  ? -13.243 72.969  132.520 1.00 27.82 ?  624  ALA A O     1 
ATOM   4672  C CB    . ALA A 1 626  ? -12.091 76.014  131.878 1.00 26.33 ?  624  ALA A CB    1 
ATOM   4673  N N     . PRO A 1 627  ? -12.367 73.933  134.344 1.00 30.71 ?  625  PRO A N     1 
ATOM   4674  C CA    . PRO A 1 627  ? -12.068 72.603  134.907 1.00 29.31 ?  625  PRO A CA    1 
ATOM   4675  C C     . PRO A 1 627  ? -13.298 71.724  135.083 1.00 26.60 ?  625  PRO A C     1 
ATOM   4676  O O     . PRO A 1 627  ? -13.215 70.506  134.863 1.00 31.68 ?  625  PRO A O     1 
ATOM   4677  C CB    . PRO A 1 627  ? -11.415 72.937  136.257 1.00 31.10 ?  625  PRO A CB    1 
ATOM   4678  C CG    . PRO A 1 627  ? -10.859 74.312  136.075 1.00 31.57 ?  625  PRO A CG    1 
ATOM   4679  C CD    . PRO A 1 627  ? -11.842 75.016  135.201 1.00 32.69 ?  625  PRO A CD    1 
ATOM   4680  N N     . ASP A 1 628  ? -14.446 72.306  135.440 1.00 27.52 ?  626  ASP A N     1 
ATOM   4681  C CA    . ASP A 1 628  ? -15.630 71.489  135.685 1.00 25.56 ?  626  ASP A CA    1 
ATOM   4682  C C     . ASP A 1 628  ? -16.177 70.897  134.394 1.00 29.39 ?  626  ASP A C     1 
ATOM   4683  O O     . ASP A 1 628  ? -16.725 69.789  134.404 1.00 29.58 ?  626  ASP A O     1 
ATOM   4684  C CB    . ASP A 1 628  ? -16.717 72.304  136.383 1.00 27.98 ?  626  ASP A CB    1 
ATOM   4685  C CG    . ASP A 1 628  ? -16.336 72.713  137.798 1.00 37.87 ?  626  ASP A CG    1 
ATOM   4686  O OD1   . ASP A 1 628  ? -15.425 72.090  138.392 1.00 40.73 ?  626  ASP A OD1   1 
ATOM   4687  O OD2   . ASP A 1 628  ? -16.969 73.652  138.320 1.00 40.85 ?  626  ASP A OD2   1 
ATOM   4688  N N     . TRP A 1 629  ? -16.032 71.610  133.277 1.00 26.56 ?  627  TRP A N     1 
ATOM   4689  C CA    . TRP A 1 629  ? -16.495 71.065  132.011 1.00 26.71 ?  627  TRP A CA    1 
ATOM   4690  C C     . TRP A 1 629  ? -15.493 70.070  131.446 1.00 27.23 ?  627  TRP A C     1 
ATOM   4691  O O     . TRP A 1 629  ? -15.887 69.039  130.891 1.00 25.33 ?  627  TRP A O     1 
ATOM   4692  C CB    . TRP A 1 629  ? -16.756 72.197  131.022 1.00 23.85 ?  627  TRP A CB    1 
ATOM   4693  C CG    . TRP A 1 629  ? -17.229 71.702  129.694 1.00 21.54 ?  627  TRP A CG    1 
ATOM   4694  C CD1   . TRP A 1 629  ? -16.628 71.901  128.489 1.00 20.73 ?  627  TRP A CD1   1 
ATOM   4695  C CD2   . TRP A 1 629  ? -18.380 70.885  129.445 1.00 23.49 ?  627  TRP A CD2   1 
ATOM   4696  N NE1   . TRP A 1 629  ? -17.345 71.275  127.497 1.00 20.79 ?  627  TRP A NE1   1 
ATOM   4697  C CE2   . TRP A 1 629  ? -18.428 70.648  128.057 1.00 22.26 ?  627  TRP A CE2   1 
ATOM   4698  C CE3   . TRP A 1 629  ? -19.383 70.347  130.256 1.00 25.31 ?  627  TRP A CE3   1 
ATOM   4699  C CZ2   . TRP A 1 629  ? -19.432 69.883  127.459 1.00 22.02 ?  627  TRP A CZ2   1 
ATOM   4700  C CZ3   . TRP A 1 629  ? -20.386 69.587  129.659 1.00 24.78 ?  627  TRP A CZ3   1 
ATOM   4701  C CH2   . TRP A 1 629  ? -20.402 69.366  128.276 1.00 26.70 ?  627  TRP A CH2   1 
ATOM   4702  N N     . ALA A 1 630  ? -14.195 70.362  131.577 1.00 24.99 ?  628  ALA A N     1 
ATOM   4703  C CA    . ALA A 1 630  ? -13.177 69.412  131.141 1.00 25.41 ?  628  ALA A CA    1 
ATOM   4704  C C     . ALA A 1 630  ? -13.305 68.083  131.875 1.00 27.93 ?  628  ALA A C     1 
ATOM   4705  O O     . ALA A 1 630  ? -12.978 67.029  131.314 1.00 29.63 ?  628  ALA A O     1 
ATOM   4706  C CB    . ALA A 1 630  ? -11.785 70.000  131.358 1.00 29.06 ?  628  ALA A CB    1 
ATOM   4707  N N     . ALA A 1 631  ? -13.791 68.114  133.118 1.00 25.74 ?  629  ALA A N     1 
ATOM   4708  C CA    . ALA A 1 631  ? -13.949 66.914  133.923 1.00 30.10 ?  629  ALA A CA    1 
ATOM   4709  C C     . ALA A 1 631  ? -15.137 66.060  133.514 1.00 28.82 ?  629  ALA A C     1 
ATOM   4710  O O     . ALA A 1 631  ? -15.223 64.906  133.942 1.00 29.31 ?  629  ALA A O     1 
ATOM   4711  C CB    . ALA A 1 631  ? -14.075 67.292  135.400 1.00 27.73 ?  629  ALA A CB    1 
ATOM   4712  N N     . VAL A 1 632  ? -16.051 66.580  132.704 1.00 25.22 ?  630  VAL A N     1 
ATOM   4713  C CA    . VAL A 1 632  ? -17.115 65.714  132.179 1.00 26.72 ?  630  VAL A CA    1 
ATOM   4714  C C     . VAL A 1 632  ? -16.492 64.767  131.161 1.00 25.02 ?  630  VAL A C     1 
ATOM   4715  O O     . VAL A 1 632  ? -15.800 65.235  130.241 1.00 26.06 ?  630  VAL A O     1 
ATOM   4716  C CB    . VAL A 1 632  ? -18.238 66.552  131.562 1.00 28.32 ?  630  VAL A CB    1 
ATOM   4717  C CG1   . VAL A 1 632  ? -19.338 65.663  131.000 1.00 25.67 ?  630  VAL A CG1   1 
ATOM   4718  C CG2   . VAL A 1 632  ? -18.823 67.495  132.613 1.00 24.60 ?  630  VAL A CG2   1 
ATOM   4719  N N     . PRO A 1 633  ? -16.649 63.452  131.310 1.00 23.88 ?  631  PRO A N     1 
ATOM   4720  C CA    . PRO A 1 633  ? -15.946 62.529  130.416 1.00 24.06 ?  631  PRO A CA    1 
ATOM   4721  C C     . PRO A 1 633  ? -16.332 62.759  128.977 1.00 25.04 ?  631  PRO A C     1 
ATOM   4722  O O     . PRO A 1 633  ? -17.490 63.106  128.663 1.00 24.60 ?  631  PRO A O     1 
ATOM   4723  C CB    . PRO A 1 633  ? -16.404 61.149  130.911 1.00 26.92 ?  631  PRO A CB    1 
ATOM   4724  C CG    . PRO A 1 633  ? -16.803 61.363  132.328 1.00 29.11 ?  631  PRO A CG    1 
ATOM   4725  C CD    . PRO A 1 633  ? -17.351 62.756  132.403 1.00 25.79 ?  631  PRO A CD    1 
ATOM   4726  N N     . PRO A 1 634  ? -15.394 62.577  128.039 1.00 19.37 ?  632  PRO A N     1 
ATOM   4727  C CA    . PRO A 1 634  ? -15.732 62.778  126.619 1.00 19.75 ?  632  PRO A CA    1 
ATOM   4728  C C     . PRO A 1 634  ? -16.990 62.046  126.179 1.00 19.87 ?  632  PRO A C     1 
ATOM   4729  O O     . PRO A 1 634  ? -17.778 62.611  125.414 1.00 20.44 ?  632  PRO A O     1 
ATOM   4730  C CB    . PRO A 1 634  ? -14.485 62.261  125.887 1.00 21.33 ?  632  PRO A CB    1 
ATOM   4731  C CG    . PRO A 1 634  ? -13.366 62.455  126.865 1.00 25.56 ?  632  PRO A CG    1 
ATOM   4732  C CD    . PRO A 1 634  ? -13.958 62.295  128.245 1.00 24.46 ?  632  PRO A CD    1 
ATOM   4733  N N     . SER A 1 635  ? -17.199 60.807  126.628 1.00 23.50 ?  633  SER A N     1 
ATOM   4734  C CA    . SER A 1 635  ? -18.393 60.065  126.223 1.00 24.58 ?  633  SER A CA    1 
ATOM   4735  C C     . SER A 1 635  ? -19.667 60.776  126.665 1.00 21.52 ?  633  SER A C     1 
ATOM   4736  O O     . SER A 1 635  ? -20.671 60.770  125.940 1.00 21.92 ?  633  SER A O     1 
ATOM   4737  C CB    . SER A 1 635  ? -18.354 58.651  126.799 1.00 29.03 ?  633  SER A CB    1 
ATOM   4738  O OG    . SER A 1 635  ? -18.283 58.690  128.213 1.00 36.24 ?  633  SER A OG    1 
ATOM   4739  N N     . GLU A 1 636  ? -19.643 61.403  127.843 1.00 19.99 ?  634  GLU A N     1 
ATOM   4740  C CA    . GLU A 1 636  ? -20.817 62.121  128.323 1.00 21.99 ?  634  GLU A CA    1 
ATOM   4741  C C     . GLU A 1 636  ? -20.975 63.463  127.614 1.00 21.02 ?  634  GLU A C     1 
ATOM   4742  O O     . GLU A 1 636  ? -22.102 63.878  127.318 1.00 23.13 ?  634  GLU A O     1 
ATOM   4743  C CB    . GLU A 1 636  ? -20.740 62.295  129.844 1.00 24.23 ?  634  GLU A CB    1 
ATOM   4744  C CG    . GLU A 1 636  ? -21.928 63.043  130.443 1.00 28.91 ?  634  GLU A CG    1 
ATOM   4745  C CD    . GLU A 1 636  ? -23.279 62.458  130.031 1.00 34.16 ?  634  GLU A CD    1 
ATOM   4746  O OE1   . GLU A 1 636  ? -23.381 61.220  129.855 1.00 31.04 ?  634  GLU A OE1   1 
ATOM   4747  O OE2   . GLU A 1 636  ? -24.240 63.245  129.867 1.00 36.71 ?  634  GLU A OE2   1 
ATOM   4748  N N     . ARG A 1 637  ? -19.868 64.151  127.314 1.00 20.06 ?  635  ARG A N     1 
ATOM   4749  C CA    . ARG A 1 637  ? -19.971 65.342  126.472 1.00 20.09 ?  635  ARG A CA    1 
ATOM   4750  C C     . ARG A 1 637  ? -20.562 64.989  125.115 1.00 19.44 ?  635  ARG A C     1 
ATOM   4751  O O     . ARG A 1 637  ? -21.430 65.708  124.603 1.00 19.99 ?  635  ARG A O     1 
ATOM   4752  C CB    . ARG A 1 637  ? -18.605 66.016  126.300 1.00 18.78 ?  635  ARG A CB    1 
ATOM   4753  C CG    . ARG A 1 637  ? -17.949 66.363  127.648 1.00 21.82 ?  635  ARG A CG    1 
ATOM   4754  C CD    . ARG A 1 637  ? -16.807 67.370  127.508 1.00 21.96 ?  635  ARG A CD    1 
ATOM   4755  N NE    . ARG A 1 637  ? -15.728 66.909  126.643 1.00 20.49 ?  635  ARG A NE    1 
ATOM   4756  C CZ    . ARG A 1 637  ? -14.526 66.521  127.057 1.00 22.92 ?  635  ARG A CZ    1 
ATOM   4757  N NH1   . ARG A 1 637  ? -14.229 66.426  128.343 1.00 24.83 ?  635  ARG A NH1   1 
ATOM   4758  N NH2   . ARG A 1 637  ? -13.591 66.241  126.155 1.00 21.41 ?  635  ARG A NH2   1 
ATOM   4759  N N     . ALA A 1 638  ? -20.122 63.872  124.530 1.00 18.17 ?  636  ALA A N     1 
ATOM   4760  C CA    . ALA A 1 638  ? -20.692 63.442  123.255 1.00 17.26 ?  636  ALA A CA    1 
ATOM   4761  C C     . ALA A 1 638  ? -22.174 63.112  123.401 1.00 19.56 ?  636  ALA A C     1 
ATOM   4762  O O     . ALA A 1 638  ? -22.970 63.374  122.489 1.00 19.40 ?  636  ALA A O     1 
ATOM   4763  C CB    . ALA A 1 638  ? -19.917 62.237  122.708 1.00 19.23 ?  636  ALA A CB    1 
ATOM   4764  N N     . ALA A 1 639  ? -22.564 62.537  124.542 1.00 18.54 ?  637  ALA A N     1 
ATOM   4765  C CA    . ALA A 1 639  ? -23.976 62.238  124.780 1.00 20.04 ?  637  ALA A CA    1 
ATOM   4766  C C     . ALA A 1 639  ? -24.824 63.504  124.783 1.00 21.43 ?  637  ALA A C     1 
ATOM   4767  O O     . ALA A 1 639  ? -25.982 63.485  124.338 1.00 20.11 ?  637  ALA A O     1 
ATOM   4768  C CB    . ALA A 1 639  ? -24.135 61.484  126.100 1.00 19.99 ?  637  ALA A CB    1 
ATOM   4769  N N     . CYS A 1 640  ? -24.282 64.608  125.306 1.00 19.65 ?  638  CYS A N     1 
ATOM   4770  C CA    . CYS A 1 640  ? -24.981 65.888  125.222 1.00 21.61 ?  638  CYS A CA    1 
ATOM   4771  C C     . CYS A 1 640  ? -25.242 66.273  123.772 1.00 20.36 ?  638  CYS A C     1 
ATOM   4772  O O     . CYS A 1 640  ? -26.348 66.700  123.419 1.00 20.19 ?  638  CYS A O     1 
ATOM   4773  C CB    . CYS A 1 640  ? -24.179 66.989  125.911 1.00 20.33 ?  638  CYS A CB    1 
ATOM   4774  S SG    . CYS A 1 640  ? -24.081 66.845  127.701 1.00 23.10 ?  638  CYS A SG    1 
ATOM   4775  N N     . LEU A 1 641  ? -24.216 66.167  122.921 1.00 18.31 ?  639  LEU A N     1 
ATOM   4776  C CA    . LEU A 1 641  ? -24.395 66.511  121.517 1.00 17.12 ?  639  LEU A CA    1 
ATOM   4777  C C     . LEU A 1 641  ? -25.461 65.635  120.880 1.00 16.79 ?  639  LEU A C     1 
ATOM   4778  O O     . LEU A 1 641  ? -26.298 66.124  120.113 1.00 19.23 ?  639  LEU A O     1 
ATOM   4779  C CB    . LEU A 1 641  ? -23.068 66.374  120.762 1.00 17.93 ?  639  LEU A CB    1 
ATOM   4780  C CG    . LEU A 1 641  ? -22.118 67.578  120.752 1.00 17.21 ?  639  LEU A CG    1 
ATOM   4781  C CD1   . LEU A 1 641  ? -21.673 67.973  122.154 1.00 20.62 ?  639  LEU A CD1   1 
ATOM   4782  C CD2   . LEU A 1 641  ? -20.914 67.290  119.869 1.00 15.75 ?  639  LEU A CD2   1 
ATOM   4783  N N     . ASP A 1 642  ? -25.439 64.331  121.174 1.00 18.96 ?  640  ASP A N     1 
ATOM   4784  C CA    . ASP A 1 642  ? -26.430 63.438  120.576 1.00 17.58 ?  640  ASP A CA    1 
ATOM   4785  C C     . ASP A 1 642  ? -27.837 63.782  121.051 1.00 18.63 ?  640  ASP A C     1 
ATOM   4786  O O     . ASP A 1 642  ? -28.790 63.730  120.265 1.00 19.41 ?  640  ASP A O     1 
ATOM   4787  C CB    . ASP A 1 642  ? -26.096 61.976  120.885 1.00 20.77 ?  640  ASP A CB    1 
ATOM   4788  C CG    . ASP A 1 642  ? -25.014 61.416  119.974 1.00 19.75 ?  640  ASP A CG    1 
ATOM   4789  O OD1   . ASP A 1 642  ? -24.793 61.972  118.882 1.00 20.07 ?  640  ASP A OD1   1 
ATOM   4790  O OD2   . ASP A 1 642  ? -24.382 60.408  120.357 1.00 21.18 ?  640  ASP A OD2   1 
ATOM   4791  N N     . ARG A 1 643  ? -27.983 64.147  122.329 1.00 19.98 ?  641  ARG A N     1 
ATOM   4792  C CA    . ARG A 1 643  ? -29.285 64.595  122.814 1.00 19.78 ?  641  ARG A CA    1 
ATOM   4793  C C     . ARG A 1 643  ? -29.722 65.872  122.105 1.00 19.59 ?  641  ARG A C     1 
ATOM   4794  O O     . ARG A 1 643  ? -30.895 66.013  121.741 1.00 21.18 ?  641  ARG A O     1 
ATOM   4795  C CB    . ARG A 1 643  ? -29.253 64.806  124.331 1.00 20.27 ?  641  ARG A CB    1 
ATOM   4796  C CG    . ARG A 1 643  ? -29.386 63.513  125.127 1.00 21.20 ?  641  ARG A CG    1 
ATOM   4797  C CD    . ARG A 1 643  ? -29.573 63.767  126.625 1.00 22.28 ?  641  ARG A CD    1 
ATOM   4798  N NE    . ARG A 1 643  ? -28.428 64.425  127.245 1.00 22.21 ?  641  ARG A NE    1 
ATOM   4799  C CZ    . ARG A 1 643  ? -27.406 63.785  127.794 1.00 22.28 ?  641  ARG A CZ    1 
ATOM   4800  N NH1   . ARG A 1 643  ? -27.343 62.464  127.799 1.00 24.66 ?  641  ARG A NH1   1 
ATOM   4801  N NH2   . ARG A 1 643  ? -26.426 64.488  128.357 1.00 24.69 ?  641  ARG A NH2   1 
ATOM   4802  N N     . ALA A 1 644  ? -28.799 66.820  121.908 1.00 18.80 ?  642  ALA A N     1 
ATOM   4803  C CA    . ALA A 1 644  ? -29.149 68.054  121.204 1.00 20.22 ?  642  ALA A CA    1 
ATOM   4804  C C     . ALA A 1 644  ? -29.591 67.770  119.780 1.00 20.13 ?  642  ALA A C     1 
ATOM   4805  O O     . ALA A 1 644  ? -30.486 68.443  119.255 1.00 19.67 ?  642  ALA A O     1 
ATOM   4806  C CB    . ALA A 1 644  ? -27.974 69.028  121.201 1.00 19.57 ?  642  ALA A CB    1 
ATOM   4807  N N     . ALA A 1 645  ? -28.946 66.800  119.121 1.00 16.54 ?  643  ALA A N     1 
ATOM   4808  C CA    . ALA A 1 645  ? -29.341 66.437  117.763 1.00 17.62 ?  643  ALA A CA    1 
ATOM   4809  C C     . ALA A 1 645  ? -30.761 65.894  117.730 1.00 17.82 ?  643  ALA A C     1 
ATOM   4810  O O     . ALA A 1 645  ? -31.528 66.203  116.809 1.00 17.88 ?  643  ALA A O     1 
ATOM   4811  C CB    . ALA A 1 645  ? -28.360 65.410  117.183 1.00 17.73 ?  643  ALA A CB    1 
ATOM   4812  N N     . GLU A 1 646  ? -31.120 65.059  118.709 1.00 20.12 ?  644  GLU A N     1 
ATOM   4813  C CA    . GLU A 1 646  ? -32.490 64.560  118.787 1.00 20.41 ?  644  GLU A CA    1 
ATOM   4814  C C     . GLU A 1 646  ? -33.477 65.702  118.958 1.00 20.14 ?  644  GLU A C     1 
ATOM   4815  O O     . GLU A 1 646  ? -34.540 65.714  118.326 1.00 20.44 ?  644  GLU A O     1 
ATOM   4816  C CB    . GLU A 1 646  ? -32.639 63.572  119.943 1.00 24.72 ?  644  GLU A CB    1 
ATOM   4817  C CG    . GLU A 1 646  ? -31.865 62.281  119.778 1.00 25.84 ?  644  GLU A CG    1 
ATOM   4818  C CD    . GLU A 1 646  ? -32.311 61.488  118.566 1.00 33.63 ?  644  GLU A CD    1 
ATOM   4819  O OE1   . GLU A 1 646  ? -33.520 61.510  118.248 1.00 39.89 ?  644  GLU A OE1   1 
ATOM   4820  O OE2   . GLU A 1 646  ? -31.444 60.857  117.925 1.00 31.21 ?  644  GLU A OE2   1 
ATOM   4821  N N     . LEU A 1 647  ? -33.130 66.680  119.794 1.00 18.51 ?  645  LEU A N     1 
ATOM   4822  C CA    . LEU A 1 647  ? -34.026 67.806  120.034 1.00 19.63 ?  645  LEU A CA    1 
ATOM   4823  C C     . LEU A 1 647  ? -34.184 68.655  118.780 1.00 20.47 ?  645  LEU A C     1 
ATOM   4824  O O     . LEU A 1 647  ? -35.290 69.113  118.465 1.00 22.39 ?  645  LEU A O     1 
ATOM   4825  C CB    . LEU A 1 647  ? -33.508 68.647  121.199 1.00 20.47 ?  645  LEU A CB    1 
ATOM   4826  C CG    . LEU A 1 647  ? -33.514 67.985  122.579 1.00 22.12 ?  645  LEU A CG    1 
ATOM   4827  C CD1   . LEU A 1 647  ? -32.818 68.865  123.603 1.00 20.53 ?  645  LEU A CD1   1 
ATOM   4828  C CD2   . LEU A 1 647  ? -34.941 67.689  123.038 1.00 26.55 ?  645  LEU A CD2   1 
ATOM   4829  N N     . MET A 1 648  ? -33.092 68.881  118.048 1.00 17.80 ?  646  MET A N     1 
ATOM   4830  C CA    . MET A 1 648  ? -33.208 69.672  116.831 1.00 17.89 ?  646  MET A CA    1 
ATOM   4831  C C     . MET A 1 648  ? -34.009 68.934  115.776 1.00 20.02 ?  646  MET A C     1 
ATOM   4832  O O     . MET A 1 648  ? -34.770 69.558  115.032 1.00 19.33 ?  646  MET A O     1 
ATOM   4833  C CB    . MET A 1 648  ? -31.835 70.032  116.274 1.00 19.75 ?  646  MET A CB    1 
ATOM   4834  C CG    . MET A 1 648  ? -31.111 71.077  117.083 1.00 21.01 ?  646  MET A CG    1 
ATOM   4835  S SD    . MET A 1 648  ? -29.742 71.729  116.120 1.00 21.68 ?  646  MET A SD    1 
ATOM   4836  C CE    . MET A 1 648  ? -28.976 72.770  117.357 1.00 22.60 ?  646  MET A CE    1 
ATOM   4837  N N     . GLN A 1 649  ? -33.853 67.607  115.695 1.00 18.79 ?  647  GLN A N     1 
ATOM   4838  C CA    . GLN A 1 649  ? -34.644 66.843  114.736 1.00 18.05 ?  647  GLN A CA    1 
ATOM   4839  C C     . GLN A 1 649  ? -36.129 66.937  115.058 1.00 21.27 ?  647  GLN A C     1 
ATOM   4840  O O     . GLN A 1 649  ? -36.958 67.108  114.154 1.00 19.85 ?  647  GLN A O     1 
ATOM   4841  C CB    . GLN A 1 649  ? -34.191 65.379  114.711 1.00 20.31 ?  647  GLN A CB    1 
ATOM   4842  C CG    . GLN A 1 649  ? -34.930 64.535  113.673 1.00 20.77 ?  647  GLN A CG    1 
ATOM   4843  C CD    . GLN A 1 649  ? -34.395 64.751  112.270 1.00 20.89 ?  647  GLN A CD    1 
ATOM   4844  O OE1   . GLN A 1 649  ? -33.321 64.268  111.932 1.00 18.23 ?  647  GLN A OE1   1 
ATOM   4845  N NE2   . GLN A 1 649  ? -35.148 65.482  111.442 1.00 21.54 ?  647  GLN A NE2   1 
ATOM   4846  N N     . ALA A 1 650  ? -36.480 66.842  116.344 1.00 20.61 ?  648  ALA A N     1 
ATOM   4847  C CA    . ALA A 1 650  ? -37.879 66.947  116.741 1.00 22.20 ?  648  ALA A CA    1 
ATOM   4848  C C     . ALA A 1 650  ? -38.429 68.341  116.480 1.00 25.42 ?  648  ALA A C     1 
ATOM   4849  O O     . ALA A 1 650  ? -39.609 68.490  116.135 1.00 26.17 ?  648  ALA A O     1 
ATOM   4850  C CB    . ALA A 1 650  ? -38.032 66.595  118.218 1.00 23.58 ?  648  ALA A CB    1 
ATOM   4851  N N     . ARG A 1 651  ? -37.597 69.365  116.645 1.00 20.52 ?  649  ARG A N     1 
ATOM   4852  C CA    . ARG A 1 651  ? -38.023 70.751  116.531 1.00 21.25 ?  649  ARG A CA    1 
ATOM   4853  C C     . ARG A 1 651  ? -37.844 71.310  115.126 1.00 21.67 ?  649  ARG A C     1 
ATOM   4854  O O     . ARG A 1 651  ? -38.067 72.508  114.917 1.00 21.79 ?  649  ARG A O     1 
ATOM   4855  C CB    . ARG A 1 651  ? -37.254 71.613  117.536 1.00 25.40 ?  649  ARG A CB    1 
ATOM   4856  C CG    . ARG A 1 651  ? -37.902 72.957  117.842 1.00 29.33 ?  649  ARG A CG    1 
ATOM   4857  C CD    . ARG A 1 651  ? -37.852 73.275  119.313 1.00 27.42 ?  649  ARG A CD    1 
ATOM   4858  N NE    . ARG A 1 651  ? -38.313 74.629  119.586 1.00 29.21 ?  649  ARG A NE    1 
ATOM   4859  C CZ    . ARG A 1 651  ? -39.588 74.970  119.721 1.00 26.44 ?  649  ARG A CZ    1 
ATOM   4860  N NH1   . ARG A 1 651  ? -40.559 74.090  119.552 1.00 30.08 ?  649  ARG A NH1   1 
ATOM   4861  N NH2   . ARG A 1 651  ? -39.894 76.229  120.022 1.00 28.38 ?  649  ARG A NH2   1 
ATOM   4862  N N     . MET A 1 652  ? -37.460 70.477  114.160 1.00 20.03 ?  650  MET A N     1 
ATOM   4863  C CA    . MET A 1 652  ? -37.124 70.988  112.831 1.00 21.30 ?  650  MET A CA    1 
ATOM   4864  C C     . MET A 1 652  ? -38.187 71.899  112.234 1.00 22.34 ?  650  MET A C     1 
ATOM   4865  O O     . MET A 1 652  ? -37.821 72.973  111.735 1.00 22.30 ?  650  MET A O     1 
ATOM   4866  C CB    . MET A 1 652  ? -36.819 69.828  111.876 1.00 18.84 ?  650  MET A CB    1 
ATOM   4867  C CG    . MET A 1 652  ? -36.543 70.301  110.455 1.00 19.62 ?  650  MET A CG    1 
ATOM   4868  S SD    . MET A 1 652  ? -36.189 68.945  109.318 1.00 22.14 ?  650  MET A SD    1 
ATOM   4869  C CE    . MET A 1 652  ? -34.466 68.629  109.699 1.00 20.48 ?  650  MET A CE    1 
ATOM   4870  N N     . PRO A 1 653  ? -39.490 71.568  112.261 1.00 21.00 ?  651  PRO A N     1 
ATOM   4871  C CA    . PRO A 1 653  ? -40.463 72.464  111.607 1.00 21.87 ?  651  PRO A CA    1 
ATOM   4872  C C     . PRO A 1 653  ? -40.487 73.860  112.200 1.00 21.89 ?  651  PRO A C     1 
ATOM   4873  O O     . PRO A 1 653  ? -40.572 74.845  111.452 1.00 21.35 ?  651  PRO A O     1 
ATOM   4874  C CB    . PRO A 1 653  ? -41.799 71.734  111.801 1.00 22.66 ?  651  PRO A CB    1 
ATOM   4875  C CG    . PRO A 1 653  ? -41.423 70.303  111.970 1.00 24.82 ?  651  PRO A CG    1 
ATOM   4876  C CD    . PRO A 1 653  ? -40.133 70.334  112.744 1.00 23.83 ?  651  PRO A CD    1 
ATOM   4877  N N     . THR A 1 654  ? -40.418 73.974  113.528 1.00 21.05 ?  652  THR A N     1 
ATOM   4878  C CA    . THR A 1 654  ? -40.345 75.291  114.152 1.00 19.52 ?  652  THR A CA    1 
ATOM   4879  C C     . THR A 1 654  ? -39.038 75.990  113.802 1.00 23.63 ?  652  THR A C     1 
ATOM   4880  O O     . THR A 1 654  ? -39.031 77.189  113.505 1.00 22.33 ?  652  THR A O     1 
ATOM   4881  C CB    . THR A 1 654  ? -40.494 75.163  115.665 1.00 23.19 ?  652  THR A CB    1 
ATOM   4882  O OG1   . THR A 1 654  ? -41.715 74.478  115.957 1.00 24.34 ?  652  THR A OG1   1 
ATOM   4883  C CG2   . THR A 1 654  ? -40.532 76.530  116.297 1.00 22.51 ?  652  THR A CG2   1 
ATOM   4884  N N     . LEU A 1 655  ? -37.922 75.256  113.830 1.00 21.23 ?  653  LEU A N     1 
ATOM   4885  C CA    . LEU A 1 655  ? -36.646 75.855  113.449 1.00 19.60 ?  653  LEU A CA    1 
ATOM   4886  C C     . LEU A 1 655  ? -36.679 76.367  112.011 1.00 23.80 ?  653  LEU A C     1 
ATOM   4887  O O     . LEU A 1 655  ? -36.115 77.429  111.714 1.00 20.40 ?  653  LEU A O     1 
ATOM   4888  C CB    . LEU A 1 655  ? -35.507 74.847  113.634 1.00 20.77 ?  653  LEU A CB    1 
ATOM   4889  C CG    . LEU A 1 655  ? -35.278 74.337  115.059 1.00 20.10 ?  653  LEU A CG    1 
ATOM   4890  C CD1   . LEU A 1 655  ? -34.045 73.453  115.121 1.00 20.75 ?  653  LEU A CD1   1 
ATOM   4891  C CD2   . LEU A 1 655  ? -35.158 75.489  116.043 1.00 25.02 ?  653  LEU A CD2   1 
ATOM   4892  N N     . LEU A 1 656  ? -37.337 75.629  111.108 1.00 22.14 ?  654  LEU A N     1 
ATOM   4893  C CA    . LEU A 1 656  ? -37.478 76.086  109.724 1.00 21.96 ?  654  LEU A CA    1 
ATOM   4894  C C     . LEU A 1 656  ? -38.120 77.461  109.664 1.00 20.97 ?  654  LEU A C     1 
ATOM   4895  O O     . LEU A 1 656  ? -37.666 78.340  108.919 1.00 23.00 ?  654  LEU A O     1 
ATOM   4896  C CB    . LEU A 1 656  ? -38.333 75.114  108.915 1.00 22.08 ?  654  LEU A CB    1 
ATOM   4897  C CG    . LEU A 1 656  ? -37.869 73.680  108.777 1.00 20.54 ?  654  LEU A CG    1 
ATOM   4898  C CD1   . LEU A 1 656  ? -38.812 72.939  107.858 1.00 22.48 ?  654  LEU A CD1   1 
ATOM   4899  C CD2   . LEU A 1 656  ? -36.448 73.639  108.271 1.00 21.78 ?  654  LEU A CD2   1 
ATOM   4900  N N     . GLY A 1 657  ? -39.216 77.641  110.404 1.00 21.47 ?  655  GLY A N     1 
ATOM   4901  C CA    . GLY A 1 657  ? -39.921 78.906  110.359 1.00 25.65 ?  655  GLY A CA    1 
ATOM   4902  C C     . GLY A 1 657  ? -39.049 80.055  110.804 1.00 21.69 ?  655  GLY A C     1 
ATOM   4903  O O     . GLY A 1 657  ? -39.112 81.150  110.245 1.00 22.78 ?  655  GLY A O     1 
ATOM   4904  N N     . LEU A 1 658  ? -38.226 79.826  111.826 1.00 21.04 ?  656  LEU A N     1 
ATOM   4905  C CA    . LEU A 1 658  ? -37.380 80.901  112.313 1.00 22.47 ?  656  LEU A CA    1 
ATOM   4906  C C     . LEU A 1 658  ? -36.262 81.210  111.322 1.00 21.09 ?  656  LEU A C     1 
ATOM   4907  O O     . LEU A 1 658  ? -35.941 82.382  111.088 1.00 22.20 ?  656  LEU A O     1 
ATOM   4908  C CB    . LEU A 1 658  ? -36.835 80.534  113.693 1.00 19.54 ?  656  LEU A CB    1 
ATOM   4909  C CG    . LEU A 1 658  ? -35.961 81.570  114.382 1.00 23.13 ?  656  LEU A CG    1 
ATOM   4910  C CD1   . LEU A 1 658  ? -36.690 82.907  114.460 1.00 23.64 ?  656  LEU A CD1   1 
ATOM   4911  C CD2   . LEU A 1 658  ? -35.608 81.065  115.775 1.00 20.03 ?  656  LEU A CD2   1 
ATOM   4912  N N     . ILE A 1 659  ? -35.680 80.181  110.700 1.00 18.15 ?  657  ILE A N     1 
ATOM   4913  C CA    . ILE A 1 659  ? -34.625 80.426  109.726 1.00 17.20 ?  657  ILE A CA    1 
ATOM   4914  C C     . ILE A 1 659  ? -35.186 81.133  108.498 1.00 20.73 ?  657  ILE A C     1 
ATOM   4915  O O     . ILE A 1 659  ? -34.561 82.052  107.955 1.00 19.13 ?  657  ILE A O     1 
ATOM   4916  C CB    . ILE A 1 659  ? -33.924 79.110  109.350 1.00 17.83 ?  657  ILE A CB    1 
ATOM   4917  C CG1   . ILE A 1 659  ? -33.196 78.559  110.579 1.00 19.94 ?  657  ILE A CG1   1 
ATOM   4918  C CG2   . ILE A 1 659  ? -32.987 79.325  108.176 1.00 18.64 ?  657  ILE A CG2   1 
ATOM   4919  C CD1   . ILE A 1 659  ? -32.688 77.149  110.394 1.00 20.66 ?  657  ILE A CD1   1 
ATOM   4920  N N     . ILE A 1 660  ? -36.369 80.716  108.039 1.00 20.29 ?  658  ILE A N     1 
ATOM   4921  C CA    . ILE A 1 660  ? -37.002 81.369  106.893 1.00 18.80 ?  658  ILE A CA    1 
ATOM   4922  C C     . ILE A 1 660  ? -37.176 82.861  107.150 1.00 18.54 ?  658  ILE A C     1 
ATOM   4923  O O     . ILE A 1 660  ? -36.828 83.701  106.309 1.00 20.93 ?  658  ILE A O     1 
ATOM   4924  C CB    . ILE A 1 660  ? -38.350 80.695  106.581 1.00 21.21 ?  658  ILE A CB    1 
ATOM   4925  C CG1   . ILE A 1 660  ? -38.130 79.319  105.953 1.00 19.49 ?  658  ILE A CG1   1 
ATOM   4926  C CG2   . ILE A 1 660  ? -39.234 81.606  105.706 1.00 19.09 ?  658  ILE A CG2   1 
ATOM   4927  C CD1   . ILE A 1 660  ? -39.391 78.495  105.871 1.00 21.37 ?  658  ILE A CD1   1 
ATOM   4928  N N     . ARG A 1 661  ? -37.714 83.215  108.317 1.00 17.83 ?  659  ARG A N     1 
ATOM   4929  C CA    . ARG A 1 661  ? -38.070 84.604  108.566 1.00 20.72 ?  659  ARG A CA    1 
ATOM   4930  C C     . ARG A 1 661  ? -36.900 85.443  109.062 1.00 22.94 ?  659  ARG A C     1 
ATOM   4931  O O     . ARG A 1 661  ? -36.781 86.607  108.670 1.00 22.89 ?  659  ARG A O     1 
ATOM   4932  C CB    . ARG A 1 661  ? -39.241 84.675  109.550 1.00 25.70 ?  659  ARG A CB    1 
ATOM   4933  C CG    . ARG A 1 661  ? -40.549 84.313  108.872 1.00 23.66 ?  659  ARG A CG    1 
ATOM   4934  C CD    . ARG A 1 661  ? -41.757 84.333  109.802 1.00 24.24 ?  659  ARG A CD    1 
ATOM   4935  N NE    . ARG A 1 661  ? -41.964 85.617  110.457 1.00 28.94 ?  659  ARG A NE    1 
ATOM   4936  C CZ    . ARG A 1 661  ? -41.929 85.798  111.771 1.00 26.96 ?  659  ARG A CZ    1 
ATOM   4937  N NH1   . ARG A 1 661  ? -41.667 84.801  112.602 1.00 28.44 ?  659  ARG A NH1   1 
ATOM   4938  N NH2   . ARG A 1 661  ? -42.174 87.008  112.267 1.00 28.41 ?  659  ARG A NH2   1 
ATOM   4939  N N     . GLU A 1 662  ? -36.022 84.895  109.910 1.00 19.34 ?  660  GLU A N     1 
ATOM   4940  C CA    . GLU A 1 662  ? -34.913 85.717  110.391 1.00 21.89 ?  660  GLU A CA    1 
ATOM   4941  C C     . GLU A 1 662  ? -33.803 85.833  109.352 1.00 20.21 ?  660  GLU A C     1 
ATOM   4942  O O     . GLU A 1 662  ? -33.220 86.909  109.182 1.00 21.39 ?  660  GLU A O     1 
ATOM   4943  C CB    . GLU A 1 662  ? -34.351 85.154  111.701 1.00 24.55 ?  660  GLU A CB    1 
ATOM   4944  C CG    . GLU A 1 662  ? -33.141 85.932  112.223 1.00 23.64 ?  660  GLU A CG    1 
ATOM   4945  C CD    . GLU A 1 662  ? -32.593 85.394  113.538 1.00 22.23 ?  660  GLU A CD    1 
ATOM   4946  O OE1   . GLU A 1 662  ? -32.520 84.155  113.708 1.00 24.25 ?  660  GLU A OE1   1 
ATOM   4947  O OE2   . GLU A 1 662  ? -32.243 86.221  114.399 1.00 25.08 ?  660  GLU A OE2   1 
ATOM   4948  N N     . ALA A 1 663  ? -33.507 84.749  108.652 1.00 19.07 ?  661  ALA A N     1 
ATOM   4949  C CA    . ALA A 1 663  ? -32.346 84.690  107.777 1.00 18.04 ?  661  ALA A CA    1 
ATOM   4950  C C     . ALA A 1 663  ? -32.698 84.828  106.301 1.00 18.28 ?  661  ALA A C     1 
ATOM   4951  O O     . ALA A 1 663  ? -31.787 84.914  105.470 1.00 20.65 ?  661  ALA A O     1 
ATOM   4952  C CB    . ALA A 1 663  ? -31.581 83.379  108.012 1.00 19.23 ?  661  ALA A CB    1 
ATOM   4953  N N     . GLY A 1 664  ? -33.985 84.875  105.957 1.00 18.11 ?  662  GLY A N     1 
ATOM   4954  C CA    . GLY A 1 664  ? -34.401 85.054  104.578 1.00 19.57 ?  662  GLY A CA    1 
ATOM   4955  C C     . GLY A 1 664  ? -34.279 83.835  103.698 1.00 20.12 ?  662  GLY A C     1 
ATOM   4956  O O     . GLY A 1 664  ? -34.203 83.981  102.473 1.00 19.52 ?  662  GLY A O     1 
ATOM   4957  N N     . LYS A 1 665  ? -34.259 82.636  104.276 1.00 18.44 ?  663  LYS A N     1 
ATOM   4958  C CA    . LYS A 1 665  ? -34.017 81.417  103.517 1.00 18.61 ?  663  LYS A CA    1 
ATOM   4959  C C     . LYS A 1 665  ? -35.315 80.766  103.061 1.00 17.23 ?  663  LYS A C     1 
ATOM   4960  O O     . LYS A 1 665  ? -36.361 80.918  103.694 1.00 18.38 ?  663  LYS A O     1 
ATOM   4961  C CB    . LYS A 1 665  ? -33.231 80.414  104.353 1.00 18.65 ?  663  LYS A CB    1 
ATOM   4962  C CG    . LYS A 1 665  ? -31.843 80.882  104.708 1.00 18.07 ?  663  LYS A CG    1 
ATOM   4963  C CD    . LYS A 1 665  ? -30.949 79.690  104.976 1.00 22.94 ?  663  LYS A CD    1 
ATOM   4964  C CE    . LYS A 1 665  ? -29.526 80.144  105.127 1.00 23.87 ?  663  LYS A CE    1 
ATOM   4965  N NZ    . LYS A 1 665  ? -28.609 78.975  105.236 1.00 21.56 ?  663  LYS A NZ    1 
ATOM   4966  N N     . SER A 1 666  ? -35.221 80.008  101.967 1.00 17.04 ?  664  SER A N     1 
ATOM   4967  C CA    . SER A 1 666  ? -36.313 79.143  101.537 1.00 17.64 ?  664  SER A CA    1 
ATOM   4968  C C     . SER A 1 666  ? -36.471 77.952  102.482 1.00 20.57 ?  664  SER A C     1 
ATOM   4969  O O     . SER A 1 666  ? -35.542 77.566  103.203 1.00 19.08 ?  664  SER A O     1 
ATOM   4970  C CB    . SER A 1 666  ? -36.061 78.618  100.131 1.00 18.77 ?  664  SER A CB    1 
ATOM   4971  O OG    . SER A 1 666  ? -34.991 77.686  100.160 1.00 17.62 ?  664  SER A OG    1 
ATOM   4972  N N     . ALA A 1 667  ? -37.668 77.359  102.473 1.00 18.78 ?  665  ALA A N     1 
ATOM   4973  C CA    . ALA A 1 667  ? -37.898 76.182  103.306 1.00 19.59 ?  665  ALA A CA    1 
ATOM   4974  C C     . ALA A 1 667  ? -36.959 75.047  102.920 1.00 19.04 ?  665  ALA A C     1 
ATOM   4975  O O     . ALA A 1 667  ? -36.432 74.346  103.790 1.00 16.77 ?  665  ALA A O     1 
ATOM   4976  C CB    . ALA A 1 667  ? -39.360 75.741  103.202 1.00 21.16 ?  665  ALA A CB    1 
ATOM   4977  N N     . LEU A 1 668  ? -36.743 74.847  101.620 1.00 18.05 ?  666  LEU A N     1 
ATOM   4978  C CA    . LEU A 1 668  ? -35.831 73.806  101.156 1.00 15.81 ?  666  LEU A CA    1 
ATOM   4979  C C     . LEU A 1 668  ? -34.444 73.986  101.756 1.00 17.28 ?  666  LEU A C     1 
ATOM   4980  O O     . LEU A 1 668  ? -33.850 73.039  102.292 1.00 17.50 ?  666  LEU A O     1 
ATOM   4981  C CB    . LEU A 1 668  ? -35.759 73.840  99.629  1.00 22.63 ?  666  LEU A CB    1 
ATOM   4982  C CG    . LEU A 1 668  ? -35.053 72.721  98.881  1.00 23.87 ?  666  LEU A CG    1 
ATOM   4983  C CD1   . LEU A 1 668  ? -35.692 71.387  99.211  1.00 32.24 ?  666  LEU A CD1   1 
ATOM   4984  C CD2   . LEU A 1 668  ? -35.176 73.004  97.389  1.00 28.85 ?  666  LEU A CD2   1 
ATOM   4985  N N     . ASN A 1 669  ? -33.913 75.206  101.689 1.00 15.24 ?  667  ASN A N     1 
ATOM   4986  C CA    . ASN A 1 669  ? -32.578 75.434  102.234 1.00 16.15 ?  667  ASN A CA    1 
ATOM   4987  C C     . ASN A 1 669  ? -32.579 75.406  103.757 1.00 16.22 ?  667  ASN A C     1 
ATOM   4988  O O     . ASN A 1 669  ? -31.567 75.033  104.360 1.00 15.49 ?  667  ASN A O     1 
ATOM   4989  C CB    . ASN A 1 669  ? -32.013 76.764  101.737 1.00 15.25 ?  667  ASN A CB    1 
ATOM   4990  C CG    . ASN A 1 669  ? -31.707 76.761  100.244 1.00 16.05 ?  667  ASN A CG    1 
ATOM   4991  O OD1   . ASN A 1 669  ? -31.277 75.748  99.661  1.00 20.24 ?  667  ASN A OD1   1 
ATOM   4992  N ND2   . ASN A 1 669  ? -31.913 77.901  99.622  1.00 15.00 ?  667  ASN A ND2   1 
ATOM   4993  N N     . ALA A 1 670  ? -33.687 75.792  104.399 1.00 15.12 ?  668  ALA A N     1 
ATOM   4994  C CA    . ALA A 1 670  ? -33.739 75.714  105.851 1.00 15.00 ?  668  ALA A CA    1 
ATOM   4995  C C     . ALA A 1 670  ? -33.733 74.264  106.319 1.00 17.60 ?  668  ALA A C     1 
ATOM   4996  O O     . ALA A 1 670  ? -33.117 73.946  107.340 1.00 16.54 ?  668  ALA A O     1 
ATOM   4997  C CB    . ALA A 1 670  ? -34.972 76.456  106.371 1.00 16.31 ?  668  ALA A CB    1 
ATOM   4998  N N     . ILE A 1 671  ? -34.427 73.376  105.603 1.00 15.54 ?  669  ILE A N     1 
ATOM   4999  C CA    . ILE A 1 671  ? -34.397 71.957  105.961 1.00 15.16 ?  669  ILE A CA    1 
ATOM   5000  C C     . ILE A 1 671  ? -32.967 71.435  105.915 1.00 17.69 ?  669  ILE A C     1 
ATOM   5001  O O     . ILE A 1 671  ? -32.491 70.769  106.850 1.00 17.85 ?  669  ILE A O     1 
ATOM   5002  C CB    . ILE A 1 671  ? -35.315 71.142  105.030 1.00 16.41 ?  669  ILE A CB    1 
ATOM   5003  C CG1   . ILE A 1 671  ? -36.778 71.528  105.259 1.00 18.13 ?  669  ILE A CG1   1 
ATOM   5004  C CG2   . ILE A 1 671  ? -35.099 69.649  105.271 1.00 18.20 ?  669  ILE A CG2   1 
ATOM   5005  C CD1   . ILE A 1 671  ? -37.707 71.050  104.133 1.00 18.79 ?  669  ILE A CD1   1 
ATOM   5006  N N     . ALA A 1 672  ? -32.261 71.727  104.819 1.00 14.71 ?  670  ALA A N     1 
ATOM   5007  C CA    . ALA A 1 672  ? -30.887 71.271  104.670 1.00 14.88 ?  670  ALA A CA    1 
ATOM   5008  C C     . ALA A 1 672  ? -29.987 71.852  105.753 1.00 16.31 ?  670  ALA A C     1 
ATOM   5009  O O     . ALA A 1 672  ? -29.048 71.181  106.203 1.00 16.79 ?  670  ALA A O     1 
ATOM   5010  C CB    . ALA A 1 672  ? -30.381 71.630  103.265 1.00 15.66 ?  670  ALA A CB    1 
ATOM   5011  N N     . GLU A 1 673  ? -30.273 73.075  106.208 1.00 14.21 ?  671  GLU A N     1 
ATOM   5012  C CA    . GLU A 1 673  ? -29.442 73.666  107.249 1.00 15.72 ?  671  GLU A CA    1 
ATOM   5013  C C     . GLU A 1 673  ? -29.679 73.001  108.597 1.00 16.64 ?  671  GLU A C     1 
ATOM   5014  O O     . GLU A 1 673  ? -28.726 72.755  109.342 1.00 16.51 ?  671  GLU A O     1 
ATOM   5015  C CB    . GLU A 1 673  ? -29.679 75.170  107.353 1.00 16.54 ?  671  GLU A CB    1 
ATOM   5016  C CG    . GLU A 1 673  ? -28.990 75.719  108.600 1.00 20.44 ?  671  GLU A CG    1 
ATOM   5017  C CD    . GLU A 1 673  ? -28.639 77.173  108.527 1.00 20.54 ?  671  GLU A CD    1 
ATOM   5018  O OE1   . GLU A 1 673  ? -29.235 77.892  107.701 1.00 21.77 ?  671  GLU A OE1   1 
ATOM   5019  O OE2   . GLU A 1 673  ? -27.764 77.599  109.316 1.00 18.95 ?  671  GLU A OE2   1 
ATOM   5020  N N     . VAL A 1 674  ? -30.942 72.732  108.956 1.00 15.74 ?  672  VAL A N     1 
ATOM   5021  C CA    . VAL A 1 674  ? -31.200 72.016  110.201 1.00 16.75 ?  672  VAL A CA    1 
ATOM   5022  C C     . VAL A 1 674  ? -30.593 70.619  110.138 1.00 16.60 ?  672  VAL A C     1 
ATOM   5023  O O     . VAL A 1 674  ? -29.999 70.143  111.113 1.00 14.60 ?  672  VAL A O     1 
ATOM   5024  C CB    . VAL A 1 674  ? -32.705 71.973  110.514 1.00 16.30 ?  672  VAL A CB    1 
ATOM   5025  C CG1   . VAL A 1 674  ? -32.946 71.160  111.780 1.00 15.93 ?  672  VAL A CG1   1 
ATOM   5026  C CG2   . VAL A 1 674  ? -33.269 73.389  110.678 1.00 17.34 ?  672  VAL A CG2   1 
ATOM   5027  N N     . ARG A 1 675  ? -30.714 69.946  108.990 1.00 15.90 ?  673  ARG A N     1 
ATOM   5028  C CA    . ARG A 1 675  ? -30.041 68.658  108.823 1.00 14.55 ?  673  ARG A CA    1 
ATOM   5029  C C     . ARG A 1 675  ? -28.547 68.778  109.098 1.00 15.77 ?  673  ARG A C     1 
ATOM   5030  O O     . ARG A 1 675  ? -27.967 67.930  109.783 1.00 15.03 ?  673  ARG A O     1 
ATOM   5031  C CB    . ARG A 1 675  ? -30.268 68.111  107.413 1.00 12.60 ?  673  ARG A CB    1 
ATOM   5032  C CG    . ARG A 1 675  ? -31.664 67.586  107.163 1.00 16.50 ?  673  ARG A CG    1 
ATOM   5033  C CD    . ARG A 1 675  ? -31.638 66.796  105.873 1.00 15.76 ?  673  ARG A CD    1 
ATOM   5034  N NE    . ARG A 1 675  ? -30.930 65.530  106.031 1.00 15.18 ?  673  ARG A NE    1 
ATOM   5035  C CZ    . ARG A 1 675  ? -30.560 64.764  105.013 1.00 15.21 ?  673  ARG A CZ    1 
ATOM   5036  N NH1   . ARG A 1 675  ? -30.804 65.121  103.758 1.00 15.20 ?  673  ARG A NH1   1 
ATOM   5037  N NH2   . ARG A 1 675  ? -29.968 63.597  105.259 1.00 15.60 ?  673  ARG A NH2   1 
ATOM   5038  N N     . GLU A 1 676  ? -27.905 69.815  108.547 1.00 13.74 ?  674  GLU A N     1 
ATOM   5039  C CA    . GLU A 1 676  ? -26.464 69.970  108.724 1.00 15.67 ?  674  GLU A CA    1 
ATOM   5040  C C     . GLU A 1 676  ? -26.115 70.191  110.191 1.00 16.21 ?  674  GLU A C     1 
ATOM   5041  O O     . GLU A 1 676  ? -25.120 69.648  110.686 1.00 14.42 ?  674  GLU A O     1 
ATOM   5042  C CB    . GLU A 1 676  ? -25.953 71.130  107.869 1.00 15.05 ?  674  GLU A CB    1 
ATOM   5043  C CG    . GLU A 1 676  ? -24.438 71.252  107.873 1.00 17.76 ?  674  GLU A CG    1 
ATOM   5044  C CD    . GLU A 1 676  ? -23.915 72.194  106.795 1.00 26.07 ?  674  GLU A CD    1 
ATOM   5045  O OE1   . GLU A 1 676  ? -24.685 72.553  105.876 1.00 29.49 ?  674  GLU A OE1   1 
ATOM   5046  O OE2   . GLU A 1 676  ? -22.721 72.557  106.856 1.00 29.97 ?  674  GLU A OE2   1 
ATOM   5047  N N     . ALA A 1 677  ? -26.928 70.969  110.911 1.00 15.04 ?  675  ALA A N     1 
ATOM   5048  C CA    . ALA A 1 677  ? -26.675 71.159  112.337 1.00 14.95 ?  675  ALA A CA    1 
ATOM   5049  C C     . ALA A 1 677  ? -26.752 69.833  113.079 1.00 14.30 ?  675  ALA A C     1 
ATOM   5050  O O     . ALA A 1 677  ? -25.893 69.519  113.918 1.00 14.87 ?  675  ALA A O     1 
ATOM   5051  C CB    . ALA A 1 677  ? -27.670 72.170  112.928 1.00 15.38 ?  675  ALA A CB    1 
ATOM   5052  N N     . ILE A 1 678  ? -27.780 69.037  112.781 1.00 14.29 ?  676  ILE A N     1 
ATOM   5053  C CA    . ILE A 1 678  ? -27.920 67.714  113.381 1.00 14.90 ?  676  ILE A CA    1 
ATOM   5054  C C     . ILE A 1 678  ? -26.707 66.857  113.048 1.00 14.43 ?  676  ILE A C     1 
ATOM   5055  O O     . ILE A 1 678  ? -26.166 66.149  113.914 1.00 14.37 ?  676  ILE A O     1 
ATOM   5056  C CB    . ILE A 1 678  ? -29.227 67.061  112.891 1.00 15.40 ?  676  ILE A CB    1 
ATOM   5057  C CG1   . ILE A 1 678  ? -30.431 67.815  113.449 1.00 16.83 ?  676  ILE A CG1   1 
ATOM   5058  C CG2   . ILE A 1 678  ? -29.290 65.586  113.284 1.00 16.71 ?  676  ILE A CG2   1 
ATOM   5059  C CD1   . ILE A 1 678  ? -31.716 67.510  112.670 1.00 16.43 ?  676  ILE A CD1   1 
ATOM   5060  N N     . ASP A 1 679  ? -26.263 66.918  111.786 1.00 13.38 ?  677  ASP A N     1 
ATOM   5061  C CA    . ASP A 1 679  ? -25.133 66.103  111.333 1.00 13.32 ?  677  ASP A CA    1 
ATOM   5062  C C     . ASP A 1 679  ? -23.842 66.489  112.043 1.00 15.72 ?  677  ASP A C     1 
ATOM   5063  O O     . ASP A 1 679  ? -23.072 65.609  112.442 1.00 13.45 ?  677  ASP A O     1 
ATOM   5064  C CB    . ASP A 1 679  ? -24.949 66.225  109.814 1.00 14.34 ?  677  ASP A CB    1 
ATOM   5065  C CG    . ASP A 1 679  ? -26.085 65.615  109.009 1.00 17.65 ?  677  ASP A CG    1 
ATOM   5066  O OD1   . ASP A 1 679  ? -26.820 64.734  109.507 1.00 18.44 ?  677  ASP A OD1   1 
ATOM   5067  O OD2   . ASP A 1 679  ? -26.207 65.994  107.823 1.00 17.66 ?  677  ASP A OD2   1 
ATOM   5068  N N     . PHE A 1 680  ? -23.592 67.793  112.219 1.00 13.91 ?  678  PHE A N     1 
ATOM   5069  C CA    . PHE A 1 680  ? -22.425 68.232  112.985 1.00 14.28 ?  678  PHE A CA    1 
ATOM   5070  C C     . PHE A 1 680  ? -22.448 67.649  114.390 1.00 13.60 ?  678  PHE A C     1 
ATOM   5071  O O     . PHE A 1 680  ? -21.437 67.144  114.891 1.00 15.43 ?  678  PHE A O     1 
ATOM   5072  C CB    . PHE A 1 680  ? -22.371 69.756  113.074 1.00 14.15 ?  678  PHE A CB    1 
ATOM   5073  C CG    . PHE A 1 680  ? -21.738 70.437  111.894 1.00 14.58 ?  678  PHE A CG    1 
ATOM   5074  C CD1   . PHE A 1 680  ? -20.502 70.056  111.407 1.00 15.41 ?  678  PHE A CD1   1 
ATOM   5075  C CD2   . PHE A 1 680  ? -22.395 71.497  111.278 1.00 14.11 ?  678  PHE A CD2   1 
ATOM   5076  C CE1   . PHE A 1 680  ? -19.931 70.725  110.337 1.00 16.55 ?  678  PHE A CE1   1 
ATOM   5077  C CE2   . PHE A 1 680  ? -21.840 72.164  110.225 1.00 16.52 ?  678  PHE A CE2   1 
ATOM   5078  C CZ    . PHE A 1 680  ? -20.606 71.775  109.737 1.00 15.49 ?  678  PHE A CZ    1 
ATOM   5079  N N     . LEU A 1 681  ? -23.595 67.747  115.056 1.00 14.00 ?  679  LEU A N     1 
ATOM   5080  C CA    . LEU A 1 681  ? -23.703 67.263  116.426 1.00 14.57 ?  679  LEU A CA    1 
ATOM   5081  C C     . LEU A 1 681  ? -23.383 65.777  116.501 1.00 15.46 ?  679  LEU A C     1 
ATOM   5082  O O     . LEU A 1 681  ? -22.583 65.343  117.337 1.00 15.20 ?  679  LEU A O     1 
ATOM   5083  C CB    . LEU A 1 681  ? -25.108 67.551  116.950 1.00 14.99 ?  679  LEU A CB    1 
ATOM   5084  C CG    . LEU A 1 681  ? -25.407 69.031  117.232 1.00 15.96 ?  679  LEU A CG    1 
ATOM   5085  C CD1   . LEU A 1 681  ? -26.915 69.284  117.322 1.00 16.70 ?  679  LEU A CD1   1 
ATOM   5086  C CD2   . LEU A 1 681  ? -24.739 69.488  118.530 1.00 17.36 ?  679  LEU A CD2   1 
ATOM   5087  N N     . ARG A 1 682  ? -23.975 64.980  115.611 1.00 15.79 ?  680  ARG A N     1 
ATOM   5088  C CA    . ARG A 1 682  ? -23.761 63.535  115.672 1.00 15.52 ?  680  ARG A CA    1 
ATOM   5089  C C     . ARG A 1 682  ? -22.373 63.146  115.185 1.00 14.92 ?  680  ARG A C     1 
ATOM   5090  O O     . ARG A 1 682  ? -21.788 62.188  115.700 1.00 15.34 ?  680  ARG A O     1 
ATOM   5091  C CB    . ARG A 1 682  ? -24.837 62.816  114.855 1.00 14.62 ?  680  ARG A CB    1 
ATOM   5092  C CG    . ARG A 1 682  ? -26.196 62.917  115.509 1.00 17.04 ?  680  ARG A CG    1 
ATOM   5093  C CD    . ARG A 1 682  ? -27.265 62.256  114.653 1.00 15.14 ?  680  ARG A CD    1 
ATOM   5094  N NE    . ARG A 1 682  ? -28.560 62.277  115.316 1.00 16.63 ?  680  ARG A NE    1 
ATOM   5095  C CZ    . ARG A 1 682  ? -29.717 62.102  114.690 1.00 18.44 ?  680  ARG A CZ    1 
ATOM   5096  N NH1   . ARG A 1 682  ? -29.774 61.893  113.383 1.00 18.47 ?  680  ARG A NH1   1 
ATOM   5097  N NH2   . ARG A 1 682  ? -30.845 62.141  115.400 1.00 21.54 ?  680  ARG A NH2   1 
ATOM   5098  N N     . TYR A 1 683  ? -21.831 63.884  114.217 1.00 14.41 ?  681  TYR A N     1 
ATOM   5099  C CA    . TYR A 1 683  ? -20.507 63.573  113.696 1.00 13.01 ?  681  TYR A CA    1 
ATOM   5100  C C     . TYR A 1 683  ? -19.427 63.900  114.716 1.00 15.21 ?  681  TYR A C     1 
ATOM   5101  O O     . TYR A 1 683  ? -18.544 63.077  114.974 1.00 14.95 ?  681  TYR A O     1 
ATOM   5102  C CB    . TYR A 1 683  ? -20.275 64.330  112.389 1.00 12.88 ?  681  TYR A CB    1 
ATOM   5103  C CG    . TYR A 1 683  ? -18.890 64.122  111.838 1.00 14.48 ?  681  TYR A CG    1 
ATOM   5104  C CD1   . TYR A 1 683  ? -18.582 62.979  111.110 1.00 14.67 ?  681  TYR A CD1   1 
ATOM   5105  C CD2   . TYR A 1 683  ? -17.886 65.049  112.078 1.00 13.16 ?  681  TYR A CD2   1 
ATOM   5106  C CE1   . TYR A 1 683  ? -17.305 62.770  110.613 1.00 13.71 ?  681  TYR A CE1   1 
ATOM   5107  C CE2   . TYR A 1 683  ? -16.602 64.851  111.592 1.00 13.25 ?  681  TYR A CE2   1 
ATOM   5108  C CZ    . TYR A 1 683  ? -16.322 63.705  110.857 1.00 14.76 ?  681  TYR A CZ    1 
ATOM   5109  O OH    . TYR A 1 683  ? -15.043 63.488  110.367 1.00 15.48 ?  681  TYR A OH    1 
ATOM   5110  N N     . TYR A 1 684  ? -19.476 65.093  115.316 1.00 14.67 ?  682  TYR A N     1 
ATOM   5111  C CA    . TYR A 1 684  ? -18.453 65.384  116.315 1.00 14.85 ?  682  TYR A CA    1 
ATOM   5112  C C     . TYR A 1 684  ? -18.618 64.503  117.552 1.00 15.70 ?  682  TYR A C     1 
ATOM   5113  O O     . TYR A 1 684  ? -17.622 64.185  118.215 1.00 15.36 ?  682  TYR A O     1 
ATOM   5114  C CB    . TYR A 1 684  ? -18.460 66.871  116.694 1.00 15.62 ?  682  TYR A CB    1 
ATOM   5115  C CG    . TYR A 1 684  ? -18.073 67.784  115.544 1.00 13.62 ?  682  TYR A CG    1 
ATOM   5116  C CD1   . TYR A 1 684  ? -17.041 67.449  114.673 1.00 13.18 ?  682  TYR A CD1   1 
ATOM   5117  C CD2   . TYR A 1 684  ? -18.775 68.966  115.302 1.00 13.67 ?  682  TYR A CD2   1 
ATOM   5118  C CE1   . TYR A 1 684  ? -16.701 68.287  113.596 1.00 15.87 ?  682  TYR A CE1   1 
ATOM   5119  C CE2   . TYR A 1 684  ? -18.449 69.803  114.244 1.00 13.30 ?  682  TYR A CE2   1 
ATOM   5120  C CZ    . TYR A 1 684  ? -17.413 69.462  113.390 1.00 13.37 ?  682  TYR A CZ    1 
ATOM   5121  O OH    . TYR A 1 684  ? -17.103 70.298  112.334 1.00 16.13 ?  682  TYR A OH    1 
ATOM   5122  N N     . ALA A 1 685  ? -19.848 64.095  117.884 1.00 14.95 ?  683  ALA A N     1 
ATOM   5123  C CA    . ALA A 1 685  ? -20.039 63.134  118.970 1.00 16.20 ?  683  ALA A CA    1 
ATOM   5124  C C     . ALA A 1 685  ? -19.343 61.814  118.657 1.00 16.36 ?  683  ALA A C     1 
ATOM   5125  O O     . ALA A 1 685  ? -18.640 61.249  119.508 1.00 16.91 ?  683  ALA A O     1 
ATOM   5126  C CB    . ALA A 1 685  ? -21.529 62.902  119.225 1.00 17.92 ?  683  ALA A CB    1 
ATOM   5127  N N     . GLU A 1 686  ? -19.540 61.295  117.443 1.00 17.14 ?  684  GLU A N     1 
ATOM   5128  C CA    . GLU A 1 686  ? -18.912 60.024  117.099 1.00 19.50 ?  684  GLU A CA    1 
ATOM   5129  C C     . GLU A 1 686  ? -17.394 60.154  117.045 1.00 17.96 ?  684  GLU A C     1 
ATOM   5130  O O     . GLU A 1 686  ? -16.678 59.282  117.554 1.00 17.92 ?  684  GLU A O     1 
ATOM   5131  C CB    . GLU A 1 686  ? -19.459 59.492  115.774 1.00 19.06 ?  684  GLU A CB    1 
ATOM   5132  C CG    . GLU A 1 686  ? -18.747 58.205  115.285 1.00 24.32 ?  684  GLU A CG    1 
ATOM   5133  C CD    . GLU A 1 686  ? -18.870 57.004  116.245 1.00 25.89 ?  684  GLU A CD    1 
ATOM   5134  O OE1   . GLU A 1 686  ? -19.674 57.036  117.208 1.00 25.07 ?  684  GLU A OE1   1 
ATOM   5135  O OE2   . GLU A 1 686  ? -18.153 55.998  116.028 1.00 27.52 ?  684  GLU A OE2   1 
ATOM   5136  N N     . GLN A 1 687  ? -16.886 61.239  116.454 1.00 16.44 ?  685  GLN A N     1 
ATOM   5137  C CA    . GLN A 1 687  ? -15.441 61.439  116.400 1.00 14.62 ?  685  GLN A CA    1 
ATOM   5138  C C     . GLN A 1 687  ? -14.852 61.509  117.799 1.00 17.18 ?  685  GLN A C     1 
ATOM   5139  O O     . GLN A 1 687  ? -13.742 61.025  118.042 1.00 17.27 ?  685  GLN A O     1 
ATOM   5140  C CB    . GLN A 1 687  ? -15.110 62.708  115.619 1.00 16.23 ?  685  GLN A CB    1 
ATOM   5141  C CG    . GLN A 1 687  ? -15.407 62.596  114.122 1.00 14.88 ?  685  GLN A CG    1 
ATOM   5142  C CD    . GLN A 1 687  ? -14.659 61.455  113.491 1.00 19.79 ?  685  GLN A CD    1 
ATOM   5143  O OE1   . GLN A 1 687  ? -13.431 61.410  113.547 1.00 17.30 ?  685  GLN A OE1   1 
ATOM   5144  N NE2   . GLN A 1 687  ? -15.389 60.509  112.915 1.00 21.63 ?  685  GLN A NE2   1 
ATOM   5145  N N     . THR A 1 688  ? -15.587 62.114  118.733 1.00 15.74 ?  686  THR A N     1 
ATOM   5146  C CA    . THR A 1 688  ? -15.144 62.149  120.123 1.00 15.16 ?  686  THR A CA    1 
ATOM   5147  C C     . THR A 1 688  ? -15.045 60.745  120.707 1.00 16.54 ?  686  THR A C     1 
ATOM   5148  O O     . THR A 1 688  ? -14.026 60.376  121.308 1.00 18.38 ?  686  THR A O     1 
ATOM   5149  C CB    . THR A 1 688  ? -16.094 63.010  120.956 1.00 16.37 ?  686  THR A CB    1 
ATOM   5150  O OG1   . THR A 1 688  ? -15.936 64.379  120.570 1.00 17.65 ?  686  THR A OG1   1 
ATOM   5151  C CG2   . THR A 1 688  ? -15.740 62.867  122.432 1.00 16.27 ?  686  THR A CG2   1 
ATOM   5152  N N     . ARG A 1 689  ? -16.096 59.943  120.526 1.00 17.14 ?  687  ARG A N     1 
ATOM   5153  C CA    . ARG A 1 689  ? -16.096 58.571  121.023 1.00 18.06 ?  687  ARG A CA    1 
ATOM   5154  C C     . ARG A 1 689  ? -14.959 57.750  120.426 1.00 19.28 ?  687  ARG A C     1 
ATOM   5155  O O     . ARG A 1 689  ? -14.480 56.813  121.080 1.00 21.30 ?  687  ARG A O     1 
ATOM   5156  C CB    . ARG A 1 689  ? -17.438 57.909  120.731 1.00 18.53 ?  687  ARG A CB    1 
ATOM   5157  C CG    . ARG A 1 689  ? -18.567 58.392  121.648 1.00 21.16 ?  687  ARG A CG    1 
ATOM   5158  C CD    . ARG A 1 689  ? -19.815 57.543  121.451 1.00 22.55 ?  687  ARG A CD    1 
ATOM   5159  N NE    . ARG A 1 689  ? -20.353 57.685  120.105 1.00 20.99 ?  687  ARG A NE    1 
ATOM   5160  C CZ    . ARG A 1 689  ? -21.326 58.525  119.773 1.00 19.97 ?  687  ARG A CZ    1 
ATOM   5161  N NH1   . ARG A 1 689  ? -21.907 59.295  120.678 1.00 24.13 ?  687  ARG A NH1   1 
ATOM   5162  N NH2   . ARG A 1 689  ? -21.733 58.582  118.506 1.00 22.11 ?  687  ARG A NH2   1 
ATOM   5163  N N     . ARG A 1 690  ? -14.513 58.088  119.204 1.00 16.78 ?  688  ARG A N     1 
ATOM   5164  C CA    A ARG A 1 690  ? -13.402 57.386  118.564 0.66 18.32 ?  688  ARG A CA    1 
ATOM   5165  C CA    B ARG A 1 690  ? -13.404 57.376  118.581 0.34 18.31 ?  688  ARG A CA    1 
ATOM   5166  C C     . ARG A 1 690  ? -12.033 57.838  119.064 1.00 18.40 ?  688  ARG A C     1 
ATOM   5167  O O     . ARG A 1 690  ? -11.050 57.116  118.864 1.00 18.11 ?  688  ARG A O     1 
ATOM   5168  C CB    A ARG A 1 690  ? -13.427 57.581  117.036 0.66 16.68 ?  688  ARG A CB    1 
ATOM   5169  C CB    B ARG A 1 690  ? -13.466 57.530  117.059 0.34 16.77 ?  688  ARG A CB    1 
ATOM   5170  C CG    A ARG A 1 690  ? -14.627 56.999  116.273 0.66 19.42 ?  688  ARG A CG    1 
ATOM   5171  C CG    B ARG A 1 690  ? -14.677 56.886  116.406 0.34 19.48 ?  688  ARG A CG    1 
ATOM   5172  C CD    A ARG A 1 690  ? -14.585 55.473  116.136 0.66 19.63 ?  688  ARG A CD    1 
ATOM   5173  C CD    B ARG A 1 690  ? -14.694 55.385  116.639 0.34 19.75 ?  688  ARG A CD    1 
ATOM   5174  N NE    A ARG A 1 690  ? -13.406 54.995  115.420 0.66 18.27 ?  688  ARG A NE    1 
ATOM   5175  N NE    B ARG A 1 690  ? -13.389 54.783  116.393 0.34 20.90 ?  688  ARG A NE    1 
ATOM   5176  C CZ    A ARG A 1 690  ? -12.386 54.380  116.002 0.66 20.27 ?  688  ARG A CZ    1 
ATOM   5177  C CZ    B ARG A 1 690  ? -12.891 54.553  115.186 0.34 19.21 ?  688  ARG A CZ    1 
ATOM   5178  N NH1   A ARG A 1 690  ? -12.379 54.135  117.299 0.66 18.25 ?  688  ARG A NH1   1 
ATOM   5179  N NH1   B ARG A 1 690  ? -13.565 54.858  114.091 0.34 17.34 ?  688  ARG A NH1   1 
ATOM   5180  N NH2   A ARG A 1 690  ? -11.344 54.009  115.266 0.66 18.51 ?  688  ARG A NH2   1 
ATOM   5181  N NH2   B ARG A 1 690  ? -11.680 54.013  115.076 0.34 18.76 ?  688  ARG A NH2   1 
ATOM   5182  N N     . THR A 1 691  ? -11.922 59.024  119.676 1.00 16.42 ?  689  THR A N     1 
ATOM   5183  C CA    . THR A 1 691  ? -10.572 59.555  119.869 1.00 17.97 ?  689  THR A CA    1 
ATOM   5184  C C     . THR A 1 691  ? -10.196 60.055  121.263 1.00 22.74 ?  689  THR A C     1 
ATOM   5185  O O     . THR A 1 691  ? -9.104  59.737  121.740 1.00 22.30 ?  689  THR A O     1 
ATOM   5186  C CB    . THR A 1 691  ? -10.301 60.699  118.885 1.00 18.17 ?  689  THR A CB    1 
ATOM   5187  O OG1   . THR A 1 691  ? -11.278 61.737  119.049 1.00 18.32 ?  689  THR A OG1   1 
ATOM   5188  C CG2   . THR A 1 691  ? -10.345 60.206  117.445 1.00 16.96 ?  689  THR A CG2   1 
ATOM   5189  N N     . LEU A 1 692  ? -11.039 60.848  121.921 1.00 18.63 ?  690  LEU A N     1 
ATOM   5190  C CA    . LEU A 1 692  ? -10.547 61.699  123.001 1.00 18.86 ?  690  LEU A CA    1 
ATOM   5191  C C     . LEU A 1 692  ? -10.324 60.925  124.297 1.00 20.36 ?  690  LEU A C     1 
ATOM   5192  O O     . LEU A 1 692  ? -11.214 60.221  124.783 1.00 22.98 ?  690  LEU A O     1 
ATOM   5193  C CB    . LEU A 1 692  ? -11.507 62.867  123.236 1.00 17.82 ?  690  LEU A CB    1 
ATOM   5194  C CG    . LEU A 1 692  ? -11.556 63.844  122.049 1.00 20.25 ?  690  LEU A CG    1 
ATOM   5195  C CD1   . LEU A 1 692  ? -12.404 65.055  122.403 1.00 21.95 ?  690  LEU A CD1   1 
ATOM   5196  C CD2   . LEU A 1 692  ? -10.169 64.298  121.626 1.00 20.96 ?  690  LEU A CD2   1 
ATOM   5197  N N     . GLY A 1 693  ? -9.130  61.083  124.862 1.00 18.69 ?  691  GLY A N     1 
ATOM   5198  C CA    . GLY A 1 693  ? -8.769  60.447  126.102 1.00 22.00 ?  691  GLY A CA    1 
ATOM   5199  C C     . GLY A 1 693  ? -8.195  61.458  127.067 1.00 21.60 ?  691  GLY A C     1 
ATOM   5200  O O     . GLY A 1 693  ? -8.177  62.664  126.802 1.00 23.51 ?  691  GLY A O     1 
ATOM   5201  N N     . PRO A 1 694  ? -7.701  60.980  128.207 1.00 24.29 ?  692  PRO A N     1 
ATOM   5202  C CA    . PRO A 1 694  ? -7.261  61.917  129.254 1.00 21.90 ?  692  PRO A CA    1 
ATOM   5203  C C     . PRO A 1 694  ? -6.087  62.782  128.835 1.00 22.95 ?  692  PRO A C     1 
ATOM   5204  O O     . PRO A 1 694  ? -5.945  63.902  129.345 1.00 27.54 ?  692  PRO A O     1 
ATOM   5205  C CB    . PRO A 1 694  ? -6.915  60.993  130.434 1.00 25.15 ?  692  PRO A CB    1 
ATOM   5206  C CG    . PRO A 1 694  ? -6.824  59.618  129.866 1.00 28.65 ?  692  PRO A CG    1 
ATOM   5207  C CD    . PRO A 1 694  ? -7.671  59.575  128.639 1.00 23.87 ?  692  PRO A CD    1 
ATOM   5208  N N     . GLY A 1 695  ? -5.258  62.314  127.898 1.00 22.74 ?  693  GLY A N     1 
ATOM   5209  C CA    . GLY A 1 695  ? -4.116  63.084  127.441 1.00 25.39 ?  693  GLY A CA    1 
ATOM   5210  C C     . GLY A 1 695  ? -4.414  64.164  126.431 1.00 25.22 ?  693  GLY A C     1 
ATOM   5211  O O     . GLY A 1 695  ? -3.499  64.894  126.038 1.00 27.26 ?  693  GLY A O     1 
ATOM   5212  N N     . HIS A 1 696  ? -5.664  64.286  125.980 1.00 22.24 ?  694  HIS A N     1 
ATOM   5213  C CA    . HIS A 1 696  ? -6.035  65.290  124.982 1.00 20.15 ?  694  HIS A CA    1 
ATOM   5214  C C     . HIS A 1 696  ? -6.782  66.402  125.708 1.00 24.12 ?  694  HIS A C     1 
ATOM   5215  O O     . HIS A 1 696  ? -8.009  66.497  125.668 1.00 26.72 ?  694  HIS A O     1 
ATOM   5216  C CB    . HIS A 1 696  ? -6.864  64.659  123.865 1.00 22.81 ?  694  HIS A CB    1 
ATOM   5217  C CG    . HIS A 1 696  ? -6.273  63.390  123.335 1.00 19.42 ?  694  HIS A CG    1 
ATOM   5218  N ND1   . HIS A 1 696  ? -6.899  62.169  123.463 1.00 22.81 ?  694  HIS A ND1   1 
ATOM   5219  C CD2   . HIS A 1 696  ? -5.101  63.148  122.701 1.00 21.07 ?  694  HIS A CD2   1 
ATOM   5220  C CE1   . HIS A 1 696  ? -6.144  61.232  122.917 1.00 19.41 ?  694  HIS A CE1   1 
ATOM   5221  N NE2   . HIS A 1 696  ? -5.046  61.799  122.453 1.00 22.78 ?  694  HIS A NE2   1 
ATOM   5222  N N     . GLY A 1 697  ? -6.020  67.228  126.418 1.00 24.21 ?  695  GLY A N     1 
ATOM   5223  C CA    . GLY A 1 697  ? -6.602  68.224  127.282 1.00 22.89 ?  695  GLY A CA    1 
ATOM   5224  C C     . GLY A 1 697  ? -7.155  69.384  126.487 1.00 24.38 ?  695  GLY A C     1 
ATOM   5225  O O     . GLY A 1 697  ? -6.637  69.739  125.427 1.00 22.12 ?  695  GLY A O     1 
ATOM   5226  N N     . PRO A 1 698  ? -8.235  69.984  126.974 1.00 24.02 ?  696  PRO A N     1 
ATOM   5227  C CA    . PRO A 1 698  ? -8.816  71.134  126.273 1.00 22.80 ?  696  PRO A CA    1 
ATOM   5228  C C     . PRO A 1 698  ? -7.873  72.330  126.243 1.00 23.66 ?  696  PRO A C     1 
ATOM   5229  O O     . PRO A 1 698  ? -6.975  72.469  127.078 1.00 25.14 ?  696  PRO A O     1 
ATOM   5230  C CB    . PRO A 1 698  ? -10.080 71.443  127.084 1.00 27.09 ?  696  PRO A CB    1 
ATOM   5231  C CG    . PRO A 1 698  ? -9.888  70.785  128.378 1.00 32.22 ?  696  PRO A CG    1 
ATOM   5232  C CD    . PRO A 1 698  ? -9.058  69.567  128.117 1.00 29.15 ?  696  PRO A CD    1 
ATOM   5233  N N     . LEU A 1 699  ? -8.068  73.183  125.232 1.00 23.36 ?  697  LEU A N     1 
ATOM   5234  C CA    . LEU A 1 699  ? -7.356  74.457  125.184 1.00 22.71 ?  697  LEU A CA    1 
ATOM   5235  C C     . LEU A 1 699  ? -7.782  75.382  126.315 1.00 21.57 ?  697  LEU A C     1 
ATOM   5236  O O     . LEU A 1 699  ? -6.940  76.021  126.957 1.00 24.12 ?  697  LEU A O     1 
ATOM   5237  C CB    . LEU A 1 699  ? -7.611  75.147  123.848 1.00 21.69 ?  697  LEU A CB    1 
ATOM   5238  C CG    . LEU A 1 699  ? -7.077  74.476  122.591 1.00 23.51 ?  697  LEU A CG    1 
ATOM   5239  C CD1   . LEU A 1 699  ? -7.554  75.267  121.370 1.00 20.53 ?  697  LEU A CD1   1 
ATOM   5240  C CD2   . LEU A 1 699  ? -5.550  74.357  122.616 1.00 25.05 ?  697  LEU A CD2   1 
ATOM   5241  N N     . GLY A 1 700  ? -9.086  75.485  126.564 1.00 20.80 ?  698  GLY A N     1 
ATOM   5242  C CA    . GLY A 1 700  ? -9.626  76.475  127.467 1.00 22.26 ?  698  GLY A CA    1 
ATOM   5243  C C     . GLY A 1 700  ? -10.781 77.191  126.795 1.00 22.22 ?  698  GLY A C     1 
ATOM   5244  O O     . GLY A 1 700  ? -11.324 76.705  125.797 1.00 21.46 ?  698  GLY A O     1 
ATOM   5245  N N     . PRO A 1 701  ? -11.171 78.359  127.308 1.00 22.52 ?  699  PRO A N     1 
ATOM   5246  C CA    . PRO A 1 701  ? -12.310 79.078  126.719 1.00 21.96 ?  699  PRO A CA    1 
ATOM   5247  C C     . PRO A 1 701  ? -12.082 79.362  125.241 1.00 20.63 ?  699  PRO A C     1 
ATOM   5248  O O     . PRO A 1 701  ? -11.043 79.894  124.846 1.00 20.64 ?  699  PRO A O     1 
ATOM   5249  C CB    . PRO A 1 701  ? -12.375 80.369  127.541 1.00 23.46 ?  699  PRO A CB    1 
ATOM   5250  C CG    . PRO A 1 701  ? -11.780 79.985  128.887 1.00 24.55 ?  699  PRO A CG    1 
ATOM   5251  C CD    . PRO A 1 701  ? -10.676 79.013  128.536 1.00 20.77 ?  699  PRO A CD    1 
ATOM   5252  N N     . ILE A 1 702  ? -13.056 78.978  124.418 1.00 18.80 ?  700  ILE A N     1 
ATOM   5253  C CA    A ILE A 1 702  ? -12.981 79.188  122.980 0.62 20.07 ?  700  ILE A CA    1 
ATOM   5254  C CA    B ILE A 1 702  ? -13.002 79.162  122.969 0.38 20.07 ?  700  ILE A CA    1 
ATOM   5255  C C     . ILE A 1 702  ? -14.073 80.165  122.580 1.00 21.48 ?  700  ILE A C     1 
ATOM   5256  O O     . ILE A 1 702  ? -15.230 80.021  122.987 1.00 20.14 ?  700  ILE A O     1 
ATOM   5257  C CB    A ILE A 1 702  ? -13.090 77.862  122.206 0.62 19.01 ?  700  ILE A CB    1 
ATOM   5258  C CB    B ILE A 1 702  ? -13.220 77.838  122.216 0.38 19.00 ?  700  ILE A CB    1 
ATOM   5259  C CG1   A ILE A 1 702  ? -11.814 77.049  122.436 0.62 18.99 ?  700  ILE A CG1   1 
ATOM   5260  C CG1   B ILE A 1 702  ? -12.183 76.795  122.624 0.38 18.98 ?  700  ILE A CG1   1 
ATOM   5261  C CG2   A ILE A 1 702  ? -13.319 78.110  120.704 0.62 19.43 ?  700  ILE A CG2   1 
ATOM   5262  C CG2   B ILE A 1 702  ? -13.185 78.062  120.697 0.38 19.39 ?  700  ILE A CG2   1 
ATOM   5263  C CD1   A ILE A 1 702  ? -11.761 75.730  121.732 0.62 17.82 ?  700  ILE A CD1   1 
ATOM   5264  C CD1   B ILE A 1 702  ? -10.774 77.171  122.282 0.38 20.34 ?  700  ILE A CD1   1 
ATOM   5265  N N     . VAL A 1 703  ? -13.692 81.165  121.798 1.00 19.34 ?  701  VAL A N     1 
ATOM   5266  C CA    . VAL A 1 703  ? -14.619 82.147  121.253 1.00 18.19 ?  701  VAL A CA    1 
ATOM   5267  C C     . VAL A 1 703  ? -15.047 81.656  119.879 1.00 17.47 ?  701  VAL A C     1 
ATOM   5268  O O     . VAL A 1 703  ? -14.201 81.454  119.004 1.00 17.43 ?  701  VAL A O     1 
ATOM   5269  C CB    . VAL A 1 703  ? -13.966 83.532  121.163 1.00 19.40 ?  701  VAL A CB    1 
ATOM   5270  C CG1   . VAL A 1 703  ? -14.848 84.489  120.406 1.00 22.30 ?  701  VAL A CG1   1 
ATOM   5271  C CG2   . VAL A 1 703  ? -13.690 84.075  122.563 1.00 19.86 ?  701  VAL A CG2   1 
ATOM   5272  N N     . CYS A 1 704  ? -16.349 81.451  119.696 1.00 18.02 ?  702  CYS A N     1 
ATOM   5273  C CA    . CYS A 1 704  ? -16.919 81.007  118.429 1.00 18.33 ?  702  CYS A CA    1 
ATOM   5274  C C     . CYS A 1 704  ? -17.696 82.161  117.812 1.00 18.48 ?  702  CYS A C     1 
ATOM   5275  O O     . CYS A 1 704  ? -18.702 82.603  118.374 1.00 19.25 ?  702  CYS A O     1 
ATOM   5276  C CB    . CYS A 1 704  ? -17.830 79.793  118.627 1.00 19.32 ?  702  CYS A CB    1 
ATOM   5277  S SG    . CYS A 1 704  ? -16.999 78.353  119.343 1.00 18.97 ?  702  CYS A SG    1 
ATOM   5278  N N     . ILE A 1 705  ? -17.241 82.622  116.651 1.00 18.47 ?  703  ILE A N     1 
ATOM   5279  C CA    . ILE A 1 705  ? -17.870 83.713  115.920 1.00 17.14 ?  703  ILE A CA    1 
ATOM   5280  C C     . ILE A 1 705  ? -18.436 83.125  114.636 1.00 17.73 ?  703  ILE A C     1 
ATOM   5281  O O     . ILE A 1 705  ? -17.690 82.580  113.814 1.00 16.92 ?  703  ILE A O     1 
ATOM   5282  C CB    . ILE A 1 705  ? -16.869 84.844  115.644 1.00 19.46 ?  703  ILE A CB    1 
ATOM   5283  C CG1   . ILE A 1 705  ? -16.350 85.406  116.968 1.00 20.33 ?  703  ILE A CG1   1 
ATOM   5284  C CG2   . ILE A 1 705  ? -17.486 85.918  114.765 1.00 21.14 ?  703  ILE A CG2   1 
ATOM   5285  C CD1   . ILE A 1 705  ? -15.190 86.348  116.812 1.00 23.31 ?  703  ILE A CD1   1 
ATOM   5286  N N     . SER A 1 706  ? -19.752 83.218  114.477 1.00 17.94 ?  704  SER A N     1 
ATOM   5287  C CA    . SER A 1 706  ? -20.475 82.521  113.430 1.00 17.31 ?  704  SER A CA    1 
ATOM   5288  C C     . SER A 1 706  ? -21.140 83.504  112.476 1.00 16.25 ?  704  SER A C     1 
ATOM   5289  O O     . SER A 1 706  ? -21.371 84.672  112.817 1.00 18.61 ?  704  SER A O     1 
ATOM   5290  C CB    . SER A 1 706  ? -21.516 81.575  114.044 1.00 19.49 ?  704  SER A CB    1 
ATOM   5291  O OG    . SER A 1 706  ? -22.382 82.273  114.905 1.00 20.80 ?  704  SER A OG    1 
ATOM   5292  N N     . PRO A 1 707  ? -21.445 83.055  111.262 1.00 16.70 ?  705  PRO A N     1 
ATOM   5293  C CA    . PRO A 1 707  ? -21.915 83.957  110.207 1.00 16.52 ?  705  PRO A CA    1 
ATOM   5294  C C     . PRO A 1 707  ? -23.431 83.997  110.119 1.00 17.43 ?  705  PRO A C     1 
ATOM   5295  O O     . PRO A 1 707  ? -24.114 83.201  110.776 1.00 17.75 ?  705  PRO A O     1 
ATOM   5296  C CB    . PRO A 1 707  ? -21.288 83.337  108.956 1.00 17.64 ?  705  PRO A CB    1 
ATOM   5297  C CG    . PRO A 1 707  ? -21.374 81.858  109.242 1.00 16.95 ?  705  PRO A CG    1 
ATOM   5298  C CD    . PRO A 1 707  ? -21.050 81.743  110.720 1.00 17.31 ?  705  PRO A CD    1 
ATOM   5299  N N     . TRP A 1 708  ? -23.970 84.927  109.331 1.00 17.94 ?  706  TRP A N     1 
ATOM   5300  C CA    . TRP A 1 708  ? -25.417 85.051  109.190 1.00 15.40 ?  706  TRP A CA    1 
ATOM   5301  C C     . TRP A 1 708  ? -25.968 84.168  108.078 1.00 17.80 ?  706  TRP A C     1 
ATOM   5302  O O     . TRP A 1 708  ? -27.186 83.971  108.002 1.00 19.40 ?  706  TRP A O     1 
ATOM   5303  C CB    . TRP A 1 708  ? -25.811 86.525  108.941 1.00 18.84 ?  706  TRP A CB    1 
ATOM   5304  C CG    . TRP A 1 708  ? -24.997 87.171  107.863 1.00 19.41 ?  706  TRP A CG    1 
ATOM   5305  C CD1   . TRP A 1 708  ? -23.922 87.991  108.032 1.00 20.54 ?  706  TRP A CD1   1 
ATOM   5306  C CD2   . TRP A 1 708  ? -25.158 87.007  106.446 1.00 18.10 ?  706  TRP A CD2   1 
ATOM   5307  N NE1   . TRP A 1 708  ? -23.410 88.361  106.815 1.00 21.24 ?  706  TRP A NE1   1 
ATOM   5308  C CE2   . TRP A 1 708  ? -24.144 87.764  105.822 1.00 20.30 ?  706  TRP A CE2   1 
ATOM   5309  C CE3   . TRP A 1 708  ? -26.055 86.288  105.646 1.00 15.63 ?  706  TRP A CE3   1 
ATOM   5310  C CZ2   . TRP A 1 708  ? -24.007 87.832  104.433 1.00 19.22 ?  706  TRP A CZ2   1 
ATOM   5311  C CZ3   . TRP A 1 708  ? -25.928 86.360  104.274 1.00 18.34 ?  706  TRP A CZ3   1 
ATOM   5312  C CH2   . TRP A 1 708  ? -24.900 87.119  103.676 1.00 20.48 ?  706  TRP A CH2   1 
ATOM   5313  N N     . ASN A 1 709  ? -25.105 83.622  107.229 1.00 16.37 ?  707  ASN A N     1 
ATOM   5314  C CA    . ASN A 1 709  ? -25.585 82.876  106.075 1.00 16.00 ?  707  ASN A CA    1 
ATOM   5315  C C     . ASN A 1 709  ? -25.879 81.418  106.397 1.00 17.36 ?  707  ASN A C     1 
ATOM   5316  O O     . ASN A 1 709  ? -26.660 80.786  105.680 1.00 19.62 ?  707  ASN A O     1 
ATOM   5317  C CB    . ASN A 1 709  ? -24.579 83.004  104.926 1.00 17.11 ?  707  ASN A CB    1 
ATOM   5318  C CG    . ASN A 1 709  ? -23.310 82.217  105.148 1.00 17.02 ?  707  ASN A CG    1 
ATOM   5319  O OD1   . ASN A 1 709  ? -22.904 81.960  106.276 1.00 19.85 ?  707  ASN A OD1   1 
ATOM   5320  N ND2   . ASN A 1 709  ? -22.650 81.855  104.046 1.00 17.69 ?  707  ASN A ND2   1 
ATOM   5321  N N     . PHE A 1 710  ? -25.294 80.881  107.465 1.00 18.62 ?  708  PHE A N     1 
ATOM   5322  C CA    . PHE A 1 710  ? -25.671 79.581  108.017 1.00 15.25 ?  708  PHE A CA    1 
ATOM   5323  C C     . PHE A 1 710  ? -25.802 79.759  109.520 1.00 15.65 ?  708  PHE A C     1 
ATOM   5324  O O     . PHE A 1 710  ? -24.972 79.288  110.312 1.00 17.79 ?  708  PHE A O     1 
ATOM   5325  C CB    . PHE A 1 710  ? -24.671 78.492  107.637 1.00 15.45 ?  708  PHE A CB    1 
ATOM   5326  C CG    . PHE A 1 710  ? -24.785 78.084  106.198 1.00 17.99 ?  708  PHE A CG    1 
ATOM   5327  C CD1   . PHE A 1 710  ? -25.713 77.135  105.819 1.00 20.42 ?  708  PHE A CD1   1 
ATOM   5328  C CD2   . PHE A 1 710  ? -23.993 78.678  105.228 1.00 18.24 ?  708  PHE A CD2   1 
ATOM   5329  C CE1   . PHE A 1 710  ? -25.840 76.759  104.492 1.00 19.59 ?  708  PHE A CE1   1 
ATOM   5330  C CE2   . PHE A 1 710  ? -24.116 78.306  103.888 1.00 19.23 ?  708  PHE A CE2   1 
ATOM   5331  C CZ    . PHE A 1 710  ? -25.043 77.347  103.525 1.00 20.48 ?  708  PHE A CZ    1 
ATOM   5332  N N     . PRO A 1 711  ? -26.854 80.461  109.944 1.00 16.19 ?  709  PRO A N     1 
ATOM   5333  C CA    . PRO A 1 711  ? -26.937 80.933  111.326 1.00 18.29 ?  709  PRO A CA    1 
ATOM   5334  C C     . PRO A 1 711  ? -27.291 79.860  112.330 1.00 16.40 ?  709  PRO A C     1 
ATOM   5335  O O     . PRO A 1 711  ? -27.205 80.119  113.536 1.00 19.13 ?  709  PRO A O     1 
ATOM   5336  C CB    . PRO A 1 711  ? -28.039 81.988  111.254 1.00 19.34 ?  709  PRO A CB    1 
ATOM   5337  C CG    . PRO A 1 711  ? -28.958 81.463  110.172 1.00 16.90 ?  709  PRO A CG    1 
ATOM   5338  C CD    . PRO A 1 711  ? -28.047 80.820  109.149 1.00 17.38 ?  709  PRO A CD    1 
ATOM   5339  N N     . LEU A 1 712  ? -27.717 78.683  111.887 1.00 16.32 ?  710  LEU A N     1 
ATOM   5340  C CA    . LEU A 1 712  ? -27.848 77.537  112.773 1.00 16.03 ?  710  LEU A CA    1 
ATOM   5341  C C     . LEU A 1 712  ? -26.744 76.517  112.551 1.00 17.03 ?  710  LEU A C     1 
ATOM   5342  O O     . LEU A 1 712  ? -26.133 76.053  113.517 1.00 16.94 ?  710  LEU A O     1 
ATOM   5343  C CB    . LEU A 1 712  ? -29.214 76.857  112.601 1.00 16.71 ?  710  LEU A CB    1 
ATOM   5344  C CG    . LEU A 1 712  ? -29.394 75.680  113.572 1.00 19.53 ?  710  LEU A CG    1 
ATOM   5345  C CD1   . LEU A 1 712  ? -29.427 76.140  115.045 1.00 17.43 ?  710  LEU A CD1   1 
ATOM   5346  C CD2   . LEU A 1 712  ? -30.621 74.863  113.206 1.00 18.67 ?  710  LEU A CD2   1 
ATOM   5347  N N     . ALA A 1 713  ? -26.440 76.179  111.298 1.00 15.04 ?  711  ALA A N     1 
ATOM   5348  C CA    . ALA A 1 713  ? -25.556 75.048  111.059 1.00 13.79 ?  711  ALA A CA    1 
ATOM   5349  C C     . ALA A 1 713  ? -24.111 75.369  111.432 1.00 15.49 ?  711  ALA A C     1 
ATOM   5350  O O     . ALA A 1 713  ? -23.466 74.602  112.155 1.00 16.14 ?  711  ALA A O     1 
ATOM   5351  C CB    . ALA A 1 713  ? -25.649 74.603  109.600 1.00 16.17 ?  711  ALA A CB    1 
ATOM   5352  N N     . ILE A 1 714  ? -23.565 76.480  110.934 1.00 14.43 ?  712  ILE A N     1 
ATOM   5353  C CA    . ILE A 1 714  ? -22.164 76.757  111.250 1.00 16.23 ?  712  ILE A CA    1 
ATOM   5354  C C     . ILE A 1 714  ? -22.042 77.215  112.701 1.00 17.78 ?  712  ILE A C     1 
ATOM   5355  O O     . ILE A 1 714  ? -21.057 76.896  113.388 1.00 17.09 ?  712  ILE A O     1 
ATOM   5356  C CB    . ILE A 1 714  ? -21.582 77.781  110.257 1.00 15.06 ?  712  ILE A CB    1 
ATOM   5357  C CG1   . ILE A 1 714  ? -21.434 77.119  108.875 1.00 16.89 ?  712  ILE A CG1   1 
ATOM   5358  C CG2   . ILE A 1 714  ? -20.229 78.313  110.748 1.00 16.34 ?  712  ILE A CG2   1 
ATOM   5359  C CD1   . ILE A 1 714  ? -20.868 78.018  107.782 1.00 19.91 ?  712  ILE A CD1   1 
ATOM   5360  N N     . PHE A 1 715  ? -23.042 77.948  113.195 1.00 17.48 ?  713  PHE A N     1 
ATOM   5361  C CA    . PHE A 1 715  ? -23.133 78.258  114.619 1.00 16.58 ?  713  PHE A CA    1 
ATOM   5362  C C     . PHE A 1 715  ? -23.006 76.994  115.464 1.00 16.79 ?  713  PHE A C     1 
ATOM   5363  O O     . PHE A 1 715  ? -22.152 76.903  116.358 1.00 15.84 ?  713  PHE A O     1 
ATOM   5364  C CB    . PHE A 1 715  ? -24.474 78.957  114.879 1.00 18.18 ?  713  PHE A CB    1 
ATOM   5365  C CG    . PHE A 1 715  ? -24.742 79.255  116.317 1.00 17.54 ?  713  PHE A CG    1 
ATOM   5366  C CD1   . PHE A 1 715  ? -24.225 80.405  116.899 1.00 18.68 ?  713  PHE A CD1   1 
ATOM   5367  C CD2   . PHE A 1 715  ? -25.523 78.404  117.093 1.00 20.82 ?  713  PHE A CD2   1 
ATOM   5368  C CE1   . PHE A 1 715  ? -24.476 80.705  118.230 1.00 21.53 ?  713  PHE A CE1   1 
ATOM   5369  C CE2   . PHE A 1 715  ? -25.772 78.699  118.431 1.00 20.26 ?  713  PHE A CE2   1 
ATOM   5370  C CZ    . PHE A 1 715  ? -25.251 79.848  118.996 1.00 19.60 ?  713  PHE A CZ    1 
ATOM   5371  N N     . THR A 1 716  ? -23.847 75.998  115.174 1.00 17.24 ?  714  THR A N     1 
ATOM   5372  C CA    . THR A 1 716  ? -23.849 74.752  115.936 1.00 17.96 ?  714  THR A CA    1 
ATOM   5373  C C     . THR A 1 716  ? -22.555 73.978  115.742 1.00 16.07 ?  714  THR A C     1 
ATOM   5374  O O     . THR A 1 716  ? -22.015 73.425  116.702 1.00 16.36 ?  714  THR A O     1 
ATOM   5375  C CB    . THR A 1 716  ? -25.042 73.893  115.518 1.00 18.03 ?  714  THR A CB    1 
ATOM   5376  O OG1   . THR A 1 716  ? -26.247 74.590  115.828 1.00 17.82 ?  714  THR A OG1   1 
ATOM   5377  C CG2   . THR A 1 716  ? -25.047 72.548  116.229 1.00 19.89 ?  714  THR A CG2   1 
ATOM   5378  N N     . GLY A 1 717  ? -22.045 73.924  114.510 1.00 15.12 ?  715  GLY A N     1 
ATOM   5379  C CA    . GLY A 1 717  ? -20.860 73.120  114.244 1.00 15.71 ?  715  GLY A CA    1 
ATOM   5380  C C     . GLY A 1 717  ? -19.654 73.571  115.048 1.00 16.67 ?  715  GLY A C     1 
ATOM   5381  O O     . GLY A 1 717  ? -18.981 72.760  115.691 1.00 17.46 ?  715  GLY A O     1 
ATOM   5382  N N     . GLN A 1 718  ? -19.368 74.878  115.029 1.00 14.69 ?  716  GLN A N     1 
ATOM   5383  C CA    . GLN A 1 718  ? -18.200 75.377  115.749 1.00 16.17 ?  716  GLN A CA    1 
ATOM   5384  C C     . GLN A 1 718  ? -18.349 75.127  117.243 1.00 15.93 ?  716  GLN A C     1 
ATOM   5385  O O     . GLN A 1 718  ? -17.425 74.634  117.900 1.00 16.74 ?  716  GLN A O     1 
ATOM   5386  C CB    . GLN A 1 718  ? -17.995 76.871  115.483 1.00 16.30 ?  716  GLN A CB    1 
ATOM   5387  C CG    . GLN A 1 718  ? -17.690 77.198  114.026 1.00 16.26 ?  716  GLN A CG    1 
ATOM   5388  C CD    . GLN A 1 718  ? -17.385 78.672  113.756 1.00 16.78 ?  716  GLN A CD    1 
ATOM   5389  O OE1   . GLN A 1 718  ? -16.492 78.987  112.965 1.00 17.68 ?  716  GLN A OE1   1 
ATOM   5390  N NE2   . GLN A 1 718  ? -18.130 79.573  114.386 1.00 16.94 ?  716  GLN A NE2   1 
ATOM   5391  N N     . ILE A 1 719  ? -19.517 75.470  117.797 1.00 16.22 ?  717  ILE A N     1 
ATOM   5392  C CA    . ILE A 1 719  ? -19.755 75.343  119.230 1.00 16.23 ?  717  ILE A CA    1 
ATOM   5393  C C     . ILE A 1 719  ? -19.716 73.885  119.673 1.00 17.68 ?  717  ILE A C     1 
ATOM   5394  O O     . ILE A 1 719  ? -19.129 73.559  120.714 1.00 17.77 ?  717  ILE A O     1 
ATOM   5395  C CB    . ILE A 1 719  ? -21.093 76.012  119.591 1.00 19.78 ?  717  ILE A CB    1 
ATOM   5396  C CG1   . ILE A 1 719  ? -20.963 77.526  119.452 1.00 19.88 ?  717  ILE A CG1   1 
ATOM   5397  C CG2   . ILE A 1 719  ? -21.540 75.610  120.983 1.00 23.57 ?  717  ILE A CG2   1 
ATOM   5398  C CD1   . ILE A 1 719  ? -22.287 78.209  119.276 1.00 23.43 ?  717  ILE A CD1   1 
ATOM   5399  N N     . ALA A 1 720  ? -20.353 72.991  118.912 1.00 16.93 ?  718  ALA A N     1 
ATOM   5400  C CA    . ALA A 1 720  ? -20.384 71.581  119.293 1.00 17.25 ?  718  ALA A CA    1 
ATOM   5401  C C     . ALA A 1 720  ? -18.984 70.993  119.331 1.00 15.87 ?  718  ALA A C     1 
ATOM   5402  O O     . ALA A 1 720  ? -18.645 70.249  120.258 1.00 17.50 ?  718  ALA A O     1 
ATOM   5403  C CB    . ALA A 1 720  ? -21.265 70.781  118.325 1.00 16.59 ?  718  ALA A CB    1 
ATOM   5404  N N     . ALA A 1 721  ? -18.168 71.312  118.327 1.00 16.06 ?  719  ALA A N     1 
ATOM   5405  C CA    . ALA A 1 721  ? -16.791 70.830  118.294 1.00 15.27 ?  719  ALA A CA    1 
ATOM   5406  C C     . ALA A 1 721  ? -16.013 71.322  119.507 1.00 15.73 ?  719  ALA A C     1 
ATOM   5407  O O     . ALA A 1 721  ? -15.369 70.536  120.209 1.00 16.93 ?  719  ALA A O     1 
ATOM   5408  C CB    . ALA A 1 721  ? -16.122 71.289  117.001 1.00 15.28 ?  719  ALA A CB    1 
ATOM   5409  N N     . ALA A 1 722  ? -16.065 72.627  119.771 1.00 15.70 ?  720  ALA A N     1 
ATOM   5410  C CA    . ALA A 1 722  ? -15.333 73.166  120.912 1.00 16.23 ?  720  ALA A CA    1 
ATOM   5411  C C     . ALA A 1 722  ? -15.809 72.538  122.221 1.00 19.10 ?  720  ALA A C     1 
ATOM   5412  O O     . ALA A 1 722  ? -14.997 72.109  123.049 1.00 18.66 ?  720  ALA A O     1 
ATOM   5413  C CB    . ALA A 1 722  ? -15.474 74.689  120.951 1.00 17.73 ?  720  ALA A CB    1 
ATOM   5414  N N     . LEU A 1 723  ? -17.130 72.456  122.414 1.00 17.44 ?  721  LEU A N     1 
ATOM   5415  C CA    . LEU A 1 723  ? -17.681 71.891  123.644 1.00 17.61 ?  721  LEU A CA    1 
ATOM   5416  C C     . LEU A 1 723  ? -17.277 70.433  123.827 1.00 17.73 ?  721  LEU A C     1 
ATOM   5417  O O     . LEU A 1 723  ? -16.887 70.017  124.927 1.00 17.96 ?  721  LEU A O     1 
ATOM   5418  C CB    . LEU A 1 723  ? -19.203 72.001  123.639 1.00 18.15 ?  721  LEU A CB    1 
ATOM   5419  C CG    . LEU A 1 723  ? -19.868 73.352  123.837 1.00 19.13 ?  721  LEU A CG    1 
ATOM   5420  C CD1   . LEU A 1 723  ? -21.365 73.213  123.569 1.00 20.06 ?  721  LEU A CD1   1 
ATOM   5421  C CD2   . LEU A 1 723  ? -19.618 73.858  125.258 1.00 20.57 ?  721  LEU A CD2   1 
ATOM   5422  N N     . VAL A 1 724  ? -17.383 69.628  122.767 1.00 17.62 ?  722  VAL A N     1 
ATOM   5423  C CA    . VAL A 1 724  ? -17.188 68.198  122.968 1.00 18.13 ?  722  VAL A CA    1 
ATOM   5424  C C     . VAL A 1 724  ? -15.707 67.894  123.166 1.00 18.53 ?  722  VAL A C     1 
ATOM   5425  O O     . VAL A 1 724  ? -15.354 66.913  123.833 1.00 18.39 ?  722  VAL A O     1 
ATOM   5426  C CB    . VAL A 1 724  ? -17.816 67.395  121.808 1.00 16.49 ?  722  VAL A CB    1 
ATOM   5427  C CG1   . VAL A 1 724  ? -16.924 67.392  120.582 1.00 18.41 ?  722  VAL A CG1   1 
ATOM   5428  C CG2   . VAL A 1 724  ? -18.155 65.981  122.259 1.00 16.50 ?  722  VAL A CG2   1 
ATOM   5429  N N     . ALA A 1 725  ? -14.823 68.746  122.632 1.00 17.20 ?  723  ALA A N     1 
ATOM   5430  C CA    . ALA A 1 725  ? -13.398 68.651  122.938 1.00 18.93 ?  723  ALA A CA    1 
ATOM   5431  C C     . ALA A 1 725  ? -13.068 69.100  124.352 1.00 20.56 ?  723  ALA A C     1 
ATOM   5432  O O     . ALA A 1 725  ? -11.880 69.080  124.706 1.00 21.76 ?  723  ALA A O     1 
ATOM   5433  C CB    . ALA A 1 725  ? -12.578 69.474  121.942 1.00 19.27 ?  723  ALA A CB    1 
ATOM   5434  N N     . GLY A 1 726  ? -14.057 69.502  125.156 1.00 18.52 ?  724  GLY A N     1 
ATOM   5435  C CA    . GLY A 1 726  ? -13.827 69.834  126.548 1.00 18.83 ?  724  GLY A CA    1 
ATOM   5436  C C     . GLY A 1 726  ? -13.631 71.299  126.876 1.00 20.40 ?  724  GLY A C     1 
ATOM   5437  O O     . GLY A 1 726  ? -13.235 71.614  128.009 1.00 22.63 ?  724  GLY A O     1 
ATOM   5438  N N     . ASN A 1 727  ? -13.884 72.198  125.936 1.00 20.93 ?  725  ASN A N     1 
ATOM   5439  C CA    . ASN A 1 727  ? -13.695 73.630  126.113 1.00 19.13 ?  725  ASN A CA    1 
ATOM   5440  C C     . ASN A 1 727  ? -15.010 74.320  126.425 1.00 21.93 ?  725  ASN A C     1 
ATOM   5441  O O     . ASN A 1 727  ? -16.020 74.049  125.767 1.00 21.84 ?  725  ASN A O     1 
ATOM   5442  C CB    . ASN A 1 727  ? -13.127 74.256  124.840 1.00 19.83 ?  725  ASN A CB    1 
ATOM   5443  C CG    . ASN A 1 727  ? -11.893 73.545  124.334 1.00 20.21 ?  725  ASN A CG    1 
ATOM   5444  O OD1   . ASN A 1 727  ? -10.796 73.718  124.875 1.00 22.59 ?  725  ASN A OD1   1 
ATOM   5445  N ND2   . ASN A 1 727  ? -12.063 72.735  123.301 1.00 18.97 ?  725  ASN A ND2   1 
ATOM   5446  N N     . PRO A 1 728  ? -15.045 75.251  127.372 1.00 19.77 ?  726  PRO A N     1 
ATOM   5447  C CA    . PRO A 1 728  ? -16.216 76.124  127.479 1.00 20.75 ?  726  PRO A CA    1 
ATOM   5448  C C     . PRO A 1 728  ? -16.207 77.132  126.341 1.00 20.92 ?  726  PRO A C     1 
ATOM   5449  O O     . PRO A 1 728  ? -15.149 77.503  125.829 1.00 21.45 ?  726  PRO A O     1 
ATOM   5450  C CB    . PRO A 1 728  ? -16.039 76.798  128.845 1.00 21.92 ?  726  PRO A CB    1 
ATOM   5451  C CG    . PRO A 1 728  ? -14.569 76.822  129.059 1.00 22.29 ?  726  PRO A CG    1 
ATOM   5452  C CD    . PRO A 1 728  ? -13.973 75.639  128.310 1.00 20.49 ?  726  PRO A CD    1 
ATOM   5453  N N     . VAL A 1 729  ? -17.403 77.567  125.934 1.00 20.43 ?  727  VAL A N     1 
ATOM   5454  C CA    . VAL A 1 729  ? -17.581 78.344  124.709 1.00 19.27 ?  727  VAL A CA    1 
ATOM   5455  C C     . VAL A 1 729  ? -18.236 79.688  125.009 1.00 19.78 ?  727  VAL A C     1 
ATOM   5456  O O     . VAL A 1 729  ? -19.213 79.771  125.762 1.00 21.98 ?  727  VAL A O     1 
ATOM   5457  C CB    . VAL A 1 729  ? -18.417 77.565  123.669 1.00 19.36 ?  727  VAL A CB    1 
ATOM   5458  C CG1   . VAL A 1 729  ? -18.776 78.455  122.478 1.00 20.26 ?  727  VAL A CG1   1 
ATOM   5459  C CG2   . VAL A 1 729  ? -17.648 76.349  123.204 1.00 20.73 ?  727  VAL A CG2   1 
ATOM   5460  N N     . LEU A 1 730  ? -17.695 80.739  124.398 1.00 19.66 ?  728  LEU A N     1 
ATOM   5461  C CA    . LEU A 1 730  ? -18.367 82.024  124.262 1.00 21.85 ?  728  LEU A CA    1 
ATOM   5462  C C     . LEU A 1 730  ? -18.868 82.095  122.827 1.00 20.02 ?  728  LEU A C     1 
ATOM   5463  O O     . LEU A 1 730  ? -18.062 82.180  121.894 1.00 19.77 ?  728  LEU A O     1 
ATOM   5464  C CB    . LEU A 1 730  ? -17.427 83.190  124.568 1.00 22.81 ?  728  LEU A CB    1 
ATOM   5465  C CG    . LEU A 1 730  ? -16.719 83.266  125.927 1.00 21.51 ?  728  LEU A CG    1 
ATOM   5466  C CD1   . LEU A 1 730  ? -17.704 82.989  127.065 1.00 22.82 ?  728  LEU A CD1   1 
ATOM   5467  C CD2   . LEU A 1 730  ? -15.514 82.341  125.999 1.00 21.49 ?  728  LEU A CD2   1 
ATOM   5468  N N     . ALA A 1 731  ? -20.186 82.045  122.645 1.00 19.76 ?  729  ALA A N     1 
ATOM   5469  C CA    . ALA A 1 731  ? -20.800 82.030  121.319 1.00 20.06 ?  729  ALA A CA    1 
ATOM   5470  C C     . ALA A 1 731  ? -21.239 83.444  120.946 1.00 19.06 ?  729  ALA A C     1 
ATOM   5471  O O     . ALA A 1 731  ? -22.149 84.007  121.567 1.00 21.01 ?  729  ALA A O     1 
ATOM   5472  C CB    . ALA A 1 731  ? -21.978 81.062  121.292 1.00 21.03 ?  729  ALA A CB    1 
ATOM   5473  N N     . LYS A 1 732  ? -20.598 84.012  119.926 1.00 19.39 ?  730  LYS A N     1 
ATOM   5474  C CA    . LYS A 1 732  ? -20.936 85.335  119.412 1.00 22.14 ?  730  LYS A CA    1 
ATOM   5475  C C     . LYS A 1 732  ? -21.606 85.168  118.053 1.00 21.02 ?  730  LYS A C     1 
ATOM   5476  O O     . LYS A 1 732  ? -20.910 84.994  117.037 1.00 20.14 ?  730  LYS A O     1 
ATOM   5477  C CB    . LYS A 1 732  ? -19.680 86.204  119.291 1.00 21.98 ?  730  LYS A CB    1 
ATOM   5478  C CG    . LYS A 1 732  ? -19.878 87.680  119.621 1.00 25.38 ?  730  LYS A CG    1 
ATOM   5479  C CD    . LYS A 1 732  ? -20.896 88.366  118.720 1.00 27.67 ?  730  LYS A CD    1 
ATOM   5480  C CE    . LYS A 1 732  ? -20.354 88.567  117.318 1.00 31.06 ?  730  LYS A CE    1 
ATOM   5481  N NZ    . LYS A 1 732  ? -21.368 89.257  116.461 1.00 30.59 ?  730  LYS A NZ    1 
ATOM   5482  N N     . PRO A 1 733  ? -22.936 85.206  117.972 1.00 18.62 ?  731  PRO A N     1 
ATOM   5483  C CA    . PRO A 1 733  ? -23.600 85.035  116.677 1.00 20.23 ?  731  PRO A CA    1 
ATOM   5484  C C     . PRO A 1 733  ? -23.563 86.316  115.863 1.00 18.49 ?  731  PRO A C     1 
ATOM   5485  O O     . PRO A 1 733  ? -23.425 87.418  116.397 1.00 21.97 ?  731  PRO A O     1 
ATOM   5486  C CB    . PRO A 1 733  ? -25.038 84.686  117.065 1.00 21.71 ?  731  PRO A CB    1 
ATOM   5487  C CG    . PRO A 1 733  ? -25.251 85.453  118.333 1.00 22.25 ?  731  PRO A CG    1 
ATOM   5488  C CD    . PRO A 1 733  ? -23.911 85.365  119.068 1.00 20.94 ?  731  PRO A CD    1 
ATOM   5489  N N     . ALA A 1 734  ? -23.734 86.153  114.549 1.00 20.73 ?  732  ALA A N     1 
ATOM   5490  C CA    . ALA A 1 734  ? -23.815 87.308  113.662 1.00 21.81 ?  732  ALA A CA    1 
ATOM   5491  C C     . ALA A 1 734  ? -24.883 88.289  114.136 1.00 20.18 ?  732  ALA A C     1 
ATOM   5492  O O     . ALA A 1 734  ? -25.949 87.897  114.628 1.00 21.57 ?  732  ALA A O     1 
ATOM   5493  C CB    . ALA A 1 734  ? -24.116 86.856  112.231 1.00 19.22 ?  732  ALA A CB    1 
ATOM   5494  N N     . GLU A 1 735  ? -24.589 89.579  113.981 1.00 22.69 ?  733  GLU A N     1 
ATOM   5495  C CA    . GLU A 1 735  ? -25.521 90.619  114.408 1.00 24.08 ?  733  GLU A CA    1 
ATOM   5496  C C     . GLU A 1 735  ? -26.908 90.440  113.789 1.00 20.97 ?  733  GLU A C     1 
ATOM   5497  O O     . GLU A 1 735  ? -27.925 90.749  114.431 1.00 23.11 ?  733  GLU A O     1 
ATOM   5498  C CB    . GLU A 1 735  ? -24.943 91.988  114.044 1.00 27.82 ?  733  GLU A CB    1 
ATOM   5499  C CG    . GLU A 1 735  ? -25.683 93.177  114.634 1.00 35.16 ?  733  GLU A CG    1 
ATOM   5500  C CD    . GLU A 1 735  ? -25.000 94.493  114.310 1.00 41.10 ?  733  GLU A CD    1 
ATOM   5501  O OE1   . GLU A 1 735  ? -23.926 94.463  113.670 1.00 42.97 ?  733  GLU A OE1   1 
ATOM   5502  O OE2   . GLU A 1 735  ? -25.537 95.554  114.699 1.00 48.61 ?  733  GLU A OE2   1 
ATOM   5503  N N     . GLU A 1 736  ? -26.965 89.922  112.557 1.00 20.61 ?  734  GLU A N     1 
ATOM   5504  C CA    . GLU A 1 736  ? -28.202 89.829  111.796 1.00 21.19 ?  734  GLU A CA    1 
ATOM   5505  C C     . GLU A 1 736  ? -29.091 88.664  112.217 1.00 22.40 ?  734  GLU A C     1 
ATOM   5506  O O     . GLU A 1 736  ? -30.301 88.710  111.972 1.00 22.59 ?  734  GLU A O     1 
ATOM   5507  C CB    . GLU A 1 736  ? -27.872 89.696  110.306 1.00 23.53 ?  734  GLU A CB    1 
ATOM   5508  C CG    . GLU A 1 736  ? -27.112 90.885  109.711 1.00 26.28 ?  734  GLU A CG    1 
ATOM   5509  C CD    . GLU A 1 736  ? -25.582 90.784  109.801 1.00 32.02 ?  734  GLU A CD    1 
ATOM   5510  O OE1   . GLU A 1 736  ? -25.037 89.951  110.577 1.00 24.08 ?  734  GLU A OE1   1 
ATOM   5511  O OE2   . GLU A 1 736  ? -24.917 91.563  109.076 1.00 34.40 ?  734  GLU A OE2   1 
ATOM   5512  N N     . THR A 1 737  ? -28.537 87.620  112.830 1.00 19.47 ?  735  THR A N     1 
ATOM   5513  C CA    . THR A 1 737  ? -29.277 86.377  113.072 1.00 21.16 ?  735  THR A CA    1 
ATOM   5514  C C     . THR A 1 737  ? -29.081 85.868  114.502 1.00 20.87 ?  735  THR A C     1 
ATOM   5515  O O     . THR A 1 737  ? -28.677 84.720  114.715 1.00 22.19 ?  735  THR A O     1 
ATOM   5516  C CB    . THR A 1 737  ? -28.857 85.310  112.059 1.00 19.14 ?  735  THR A CB    1 
ATOM   5517  O OG1   . THR A 1 737  ? -27.437 85.130  112.124 1.00 18.87 ?  735  THR A OG1   1 
ATOM   5518  C CG2   . THR A 1 737  ? -29.238 85.733  110.636 1.00 19.54 ?  735  THR A CG2   1 
ATOM   5519  N N     . PRO A 1 738  ? -29.395 86.687  115.512 1.00 19.44 ?  736  PRO A N     1 
ATOM   5520  C CA    . PRO A 1 738  ? -29.252 86.219  116.901 1.00 20.84 ?  736  PRO A CA    1 
ATOM   5521  C C     . PRO A 1 738  ? -30.339 85.265  117.372 1.00 20.34 ?  736  PRO A C     1 
ATOM   5522  O O     . PRO A 1 738  ? -30.094 84.526  118.338 1.00 22.46 ?  736  PRO A O     1 
ATOM   5523  C CB    . PRO A 1 738  ? -29.308 87.524  117.709 1.00 20.23 ?  736  PRO A CB    1 
ATOM   5524  C CG    . PRO A 1 738  ? -30.248 88.362  116.918 1.00 20.40 ?  736  PRO A CG    1 
ATOM   5525  C CD    . PRO A 1 738  ? -29.902 88.073  115.465 1.00 19.71 ?  736  PRO A CD    1 
ATOM   5526  N N     . LEU A 1 739  ? -31.537 85.281  116.774 1.00 20.18 ?  737  LEU A N     1 
ATOM   5527  C CA    . LEU A 1 739  ? -32.650 84.533  117.363 1.00 20.22 ?  737  LEU A CA    1 
ATOM   5528  C C     . LEU A 1 739  ? -32.448 83.033  117.214 1.00 19.93 ?  737  LEU A C     1 
ATOM   5529  O O     . LEU A 1 739  ? -32.644 82.276  118.173 1.00 21.33 ?  737  LEU A O     1 
ATOM   5530  C CB    . LEU A 1 739  ? -33.976 84.955  116.736 1.00 21.56 ?  737  LEU A CB    1 
ATOM   5531  C CG    . LEU A 1 739  ? -34.302 86.434  116.883 1.00 23.12 ?  737  LEU A CG    1 
ATOM   5532  C CD1   . LEU A 1 739  ? -35.580 86.745  116.112 1.00 22.59 ?  737  LEU A CD1   1 
ATOM   5533  C CD2   . LEU A 1 739  ? -34.444 86.827  118.352 1.00 22.34 ?  737  LEU A CD2   1 
ATOM   5534  N N     . ILE A 1 740  ? -32.056 82.582  116.017 1.00 18.67 ?  738  ILE A N     1 
ATOM   5535  C CA    . ILE A 1 740  ? -31.839 81.154  115.827 1.00 20.69 ?  738  ILE A CA    1 
ATOM   5536  C C     . ILE A 1 740  ? -30.644 80.700  116.647 1.00 19.22 ?  738  ILE A C     1 
ATOM   5537  O O     . ILE A 1 740  ? -30.597 79.552  117.103 1.00 20.94 ?  738  ILE A O     1 
ATOM   5538  C CB    . ILE A 1 740  ? -31.670 80.824  114.329 1.00 19.82 ?  738  ILE A CB    1 
ATOM   5539  C CG1   . ILE A 1 740  ? -31.564 79.309  114.095 1.00 20.26 ?  738  ILE A CG1   1 
ATOM   5540  C CG2   . ILE A 1 740  ? -30.450 81.516  113.758 1.00 21.10 ?  738  ILE A CG2   1 
ATOM   5541  C CD1   . ILE A 1 740  ? -32.857 78.532  114.386 1.00 22.08 ?  738  ILE A CD1   1 
ATOM   5542  N N     . ALA A 1 741  ? -29.687 81.603  116.898 1.00 20.41 ?  739  ALA A N     1 
ATOM   5543  C CA    . ALA A 1 741  ? -28.569 81.263  117.771 1.00 20.30 ?  739  ALA A CA    1 
ATOM   5544  C C     . ALA A 1 741  ? -29.033 81.064  119.207 1.00 19.33 ?  739  ALA A C     1 
ATOM   5545  O O     . ALA A 1 741  ? -28.632 80.098  119.861 1.00 20.43 ?  739  ALA A O     1 
ATOM   5546  C CB    . ALA A 1 741  ? -27.499 82.348  117.712 1.00 21.08 ?  739  ALA A CB    1 
ATOM   5547  N N     . ALA A 1 742  ? -29.885 81.962  119.709 1.00 20.23 ?  740  ALA A N     1 
ATOM   5548  C CA    . ALA A 1 742  ? -30.418 81.800  121.055 1.00 20.06 ?  740  ALA A CA    1 
ATOM   5549  C C     . ALA A 1 742  ? -31.200 80.503  121.180 1.00 19.88 ?  740  ALA A C     1 
ATOM   5550  O O     . ALA A 1 742  ? -31.124 79.823  122.208 1.00 22.83 ?  740  ALA A O     1 
ATOM   5551  C CB    . ALA A 1 742  ? -31.295 83.000  121.423 1.00 21.23 ?  740  ALA A CB    1 
ATOM   5552  N N     . GLU A 1 743  ? -31.929 80.122  120.127 1.00 20.39 ?  741  GLU A N     1 
ATOM   5553  C CA    . GLU A 1 743  ? -32.675 78.869  120.173 1.00 21.93 ?  741  GLU A CA    1 
ATOM   5554  C C     . GLU A 1 743  ? -31.732 77.674  120.159 1.00 20.82 ?  741  GLU A C     1 
ATOM   5555  O O     . GLU A 1 743  ? -31.951 76.690  120.881 1.00 21.97 ?  741  GLU A O     1 
ATOM   5556  C CB    . GLU A 1 743  ? -33.668 78.812  119.011 1.00 21.27 ?  741  GLU A CB    1 
ATOM   5557  C CG    . GLU A 1 743  ? -34.424 77.489  118.870 1.00 22.85 ?  741  GLU A CG    1 
ATOM   5558  C CD    . GLU A 1 743  ? -35.368 77.188  120.030 1.00 23.97 ?  741  GLU A CD    1 
ATOM   5559  O OE1   . GLU A 1 743  ? -35.599 78.074  120.878 1.00 25.87 ?  741  GLU A OE1   1 
ATOM   5560  O OE2   . GLU A 1 743  ? -35.869 76.044  120.086 1.00 26.88 ?  741  GLU A OE2   1 
ATOM   5561  N N     . GLY A 1 744  ? -30.652 77.766  119.382 1.00 21.08 ?  742  GLY A N     1 
ATOM   5562  C CA    . GLY A 1 744  ? -29.641 76.723  119.411 1.00 19.06 ?  742  GLY A CA    1 
ATOM   5563  C C     . GLY A 1 744  ? -29.013 76.556  120.784 1.00 18.64 ?  742  GLY A C     1 
ATOM   5564  O O     . GLY A 1 744  ? -28.783 75.432  121.236 1.00 20.75 ?  742  GLY A O     1 
ATOM   5565  N N     . VAL A 1 745  ? -28.735 77.668  121.468 1.00 20.13 ?  743  VAL A N     1 
ATOM   5566  C CA    . VAL A 1 745  ? -28.164 77.591  122.813 1.00 20.82 ?  743  VAL A CA    1 
ATOM   5567  C C     . VAL A 1 745  ? -29.172 76.999  123.791 1.00 20.96 ?  743  VAL A C     1 
ATOM   5568  O O     . VAL A 1 745  ? -28.811 76.198  124.666 1.00 24.02 ?  743  VAL A O     1 
ATOM   5569  C CB    . VAL A 1 745  ? -27.665 78.977  123.263 1.00 20.85 ?  743  VAL A CB    1 
ATOM   5570  C CG1   . VAL A 1 745  ? -27.355 78.993  124.775 1.00 25.37 ?  743  VAL A CG1   1 
ATOM   5571  C CG2   . VAL A 1 745  ? -26.435 79.376  122.439 1.00 24.38 ?  743  VAL A CG2   1 
ATOM   5572  N N     . ARG A 1 746  ? -30.451 77.372  123.659 1.00 22.36 ?  744  ARG A N     1 
ATOM   5573  C CA    . ARG A 1 746  ? -31.470 76.778  124.521 1.00 20.95 ?  744  ARG A CA    1 
ATOM   5574  C C     . ARG A 1 746  ? -31.501 75.263  124.360 1.00 23.27 ?  744  ARG A C     1 
ATOM   5575  O O     . ARG A 1 746  ? -31.581 74.528  125.355 1.00 24.67 ?  744  ARG A O     1 
ATOM   5576  C CB    . ARG A 1 746  ? -32.842 77.381  124.205 1.00 21.72 ?  744  ARG A CB    1 
ATOM   5577  C CG    . ARG A 1 746  ? -33.929 76.952  125.152 1.00 25.94 ?  744  ARG A CG    1 
ATOM   5578  C CD    . ARG A 1 746  ? -35.319 77.241  124.595 1.00 24.91 ?  744  ARG A CD    1 
ATOM   5579  N NE    . ARG A 1 746  ? -35.625 76.402  123.442 1.00 27.16 ?  744  ARG A NE    1 
ATOM   5580  C CZ    . ARG A 1 746  ? -35.867 75.097  123.503 1.00 30.68 ?  744  ARG A CZ    1 
ATOM   5581  N NH1   . ARG A 1 746  ? -35.847 74.441  124.655 1.00 31.40 ?  744  ARG A NH1   1 
ATOM   5582  N NH2   . ARG A 1 746  ? -36.137 74.434  122.380 1.00 24.38 ?  744  ARG A NH2   1 
ATOM   5583  N N     . ILE A 1 747  ? -31.399 74.780  123.116 1.00 20.96 ?  745  ILE A N     1 
ATOM   5584  C CA    . ILE A 1 747  ? -31.440 73.343  122.850 1.00 21.92 ?  745  ILE A CA    1 
ATOM   5585  C C     . ILE A 1 747  ? -30.219 72.646  123.435 1.00 19.46 ?  745  ILE A C     1 
ATOM   5586  O O     . ILE A 1 747  ? -30.337 71.590  124.066 1.00 21.41 ?  745  ILE A O     1 
ATOM   5587  C CB    . ILE A 1 747  ? -31.584 73.089  121.337 1.00 20.40 ?  745  ILE A CB    1 
ATOM   5588  C CG1   . ILE A 1 747  ? -33.003 73.453  120.883 1.00 19.91 ?  745  ILE A CG1   1 
ATOM   5589  C CG2   . ILE A 1 747  ? -31.228 71.647  120.992 1.00 21.59 ?  745  ILE A CG2   1 
ATOM   5590  C CD1   . ILE A 1 747  ? -33.171 73.522  119.374 1.00 22.09 ?  745  ILE A CD1   1 
ATOM   5591  N N     . LEU A 1 748  ? -29.024 73.217  123.241 1.00 19.28 ?  746  LEU A N     1 
ATOM   5592  C CA    . LEU A 1 748  ? -27.815 72.604  123.793 1.00 20.83 ?  746  LEU A CA    1 
ATOM   5593  C C     . LEU A 1 748  ? -27.840 72.585  125.312 1.00 22.37 ?  746  LEU A C     1 
ATOM   5594  O O     . LEU A 1 748  ? -27.375 71.626  125.942 1.00 21.04 ?  746  LEU A O     1 
ATOM   5595  C CB    . LEU A 1 748  ? -26.576 73.349  123.304 1.00 19.97 ?  746  LEU A CB    1 
ATOM   5596  C CG    . LEU A 1 748  ? -26.147 72.973  121.892 1.00 23.64 ?  746  LEU A CG    1 
ATOM   5597  C CD1   . LEU A 1 748  ? -25.310 74.088  121.260 1.00 24.66 ?  746  LEU A CD1   1 
ATOM   5598  C CD2   . LEU A 1 748  ? -25.379 71.665  121.925 1.00 23.23 ?  746  LEU A CD2   1 
ATOM   5599  N N     . ARG A 1 749  ? -28.359 73.644  125.925 1.00 21.23 ?  747  ARG A N     1 
ATOM   5600  C CA    . ARG A 1 749  ? -28.470 73.644  127.377 1.00 22.66 ?  747  ARG A CA    1 
ATOM   5601  C C     . ARG A 1 749  ? -29.498 72.617  127.844 1.00 22.09 ?  747  ARG A C     1 
ATOM   5602  O O     . ARG A 1 749  ? -29.278 71.916  128.843 1.00 24.07 ?  747  ARG A O     1 
ATOM   5603  C CB    . ARG A 1 749  ? -28.809 75.053  127.864 1.00 23.70 ?  747  ARG A CB    1 
ATOM   5604  C CG    . ARG A 1 749  ? -27.594 75.986  127.924 1.00 25.37 ?  747  ARG A CG    1 
ATOM   5605  C CD    . ARG A 1 749  ? -27.989 77.405  128.293 1.00 29.57 ?  747  ARG A CD    1 
ATOM   5606  N NE    . ARG A 1 749  ? -26.834 78.271  128.505 1.00 26.22 ?  747  ARG A NE    1 
ATOM   5607  C CZ    . ARG A 1 749  ? -26.870 79.405  129.194 1.00 25.95 ?  747  ARG A CZ    1 
ATOM   5608  N NH1   . ARG A 1 749  ? -27.993 79.848  129.741 1.00 27.73 ?  747  ARG A NH1   1 
ATOM   5609  N NH2   . ARG A 1 749  ? -25.748 80.098  129.366 1.00 28.47 ?  747  ARG A NH2   1 
ATOM   5610  N N     . GLU A 1 750  ? -30.620 72.496  127.127 1.00 21.61 ?  748  GLU A N     1 
ATOM   5611  C CA    . GLU A 1 750  ? -31.595 71.469  127.481 1.00 22.64 ?  748  GLU A CA    1 
ATOM   5612  C C     . GLU A 1 750  ? -30.977 70.079  127.384 1.00 22.64 ?  748  GLU A C     1 
ATOM   5613  O O     . GLU A 1 750  ? -31.263 69.196  128.204 1.00 25.84 ?  748  GLU A O     1 
ATOM   5614  C CB    . GLU A 1 750  ? -32.827 71.570  126.578 1.00 22.03 ?  748  GLU A CB    1 
ATOM   5615  C CG    . GLU A 1 750  ? -33.934 70.589  126.965 1.00 26.80 ?  748  GLU A CG    1 
ATOM   5616  C CD    . GLU A 1 750  ? -35.072 70.542  125.962 1.00 29.44 ?  748  GLU A CD    1 
ATOM   5617  O OE1   . GLU A 1 750  ? -35.252 71.520  125.211 1.00 35.37 ?  748  GLU A OE1   1 
ATOM   5618  O OE2   . GLU A 1 750  ? -35.782 69.517  125.916 1.00 28.95 ?  748  GLU A OE2   1 
ATOM   5619  N N     . ALA A 1 751  ? -30.103 69.879  126.397 1.00 20.80 ?  749  ALA A N     1 
ATOM   5620  C CA    . ALA A 1 751  ? -29.426 68.606  126.174 1.00 23.32 ?  749  ALA A CA    1 
ATOM   5621  C C     . ALA A 1 751  ? -28.384 68.287  127.238 1.00 23.86 ?  749  ALA A C     1 
ATOM   5622  O O     . ALA A 1 751  ? -27.850 67.170  127.243 1.00 23.33 ?  749  ALA A O     1 
ATOM   5623  C CB    . ALA A 1 751  ? -28.769 68.614  124.791 1.00 21.68 ?  749  ALA A CB    1 
ATOM   5624  N N     . GLY A 1 752  ? -28.072 69.235  128.118 1.00 22.58 ?  750  GLY A N     1 
ATOM   5625  C CA    . GLY A 1 752  ? -27.172 68.996  129.233 1.00 24.59 ?  750  GLY A CA    1 
ATOM   5626  C C     . GLY A 1 752  ? -25.918 69.847  129.263 1.00 24.51 ?  750  GLY A C     1 
ATOM   5627  O O     . GLY A 1 752  ? -25.128 69.711  130.209 1.00 24.84 ?  750  GLY A O     1 
ATOM   5628  N N     . ILE A 1 753  ? -25.671 70.712  128.283 1.00 22.66 ?  751  ILE A N     1 
ATOM   5629  C CA    . ILE A 1 753  ? -24.512 71.600  128.337 1.00 23.38 ?  751  ILE A CA    1 
ATOM   5630  C C     . ILE A 1 753  ? -24.732 72.599  129.466 1.00 23.07 ?  751  ILE A C     1 
ATOM   5631  O O     . ILE A 1 753  ? -25.713 73.356  129.431 1.00 26.00 ?  751  ILE A O     1 
ATOM   5632  C CB    . ILE A 1 753  ? -24.301 72.329  127.002 1.00 21.48 ?  751  ILE A CB    1 
ATOM   5633  C CG1   . ILE A 1 753  ? -24.120 71.334  125.857 1.00 22.15 ?  751  ILE A CG1   1 
ATOM   5634  C CG2   . ILE A 1 753  ? -23.111 73.261  127.092 1.00 24.17 ?  751  ILE A CG2   1 
ATOM   5635  C CD1   . ILE A 1 753  ? -22.938 70.438  126.024 1.00 24.28 ?  751  ILE A CD1   1 
ATOM   5636  N N     . PRO A 1 754  ? -23.866 72.639  130.477 1.00 23.87 ?  752  PRO A N     1 
ATOM   5637  C CA    . PRO A 1 754  ? -24.073 73.585  131.579 1.00 26.13 ?  752  PRO A CA    1 
ATOM   5638  C C     . PRO A 1 754  ? -23.989 75.027  131.101 1.00 23.16 ?  752  PRO A C     1 
ATOM   5639  O O     . PRO A 1 754  ? -23.296 75.347  130.130 1.00 23.79 ?  752  PRO A O     1 
ATOM   5640  C CB    . PRO A 1 754  ? -22.938 73.252  132.553 1.00 27.55 ?  752  PRO A CB    1 
ATOM   5641  C CG    . PRO A 1 754  ? -22.494 71.879  132.175 1.00 26.18 ?  752  PRO A CG    1 
ATOM   5642  C CD    . PRO A 1 754  ? -22.688 71.787  130.690 1.00 23.42 ?  752  PRO A CD    1 
ATOM   5643  N N     . ALA A 1 755  ? -24.736 75.898  131.791 1.00 25.85 ?  753  ALA A N     1 
ATOM   5644  C CA    . ALA A 1 755  ? -24.761 77.312  131.432 1.00 23.92 ?  753  ALA A CA    1 
ATOM   5645  C C     . ALA A 1 755  ? -23.370 77.927  131.475 1.00 26.07 ?  753  ALA A C     1 
ATOM   5646  O O     . ALA A 1 755  ? -23.058 78.820  130.680 1.00 27.73 ?  753  ALA A O     1 
ATOM   5647  C CB    . ALA A 1 755  ? -25.702 78.074  132.371 1.00 28.04 ?  753  ALA A CB    1 
ATOM   5648  N N     . SER A 1 756  ? -22.523 77.467  132.393 1.00 25.93 ?  754  SER A N     1 
ATOM   5649  C CA    . SER A 1 756  ? -21.165 77.985  132.455 1.00 27.33 ?  754  SER A CA    1 
ATOM   5650  C C     . SER A 1 756  ? -20.304 77.501  131.297 1.00 26.17 ?  754  SER A C     1 
ATOM   5651  O O     . SER A 1 756  ? -19.258 78.102  131.029 1.00 25.89 ?  754  SER A O     1 
ATOM   5652  C CB    . SER A 1 756  ? -20.522 77.587  133.776 1.00 25.72 ?  754  SER A CB    1 
ATOM   5653  O OG    . SER A 1 756  ? -20.335 76.180  133.843 1.00 31.35 ?  754  SER A OG    1 
ATOM   5654  N N     . ALA A 1 757  ? -20.704 76.425  130.619 1.00 23.03 ?  755  ALA A N     1 
ATOM   5655  C CA    . ALA A 1 757  ? -19.931 75.909  129.497 1.00 22.26 ?  755  ALA A CA    1 
ATOM   5656  C C     . ALA A 1 757  ? -20.340 76.514  128.165 1.00 23.99 ?  755  ALA A C     1 
ATOM   5657  O O     . ALA A 1 757  ? -19.587 76.401  127.192 1.00 22.11 ?  755  ALA A O     1 
ATOM   5658  C CB    . ALA A 1 757  ? -20.062 74.383  129.417 1.00 25.33 ?  755  ALA A CB    1 
ATOM   5659  N N     . LEU A 1 758  ? -21.500 77.159  128.096 1.00 22.71 ?  756  LEU A N     1 
ATOM   5660  C CA    . LEU A 1 758  ? -21.991 77.710  126.839 1.00 22.14 ?  756  LEU A CA    1 
ATOM   5661  C C     . LEU A 1 758  ? -22.730 79.004  127.130 1.00 22.79 ?  756  LEU A C     1 
ATOM   5662  O O     . LEU A 1 758  ? -23.864 78.978  127.616 1.00 24.02 ?  756  LEU A O     1 
ATOM   5663  C CB    . LEU A 1 758  ? -22.890 76.716  126.111 1.00 22.33 ?  756  LEU A CB    1 
ATOM   5664  C CG    . LEU A 1 758  ? -23.570 77.242  124.847 1.00 22.09 ?  756  LEU A CG    1 
ATOM   5665  C CD1   . LEU A 1 758  ? -22.558 77.834  123.859 1.00 22.16 ?  756  LEU A CD1   1 
ATOM   5666  C CD2   . LEU A 1 758  ? -24.340 76.113  124.198 1.00 23.32 ?  756  LEU A CD2   1 
ATOM   5667  N N     . GLN A 1 759  ? -22.086 80.125  126.821 1.00 21.60 ?  757  GLN A N     1 
ATOM   5668  C CA    . GLN A 1 759  ? -22.630 81.454  127.036 1.00 23.08 ?  757  GLN A CA    1 
ATOM   5669  C C     . GLN A 1 759  ? -22.875 82.118  125.689 1.00 23.84 ?  757  GLN A C     1 
ATOM   5670  O O     . GLN A 1 759  ? -22.036 82.037  124.785 1.00 24.61 ?  757  GLN A O     1 
ATOM   5671  C CB    . GLN A 1 759  ? -21.680 82.305  127.889 1.00 23.49 ?  757  GLN A CB    1 
ATOM   5672  C CG    . GLN A 1 759  ? -21.499 81.779  129.296 1.00 23.29 ?  757  GLN A CG    1 
ATOM   5673  C CD    . GLN A 1 759  ? -20.450 82.548  130.082 1.00 24.46 ?  757  GLN A CD    1 
ATOM   5674  O OE1   . GLN A 1 759  ? -20.763 83.529  130.757 1.00 26.60 ?  757  GLN A OE1   1 
ATOM   5675  N NE2   . GLN A 1 759  ? -19.198 82.103  129.999 1.00 24.16 ?  757  GLN A NE2   1 
ATOM   5676  N N     . LEU A 1 760  ? -24.035 82.751  125.549 1.00 24.29 ?  758  LEU A N     1 
ATOM   5677  C CA    . LEU A 1 760  ? -24.423 83.420  124.314 1.00 22.58 ?  758  LEU A CA    1 
ATOM   5678  C C     . LEU A 1 760  ? -24.240 84.920  124.486 1.00 24.54 ?  758  LEU A C     1 
ATOM   5679  O O     . LEU A 1 760  ? -24.753 85.497  125.448 1.00 24.56 ?  758  LEU A O     1 
ATOM   5680  C CB    . LEU A 1 760  ? -25.879 83.112  123.962 1.00 22.11 ?  758  LEU A CB    1 
ATOM   5681  C CG    . LEU A 1 760  ? -26.370 83.765  122.668 1.00 23.10 ?  758  LEU A CG    1 
ATOM   5682  C CD1   . LEU A 1 760  ? -25.854 82.998  121.453 1.00 24.32 ?  758  LEU A CD1   1 
ATOM   5683  C CD2   . LEU A 1 760  ? -27.886 83.862  122.646 1.00 25.57 ?  758  LEU A CD2   1 
ATOM   5684  N N     . LEU A 1 761  ? -23.522 85.550  123.549 1.00 21.55 ?  759  LEU A N     1 
ATOM   5685  C CA    . LEU A 1 761  ? -23.209 86.982  123.609 1.00 24.01 ?  759  LEU A CA    1 
ATOM   5686  C C     . LEU A 1 761  ? -23.632 87.658  122.312 1.00 24.25 ?  759  LEU A C     1 
ATOM   5687  O O     . LEU A 1 761  ? -22.803 87.884  121.419 1.00 24.32 ?  759  LEU A O     1 
ATOM   5688  C CB    . LEU A 1 761  ? -21.718 87.222  123.851 1.00 22.46 ?  759  LEU A CB    1 
ATOM   5689  C CG    . LEU A 1 761  ? -21.039 86.811  125.161 1.00 25.62 ?  759  LEU A CG    1 
ATOM   5690  C CD1   . LEU A 1 761  ? -21.942 87.058  126.370 1.00 25.89 ?  759  LEU A CD1   1 
ATOM   5691  C CD2   . LEU A 1 761  ? -20.555 85.371  125.107 1.00 28.72 ?  759  LEU A CD2   1 
ATOM   5692  N N     . PRO A 1 762  ? -24.913 87.989  122.166 1.00 23.61 ?  760  PRO A N     1 
ATOM   5693  C CA    . PRO A 1 762  ? -25.358 88.669  120.943 1.00 24.24 ?  760  PRO A CA    1 
ATOM   5694  C C     . PRO A 1 762  ? -24.751 90.059  120.826 1.00 29.60 ?  760  PRO A C     1 
ATOM   5695  O O     . PRO A 1 762  ? -24.422 90.707  121.822 1.00 26.12 ?  760  PRO A O     1 
ATOM   5696  C CB    . PRO A 1 762  ? -26.884 88.752  121.109 1.00 24.01 ?  760  PRO A CB    1 
ATOM   5697  C CG    . PRO A 1 762  ? -27.224 87.806  122.234 1.00 21.96 ?  760  PRO A CG    1 
ATOM   5698  C CD    . PRO A 1 762  ? -26.019 87.761  123.113 1.00 22.69 ?  760  PRO A CD    1 
ATOM   5699  N N     . GLY A 1 763  ? -24.613 90.522  119.593 1.00 25.87 ?  761  GLY A N     1 
ATOM   5700  C CA    . GLY A 1 763  ? -24.159 91.875  119.357 1.00 31.34 ?  761  GLY A CA    1 
ATOM   5701  C C     . GLY A 1 763  ? -23.355 91.970  118.077 1.00 34.98 ?  761  GLY A C     1 
ATOM   5702  O O     . GLY A 1 763  ? -23.311 91.039  117.274 1.00 33.09 ?  761  GLY A O     1 
ATOM   5703  N N     . ASP A 1 764  ? -22.708 93.123  117.917 1.00 38.10 ?  762  ASP A N     1 
ATOM   5704  C CA    . ASP A 1 764  ? -21.963 93.451  116.709 1.00 37.22 ?  762  ASP A CA    1 
ATOM   5705  C C     . ASP A 1 764  ? -20.513 92.980  116.847 1.00 41.51 ?  762  ASP A C     1 
ATOM   5706  O O     . ASP A 1 764  ? -20.192 92.137  117.690 1.00 38.14 ?  762  ASP A O     1 
ATOM   5707  C CB    . ASP A 1 764  ? -22.066 94.955  116.427 1.00 43.28 ?  762  ASP A CB    1 
ATOM   5708  C CG    . ASP A 1 764  ? -21.626 95.808  117.607 1.00 48.06 ?  762  ASP A CG    1 
ATOM   5709  O OD1   . ASP A 1 764  ? -20.541 95.546  118.167 1.00 47.40 ?  762  ASP A OD1   1 
ATOM   5710  O OD2   . ASP A 1 764  ? -22.362 96.751  117.968 1.00 52.46 ?  762  ASP A OD2   1 
ATOM   5711  N N     . GLY A 1 765  ? -19.614 93.539  116.031 1.00 39.84 ?  763  GLY A N     1 
ATOM   5712  C CA    . GLY A 1 765  ? -18.248 93.054  115.967 1.00 43.04 ?  763  GLY A CA    1 
ATOM   5713  C C     . GLY A 1 765  ? -17.374 93.424  117.145 1.00 38.34 ?  763  GLY A C     1 
ATOM   5714  O O     . GLY A 1 765  ? -16.363 92.756  117.380 1.00 40.00 ?  763  GLY A O     1 
ATOM   5715  N N     . ARG A 1 766  ? -17.720 94.475  117.888 1.00 36.97 ?  764  ARG A N     1 
ATOM   5716  C CA    . ARG A 1 766  ? -16.910 94.816  119.048 1.00 41.05 ?  764  ARG A CA    1 
ATOM   5717  C C     . ARG A 1 766  ? -17.138 93.852  120.204 1.00 36.61 ?  764  ARG A C     1 
ATOM   5718  O O     . ARG A 1 766  ? -16.264 93.719  121.066 1.00 34.21 ?  764  ARG A O     1 
ATOM   5719  C CB    . ARG A 1 766  ? -17.178 96.258  119.491 1.00 46.44 ?  764  ARG A CB    1 
ATOM   5720  C CG    . ARG A 1 766  ? -18.443 96.447  120.282 1.00 49.33 ?  764  ARG A CG    1 
ATOM   5721  C CD    . ARG A 1 766  ? -19.080 97.783  119.969 1.00 52.33 ?  764  ARG A CD    1 
ATOM   5722  N NE    . ARG A 1 766  ? -20.533 97.683  120.009 1.00 55.25 ?  764  ARG A NE    1 
ATOM   5723  C CZ    . ARG A 1 766  ? -21.291 98.158  120.986 1.00 59.49 ?  764  ARG A CZ    1 
ATOM   5724  N NH1   . ARG A 1 766  ? -20.771 98.826  122.004 1.00 58.20 ?  764  ARG A NH1   1 
ATOM   5725  N NH2   . ARG A 1 766  ? -22.608 97.973  120.932 1.00 60.87 ?  764  ARG A NH2   1 
ATOM   5726  N N     . VAL A 1 767  ? -18.283 93.169  120.239 1.00 37.87 ?  765  VAL A N     1 
ATOM   5727  C CA    . VAL A 1 767  ? -18.431 92.051  121.163 1.00 34.27 ?  765  VAL A CA    1 
ATOM   5728  C C     . VAL A 1 767  ? -17.449 90.948  120.796 1.00 27.22 ?  765  VAL A C     1 
ATOM   5729  O O     . VAL A 1 767  ? -16.720 90.430  121.650 1.00 30.27 ?  765  VAL A O     1 
ATOM   5730  C CB    . VAL A 1 767  ? -19.883 91.541  121.172 1.00 29.20 ?  765  VAL A CB    1 
ATOM   5731  C CG1   . VAL A 1 767  ? -20.000 90.312  122.071 1.00 28.79 ?  765  VAL A CG1   1 
ATOM   5732  C CG2   . VAL A 1 767  ? -20.824 92.642  121.624 1.00 35.24 ?  765  VAL A CG2   1 
ATOM   5733  N N     . GLY A 1 768  ? -17.403 90.580  119.513 1.00 30.72 ?  766  GLY A N     1 
ATOM   5734  C CA    . GLY A 1 768  ? -16.428 89.593  119.081 1.00 26.87 ?  766  GLY A CA    1 
ATOM   5735  C C     . GLY A 1 768  ? -15.003 90.039  119.342 1.00 29.24 ?  766  GLY A C     1 
ATOM   5736  O O     . GLY A 1 768  ? -14.160 89.244  119.768 1.00 26.42 ?  766  GLY A O     1 
ATOM   5737  N N     . ALA A 1 769  ? -14.718 91.322  119.112 1.00 30.79 ?  767  ALA A N     1 
ATOM   5738  C CA    . ALA A 1 769  ? -13.363 91.819  119.320 1.00 30.07 ?  767  ALA A CA    1 
ATOM   5739  C C     . ALA A 1 769  ? -12.982 91.769  120.794 1.00 31.36 ?  767  ALA A C     1 
ATOM   5740  O O     . ALA A 1 769  ? -11.866 91.360  121.137 1.00 29.00 ?  767  ALA A O     1 
ATOM   5741  C CB    . ALA A 1 769  ? -13.238 93.242  118.779 1.00 32.43 ?  767  ALA A CB    1 
ATOM   5742  N N     . ALA A 1 770  ? -13.904 92.166  121.677 1.00 30.89 ?  768  ALA A N     1 
ATOM   5743  C CA    . ALA A 1 770  ? -13.644 92.107  123.113 1.00 31.65 ?  768  ALA A CA    1 
ATOM   5744  C C     . ALA A 1 770  ? -13.392 90.677  123.570 1.00 26.74 ?  768  ALA A C     1 
ATOM   5745  O O     . ALA A 1 770  ? -12.514 90.425  124.406 1.00 28.00 ?  768  ALA A O     1 
ATOM   5746  C CB    . ALA A 1 770  ? -14.819 92.710  123.882 1.00 31.88 ?  768  ALA A CB    1 
ATOM   5747  N N     . LEU A 1 771  ? -14.162 89.729  123.037 1.00 25.53 ?  769  LEU A N     1 
ATOM   5748  C CA    . LEU A 1 771  ? -13.952 88.326  123.371 1.00 24.92 ?  769  LEU A CA    1 
ATOM   5749  C C     . LEU A 1 771  ? -12.586 87.846  122.901 1.00 25.78 ?  769  LEU A C     1 
ATOM   5750  O O     . LEU A 1 771  ? -11.877 87.148  123.636 1.00 25.60 ?  769  LEU A O     1 
ATOM   5751  C CB    . LEU A 1 771  ? -15.060 87.475  122.743 1.00 25.18 ?  769  LEU A CB    1 
ATOM   5752  C CG    . LEU A 1 771  ? -16.486 87.712  123.250 1.00 24.00 ?  769  LEU A CG    1 
ATOM   5753  C CD1   . LEU A 1 771  ? -17.500 86.934  122.408 1.00 24.23 ?  769  LEU A CD1   1 
ATOM   5754  C CD2   . LEU A 1 771  ? -16.577 87.304  124.700 1.00 26.63 ?  769  LEU A CD2   1 
ATOM   5755  N N     . VAL A 1 772  ? -12.204 88.201  121.672 1.00 25.06 ?  770  VAL A N     1 
ATOM   5756  C CA    . VAL A 1 772  ? -10.944 87.713  121.119 1.00 24.07 ?  770  VAL A CA    1 
ATOM   5757  C C     . VAL A 1 772  ? -9.766  88.253  121.919 1.00 26.10 ?  770  VAL A C     1 
ATOM   5758  O O     . VAL A 1 772  ? -8.778  87.548  122.152 1.00 26.80 ?  770  VAL A O     1 
ATOM   5759  C CB    . VAL A 1 772  ? -10.842 88.080  119.623 1.00 22.05 ?  770  VAL A CB    1 
ATOM   5760  C CG1   . VAL A 1 772  ? -9.427  87.864  119.103 1.00 25.69 ?  770  VAL A CG1   1 
ATOM   5761  C CG2   . VAL A 1 772  ? -11.829 87.264  118.796 1.00 24.29 ?  770  VAL A CG2   1 
ATOM   5762  N N     . ALA A 1 773  ? -9.856  89.503  122.361 1.00 27.37 ?  771  ALA A N     1 
ATOM   5763  C CA    . ALA A 1 773  ? -8.755  90.139  123.075 1.00 26.04 ?  771  ALA A CA    1 
ATOM   5764  C C     . ALA A 1 773  ? -8.619  89.678  124.521 1.00 32.22 ?  771  ALA A C     1 
ATOM   5765  O O     . ALA A 1 773  ? -7.588  89.960  125.142 1.00 31.43 ?  771  ALA A O     1 
ATOM   5766  C CB    . ALA A 1 773  ? -8.925  91.657  123.042 1.00 30.79 ?  771  ALA A CB    1 
ATOM   5767  N N     . ALA A 1 774  ? -9.614  88.989  125.077 1.00 29.10 ?  772  ALA A N     1 
ATOM   5768  C CA    . ALA A 1 774  ? -9.584  88.687  126.506 1.00 28.53 ?  772  ALA A CA    1 
ATOM   5769  C C     . ALA A 1 774  ? -8.466  87.701  126.824 1.00 25.60 ?  772  ALA A C     1 
ATOM   5770  O O     . ALA A 1 774  ? -8.261  86.717  126.112 1.00 25.54 ?  772  ALA A O     1 
ATOM   5771  C CB    . ALA A 1 774  ? -10.930 88.132  126.966 1.00 28.22 ?  772  ALA A CB    1 
ATOM   5772  N N     . ALA A 1 775  ? -7.744  87.968  127.920 1.00 30.49 ?  773  ALA A N     1 
ATOM   5773  C CA    . ALA A 1 775  ? -6.533  87.209  128.212 1.00 30.14 ?  773  ALA A CA    1 
ATOM   5774  C C     . ALA A 1 775  ? -6.810  85.724  128.395 1.00 26.99 ?  773  ALA A C     1 
ATOM   5775  O O     . ALA A 1 775  ? -5.935  84.894  128.130 1.00 30.98 ?  773  ALA A O     1 
ATOM   5776  C CB    . ALA A 1 775  ? -5.849  87.774  129.459 1.00 35.39 ?  773  ALA A CB    1 
ATOM   5777  N N     . GLU A 1 776  ? -8.008  85.360  128.840 1.00 27.77 ?  774  GLU A N     1 
ATOM   5778  C CA    . GLU A 1 776  ? -8.305  83.961  129.102 1.00 25.75 ?  774  GLU A CA    1 
ATOM   5779  C C     . GLU A 1 776  ? -8.797  83.219  127.872 1.00 21.39 ?  774  GLU A C     1 
ATOM   5780  O O     . GLU A 1 776  ? -8.982  82.002  127.936 1.00 26.71 ?  774  GLU A O     1 
ATOM   5781  C CB    . GLU A 1 776  ? -9.342  83.834  130.220 1.00 27.19 ?  774  GLU A CB    1 
ATOM   5782  C CG    . GLU A 1 776  ? -8.928  84.510  131.512 1.00 37.36 ?  774  GLU A CG    1 
ATOM   5783  C CD    . GLU A 1 776  ? -9.557  85.883  131.671 1.00 38.38 ?  774  GLU A CD    1 
ATOM   5784  O OE1   . GLU A 1 776  ? -9.849  86.548  130.645 1.00 32.40 ?  774  GLU A OE1   1 
ATOM   5785  O OE2   . GLU A 1 776  ? -9.769  86.293  132.832 1.00 45.96 ?  774  GLU A OE2   1 
ATOM   5786  N N     . THR A 1 777  ? -8.992  83.914  126.755 1.00 22.52 ?  775  THR A N     1 
ATOM   5787  C CA    . THR A 1 777  ? -9.412  83.254  125.524 1.00 22.01 ?  775  THR A CA    1 
ATOM   5788  C C     . THR A 1 777  ? -8.283  82.382  124.992 1.00 21.78 ?  775  THR A C     1 
ATOM   5789  O O     . THR A 1 777  ? -7.169  82.863  124.762 1.00 25.40 ?  775  THR A O     1 
ATOM   5790  C CB    . THR A 1 777  ? -9.833  84.297  124.497 1.00 22.25 ?  775  THR A CB    1 
ATOM   5791  O OG1   . THR A 1 777  ? -11.021 84.936  124.969 1.00 23.81 ?  775  THR A OG1   1 
ATOM   5792  C CG2   . THR A 1 777  ? -10.105 83.645  123.132 1.00 20.75 ?  775  THR A CG2   1 
ATOM   5793  N N     . ALA A 1 778  ? -8.567  81.093  124.830 1.00 19.61 ?  776  ALA A N     1 
ATOM   5794  C CA    . ALA A 1 778  ? -7.560  80.105  124.502 1.00 19.84 ?  776  ALA A CA    1 
ATOM   5795  C C     . ALA A 1 778  ? -7.616  79.654  123.055 1.00 22.17 ?  776  ALA A C     1 
ATOM   5796  O O     . ALA A 1 778  ? -6.733  78.908  122.620 1.00 20.76 ?  776  ALA A O     1 
ATOM   5797  C CB    . ALA A 1 778  ? -7.696  78.886  125.432 1.00 20.67 ?  776  ALA A CB    1 
ATOM   5798  N N     . GLY A 1 779  ? -8.626  80.072  122.311 1.00 20.33 ?  777  GLY A N     1 
ATOM   5799  C CA    . GLY A 1 779  ? -8.735  79.704  120.912 1.00 19.49 ?  777  GLY A CA    1 
ATOM   5800  C C     . GLY A 1 779  ? -9.926  80.421  120.325 1.00 18.20 ?  777  GLY A C     1 
ATOM   5801  O O     . GLY A 1 779  ? -10.839 80.842  121.044 1.00 19.29 ?  777  GLY A O     1 
ATOM   5802  N N     . VAL A 1 780  ? -9.897  80.575  119.005 1.00 17.51 ?  778  VAL A N     1 
ATOM   5803  C CA    . VAL A 1 780  ? -10.943 81.295  118.294 1.00 18.27 ?  778  VAL A CA    1 
ATOM   5804  C C     . VAL A 1 780  ? -11.340 80.483  117.070 1.00 17.90 ?  778  VAL A C     1 
ATOM   5805  O O     . VAL A 1 780  ? -10.478 80.014  116.321 1.00 17.28 ?  778  VAL A O     1 
ATOM   5806  C CB    . VAL A 1 780  ? -10.490 82.712  117.881 1.00 18.31 ?  778  VAL A CB    1 
ATOM   5807  C CG1   . VAL A 1 780  ? -11.577 83.407  117.075 1.00 18.51 ?  778  VAL A CG1   1 
ATOM   5808  C CG2   . VAL A 1 780  ? -10.119 83.544  119.102 1.00 20.20 ?  778  VAL A CG2   1 
ATOM   5809  N N     . MET A 1 781  ? -12.645 80.303  116.885 1.00 17.01 ?  779  MET A N     1 
ATOM   5810  C CA    . MET A 1 781  ? -13.221 79.711  115.686 1.00 16.26 ?  779  MET A CA    1 
ATOM   5811  C C     . MET A 1 781  ? -14.041 80.786  115.000 1.00 16.40 ?  779  MET A C     1 
ATOM   5812  O O     . MET A 1 781  ? -15.014 81.291  115.578 1.00 17.31 ?  779  MET A O     1 
ATOM   5813  C CB    . MET A 1 781  ? -14.086 78.502  116.032 1.00 18.32 ?  779  MET A CB    1 
ATOM   5814  C CG    . MET A 1 781  ? -13.322 77.445  116.809 1.00 17.85 ?  779  MET A CG    1 
ATOM   5815  S SD    . MET A 1 781  ? -14.362 76.127  117.470 1.00 18.23 ?  779  MET A SD    1 
ATOM   5816  C CE    . MET A 1 781  ? -14.487 75.066  116.032 1.00 16.35 ?  779  MET A CE    1 
ATOM   5817  N N     . PHE A 1 782  ? -13.636 81.147  113.785 1.00 17.56 ?  780  PHE A N     1 
ATOM   5818  C CA    . PHE A 1 782  ? -14.254 82.233  113.042 1.00 17.70 ?  780  PHE A CA    1 
ATOM   5819  C C     . PHE A 1 782  ? -14.670 81.762  111.661 1.00 18.13 ?  780  PHE A C     1 
ATOM   5820  O O     . PHE A 1 782  ? -13.868 81.159  110.943 1.00 15.56 ?  780  PHE A O     1 
ATOM   5821  C CB    . PHE A 1 782  ? -13.296 83.418  112.897 1.00 18.22 ?  780  PHE A CB    1 
ATOM   5822  C CG    . PHE A 1 782  ? -13.828 84.509  112.012 1.00 18.42 ?  780  PHE A CG    1 
ATOM   5823  C CD1   . PHE A 1 782  ? -14.726 85.446  112.520 1.00 20.26 ?  780  PHE A CD1   1 
ATOM   5824  C CD2   . PHE A 1 782  ? -13.434 84.603  110.681 1.00 19.55 ?  780  PHE A CD2   1 
ATOM   5825  C CE1   . PHE A 1 782  ? -15.235 86.452  111.720 1.00 23.03 ?  780  PHE A CE1   1 
ATOM   5826  C CE2   . PHE A 1 782  ? -13.941 85.617  109.876 1.00 17.95 ?  780  PHE A CE2   1 
ATOM   5827  C CZ    . PHE A 1 782  ? -14.835 86.544  110.400 1.00 20.95 ?  780  PHE A CZ    1 
ATOM   5828  N N     . THR A 1 783  ? -15.895 82.084  111.267 1.00 16.76 ?  781  THR A N     1 
ATOM   5829  C CA    . THR A 1 783  ? -16.323 81.915  109.884 1.00 17.56 ?  781  THR A CA    1 
ATOM   5830  C C     . THR A 1 783  ? -16.929 83.233  109.429 1.00 19.70 ?  781  THR A C     1 
ATOM   5831  O O     . THR A 1 783  ? -17.866 83.734  110.057 1.00 18.98 ?  781  THR A O     1 
ATOM   5832  C CB    . THR A 1 783  ? -17.325 80.765  109.736 1.00 16.95 ?  781  THR A CB    1 
ATOM   5833  O OG1   . THR A 1 783  ? -16.741 79.554  110.236 1.00 18.50 ?  781  THR A OG1   1 
ATOM   5834  C CG2   . THR A 1 783  ? -17.688 80.564  108.270 1.00 20.30 ?  781  THR A CG2   1 
ATOM   5835  N N     . GLY A 1 784  ? -16.382 83.793  108.353 1.00 20.19 ?  782  GLY A N     1 
ATOM   5836  C CA    . GLY A 1 784  ? -16.762 85.129  107.912 1.00 19.99 ?  782  GLY A CA    1 
ATOM   5837  C C     . GLY A 1 784  ? -15.769 85.646  106.893 1.00 20.46 ?  782  GLY A C     1 
ATOM   5838  O O     . GLY A 1 784  ? -15.086 84.865  106.226 1.00 23.00 ?  782  GLY A O     1 
ATOM   5839  N N     . SER A 1 785  ? -15.679 86.972  106.795 1.00 23.07 ?  783  SER A N     1 
ATOM   5840  C CA    . SER A 1 785  ? -14.879 87.582  105.737 1.00 25.34 ?  783  SER A CA    1 
ATOM   5841  C C     . SER A 1 785  ? -13.381 87.468  106.014 1.00 24.01 ?  783  SER A C     1 
ATOM   5842  O O     . SER A 1 785  ? -12.943 87.371  107.165 1.00 24.35 ?  783  SER A O     1 
ATOM   5843  C CB    . SER A 1 785  ? -15.252 89.053  105.563 1.00 23.51 ?  783  SER A CB    1 
ATOM   5844  O OG    . SER A 1 785  ? -14.763 89.856  106.628 1.00 29.79 ?  783  SER A OG    1 
ATOM   5845  N N     . THR A 1 786  ? -12.590 87.492  104.933 1.00 26.10 ?  784  THR A N     1 
ATOM   5846  C CA    A THR A 1 786  ? -11.133 87.464  105.069 0.72 24.10 ?  784  THR A CA    1 
ATOM   5847  C CA    B THR A 1 786  ? -11.141 87.450  105.092 0.28 24.14 ?  784  THR A CA    1 
ATOM   5848  C C     . THR A 1 786  ? -10.620 88.691  105.805 1.00 26.27 ?  784  THR A C     1 
ATOM   5849  O O     . THR A 1 786  ? -9.657  88.601  106.578 1.00 24.25 ?  784  THR A O     1 
ATOM   5850  C CB    A THR A 1 786  ? -10.459 87.387  103.698 0.72 27.02 ?  784  THR A CB    1 
ATOM   5851  C CB    B THR A 1 786  ? -10.467 87.280  103.726 0.28 26.92 ?  784  THR A CB    1 
ATOM   5852  O OG1   A THR A 1 786  ? -10.748 88.584  102.958 0.72 32.33 ?  784  THR A OG1   1 
ATOM   5853  O OG1   B THR A 1 786  ? -9.043  87.289  103.882 0.28 26.64 ?  784  THR A OG1   1 
ATOM   5854  C CG2   A THR A 1 786  ? -10.933 86.177  102.928 0.72 21.19 ?  784  THR A CG2   1 
ATOM   5855  C CG2   B THR A 1 786  ? -10.884 88.392  102.768 0.28 31.34 ?  784  THR A CG2   1 
ATOM   5856  N N     . GLU A 1 787  ? -11.244 89.850  105.566 1.00 26.70 ?  785  GLU A N     1 
ATOM   5857  C CA    . GLU A 1 787  ? -10.793 91.084  106.194 1.00 29.07 ?  785  GLU A CA    1 
ATOM   5858  C C     . GLU A 1 787  ? -10.938 91.008  107.706 1.00 19.79 ?  785  GLU A C     1 
ATOM   5859  O O     . GLU A 1 787  ? -10.028 91.397  108.448 1.00 25.24 ?  785  GLU A O     1 
ATOM   5860  C CB    . GLU A 1 787  ? -11.575 92.276  105.626 1.00 33.54 ?  785  GLU A CB    1 
ATOM   5861  N N     . VAL A 1 788  ? -12.072 90.492  108.181 1.00 26.64 ?  786  VAL A N     1 
ATOM   5862  C CA    . VAL A 1 788  ? -12.288 90.398  109.619 1.00 23.42 ?  786  VAL A CA    1 
ATOM   5863  C C     . VAL A 1 788  ? -11.408 89.307  110.220 1.00 20.47 ?  786  VAL A C     1 
ATOM   5864  O O     . VAL A 1 788  ? -10.833 89.486  111.303 1.00 22.19 ?  786  VAL A O     1 
ATOM   5865  C CB    . VAL A 1 788  ? -13.778 90.167  109.921 1.00 24.99 ?  786  VAL A CB    1 
ATOM   5866  C CG1   . VAL A 1 788  ? -13.970 89.869  111.393 1.00 23.55 ?  786  VAL A CG1   1 
ATOM   5867  C CG2   . VAL A 1 788  ? -14.588 91.407  109.530 1.00 30.92 ?  786  VAL A CG2   1 
ATOM   5868  N N     . ALA A 1 789  ? -11.269 88.170  109.528 1.00 22.38 ?  787  ALA A N     1 
ATOM   5869  C CA    . ALA A 1 789  ? -10.340 87.146  110.000 1.00 20.45 ?  787  ALA A CA    1 
ATOM   5870  C C     . ALA A 1 789  ? -8.936  87.715  110.152 1.00 20.47 ?  787  ALA A C     1 
ATOM   5871  O O     . ALA A 1 789  ? -8.220  87.379  111.102 1.00 17.58 ?  787  ALA A O     1 
ATOM   5872  C CB    . ALA A 1 789  ? -10.330 85.948  109.050 1.00 18.65 ?  787  ALA A CB    1 
ATOM   5873  N N     . ARG A 1 790  ? -8.522  88.576  109.217 1.00 20.82 ?  788  ARG A N     1 
ATOM   5874  C CA    . ARG A 1 790  ? -7.193  89.177  109.286 1.00 20.65 ?  788  ARG A CA    1 
ATOM   5875  C C     . ARG A 1 790  ? -7.061  90.093  110.505 1.00 19.57 ?  788  ARG A C     1 
ATOM   5876  O O     . ARG A 1 790  ? -6.019  90.109  111.172 1.00 20.82 ?  788  ARG A O     1 
ATOM   5877  C CB    . ARG A 1 790  ? -6.920  89.929  107.975 1.00 26.10 ?  788  ARG A CB    1 
ATOM   5878  C CG    . ARG A 1 790  ? -5.476  90.346  107.733 1.00 26.62 ?  788  ARG A CG    1 
ATOM   5879  C CD    . ARG A 1 790  ? -5.254  90.896  106.296 1.00 29.26 ?  788  ARG A CD    1 
ATOM   5880  N NE    . ARG A 1 790  ? -5.140  89.866  105.262 1.00 28.88 ?  788  ARG A NE    1 
ATOM   5881  C CZ    . ARG A 1 790  ? -5.973  89.724  104.237 1.00 31.40 ?  788  ARG A CZ    1 
ATOM   5882  N NH1   . ARG A 1 790  ? -7.027  90.513  104.082 1.00 33.35 ?  788  ARG A NH1   1 
ATOM   5883  N NH2   . ARG A 1 790  ? -5.732  88.782  103.330 1.00 30.20 ?  788  ARG A NH2   1 
ATOM   5884  N N     . LEU A 1 791  ? -8.113  90.854  110.825 1.00 20.44 ?  789  LEU A N     1 
ATOM   5885  C CA    . LEU A 1 791  ? -8.090  91.676  112.034 1.00 22.68 ?  789  LEU A CA    1 
ATOM   5886  C C     . LEU A 1 791  ? -8.031  90.816  113.297 1.00 20.44 ?  789  LEU A C     1 
ATOM   5887  O O     . LEU A 1 791  ? -7.326  91.158  114.257 1.00 22.11 ?  789  LEU A O     1 
ATOM   5888  C CB    . LEU A 1 791  ? -9.311  92.591  112.062 1.00 24.04 ?  789  LEU A CB    1 
ATOM   5889  C CG    . LEU A 1 791  ? -9.323  93.775  111.094 1.00 26.27 ?  789  LEU A CG    1 
ATOM   5890  C CD1   . LEU A 1 791  ? -10.708 94.370  111.074 1.00 25.91 ?  789  LEU A CD1   1 
ATOM   5891  C CD2   . LEU A 1 791  ? -8.294  94.828  111.511 1.00 28.78 ?  789  LEU A CD2   1 
ATOM   5892  N N     . ILE A 1 792  ? -8.736  89.679  113.299 1.00 20.51 ?  790  ILE A N     1 
ATOM   5893  C CA    . ILE A 1 792  ? -8.655  88.761  114.437 1.00 23.26 ?  790  ILE A CA    1 
ATOM   5894  C C     . ILE A 1 792  ? -7.248  88.192  114.571 1.00 20.64 ?  790  ILE A C     1 
ATOM   5895  O O     . ILE A 1 792  ? -6.685  88.152  115.672 1.00 19.62 ?  790  ILE A O     1 
ATOM   5896  C CB    . ILE A 1 792  ? -9.714  87.653  114.301 1.00 20.14 ?  790  ILE A CB    1 
ATOM   5897  C CG1   . ILE A 1 792  ? -11.094 88.245  114.566 1.00 20.61 ?  790  ILE A CG1   1 
ATOM   5898  C CG2   . ILE A 1 792  ? -9.448  86.496  115.266 1.00 20.87 ?  790  ILE A CG2   1 
ATOM   5899  C CD1   . ILE A 1 792  ? -12.234 87.374  114.085 1.00 23.75 ?  790  ILE A CD1   1 
ATOM   5900  N N     . GLN A 1 793  ? -6.649  87.770  113.454 1.00 17.05 ?  791  GLN A N     1 
ATOM   5901  C CA    . GLN A 1 793  ? -5.286  87.248  113.483 1.00 19.06 ?  791  GLN A CA    1 
ATOM   5902  C C     . GLN A 1 793  ? -4.310  88.259  114.085 1.00 19.50 ?  791  GLN A C     1 
ATOM   5903  O O     . GLN A 1 793  ? -3.410  87.886  114.846 1.00 20.83 ?  791  GLN A O     1 
ATOM   5904  C CB    . GLN A 1 793  ? -4.869  86.853  112.065 1.00 20.34 ?  791  GLN A CB    1 
ATOM   5905  C CG    . GLN A 1 793  ? -3.415  86.424  111.909 1.00 22.86 ?  791  GLN A CG    1 
ATOM   5906  C CD    . GLN A 1 793  ? -3.012  86.309  110.440 1.00 29.56 ?  791  GLN A CD    1 
ATOM   5907  O OE1   . GLN A 1 793  ? -2.583  85.248  109.979 1.00 33.13 ?  791  GLN A OE1   1 
ATOM   5908  N NE2   . GLN A 1 793  ? -3.169  87.400  109.694 1.00 29.29 ?  791  GLN A NE2   1 
ATOM   5909  N N     . ALA A 1 794  ? -4.478  89.545  113.765 1.00 21.06 ?  792  ALA A N     1 
ATOM   5910  C CA    . ALA A 1 794  ? -3.601  90.561  114.336 1.00 23.66 ?  792  ALA A CA    1 
ATOM   5911  C C     . ALA A 1 794  ? -3.812  90.698  115.843 1.00 21.61 ?  792  ALA A C     1 
ATOM   5912  O O     . ALA A 1 794  ? -2.842  90.841  116.597 1.00 24.70 ?  792  ALA A O     1 
ATOM   5913  C CB    . ALA A 1 794  ? -3.829  91.899  113.631 1.00 22.53 ?  792  ALA A CB    1 
ATOM   5914  N N     . GLN A 1 795  ? -5.071  90.670  116.293 1.00 22.51 ?  793  GLN A N     1 
ATOM   5915  C CA    . GLN A 1 795  ? -5.364  90.642  117.724 1.00 23.30 ?  793  GLN A CA    1 
ATOM   5916  C C     . GLN A 1 795  ? -4.629  89.501  118.410 1.00 23.52 ?  793  GLN A C     1 
ATOM   5917  O O     . GLN A 1 795  ? -3.973  89.695  119.440 1.00 22.22 ?  793  GLN A O     1 
ATOM   5918  C CB    . GLN A 1 795  ? -6.869  90.488  117.962 1.00 27.56 ?  793  GLN A CB    1 
ATOM   5919  C CG    . GLN A 1 795  ? -7.746  91.687  117.652 1.00 25.19 ?  793  GLN A CG    1 
ATOM   5920  C CD    . GLN A 1 795  ? -9.175  91.496  118.167 1.00 26.50 ?  793  GLN A CD    1 
ATOM   5921  O OE1   . GLN A 1 795  ? -10.021 90.909  117.488 1.00 30.66 ?  793  GLN A OE1   1 
ATOM   5922  N NE2   . GLN A 1 795  ? -9.440  91.980  119.375 1.00 27.07 ?  793  GLN A NE2   1 
ATOM   5923  N N     . LEU A 1 796  ? -4.745  88.294  117.856 1.00 22.81 ?  794  LEU A N     1 
ATOM   5924  C CA    . LEU A 1 796  ? -4.190  87.123  118.524 1.00 22.94 ?  794  LEU A CA    1 
ATOM   5925  C C     . LEU A 1 796  ? -2.670  87.117  118.506 1.00 23.40 ?  794  LEU A C     1 
ATOM   5926  O O     . LEU A 1 796  ? -2.049  86.559  119.417 1.00 25.89 ?  794  LEU A O     1 
ATOM   5927  C CB    . LEU A 1 796  ? -4.718  85.847  117.881 1.00 19.60 ?  794  LEU A CB    1 
ATOM   5928  C CG    . LEU A 1 796  ? -6.208  85.573  118.056 1.00 18.51 ?  794  LEU A CG    1 
ATOM   5929  C CD1   . LEU A 1 796  ? -6.593  84.298  117.331 1.00 20.97 ?  794  LEU A CD1   1 
ATOM   5930  C CD2   . LEU A 1 796  ? -6.519  85.506  119.564 1.00 18.28 ?  794  LEU A CD2   1 
ATOM   5931  N N     . ALA A 1 797  ? -2.050  87.712  117.487 1.00 21.57 ?  795  ALA A N     1 
ATOM   5932  C CA    . ALA A 1 797  ? -0.593  87.728  117.456 1.00 24.43 ?  795  ALA A CA    1 
ATOM   5933  C C     . ALA A 1 797  ? -0.009  88.559  118.589 1.00 25.98 ?  795  ALA A C     1 
ATOM   5934  O O     . ALA A 1 797  ? 1.175   88.412  118.909 1.00 26.19 ?  795  ALA A O     1 
ATOM   5935  C CB    . ALA A 1 797  ? -0.101  88.236  116.100 1.00 24.40 ?  795  ALA A CB    1 
ATOM   5936  N N     . ASP A 1 798  ? -0.820  89.415  119.213 1.00 25.90 ?  796  ASP A N     1 
ATOM   5937  C CA    . ASP A 1 798  ? -0.382  90.111  120.416 1.00 25.53 ?  796  ASP A CA    1 
ATOM   5938  C C     . ASP A 1 798  ? -0.251  89.182  121.613 1.00 28.67 ?  796  ASP A C     1 
ATOM   5939  O O     . ASP A 1 798  ? 0.427   89.544  122.577 1.00 27.60 ?  796  ASP A O     1 
ATOM   5940  C CB    . ASP A 1 798  ? -1.352  91.237  120.779 1.00 25.66 ?  796  ASP A CB    1 
ATOM   5941  C CG    . ASP A 1 798  ? -1.176  92.468  119.911 1.00 36.40 ?  796  ASP A CG    1 
ATOM   5942  O OD1   . ASP A 1 798  ? -0.124  92.592  119.239 1.00 34.50 ?  796  ASP A OD1   1 
ATOM   5943  O OD2   . ASP A 1 798  ? -2.089  93.320  119.915 1.00 34.46 ?  796  ASP A OD2   1 
ATOM   5944  N N     . ARG A 1 799  ? -0.876  88.004  121.579 1.00 26.15 ?  797  ARG A N     1 
ATOM   5945  C CA    . ARG A 1 799  ? -1.039  87.196  122.778 1.00 26.37 ?  797  ARG A CA    1 
ATOM   5946  C C     . ARG A 1 799  ? -0.346  85.845  122.645 1.00 25.58 ?  797  ARG A C     1 
ATOM   5947  O O     . ARG A 1 799  ? -0.073  85.357  121.545 1.00 26.04 ?  797  ARG A O     1 
ATOM   5948  C CB    . ARG A 1 799  ? -2.532  86.978  123.106 1.00 32.85 ?  797  ARG A CB    1 
ATOM   5949  C CG    . ARG A 1 799  ? -3.319  88.265  123.317 1.00 30.52 ?  797  ARG A CG    1 
ATOM   5950  C CD    . ARG A 1 799  ? -4.541  88.076  124.216 1.00 31.46 ?  797  ARG A CD    1 
ATOM   5951  N NE    . ARG A 1 799  ? -5.636  87.377  123.556 1.00 34.09 ?  797  ARG A NE    1 
ATOM   5952  C CZ    . ARG A 1 799  ? -5.918  86.091  123.728 1.00 32.42 ?  797  ARG A CZ    1 
ATOM   5953  N NH1   . ARG A 1 799  ? -5.222  85.333  124.562 1.00 32.72 ?  797  ARG A NH1   1 
ATOM   5954  N NH2   . ARG A 1 799  ? -6.935  85.555  123.060 1.00 26.81 ?  797  ARG A NH2   1 
ATOM   5955  N N     . LEU A 1 800  ? -0.055  85.257  123.801 1.00 25.12 ?  798  LEU A N     1 
ATOM   5956  C CA    . LEU A 1 800  ? 0.406   83.884  123.910 1.00 25.95 ?  798  LEU A CA    1 
ATOM   5957  C C     . LEU A 1 800  ? -0.427  83.184  124.976 1.00 24.23 ?  798  LEU A C     1 
ATOM   5958  O O     . LEU A 1 800  ? -0.999  83.819  125.864 1.00 28.73 ?  798  LEU A O     1 
ATOM   5959  C CB    . LEU A 1 800  ? 1.897   83.798  124.282 1.00 29.12 ?  798  LEU A CB    1 
ATOM   5960  C CG    . LEU A 1 800  ? 2.920   84.337  123.279 1.00 29.04 ?  798  LEU A CG    1 
ATOM   5961  C CD1   . LEU A 1 800  ? 4.321   84.364  123.913 1.00 26.30 ?  798  LEU A CD1   1 
ATOM   5962  C CD2   . LEU A 1 800  ? 2.901   83.530  121.983 1.00 26.94 ?  798  LEU A CD2   1 
ATOM   5963  N N     . SER A 1 801  ? -0.491  81.859  124.872 1.00 27.22 ?  799  SER A N     1 
ATOM   5964  C CA    . SER A 1 801  ? -1.101  81.051  125.914 1.00 32.15 ?  799  SER A CA    1 
ATOM   5965  C C     . SER A 1 801  ? -0.256  81.145  127.185 1.00 33.40 ?  799  SER A C     1 
ATOM   5966  O O     . SER A 1 801  ? 0.875   81.639  127.154 1.00 32.75 ?  799  SER A O     1 
ATOM   5967  C CB    . SER A 1 801  ? -1.212  79.602  125.448 1.00 31.82 ?  799  SER A CB    1 
ATOM   5968  O OG    . SER A 1 801  ? 0.073   79.005  125.409 1.00 31.73 ?  799  SER A OG    1 
ATOM   5969  N N     . PRO A 1 802  ? -0.777  80.685  128.330 1.00 31.77 ?  800  PRO A N     1 
ATOM   5970  C CA    . PRO A 1 802  ? 0.075   80.632  129.531 1.00 33.35 ?  800  PRO A CA    1 
ATOM   5971  C C     . PRO A 1 802  ? 1.350   79.835  129.323 1.00 35.20 ?  800  PRO A C     1 
ATOM   5972  O O     . PRO A 1 802  ? 2.364   80.117  129.976 1.00 39.18 ?  800  PRO A O     1 
ATOM   5973  C CB    . PRO A 1 802  ? -0.840  79.983  130.582 1.00 35.49 ?  800  PRO A CB    1 
ATOM   5974  C CG    . PRO A 1 802  ? -1.959  79.357  129.812 1.00 41.46 ?  800  PRO A CG    1 
ATOM   5975  C CD    . PRO A 1 802  ? -2.154  80.252  128.627 1.00 32.72 ?  800  PRO A CD    1 
ATOM   5976  N N     . ALA A 1 803  ? 1.332   78.851  128.427 1.00 34.91 ?  801  ALA A N     1 
ATOM   5977  C CA    . ALA A 1 803  ? 2.525   78.086  128.095 1.00 37.91 ?  801  ALA A CA    1 
ATOM   5978  C C     . ALA A 1 803  ? 3.447   78.810  127.120 1.00 38.09 ?  801  ALA A C     1 
ATOM   5979  O O     . ALA A 1 803  ? 4.519   78.282  126.806 1.00 35.35 ?  801  ALA A O     1 
ATOM   5980  C CB    . ALA A 1 803  ? 2.132   76.724  127.515 1.00 34.35 ?  801  ALA A CB    1 
ATOM   5981  N N     . GLY A 1 804  ? 3.064   79.990  126.638 1.00 34.82 ?  802  GLY A N     1 
ATOM   5982  C CA    . GLY A 1 804  ? 3.911   80.746  125.732 1.00 30.51 ?  802  GLY A CA    1 
ATOM   5983  C C     . GLY A 1 804  ? 3.853   80.313  124.282 1.00 32.08 ?  802  GLY A C     1 
ATOM   5984  O O     . GLY A 1 804  ? 4.867   80.389  123.573 1.00 28.52 ?  802  GLY A O     1 
ATOM   5985  N N     . ARG A 1 805  ? 2.696   79.864  123.815 1.00 30.76 ?  803  ARG A N     1 
ATOM   5986  C CA    . ARG A 1 805  ? 2.501   79.386  122.457 1.00 27.35 ?  803  ARG A CA    1 
ATOM   5987  C C     . ARG A 1 805  ? 1.348   80.135  121.807 1.00 21.16 ?  803  ARG A C     1 
ATOM   5988  O O     . ARG A 1 805  ? 0.515   80.728  122.501 1.00 24.08 ?  803  ARG A O     1 
ATOM   5989  C CB    . ARG A 1 805  ? 2.229   77.875  122.450 1.00 30.48 ?  803  ARG A CB    1 
ATOM   5990  C CG    . ARG A 1 805  ? 3.343   77.058  123.108 1.00 30.14 ?  803  ARG A CG    1 
ATOM   5991  C CD    . ARG A 1 805  ? 4.656   77.199  122.326 1.00 29.17 ?  803  ARG A CD    1 
ATOM   5992  N NE    . ARG A 1 805  ? 5.743   76.414  122.911 1.00 29.73 ?  803  ARG A NE    1 
ATOM   5993  C CZ    . ARG A 1 805  ? 6.691   76.900  123.701 1.00 30.68 ?  803  ARG A CZ    1 
ATOM   5994  N NH1   . ARG A 1 805  ? 6.728   78.180  124.040 1.00 31.39 ?  803  ARG A NH1   1 
ATOM   5995  N NH2   . ARG A 1 805  ? 7.626   76.078  124.170 1.00 35.62 ?  803  ARG A NH2   1 
ATOM   5996  N N     . PRO A 1 806  ? 1.291   80.164  120.475 1.00 22.43 ?  804  PRO A N     1 
ATOM   5997  C CA    . PRO A 1 806  ? 0.217   80.911  119.806 1.00 22.79 ?  804  PRO A CA    1 
ATOM   5998  C C     . PRO A 1 806  ? -1.166  80.374  120.148 1.00 22.64 ?  804  PRO A C     1 
ATOM   5999  O O     . PRO A 1 806  ? -1.362  79.174  120.351 1.00 20.24 ?  804  PRO A O     1 
ATOM   6000  C CB    . PRO A 1 806  ? 0.526   80.720  118.318 1.00 22.44 ?  804  PRO A CB    1 
ATOM   6001  C CG    . PRO A 1 806  ? 2.003   80.451  118.275 1.00 26.08 ?  804  PRO A CG    1 
ATOM   6002  C CD    . PRO A 1 806  ? 2.303   79.676  119.524 1.00 24.21 ?  804  PRO A CD    1 
ATOM   6003  N N     . ILE A 1 807  ? -2.133  81.289  120.193 1.00 21.37 ?  805  ILE A N     1 
ATOM   6004  C CA    . ILE A 1 807  ? -3.552  80.971  120.366 1.00 19.99 ?  805  ILE A CA    1 
ATOM   6005  C C     . ILE A 1 807  ? -4.107  80.428  119.054 1.00 19.78 ?  805  ILE A C     1 
ATOM   6006  O O     . ILE A 1 807  ? -4.047  81.132  118.037 1.00 20.99 ?  805  ILE A O     1 
ATOM   6007  C CB    . ILE A 1 807  ? -4.346  82.210  120.795 1.00 19.73 ?  805  ILE A CB    1 
ATOM   6008  C CG1   . ILE A 1 807  ? -3.753  82.823  122.065 1.00 24.05 ?  805  ILE A CG1   1 
ATOM   6009  C CG2   . ILE A 1 807  ? -5.825  81.862  120.961 1.00 23.43 ?  805  ILE A CG2   1 
ATOM   6010  C CD1   . ILE A 1 807  ? -3.860  81.946  123.275 1.00 24.18 ?  805  ILE A CD1   1 
ATOM   6011  N N     . PRO A 1 808  ? -4.647  79.204  119.014 1.00 18.62 ?  806  PRO A N     1 
ATOM   6012  C CA    . PRO A 1 808  ? -5.113  78.649  117.735 1.00 18.87 ?  806  PRO A CA    1 
ATOM   6013  C C     . PRO A 1 808  ? -6.296  79.416  117.170 1.00 19.31 ?  806  PRO A C     1 
ATOM   6014  O O     . PRO A 1 808  ? -7.218  79.817  117.890 1.00 19.22 ?  806  PRO A O     1 
ATOM   6015  C CB    . PRO A 1 808  ? -5.503  77.209  118.090 1.00 22.36 ?  806  PRO A CB    1 
ATOM   6016  C CG    . PRO A 1 808  ? -4.737  76.901  119.334 1.00 22.20 ?  806  PRO A CG    1 
ATOM   6017  C CD    . PRO A 1 808  ? -4.671  78.198  120.089 1.00 21.78 ?  806  PRO A CD    1 
ATOM   6018  N N     . LEU A 1 809  ? -6.260  79.605  115.854 1.00 20.74 ?  807  LEU A N     1 
ATOM   6019  C CA    . LEU A 1 809  ? -7.326  80.255  115.108 1.00 19.18 ?  807  LEU A CA    1 
ATOM   6020  C C     . LEU A 1 809  ? -7.745  79.333  113.974 1.00 18.40 ?  807  LEU A C     1 
ATOM   6021  O O     . LEU A 1 809  ? -6.915  78.964  113.136 1.00 18.29 ?  807  LEU A O     1 
ATOM   6022  C CB    . LEU A 1 809  ? -6.870  81.601  114.537 1.00 17.29 ?  807  LEU A CB    1 
ATOM   6023  C CG    . LEU A 1 809  ? -7.844  82.277  113.570 1.00 18.98 ?  807  LEU A CG    1 
ATOM   6024  C CD1   . LEU A 1 809  ? -9.162  82.615  114.252 1.00 20.05 ?  807  LEU A CD1   1 
ATOM   6025  C CD2   . LEU A 1 809  ? -7.236  83.517  112.938 1.00 24.57 ?  807  LEU A CD2   1 
ATOM   6026  N N     . ILE A 1 810  ? -9.017  78.948  113.956 1.00 15.68 ?  808  ILE A N     1 
ATOM   6027  C CA    . ILE A 1 810  ? -9.616  78.281  112.808 1.00 14.93 ?  808  ILE A CA    1 
ATOM   6028  C C     . ILE A 1 810  ? -10.469 79.326  112.116 1.00 16.39 ?  808  ILE A C     1 
ATOM   6029  O O     . ILE A 1 810  ? -11.475 79.775  112.673 1.00 18.54 ?  808  ILE A O     1 
ATOM   6030  C CB    . ILE A 1 810  ? -10.460 77.067  113.208 1.00 15.45 ?  808  ILE A CB    1 
ATOM   6031  C CG1   . ILE A 1 810  ? -9.633  76.068  114.009 1.00 19.67 ?  808  ILE A CG1   1 
ATOM   6032  C CG2   . ILE A 1 810  ? -11.039 76.404  111.979 1.00 16.76 ?  808  ILE A CG2   1 
ATOM   6033  C CD1   . ILE A 1 810  ? -10.415 74.810  114.343 1.00 22.90 ?  808  ILE A CD1   1 
ATOM   6034  N N     . ALA A 1 811  ? -10.073 79.706  110.899 1.00 16.06 ?  809  ALA A N     1 
ATOM   6035  C CA    . ALA A 1 811  ? -10.768 80.748  110.149 1.00 16.43 ?  809  ALA A CA    1 
ATOM   6036  C C     . ALA A 1 811  ? -11.141 80.227  108.771 1.00 18.15 ?  809  ALA A C     1 
ATOM   6037  O O     . ALA A 1 811  ? -10.260 79.890  107.973 1.00 19.04 ?  809  ALA A O     1 
ATOM   6038  C CB    . ALA A 1 811  ? -9.904  82.006  110.020 1.00 21.94 ?  809  ALA A CB    1 
ATOM   6039  N N     . GLU A 1 812  ? -12.439 80.156  108.499 1.00 16.49 ?  810  GLU A N     1 
ATOM   6040  C CA    . GLU A 1 812  ? -12.974 79.771  107.200 1.00 16.58 ?  810  GLU A CA    1 
ATOM   6041  C C     . GLU A 1 812  ? -13.508 81.031  106.536 1.00 18.70 ?  810  GLU A C     1 
ATOM   6042  O O     . GLU A 1 812  ? -14.359 81.718  107.109 1.00 18.38 ?  810  GLU A O     1 
ATOM   6043  C CB    . GLU A 1 812  ? -14.073 78.718  107.350 1.00 20.21 ?  810  GLU A CB    1 
ATOM   6044  N N     A THR A 1 813  ? -13.025 81.345  105.321 0.56 17.26 ?  811  THR A N     1 
ATOM   6045  N N     B THR A 1 813  ? -12.987 81.336  105.360 0.44 17.27 ?  811  THR A N     1 
ATOM   6046  C CA    A THR A 1 813  ? -13.159 82.716  104.804 0.56 19.16 ?  811  THR A CA    1 
ATOM   6047  C CA    B THR A 1 813  ? -13.380 82.547  104.669 0.44 19.16 ?  811  THR A CA    1 
ATOM   6048  C C     A THR A 1 813  ? -13.497 82.792  103.305 0.56 19.73 ?  811  THR A C     1 
ATOM   6049  C C     B THR A 1 813  ? -13.949 82.193  103.304 0.44 18.78 ?  811  THR A C     1 
ATOM   6050  O O     A THR A 1 813  ? -13.062 83.718  102.612 0.56 20.23 ?  811  THR A O     1 
ATOM   6051  O O     B THR A 1 813  ? -14.348 81.047  103.075 0.44 18.43 ?  811  THR A O     1 
ATOM   6052  C CB    A THR A 1 813  ? -11.889 83.525  105.079 0.56 19.64 ?  811  THR A CB    1 
ATOM   6053  C CB    B THR A 1 813  ? -12.184 83.489  104.575 0.44 18.81 ?  811  THR A CB    1 
ATOM   6054  O OG1   A THR A 1 813  ? -10.738 82.822  104.591 0.56 18.57 ?  811  THR A OG1   1 
ATOM   6055  O OG1   B THR A 1 813  ? -11.025 82.741  104.192 0.44 19.78 ?  811  THR A OG1   1 
ATOM   6056  C CG2   A THR A 1 813  ? -11.726 83.778  106.567 0.56 18.04 ?  811  THR A CG2   1 
ATOM   6057  C CG2   B THR A 1 813  ? -11.922 84.116  105.938 0.44 20.14 ?  811  THR A CG2   1 
ATOM   6058  N N     A GLY A 1 814  ? -14.303 81.869  102.778 0.56 18.97 ?  812  GLY A N     1 
ATOM   6059  N N     B GLY A 1 814  ? -13.987 83.159  102.395 0.44 20.13 ?  812  GLY A N     1 
ATOM   6060  C CA    A GLY A 1 814  ? -14.909 82.096  101.461 0.56 18.24 ?  812  GLY A CA    1 
ATOM   6061  C CA    B GLY A 1 814  ? -14.698 82.992  101.151 0.44 18.65 ?  812  GLY A CA    1 
ATOM   6062  C C     A GLY A 1 814  ? -14.044 81.712  100.267 0.56 17.48 ?  812  GLY A C     1 
ATOM   6063  C C     B GLY A 1 814  ? -13.892 82.309  100.068 0.44 18.83 ?  812  GLY A C     1 
ATOM   6064  O O     A GLY A 1 814  ? -13.068 80.970  100.389 0.56 15.56 ?  812  GLY A O     1 
ATOM   6065  O O     B GLY A 1 814  ? -12.734 81.921  100.232 0.44 17.98 ?  812  GLY A O     1 
ATOM   6066  N N     A GLY A 1 815  ? -14.416 82.223  99.091  0.56 17.36 ?  813  GLY A N     1 
ATOM   6067  N N     B GLY A 1 815  ? -14.544 82.162  98.920  0.44 17.18 ?  813  GLY A N     1 
ATOM   6068  C CA    A GLY A 1 815  ? -13.662 81.903  97.887  0.56 17.49 ?  813  GLY A CA    1 
ATOM   6069  C CA    B GLY A 1 815  ? -13.927 81.533  97.774  0.44 16.83 ?  813  GLY A CA    1 
ATOM   6070  C C     A GLY A 1 815  ? -14.175 82.643  96.665  0.56 17.62 ?  813  GLY A C     1 
ATOM   6071  C C     B GLY A 1 815  ? -14.437 82.137  96.488  0.44 16.27 ?  813  GLY A C     1 
ATOM   6072  O O     A GLY A 1 815  ? -15.076 83.477  96.741  0.56 19.21 ?  813  GLY A O     1 
ATOM   6073  O O     B GLY A 1 815  ? -15.627 82.428  96.364  0.44 16.13 ?  813  GLY A O     1 
ATOM   6074  N N     . GLN A 1 816  ? -13.543 82.340  95.528  1.00 18.32 ?  814  GLN A N     1 
ATOM   6075  C CA    . GLN A 1 816  ? -13.935 82.851  94.213  1.00 15.47 ?  814  GLN A CA    1 
ATOM   6076  C C     . GLN A 1 816  ? -14.118 81.640  93.303  1.00 12.99 ?  814  GLN A C     1 
ATOM   6077  O O     . GLN A 1 816  ? -13.286 81.339  92.449  1.00 17.23 ?  814  GLN A O     1 
ATOM   6078  C CB    . GLN A 1 816  ? -12.880 83.810  93.670  1.00 17.83 ?  814  GLN A CB    1 
ATOM   6079  C CG    . GLN A 1 816  ? -13.342 84.628  92.500  1.00 20.38 ?  814  GLN A CG    1 
ATOM   6080  C CD    . GLN A 1 816  ? -14.341 85.700  92.903  1.00 26.49 ?  814  GLN A CD    1 
ATOM   6081  O OE1   . GLN A 1 816  ? -15.521 85.415  93.088  1.00 28.43 ?  814  GLN A OE1   1 
ATOM   6082  N NE2   . GLN A 1 816  ? -13.872 86.940  93.039  1.00 27.63 ?  814  GLN A NE2   1 
ATOM   6083  N N     . ASN A 1 817  ? -15.191 80.901  93.559  1.00 12.14 ?  815  ASN A N     1 
ATOM   6084  C CA    . ASN A 1 817  ? -15.276 79.516  93.116  1.00 11.13 ?  815  ASN A CA    1 
ATOM   6085  C C     . ASN A 1 817  ? -15.651 79.437  91.648  1.00 11.73 ?  815  ASN A C     1 
ATOM   6086  O O     . ASN A 1 817  ? -16.583 80.116  91.186  1.00 13.32 ?  815  ASN A O     1 
ATOM   6087  C CB    . ASN A 1 817  ? -16.298 78.761  93.961  1.00 13.12 ?  815  ASN A CB    1 
ATOM   6088  C CG    . ASN A 1 817  ? -16.094 79.001  95.428  1.00 12.48 ?  815  ASN A CG    1 
ATOM   6089  O OD1   . ASN A 1 817  ? -15.027 78.725  95.978  1.00 12.17 ?  815  ASN A OD1   1 
ATOM   6090  N ND2   . ASN A 1 817  ? -17.111 79.533  96.081  1.00 11.44 ?  815  ASN A ND2   1 
ATOM   6091  N N     . ALA A 1 818  ? -14.932 78.573  90.926  1.00 11.05 ?  816  ALA A N     1 
ATOM   6092  C CA    . ALA A 1 818  ? -15.085 78.372  89.495  1.00 11.40 ?  816  ALA A CA    1 
ATOM   6093  C C     . ALA A 1 818  ? -15.677 77.009  89.178  1.00 11.77 ?  816  ALA A C     1 
ATOM   6094  O O     . ALA A 1 818  ? -15.548 76.046  89.940  1.00 12.75 ?  816  ALA A O     1 
ATOM   6095  C CB    . ALA A 1 818  ? -13.732 78.500  88.790  1.00 12.96 ?  816  ALA A CB    1 
ATOM   6096  N N     . MET A 1 819  ? -16.323 76.941  88.014  1.00 10.86 ?  817  MET A N     1 
ATOM   6097  C CA    . MET A 1 819  ? -16.722 75.681  87.416  1.00 11.92 ?  817  MET A CA    1 
ATOM   6098  C C     . MET A 1 819  ? -16.248 75.696  85.976  1.00 11.20 ?  817  MET A C     1 
ATOM   6099  O O     . MET A 1 819  ? -16.504 76.664  85.255  1.00 12.69 ?  817  MET A O     1 
ATOM   6100  C CB    . MET A 1 819  ? -18.237 75.477  87.466  1.00 12.69 ?  817  MET A CB    1 
ATOM   6101  C CG    . MET A 1 819  ? -18.683 74.208  86.746  1.00 12.74 ?  817  MET A CG    1 
ATOM   6102  S SD    . MET A 1 819  ? -20.483 74.024  86.639  1.00 14.60 ?  817  MET A SD    1 
ATOM   6103  C CE    . MET A 1 819  ? -20.879 73.672  88.350  1.00 16.08 ?  817  MET A CE    1 
ATOM   6104  N N     . ILE A 1 820  ? -15.550 74.640  85.563  1.00 10.02 ?  818  ILE A N     1 
ATOM   6105  C CA    . ILE A 1 820  ? -15.079 74.504  84.188  1.00 11.70 ?  818  ILE A CA    1 
ATOM   6106  C C     . ILE A 1 820  ? -15.943 73.476  83.473  1.00 9.81  ?  818  ILE A C     1 
ATOM   6107  O O     . ILE A 1 820  ? -16.207 72.390  84.007  1.00 12.13 ?  818  ILE A O     1 
ATOM   6108  C CB    . ILE A 1 820  ? -13.598 74.103  84.139  1.00 11.09 ?  818  ILE A CB    1 
ATOM   6109  C CG1   . ILE A 1 820  ? -12.746 75.197  84.784  1.00 12.79 ?  818  ILE A CG1   1 
ATOM   6110  C CG2   . ILE A 1 820  ? -13.171 73.855  82.685  1.00 13.10 ?  818  ILE A CG2   1 
ATOM   6111  C CD1   . ILE A 1 820  ? -11.245 74.916  84.784  1.00 14.65 ?  818  ILE A CD1   1 
ATOM   6112  N N     . VAL A 1 821  ? -16.385 73.818  82.263  1.00 11.01 ?  819  VAL A N     1 
ATOM   6113  C CA    . VAL A 1 821  ? -17.307 72.991  81.493  1.00 11.70 ?  819  VAL A CA    1 
ATOM   6114  C C     . VAL A 1 821  ? -16.703 72.803  80.112  1.00 12.20 ?  819  VAL A C     1 
ATOM   6115  O O     . VAL A 1 821  ? -16.404 73.794  79.438  1.00 14.00 ?  819  VAL A O     1 
ATOM   6116  C CB    . VAL A 1 821  ? -18.701 73.650  81.357  1.00 11.91 ?  819  VAL A CB    1 
ATOM   6117  C CG1   . VAL A 1 821  ? -19.608 72.810  80.468  1.00 15.16 ?  819  VAL A CG1   1 
ATOM   6118  C CG2   . VAL A 1 821  ? -19.331 73.898  82.706  1.00 12.76 ?  819  VAL A CG2   1 
ATOM   6119  N N     . ASP A 1 822  ? -16.548 71.549  79.674  1.00 11.56 ?  820  ASP A N     1 
ATOM   6120  C CA    . ASP A 1 822  ? -16.012 71.339  78.328  1.00 11.91 ?  820  ASP A CA    1 
ATOM   6121  C C     . ASP A 1 822  ? -17.123 70.894  77.382  1.00 13.27 ?  820  ASP A C     1 
ATOM   6122  O O     . ASP A 1 822  ? -18.299 70.812  77.745  1.00 14.16 ?  820  ASP A O     1 
ATOM   6123  C CB    . ASP A 1 822  ? -14.806 70.383  78.329  1.00 14.74 ?  820  ASP A CB    1 
ATOM   6124  C CG    . ASP A 1 822  ? -15.167 68.913  78.554  1.00 14.10 ?  820  ASP A CG    1 
ATOM   6125  O OD1   . ASP A 1 822  ? -16.345 68.498  78.540  1.00 14.35 ?  820  ASP A OD1   1 
ATOM   6126  O OD2   . ASP A 1 822  ? -14.191 68.157  78.776  1.00 15.90 ?  820  ASP A OD2   1 
ATOM   6127  N N     . SER A 1 823  ? -16.743 70.641  76.128  1.00 14.38 ?  821  SER A N     1 
ATOM   6128  C CA    . SER A 1 823  ? -17.741 70.349  75.106  1.00 15.52 ?  821  SER A CA    1 
ATOM   6129  C C     . SER A 1 823  ? -18.339 68.948  75.198  1.00 15.71 ?  821  SER A C     1 
ATOM   6130  O O     . SER A 1 823  ? -19.236 68.633  74.408  1.00 19.72 ?  821  SER A O     1 
ATOM   6131  C CB    . SER A 1 823  ? -17.136 70.545  73.711  1.00 16.77 ?  821  SER A CB    1 
ATOM   6132  O OG    . SER A 1 823  ? -16.031 69.678  73.514  1.00 18.88 ?  821  SER A OG    1 
ATOM   6133  N N     . SER A 1 824  ? -17.886 68.101  76.133  1.00 15.31 ?  822  SER A N     1 
ATOM   6134  C CA    . SER A 1 824  ? -18.456 66.774  76.329  1.00 14.98 ?  822  SER A CA    1 
ATOM   6135  C C     . SER A 1 824  ? -19.582 66.760  77.357  1.00 15.93 ?  822  SER A C     1 
ATOM   6136  O O     . SER A 1 824  ? -20.293 65.755  77.473  1.00 16.83 ?  822  SER A O     1 
ATOM   6137  C CB    . SER A 1 824  ? -17.361 65.780  76.752  1.00 14.42 ?  822  SER A CB    1 
ATOM   6138  O OG    . SER A 1 824  ? -16.979 65.975  78.118  1.00 14.65 ?  822  SER A OG    1 
ATOM   6139  N N     . ALA A 1 825  ? -19.741 67.843  78.115  1.00 14.92 ?  823  ALA A N     1 
ATOM   6140  C CA    . ALA A 1 825  ? -20.772 67.909  79.136  1.00 15.75 ?  823  ALA A CA    1 
ATOM   6141  C C     . ALA A 1 825  ? -22.151 68.045  78.502  1.00 15.43 ?  823  ALA A C     1 
ATOM   6142  O O     . ALA A 1 825  ? -22.299 68.554  77.392  1.00 18.55 ?  823  ALA A O     1 
ATOM   6143  C CB    . ALA A 1 825  ? -20.498 69.099  80.053  1.00 16.54 ?  823  ALA A CB    1 
ATOM   6144  N N     . LEU A 1 826  ? -23.167 67.578  79.217  1.00 16.98 ?  824  LEU A N     1 
ATOM   6145  C CA    . LEU A 1 826  ? -24.549 67.678  78.762  1.00 19.73 ?  824  LEU A CA    1 
ATOM   6146  C C     . LEU A 1 826  ? -25.113 69.019  79.225  1.00 19.00 ?  824  LEU A C     1 
ATOM   6147  O O     . LEU A 1 826  ? -25.180 69.283  80.432  1.00 19.25 ?  824  LEU A O     1 
ATOM   6148  C CB    . LEU A 1 826  ? -25.385 66.517  79.302  1.00 22.15 ?  824  LEU A CB    1 
ATOM   6149  C CG    . LEU A 1 826  ? -26.791 66.396  78.700  1.00 27.56 ?  824  LEU A CG    1 
ATOM   6150  C CD1   . LEU A 1 826  ? -26.702 66.089  77.208  1.00 28.74 ?  824  LEU A CD1   1 
ATOM   6151  C CD2   . LEU A 1 826  ? -27.640 65.351  79.418  1.00 30.63 ?  824  LEU A CD2   1 
ATOM   6152  N N     . ALA A 1 827  ? -25.517 69.861  78.268  1.00 19.16 ?  825  ALA A N     1 
ATOM   6153  C CA    . ALA A 1 827  ? -25.859 71.244  78.585  1.00 17.17 ?  825  ALA A CA    1 
ATOM   6154  C C     . ALA A 1 827  ? -26.949 71.338  79.651  1.00 17.23 ?  825  ALA A C     1 
ATOM   6155  O O     . ALA A 1 827  ? -26.854 72.166  80.562  1.00 14.99 ?  825  ALA A O     1 
ATOM   6156  C CB    . ALA A 1 827  ? -26.285 71.980  77.311  1.00 19.41 ?  825  ALA A CB    1 
ATOM   6157  N N     . GLU A 1 828  ? -27.996 70.513  79.551  1.00 17.09 ?  826  GLU A N     1 
ATOM   6158  C CA    . GLU A 1 828  ? -29.094 70.584  80.513  1.00 18.01 ?  826  GLU A CA    1 
ATOM   6159  C C     . GLU A 1 828  ? -28.625 70.277  81.937  1.00 16.93 ?  826  GLU A C     1 
ATOM   6160  O O     . GLU A 1 828  ? -29.102 70.894  82.904  1.00 17.79 ?  826  GLU A O     1 
ATOM   6161  C CB    . GLU A 1 828  ? -30.211 69.626  80.099  1.00 22.15 ?  826  GLU A CB    1 
ATOM   6162  C CG    . GLU A 1 828  ? -31.054 70.112  78.929  1.00 28.07 ?  826  GLU A CG    1 
ATOM   6163  C CD    . GLU A 1 828  ? -30.481 69.766  77.554  1.00 30.75 ?  826  GLU A CD    1 
ATOM   6164  O OE1   . GLU A 1 828  ? -29.332 69.274  77.463  1.00 28.79 ?  826  GLU A OE1   1 
ATOM   6165  O OE2   . GLU A 1 828  ? -31.201 69.990  76.554  1.00 36.45 ?  826  GLU A OE2   1 
ATOM   6166  N N     . GLN A 1 829  ? -27.725 69.301  82.090  1.00 17.32 ?  827  GLN A N     1 
ATOM   6167  C CA    . GLN A 1 829  ? -27.149 69.007  83.403  1.00 15.29 ?  827  GLN A CA    1 
ATOM   6168  C C     . GLN A 1 829  ? -26.353 70.190  83.915  1.00 14.06 ?  827  GLN A C     1 
ATOM   6169  O O     . GLN A 1 829  ? -26.455 70.575  85.092  1.00 14.88 ?  827  GLN A O     1 
ATOM   6170  C CB    . GLN A 1 829  ? -26.228 67.787  83.319  1.00 19.42 ?  827  GLN A CB    1 
ATOM   6171  C CG    . GLN A 1 829  ? -26.886 66.450  83.270  1.00 27.02 ?  827  GLN A CG    1 
ATOM   6172  C CD    . GLN A 1 829  ? -25.866 65.325  83.426  1.00 28.31 ?  827  GLN A CD    1 
ATOM   6173  O OE1   . GLN A 1 829  ? -24.674 65.496  83.132  1.00 23.76 ?  827  GLN A OE1   1 
ATOM   6174  N NE2   . GLN A 1 829  ? -26.328 64.176  83.903  1.00 29.64 ?  827  GLN A NE2   1 
ATOM   6175  N N     . VAL A 1 830  ? -25.478 70.719  83.061  1.00 15.18 ?  828  VAL A N     1 
ATOM   6176  C CA    . VAL A 1 830  ? -24.662 71.872  83.424  1.00 11.93 ?  828  VAL A CA    1 
ATOM   6177  C C     . VAL A 1 830  ? -25.548 73.001  83.913  1.00 13.32 ?  828  VAL A C     1 
ATOM   6178  O O     . VAL A 1 830  ? -25.315 73.585  84.974  1.00 13.45 ?  828  VAL A O     1 
ATOM   6179  C CB    . VAL A 1 830  ? -23.812 72.331  82.225  1.00 13.57 ?  828  VAL A CB    1 
ATOM   6180  C CG1   . VAL A 1 830  ? -23.155 73.671  82.504  1.00 15.19 ?  828  VAL A CG1   1 
ATOM   6181  C CG2   . VAL A 1 830  ? -22.766 71.259  81.863  1.00 15.15 ?  828  VAL A CG2   1 
ATOM   6182  N N     . VAL A 1 831  ? -26.570 73.339  83.127  1.00 14.13 ?  829  VAL A N     1 
ATOM   6183  C CA    . VAL A 1 831  ? -27.370 74.518  83.441  1.00 13.07 ?  829  VAL A CA    1 
ATOM   6184  C C     . VAL A 1 831  ? -28.075 74.351  84.782  1.00 12.21 ?  829  VAL A C     1 
ATOM   6185  O O     . VAL A 1 831  ? -28.117 75.283  85.596  1.00 12.60 ?  829  VAL A O     1 
ATOM   6186  C CB    . VAL A 1 831  ? -28.353 74.808  82.292  1.00 13.07 ?  829  VAL A CB    1 
ATOM   6187  C CG1   . VAL A 1 831  ? -29.409 75.851  82.718  1.00 14.48 ?  829  VAL A CG1   1 
ATOM   6188  C CG2   . VAL A 1 831  ? -27.577 75.348  81.101  1.00 14.69 ?  829  VAL A CG2   1 
ATOM   6189  N N     . GLY A 1 832  ? -28.625 73.167  85.042  1.00 13.16 ?  830  GLY A N     1 
ATOM   6190  C CA    . GLY A 1 832  ? -29.246 72.924  86.336  1.00 12.40 ?  830  GLY A CA    1 
ATOM   6191  C C     . GLY A 1 832  ? -28.271 73.090  87.484  1.00 14.09 ?  830  GLY A C     1 
ATOM   6192  O O     . GLY A 1 832  ? -28.591 73.722  88.495  1.00 13.95 ?  830  GLY A O     1 
ATOM   6193  N N     . ASP A 1 833  ? -27.064 72.550  87.332  1.00 12.63 ?  831  ASP A N     1 
ATOM   6194  C CA    . ASP A 1 833  ? -26.085 72.664  88.405  1.00 10.94 ?  831  ASP A CA    1 
ATOM   6195  C C     . ASP A 1 833  ? -25.562 74.089  88.550  1.00 12.68 ?  831  ASP A C     1 
ATOM   6196  O O     . ASP A 1 833  ? -25.186 74.502  89.655  1.00 13.18 ?  831  ASP A O     1 
ATOM   6197  C CB    . ASP A 1 833  ? -24.928 71.695  88.162  1.00 11.39 ?  831  ASP A CB    1 
ATOM   6198  C CG    . ASP A 1 833  ? -25.345 70.239  88.310  1.00 14.51 ?  831  ASP A CG    1 
ATOM   6199  O OD1   . ASP A 1 833  ? -26.398 69.959  88.935  1.00 15.87 ?  831  ASP A OD1   1 
ATOM   6200  O OD2   . ASP A 1 833  ? -24.616 69.361  87.799  1.00 14.63 ?  831  ASP A OD2   1 
ATOM   6201  N N     . VAL A 1 834  ? -25.514 74.853  87.463  1.00 11.85 ?  832  VAL A N     1 
ATOM   6202  C CA    . VAL A 1 834  ? -25.056 76.236  87.541  1.00 10.68 ?  832  VAL A CA    1 
ATOM   6203  C C     . VAL A 1 834  ? -26.111 77.110  88.211  1.00 11.82 ?  832  VAL A C     1 
ATOM   6204  O O     . VAL A 1 834  ? -25.805 77.911  89.099  1.00 12.95 ?  832  VAL A O     1 
ATOM   6205  C CB    . VAL A 1 834  ? -24.704 76.761  86.136  1.00 10.39 ?  832  VAL A CB    1 
ATOM   6206  C CG1   . VAL A 1 834  ? -24.541 78.262  86.146  1.00 12.30 ?  832  VAL A CG1   1 
ATOM   6207  C CG2   . VAL A 1 834  ? -23.413 76.106  85.644  1.00 13.18 ?  832  VAL A CG2   1 
ATOM   6208  N N     . ILE A 1 835  ? -27.371 76.978  87.782  1.00 12.96 ?  833  ILE A N     1 
ATOM   6209  C CA    . ILE A 1 835  ? -28.451 77.760  88.380  1.00 12.66 ?  833  ILE A CA    1 
ATOM   6210  C C     . ILE A 1 835  ? -28.509 77.523  89.885  1.00 14.47 ?  833  ILE A C     1 
ATOM   6211  O O     . ILE A 1 835  ? -28.617 78.470  90.677  1.00 14.05 ?  833  ILE A O     1 
ATOM   6212  C CB    . ILE A 1 835  ? -29.789 77.424  87.694  1.00 14.12 ?  833  ILE A CB    1 
ATOM   6213  C CG1   . ILE A 1 835  ? -29.829 77.941  86.241  1.00 14.62 ?  833  ILE A CG1   1 
ATOM   6214  C CG2   . ILE A 1 835  ? -30.986 77.972  88.508  1.00 16.97 ?  833  ILE A CG2   1 
ATOM   6215  C CD1   . ILE A 1 835  ? -29.998 79.460  86.096  1.00 16.79 ?  833  ILE A CD1   1 
ATOM   6216  N N     . THR A 1 836  ? -28.410 76.257  90.297  1.00 11.81 ?  834  THR A N     1 
ATOM   6217  C CA    . THR A 1 836  ? -28.383 75.935  91.718  1.00 13.72 ?  834  THR A CA    1 
ATOM   6218  C C     . THR A 1 836  ? -27.150 76.521  92.393  1.00 12.65 ?  834  THR A C     1 
ATOM   6219  O O     . THR A 1 836  ? -27.252 77.192  93.428  1.00 13.61 ?  834  THR A O     1 
ATOM   6220  C CB    . THR A 1 836  ? -28.425 74.422  91.893  1.00 17.14 ?  834  THR A CB    1 
ATOM   6221  O OG1   . THR A 1 836  ? -29.681 73.938  91.404  1.00 20.60 ?  834  THR A OG1   1 
ATOM   6222  C CG2   . THR A 1 836  ? -28.278 74.033  93.348  1.00 18.47 ?  834  THR A CG2   1 
ATOM   6223  N N     . SER A 1 837  ? -25.968 76.297  91.812  1.00 11.67 ?  835  SER A N     1 
ATOM   6224  C CA    . SER A 1 837  ? -24.739 76.664  92.516  1.00 10.62 ?  835  SER A CA    1 
ATOM   6225  C C     . SER A 1 837  ? -24.577 78.169  92.638  1.00 12.17 ?  835  SER A C     1 
ATOM   6226  O O     . SER A 1 837  ? -24.020 78.649  93.631  1.00 14.10 ?  835  SER A O     1 
ATOM   6227  C CB    . SER A 1 837  ? -23.514 76.079  91.807  1.00 11.47 ?  835  SER A CB    1 
ATOM   6228  O OG    . SER A 1 837  ? -23.550 74.659  91.787  1.00 12.86 ?  835  SER A OG    1 
ATOM   6229  N N     . ALA A 1 838  ? -25.031 78.932  91.644  1.00 11.77 ?  836  ALA A N     1 
ATOM   6230  C CA    . ALA A 1 838  ? -24.828 80.370  91.661  1.00 12.00 ?  836  ALA A CA    1 
ATOM   6231  C C     . ALA A 1 838  ? -25.904 81.115  92.431  1.00 13.27 ?  836  ALA A C     1 
ATOM   6232  O O     . ALA A 1 838  ? -25.610 82.152  93.030  1.00 12.62 ?  836  ALA A O     1 
ATOM   6233  C CB    . ALA A 1 838  ? -24.780 80.921  90.229  1.00 12.53 ?  836  ALA A CB    1 
ATOM   6234  N N     . PHE A 1 839  ? -27.149 80.637  92.408  1.00 14.60 ?  837  PHE A N     1 
ATOM   6235  C CA    . PHE A 1 839  ? -28.267 81.460  92.864  1.00 11.96 ?  837  PHE A CA    1 
ATOM   6236  C C     . PHE A 1 839  ? -29.035 80.892  94.044  1.00 14.59 ?  837  PHE A C     1 
ATOM   6237  O O     . PHE A 1 839  ? -29.804 81.639  94.664  1.00 14.71 ?  837  PHE A O     1 
ATOM   6238  C CB    . PHE A 1 839  ? -29.237 81.725  91.696  1.00 12.68 ?  837  PHE A CB    1 
ATOM   6239  C CG    . PHE A 1 839  ? -28.569 82.324  90.493  1.00 13.03 ?  837  PHE A CG    1 
ATOM   6240  C CD1   . PHE A 1 839  ? -27.796 83.472  90.600  1.00 14.11 ?  837  PHE A CD1   1 
ATOM   6241  C CD2   . PHE A 1 839  ? -28.689 81.716  89.256  1.00 14.70 ?  837  PHE A CD2   1 
ATOM   6242  C CE1   . PHE A 1 839  ? -27.168 84.019  89.494  1.00 13.41 ?  837  PHE A CE1   1 
ATOM   6243  C CE2   . PHE A 1 839  ? -28.058 82.256  88.140  1.00 14.16 ?  837  PHE A CE2   1 
ATOM   6244  C CZ    . PHE A 1 839  ? -27.303 83.417  88.264  1.00 13.68 ?  837  PHE A CZ    1 
ATOM   6245  N N     . ASP A 1 840  ? -28.842 79.622  94.390  1.00 14.81 ?  838  ASP A N     1 
ATOM   6246  C CA    . ASP A 1 840  ? -29.381 79.093  95.638  1.00 14.18 ?  838  ASP A CA    1 
ATOM   6247  C C     . ASP A 1 840  ? -28.967 79.986  96.797  1.00 15.28 ?  838  ASP A C     1 
ATOM   6248  O O     . ASP A 1 840  ? -27.839 80.484  96.836  1.00 14.30 ?  838  ASP A O     1 
ATOM   6249  C CB    . ASP A 1 840  ? -28.858 77.670  95.842  1.00 14.95 ?  838  ASP A CB    1 
ATOM   6250  C CG    . ASP A 1 840  ? -29.308 77.052  97.130  1.00 16.90 ?  838  ASP A CG    1 
ATOM   6251  O OD1   . ASP A 1 840  ? -28.765 77.419  98.200  1.00 15.93 ?  838  ASP A OD1   1 
ATOM   6252  O OD2   . ASP A 1 840  ? -30.194 76.171  97.058  1.00 19.44 ?  838  ASP A OD2   1 
ATOM   6253  N N     . SER A 1 841  ? -29.899 80.231  97.722  1.00 14.50 ?  839  SER A N     1 
ATOM   6254  C CA    . SER A 1 841  ? -29.612 81.057  98.900  1.00 14.03 ?  839  SER A CA    1 
ATOM   6255  C C     . SER A 1 841  ? -29.161 82.468  98.514  1.00 13.85 ?  839  SER A C     1 
ATOM   6256  O O     . SER A 1 841  ? -28.409 83.122  99.248  1.00 15.20 ?  839  SER A O     1 
ATOM   6257  C CB    . SER A 1 841  ? -28.580 80.372  99.805  1.00 14.74 ?  839  SER A CB    1 
ATOM   6258  O OG    . SER A 1 841  ? -29.086 79.121  100.247 1.00 16.82 ?  839  SER A OG    1 
ATOM   6259  N N     . ALA A 1 842  ? -29.632 82.954  97.359  1.00 13.70 ?  840  ALA A N     1 
ATOM   6260  C CA    . ALA A 1 842  ? -29.275 84.277  96.844  1.00 13.05 ?  840  ALA A CA    1 
ATOM   6261  C C     . ALA A 1 842  ? -27.764 84.420  96.696  1.00 12.51 ?  840  ALA A C     1 
ATOM   6262  O O     . ALA A 1 842  ? -27.210 85.510  96.843  1.00 15.90 ?  840  ALA A O     1 
ATOM   6263  C CB    . ALA A 1 842  ? -29.861 85.399  97.716  1.00 16.37 ?  840  ALA A CB    1 
ATOM   6264  N N     . GLY A 1 843  ? -27.100 83.311  96.385  1.00 14.92 ?  841  GLY A N     1 
ATOM   6265  C CA    . GLY A 1 843  ? -25.653 83.327  96.230  1.00 14.39 ?  841  GLY A CA    1 
ATOM   6266  C C     . GLY A 1 843  ? -24.897 83.626  97.504  1.00 15.35 ?  841  GLY A C     1 
ATOM   6267  O O     . GLY A 1 843  ? -23.706 83.938  97.455  1.00 15.88 ?  841  GLY A O     1 
ATOM   6268  N N     . GLN A 1 844  ? -25.556 83.524  98.654  1.00 13.35 ?  842  GLN A N     1 
ATOM   6269  C CA    . GLN A 1 844  ? -24.934 83.825  99.935  1.00 13.95 ?  842  GLN A CA    1 
ATOM   6270  C C     . GLN A 1 844  ? -24.311 82.597  100.582 1.00 17.19 ?  842  GLN A C     1 
ATOM   6271  O O     . GLN A 1 844  ? -24.382 82.427  101.807 1.00 22.06 ?  842  GLN A O     1 
ATOM   6272  C CB    . GLN A 1 844  ? -25.961 84.478  100.861 1.00 16.02 ?  842  GLN A CB    1 
ATOM   6273  C CG    . GLN A 1 844  ? -26.409 85.847  100.368 1.00 15.60 ?  842  GLN A CG    1 
ATOM   6274  C CD    . GLN A 1 844  ? -27.490 86.485  101.245 1.00 15.56 ?  842  GLN A CD    1 
ATOM   6275  O OE1   . GLN A 1 844  ? -27.464 87.685  101.497 1.00 16.36 ?  842  GLN A OE1   1 
ATOM   6276  N NE2   . GLN A 1 844  ? -28.444 85.687  101.701 1.00 18.64 ?  842  GLN A NE2   1 
ATOM   6277  N N     . ARG A 1 845  ? -23.742 81.711  99.788  1.00 14.92 ?  843  ARG A N     1 
ATOM   6278  C CA    . ARG A 1 845  ? -22.929 80.618  100.282 1.00 14.43 ?  843  ARG A CA    1 
ATOM   6279  C C     . ARG A 1 845  ? -21.477 80.933  99.981  1.00 16.08 ?  843  ARG A C     1 
ATOM   6280  O O     . ARG A 1 845  ? -21.151 81.401  98.886  1.00 15.55 ?  843  ARG A O     1 
ATOM   6281  C CB    . ARG A 1 845  ? -23.301 79.294  99.606  1.00 13.13 ?  843  ARG A CB    1 
ATOM   6282  C CG    . ARG A 1 845  ? -24.708 78.820  99.867  1.00 15.34 ?  843  ARG A CG    1 
ATOM   6283  C CD    . ARG A 1 845  ? -24.897 77.496  99.160  1.00 17.01 ?  843  ARG A CD    1 
ATOM   6284  N NE    . ARG A 1 845  ? -26.246 76.981  99.327  1.00 16.07 ?  843  ARG A NE    1 
ATOM   6285  C CZ    . ARG A 1 845  ? -26.564 75.937  100.082 1.00 16.56 ?  843  ARG A CZ    1 
ATOM   6286  N NH1   . ARG A 1 845  ? -25.646 75.270  100.774 1.00 15.95 ?  843  ARG A NH1   1 
ATOM   6287  N NH2   . ARG A 1 845  ? -27.837 75.551  100.144 1.00 16.40 ?  843  ARG A NH2   1 
ATOM   6288  N N     . CYS A 1 846  ? -20.595 80.649  100.937 1.00 15.31 ?  844  CYS A N     1 
ATOM   6289  C CA    . CYS A 1 846  ? -19.178 80.785  100.618 1.00 18.55 ?  844  CYS A CA    1 
ATOM   6290  C C     . CYS A 1 846  ? -18.754 79.833  99.510  1.00 14.61 ?  844  CYS A C     1 
ATOM   6291  O O     . CYS A 1 846  ? -17.782 80.120  98.810  1.00 16.12 ?  844  CYS A O     1 
ATOM   6292  C CB    . CYS A 1 846  ? -18.334 80.562  101.867 1.00 18.34 ?  844  CYS A CB    1 
ATOM   6293  S SG    . CYS A 1 846  ? -18.561 81.919  103.035 1.00 26.38 ?  844  CYS A SG    1 
ATOM   6294  N N     . SER A 1 847  ? -19.485 78.733  99.328  1.00 14.00 ?  845  SER A N     1 
ATOM   6295  C CA    . SER A 1 847  ? -19.271 77.733  98.287  1.00 12.52 ?  845  SER A CA    1 
ATOM   6296  C C     . SER A 1 847  ? -19.855 78.115  96.936  1.00 12.99 ?  845  SER A C     1 
ATOM   6297  O O     . SER A 1 847  ? -19.665 77.358  95.982  1.00 13.41 ?  845  SER A O     1 
ATOM   6298  C CB    . SER A 1 847  ? -19.925 76.419  98.717  1.00 14.83 ?  845  SER A CB    1 
ATOM   6299  O OG    . SER A 1 847  ? -21.300 76.682  99.020  1.00 14.49 ?  845  SER A OG    1 
ATOM   6300  N N     . ALA A 1 848  ? -20.602 79.214  96.847  1.00 12.49 ?  846  ALA A N     1 
ATOM   6301  C CA    . ALA A 1 848  ? -21.394 79.477  95.648  1.00 11.44 ?  846  ALA A CA    1 
ATOM   6302  C C     . ALA A 1 848  ? -20.526 79.633  94.408  1.00 11.39 ?  846  ALA A C     1 
ATOM   6303  O O     . ALA A 1 848  ? -19.392 80.114  94.462  1.00 12.98 ?  846  ALA A O     1 
ATOM   6304  C CB    . ALA A 1 848  ? -22.237 80.738  95.841  1.00 15.07 ?  846  ALA A CB    1 
ATOM   6305  N N     . LEU A 1 849  ? -21.112 79.286  93.265  1.00 11.26 ?  847  LEU A N     1 
ATOM   6306  C CA    . LEU A 1 849  ? -20.420 79.413  91.993  1.00 12.28 ?  847  LEU A CA    1 
ATOM   6307  C C     . LEU A 1 849  ? -20.335 80.882  91.598  1.00 12.42 ?  847  LEU A C     1 
ATOM   6308  O O     . LEU A 1 849  ? -21.365 81.552  91.454  1.00 12.60 ?  847  LEU A O     1 
ATOM   6309  C CB    . LEU A 1 849  ? -21.154 78.622  90.920  1.00 11.13 ?  847  LEU A CB    1 
ATOM   6310  C CG    . LEU A 1 849  ? -20.572 78.793  89.528  1.00 11.77 ?  847  LEU A CG    1 
ATOM   6311  C CD1   . LEU A 1 849  ? -19.123 78.315  89.483  1.00 13.04 ?  847  LEU A CD1   1 
ATOM   6312  C CD2   . LEU A 1 849  ? -21.433 78.032  88.522  1.00 12.09 ?  847  LEU A CD2   1 
ATOM   6313  N N     . ARG A 1 850  ? -19.109 81.386  91.431  1.00 11.54 ?  848  ARG A N     1 
ATOM   6314  C CA    . ARG A 1 850  ? -18.882 82.776  91.072  1.00 12.73 ?  848  ARG A CA    1 
ATOM   6315  C C     . ARG A 1 850  ? -18.429 82.972  89.631  1.00 13.49 ?  848  ARG A C     1 
ATOM   6316  O O     . ARG A 1 850  ? -18.743 84.007  89.042  1.00 13.35 ?  848  ARG A O     1 
ATOM   6317  C CB    . ARG A 1 850  ? -17.829 83.413  91.998  1.00 14.28 ?  848  ARG A CB    1 
ATOM   6318  C CG    . ARG A 1 850  ? -18.090 83.253  93.476  1.00 14.99 ?  848  ARG A CG    1 
ATOM   6319  C CD    . ARG A 1 850  ? -19.464 83.755  93.848  1.00 15.00 ?  848  ARG A CD    1 
ATOM   6320  N NE    . ARG A 1 850  ? -19.656 83.725  95.296  1.00 14.75 ?  848  ARG A NE    1 
ATOM   6321  C CZ    . ARG A 1 850  ? -20.790 84.052  95.895  1.00 16.48 ?  848  ARG A CZ    1 
ATOM   6322  N NH1   . ARG A 1 850  ? -21.852 84.423  95.196  1.00 15.77 ?  848  ARG A NH1   1 
ATOM   6323  N NH2   . ARG A 1 850  ? -20.854 84.021  97.227  1.00 16.18 ?  848  ARG A NH2   1 
ATOM   6324  N N     . VAL A 1 851  ? -17.660 82.036  89.066  1.00 13.42 ?  849  VAL A N     1 
ATOM   6325  C CA    A VAL A 1 851  ? -17.131 82.158  87.707  0.67 12.87 ?  849  VAL A CA    1 
ATOM   6326  C CA    B VAL A 1 851  ? -17.175 82.166  87.698  0.33 12.90 ?  849  VAL A CA    1 
ATOM   6327  C C     . VAL A 1 851  ? -17.372 80.845  86.971  1.00 12.98 ?  849  VAL A C     1 
ATOM   6328  O O     . VAL A 1 851  ? -16.792 79.819  87.339  1.00 13.32 ?  849  VAL A O     1 
ATOM   6329  C CB    A VAL A 1 851  ? -15.633 82.497  87.692  0.67 15.38 ?  849  VAL A CB    1 
ATOM   6330  C CB    B VAL A 1 851  ? -15.707 82.619  87.620  0.33 15.31 ?  849  VAL A CB    1 
ATOM   6331  C CG1   A VAL A 1 851  ? -15.203 82.836  86.273  0.67 14.02 ?  849  VAL A CG1   1 
ATOM   6332  C CG1   B VAL A 1 851  ? -15.615 84.121  87.794  0.33 16.43 ?  849  VAL A CG1   1 
ATOM   6333  C CG2   A VAL A 1 851  ? -15.296 83.618  88.649  0.67 18.33 ?  849  VAL A CG2   1 
ATOM   6334  C CG2   B VAL A 1 851  ? -14.857 81.915  88.644  0.33 15.52 ?  849  VAL A CG2   1 
ATOM   6335  N N     . LEU A 1 852  ? -18.205 80.876  85.940  1.00 12.23 ?  850  LEU A N     1 
ATOM   6336  C CA    . LEU A 1 852  ? -18.440 79.734  85.069  1.00 13.66 ?  850  LEU A CA    1 
ATOM   6337  C C     . LEU A 1 852  ? -17.546 79.877  83.846  1.00 11.16 ?  850  LEU A C     1 
ATOM   6338  O O     . LEU A 1 852  ? -17.526 80.939  83.219  1.00 12.35 ?  850  LEU A O     1 
ATOM   6339  C CB    . LEU A 1 852  ? -19.910 79.685  84.641  1.00 12.80 ?  850  LEU A CB    1 
ATOM   6340  C CG    . LEU A 1 852  ? -20.318 78.621  83.627  1.00 13.79 ?  850  LEU A CG    1 
ATOM   6341  C CD1   . LEU A 1 852  ? -20.165 77.227  84.227  1.00 13.66 ?  850  LEU A CD1   1 
ATOM   6342  C CD2   . LEU A 1 852  ? -21.768 78.876  83.162  1.00 13.81 ?  850  LEU A CD2   1 
ATOM   6343  N N     . CYS A 1 853  ? -16.807 78.813  83.515  1.00 11.90 ?  851  CYS A N     1 
ATOM   6344  C CA    . CYS A 1 853  ? -15.837 78.834  82.421  1.00 12.69 ?  851  CYS A CA    1 
ATOM   6345  C C     . CYS A 1 853  ? -16.283 77.837  81.365  1.00 11.83 ?  851  CYS A C     1 
ATOM   6346  O O     . CYS A 1 853  ? -16.298 76.635  81.622  1.00 12.00 ?  851  CYS A O     1 
ATOM   6347  C CB    . CYS A 1 853  ? -14.438 78.492  82.925  1.00 13.16 ?  851  CYS A CB    1 
ATOM   6348  S SG    . CYS A 1 853  ? -13.932 79.406  84.401  1.00 15.73 ?  851  CYS A SG    1 
ATOM   6349  N N     . LEU A 1 854  ? -16.648 78.339  80.188  1.00 12.61 ?  852  LEU A N     1 
ATOM   6350  C CA    . LEU A 1 854  ? -17.266 77.546  79.132  1.00 12.41 ?  852  LEU A CA    1 
ATOM   6351  C C     . LEU A 1 854  ? -16.295 77.387  77.974  1.00 12.19 ?  852  LEU A C     1 
ATOM   6352  O O     . LEU A 1 854  ? -15.772 78.383  77.448  1.00 12.86 ?  852  LEU A O     1 
ATOM   6353  C CB    . LEU A 1 854  ? -18.541 78.217  78.619  1.00 12.75 ?  852  LEU A CB    1 
ATOM   6354  C CG    . LEU A 1 854  ? -19.640 78.393  79.672  1.00 11.94 ?  852  LEU A CG    1 
ATOM   6355  C CD1   . LEU A 1 854  ? -20.851 79.092  79.025  1.00 14.35 ?  852  LEU A CD1   1 
ATOM   6356  C CD2   . LEU A 1 854  ? -20.070 77.069  80.271  1.00 14.66 ?  852  LEU A CD2   1 
ATOM   6357  N N     . GLN A 1 855  ? -16.086 76.144  77.554  1.00 13.71 ?  853  GLN A N     1 
ATOM   6358  C CA    . GLN A 1 855  ? -15.279 75.930  76.363  1.00 12.55 ?  853  GLN A CA    1 
ATOM   6359  C C     . GLN A 1 855  ? -15.927 76.641  75.181  1.00 13.93 ?  853  GLN A C     1 
ATOM   6360  O O     . GLN A 1 855  ? -17.149 76.574  75.001  1.00 14.40 ?  853  GLN A O     1 
ATOM   6361  C CB    . GLN A 1 855  ? -15.124 74.442  76.079  1.00 14.13 ?  853  GLN A CB    1 
ATOM   6362  C CG    . GLN A 1 855  ? -14.070 74.183  75.013  1.00 13.12 ?  853  GLN A CG    1 
ATOM   6363  C CD    . GLN A 1 855  ? -14.024 72.741  74.569  1.00 16.46 ?  853  GLN A CD    1 
ATOM   6364  O OE1   . GLN A 1 855  ? -14.103 71.832  75.387  1.00 17.93 ?  853  GLN A OE1   1 
ATOM   6365  N NE2   . GLN A 1 855  ? -13.896 72.523  73.247  1.00 18.37 ?  853  GLN A NE2   1 
ATOM   6366  N N     . GLU A 1 856  ? -15.094 77.322  74.380  1.00 14.35 ?  854  GLU A N     1 
ATOM   6367  C CA    . GLU A 1 856  ? -15.601 78.266  73.378  1.00 16.28 ?  854  GLU A CA    1 
ATOM   6368  C C     . GLU A 1 856  ? -16.638 77.627  72.455  1.00 15.19 ?  854  GLU A C     1 
ATOM   6369  O O     . GLU A 1 856  ? -17.682 78.229  72.172  1.00 18.63 ?  854  GLU A O     1 
ATOM   6370  C CB    . GLU A 1 856  ? -14.431 78.846  72.572  1.00 16.72 ?  854  GLU A CB    1 
ATOM   6371  C CG    . GLU A 1 856  ? -14.848 79.729  71.385  1.00 19.26 ?  854  GLU A CG    1 
ATOM   6372  C CD    . GLU A 1 856  ? -15.595 80.977  71.813  1.00 27.06 ?  854  GLU A CD    1 
ATOM   6373  O OE1   . GLU A 1 856  ? -15.317 81.481  72.923  1.00 24.87 ?  854  GLU A OE1   1 
ATOM   6374  O OE2   . GLU A 1 856  ? -16.465 81.448  71.041  1.00 25.18 ?  854  GLU A OE2   1 
ATOM   6375  N N     . ASP A 1 857  ? -16.407 76.383  72.031  1.00 16.10 ?  855  ASP A N     1 
ATOM   6376  C CA    . ASP A 1 857  ? -17.270 75.769  71.026  1.00 20.17 ?  855  ASP A CA    1 
ATOM   6377  C C     . ASP A 1 857  ? -18.704 75.571  71.510  1.00 19.91 ?  855  ASP A C     1 
ATOM   6378  O O     . ASP A 1 857  ? -19.626 75.528  70.686  1.00 23.94 ?  855  ASP A O     1 
ATOM   6379  C CB    . ASP A 1 857  ? -16.680 74.433  70.572  1.00 23.10 ?  855  ASP A CB    1 
ATOM   6380  C CG    . ASP A 1 857  ? -17.258 73.968  69.241  1.00 32.92 ?  855  ASP A CG    1 
ATOM   6381  O OD1   . ASP A 1 857  ? -17.170 74.734  68.255  1.00 39.67 ?  855  ASP A OD1   1 
ATOM   6382  O OD2   . ASP A 1 857  ? -17.795 72.841  69.182  1.00 42.56 ?  855  ASP A OD2   1 
ATOM   6383  N N     . VAL A 1 858  ? -18.927 75.450  72.821  1.00 16.41 ?  856  VAL A N     1 
ATOM   6384  C CA    . VAL A 1 858  ? -20.268 75.232  73.361  1.00 16.46 ?  856  VAL A CA    1 
ATOM   6385  C C     . VAL A 1 858  ? -20.774 76.424  74.143  1.00 14.68 ?  856  VAL A C     1 
ATOM   6386  O O     . VAL A 1 858  ? -21.897 76.374  74.671  1.00 15.60 ?  856  VAL A O     1 
ATOM   6387  C CB    . VAL A 1 858  ? -20.334 73.966  74.236  1.00 16.11 ?  856  VAL A CB    1 
ATOM   6388  C CG1   . VAL A 1 858  ? -20.117 72.727  73.368  1.00 21.05 ?  856  VAL A CG1   1 
ATOM   6389  C CG2   . VAL A 1 858  ? -19.299 74.038  75.382  1.00 15.80 ?  856  VAL A CG2   1 
ATOM   6390  N N     . ALA A 1 859  ? -19.995 77.503  74.218  1.00 14.15 ?  857  ALA A N     1 
ATOM   6391  C CA    . ALA A 1 859  ? -20.335 78.604  75.114  1.00 13.92 ?  857  ALA A CA    1 
ATOM   6392  C C     . ALA A 1 859  ? -21.646 79.275  74.725  1.00 17.06 ?  857  ALA A C     1 
ATOM   6393  O O     . ALA A 1 859  ? -22.467 79.593  75.594  1.00 16.02 ?  857  ALA A O     1 
ATOM   6394  C CB    . ALA A 1 859  ? -19.199 79.628  75.136  1.00 16.76 ?  857  ALA A CB    1 
ATOM   6395  N N     . ASP A 1 860  ? -21.867 79.508  73.429  1.00 16.83 ?  858  ASP A N     1 
ATOM   6396  C CA    . ASP A 1 860  ? -23.070 80.232  73.041  1.00 18.78 ?  858  ASP A CA    1 
ATOM   6397  C C     . ASP A 1 860  ? -24.324 79.419  73.332  1.00 16.28 ?  858  ASP A C     1 
ATOM   6398  O O     . ASP A 1 860  ? -25.325 79.966  73.817  1.00 16.98 ?  858  ASP A O     1 
ATOM   6399  C CB    . ASP A 1 860  ? -23.005 80.605  71.561  1.00 17.95 ?  858  ASP A CB    1 
ATOM   6400  C CG    . ASP A 1 860  ? -22.027 81.728  71.280  1.00 24.88 ?  858  ASP A CG    1 
ATOM   6401  O OD1   . ASP A 1 860  ? -21.872 82.625  72.136  1.00 28.49 ?  858  ASP A OD1   1 
ATOM   6402  O OD2   . ASP A 1 860  ? -21.418 81.723  70.191  1.00 39.43 ?  858  ASP A OD2   1 
ATOM   6403  N N     . ARG A 1 861  ? -24.292 78.112  73.061  1.00 14.88 ?  859  ARG A N     1 
ATOM   6404  C CA    . ARG A 1 861  ? -25.467 77.292  73.312  1.00 15.59 ?  859  ARG A CA    1 
ATOM   6405  C C     . ARG A 1 861  ? -25.769 77.204  74.803  1.00 14.59 ?  859  ARG A C     1 
ATOM   6406  O O     . ARG A 1 861  ? -26.926 77.324  75.222  1.00 16.12 ?  859  ARG A O     1 
ATOM   6407  C CB    . ARG A 1 861  ? -25.275 75.896  72.716  1.00 20.63 ?  859  ARG A CB    1 
ATOM   6408  C CG    . ARG A 1 861  ? -26.463 75.004  73.004  1.00 28.03 ?  859  ARG A CG    1 
ATOM   6409  C CD    . ARG A 1 861  ? -26.545 73.794  72.112  1.00 37.50 ?  859  ARG A CD    1 
ATOM   6410  N NE    . ARG A 1 861  ? -27.635 72.932  72.555  1.00 44.77 ?  859  ARG A NE    1 
ATOM   6411  C CZ    . ARG A 1 861  ? -27.495 71.956  73.441  1.00 41.31 ?  859  ARG A CZ    1 
ATOM   6412  N NH1   . ARG A 1 861  ? -26.313 71.659  73.958  1.00 43.17 ?  859  ARG A NH1   1 
ATOM   6413  N NH2   . ARG A 1 861  ? -28.563 71.257  73.812  1.00 35.15 ?  859  ARG A NH2   1 
ATOM   6414  N N     . ILE A 1 862  ? -24.740 77.012  75.623  1.00 14.35 ?  860  ILE A N     1 
ATOM   6415  C CA    . ILE A 1 862  ? -24.973 76.903  77.059  1.00 13.28 ?  860  ILE A CA    1 
ATOM   6416  C C     . ILE A 1 862  ? -25.415 78.243  77.637  1.00 14.72 ?  860  ILE A C     1 
ATOM   6417  O O     . ILE A 1 862  ? -26.312 78.299  78.488  1.00 14.83 ?  860  ILE A O     1 
ATOM   6418  C CB    . ILE A 1 862  ? -23.707 76.366  77.747  1.00 13.62 ?  860  ILE A CB    1 
ATOM   6419  C CG1   . ILE A 1 862  ? -23.500 74.899  77.337  1.00 17.90 ?  860  ILE A CG1   1 
ATOM   6420  C CG2   . ILE A 1 862  ? -23.803 76.517  79.268  1.00 15.50 ?  860  ILE A CG2   1 
ATOM   6421  C CD1   . ILE A 1 862  ? -22.219 74.286  77.876  1.00 21.24 ?  860  ILE A CD1   1 
ATOM   6422  N N     . LEU A 1 863  ? -24.811 79.339  77.181  1.00 13.66 ?  861  LEU A N     1 
ATOM   6423  C CA    . LEU A 1 863  ? -25.220 80.655  77.658  1.00 14.82 ?  861  LEU A CA    1 
ATOM   6424  C C     . LEU A 1 863  ? -26.683 80.940  77.331  1.00 15.50 ?  861  LEU A C     1 
ATOM   6425  O O     . LEU A 1 863  ? -27.426 81.446  78.180  1.00 14.43 ?  861  LEU A O     1 
ATOM   6426  C CB    . LEU A 1 863  ? -24.307 81.718  77.063  1.00 18.19 ?  861  LEU A CB    1 
ATOM   6427  C CG    . LEU A 1 863  ? -24.281 83.076  77.741  1.00 24.72 ?  861  LEU A CG    1 
ATOM   6428  C CD1   . LEU A 1 863  ? -24.075 82.938  79.240  1.00 20.60 ?  861  LEU A CD1   1 
ATOM   6429  C CD2   . LEU A 1 863  ? -23.182 83.908  77.106  1.00 26.55 ?  861  LEU A CD2   1 
ATOM   6430  N N     . THR A 1 864  ? -27.123 80.607  76.114  1.00 13.25 ?  862  THR A N     1 
ATOM   6431  C CA    . THR A 1 864  ? -28.535 80.784  75.771  1.00 14.88 ?  862  THR A CA    1 
ATOM   6432  C C     . THR A 1 864  ? -29.434 79.997  76.718  1.00 12.42 ?  862  THR A C     1 
ATOM   6433  O O     . THR A 1 864  ? -30.447 80.511  77.213  1.00 13.71 ?  862  THR A O     1 
ATOM   6434  C CB    . THR A 1 864  ? -28.774 80.343  74.326  1.00 15.10 ?  862  THR A CB    1 
ATOM   6435  O OG1   . THR A 1 864  ? -28.043 81.207  73.451  1.00 18.78 ?  862  THR A OG1   1 
ATOM   6436  C CG2   . THR A 1 864  ? -30.272 80.361  73.971  1.00 16.61 ?  862  THR A CG2   1 
ATOM   6437  N N     . MET A 1 865  ? -29.077 78.738  76.983  1.00 13.01 ?  863  MET A N     1 
ATOM   6438  C CA    . MET A 1 865  ? -29.882 77.915  77.873  1.00 11.51 ?  863  MET A CA    1 
ATOM   6439  C C     . MET A 1 865  ? -29.847 78.465  79.295  1.00 12.67 ?  863  MET A C     1 
ATOM   6440  O O     . MET A 1 865  ? -30.872 78.501  79.988  1.00 11.96 ?  863  MET A O     1 
ATOM   6441  C CB    . MET A 1 865  ? -29.373 76.470  77.822  1.00 13.32 ?  863  MET A CB    1 
ATOM   6442  C CG    . MET A 1 865  ? -30.222 75.494  78.602  1.00 17.07 ?  863  MET A CG    1 
ATOM   6443  S SD    . MET A 1 865  ? -29.623 73.797  78.434  1.00 19.51 ?  863  MET A SD    1 
ATOM   6444  C CE    . MET A 1 865  ? -29.250 73.857  76.671  1.00 19.92 ?  863  MET A CE    1 
ATOM   6445  N N     . LEU A 1 866  ? -28.676 78.926  79.734  1.00 11.61 ?  864  LEU A N     1 
ATOM   6446  C CA    . LEU A 1 866  ? -28.552 79.473  81.079  1.00 11.06 ?  864  LEU A CA    1 
ATOM   6447  C C     . LEU A 1 866  ? -29.420 80.720  81.266  1.00 10.37 ?  864  LEU A C     1 
ATOM   6448  O O     . LEU A 1 866  ? -30.105 80.860  82.291  1.00 13.03 ?  864  LEU A O     1 
ATOM   6449  C CB    . LEU A 1 866  ? -27.079 79.775  81.350  1.00 14.10 ?  864  LEU A CB    1 
ATOM   6450  C CG    . LEU A 1 866  ? -26.737 80.332  82.725  1.00 17.37 ?  864  LEU A CG    1 
ATOM   6451  C CD1   . LEU A 1 866  ? -27.178 79.340  83.779  1.00 17.28 ?  864  LEU A CD1   1 
ATOM   6452  C CD2   . LEU A 1 866  ? -25.239 80.583  82.801  1.00 19.28 ?  864  LEU A CD2   1 
ATOM   6453  N N     . LYS A 1 867  ? -29.395 81.649  80.299  1.00 12.00 ?  865  LYS A N     1 
ATOM   6454  C CA    . LYS A 1 867  ? -30.239 82.835  80.419  1.00 13.30 ?  865  LYS A CA    1 
ATOM   6455  C C     . LYS A 1 867  ? -31.714 82.455  80.426  1.00 13.90 ?  865  LYS A C     1 
ATOM   6456  O O     . LYS A 1 867  ? -32.508 83.022  81.192  1.00 13.78 ?  865  LYS A O     1 
ATOM   6457  C CB    . LYS A 1 867  ? -29.929 83.825  79.296  1.00 15.81 ?  865  LYS A CB    1 
ATOM   6458  C CG    . LYS A 1 867  ? -28.509 84.368  79.398  1.00 13.80 ?  865  LYS A CG    1 
ATOM   6459  C CD    . LYS A 1 867  ? -28.163 85.235  78.194  1.00 18.61 ?  865  LYS A CD    1 
ATOM   6460  C CE    . LYS A 1 867  ? -26.721 85.719  78.280  1.00 21.16 ?  865  LYS A CE    1 
ATOM   6461  N NZ    . LYS A 1 867  ? -26.280 86.476  77.064  1.00 24.36 ?  865  LYS A NZ    1 
ATOM   6462  N N     . GLY A 1 868  ? -32.096 81.481  79.601  1.00 13.41 ?  866  GLY A N     1 
ATOM   6463  C CA    . GLY A 1 868  ? -33.478 81.031  79.613  1.00 13.82 ?  866  GLY A CA    1 
ATOM   6464  C C     . GLY A 1 868  ? -33.889 80.438  80.949  1.00 14.04 ?  866  GLY A C     1 
ATOM   6465  O O     . GLY A 1 868  ? -35.000 80.675  81.432  1.00 13.81 ?  866  GLY A O     1 
ATOM   6466  N N     . ALA A 1 869  ? -32.998 79.661  81.566  1.00 12.75 ?  867  ALA A N     1 
ATOM   6467  C CA    . ALA A 1 869  ? -33.302 79.078  82.871  1.00 10.82 ?  867  ALA A CA    1 
ATOM   6468  C C     . ALA A 1 869  ? -33.359 80.158  83.942  1.00 12.95 ?  867  ALA A C     1 
ATOM   6469  O O     . ALA A 1 869  ? -34.163 80.074  84.881  1.00 12.97 ?  867  ALA A O     1 
ATOM   6470  C CB    . ALA A 1 869  ? -32.256 78.024  83.240  1.00 12.07 ?  867  ALA A CB    1 
ATOM   6471  N N     . LEU A 1 870  ? -32.499 81.172  83.820  1.00 11.60 ?  868  LEU A N     1 
ATOM   6472  C CA    . LEU A 1 870  ? -32.505 82.274  84.778  1.00 12.61 ?  868  LEU A CA    1 
ATOM   6473  C C     . LEU A 1 870  ? -33.885 82.903  84.884  1.00 14.49 ?  868  LEU A C     1 
ATOM   6474  O O     . LEU A 1 870  ? -34.370 83.191  85.985  1.00 14.69 ?  868  LEU A O     1 
ATOM   6475  C CB    . LEU A 1 870  ? -31.477 83.322  84.344  1.00 13.90 ?  868  LEU A CB    1 
ATOM   6476  C CG    . LEU A 1 870  ? -31.255 84.490  85.308  1.00 14.10 ?  868  LEU A CG    1 
ATOM   6477  C CD1   . LEU A 1 870  ? -30.277 84.066  86.356  1.00 17.56 ?  868  LEU A CD1   1 
ATOM   6478  C CD2   . LEU A 1 870  ? -30.794 85.790  84.598  1.00 16.29 ?  868  LEU A CD2   1 
ATOM   6479  N N     . HIS A 1 871  ? -34.541 83.106  83.747  1.00 13.38 ?  869  HIS A N     1 
ATOM   6480  C CA    . HIS A 1 871  ? -35.810 83.818  83.747  1.00 14.36 ?  869  HIS A CA    1 
ATOM   6481  C C     . HIS A 1 871  ? -36.974 82.978  84.241  1.00 15.17 ?  869  HIS A C     1 
ATOM   6482  O O     . HIS A 1 871  ? -38.086 83.506  84.366  1.00 18.60 ?  869  HIS A O     1 
ATOM   6483  C CB    . HIS A 1 871  ? -36.082 84.362  82.352  1.00 17.31 ?  869  HIS A CB    1 
ATOM   6484  C CG    . HIS A 1 871  ? -35.185 85.503  82.002  1.00 17.91 ?  869  HIS A CG    1 
ATOM   6485  N ND1   . HIS A 1 871  ? -35.328 86.754  82.565  1.00 21.63 ?  869  HIS A ND1   1 
ATOM   6486  C CD2   . HIS A 1 871  ? -34.103 85.575  81.192  1.00 17.42 ?  869  HIS A CD2   1 
ATOM   6487  C CE1   . HIS A 1 871  ? -34.384 87.553  82.101  1.00 22.34 ?  869  HIS A CE1   1 
ATOM   6488  N NE2   . HIS A 1 871  ? -33.634 86.867  81.257  1.00 19.73 ?  869  HIS A NE2   1 
ATOM   6489  N N     . GLU A 1 872  ? -36.746 81.713  84.561  1.00 13.66 ?  870  GLU A N     1 
ATOM   6490  C CA    . GLU A 1 872  ? -37.771 80.869  85.155  1.00 14.29 ?  870  GLU A CA    1 
ATOM   6491  C C     . GLU A 1 872  ? -37.733 80.872  86.678  1.00 15.15 ?  870  GLU A C     1 
ATOM   6492  O O     . GLU A 1 872  ? -38.542 80.176  87.307  1.00 15.63 ?  870  GLU A O     1 
ATOM   6493  C CB    . GLU A 1 872  ? -37.637 79.432  84.635  1.00 15.65 ?  870  GLU A CB    1 
ATOM   6494  C CG    . GLU A 1 872  ? -37.844 79.314  83.129  1.00 16.82 ?  870  GLU A CG    1 
ATOM   6495  C CD    . GLU A 1 872  ? -39.230 79.738  82.688  1.00 17.29 ?  870  GLU A CD    1 
ATOM   6496  O OE1   . GLU A 1 872  ? -40.172 79.631  83.509  1.00 17.62 ?  870  GLU A OE1   1 
ATOM   6497  O OE2   . GLU A 1 872  ? -39.387 80.169  81.521  1.00 19.41 ?  870  GLU A OE2   1 
ATOM   6498  N N     . LEU A 1 873  ? -36.825 81.629  87.289  1.00 13.94 ?  871  LEU A N     1 
ATOM   6499  C CA    . LEU A 1 873  ? -36.720 81.659  88.739  1.00 13.99 ?  871  LEU A CA    1 
ATOM   6500  C C     . LEU A 1 873  ? -37.724 82.635  89.339  1.00 14.42 ?  871  LEU A C     1 
ATOM   6501  O O     . LEU A 1 873  ? -37.975 83.707  88.787  1.00 17.02 ?  871  LEU A O     1 
ATOM   6502  C CB    . LEU A 1 873  ? -35.305 82.053  89.168  1.00 14.46 ?  871  LEU A CB    1 
ATOM   6503  C CG    . LEU A 1 873  ? -34.177 81.125  88.710  1.00 14.45 ?  871  LEU A CG    1 
ATOM   6504  C CD1   . LEU A 1 873  ? -32.819 81.777  89.020  1.00 15.78 ?  871  LEU A CD1   1 
ATOM   6505  C CD2   . LEU A 1 873  ? -34.285 79.758  89.395  1.00 15.92 ?  871  LEU A CD2   1 
ATOM   6506  N N     . HIS A 1 874  ? -38.291 82.250  90.476  1.00 15.26 ?  872  HIS A N     1 
ATOM   6507  C CA    . HIS A 1 874  ? -39.228 83.076  91.224  1.00 14.96 ?  872  HIS A CA    1 
ATOM   6508  C C     . HIS A 1 874  ? -38.503 83.657  92.436  1.00 16.49 ?  872  HIS A C     1 
ATOM   6509  O O     . HIS A 1 874  ? -37.990 82.908  93.282  1.00 15.80 ?  872  HIS A O     1 
ATOM   6510  C CB    . HIS A 1 874  ? -40.446 82.252  91.649  1.00 17.09 ?  872  HIS A CB    1 
ATOM   6511  C CG    . HIS A 1 874  ? -41.474 83.030  92.414  1.00 19.62 ?  872  HIS A CG    1 
ATOM   6512  N ND1   . HIS A 1 874  ? -41.557 84.404  92.365  1.00 28.99 ?  872  HIS A ND1   1 
ATOM   6513  C CD2   . HIS A 1 874  ? -42.454 82.624  93.257  1.00 23.94 ?  872  HIS A CD2   1 
ATOM   6514  C CE1   . HIS A 1 874  ? -42.539 84.813  93.149  1.00 24.63 ?  872  HIS A CE1   1 
ATOM   6515  N NE2   . HIS A 1 874  ? -43.098 83.754  93.701  1.00 24.51 ?  872  HIS A NE2   1 
ATOM   6516  N N     . ILE A 1 875  ? -38.449 84.985  92.510  1.00 16.58 ?  873  ILE A N     1 
ATOM   6517  C CA    . ILE A 1 875  ? -37.793 85.697  93.603  1.00 17.13 ?  873  ILE A CA    1 
ATOM   6518  C C     . ILE A 1 875  ? -38.867 86.359  94.461  1.00 18.52 ?  873  ILE A C     1 
ATOM   6519  O O     . ILE A 1 875  ? -39.763 87.028  93.933  1.00 19.74 ?  873  ILE A O     1 
ATOM   6520  C CB    . ILE A 1 875  ? -36.791 86.744  93.080  1.00 18.79 ?  873  ILE A CB    1 
ATOM   6521  C CG1   . ILE A 1 875  ? -35.509 86.111  92.532  1.00 23.42 ?  873  ILE A CG1   1 
ATOM   6522  C CG2   . ILE A 1 875  ? -36.335 87.639  94.207  1.00 20.38 ?  873  ILE A CG2   1 
ATOM   6523  C CD1   . ILE A 1 875  ? -35.647 85.206  91.341  1.00 23.92 ?  873  ILE A CD1   1 
ATOM   6524  N N     . GLY A 1 876  ? -38.776 86.193  95.779  1.00 16.47 ?  874  GLY A N     1 
ATOM   6525  C CA    . GLY A 1 876  ? -39.705 86.875  96.663  1.00 15.07 ?  874  GLY A CA    1 
ATOM   6526  C C     . GLY A 1 876  ? -39.544 86.438  98.106  1.00 17.83 ?  874  GLY A C     1 
ATOM   6527  O O     . GLY A 1 876  ? -38.637 85.674  98.452  1.00 17.52 ?  874  GLY A O     1 
ATOM   6528  N N     . ARG A 1 877  ? -40.449 86.948  98.950  1.00 18.03 ?  875  ARG A N     1 
ATOM   6529  C CA    . ARG A 1 877  ? -40.441 86.575  100.360 1.00 17.53 ?  875  ARG A CA    1 
ATOM   6530  C C     . ARG A 1 877  ? -40.569 85.061  100.489 1.00 19.09 ?  875  ARG A C     1 
ATOM   6531  O O     . ARG A 1 877  ? -41.369 84.431  99.793  1.00 18.54 ?  875  ARG A O     1 
ATOM   6532  C CB    . ARG A 1 877  ? -41.585 87.277  101.103 1.00 19.13 ?  875  ARG A CB    1 
ATOM   6533  C CG    . ARG A 1 877  ? -41.362 87.327  102.606 1.00 20.15 ?  875  ARG A CG    1 
ATOM   6534  C CD    . ARG A 1 877  ? -42.440 88.148  103.301 1.00 25.11 ?  875  ARG A CD    1 
ATOM   6535  N NE    . ARG A 1 877  ? -43.659 87.386  103.528 1.00 25.94 ?  875  ARG A NE    1 
ATOM   6536  C CZ    . ARG A 1 877  ? -44.731 87.865  104.146 1.00 31.43 ?  875  ARG A CZ    1 
ATOM   6537  N NH1   . ARG A 1 877  ? -44.783 89.119  104.566 1.00 31.72 ?  875  ARG A NH1   1 
ATOM   6538  N NH2   . ARG A 1 877  ? -45.773 87.065  104.353 1.00 32.40 ?  875  ARG A NH2   1 
ATOM   6539  N N     . THR A 1 878  ? -39.764 84.467  101.369 1.00 19.66 ?  876  THR A N     1 
ATOM   6540  C CA    . THR A 1 878  ? -39.556 83.027  101.318 1.00 18.51 ?  876  THR A CA    1 
ATOM   6541  C C     . THR A 1 878  ? -40.565 82.229  102.127 1.00 20.58 ?  876  THR A C     1 
ATOM   6542  O O     . THR A 1 878  ? -40.320 81.048  102.400 1.00 21.34 ?  876  THR A O     1 
ATOM   6543  C CB    . THR A 1 878  ? -38.139 82.665  101.764 1.00 18.37 ?  876  THR A CB    1 
ATOM   6544  O OG1   . THR A 1 878  ? -37.830 83.313  103.000 1.00 22.95 ?  876  THR A OG1   1 
ATOM   6545  C CG2   . THR A 1 878  ? -37.150 83.088  100.696 1.00 20.15 ?  876  THR A CG2   1 
ATOM   6546  N N     . ASP A 1 879  ? -41.702 82.812  102.489 1.00 20.77 ?  877  ASP A N     1 
ATOM   6547  C CA    . ASP A 1 879  ? -42.740 82.006  103.116 1.00 23.45 ?  877  ASP A CA    1 
ATOM   6548  C C     . ASP A 1 879  ? -43.713 81.424  102.097 1.00 21.96 ?  877  ASP A C     1 
ATOM   6549  O O     . ASP A 1 879  ? -44.861 81.122  102.441 1.00 21.02 ?  877  ASP A O     1 
ATOM   6550  C CB    . ASP A 1 879  ? -43.464 82.804  104.204 1.00 22.57 ?  877  ASP A CB    1 
ATOM   6551  C CG    . ASP A 1 879  ? -44.166 84.033  103.680 1.00 25.75 ?  877  ASP A CG    1 
ATOM   6552  O OD1   . ASP A 1 879  ? -43.775 84.573  102.621 1.00 25.16 ?  877  ASP A OD1   1 
ATOM   6553  O OD2   . ASP A 1 879  ? -45.123 84.473  104.358 1.00 27.75 ?  877  ASP A OD2   1 
ATOM   6554  N N     . ARG A 1 880  ? -43.267 81.233  100.853 1.00 18.74 ?  878  ARG A N     1 
ATOM   6555  C CA    . ARG A 1 880  ? -44.016 80.514  99.826  1.00 17.31 ?  878  ARG A CA    1 
ATOM   6556  C C     . ARG A 1 880  ? -43.110 79.457  99.216  1.00 15.46 ?  878  ARG A C     1 
ATOM   6557  O O     . ARG A 1 880  ? -41.978 79.765  98.837  1.00 17.84 ?  878  ARG A O     1 
ATOM   6558  C CB    . ARG A 1 880  ? -44.520 81.451  98.722  1.00 19.40 ?  878  ARG A CB    1 
ATOM   6559  C CG    . ARG A 1 880  ? -45.632 82.385  99.173  1.00 25.01 ?  878  ARG A CG    1 
ATOM   6560  C CD    . ARG A 1 880  ? -45.967 83.383  98.064  1.00 28.32 ?  878  ARG A CD    1 
ATOM   6561  N NE    . ARG A 1 880  ? -46.946 84.371  98.503  1.00 39.82 ?  878  ARG A NE    1 
ATOM   6562  C CZ    . ARG A 1 880  ? -48.208 84.398  98.099  1.00 43.59 ?  878  ARG A CZ    1 
ATOM   6563  N NH1   . ARG A 1 880  ? -48.674 83.512  97.234  1.00 45.95 ?  878  ARG A NH1   1 
ATOM   6564  N NH2   . ARG A 1 880  ? -49.020 85.340  98.572  1.00 43.67 ?  878  ARG A NH2   1 
ATOM   6565  N N     . LEU A 1 881  ? -43.619 78.223  99.106  1.00 15.57 ?  879  LEU A N     1 
ATOM   6566  C CA    . LEU A 1 881  ? -42.869 77.126  98.489  1.00 17.15 ?  879  LEU A CA    1 
ATOM   6567  C C     . LEU A 1 881  ? -42.418 77.457  97.070  1.00 14.93 ?  879  LEU A C     1 
ATOM   6568  O O     . LEU A 1 881  ? -41.374 76.970  96.620  1.00 16.75 ?  879  LEU A O     1 
ATOM   6569  C CB    . LEU A 1 881  ? -43.729 75.860  98.487  1.00 17.33 ?  879  LEU A CB    1 
ATOM   6570  C CG    . LEU A 1 881  ? -43.110 74.572  97.938  1.00 18.15 ?  879  LEU A CG    1 
ATOM   6571  C CD1   . LEU A 1 881  ? -41.981 74.080  98.852  1.00 17.79 ?  879  LEU A CD1   1 
ATOM   6572  C CD2   . LEU A 1 881  ? -44.193 73.505  97.768  1.00 20.14 ?  879  LEU A CD2   1 
ATOM   6573  N N     . SER A 1 882  ? -43.171 78.299  96.358  1.00 15.52 ?  880  SER A N     1 
ATOM   6574  C CA    . SER A 1 882  ? -42.832 78.599  94.970  1.00 14.77 ?  880  SER A CA    1 
ATOM   6575  C C     . SER A 1 882  ? -41.612 79.501  94.820  1.00 17.21 ?  880  SER A C     1 
ATOM   6576  O O     . SER A 1 882  ? -41.132 79.676  93.695  1.00 17.96 ?  880  SER A O     1 
ATOM   6577  C CB    . SER A 1 882  ? -44.032 79.253  94.271  1.00 15.90 ?  880  SER A CB    1 
ATOM   6578  O OG    . SER A 1 882  ? -44.387 80.466  94.923  1.00 20.53 ?  880  SER A OG    1 
ATOM   6579  N N     . VAL A 1 883  ? -41.086 80.071  95.899  1.00 16.14 ?  881  VAL A N     1 
ATOM   6580  C CA    . VAL A 1 883  ? -39.961 80.990  95.765  1.00 16.57 ?  881  VAL A CA    1 
ATOM   6581  C C     . VAL A 1 883  ? -38.666 80.201  95.646  1.00 15.68 ?  881  VAL A C     1 
ATOM   6582  O O     . VAL A 1 883  ? -38.380 79.321  96.462  1.00 18.12 ?  881  VAL A O     1 
ATOM   6583  C CB    . VAL A 1 883  ? -39.910 81.971  96.946  1.00 16.88 ?  881  VAL A CB    1 
ATOM   6584  C CG1   . VAL A 1 883  ? -38.568 82.690  96.966  1.00 18.46 ?  881  VAL A CG1   1 
ATOM   6585  C CG2   . VAL A 1 883  ? -41.057 82.959  96.831  1.00 16.56 ?  881  VAL A CG2   1 
ATOM   6586  N N     . ASP A 1 884  ? -37.879 80.526  94.626  1.00 14.43 ?  882  ASP A N     1 
ATOM   6587  C CA    . ASP A 1 884  ? -36.589 79.894  94.392  1.00 15.95 ?  882  ASP A CA    1 
ATOM   6588  C C     . ASP A 1 884  ? -35.444 80.659  95.029  1.00 16.89 ?  882  ASP A C     1 
ATOM   6589  O O     . ASP A 1 884  ? -34.472 80.049  95.492  1.00 18.18 ?  882  ASP A O     1 
ATOM   6590  C CB    . ASP A 1 884  ? -36.340 79.786  92.892  1.00 14.64 ?  882  ASP A CB    1 
ATOM   6591  C CG    . ASP A 1 884  ? -37.412 79.007  92.203  1.00 14.69 ?  882  ASP A CG    1 
ATOM   6592  O OD1   . ASP A 1 884  ? -37.625 77.839  92.605  1.00 15.57 ?  882  ASP A OD1   1 
ATOM   6593  O OD2   . ASP A 1 884  ? -38.048 79.578  91.290  1.00 16.57 ?  882  ASP A OD2   1 
ATOM   6594  N N     . VAL A 1 885  ? -35.522 81.981  95.018  1.00 14.29 ?  883  VAL A N     1 
ATOM   6595  C CA    . VAL A 1 885  ? -34.452 82.841  95.502  1.00 14.62 ?  883  VAL A CA    1 
ATOM   6596  C C     . VAL A 1 885  ? -35.065 83.888  96.412  1.00 15.36 ?  883  VAL A C     1 
ATOM   6597  O O     . VAL A 1 885  ? -35.985 84.606  96.003  1.00 16.40 ?  883  VAL A O     1 
ATOM   6598  C CB    . VAL A 1 885  ? -33.692 83.517  94.345  1.00 17.84 ?  883  VAL A CB    1 
ATOM   6599  C CG1   . VAL A 1 885  ? -32.594 84.423  94.892  1.00 18.72 ?  883  VAL A CG1   1 
ATOM   6600  C CG2   . VAL A 1 885  ? -33.091 82.471  93.404  1.00 16.74 ?  883  VAL A CG2   1 
ATOM   6601  N N     . GLY A 1 886  ? -34.554 83.980  97.639  1.00 15.03 ?  884  GLY A N     1 
ATOM   6602  C CA    . GLY A 1 886  ? -35.036 84.935  98.610  1.00 14.71 ?  884  GLY A CA    1 
ATOM   6603  C C     . GLY A 1 886  ? -34.232 86.220  98.615  1.00 15.04 ?  884  GLY A C     1 
ATOM   6604  O O     . GLY A 1 886  ? -33.472 86.508  97.682  1.00 16.72 ?  884  GLY A O     1 
ATOM   6605  N N     . PRO A 1 887  ? -34.365 87.003  99.683  1.00 15.63 ?  885  PRO A N     1 
ATOM   6606  C CA    . PRO A 1 887  ? -33.644 88.274  99.778  1.00 14.56 ?  885  PRO A CA    1 
ATOM   6607  C C     . PRO A 1 887  ? -32.187 88.066  100.171 1.00 15.72 ?  885  PRO A C     1 
ATOM   6608  O O     . PRO A 1 887  ? -31.780 87.002  100.632 1.00 16.00 ?  885  PRO A O     1 
ATOM   6609  C CB    . PRO A 1 887  ? -34.404 89.010  100.888 1.00 17.01 ?  885  PRO A CB    1 
ATOM   6610  C CG    . PRO A 1 887  ? -34.832 87.890  101.796 1.00 20.22 ?  885  PRO A CG    1 
ATOM   6611  C CD    . PRO A 1 887  ? -35.192 86.748  100.871 1.00 16.50 ?  885  PRO A CD    1 
ATOM   6612  N N     . VAL A 1 888  ? -31.396 89.120  99.982  1.00 17.36 ?  886  VAL A N     1 
ATOM   6613  C CA    . VAL A 1 888  ? -30.084 89.162  100.617 1.00 16.36 ?  886  VAL A CA    1 
ATOM   6614  C C     . VAL A 1 888  ? -30.277 89.715  102.028 1.00 18.50 ?  886  VAL A C     1 
ATOM   6615  O O     . VAL A 1 888  ? -31.338 90.257  102.363 1.00 17.66 ?  886  VAL A O     1 
ATOM   6616  C CB    . VAL A 1 888  ? -29.066 89.978  99.797  1.00 16.55 ?  886  VAL A CB    1 
ATOM   6617  C CG1   . VAL A 1 888  ? -28.820 89.294  98.453  1.00 18.53 ?  886  VAL A CG1   1 
ATOM   6618  C CG2   . VAL A 1 888  ? -29.536 91.423  99.595  1.00 19.14 ?  886  VAL A CG2   1 
ATOM   6619  N N     . ILE A 1 889  ? -29.251 89.580  102.868 1.00 18.45 ?  887  ILE A N     1 
ATOM   6620  C CA    . ILE A 1 889  ? -29.462 89.674  104.314 1.00 17.56 ?  887  ILE A CA    1 
ATOM   6621  C C     . ILE A 1 889  ? -29.747 91.101  104.784 1.00 20.46 ?  887  ILE A C     1 
ATOM   6622  O O     . ILE A 1 889  ? -30.519 91.285  105.731 1.00 20.82 ?  887  ILE A O     1 
ATOM   6623  C CB    . ILE A 1 889  ? -28.259 89.056  105.059 1.00 18.17 ?  887  ILE A CB    1 
ATOM   6624  C CG1   . ILE A 1 889  ? -28.530 88.962  106.569 1.00 20.82 ?  887  ILE A CG1   1 
ATOM   6625  C CG2   . ILE A 1 889  ? -26.978 89.821  104.766 1.00 18.81 ?  887  ILE A CG2   1 
ATOM   6626  C CD1   . ILE A 1 889  ? -29.575 87.927  106.933 1.00 19.94 ?  887  ILE A CD1   1 
ATOM   6627  N N     . THR A 1 890  ? -29.166 92.124  104.146 1.00 19.17 ?  888  THR A N     1 
ATOM   6628  C CA    . THR A 1 890  ? -29.317 93.506  104.606 1.00 19.98 ?  888  THR A CA    1 
ATOM   6629  C C     . THR A 1 890  ? -29.321 94.468  103.428 1.00 19.98 ?  888  THR A C     1 
ATOM   6630  O O     . THR A 1 890  ? -28.931 94.123  102.308 1.00 19.99 ?  888  THR A O     1 
ATOM   6631  C CB    . THR A 1 890  ? -28.176 93.953  105.532 1.00 22.50 ?  888  THR A CB    1 
ATOM   6632  O OG1   . THR A 1 890  ? -26.933 93.845  104.826 1.00 22.40 ?  888  THR A OG1   1 
ATOM   6633  C CG2   . THR A 1 890  ? -28.125 93.148  106.836 1.00 25.19 ?  888  THR A CG2   1 
ATOM   6634  N N     . SER A 1 891  ? -29.732 95.712  103.709 1.00 22.39 ?  889  SER A N     1 
ATOM   6635  C CA    A SER A 1 891  ? -29.639 96.749  102.688 0.48 22.30 ?  889  SER A CA    1 
ATOM   6636  C CA    B SER A 1 891  ? -29.639 96.775  102.711 0.52 22.29 ?  889  SER A CA    1 
ATOM   6637  C C     . SER A 1 891  ? -28.190 97.045  102.330 1.00 23.21 ?  889  SER A C     1 
ATOM   6638  O O     . SER A 1 891  ? -27.891 97.356  101.173 1.00 23.52 ?  889  SER A O     1 
ATOM   6639  C CB    A SER A 1 891  ? -30.342 98.021  103.157 0.48 24.81 ?  889  SER A CB    1 
ATOM   6640  C CB    B SER A 1 891  ? -30.295 98.058  103.232 0.52 24.81 ?  889  SER A CB    1 
ATOM   6641  O OG    A SER A 1 891  ? -29.705 98.542  104.305 0.48 25.46 ?  889  SER A OG    1 
ATOM   6642  O OG    B SER A 1 891  ? -31.684 97.895  103.470 0.52 24.85 ?  889  SER A OG    1 
ATOM   6643  N N     . GLU A 1 892  ? -27.274 96.943  103.297 1.00 22.53 ?  890  GLU A N     1 
ATOM   6644  C CA    . GLU A 1 892  ? -25.868 97.182  102.990 1.00 22.93 ?  890  GLU A CA    1 
ATOM   6645  C C     . GLU A 1 892  ? -25.331 96.115  102.044 1.00 22.62 ?  890  GLU A C     1 
ATOM   6646  O O     . GLU A 1 892  ? -24.569 96.423  101.119 1.00 23.51 ?  890  GLU A O     1 
ATOM   6647  C CB    . GLU A 1 892  ? -25.036 97.223  104.274 1.00 24.99 ?  890  GLU A CB    1 
ATOM   6648  C CG    . GLU A 1 892  ? -25.565 98.135  105.374 1.00 32.25 ?  890  GLU A CG    1 
ATOM   6649  C CD    . GLU A 1 892  ? -26.586 97.439  106.273 1.00 33.73 ?  890  GLU A CD    1 
ATOM   6650  O OE1   . GLU A 1 892  ? -27.779 97.414  105.916 1.00 32.15 ?  890  GLU A OE1   1 
ATOM   6651  O OE2   . GLU A 1 892  ? -26.189 96.905  107.336 1.00 46.43 ?  890  GLU A OE2   1 
ATOM   6652  N N     . ALA A 1 893  ? -25.695 94.852  102.277 1.00 20.96 ?  891  ALA A N     1 
ATOM   6653  C CA    . ALA A 1 893  ? -25.313 93.793  101.349 1.00 19.85 ?  891  ALA A CA    1 
ATOM   6654  C C     . ALA A 1 893  ? -25.877 94.064  99.964  1.00 20.60 ?  891  ALA A C     1 
ATOM   6655  O O     . ALA A 1 893  ? -25.170 93.940  98.958  1.00 21.56 ?  891  ALA A O     1 
ATOM   6656  C CB    . ALA A 1 893  ? -25.794 92.435  101.865 1.00 18.84 ?  891  ALA A CB    1 
ATOM   6657  N N     . LYS A 1 894  ? -27.159 94.423  99.897  1.00 19.20 ?  892  LYS A N     1 
ATOM   6658  C CA    . LYS A 1 894  ? -27.787 94.751  98.623  1.00 22.33 ?  892  LYS A CA    1 
ATOM   6659  C C     . LYS A 1 894  ? -27.037 95.869  97.908  1.00 23.54 ?  892  LYS A C     1 
ATOM   6660  O O     . LYS A 1 894  ? -26.744 95.767  96.711  1.00 22.06 ?  892  LYS A O     1 
ATOM   6661  C CB    . LYS A 1 894  ? -29.251 95.134  98.856  1.00 22.66 ?  892  LYS A CB    1 
ATOM   6662  C CG    . LYS A 1 894  ? -29.986 95.598  97.611  1.00 22.19 ?  892  LYS A CG    1 
ATOM   6663  C CD    . LYS A 1 894  ? -31.431 95.943  97.920  1.00 23.65 ?  892  LYS A CD    1 
ATOM   6664  C CE    . LYS A 1 894  ? -32.124 96.514  96.682  1.00 27.69 ?  892  LYS A CE    1 
ATOM   6665  N NZ    . LYS A 1 894  ? -33.451 97.088  97.006  1.00 34.52 ?  892  LYS A NZ    1 
ATOM   6666  N N     . ASP A 1 895  ? -26.706 96.944  98.632  1.00 22.11 ?  893  ASP A N     1 
ATOM   6667  C CA    . ASP A 1 895  ? -26.038 98.077  98.001  1.00 23.57 ?  893  ASP A CA    1 
ATOM   6668  C C     . ASP A 1 895  ? -24.666 97.678  97.476  1.00 23.56 ?  893  ASP A C     1 
ATOM   6669  O O     . ASP A 1 895  ? -24.253 98.112  96.394  1.00 22.47 ?  893  ASP A O     1 
ATOM   6670  C CB    . ASP A 1 895  ? -25.896 99.238  98.991  1.00 23.15 ?  893  ASP A CB    1 
ATOM   6671  C CG    . ASP A 1 895  ? -27.229 99.800  99.442  1.00 34.10 ?  893  ASP A CG    1 
ATOM   6672  O OD1   . ASP A 1 895  ? -28.277 99.427  98.865  1.00 37.70 ?  893  ASP A OD1   1 
ATOM   6673  O OD2   . ASP A 1 895  ? -27.218 100.623 100.387 1.00 38.23 ?  893  ASP A OD2   1 
ATOM   6674  N N     . ASN A 1 896  ? -23.942 96.863  98.238  1.00 21.01 ?  894  ASN A N     1 
ATOM   6675  C CA    . ASN A 1 896  ? -22.615 96.437  97.817  1.00 22.23 ?  894  ASN A CA    1 
ATOM   6676  C C     . ASN A 1 896  ? -22.688 95.612  96.537  1.00 24.25 ?  894  ASN A C     1 
ATOM   6677  O O     . ASN A 1 896  ? -21.907 95.827  95.602  1.00 23.62 ?  894  ASN A O     1 
ATOM   6678  C CB    . ASN A 1 896  ? -21.956 95.653  98.954  1.00 27.09 ?  894  ASN A CB    1 
ATOM   6679  C CG    . ASN A 1 896  ? -20.556 95.182  98.614  1.00 35.30 ?  894  ASN A CG    1 
ATOM   6680  O OD1   . ASN A 1 896  ? -20.374 94.095  98.067  1.00 39.35 ?  894  ASN A OD1   1 
ATOM   6681  N ND2   . ASN A 1 896  ? -19.560 95.993  98.944  1.00 38.81 ?  894  ASN A ND2   1 
ATOM   6682  N N     . ILE A 1 897  ? -23.641 94.682  96.469  1.00 21.30 ?  895  ILE A N     1 
ATOM   6683  C CA    . ILE A 1 897  ? -23.764 93.824  95.295  1.00 22.08 ?  895  ILE A CA    1 
ATOM   6684  C C     . ILE A 1 897  ? -24.184 94.642  94.080  1.00 21.09 ?  895  ILE A C     1 
ATOM   6685  O O     . ILE A 1 897  ? -23.634 94.481  92.984  1.00 22.60 ?  895  ILE A O     1 
ATOM   6686  C CB    . ILE A 1 897  ? -24.756 92.681  95.578  1.00 17.95 ?  895  ILE A CB    1 
ATOM   6687  C CG1   . ILE A 1 897  ? -24.253 91.795  96.724  1.00 20.80 ?  895  ILE A CG1   1 
ATOM   6688  C CG2   . ILE A 1 897  ? -25.010 91.864  94.307  1.00 21.38 ?  895  ILE A CG2   1 
ATOM   6689  C CD1   . ILE A 1 897  ? -25.349 90.984  97.387  1.00 20.58 ?  895  ILE A CD1   1 
ATOM   6690  N N     . GLU A 1 898  ? -25.158 95.537  94.253  1.00 20.90 ?  896  GLU A N     1 
ATOM   6691  C CA    . GLU A 1 898  ? -25.634 96.333  93.127  1.00 21.66 ?  896  GLU A CA    1 
ATOM   6692  C C     . GLU A 1 898  ? -24.561 97.279  92.602  1.00 23.82 ?  896  GLU A C     1 
ATOM   6693  O O     . GLU A 1 898  ? -24.501 97.528  91.393  1.00 23.04 ?  896  GLU A O     1 
ATOM   6694  C CB    . GLU A 1 898  ? -26.886 97.110  93.527  1.00 23.47 ?  896  GLU A CB    1 
ATOM   6695  C CG    . GLU A 1 898  ? -28.114 96.232  93.634  1.00 25.21 ?  896  GLU A CG    1 
ATOM   6696  C CD    . GLU A 1 898  ? -29.337 96.998  94.117  1.00 28.45 ?  896  GLU A CD    1 
ATOM   6697  O OE1   . GLU A 1 898  ? -29.173 98.118  94.650  1.00 39.82 ?  896  GLU A OE1   1 
ATOM   6698  O OE2   . GLU A 1 898  ? -30.458 96.473  93.962  1.00 41.39 ?  896  GLU A OE2   1 
ATOM   6699  N N     . LYS A 1 899  ? -23.713 97.818  93.480  1.00 23.70 ?  897  LYS A N     1 
ATOM   6700  C CA    . LYS A 1 899  ? -22.617 98.654  93.002  1.00 23.43 ?  897  LYS A CA    1 
ATOM   6701  C C     . LYS A 1 899  ? -21.696 97.874  92.074  1.00 22.11 ?  897  LYS A C     1 
ATOM   6702  O O     . LYS A 1 899  ? -21.232 98.409  91.062  1.00 23.28 ?  897  LYS A O     1 
ATOM   6703  C CB    . LYS A 1 899  ? -21.832 99.232  94.178  1.00 25.42 ?  897  LYS A CB    1 
ATOM   6704  C CG    . LYS A 1 899  ? -22.526 100.401 94.856  1.00 34.90 ?  897  LYS A CG    1 
ATOM   6705  C CD    . LYS A 1 899  ? -21.691 100.961 96.001  1.00 39.55 ?  897  LYS A CD    1 
ATOM   6706  C CE    . LYS A 1 899  ? -22.466 102.031 96.744  1.00 43.46 ?  897  LYS A CE    1 
ATOM   6707  N NZ    . LYS A 1 899  ? -23.117 102.975 95.789  1.00 45.68 ?  897  LYS A NZ    1 
ATOM   6708  N N     . HIS A 1 900  ? -21.428 96.607  92.396  1.00 18.84 ?  898  HIS A N     1 
ATOM   6709  C CA    . HIS A 1 900  ? -20.594 95.783  91.527  1.00 20.79 ?  898  HIS A CA    1 
ATOM   6710  C C     . HIS A 1 900  ? -21.257 95.589  90.171  1.00 19.58 ?  898  HIS A C     1 
ATOM   6711  O O     . HIS A 1 900  ? -20.622 95.768  89.128  1.00 22.40 ?  898  HIS A O     1 
ATOM   6712  C CB    . HIS A 1 900  ? -20.321 94.432  92.185  1.00 20.03 ?  898  HIS A CB    1 
ATOM   6713  C CG    . HIS A 1 900  ? -19.685 93.436  91.270  1.00 20.79 ?  898  HIS A CG    1 
ATOM   6714  N ND1   . HIS A 1 900  ? -18.334 93.439  90.992  1.00 23.48 ?  898  HIS A ND1   1 
ATOM   6715  C CD2   . HIS A 1 900  ? -20.211 92.395  90.578  1.00 20.36 ?  898  HIS A CD2   1 
ATOM   6716  C CE1   . HIS A 1 900  ? -18.055 92.444  90.168  1.00 24.49 ?  898  HIS A CE1   1 
ATOM   6717  N NE2   . HIS A 1 900  ? -19.175 91.796  89.901  1.00 20.49 ?  898  HIS A NE2   1 
ATOM   6718  N N     . ILE A 1 901  ? -22.544 95.225  90.169  1.00 18.91 ?  899  ILE A N     1 
ATOM   6719  C CA    . ILE A 1 901  ? -23.246 94.984  88.911  1.00 20.57 ?  899  ILE A CA    1 
ATOM   6720  C C     . ILE A 1 901  ? -23.195 96.224  88.034  1.00 22.34 ?  899  ILE A C     1 
ATOM   6721  O O     . ILE A 1 901  ? -22.912 96.143  86.831  1.00 23.28 ?  899  ILE A O     1 
ATOM   6722  C CB    . ILE A 1 901  ? -24.695 94.542  89.181  1.00 19.47 ?  899  ILE A CB    1 
ATOM   6723  C CG1   . ILE A 1 901  ? -24.701 93.220  89.944  1.00 19.47 ?  899  ILE A CG1   1 
ATOM   6724  C CG2   . ILE A 1 901  ? -25.470 94.410  87.869  1.00 19.11 ?  899  ILE A CG2   1 
ATOM   6725  C CD1   . ILE A 1 901  ? -26.054 92.817  90.495  1.00 18.53 ?  899  ILE A CD1   1 
ATOM   6726  N N     . GLU A 1 902  ? -23.439 97.393  88.625  1.00 23.07 ?  900  GLU A N     1 
ATOM   6727  C CA    . GLU A 1 902  ? -23.457 98.610  87.825  1.00 23.54 ?  900  GLU A CA    1 
ATOM   6728  C C     . GLU A 1 902  ? -22.070 98.975  87.312  1.00 23.49 ?  900  GLU A C     1 
ATOM   6729  O O     . GLU A 1 902  ? -21.947 99.501  86.200  1.00 25.17 ?  900  GLU A O     1 
ATOM   6730  C CB    . GLU A 1 902  ? -24.058 99.764  88.628  1.00 24.07 ?  900  GLU A CB    1 
ATOM   6731  C CG    . GLU A 1 902  ? -25.541 99.578  88.908  1.00 31.73 ?  900  GLU A CG    1 
ATOM   6732  C CD    . GLU A 1 902  ? -26.316 99.106  87.683  1.00 32.03 ?  900  GLU A CD    1 
ATOM   6733  O OE1   . GLU A 1 902  ? -26.195 99.744  86.616  1.00 35.14 ?  900  GLU A OE1   1 
ATOM   6734  O OE2   . GLU A 1 902  ? -27.043 98.088  87.784  1.00 31.98 ?  900  GLU A OE2   1 
ATOM   6735  N N     . ARG A 1 903  ? -21.022 98.703  88.094  1.00 22.90 ?  901  ARG A N     1 
ATOM   6736  C CA    . ARG A 1 903  ? -19.666 98.927  87.605  1.00 23.69 ?  901  ARG A CA    1 
ATOM   6737  C C     . ARG A 1 903  ? -19.383 98.066  86.378  1.00 26.19 ?  901  ARG A C     1 
ATOM   6738  O O     . ARG A 1 903  ? -18.859 98.557  85.371  1.00 25.97 ?  901  ARG A O     1 
ATOM   6739  C CB    . ARG A 1 903  ? -18.645 98.644  88.709  1.00 27.25 ?  901  ARG A CB    1 
ATOM   6740  N N     . MET A 1 904  ? -19.735 96.776  86.445  1.00 23.38 ?  902  MET A N     1 
ATOM   6741  C CA    . MET A 1 904  ? -19.587 95.898  85.286  1.00 22.02 ?  902  MET A CA    1 
ATOM   6742  C C     . MET A 1 904  ? -20.400 96.403  84.103  1.00 23.05 ?  902  MET A C     1 
ATOM   6743  O O     . MET A 1 904  ? -19.922 96.399  82.963  1.00 23.96 ?  902  MET A O     1 
ATOM   6744  C CB    . MET A 1 904  ? -20.019 94.473  85.641  1.00 19.59 ?  902  MET A CB    1 
ATOM   6745  C CG    . MET A 1 904  ? -19.188 93.791  86.707  1.00 20.80 ?  902  MET A CG    1 
ATOM   6746  S SD    . MET A 1 904  ? -17.463 93.618  86.222  1.00 29.01 ?  902  MET A SD    1 
ATOM   6747  C CE    . MET A 1 904  ? -16.693 94.946  87.156  1.00 29.09 ?  902  MET A CE    1 
ATOM   6748  N N     . ARG A 1 905  ? -21.641 96.819  84.351  1.00 21.74 ?  903  ARG A N     1 
ATOM   6749  C CA    . ARG A 1 905  ? -22.468 97.331  83.268  1.00 22.33 ?  903  ARG A CA    1 
ATOM   6750  C C     . ARG A 1 905  ? -21.832 98.563  82.642  1.00 24.41 ?  903  ARG A C     1 
ATOM   6751  O O     . ARG A 1 905  ? -21.786 98.691  81.415  1.00 26.10 ?  903  ARG A O     1 
ATOM   6752  C CB    . ARG A 1 905  ? -23.872 97.649  83.782  1.00 26.37 ?  903  ARG A CB    1 
ATOM   6753  C CG    . ARG A 1 905  ? -24.919 97.726  82.696  1.00 28.00 ?  903  ARG A CG    1 
ATOM   6754  C CD    . ARG A 1 905  ? -26.230 98.289  83.221  1.00 26.91 ?  903  ARG A CD    1 
ATOM   6755  N NE    . ARG A 1 905  ? -26.701 97.615  84.425  1.00 26.51 ?  903  ARG A NE    1 
ATOM   6756  C CZ    . ARG A 1 905  ? -27.512 96.568  84.422  1.00 24.78 ?  903  ARG A CZ    1 
ATOM   6757  N NH1   . ARG A 1 905  ? -27.887 95.987  83.293  1.00 24.13 ?  903  ARG A NH1   1 
ATOM   6758  N NH2   . ARG A 1 905  ? -27.961 96.093  85.582  1.00 30.12 ?  903  ARG A NH2   1 
ATOM   6759  N N     . GLY A 1 906  ? -21.320 99.471  83.476  1.00 25.55 ?  904  GLY A N     1 
ATOM   6760  C CA    . GLY A 1 906  ? -20.682 100.671 82.976  1.00 26.21 ?  904  GLY A CA    1 
ATOM   6761  C C     . GLY A 1 906  ? -19.433 100.408 82.162  1.00 28.05 ?  904  GLY A C     1 
ATOM   6762  O O     . GLY A 1 906  ? -19.073 101.235 81.319  1.00 30.43 ?  904  GLY A O     1 
ATOM   6763  N N     . LEU A 1 907  ? -18.768 99.276  82.389  1.00 27.87 ?  905  LEU A N     1 
ATOM   6764  C CA    . LEU A 1 907  ? -17.609 98.891  81.592  1.00 26.12 ?  905  LEU A CA    1 
ATOM   6765  C C     . LEU A 1 907  ? -17.992 98.228  80.279  1.00 26.85 ?  905  LEU A C     1 
ATOM   6766  O O     . LEU A 1 907  ? -17.098 97.854  79.514  1.00 32.98 ?  905  LEU A O     1 
ATOM   6767  C CB    . LEU A 1 907  ? -16.704 97.952  82.392  1.00 25.93 ?  905  LEU A CB    1 
ATOM   6768  C CG    . LEU A 1 907  ? -16.084 98.556  83.649  1.00 29.30 ?  905  LEU A CG    1 
ATOM   6769  C CD1   . LEU A 1 907  ? -15.384 97.485  84.458  1.00 31.17 ?  905  LEU A CD1   1 
ATOM   6770  C CD2   . LEU A 1 907  ? -15.121 99.675  83.284  1.00 34.89 ?  905  LEU A CD2   1 
ATOM   6771  N N     . GLY A 1 908  ? -19.283 98.075  80.004  1.00 26.37 ?  906  GLY A N     1 
ATOM   6772  C CA    . GLY A 1 908  ? -19.736 97.522  78.750  1.00 26.41 ?  906  GLY A CA    1 
ATOM   6773  C C     . GLY A 1 908  ? -19.933 96.024  78.738  1.00 25.19 ?  906  GLY A C     1 
ATOM   6774  O O     . GLY A 1 908  ? -20.141 95.455  77.662  1.00 26.26 ?  906  GLY A O     1 
ATOM   6775  N N     . ARG A 1 909  ? -19.880 95.368  79.890  1.00 22.30 ?  907  ARG A N     1 
ATOM   6776  C CA    . ARG A 1 909  ? -20.063 93.925  79.943  1.00 20.58 ?  907  ARG A CA    1 
ATOM   6777  C C     . ARG A 1 909  ? -21.546 93.583  79.864  1.00 24.49 ?  907  ARG A C     1 
ATOM   6778  O O     . ARG A 1 909  ? -22.395 94.308  80.396  1.00 24.86 ?  907  ARG A O     1 
ATOM   6779  C CB    . ARG A 1 909  ? -19.443 93.368  81.221  1.00 22.09 ?  907  ARG A CB    1 
ATOM   6780  C CG    . ARG A 1 909  ? -18.045 93.896  81.466  1.00 26.83 ?  907  ARG A CG    1 
ATOM   6781  C CD    . ARG A 1 909  ? -16.991 92.830  81.250  1.00 33.15 ?  907  ARG A CD    1 
ATOM   6782  N NE    . ARG A 1 909  ? -15.641 93.375  81.139  1.00 36.65 ?  907  ARG A NE    1 
ATOM   6783  C CZ    . ARG A 1 909  ? -14.954 93.927  82.134  1.00 42.84 ?  907  ARG A CZ    1 
ATOM   6784  N NH1   . ARG A 1 909  ? -15.478 94.083  83.340  1.00 44.92 ?  907  ARG A NH1   1 
ATOM   6785  N NH2   . ARG A 1 909  ? -13.708 94.337  81.913  1.00 44.89 ?  907  ARG A NH2   1 
ATOM   6786  N N     . LYS A 1 910  ? -21.855 92.473  79.188  1.00 18.82 ?  908  LYS A N     1 
ATOM   6787  C CA    . LYS A 1 910  ? -23.241 92.059  79.024  1.00 19.69 ?  908  LYS A CA    1 
ATOM   6788  C C     . LYS A 1 910  ? -23.794 91.573  80.353  1.00 19.09 ?  908  LYS A C     1 
ATOM   6789  O O     . LYS A 1 910  ? -23.233 90.664  80.970  1.00 18.91 ?  908  LYS A O     1 
ATOM   6790  C CB    . LYS A 1 910  ? -23.362 90.968  77.964  1.00 20.19 ?  908  LYS A CB    1 
ATOM   6791  C CG    . LYS A 1 910  ? -23.096 91.435  76.537  1.00 28.10 ?  908  LYS A CG    1 
ATOM   6792  C CD    . LYS A 1 910  ? -23.406 90.332  75.529  1.00 26.20 ?  908  LYS A CD    1 
ATOM   6793  C CE    . LYS A 1 910  ? -24.851 89.875  75.648  1.00 30.23 ?  908  LYS A CE    1 
ATOM   6794  N NZ    . LYS A 1 910  ? -25.286 89.096  74.449  1.00 38.17 ?  908  LYS A NZ    1 
ATOM   6795  N N     . VAL A 1 911  ? -24.891 92.186  80.793  1.00 18.23 ?  909  VAL A N     1 
ATOM   6796  C CA    . VAL A 1 911  ? -25.523 91.879  82.071  1.00 18.15 ?  909  VAL A CA    1 
ATOM   6797  C C     . VAL A 1 911  ? -26.943 91.390  81.810  1.00 19.25 ?  909  VAL A C     1 
ATOM   6798  O O     . VAL A 1 911  ? -27.736 92.083  81.156  1.00 21.22 ?  909  VAL A O     1 
ATOM   6799  C CB    . VAL A 1 911  ? -25.526 93.106  82.997  1.00 17.26 ?  909  VAL A CB    1 
ATOM   6800  C CG1   . VAL A 1 911  ? -26.264 92.798  84.288  1.00 19.76 ?  909  VAL A CG1   1 
ATOM   6801  C CG2   . VAL A 1 911  ? -24.097 93.556  83.278  1.00 19.32 ?  909  VAL A CG2   1 
ATOM   6802  N N     . GLU A 1 912  ? -27.260 90.200  82.313  1.00 17.88 ?  910  GLU A N     1 
ATOM   6803  C CA    . GLU A 1 912  ? -28.600 89.628  82.239  1.00 17.04 ?  910  GLU A CA    1 
ATOM   6804  C C     . GLU A 1 912  ? -29.189 89.575  83.642  1.00 17.29 ?  910  GLU A C     1 
ATOM   6805  O O     . GLU A 1 912  ? -28.540 89.076  84.566  1.00 16.91 ?  910  GLU A O     1 
ATOM   6806  C CB    . GLU A 1 912  ? -28.559 88.219  81.636  1.00 16.73 ?  910  GLU A CB    1 
ATOM   6807  C CG    . GLU A 1 912  ? -29.926 87.633  81.301  1.00 18.64 ?  910  GLU A CG    1 
ATOM   6808  C CD    . GLU A 1 912  ? -30.514 88.186  80.011  1.00 21.54 ?  910  GLU A CD    1 
ATOM   6809  O OE1   . GLU A 1 912  ? -29.771 88.814  79.223  1.00 22.59 ?  910  GLU A OE1   1 
ATOM   6810  O OE2   . GLU A 1 912  ? -31.730 87.999  79.786  1.00 23.79 ?  910  GLU A OE2   1 
ATOM   6811  N N     . GLN A 1 913  ? -30.410 90.090  83.810  1.00 17.06 ?  911  GLN A N     1 
ATOM   6812  C CA    . GLN A 1 913  ? -31.075 90.093  85.108  1.00 17.80 ?  911  GLN A CA    1 
ATOM   6813  C C     . GLN A 1 913  ? -32.543 89.745  84.951  1.00 19.26 ?  911  GLN A C     1 
ATOM   6814  O O     . GLN A 1 913  ? -33.172 90.131  83.966  1.00 21.33 ?  911  GLN A O     1 
ATOM   6815  C CB    . GLN A 1 913  ? -30.981 91.462  85.794  1.00 19.53 ?  911  GLN A CB    1 
ATOM   6816  C CG    . GLN A 1 913  ? -29.583 91.896  86.112  1.00 21.54 ?  911  GLN A CG    1 
ATOM   6817  C CD    . GLN A 1 913  ? -29.546 93.116  87.009  1.00 23.13 ?  911  GLN A CD    1 
ATOM   6818  O OE1   . GLN A 1 913  ? -29.954 94.204  86.608  1.00 23.17 ?  911  GLN A OE1   1 
ATOM   6819  N NE2   . GLN A 1 913  ? -29.059 92.941  88.232  1.00 20.46 ?  911  GLN A NE2   1 
ATOM   6820  N N     . ILE A 1 914  ? -33.097 89.045  85.935  1.00 21.90 ?  912  ILE A N     1 
ATOM   6821  C CA    . ILE A 1 914  ? -34.539 88.829  85.935  1.00 21.11 ?  912  ILE A CA    1 
ATOM   6822  C C     . ILE A 1 914  ? -35.216 90.054  86.536  1.00 24.75 ?  912  ILE A C     1 
ATOM   6823  O O     . ILE A 1 914  ? -34.635 90.781  87.350  1.00 24.54 ?  912  ILE A O     1 
ATOM   6824  C CB    . ILE A 1 914  ? -34.906 87.530  86.682  1.00 25.44 ?  912  ILE A CB    1 
ATOM   6825  C CG1   . ILE A 1 914  ? -34.608 87.643  88.171  1.00 26.73 ?  912  ILE A CG1   1 
ATOM   6826  C CG2   . ILE A 1 914  ? -34.137 86.370  86.122  1.00 26.10 ?  912  ILE A CG2   1 
ATOM   6827  C CD1   . ILE A 1 914  ? -35.857 87.797  89.007  1.00 33.31 ?  912  ILE A CD1   1 
ATOM   6828  N N     . GLY A 1 915  ? -36.438 90.326  86.095  1.00 25.68 ?  913  GLY A N     1 
ATOM   6829  C CA    . GLY A 1 915  ? -37.190 91.427  86.670  1.00 26.47 ?  913  GLY A CA    1 
ATOM   6830  C C     . GLY A 1 915  ? -37.797 91.005  87.996  1.00 28.13 ?  913  GLY A C     1 
ATOM   6831  O O     . GLY A 1 915  ? -38.264 89.878  88.158  1.00 33.79 ?  913  GLY A O     1 
ATOM   6832  N N     . LEU A 1 916  ? -37.764 91.920  88.959  1.00 25.94 ?  914  LEU A N     1 
ATOM   6833  C CA    . LEU A 1 916  ? -38.304 91.676  90.289  1.00 27.06 ?  914  LEU A CA    1 
ATOM   6834  C C     . LEU A 1 916  ? -39.734 92.188  90.381  1.00 29.56 ?  914  LEU A C     1 
ATOM   6835  O O     . LEU A 1 916  ? -40.067 93.231  89.811  1.00 30.13 ?  914  LEU A O     1 
ATOM   6836  C CB    . LEU A 1 916  ? -37.447 92.348  91.361  1.00 29.57 ?  914  LEU A CB    1 
ATOM   6837  C CG    . LEU A 1 916  ? -36.048 91.758  91.523  1.00 29.22 ?  914  LEU A CG    1 
ATOM   6838  C CD1   . LEU A 1 916  ? -35.387 92.278  92.786  1.00 28.87 ?  914  LEU A CD1   1 
ATOM   6839  C CD2   . LEU A 1 916  ? -36.113 90.250  91.536  1.00 31.12 ?  914  LEU A CD2   1 
ATOM   6840  N N     . ALA A 1 917  ? -40.573 91.450  91.101  1.00 27.88 ?  915  ALA A N     1 
ATOM   6841  C CA    . ALA A 1 917  ? -41.938 91.899  91.333  1.00 29.74 ?  915  ALA A CA    1 
ATOM   6842  C C     . ALA A 1 917  ? -41.956 93.068  92.313  1.00 31.41 ?  915  ALA A C     1 
ATOM   6843  O O     . ALA A 1 917  ? -41.029 93.270  93.104  1.00 28.42 ?  915  ALA A O     1 
ATOM   6844  C CB    . ALA A 1 917  ? -42.800 90.755  91.864  1.00 31.37 ?  915  ALA A CB    1 
ATOM   6845  N N     . SER A 1 918  ? -43.043 93.844  92.255  1.00 31.47 ?  916  SER A N     1 
ATOM   6846  C CA    . SER A 1 918  ? -43.165 95.021  93.112  1.00 31.12 ?  916  SER A CA    1 
ATOM   6847  C C     . SER A 1 918  ? -43.163 94.653  94.593  1.00 29.94 ?  916  SER A C     1 
ATOM   6848  O O     . SER A 1 918  ? -42.743 95.460  95.428  1.00 28.18 ?  916  SER A O     1 
ATOM   6849  C CB    . SER A 1 918  ? -44.437 95.792  92.756  1.00 33.98 ?  916  SER A CB    1 
ATOM   6850  O OG    . SER A 1 918  ? -45.546 94.912  92.727  1.00 42.02 ?  916  SER A OG    1 
ATOM   6851  N N     . GLU A 1 919  ? -43.617 93.442  94.932  1.00 33.18 ?  917  GLU A N     1 
ATOM   6852  C CA    . GLU A 1 919  ? -43.646 92.996  96.322  1.00 30.64 ?  917  GLU A CA    1 
ATOM   6853  C C     . GLU A 1 919  ? -42.262 92.946  96.957  1.00 28.71 ?  917  GLU A C     1 
ATOM   6854  O O     . GLU A 1 919  ? -42.160 92.991  98.188  1.00 30.00 ?  917  GLU A O     1 
ATOM   6855  C CB    . GLU A 1 919  ? -44.290 91.610  96.414  1.00 31.85 ?  917  GLU A CB    1 
ATOM   6856  C CG    . GLU A 1 919  ? -45.806 91.586  96.228  1.00 37.90 ?  917  GLU A CG    1 
ATOM   6857  C CD    . GLU A 1 919  ? -46.233 91.620  94.771  1.00 41.80 ?  917  GLU A CD    1 
ATOM   6858  O OE1   . GLU A 1 919  ? -45.359 91.550  93.879  1.00 41.34 ?  917  GLU A OE1   1 
ATOM   6859  O OE2   . GLU A 1 919  ? -47.451 91.712  94.521  1.00 45.34 ?  917  GLU A OE2   1 
ATOM   6860  N N     . THR A 1 920  ? -41.196 92.860  96.160  1.00 28.43 ?  918  THR A N     1 
ATOM   6861  C CA    . THR A 1 920  ? -39.860 92.804  96.744  1.00 25.29 ?  918  THR A CA    1 
ATOM   6862  C C     . THR A 1 920  ? -39.443 94.130  97.378  1.00 23.66 ?  918  THR A C     1 
ATOM   6863  O O     . THR A 1 920  ? -38.491 94.149  98.163  1.00 23.80 ?  918  THR A O     1 
ATOM   6864  C CB    . THR A 1 920  ? -38.836 92.364  95.685  1.00 24.12 ?  918  THR A CB    1 
ATOM   6865  O OG1   . THR A 1 920  ? -38.852 93.268  94.573  1.00 25.83 ?  918  THR A OG1   1 
ATOM   6866  C CG2   . THR A 1 920  ? -39.154 90.961  95.194  1.00 24.63 ?  918  THR A CG2   1 
ATOM   6867  N N     . GLY A 1 921  ? -40.162 95.224  97.105  1.00 27.63 ?  919  GLY A N     1 
ATOM   6868  C CA    . GLY A 1 921  ? -39.723 96.530  97.575  1.00 29.55 ?  919  GLY A CA    1 
ATOM   6869  C C     . GLY A 1 921  ? -39.655 96.672  99.086  1.00 26.11 ?  919  GLY A C     1 
ATOM   6870  O O     . GLY A 1 921  ? -38.877 97.483  99.598  1.00 28.59 ?  919  GLY A O     1 
ATOM   6871  N N     . VAL A 1 922  ? -40.463 95.897  99.822  1.00 25.11 ?  920  VAL A N     1 
ATOM   6872  C CA    . VAL A 1 922  ? -40.471 95.992  101.284 1.00 26.03 ?  920  VAL A CA    1 
ATOM   6873  C C     . VAL A 1 922  ? -39.324 95.237  101.939 1.00 23.48 ?  920  VAL A C     1 
ATOM   6874  O O     . VAL A 1 922  ? -39.154 95.335  103.163 1.00 24.99 ?  920  VAL A O     1 
ATOM   6875  C CB    . VAL A 1 922  ? -41.792 95.479  101.887 1.00 24.52 ?  920  VAL A CB    1 
ATOM   6876  C CG1   . VAL A 1 922  ? -42.925 96.452  101.585 1.00 27.93 ?  920  VAL A CG1   1 
ATOM   6877  C CG2   . VAL A 1 922  ? -42.121 94.099  101.353 1.00 26.67 ?  920  VAL A CG2   1 
ATOM   6878  N N     . GLY A 1 923  ? -38.533 94.490  101.166 1.00 25.11 ?  921  GLY A N     1 
ATOM   6879  C CA    . GLY A 1 923  ? -37.355 93.813  101.682 1.00 25.13 ?  921  GLY A CA    1 
ATOM   6880  C C     . GLY A 1 923  ? -36.104 94.187  100.910 1.00 22.92 ?  921  GLY A C     1 
ATOM   6881  O O     . GLY A 1 923  ? -36.104 95.184  100.184 1.00 21.79 ?  921  GLY A O     1 
ATOM   6882  N N     . THR A 1 924  ? -35.029 93.407  101.052 1.00 20.80 ?  922  THR A N     1 
ATOM   6883  C CA    . THR A 1 924  ? -33.748 93.707  100.408 1.00 19.85 ?  922  THR A CA    1 
ATOM   6884  C C     . THR A 1 924  ? -33.415 92.585  99.422  1.00 19.58 ?  922  THR A C     1 
ATOM   6885  O O     . THR A 1 924  ? -32.841 91.559  99.801  1.00 18.86 ?  922  THR A O     1 
ATOM   6886  C CB    . THR A 1 924  ? -32.640 93.897  101.453 1.00 19.50 ?  922  THR A CB    1 
ATOM   6887  O OG1   . THR A 1 924  ? -32.617 92.786  102.355 1.00 19.61 ?  922  THR A OG1   1 
ATOM   6888  C CG2   . THR A 1 924  ? -32.893 95.157  102.256 1.00 22.70 ?  922  THR A CG2   1 
ATOM   6889  N N     . PHE A 1 925  ? -33.754 92.788  98.150  1.00 18.73 ?  923  PHE A N     1 
ATOM   6890  C CA    . PHE A 1 925  ? -33.573 91.773  97.123  1.00 17.98 ?  923  PHE A CA    1 
ATOM   6891  C C     . PHE A 1 925  ? -32.604 92.242  96.045  1.00 17.40 ?  923  PHE A C     1 
ATOM   6892  O O     . PHE A 1 925  ? -32.589 93.422  95.671  1.00 20.51 ?  923  PHE A O     1 
ATOM   6893  C CB    . PHE A 1 925  ? -34.912 91.415  96.458  1.00 18.27 ?  923  PHE A CB    1 
ATOM   6894  C CG    . PHE A 1 925  ? -35.877 90.693  97.359  1.00 16.83 ?  923  PHE A CG    1 
ATOM   6895  C CD1   . PHE A 1 925  ? -36.708 91.403  98.214  1.00 17.93 ?  923  PHE A CD1   1 
ATOM   6896  C CD2   . PHE A 1 925  ? -35.973 89.312  97.327  1.00 17.18 ?  923  PHE A CD2   1 
ATOM   6897  C CE1   . PHE A 1 925  ? -37.617 90.743  99.030  1.00 18.88 ?  923  PHE A CE1   1 
ATOM   6898  C CE2   . PHE A 1 925  ? -36.874 88.648  98.140  1.00 15.83 ?  923  PHE A CE2   1 
ATOM   6899  C CZ    . PHE A 1 925  ? -37.699 89.373  98.994  1.00 16.81 ?  923  PHE A CZ    1 
ATOM   6900  N N     . VAL A 1 926  ? -31.798 91.305  95.553  1.00 17.53 ?  924  VAL A N     1 
ATOM   6901  C CA    . VAL A 1 926  ? -30.985 91.483  94.357  1.00 17.56 ?  924  VAL A CA    1 
ATOM   6902  C C     . VAL A 1 926  ? -31.444 90.440  93.348  1.00 17.59 ?  924  VAL A C     1 
ATOM   6903  O O     . VAL A 1 926  ? -31.504 89.259  93.688  1.00 17.35 ?  924  VAL A O     1 
ATOM   6904  C CB    . VAL A 1 926  ? -29.479 91.324  94.641  1.00 17.33 ?  924  VAL A CB    1 
ATOM   6905  C CG1   . VAL A 1 926  ? -28.675 91.408  93.363  1.00 19.75 ?  924  VAL A CG1   1 
ATOM   6906  C CG2   . VAL A 1 926  ? -29.001 92.394  95.636  1.00 19.36 ?  924  VAL A CG2   1 
ATOM   6907  N N     . PRO A 1 927  ? -31.792 90.812  92.118  1.00 17.90 ?  925  PRO A N     1 
ATOM   6908  C CA    . PRO A 1 927  ? -32.196 89.799  91.135  1.00 18.21 ?  925  PRO A CA    1 
ATOM   6909  C C     . PRO A 1 927  ? -31.012 88.936  90.752  1.00 17.35 ?  925  PRO A C     1 
ATOM   6910  O O     . PRO A 1 927  ? -29.887 89.444  90.635  1.00 16.94 ?  925  PRO A O     1 
ATOM   6911  C CB    . PRO A 1 927  ? -32.683 90.627  89.937  1.00 21.87 ?  925  PRO A CB    1 
ATOM   6912  C CG    . PRO A 1 927  ? -31.997 91.939  90.068  1.00 23.55 ?  925  PRO A CG    1 
ATOM   6913  C CD    . PRO A 1 927  ? -31.741 92.167  91.539  1.00 22.63 ?  925  PRO A CD    1 
ATOM   6914  N N     . PRO A 1 928  ? -31.217 87.634  90.576  1.00 16.78 ?  926  PRO A N     1 
ATOM   6915  C CA    . PRO A 1 928  ? -30.186 86.801  89.943  1.00 15.96 ?  926  PRO A CA    1 
ATOM   6916  C C     . PRO A 1 928  ? -29.683 87.444  88.657  1.00 15.57 ?  926  PRO A C     1 
ATOM   6917  O O     . PRO A 1 928  ? -30.464 87.948  87.845  1.00 15.09 ?  926  PRO A O     1 
ATOM   6918  C CB    . PRO A 1 928  ? -30.915 85.483  89.683  1.00 15.43 ?  926  PRO A CB    1 
ATOM   6919  C CG    . PRO A 1 928  ? -31.917 85.408  90.814  1.00 17.92 ?  926  PRO A CG    1 
ATOM   6920  C CD    . PRO A 1 928  ? -32.347 86.833  91.087  1.00 15.89 ?  926  PRO A CD    1 
ATOM   6921  N N     . THR A 1 929  ? -28.358 87.421  88.485  1.00 14.70 ?  927  THR A N     1 
ATOM   6922  C CA    . THR A 1 929  ? -27.656 88.199  87.477  1.00 14.05 ?  927  THR A CA    1 
ATOM   6923  C C     . THR A 1 929  ? -26.555 87.359  86.842  1.00 15.71 ?  927  THR A C     1 
ATOM   6924  O O     . THR A 1 929  ? -25.859 86.619  87.540  1.00 16.31 ?  927  THR A O     1 
ATOM   6925  C CB    . THR A 1 929  ? -27.048 89.462  88.119  1.00 16.61 ?  927  THR A CB    1 
ATOM   6926  O OG1   . THR A 1 929  ? -28.098 90.242  88.700  1.00 17.28 ?  927  THR A OG1   1 
ATOM   6927  C CG2   . THR A 1 929  ? -26.288 90.310  87.103  1.00 16.73 ?  927  THR A CG2   1 
ATOM   6928  N N     . ILE A 1 930  ? -26.402 87.481  85.522  1.00 14.65 ?  928  ILE A N     1 
ATOM   6929  C CA    . ILE A 1 930  ? -25.305 86.865  84.782  1.00 13.15 ?  928  ILE A CA    1 
ATOM   6930  C C     . ILE A 1 930  ? -24.500 87.979  84.133  1.00 15.60 ?  928  ILE A C     1 
ATOM   6931  O O     . ILE A 1 930  ? -25.062 88.819  83.424  1.00 17.13 ?  928  ILE A O     1 
ATOM   6932  C CB    . ILE A 1 930  ? -25.818 85.879  83.717  1.00 14.15 ?  928  ILE A CB    1 
ATOM   6933  C CG1   . ILE A 1 930  ? -26.581 84.728  84.366  1.00 15.11 ?  928  ILE A CG1   1 
ATOM   6934  C CG2   . ILE A 1 930  ? -24.635 85.333  82.891  1.00 13.95 ?  928  ILE A CG2   1 
ATOM   6935  C CD1   . ILE A 1 930  ? -27.379 83.866  83.336  1.00 17.94 ?  928  ILE A CD1   1 
ATOM   6936  N N     . ILE A 1 931  ? -23.189 87.981  84.354  1.00 14.00 ?  929  ILE A N     1 
ATOM   6937  C CA    . ILE A 1 931  ? -22.295 88.995  83.807  1.00 13.28 ?  929  ILE A CA    1 
ATOM   6938  C C     . ILE A 1 931  ? -21.232 88.296  82.978  1.00 16.59 ?  929  ILE A C     1 
ATOM   6939  O O     . ILE A 1 931  ? -20.526 87.420  83.484  1.00 15.77 ?  929  ILE A O     1 
ATOM   6940  C CB    . ILE A 1 931  ? -21.645 89.833  84.919  1.00 15.39 ?  929  ILE A CB    1 
ATOM   6941  C CG1   . ILE A 1 931  ? -22.723 90.476  85.793  1.00 17.47 ?  929  ILE A CG1   1 
ATOM   6942  C CG2   . ILE A 1 931  ? -20.708 90.879  84.308  1.00 18.44 ?  929  ILE A CG2   1 
ATOM   6943  C CD1   . ILE A 1 931  ? -22.150 91.297  86.945  1.00 20.41 ?  929  ILE A CD1   1 
ATOM   6944  N N     . GLU A 1 932  ? -21.099 88.694  81.715  1.00 15.98 ?  930  GLU A N     1 
ATOM   6945  C CA    . GLU A 1 932  ? -20.126 88.074  80.822  1.00 15.96 ?  930  GLU A CA    1 
ATOM   6946  C C     . GLU A 1 932  ? -18.816 88.849  80.874  1.00 15.19 ?  930  GLU A C     1 
ATOM   6947  O O     . GLU A 1 932  ? -18.790 90.056  80.612  1.00 17.21 ?  930  GLU A O     1 
ATOM   6948  C CB    . GLU A 1 932  ? -20.682 88.013  79.402  1.00 17.14 ?  930  GLU A CB    1 
ATOM   6949  C CG    . GLU A 1 932  ? -21.790 86.996  79.280  1.00 16.24 ?  930  GLU A CG    1 
ATOM   6950  C CD    . GLU A 1 932  ? -22.540 87.100  77.983  1.00 21.36 ?  930  GLU A CD    1 
ATOM   6951  O OE1   . GLU A 1 932  ? -21.882 87.043  76.922  1.00 21.46 ?  930  GLU A OE1   1 
ATOM   6952  O OE2   . GLU A 1 932  ? -23.782 87.249  78.027  1.00 20.32 ?  930  GLU A OE2   1 
ATOM   6953  N N     . LEU A 1 933  ? -17.738 88.166  81.240  1.00 15.94 ?  931  LEU A N     1 
ATOM   6954  C CA    . LEU A 1 933  ? -16.426 88.786  81.348  1.00 16.03 ?  931  LEU A CA    1 
ATOM   6955  C C     . LEU A 1 933  ? -15.510 88.299  80.235  1.00 18.87 ?  931  LEU A C     1 
ATOM   6956  O O     . LEU A 1 933  ? -15.682 87.204  79.692  1.00 21.22 ?  931  LEU A O     1 
ATOM   6957  C CB    . LEU A 1 933  ? -15.775 88.480  82.704  1.00 19.23 ?  931  LEU A CB    1 
ATOM   6958  C CG    . LEU A 1 933  ? -16.537 88.949  83.948  1.00 21.41 ?  931  LEU A CG    1 
ATOM   6959  C CD1   . LEU A 1 933  ? -15.809 88.506  85.196  1.00 22.75 ?  931  LEU A CD1   1 
ATOM   6960  C CD2   . LEU A 1 933  ? -16.711 90.455  83.929  1.00 22.97 ?  931  LEU A CD2   1 
ATOM   6961  N N     . GLU A 1 934  ? -14.505 89.123  79.921  1.00 21.26 ?  932  GLU A N     1 
ATOM   6962  C CA    . GLU A 1 934  ? -13.504 88.725  78.933  1.00 25.22 ?  932  GLU A CA    1 
ATOM   6963  C C     . GLU A 1 934  ? -12.514 87.713  79.500  1.00 28.34 ?  932  GLU A C     1 
ATOM   6964  O O     . GLU A 1 934  ? -12.195 86.719  78.840  1.00 28.99 ?  932  GLU A O     1 
ATOM   6965  C CB    . GLU A 1 934  ? -12.764 89.956  78.409  1.00 30.80 ?  932  GLU A CB    1 
ATOM   6966  C CG    . GLU A 1 934  ? -13.665 90.977  77.727  1.00 38.23 ?  932  GLU A CG    1 
ATOM   6967  C CD    . GLU A 1 934  ? -14.313 90.434  76.464  1.00 46.38 ?  932  GLU A CD    1 
ATOM   6968  O OE1   . GLU A 1 934  ? -13.571 90.011  75.550  1.00 51.93 ?  932  GLU A OE1   1 
ATOM   6969  O OE2   . GLU A 1 934  ? -15.563 90.421  76.390  1.00 47.24 ?  932  GLU A OE2   1 
ATOM   6970  N N     . LYS A 1 935  ? -12.015 87.942  80.714  1.00 24.94 ?  933  LYS A N     1 
ATOM   6971  C CA    . LYS A 1 935  ? -11.070 87.016  81.324  1.00 26.59 ?  933  LYS A CA    1 
ATOM   6972  C C     . LYS A 1 935  ? -11.291 86.989  82.827  1.00 26.69 ?  933  LYS A C     1 
ATOM   6973  O O     . LYS A 1 935  ? -11.926 87.878  83.395  1.00 23.41 ?  933  LYS A O     1 
ATOM   6974  C CB    . LYS A 1 935  ? -9.617  87.386  80.997  1.00 31.95 ?  933  LYS A CB    1 
ATOM   6975  C CG    . LYS A 1 935  ? -9.304  88.861  81.138  1.00 36.30 ?  933  LYS A CG    1 
ATOM   6976  C CD    . LYS A 1 935  ? -8.022  89.233  80.398  1.00 39.15 ?  933  LYS A CD    1 
ATOM   6977  C CE    . LYS A 1 935  ? -7.833  90.739  80.386  1.00 41.63 ?  933  LYS A CE    1 
ATOM   6978  N NZ    . LYS A 1 935  ? -8.070  91.305  81.747  1.00 45.90 ?  933  LYS A NZ    1 
ATOM   6979  N N     . LEU A 1 936  ? -10.753 85.945  83.467  1.00 27.65 ?  934  LEU A N     1 
ATOM   6980  C CA    . LEU A 1 936  ? -10.974 85.757  84.900  1.00 28.16 ?  934  LEU A CA    1 
ATOM   6981  C C     . LEU A 1 936  ? -10.428 86.917  85.719  1.00 27.48 ?  934  LEU A C     1 
ATOM   6982  O O     . LEU A 1 936  ? -11.007 87.265  86.756  1.00 30.00 ?  934  LEU A O     1 
ATOM   6983  C CB    . LEU A 1 936  ? -10.341 84.447  85.375  1.00 30.72 ?  934  LEU A CB    1 
ATOM   6984  C CG    . LEU A 1 936  ? -11.238 83.547  86.232  1.00 33.02 ?  934  LEU A CG    1 
ATOM   6985  C CD1   . LEU A 1 936  ? -10.497 82.286  86.642  1.00 36.31 ?  934  LEU A CD1   1 
ATOM   6986  C CD2   . LEU A 1 936  ? -11.776 84.268  87.455  1.00 31.23 ?  934  LEU A CD2   1 
ATOM   6987  N N     . SER A 1 937  ? -9.325  87.525  85.282  1.00 30.83 ?  935  SER A N     1 
ATOM   6988  C CA    . SER A 1 937  ? -8.753  88.646  86.020  1.00 32.25 ?  935  SER A CA    1 
ATOM   6989  C C     . SER A 1 937  ? -9.651  89.879  86.015  1.00 32.44 ?  935  SER A C     1 
ATOM   6990  O O     . SER A 1 937  ? -9.364  90.832  86.749  1.00 32.72 ?  935  SER A O     1 
ATOM   6991  C CB    . SER A 1 937  ? -7.368  88.999  85.461  1.00 33.55 ?  935  SER A CB    1 
ATOM   6992  O OG    . SER A 1 937  ? -7.420  89.315  84.082  1.00 36.56 ?  935  SER A OG    1 
ATOM   6993  N N     . ASP A 1 938  ? -10.728 89.888  85.223  1.00 31.65 ?  936  ASP A N     1 
ATOM   6994  C CA    . ASP A 1 938  ? -11.676 90.994  85.290  1.00 26.76 ?  936  ASP A CA    1 
ATOM   6995  C C     . ASP A 1 938  ? -12.462 91.015  86.599  1.00 28.15 ?  936  ASP A C     1 
ATOM   6996  O O     . ASP A 1 938  ? -13.074 92.035  86.926  1.00 29.88 ?  936  ASP A O     1 
ATOM   6997  C CB    . ASP A 1 938  ? -12.665 90.938  84.119  1.00 27.61 ?  936  ASP A CB    1 
ATOM   6998  C CG    . ASP A 1 938  ? -12.010 91.203  82.774  1.00 35.10 ?  936  ASP A CG    1 
ATOM   6999  O OD1   . ASP A 1 938  ? -10.927 91.828  82.734  1.00 35.63 ?  936  ASP A OD1   1 
ATOM   7000  O OD2   . ASP A 1 938  ? -12.598 90.796  81.748  1.00 34.18 ?  936  ASP A OD2   1 
ATOM   7001  N N     . LEU A 1 939  ? -12.480 89.920  87.345  1.00 26.69 ?  937  LEU A N     1 
ATOM   7002  C CA    . LEU A 1 939  ? -13.227 89.844  88.592  1.00 32.61 ?  937  LEU A CA    1 
ATOM   7003  C C     . LEU A 1 939  ? -12.247 89.951  89.752  1.00 40.05 ?  937  LEU A C     1 
ATOM   7004  O O     . LEU A 1 939  ? -11.394 89.073  89.930  1.00 39.47 ?  937  LEU A O     1 
ATOM   7005  C CB    . LEU A 1 939  ? -14.022 88.544  88.667  1.00 32.45 ?  937  LEU A CB    1 
ATOM   7006  C CG    . LEU A 1 939  ? -14.761 88.273  89.976  1.00 32.28 ?  937  LEU A CG    1 
ATOM   7007  C CD1   . LEU A 1 939  ? -15.763 89.383  90.271  1.00 28.92 ?  937  LEU A CD1   1 
ATOM   7008  C CD2   . LEU A 1 939  ? -15.450 86.933  89.902  1.00 27.07 ?  937  LEU A CD2   1 
ATOM   7009  N N     . GLN A 1 940  ? -12.365 91.022  90.536  1.00 40.10 ?  938  GLN A N     1 
ATOM   7010  C CA    . GLN A 1 940  ? -11.318 91.377  91.486  1.00 46.96 ?  938  GLN A CA    1 
ATOM   7011  C C     . GLN A 1 940  ? -11.701 91.235  92.953  1.00 48.35 ?  938  GLN A C     1 
ATOM   7012  O O     . GLN A 1 940  ? -10.810 91.049  93.783  1.00 50.82 ?  938  GLN A O     1 
ATOM   7013  C CB    . GLN A 1 940  ? -10.838 92.811  91.226  1.00 52.56 ?  938  GLN A CB    1 
ATOM   7014  C CG    . GLN A 1 940  ? -9.618  92.862  90.312  1.00 57.61 ?  938  GLN A CG    1 
ATOM   7015  C CD    . GLN A 1 940  ? -9.506  94.156  89.525  1.00 64.00 ?  938  GLN A CD    1 
ATOM   7016  O OE1   . GLN A 1 940  ? -10.442 94.958  89.479  1.00 62.99 ?  938  GLN A OE1   1 
ATOM   7017  N NE2   . GLN A 1 940  ? -8.355  94.362  88.892  1.00 67.51 ?  938  GLN A NE2   1 
ATOM   7018  N N     . ARG A 1 941  ? -12.983 91.317  93.306  1.00 45.46 ?  939  ARG A N     1 
ATOM   7019  C CA    . ARG A 1 941  ? -13.412 91.115  94.684  1.00 42.18 ?  939  ARG A CA    1 
ATOM   7020  C C     . ARG A 1 941  ? -14.492 90.043  94.729  1.00 34.23 ?  939  ARG A C     1 
ATOM   7021  O O     . ARG A 1 941  ? -15.138 89.741  93.722  1.00 38.05 ?  939  ARG A O     1 
ATOM   7022  C CB    . ARG A 1 941  ? -13.933 92.414  95.326  1.00 44.92 ?  939  ARG A CB    1 
ATOM   7023  C CG    . ARG A 1 941  ? -12.855 93.459  95.607  1.00 49.32 ?  939  ARG A CG    1 
ATOM   7024  C CD    . ARG A 1 941  ? -13.233 94.413  96.752  1.00 54.63 ?  939  ARG A CD    1 
ATOM   7025  N NE    . ARG A 1 941  ? -13.163 93.773  98.064  1.00 55.00 ?  939  ARG A NE    1 
ATOM   7026  C CZ    . ARG A 1 941  ? -14.175 93.686  98.918  1.00 54.13 ?  939  ARG A CZ    1 
ATOM   7027  N NH1   . ARG A 1 941  ? -15.355 94.222  98.651  1.00 51.96 ?  939  ARG A NH1   1 
ATOM   7028  N NH2   . ARG A 1 941  ? -13.996 93.053  100.075 1.00 49.92 ?  939  ARG A NH2   1 
ATOM   7029  N N     . GLU A 1 942  ? -14.663 89.446  95.908  1.00 36.25 ?  940  GLU A N     1 
ATOM   7030  C CA    . GLU A 1 942  ? -15.750 88.497  96.117  1.00 34.10 ?  940  GLU A CA    1 
ATOM   7031  C C     . GLU A 1 942  ? -17.060 89.266  96.236  1.00 31.61 ?  940  GLU A C     1 
ATOM   7032  O O     . GLU A 1 942  ? -17.161 90.223  97.009  1.00 32.89 ?  940  GLU A O     1 
ATOM   7033  C CB    . GLU A 1 942  ? -15.499 87.653  97.373  1.00 36.94 ?  940  GLU A CB    1 
ATOM   7034  C CG    . GLU A 1 942  ? -16.397 86.413  97.526  1.00 33.68 ?  940  GLU A CG    1 
ATOM   7035  C CD    . GLU A 1 942  ? -16.350 85.800  98.936  1.00 35.91 ?  940  GLU A CD    1 
ATOM   7036  O OE1   . GLU A 1 942  ? -16.132 86.554  99.911  1.00 33.93 ?  940  GLU A OE1   1 
ATOM   7037  O OE2   . GLU A 1 942  ? -16.535 84.564  99.076  1.00 28.88 ?  940  GLU A OE2   1 
ATOM   7038  N N     . VAL A 1 943  ? -18.052 88.871  95.442  1.00 25.79 ?  941  VAL A N     1 
ATOM   7039  C CA    . VAL A 1 943  ? -19.360 89.516  95.413  1.00 23.80 ?  941  VAL A CA    1 
ATOM   7040  C C     . VAL A 1 943  ? -20.350 88.523  95.993  1.00 20.94 ?  941  VAL A C     1 
ATOM   7041  O O     . VAL A 1 943  ? -20.708 87.537  95.337  1.00 20.25 ?  941  VAL A O     1 
ATOM   7042  C CB    . VAL A 1 943  ? -19.759 89.939  93.992  1.00 24.95 ?  941  VAL A CB    1 
ATOM   7043  C CG1   . VAL A 1 943  ? -21.115 90.640  94.002  1.00 27.03 ?  941  VAL A CG1   1 
ATOM   7044  C CG2   . VAL A 1 943  ? -18.692 90.840  93.392  1.00 27.81 ?  941  VAL A CG2   1 
ATOM   7045  N N     . PHE A 1 944  ? -20.792 88.775  97.225  1.00 21.47 ?  942  PHE A N     1 
ATOM   7046  C CA    . PHE A 1 944  ? -21.504 87.763  98.010  1.00 20.26 ?  942  PHE A CA    1 
ATOM   7047  C C     . PHE A 1 944  ? -23.007 87.877  97.766  1.00 20.09 ?  942  PHE A C     1 
ATOM   7048  O O     . PHE A 1 944  ? -23.796 88.219  98.647  1.00 21.28 ?  942  PHE A O     1 
ATOM   7049  C CB    . PHE A 1 944  ? -21.167 87.913  99.488  1.00 19.50 ?  942  PHE A CB    1 
ATOM   7050  C CG    . PHE A 1 944  ? -21.226 86.623  100.254 1.00 21.53 ?  942  PHE A CG    1 
ATOM   7051  C CD1   . PHE A 1 944  ? -20.275 85.639  100.045 1.00 19.55 ?  942  PHE A CD1   1 
ATOM   7052  C CD2   . PHE A 1 944  ? -22.218 86.405  101.199 1.00 23.71 ?  942  PHE A CD2   1 
ATOM   7053  C CE1   . PHE A 1 944  ? -20.323 84.456  100.747 1.00 21.59 ?  942  PHE A CE1   1 
ATOM   7054  C CE2   . PHE A 1 944  ? -22.265 85.221  101.916 1.00 20.30 ?  942  PHE A CE2   1 
ATOM   7055  C CZ    . PHE A 1 944  ? -21.323 84.241  101.677 1.00 22.47 ?  942  PHE A CZ    1 
ATOM   7056  N N     . GLY A 1 945  ? -23.395 87.569  96.527  1.00 17.44 ?  943  GLY A N     1 
ATOM   7057  C CA    . GLY A 1 945  ? -24.767 87.702  96.107  1.00 16.54 ?  943  GLY A CA    1 
ATOM   7058  C C     . GLY A 1 945  ? -25.040 86.828  94.907  1.00 15.57 ?  943  GLY A C     1 
ATOM   7059  O O     . GLY A 1 945  ? -24.209 86.006  94.504  1.00 14.43 ?  943  GLY A O     1 
ATOM   7060  N N     . PRO A 1 946  ? -26.231 86.968  94.329  1.00 15.26 ?  944  PRO A N     1 
ATOM   7061  C CA    . PRO A 1 946  ? -26.659 86.085  93.224  1.00 16.52 ?  944  PRO A CA    1 
ATOM   7062  C C     . PRO A 1 946  ? -26.153 86.595  91.882  1.00 14.96 ?  944  PRO A C     1 
ATOM   7063  O O     . PRO A 1 946  ? -26.910 87.030  91.007  1.00 14.27 ?  944  PRO A O     1 
ATOM   7064  C CB    . PRO A 1 946  ? -28.186 86.129  93.342  1.00 14.15 ?  944  PRO A CB    1 
ATOM   7065  C CG    . PRO A 1 946  ? -28.471 87.516  93.850  1.00 15.06 ?  944  PRO A CG    1 
ATOM   7066  C CD    . PRO A 1 946  ? -27.304 87.879  94.772  1.00 14.14 ?  944  PRO A CD    1 
ATOM   7067  N N     . VAL A 1 947  ? -24.831 86.557  91.722  1.00 15.35 ?  945  VAL A N     1 
ATOM   7068  C CA    . VAL A 1 947  ? -24.168 87.183  90.591  1.00 14.26 ?  945  VAL A CA    1 
ATOM   7069  C C     . VAL A 1 947  ? -23.166 86.187  90.033  1.00 14.21 ?  945  VAL A C     1 
ATOM   7070  O O     . VAL A 1 947  ? -22.127 85.916  90.655  1.00 14.89 ?  945  VAL A O     1 
ATOM   7071  C CB    . VAL A 1 947  ? -23.488 88.508  90.971  1.00 17.58 ?  945  VAL A CB    1 
ATOM   7072  C CG1   . VAL A 1 947  ? -22.884 89.159  89.759  1.00 17.32 ?  945  VAL A CG1   1 
ATOM   7073  C CG2   . VAL A 1 947  ? -24.494 89.449  91.603  1.00 18.77 ?  945  VAL A CG2   1 
ATOM   7074  N N     . LEU A 1 948  ? -23.474 85.646  88.860  1.00 13.76 ?  946  LEU A N     1 
ATOM   7075  C CA    . LEU A 1 948  ? -22.631 84.671  88.190  1.00 11.85 ?  946  LEU A CA    1 
ATOM   7076  C C     . LEU A 1 948  ? -21.857 85.368  87.086  1.00 15.07 ?  946  LEU A C     1 
ATOM   7077  O O     . LEU A 1 948  ? -22.443 86.088  86.269  1.00 16.52 ?  946  LEU A O     1 
ATOM   7078  C CB    . LEU A 1 948  ? -23.476 83.561  87.580  1.00 12.37 ?  946  LEU A CB    1 
ATOM   7079  C CG    . LEU A 1 948  ? -22.696 82.583  86.702  1.00 12.61 ?  946  LEU A CG    1 
ATOM   7080  C CD1   . LEU A 1 948  ? -21.768 81.723  87.585  1.00 14.05 ?  946  LEU A CD1   1 
ATOM   7081  C CD2   . LEU A 1 948  ? -23.681 81.730  85.907  1.00 16.99 ?  946  LEU A CD2   1 
ATOM   7082  N N     . HIS A 1 949  ? -20.552 85.150  87.057  1.00 14.23 ?  947  HIS A N     1 
ATOM   7083  C CA    . HIS A 1 949  ? -19.709 85.674  85.995  1.00 14.09 ?  947  HIS A CA    1 
ATOM   7084  C C     . HIS A 1 949  ? -19.371 84.538  85.039  1.00 14.67 ?  947  HIS A C     1 
ATOM   7085  O O     . HIS A 1 949  ? -19.190 83.396  85.467  1.00 15.66 ?  947  HIS A O     1 
ATOM   7086  C CB    . HIS A 1 949  ? -18.444 86.299  86.570  1.00 15.72 ?  947  HIS A CB    1 
ATOM   7087  C CG    . HIS A 1 949  ? -18.720 87.348  87.597  1.00 15.90 ?  947  HIS A CG    1 
ATOM   7088  N ND1   . HIS A 1 949  ? -18.976 87.045  88.919  1.00 16.25 ?  947  HIS A ND1   1 
ATOM   7089  C CD2   . HIS A 1 949  ? -18.855 88.691  87.482  1.00 18.88 ?  947  HIS A CD2   1 
ATOM   7090  C CE1   . HIS A 1 949  ? -19.220 88.164  89.580  1.00 19.05 ?  947  HIS A CE1   1 
ATOM   7091  N NE2   . HIS A 1 949  ? -19.154 89.174  88.733  1.00 19.28 ?  947  HIS A NE2   1 
ATOM   7092  N N     . VAL A 1 950  ? -19.342 84.835  83.742  1.00 13.55 ?  948  VAL A N     1 
ATOM   7093  C CA    . VAL A 1 950  ? -19.128 83.806  82.728  1.00 12.99 ?  948  VAL A CA    1 
ATOM   7094  C C     . VAL A 1 950  ? -17.954 84.213  81.857  1.00 16.00 ?  948  VAL A C     1 
ATOM   7095  O O     . VAL A 1 950  ? -17.924 85.333  81.337  1.00 17.13 ?  948  VAL A O     1 
ATOM   7096  C CB    . VAL A 1 950  ? -20.377 83.583  81.856  1.00 14.70 ?  948  VAL A CB    1 
ATOM   7097  C CG1   . VAL A 1 950  ? -20.104 82.490  80.816  1.00 18.04 ?  948  VAL A CG1   1 
ATOM   7098  C CG2   . VAL A 1 950  ? -21.558 83.205  82.733  1.00 16.79 ?  948  VAL A CG2   1 
ATOM   7099  N N     . ILE A 1 951  ? -16.998 83.298  81.684  1.00 13.30 ?  949  ILE A N     1 
ATOM   7100  C CA    . ILE A 1 951  ? -15.892 83.489  80.757  1.00 15.94 ?  949  ILE A CA    1 
ATOM   7101  C C     . ILE A 1 951  ? -15.835 82.298  79.807  1.00 17.80 ?  949  ILE A C     1 
ATOM   7102  O O     . ILE A 1 951  ? -16.363 81.223  80.084  1.00 14.38 ?  949  ILE A O     1 
ATOM   7103  C CB    . ILE A 1 951  ? -14.536 83.677  81.469  1.00 16.17 ?  949  ILE A CB    1 
ATOM   7104  C CG1   . ILE A 1 951  ? -14.176 82.446  82.290  1.00 17.95 ?  949  ILE A CG1   1 
ATOM   7105  C CG2   . ILE A 1 951  ? -14.560 84.937  82.356  1.00 18.22 ?  949  ILE A CG2   1 
ATOM   7106  C CD1   . ILE A 1 951  ? -12.829 82.574  82.945  1.00 22.48 ?  949  ILE A CD1   1 
ATOM   7107  N N     . ARG A 1 952  ? -15.189 82.513  78.662  1.00 17.21 ?  950  ARG A N     1 
ATOM   7108  C CA    . ARG A 1 952  ? -15.025 81.490  77.638  1.00 15.30 ?  950  ARG A CA    1 
ATOM   7109  C C     . ARG A 1 952  ? -13.544 81.151  77.512  1.00 16.32 ?  950  ARG A C     1 
ATOM   7110  O O     . ARG A 1 952  ? -12.686 82.001  77.750  1.00 18.01 ?  950  ARG A O     1 
ATOM   7111  C CB    . ARG A 1 952  ? -15.554 81.996  76.296  1.00 17.91 ?  950  ARG A CB    1 
ATOM   7112  C CG    . ARG A 1 952  ? -16.951 82.582  76.377  1.00 21.82 ?  950  ARG A CG    1 
ATOM   7113  C CD    . ARG A 1 952  ? -17.191 83.563  75.248  1.00 24.72 ?  950  ARG A CD    1 
ATOM   7114  N NE    . ARG A 1 952  ? -17.490 82.883  73.995  1.00 24.30 ?  950  ARG A NE    1 
ATOM   7115  C CZ    . ARG A 1 952  ? -18.711 82.752  73.495  1.00 22.90 ?  950  ARG A CZ    1 
ATOM   7116  N NH1   . ARG A 1 952  ? -19.769 83.257  74.111  1.00 24.10 ?  950  ARG A NH1   1 
ATOM   7117  N NH2   . ARG A 1 952  ? -18.875 82.107  72.344  1.00 23.85 ?  950  ARG A NH2   1 
ATOM   7118  N N     . TYR A 1 953  ? -13.235 79.907  77.132  1.00 16.47 ?  951  TYR A N     1 
ATOM   7119  C CA    . TYR A 1 953  ? -11.838 79.519  76.956  1.00 15.88 ?  951  TYR A CA    1 
ATOM   7120  C C     . TYR A 1 953  ? -11.709 78.580  75.766  1.00 15.14 ?  951  TYR A C     1 
ATOM   7121  O O     . TYR A 1 953  ? -12.597 77.767  75.501  1.00 15.57 ?  951  TYR A O     1 
ATOM   7122  C CB    . TYR A 1 953  ? -11.253 78.848  78.222  1.00 14.99 ?  951  TYR A CB    1 
ATOM   7123  C CG    . TYR A 1 953  ? -11.774 77.454  78.489  1.00 13.36 ?  951  TYR A CG    1 
ATOM   7124  C CD1   . TYR A 1 953  ? -12.982 77.243  79.164  1.00 13.39 ?  951  TYR A CD1   1 
ATOM   7125  C CD2   . TYR A 1 953  ? -11.056 76.334  78.067  1.00 15.43 ?  951  TYR A CD2   1 
ATOM   7126  C CE1   . TYR A 1 953  ? -13.460 75.965  79.402  1.00 13.75 ?  951  TYR A CE1   1 
ATOM   7127  C CE2   . TYR A 1 953  ? -11.534 75.045  78.291  1.00 14.32 ?  951  TYR A CE2   1 
ATOM   7128  C CZ    . TYR A 1 953  ? -12.732 74.868  78.971  1.00 14.65 ?  951  TYR A CZ    1 
ATOM   7129  O OH    . TYR A 1 953  ? -13.199 73.603  79.186  1.00 16.25 ?  951  TYR A OH    1 
ATOM   7130  N N     . ARG A 1 954  ? -10.574 78.690  75.063  1.00 17.17 ?  952  ARG A N     1 
ATOM   7131  C CA    . ARG A 1 954  ? -10.224 77.725  74.024  1.00 18.51 ?  952  ARG A CA    1 
ATOM   7132  C C     . ARG A 1 954  ? -9.672  76.454  74.661  1.00 15.79 ?  952  ARG A C     1 
ATOM   7133  O O     . ARG A 1 954  ? -8.964  76.514  75.667  1.00 16.38 ?  952  ARG A O     1 
ATOM   7134  C CB    . ARG A 1 954  ? -9.190  78.322  73.071  1.00 22.55 ?  952  ARG A CB    1 
ATOM   7135  C CG    . ARG A 1 954  ? -9.597  79.654  72.449  1.00 30.10 ?  952  ARG A CG    1 
ATOM   7136  C CD    . ARG A 1 954  ? -10.894 79.510  71.669  1.00 32.50 ?  952  ARG A CD    1 
ATOM   7137  N NE    . ARG A 1 954  ? -10.772 78.512  70.616  1.00 35.65 ?  952  ARG A NE    1 
ATOM   7138  C CZ    . ARG A 1 954  ? -10.608 78.798  69.332  1.00 46.20 ?  952  ARG A CZ    1 
ATOM   7139  N NH1   . ARG A 1 954  ? -10.614 80.048  68.897  1.00 49.49 ?  952  ARG A NH1   1 
ATOM   7140  N NH2   . ARG A 1 954  ? -10.433 77.806  68.464  1.00 44.60 ?  952  ARG A NH2   1 
ATOM   7141  N N     . ARG A 1 955  ? -10.002 75.290  74.081  1.00 19.22 ?  953  ARG A N     1 
ATOM   7142  C CA    . ARG A 1 955  ? -9.683  74.032  74.760  1.00 19.98 ?  953  ARG A CA    1 
ATOM   7143  C C     . ARG A 1 955  ? -8.183  73.889  75.010  1.00 17.58 ?  953  ARG A C     1 
ATOM   7144  O O     . ARG A 1 955  ? -7.771  73.399  76.070  1.00 18.64 ?  953  ARG A O     1 
ATOM   7145  C CB    . ARG A 1 955  ? -10.216 72.827  73.980  1.00 23.18 ?  953  ARG A CB    1 
ATOM   7146  C CG    . ARG A 1 955  ? -9.916  71.460  74.653  1.00 28.89 ?  953  ARG A CG    1 
ATOM   7147  C CD    . ARG A 1 955  ? -10.168 71.477  76.180  1.00 30.72 ?  953  ARG A CD    1 
ATOM   7148  N NE    . ARG A 1 955  ? -9.828  70.228  76.857  1.00 31.40 ?  953  ARG A NE    1 
ATOM   7149  C CZ    . ARG A 1 955  ? -8.607  69.891  77.257  1.00 32.23 ?  953  ARG A CZ    1 
ATOM   7150  N NH1   . ARG A 1 955  ? -7.561  70.676  77.037  1.00 30.31 ?  953  ARG A NH1   1 
ATOM   7151  N NH2   . ARG A 1 955  ? -8.430  68.736  77.898  1.00 30.17 ?  953  ARG A NH2   1 
ATOM   7152  N N     . ASP A 1 956  ? -7.347  74.339  74.071  1.00 18.84 ?  954  ASP A N     1 
ATOM   7153  C CA    . ASP A 1 956  ? -5.909  74.232  74.297  1.00 18.35 ?  954  ASP A CA    1 
ATOM   7154  C C     . ASP A 1 956  ? -5.432  75.092  75.460  1.00 19.12 ?  954  ASP A C     1 
ATOM   7155  O O     . ASP A 1 956  ? -4.331  74.863  75.971  1.00 19.82 ?  954  ASP A O     1 
ATOM   7156  C CB    . ASP A 1 956  ? -5.131  74.619  73.039  1.00 20.55 ?  954  ASP A CB    1 
ATOM   7157  C CG    . ASP A 1 956  ? -5.271  73.602  71.924  1.00 24.94 ?  954  ASP A CG    1 
ATOM   7158  O OD1   . ASP A 1 956  ? -5.704  72.462  72.198  1.00 29.54 ?  954  ASP A OD1   1 
ATOM   7159  O OD2   . ASP A 1 956  ? -4.937  73.953  70.772  1.00 32.80 ?  954  ASP A OD2   1 
ATOM   7160  N N     . ASP A 1 957  ? -6.230  76.068  75.896  1.00 17.26 ?  955  ASP A N     1 
ATOM   7161  C CA    . ASP A 1 957  ? -5.856  76.946  76.995  1.00 17.62 ?  955  ASP A CA    1 
ATOM   7162  C C     . ASP A 1 957  ? -6.406  76.473  78.337  1.00 17.93 ?  955  ASP A C     1 
ATOM   7163  O O     . ASP A 1 957  ? -6.388  77.233  79.312  1.00 17.46 ?  955  ASP A O     1 
ATOM   7164  C CB    . ASP A 1 957  ? -6.320  78.375  76.717  1.00 19.64 ?  955  ASP A CB    1 
ATOM   7165  C CG    . ASP A 1 957  ? -5.589  79.002  75.556  1.00 28.32 ?  955  ASP A CG    1 
ATOM   7166  O OD1   . ASP A 1 957  ? -4.412  78.653  75.337  1.00 26.01 ?  955  ASP A OD1   1 
ATOM   7167  O OD2   . ASP A 1 957  ? -6.194  79.841  74.862  1.00 28.26 ?  955  ASP A OD2   1 
ATOM   7168  N N     . LEU A 1 958  ? -6.876  75.229  78.414  1.00 15.65 ?  956  LEU A N     1 
ATOM   7169  C CA    . LEU A 1 958  ? -7.416  74.716  79.672  1.00 14.20 ?  956  LEU A CA    1 
ATOM   7170  C C     . LEU A 1 958  ? -6.393  74.788  80.811  1.00 15.77 ?  956  LEU A C     1 
ATOM   7171  O O     . LEU A 1 958  ? -6.720  75.216  81.928  1.00 14.77 ?  956  LEU A O     1 
ATOM   7172  C CB    . LEU A 1 958  ? -7.910  73.283  79.475  1.00 16.08 ?  956  LEU A CB    1 
ATOM   7173  C CG    . LEU A 1 958  ? -8.442  72.590  80.729  1.00 16.23 ?  956  LEU A CG    1 
ATOM   7174  C CD1   . LEU A 1 958  ? -9.617  73.345  81.330  1.00 16.13 ?  956  LEU A CD1   1 
ATOM   7175  C CD2   . LEU A 1 958  ? -8.842  71.156  80.398  1.00 15.02 ?  956  LEU A CD2   1 
ATOM   7176  N N     . ASP A 1 959  ? -5.149  74.344  80.568  1.00 14.82 ?  957  ASP A N     1 
ATOM   7177  C CA    . ASP A 1 959  ? -4.174  74.342  81.656  1.00 14.59 ?  957  ASP A CA    1 
ATOM   7178  C C     . ASP A 1 959  ? -3.909  75.756  82.149  1.00 16.70 ?  957  ASP A C     1 
ATOM   7179  O O     . ASP A 1 959  ? -3.757  75.982  83.356  1.00 15.19 ?  957  ASP A O     1 
ATOM   7180  C CB    . ASP A 1 959  ? -2.873  73.681  81.193  1.00 14.52 ?  957  ASP A CB    1 
ATOM   7181  C CG    . ASP A 1 959  ? -1.948  73.353  82.339  1.00 18.84 ?  957  ASP A CG    1 
ATOM   7182  O OD1   . ASP A 1 959  ? -2.379  72.645  83.271  1.00 17.46 ?  957  ASP A OD1   1 
ATOM   7183  O OD2   . ASP A 1 959  ? -0.784  73.789  82.295  1.00 21.91 ?  957  ASP A OD2   1 
ATOM   7184  N N     . ARG A 1 960  ? -3.848  76.720  81.228  1.00 16.07 ?  958  ARG A N     1 
ATOM   7185  C CA    . ARG A 1 960  ? -3.647  78.111  81.620  1.00 16.80 ?  958  ARG A CA    1 
ATOM   7186  C C     . ARG A 1 960  ? -4.822  78.612  82.444  1.00 17.64 ?  958  ARG A C     1 
ATOM   7187  O O     . ARG A 1 960  ? -4.638  79.346  83.428  1.00 18.48 ?  958  ARG A O     1 
ATOM   7188  C CB    . ARG A 1 960  ? -3.453  78.983  80.376  1.00 18.47 ?  958  ARG A CB    1 
ATOM   7189  C CG    . ARG A 1 960  ? -3.291  80.464  80.690  1.00 20.30 ?  958  ARG A CG    1 
ATOM   7190  C CD    . ARG A 1 960  ? -2.925  81.264  79.449  1.00 34.17 ?  958  ARG A CD    1 
ATOM   7191  N NE    . ARG A 1 960  ? -4.089  81.488  78.595  1.00 40.85 ?  958  ARG A NE    1 
ATOM   7192  C CZ    . ARG A 1 960  ? -4.037  81.992  77.369  1.00 41.20 ?  958  ARG A CZ    1 
ATOM   7193  N NH1   . ARG A 1 960  ? -2.887  82.315  76.802  1.00 44.97 ?  958  ARG A NH1   1 
ATOM   7194  N NH2   . ARG A 1 960  ? -5.170  82.173  76.694  1.00 40.25 ?  958  ARG A NH2   1 
ATOM   7195  N N     . LEU A 1 961  ? -6.035  78.210  82.060  1.00 15.66 ?  959  LEU A N     1 
ATOM   7196  C CA    . LEU A 1 961  ? -7.228  78.599  82.803  1.00 16.04 ?  959  LEU A CA    1 
ATOM   7197  C C     . LEU A 1 961  ? -7.169  78.095  84.233  1.00 18.32 ?  959  LEU A C     1 
ATOM   7198  O O     . LEU A 1 961  ? -7.504  78.829  85.169  1.00 16.45 ?  959  LEU A O     1 
ATOM   7199  C CB    . LEU A 1 961  ? -8.473  78.064  82.109  1.00 15.21 ?  959  LEU A CB    1 
ATOM   7200  C CG    . LEU A 1 961  ? -9.759  78.250  82.917  1.00 17.12 ?  959  LEU A CG    1 
ATOM   7201  C CD1   . LEU A 1 961  ? -10.026 79.739  83.121  1.00 18.88 ?  959  LEU A CD1   1 
ATOM   7202  C CD2   . LEU A 1 961  ? -10.921 77.561  82.242  1.00 18.92 ?  959  LEU A CD2   1 
ATOM   7203  N N     . VAL A 1 962  ? -6.769  76.833  84.422  1.00 14.66 ?  960  VAL A N     1 
ATOM   7204  C CA    . VAL A 1 962  ? -6.633  76.305  85.780  1.00 14.05 ?  960  VAL A CA    1 
ATOM   7205  C C     . VAL A 1 962  ? -5.615  77.124  86.557  1.00 18.24 ?  960  VAL A C     1 
ATOM   7206  O O     . VAL A 1 962  ? -5.823  77.447  87.734  1.00 16.23 ?  960  VAL A O     1 
ATOM   7207  C CB    . VAL A 1 962  ? -6.259  74.812  85.743  1.00 15.12 ?  960  VAL A CB    1 
ATOM   7208  C CG1   . VAL A 1 962  ? -5.925  74.293  87.158  1.00 17.92 ?  960  VAL A CG1   1 
ATOM   7209  C CG2   . VAL A 1 962  ? -7.396  74.004  85.144  1.00 14.59 ?  960  VAL A CG2   1 
ATOM   7210  N N     . ASP A 1 963  ? -4.507  77.494  85.910  1.00 16.53 ?  961  ASP A N     1 
ATOM   7211  C CA    . ASP A 1 963  ? -3.561  78.414  86.538  1.00 19.38 ?  961  ASP A CA    1 
ATOM   7212  C C     . ASP A 1 963  ? -4.246  79.711  86.934  1.00 19.91 ?  961  ASP A C     1 
ATOM   7213  O O     . ASP A 1 963  ? -4.023  80.223  88.040  1.00 23.12 ?  961  ASP A O     1 
ATOM   7214  C CB    . ASP A 1 963  ? -2.406  78.732  85.593  1.00 22.19 ?  961  ASP A CB    1 
ATOM   7215  C CG    . ASP A 1 963  ? -1.399  77.626  85.494  1.00 23.88 ?  961  ASP A CG    1 
ATOM   7216  O OD1   . ASP A 1 963  ? -1.484  76.636  86.247  1.00 33.58 ?  961  ASP A OD1   1 
ATOM   7217  O OD2   . ASP A 1 963  ? -0.497  77.767  84.637  1.00 39.35 ?  961  ASP A OD2   1 
ATOM   7218  N N     . ASP A 1 964  ? -5.084  80.251  86.045  1.00 20.93 ?  962  ASP A N     1 
ATOM   7219  C CA    . ASP A 1 964  ? -5.770  81.508  86.331  1.00 24.43 ?  962  ASP A CA    1 
ATOM   7220  C C     . ASP A 1 964  ? -6.672  81.368  87.552  1.00 25.69 ?  962  ASP A C     1 
ATOM   7221  O O     . ASP A 1 964  ? -6.696  82.251  88.419  1.00 27.76 ?  962  ASP A O     1 
ATOM   7222  C CB    . ASP A 1 964  ? -6.578  81.961  85.114  1.00 25.45 ?  962  ASP A CB    1 
ATOM   7223  C CG    . ASP A 1 964  ? -5.698  82.462  83.968  1.00 28.68 ?  962  ASP A CG    1 
ATOM   7224  O OD1   . ASP A 1 964  ? -4.477  82.656  84.175  1.00 30.16 ?  962  ASP A OD1   1 
ATOM   7225  O OD2   . ASP A 1 964  ? -6.240  82.655  82.858  1.00 37.45 ?  962  ASP A OD2   1 
ATOM   7226  N N     . VAL A 1 965  ? -7.402  80.255  87.646  1.00 19.88 ?  963  VAL A N     1 
ATOM   7227  C CA    . VAL A 1 965  ? -8.257  80.021  88.811  1.00 17.66 ?  963  VAL A CA    1 
ATOM   7228  C C     . VAL A 1 965  ? -7.414  79.958  90.081  1.00 21.48 ?  963  VAL A C     1 
ATOM   7229  O O     . VAL A 1 965  ? -7.752  80.573  91.102  1.00 22.82 ?  963  VAL A O     1 
ATOM   7230  C CB    . VAL A 1 965  ? -9.092  78.740  88.633  1.00 17.45 ?  963  VAL A CB    1 
ATOM   7231  C CG1   . VAL A 1 965  ? -9.896  78.459  89.903  1.00 17.65 ?  963  VAL A CG1   1 
ATOM   7232  C CG2   . VAL A 1 965  ? -10.029 78.838  87.421  1.00 17.52 ?  963  VAL A CG2   1 
ATOM   7233  N N     . ASN A 1 966  ? -6.301  79.215  90.038  1.00 17.33 ?  964  ASN A N     1 
ATOM   7234  C CA    . ASN A 1 966  ? -5.430  79.114  91.205  1.00 17.36 ?  964  ASN A CA    1 
ATOM   7235  C C     . ASN A 1 966  ? -4.816  80.457  91.559  1.00 22.68 ?  964  ASN A C     1 
ATOM   7236  O O     . ASN A 1 966  ? -4.605  80.752  92.743  1.00 23.43 ?  964  ASN A O     1 
ATOM   7237  C CB    . ASN A 1 966  ? -4.311  78.102  90.961  1.00 17.69 ?  964  ASN A CB    1 
ATOM   7238  C CG    . ASN A 1 966  ? -4.796  76.662  90.972  1.00 16.98 ?  964  ASN A CG    1 
ATOM   7239  O OD1   . ASN A 1 966  ? -5.846  76.344  91.547  1.00 17.65 ?  964  ASN A OD1   1 
ATOM   7240  N ND2   . ASN A 1 966  ? -4.015  75.778  90.359  1.00 17.46 ?  964  ASN A ND2   1 
ATOM   7241  N N     . ALA A 1 967  ? -4.526  81.279  90.547  1.00 23.45 ?  965  ALA A N     1 
ATOM   7242  C CA    . ALA A 1 967  ? -3.778  82.513  90.766  1.00 26.79 ?  965  ALA A CA    1 
ATOM   7243  C C     . ALA A 1 967  ? -4.522  83.511  91.642  1.00 24.32 ?  965  ALA A C     1 
ATOM   7244  O O     . ALA A 1 967  ? -3.882  84.396  92.221  1.00 29.48 ?  965  ALA A O     1 
ATOM   7245  C CB    . ALA A 1 967  ? -3.433  83.157  89.419  1.00 28.10 ?  965  ALA A CB    1 
ATOM   7246  N N     . THR A 1 968  ? -5.850  83.400  91.752  1.00 23.09 ?  966  THR A N     1 
ATOM   7247  C CA    . THR A 1 968  ? -6.593  84.302  92.629  1.00 22.93 ?  966  THR A CA    1 
ATOM   7248  C C     . THR A 1 968  ? -6.181  84.161  94.081  1.00 20.14 ?  966  THR A C     1 
ATOM   7249  O O     . THR A 1 968  ? -6.375  85.107  94.857  1.00 24.67 ?  966  THR A O     1 
ATOM   7250  C CB    . THR A 1 968  ? -8.097  84.053  92.543  1.00 25.22 ?  966  THR A CB    1 
ATOM   7251  O OG1   . THR A 1 968  ? -8.419  82.821  93.205  1.00 22.72 ?  966  THR A OG1   1 
ATOM   7252  C CG2   . THR A 1 968  ? -8.570  84.001  91.082  1.00 26.64 ?  966  THR A CG2   1 
ATOM   7253  N N     . GLY A 1 969  ? -5.640  83.003  94.468  1.00 21.34 ?  967  GLY A N     1 
ATOM   7254  C CA    . GLY A 1 969  ? -5.251  82.738  95.839  1.00 19.24 ?  967  GLY A CA    1 
ATOM   7255  C C     . GLY A 1 969  ? -6.316  82.074  96.685  1.00 18.36 ?  967  GLY A C     1 
ATOM   7256  O O     . GLY A 1 969  ? -6.007  81.621  97.794  1.00 17.15 ?  967  GLY A O     1 
ATOM   7257  N N     . TYR A 1 970  ? -7.556  82.019  96.209  1.00 16.69 ?  968  TYR A N     1 
ATOM   7258  C CA    . TYR A 1 970  ? -8.613  81.282  96.877  1.00 17.28 ?  968  TYR A CA    1 
ATOM   7259  C C     . TYR A 1 970  ? -8.500  79.796  96.552  1.00 16.63 ?  968  TYR A C     1 
ATOM   7260  O O     . TYR A 1 970  ? -7.731  79.377  95.684  1.00 18.70 ?  968  TYR A O     1 
ATOM   7261  C CB    . TYR A 1 970  ? -9.980  81.819  96.463  1.00 18.43 ?  968  TYR A CB    1 
ATOM   7262  C CG    . TYR A 1 970  ? -10.242 83.223  96.972  1.00 21.38 ?  968  TYR A CG    1 
ATOM   7263  C CD1   . TYR A 1 970  ? -10.639 83.438  98.280  1.00 23.98 ?  968  TYR A CD1   1 
ATOM   7264  C CD2   . TYR A 1 970  ? -10.092 84.324  96.137  1.00 28.96 ?  968  TYR A CD2   1 
ATOM   7265  C CE1   . TYR A 1 970  ? -10.882 84.725  98.757  1.00 26.83 ?  968  TYR A CE1   1 
ATOM   7266  C CE2   . TYR A 1 970  ? -10.336 85.612  96.601  1.00 26.21 ?  968  TYR A CE2   1 
ATOM   7267  C CZ    . TYR A 1 970  ? -10.721 85.803  97.907  1.00 28.49 ?  968  TYR A CZ    1 
ATOM   7268  O OH    . TYR A 1 970  ? -10.958 87.084  98.362  1.00 37.47 ?  968  TYR A OH    1 
ATOM   7269  N N     . GLY A 1 971  ? -9.275  78.992  97.265  1.00 13.29 ?  969  GLY A N     1 
ATOM   7270  C CA    . GLY A 1 971  ? -9.216  77.558  97.057  1.00 13.15 ?  969  GLY A CA    1 
ATOM   7271  C C     . GLY A 1 971  ? -10.283 76.843  97.851  1.00 14.04 ?  969  GLY A C     1 
ATOM   7272  O O     . GLY A 1 971  ? -9.977  75.960  98.660  1.00 13.75 ?  969  GLY A O     1 
ATOM   7273  N N     . LEU A 1 972  ? -11.541 77.230  97.639  1.00 12.66 ?  970  LEU A N     1 
ATOM   7274  C CA    . LEU A 1 972  ? -12.614 76.643  98.428  1.00 12.31 ?  970  LEU A CA    1 
ATOM   7275  C C     . LEU A 1 972  ? -13.316 75.563  97.609  1.00 12.41 ?  970  LEU A C     1 
ATOM   7276  O O     . LEU A 1 972  ? -12.920 74.396  97.662  1.00 13.66 ?  970  LEU A O     1 
ATOM   7277  C CB    . LEU A 1 972  ? -13.584 77.724  98.921  1.00 13.31 ?  970  LEU A CB    1 
ATOM   7278  C CG    . LEU A 1 972  ? -14.619 77.256  99.949  1.00 14.86 ?  970  LEU A CG    1 
ATOM   7279  C CD1   . LEU A 1 972  ? -13.987 76.477  101.109 1.00 17.54 ?  970  LEU A CD1   1 
ATOM   7280  C CD2   . LEU A 1 972  ? -15.384 78.472  100.474 1.00 14.77 ?  970  LEU A CD2   1 
ATOM   7281  N N     . THR A 1 973  ? -14.330 75.919  96.822  1.00 11.89 ?  971  THR A N     1 
ATOM   7282  C CA    . THR A 1 973  ? -15.022 74.924  96.017  1.00 10.77 ?  971  THR A CA    1 
ATOM   7283  C C     . THR A 1 973  ? -14.657 75.086  94.547  1.00 10.29 ?  971  THR A C     1 
ATOM   7284  O O     . THR A 1 973  ? -14.260 76.160  94.095  1.00 10.77 ?  971  THR A O     1 
ATOM   7285  C CB    . THR A 1 973  ? -16.548 75.011  96.179  1.00 11.49 ?  971  THR A CB    1 
ATOM   7286  O OG1   . THR A 1 973  ? -17.002 76.306  95.776  1.00 11.40 ?  971  THR A OG1   1 
ATOM   7287  C CG2   . THR A 1 973  ? -16.989 74.719  97.621  1.00 11.94 ?  971  THR A CG2   1 
ATOM   7288  N N     . PHE A 1 974  ? -14.810 73.989  93.811  1.00 10.07 ?  972  PHE A N     1 
ATOM   7289  C CA    . PHE A 1 974  ? -14.458 73.954  92.398  1.00 10.17 ?  972  PHE A CA    1 
ATOM   7290  C C     . PHE A 1 974  ? -15.274 72.867  91.730  1.00 9.97  ?  972  PHE A C     1 
ATOM   7291  O O     . PHE A 1 974  ? -15.382 71.767  92.265  1.00 11.63 ?  972  PHE A O     1 
ATOM   7292  C CB    . PHE A 1 974  ? -12.966 73.653  92.195  1.00 11.01 ?  972  PHE A CB    1 
ATOM   7293  C CG    . PHE A 1 974  ? -12.607 73.455  90.753  1.00 10.68 ?  972  PHE A CG    1 
ATOM   7294  C CD1   . PHE A 1 974  ? -12.391 74.550  89.945  1.00 12.06 ?  972  PHE A CD1   1 
ATOM   7295  C CD2   . PHE A 1 974  ? -12.528 72.179  90.209  1.00 11.98 ?  972  PHE A CD2   1 
ATOM   7296  C CE1   . PHE A 1 974  ? -12.090 74.399  88.602  1.00 12.79 ?  972  PHE A CE1   1 
ATOM   7297  C CE2   . PHE A 1 974  ? -12.219 72.000  88.864  1.00 11.56 ?  972  PHE A CE2   1 
ATOM   7298  C CZ    . PHE A 1 974  ? -11.993 73.107  88.059  1.00 13.02 ?  972  PHE A CZ    1 
ATOM   7299  N N     . GLY A 1 975  ? -15.831 73.163  90.559  1.00 10.14 ?  973  GLY A N     1 
ATOM   7300  C CA    . GLY A 1 975  ? -16.600 72.185  89.809  1.00 9.84  ?  973  GLY A CA    1 
ATOM   7301  C C     . GLY A 1 975  ? -16.021 71.921  88.435  1.00 10.52 ?  973  GLY A C     1 
ATOM   7302  O O     . GLY A 1 975  ? -15.419 72.798  87.818  1.00 9.91  ?  973  GLY A O     1 
ATOM   7303  N N     . LEU A 1 976  ? -16.214 70.696  87.967  1.00 10.27 ?  974  LEU A N     1 
ATOM   7304  C CA    . LEU A 1 976  ? -15.800 70.319  86.622  1.00 10.31 ?  974  LEU A CA    1 
ATOM   7305  C C     . LEU A 1 976  ? -16.896 69.470  86.013  1.00 9.93  ?  974  LEU A C     1 
ATOM   7306  O O     . LEU A 1 976  ? -17.328 68.485  86.620  1.00 10.42 ?  974  LEU A O     1 
ATOM   7307  C CB    . LEU A 1 976  ? -14.483 69.541  86.655  1.00 11.87 ?  974  LEU A CB    1 
ATOM   7308  C CG    . LEU A 1 976  ? -14.010 68.933  85.339  1.00 11.77 ?  974  LEU A CG    1 
ATOM   7309  C CD1   . LEU A 1 976  ? -13.603 70.007  84.350  1.00 13.68 ?  974  LEU A CD1   1 
ATOM   7310  C CD2   . LEU A 1 976  ? -12.843 67.986  85.587  1.00 13.94 ?  974  LEU A CD2   1 
ATOM   7311  N N     . HIS A 1 977  ? -17.366 69.871  84.823  1.00 9.21  ?  975  HIS A N     1 
ATOM   7312  C CA    . HIS A 1 977  ? -18.315 69.078  84.052  1.00 11.73 ?  975  HIS A CA    1 
ATOM   7313  C C     . HIS A 1 977  ? -17.610 68.590  82.794  1.00 11.02 ?  975  HIS A C     1 
ATOM   7314  O O     . HIS A 1 977  ? -17.283 69.385  81.902  1.00 11.38 ?  975  HIS A O     1 
ATOM   7315  C CB    . HIS A 1 977  ? -19.561 69.887  83.702  1.00 10.47 ?  975  HIS A CB    1 
ATOM   7316  C CG    . HIS A 1 977  ? -20.685 69.730  84.672  1.00 15.02 ?  975  HIS A CG    1 
ATOM   7317  N ND1   . HIS A 1 977  ? -21.778 68.929  84.423  1.00 19.63 ?  975  HIS A ND1   1 
ATOM   7318  C CD2   . HIS A 1 977  ? -20.884 70.271  85.896  1.00 19.42 ?  975  HIS A CD2   1 
ATOM   7319  C CE1   . HIS A 1 977  ? -22.613 69.001  85.443  1.00 17.17 ?  975  HIS A CE1   1 
ATOM   7320  N NE2   . HIS A 1 977  ? -22.092 69.805  86.352  1.00 16.76 ?  975  HIS A NE2   1 
ATOM   7321  N N     . THR A 1 978  ? -17.386 67.284  82.737  1.00 10.72 ?  976  THR A N     1 
ATOM   7322  C CA    . THR A 1 978  ? -16.769 66.628  81.591  1.00 11.01 ?  976  THR A CA    1 
ATOM   7323  C C     . THR A 1 978  ? -17.069 65.147  81.701  1.00 10.18 ?  976  THR A C     1 
ATOM   7324  O O     . THR A 1 978  ? -17.234 64.622  82.806  1.00 12.73 ?  976  THR A O     1 
ATOM   7325  C CB    . THR A 1 978  ? -15.243 66.832  81.529  1.00 11.48 ?  976  THR A CB    1 
ATOM   7326  O OG1   . THR A 1 978  ? -14.733 66.150  80.370  1.00 13.03 ?  976  THR A OG1   1 
ATOM   7327  C CG2   . THR A 1 978  ? -14.555 66.248  82.755  1.00 14.28 ?  976  THR A CG2   1 
ATOM   7328  N N     . ARG A 1 979  ? -17.094 64.473  80.556  1.00 11.82 ?  977  ARG A N     1 
ATOM   7329  C CA    . ARG A 1 979  ? -17.168 63.022  80.551  1.00 11.00 ?  977  ARG A CA    1 
ATOM   7330  C C     . ARG A 1 979  ? -15.812 62.362  80.374  1.00 12.20 ?  977  ARG A C     1 
ATOM   7331  O O     . ARG A 1 979  ? -15.731 61.124  80.421  1.00 14.37 ?  977  ARG A O     1 
ATOM   7332  C CB    . ARG A 1 979  ? -18.107 62.551  79.450  1.00 15.19 ?  977  ARG A CB    1 
ATOM   7333  C CG    . ARG A 1 979  ? -19.536 62.977  79.716  1.00 16.78 ?  977  ARG A CG    1 
ATOM   7334  C CD    . ARG A 1 979  ? -20.373 62.671  78.527  1.00 21.30 ?  977  ARG A CD    1 
ATOM   7335  N NE    . ARG A 1 979  ? -21.773 62.943  78.807  1.00 23.11 ?  977  ARG A NE    1 
ATOM   7336  C CZ    . ARG A 1 979  ? -22.770 62.619  77.999  1.00 27.45 ?  977  ARG A CZ    1 
ATOM   7337  N NH1   . ARG A 1 979  ? -22.550 62.009  76.843  1.00 23.68 ?  977  ARG A NH1   1 
ATOM   7338  N NH2   . ARG A 1 979  ? -24.018 62.905  78.363  1.00 28.25 ?  977  ARG A NH2   1 
ATOM   7339  N N     . LEU A 1 980  ? -14.755 63.141  80.207  1.00 10.81 ?  978  LEU A N     1 
ATOM   7340  C CA    . LEU A 1 980  ? -13.494 62.604  79.700  1.00 10.27 ?  978  LEU A CA    1 
ATOM   7341  C C     . LEU A 1 980  ? -12.481 62.408  80.825  1.00 12.92 ?  978  LEU A C     1 
ATOM   7342  O O     . LEU A 1 980  ? -12.111 63.371  81.512  1.00 13.20 ?  978  LEU A O     1 
ATOM   7343  C CB    . LEU A 1 980  ? -12.912 63.523  78.625  1.00 11.04 ?  978  LEU A CB    1 
ATOM   7344  C CG    . LEU A 1 980  ? -13.894 63.833  77.493  1.00 12.14 ?  978  LEU A CG    1 
ATOM   7345  C CD1   . LEU A 1 980  ? -13.322 64.870  76.558  1.00 15.41 ?  978  LEU A CD1   1 
ATOM   7346  C CD2   . LEU A 1 980  ? -14.252 62.553  76.750  1.00 14.20 ?  978  LEU A CD2   1 
ATOM   7347  N N     . ASP A 1 981  ? -11.994 61.170  80.971  1.00 11.32 ?  979  ASP A N     1 
ATOM   7348  C CA    . ASP A 1 981  ? -11.042 60.857  82.036  1.00 12.69 ?  979  ASP A CA    1 
ATOM   7349  C C     . ASP A 1 981  ? -9.766  61.682  81.928  1.00 12.33 ?  979  ASP A C     1 
ATOM   7350  O O     . ASP A 1 981  ? -9.168  62.023  82.957  1.00 12.52 ?  979  ASP A O     1 
ATOM   7351  C CB    . ASP A 1 981  ? -10.673 59.370  82.014  1.00 12.60 ?  979  ASP A CB    1 
ATOM   7352  C CG    . ASP A 1 981  ? -11.778 58.474  82.515  1.00 15.94 ?  979  ASP A CG    1 
ATOM   7353  O OD1   . ASP A 1 981  ? -12.720 58.965  83.170  1.00 18.10 ?  979  ASP A OD1   1 
ATOM   7354  O OD2   . ASP A 1 981  ? -11.662 57.248  82.275  1.00 17.90 ?  979  ASP A OD2   1 
ATOM   7355  N N     . GLU A 1 982  ? -9.268  61.931  80.701  1.00 12.38 ?  980  GLU A N     1 
ATOM   7356  C CA    . GLU A 1 982  ? -8.032  62.707  80.574  1.00 11.99 ?  980  GLU A CA    1 
ATOM   7357  C C     . GLU A 1 982  ? -8.235  64.110  81.132  1.00 13.31 ?  980  GLU A C     1 
ATOM   7358  O O     . GLU A 1 982  ? -7.362  64.653  81.819  1.00 13.92 ?  980  GLU A O     1 
ATOM   7359  C CB    . GLU A 1 982  ? -7.554  62.778  79.115  1.00 14.13 ?  980  GLU A CB    1 
ATOM   7360  C CG    . GLU A 1 982  ? -6.342  63.719  78.952  1.00 15.73 ?  980  GLU A CG    1 
ATOM   7361  C CD    . GLU A 1 982  ? -5.996  64.052  77.508  1.00 19.89 ?  980  GLU A CD    1 
ATOM   7362  O OE1   . GLU A 1 982  ? -6.885  64.542  76.779  1.00 24.85 ?  980  GLU A OE1   1 
ATOM   7363  O OE2   . GLU A 1 982  ? -4.827  63.858  77.099  1.00 20.79 ?  980  GLU A OE2   1 
ATOM   7364  N N     . THR A 1 983  ? -9.407  64.697  80.878  1.00 12.60 ?  981  THR A N     1 
ATOM   7365  C CA    . THR A 1 983  ? -9.660  66.043  81.381  1.00 13.35 ?  981  THR A CA    1 
ATOM   7366  C C     . THR A 1 983  ? -9.854  66.034  82.897  1.00 11.95 ?  981  THR A C     1 
ATOM   7367  O O     . THR A 1 983  ? -9.358  66.934  83.592  1.00 13.05 ?  981  THR A O     1 
ATOM   7368  C CB    . THR A 1 983  ? -10.863 66.631  80.641  1.00 13.96 ?  981  THR A CB    1 
ATOM   7369  O OG1   . THR A 1 983  ? -10.528 66.724  79.251  1.00 15.59 ?  981  THR A OG1   1 
ATOM   7370  C CG2   . THR A 1 983  ? -11.188 68.020  81.156  1.00 14.48 ?  981  THR A CG2   1 
ATOM   7371  N N     . ILE A 1 984  ? -10.559 65.023  83.438  1.00 11.95 ?  982  ILE A N     1 
ATOM   7372  C CA    . ILE A 1 984  ? -10.702 64.897  84.892  1.00 10.93 ?  982  ILE A CA    1 
ATOM   7373  C C     . ILE A 1 984  ? -9.335  64.794  85.554  1.00 10.96 ?  982  ILE A C     1 
ATOM   7374  O O     . ILE A 1 984  ? -9.055  65.487  86.541  1.00 12.03 ?  982  ILE A O     1 
ATOM   7375  C CB    . ILE A 1 984  ? -11.586 63.688  85.254  1.00 11.86 ?  982  ILE A CB    1 
ATOM   7376  C CG1   . ILE A 1 984  ? -13.008 63.907  84.737  1.00 14.21 ?  982  ILE A CG1   1 
ATOM   7377  C CG2   . ILE A 1 984  ? -11.620 63.461  86.777  1.00 14.30 ?  982  ILE A CG2   1 
ATOM   7378  C CD1   . ILE A 1 984  ? -13.902 62.663  84.781  1.00 15.54 ?  982  ILE A CD1   1 
ATOM   7379  N N     . ALA A 1 985  ? -8.468  63.922  85.022  1.00 11.78 ?  983  ALA A N     1 
ATOM   7380  C CA    . ALA A 1 985  ? -7.153  63.724  85.627  1.00 12.03 ?  983  ALA A CA    1 
ATOM   7381  C C     . ALA A 1 985  ? -6.339  65.006  85.578  1.00 11.31 ?  983  ALA A C     1 
ATOM   7382  O O     . ALA A 1 985  ? -5.743  65.413  86.580  1.00 13.57 ?  983  ALA A O     1 
ATOM   7383  C CB    . ALA A 1 985  ? -6.404  62.594  84.917  1.00 13.24 ?  983  ALA A CB    1 
ATOM   7384  N N     . HIS A 1 986  ? -6.319  65.661  84.416  1.00 11.96 ?  984  HIS A N     1 
ATOM   7385  C CA    . HIS A 1 986  ? -5.568  66.902  84.254  1.00 12.15 ?  984  HIS A CA    1 
ATOM   7386  C C     . HIS A 1 986  ? -6.065  67.971  85.218  1.00 12.94 ?  984  HIS A C     1 
ATOM   7387  O O     . HIS A 1 986  ? -5.291  68.543  85.989  1.00 12.92 ?  984  HIS A O     1 
ATOM   7388  C CB    . HIS A 1 986  ? -5.697  67.373  82.802  1.00 14.38 ?  984  HIS A CB    1 
ATOM   7389  C CG    . HIS A 1 986  ? -5.105  68.722  82.526  1.00 13.56 ?  984  HIS A CG    1 
ATOM   7390  N ND1   . HIS A 1 986  ? -5.308  69.370  81.330  1.00 20.27 ?  984  HIS A ND1   1 
ATOM   7391  C CD2   . HIS A 1 986  ? -4.301  69.530  83.259  1.00 16.25 ?  984  HIS A CD2   1 
ATOM   7392  C CE1   . HIS A 1 986  ? -4.666  70.526  81.339  1.00 19.40 ?  984  HIS A CE1   1 
ATOM   7393  N NE2   . HIS A 1 986  ? -4.064  70.657  82.506  1.00 17.14 ?  984  HIS A NE2   1 
ATOM   7394  N N     . VAL A 1 987  ? -7.363  68.273  85.164  1.00 13.46 ?  985  VAL A N     1 
ATOM   7395  C CA    . VAL A 1 987  ? -7.872  69.396  85.936  1.00 12.35 ?  985  VAL A CA    1 
ATOM   7396  C C     . VAL A 1 987  ? -7.771  69.113  87.425  1.00 13.09 ?  985  VAL A C     1 
ATOM   7397  O O     . VAL A 1 987  ? -7.349  69.983  88.194  1.00 13.93 ?  985  VAL A O     1 
ATOM   7398  C CB    . VAL A 1 987  ? -9.315  69.718  85.517  1.00 10.85 ?  985  VAL A CB    1 
ATOM   7399  C CG1   . VAL A 1 987  ? -9.934  70.742  86.488  1.00 12.12 ?  985  VAL A CG1   1 
ATOM   7400  C CG2   . VAL A 1 987  ? -9.352  70.256  84.089  1.00 12.75 ?  985  VAL A CG2   1 
ATOM   7401  N N     . THR A 1 988  ? -8.151  67.904  87.863  1.00 12.07 ?  986  THR A N     1 
ATOM   7402  C CA    . THR A 1 988  ? -8.139  67.659  89.302  1.00 11.86 ?  986  THR A CA    1 
ATOM   7403  C C     . THR A 1 988  ? -6.724  67.544  89.845  1.00 14.47 ?  986  THR A C     1 
ATOM   7404  O O     . THR A 1 988  ? -6.511  67.813  91.033  1.00 18.52 ?  986  THR A O     1 
ATOM   7405  C CB    . THR A 1 988  ? -8.941  66.408  89.695  1.00 15.83 ?  986  THR A CB    1 
ATOM   7406  O OG1   . THR A 1 988  ? -8.371  65.237  89.103  1.00 16.64 ?  986  THR A OG1   1 
ATOM   7407  C CG2   . THR A 1 988  ? -10.395 66.547  89.293  1.00 17.37 ?  986  THR A CG2   1 
ATOM   7408  N N     . SER A 1 989  ? -5.749  67.207  89.005  1.00 13.76 ?  987  SER A N     1 
ATOM   7409  C CA    . SER A 1 989  ? -4.380  67.181  89.509  1.00 16.61 ?  987  SER A CA    1 
ATOM   7410  C C     . SER A 1 989  ? -3.807  68.586  89.644  1.00 18.33 ?  987  SER A C     1 
ATOM   7411  O O     . SER A 1 989  ? -2.950  68.814  90.503  1.00 22.88 ?  987  SER A O     1 
ATOM   7412  C CB    . SER A 1 989  ? -3.485  66.310  88.615  1.00 19.63 ?  987  SER A CB    1 
ATOM   7413  O OG    . SER A 1 989  ? -3.206  66.922  87.374  1.00 26.32 ?  987  SER A OG    1 
ATOM   7414  N N     . ARG A 1 990  ? -4.292  69.543  88.855  1.00 14.75 ?  988  ARG A N     1 
ATOM   7415  C CA    . ARG A 1 990  ? -3.694  70.869  88.784  1.00 15.52 ?  988  ARG A CA    1 
ATOM   7416  C C     . ARG A 1 990  ? -4.433  71.922  89.599  1.00 15.80 ?  988  ARG A C     1 
ATOM   7417  O O     . ARG A 1 990  ? -3.811  72.895  90.039  1.00 18.08 ?  988  ARG A O     1 
ATOM   7418  C CB    . ARG A 1 990  ? -3.619  71.331  87.329  1.00 18.18 ?  988  ARG A CB    1 
ATOM   7419  C CG    . ARG A 1 990  ? -2.783  70.420  86.439  1.00 22.74 ?  988  ARG A CG    1 
ATOM   7420  C CD    . ARG A 1 990  ? -1.312  70.699  86.617  1.00 26.20 ?  988  ARG A CD    1 
ATOM   7421  N NE    . ARG A 1 990  ? -0.822  71.605  85.587  1.00 24.69 ?  988  ARG A NE    1 
ATOM   7422  C CZ    . ARG A 1 990  ? 0.434   72.013  85.497  1.00 22.40 ?  988  ARG A CZ    1 
ATOM   7423  N NH1   . ARG A 1 990  ? 1.335   71.688  86.413  1.00 24.65 ?  988  ARG A NH1   1 
ATOM   7424  N NH2   . ARG A 1 990  ? 0.796   72.762  84.465  1.00 21.52 ?  988  ARG A NH2   1 
ATOM   7425  N N     . ILE A 1 991  ? -5.742  71.758  89.809  1.00 13.87 ?  989  ILE A N     1 
ATOM   7426  C CA    . ILE A 1 991  ? -6.496  72.708  90.620  1.00 13.94 ?  989  ILE A CA    1 
ATOM   7427  C C     . ILE A 1 991  ? -6.052  72.602  92.076  1.00 13.33 ?  989  ILE A C     1 
ATOM   7428  O O     . ILE A 1 991  ? -5.689  71.528  92.562  1.00 15.14 ?  989  ILE A O     1 
ATOM   7429  C CB    . ILE A 1 991  ? -8.007  72.437  90.465  1.00 12.65 ?  989  ILE A CB    1 
ATOM   7430  C CG1   . ILE A 1 991  ? -8.843  73.584  91.044  1.00 13.91 ?  989  ILE A CG1   1 
ATOM   7431  C CG2   . ILE A 1 991  ? -8.397  71.103  91.087  1.00 14.74 ?  989  ILE A CG2   1 
ATOM   7432  C CD1   . ILE A 1 991  ? -8.798  74.826  90.195  1.00 16.09 ?  989  ILE A CD1   1 
ATOM   7433  N N     . LYS A 1 992  ? -6.077  73.728  92.783  1.00 12.88 ?  990  LYS A N     1 
ATOM   7434  C CA    . LYS A 1 992  ? -5.746  73.746  94.207  1.00 14.92 ?  990  LYS A CA    1 
ATOM   7435  C C     . LYS A 1 992  ? -6.949  74.276  94.981  1.00 12.89 ?  990  LYS A C     1 
ATOM   7436  O O     . LYS A 1 992  ? -7.037  75.476  95.243  1.00 17.23 ?  990  LYS A O     1 
ATOM   7437  C CB    . LYS A 1 992  ? -4.498  74.595  94.459  1.00 16.41 ?  990  LYS A CB    1 
ATOM   7438  C CG    . LYS A 1 992  ? -3.230  74.011  93.841  1.00 21.90 ?  990  LYS A CG    1 
ATOM   7439  C CD    . LYS A 1 992  ? -2.040  74.962  94.035  1.00 28.86 ?  990  LYS A CD    1 
ATOM   7440  C CE    . LYS A 1 992  ? -0.774  74.436  93.361  1.00 36.52 ?  990  LYS A CE    1 
ATOM   7441  N NZ    . LYS A 1 992  ? -0.463  73.030  93.755  1.00 41.07 ?  990  LYS A NZ    1 
ATOM   7442  N N     . ALA A 1 993  ? -7.878  73.385  95.334  1.00 14.63 ?  991  ALA A N     1 
ATOM   7443  C CA    . ALA A 1 993  ? -9.062  73.780  96.092  1.00 13.21 ?  991  ALA A CA    1 
ATOM   7444  C C     . ALA A 1 993  ? -9.436  72.656  97.047  1.00 13.44 ?  991  ALA A C     1 
ATOM   7445  O O     . ALA A 1 993  ? -9.110  71.491  96.821  1.00 14.23 ?  991  ALA A O     1 
ATOM   7446  C CB    . ALA A 1 993  ? -10.228 74.125  95.167  1.00 13.34 ?  991  ALA A CB    1 
ATOM   7447  N N     . GLY A 1 994  ? -10.142 73.016  98.121  1.00 11.46 ?  992  GLY A N     1 
ATOM   7448  C CA    . GLY A 1 994  ? -10.447 72.049  99.161  1.00 13.49 ?  992  GLY A CA    1 
ATOM   7449  C C     . GLY A 1 994  ? -11.618 71.131  98.882  1.00 12.13 ?  992  GLY A C     1 
ATOM   7450  O O     . GLY A 1 994  ? -11.651 70.005  99.387  1.00 10.91 ?  992  GLY A O     1 
ATOM   7451  N N     . ASN A 1 995  ? -12.589 71.581  98.087  1.00 10.48 ?  993  ASN A N     1 
ATOM   7452  C CA    . ASN A 1 995  ? -13.808 70.818  97.821  1.00 12.15 ?  993  ASN A CA    1 
ATOM   7453  C C     . ASN A 1 995  ? -14.043 70.787  96.323  1.00 11.06 ?  993  ASN A C     1 
ATOM   7454  O O     . ASN A 1 995  ? -14.433 71.799  95.736  1.00 11.97 ?  993  ASN A O     1 
ATOM   7455  C CB    . ASN A 1 995  ? -15.012 71.417  98.554  1.00 10.44 ?  993  ASN A CB    1 
ATOM   7456  C CG    . ASN A 1 995  ? -15.046 70.996  100.008 1.00 11.93 ?  993  ASN A CG    1 
ATOM   7457  O OD1   . ASN A 1 995  ? -14.425 71.623  100.864 1.00 12.19 ?  993  ASN A OD1   1 
ATOM   7458  N ND2   . ASN A 1 995  ? -15.735 69.903  100.286 1.00 12.91 ?  993  ASN A ND2   1 
ATOM   7459  N N     . LEU A 1 996  ? -13.790 69.630  95.727  1.00 10.66 ?  994  LEU A N     1 
ATOM   7460  C CA    . LEU A 1 996  ? -13.943 69.428  94.293  1.00 9.97  ?  994  LEU A CA    1 
ATOM   7461  C C     . LEU A 1 996  ? -15.218 68.657  94.028  1.00 9.23  ?  994  LEU A C     1 
ATOM   7462  O O     . LEU A 1 996  ? -15.588 67.761  94.797  1.00 10.44 ?  994  LEU A O     1 
ATOM   7463  C CB    . LEU A 1 996  ? -12.764 68.656  93.705  1.00 11.29 ?  994  LEU A CB    1 
ATOM   7464  C CG    . LEU A 1 996  ? -11.389 69.126  94.159  1.00 12.18 ?  994  LEU A CG    1 
ATOM   7465  C CD1   . LEU A 1 996  ? -10.327 68.271  93.473  1.00 14.92 ?  994  LEU A CD1   1 
ATOM   7466  C CD2   . LEU A 1 996  ? -11.165 70.589  93.846  1.00 14.50 ?  994  LEU A CD2   1 
ATOM   7467  N N     . TYR A 1 997  ? -15.879 69.009  92.921  1.00 10.01 ?  995  TYR A N     1 
ATOM   7468  C CA    . TYR A 1 997  ? -17.153 68.407  92.542  1.00 9.25  ?  995  TYR A CA    1 
ATOM   7469  C C     . TYR A 1 997  ? -17.135 68.119  91.051  1.00 9.94  ?  995  TYR A C     1 
ATOM   7470  O O     . TYR A 1 997  ? -16.854 69.023  90.255  1.00 11.26 ?  995  TYR A O     1 
ATOM   7471  C CB    . TYR A 1 997  ? -18.315 69.341  92.887  1.00 10.78 ?  995  TYR A CB    1 
ATOM   7472  C CG    . TYR A 1 997  ? -18.440 69.622  94.363  1.00 10.69 ?  995  TYR A CG    1 
ATOM   7473  C CD1   . TYR A 1 997  ? -19.084 68.721  95.203  1.00 11.60 ?  995  TYR A CD1   1 
ATOM   7474  C CD2   . TYR A 1 997  ? -17.917 70.790  94.916  1.00 11.86 ?  995  TYR A CD2   1 
ATOM   7475  C CE1   . TYR A 1 997  ? -19.222 68.977  96.578  1.00 12.07 ?  995  TYR A CE1   1 
ATOM   7476  C CE2   . TYR A 1 997  ? -18.042 71.056  96.294  1.00 12.48 ?  995  TYR A CE2   1 
ATOM   7477  C CZ    . TYR A 1 997  ? -18.701 70.146  97.100  1.00 14.46 ?  995  TYR A CZ    1 
ATOM   7478  O OH    . TYR A 1 997  ? -18.818 70.416  98.454  1.00 13.97 ?  995  TYR A OH    1 
ATOM   7479  N N     . ILE A 1 998  ? -17.403 66.869  90.678  1.00 9.94  ?  996  ILE A N     1 
ATOM   7480  C CA    A ILE A 1 998  ? -17.337 66.443  89.284  0.51 11.01 ?  996  ILE A CA    1 
ATOM   7481  C CA    B ILE A 1 998  ? -17.333 66.432  89.285  0.49 11.01 ?  996  ILE A CA    1 
ATOM   7482  C C     . ILE A 1 998  ? -18.731 66.041  88.833  1.00 10.16 ?  996  ILE A C     1 
ATOM   7483  O O     . ILE A 1 998  ? -19.331 65.118  89.393  1.00 10.59 ?  996  ILE A O     1 
ATOM   7484  C CB    A ILE A 1 998  ? -16.343 65.292  89.083  0.51 10.23 ?  996  ILE A CB    1 
ATOM   7485  C CB    B ILE A 1 998  ? -16.359 65.259  89.092  0.49 10.23 ?  996  ILE A CB    1 
ATOM   7486  C CG1   A ILE A 1 998  ? -14.928 65.772  89.393  0.51 13.58 ?  996  ILE A CG1   1 
ATOM   7487  C CG1   B ILE A 1 998  ? -15.025 65.534  89.790  0.49 14.57 ?  996  ILE A CG1   1 
ATOM   7488  C CG2   A ILE A 1 998  ? -16.427 64.779  87.645  0.51 11.72 ?  996  ILE A CG2   1 
ATOM   7489  C CG2   B ILE A 1 998  ? -16.149 65.012  87.588  0.49 11.61 ?  996  ILE A CG2   1 
ATOM   7490  C CD1   A ILE A 1 998  ? -13.885 64.702  89.228  0.51 15.77 ?  996  ILE A CD1   1 
ATOM   7491  C CD1   B ILE A 1 998  ? -14.205 66.606  89.132  0.49 15.05 ?  996  ILE A CD1   1 
ATOM   7492  N N     . ASN A 1 999  ? -19.235 66.748  87.813  1.00 9.68  ?  997  ASN A N     1 
ATOM   7493  C CA    . ASN A 1 999  ? -20.517 66.462  87.154  1.00 10.08 ?  997  ASN A CA    1 
ATOM   7494  C C     . ASN A 1 999  ? -21.703 66.585  88.108  1.00 10.15 ?  997  ASN A C     1 
ATOM   7495  O O     . ASN A 1 999  ? -22.679 65.840  88.020  1.00 11.53 ?  997  ASN A O     1 
ATOM   7496  C CB    . ASN A 1 999  ? -20.473 65.091  86.482  1.00 9.77  ?  997  ASN A CB    1 
ATOM   7497  C CG    . ASN A 1 999  ? -19.511 65.077  85.313  1.00 9.85  ?  997  ASN A CG    1 
ATOM   7498  O OD1   . ASN A 1 999  ? -19.320 66.105  84.665  1.00 11.28 ?  997  ASN A OD1   1 
ATOM   7499  N ND2   . ASN A 1 999  ? -18.896 63.924  85.043  1.00 12.06 ?  997  ASN A ND2   1 
ATOM   7500  N N     . ARG A 1 1000 ? -21.623 67.563  89.004  1.00 10.23 ?  998  ARG A N     1 
ATOM   7501  C CA    . ARG A 1 1000 ? -22.696 67.864  89.953  1.00 9.56  ?  998  ARG A CA    1 
ATOM   7502  C C     . ARG A 1 1000 ? -22.540 69.327  90.365  1.00 11.15 ?  998  ARG A C     1 
ATOM   7503  O O     . ARG A 1 1000 ? -21.626 70.020  89.916  1.00 12.52 ?  998  ARG A O     1 
ATOM   7504  C CB    . ARG A 1 1000 ? -22.660 66.902  91.148  1.00 10.13 ?  998  ARG A CB    1 
ATOM   7505  C CG    . ARG A 1 1000 ? -21.305 66.794  91.828  1.00 9.96  ?  998  ARG A CG    1 
ATOM   7506  C CD    . ARG A 1 1000 ? -21.442 66.435  93.296  1.00 11.96 ?  998  ARG A CD    1 
ATOM   7507  N NE    . ARG A 1 1000 ? -22.050 67.547  94.008  1.00 10.71 ?  998  ARG A NE    1 
ATOM   7508  C CZ    . ARG A 1 1000 ? -22.288 67.555  95.311  1.00 11.55 ?  998  ARG A CZ    1 
ATOM   7509  N NH1   . ARG A 1 1000 ? -21.999 66.509  96.069  1.00 13.96 ?  998  ARG A NH1   1 
ATOM   7510  N NH2   . ARG A 1 1000 ? -22.794 68.653  95.868  1.00 12.01 ?  998  ARG A NH2   1 
ATOM   7511  N N     . ASN A 1 1001 ? -23.460 69.812  91.207  1.00 10.40 ?  999  ASN A N     1 
ATOM   7512  C CA    . ASN A 1 1001 ? -23.313 71.179  91.697  1.00 9.58  ?  999  ASN A CA    1 
ATOM   7513  C C     . ASN A 1 1001 ? -22.178 71.249  92.734  1.00 11.00 ?  999  ASN A C     1 
ATOM   7514  O O     . ASN A 1 1001 ? -21.598 70.227  93.131  1.00 12.04 ?  999  ASN A O     1 
ATOM   7515  C CB    . ASN A 1 1001 ? -24.658 71.707  92.243  1.00 11.07 ?  999  ASN A CB    1 
ATOM   7516  C CG    . ASN A 1 1001 ? -25.086 71.052  93.550  1.00 14.98 ?  999  ASN A CG    1 
ATOM   7517  O OD1   . ASN A 1 1001 ? -24.287 70.856  94.464  1.00 13.91 ?  999  ASN A OD1   1 
ATOM   7518  N ND2   . ASN A 1 1001 ? -26.370 70.730  93.651  1.00 17.31 ?  999  ASN A ND2   1 
ATOM   7519  N N     . ILE A 1 1002 ? -21.838 72.467  93.147  1.00 9.88  ?  1000 ILE A N     1 
ATOM   7520  C CA    . ILE A 1 1002 ? -20.679 72.665  94.018  1.00 10.47 ?  1000 ILE A CA    1 
ATOM   7521  C C     . ILE A 1 1002 ? -21.089 73.144  95.407  1.00 12.42 ?  1000 ILE A C     1 
ATOM   7522  O O     . ILE A 1 1002 ? -20.239 73.619  96.162  1.00 12.69 ?  1000 ILE A O     1 
ATOM   7523  C CB    . ILE A 1 1002 ? -19.639 73.616  93.391  1.00 10.34 ?  1000 ILE A CB    1 
ATOM   7524  C CG1   . ILE A 1 1002 ? -20.142 75.060  93.268  1.00 11.52 ?  1000 ILE A CG1   1 
ATOM   7525  C CG2   . ILE A 1 1002 ? -19.168 73.098  92.035  1.00 10.75 ?  1000 ILE A CG2   1 
ATOM   7526  C CD1   . ILE A 1 1002 ? -19.051 76.037  92.857  1.00 13.18 ?  1000 ILE A CD1   1 
ATOM   7527  N N     . ILE A 1 1003 ? -22.363 73.001  95.776  1.00 11.12 ?  1001 ILE A N     1 
ATOM   7528  C CA    . ILE A 1 1003 ? -22.849 73.503  97.059  1.00 11.90 ?  1001 ILE A CA    1 
ATOM   7529  C C     . ILE A 1 1003 ? -23.393 72.366  97.923  1.00 13.54 ?  1001 ILE A C     1 
ATOM   7530  O O     . ILE A 1 1003 ? -23.592 71.239  97.483  1.00 13.69 ?  1001 ILE A O     1 
ATOM   7531  C CB    . ILE A 1 1003 ? -23.919 74.603  96.884  1.00 12.51 ?  1001 ILE A CB    1 
ATOM   7532  C CG1   . ILE A 1 1003 ? -25.148 74.071  96.147  1.00 13.88 ?  1001 ILE A CG1   1 
ATOM   7533  C CG2   . ILE A 1 1003 ? -23.346 75.783  96.144  1.00 14.61 ?  1001 ILE A CG2   1 
ATOM   7534  C CD1   . ILE A 1 1003 ? -26.376 74.999  96.312  1.00 17.95 ?  1001 ILE A CD1   1 
ATOM   7535  N N     . GLY A 1 1004 ? -23.665 72.703  99.179  1.00 14.05 ?  1002 GLY A N     1 
ATOM   7536  C CA    . GLY A 1 1004 ? -24.313 71.756  100.065 1.00 14.96 ?  1002 GLY A CA    1 
ATOM   7537  C C     . GLY A 1 1004 ? -23.430 70.609  100.505 1.00 14.75 ?  1002 GLY A C     1 
ATOM   7538  O O     . GLY A 1 1004 ? -23.891 69.460  100.552 1.00 14.92 ?  1002 GLY A O     1 
ATOM   7539  N N     . ALA A 1 1005 ? -22.167 70.894  100.829 1.00 14.35 ?  1003 ALA A N     1 
ATOM   7540  C CA    . ALA A 1 1005 ? -21.283 69.866  101.350 1.00 14.24 ?  1003 ALA A CA    1 
ATOM   7541  C C     . ALA A 1 1005 ? -21.936 69.172  102.540 1.00 15.30 ?  1003 ALA A C     1 
ATOM   7542  O O     . ALA A 1 1005 ? -22.568 69.818  103.385 1.00 16.34 ?  1003 ALA A O     1 
ATOM   7543  C CB    . ALA A 1 1005 ? -19.942 70.490  101.753 1.00 14.52 ?  1003 ALA A CB    1 
ATOM   7544  N N     . VAL A 1 1006 ? -21.782 67.849  102.596 1.00 12.28 ?  1004 VAL A N     1 
ATOM   7545  C CA    . VAL A 1 1006 ? -22.424 67.008  103.603 1.00 12.57 ?  1004 VAL A CA    1 
ATOM   7546  C C     . VAL A 1 1006 ? -21.394 66.612  104.660 1.00 13.41 ?  1004 VAL A C     1 
ATOM   7547  O O     . VAL A 1 1006 ? -20.308 66.123  104.333 1.00 13.23 ?  1004 VAL A O     1 
ATOM   7548  C CB    . VAL A 1 1006 ? -23.067 65.770  102.950 1.00 14.66 ?  1004 VAL A CB    1 
ATOM   7549  C CG1   . VAL A 1 1006 ? -23.555 64.785  103.991 1.00 16.88 ?  1004 VAL A CG1   1 
ATOM   7550  C CG2   . VAL A 1 1006 ? -24.214 66.186  102.017 1.00 15.84 ?  1004 VAL A CG2   1 
ATOM   7551  N N     . VAL A 1 1007 ? -21.741 66.830  105.929 1.00 13.54 ?  1005 VAL A N     1 
ATOM   7552  C CA    . VAL A 1 1007 ? -20.842 66.536  107.045 1.00 11.96 ?  1005 VAL A CA    1 
ATOM   7553  C C     . VAL A 1 1007 ? -20.387 65.087  106.971 1.00 13.37 ?  1005 VAL A C     1 
ATOM   7554  O O     . VAL A 1 1007 ? -21.201 64.173  106.795 1.00 13.58 ?  1005 VAL A O     1 
ATOM   7555  C CB    . VAL A 1 1007 ? -21.566 66.848  108.364 1.00 12.69 ?  1005 VAL A CB    1 
ATOM   7556  C CG1   . VAL A 1 1007 ? -20.778 66.322  109.555 1.00 13.56 ?  1005 VAL A CG1   1 
ATOM   7557  C CG2   . VAL A 1 1007 ? -21.759 68.341  108.481 1.00 15.22 ?  1005 VAL A CG2   1 
ATOM   7558  N N     . GLY A 1 1008 ? -19.072 64.865  107.119 1.00 13.00 ?  1006 GLY A N     1 
ATOM   7559  C CA    . GLY A 1 1008 ? -18.513 63.521  107.114 1.00 12.80 ?  1006 GLY A CA    1 
ATOM   7560  C C     . GLY A 1 1008 ? -18.508 62.825  105.769 1.00 13.86 ?  1006 GLY A C     1 
ATOM   7561  O O     . GLY A 1 1008 ? -18.061 61.674  105.689 1.00 14.81 ?  1006 GLY A O     1 
ATOM   7562  N N     . VAL A 1 1009 ? -19.045 63.456  104.728 1.00 12.47 ?  1007 VAL A N     1 
ATOM   7563  C CA    . VAL A 1 1009 ? -19.078 62.906  103.380 1.00 13.54 ?  1007 VAL A CA    1 
ATOM   7564  C C     . VAL A 1 1009 ? -18.272 63.774  102.423 1.00 12.24 ?  1007 VAL A C     1 
ATOM   7565  O O     . VAL A 1 1009 ? -17.408 63.276  101.688 1.00 12.53 ?  1007 VAL A O     1 
ATOM   7566  C CB    . VAL A 1 1009 ? -20.529 62.737  102.884 1.00 12.91 ?  1007 VAL A CB    1 
ATOM   7567  C CG1   . VAL A 1 1009 ? -20.541 62.077  101.496 1.00 12.90 ?  1007 VAL A CG1   1 
ATOM   7568  C CG2   . VAL A 1 1009 ? -21.329 61.896  103.878 1.00 13.14 ?  1007 VAL A CG2   1 
ATOM   7569  N N     . GLN A 1 1010 ? -18.522 65.090  102.435 1.00 12.80 ?  1008 GLN A N     1 
ATOM   7570  C CA    . GLN A 1 1010 ? -17.608 66.088  101.880 1.00 11.60 ?  1008 GLN A CA    1 
ATOM   7571  C C     . GLN A 1 1010 ? -17.208 67.022  103.014 1.00 13.49 ?  1008 GLN A C     1 
ATOM   7572  O O     . GLN A 1 1010 ? -17.780 68.107  103.151 1.00 15.65 ?  1008 GLN A O     1 
ATOM   7573  C CB    . GLN A 1 1010 ? -18.229 66.877  100.730 1.00 13.34 ?  1008 GLN A CB    1 
ATOM   7574  C CG    . GLN A 1 1010 ? -18.746 66.009  99.587  1.00 13.13 ?  1008 GLN A CG    1 
ATOM   7575  C CD    . GLN A 1 1010 ? -20.242 65.768  99.667  1.00 12.84 ?  1008 GLN A CD    1 
ATOM   7576  O OE1   . GLN A 1 1010 ? -20.994 66.570  100.246 1.00 14.03 ?  1008 GLN A OE1   1 
ATOM   7577  N NE2   . GLN A 1 1010 ? -20.681 64.637  99.129  1.00 13.38 ?  1008 GLN A NE2   1 
ATOM   7578  N N     . PRO A 1 1011 ? -16.253 66.621  103.855 1.00 13.46 ?  1009 PRO A N     1 
ATOM   7579  C CA    . PRO A 1 1011 ? -15.674 67.562  104.826 1.00 15.01 ?  1009 PRO A CA    1 
ATOM   7580  C C     . PRO A 1 1011 ? -15.321 68.864  104.129 1.00 12.60 ?  1009 PRO A C     1 
ATOM   7581  O O     . PRO A 1 1011 ? -14.765 68.858  103.034 1.00 13.11 ?  1009 PRO A O     1 
ATOM   7582  C CB    . PRO A 1 1011 ? -14.421 66.834  105.312 1.00 14.26 ?  1009 PRO A CB    1 
ATOM   7583  C CG    . PRO A 1 1011 ? -14.765 65.390  105.192 1.00 13.84 ?  1009 PRO A CG    1 
ATOM   7584  C CD    . PRO A 1 1011 ? -15.592 65.304  103.906 1.00 14.69 ?  1009 PRO A CD    1 
ATOM   7585  N N     . PHE A 1 1012 ? -15.667 69.982  104.762 1.00 13.17 ?  1010 PHE A N     1 
ATOM   7586  C CA    . PHE A 1 1012 ? -15.748 71.252  104.062 1.00 11.79 ?  1010 PHE A CA    1 
ATOM   7587  C C     . PHE A 1 1012 ? -14.686 72.229  104.534 1.00 12.66 ?  1010 PHE A C     1 
ATOM   7588  O O     . PHE A 1 1012 ? -14.557 72.491  105.740 1.00 13.91 ?  1010 PHE A O     1 
ATOM   7589  C CB    . PHE A 1 1012 ? -17.116 71.900  104.245 1.00 12.85 ?  1010 PHE A CB    1 
ATOM   7590  C CG    . PHE A 1 1012 ? -17.275 73.140  103.440 1.00 11.66 ?  1010 PHE A CG    1 
ATOM   7591  C CD1   . PHE A 1 1012 ? -17.483 73.062  102.070 1.00 14.95 ?  1010 PHE A CD1   1 
ATOM   7592  C CD2   . PHE A 1 1012 ? -17.205 74.397  104.037 1.00 13.39 ?  1010 PHE A CD2   1 
ATOM   7593  C CE1   . PHE A 1 1012 ? -17.614 74.211  101.307 1.00 14.15 ?  1010 PHE A CE1   1 
ATOM   7594  C CE2   . PHE A 1 1012 ? -17.336 75.546  103.272 1.00 14.30 ?  1010 PHE A CE2   1 
ATOM   7595  C CZ    . PHE A 1 1012 ? -17.554 75.448  101.903 1.00 15.23 ?  1010 PHE A CZ    1 
ATOM   7596  N N     . GLY A 1 1013 ? -13.974 72.804  103.589 1.00 12.72 ?  1011 GLY A N     1 
ATOM   7597  C CA    . GLY A 1 1013 ? -13.020 73.838  103.930 1.00 13.78 ?  1011 GLY A CA    1 
ATOM   7598  C C     . GLY A 1 1013 ? -11.937 73.896  102.884 1.00 12.82 ?  1011 GLY A C     1 
ATOM   7599  O O     . GLY A 1 1013 ? -11.595 72.903  102.262 1.00 14.95 ?  1011 GLY A O     1 
ATOM   7600  N N     . GLY A 1 1014 ? -11.381 75.095  102.705 1.00 14.84 ?  1012 GLY A N     1 
ATOM   7601  C CA    . GLY A 1 1014 ? -10.371 75.267  101.685 1.00 18.21 ?  1012 GLY A CA    1 
ATOM   7602  C C     . GLY A 1 1014 ? -9.015  75.720  102.169 1.00 17.17 ?  1012 GLY A C     1 
ATOM   7603  O O     . GLY A 1 1014 ? -8.657  75.569  103.344 1.00 20.61 ?  1012 GLY A O     1 
ATOM   7604  N N     . ARG A 1 1015 ? -8.254  76.290  101.243 1.00 15.47 ?  1013 ARG A N     1 
ATOM   7605  C CA    . ARG A 1 1015 ? -6.857  76.623  101.443 1.00 17.02 ?  1013 ARG A CA    1 
ATOM   7606  C C     . ARG A 1 1015 ? -6.623  78.051  100.985 1.00 16.58 ?  1013 ARG A C     1 
ATOM   7607  O O     . ARG A 1 1015 ? -7.514  78.713  100.446 1.00 13.86 ?  1013 ARG A O     1 
ATOM   7608  C CB    . ARG A 1 1015 ? -5.949  75.666  100.668 1.00 17.47 ?  1013 ARG A CB    1 
ATOM   7609  C CG    . ARG A 1 1015 ? -6.205  75.745  99.148  1.00 15.97 ?  1013 ARG A CG    1 
ATOM   7610  C CD    . ARG A 1 1015 ? -5.141  75.034  98.325  1.00 21.11 ?  1013 ARG A CD    1 
ATOM   7611  N NE    . ARG A 1 1015 ? -3.828  75.162  98.939  1.00 25.18 ?  1013 ARG A NE    1 
ATOM   7612  C CZ    . ARG A 1 1015 ? -3.054  76.232  98.832  1.00 27.04 ?  1013 ARG A CZ    1 
ATOM   7613  N NH1   . ARG A 1 1015 ? -3.417  77.276  98.104  1.00 22.22 ?  1013 ARG A NH1   1 
ATOM   7614  N NH2   . ARG A 1 1015 ? -1.896  76.264  99.492  1.00 27.29 ?  1013 ARG A NH2   1 
ATOM   7615  N N     . GLY A 1 1016 ? -5.395  78.512  101.164 1.00 15.45 ?  1014 GLY A N     1 
ATOM   7616  C CA    . GLY A 1 1016 ? -5.063  79.852  100.710 1.00 15.41 ?  1014 GLY A CA    1 
ATOM   7617  C C     . GLY A 1 1016 ? -5.930  80.893  101.402 1.00 15.81 ?  1014 GLY A C     1 
ATOM   7618  O O     . GLY A 1 1016 ? -6.138  80.861  102.623 1.00 16.89 ?  1014 GLY A O     1 
ATOM   7619  N N     . LEU A 1 1017 ? -6.450  81.832  100.604 1.00 15.66 ?  1015 LEU A N     1 
ATOM   7620  C CA    . LEU A 1 1017 ? -7.319  82.895  101.099 1.00 17.59 ?  1015 LEU A CA    1 
ATOM   7621  C C     . LEU A 1 1017 ? -8.652  82.372  101.612 1.00 15.61 ?  1015 LEU A C     1 
ATOM   7622  O O     . LEU A 1 1017 ? -9.431  83.144  102.188 1.00 16.40 ?  1015 LEU A O     1 
ATOM   7623  C CB    . LEU A 1 1017 ? -7.573  83.918  99.988  1.00 17.07 ?  1015 LEU A CB    1 
ATOM   7624  C CG    . LEU A 1 1017 ? -6.362  84.692  99.492  1.00 17.40 ?  1015 LEU A CG    1 
ATOM   7625  C CD1   . LEU A 1 1017 ? -6.782  85.573  98.326  1.00 19.57 ?  1015 LEU A CD1   1 
ATOM   7626  C CD2   . LEU A 1 1017 ? -5.794  85.552  100.618 1.00 19.83 ?  1015 LEU A CD2   1 
ATOM   7627  N N     . SER A 1 1018 ? -8.928  81.089  101.414 1.00 14.39 ?  1016 SER A N     1 
ATOM   7628  C CA    . SER A 1 1018 ? -10.191 80.507  101.823 1.00 15.38 ?  1016 SER A CA    1 
ATOM   7629  C C     . SER A 1 1018 ? -10.158 79.953  103.231 1.00 14.84 ?  1016 SER A C     1 
ATOM   7630  O O     . SER A 1 1018 ? -11.218 79.639  103.775 1.00 16.12 ?  1016 SER A O     1 
ATOM   7631  C CB    . SER A 1 1018 ? -10.602 79.391  100.858 1.00 15.02 ?  1016 SER A CB    1 
ATOM   7632  O OG    . SER A 1 1018 ? -10.813 79.935  99.574  1.00 16.35 ?  1016 SER A OG    1 
ATOM   7633  N N     . GLY A 1 1019 ? -8.999  79.817  103.845 1.00 15.92 ?  1017 GLY A N     1 
ATOM   7634  C CA    . GLY A 1 1019 ? -9.047  79.379  105.223 1.00 22.40 ?  1017 GLY A CA    1 
ATOM   7635  C C     . GLY A 1 1019 ? -7.778  78.713  105.683 1.00 16.82 ?  1017 GLY A C     1 
ATOM   7636  O O     . GLY A 1 1019 ? -6.854  78.455  104.913 1.00 17.93 ?  1017 GLY A O     1 
ATOM   7637  N N     . THR A 1 1020 ? -7.766  78.443  106.985 1.00 16.99 ?  1018 THR A N     1 
ATOM   7638  C CA    . THR A 1 1020 ? -6.644  77.813  107.662 1.00 15.90 ?  1018 THR A CA    1 
ATOM   7639  C C     . THR A 1 1020 ? -6.771  76.306  107.719 1.00 17.08 ?  1018 THR A C     1 
ATOM   7640  O O     . THR A 1 1020 ? -5.759  75.613  107.885 1.00 16.60 ?  1018 THR A O     1 
ATOM   7641  C CB    . THR A 1 1020 ? -6.546  78.318  109.108 1.00 13.78 ?  1018 THR A CB    1 
ATOM   7642  O OG1   . THR A 1 1020 ? -7.792  78.054  109.787 1.00 15.57 ?  1018 THR A OG1   1 
ATOM   7643  C CG2   . THR A 1 1020 ? -6.291  79.811  109.152 1.00 20.46 ?  1018 THR A CG2   1 
ATOM   7644  N N     . GLY A 1 1021 ? -7.992  75.793  107.624 1.00 14.02 ?  1019 GLY A N     1 
ATOM   7645  C CA    . GLY A 1 1021 ? -8.283  74.456  108.066 1.00 16.31 ?  1019 GLY A CA    1 
ATOM   7646  C C     . GLY A 1 1021 ? -8.136  74.341  109.571 1.00 17.37 ?  1019 GLY A C     1 
ATOM   7647  O O     . GLY A 1 1021 ? -7.829  75.318  110.269 1.00 16.48 ?  1019 GLY A O     1 
ATOM   7648  N N     . PRO A 1 1022 ? -8.379  73.140  110.108 1.00 15.25 ?  1020 PRO A N     1 
ATOM   7649  C CA    . PRO A 1 1022 ? -8.817  71.925  109.403 1.00 16.36 ?  1020 PRO A CA    1 
ATOM   7650  C C     . PRO A 1 1022 ? -10.267 72.023  108.926 1.00 15.28 ?  1020 PRO A C     1 
ATOM   7651  O O     . PRO A 1 1022 ? -11.016 72.926  109.307 1.00 17.29 ?  1020 PRO A O     1 
ATOM   7652  C CB    . PRO A 1 1022 ? -8.643  70.827  110.464 1.00 17.08 ?  1020 PRO A CB    1 
ATOM   7653  C CG    . PRO A 1 1022 ? -8.808  71.546  111.771 1.00 18.01 ?  1020 PRO A CG    1 
ATOM   7654  C CD    . PRO A 1 1022 ? -8.157  72.884  111.544 1.00 17.39 ?  1020 PRO A CD    1 
ATOM   7655  N N     . LYS A 1 1023 ? -10.679 71.078  108.089 1.00 13.41 ?  1021 LYS A N     1 
ATOM   7656  C CA    . LYS A 1 1023 ? -12.035 71.086  107.552 1.00 13.34 ?  1021 LYS A CA    1 
ATOM   7657  C C     . LYS A 1 1023 ? -13.077 70.821  108.629 1.00 13.05 ?  1021 LYS A C     1 
ATOM   7658  O O     . LYS A 1 1023 ? -12.939 69.913  109.456 1.00 13.53 ?  1021 LYS A O     1 
ATOM   7659  C CB    . LYS A 1 1023 ? -12.184 70.020  106.469 1.00 14.20 ?  1021 LYS A CB    1 
ATOM   7660  C CG    . LYS A 1 1023 ? -11.484 70.335  105.162 1.00 12.44 ?  1021 LYS A CG    1 
ATOM   7661  C CD    . LYS A 1 1023 ? -11.571 69.099  104.278 1.00 11.83 ?  1021 LYS A CD    1 
ATOM   7662  C CE    . LYS A 1 1023 ? -11.216 69.362  102.808 1.00 14.08 ?  1021 LYS A CE    1 
ATOM   7663  N NZ    . LYS A 1 1023 ? -12.268 70.176  102.136 1.00 12.14 ?  1021 LYS A NZ    1 
ATOM   7664  N N     . ALA A 1 1024 ? -14.149 71.605  108.588 1.00 14.44 ?  1022 ALA A N     1 
ATOM   7665  C CA    . ALA A 1 1024 ? -15.336 71.302  109.366 1.00 12.93 ?  1022 ALA A CA    1 
ATOM   7666  C C     . ALA A 1 1024 ? -15.992 70.034  108.835 1.00 13.81 ?  1022 ALA A C     1 
ATOM   7667  O O     . ALA A 1 1024 ? -15.964 69.749  107.627 1.00 15.69 ?  1022 ALA A O     1 
ATOM   7668  C CB    . ALA A 1 1024 ? -16.316 72.469  109.293 1.00 15.36 ?  1022 ALA A CB    1 
ATOM   7669  N N     . GLY A 1 1025 ? -16.609 69.281  109.738 1.00 13.28 ?  1023 GLY A N     1 
ATOM   7670  C CA    . GLY A 1 1025 ? -17.210 68.029  109.333 1.00 14.57 ?  1023 GLY A CA    1 
ATOM   7671  C C     . GLY A 1 1025 ? -16.217 67.010  108.853 1.00 14.09 ?  1023 GLY A C     1 
ATOM   7672  O O     . GLY A 1 1025 ? -16.578 66.115  108.078 1.00 13.69 ?  1023 GLY A O     1 
ATOM   7673  N N     . GLY A 1 1026 ? -14.962 67.121  109.298 1.00 12.34 ?  1024 GLY A N     1 
ATOM   7674  C CA    . GLY A 1 1026 ? -13.929 66.177  108.938 1.00 12.56 ?  1024 GLY A CA    1 
ATOM   7675  C C     . GLY A 1 1026 ? -13.172 65.721  110.174 1.00 13.32 ?  1024 GLY A C     1 
ATOM   7676  O O     . GLY A 1 1026 ? -13.349 66.246  111.280 1.00 15.11 ?  1024 GLY A O     1 
ATOM   7677  N N     . PRO A 1 1027 ? -12.284 64.741  109.986 1.00 11.86 ?  1025 PRO A N     1 
ATOM   7678  C CA    . PRO A 1 1027 ? -11.695 64.024  111.126 1.00 13.95 ?  1025 PRO A CA    1 
ATOM   7679  C C     . PRO A 1 1027 ? -10.523 64.728  111.801 1.00 11.70 ?  1025 PRO A C     1 
ATOM   7680  O O     . PRO A 1 1027 ? -10.084 64.268  112.864 1.00 14.93 ?  1025 PRO A O     1 
ATOM   7681  C CB    . PRO A 1 1027 ? -11.245 62.694  110.491 1.00 14.47 ?  1025 PRO A CB    1 
ATOM   7682  C CG    . PRO A 1 1027 ? -10.900 63.090  109.072 1.00 15.40 ?  1025 PRO A CG    1 
ATOM   7683  C CD    . PRO A 1 1027 ? -11.945 64.118  108.687 1.00 12.55 ?  1025 PRO A CD    1 
ATOM   7684  N N     . LEU A 1 1028 ? -10.011 65.824  111.240 1.00 12.90 ?  1026 LEU A N     1 
ATOM   7685  C CA    . LEU A 1 1028 ? -8.929  66.576  111.875 1.00 13.93 ?  1026 LEU A CA    1 
ATOM   7686  C C     . LEU A 1 1028 ? -9.427  67.747  112.703 1.00 13.44 ?  1026 LEU A C     1 
ATOM   7687  O O     . LEU A 1 1028 ? -8.625  68.386  113.390 1.00 15.38 ?  1026 LEU A O     1 
ATOM   7688  C CB    . LEU A 1 1028 ? -7.943  67.086  110.818 1.00 13.78 ?  1026 LEU A CB    1 
ATOM   7689  C CG    . LEU A 1 1028 ? -6.995  66.025  110.247 1.00 13.83 ?  1026 LEU A CG    1 
ATOM   7690  C CD1   . LEU A 1 1028 ? -6.353  66.497  108.942 1.00 18.01 ?  1026 LEU A CD1   1 
ATOM   7691  C CD2   . LEU A 1 1028 ? -5.933  65.765  111.300 1.00 17.89 ?  1026 LEU A CD2   1 
ATOM   7692  N N     . TYR A 1 1029 ? -10.737 68.009  112.692 1.00 13.20 ?  1027 TYR A N     1 
ATOM   7693  C CA    . TYR A 1 1029 ? -11.275 69.224  113.299 1.00 14.13 ?  1027 TYR A CA    1 
ATOM   7694  C C     . TYR A 1 1029 ? -11.080 69.240  114.808 1.00 15.17 ?  1027 TYR A C     1 
ATOM   7695  O O     . TYR A 1 1029 ? -10.566 70.216  115.365 1.00 15.30 ?  1027 TYR A O     1 
ATOM   7696  C CB    . TYR A 1 1029 ? -12.754 69.322  112.967 1.00 15.77 ?  1027 TYR A CB    1 
ATOM   7697  C CG    . TYR A 1 1029 ? -13.385 70.691  113.015 1.00 12.99 ?  1027 TYR A CG    1 
ATOM   7698  C CD1   . TYR A 1 1029 ? -12.999 71.683  112.130 1.00 14.64 ?  1027 TYR A CD1   1 
ATOM   7699  C CD2   . TYR A 1 1029 ? -14.420 70.958  113.906 1.00 14.77 ?  1027 TYR A CD2   1 
ATOM   7700  C CE1   . TYR A 1 1029 ? -13.621 72.926  112.131 1.00 15.56 ?  1027 TYR A CE1   1 
ATOM   7701  C CE2   . TYR A 1 1029 ? -15.049 72.203  113.911 1.00 16.28 ?  1027 TYR A CE2   1 
ATOM   7702  C CZ    . TYR A 1 1029 ? -14.646 73.169  113.009 1.00 14.18 ?  1027 TYR A CZ    1 
ATOM   7703  O OH    . TYR A 1 1029 ? -15.257 74.392  112.986 1.00 16.68 ?  1027 TYR A OH    1 
ATOM   7704  N N     . LEU A 1 1030 ? -11.525 68.181  115.493 1.00 13.39 ?  1028 LEU A N     1 
ATOM   7705  C CA    . LEU A 1 1030 ? -11.490 68.190  116.954 1.00 15.09 ?  1028 LEU A CA    1 
ATOM   7706  C C     . LEU A 1 1030 ? -10.064 68.282  117.465 1.00 15.80 ?  1028 LEU A C     1 
ATOM   7707  O O     . LEU A 1 1030 ? -9.824  68.878  118.521 1.00 16.84 ?  1028 LEU A O     1 
ATOM   7708  C CB    . LEU A 1 1030 ? -12.162 66.941  117.514 1.00 18.87 ?  1028 LEU A CB    1 
ATOM   7709  C CG    . LEU A 1 1030 ? -13.661 66.783  117.267 1.00 18.71 ?  1028 LEU A CG    1 
ATOM   7710  C CD1   . LEU A 1 1030 ? -14.185 65.544  117.951 1.00 18.76 ?  1028 LEU A CD1   1 
ATOM   7711  C CD2   . LEU A 1 1030 ? -14.439 68.019  117.723 1.00 20.70 ?  1028 LEU A CD2   1 
ATOM   7712  N N     . GLY A 1 1031 ? -9.107  67.726  116.721 1.00 15.05 ?  1029 GLY A N     1 
ATOM   7713  C CA    . GLY A 1 1031 ? -7.727  67.717  117.173 1.00 19.16 ?  1029 GLY A CA    1 
ATOM   7714  C C     . GLY A 1 1031 ? -7.112  69.092  117.305 1.00 18.01 ?  1029 GLY A C     1 
ATOM   7715  O O     . GLY A 1 1031 ? -6.124  69.254  118.034 1.00 17.85 ?  1029 GLY A O     1 
ATOM   7716  N N     . ARG A 1 1032 ? -7.663  70.085  116.612 1.00 17.15 ?  1030 ARG A N     1 
ATOM   7717  C CA    . ARG A 1 1032 ? -7.187  71.456  116.713 1.00 14.44 ?  1030 ARG A CA    1 
ATOM   7718  C C     . ARG A 1 1032 ? -7.661  72.137  117.994 1.00 16.28 ?  1030 ARG A C     1 
ATOM   7719  O O     . ARG A 1 1032 ? -7.118  73.186  118.370 1.00 18.53 ?  1030 ARG A O     1 
ATOM   7720  C CB    . ARG A 1 1032 ? -7.663  72.240  115.483 1.00 17.26 ?  1030 ARG A CB    1 
ATOM   7721  C CG    . ARG A 1 1032 ? -7.018  73.595  115.307 1.00 17.29 ?  1030 ARG A CG    1 
ATOM   7722  C CD    . ARG A 1 1032 ? -5.566  73.479  114.833 1.00 18.83 ?  1030 ARG A CD    1 
ATOM   7723  N NE    . ARG A 1 1032 ? -5.003  74.793  114.533 1.00 18.74 ?  1030 ARG A NE    1 
ATOM   7724  C CZ    . ARG A 1 1032 ? -3.938  75.313  115.133 1.00 21.69 ?  1030 ARG A CZ    1 
ATOM   7725  N NH1   . ARG A 1 1032 ? -3.297  74.665  116.094 1.00 21.97 ?  1030 ARG A NH1   1 
ATOM   7726  N NH2   . ARG A 1 1032 ? -3.504  76.511  114.757 1.00 24.12 ?  1030 ARG A NH2   1 
ATOM   7727  N N     . LEU A 1 1033 ? -8.643  71.551  118.676 1.00 15.37 ?  1031 LEU A N     1 
ATOM   7728  C CA    . LEU A 1 1033 ? -9.312  72.162  119.812 1.00 15.96 ?  1031 LEU A CA    1 
ATOM   7729  C C     . LEU A 1 1033 ? -8.856  71.579  121.150 1.00 19.26 ?  1031 LEU A C     1 
ATOM   7730  O O     . LEU A 1 1033 ? -9.499  71.820  122.180 1.00 18.68 ?  1031 LEU A O     1 
ATOM   7731  C CB    . LEU A 1 1033 ? -10.826 72.006  119.645 1.00 16.37 ?  1031 LEU A CB    1 
ATOM   7732  C CG    . LEU A 1 1033 ? -11.343 72.577  118.325 1.00 17.81 ?  1031 LEU A CG    1 
ATOM   7733  C CD1   . LEU A 1 1033 ? -12.853 72.379  118.177 1.00 17.91 ?  1031 LEU A CD1   1 
ATOM   7734  C CD2   . LEU A 1 1033 ? -10.979 74.043  118.205 1.00 23.48 ?  1031 LEU A CD2   1 
ATOM   7735  N N     . VAL A 1 1034 ? -7.775  70.795  121.141 1.00 18.26 ?  1032 VAL A N     1 
ATOM   7736  C CA    . VAL A 1 1034 ? -7.153  70.247  122.339 1.00 18.23 ?  1032 VAL A CA    1 
ATOM   7737  C C     . VAL A 1 1034 ? -5.667  70.572  122.278 1.00 20.12 ?  1032 VAL A C     1 
ATOM   7738  O O     . VAL A 1 1034 ? -5.136  70.938  121.230 1.00 19.79 ?  1032 VAL A O     1 
ATOM   7739  C CB    . VAL A 1 1034 ? -7.370  68.726  122.456 1.00 19.58 ?  1032 VAL A CB    1 
ATOM   7740  C CG1   . VAL A 1 1034 ? -8.854  68.409  122.741 1.00 20.04 ?  1032 VAL A CG1   1 
ATOM   7741  C CG2   . VAL A 1 1034 ? -6.892  68.031  121.177 1.00 18.68 ?  1032 VAL A CG2   1 
ATOM   7742  N N     . THR A 1 1035 ? -4.986  70.421  123.418 1.00 20.95 ?  1033 THR A N     1 
ATOM   7743  C CA    . THR A 1 1035 ? -3.574  70.798  123.470 1.00 22.96 ?  1033 THR A CA    1 
ATOM   7744  C C     . THR A 1 1035 ? -2.696  69.775  122.757 1.00 25.66 ?  1033 THR A C     1 
ATOM   7745  O O     . THR A 1 1035 ? -1.710  70.144  122.109 1.00 27.88 ?  1033 THR A O     1 
ATOM   7746  C CB    . THR A 1 1035 ? -3.123  70.993  124.922 1.00 25.41 ?  1033 THR A CB    1 
ATOM   7747  O OG1   . THR A 1 1035 ? -3.357  69.798  125.682 1.00 35.12 ?  1033 THR A OG1   1 
ATOM   7748  C CG2   . THR A 1 1035 ? -3.898  72.119  125.556 1.00 22.72 ?  1033 THR A CG2   1 
ATOM   7749  N N     . THR A 1 1036 ? -3.048  68.495  122.840 1.00 20.85 ?  1034 THR A N     1 
ATOM   7750  C CA    . THR A 1 1036 ? -2.321  67.420  122.176 1.00 23.05 ?  1034 THR A CA    1 
ATOM   7751  C C     . THR A 1 1036 ? -3.319  66.673  121.306 1.00 20.65 ?  1034 THR A C     1 
ATOM   7752  O O     . THR A 1 1036 ? -4.284  66.108  121.829 1.00 21.44 ?  1034 THR A O     1 
ATOM   7753  C CB    . THR A 1 1036 ? -1.674  66.475  123.192 1.00 26.60 ?  1034 THR A CB    1 
ATOM   7754  O OG1   . THR A 1 1036 ? -0.913  67.237  124.145 1.00 26.93 ?  1034 THR A OG1   1 
ATOM   7755  C CG2   . THR A 1 1036 ? -0.752  65.483  122.492 1.00 29.82 ?  1034 THR A CG2   1 
ATOM   7756  N N     . ALA A 1 1037 ? -3.083  66.671  119.993 1.00 19.47 ?  1035 ALA A N     1 
ATOM   7757  C CA    . ALA A 1 1037 ? -4.061  66.133  119.055 1.00 18.69 ?  1035 ALA A CA    1 
ATOM   7758  C C     . ALA A 1 1037 ? -4.064  64.606  119.096 1.00 19.99 ?  1035 ALA A C     1 
ATOM   7759  O O     . ALA A 1 1037 ? -3.000  63.982  119.176 1.00 20.54 ?  1035 ALA A O     1 
ATOM   7760  C CB    . ALA A 1 1037 ? -3.760  66.611  117.638 1.00 20.72 ?  1035 ALA A CB    1 
ATOM   7761  N N     . PRO A 1 1038 ? -5.234  63.981  119.074 1.00 17.84 ?  1036 PRO A N     1 
ATOM   7762  C CA    . PRO A 1 1038 ? -5.303  62.523  118.976 1.00 17.20 ?  1036 PRO A CA    1 
ATOM   7763  C C     . PRO A 1 1038 ? -5.044  62.082  117.543 1.00 17.95 ?  1036 PRO A C     1 
ATOM   7764  O O     . PRO A 1 1038 ? -4.985  62.888  116.620 1.00 17.25 ?  1036 PRO A O     1 
ATOM   7765  C CB    . PRO A 1 1038 ? -6.745  62.220  119.379 1.00 18.24 ?  1036 PRO A CB    1 
ATOM   7766  C CG    . PRO A 1 1038 ? -7.491  63.389  118.831 1.00 19.73 ?  1036 PRO A CG    1 
ATOM   7767  C CD    . PRO A 1 1038 ? -6.578  64.587  119.106 1.00 20.47 ?  1036 PRO A CD    1 
ATOM   7768  N N     . VAL A 1 1039 ? -4.909  60.771  117.375 1.00 16.56 ?  1037 VAL A N     1 
ATOM   7769  C CA    . VAL A 1 1039 ? -4.828  60.182  116.038 1.00 16.10 ?  1037 VAL A CA    1 
ATOM   7770  C C     . VAL A 1 1039 ? -6.247  60.009  115.512 1.00 13.86 ?  1037 VAL A C     1 
ATOM   7771  O O     . VAL A 1 1039 ? -7.015  59.222  116.088 1.00 16.43 ?  1037 VAL A O     1 
ATOM   7772  C CB    . VAL A 1 1039 ? -4.097  58.832  116.072 1.00 15.53 ?  1037 VAL A CB    1 
ATOM   7773  C CG1   . VAL A 1 1039 ? -4.018  58.232  114.687 1.00 18.43 ?  1037 VAL A CG1   1 
ATOM   7774  C CG2   . VAL A 1 1039 ? -2.716  58.991  116.689 1.00 19.99 ?  1037 VAL A CG2   1 
ATOM   7775  N N     . PRO A 1 1040 ? -6.651  60.714  114.457 1.00 14.36 ?  1038 PRO A N     1 
ATOM   7776  C CA    . PRO A 1 1040 ? -8.020  60.577  113.970 1.00 16.93 ?  1038 PRO A CA    1 
ATOM   7777  C C     . PRO A 1 1040 ? -8.272  59.182  113.429 1.00 16.65 ?  1038 PRO A C     1 
ATOM   7778  O O     . PRO A 1 1040 ? -7.327  58.469  113.054 1.00 14.88 ?  1038 PRO A O     1 
ATOM   7779  C CB    . PRO A 1 1040 ? -8.120  61.636  112.856 1.00 15.36 ?  1038 PRO A CB    1 
ATOM   7780  C CG    . PRO A 1 1040 ? -6.979  62.570  113.078 1.00 18.27 ?  1038 PRO A CG    1 
ATOM   7781  C CD    . PRO A 1 1040 ? -5.889  61.724  113.705 1.00 15.98 ?  1038 PRO A CD    1 
ATOM   7782  N N     . PRO A 1 1041 ? -9.531  58.757  113.381 1.00 14.98 ?  1039 PRO A N     1 
ATOM   7783  C CA    . PRO A 1 1041 ? -9.867  57.499  112.710 1.00 14.51 ?  1039 PRO A CA    1 
ATOM   7784  C C     . PRO A 1 1041 ? -9.354  57.489  111.278 1.00 15.14 ?  1039 PRO A C     1 
ATOM   7785  O O     . PRO A 1 1041 ? -9.414  58.498  110.568 1.00 14.73 ?  1039 PRO A O     1 
ATOM   7786  C CB    . PRO A 1 1041 ? -11.401 57.469  112.752 1.00 17.56 ?  1039 PRO A CB    1 
ATOM   7787  C CG    . PRO A 1 1041 ? -11.781 58.445  113.819 1.00 20.77 ?  1039 PRO A CG    1 
ATOM   7788  C CD    . PRO A 1 1041 ? -10.741 59.505  113.785 1.00 18.71 ?  1039 PRO A CD    1 
ATOM   7789  N N     . GLN A 1 1042 ? -8.832  56.330  110.869 1.00 14.96 ?  1040 GLN A N     1 
ATOM   7790  C CA    . GLN A 1 1042 ? -8.361  56.060  109.513 1.00 14.94 ?  1040 GLN A CA    1 
ATOM   7791  C C     . GLN A 1 1042 ? -7.189  56.938  109.093 1.00 15.03 ?  1040 GLN A C     1 
ATOM   7792  O O     . GLN A 1 1042 ? -6.813  56.936  107.917 1.00 15.78 ?  1040 GLN A O     1 
ATOM   7793  C CB    . GLN A 1 1042 ? -9.490  56.219  108.482 1.00 18.36 ?  1040 GLN A CB    1 
ATOM   7794  C CG    . GLN A 1 1042 ? -10.746 55.466  108.835 1.00 20.25 ?  1040 GLN A CG    1 
ATOM   7795  C CD    . GLN A 1 1042 ? -11.808 55.647  107.764 1.00 24.23 ?  1040 GLN A CD    1 
ATOM   7796  O OE1   . GLN A 1 1042 ? -12.059 54.741  106.981 1.00 35.23 ?  1040 GLN A OE1   1 
ATOM   7797  N NE2   . GLN A 1 1042 ? -12.412 56.832  107.709 1.00 30.52 ?  1040 GLN A NE2   1 
ATOM   7798  N N     . HIS A 1 1043 ? -6.556  57.648  110.028 1.00 14.33 ?  1041 HIS A N     1 
ATOM   7799  C CA    . HIS A 1 1043 ? -5.560  58.662  109.675 1.00 12.95 ?  1041 HIS A CA    1 
ATOM   7800  C C     . HIS A 1 1043 ? -4.170  58.030  109.711 1.00 13.98 ?  1041 HIS A C     1 
ATOM   7801  O O     . HIS A 1 1043 ? -3.549  57.926  110.774 1.00 14.80 ?  1041 HIS A O     1 
ATOM   7802  C CB    . HIS A 1 1043 ? -5.676  59.841  110.637 1.00 14.61 ?  1041 HIS A CB    1 
ATOM   7803  C CG    . HIS A 1 1043 ? -4.697  60.944  110.390 1.00 13.99 ?  1041 HIS A CG    1 
ATOM   7804  N ND1   . HIS A 1 1043 ? -4.973  62.031  109.586 1.00 13.73 ?  1041 HIS A ND1   1 
ATOM   7805  C CD2   . HIS A 1 1043 ? -3.456  61.153  110.892 1.00 14.17 ?  1041 HIS A CD2   1 
ATOM   7806  C CE1   . HIS A 1 1043 ? -3.937  62.850  109.586 1.00 14.17 ?  1041 HIS A CE1   1 
ATOM   7807  N NE2   . HIS A 1 1043 ? -3.003  62.340  110.372 1.00 14.60 ?  1041 HIS A NE2   1 
ATOM   7808  N N     . SER A 1 1044 ? -3.682  57.603  108.546 1.00 11.85 ?  1042 SER A N     1 
ATOM   7809  C CA    . SER A 1 1044 ? -2.341  57.042  108.388 1.00 13.59 ?  1042 SER A CA    1 
ATOM   7810  C C     . SER A 1 1044 ? -2.048  56.960  106.896 1.00 13.44 ?  1042 SER A C     1 
ATOM   7811  O O     . SER A 1 1044 ? -2.942  57.109  106.062 1.00 14.22 ?  1042 SER A O     1 
ATOM   7812  C CB    . SER A 1 1044 ? -2.212  55.659  109.023 1.00 15.37 ?  1042 SER A CB    1 
ATOM   7813  O OG    . SER A 1 1044 ? -2.984  54.712  108.304 1.00 14.11 ?  1042 SER A OG    1 
ATOM   7814  N N     . SER A 1 1045 ? -0.782  56.685  106.573 1.00 13.05 ?  1043 SER A N     1 
ATOM   7815  C CA    . SER A 1 1045 ? -0.387  56.469  105.189 1.00 11.96 ?  1043 SER A CA    1 
ATOM   7816  C C     . SER A 1 1045 ? 0.821   55.548  105.148 1.00 12.04 ?  1043 SER A C     1 
ATOM   7817  O O     . SER A 1 1045 ? 1.749   55.711  105.941 1.00 13.30 ?  1043 SER A O     1 
ATOM   7818  C CB    . SER A 1 1045 ? -0.046  57.789  104.510 1.00 12.19 ?  1043 SER A CB    1 
ATOM   7819  O OG    . SER A 1 1045 ? 0.476   57.540  103.219 1.00 12.98 ?  1043 SER A OG    1 
ATOM   7820  N N     . VAL A 1 1046 ? 0.814   54.598  104.206 1.00 12.94 ?  1044 VAL A N     1 
ATOM   7821  C CA    . VAL A 1 1046 ? 1.970   53.718  104.055 1.00 14.11 ?  1044 VAL A CA    1 
ATOM   7822  C C     . VAL A 1 1046 ? 3.047   54.334  103.188 1.00 13.14 ?  1044 VAL A C     1 
ATOM   7823  O O     . VAL A 1 1046 ? 4.114   53.729  103.040 1.00 15.28 ?  1044 VAL A O     1 
ATOM   7824  C CB    . VAL A 1 1046 ? 1.619   52.339  103.460 1.00 14.37 ?  1044 VAL A CB    1 
ATOM   7825  C CG1   . VAL A 1 1046 ? 0.640   51.613  104.367 1.00 16.96 ?  1044 VAL A CG1   1 
ATOM   7826  C CG2   . VAL A 1 1046 ? 1.081   52.473  102.057 1.00 14.44 ?  1044 VAL A CG2   1 
ATOM   7827  N N     . HIS A 1 1047 ? 2.813   55.518  102.629 1.00 12.88 ?  1045 HIS A N     1 
ATOM   7828  C CA    . HIS A 1 1047 ? 3.754   56.136  101.714 1.00 13.00 ?  1045 HIS A CA    1 
ATOM   7829  C C     . HIS A 1 1047 ? 4.714   57.037  102.472 1.00 15.38 ?  1045 HIS A C     1 
ATOM   7830  O O     . HIS A 1 1047 ? 4.345   57.672  103.463 1.00 15.53 ?  1045 HIS A O     1 
ATOM   7831  C CB    . HIS A 1 1047 ? 2.979   56.892  100.647 1.00 14.89 ?  1045 HIS A CB    1 
ATOM   7832  C CG    . HIS A 1 1047 ? 2.003   56.006  99.940  1.00 18.25 ?  1045 HIS A CG    1 
ATOM   7833  N ND1   . HIS A 1 1047 ? 2.407   54.988  99.096  1.00 20.69 ?  1045 HIS A ND1   1 
ATOM   7834  C CD2   . HIS A 1 1047 ? 0.652   55.920  100.017 1.00 21.58 ?  1045 HIS A CD2   1 
ATOM   7835  C CE1   . HIS A 1 1047 ? 1.341   54.349  98.644  1.00 22.23 ?  1045 HIS A CE1   1 
ATOM   7836  N NE2   . HIS A 1 1047 ? 0.264   54.898  99.184  1.00 23.29 ?  1045 HIS A NE2   1 
ATOM   7837  N N     . THR A 1 1048 ? 5.968   57.026  102.044 1.00 14.18 ?  1046 THR A N     1 
ATOM   7838  C CA    . THR A 1 1048 ? 7.013   57.832  102.653 1.00 14.02 ?  1046 THR A CA    1 
ATOM   7839  C C     . THR A 1 1048 ? 7.511   58.826  101.617 1.00 13.55 ?  1046 THR A C     1 
ATOM   7840  O O     . THR A 1 1048 ? 7.856   58.437  100.497 1.00 16.04 ?  1046 THR A O     1 
ATOM   7841  C CB    . THR A 1 1048 ? 8.163   56.967  103.146 1.00 14.65 ?  1046 THR A CB    1 
ATOM   7842  O OG1   . THR A 1 1048 ? 7.642   55.938  104.000 1.00 17.01 ?  1046 THR A OG1   1 
ATOM   7843  C CG2   . THR A 1 1048 ? 9.167   57.824  103.939 1.00 18.02 ?  1046 THR A CG2   1 
ATOM   7844  N N     . ASP A 1 1049 ? 7.569   60.095  101.988 1.00 13.86 ?  1047 ASP A N     1 
ATOM   7845  C CA    . ASP A 1 1049 ? 8.005   61.111  101.043 1.00 11.91 ?  1047 ASP A CA    1 
ATOM   7846  C C     . ASP A 1 1049 ? 9.467   60.875  100.660 1.00 13.42 ?  1047 ASP A C     1 
ATOM   7847  O O     . ASP A 1 1049 ? 10.306  60.679  101.544 1.00 13.48 ?  1047 ASP A O     1 
ATOM   7848  C CB    . ASP A 1 1049 ? 7.819   62.502  101.659 1.00 12.16 ?  1047 ASP A CB    1 
ATOM   7849  C CG    . ASP A 1 1049 ? 8.261   63.606  100.724 1.00 13.91 ?  1047 ASP A CG    1 
ATOM   7850  O OD1   . ASP A 1 1049 ? 9.486   63.850  100.627 1.00 14.74 ?  1047 ASP A OD1   1 
ATOM   7851  O OD2   . ASP A 1 1049 ? 7.381   64.189  100.040 1.00 15.73 ?  1047 ASP A OD2   1 
ATOM   7852  N N     . PRO A 1 1050 ? 9.812   60.880  99.367  1.00 13.33 ?  1048 PRO A N     1 
ATOM   7853  C CA    . PRO A 1 1050 ? 11.186  60.511  98.981  1.00 13.43 ?  1048 PRO A CA    1 
ATOM   7854  C C     . PRO A 1 1050 ? 12.207  61.595  99.267  1.00 14.17 ?  1048 PRO A C     1 
ATOM   7855  O O     . PRO A 1 1050 ? 13.397  61.284  99.428  1.00 15.16 ?  1048 PRO A O     1 
ATOM   7856  C CB    . PRO A 1 1050 ? 11.064  60.239  97.474  1.00 15.42 ?  1048 PRO A CB    1 
ATOM   7857  C CG    . PRO A 1 1050 ? 9.927   61.097  97.051  1.00 15.59 ?  1048 PRO A CG    1 
ATOM   7858  C CD    . PRO A 1 1050 ? 8.939   61.077  98.199  1.00 14.28 ?  1048 PRO A CD    1 
ATOM   7859  N N     . VAL A 1 1051 ? 11.786  62.858  99.298  1.00 12.67 ?  1049 VAL A N     1 
ATOM   7860  C CA    . VAL A 1 1051 ? 12.715  63.924  99.645  1.00 13.34 ?  1049 VAL A CA    1 
ATOM   7861  C C     . VAL A 1 1051 ? 13.022  63.875  101.134 1.00 14.17 ?  1049 VAL A C     1 
ATOM   7862  O O     . VAL A 1 1051 ? 14.168  64.082  101.551 1.00 14.41 ?  1049 VAL A O     1 
ATOM   7863  C CB    . VAL A 1 1051 ? 12.150  65.285  99.212  1.00 13.87 ?  1049 VAL A CB    1 
ATOM   7864  C CG1   . VAL A 1 1051 ? 13.128  66.387  99.539  1.00 16.19 ?  1049 VAL A CG1   1 
ATOM   7865  C CG2   . VAL A 1 1051 ? 11.846  65.262  97.699  1.00 15.94 ?  1049 VAL A CG2   1 
ATOM   7866  N N     . LEU A 1 1052 ? 12.016  63.570  101.958 1.00 12.34 ?  1050 LEU A N     1 
ATOM   7867  C CA    . LEU A 1 1052 ? 12.280  63.263  103.364 1.00 12.72 ?  1050 LEU A CA    1 
ATOM   7868  C C     . LEU A 1 1052 ? 13.352  62.187  103.500 1.00 13.89 ?  1050 LEU A C     1 
ATOM   7869  O O     . LEU A 1 1052 ? 14.290  62.326  104.296 1.00 12.88 ?  1050 LEU A O     1 
ATOM   7870  C CB    . LEU A 1 1052 ? 10.978  62.834  104.054 1.00 14.11 ?  1050 LEU A CB    1 
ATOM   7871  C CG    . LEU A 1 1052 ? 11.015  62.434  105.541 1.00 11.52 ?  1050 LEU A CG    1 
ATOM   7872  C CD1   . LEU A 1 1052 ? 11.573  61.026  105.764 1.00 12.95 ?  1050 LEU A CD1   1 
ATOM   7873  C CD2   . LEU A 1 1052 ? 11.753  63.469  106.415 1.00 14.04 ?  1050 LEU A CD2   1 
ATOM   7874  N N     . LEU A 1 1053 ? 13.226  61.098  102.732 1.00 13.78 ?  1051 LEU A N     1 
ATOM   7875  C CA    . LEU A 1 1053 ? 14.192  60.014  102.843 1.00 14.54 ?  1051 LEU A CA    1 
ATOM   7876  C C     . LEU A 1 1053 ? 15.580  60.478  102.434 1.00 13.42 ?  1051 LEU A C     1 
ATOM   7877  O O     . LEU A 1 1053 ? 16.572  60.127  103.080 1.00 14.28 ?  1051 LEU A O     1 
ATOM   7878  C CB    . LEU A 1 1053 ? 13.753  58.812  101.994 1.00 13.98 ?  1051 LEU A CB    1 
ATOM   7879  C CG    . LEU A 1 1053 ? 12.565  58.027  102.573 1.00 16.28 ?  1051 LEU A CG    1 
ATOM   7880  C CD1   . LEU A 1 1053 ? 12.048  57.024  101.541 1.00 14.47 ?  1051 LEU A CD1   1 
ATOM   7881  C CD2   . LEU A 1 1053 ? 12.909  57.338  103.877 1.00 18.49 ?  1051 LEU A CD2   1 
ATOM   7882  N N     . ASP A 1 1054 ? 15.666  61.287  101.376 1.00 12.85 ?  1052 ASP A N     1 
ATOM   7883  C CA    . ASP A 1 1054 ? 16.961  61.802  100.946 1.00 14.52 ?  1052 ASP A CA    1 
ATOM   7884  C C     . ASP A 1 1054 ? 17.559  62.716  102.003 1.00 14.81 ?  1052 ASP A C     1 
ATOM   7885  O O     . ASP A 1 1054 ? 18.772  62.718  102.212 1.00 16.02 ?  1052 ASP A O     1 
ATOM   7886  C CB    . ASP A 1 1054 ? 16.826  62.549  99.621  1.00 15.13 ?  1052 ASP A CB    1 
ATOM   7887  C CG    . ASP A 1 1054 ? 16.587  61.620  98.441  1.00 17.40 ?  1052 ASP A CG    1 
ATOM   7888  O OD1   . ASP A 1 1054 ? 16.651  60.380  98.619  1.00 17.75 ?  1052 ASP A OD1   1 
ATOM   7889  O OD2   . ASP A 1 1054 ? 16.324  62.151  97.340  1.00 20.11 ?  1052 ASP A OD2   1 
ATOM   7890  N N     . PHE A 1 1055 ? 16.716  63.497  102.679 1.00 13.19 ?  1053 PHE A N     1 
ATOM   7891  C CA    . PHE A 1 1055 ? 17.198  64.365  103.748 1.00 14.18 ?  1053 PHE A CA    1 
ATOM   7892  C C     . PHE A 1 1055 ? 17.705  63.551  104.934 1.00 14.61 ?  1053 PHE A C     1 
ATOM   7893  O O     . PHE A 1 1055 ? 18.751  63.872  105.516 1.00 14.85 ?  1053 PHE A O     1 
ATOM   7894  C CB    . PHE A 1 1055 ? 16.074  65.320  104.166 1.00 14.65 ?  1053 PHE A CB    1 
ATOM   7895  C CG    . PHE A 1 1055 ? 16.444  66.255  105.290 1.00 14.40 ?  1053 PHE A CG    1 
ATOM   7896  C CD1   . PHE A 1 1055 ? 17.512  67.127  105.156 1.00 17.33 ?  1053 PHE A CD1   1 
ATOM   7897  C CD2   . PHE A 1 1055 ? 15.688  66.290  106.448 1.00 15.16 ?  1053 PHE A CD2   1 
ATOM   7898  C CE1   . PHE A 1 1055 ? 17.848  68.001  106.188 1.00 18.76 ?  1053 PHE A CE1   1 
ATOM   7899  C CE2   . PHE A 1 1055 ? 16.024  67.168  107.495 1.00 16.62 ?  1053 PHE A CE2   1 
ATOM   7900  C CZ    . PHE A 1 1055 ? 17.095  68.013  107.356 1.00 16.08 ?  1053 PHE A CZ    1 
ATOM   7901  N N     . ALA A 1 1056 ? 16.986  62.489  105.307 1.00 14.47 ?  1054 ALA A N     1 
ATOM   7902  C CA    . ALA A 1 1056 ? 17.455  61.641  106.398 1.00 14.50 ?  1054 ALA A CA    1 
ATOM   7903  C C     . ALA A 1 1056 ? 18.812  61.036  106.072 1.00 16.75 ?  1054 ALA A C     1 
ATOM   7904  O O     . ALA A 1 1056 ? 19.680  60.937  106.941 1.00 17.19 ?  1054 ALA A O     1 
ATOM   7905  C CB    . ALA A 1 1056 ? 16.437  60.540  106.693 1.00 17.31 ?  1054 ALA A CB    1 
ATOM   7906  N N     . LYS A 1 1057 ? 19.015  60.632  104.818 1.00 15.50 ?  1055 LYS A N     1 
ATOM   7907  C CA    . LYS A 1 1057 ? 20.319  60.104  104.421 1.00 17.15 ?  1055 LYS A CA    1 
ATOM   7908  C C     . LYS A 1 1057 ? 21.394  61.180  104.480 1.00 16.87 ?  1055 LYS A C     1 
ATOM   7909  O O     . LYS A 1 1057 ? 22.527  60.912  104.907 1.00 18.95 ?  1055 LYS A O     1 
ATOM   7910  C CB    . LYS A 1 1057 ? 20.229  59.501  103.019 1.00 18.99 ?  1055 LYS A CB    1 
ATOM   7911  C CG    . LYS A 1 1057 ? 19.676  58.091  103.042 1.00 22.32 ?  1055 LYS A CG    1 
ATOM   7912  C CD    . LYS A 1 1057 ? 19.825  57.405  101.687 1.00 23.41 ?  1055 LYS A CD    1 
ATOM   7913  C CE    . LYS A 1 1057 ? 19.153  58.226  100.604 1.00 26.15 ?  1055 LYS A CE    1 
ATOM   7914  N NZ    . LYS A 1 1057 ? 19.046  57.451  99.336  1.00 28.38 ?  1055 LYS A NZ    1 
ATOM   7915  N N     . TRP A 1 1058 ? 21.059  62.400  104.055 1.00 17.49 ?  1056 TRP A N     1 
ATOM   7916  C CA    . TRP A 1 1058 ? 21.990  63.518  104.188 1.00 17.27 ?  1056 TRP A CA    1 
ATOM   7917  C C     . TRP A 1 1058 ? 22.342  63.772  105.649 1.00 18.91 ?  1056 TRP A C     1 
ATOM   7918  O O     . TRP A 1 1058 ? 23.515  63.986  105.981 1.00 21.30 ?  1056 TRP A O     1 
ATOM   7919  C CB    . TRP A 1 1058 ? 21.395  64.771  103.549 1.00 18.42 ?  1056 TRP A CB    1 
ATOM   7920  C CG    . TRP A 1 1058 ? 22.248  66.015  103.681 1.00 19.00 ?  1056 TRP A CG    1 
ATOM   7921  C CD1   . TRP A 1 1058 ? 23.263  66.413  102.850 1.00 24.34 ?  1056 TRP A CD1   1 
ATOM   7922  C CD2   . TRP A 1 1058 ? 22.133  67.033  104.688 1.00 21.48 ?  1056 TRP A CD2   1 
ATOM   7923  N NE1   . TRP A 1 1058 ? 23.789  67.611  103.285 1.00 24.42 ?  1056 TRP A NE1   1 
ATOM   7924  C CE2   . TRP A 1 1058 ? 23.112  68.012  104.408 1.00 20.88 ?  1056 TRP A CE2   1 
ATOM   7925  C CE3   . TRP A 1 1058 ? 21.297  67.211  105.796 1.00 21.75 ?  1056 TRP A CE3   1 
ATOM   7926  C CZ2   . TRP A 1 1058 ? 23.285  69.148  105.204 1.00 23.38 ?  1056 TRP A CZ2   1 
ATOM   7927  C CZ3   . TRP A 1 1058 ? 21.470  68.341  106.586 1.00 22.72 ?  1056 TRP A CZ3   1 
ATOM   7928  C CH2   . TRP A 1 1058 ? 22.459  69.293  106.284 1.00 23.99 ?  1056 TRP A CH2   1 
ATOM   7929  N N     . LEU A 1 1059 ? 21.347  63.723  106.542 1.00 17.07 ?  1057 LEU A N     1 
ATOM   7930  C CA    . LEU A 1 1059 ? 21.633  63.887  107.966 1.00 19.82 ?  1057 LEU A CA    1 
ATOM   7931  C C     . LEU A 1 1059 ? 22.599  62.823  108.461 1.00 21.37 ?  1057 LEU A C     1 
ATOM   7932  O O     . LEU A 1 1059 ? 23.564  63.132  109.170 1.00 20.92 ?  1057 LEU A O     1 
ATOM   7933  C CB    . LEU A 1 1059 ? 20.339  63.844  108.778 1.00 17.74 ?  1057 LEU A CB    1 
ATOM   7934  C CG    . LEU A 1 1059 ? 19.477  65.090  108.650 1.00 16.35 ?  1057 LEU A CG    1 
ATOM   7935  C CD1   . LEU A 1 1059 ? 18.090  64.844  109.218 1.00 15.54 ?  1057 LEU A CD1   1 
ATOM   7936  C CD2   . LEU A 1 1059 ? 20.153  66.265  109.382 1.00 18.53 ?  1057 LEU A CD2   1 
ATOM   7937  N N     . ASP A 1 1060 ? 22.345  61.556  108.114 1.00 18.33 ?  1058 ASP A N     1 
ATOM   7938  C CA    . ASP A 1 1060 ? 23.269  60.492  108.500 1.00 20.24 ?  1058 ASP A CA    1 
ATOM   7939  C C     . ASP A 1 1060 ? 24.676  60.775  107.985 1.00 19.37 ?  1058 ASP A C     1 
ATOM   7940  O O     . ASP A 1 1060 ? 25.660  60.572  108.708 1.00 24.09 ?  1058 ASP A O     1 
ATOM   7941  C CB    . ASP A 1 1060 ? 22.771  59.143  107.977 1.00 24.10 ?  1058 ASP A CB    1 
ATOM   7942  C CG    . ASP A 1 1060 ? 21.801  58.463  108.930 1.00 23.57 ?  1058 ASP A CG    1 
ATOM   7943  O OD1   . ASP A 1 1060 ? 21.996  58.563  110.156 1.00 32.29 ?  1058 ASP A OD1   1 
ATOM   7944  O OD2   . ASP A 1 1060 ? 20.849  57.814  108.440 1.00 31.91 ?  1058 ASP A OD2   1 
ATOM   7945  N N     . GLY A 1 1061 ? 24.793  61.264  106.748 1.00 21.03 ?  1059 GLY A N     1 
ATOM   7946  C CA    . GLY A 1 1061 ? 26.106  61.556  106.196 1.00 22.62 ?  1059 GLY A CA    1 
ATOM   7947  C C     . GLY A 1 1061 ? 26.826  62.690  106.901 1.00 26.38 ?  1059 GLY A C     1 
ATOM   7948  O O     . GLY A 1 1061 ? 28.061  62.707  106.952 1.00 30.81 ?  1059 GLY A O     1 
ATOM   7949  N N     . LYS A 1 1062 ? 26.079  63.656  107.434 1.00 25.09 ?  1060 LYS A N     1 
ATOM   7950  C CA    . LYS A 1 1062 ? 26.660  64.741  108.212 1.00 26.20 ?  1060 LYS A CA    1 
ATOM   7951  C C     . LYS A 1 1062 ? 26.934  64.336  109.653 1.00 25.62 ?  1060 LYS A C     1 
ATOM   7952  O O     . LYS A 1 1062 ? 27.503  65.133  110.408 1.00 30.20 ?  1060 LYS A O     1 
ATOM   7953  C CB    . LYS A 1 1062 ? 25.738  65.966  108.192 1.00 27.21 ?  1060 LYS A CB    1 
ATOM   7954  C CG    . LYS A 1 1062 ? 25.563  66.636  106.825 1.00 27.04 ?  1060 LYS A CG    1 
ATOM   7955  C CD    . LYS A 1 1062 ? 26.852  67.316  106.374 1.00 32.06 ?  1060 LYS A CD    1 
ATOM   7956  C CE    . LYS A 1 1062 ? 26.664  68.099  105.077 1.00 36.03 ?  1060 LYS A CE    1 
ATOM   7957  N NZ    . LYS A 1 1062 ? 27.950  68.662  104.564 1.00 38.93 ?  1060 LYS A NZ    1 
ATOM   7958  N N     . GLY A 1 1063 ? 26.545  63.127  110.049 1.00 23.70 ?  1061 GLY A N     1 
ATOM   7959  C CA    . GLY A 1 1063 ? 26.730  62.656  111.406 1.00 23.88 ?  1061 GLY A CA    1 
ATOM   7960  C C     . GLY A 1 1063 ? 25.625  63.008  112.380 1.00 24.91 ?  1061 GLY A C     1 
ATOM   7961  O O     . GLY A 1 1063 ? 25.784  62.775  113.587 1.00 24.11 ?  1061 GLY A O     1 
ATOM   7962  N N     . ALA A 1 1064 ? 24.510  63.564  111.905 1.00 22.99 ?  1062 ALA A N     1 
ATOM   7963  C CA    . ALA A 1 1064 ? 23.417  63.967  112.789 1.00 20.46 ?  1062 ALA A CA    1 
ATOM   7964  C C     . ALA A 1 1064 ? 22.442  62.802  112.953 1.00 20.91 ?  1062 ALA A C     1 
ATOM   7965  O O     . ALA A 1 1064 ? 21.321  62.801  112.432 1.00 18.05 ?  1062 ALA A O     1 
ATOM   7966  C CB    . ALA A 1 1064 ? 22.735  65.216  112.247 1.00 23.00 ?  1062 ALA A CB    1 
ATOM   7967  N N     . ARG A 1 1065 ? 22.909  61.787  113.689 1.00 19.66 ?  1063 ARG A N     1 
ATOM   7968  C CA    . ARG A 1 1065 ? 22.184  60.520  113.771 1.00 22.65 ?  1063 ARG A CA    1 
ATOM   7969  C C     . ARG A 1 1065 ? 20.850  60.685  114.490 1.00 22.59 ?  1063 ARG A C     1 
ATOM   7970  O O     . ARG A 1 1065 ? 19.837  60.127  114.056 1.00 20.02 ?  1063 ARG A O     1 
ATOM   7971  C CB    . ARG A 1 1065 ? 23.060  59.455  114.448 1.00 23.69 ?  1063 ARG A CB    1 
ATOM   7972  C CG    . ARG A 1 1065 ? 22.317  58.395  115.279 1.00 28.05 ?  1063 ARG A CG    1 
ATOM   7973  C CD    . ARG A 1 1065 ? 21.467  57.419  114.468 1.00 36.95 ?  1063 ARG A CD    1 
ATOM   7974  N NE    . ARG A 1 1065 ? 20.238  57.088  115.190 1.00 41.01 ?  1063 ARG A NE    1 
ATOM   7975  C CZ    . ARG A 1 1065 ? 20.046  55.986  115.904 1.00 34.02 ?  1063 ARG A CZ    1 
ATOM   7976  N NH1   . ARG A 1 1065 ? 20.973  55.047  115.991 1.00 44.82 ?  1063 ARG A NH1   1 
ATOM   7977  N NH2   . ARG A 1 1065 ? 18.894  55.824  116.550 1.00 43.68 ?  1063 ARG A NH2   1 
ATOM   7978  N N     . ALA A 1 1066 ? 20.818  61.452  115.582 1.00 18.59 ?  1064 ALA A N     1 
ATOM   7979  C CA    . ALA A 1 1066 ? 19.551  61.679  116.270 1.00 19.18 ?  1064 ALA A CA    1 
ATOM   7980  C C     . ALA A 1 1066 ? 18.527  62.337  115.347 1.00 18.40 ?  1064 ALA A C     1 
ATOM   7981  O O     . ALA A 1 1066 ? 17.364  61.924  115.298 1.00 17.70 ?  1064 ALA A O     1 
ATOM   7982  C CB    . ALA A 1 1066 ? 19.768  62.530  117.522 1.00 22.09 ?  1064 ALA A CB    1 
ATOM   7983  N N     . GLU A 1 1067 ? 18.936  63.377  114.618 1.00 19.22 ?  1065 GLU A N     1 
ATOM   7984  C CA    . GLU A 1 1067 ? 17.992  64.044  113.736 1.00 17.49 ?  1065 GLU A CA    1 
ATOM   7985  C C     . GLU A 1 1067 ? 17.610  63.161  112.557 1.00 17.36 ?  1065 GLU A C     1 
ATOM   7986  O O     . GLU A 1 1067 ? 16.480  63.258  112.061 1.00 17.56 ?  1065 GLU A O     1 
ATOM   7987  C CB    . GLU A 1 1067 ? 18.565  65.374  113.250 1.00 18.95 ?  1065 GLU A CB    1 
ATOM   7988  C CG    . GLU A 1 1067 ? 18.582  66.468  114.326 1.00 18.13 ?  1065 GLU A CG    1 
ATOM   7989  C CD    . GLU A 1 1067 ? 19.772  66.367  115.260 1.00 20.50 ?  1065 GLU A CD    1 
ATOM   7990  O OE1   . GLU A 1 1067 ? 20.693  65.546  115.015 1.00 19.72 ?  1065 GLU A OE1   1 
ATOM   7991  O OE2   . GLU A 1 1067 ? 19.776  67.132  116.244 1.00 20.61 ?  1065 GLU A OE2   1 
ATOM   7992  N N     . ALA A 1 1068 ? 18.531  62.310  112.084 1.00 18.20 ?  1066 ALA A N     1 
ATOM   7993  C CA    . ALA A 1 1068 ? 18.179  61.379  111.009 1.00 17.49 ?  1066 ALA A CA    1 
ATOM   7994  C C     . ALA A 1 1068 ? 17.097  60.401  111.456 1.00 16.49 ?  1066 ALA A C     1 
ATOM   7995  O O     . ALA A 1 1068 ? 16.156  60.113  110.693 1.00 15.89 ?  1066 ALA A O     1 
ATOM   7996  C CB    . ALA A 1 1068 ? 19.421  60.623  110.524 1.00 18.02 ?  1066 ALA A CB    1 
ATOM   7997  N N     . GLU A 1 1069 ? 17.214  59.876  112.682 1.00 19.55 ?  1067 GLU A N     1 
ATOM   7998  C CA    . GLU A 1 1069 ? 16.174  59.017  113.239 1.00 18.23 ?  1067 GLU A CA    1 
ATOM   7999  C C     . GLU A 1 1069 ? 14.851  59.764  113.365 1.00 18.89 ?  1067 GLU A C     1 
ATOM   8000  O O     . GLU A 1 1069 ? 13.793  59.236  113.002 1.00 18.49 ?  1067 GLU A O     1 
ATOM   8001  C CB    . GLU A 1 1069 ? 16.614  58.465  114.603 1.00 23.36 ?  1067 GLU A CB    1 
ATOM   8002  C CG    . GLU A 1 1069 ? 15.555  57.575  115.247 1.00 25.34 ?  1067 GLU A CG    1 
ATOM   8003  C CD    . GLU A 1 1069 ? 16.005  56.927  116.543 1.00 40.99 ?  1067 GLU A CD    1 
ATOM   8004  O OE1   . GLU A 1 1069 ? 16.910  57.472  117.212 1.00 41.71 ?  1067 GLU A OE1   1 
ATOM   8005  O OE2   . GLU A 1 1069 ? 15.443  55.865  116.891 1.00 48.26 ?  1067 GLU A OE2   1 
ATOM   8006  N N     . ALA A 1 1070 ? 14.887  60.997  113.880 1.00 18.97 ?  1068 ALA A N     1 
ATOM   8007  C CA    . ALA A 1 1070 ? 13.667  61.792  113.974 1.00 17.65 ?  1068 ALA A CA    1 
ATOM   8008  C C     . ALA A 1 1070 ? 13.066  62.051  112.595 1.00 17.36 ?  1068 ALA A C     1 
ATOM   8009  O O     . ALA A 1 1070 ? 11.839  62.085  112.440 1.00 16.55 ?  1068 ALA A O     1 
ATOM   8010  C CB    . ALA A 1 1070 ? 13.953  63.114  114.687 1.00 21.66 ?  1068 ALA A CB    1 
ATOM   8011  N N     . ALA A 1 1071 ? 13.912  62.246  111.584 1.00 15.35 ?  1069 ALA A N     1 
ATOM   8012  C CA    . ALA A 1 1071 ? 13.413  62.454  110.229 1.00 13.55 ?  1069 ALA A CA    1 
ATOM   8013  C C     . ALA A 1 1071 ? 12.711  61.206  109.714 1.00 13.85 ?  1069 ALA A C     1 
ATOM   8014  O O     . ALA A 1 1071 ? 11.613  61.288  109.148 1.00 13.47 ?  1069 ALA A O     1 
ATOM   8015  C CB    . ALA A 1 1071 ? 14.570  62.853  109.308 1.00 14.00 ?  1069 ALA A CB    1 
ATOM   8016  N N     . ARG A 1 1072 ? 13.328  60.035  109.899 1.00 15.13 ?  1070 ARG A N     1 
ATOM   8017  C CA    A ARG A 1 1072 ? 12.680  58.799  109.465 0.56 15.19 ?  1070 ARG A CA    1 
ATOM   8018  C CA    B ARG A 1 1072 ? 12.677  58.804  109.461 0.44 15.20 ?  1070 ARG A CA    1 
ATOM   8019  C C     . ARG A 1 1072 ? 11.371  58.577  110.209 1.00 13.61 ?  1070 ARG A C     1 
ATOM   8020  O O     . ARG A 1 1072 ? 10.387  58.117  109.622 1.00 16.14 ?  1070 ARG A O     1 
ATOM   8021  C CB    A ARG A 1 1072 ? 13.616  57.606  109.659 0.56 17.57 ?  1070 ARG A CB    1 
ATOM   8022  C CB    B ARG A 1 1072 ? 13.621  57.615  109.632 0.44 17.57 ?  1070 ARG A CB    1 
ATOM   8023  C CG    A ARG A 1 1072 ? 14.712  57.503  108.609 0.56 18.95 ?  1070 ARG A CG    1 
ATOM   8024  C CG    B ARG A 1 1072 ? 14.865  57.744  108.779 0.44 18.91 ?  1070 ARG A CG    1 
ATOM   8025  C CD    A ARG A 1 1072 ? 15.523  56.228  108.813 0.56 20.41 ?  1070 ARG A CD    1 
ATOM   8026  C CD    B ARG A 1 1072 ? 15.773  56.536  108.881 0.44 20.95 ?  1070 ARG A CD    1 
ATOM   8027  N NE    A ARG A 1 1072 ? 16.277  56.250  110.062 0.56 22.03 ?  1070 ARG A NE    1 
ATOM   8028  N NE    B ARG A 1 1072 ? 17.054  56.829  108.253 0.44 24.13 ?  1070 ARG A NE    1 
ATOM   8029  C CZ    A ARG A 1 1072 ? 17.519  56.695  110.174 0.56 22.48 ?  1070 ARG A CZ    1 
ATOM   8030  C CZ    B ARG A 1 1072 ? 17.243  56.888  106.943 0.44 20.26 ?  1070 ARG A CZ    1 
ATOM   8031  N NH1   A ARG A 1 1072 ? 18.179  57.175  109.128 0.56 18.86 ?  1070 ARG A NH1   1 
ATOM   8032  N NH1   B ARG A 1 1072 ? 16.268  56.620  106.091 0.44 22.79 ?  1070 ARG A NH1   1 
ATOM   8033  N NH2   A ARG A 1 1072 ? 18.116  56.659  111.364 0.56 24.21 ?  1070 ARG A NH2   1 
ATOM   8034  N NH2   B ARG A 1 1072 ? 18.441  57.224  106.475 0.44 16.89 ?  1070 ARG A NH2   1 
ATOM   8035  N N     . ASN A 1 1073 ? 11.336  58.900  111.506 1.00 14.87 ?  1071 ASN A N     1 
ATOM   8036  C CA    . ASN A 1 1073 ? 10.101  58.763  112.270 1.00 15.47 ?  1071 ASN A CA    1 
ATOM   8037  C C     . ASN A 1 1073 ? 9.017   59.686  111.730 1.00 15.88 ?  1071 ASN A C     1 
ATOM   8038  O O     . ASN A 1 1073 ? 7.848   59.297  111.649 1.00 17.36 ?  1071 ASN A O     1 
ATOM   8039  C CB    . ASN A 1 1073 ? 10.359  59.051  113.749 1.00 16.87 ?  1071 ASN A CB    1 
ATOM   8040  C CG    . ASN A 1 1073 ? 11.138  57.954  114.420 1.00 21.65 ?  1071 ASN A CG    1 
ATOM   8041  O OD1   . ASN A 1 1073 ? 11.225  56.830  113.914 1.00 24.09 ?  1071 ASN A OD1   1 
ATOM   8042  N ND2   . ASN A 1 1073 ? 11.710  58.270  115.572 1.00 23.63 ?  1071 ASN A ND2   1 
ATOM   8043  N N     . ALA A 1 1074 ? 9.385   60.924  111.378 1.00 14.46 ?  1072 ALA A N     1 
ATOM   8044  C CA    . ALA A 1 1074 ? 8.420   61.832  110.758 1.00 13.89 ?  1072 ALA A CA    1 
ATOM   8045  C C     . ALA A 1 1074 ? 7.921   61.283  109.430 1.00 13.57 ?  1072 ALA A C     1 
ATOM   8046  O O     . ALA A 1 1074 ? 6.727   61.380  109.122 1.00 14.44 ?  1072 ALA A O     1 
ATOM   8047  C CB    . ALA A 1 1074 ? 9.040   63.215  110.559 1.00 16.72 ?  1072 ALA A CB    1 
ATOM   8048  N N     . GLY A 1 1075 ? 8.817   60.698  108.630 1.00 14.01 ?  1073 GLY A N     1 
ATOM   8049  C CA    . GLY A 1 1075 ? 8.390   60.109  107.368 1.00 14.06 ?  1073 GLY A CA    1 
ATOM   8050  C C     . GLY A 1 1075 ? 7.325   59.040  107.545 1.00 16.88 ?  1073 GLY A C     1 
ATOM   8051  O O     . GLY A 1 1075 ? 6.373   58.968  106.756 1.00 16.03 ?  1073 GLY A O     1 
ATOM   8052  N N     . SER A 1 1076 ? 7.468   58.204  108.585 1.00 15.12 ?  1074 SER A N     1 
ATOM   8053  C CA    . SER A 1 1076 ? 6.492   57.153  108.888 1.00 14.24 ?  1074 SER A CA    1 
ATOM   8054  C C     . SER A 1 1076 ? 5.213   57.719  109.484 1.00 17.26 ?  1074 SER A C     1 
ATOM   8055  O O     . SER A 1 1076 ? 4.111   57.276  109.137 1.00 18.76 ?  1074 SER A O     1 
ATOM   8056  C CB    . SER A 1 1076 ? 7.095   56.131  109.861 1.00 18.45 ?  1074 SER A CB    1 
ATOM   8057  O OG    . SER A 1 1076 ? 8.143   55.409  109.263 1.00 25.55 ?  1074 SER A OG    1 
ATOM   8058  N N     . SER A 1 1077 ? 5.334   58.683  110.397 1.00 16.15 ?  1075 SER A N     1 
ATOM   8059  C CA    A SER A 1 1077 ? 4.177   59.247  111.090 0.38 17.22 ?  1075 SER A CA    1 
ATOM   8060  C CA    B SER A 1 1077 ? 4.156   59.213  111.074 0.41 17.22 ?  1075 SER A CA    1 
ATOM   8061  C CA    C SER A 1 1077 ? 4.145   59.196  111.068 0.21 17.22 ?  1075 SER A CA    1 
ATOM   8062  C C     . SER A 1 1077 ? 3.309   60.095  110.168 1.00 16.55 ?  1075 SER A C     1 
ATOM   8063  O O     . SER A 1 1077 ? 2.100   60.223  110.399 1.00 16.86 ?  1075 SER A O     1 
ATOM   8064  C CB    A SER A 1 1077 ? 4.653   60.085  112.279 0.38 17.21 ?  1075 SER A CB    1 
ATOM   8065  C CB    B SER A 1 1077 ? 4.580   59.995  112.316 0.41 17.24 ?  1075 SER A CB    1 
ATOM   8066  C CB    C SER A 1 1077 ? 4.537   59.944  112.342 0.21 17.26 ?  1075 SER A CB    1 
ATOM   8067  O OG    A SER A 1 1077 ? 3.584   60.781  112.898 0.38 18.68 ?  1075 SER A OG    1 
ATOM   8068  O OG    B SER A 1 1077 ? 5.107   59.119  113.296 0.41 17.52 ?  1075 SER A OG    1 
ATOM   8069  O OG    C SER A 1 1077 ? 5.437   60.996  112.064 0.21 17.20 ?  1075 SER A OG    1 
ATOM   8070  N N     . SER A 1 1078 ? 3.907   60.703  109.152 1.00 14.12 ?  1076 SER A N     1 
ATOM   8071  C CA    . SER A 1 1078 ? 3.154   61.547  108.233 1.00 12.95 ?  1076 SER A CA    1 
ATOM   8072  C C     . SER A 1 1078 ? 2.002   60.763  107.610 1.00 14.44 ?  1076 SER A C     1 
ATOM   8073  O O     . SER A 1 1078 ? 2.153   59.594  107.251 1.00 14.44 ?  1076 SER A O     1 
ATOM   8074  C CB    . SER A 1 1078 ? 4.085   62.049  107.134 1.00 13.64 ?  1076 SER A CB    1 
ATOM   8075  O OG    . SER A 1 1078 ? 3.343   62.733  106.139 1.00 13.20 ?  1076 SER A OG    1 
ATOM   8076  N N     . ALA A 1 1079 ? 0.847   61.410  107.474 1.00 12.22 ?  1077 ALA A N     1 
ATOM   8077  C CA    . ALA A 1 1079 ? -0.283  60.806  106.776 1.00 12.30 ?  1077 ALA A CA    1 
ATOM   8078  C C     . ALA A 1 1079 ? -0.424  61.330  105.354 1.00 12.21 ?  1077 ALA A C     1 
ATOM   8079  O O     . ALA A 1 1079 ? -1.448  61.082  104.705 1.00 12.37 ?  1077 ALA A O     1 
ATOM   8080  C CB    . ALA A 1 1079 ? -1.580  61.030  107.562 1.00 11.20 ?  1077 ALA A CB    1 
ATOM   8081  N N     . LEU A 1 1080 ? 0.580   62.050  104.855 1.00 12.74 ?  1078 LEU A N     1 
ATOM   8082  C CA    . LEU A 1 1080 ? 0.629   62.425  103.447 1.00 12.22 ?  1078 LEU A CA    1 
ATOM   8083  C C     . LEU A 1 1080 ? 0.388   61.204  102.576 1.00 11.93 ?  1078 LEU A C     1 
ATOM   8084  O O     . LEU A 1 1080 ? 1.051   60.178  102.741 1.00 12.03 ?  1078 LEU A O     1 
ATOM   8085  C CB    . LEU A 1 1080 ? 2.003   63.027  103.134 1.00 11.04 ?  1078 LEU A CB    1 
ATOM   8086  C CG    . LEU A 1 1080 ? 2.283   63.329  101.665 1.00 11.15 ?  1078 LEU A CG    1 
ATOM   8087  C CD1   . LEU A 1 1080 ? 1.432   64.503  101.231 1.00 12.94 ?  1078 LEU A CD1   1 
ATOM   8088  C CD2   . LEU A 1 1080 ? 3.766   63.596  101.435 1.00 12.18 ?  1078 LEU A CD2   1 
ATOM   8089  N N     . GLY A 1 1081 ? -0.560  61.317  101.636 1.00 10.59 ?  1079 GLY A N     1 
ATOM   8090  C CA    . GLY A 1 1081 ? -0.883  60.199  100.774 1.00 13.16 ?  1079 GLY A CA    1 
ATOM   8091  C C     . GLY A 1 1081 ? -2.090  59.384  101.192 1.00 12.46 ?  1079 GLY A C     1 
ATOM   8092  O O     . GLY A 1 1081 ? -2.482  58.480  100.439 1.00 14.58 ?  1079 GLY A O     1 
ATOM   8093  N N     . LEU A 1 1082 ? -2.656  59.636  102.380 1.00 11.70 ?  1080 LEU A N     1 
ATOM   8094  C CA    . LEU A 1 1082 ? -3.951  59.067  102.743 1.00 10.29 ?  1080 LEU A CA    1 
ATOM   8095  C C     . LEU A 1 1082 ? -4.949  59.277  101.607 1.00 11.66 ?  1080 LEU A C     1 
ATOM   8096  O O     . LEU A 1 1082 ? -5.034  60.368  101.039 1.00 11.80 ?  1080 LEU A O     1 
ATOM   8097  C CB    . LEU A 1 1082 ? -4.467  59.735  104.019 1.00 10.96 ?  1080 LEU A CB    1 
ATOM   8098  C CG    . LEU A 1 1082 ? -5.800  59.251  104.559 1.00 11.60 ?  1080 LEU A CG    1 
ATOM   8099  C CD1   . LEU A 1 1082 ? -5.808  57.755  104.640 1.00 19.88 ?  1080 LEU A CD1   1 
ATOM   8100  C CD2   . LEU A 1 1082 ? -6.019  59.826  105.941 1.00 16.56 ?  1080 LEU A CD2   1 
ATOM   8101  N N     . ASP A 1 1083 ? -5.705  58.220  101.283 1.00 11.88 ?  1081 ASP A N     1 
ATOM   8102  C CA    . ASP A 1 1083 ? -6.597  58.226  100.119 1.00 13.57 ?  1081 ASP A CA    1 
ATOM   8103  C C     . ASP A 1 1083 ? -7.790  57.331  100.457 1.00 16.98 ?  1081 ASP A C     1 
ATOM   8104  O O     . ASP A 1 1083 ? -7.691  56.103  100.354 1.00 18.78 ?  1081 ASP A O     1 
ATOM   8105  C CB    . ASP A 1 1083 ? -5.845  57.732  98.888  1.00 16.35 ?  1081 ASP A CB    1 
ATOM   8106  C CG    . ASP A 1 1083 ? -6.680  57.774  97.626  1.00 23.31 ?  1081 ASP A CG    1 
ATOM   8107  O OD1   . ASP A 1 1083 ? -7.704  58.479  97.604  1.00 26.74 ?  1081 ASP A OD1   1 
ATOM   8108  O OD2   . ASP A 1 1083 ? -6.291  57.086  96.659  1.00 30.41 ?  1081 ASP A OD2   1 
ATOM   8109  N N     . LEU A 1 1084 ? -8.896  57.940  100.886 1.00 13.01 ?  1082 LEU A N     1 
ATOM   8110  C CA    . LEU A 1 1084 ? -10.036 57.203  101.411 1.00 14.29 ?  1082 LEU A CA    1 
ATOM   8111  C C     . LEU A 1 1084 ? -11.290 57.502  100.610 1.00 13.67 ?  1082 LEU A C     1 
ATOM   8112  O O     . LEU A 1 1084 ? -11.431 58.575  100.023 1.00 16.30 ?  1082 LEU A O     1 
ATOM   8113  C CB    . LEU A 1 1084 ? -10.332 57.560  102.875 1.00 15.90 ?  1082 LEU A CB    1 
ATOM   8114  C CG    . LEU A 1 1084 ? -9.247  57.287  103.899 1.00 18.30 ?  1082 LEU A CG    1 
ATOM   8115  C CD1   . LEU A 1 1084 ? -9.658  57.938  105.212 1.00 19.66 ?  1082 LEU A CD1   1 
ATOM   8116  C CD2   . LEU A 1 1084 ? -9.060  55.793  104.050 1.00 22.13 ?  1082 LEU A CD2   1 
ATOM   8117  N N     . GLU A 1 1085 ? -12.209 56.544  100.616 1.00 13.88 ?  1083 GLU A N     1 
ATOM   8118  C CA    . GLU A 1 1085 ? -13.565 56.776  100.140 1.00 13.81 ?  1083 GLU A CA    1 
ATOM   8119  C C     . GLU A 1 1085 ? -14.477 56.763  101.352 1.00 14.44 ?  1083 GLU A C     1 
ATOM   8120  O O     . GLU A 1 1085 ? -14.453 55.809  102.136 1.00 16.98 ?  1083 GLU A O     1 
ATOM   8121  C CB    . GLU A 1 1085 ? -14.013 55.723  99.119  1.00 14.43 ?  1083 GLU A CB    1 
ATOM   8122  C CG    . GLU A 1 1085 ? -15.461 55.979  98.675  1.00 17.63 ?  1083 GLU A CG    1 
ATOM   8123  C CD    . GLU A 1 1085 ? -15.978 55.121  97.521  1.00 22.67 ?  1083 GLU A CD    1 
ATOM   8124  O OE1   . GLU A 1 1085 ? -15.178 54.463  96.819  1.00 23.70 ?  1083 GLU A OE1   1 
ATOM   8125  O OE2   . GLU A 1 1085 ? -17.218 55.121  97.320  1.00 22.98 ?  1083 GLU A OE2   1 
ATOM   8126  N N     . LEU A 1 1086 ? -15.261 57.826  101.511 1.00 12.86 ?  1084 LEU A N     1 
ATOM   8127  C CA    . LEU A 1 1086 ? -16.168 57.986  102.643 1.00 13.75 ?  1084 LEU A CA    1 
ATOM   8128  C C     . LEU A 1 1086 ? -17.561 57.450  102.299 1.00 15.96 ?  1084 LEU A C     1 
ATOM   8129  O O     . LEU A 1 1086 ? -18.038 57.645  101.178 1.00 16.92 ?  1084 LEU A O     1 
ATOM   8130  C CB    . LEU A 1 1086 ? -16.270 59.460  103.044 1.00 16.37 ?  1084 LEU A CB    1 
ATOM   8131  C CG    . LEU A 1 1086 ? -14.913 60.109  103.359 1.00 15.18 ?  1084 LEU A CG    1 
ATOM   8132  C CD1   . LEU A 1 1086 ? -15.099 61.574  103.789 1.00 16.76 ?  1084 LEU A CD1   1 
ATOM   8133  C CD2   . LEU A 1 1086 ? -14.151 59.316  104.419 1.00 21.42 ?  1084 LEU A CD2   1 
ATOM   8134  N N     . PRO A 1 1087 ? -18.218 56.779  103.245 1.00 15.87 ?  1085 PRO A N     1 
ATOM   8135  C CA    . PRO A 1 1087 ? -19.575 56.272  102.995 1.00 15.76 ?  1085 PRO A CA    1 
ATOM   8136  C C     . PRO A 1 1087 ? -20.548 57.403  102.721 1.00 16.48 ?  1085 PRO A C     1 
ATOM   8137  O O     . PRO A 1 1087 ? -20.524 58.442  103.380 1.00 17.84 ?  1085 PRO A O     1 
ATOM   8138  C CB    . PRO A 1 1087 ? -19.934 55.547  104.298 1.00 18.21 ?  1085 PRO A CB    1 
ATOM   8139  C CG    . PRO A 1 1087 ? -18.647 55.295  104.971 1.00 21.98 ?  1085 PRO A CG    1 
ATOM   8140  C CD    . PRO A 1 1087 ? -17.696 56.363  104.557 1.00 16.25 ?  1085 PRO A CD    1 
ATOM   8141  N N     . GLY A 1 1088 ? -21.431 57.180  101.753 1.00 16.38 ?  1086 GLY A N     1 
ATOM   8142  C CA    . GLY A 1 1088 ? -22.384 58.184  101.357 1.00 18.86 ?  1086 GLY A CA    1 
ATOM   8143  C C     . GLY A 1 1088 ? -23.496 57.569  100.540 1.00 15.63 ?  1086 GLY A C     1 
ATOM   8144  O O     . GLY A 1 1088 ? -23.705 56.353  100.551 1.00 14.97 ?  1086 GLY A O     1 
ATOM   8145  N N     . PRO A 1 1089 ? -24.216 58.398  99.793  1.00 16.34 ?  1087 PRO A N     1 
ATOM   8146  C CA    . PRO A 1 1089 ? -25.317 57.884  98.978  1.00 14.97 ?  1087 PRO A CA    1 
ATOM   8147  C C     . PRO A 1 1089 ? -24.813 57.090  97.779  1.00 12.90 ?  1087 PRO A C     1 
ATOM   8148  O O     . PRO A 1 1089 ? -23.665 57.220  97.341  1.00 14.40 ?  1087 PRO A O     1 
ATOM   8149  C CB    . PRO A 1 1089 ? -26.037 59.157  98.533  1.00 18.73 ?  1087 PRO A CB    1 
ATOM   8150  C CG    . PRO A 1 1089 ? -24.916 60.169  98.460  1.00 19.10 ?  1087 PRO A CG    1 
ATOM   8151  C CD    . PRO A 1 1089 ? -24.027 59.847  99.624  1.00 18.18 ?  1087 PRO A CD    1 
ATOM   8152  N N     . VAL A 1 1090 ? -25.710 56.258  97.240  1.00 14.97 ?  1088 VAL A N     1 
ATOM   8153  C CA    . VAL A 1 1090 ? -25.413 55.582  95.977  1.00 13.27 ?  1088 VAL A CA    1 
ATOM   8154  C C     . VAL A 1 1090 ? -25.301 56.618  94.854  1.00 13.11 ?  1088 VAL A C     1 
ATOM   8155  O O     . VAL A 1 1090 ? -25.811 57.739  94.946  1.00 14.34 ?  1088 VAL A O     1 
ATOM   8156  C CB    . VAL A 1 1090 ? -26.472 54.529  95.622  1.00 15.59 ?  1088 VAL A CB    1 
ATOM   8157  C CG1   . VAL A 1 1090 ? -26.546 53.443  96.686  1.00 16.41 ?  1088 VAL A CG1   1 
ATOM   8158  C CG2   . VAL A 1 1090 ? -27.830 55.186  95.429  1.00 15.35 ?  1088 VAL A CG2   1 
ATOM   8159  N N     . GLY A 1 1091 ? -24.621 56.224  93.781  1.00 14.44 ?  1089 GLY A N     1 
ATOM   8160  C CA    . GLY A 1 1091 ? -24.491 57.080  92.612  1.00 13.34 ?  1089 GLY A CA    1 
ATOM   8161  C C     . GLY A 1 1091 ? -23.539 58.234  92.801  1.00 11.78 ?  1089 GLY A C     1 
ATOM   8162  O O     . GLY A 1 1091 ? -23.556 59.190  92.012  1.00 11.98 ?  1089 GLY A O     1 
ATOM   8163  N N     . GLU A 1 1092 ? -22.705 58.164  93.834  1.00 12.91 ?  1090 GLU A N     1 
ATOM   8164  C CA    . GLU A 1 1092 ? -21.725 59.195  94.108  1.00 13.96 ?  1090 GLU A CA    1 
ATOM   8165  C C     . GLU A 1 1092 ? -20.507 58.520  94.712  1.00 11.02 ?  1090 GLU A C     1 
ATOM   8166  O O     . GLU A 1 1092 ? -20.646 57.553  95.465  1.00 14.75 ?  1090 GLU A O     1 
ATOM   8167  C CB    . GLU A 1 1092 ? -22.297 60.235  95.074  1.00 16.25 ?  1090 GLU A CB    1 
ATOM   8168  C CG    . GLU A 1 1092 ? -21.656 61.600  95.001  1.00 20.53 ?  1090 GLU A CG    1 
ATOM   8169  C CD    . GLU A 1 1092 ? -22.441 62.599  95.818  1.00 19.89 ?  1090 GLU A CD    1 
ATOM   8170  O OE1   . GLU A 1 1092 ? -22.396 62.492  97.056  1.00 18.12 ?  1090 GLU A OE1   1 
ATOM   8171  O OE2   . GLU A 1 1092 ? -23.136 63.452  95.220  1.00 21.69 ?  1090 GLU A OE2   1 
ATOM   8172  N N     . ARG A 1 1093 ? -19.319 59.002  94.356  1.00 10.87 ?  1091 ARG A N     1 
ATOM   8173  C CA    . ARG A 1 1093 ? -18.089 58.575  95.021  1.00 12.51 ?  1091 ARG A CA    1 
ATOM   8174  C C     . ARG A 1 1093 ? -17.495 59.773  95.742  1.00 11.83 ?  1091 ARG A C     1 
ATOM   8175  O O     . ARG A 1 1093 ? -17.222 60.804  95.121  1.00 11.50 ?  1091 ARG A O     1 
ATOM   8176  C CB    . ARG A 1 1093 ? -17.086 58.005  94.015  1.00 15.67 ?  1091 ARG A CB    1 
ATOM   8177  C CG    . ARG A 1 1093 ? -15.858 57.376  94.648  1.00 21.23 ?  1091 ARG A CG    1 
ATOM   8178  C CD    . ARG A 1 1093 ? -14.972 56.719  93.583  1.00 29.11 ?  1091 ARG A CD    1 
ATOM   8179  N NE    . ARG A 1 1093 ? -15.755 55.840  92.724  1.00 31.92 ?  1091 ARG A NE    1 
ATOM   8180  C CZ    . ARG A 1 1093 ? -15.945 56.024  91.424  1.00 31.04 ?  1091 ARG A CZ    1 
ATOM   8181  N NH1   . ARG A 1 1093 ? -15.356 57.015  90.770  1.00 37.76 ?  1091 ARG A NH1   1 
ATOM   8182  N NH2   . ARG A 1 1093 ? -16.735 55.185  90.759  1.00 31.19 ?  1091 ARG A NH2   1 
ATOM   8183  N N     . ASN A 1 1094 ? -17.281 59.635  97.046  1.00 12.36 ?  1092 ASN A N     1 
ATOM   8184  C CA    . ASN A 1 1094 ? -16.832 60.751  97.867  1.00 10.59 ?  1092 ASN A CA    1 
ATOM   8185  C C     . ASN A 1 1094 ? -15.479 60.411  98.455  1.00 12.04 ?  1092 ASN A C     1 
ATOM   8186  O O     . ASN A 1 1094 ? -15.361 59.468  99.241  1.00 14.66 ?  1092 ASN A O     1 
ATOM   8187  C CB    . ASN A 1 1094 ? -17.876 61.042  98.931  1.00 11.47 ?  1092 ASN A CB    1 
ATOM   8188  C CG    . ASN A 1 1094 ? -19.095 61.682  98.325  1.00 12.02 ?  1092 ASN A CG    1 
ATOM   8189  O OD1   . ASN A 1 1094 ? -19.010 62.805  97.853  1.00 12.60 ?  1092 ASN A OD1   1 
ATOM   8190  N ND2   . ASN A 1 1094 ? -20.224 60.964  98.294  1.00 12.44 ?  1092 ASN A ND2   1 
ATOM   8191  N N     . LEU A 1 1095 ? -14.467 61.144  98.015  1.00 12.29 ?  1093 LEU A N     1 
ATOM   8192  C CA    . LEU A 1 1095 ? -13.079 60.825  98.288  1.00 11.76 ?  1093 LEU A CA    1 
ATOM   8193  C C     . LEU A 1 1095 ? -12.479 61.873  99.213  1.00 11.45 ?  1093 LEU A C     1 
ATOM   8194  O O     . LEU A 1 1095 ? -12.827 63.055  99.156  1.00 12.72 ?  1093 LEU A O     1 
ATOM   8195  C CB    . LEU A 1 1095 ? -12.288 60.754  96.982  1.00 13.81 ?  1093 LEU A CB    1 
ATOM   8196  C CG    . LEU A 1 1095 ? -12.934 59.800  95.972  1.00 14.17 ?  1093 LEU A CG    1 
ATOM   8197  C CD1   . LEU A 1 1095 ? -12.147 59.820  94.660  1.00 22.19 ?  1093 LEU A CD1   1 
ATOM   8198  C CD2   . LEU A 1 1095 ? -13.075 58.385  96.532  1.00 18.09 ?  1093 LEU A CD2   1 
ATOM   8199  N N     . TYR A 1 1096 ? -11.558 61.425  100.066 1.00 11.88 ?  1094 TYR A N     1 
ATOM   8200  C CA    . TYR A 1 1096 ? -10.901 62.304  101.033 1.00 11.95 ?  1094 TYR A CA    1 
ATOM   8201  C C     . TYR A 1 1096 ? -9.423  61.959  101.009 1.00 12.43 ?  1094 TYR A C     1 
ATOM   8202  O O     . TYR A 1 1096 ? -9.065  60.787  101.155 1.00 13.13 ?  1094 TYR A O     1 
ATOM   8203  C CB    . TYR A 1 1096 ? -11.511 62.111  102.425 1.00 13.07 ?  1094 TYR A CB    1 
ATOM   8204  C CG    . TYR A 1 1096 ? -10.792 62.800  103.563 1.00 13.96 ?  1094 TYR A CG    1 
ATOM   8205  C CD1   . TYR A 1 1096 ? -9.801  62.143  104.291 1.00 16.08 ?  1094 TYR A CD1   1 
ATOM   8206  C CD2   . TYR A 1 1096 ? -11.153 64.080  103.953 1.00 12.43 ?  1094 TYR A CD2   1 
ATOM   8207  C CE1   . TYR A 1 1096 ? -9.167  62.771  105.361 1.00 13.97 ?  1094 TYR A CE1   1 
ATOM   8208  C CE2   . TYR A 1 1096 ? -10.523 64.711  105.028 1.00 14.46 ?  1094 TYR A CE2   1 
ATOM   8209  C CZ    . TYR A 1 1096 ? -9.543  64.057  105.721 1.00 15.47 ?  1094 TYR A CZ    1 
ATOM   8210  O OH    . TYR A 1 1096 ? -8.942  64.704  106.787 1.00 15.09 ?  1094 TYR A OH    1 
ATOM   8211  N N     . THR A 1 1097 ? -8.573  62.959  100.765 1.00 11.01 ?  1095 THR A N     1 
ATOM   8212  C CA    . THR A 1 1097 ? -7.148  62.717  100.552 1.00 12.76 ?  1095 THR A CA    1 
ATOM   8213  C C     . THR A 1 1097 ? -6.320  63.763  101.289 1.00 13.60 ?  1095 THR A C     1 
ATOM   8214  O O     . THR A 1 1097 ? -6.780  64.877  101.531 1.00 12.87 ?  1095 THR A O     1 
ATOM   8215  C CB    . THR A 1 1097 ? -6.789  62.747  99.062  1.00 15.79 ?  1095 THR A CB    1 
ATOM   8216  O OG1   . THR A 1 1097 ? -7.203  63.993  98.498  1.00 17.99 ?  1095 THR A OG1   1 
ATOM   8217  C CG2   . THR A 1 1097 ? -7.500  61.633  98.324  1.00 14.94 ?  1095 THR A CG2   1 
ATOM   8218  N N     . LEU A 1 1098 ? -5.087  63.398  101.646 1.00 12.66 ?  1096 LEU A N     1 
ATOM   8219  C CA    . LEU A 1 1098 ? -4.157  64.323  102.289 1.00 9.40  ?  1096 LEU A CA    1 
ATOM   8220  C C     . LEU A 1 1098 ? -2.967  64.610  101.382 1.00 11.21 ?  1096 LEU A C     1 
ATOM   8221  O O     . LEU A 1 1098 ? -2.280  63.686  100.920 1.00 12.18 ?  1096 LEU A O     1 
ATOM   8222  C CB    . LEU A 1 1098 ? -3.673  63.765  103.625 1.00 10.01 ?  1096 LEU A CB    1 
ATOM   8223  C CG    . LEU A 1 1098 ? -4.784  63.568  104.657 1.00 10.73 ?  1096 LEU A CG    1 
ATOM   8224  C CD1   . LEU A 1 1098 ? -4.184  63.069  105.960 1.00 12.81 ?  1096 LEU A CD1   1 
ATOM   8225  C CD2   . LEU A 1 1098 ? -5.528  64.890  104.913 1.00 11.93 ?  1096 LEU A CD2   1 
ATOM   8226  N N     . HIS A 1 1099 ? -2.723  65.893  101.142 1.00 11.57 ?  1097 HIS A N     1 
ATOM   8227  C CA    . HIS A 1 1099 ? -1.688  66.369  100.241 1.00 10.08 ?  1097 HIS A CA    1 
ATOM   8228  C C     . HIS A 1 1099 ? -0.745  67.282  101.000 1.00 13.34 ?  1097 HIS A C     1 
ATOM   8229  O O     . HIS A 1 1099 ? -1.005  67.675  102.138 1.00 13.83 ?  1097 HIS A O     1 
ATOM   8230  C CB    . HIS A 1 1099 ? -2.287  67.148  99.057  1.00 13.01 ?  1097 HIS A CB    1 
ATOM   8231  C CG    . HIS A 1 1099 ? -3.268  66.364  98.246  1.00 14.07 ?  1097 HIS A CG    1 
ATOM   8232  N ND1   . HIS A 1 1099 ? -2.969  65.880  96.991  1.00 18.41 ?  1097 HIS A ND1   1 
ATOM   8233  C CD2   . HIS A 1 1099 ? -4.546  65.995  98.500  1.00 15.83 ?  1097 HIS A CD2   1 
ATOM   8234  C CE1   . HIS A 1 1099 ? -4.020  65.236  96.511  1.00 18.94 ?  1097 HIS A CE1   1 
ATOM   8235  N NE2   . HIS A 1 1099 ? -4.989  65.292  97.407  1.00 16.37 ?  1097 HIS A NE2   1 
ATOM   8236  N N     . ALA A 1 1100 ? 0.345   67.652  100.340 1.00 13.59 ?  1098 ALA A N     1 
ATOM   8237  C CA    . ALA A 1 1100 ? 1.179   68.705  100.890 1.00 12.98 ?  1098 ALA A CA    1 
ATOM   8238  C C     . ALA A 1 1100 ? 0.405   70.013  100.888 1.00 13.39 ?  1098 ALA A C     1 
ATOM   8239  O O     . ALA A 1 1100 ? -0.488  70.225  100.062 1.00 15.16 ?  1098 ALA A O     1 
ATOM   8240  C CB    . ALA A 1 1100 ? 2.454   68.854  100.066 1.00 13.46 ?  1098 ALA A CB    1 
ATOM   8241  N N     . ARG A 1 1101 ? 0.737   70.893  101.836 1.00 15.52 ?  1099 ARG A N     1 
ATOM   8242  C CA    . ARG A 1 1101 ? 0.104   72.208  101.877 1.00 14.25 ?  1099 ARG A CA    1 
ATOM   8243  C C     . ARG A 1 1101 ? 0.707   73.158  100.849 1.00 14.61 ?  1099 ARG A C     1 
ATOM   8244  O O     . ARG A 1 1101 ? -0.020  73.928  100.214 1.00 17.45 ?  1099 ARG A O     1 
ATOM   8245  C CB    . ARG A 1 1101 ? 0.222   72.817  103.277 1.00 15.73 ?  1099 ARG A CB    1 
ATOM   8246  C CG    . ARG A 1 1101 ? -0.591  72.096  104.345 1.00 17.76 ?  1099 ARG A CG    1 
ATOM   8247  C CD    . ARG A 1 1101 ? -0.412  72.751  105.713 1.00 15.23 ?  1099 ARG A CD    1 
ATOM   8248  N NE    . ARG A 1 1101 ? -1.249  73.925  105.932 1.00 17.09 ?  1099 ARG A NE    1 
ATOM   8249  C CZ    . ARG A 1 1101 ? -2.488  73.877  106.411 1.00 20.62 ?  1099 ARG A CZ    1 
ATOM   8250  N NH1   . ARG A 1 1101 ? -3.116  72.726  106.594 1.00 21.62 ?  1099 ARG A NH1   1 
ATOM   8251  N NH2   . ARG A 1 1101 ? -3.111  75.012  106.719 1.00 20.94 ?  1099 ARG A NH2   1 
ATOM   8252  N N     . GLY A 1 1102 ? 2.023   73.124  100.671 1.00 13.28 ?  1100 GLY A N     1 
ATOM   8253  C CA    . GLY A 1 1102 ? 2.693   74.055  99.782  1.00 14.11 ?  1100 GLY A CA    1 
ATOM   8254  C C     . GLY A 1 1102 ? 4.089   74.386  100.258 1.00 12.53 ?  1100 GLY A C     1 
ATOM   8255  O O     . GLY A 1 1102 ? 4.885   73.483  100.531 1.00 15.76 ?  1100 GLY A O     1 
ATOM   8256  N N     . ARG A 1 1103 ? 4.410   75.675  100.353 1.00 13.81 ?  1101 ARG A N     1 
ATOM   8257  C CA    . ARG A 1 1103 ? 5.700   76.108  100.869 1.00 14.40 ?  1101 ARG A CA    1 
ATOM   8258  C C     . ARG A 1 1103 ? 5.501   76.582  102.302 1.00 14.62 ?  1101 ARG A C     1 
ATOM   8259  O O     . ARG A 1 1103 ? 4.691   77.484  102.559 1.00 15.91 ?  1101 ARG A O     1 
ATOM   8260  C CB    . ARG A 1 1103 ? 6.311   77.221  100.015 1.00 17.06 ?  1101 ARG A CB    1 
ATOM   8261  C CG    . ARG A 1 1103 ? 7.791   77.444  100.344 1.00 18.20 ?  1101 ARG A CG    1 
ATOM   8262  C CD    . ARG A 1 1103 ? 8.505   78.383  99.362  1.00 23.95 ?  1101 ARG A CD    1 
ATOM   8263  N NE    . ARG A 1 1103 ? 8.630   77.799  98.030  1.00 23.34 ?  1101 ARG A NE    1 
ATOM   8264  C CZ    . ARG A 1 1103 ? 9.670   77.102  97.580  1.00 27.11 ?  1101 ARG A CZ    1 
ATOM   8265  N NH1   . ARG A 1 1103 ? 10.735  76.852  98.338  1.00 24.69 ?  1101 ARG A NH1   1 
ATOM   8266  N NH2   . ARG A 1 1103 ? 9.639   76.631  96.335  1.00 33.05 ?  1101 ARG A NH2   1 
ATOM   8267  N N     . ILE A 1 1104 ? 6.224   75.959  103.228 1.00 13.44 ?  1102 ILE A N     1 
ATOM   8268  C CA    . ILE A 1 1104 ? 6.128   76.265  104.652 1.00 13.20 ?  1102 ILE A CA    1 
ATOM   8269  C C     . ILE A 1 1104 ? 7.252   77.229  105.006 1.00 15.71 ?  1102 ILE A C     1 
ATOM   8270  O O     . ILE A 1 1104 ? 8.413   76.995  104.649 1.00 14.80 ?  1102 ILE A O     1 
ATOM   8271  C CB    . ILE A 1 1104 ? 6.219   74.978  105.492 1.00 12.73 ?  1102 ILE A CB    1 
ATOM   8272  C CG1   . ILE A 1 1104 ? 5.188   73.942  105.030 1.00 14.04 ?  1102 ILE A CG1   1 
ATOM   8273  C CG2   . ILE A 1 1104 ? 6.045   75.274  106.982 1.00 14.07 ?  1102 ILE A CG2   1 
ATOM   8274  C CD1   . ILE A 1 1104 ? 3.768   74.400  105.154 1.00 16.30 ?  1102 ILE A CD1   1 
ATOM   8275  N N     . LEU A 1 1105 ? 6.911   78.307  105.718 1.00 14.76 ?  1103 LEU A N     1 
ATOM   8276  C CA    . LEU A 1 1105 ? 7.915   79.233  106.221 1.00 15.29 ?  1103 LEU A CA    1 
ATOM   8277  C C     . LEU A 1 1105 ? 8.546   78.634  107.465 1.00 14.56 ?  1103 LEU A C     1 
ATOM   8278  O O     . LEU A 1 1105 ? 7.834   78.311  108.421 1.00 15.89 ?  1103 LEU A O     1 
ATOM   8279  C CB    . LEU A 1 1105 ? 7.283   80.585  106.540 1.00 16.91 ?  1103 LEU A CB    1 
ATOM   8280  C CG    . LEU A 1 1105 ? 8.181   81.608  107.233 1.00 17.79 ?  1103 LEU A CG    1 
ATOM   8281  C CD1   . LEU A 1 1105 ? 9.320   82.038  106.305 1.00 19.32 ?  1103 LEU A CD1   1 
ATOM   8282  C CD2   . LEU A 1 1105 ? 7.354   82.817  107.683 1.00 19.70 ?  1103 LEU A CD2   1 
ATOM   8283  N N     . LEU A 1 1106 ? 9.866   78.490  107.462 1.00 14.15 ?  1104 LEU A N     1 
ATOM   8284  C CA    . LEU A 1 1106 ? 10.606  77.959  108.600 1.00 14.95 ?  1104 LEU A CA    1 
ATOM   8285  C C     . LEU A 1 1106 ? 11.351  79.104  109.263 1.00 18.22 ?  1104 LEU A C     1 
ATOM   8286  O O     . LEU A 1 1106 ? 12.135  79.794  108.606 1.00 16.92 ?  1104 LEU A O     1 
ATOM   8287  C CB    . LEU A 1 1106 ? 11.591  76.877  108.161 1.00 16.24 ?  1104 LEU A CB    1 
ATOM   8288  C CG    . LEU A 1 1106 ? 11.094  75.426  108.156 1.00 21.17 ?  1104 LEU A CG    1 
ATOM   8289  C CD1   . LEU A 1 1106 ? 9.740   75.246  107.503 1.00 20.41 ?  1104 LEU A CD1   1 
ATOM   8290  C CD2   . LEU A 1 1106 ? 12.143  74.532  107.506 1.00 17.64 ?  1104 LEU A CD2   1 
ATOM   8291  N N     . VAL A 1 1107 ? 11.119  79.294  110.556 1.00 15.36 ?  1105 VAL A N     1 
ATOM   8292  C CA    . VAL A 1 1107 ? 11.835  80.311  111.320 1.00 16.69 ?  1105 VAL A CA    1 
ATOM   8293  C C     . VAL A 1 1107 ? 12.581  79.588  112.429 1.00 15.32 ?  1105 VAL A C     1 
ATOM   8294  O O     . VAL A 1 1107 ? 12.082  79.496  113.560 1.00 18.31 ?  1105 VAL A O     1 
ATOM   8295  C CB    . VAL A 1 1107 ? 10.887  81.383  111.875 1.00 14.98 ?  1105 VAL A CB    1 
ATOM   8296  C CG1   . VAL A 1 1107 ? 11.699  82.558  112.405 1.00 16.53 ?  1105 VAL A CG1   1 
ATOM   8297  C CG2   . VAL A 1 1107 ? 9.936   81.855  110.782 1.00 18.20 ?  1105 VAL A CG2   1 
ATOM   8298  N N     . PRO A 1 1108 ? 13.768  79.069  112.162 1.00 14.79 ?  1106 PRO A N     1 
ATOM   8299  C CA    . PRO A 1 1108 ? 14.505  78.312  113.172 1.00 14.99 ?  1106 PRO A CA    1 
ATOM   8300  C C     . PRO A 1 1108 ? 15.352  79.235  114.036 1.00 19.01 ?  1106 PRO A C     1 
ATOM   8301  O O     . PRO A 1 1108 ? 15.568  80.406  113.714 1.00 19.72 ?  1106 PRO A O     1 
ATOM   8302  C CB    . PRO A 1 1108 ? 15.400  77.407  112.321 1.00 17.85 ?  1106 PRO A CB    1 
ATOM   8303  C CG    . PRO A 1 1108 ? 15.716  78.282  111.144 1.00 19.10 ?  1106 PRO A CG    1 
ATOM   8304  C CD    . PRO A 1 1108 ? 14.432  79.017  110.847 1.00 17.83 ?  1106 PRO A CD    1 
ATOM   8305  N N     . ALA A 1 1109 ? 15.843  78.671  115.134 1.00 16.72 ?  1107 ALA A N     1 
ATOM   8306  C CA    . ALA A 1 1109 ? 16.824  79.337  115.983 1.00 17.06 ?  1107 ALA A CA    1 
ATOM   8307  C C     . ALA A 1 1109 ? 18.124  78.566  116.136 1.00 19.34 ?  1107 ALA A C     1 
ATOM   8308  O O     . ALA A 1 1109 ? 19.173  79.191  116.316 1.00 21.51 ?  1107 ALA A O     1 
ATOM   8309  C CB    . ALA A 1 1109 ? 16.241  79.606  117.382 1.00 20.20 ?  1107 ALA A CB    1 
ATOM   8310  N N     . THR A 1 1110 ? 18.085  77.233  116.098 1.00 16.89 ?  1108 THR A N     1 
ATOM   8311  C CA    . THR A 1 1110 ? 19.253  76.391  116.291 1.00 18.47 ?  1108 THR A CA    1 
ATOM   8312  C C     . THR A 1 1110 ? 19.366  75.408  115.138 1.00 16.75 ?  1108 THR A C     1 
ATOM   8313  O O     . THR A 1 1110 ? 18.394  75.144  114.422 1.00 15.88 ?  1108 THR A O     1 
ATOM   8314  C CB    . THR A 1 1110 ? 19.191  75.601  117.609 1.00 18.55 ?  1108 THR A CB    1 
ATOM   8315  O OG1   . THR A 1 1110 ? 18.093  74.677  117.564 1.00 18.47 ?  1108 THR A OG1   1 
ATOM   8316  C CG2   . THR A 1 1110 ? 19.000  76.537  118.783 1.00 19.69 ?  1108 THR A CG2   1 
ATOM   8317  N N     . GLU A 1 1111 ? 20.569  74.845  115.001 1.00 20.12 ?  1109 GLU A N     1 
ATOM   8318  C CA    . GLU A 1 1111 ? 20.818  73.839  113.972 1.00 18.54 ?  1109 GLU A CA    1 
ATOM   8319  C C     . GLU A 1 1111 ? 19.889  72.640  114.138 1.00 18.83 ?  1109 GLU A C     1 
ATOM   8320  O O     . GLU A 1 1111 ? 19.257  72.189  113.172 1.00 16.62 ?  1109 GLU A O     1 
ATOM   8321  C CB    . GLU A 1 1111 ? 22.279  73.401  114.024 1.00 21.54 ?  1109 GLU A CB    1 
ATOM   8322  C CG    . GLU A 1 1111 ? 22.578  72.213  113.143 1.00 23.54 ?  1109 GLU A CG    1 
ATOM   8323  C CD    . GLU A 1 1111 ? 24.051  72.085  112.829 1.00 28.09 ?  1109 GLU A CD    1 
ATOM   8324  O OE1   . GLU A 1 1111 ? 24.610  73.013  112.198 1.00 29.09 ?  1109 GLU A OE1   1 
ATOM   8325  O OE2   . GLU A 1 1111 ? 24.644  71.057  113.207 1.00 26.70 ?  1109 GLU A OE2   1 
ATOM   8326  N N     . SER A 1 1112 ? 19.784  72.110  115.355 1.00 18.05 ?  1110 SER A N     1 
ATOM   8327  C CA    . SER A 1 1112 ? 18.905  70.964  115.573 1.00 17.11 ?  1110 SER A CA    1 
ATOM   8328  C C     . SER A 1 1112 ? 17.448  71.337  115.334 1.00 16.18 ?  1110 SER A C     1 
ATOM   8329  O O     . SER A 1 1112 ? 16.686  70.544  114.774 1.00 16.72 ?  1110 SER A O     1 
ATOM   8330  C CB    . SER A 1 1112 ? 19.090  70.402  116.985 1.00 19.72 ?  1110 SER A CB    1 
ATOM   8331  O OG    . SER A 1 1112 ? 18.315  69.223  117.147 1.00 18.23 ?  1110 SER A OG    1 
ATOM   8332  N N     . GLY A 1 1113 ? 17.036  72.530  115.764 1.00 15.36 ?  1111 GLY A N     1 
ATOM   8333  C CA    . GLY A 1 1113 ? 15.675  72.966  115.490 1.00 14.69 ?  1111 GLY A CA    1 
ATOM   8334  C C     . GLY A 1 1113 ? 15.380  73.030  114.004 1.00 14.26 ?  1111 GLY A C     1 
ATOM   8335  O O     . GLY A 1 1113 ? 14.323  72.579  113.550 1.00 14.34 ?  1111 GLY A O     1 
ATOM   8336  N N     . LEU A 1 1114 ? 16.323  73.562  113.221 1.00 14.26 ?  1112 LEU A N     1 
ATOM   8337  C CA    . LEU A 1 1114 ? 16.133  73.615  111.776 1.00 15.19 ?  1112 LEU A CA    1 
ATOM   8338  C C     . LEU A 1 1114 ? 15.991  72.220  111.187 1.00 13.71 ?  1112 LEU A C     1 
ATOM   8339  O O     . LEU A 1 1114 ? 15.114  71.989  110.347 1.00 14.82 ?  1112 LEU A O     1 
ATOM   8340  C CB    . LEU A 1 1114 ? 17.301  74.341  111.116 1.00 15.37 ?  1112 LEU A CB    1 
ATOM   8341  C CG    . LEU A 1 1114 ? 17.338  74.266  109.582 1.00 15.85 ?  1112 LEU A CG    1 
ATOM   8342  C CD1   . LEU A 1 1114 ? 16.070  74.837  108.943 1.00 18.29 ?  1112 LEU A CD1   1 
ATOM   8343  C CD2   . LEU A 1 1114 ? 18.580  74.961  109.047 1.00 20.61 ?  1112 LEU A CD2   1 
ATOM   8344  N N     . TYR A 1 1115 ? 16.841  71.280  111.607 1.00 15.55 ?  1113 TYR A N     1 
ATOM   8345  C CA    . TYR A 1 1115 ? 16.736  69.917  111.087 1.00 14.58 ?  1113 TYR A CA    1 
ATOM   8346  C C     . TYR A 1 1115 ? 15.383  69.301  111.440 1.00 14.73 ?  1113 TYR A C     1 
ATOM   8347  O O     . TYR A 1 1115 ? 14.770  68.621  110.605 1.00 14.68 ?  1113 TYR A O     1 
ATOM   8348  C CB    . TYR A 1 1115 ? 17.868  69.043  111.618 1.00 14.54 ?  1113 TYR A CB    1 
ATOM   8349  C CG    . TYR A 1 1115 ? 19.267  69.429  111.167 1.00 15.86 ?  1113 TYR A CG    1 
ATOM   8350  C CD1   . TYR A 1 1115 ? 19.473  70.262  110.077 1.00 17.65 ?  1113 TYR A CD1   1 
ATOM   8351  C CD2   . TYR A 1 1115 ? 20.376  68.952  111.853 1.00 18.37 ?  1113 TYR A CD2   1 
ATOM   8352  C CE1   . TYR A 1 1115 ? 20.762  70.601  109.675 1.00 18.45 ?  1113 TYR A CE1   1 
ATOM   8353  C CE2   . TYR A 1 1115 ? 21.657  69.284  111.465 1.00 18.65 ?  1113 TYR A CE2   1 
ATOM   8354  C CZ    . TYR A 1 1115 ? 21.842  70.108  110.386 1.00 20.27 ?  1113 TYR A CZ    1 
ATOM   8355  O OH    . TYR A 1 1115 ? 23.132  70.426  110.019 1.00 24.16 ?  1113 TYR A OH    1 
ATOM   8356  N N     . HIS A 1 1116 ? 14.892  69.541  112.664 1.00 14.36 ?  1114 HIS A N     1 
ATOM   8357  C CA    . HIS A 1 1116 ? 13.579  69.027  113.037 1.00 14.85 ?  1114 HIS A CA    1 
ATOM   8358  C C     . HIS A 1 1116 ? 12.470  69.685  112.224 1.00 14.13 ?  1114 HIS A C     1 
ATOM   8359  O O     . HIS A 1 1116 ? 11.525  69.011  111.788 1.00 15.06 ?  1114 HIS A O     1 
ATOM   8360  C CB    . HIS A 1 1116 ? 13.337  69.225  114.532 1.00 15.16 ?  1114 HIS A CB    1 
ATOM   8361  C CG    . HIS A 1 1116 ? 13.961  68.170  115.391 1.00 16.77 ?  1114 HIS A CG    1 
ATOM   8362  N ND1   . HIS A 1 1116 ? 15.264  68.247  115.845 1.00 19.56 ?  1114 HIS A ND1   1 
ATOM   8363  C CD2   . HIS A 1 1116 ? 13.455  67.019  115.897 1.00 19.12 ?  1114 HIS A CD2   1 
ATOM   8364  C CE1   . HIS A 1 1116 ? 15.534  67.185  116.586 1.00 18.33 ?  1114 HIS A CE1   1 
ATOM   8365  N NE2   . HIS A 1 1116 ? 14.451  66.431  116.644 1.00 22.24 ?  1114 HIS A NE2   1 
ATOM   8366  N N     . GLN A 1 1117 ? 12.556  71.002  112.008 1.00 13.12 ?  1115 GLN A N     1 
ATOM   8367  C CA    . GLN A 1 1117 ? 11.549  71.690  111.198 1.00 12.90 ?  1115 GLN A CA    1 
ATOM   8368  C C     . GLN A 1 1117 ? 11.535  71.173  109.764 1.00 12.50 ?  1115 GLN A C     1 
ATOM   8369  O O     . GLN A 1 1117 ? 10.465  70.955  109.179 1.00 13.06 ?  1115 GLN A O     1 
ATOM   8370  C CB    . GLN A 1 1117 ? 11.815  73.198  111.204 1.00 14.19 ?  1115 GLN A CB    1 
ATOM   8371  C CG    . GLN A 1 1117 ? 11.579  73.893  112.537 1.00 15.74 ?  1115 GLN A CG    1 
ATOM   8372  C CD    . GLN A 1 1117 ? 11.834  75.379  112.445 1.00 16.92 ?  1115 GLN A CD    1 
ATOM   8373  O OE1   . GLN A 1 1117 ? 12.388  75.860  111.457 1.00 16.28 ?  1115 GLN A OE1   1 
ATOM   8374  N NE2   . GLN A 1 1117 ? 11.423  76.119  113.469 1.00 14.99 ?  1115 GLN A NE2   1 
ATOM   8375  N N     . LEU A 1 1118 ? 12.722  70.992  109.186 1.00 12.49 ?  1116 LEU A N     1 
ATOM   8376  C CA    A LEU A 1 1118 ? 12.805  70.513  107.812 0.48 13.74 ?  1116 LEU A CA    1 
ATOM   8377  C CA    B LEU A 1 1118 ? 12.840  70.492  107.819 0.52 13.74 ?  1116 LEU A CA    1 
ATOM   8378  C C     . LEU A 1 1118 ? 12.278  69.087  107.700 1.00 12.68 ?  1116 LEU A C     1 
ATOM   8379  O O     . LEU A 1 1118 ? 11.567  68.768  106.738 1.00 12.54 ?  1116 LEU A O     1 
ATOM   8380  C CB    A LEU A 1 1118 ? 14.245  70.619  107.306 0.48 14.79 ?  1116 LEU A CB    1 
ATOM   8381  C CB    B LEU A 1 1118 ? 14.303  70.502  107.390 0.52 14.80 ?  1116 LEU A CB    1 
ATOM   8382  C CG    A LEU A 1 1118 ? 14.454  70.468  105.796 0.48 13.34 ?  1116 LEU A CG    1 
ATOM   8383  C CG    B LEU A 1 1118 ? 14.869  71.850  106.986 0.52 14.02 ?  1116 LEU A CG    1 
ATOM   8384  C CD1   A LEU A 1 1118 ? 13.454  71.310  105.023 0.48 13.46 ?  1116 LEU A CD1   1 
ATOM   8385  C CD1   B LEU A 1 1118 ? 16.372  71.764  106.921 0.52 15.37 ?  1116 LEU A CD1   1 
ATOM   8386  C CD2   A LEU A 1 1118 ? 15.867  70.858  105.409 0.48 16.68 ?  1116 LEU A CD2   1 
ATOM   8387  C CD2   B LEU A 1 1118 ? 14.309  72.223  105.633 0.52 14.41 ?  1116 LEU A CD2   1 
ATOM   8388  N N     . ALA A 1 1119 ? 12.587  68.231  108.676 1.00 14.96 ?  1117 ALA A N     1 
ATOM   8389  C CA    . ALA A 1 1119 ? 12.060  66.871  108.650 1.00 15.06 ?  1117 ALA A CA    1 
ATOM   8390  C C     . ALA A 1 1119 ? 10.533  66.876  108.671 1.00 14.37 ?  1117 ALA A C     1 
ATOM   8391  O O     . ALA A 1 1119 ? 9.890   66.168  107.886 1.00 14.42 ?  1117 ALA A O     1 
ATOM   8392  C CB    . ALA A 1 1119 ? 12.624  66.071  109.823 1.00 16.90 ?  1117 ALA A CB    1 
ATOM   8393  N N     . ALA A 1 1120 ? 9.933   67.691  109.549 1.00 13.57 ?  1118 ALA A N     1 
ATOM   8394  C CA    . ALA A 1 1120 ? 8.475   67.748  109.635 1.00 13.56 ?  1118 ALA A CA    1 
ATOM   8395  C C     . ALA A 1 1120 ? 7.856   68.230  108.329 1.00 13.26 ?  1118 ALA A C     1 
ATOM   8396  O O     . ALA A 1 1120 ? 6.874   67.649  107.844 1.00 13.17 ?  1118 ALA A O     1 
ATOM   8397  C CB    . ALA A 1 1120 ? 8.054   68.663  110.787 1.00 12.12 ?  1118 ALA A CB    1 
ATOM   8398  N N     . ALA A 1 1121 ? 8.412   69.293  107.744 1.00 11.52 ?  1119 ALA A N     1 
ATOM   8399  C CA    . ALA A 1 1121 ? 7.857   69.840  106.505 1.00 13.51 ?  1119 ALA A CA    1 
ATOM   8400  C C     . ALA A 1 1121 ? 8.051   68.898  105.321 1.00 11.76 ?  1119 ALA A C     1 
ATOM   8401  O O     . ALA A 1 1121 ? 7.142   68.748  104.487 1.00 11.61 ?  1119 ALA A O     1 
ATOM   8402  C CB    . ALA A 1 1121 ? 8.500   71.196  106.219 1.00 15.35 ?  1119 ALA A CB    1 
ATOM   8403  N N     . LEU A 1 1122 ? 9.231   68.283  105.207 1.00 12.38 ?  1120 LEU A N     1 
ATOM   8404  C CA    . LEU A 1 1122 ? 9.490   67.404  104.065 1.00 11.20 ?  1120 LEU A CA    1 
ATOM   8405  C C     . LEU A 1 1122 ? 8.690   66.111  104.169 1.00 11.40 ?  1120 LEU A C     1 
ATOM   8406  O O     . LEU A 1 1122 ? 8.227   65.581  103.146 1.00 12.12 ?  1120 LEU A O     1 
ATOM   8407  C CB    . LEU A 1 1122 ? 10.984  67.092  103.958 1.00 14.29 ?  1120 LEU A CB    1 
ATOM   8408  C CG    . LEU A 1 1122 ? 11.930  68.253  103.678 1.00 14.11 ?  1120 LEU A CG    1 
ATOM   8409  C CD1   . LEU A 1 1122 ? 13.356  67.737  103.730 1.00 16.28 ?  1120 LEU A CD1   1 
ATOM   8410  C CD2   . LEU A 1 1122 ? 11.607  68.851  102.301 1.00 14.63 ?  1120 LEU A CD2   1 
ATOM   8411  N N     . ALA A 1 1123 ? 8.526   65.582  105.393 1.00 11.75 ?  1121 ALA A N     1 
ATOM   8412  C CA    . ALA A 1 1123 ? 7.755   64.354  105.589 1.00 11.47 ?  1121 ALA A CA    1 
ATOM   8413  C C     . ALA A 1 1123 ? 6.312   64.507  105.152 1.00 12.91 ?  1121 ALA A C     1 
ATOM   8414  O O     . ALA A 1 1123 ? 5.659   63.503  104.844 1.00 13.01 ?  1121 ALA A O     1 
ATOM   8415  C CB    . ALA A 1 1123 ? 7.779   63.941  107.058 1.00 12.37 ?  1121 ALA A CB    1 
ATOM   8416  N N     . THR A 1 1124 ? 5.798   65.734  105.141 1.00 10.57 ?  1122 THR A N     1 
ATOM   8417  C CA    . THR A 1 1124 ? 4.439   66.024  104.730 1.00 11.92 ?  1122 THR A CA    1 
ATOM   8418  C C     . THR A 1 1124 ? 4.383   66.601  103.313 1.00 11.86 ?  1122 THR A C     1 
ATOM   8419  O O     . THR A 1 1124 ? 3.345   67.126  102.897 1.00 12.64 ?  1122 THR A O     1 
ATOM   8420  C CB    . THR A 1 1124 ? 3.791   66.941  105.782 1.00 12.29 ?  1122 THR A CB    1 
ATOM   8421  O OG1   . THR A 1 1124 ? 4.687   68.013  106.110 1.00 12.28 ?  1122 THR A OG1   1 
ATOM   8422  C CG2   . THR A 1 1124 ? 3.547   66.135  107.073 1.00 13.07 ?  1122 THR A CG2   1 
ATOM   8423  N N     . GLY A 1 1125 ? 5.481   66.482  102.556 1.00 11.02 ?  1123 GLY A N     1 
ATOM   8424  C CA    . GLY A 1 1125 ? 5.483   66.748  101.128 1.00 13.19 ?  1123 GLY A CA    1 
ATOM   8425  C C     . GLY A 1 1125 ? 5.715   68.189  100.739 1.00 12.65 ?  1123 GLY A C     1 
ATOM   8426  O O     . GLY A 1 1125 ? 5.613   68.529  99.547  1.00 14.03 ?  1123 GLY A O     1 
ATOM   8427  N N     . ASN A 1 1126 ? 6.014   69.051  101.703 1.00 12.47 ?  1124 ASN A N     1 
ATOM   8428  C CA    . ASN A 1 1126 ? 6.094   70.480  101.470 1.00 12.74 ?  1124 ASN A CA    1 
ATOM   8429  C C     . ASN A 1 1126 ? 7.480   70.902  101.004 1.00 12.00 ?  1124 ASN A C     1 
ATOM   8430  O O     . ASN A 1 1126 ? 8.480   70.208  101.208 1.00 13.43 ?  1124 ASN A O     1 
ATOM   8431  C CB    . ASN A 1 1126 ? 5.758   71.251  102.754 1.00 12.44 ?  1124 ASN A CB    1 
ATOM   8432  C CG    . ASN A 1 1126 ? 4.364   70.955  103.252 1.00 13.64 ?  1124 ASN A CG    1 
ATOM   8433  O OD1   . ASN A 1 1126 ? 3.379   71.387  102.651 1.00 13.82 ?  1124 ASN A OD1   1 
ATOM   8434  N ND2   . ASN A 1 1126 ? 4.270   70.220  104.353 1.00 11.79 ?  1124 ASN A ND2   1 
ATOM   8435  N N     . SER A 1 1127 ? 7.516   72.067  100.367 1.00 14.08 ?  1125 SER A N     1 
ATOM   8436  C CA    . SER A 1 1127 ? 8.747   72.818  100.204 1.00 12.66 ?  1125 SER A CA    1 
ATOM   8437  C C     . SER A 1 1127 ? 8.851   73.787  101.369 1.00 14.31 ?  1125 SER A C     1 
ATOM   8438  O O     . SER A 1 1127 ? 7.908   73.941  102.153 1.00 14.53 ?  1125 SER A O     1 
ATOM   8439  C CB    . SER A 1 1127 ? 8.771   73.560  98.868  1.00 16.53 ?  1125 SER A CB    1 
ATOM   8440  O OG    . SER A 1 1127 ? 7.713   74.487  98.775  1.00 20.19 ?  1125 SER A OG    1 
ATOM   8441  N N     . VAL A 1 1128 ? 10.010  74.434  101.494 1.00 15.93 ?  1126 VAL A N     1 
ATOM   8442  C CA    . VAL A 1 1128 ? 10.237  75.351  102.603 1.00 15.05 ?  1126 VAL A CA    1 
ATOM   8443  C C     . VAL A 1 1128 ? 10.922  76.618  102.121 1.00 17.51 ?  1126 VAL A C     1 
ATOM   8444  O O     . VAL A 1 1128 ? 11.678  76.615  101.145 1.00 17.84 ?  1126 VAL A O     1 
ATOM   8445  C CB    . VAL A 1 1128 ? 11.081  74.718  103.732 1.00 16.87 ?  1126 VAL A CB    1 
ATOM   8446  C CG1   . VAL A 1 1128 ? 10.413  73.467  104.252 1.00 15.64 ?  1126 VAL A CG1   1 
ATOM   8447  C CG2   . VAL A 1 1128 ? 12.508  74.413  103.254 1.00 16.54 ?  1126 VAL A CG2   1 
ATOM   8448  N N     . ALA A 1 1129 ? 10.654  77.703  102.838 1.00 16.72 ?  1127 ALA A N     1 
ATOM   8449  C CA    . ALA A 1 1129 ? 11.447  78.919  102.784 1.00 15.93 ?  1127 ALA A CA    1 
ATOM   8450  C C     . ALA A 1 1129 ? 12.007  79.137  104.180 1.00 16.84 ?  1127 ALA A C     1 
ATOM   8451  O O     . ALA A 1 1129 ? 11.240  79.278  105.137 1.00 18.10 ?  1127 ALA A O     1 
ATOM   8452  C CB    . ALA A 1 1129 ? 10.606  80.115  102.346 1.00 18.81 ?  1127 ALA A CB    1 
ATOM   8453  N N     . ILE A 1 1130 ? 13.325  79.141  104.300 1.00 15.72 ?  1128 ILE A N     1 
ATOM   8454  C CA    . ILE A 1 1130 ? 13.978  79.256  105.602 1.00 16.75 ?  1128 ILE A CA    1 
ATOM   8455  C C     . ILE A 1 1130 ? 14.395  80.702  105.827 1.00 20.05 ?  1128 ILE A C     1 
ATOM   8456  O O     . ILE A 1 1130 ? 15.028  81.317  104.961 1.00 21.21 ?  1128 ILE A O     1 
ATOM   8457  C CB    . ILE A 1 1130 ? 15.195  78.325  105.713 1.00 15.85 ?  1128 ILE A CB    1 
ATOM   8458  C CG1   . ILE A 1 1130 ? 14.846  76.902  105.260 1.00 18.83 ?  1128 ILE A CG1   1 
ATOM   8459  C CG2   . ILE A 1 1130 ? 15.707  78.313  107.160 1.00 17.40 ?  1128 ILE A CG2   1 
ATOM   8460  C CD1   . ILE A 1 1130 ? 16.054  76.002  105.120 1.00 16.90 ?  1128 ILE A CD1   1 
ATOM   8461  N N     . ASP A 1 1131 ? 14.069  81.231  107.003 1.00 17.65 ?  1129 ASP A N     1 
ATOM   8462  C CA    . ASP A 1 1131 ? 14.474  82.578  107.383 1.00 19.80 ?  1129 ASP A CA    1 
ATOM   8463  C C     . ASP A 1 1131 ? 15.987  82.756  107.310 1.00 18.78 ?  1129 ASP A C     1 
ATOM   8464  O O     . ASP A 1 1131 ? 16.737  82.136  108.071 1.00 20.13 ?  1129 ASP A O     1 
ATOM   8465  C CB    . ASP A 1 1131 ? 13.973  82.882  108.791 1.00 17.01 ?  1129 ASP A CB    1 
ATOM   8466  C CG    . ASP A 1 1131 ? 14.332  84.270  109.246 1.00 23.46 ?  1129 ASP A CG    1 
ATOM   8467  O OD1   . ASP A 1 1131 ? 14.428  85.191  108.400 1.00 21.94 ?  1129 ASP A OD1   1 
ATOM   8468  O OD2   . ASP A 1 1131 ? 14.523  84.432  110.459 1.00 21.88 ?  1129 ASP A OD2   1 
ATOM   8469  N N     . ALA A 1 1132 ? 16.450  83.607  106.389 1.00 23.11 ?  1130 ALA A N     1 
ATOM   8470  C CA    . ALA A 1 1132 ? 17.883  83.851  106.279 1.00 21.14 ?  1130 ALA A CA    1 
ATOM   8471  C C     . ALA A 1 1132 ? 18.431  84.617  107.476 1.00 23.14 ?  1130 ALA A C     1 
ATOM   8472  O O     . ALA A 1 1132 ? 19.624  84.502  107.778 1.00 28.66 ?  1130 ALA A O     1 
ATOM   8473  C CB    . ALA A 1 1132 ? 18.183  84.602  104.982 1.00 27.50 ?  1130 ALA A CB    1 
ATOM   8474  N N     . ALA A 1 1133 ? 17.584  85.371  108.179 1.00 23.95 ?  1131 ALA A N     1 
ATOM   8475  C CA    . ALA A 1 1133 ? 18.032  86.071  109.378 1.00 24.99 ?  1131 ALA A CA    1 
ATOM   8476  C C     . ALA A 1 1133 ? 18.377  85.124  110.522 1.00 27.64 ?  1131 ALA A C     1 
ATOM   8477  O O     . ALA A 1 1133 ? 18.899  85.577  111.542 1.00 30.01 ?  1131 ALA A O     1 
ATOM   8478  C CB    . ALA A 1 1133 ? 16.968  87.076  109.826 1.00 28.44 ?  1131 ALA A CB    1 
ATOM   8479  N N     . SER A 1 1134 ? 18.102  83.826  110.382 1.00 24.85 ?  1132 SER A N     1 
ATOM   8480  C CA    . SER A 1 1134 ? 18.518  82.850  111.384 1.00 23.41 ?  1132 SER A CA    1 
ATOM   8481  C C     . SER A 1 1134 ? 20.025  82.673  111.441 1.00 22.16 ?  1132 SER A C     1 
ATOM   8482  O O     . SER A 1 1134 ? 20.542  82.218  112.466 1.00 23.41 ?  1132 SER A O     1 
ATOM   8483  C CB    . SER A 1 1134 ? 17.894  81.486  111.090 1.00 22.21 ?  1132 SER A CB    1 
ATOM   8484  O OG    . SER A 1 1134 ? 18.383  80.958  109.858 1.00 23.62 ?  1132 SER A OG    1 
ATOM   8485  N N     . GLY A 1 1135 ? 20.729  82.976  110.352 1.00 25.99 ?  1133 GLY A N     1 
ATOM   8486  C CA    . GLY A 1 1135 ? 22.157  82.747  110.275 1.00 24.79 ?  1133 GLY A CA    1 
ATOM   8487  C C     . GLY A 1 1135 ? 22.583  81.299  110.183 1.00 27.34 ?  1133 GLY A C     1 
ATOM   8488  O O     . GLY A 1 1135 ? 23.755  80.996  110.421 1.00 28.42 ?  1133 GLY A O     1 
ATOM   8489  N N     . LEU A 1 1136 ? 21.672  80.386  109.844 1.00 23.20 ?  1134 LEU A N     1 
ATOM   8490  C CA    . LEU A 1 1136 ? 21.970  78.960  109.885 1.00 24.11 ?  1134 LEU A CA    1 
ATOM   8491  C C     . LEU A 1 1136 ? 22.304  78.383  108.512 1.00 27.27 ?  1134 LEU A C     1 
ATOM   8492  O O     . LEU A 1 1136 ? 22.241  77.162  108.336 1.00 26.09 ?  1134 LEU A O     1 
ATOM   8493  C CB    . LEU A 1 1136 ? 20.795  78.196  110.507 1.00 23.11 ?  1134 LEU A CB    1 
ATOM   8494  C CG    . LEU A 1 1136 ? 20.515  78.481  111.987 1.00 20.53 ?  1134 LEU A CG    1 
ATOM   8495  C CD1   . LEU A 1 1136 ? 19.200  77.833  112.403 1.00 19.57 ?  1134 LEU A CD1   1 
ATOM   8496  C CD2   . LEU A 1 1136 ? 21.648  77.966  112.850 1.00 23.09 ?  1134 LEU A CD2   1 
ATOM   8497  N N     . GLN A 1 1137 ? 22.673  79.227  107.543 1.00 24.04 ?  1135 GLN A N     1 
ATOM   8498  C CA    . GLN A 1 1137 ? 22.933  78.730  106.192 1.00 25.80 ?  1135 GLN A CA    1 
ATOM   8499  C C     . GLN A 1 1137 ? 24.020  77.659  106.185 1.00 24.28 ?  1135 GLN A C     1 
ATOM   8500  O O     . GLN A 1 1137 ? 23.932  76.680  105.431 1.00 24.39 ?  1135 GLN A O     1 
ATOM   8501  C CB    . GLN A 1 1137 ? 23.310  79.888  105.268 1.00 25.08 ?  1135 GLN A CB    1 
ATOM   8502  C CG    . GLN A 1 1137 ? 22.156  80.810  104.924 1.00 25.95 ?  1135 GLN A CG    1 
ATOM   8503  C CD    . GLN A 1 1137 ? 21.949  81.908  105.953 1.00 26.13 ?  1135 GLN A CD    1 
ATOM   8504  O OE1   . GLN A 1 1137 ? 22.544  81.896  107.038 1.00 29.10 ?  1135 GLN A OE1   1 
ATOM   8505  N NE2   . GLN A 1 1137 ? 21.111  82.873  105.610 1.00 30.04 ?  1135 GLN A NE2   1 
ATOM   8506  N N     . ALA A 1 1138 ? 25.039  77.810  107.031 1.00 24.43 ?  1136 ALA A N     1 
ATOM   8507  C CA    . ALA A 1 1138 ? 26.131  76.846  107.080 1.00 26.46 ?  1136 ALA A CA    1 
ATOM   8508  C C     . ALA A 1 1138 ? 25.716  75.495  107.650 1.00 28.31 ?  1136 ALA A C     1 
ATOM   8509  O O     . ALA A 1 1138 ? 26.507  74.548  107.584 1.00 30.23 ?  1136 ALA A O     1 
ATOM   8510  C CB    . ALA A 1 1138 ? 27.291  77.416  107.899 1.00 25.07 ?  1136 ALA A CB    1 
ATOM   8511  N N     . SER A 1 1139 ? 24.509  75.376  108.202 1.00 27.36 ?  1137 SER A N     1 
ATOM   8512  C CA    . SER A 1 1139 ? 24.033  74.089  108.690 1.00 25.00 ?  1137 SER A CA    1 
ATOM   8513  C C     . SER A 1 1139 ? 23.451  73.216  107.584 1.00 24.75 ?  1137 SER A C     1 
ATOM   8514  O O     . SER A 1 1139 ? 23.186  72.037  107.833 1.00 26.63 ?  1137 SER A O     1 
ATOM   8515  C CB    . SER A 1 1139 ? 22.974  74.294  109.785 1.00 23.92 ?  1137 SER A CB    1 
ATOM   8516  O OG    . SER A 1 1139 ? 23.529  74.890  110.946 1.00 25.93 ?  1137 SER A OG    1 
ATOM   8517  N N     . LEU A 1 1140 ? 23.258  73.753  106.381 1.00 23.59 ?  1138 LEU A N     1 
ATOM   8518  C CA    . LEU A 1 1140 ? 22.578  73.049  105.292 1.00 24.85 ?  1138 LEU A CA    1 
ATOM   8519  C C     . LEU A 1 1140 ? 23.424  73.042  104.031 1.00 25.27 ?  1138 LEU A C     1 
ATOM   8520  O O     . LEU A 1 1140 ? 22.932  73.323  102.938 1.00 28.50 ?  1138 LEU A O     1 
ATOM   8521  C CB    . LEU A 1 1140 ? 21.227  73.674  104.958 1.00 29.05 ?  1138 LEU A CB    1 
ATOM   8522  C CG    . LEU A 1 1140 ? 19.947  73.310  105.704 1.00 29.55 ?  1138 LEU A CG    1 
ATOM   8523  C CD1   . LEU A 1 1140 ? 18.794  73.654  104.785 1.00 26.35 ?  1138 LEU A CD1   1 
ATOM   8524  C CD2   . LEU A 1 1140 ? 19.893  71.851  106.135 1.00 22.76 ?  1138 LEU A CD2   1 
ATOM   8525  N N     . LYS A 1 1141 ? 24.709  72.727  104.160 1.00 25.95 ?  1139 LYS A N     1 
ATOM   8526  C CA    . LYS A 1 1141 ? 25.595  72.684  103.004 1.00 29.80 ?  1139 LYS A CA    1 
ATOM   8527  C C     . LYS A 1 1141 ? 25.520  71.336  102.295 1.00 28.05 ?  1139 LYS A C     1 
ATOM   8528  O O     . LYS A 1 1141 ? 25.346  70.288  102.922 1.00 28.02 ?  1139 LYS A O     1 
ATOM   8529  C CB    . LYS A 1 1141 ? 27.043  72.954  103.417 1.00 32.18 ?  1139 LYS A CB    1 
ATOM   8530  C CG    . LYS A 1 1141 ? 27.323  74.379  103.845 1.00 34.64 ?  1139 LYS A CG    1 
ATOM   8531  C CD    . LYS A 1 1141 ? 28.811  74.586  104.087 1.00 35.16 ?  1139 LYS A CD    1 
ATOM   8532  N N     . ASN A 1 1142 ? 25.678  71.374  100.973 1.00 28.42 ?  1140 ASN A N     1 
ATOM   8533  C CA    . ASN A 1 1142 ? 25.825  70.164  100.164 1.00 29.75 ?  1140 ASN A CA    1 
ATOM   8534  C C     . ASN A 1 1142 ? 24.591  69.269  100.242 1.00 24.58 ?  1140 ASN A C     1 
ATOM   8535  O O     . ASN A 1 1142 ? 24.703  68.047  100.351 1.00 25.98 ?  1140 ASN A O     1 
ATOM   8536  C CB    . ASN A 1 1142 ? 27.069  69.376  100.574 1.00 30.42 ?  1140 ASN A CB    1 
ATOM   8537  C CG    . ASN A 1 1142 ? 28.277  70.263  100.775 1.00 40.33 ?  1140 ASN A CG    1 
ATOM   8538  O OD1   . ASN A 1 1142 ? 28.778  70.402  101.891 1.00 40.72 ?  1140 ASN A OD1   1 
ATOM   8539  N ND2   . ASN A 1 1142 ? 28.750  70.873  99.694  1.00 42.76 ?  1140 ASN A ND2   1 
ATOM   8540  N N     . LEU A 1 1143 ? 23.409  69.872  100.183 1.00 25.43 ?  1141 LEU A N     1 
ATOM   8541  C CA    . LEU A 1 1143 ? 22.191  69.078  100.159 1.00 24.06 ?  1141 LEU A CA    1 
ATOM   8542  C C     . LEU A 1 1143 ? 22.092  68.273  98.865  1.00 24.38 ?  1141 LEU A C     1 
ATOM   8543  O O     . LEU A 1 1143 ? 22.536  68.727  97.806  1.00 25.73 ?  1141 LEU A O     1 
ATOM   8544  C CB    . LEU A 1 1143 ? 20.960  69.968  100.279 1.00 22.85 ?  1141 LEU A CB    1 
ATOM   8545  C CG    . LEU A 1 1143 ? 20.558  70.501  101.648 1.00 24.86 ?  1141 LEU A CG    1 
ATOM   8546  C CD1   . LEU A 1 1143 ? 19.430  71.491  101.437 1.00 22.21 ?  1141 LEU A CD1   1 
ATOM   8547  C CD2   . LEU A 1 1143 ? 20.134  69.366  102.585 1.00 21.25 ?  1141 LEU A CD2   1 
ATOM   8548  N N     . PRO A 1 1144 ? 21.494  67.082  98.917  1.00 22.79 ?  1142 PRO A N     1 
ATOM   8549  C CA    . PRO A 1 1144 ? 21.130  66.398  97.673  1.00 24.95 ?  1142 PRO A CA    1 
ATOM   8550  C C     . PRO A 1 1144 ? 20.248  67.303  96.828  1.00 23.22 ?  1142 PRO A C     1 
ATOM   8551  O O     . PRO A 1 1144 ? 19.450  68.088  97.346  1.00 20.60 ?  1142 PRO A O     1 
ATOM   8552  C CB    . PRO A 1 1144 ? 20.362  65.158  98.151  1.00 25.51 ?  1142 PRO A CB    1 
ATOM   8553  C CG    . PRO A 1 1144 ? 20.715  65.001  99.603  1.00 25.36 ?  1142 PRO A CG    1 
ATOM   8554  C CD    . PRO A 1 1144 ? 20.994  66.380  100.112 1.00 24.44 ?  1142 PRO A CD    1 
ATOM   8555  N N     . GLN A 1 1145 ? 20.397  67.201  95.508  1.00 23.49 ?  1143 GLN A N     1 
ATOM   8556  C CA    . GLN A 1 1145 ? 19.614  68.081  94.653  1.00 21.11 ?  1143 GLN A CA    1 
ATOM   8557  C C     . GLN A 1 1145 ? 18.115  67.913  94.884  1.00 21.00 ?  1143 GLN A C     1 
ATOM   8558  O O     . GLN A 1 1145 ? 17.366  68.890  94.782  1.00 23.03 ?  1143 GLN A O     1 
ATOM   8559  C CB    . GLN A 1 1145 ? 19.960  67.842  93.182  1.00 29.04 ?  1143 GLN A CB    1 
ATOM   8560  C CG    . GLN A 1 1145 ? 19.581  69.028  92.299  1.00 37.16 ?  1143 GLN A CG    1 
ATOM   8561  C CD    . GLN A 1 1145 ? 19.956  70.367  92.941  1.00 41.15 ?  1143 GLN A CD    1 
ATOM   8562  O OE1   . GLN A 1 1145 ? 19.097  71.080  93.472  1.00 39.78 ?  1143 GLN A OE1   1 
ATOM   8563  N NE2   . GLN A 1 1145 ? 21.242  70.707  92.898  1.00 46.84 ?  1143 GLN A NE2   1 
ATOM   8564  N N     . THR A 1 1146 ? 17.655  66.692  95.188  1.00 21.06 ?  1144 THR A N     1 
ATOM   8565  C CA    . THR A 1 1146 ? 16.227  66.479  95.418  1.00 21.86 ?  1144 THR A CA    1 
ATOM   8566  C C     . THR A 1 1146 ? 15.726  67.326  96.576  1.00 22.57 ?  1144 THR A C     1 
ATOM   8567  O O     . THR A 1 1146 ? 14.598  67.837  96.542  1.00 21.53 ?  1144 THR A O     1 
ATOM   8568  C CB    . THR A 1 1146 ? 15.940  65.007  95.707  1.00 23.10 ?  1144 THR A CB    1 
ATOM   8569  O OG1   . THR A 1 1146 ? 16.760  64.572  96.799  1.00 22.86 ?  1144 THR A OG1   1 
ATOM   8570  C CG2   . THR A 1 1146 ? 16.226  64.151  94.476  1.00 24.27 ?  1144 THR A CG2   1 
ATOM   8571  N N     . VAL A 1 1147 ? 16.544  67.462  97.622  1.00 22.10 ?  1145 VAL A N     1 
ATOM   8572  C CA    . VAL A 1 1147 ? 16.166  68.286  98.762  1.00 18.06 ?  1145 VAL A CA    1 
ATOM   8573  C C     . VAL A 1 1147 ? 16.376  69.761  98.450  1.00 16.52 ?  1145 VAL A C     1 
ATOM   8574  O O     . VAL A 1 1147 ? 15.540  70.601  98.791  1.00 19.40 ?  1145 VAL A O     1 
ATOM   8575  C CB    . VAL A 1 1147 ? 16.950  67.857  100.013 1.00 16.88 ?  1145 VAL A CB    1 
ATOM   8576  C CG1   . VAL A 1 1147 ? 16.500  68.681  101.238 1.00 17.35 ?  1145 VAL A CG1   1 
ATOM   8577  C CG2   . VAL A 1 1147 ? 16.807  66.350  100.274 1.00 18.85 ?  1145 VAL A CG2   1 
ATOM   8578  N N     . GLY A 1 1148 ? 17.488  70.102  97.786  1.00 18.22 ?  1146 GLY A N     1 
ATOM   8579  C CA    . GLY A 1 1148 ? 17.717  71.492  97.419  1.00 20.03 ?  1146 GLY A CA    1 
ATOM   8580  C C     . GLY A 1 1148 ? 16.593  72.085  96.587  1.00 21.12 ?  1146 GLY A C     1 
ATOM   8581  O O     . GLY A 1 1148 ? 16.273  73.272  96.717  1.00 21.31 ?  1146 GLY A O     1 
ATOM   8582  N N     . LEU A 1 1149 ? 15.974  71.270  95.720  1.00 20.10 ?  1147 LEU A N     1 
ATOM   8583  C CA    . LEU A 1 1149 ? 14.853  71.743  94.908  1.00 21.12 ?  1147 LEU A CA    1 
ATOM   8584  C C     . LEU A 1 1149 ? 13.692  72.218  95.769  1.00 18.31 ?  1147 LEU A C     1 
ATOM   8585  O O     . LEU A 1 1149 ? 12.883  73.044  95.325  1.00 22.26 ?  1147 LEU A O     1 
ATOM   8586  C CB    . LEU A 1 1149 ? 14.361  70.641  93.964  1.00 24.33 ?  1147 LEU A CB    1 
ATOM   8587  C CG    . LEU A 1 1149 ? 15.263  70.187  92.820  1.00 31.50 ?  1147 LEU A CG    1 
ATOM   8588  C CD1   . LEU A 1 1149 ? 14.602  69.024  92.120  1.00 28.90 ?  1147 LEU A CD1   1 
ATOM   8589  C CD2   . LEU A 1 1149 ? 15.521  71.324  91.857  1.00 33.27 ?  1147 LEU A CD2   1 
ATOM   8590  N N     . ARG A 1 1150 ? 13.595  71.708  96.996  1.00 18.51 ?  1148 ARG A N     1 
ATOM   8591  C CA    . ARG A 1 1150 ? 12.522  72.069  97.910  1.00 17.20 ?  1148 ARG A CA    1 
ATOM   8592  C C     . ARG A 1 1150 ? 12.898  73.165  98.892  1.00 17.52 ?  1148 ARG A C     1 
ATOM   8593  O O     . ARG A 1 1150 ? 12.030  73.610  99.649  1.00 19.62 ?  1148 ARG A O     1 
ATOM   8594  C CB    . ARG A 1 1150 ? 12.077  70.841  98.702  1.00 16.55 ?  1148 ARG A CB    1 
ATOM   8595  C CG    . ARG A 1 1150 ? 11.285  69.849  97.875  1.00 19.52 ?  1148 ARG A CG    1 
ATOM   8596  C CD    . ARG A 1 1150 ? 10.192  69.284  98.734  1.00 17.77 ?  1148 ARG A CD    1 
ATOM   8597  N NE    . ARG A 1 1150 ? 9.574   68.103  98.147  1.00 16.90 ?  1148 ARG A NE    1 
ATOM   8598  C CZ    . ARG A 1 1150 ? 9.031   67.146  98.879  1.00 18.19 ?  1148 ARG A CZ    1 
ATOM   8599  N NH1   . ARG A 1 1150 ? 8.984   67.237  100.206 1.00 15.43 ?  1148 ARG A NH1   1 
ATOM   8600  N NH2   . ARG A 1 1150 ? 8.534   66.071  98.275  1.00 16.69 ?  1148 ARG A NH2   1 
ATOM   8601  N N     . VAL A 1 1151 ? 14.154  73.601  98.907  1.00 17.63 ?  1149 VAL A N     1 
ATOM   8602  C CA    . VAL A 1 1151 ? 14.660  74.516  99.925  1.00 18.61 ?  1149 VAL A CA    1 
ATOM   8603  C C     . VAL A 1 1151 ? 14.979  75.856  99.285  1.00 22.27 ?  1149 VAL A C     1 
ATOM   8604  O O     . VAL A 1 1151 ? 15.672  75.925  98.264  1.00 22.50 ?  1149 VAL A O     1 
ATOM   8605  C CB    . VAL A 1 1151 ? 15.900  73.944  100.632 1.00 20.17 ?  1149 VAL A CB    1 
ATOM   8606  C CG1   . VAL A 1 1151 ? 16.552  75.001  101.529 1.00 21.28 ?  1149 VAL A CG1   1 
ATOM   8607  C CG2   . VAL A 1 1151 ? 15.528  72.733  101.450 1.00 18.06 ?  1149 VAL A CG2   1 
ATOM   8608  N N     . SER A 1 1152 ? 14.475  76.920  99.886  1.00 21.06 ?  1150 SER A N     1 
ATOM   8609  C CA    . SER A 1 1152 ? 14.910  78.258  99.549  1.00 20.82 ?  1150 SER A CA    1 
ATOM   8610  C C     . SER A 1 1152 ? 15.133  79.014  100.845 1.00 21.92 ?  1150 SER A C     1 
ATOM   8611  O O     . SER A 1 1152 ? 14.622  78.640  101.905 1.00 22.10 ?  1150 SER A O     1 
ATOM   8612  C CB    . SER A 1 1152 ? 13.899  78.994  98.670  1.00 24.40 ?  1150 SER A CB    1 
ATOM   8613  O OG    . SER A 1 1152 ? 12.676  79.179  99.351  1.00 27.10 ?  1150 SER A OG    1 
ATOM   8614  N N     . TRP A 1 1153 ? 15.932  80.065  100.753 1.00 22.31 ?  1151 TRP A N     1 
ATOM   8615  C CA    . TRP A 1 1153 ? 16.212  80.935  101.880 1.00 22.61 ?  1151 TRP A CA    1 
ATOM   8616  C C     . TRP A 1 1153 ? 15.589  82.294  101.608 1.00 25.95 ?  1151 TRP A C     1 
ATOM   8617  O O     . TRP A 1 1153 ? 15.676  82.811  100.490 1.00 29.70 ?  1151 TRP A O     1 
ATOM   8618  C CB    . TRP A 1 1153 ? 17.712  81.068  102.106 1.00 21.40 ?  1151 TRP A CB    1 
ATOM   8619  C CG    . TRP A 1 1153 ? 18.358  79.834  102.657 1.00 23.93 ?  1151 TRP A CG    1 
ATOM   8620  C CD1   . TRP A 1 1153 ? 18.821  78.760  101.945 1.00 24.51 ?  1151 TRP A CD1   1 
ATOM   8621  C CD2   . TRP A 1 1153 ? 18.625  79.543  104.036 1.00 22.11 ?  1151 TRP A CD2   1 
ATOM   8622  N NE1   . TRP A 1 1153 ? 19.357  77.827  102.795 1.00 24.76 ?  1151 TRP A NE1   1 
ATOM   8623  C CE2   . TRP A 1 1153 ? 19.249  78.280  104.085 1.00 21.98 ?  1151 TRP A CE2   1 
ATOM   8624  C CE3   . TRP A 1 1153 ? 18.393  80.226  105.234 1.00 21.70 ?  1151 TRP A CE3   1 
ATOM   8625  C CZ2   . TRP A 1 1153 ? 19.644  77.687  105.281 1.00 23.36 ?  1151 TRP A CZ2   1 
ATOM   8626  C CZ3   . TRP A 1 1153 ? 18.798  79.634  106.426 1.00 21.42 ?  1151 TRP A CZ3   1 
ATOM   8627  C CH2   . TRP A 1 1153 ? 19.411  78.379  106.439 1.00 24.91 ?  1151 TRP A CH2   1 
ATOM   8628  N N     . SER A 1 1154 ? 14.938  82.858  102.620 1.00 22.49 ?  1152 SER A N     1 
ATOM   8629  C CA    . SER A 1 1154 ? 14.150  84.069  102.449 1.00 22.15 ?  1152 SER A CA    1 
ATOM   8630  C C     . SER A 1 1154 ? 14.665  85.149  103.387 1.00 27.21 ?  1152 SER A C     1 
ATOM   8631  O O     . SER A 1 1154 ? 14.737  84.941  104.604 1.00 24.20 ?  1152 SER A O     1 
ATOM   8632  C CB    . SER A 1 1154 ? 12.668  83.803  102.711 1.00 22.99 ?  1152 SER A CB    1 
ATOM   8633  O OG    . SER A 1 1154 ? 11.909  84.983  102.520 1.00 25.48 ?  1152 SER A OG    1 
ATOM   8634  N N     . LYS A 1 1155 ? 15.022  86.298  102.819 1.00 24.04 ?  1153 LYS A N     1 
ATOM   8635  C CA    . LYS A 1 1155 ? 15.309  87.474  103.628 1.00 29.32 ?  1153 LYS A CA    1 
ATOM   8636  C C     . LYS A 1 1155 ? 14.068  88.341  103.814 1.00 30.03 ?  1153 LYS A C     1 
ATOM   8637  O O     . LYS A 1 1155 ? 13.833  88.860  104.912 1.00 37.70 ?  1153 LYS A O     1 
ATOM   8638  C CB    . LYS A 1 1155 ? 16.446  88.286  102.994 1.00 26.92 ?  1153 LYS A CB    1 
ATOM   8639  N N     . ASP A 1 1156 ? 13.253  88.474  102.773 1.00 29.21 ?  1154 ASP A N     1 
ATOM   8640  C CA    . ASP A 1 1156 ? 12.030  89.275  102.780 1.00 29.41 ?  1154 ASP A CA    1 
ATOM   8641  C C     . ASP A 1 1156 ? 10.860  88.301  102.669 1.00 27.38 ?  1154 ASP A C     1 
ATOM   8642  O O     . ASP A 1 1156 ? 10.458  87.921  101.570 1.00 27.13 ?  1154 ASP A O     1 
ATOM   8643  C CB    . ASP A 1 1156 ? 12.035  90.294  101.621 1.00 32.05 ?  1154 ASP A CB    1 
ATOM   8644  C CG    . ASP A 1 1156 ? 10.797  91.185  101.603 1.00 38.91 ?  1154 ASP A CG    1 
ATOM   8645  O OD1   . ASP A 1 1156 ? 9.879   90.968  102.423 1.00 42.82 ?  1154 ASP A OD1   1 
ATOM   8646  O OD2   . ASP A 1 1156 ? 10.743  92.116  100.762 1.00 42.29 ?  1154 ASP A OD2   1 
ATOM   8647  N N     . TRP A 1 1157 ? 10.301  87.907  103.817 1.00 26.43 ?  1155 TRP A N     1 
ATOM   8648  C CA    . TRP A 1 1157 ? 9.256   86.886  103.804 1.00 24.58 ?  1155 TRP A CA    1 
ATOM   8649  C C     . TRP A 1 1157 ? 8.062   87.308  102.950 1.00 25.49 ?  1155 TRP A C     1 
ATOM   8650  O O     . TRP A 1 1157 ? 7.440   86.470  102.287 1.00 23.37 ?  1155 TRP A O     1 
ATOM   8651  C CB    . TRP A 1 1157 ? 8.787   86.575  105.226 1.00 24.10 ?  1155 TRP A CB    1 
ATOM   8652  C CG    . TRP A 1 1157 ? 9.840   86.146  106.195 1.00 22.40 ?  1155 TRP A CG    1 
ATOM   8653  C CD1   . TRP A 1 1157 ? 11.129  85.791  105.925 1.00 22.20 ?  1155 TRP A CD1   1 
ATOM   8654  C CD2   . TRP A 1 1157 ? 9.687   86.046  107.611 1.00 22.06 ?  1155 TRP A CD2   1 
ATOM   8655  N NE1   . TRP A 1 1157 ? 11.787  85.469  107.088 1.00 23.54 ?  1155 TRP A NE1   1 
ATOM   8656  C CE2   . TRP A 1 1157 ? 10.920  85.624  108.139 1.00 23.91 ?  1155 TRP A CE2   1 
ATOM   8657  C CE3   . TRP A 1 1157 ? 8.620   86.284  108.488 1.00 22.69 ?  1155 TRP A CE3   1 
ATOM   8658  C CZ2   . TRP A 1 1157 ? 11.115  85.418  109.504 1.00 23.68 ?  1155 TRP A CZ2   1 
ATOM   8659  C CZ3   . TRP A 1 1157 ? 8.816   86.084  109.840 1.00 20.88 ?  1155 TRP A CZ3   1 
ATOM   8660  C CH2   . TRP A 1 1157 ? 10.050  85.661  110.335 1.00 22.49 ?  1155 TRP A CH2   1 
ATOM   8661  N N     . ALA A 1 1158 ? 7.719   88.601  102.959 1.00 24.95 ?  1156 ALA A N     1 
ATOM   8662  C CA    . ALA A 1 1158 ? 6.557   89.054  102.203 1.00 26.54 ?  1156 ALA A CA    1 
ATOM   8663  C C     . ALA A 1 1158 ? 6.758   88.886  100.702 1.00 29.49 ?  1156 ALA A C     1 
ATOM   8664  O O     . ALA A 1 1158 ? 5.787   88.665  99.968  1.00 34.76 ?  1156 ALA A O     1 
ATOM   8665  C CB    . ALA A 1 1158 ? 6.248   90.512  102.538 1.00 30.30 ?  1156 ALA A CB    1 
ATOM   8666  N N     . ALA A 1 1159 ? 8.002   88.978  100.227 1.00 28.03 ?  1157 ALA A N     1 
ATOM   8667  C CA    . ALA A 1 1159 ? 8.270   88.843  98.800  1.00 31.45 ?  1157 ALA A CA    1 
ATOM   8668  C C     . ALA A 1 1159 ? 8.243   87.398  98.319  1.00 29.48 ?  1157 ALA A C     1 
ATOM   8669  O O     . ALA A 1 1159 ? 8.059   87.161  97.120  1.00 30.46 ?  1157 ALA A O     1 
ATOM   8670  C CB    . ALA A 1 1159 ? 9.629   89.460  98.456  1.00 28.49 ?  1157 ALA A CB    1 
ATOM   8671  N N     . ASP A 1 1160 ? 8.410   86.431  99.217  1.00 26.67 ?  1158 ASP A N     1 
ATOM   8672  C CA    . ASP A 1 1160 ? 8.625   85.042  98.835  1.00 28.47 ?  1158 ASP A CA    1 
ATOM   8673  C C     . ASP A 1 1160 ? 7.405   84.163  99.068  1.00 24.59 ?  1158 ASP A C     1 
ATOM   8674  O O     . ASP A 1 1160 ? 7.490   82.944  98.886  1.00 26.49 ?  1158 ASP A O     1 
ATOM   8675  C CB    . ASP A 1 1160 ? 9.841   84.483  99.575  1.00 30.28 ?  1158 ASP A CB    1 
ATOM   8676  C CG    . ASP A 1 1160 ? 11.124  85.167  99.157  1.00 33.52 ?  1158 ASP A CG    1 
ATOM   8677  O OD1   . ASP A 1 1160 ? 11.133  85.756  98.049  1.00 37.48 ?  1158 ASP A OD1   1 
ATOM   8678  O OD2   . ASP A 1 1160 ? 12.118  85.119  99.916  1.00 31.64 ?  1158 ASP A OD2   1 
ATOM   8679  N N     . GLY A 1 1161 ? 6.276   84.751  99.444  1.00 25.73 ?  1159 GLY A N     1 
ATOM   8680  C CA    . GLY A 1 1161 ? 5.053   84.012  99.631  1.00 23.49 ?  1159 GLY A CA    1 
ATOM   8681  C C     . GLY A 1 1161 ? 4.304   83.850  98.325  1.00 26.43 ?  1159 GLY A C     1 
ATOM   8682  O O     . GLY A 1 1161 ? 4.803   84.220  97.258  1.00 30.00 ?  1159 GLY A O     1 
ATOM   8683  N N     . PRO A 1 1162 ? 3.077   83.313  98.381  1.00 25.43 ?  1160 PRO A N     1 
ATOM   8684  C CA    . PRO A 1 1162 ? 2.342   82.913  99.588  1.00 26.27 ?  1160 PRO A CA    1 
ATOM   8685  C C     . PRO A 1 1162 ? 2.879   81.636  100.214 1.00 23.27 ?  1160 PRO A C     1 
ATOM   8686  O O     . PRO A 1 1162 ? 3.288   80.687  99.549  1.00 21.44 ?  1160 PRO A O     1 
ATOM   8687  C CB    . PRO A 1 1162 ? 0.909   82.726  99.071  1.00 24.59 ?  1160 PRO A CB    1 
ATOM   8688  C CG    . PRO A 1 1162 ? 1.097   82.267  97.651  1.00 29.06 ?  1160 PRO A CG    1 
ATOM   8689  C CD    . PRO A 1 1162 ? 2.306   83.038  97.155  1.00 26.76 ?  1160 PRO A CD    1 
ATOM   8690  N N     . PHE A 1 1163 ? 2.901   81.618  101.537 1.00 17.39 ?  1161 PHE A N     1 
ATOM   8691  C CA    . PHE A 1 1163 ? 3.200   80.401  102.260 1.00 15.80 ?  1161 PHE A CA    1 
ATOM   8692  C C     . PHE A 1 1163 ? 1.906   79.674  102.603 1.00 18.45 ?  1161 PHE A C     1 
ATOM   8693  O O     . PHE A 1 1163 ? 0.804   80.214  102.476 1.00 20.33 ?  1161 PHE A O     1 
ATOM   8694  C CB    . PHE A 1 1163 ? 4.015   80.735  103.506 1.00 14.57 ?  1161 PHE A CB    1 
ATOM   8695  C CG    . PHE A 1 1163 ? 5.278   81.486  103.194 1.00 18.04 ?  1161 PHE A CG    1 
ATOM   8696  C CD1   . PHE A 1 1163 ? 6.264   80.897  102.406 1.00 21.63 ?  1161 PHE A CD1   1 
ATOM   8697  C CD2   . PHE A 1 1163 ? 5.478   82.780  103.655 1.00 20.17 ?  1161 PHE A CD2   1 
ATOM   8698  C CE1   . PHE A 1 1163 ? 7.432   81.578  102.092 1.00 20.22 ?  1161 PHE A CE1   1 
ATOM   8699  C CE2   . PHE A 1 1163 ? 6.650   83.470  103.345 1.00 21.62 ?  1161 PHE A CE2   1 
ATOM   8700  C CZ    . PHE A 1 1163 ? 7.625   82.871  102.564 1.00 21.24 ?  1161 PHE A CZ    1 
ATOM   8701  N N     . ALA A 1 1164 ? 2.045   78.413  103.006 1.00 16.65 ?  1162 ALA A N     1 
ATOM   8702  C CA    . ALA A 1 1164 ? 0.891   77.590  103.348 1.00 17.13 ?  1162 ALA A CA    1 
ATOM   8703  C C     . ALA A 1 1164 ? 0.912   77.164  104.812 1.00 15.94 ?  1162 ALA A C     1 
ATOM   8704  O O     . ALA A 1 1164 ? 0.074   76.360  105.232 1.00 19.78 ?  1162 ALA A O     1 
ATOM   8705  C CB    . ALA A 1 1164 ? 0.829   76.376  102.412 1.00 17.56 ?  1162 ALA A CB    1 
ATOM   8706  N N     . GLY A 1 1165 ? 1.845   77.694  105.586 1.00 14.62 ?  1163 GLY A N     1 
ATOM   8707  C CA    . GLY A 1 1165 ? 1.963   77.411  107.005 1.00 15.47 ?  1163 GLY A CA    1 
ATOM   8708  C C     . GLY A 1 1165 ? 3.332   77.861  107.466 1.00 16.64 ?  1163 GLY A C     1 
ATOM   8709  O O     . GLY A 1 1165 ? 4.153   78.312  106.665 1.00 16.63 ?  1163 GLY A O     1 
ATOM   8710  N N     . ALA A 1 1166 ? 3.566   77.751  108.778 1.00 14.49 ?  1164 ALA A N     1 
ATOM   8711  C CA    . ALA A 1 1166 ? 4.866   78.131  109.312 1.00 14.74 ?  1164 ALA A CA    1 
ATOM   8712  C C     . ALA A 1 1166 ? 5.226   77.281  110.521 1.00 15.55 ?  1164 ALA A C     1 
ATOM   8713  O O     . ALA A 1 1166 ? 4.350   76.770  111.229 1.00 16.97 ?  1164 ALA A O     1 
ATOM   8714  C CB    . ALA A 1 1166 ? 4.914   79.618  109.701 1.00 16.87 ?  1164 ALA A CB    1 
ATOM   8715  N N     . LEU A 1 1167 ? 6.536   77.113  110.713 1.00 13.23 ?  1165 LEU A N     1 
ATOM   8716  C CA    . LEU A 1 1167 ? 7.144   76.462  111.872 1.00 13.45 ?  1165 LEU A CA    1 
ATOM   8717  C C     . LEU A 1 1167 ? 8.143   77.432  112.488 1.00 15.98 ?  1165 LEU A C     1 
ATOM   8718  O O     . LEU A 1 1167 ? 9.025   77.938  111.786 1.00 15.98 ?  1165 LEU A O     1 
ATOM   8719  C CB    . LEU A 1 1167 ? 7.851   75.166  111.471 1.00 14.92 ?  1165 LEU A CB    1 
ATOM   8720  C CG    . LEU A 1 1167 ? 6.964   74.114  110.799 1.00 13.46 ?  1165 LEU A CG    1 
ATOM   8721  C CD1   . LEU A 1 1167 ? 7.801   72.952  110.293 1.00 17.66 ?  1165 LEU A CD1   1 
ATOM   8722  C CD2   . LEU A 1 1167 ? 5.927   73.627  111.791 1.00 15.53 ?  1165 LEU A CD2   1 
ATOM   8723  N N     . VAL A 1 1168 ? 8.014   77.683  113.790 1.00 15.59 ?  1166 VAL A N     1 
ATOM   8724  C CA    . VAL A 1 1168 ? 8.806   78.696  114.480 1.00 15.41 ?  1166 VAL A CA    1 
ATOM   8725  C C     . VAL A 1 1168 ? 9.490   78.059  115.677 1.00 16.99 ?  1166 VAL A C     1 
ATOM   8726  O O     . VAL A 1 1168 ? 8.872   77.280  116.410 1.00 15.99 ?  1166 VAL A O     1 
ATOM   8727  C CB    . VAL A 1 1168 ? 7.936   79.882  114.948 1.00 17.46 ?  1166 VAL A CB    1 
ATOM   8728  C CG1   . VAL A 1 1168 ? 8.807   80.954  115.604 1.00 18.22 ?  1166 VAL A CG1   1 
ATOM   8729  C CG2   . VAL A 1 1168 ? 7.149   80.461  113.781 1.00 18.60 ?  1166 VAL A CG2   1 
ATOM   8730  N N     . GLU A 1 1169 ? 10.760  78.398  115.878 1.00 15.34 ?  1167 GLU A N     1 
ATOM   8731  C CA    . GLU A 1 1169 ? 11.524  78.005  117.060 1.00 16.92 ?  1167 GLU A CA    1 
ATOM   8732  C C     . GLU A 1 1169 ? 11.999  79.251  117.791 1.00 18.74 ?  1167 GLU A C     1 
ATOM   8733  O O     . GLU A 1 1169 ? 12.535  80.174  117.167 1.00 19.95 ?  1167 GLU A O     1 
ATOM   8734  C CB    . GLU A 1 1169 ? 12.729  77.143  116.678 1.00 16.04 ?  1167 GLU A CB    1 
ATOM   8735  C CG    . GLU A 1 1169 ? 13.612  76.692  117.843 1.00 17.24 ?  1167 GLU A CG    1 
ATOM   8736  C CD    . GLU A 1 1169 ? 14.956  76.129  117.376 1.00 18.32 ?  1167 GLU A CD    1 
ATOM   8737  O OE1   . GLU A 1 1169 ? 15.279  76.239  116.175 1.00 18.28 ?  1167 GLU A OE1   1 
ATOM   8738  O OE2   . GLU A 1 1169 ? 15.703  75.595  118.215 1.00 18.55 ?  1167 GLU A OE2   1 
ATOM   8739  N N     . GLY A 1 1170 ? 11.817  79.277  119.102 1.00 16.99 ?  1168 GLY A N     1 
ATOM   8740  C CA    . GLY A 1 1170 ? 12.333  80.389  119.873 1.00 19.05 ?  1168 GLY A CA    1 
ATOM   8741  C C     . GLY A 1 1170 ? 11.774  80.379  121.275 1.00 19.01 ?  1168 GLY A C     1 
ATOM   8742  O O     . GLY A 1 1170 ? 10.898  79.580  121.616 1.00 19.93 ?  1168 GLY A O     1 
ATOM   8743  N N     . ASP A 1 1171 ? 12.277  81.311  122.082 1.00 20.37 ?  1169 ASP A N     1 
ATOM   8744  C CA    . ASP A 1 1171 ? 11.660  81.508  123.382 1.00 20.46 ?  1169 ASP A CA    1 
ATOM   8745  C C     . ASP A 1 1171 ? 10.354  82.280  123.205 1.00 22.46 ?  1169 ASP A C     1 
ATOM   8746  O O     . ASP A 1 1171 ? 9.962   82.638  122.088 1.00 20.44 ?  1169 ASP A O     1 
ATOM   8747  C CB    . ASP A 1 1171 ? 12.636  82.177  124.362 1.00 21.85 ?  1169 ASP A CB    1 
ATOM   8748  C CG    . ASP A 1 1171 ? 13.117  83.561  123.915 1.00 27.96 ?  1169 ASP A CG    1 
ATOM   8749  O OD1   . ASP A 1 1171 ? 12.392  84.288  123.202 1.00 24.72 ?  1169 ASP A OD1   1 
ATOM   8750  O OD2   . ASP A 1 1171 ? 14.245  83.935  124.319 1.00 33.85 ?  1169 ASP A OD2   1 
ATOM   8751  N N     . ALA A 1 1172 ? 9.652   82.522  124.315 1.00 22.34 ?  1170 ALA A N     1 
ATOM   8752  C CA    . ALA A 1 1172 ? 8.287   83.029  124.209 1.00 21.94 ?  1170 ALA A CA    1 
ATOM   8753  C C     . ALA A 1 1172 ? 8.244   84.381  123.508 1.00 20.32 ?  1170 ALA A C     1 
ATOM   8754  O O     . ALA A 1 1172 ? 7.360   84.632  122.681 1.00 23.28 ?  1170 ALA A O     1 
ATOM   8755  C CB    . ALA A 1 1172 ? 7.648   83.129  125.593 1.00 22.54 ?  1170 ALA A CB    1 
ATOM   8756  N N     . GLU A 1 1173 ? 9.181   85.274  123.828 1.00 25.19 ?  1171 GLU A N     1 
ATOM   8757  C CA    . GLU A 1 1173 ? 9.113   86.582  123.193 1.00 24.49 ?  1171 GLU A CA    1 
ATOM   8758  C C     . GLU A 1 1173 ? 9.569   86.527  121.743 1.00 20.66 ?  1171 GLU A C     1 
ATOM   8759  O O     . GLU A 1 1173 ? 9.075   87.307  120.918 1.00 24.16 ?  1171 GLU A O     1 
ATOM   8760  C CB    . GLU A 1 1173 ? 9.921   87.609  123.979 1.00 29.26 ?  1171 GLU A CB    1 
ATOM   8761  C CG    . GLU A 1 1173 ? 9.241   88.018  125.280 1.00 31.62 ?  1171 GLU A CG    1 
ATOM   8762  C CD    . GLU A 1 1173 ? 7.755   88.367  125.116 1.00 33.20 ?  1171 GLU A CD    1 
ATOM   8763  O OE1   . GLU A 1 1173 ? 7.381   89.033  124.122 1.00 31.32 ?  1171 GLU A OE1   1 
ATOM   8764  O OE2   . GLU A 1 1173 ? 6.953   87.974  125.994 1.00 33.35 ?  1171 GLU A OE2   1 
ATOM   8765  N N     . ARG A 1 1174 ? 10.476  85.603  121.405 1.00 19.97 ?  1172 ARG A N     1 
ATOM   8766  C CA    . ARG A 1 1174 ? 10.810  85.390  119.998 1.00 20.77 ?  1172 ARG A CA    1 
ATOM   8767  C C     . ARG A 1 1174 ? 9.593   84.896  119.234 1.00 19.25 ?  1172 ARG A C     1 
ATOM   8768  O O     . ARG A 1 1174 ? 9.316   85.356  118.120 1.00 19.90 ?  1172 ARG A O     1 
ATOM   8769  C CB    . ARG A 1 1174 ? 11.965  84.392  119.865 1.00 19.44 ?  1172 ARG A CB    1 
ATOM   8770  C CG    . ARG A 1 1174 ? 12.298  84.008  118.415 1.00 19.24 ?  1172 ARG A CG    1 
ATOM   8771  C CD    . ARG A 1 1174 ? 12.780  85.202  117.596 1.00 20.78 ?  1172 ARG A CD    1 
ATOM   8772  N NE    . ARG A 1 1174 ? 13.132  84.805  116.236 1.00 21.30 ?  1172 ARG A NE    1 
ATOM   8773  C CZ    . ARG A 1 1174 ? 13.164  85.638  115.203 1.00 24.62 ?  1172 ARG A CZ    1 
ATOM   8774  N NH1   . ARG A 1 1174 ? 12.880  86.923  115.345 1.00 25.99 ?  1172 ARG A NH1   1 
ATOM   8775  N NH2   . ARG A 1 1174 ? 13.486  85.170  113.999 1.00 21.83 ?  1172 ARG A NH2   1 
ATOM   8776  N N     . ILE A 1 1175 ? 8.829   83.988  119.843 1.00 19.19 ?  1173 ILE A N     1 
ATOM   8777  C CA    . ILE A 1 1175 ? 7.638   83.443  119.198 1.00 17.57 ?  1173 ILE A CA    1 
ATOM   8778  C C     . ILE A 1 1175 ? 6.606   84.540  118.977 1.00 17.77 ?  1173 ILE A C     1 
ATOM   8779  O O     . ILE A 1 1175 ? 6.002   84.638  117.900 1.00 20.42 ?  1173 ILE A O     1 
ATOM   8780  C CB    . ILE A 1 1175 ? 7.070   82.285  120.039 1.00 19.75 ?  1173 ILE A CB    1 
ATOM   8781  C CG1   . ILE A 1 1175 ? 8.009   81.076  119.976 1.00 20.73 ?  1173 ILE A CG1   1 
ATOM   8782  C CG2   . ILE A 1 1175 ? 5.648   81.920  119.598 1.00 18.85 ?  1173 ILE A CG2   1 
ATOM   8783  C CD1   . ILE A 1 1175 ? 7.570   79.911  120.847 1.00 21.34 ?  1173 ILE A CD1   1 
ATOM   8784  N N     . ARG A 1 1176 ? 6.404   85.399  119.984 1.00 20.84 ?  1174 ARG A N     1 
ATOM   8785  C CA    . ARG A 1 1176 ? 5.434   86.483  119.844 1.00 18.86 ?  1174 ARG A CA    1 
ATOM   8786  C C     . ARG A 1 1176 ? 5.842   87.441  118.734 1.00 19.16 ?  1174 ARG A C     1 
ATOM   8787  O O     . ARG A 1 1176 ? 5.003   87.867  117.933 1.00 20.41 ?  1174 ARG A O     1 
ATOM   8788  C CB    . ARG A 1 1176 ? 5.281   87.243  121.167 1.00 21.67 ?  1174 ARG A CB    1 
ATOM   8789  C CG    . ARG A 1 1176 ? 4.084   88.185  121.164 1.00 24.46 ?  1174 ARG A CG    1 
ATOM   8790  C CD    . ARG A 1 1176 ? 4.126   89.199  122.307 1.00 24.97 ?  1174 ARG A CD    1 
ATOM   8791  N NE    . ARG A 1 1176 ? 4.489   88.592  123.581 1.00 23.81 ?  1174 ARG A NE    1 
ATOM   8792  C CZ    . ARG A 1 1176 ? 3.623   88.126  124.471 1.00 29.42 ?  1174 ARG A CZ    1 
ATOM   8793  N NH1   . ARG A 1 1176 ? 2.315   88.164  124.253 1.00 26.90 ?  1174 ARG A NH1   1 
ATOM   8794  N NH2   . ARG A 1 1176 ? 4.080   87.613  125.611 1.00 28.28 ?  1174 ARG A NH2   1 
ATOM   8795  N N     . ALA A 1 1177 ? 7.134   87.776  118.665 1.00 19.88 ?  1175 ALA A N     1 
ATOM   8796  C CA    . ALA A 1 1177 ? 7.622   88.683  117.628 1.00 23.49 ?  1175 ALA A CA    1 
ATOM   8797  C C     . ALA A 1 1177 ? 7.430   88.090  116.240 1.00 19.72 ?  1175 ALA A C     1 
ATOM   8798  O O     . ALA A 1 1177 ? 6.984   88.774  115.313 1.00 21.05 ?  1175 ALA A O     1 
ATOM   8799  C CB    . ALA A 1 1177 ? 9.096   89.001  117.866 1.00 22.54 ?  1175 ALA A CB    1 
ATOM   8800  N N     . VAL A 1 1178 ? 7.797   86.820  116.074 1.00 20.73 ?  1176 VAL A N     1 
ATOM   8801  C CA    . VAL A 1 1178 ? 7.652   86.169  114.779 1.00 17.83 ?  1176 VAL A CA    1 
ATOM   8802  C C     . VAL A 1 1178 ? 6.184   86.058  114.408 1.00 19.64 ?  1176 VAL A C     1 
ATOM   8803  O O     . VAL A 1 1178 ? 5.805   86.231  113.239 1.00 19.01 ?  1176 VAL A O     1 
ATOM   8804  C CB    . VAL A 1 1178 ? 8.346   84.792  114.801 1.00 17.95 ?  1176 VAL A CB    1 
ATOM   8805  C CG1   . VAL A 1 1178 ? 7.986   83.993  113.568 1.00 17.48 ?  1176 VAL A CG1   1 
ATOM   8806  C CG2   . VAL A 1 1178 ? 9.846   84.958  114.895 1.00 18.39 ?  1176 VAL A CG2   1 
ATOM   8807  N N     . ASN A 1 1179 ? 5.331   85.777  115.394 1.00 19.66 ?  1177 ASN A N     1 
ATOM   8808  C CA    . ASN A 1 1179 ? 3.903   85.642  115.118 1.00 18.84 ?  1177 ASN A CA    1 
ATOM   8809  C C     . ASN A 1 1179 ? 3.325   86.949  114.579 1.00 19.00 ?  1177 ASN A C     1 
ATOM   8810  O O     . ASN A 1 1179 ? 2.473   86.936  113.681 1.00 19.26 ?  1177 ASN A O     1 
ATOM   8811  C CB    . ASN A 1 1179 ? 3.188   85.193  116.397 1.00 22.38 ?  1177 ASN A CB    1 
ATOM   8812  C CG    . ASN A 1 1179 ? 1.939   84.369  116.133 1.00 26.24 ?  1177 ASN A CG    1 
ATOM   8813  O OD1   . ASN A 1 1179 ? 1.731   83.832  115.036 1.00 27.78 ?  1177 ASN A OD1   1 
ATOM   8814  N ND2   . ASN A 1 1179 ? 1.088   84.271  117.150 1.00 27.26 ?  1177 ASN A ND2   1 
ATOM   8815  N N     . LYS A 1 1180 ? 3.807   88.085  115.090 1.00 21.03 ?  1178 LYS A N     1 
ATOM   8816  C CA    . LYS A 1 1180 ? 3.382   89.381  114.574 1.00 19.58 ?  1178 LYS A CA    1 
ATOM   8817  C C     . LYS A 1 1180 ? 3.908   89.610  113.161 1.00 22.56 ?  1178 LYS A C     1 
ATOM   8818  O O     . LYS A 1 1180 ? 3.161   90.060  112.283 1.00 24.47 ?  1178 LYS A O     1 
ATOM   8819  C CB    . LYS A 1 1180 ? 3.840   90.489  115.525 1.00 20.46 ?  1178 LYS A CB    1 
ATOM   8820  C CG    . LYS A 1 1180 ? 3.119   90.431  116.863 1.00 24.27 ?  1178 LYS A CG    1 
ATOM   8821  C CD    . LYS A 1 1180 ? 3.732   91.369  117.876 1.00 26.54 ?  1178 LYS A CD    1 
ATOM   8822  C CE    . LYS A 1 1180 ? 2.949   91.320  119.181 1.00 27.12 ?  1178 LYS A CE    1 
ATOM   8823  N NZ    . LYS A 1 1180 ? 3.701   92.015  120.256 1.00 29.11 ?  1178 LYS A NZ    1 
ATOM   8824  N N     . ALA A 1 1181 ? 5.185   89.288  112.915 1.00 20.46 ?  1179 ALA A N     1 
ATOM   8825  C CA    . ALA A 1 1181 ? 5.734   89.424  111.566 1.00 20.51 ?  1179 ALA A CA    1 
ATOM   8826  C C     . ALA A 1 1181 ? 4.992   88.544  110.570 1.00 22.85 ?  1179 ALA A C     1 
ATOM   8827  O O     . ALA A 1 1181 ? 4.794   88.936  109.414 1.00 22.87 ?  1179 ALA A O     1 
ATOM   8828  C CB    . ALA A 1 1181 ? 7.219   89.081  111.553 1.00 20.57 ?  1179 ALA A CB    1 
ATOM   8829  N N     . ILE A 1 1182 ? 4.568   87.351  110.995 1.00 20.47 ?  1180 ILE A N     1 
ATOM   8830  C CA    . ILE A 1 1182 ? 3.848   86.469  110.077 1.00 17.50 ?  1180 ILE A CA    1 
ATOM   8831  C C     . ILE A 1 1182 ? 2.451   87.009  109.803 1.00 20.31 ?  1180 ILE A C     1 
ATOM   8832  O O     . ILE A 1 1182 ? 1.980   87.006  108.656 1.00 19.59 ?  1180 ILE A O     1 
ATOM   8833  C CB    . ILE A 1 1182 ? 3.813   85.034  110.636 1.00 19.91 ?  1180 ILE A CB    1 
ATOM   8834  C CG1   . ILE A 1 1182 ? 5.213   84.415  110.570 1.00 18.92 ?  1180 ILE A CG1   1 
ATOM   8835  C CG2   . ILE A 1 1182 ? 2.774   84.186  109.904 1.00 20.97 ?  1180 ILE A CG2   1 
ATOM   8836  C CD1   . ILE A 1 1182 ? 5.308   83.036  111.244 1.00 20.88 ?  1180 ILE A CD1   1 
ATOM   8837  N N     . ALA A 1 1183 ? 1.776   87.518  110.833 1.00 21.32 ?  1181 ALA A N     1 
ATOM   8838  C CA    . ALA A 1 1183 ? 0.454   88.097  110.615 1.00 20.15 ?  1181 ALA A CA    1 
ATOM   8839  C C     . ALA A 1 1183 ? 0.518   89.282  109.656 1.00 21.86 ?  1181 ALA A C     1 
ATOM   8840  O O     . ALA A 1 1183 ? -0.457  89.559  108.943 1.00 24.16 ?  1181 ALA A O     1 
ATOM   8841  C CB    . ALA A 1 1183 ? -0.167  88.509  111.951 1.00 21.95 ?  1181 ALA A CB    1 
ATOM   8842  N N     . ALA A 1 1184 ? 1.663   89.971  109.597 1.00 21.50 ?  1182 ALA A N     1 
ATOM   8843  C CA    . ALA A 1 1184 ? 1.818   91.120  108.713 1.00 21.96 ?  1182 ALA A CA    1 
ATOM   8844  C C     . ALA A 1 1184 ? 2.057   90.729  107.262 1.00 25.21 ?  1182 ALA A C     1 
ATOM   8845  O O     . ALA A 1 1184 ? 2.058   91.609  106.393 1.00 25.17 ?  1182 ALA A O     1 
ATOM   8846  C CB    . ALA A 1 1184 ? 2.969   92.012  109.195 1.00 22.11 ?  1182 ALA A CB    1 
ATOM   8847  N N     . LEU A 1 1185 ? 2.279   89.451  106.979 1.00 19.62 ?  1183 LEU A N     1 
ATOM   8848  C CA    . LEU A 1 1185 ? 2.490   89.036  105.601 1.00 21.41 ?  1183 LEU A CA    1 
ATOM   8849  C C     . LEU A 1 1185 ? 1.190   89.173  104.816 1.00 21.02 ?  1183 LEU A C     1 
ATOM   8850  O O     . LEU A 1 1185 ? 0.125   88.778  105.301 1.00 22.87 ?  1183 LEU A O     1 
ATOM   8851  C CB    . LEU A 1 1185 ? 2.980   87.598  105.543 1.00 18.79 ?  1183 LEU A CB    1 
ATOM   8852  C CG    . LEU A 1 1185 ? 4.302   87.334  106.258 1.00 23.20 ?  1183 LEU A CG    1 
ATOM   8853  C CD1   . LEU A 1 1185 ? 4.646   85.867  106.167 1.00 21.72 ?  1183 LEU A CD1   1 
ATOM   8854  C CD2   . LEU A 1 1185 ? 5.413   88.195  105.673 1.00 21.58 ?  1183 LEU A CD2   1 
ATOM   8855  N N     . PRO A 1 1186 ? 1.246   89.713  103.602 1.00 24.68 ?  1184 PRO A N     1 
ATOM   8856  C CA    . PRO A 1 1186 ? 0.035   89.811  102.788 1.00 21.97 ?  1184 PRO A CA    1 
ATOM   8857  C C     . PRO A 1 1186 ? -0.439  88.432  102.367 1.00 19.60 ?  1184 PRO A C     1 
ATOM   8858  O O     . PRO A 1 1186 ? 0.347   87.492  102.236 1.00 22.74 ?  1184 PRO A O     1 
ATOM   8859  C CB    . PRO A 1 1186 ? 0.489   90.626  101.573 1.00 27.83 ?  1184 PRO A CB    1 
ATOM   8860  C CG    . PRO A 1 1186 ? 1.938   90.255  101.424 1.00 30.14 ?  1184 PRO A CG    1 
ATOM   8861  C CD    . PRO A 1 1186 ? 2.460   90.064  102.843 1.00 25.81 ?  1184 PRO A CD    1 
ATOM   8862  N N     . GLY A 1 1187 ? -1.745  88.322  102.153 1.00 20.04 ?  1185 GLY A N     1 
ATOM   8863  C CA    . GLY A 1 1187 ? -2.304  87.105  101.613 1.00 23.75 ?  1185 GLY A CA    1 
ATOM   8864  C C     . GLY A 1 1187 ? -2.958  86.222  102.654 1.00 22.58 ?  1185 GLY A C     1 
ATOM   8865  O O     . GLY A 1 1187 ? -3.682  86.685  103.539 1.00 21.93 ?  1185 GLY A O     1 
ATOM   8866  N N     . PRO A 1 1188 ? -2.728  84.917  102.550 1.00 17.64 ?  1186 PRO A N     1 
ATOM   8867  C CA    . PRO A 1 1188 ? -3.494  83.971  103.369 1.00 18.12 ?  1186 PRO A CA    1 
ATOM   8868  C C     . PRO A 1 1188 ? -3.095  84.011  104.834 1.00 17.17 ?  1186 PRO A C     1 
ATOM   8869  O O     . PRO A 1 1188 ? -1.976  84.378  105.192 1.00 20.22 ?  1186 PRO A O     1 
ATOM   8870  C CB    . PRO A 1 1188 ? -3.160  82.612  102.749 1.00 21.13 ?  1186 PRO A CB    1 
ATOM   8871  C CG    . PRO A 1 1188 ? -1.823  82.809  102.114 1.00 21.82 ?  1186 PRO A CG    1 
ATOM   8872  C CD    . PRO A 1 1188 ? -1.795  84.240  101.635 1.00 19.61 ?  1186 PRO A CD    1 
ATOM   8873  N N     . LEU A 1 1189 ? -4.045  83.633  105.681 1.00 17.61 ?  1187 LEU A N     1 
ATOM   8874  C CA    . LEU A 1 1189 ? -3.779  83.452  107.105 1.00 15.76 ?  1187 LEU A CA    1 
ATOM   8875  C C     . LEU A 1 1189 ? -3.029  82.142  107.282 1.00 21.73 ?  1187 LEU A C     1 
ATOM   8876  O O     . LEU A 1 1189 ? -3.501  81.095  106.828 1.00 31.53 ?  1187 LEU A O     1 
ATOM   8877  C CB    . LEU A 1 1189 ? -5.086  83.433  107.890 1.00 17.42 ?  1187 LEU A CB    1 
ATOM   8878  C CG    . LEU A 1 1189 ? -5.736  84.772  108.227 1.00 24.16 ?  1187 LEU A CG    1 
ATOM   8879  C CD1   . LEU A 1 1189 ? -6.443  85.357  107.017 1.00 23.97 ?  1187 LEU A CD1   1 
ATOM   8880  C CD2   . LEU A 1 1189 ? -6.700  84.614  109.387 1.00 26.77 ?  1187 LEU A CD2   1 
ATOM   8881  N N     . LEU A 1 1190 ? -1.857  82.194  107.911 1.00 18.20 ?  1188 LEU A N     1 
ATOM   8882  C CA    . LEU A 1 1190 ? -1.017  81.011  108.025 1.00 17.77 ?  1188 LEU A CA    1 
ATOM   8883  C C     . LEU A 1 1190 ? -1.298  80.277  109.326 1.00 16.45 ?  1188 LEU A C     1 
ATOM   8884  O O     . LEU A 1 1190 ? -1.420  80.892  110.391 1.00 21.47 ?  1188 LEU A O     1 
ATOM   8885  C CB    . LEU A 1 1190 ? 0.464   81.380  107.964 1.00 20.73 ?  1188 LEU A CB    1 
ATOM   8886  C CG    . LEU A 1 1190 ? 0.915   82.103  106.697 1.00 22.58 ?  1188 LEU A CG    1 
ATOM   8887  C CD1   . LEU A 1 1190 ? 2.435   82.187  106.678 1.00 23.78 ?  1188 LEU A CD1   1 
ATOM   8888  C CD2   . LEU A 1 1190 ? 0.401   81.386  105.457 1.00 24.66 ?  1188 LEU A CD2   1 
ATOM   8889  N N     . LEU A 1 1191 ? -1.398  78.955  109.227 1.00 16.99 ?  1189 LEU A N     1 
ATOM   8890  C CA    . LEU A 1 1191 ? -1.448  78.102  110.410 1.00 19.30 ?  1189 LEU A CA    1 
ATOM   8891  C C     . LEU A 1 1191 ? -0.019  77.937  110.910 1.00 19.72 ?  1189 LEU A C     1 
ATOM   8892  O O     . LEU A 1 1191 ? 0.803   77.278  110.259 1.00 19.16 ?  1189 LEU A O     1 
ATOM   8893  C CB    . LEU A 1 1191 ? -2.107  76.764  110.086 1.00 18.34 ?  1189 LEU A CB    1 
ATOM   8894  C CG    . LEU A 1 1191 ? -2.617  75.875  111.234 1.00 16.83 ?  1189 LEU A CG    1 
ATOM   8895  C CD1   . LEU A 1 1191 ? -3.451  74.737  110.668 1.00 19.76 ?  1189 LEU A CD1   1 
ATOM   8896  C CD2   . LEU A 1 1191 ? -1.475  75.306  112.086 1.00 16.53 ?  1189 LEU A CD2   1 
ATOM   8897  N N     . VAL A 1 1192 ? 0.267   78.538  112.066 1.00 17.52 ?  1190 VAL A N     1 
ATOM   8898  C CA    . VAL A 1 1192 ? 1.609   78.654  112.624 1.00 18.69 ?  1190 VAL A CA    1 
ATOM   8899  C C     . VAL A 1 1192 ? 1.746   77.683  113.787 1.00 17.56 ?  1190 VAL A C     1 
ATOM   8900  O O     . VAL A 1 1192 ? 0.868   77.618  114.656 1.00 20.70 ?  1190 VAL A O     1 
ATOM   8901  C CB    . VAL A 1 1192 ? 1.892   80.091  113.091 1.00 19.40 ?  1190 VAL A CB    1 
ATOM   8902  C CG1   . VAL A 1 1192 ? 3.266   80.185  113.726 1.00 21.92 ?  1190 VAL A CG1   1 
ATOM   8903  C CG2   . VAL A 1 1192 ? 1.776   81.062  111.929 1.00 23.13 ?  1190 VAL A CG2   1 
ATOM   8904  N N     . GLN A 1 1193 ? 2.848   76.941  113.817 1.00 17.52 ?  1191 GLN A N     1 
ATOM   8905  C CA    . GLN A 1 1193 ? 3.195   76.133  114.978 1.00 14.22 ?  1191 GLN A CA    1 
ATOM   8906  C C     . GLN A 1 1193 ? 4.536   76.589  115.524 1.00 14.86 ?  1191 GLN A C     1 
ATOM   8907  O O     . GLN A 1 1193 ? 5.499   76.747  114.763 1.00 17.42 ?  1191 GLN A O     1 
ATOM   8908  C CB    . GLN A 1 1193 ? 3.269   74.649  114.629 1.00 15.66 ?  1191 GLN A CB    1 
ATOM   8909  C CG    . GLN A 1 1193 ? 1.981   74.055  114.081 1.00 15.37 ?  1191 GLN A CG    1 
ATOM   8910  C CD    . GLN A 1 1193 ? 2.072   72.557  114.006 1.00 15.24 ?  1191 GLN A CD    1 
ATOM   8911  O OE1   . GLN A 1 1193 ? 1.971   71.864  115.021 1.00 18.31 ?  1191 GLN A OE1   1 
ATOM   8912  N NE2   . GLN A 1 1193 ? 2.278   72.044  112.802 1.00 16.52 ?  1191 GLN A NE2   1 
ATOM   8913  N N     . ALA A 1 1194 ? 4.608   76.773  116.842 1.00 15.20 ?  1192 ALA A N     1 
ATOM   8914  C CA    . ALA A 1 1194 ? 5.819   77.243  117.485 1.00 15.25 ?  1192 ALA A CA    1 
ATOM   8915  C C     . ALA A 1 1194 ? 6.263   76.272  118.570 1.00 16.91 ?  1192 ALA A C     1 
ATOM   8916  O O     . ALA A 1 1194 ? 5.448   75.558  119.166 1.00 17.74 ?  1192 ALA A O     1 
ATOM   8917  C CB    . ALA A 1 1194 ? 5.604   78.632  118.104 1.00 17.56 ?  1192 ALA A CB    1 
ATOM   8918  N N     . ALA A 1 1195 ? 7.562   76.289  118.849 1.00 15.63 ?  1193 ALA A N     1 
ATOM   8919  C CA    . ALA A 1 1195 ? 8.124   75.473  119.914 1.00 17.96 ?  1193 ALA A CA    1 
ATOM   8920  C C     . ALA A 1 1195 ? 9.446   76.094  120.340 1.00 16.90 ?  1193 ALA A C     1 
ATOM   8921  O O     . ALA A 1 1195 ? 10.122  76.731  119.535 1.00 19.30 ?  1193 ALA A O     1 
ATOM   8922  C CB    . ALA A 1 1195 ? 8.332   74.025  119.456 1.00 18.45 ?  1193 ALA A CB    1 
ATOM   8923  N N     . SER A 1 1196 ? 9.795   75.915  121.612 1.00 17.61 ?  1194 SER A N     1 
ATOM   8924  C CA    . SER A 1 1196 ? 11.118  76.272  122.104 1.00 18.39 ?  1194 SER A CA    1 
ATOM   8925  C C     . SER A 1 1196 ? 12.142  75.205  121.721 1.00 17.97 ?  1194 SER A C     1 
ATOM   8926  O O     . SER A 1 1196 ? 11.800  74.078  121.351 1.00 17.13 ?  1194 SER A O     1 
ATOM   8927  C CB    . SER A 1 1196 ? 11.097  76.421  123.620 1.00 21.71 ?  1194 SER A CB    1 
ATOM   8928  O OG    . SER A 1 1196 ? 10.824  75.162  124.219 1.00 19.59 ?  1194 SER A OG    1 
ATOM   8929  N N     . SER A 1 1197 ? 13.422  75.569  121.808 1.00 17.45 ?  1195 SER A N     1 
ATOM   8930  C CA    . SER A 1 1197 ? 14.462  74.579  121.548 1.00 20.16 ?  1195 SER A CA    1 
ATOM   8931  C C     . SER A 1 1197 ? 14.349  73.401  122.507 1.00 20.24 ?  1195 SER A C     1 
ATOM   8932  O O     . SER A 1 1197 ? 14.523  72.241  122.103 1.00 18.24 ?  1195 SER A O     1 
ATOM   8933  C CB    . SER A 1 1197 ? 15.840  75.221  121.648 1.00 20.15 ?  1195 SER A CB    1 
ATOM   8934  O OG    . SER A 1 1197 ? 15.928  76.311  120.753 1.00 21.83 ?  1195 SER A OG    1 
ATOM   8935  N N     . GLY A 1 1198 ? 14.059  73.678  123.782 1.00 21.02 ?  1196 GLY A N     1 
ATOM   8936  C CA    . GLY A 1 1198 ? 13.901  72.598  124.741 1.00 19.11 ?  1196 GLY A CA    1 
ATOM   8937  C C     . GLY A 1 1198 ? 12.720  71.704  124.417 1.00 19.90 ?  1196 GLY A C     1 
ATOM   8938  O O     . GLY A 1 1198 ? 12.794  70.483  124.573 1.00 20.16 ?  1196 GLY A O     1 
ATOM   8939  N N     . GLU A 1 1199 ? 11.614  72.298  123.964 1.00 18.27 ?  1197 GLU A N     1 
ATOM   8940  C CA    . GLU A 1 1199 ? 10.457  71.498  123.577 1.00 19.44 ?  1197 GLU A CA    1 
ATOM   8941  C C     . GLU A 1 1199 ? 10.785  70.604  122.390 1.00 21.16 ?  1197 GLU A C     1 
ATOM   8942  O O     . GLU A 1 1199 ? 10.366  69.443  122.345 1.00 19.04 ?  1197 GLU A O     1 
ATOM   8943  C CB    . GLU A 1 1199 ? 9.280   72.414  123.255 1.00 22.14 ?  1197 GLU A CB    1 
ATOM   8944  C CG    . GLU A 1 1199 ? 7.963   71.698  123.012 1.00 22.01 ?  1197 GLU A CG    1 
ATOM   8945  C CD    . GLU A 1 1199 ? 6.830   72.675  122.728 1.00 29.14 ?  1197 GLU A CD    1 
ATOM   8946  O OE1   . GLU A 1 1199 ? 7.084   73.901  122.760 1.00 31.00 ?  1197 GLU A OE1   1 
ATOM   8947  O OE2   . GLU A 1 1199 ? 5.691   72.222  122.480 1.00 34.64 ?  1197 GLU A OE2   1 
ATOM   8948  N N     . ILE A 1 1200 ? 11.548  71.121  121.423 1.00 17.28 ?  1198 ILE A N     1 
ATOM   8949  C CA    . ILE A 1 1200 ? 11.971  70.287  120.300 1.00 18.12 ?  1198 ILE A CA    1 
ATOM   8950  C C     . ILE A 1 1200 ? 12.826  69.118  120.788 1.00 18.14 ?  1198 ILE A C     1 
ATOM   8951  O O     . ILE A 1 1200 ? 12.710  67.993  120.283 1.00 17.52 ?  1198 ILE A O     1 
ATOM   8952  C CB    . ILE A 1 1200 ? 12.713  71.138  119.250 1.00 17.29 ?  1198 ILE A CB    1 
ATOM   8953  C CG1   . ILE A 1 1200 ? 11.750  72.122  118.575 1.00 17.07 ?  1198 ILE A CG1   1 
ATOM   8954  C CG2   . ILE A 1 1200 ? 13.371  70.240  118.172 1.00 16.96 ?  1198 ILE A CG2   1 
ATOM   8955  C CD1   . ILE A 1 1200 ? 12.427  73.155  117.690 1.00 16.45 ?  1198 ILE A CD1   1 
ATOM   8956  N N     . ALA A 1 1201 ? 13.686  69.355  121.787 1.00 17.67 ?  1199 ALA A N     1 
ATOM   8957  C CA    . ALA A 1 1201 ? 14.515  68.274  122.312 1.00 20.19 ?  1199 ALA A CA    1 
ATOM   8958  C C     . ALA A 1 1201 ? 13.690  67.252  123.086 1.00 20.63 ?  1199 ALA A C     1 
ATOM   8959  O O     . ALA A 1 1201 ? 13.977  66.049  123.033 1.00 19.55 ?  1199 ALA A O     1 
ATOM   8960  C CB    . ALA A 1 1201 ? 15.619  68.834  123.214 1.00 20.90 ?  1199 ALA A CB    1 
ATOM   8961  N N     . ARG A 1 1202 ? 12.681  67.710  123.827 1.00 19.27 ?  1200 ARG A N     1 
ATOM   8962  C CA    . ARG A 1 1202 ? 11.927  66.829  124.714 1.00 20.67 ?  1200 ARG A CA    1 
ATOM   8963  C C     . ARG A 1 1202 ? 10.777  66.110  124.019 1.00 21.25 ?  1200 ARG A C     1 
ATOM   8964  O O     . ARG A 1 1202 ? 10.462  64.972  124.384 1.00 23.86 ?  1200 ARG A O     1 
ATOM   8965  C CB    . ARG A 1 1202 ? 11.352  67.622  125.889 1.00 21.14 ?  1200 ARG A CB    1 
ATOM   8966  C CG    . ARG A 1 1202 ? 12.378  68.122  126.904 1.00 18.24 ?  1200 ARG A CG    1 
ATOM   8967  C CD    . ARG A 1 1202 ? 11.694  68.775  128.098 1.00 21.75 ?  1200 ARG A CD    1 
ATOM   8968  N NE    . ARG A 1 1202 ? 10.863  69.891  127.671 1.00 25.38 ?  1200 ARG A NE    1 
ATOM   8969  C CZ    . ARG A 1 1202 ? 11.247  71.161  127.671 1.00 23.95 ?  1200 ARG A CZ    1 
ATOM   8970  N NH1   . ARG A 1 1202 ? 12.415  71.535  128.176 1.00 23.13 ?  1200 ARG A NH1   1 
ATOM   8971  N NH2   . ARG A 1 1202 ? 10.442  72.079  127.146 1.00 25.22 ?  1200 ARG A NH2   1 
ATOM   8972  N N     . ASN A 1 1203 ? 10.135  66.744  123.048 1.00 19.20 ?  1201 ASN A N     1 
ATOM   8973  C CA    . ASN A 1 1203 ? 8.895   66.221  122.481 1.00 21.01 ?  1201 ASN A CA    1 
ATOM   8974  C C     . ASN A 1 1203 ? 9.033   65.968  120.986 1.00 21.25 ?  1201 ASN A C     1 
ATOM   8975  O O     . ASN A 1 1203 ? 9.061   66.932  120.196 1.00 18.99 ?  1201 ASN A O     1 
ATOM   8976  C CB    . ASN A 1 1203 ? 7.754   67.198  122.757 1.00 22.31 ?  1201 ASN A CB    1 
ATOM   8977  C CG    . ASN A 1 1203 ? 6.421   66.703  122.226 1.00 21.98 ?  1201 ASN A CG    1 
ATOM   8978  O OD1   . ASN A 1 1203 ? 6.320   65.593  121.707 1.00 23.27 ?  1201 ASN A OD1   1 
ATOM   8979  N ND2   . ASN A 1 1203 ? 5.387   67.521  122.379 1.00 23.29 ?  1201 ASN A ND2   1 
ATOM   8980  N N     . PRO A 1 1204 ? 9.084   64.708  120.547 1.00 20.28 ?  1202 PRO A N     1 
ATOM   8981  C CA    . PRO A 1 1204 ? 9.167   64.427  119.101 1.00 23.10 ?  1202 PRO A CA    1 
ATOM   8982  C C     . PRO A 1 1204 ? 8.001   64.992  118.307 1.00 21.02 ?  1202 PRO A C     1 
ATOM   8983  O O     . PRO A 1 1204 ? 8.140   65.229  117.103 1.00 21.91 ?  1202 PRO A O     1 
ATOM   8984  C CB    . PRO A 1 1204 ? 9.188   62.893  119.043 1.00 23.88 ?  1202 PRO A CB    1 
ATOM   8985  C CG    . PRO A 1 1204 ? 9.655   62.460  120.401 1.00 26.88 ?  1202 PRO A CG    1 
ATOM   8986  C CD    . PRO A 1 1204 ? 9.104   63.481  121.365 1.00 22.39 ?  1202 PRO A CD    1 
ATOM   8987  N N     . ASP A 1 1205 ? 6.859   65.230  118.950 1.00 21.47 ?  1203 ASP A N     1 
ATOM   8988  C CA    . ASP A 1 1205 ? 5.682   65.781  118.292 1.00 20.96 ?  1203 ASP A CA    1 
ATOM   8989  C C     . ASP A 1 1205 ? 5.534   67.284  118.519 1.00 23.62 ?  1203 ASP A C     1 
ATOM   8990  O O     . ASP A 1 1205 ? 4.427   67.817  118.377 1.00 22.63 ?  1203 ASP A O     1 
ATOM   8991  C CB    . ASP A 1 1205 ? 4.427   65.055  118.778 1.00 23.09 ?  1203 ASP A CB    1 
ATOM   8992  C CG    . ASP A 1 1205 ? 4.457   63.567  118.479 1.00 29.56 ?  1203 ASP A CG    1 
ATOM   8993  O OD1   . ASP A 1 1205 ? 5.159   63.154  117.531 1.00 28.37 ?  1203 ASP A OD1   1 
ATOM   8994  O OD2   . ASP A 1 1205 ? 3.772   62.811  119.199 1.00 37.87 ?  1203 ASP A OD2   1 
ATOM   8995  N N     . ALA A 1 1206 ? 6.625   67.973  118.878 1.00 18.21 ?  1204 ALA A N     1 
ATOM   8996  C CA    . ALA A 1 1206 ? 6.566   69.414  119.111 1.00 16.38 ?  1204 ALA A CA    1 
ATOM   8997  C C     . ALA A 1 1206 ? 5.884   70.138  117.960 1.00 17.67 ?  1204 ALA A C     1 
ATOM   8998  O O     . ALA A 1 1206 ? 5.082   71.058  118.176 1.00 21.89 ?  1204 ALA A O     1 
ATOM   8999  C CB    . ALA A 1 1206 ? 7.977   69.968  119.320 1.00 20.36 ?  1204 ALA A CB    1 
ATOM   9000  N N     . TYR A 1 1207 ? 6.204   69.746  116.733 1.00 17.83 ?  1205 TYR A N     1 
ATOM   9001  C CA    . TYR A 1 1207 ? 5.509   70.223  115.548 1.00 15.63 ?  1205 TYR A CA    1 
ATOM   9002  C C     . TYR A 1 1207 ? 4.590   69.107  115.074 1.00 18.24 ?  1205 TYR A C     1 
ATOM   9003  O O     . TYR A 1 1207 ? 5.061   68.021  114.719 1.00 23.15 ?  1205 TYR A O     1 
ATOM   9004  C CB    . TYR A 1 1207 ? 6.495   70.616  114.451 1.00 15.69 ?  1205 TYR A CB    1 
ATOM   9005  C CG    . TYR A 1 1207 ? 7.422   71.743  114.838 1.00 16.06 ?  1205 TYR A CG    1 
ATOM   9006  C CD1   . TYR A 1 1207 ? 6.918   73.003  115.189 1.00 15.96 ?  1205 TYR A CD1   1 
ATOM   9007  C CD2   . TYR A 1 1207 ? 8.804   71.556  114.849 1.00 14.72 ?  1205 TYR A CD2   1 
ATOM   9008  C CE1   . TYR A 1 1207 ? 7.773   74.038  115.546 1.00 16.80 ?  1205 TYR A CE1   1 
ATOM   9009  C CE2   . TYR A 1 1207 ? 9.664   72.588  115.208 1.00 15.50 ?  1205 TYR A CE2   1 
ATOM   9010  C CZ    . TYR A 1 1207 ? 9.139   73.828  115.546 1.00 16.01 ?  1205 TYR A CZ    1 
ATOM   9011  O OH    . TYR A 1 1207 ? 9.989   74.853  115.895 1.00 17.44 ?  1205 TYR A OH    1 
ATOM   9012  N N     . CYS A 1 1208 ? 3.290   69.354  115.112 1.00 16.60 ?  1206 CYS A N     1 
ATOM   9013  C CA    . CYS A 1 1208 ? 2.336   68.293  114.829 1.00 17.84 ?  1206 CYS A CA    1 
ATOM   9014  C C     . CYS A 1 1208 ? 2.138   68.162  113.322 1.00 16.88 ?  1206 CYS A C     1 
ATOM   9015  O O     . CYS A 1 1208 ? 1.864   69.141  112.628 1.00 15.08 ?  1206 CYS A O     1 
ATOM   9016  C CB    . CYS A 1 1208 ? 1.015   68.583  115.535 1.00 17.64 ?  1206 CYS A CB    1 
ATOM   9017  S SG    . CYS A 1 1208 ? -0.248  67.325  115.272 1.00 21.91 ?  1206 CYS A SG    1 
ATOM   9018  N N     . LEU A 1 1209 ? 2.294   66.942  112.816 1.00 13.54 ?  1207 LEU A N     1 
ATOM   9019  C CA    . LEU A 1 1209 ? 2.195   66.737  111.384 1.00 14.21 ?  1207 LEU A CA    1 
ATOM   9020  C C     . LEU A 1 1209 ? 0.766   66.855  110.875 1.00 14.49 ?  1207 LEU A C     1 
ATOM   9021  O O     . LEU A 1 1209 ? 0.572   66.991  109.667 1.00 13.86 ?  1207 LEU A O     1 
ATOM   9022  C CB    . LEU A 1 1209 ? 2.776   65.371  111.019 1.00 13.87 ?  1207 LEU A CB    1 
ATOM   9023  C CG    . LEU A 1 1209 ? 4.223   65.163  111.449 1.00 15.06 ?  1207 LEU A CG    1 
ATOM   9024  C CD1   . LEU A 1 1209 ? 4.710   63.838  110.913 1.00 18.60 ?  1207 LEU A CD1   1 
ATOM   9025  C CD2   . LEU A 1 1209 ? 5.122   66.274  110.938 1.00 16.40 ?  1207 LEU A CD2   1 
ATOM   9026  N N     . ASN A 1 1210 ? -0.233  66.808  111.762 1.00 16.38 ?  1208 ASN A N     1 
ATOM   9027  C CA    . ASN A 1 1210 ? -1.615  66.988  111.318 1.00 17.23 ?  1208 ASN A CA    1 
ATOM   9028  C C     . ASN A 1 1210 ? -1.786  68.303  110.567 1.00 15.21 ?  1208 ASN A C     1 
ATOM   9029  O O     . ASN A 1 1210 ? -2.596  68.402  109.642 1.00 16.74 ?  1208 ASN A O     1 
ATOM   9030  C CB    . ASN A 1 1210 ? -2.595  66.977  112.498 1.00 17.03 ?  1208 ASN A CB    1 
ATOM   9031  C CG    . ASN A 1 1210 ? -2.692  65.629  113.203 1.00 18.45 ?  1208 ASN A CG    1 
ATOM   9032  O OD1   . ASN A 1 1210 ? -1.888  64.723  112.989 1.00 23.50 ?  1208 ASN A OD1   1 
ATOM   9033  N ND2   . ASN A 1 1210 ? -3.673  65.518  114.108 1.00 24.44 ?  1208 ASN A ND2   1 
ATOM   9034  N N     . TRP A 1 1211 ? -1.067  69.341  110.980 1.00 14.19 ?  1209 TRP A N     1 
ATOM   9035  C CA    . TRP A 1 1211 ? -1.309  70.680  110.460 1.00 13.17 ?  1209 TRP A CA    1 
ATOM   9036  C C     . TRP A 1 1211 ? -0.352  71.054  109.343 1.00 14.44 ?  1209 TRP A C     1 
ATOM   9037  O O     . TRP A 1 1211 ? -0.346  72.208  108.901 1.00 16.40 ?  1209 TRP A O     1 
ATOM   9038  C CB    . TRP A 1 1211 ? -1.233  71.705  111.605 1.00 14.26 ?  1209 TRP A CB    1 
ATOM   9039  C CG    . TRP A 1 1211 ? -1.883  71.206  112.856 1.00 15.96 ?  1209 TRP A CG    1 
ATOM   9040  C CD1   . TRP A 1 1211 ? -1.312  71.133  114.099 1.00 15.38 ?  1209 TRP A CD1   1 
ATOM   9041  C CD2   . TRP A 1 1211 ? -3.209  70.668  112.994 1.00 16.08 ?  1209 TRP A CD2   1 
ATOM   9042  N NE1   . TRP A 1 1211 ? -2.202  70.593  115.001 1.00 17.14 ?  1209 TRP A NE1   1 
ATOM   9043  C CE2   . TRP A 1 1211 ? -3.369  70.297  114.348 1.00 16.23 ?  1209 TRP A CE2   1 
ATOM   9044  C CE3   . TRP A 1 1211 ? -4.271  70.456  112.103 1.00 15.51 ?  1209 TRP A CE3   1 
ATOM   9045  C CZ2   . TRP A 1 1211 ? -4.551  69.734  114.837 1.00 18.42 ?  1209 TRP A CZ2   1 
ATOM   9046  C CZ3   . TRP A 1 1211 ? -5.441  69.896  112.592 1.00 18.45 ?  1209 TRP A CZ3   1 
ATOM   9047  C CH2   . TRP A 1 1211 ? -5.569  69.541  113.940 1.00 16.70 ?  1209 TRP A CH2   1 
ATOM   9048  N N     . LEU A 1 1212 ? 0.440   70.096  108.861 1.00 13.05 ?  1210 LEU A N     1 
ATOM   9049  C CA    . LEU A 1 1212 ? 1.362   70.301  107.753 1.00 13.36 ?  1210 LEU A CA    1 
ATOM   9050  C C     . LEU A 1 1212 ? 0.909   69.605  106.468 1.00 13.70 ?  1210 LEU A C     1 
ATOM   9051  O O     . LEU A 1 1212 ? 1.634   69.640  105.465 1.00 13.28 ?  1210 LEU A O     1 
ATOM   9052  C CB    . LEU A 1 1212 ? 2.767   69.830  108.153 1.00 13.40 ?  1210 LEU A CB    1 
ATOM   9053  C CG    . LEU A 1 1212 ? 3.468   70.805  109.097 1.00 12.19 ?  1210 LEU A CG    1 
ATOM   9054  C CD1   . LEU A 1 1212 ? 4.602   70.120  109.824 1.00 14.46 ?  1210 LEU A CD1   1 
ATOM   9055  C CD2   . LEU A 1 1212 ? 3.984   72.026  108.324 1.00 15.35 ?  1210 LEU A CD2   1 
ATOM   9056  N N     . VAL A 1 1213 ? -0.267  68.976  106.474 1.00 13.61 ?  1211 VAL A N     1 
ATOM   9057  C CA    . VAL A 1 1213 ? -0.884  68.433  105.272 1.00 14.02 ?  1211 VAL A CA    1 
ATOM   9058  C C     . VAL A 1 1213 ? -2.158  69.212  105.001 1.00 12.17 ?  1211 VAL A C     1 
ATOM   9059  O O     . VAL A 1 1213 ? -2.704  69.912  105.863 1.00 15.03 ?  1211 VAL A O     1 
ATOM   9060  C CB    . VAL A 1 1213 ? -1.202  66.916  105.369 1.00 12.85 ?  1211 VAL A CB    1 
ATOM   9061  C CG1   . VAL A 1 1213 ? 0.084   66.090  105.434 1.00 15.26 ?  1211 VAL A CG1   1 
ATOM   9062  C CG2   . VAL A 1 1213 ? -2.079  66.615  106.564 1.00 13.43 ?  1211 VAL A CG2   1 
ATOM   9063  N N     . GLU A 1 1214 ? -2.652  69.048  103.782 1.00 12.96 ?  1212 GLU A N     1 
ATOM   9064  C CA    . GLU A 1 1214 ? -3.829  69.741  103.300 1.00 14.57 ?  1212 GLU A CA    1 
ATOM   9065  C C     . GLU A 1 1214 ? -4.878  68.698  102.968 1.00 13.17 ?  1212 GLU A C     1 
ATOM   9066  O O     . GLU A 1 1214 ? -4.580  67.731  102.261 1.00 13.22 ?  1212 GLU A O     1 
ATOM   9067  C CB    . GLU A 1 1214 ? -3.462  70.572  102.074 1.00 18.08 ?  1212 GLU A CB    1 
ATOM   9068  C CG    . GLU A 1 1214 ? -4.592  71.279  101.398 1.00 21.28 ?  1212 GLU A CG    1 
ATOM   9069  C CD    . GLU A 1 1214 ? -4.054  72.187  100.312 1.00 26.44 ?  1212 GLU A CD    1 
ATOM   9070  O OE1   . GLU A 1 1214 ? -3.219  73.063  100.634 1.00 30.27 ?  1212 GLU A OE1   1 
ATOM   9071  O OE2   . GLU A 1 1214 ? -4.439  72.004  99.140  1.00 35.06 ?  1212 GLU A OE2   1 
ATOM   9072  N N     . GLU A 1 1215 ? -6.092  68.892  103.478 1.00 13.20 ?  1213 GLU A N     1 
ATOM   9073  C CA    . GLU A 1 1215 ? -7.193  67.986  103.178 1.00 12.04 ?  1213 GLU A CA    1 
ATOM   9074  C C     . GLU A 1 1215 ? -7.866  68.377  101.873 1.00 11.78 ?  1213 GLU A C     1 
ATOM   9075  O O     . GLU A 1 1215 ? -8.147  69.556  101.639 1.00 11.98 ?  1213 GLU A O     1 
ATOM   9076  C CB    . GLU A 1 1215 ? -8.234  68.025  104.286 1.00 12.31 ?  1213 GLU A CB    1 
ATOM   9077  C CG    . GLU A 1 1215 ? -7.735  67.660  105.688 1.00 12.86 ?  1213 GLU A CG    1 
ATOM   9078  C CD    . GLU A 1 1215 ? -8.757  68.044  106.742 1.00 12.84 ?  1213 GLU A CD    1 
ATOM   9079  O OE1   . GLU A 1 1215 ? -8.769  69.226  107.144 1.00 15.19 ?  1213 GLU A OE1   1 
ATOM   9080  O OE2   . GLU A 1 1215 ? -9.563  67.179  107.121 1.00 14.92 ?  1213 GLU A OE2   1 
ATOM   9081  N N     . VAL A 1 1216 ? -8.173  67.380  101.044 1.00 10.66 ?  1214 VAL A N     1 
ATOM   9082  C CA    . VAL A 1 1216 ? -8.945  67.612  99.827  1.00 10.98 ?  1214 VAL A CA    1 
ATOM   9083  C C     . VAL A 1 1216 ? -10.119 66.638  99.791  1.00 12.28 ?  1214 VAL A C     1 
ATOM   9084  O O     . VAL A 1 1216 ? -9.942  65.430  99.975  1.00 12.02 ?  1214 VAL A O     1 
ATOM   9085  C CB    . VAL A 1 1216 ? -8.081  67.470  98.564  1.00 12.73 ?  1214 VAL A CB    1 
ATOM   9086  C CG1   . VAL A 1 1216 ? -8.942  67.650  97.317  1.00 12.97 ?  1214 VAL A CG1   1 
ATOM   9087  C CG2   . VAL A 1 1216 ? -6.974  68.511  98.575  1.00 12.71 ?  1214 VAL A CG2   1 
ATOM   9088  N N     . SER A 1 1217 ? -11.312 67.174  99.563  1.00 10.95 ?  1215 SER A N     1 
ATOM   9089  C CA    . SER A 1 1217 ? -12.535 66.403  99.353  1.00 10.76 ?  1215 SER A CA    1 
ATOM   9090  C C     . SER A 1 1217 ? -12.921 66.450  97.885  1.00 9.79  ?  1215 SER A C     1 
ATOM   9091  O O     . SER A 1 1217 ? -12.892 67.521  97.281  1.00 11.72 ?  1215 SER A O     1 
ATOM   9092  C CB    . SER A 1 1217 ? -13.670 66.992  100.182 1.00 13.28 ?  1215 SER A CB    1 
ATOM   9093  O OG    . SER A 1 1217 ? -14.930 66.483  99.780  1.00 14.97 ?  1215 SER A OG    1 
ATOM   9094  N N     . ALA A 1 1218 ? -13.272 65.298  97.317  1.00 9.90  ?  1216 ALA A N     1 
ATOM   9095  C CA    . ALA A 1 1218 ? -13.749 65.254  95.937  1.00 10.85 ?  1216 ALA A CA    1 
ATOM   9096  C C     . ALA A 1 1218 ? -15.019 64.428  95.878  1.00 12.53 ?  1216 ALA A C     1 
ATOM   9097  O O     . ALA A 1 1218 ? -15.044 63.287  96.348  1.00 13.94 ?  1216 ALA A O     1 
ATOM   9098  C CB    . ALA A 1 1218 ? -12.705 64.665  94.989  1.00 12.46 ?  1216 ALA A CB    1 
ATOM   9099  N N     . SER A 1 1219 ? -16.065 65.000  95.290  1.00 10.50 ?  1217 SER A N     1 
ATOM   9100  C CA    . SER A 1 1219 ? -17.358 64.336  95.168  1.00 11.77 ?  1217 SER A CA    1 
ATOM   9101  C C     . SER A 1 1219 ? -17.662 64.168  93.685  1.00 10.83 ?  1217 SER A C     1 
ATOM   9102  O O     . SER A 1 1219 ? -17.801 65.158  92.964  1.00 12.60 ?  1217 SER A O     1 
ATOM   9103  C CB    . SER A 1 1219 ? -18.458 65.145  95.851  1.00 13.24 ?  1217 SER A CB    1 
ATOM   9104  O OG    . SER A 1 1219 ? -19.715 64.481  95.756  1.00 12.68 ?  1217 SER A OG    1 
ATOM   9105  N N     . ILE A 1 1220 ? -17.767 62.919  93.243  1.00 10.41 ?  1218 ILE A N     1 
ATOM   9106  C CA    . ILE A 1 1220 ? -17.974 62.584  91.836  1.00 11.50 ?  1218 ILE A CA    1 
ATOM   9107  C C     . ILE A 1 1220 ? -19.370 62.004  91.671  1.00 11.58 ?  1218 ILE A C     1 
ATOM   9108  O O     . ILE A 1 1220 ? -19.704 60.995  92.301  1.00 11.85 ?  1218 ILE A O     1 
ATOM   9109  C CB    . ILE A 1 1220 ? -16.927 61.582  91.343  1.00 14.66 ?  1218 ILE A CB    1 
ATOM   9110  C CG1   . ILE A 1 1220 ? -15.525 62.162  91.552  1.00 18.39 ?  1218 ILE A CG1   1 
ATOM   9111  C CG2   . ILE A 1 1220 ? -17.204 61.252  89.885  1.00 15.72 ?  1218 ILE A CG2   1 
ATOM   9112  C CD1   . ILE A 1 1220 ? -14.416 61.128  91.532  1.00 25.66 ?  1218 ILE A CD1   1 
ATOM   9113  N N     . ASN A 1 1221 ? -20.173 62.620  90.796  1.00 10.73 ?  1219 ASN A N     1 
ATOM   9114  C CA    . ASN A 1 1221 ? -21.496 62.089  90.465  1.00 10.72 ?  1219 ASN A CA    1 
ATOM   9115  C C     . ASN A 1 1221 ? -21.318 60.954  89.465  1.00 12.41 ?  1219 ASN A C     1 
ATOM   9116  O O     . ASN A 1 1221 ? -21.152 61.192  88.270  1.00 13.99 ?  1219 ASN A O     1 
ATOM   9117  C CB    . ASN A 1 1221 ? -22.381 63.196  89.905  1.00 11.44 ?  1219 ASN A CB    1 
ATOM   9118  C CG    . ASN A 1 1221 ? -23.722 62.679  89.393  1.00 11.23 ?  1219 ASN A CG    1 
ATOM   9119  O OD1   . ASN A 1 1221 ? -24.109 61.544  89.658  1.00 11.51 ?  1219 ASN A OD1   1 
ATOM   9120  N ND2   . ASN A 1 1221 ? -24.443 63.535  88.665  1.00 14.08 ?  1219 ASN A ND2   1 
ATOM   9121  N N     . THR A 1 1222 ? -21.369 59.716  89.943  1.00 11.30 ?  1220 THR A N     1 
ATOM   9122  C CA    . THR A 1 1222 ? -21.140 58.563  89.081  1.00 11.55 ?  1220 THR A CA    1 
ATOM   9123  C C     . THR A 1 1222 ? -22.398 58.141  88.352  1.00 15.26 ?  1220 THR A C     1 
ATOM   9124  O O     . THR A 1 1222 ? -22.345 57.213  87.547  1.00 19.10 ?  1220 THR A O     1 
ATOM   9125  C CB    . THR A 1 1222 ? -20.587 57.389  89.894  1.00 15.43 ?  1220 THR A CB    1 
ATOM   9126  O OG1   . THR A 1 1222 ? -21.532 57.001  90.904  1.00 14.55 ?  1220 THR A OG1   1 
ATOM   9127  C CG2   . THR A 1 1222 ? -19.259 57.772  90.542  1.00 15.22 ?  1220 THR A CG2   1 
ATOM   9128  N N     . ALA A 1 1223 ? -23.526 58.778  88.631  1.00 11.52 ?  1221 ALA A N     1 
ATOM   9129  C CA    . ALA A 1 1223 ? -24.736 58.521  87.867  1.00 14.70 ?  1221 ALA A CA    1 
ATOM   9130  C C     . ALA A 1 1223 ? -24.914 59.492  86.707  1.00 17.20 ?  1221 ALA A C     1 
ATOM   9131  O O     . ALA A 1 1223 ? -25.939 59.429  86.025  1.00 17.47 ?  1221 ALA A O     1 
ATOM   9132  C CB    . ALA A 1 1223 ? -25.960 58.582  88.786  1.00 16.21 ?  1221 ALA A CB    1 
ATOM   9133  N N     . ALA A 1 1224 ? -23.937 60.375  86.460  1.00 17.24 ?  1222 ALA A N     1 
ATOM   9134  C CA    . ALA A 1 1224 ? -24.134 61.473  85.517  1.00 17.79 ?  1222 ALA A CA    1 
ATOM   9135  C C     . ALA A 1 1224 ? -24.351 60.997  84.084  1.00 20.61 ?  1222 ALA A C     1 
ATOM   9136  O O     . ALA A 1 1224 ? -24.947 61.736  83.298  1.00 20.68 ?  1222 ALA A O     1 
ATOM   9137  C CB    . ALA A 1 1224 ? -22.946 62.438  85.581  1.00 18.77 ?  1222 ALA A CB    1 
ATOM   9138  N N     . ALA A 1 1225 ? -23.903 59.786  83.725  1.00 18.23 ?  1223 ALA A N     1 
ATOM   9139  C CA    . ALA A 1 1225 ? -24.122 59.277  82.373  1.00 20.40 ?  1223 ALA A CA    1 
ATOM   9140  C C     . ALA A 1 1225 ? -25.543 58.787  82.138  1.00 22.02 ?  1223 ALA A C     1 
ATOM   9141  O O     . ALA A 1 1225 ? -25.878 58.439  80.999  1.00 23.79 ?  1223 ALA A O     1 
ATOM   9142  C CB    . ALA A 1 1225 ? -23.135 58.154  82.060  1.00 19.81 ?  1223 ALA A CB    1 
ATOM   9143  N N     . GLY A 1 1226 ? -26.387 58.766  83.162  1.00 19.39 ?  1224 GLY A N     1 
ATOM   9144  C CA    . GLY A 1 1226 ? -27.789 58.423  83.000  1.00 20.47 ?  1224 GLY A CA    1 
ATOM   9145  C C     . GLY A 1 1226 ? -28.243 57.248  83.830  1.00 18.85 ?  1224 GLY A C     1 
ATOM   9146  O O     . GLY A 1 1226 ? -29.450 56.961  83.869  1.00 22.44 ?  1224 GLY A O     1 
ATOM   9147  N N     . GLY A 1 1227 ? -27.319 56.566  84.500  1.00 18.32 ?  1225 GLY A N     1 
ATOM   9148  C CA    . GLY A 1 1227 ? -27.650 55.432  85.340  1.00 22.98 ?  1225 GLY A CA    1 
ATOM   9149  C C     . GLY A 1 1227 ? -26.499 55.092  86.263  1.00 19.76 ?  1225 GLY A C     1 
ATOM   9150  O O     . GLY A 1 1227 ? -25.412 55.673  86.189  1.00 17.48 ?  1225 GLY A O     1 
ATOM   9151  N N     . ASN A 1 1228 ? -26.760 54.117  87.134  1.00 16.83 ?  1226 ASN A N     1 
ATOM   9152  C CA    . ASN A 1 1228 ? -25.848 53.693  88.196  1.00 18.00 ?  1226 ASN A CA    1 
ATOM   9153  C C     . ASN A 1 1228 ? -25.377 52.266  87.902  1.00 18.51 ?  1226 ASN A C     1 
ATOM   9154  O O     . ASN A 1 1228 ? -26.152 51.308  88.013  1.00 20.04 ?  1226 ASN A O     1 
ATOM   9155  C CB    . ASN A 1 1228 ? -26.572 53.794  89.543  1.00 18.10 ?  1226 ASN A CB    1 
ATOM   9156  C CG    . ASN A 1 1228 ? -25.689 53.450  90.732  1.00 20.93 ?  1226 ASN A CG    1 
ATOM   9157  O OD1   . ASN A 1 1228 ? -24.846 52.555  90.675  1.00 21.71 ?  1226 ASN A OD1   1 
ATOM   9158  N ND2   . ASN A 1 1228 ? -25.904 54.162  91.832  1.00 22.03 ?  1226 ASN A ND2   1 
ATOM   9159  N N     . ALA A 1 1229 ? -24.103 52.125  87.523  1.00 19.13 ?  1227 ALA A N     1 
ATOM   9160  C CA    . ALA A 1 1229 ? -23.577 50.810  87.168  1.00 20.07 ?  1227 ALA A CA    1 
ATOM   9161  C C     . ALA A 1 1229 ? -23.615 49.842  88.346  1.00 19.24 ?  1227 ALA A C     1 
ATOM   9162  O O     . ALA A 1 1229 ? -23.966 48.665  88.183  1.00 22.19 ?  1227 ALA A O     1 
ATOM   9163  C CB    . ALA A 1 1229 ? -22.147 50.954  86.641  1.00 21.84 ?  1227 ALA A CB    1 
ATOM   9164  N N     . SER A 1 1230 ? -23.244 50.310  89.543  1.00 22.04 ?  1228 SER A N     1 
ATOM   9165  C CA    . SER A 1 1230 ? -23.245 49.431  90.709  1.00 23.88 ?  1228 SER A CA    1 
ATOM   9166  C C     . SER A 1 1230 ? -24.637 48.879  90.990  1.00 22.89 ?  1228 SER A C     1 
ATOM   9167  O O     . SER A 1 1230 ? -24.792 47.693  91.308  1.00 23.12 ?  1228 SER A O     1 
ATOM   9168  C CB    . SER A 1 1230 ? -22.707 50.179  91.930  1.00 30.12 ?  1228 SER A CB    1 
ATOM   9169  O OG    . SER A 1 1230 ? -21.305 50.347  91.825  1.00 35.24 ?  1228 SER A OG    1 
ATOM   9170  N N     . LEU A 1 1231 ? -25.666 49.714  90.846  1.00 21.74 ?  1229 LEU A N     1 
ATOM   9171  C CA    . LEU A 1 1231 ? -27.025 49.269  91.124  1.00 21.65 ?  1229 LEU A CA    1 
ATOM   9172  C C     . LEU A 1 1231 ? -27.607 48.399  90.017  1.00 23.52 ?  1229 LEU A C     1 
ATOM   9173  O O     . LEU A 1 1231 ? -28.673 47.801  90.221  1.00 24.69 ?  1229 LEU A O     1 
ATOM   9174  C CB    . LEU A 1 1231 ? -27.937 50.473  91.383  1.00 22.82 ?  1229 LEU A CB    1 
ATOM   9175  C CG    . LEU A 1 1231 ? -28.136 50.806  92.871  1.00 24.43 ?  1229 LEU A CG    1 
ATOM   9176  C CD1   . LEU A 1 1231 ? -26.807 51.078  93.563  1.00 26.64 ?  1229 LEU A CD1   1 
ATOM   9177  C CD2   . LEU A 1 1231 ? -29.076 52.007  93.017  1.00 22.90 ?  1229 LEU A CD2   1 
ATOM   9178  N N     . MET A 1 1232 ? -26.934 48.282  88.867  1.00 22.65 ?  1230 MET A N     1 
ATOM   9179  C CA    . MET A 1 1232 ? -27.390 47.318  87.869  1.00 23.31 ?  1230 MET A CA    1 
ATOM   9180  C C     . MET A 1 1232 ? -27.260 45.883  88.370  1.00 26.20 ?  1230 MET A C     1 
ATOM   9181  O O     . MET A 1 1232 ? -27.900 44.983  87.816  1.00 26.38 ?  1230 MET A O     1 
ATOM   9182  C CB    . MET A 1 1232 ? -26.613 47.487  86.556  1.00 23.25 ?  1230 MET A CB    1 
ATOM   9183  C CG    . MET A 1 1232 ? -26.951 48.752  85.773  1.00 21.60 ?  1230 MET A CG    1 
ATOM   9184  S SD    . MET A 1 1232 ? -25.796 48.994  84.387  1.00 24.62 ?  1230 MET A SD    1 
ATOM   9185  C CE    . MET A 1 1232 ? -26.334 47.740  83.202  1.00 24.15 ?  1230 MET A CE    1 
ATOM   9186  N N     . ALA A 1 1233 ? -26.453 45.653  89.403  1.00 25.86 ?  1231 ALA A N     1 
ATOM   9187  C CA    . ALA A 1 1233 ? -26.287 44.325  89.980  1.00 26.05 ?  1231 ALA A CA    1 
ATOM   9188  C C     . ALA A 1 1233 ? -27.208 44.062  91.169  1.00 30.24 ?  1231 ALA A C     1 
ATOM   9189  O O     . ALA A 1 1233 ? -27.158 42.963  91.736  1.00 31.33 ?  1231 ALA A O     1 
ATOM   9190  C CB    . ALA A 1 1233 ? -24.831 44.122  90.413  1.00 27.78 ?  1231 ALA A CB    1 
ATOM   9191  N N     . ILE A 1 1234 ? -28.050 45.022  91.554  1.00 27.70 ?  1232 ILE A N     1 
ATOM   9192  C CA    . ILE A 1 1234 ? -28.870 44.913  92.761  1.00 29.23 ?  1232 ILE A CA    1 
ATOM   9193  C C     . ILE A 1 1234 ? -30.323 44.686  92.354  1.00 30.37 ?  1232 ILE A C     1 
ATOM   9194  O O     . ILE A 1 1234 ? -30.987 45.584  91.817  1.00 27.06 ?  1232 ILE A O     1 
ATOM   9195  C CB    . ILE A 1 1234 ? -28.727 46.145  93.661  1.00 26.25 ?  1232 ILE A CB    1 
ATOM   9196  C CG1   . ILE A 1 1234 ? -27.272 46.288  94.104  1.00 28.86 ?  1232 ILE A CG1   1 
ATOM   9197  C CG2   . ILE A 1 1234 ? -29.645 46.029  94.869  1.00 25.48 ?  1232 ILE A CG2   1 
ATOM   9198  C CD1   . ILE A 1 1234 ? -27.059 47.349  95.147  1.00 29.78 ?  1232 ILE A CD1   1 
ATOM   9199  N N     . GLY A 1 1235 ? -30.819 43.485  92.635  1.00 29.37 ?  1233 GLY A N     1 
ATOM   9200  C CA    . GLY A 1 1235 ? -32.179 43.106  92.310  1.00 25.29 ?  1233 GLY A CA    1 
ATOM   9201  C C     . GLY A 1 1235 ? -32.761 42.194  93.369  1.00 30.35 ?  1233 GLY A C     1 
ATOM   9202  O O     . GLY A 1 1235 ? -33.956 42.234  93.650  1.00 25.35 ?  1233 GLY A O     1 
ATOM   9203  O OXT   . GLY A 1 1235 ? -32.042 41.389  93.976  1.00 32.29 ?  1233 GLY A OXT   1 
ATOM   9204  N N     . PRO B 1 17   ? 26.824  5.052   83.126  1.00 45.76 ?  15   PRO B N     1 
ATOM   9205  C CA    . PRO B 1 17   ? 25.395  4.731   83.233  1.00 37.54 ?  15   PRO B CA    1 
ATOM   9206  C C     . PRO B 1 17   ? 24.619  5.128   81.979  1.00 39.91 ?  15   PRO B C     1 
ATOM   9207  O O     . PRO B 1 17   ? 24.821  6.237   81.473  1.00 39.98 ?  15   PRO B O     1 
ATOM   9208  C CB    . PRO B 1 17   ? 24.937  5.557   84.443  1.00 38.93 ?  15   PRO B CB    1 
ATOM   9209  C CG    . PRO B 1 17   ? 26.180  5.760   85.253  1.00 42.27 ?  15   PRO B CG    1 
ATOM   9210  C CD    . PRO B 1 17   ? 27.292  5.884   84.250  1.00 42.43 ?  15   PRO B CD    1 
ATOM   9211  N N     . ALA B 1 18   ? 23.758  4.237   81.488  1.00 33.87 ?  16   ALA B N     1 
ATOM   9212  C CA    . ALA B 1 18   ? 22.974  4.543   80.299  1.00 38.11 ?  16   ALA B CA    1 
ATOM   9213  C C     . ALA B 1 18   ? 22.034  5.714   80.581  1.00 34.84 ?  16   ALA B C     1 
ATOM   9214  O O     . ALA B 1 18   ? 21.513  5.840   81.697  1.00 32.82 ?  16   ALA B O     1 
ATOM   9215  C CB    . ALA B 1 18   ? 22.169  3.324   79.849  1.00 35.89 ?  16   ALA B CB    1 
ATOM   9216  N N     . PRO B 1 19   ? 21.803  6.587   79.603  1.00 30.15 ?  17   PRO B N     1 
ATOM   9217  C CA    . PRO B 1 19   ? 20.919  7.738   79.834  1.00 27.44 ?  17   PRO B CA    1 
ATOM   9218  C C     . PRO B 1 19   ? 19.512  7.311   80.240  1.00 27.92 ?  17   PRO B C     1 
ATOM   9219  O O     . PRO B 1 19   ? 18.890  6.455   79.605  1.00 26.59 ?  17   PRO B O     1 
ATOM   9220  C CB    . PRO B 1 19   ? 20.927  8.465   78.483  1.00 30.53 ?  17   PRO B CB    1 
ATOM   9221  C CG    . PRO B 1 19   ? 22.237  8.066   77.853  1.00 34.08 ?  17   PRO B CG    1 
ATOM   9222  C CD    . PRO B 1 19   ? 22.454  6.639   78.282  1.00 32.07 ?  17   PRO B CD    1 
ATOM   9223  N N     . PHE B 1 20   ? 19.032  7.900   81.335  1.00 28.39 ?  18   PHE B N     1 
ATOM   9224  C CA    . PHE B 1 20   ? 17.654  7.784   81.808  1.00 25.97 ?  18   PHE B CA    1 
ATOM   9225  C C     . PHE B 1 20   ? 17.282  6.369   82.249  1.00 28.39 ?  18   PHE B C     1 
ATOM   9226  O O     . PHE B 1 20   ? 16.100  6.080   82.461  1.00 28.33 ?  18   PHE B O     1 
ATOM   9227  C CB    . PHE B 1 20   ? 16.671  8.288   80.749  1.00 21.70 ?  18   PHE B CB    1 
ATOM   9228  C CG    . PHE B 1 20   ? 16.950  9.689   80.295  1.00 22.91 ?  18   PHE B CG    1 
ATOM   9229  C CD1   . PHE B 1 20   ? 16.655  10.771  81.114  1.00 23.89 ?  18   PHE B CD1   1 
ATOM   9230  C CD2   . PHE B 1 20   ? 17.516  9.926   79.054  1.00 20.32 ?  18   PHE B CD2   1 
ATOM   9231  C CE1   . PHE B 1 20   ? 16.912  12.066  80.698  1.00 23.44 ?  18   PHE B CE1   1 
ATOM   9232  C CE2   . PHE B 1 20   ? 17.774  11.217  78.629  1.00 22.37 ?  18   PHE B CE2   1 
ATOM   9233  C CZ    . PHE B 1 20   ? 17.475  12.291  79.455  1.00 23.35 ?  18   PHE B CZ    1 
ATOM   9234  N N     . ALA B 1 21   ? 18.273  5.488   82.420  1.00 29.87 ?  19   ALA B N     1 
ATOM   9235  C CA    . ALA B 1 21   ? 18.016  4.133   82.893  1.00 29.88 ?  19   ALA B CA    1 
ATOM   9236  C C     . ALA B 1 21   ? 17.507  4.100   84.332  1.00 34.21 ?  19   ALA B C     1 
ATOM   9237  O O     . ALA B 1 21   ? 16.867  3.120   84.727  1.00 35.11 ?  19   ALA B O     1 
ATOM   9238  C CB    . ALA B 1 21   ? 19.289  3.292   82.773  1.00 30.99 ?  19   ALA B CB    1 
ATOM   9239  N N     . ASP B 1 22   ? 17.774  5.138   85.123  1.00 29.21 ?  20   ASP B N     1 
ATOM   9240  C CA    . ASP B 1 22   ? 17.304  5.206   86.498  1.00 24.61 ?  20   ASP B CA    1 
ATOM   9241  C C     . ASP B 1 22   ? 16.598  6.530   86.749  1.00 23.85 ?  20   ASP B C     1 
ATOM   9242  O O     . ASP B 1 22   ? 16.764  7.153   87.799  1.00 25.25 ?  20   ASP B O     1 
ATOM   9243  C CB    . ASP B 1 22   ? 18.455  5.010   87.481  1.00 33.66 ?  20   ASP B CB    1 
ATOM   9244  N N     . PHE B 1 23   ? 15.777  6.972   85.794  1.00 18.54 ?  21   PHE B N     1 
ATOM   9245  C CA    . PHE B 1 23   ? 15.238  8.328   85.881  1.00 18.30 ?  21   PHE B CA    1 
ATOM   9246  C C     . PHE B 1 23   ? 14.313  8.481   87.081  1.00 17.77 ?  21   PHE B C     1 
ATOM   9247  O O     . PHE B 1 23   ? 14.504  9.371   87.921  1.00 18.32 ?  21   PHE B O     1 
ATOM   9248  C CB    . PHE B 1 23   ? 14.504  8.697   84.592  1.00 18.31 ?  21   PHE B CB    1 
ATOM   9249  C CG    . PHE B 1 23   ? 13.830  10.029  84.662  1.00 18.59 ?  21   PHE B CG    1 
ATOM   9250  C CD1   . PHE B 1 23   ? 14.577  11.187  84.815  1.00 18.90 ?  21   PHE B CD1   1 
ATOM   9251  C CD2   . PHE B 1 23   ? 12.449  10.124  84.601  1.00 20.08 ?  21   PHE B CD2   1 
ATOM   9252  C CE1   . PHE B 1 23   ? 13.955  12.428  84.908  1.00 16.72 ?  21   PHE B CE1   1 
ATOM   9253  C CE2   . PHE B 1 23   ? 11.827  11.358  84.691  1.00 22.17 ?  21   PHE B CE2   1 
ATOM   9254  C CZ    . PHE B 1 23   ? 12.580  12.506  84.844  1.00 20.29 ?  21   PHE B CZ    1 
ATOM   9255  N N     . ALA B 1 24   ? 13.292  7.631   87.166  1.00 18.46 ?  22   ALA B N     1 
ATOM   9256  C CA    . ALA B 1 24   ? 12.309  7.760   88.239  1.00 18.85 ?  22   ALA B CA    1 
ATOM   9257  C C     . ALA B 1 24   ? 11.606  6.435   88.513  1.00 18.25 ?  22   ALA B C     1 
ATOM   9258  O O     . ALA B 1 24   ? 10.376  6.361   88.422  1.00 19.38 ?  22   ALA B O     1 
ATOM   9259  C CB    . ALA B 1 24   ? 11.273  8.830   87.887  1.00 20.43 ?  22   ALA B CB    1 
ATOM   9260  N N     . PRO B 1 25   ? 12.329  5.382   88.876  1.00 19.85 ?  23   PRO B N     1 
ATOM   9261  C CA    . PRO B 1 25   ? 11.676  4.095   89.140  1.00 22.01 ?  23   PRO B CA    1 
ATOM   9262  C C     . PRO B 1 25   ? 10.738  4.201   90.329  1.00 20.70 ?  23   PRO B C     1 
ATOM   9263  O O     . PRO B 1 25   ? 11.079  4.822   91.347  1.00 20.27 ?  23   PRO B O     1 
ATOM   9264  C CB    . PRO B 1 25   ? 12.856  3.160   89.437  1.00 24.52 ?  23   PRO B CB    1 
ATOM   9265  C CG    . PRO B 1 25   ? 13.904  4.065   89.993  1.00 24.37 ?  23   PRO B CG    1 
ATOM   9266  C CD    . PRO B 1 25   ? 13.755  5.371   89.252  1.00 22.36 ?  23   PRO B CD    1 
ATOM   9267  N N     . PRO B 1 26   ? 9.541   3.627   90.237  1.00 19.50 ?  24   PRO B N     1 
ATOM   9268  C CA    . PRO B 1 26   ? 8.599   3.705   91.360  1.00 19.88 ?  24   PRO B CA    1 
ATOM   9269  C C     . PRO B 1 26   ? 9.075   2.872   92.543  1.00 21.22 ?  24   PRO B C     1 
ATOM   9270  O O     . PRO B 1 26   ? 9.877   1.946   92.404  1.00 22.97 ?  24   PRO B O     1 
ATOM   9271  C CB    . PRO B 1 26   ? 7.300   3.143   90.771  1.00 21.18 ?  24   PRO B CB    1 
ATOM   9272  C CG    . PRO B 1 26   ? 7.756   2.225   89.693  1.00 23.73 ?  24   PRO B CG    1 
ATOM   9273  C CD    . PRO B 1 26   ? 8.981   2.882   89.096  1.00 21.78 ?  24   PRO B CD    1 
ATOM   9274  N N     . VAL B 1 27   ? 8.567   3.229   93.733  1.00 19.74 ?  25   VAL B N     1 
ATOM   9275  C CA    . VAL B 1 27   ? 8.929   2.510   94.957  1.00 18.25 ?  25   VAL B CA    1 
ATOM   9276  C C     . VAL B 1 27   ? 8.585   1.023   94.839  1.00 20.65 ?  25   VAL B C     1 
ATOM   9277  O O     . VAL B 1 27   ? 9.358   0.156   95.274  1.00 22.06 ?  25   VAL B O     1 
ATOM   9278  C CB    . VAL B 1 27   ? 8.250   3.161   96.182  1.00 19.75 ?  25   VAL B CB    1 
ATOM   9279  C CG1   . VAL B 1 27   ? 8.454   2.304   97.424  1.00 22.44 ?  25   VAL B CG1   1 
ATOM   9280  C CG2   . VAL B 1 27   ? 8.798   4.553   96.413  1.00 21.46 ?  25   VAL B CG2   1 
ATOM   9281  N N     . ARG B 1 28   ? 7.443   0.705   94.241  1.00 20.77 ?  26   ARG B N     1 
ATOM   9282  C CA    . ARG B 1 28   ? 7.026   -0.673  94.015  1.00 19.96 ?  26   ARG B CA    1 
ATOM   9283  C C     . ARG B 1 28   ? 6.287   -0.739  92.691  1.00 22.51 ?  26   ARG B C     1 
ATOM   9284  O O     . ARG B 1 28   ? 5.784   0.281   92.208  1.00 21.24 ?  26   ARG B O     1 
ATOM   9285  C CB    . ARG B 1 28   ? 6.124   -1.175  95.150  1.00 25.53 ?  26   ARG B CB    1 
ATOM   9286  C CG    . ARG B 1 28   ? 4.781   -0.460  95.228  1.00 23.32 ?  26   ARG B CG    1 
ATOM   9287  C CD    . ARG B 1 28   ? 4.074   -0.765  96.550  1.00 26.19 ?  26   ARG B CD    1 
ATOM   9288  N NE    . ARG B 1 28   ? 4.732   -0.096  97.668  1.00 28.89 ?  26   ARG B NE    1 
ATOM   9289  C CZ    . ARG B 1 28   ? 5.492   -0.710  98.565  1.00 28.43 ?  26   ARG B CZ    1 
ATOM   9290  N NH1   . ARG B 1 28   ? 5.684   -2.019  98.528  1.00 31.58 ?  26   ARG B NH1   1 
ATOM   9291  N NH2   . ARG B 1 28   ? 6.073   0.007   99.523  1.00 26.53 ?  26   ARG B NH2   1 
ATOM   9292  N N     . PRO B 1 29   ? 6.214   -1.913  92.067  1.00 23.26 ?  27   PRO B N     1 
ATOM   9293  C CA    . PRO B 1 29   ? 5.351   -2.043  90.886  1.00 25.16 ?  27   PRO B CA    1 
ATOM   9294  C C     . PRO B 1 29   ? 3.914   -1.702  91.255  1.00 22.04 ?  27   PRO B C     1 
ATOM   9295  O O     . PRO B 1 29   ? 3.417   -2.088  92.317  1.00 25.14 ?  27   PRO B O     1 
ATOM   9296  C CB    . PRO B 1 29   ? 5.507   -3.516  90.483  1.00 24.17 ?  27   PRO B CB    1 
ATOM   9297  C CG    . PRO B 1 29   ? 6.787   -3.957  91.116  1.00 25.38 ?  27   PRO B CG    1 
ATOM   9298  C CD    . PRO B 1 29   ? 6.904   -3.174  92.393  1.00 26.39 ?  27   PRO B CD    1 
ATOM   9299  N N     . GLN B 1 30   ? 3.257   -0.947  90.375  1.00 23.58 ?  28   GLN B N     1 
ATOM   9300  C CA    . GLN B 1 30   ? 1.931   -0.406  90.653  1.00 23.86 ?  28   GLN B CA    1 
ATOM   9301  C C     . GLN B 1 30   ? 0.860   -1.462  90.406  1.00 21.15 ?  28   GLN B C     1 
ATOM   9302  O O     . GLN B 1 30   ? 0.695   -1.935  89.275  1.00 26.34 ?  28   GLN B O     1 
ATOM   9303  C CB    . GLN B 1 30   ? 1.675   0.820   89.784  1.00 22.93 ?  28   GLN B CB    1 
ATOM   9304  C CG    . GLN B 1 30   ? 2.737   1.889   89.924  1.00 21.29 ?  28   GLN B CG    1 
ATOM   9305  C CD    . GLN B 1 30   ? 2.712   2.552   91.287  1.00 22.61 ?  28   GLN B CD    1 
ATOM   9306  O OE1   . GLN B 1 30   ? 1.834   3.371   91.566  1.00 19.58 ?  28   GLN B OE1   1 
ATOM   9307  N NE2   . GLN B 1 30   ? 3.676   2.202   92.149  1.00 21.16 ?  28   GLN B NE2   1 
ATOM   9308  N N     . SER B 1 31   ? 0.124   -1.810  91.460  1.00 23.61 ?  29   SER B N     1 
ATOM   9309  C CA    . SER B 1 31   ? -0.970  -2.767  91.376  1.00 20.78 ?  29   SER B CA    1 
ATOM   9310  C C     . SER B 1 31   ? -2.139  -2.190  90.578  1.00 22.67 ?  29   SER B C     1 
ATOM   9311  O O     . SER B 1 31   ? -2.185  -1.001  90.253  1.00 21.00 ?  29   SER B O     1 
ATOM   9312  C CB    . SER B 1 31   ? -1.457  -3.149  92.774  1.00 23.24 ?  29   SER B CB    1 
ATOM   9313  O OG    . SER B 1 31   ? -2.018  -2.016  93.415  1.00 22.08 ?  29   SER B OG    1 
ATOM   9314  N N     . THR B 1 32   ? -3.103  -3.064  90.269  1.00 25.47 ?  30   THR B N     1 
ATOM   9315  C CA    . THR B 1 32   ? -4.342  -2.611  89.642  1.00 21.99 ?  30   THR B CA    1 
ATOM   9316  C C     . THR B 1 32   ? -5.002  -1.508  90.461  1.00 20.09 ?  30   THR B C     1 
ATOM   9317  O O     . THR B 1 32   ? -5.421  -0.483  89.910  1.00 21.27 ?  30   THR B O     1 
ATOM   9318  C CB    . THR B 1 32   ? -5.299  -3.792  89.458  1.00 24.63 ?  30   THR B CB    1 
ATOM   9319  O OG1   . THR B 1 32   ? -4.712  -4.745  88.565  1.00 32.94 ?  30   THR B OG1   1 
ATOM   9320  C CG2   . THR B 1 32   ? -6.628  -3.333  88.886  1.00 24.78 ?  30   THR B CG2   1 
ATOM   9321  N N     . LEU B 1 33   ? -5.084  -1.689  91.781  1.00 21.77 ?  31   LEU B N     1 
ATOM   9322  C CA    . LEU B 1 33   ? -5.717  -0.679  92.621  1.00 19.27 ?  31   LEU B CA    1 
ATOM   9323  C C     . LEU B 1 33   ? -4.907  0.611   92.653  1.00 20.20 ?  31   LEU B C     1 
ATOM   9324  O O     . LEU B 1 33   ? -5.482  1.705   92.641  1.00 19.59 ?  31   LEU B O     1 
ATOM   9325  C CB    . LEU B 1 33   ? -5.924  -1.224  94.033  1.00 20.66 ?  31   LEU B CB    1 
ATOM   9326  C CG    . LEU B 1 33   ? -7.002  -2.302  94.121  1.00 24.10 ?  31   LEU B CG    1 
ATOM   9327  C CD1   . LEU B 1 33   ? -6.873  -3.069  95.418  1.00 22.92 ?  31   LEU B CD1   1 
ATOM   9328  C CD2   . LEU B 1 33   ? -8.385  -1.678  94.006  1.00 25.87 ?  31   LEU B CD2   1 
ATOM   9329  N N     . ARG B 1 34   ? -3.576  0.515   92.698  1.00 19.65 ?  32   ARG B N     1 
ATOM   9330  C CA    . ARG B 1 34   ? -2.777  1.738   92.678  1.00 18.43 ?  32   ARG B CA    1 
ATOM   9331  C C     . ARG B 1 34   ? -2.917  2.455   91.340  1.00 19.70 ?  32   ARG B C     1 
ATOM   9332  O O     . ARG B 1 34   ? -2.983  3.689   91.295  1.00 18.10 ?  32   ARG B O     1 
ATOM   9333  C CB    . ARG B 1 34   ? -1.308  1.435   92.983  1.00 17.31 ?  32   ARG B CB    1 
ATOM   9334  C CG    . ARG B 1 34   ? -1.024  1.063   94.446  1.00 19.20 ?  32   ARG B CG    1 
ATOM   9335  C CD    . ARG B 1 34   ? -1.116  2.269   95.382  1.00 19.64 ?  32   ARG B CD    1 
ATOM   9336  N NE    . ARG B 1 34   ? -0.079  3.263   95.120  1.00 19.25 ?  32   ARG B NE    1 
ATOM   9337  C CZ    . ARG B 1 34   ? 1.121   3.270   95.691  1.00 20.76 ?  32   ARG B CZ    1 
ATOM   9338  N NH1   . ARG B 1 34   ? 1.469   2.356   96.585  1.00 20.47 ?  32   ARG B NH1   1 
ATOM   9339  N NH2   . ARG B 1 34   ? 1.996   4.216   95.355  1.00 19.54 ?  32   ARG B NH2   1 
ATOM   9340  N N     . ARG B 1 35   ? -3.001  1.703   90.239  1.00 19.44 ?  33   ARG B N     1 
ATOM   9341  C CA    . ARG B 1 35   ? -3.131  2.351   88.939  1.00 18.69 ?  33   ARG B CA    1 
ATOM   9342  C C     . ARG B 1 35   ? -4.462  3.072   88.798  1.00 15.81 ?  33   ARG B C     1 
ATOM   9343  O O     . ARG B 1 35   ? -4.537  4.103   88.114  1.00 18.09 ?  33   ARG B O     1 
ATOM   9344  C CB    . ARG B 1 35   ? -2.974  1.325   87.816  1.00 20.15 ?  33   ARG B CB    1 
ATOM   9345  C CG    . ARG B 1 35   ? -1.561  0.838   87.655  1.00 24.09 ?  33   ARG B CG    1 
ATOM   9346  C CD    . ARG B 1 35   ? -1.459  -0.252  86.591  1.00 27.91 ?  33   ARG B CD    1 
ATOM   9347  N NE    . ARG B 1 35   ? -0.098  -0.768  86.548  1.00 37.76 ?  33   ARG B NE    1 
ATOM   9348  C CZ    . ARG B 1 35   ? 0.926   -0.136  85.989  1.00 41.32 ?  33   ARG B CZ    1 
ATOM   9349  N NH1   . ARG B 1 35   ? 0.769   1.026   85.372  1.00 44.48 ?  33   ARG B NH1   1 
ATOM   9350  N NH2   . ARG B 1 35   ? 2.140   -0.677  86.055  1.00 44.71 ?  33   ARG B NH2   1 
ATOM   9351  N N     . ALA B 1 36   ? -5.523  2.544   89.411  1.00 17.76 ?  34   ALA B N     1 
ATOM   9352  C CA    . ALA B 1 36   ? -6.812  3.219   89.331  1.00 17.93 ?  34   ALA B CA    1 
ATOM   9353  C C     . ALA B 1 36   ? -6.790  4.540   90.088  1.00 15.62 ?  34   ALA B C     1 
ATOM   9354  O O     . ALA B 1 36   ? -7.438  5.500   89.663  1.00 20.77 ?  34   ALA B O     1 
ATOM   9355  C CB    . ALA B 1 36   ? -7.924  2.320   89.857  1.00 20.78 ?  34   ALA B CB    1 
ATOM   9356  N N     . ILE B 1 37   ? -6.052  4.610   91.200  1.00 16.98 ?  35   ILE B N     1 
ATOM   9357  C CA    . ILE B 1 37   ? -5.835  5.893   91.867  1.00 17.02 ?  35   ILE B CA    1 
ATOM   9358  C C     . ILE B 1 37   ? -5.172  6.877   90.918  1.00 17.80 ?  35   ILE B C     1 
ATOM   9359  O O     . ILE B 1 37   ? -5.659  7.996   90.711  1.00 15.96 ?  35   ILE B O     1 
ATOM   9360  C CB    . ILE B 1 37   ? -4.991  5.691   93.135  1.00 15.34 ?  35   ILE B CB    1 
ATOM   9361  C CG1   . ILE B 1 37   ? -5.755  4.841   94.143  1.00 15.92 ?  35   ILE B CG1   1 
ATOM   9362  C CG2   . ILE B 1 37   ? -4.560  7.038   93.725  1.00 17.02 ?  35   ILE B CG2   1 
ATOM   9363  C CD1   . ILE B 1 37   ? -4.855  4.303   95.232  1.00 15.80 ?  35   ILE B CD1   1 
ATOM   9364  N N     . THR B 1 38   ? -4.038  6.480   90.338  1.00 16.15 ?  36   THR B N     1 
ATOM   9365  C CA    . THR B 1 38   ? -3.284  7.392   89.484  1.00 14.82 ?  36   THR B CA    1 
ATOM   9366  C C     . THR B 1 38   ? -4.118  7.853   88.291  1.00 15.83 ?  36   THR B C     1 
ATOM   9367  O O     . THR B 1 38   ? -4.058  9.024   87.903  1.00 14.67 ?  36   THR B O     1 
ATOM   9368  C CB    . THR B 1 38   ? -1.981  6.730   89.023  1.00 17.92 ?  36   THR B CB    1 
ATOM   9369  O OG1   . THR B 1 38   ? -1.264  6.217   90.166  1.00 17.25 ?  36   THR B OG1   1 
ATOM   9370  C CG2   . THR B 1 38   ? -1.109  7.739   88.291  1.00 17.01 ?  36   THR B CG2   1 
ATOM   9371  N N     . ALA B 1 39   ? -4.915  6.952   87.712  1.00 15.94 ?  37   ALA B N     1 
ATOM   9372  C CA    . ALA B 1 39   ? -5.751  7.300   86.566  1.00 16.78 ?  37   ALA B CA    1 
ATOM   9373  C C     . ALA B 1 39   ? -6.755  8.406   86.871  1.00 18.80 ?  37   ALA B C     1 
ATOM   9374  O O     . ALA B 1 39   ? -7.177  9.115   85.952  1.00 18.06 ?  37   ALA B O     1 
ATOM   9375  C CB    . ALA B 1 39   ? -6.489  6.050   86.085  1.00 18.09 ?  37   ALA B CB    1 
ATOM   9376  N N     . ALA B 1 40   ? -7.144  8.579   88.128  1.00 16.53 ?  38   ALA B N     1 
ATOM   9377  C CA    . ALA B 1 40   ? -8.142  9.577   88.489  1.00 15.00 ?  38   ALA B CA    1 
ATOM   9378  C C     . ALA B 1 40   ? -7.538  10.921  88.877  1.00 15.53 ?  38   ALA B C     1 
ATOM   9379  O O     . ALA B 1 40   ? -8.296  11.862  89.137  1.00 16.87 ?  38   ALA B O     1 
ATOM   9380  C CB    . ALA B 1 40   ? -8.998  9.068   89.657  1.00 16.79 ?  38   ALA B CB    1 
ATOM   9381  N N     . TYR B 1 41   ? -6.204  11.017  88.957  1.00 15.82 ?  39   TYR B N     1 
ATOM   9382  C CA    . TYR B 1 41   ? -5.527  12.186  89.518  1.00 13.68 ?  39   TYR B CA    1 
ATOM   9383  C C     . TYR B 1 41   ? -6.137  13.512  89.049  1.00 14.06 ?  39   TYR B C     1 
ATOM   9384  O O     . TYR B 1 41   ? -6.531  14.347  89.875  1.00 13.94 ?  39   TYR B O     1 
ATOM   9385  C CB    . TYR B 1 41   ? -4.039  12.091  89.163  1.00 14.55 ?  39   TYR B CB    1 
ATOM   9386  C CG    . TYR B 1 41   ? -3.049  12.797  90.076  1.00 13.27 ?  39   TYR B CG    1 
ATOM   9387  C CD1   . TYR B 1 41   ? -3.373  13.966  90.773  1.00 13.60 ?  39   TYR B CD1   1 
ATOM   9388  C CD2   . TYR B 1 41   ? -1.750  12.318  90.185  1.00 14.06 ?  39   TYR B CD2   1 
ATOM   9389  C CE1   . TYR B 1 41   ? -2.424  14.619  91.565  1.00 14.18 ?  39   TYR B CE1   1 
ATOM   9390  C CE2   . TYR B 1 41   ? -0.799  12.953  90.976  1.00 13.63 ?  39   TYR B CE2   1 
ATOM   9391  C CZ    . TYR B 1 41   ? -1.139  14.107  91.660  1.00 15.41 ?  39   TYR B CZ    1 
ATOM   9392  O OH    . TYR B 1 41   ? -0.191  14.745  92.430  1.00 14.20 ?  39   TYR B OH    1 
ATOM   9393  N N     . ARG B 1 42   ? -6.267  13.712  87.730  1.00 16.29 ?  40   ARG B N     1 
ATOM   9394  C CA    . ARG B 1 42   ? -6.814  14.972  87.219  1.00 18.55 ?  40   ARG B CA    1 
ATOM   9395  C C     . ARG B 1 42   ? -7.997  14.732  86.300  1.00 17.84 ?  40   ARG B C     1 
ATOM   9396  O O     . ARG B 1 42   ? -8.196  15.451  85.317  1.00 17.58 ?  40   ARG B O     1 
ATOM   9397  C CB    . ARG B 1 42   ? -5.734  15.797  86.532  1.00 16.42 ?  40   ARG B CB    1 
ATOM   9398  C CG    . ARG B 1 42   ? -4.716  16.257  87.566  1.00 16.18 ?  40   ARG B CG    1 
ATOM   9399  C CD    . ARG B 1 42   ? -3.489  16.870  86.960  1.00 17.24 ?  40   ARG B CD    1 
ATOM   9400  N NE    . ARG B 1 42   ? -2.420  16.825  87.945  1.00 15.69 ?  40   ARG B NE    1 
ATOM   9401  C CZ    . ARG B 1 42   ? -2.252  17.717  88.910  1.00 13.95 ?  40   ARG B CZ    1 
ATOM   9402  N NH1   . ARG B 1 42   ? -3.008  18.806  88.987  1.00 14.79 ?  40   ARG B NH1   1 
ATOM   9403  N NH2   . ARG B 1 42   ? -1.303  17.517  89.814  1.00 14.77 ?  40   ARG B NH2   1 
ATOM   9404  N N     . ARG B 1 43   ? -8.820  13.747  86.647  1.00 16.45 ?  41   ARG B N     1 
ATOM   9405  C CA    . ARG B 1 43   ? -9.984  13.395  85.850  1.00 16.86 ?  41   ARG B CA    1 
ATOM   9406  C C     . ARG B 1 43   ? -10.937 14.584  85.751  1.00 18.41 ?  41   ARG B C     1 
ATOM   9407  O O     . ARG B 1 43   ? -11.158 15.289  86.738  1.00 18.34 ?  41   ARG B O     1 
ATOM   9408  C CB    . ARG B 1 43   ? -10.689 12.190  86.485  1.00 17.32 ?  41   ARG B CB    1 
ATOM   9409  C CG    . ARG B 1 43   ? -11.937 11.698  85.771  1.00 16.86 ?  41   ARG B CG    1 
ATOM   9410  C CD    . ARG B 1 43   ? -12.327 10.309  86.255  1.00 18.25 ?  41   ARG B CD    1 
ATOM   9411  N NE    . ARG B 1 43   ? -11.336 9.316   85.855  1.00 18.50 ?  41   ARG B NE    1 
ATOM   9412  C CZ    . ARG B 1 43   ? -11.070 8.208   86.533  1.00 19.79 ?  41   ARG B CZ    1 
ATOM   9413  N NH1   . ARG B 1 43   ? -11.715 7.905   87.645  1.00 20.64 ?  41   ARG B NH1   1 
ATOM   9414  N NH2   . ARG B 1 43   ? -10.125 7.387   86.089  1.00 22.46 ?  41   ARG B NH2   1 
ATOM   9415  N N     . PRO B 1 44   ? -11.515 14.843  84.580  1.00 16.78 ?  42   PRO B N     1 
ATOM   9416  C CA    . PRO B 1 44   ? -12.465 15.951  84.469  1.00 17.69 ?  42   PRO B CA    1 
ATOM   9417  C C     . PRO B 1 44   ? -13.574 15.844  85.508  1.00 16.37 ?  42   PRO B C     1 
ATOM   9418  O O     . PRO B 1 44   ? -14.081 14.760  85.810  1.00 16.91 ?  42   PRO B O     1 
ATOM   9419  C CB    . PRO B 1 44   ? -13.005 15.808  83.041  1.00 17.19 ?  42   PRO B CB    1 
ATOM   9420  C CG    . PRO B 1 44   ? -11.848 15.221  82.301  1.00 22.27 ?  42   PRO B CG    1 
ATOM   9421  C CD    . PRO B 1 44   ? -11.216 14.245  83.265  1.00 19.87 ?  42   PRO B CD    1 
ATOM   9422  N N     . GLU B 1 45   ? -13.963 17.002  86.035  1.00 17.73 ?  43   GLU B N     1 
ATOM   9423  C CA    . GLU B 1 45   ? -14.990 17.056  87.065  1.00 19.13 ?  43   GLU B CA    1 
ATOM   9424  C C     . GLU B 1 45   ? -16.310 16.450  86.581  1.00 18.23 ?  43   GLU B C     1 
ATOM   9425  O O     . GLU B 1 45   ? -17.000 15.762  87.342  1.00 20.49 ?  43   GLU B O     1 
ATOM   9426  C CB    . GLU B 1 45   ? -15.159 18.514  87.500  1.00 22.73 ?  43   GLU B CB    1 
ATOM   9427  C CG    . GLU B 1 45   ? -15.493 18.678  88.948  1.00 23.44 ?  43   GLU B CG    1 
ATOM   9428  C CD    . GLU B 1 45   ? -15.023 20.001  89.564  1.00 15.80 ?  43   GLU B CD    1 
ATOM   9429  O OE1   . GLU B 1 45   ? -14.250 20.794  88.963  1.00 17.18 ?  43   GLU B OE1   1 
ATOM   9430  O OE2   . GLU B 1 45   ? -15.451 20.232  90.708  1.00 17.51 ?  43   GLU B OE2   1 
ATOM   9431  N N     . THR B 1 46   ? -16.664 16.664  85.307  1.00 19.61 ?  44   THR B N     1 
ATOM   9432  C CA    . THR B 1 46   ? -17.900 16.093  84.785  1.00 19.02 ?  44   THR B CA    1 
ATOM   9433  C C     . THR B 1 46   ? -17.864 14.569  84.729  1.00 19.96 ?  44   THR B C     1 
ATOM   9434  O O     . THR B 1 46   ? -18.927 13.939  84.710  1.00 23.16 ?  44   THR B O     1 
ATOM   9435  C CB    . THR B 1 46   ? -18.191 16.650  83.391  1.00 22.08 ?  44   THR B CB    1 
ATOM   9436  O OG1   . THR B 1 46   ? -17.012 16.545  82.586  1.00 21.41 ?  44   THR B OG1   1 
ATOM   9437  C CG2   . THR B 1 46   ? -18.600 18.112  83.482  1.00 22.08 ?  44   THR B CG2   1 
ATOM   9438  N N     . GLU B 1 47   ? -16.672 13.965  84.695  1.00 17.63 ?  45   GLU B N     1 
ATOM   9439  C CA    . GLU B 1 47   ? -16.559 12.514  84.768  1.00 17.47 ?  45   GLU B CA    1 
ATOM   9440  C C     . GLU B 1 47   ? -16.561 11.999  86.200  1.00 19.17 ?  45   GLU B C     1 
ATOM   9441  O O     . GLU B 1 47   ? -17.020 10.879  86.453  1.00 22.26 ?  45   GLU B O     1 
ATOM   9442  C CB    . GLU B 1 47   ? -15.279 12.051  84.062  1.00 19.51 ?  45   GLU B CB    1 
ATOM   9443  C CG    . GLU B 1 47   ? -15.286 12.253  82.553  1.00 25.16 ?  45   GLU B CG    1 
ATOM   9444  C CD    . GLU B 1 47   ? -13.984 11.818  81.924  1.00 28.57 ?  45   GLU B CD    1 
ATOM   9445  O OE1   . GLU B 1 47   ? -13.382 10.850  82.431  1.00 30.65 ?  45   GLU B OE1   1 
ATOM   9446  O OE2   . GLU B 1 47   ? -13.559 12.454  80.934  1.00 32.52 ?  45   GLU B OE2   1 
ATOM   9447  N N     . CYS B 1 48   ? -16.069 12.799  87.143  1.00 19.47 ?  46   CYS B N     1 
ATOM   9448  C CA    . CYS B 1 48   ? -15.969 12.331  88.519  1.00 19.40 ?  46   CYS B CA    1 
ATOM   9449  C C     . CYS B 1 48   ? -17.325 12.283  89.197  1.00 18.88 ?  46   CYS B C     1 
ATOM   9450  O O     . CYS B 1 48   ? -17.598 11.372  89.985  1.00 19.50 ?  46   CYS B O     1 
ATOM   9451  C CB    . CYS B 1 48   ? -15.051 13.242  89.329  1.00 18.21 ?  46   CYS B CB    1 
ATOM   9452  S SG    . CYS B 1 48   ? -13.320 13.243  88.884  1.00 19.14 ?  46   CYS B SG    1 
ATOM   9453  N N     . LEU B 1 49   ? -18.169 13.267  88.936  1.00 18.80 ?  47   LEU B N     1 
ATOM   9454  C CA    . LEU B 1 49   ? -19.341 13.441  89.780  1.00 19.78 ?  47   LEU B CA    1 
ATOM   9455  C C     . LEU B 1 49   ? -20.457 12.416  89.574  1.00 19.61 ?  47   LEU B C     1 
ATOM   9456  O O     . LEU B 1 49   ? -21.091 12.050  90.563  1.00 20.34 ?  47   LEU B O     1 
ATOM   9457  C CB    . LEU B 1 49   ? -19.890 14.863  89.621  1.00 19.62 ?  47   LEU B CB    1 
ATOM   9458  C CG    . LEU B 1 49   ? -19.456 15.810  90.759  1.00 18.03 ?  47   LEU B CG    1 
ATOM   9459  C CD1   . LEU B 1 49   ? -19.931 15.314  92.131  1.00 20.52 ?  47   LEU B CD1   1 
ATOM   9460  C CD2   . LEU B 1 49   ? -17.951 16.014  90.761  1.00 19.15 ?  47   LEU B CD2   1 
ATOM   9461  N N     . PRO B 1 50   ? -20.755 11.930  88.366  1.00 21.50 ?  48   PRO B N     1 
ATOM   9462  C CA    . PRO B 1 50   ? -21.898 11.000  88.226  1.00 22.94 ?  48   PRO B CA    1 
ATOM   9463  C C     . PRO B 1 50   ? -21.773 9.750   89.090  1.00 23.78 ?  48   PRO B C     1 
ATOM   9464  O O     . PRO B 1 50   ? -22.755 9.371   89.743  1.00 23.81 ?  48   PRO B O     1 
ATOM   9465  C CB    . PRO B 1 50   ? -21.905 10.669  86.726  1.00 23.53 ?  48   PRO B CB    1 
ATOM   9466  C CG    . PRO B 1 50   ? -21.403 11.934  86.106  1.00 21.98 ?  48   PRO B CG    1 
ATOM   9467  C CD    . PRO B 1 50   ? -20.286 12.378  87.035  1.00 21.18 ?  48   PRO B CD    1 
ATOM   9468  N N     . PRO B 1 51   ? -20.612 9.075   89.149  1.00 22.30 ?  49   PRO B N     1 
ATOM   9469  C CA    . PRO B 1 51   ? -20.541 7.897   90.036  1.00 22.58 ?  49   PRO B CA    1 
ATOM   9470  C C     . PRO B 1 51   ? -20.589 8.237   91.518  1.00 23.05 ?  49   PRO B C     1 
ATOM   9471  O O     . PRO B 1 51   ? -21.055 7.410   92.311  1.00 23.56 ?  49   PRO B O     1 
ATOM   9472  C CB    . PRO B 1 51   ? -19.211 7.232   89.651  1.00 25.00 ?  49   PRO B CB    1 
ATOM   9473  C CG    . PRO B 1 51   ? -18.422 8.295   89.006  1.00 26.37 ?  49   PRO B CG    1 
ATOM   9474  C CD    . PRO B 1 51   ? -19.402 9.180   88.309  1.00 20.52 ?  49   PRO B CD    1 
ATOM   9475  N N     . LEU B 1 52   ? -20.121 9.424   91.914  1.00 22.36 ?  50   LEU B N     1 
ATOM   9476  C CA    . LEU B 1 52   ? -20.273 9.843   93.304  1.00 21.17 ?  50   LEU B CA    1 
ATOM   9477  C C     . LEU B 1 52   ? -21.738 10.124  93.638  1.00 23.96 ?  50   LEU B C     1 
ATOM   9478  O O     . LEU B 1 52   ? -22.219 9.750   94.716  1.00 23.97 ?  50   LEU B O     1 
ATOM   9479  C CB    . LEU B 1 52   ? -19.402 11.076  93.575  1.00 19.96 ?  50   LEU B CB    1 
ATOM   9480  C CG    . LEU B 1 52   ? -17.890 10.925  93.375  1.00 21.11 ?  50   LEU B CG    1 
ATOM   9481  C CD1   . LEU B 1 52   ? -17.188 12.282  93.464  1.00 18.86 ?  50   LEU B CD1   1 
ATOM   9482  C CD2   . LEU B 1 52   ? -17.291 9.938   94.380  1.00 20.45 ?  50   LEU B CD2   1 
ATOM   9483  N N     . VAL B 1 53   ? -22.464 10.777  92.725  1.00 21.91 ?  51   VAL B N     1 
ATOM   9484  C CA    . VAL B 1 53   ? -23.894 11.005  92.931  1.00 24.00 ?  51   VAL B CA    1 
ATOM   9485  C C     . VAL B 1 53   ? -24.612 9.681   93.143  1.00 25.75 ?  51   VAL B C     1 
ATOM   9486  O O     . VAL B 1 53   ? -25.441 9.538   94.051  1.00 27.45 ?  51   VAL B O     1 
ATOM   9487  C CB    . VAL B 1 53   ? -24.497 11.779  91.745  1.00 24.94 ?  51   VAL B CB    1 
ATOM   9488  C CG1   . VAL B 1 53   ? -26.027 11.802  91.848  1.00 25.43 ?  51   VAL B CG1   1 
ATOM   9489  C CG2   . VAL B 1 53   ? -23.936 13.192  91.684  1.00 27.22 ?  51   VAL B CG2   1 
ATOM   9490  N N     . GLU B 1 54   ? -24.297 8.688   92.308  1.00 26.26 ?  52   GLU B N     1 
ATOM   9491  C CA    . GLU B 1 54   ? -24.935 7.382   92.434  1.00 26.28 ?  52   GLU B CA    1 
ATOM   9492  C C     . GLU B 1 54   ? -24.642 6.758   93.793  1.00 28.14 ?  52   GLU B C     1 
ATOM   9493  O O     . GLU B 1 54   ? -25.553 6.281   94.478  1.00 26.81 ?  52   GLU B O     1 
ATOM   9494  C CB    . GLU B 1 54   ? -24.470 6.465   91.301  1.00 28.10 ?  52   GLU B CB    1 
ATOM   9495  N N     . ALA B 1 55   ? -23.371 6.776   94.208  1.00 24.65 ?  53   ALA B N     1 
ATOM   9496  C CA    . ALA B 1 55   ? -22.979 6.137   95.458  1.00 28.44 ?  53   ALA B CA    1 
ATOM   9497  C C     . ALA B 1 55   ? -23.506 6.888   96.679  1.00 25.17 ?  53   ALA B C     1 
ATOM   9498  O O     . ALA B 1 55   ? -23.710 6.280   97.736  1.00 29.62 ?  53   ALA B O     1 
ATOM   9499  C CB    . ALA B 1 55   ? -21.454 6.021   95.516  1.00 30.34 ?  53   ALA B CB    1 
ATOM   9500  N N     . ALA B 1 56   ? -23.727 8.197   96.561  1.00 24.37 ?  54   ALA B N     1 
ATOM   9501  C CA    . ALA B 1 56   ? -24.235 8.998   97.669  1.00 24.58 ?  54   ALA B CA    1 
ATOM   9502  C C     . ALA B 1 56   ? -25.754 9.031   97.742  1.00 28.86 ?  54   ALA B C     1 
ATOM   9503  O O     . ALA B 1 56   ? -26.299 9.682   98.641  1.00 32.14 ?  54   ALA B O     1 
ATOM   9504  C CB    . ALA B 1 56   ? -23.711 10.432  97.572  1.00 24.99 ?  54   ALA B CB    1 
ATOM   9505  N N     . THR B 1 57   ? -26.445 8.363   96.821  1.00 27.24 ?  55   THR B N     1 
ATOM   9506  C CA    . THR B 1 57   ? -27.902 8.382   96.808  1.00 31.19 ?  55   THR B CA    1 
ATOM   9507  C C     . THR B 1 57   ? -28.461 7.628   98.010  1.00 30.63 ?  55   THR B C     1 
ATOM   9508  O O     . THR B 1 57   ? -28.009 6.524   98.331  1.00 33.31 ?  55   THR B O     1 
ATOM   9509  C CB    . THR B 1 57   ? -28.423 7.772   95.506  1.00 27.88 ?  55   THR B CB    1 
ATOM   9510  O OG1   . THR B 1 57   ? -27.986 8.566   94.398  1.00 32.41 ?  55   THR B OG1   1 
ATOM   9511  C CG2   . THR B 1 57   ? -29.954 7.709   95.514  1.00 32.48 ?  55   THR B CG2   1 
ATOM   9512  N N     . GLN B 1 58   ? -29.445 8.233   98.679  1.00 29.52 ?  56   GLN B N     1 
ATOM   9513  C CA    . GLN B 1 58   ? -30.147 7.613   99.794  1.00 31.34 ?  56   GLN B CA    1 
ATOM   9514  C C     . GLN B 1 58   ? -31.654 7.703   99.576  1.00 34.96 ?  56   GLN B C     1 
ATOM   9515  O O     . GLN B 1 58   ? -32.143 8.585   98.867  1.00 34.07 ?  56   GLN B O     1 
ATOM   9516  C CB    . GLN B 1 58   ? -29.767 8.267   101.132 1.00 34.42 ?  56   GLN B CB    1 
ATOM   9517  C CG    . GLN B 1 58   ? -28.274 8.229   101.426 1.00 29.67 ?  56   GLN B CG    1 
ATOM   9518  C CD    . GLN B 1 58   ? -27.957 8.471   102.889 1.00 33.72 ?  56   GLN B CD    1 
ATOM   9519  O OE1   . GLN B 1 58   ? -28.011 7.553   103.708 1.00 34.32 ?  56   GLN B OE1   1 
ATOM   9520  N NE2   . GLN B 1 58   ? -27.625 9.715   103.228 1.00 32.31 ?  56   GLN B NE2   1 
ATOM   9521  N N     . SER B 1 59   ? -32.384 6.783   100.206 1.00 37.76 ?  57   SER B N     1 
ATOM   9522  C CA    . SER B 1 59   ? -33.834 6.731   100.068 1.00 40.24 ?  57   SER B CA    1 
ATOM   9523  C C     . SER B 1 59   ? -34.481 8.024   100.563 1.00 40.01 ?  57   SER B C     1 
ATOM   9524  O O     . SER B 1 59   ? -33.900 8.788   101.337 1.00 34.76 ?  57   SER B O     1 
ATOM   9525  C CB    . SER B 1 59   ? -34.405 5.544   100.845 1.00 37.94 ?  57   SER B CB    1 
ATOM   9526  O OG    . SER B 1 59   ? -34.187 5.680   102.245 1.00 36.05 ?  57   SER B OG    1 
ATOM   9527  N N     . LYS B 1 60   ? -35.714 8.254   100.108 1.00 38.19 ?  58   LYS B N     1 
ATOM   9528  C CA    . LYS B 1 60   ? -36.447 9.452   100.510 1.00 38.25 ?  58   LYS B CA    1 
ATOM   9529  C C     . LYS B 1 60   ? -36.669 9.486   102.019 1.00 39.38 ?  58   LYS B C     1 
ATOM   9530  O O     . LYS B 1 60   ? -36.560 10.546  102.648 1.00 34.14 ?  58   LYS B O     1 
ATOM   9531  C CB    . LYS B 1 60   ? -37.781 9.517   99.760  1.00 44.75 ?  58   LYS B CB    1 
ATOM   9532  C CG    . LYS B 1 60   ? -38.729 10.617  100.223 1.00 42.46 ?  58   LYS B CG    1 
ATOM   9533  C CD    . LYS B 1 60   ? -38.306 11.988  99.722  1.00 47.16 ?  58   LYS B CD    1 
ATOM   9534  C CE    . LYS B 1 60   ? -39.297 13.057  100.172 1.00 49.29 ?  58   LYS B CE    1 
ATOM   9535  N NZ    . LYS B 1 60   ? -38.906 14.413  99.692  1.00 52.24 ?  58   LYS B NZ    1 
ATOM   9536  N N     . GLU B 1 61   ? -36.973 8.335   102.623 1.00 36.68 ?  59   GLU B N     1 
ATOM   9537  C CA    . GLU B 1 61   ? -37.209 8.312   104.064 1.00 38.89 ?  59   GLU B CA    1 
ATOM   9538  C C     . GLU B 1 61   ? -35.935 8.630   104.838 1.00 35.90 ?  59   GLU B C     1 
ATOM   9539  O O     . GLU B 1 61   ? -35.985 9.323   105.861 1.00 34.55 ?  59   GLU B O     1 
ATOM   9540  C CB    . GLU B 1 61   ? -37.784 6.961   104.499 1.00 42.58 ?  59   GLU B CB    1 
ATOM   9541  C CG    . GLU B 1 61   ? -37.613 5.834   103.491 1.00 49.70 ?  59   GLU B CG    1 
ATOM   9542  C CD    . GLU B 1 61   ? -38.633 5.894   102.366 1.00 53.13 ?  59   GLU B CD    1 
ATOM   9543  O OE1   . GLU B 1 61   ? -39.812 6.205   102.643 1.00 61.37 ?  59   GLU B OE1   1 
ATOM   9544  O OE2   . GLU B 1 61   ? -38.249 5.641   101.203 1.00 53.10 ?  59   GLU B OE2   1 
ATOM   9545  N N     . ILE B 1 62   ? -34.785 8.136   104.371 1.00 35.68 ?  60   ILE B N     1 
ATOM   9546  C CA    . ILE B 1 62   ? -33.527 8.465   105.036 1.00 34.26 ?  60   ILE B CA    1 
ATOM   9547  C C     . ILE B 1 62   ? -33.200 9.938   104.843 1.00 35.21 ?  60   ILE B C     1 
ATOM   9548  O O     . ILE B 1 62   ? -32.816 10.631  105.794 1.00 35.48 ?  60   ILE B O     1 
ATOM   9549  C CB    . ILE B 1 62   ? -32.393 7.554   104.527 1.00 36.17 ?  60   ILE B CB    1 
ATOM   9550  C CG1   . ILE B 1 62   ? -32.510 6.165   105.154 1.00 39.51 ?  60   ILE B CG1   1 
ATOM   9551  C CG2   . ILE B 1 62   ? -31.024 8.168   104.823 1.00 37.50 ?  60   ILE B CG2   1 
ATOM   9552  C CD1   . ILE B 1 62   ? -31.572 5.147   104.554 1.00 39.22 ?  60   ILE B CD1   1 
ATOM   9553  N N     . ARG B 1 63   ? -33.367 10.446  103.619 1.00 34.58 ?  61   ARG B N     1 
ATOM   9554  C CA    . ARG B 1 63   ? -33.120 11.862  103.368 1.00 35.79 ?  61   ARG B CA    1 
ATOM   9555  C C     . ARG B 1 63   ? -34.046 12.740  104.203 1.00 32.85 ?  61   ARG B C     1 
ATOM   9556  O O     . ARG B 1 63   ? -33.620 13.775  104.728 1.00 35.74 ?  61   ARG B O     1 
ATOM   9557  C CB    . ARG B 1 63   ? -33.264 12.160  101.873 1.00 34.65 ?  61   ARG B CB    1 
ATOM   9558  C CG    . ARG B 1 63   ? -32.203 11.452  101.041 1.00 35.07 ?  61   ARG B CG    1 
ATOM   9559  C CD    . ARG B 1 63   ? -32.173 11.897  99.589  1.00 37.12 ?  61   ARG B CD    1 
ATOM   9560  N NE    . ARG B 1 63   ? -33.207 11.262  98.780  1.00 36.86 ?  61   ARG B NE    1 
ATOM   9561  C CZ    . ARG B 1 63   ? -34.274 11.888  98.302  1.00 41.56 ?  61   ARG B CZ    1 
ATOM   9562  N NH1   . ARG B 1 63   ? -34.494 13.169  98.553  1.00 42.56 ?  61   ARG B NH1   1 
ATOM   9563  N NH2   . ARG B 1 63   ? -35.138 11.215  97.545  1.00 41.59 ?  61   ARG B NH2   1 
ATOM   9564  N N     . ASP B 1 64   ? -35.313 12.340  104.346 1.00 33.40 ?  62   ASP B N     1 
ATOM   9565  C CA    . ASP B 1 64   ? -36.231 13.104  105.187 1.00 31.06 ?  62   ASP B CA    1 
ATOM   9566  C C     . ASP B 1 64   ? -35.785 13.082  106.644 1.00 33.02 ?  62   ASP B C     1 
ATOM   9567  O O     . ASP B 1 64   ? -35.782 14.118  107.320 1.00 35.03 ?  62   ASP B O     1 
ATOM   9568  C CB    . ASP B 1 64   ? -37.655 12.561  105.048 1.00 34.59 ?  62   ASP B CB    1 
ATOM   9569  C CG    . ASP B 1 64   ? -38.288 12.906  103.706 1.00 39.71 ?  62   ASP B CG    1 
ATOM   9570  O OD1   . ASP B 1 64   ? -37.778 13.812  103.011 1.00 40.97 ?  62   ASP B OD1   1 
ATOM   9571  O OD2   . ASP B 1 64   ? -39.309 12.275  103.353 1.00 43.88 ?  62   ASP B OD2   1 
ATOM   9572  N N     . ALA B 1 65   ? -35.399 11.907  107.149 1.00 31.06 ?  63   ALA B N     1 
ATOM   9573  C CA    . ALA B 1 65   ? -35.009 11.814  108.554 1.00 31.42 ?  63   ALA B CA    1 
ATOM   9574  C C     . ALA B 1 65   ? -33.709 12.565  108.821 1.00 32.26 ?  63   ALA B C     1 
ATOM   9575  O O     . ALA B 1 65   ? -33.544 13.174  109.886 1.00 32.65 ?  63   ALA B O     1 
ATOM   9576  C CB    . ALA B 1 65   ? -34.880 10.349  108.973 1.00 33.75 ?  63   ALA B CB    1 
ATOM   9577  N N     . ALA B 1 66   ? -32.781 12.547  107.863 1.00 33.56 ?  64   ALA B N     1 
ATOM   9578  C CA    . ALA B 1 66   ? -31.524 13.263  108.053 1.00 32.40 ?  64   ALA B CA    1 
ATOM   9579  C C     . ALA B 1 66   ? -31.736 14.771  108.016 1.00 32.77 ?  64   ALA B C     1 
ATOM   9580  O O     . ALA B 1 66   ? -31.075 15.515  108.752 1.00 30.47 ?  64   ALA B O     1 
ATOM   9581  C CB    . ALA B 1 66   ? -30.510 12.827  107.000 1.00 26.45 ?  64   ALA B CB    1 
ATOM   9582  N N     . ALA B 1 67   ? -32.662 15.243  107.177 1.00 30.96 ?  65   ALA B N     1 
ATOM   9583  C CA    . ALA B 1 67   ? -32.976 16.666  107.171 1.00 32.06 ?  65   ALA B CA    1 
ATOM   9584  C C     . ALA B 1 67   ? -33.561 17.109  108.506 1.00 31.09 ?  65   ALA B C     1 
ATOM   9585  O O     . ALA B 1 67   ? -33.319 18.239  108.947 1.00 36.37 ?  65   ALA B O     1 
ATOM   9586  C CB    . ALA B 1 67   ? -33.939 16.989  106.030 1.00 32.95 ?  65   ALA B CB    1 
ATOM   9587  N N     . SER B 1 68   ? -34.322 16.234  109.169 1.00 33.69 ?  66   SER B N     1 
ATOM   9588  C CA    . SER B 1 68   ? -34.854 16.583  110.481 1.00 31.41 ?  66   SER B CA    1 
ATOM   9589  C C     . SER B 1 68   ? -33.766 16.545  111.546 1.00 34.64 ?  66   SER B C     1 
ATOM   9590  O O     . SER B 1 68   ? -33.764 17.373  112.465 1.00 31.75 ?  66   SER B O     1 
ATOM   9591  C CB    . SER B 1 68   ? -35.999 15.644  110.859 1.00 40.69 ?  66   SER B CB    1 
ATOM   9592  O OG    . SER B 1 68   ? -37.168 15.945  110.115 1.00 44.16 ?  66   SER B OG    1 
ATOM   9593  N N     . THR B 1 69   ? -32.853 15.572  111.461 1.00 32.42 ?  67   THR B N     1 
ATOM   9594  C CA    . THR B 1 69   ? -31.738 15.534  112.403 1.00 31.95 ?  67   THR B CA    1 
ATOM   9595  C C     . THR B 1 69   ? -30.850 16.754  112.227 1.00 28.54 ?  67   THR B C     1 
ATOM   9596  O O     . THR B 1 69   ? -30.412 17.360  113.212 1.00 29.00 ?  67   THR B O     1 
ATOM   9597  C CB    . THR B 1 69   ? -30.923 14.250  112.220 1.00 32.89 ?  67   THR B CB    1 
ATOM   9598  O OG1   . THR B 1 69   ? -31.709 13.117  112.611 1.00 29.48 ?  67   THR B OG1   1 
ATOM   9599  C CG2   . THR B 1 69   ? -29.651 14.286  113.069 1.00 30.81 ?  67   THR B CG2   1 
ATOM   9600  N N     . ALA B 1 70   ? -30.581 17.133  110.974 1.00 29.21 ?  68   ALA B N     1 
ATOM   9601  C CA    . ALA B 1 70   ? -29.749 18.301  110.710 1.00 31.68 ?  68   ALA B CA    1 
ATOM   9602  C C     . ALA B 1 70   ? -30.414 19.576  111.207 1.00 33.76 ?  68   ALA B C     1 
ATOM   9603  O O     . ALA B 1 70   ? -29.749 20.443  111.785 1.00 32.51 ?  68   ALA B O     1 
ATOM   9604  C CB    . ALA B 1 70   ? -29.442 18.404  109.215 1.00 32.15 ?  68   ALA B CB    1 
ATOM   9605  N N     . ARG B 1 71   ? -31.728 19.711  110.991 1.00 33.51 ?  69   ARG B N     1 
ATOM   9606  C CA    . ARG B 1 71   ? -32.431 20.902  111.459 1.00 31.62 ?  69   ARG B CA    1 
ATOM   9607  C C     . ARG B 1 71   ? -32.345 21.027  112.974 1.00 32.61 ?  69   ARG B C     1 
ATOM   9608  O O     . ARG B 1 71   ? -32.098 22.117  113.500 1.00 30.93 ?  69   ARG B O     1 
ATOM   9609  C CB    . ARG B 1 71   ? -33.893 20.874  111.002 1.00 35.89 ?  69   ARG B CB    1 
ATOM   9610  C CG    . ARG B 1 71   ? -34.738 21.983  111.612 1.00 40.57 ?  69   ARG B CG    1 
ATOM   9611  C CD    . ARG B 1 71   ? -36.183 21.966  111.124 1.00 45.76 ?  69   ARG B CD    1 
ATOM   9612  N NE    . ARG B 1 71   ? -36.314 22.427  109.747 1.00 43.25 ?  69   ARG B NE    1 
ATOM   9613  C CZ    . ARG B 1 71   ? -36.253 23.698  109.371 1.00 47.96 ?  69   ARG B CZ    1 
ATOM   9614  N NH1   . ARG B 1 71   ? -36.021 24.668  110.242 1.00 45.06 ?  69   ARG B NH1   1 
ATOM   9615  N NH2   . ARG B 1 71   ? -36.427 24.004  108.088 1.00 49.26 ?  69   ARG B NH2   1 
ATOM   9616  N N     . LYS B 1 72   ? -32.529 19.914  113.689 1.00 29.79 ?  70   LYS B N     1 
ATOM   9617  C CA    . LYS B 1 72   ? -32.412 19.935  115.143 1.00 31.02 ?  70   LYS B CA    1 
ATOM   9618  C C     . LYS B 1 72   ? -31.007 20.337  115.577 1.00 32.26 ?  70   LYS B C     1 
ATOM   9619  O O     . LYS B 1 72   ? -30.839 21.110  116.528 1.00 33.18 ?  70   LYS B O     1 
ATOM   9620  C CB    . LYS B 1 72   ? -32.787 18.566  115.713 1.00 31.36 ?  70   LYS B CB    1 
ATOM   9621  C CG    . LYS B 1 72   ? -32.727 18.461  117.239 1.00 35.53 ?  70   LYS B CG    1 
ATOM   9622  C CD    . LYS B 1 72   ? -33.296 17.119  117.702 1.00 34.01 ?  70   LYS B CD    1 
ATOM   9623  C CE    . LYS B 1 72   ? -33.126 16.919  119.198 1.00 38.30 ?  70   LYS B CE    1 
ATOM   9624  N NZ    . LYS B 1 72   ? -33.914 17.889  120.018 1.00 32.22 ?  70   LYS B NZ    1 
ATOM   9625  N N     . LEU B 1 73   ? -29.981 19.828  114.890 1.00 31.43 ?  71   LEU B N     1 
ATOM   9626  C CA    . LEU B 1 73   ? -28.616 20.221  115.232 1.00 31.99 ?  71   LEU B CA    1 
ATOM   9627  C C     . LEU B 1 73   ? -28.395 21.709  114.995 1.00 32.28 ?  71   LEU B C     1 
ATOM   9628  O O     . LEU B 1 73   ? -27.772 22.391  115.818 1.00 28.26 ?  71   LEU B O     1 
ATOM   9629  C CB    . LEU B 1 73   ? -27.610 19.408  114.418 1.00 28.07 ?  71   LEU B CB    1 
ATOM   9630  C CG    . LEU B 1 73   ? -27.630 17.901  114.655 1.00 26.81 ?  71   LEU B CG    1 
ATOM   9631  C CD1   . LEU B 1 73   ? -26.717 17.242  113.617 1.00 25.69 ?  71   LEU B CD1   1 
ATOM   9632  C CD2   . LEU B 1 73   ? -27.194 17.566  116.075 1.00 32.74 ?  71   LEU B CD2   1 
ATOM   9633  N N     . ILE B 1 74   ? -28.898 22.227  113.873 1.00 30.89 ?  72   ILE B N     1 
ATOM   9634  C CA    . ILE B 1 74   ? -28.641 23.616  113.508 1.00 30.72 ?  72   ILE B CA    1 
ATOM   9635  C C     . ILE B 1 74   ? -29.399 24.560  114.429 1.00 33.31 ?  72   ILE B C     1 
ATOM   9636  O O     . ILE B 1 74   ? -28.869 25.597  114.851 1.00 33.52 ?  72   ILE B O     1 
ATOM   9637  C CB    . ILE B 1 74   ? -28.995 23.842  112.029 1.00 31.85 ?  72   ILE B CB    1 
ATOM   9638  C CG1   . ILE B 1 74   ? -27.988 23.096  111.153 1.00 31.87 ?  72   ILE B CG1   1 
ATOM   9639  C CG2   . ILE B 1 74   ? -28.996 25.324  111.699 1.00 31.78 ?  72   ILE B CG2   1 
ATOM   9640  C CD1   . ILE B 1 74   ? -28.397 22.968  109.720 1.00 29.63 ?  72   ILE B CD1   1 
ATOM   9641  N N     . GLU B 1 75   ? -30.645 24.215  114.761 1.00 34.28 ?  73   GLU B N     1 
ATOM   9642  C CA    . GLU B 1 75   ? -31.396 24.996  115.738 1.00 31.24 ?  73   GLU B CA    1 
ATOM   9643  C C     . GLU B 1 75   ? -30.668 25.037  117.076 1.00 32.75 ?  73   GLU B C     1 
ATOM   9644  O O     . GLU B 1 75   ? -30.567 26.097  117.705 1.00 38.50 ?  73   GLU B O     1 
ATOM   9645  C CB    . GLU B 1 75   ? -32.802 24.415  115.894 1.00 32.33 ?  73   GLU B CB    1 
ATOM   9646  N N     . ALA B 1 76   ? -30.130 23.897  117.515 1.00 32.52 ?  74   ALA B N     1 
ATOM   9647  C CA    . ALA B 1 76   ? -29.380 23.866  118.765 1.00 29.71 ?  74   ALA B CA    1 
ATOM   9648  C C     . ALA B 1 76   ? -28.127 24.736  118.685 1.00 36.41 ?  74   ALA B C     1 
ATOM   9649  O O     . ALA B 1 76   ? -27.785 25.431  119.648 1.00 37.15 ?  74   ALA B O     1 
ATOM   9650  C CB    . ALA B 1 76   ? -29.024 22.424  119.128 1.00 32.24 ?  74   ALA B CB    1 
ATOM   9651  N N     . LEU B 1 77   ? -27.431 24.712  117.544 1.00 31.17 ?  75   LEU B N     1 
ATOM   9652  C CA    . LEU B 1 77   ? -26.225 25.524  117.386 1.00 32.11 ?  75   LEU B CA    1 
ATOM   9653  C C     . LEU B 1 77   ? -26.550 27.013  117.421 1.00 33.93 ?  75   LEU B C     1 
ATOM   9654  O O     . LEU B 1 77   ? -25.882 27.790  118.115 1.00 36.28 ?  75   LEU B O     1 
ATOM   9655  C CB    . LEU B 1 77   ? -25.510 25.170  116.073 1.00 28.34 ?  75   LEU B CB    1 
ATOM   9656  C CG    . LEU B 1 77   ? -24.617 23.922  116.030 1.00 32.81 ?  75   LEU B CG    1 
ATOM   9657  C CD1   . LEU B 1 77   ? -24.217 23.561  114.609 1.00 30.67 ?  75   LEU B CD1   1 
ATOM   9658  C CD2   . LEU B 1 77   ? -23.371 24.120  116.874 1.00 34.07 ?  75   LEU B CD2   1 
ATOM   9659  N N     . ARG B 1 78   ? -27.560 27.436  116.660 1.00 31.35 ?  76   ARG B N     1 
ATOM   9660  C CA    . ARG B 1 78   ? -27.910 28.850  116.613 1.00 31.72 ?  76   ARG B CA    1 
ATOM   9661  C C     . ARG B 1 78   ? -28.623 29.317  117.873 1.00 37.42 ?  76   ARG B C     1 
ATOM   9662  O O     . ARG B 1 78   ? -28.628 30.520  118.158 1.00 34.90 ?  76   ARG B O     1 
ATOM   9663  C CB    . ARG B 1 78   ? -28.780 29.133  115.393 1.00 32.84 ?  76   ARG B CB    1 
ATOM   9664  C CG    . ARG B 1 78   ? -28.062 28.857  114.097 1.00 31.55 ?  76   ARG B CG    1 
ATOM   9665  C CD    . ARG B 1 78   ? -28.910 29.230  112.899 1.00 31.36 ?  76   ARG B CD    1 
ATOM   9666  N NE    . ARG B 1 78   ? -28.089 29.761  111.815 1.00 30.75 ?  76   ARG B NE    1 
ATOM   9667  C CZ    . ARG B 1 78   ? -28.567 30.178  110.651 1.00 31.74 ?  76   ARG B CZ    1 
ATOM   9668  N NH1   . ARG B 1 78   ? -29.857 30.093  110.362 1.00 36.36 ?  76   ARG B NH1   1 
ATOM   9669  N NH2   . ARG B 1 78   ? -27.730 30.695  109.756 1.00 38.36 ?  76   ARG B NH2   1 
ATOM   9670  N N     . GLY B 1 79   ? -29.224 28.400  118.623 1.00 35.19 ?  77   GLY B N     1 
ATOM   9671  C CA    . GLY B 1 79   ? -29.951 28.773  119.821 1.00 37.12 ?  77   GLY B CA    1 
ATOM   9672  C C     . GLY B 1 79   ? -29.052 29.071  121.002 1.00 45.91 ?  77   GLY B C     1 
ATOM   9673  O O     . GLY B 1 79   ? -29.325 29.986  121.787 1.00 43.47 ?  77   GLY B O     1 
ATOM   9674  N N     . LYS B 1 80   ? -27.982 28.294  121.150 1.00 41.81 ?  78   LYS B N     1 
ATOM   9675  C CA    . LYS B 1 80   ? -27.039 28.491  122.241 1.00 46.68 ?  78   LYS B CA    1 
ATOM   9676  C C     . LYS B 1 80   ? -25.868 29.370  121.834 1.00 47.02 ?  78   LYS B C     1 
ATOM   9677  O O     . LYS B 1 80   ? -24.928 29.538  122.617 1.00 49.96 ?  78   LYS B O     1 
ATOM   9678  C CB    . LYS B 1 80   ? -26.535 27.140  122.761 1.00 44.62 ?  78   LYS B CB    1 
ATOM   9679  C CG    . LYS B 1 80   ? -25.679 26.360  121.779 1.00 40.41 ?  78   LYS B CG    1 
ATOM   9680  C CD    . LYS B 1 80   ? -25.538 24.911  122.222 1.00 43.33 ?  78   LYS B CD    1 
ATOM   9681  C CE    . LYS B 1 80   ? -24.698 24.113  121.239 1.00 32.35 ?  78   LYS B CE    1 
ATOM   9682  N NZ    . LYS B 1 80   ? -24.553 22.696  121.661 1.00 31.41 ?  78   LYS B NZ    1 
ATOM   9683  N N     . HIS B 1 81   ? -25.909 29.933  120.631 1.00 47.16 ?  79   HIS B N     1 
ATOM   9684  C CA    . HIS B 1 81   ? -24.863 30.844  120.199 1.00 52.11 ?  79   HIS B CA    1 
ATOM   9685  C C     . HIS B 1 81   ? -24.919 32.133  121.008 1.00 56.87 ?  79   HIS B C     1 
ATOM   9686  O O     . HIS B 1 81   ? -25.995 32.701  121.226 1.00 54.51 ?  79   HIS B O     1 
ATOM   9687  C CB    . HIS B 1 81   ? -25.003 31.153  118.709 1.00 53.35 ?  79   HIS B CB    1 
ATOM   9688  C CG    . HIS B 1 81   ? -24.083 32.234  118.235 1.00 60.29 ?  79   HIS B CG    1 
ATOM   9689  N ND1   . HIS B 1 81   ? -22.814 31.977  117.761 1.00 62.33 ?  79   HIS B ND1   1 
ATOM   9690  C CD2   . HIS B 1 81   ? -24.239 33.579  118.182 1.00 62.03 ?  79   HIS B CD2   1 
ATOM   9691  C CE1   . HIS B 1 81   ? -22.233 33.116  117.425 1.00 63.34 ?  79   HIS B CE1   1 
ATOM   9692  N NE2   . HIS B 1 81   ? -23.075 34.103  117.674 1.00 64.07 ?  79   HIS B NE2   1 
ATOM   9693  N N     . SER B 1 82   ? -23.754 32.589  121.461 1.00 59.59 ?  80   SER B N     1 
ATOM   9694  C CA    . SER B 1 82   ? -23.599 33.901  122.068 1.00 59.65 ?  80   SER B CA    1 
ATOM   9695  C C     . SER B 1 82   ? -22.308 34.512  121.538 1.00 61.10 ?  80   SER B C     1 
ATOM   9696  O O     . SER B 1 82   ? -21.562 33.880  120.781 1.00 61.62 ?  80   SER B O     1 
ATOM   9697  C CB    . SER B 1 82   ? -23.613 33.811  123.598 1.00 54.90 ?  80   SER B CB    1 
ATOM   9698  O OG    . SER B 1 82   ? -22.796 32.747  124.052 1.00 57.63 ?  80   SER B OG    1 
ATOM   9699  N N     . GLY B 1 83   ? -22.043 35.753  121.934 1.00 60.04 ?  81   GLY B N     1 
ATOM   9700  C CA    . GLY B 1 83   ? -20.883 36.455  121.410 1.00 57.49 ?  81   GLY B CA    1 
ATOM   9701  C C     . GLY B 1 83   ? -19.581 35.847  121.904 1.00 56.85 ?  81   GLY B C     1 
ATOM   9702  O O     . GLY B 1 83   ? -19.457 35.434  123.059 1.00 54.23 ?  81   GLY B O     1 
ATOM   9703  N N     . SER B 1 84   ? -18.598 35.792  121.008 1.00 55.02 ?  82   SER B N     1 
ATOM   9704  C CA    . SER B 1 84   ? -17.277 35.308  121.377 1.00 49.94 ?  82   SER B CA    1 
ATOM   9705  C C     . SER B 1 84   ? -16.574 36.322  122.279 1.00 45.48 ?  82   SER B C     1 
ATOM   9706  O O     . SER B 1 84   ? -17.056 37.435  122.515 1.00 39.50 ?  82   SER B O     1 
ATOM   9707  C CB    . SER B 1 84   ? -16.434 35.035  120.133 1.00 46.88 ?  82   SER B CB    1 
ATOM   9708  O OG    . SER B 1 84   ? -16.147 36.238  119.445 1.00 43.01 ?  82   SER B OG    1 
ATOM   9709  N N     . GLY B 1 85   ? -15.416 35.916  122.798 1.00 44.44 ?  83   GLY B N     1 
ATOM   9710  C CA    . GLY B 1 85   ? -14.666 36.806  123.666 1.00 37.43 ?  83   GLY B CA    1 
ATOM   9711  C C     . GLY B 1 85   ? -14.211 38.064  122.951 1.00 37.94 ?  83   GLY B C     1 
ATOM   9712  O O     . GLY B 1 85   ? -14.314 39.168  123.493 1.00 34.96 ?  83   GLY B O     1 
ATOM   9713  N N     . VAL B 1 86   ? -13.710 37.914  121.722 1.00 37.45 ?  84   VAL B N     1 
ATOM   9714  C CA    . VAL B 1 86   ? -13.197 39.063  120.979 1.00 35.04 ?  84   VAL B CA    1 
ATOM   9715  C C     . VAL B 1 86   ? -14.322 40.039  120.651 1.00 35.00 ?  84   VAL B C     1 
ATOM   9716  O O     . VAL B 1 86   ? -14.140 41.260  120.724 1.00 30.54 ?  84   VAL B O     1 
ATOM   9717  C CB    . VAL B 1 86   ? -12.455 38.590  119.716 1.00 35.32 ?  84   VAL B CB    1 
ATOM   9718  C CG1   . VAL B 1 86   ? -12.214 39.748  118.770 1.00 35.12 ?  84   VAL B CG1   1 
ATOM   9719  C CG2   . VAL B 1 86   ? -11.133 37.976  120.105 1.00 39.25 ?  84   VAL B CG2   1 
ATOM   9720  N N     . GLU B 1 87   ? -15.508 39.521  120.321 1.00 37.20 ?  85   GLU B N     1 
ATOM   9721  C CA    . GLU B 1 87   ? -16.647 40.388  120.027 1.00 36.63 ?  85   GLU B CA    1 
ATOM   9722  C C     . GLU B 1 87   ? -17.027 41.244  121.231 1.00 36.18 ?  85   GLU B C     1 
ATOM   9723  O O     . GLU B 1 87   ? -17.240 42.456  121.102 1.00 33.38 ?  85   GLU B O     1 
ATOM   9724  C CB    . GLU B 1 87   ? -17.838 39.545  119.572 1.00 41.63 ?  85   GLU B CB    1 
ATOM   9725  C CG    . GLU B 1 87   ? -17.592 38.802  118.276 1.00 40.68 ?  85   GLU B CG    1 
ATOM   9726  C CD    . GLU B 1 87   ? -18.819 38.055  117.787 1.00 56.30 ?  85   GLU B CD    1 
ATOM   9727  O OE1   . GLU B 1 87   ? -19.619 37.601  118.636 1.00 55.32 ?  85   GLU B OE1   1 
ATOM   9728  O OE2   . GLU B 1 87   ? -18.985 37.933  116.552 1.00 53.82 ?  85   GLU B OE2   1 
ATOM   9729  N N     . GLY B 1 88   ? -17.136 40.629  122.415 1.00 32.76 ?  86   GLY B N     1 
ATOM   9730  C CA    . GLY B 1 88   ? -17.455 41.398  123.606 1.00 34.59 ?  86   GLY B CA    1 
ATOM   9731  C C     . GLY B 1 88   ? -16.383 42.407  123.964 1.00 30.23 ?  86   GLY B C     1 
ATOM   9732  O O     . GLY B 1 88   ? -16.680 43.465  124.523 1.00 33.04 ?  86   GLY B O     1 
ATOM   9733  N N     . LEU B 1 89   ? -15.126 42.097  123.648 1.00 30.57 ?  87   LEU B N     1 
ATOM   9734  C CA    . LEU B 1 89   ? -14.043 43.047  123.878 1.00 32.55 ?  87   LEU B CA    1 
ATOM   9735  C C     . LEU B 1 89   ? -14.166 44.243  122.942 1.00 29.20 ?  87   LEU B C     1 
ATOM   9736  O O     . LEU B 1 89   ? -14.059 45.399  123.372 1.00 27.03 ?  87   LEU B O     1 
ATOM   9737  C CB    . LEU B 1 89   ? -12.700 42.343  123.691 1.00 33.11 ?  87   LEU B CB    1 
ATOM   9738  C CG    . LEU B 1 89   ? -11.437 43.195  123.767 1.00 35.72 ?  87   LEU B CG    1 
ATOM   9739  C CD1   . LEU B 1 89   ? -11.293 43.775  125.146 1.00 35.98 ?  87   LEU B CD1   1 
ATOM   9740  C CD2   . LEU B 1 89   ? -10.223 42.349  123.407 1.00 36.34 ?  87   LEU B CD2   1 
ATOM   9741  N N     . VAL B 1 90   ? -14.411 43.974  121.659 1.00 28.82 ?  88   VAL B N     1 
ATOM   9742  C CA    . VAL B 1 90   ? -14.617 45.039  120.680 1.00 28.97 ?  88   VAL B CA    1 
ATOM   9743  C C     . VAL B 1 90   ? -15.816 45.899  121.067 1.00 32.32 ?  88   VAL B C     1 
ATOM   9744  O O     . VAL B 1 90   ? -15.770 47.132  120.978 1.00 29.54 ?  88   VAL B O     1 
ATOM   9745  C CB    . VAL B 1 90   ? -14.775 44.426  119.275 1.00 27.09 ?  88   VAL B CB    1 
ATOM   9746  C CG1   . VAL B 1 90   ? -15.283 45.462  118.286 1.00 29.28 ?  88   VAL B CG1   1 
ATOM   9747  C CG2   . VAL B 1 90   ? -13.453 43.840  118.809 1.00 25.95 ?  88   VAL B CG2   1 
ATOM   9748  N N     . GLN B 1 91   ? -16.899 45.269  121.530 1.00 30.08 ?  89   GLN B N     1 
ATOM   9749  C CA    . GLN B 1 91   ? -18.082 46.041  121.900 1.00 33.39 ?  89   GLN B CA    1 
ATOM   9750  C C     . GLN B 1 91   ? -17.850 46.852  123.173 1.00 31.81 ?  89   GLN B C     1 
ATOM   9751  O O     . GLN B 1 91   ? -18.250 48.020  123.252 1.00 32.14 ?  89   GLN B O     1 
ATOM   9752  C CB    . GLN B 1 91   ? -19.287 45.110  122.053 1.00 34.92 ?  89   GLN B CB    1 
ATOM   9753  N N     . GLU B 1 92   ? -17.196 46.262  124.180 1.00 30.54 ?  90   GLU B N     1 
ATOM   9754  C CA    . GLU B 1 92   ? -17.039 46.958  125.454 1.00 31.64 ?  90   GLU B CA    1 
ATOM   9755  C C     . GLU B 1 92   ? -16.212 48.228  125.297 1.00 33.12 ?  90   GLU B C     1 
ATOM   9756  O O     . GLU B 1 92   ? -16.498 49.246  125.937 1.00 31.67 ?  90   GLU B O     1 
ATOM   9757  C CB    . GLU B 1 92   ? -16.405 46.036  126.503 1.00 30.32 ?  90   GLU B CB    1 
ATOM   9758  C CG    . GLU B 1 92   ? -16.264 46.682  127.879 1.00 36.76 ?  90   GLU B CG    1 
ATOM   9759  C CD    . GLU B 1 92   ? -15.587 45.787  128.915 1.00 35.12 ?  90   GLU B CD    1 
ATOM   9760  O OE1   . GLU B 1 92   ? -15.313 44.605  128.613 1.00 41.50 ?  90   GLU B OE1   1 
ATOM   9761  O OE2   . GLU B 1 92   ? -15.325 46.280  130.031 1.00 37.46 ?  90   GLU B OE2   1 
ATOM   9762  N N     . TYR B 1 93   ? -15.188 48.201  124.448 1.00 28.10 ?  91   TYR B N     1 
ATOM   9763  C CA    . TYR B 1 93   ? -14.323 49.364  124.306 1.00 31.06 ?  91   TYR B CA    1 
ATOM   9764  C C     . TYR B 1 93   ? -14.547 50.105  122.994 1.00 27.86 ?  91   TYR B C     1 
ATOM   9765  O O     . TYR B 1 93   ? -13.769 51.009  122.670 1.00 27.96 ?  91   TYR B O     1 
ATOM   9766  C CB    . TYR B 1 93   ? -12.857 48.949  124.464 1.00 28.04 ?  91   TYR B CB    1 
ATOM   9767  C CG    . TYR B 1 93   ? -12.537 48.571  125.893 1.00 27.97 ?  91   TYR B CG    1 
ATOM   9768  C CD1   . TYR B 1 93   ? -12.154 49.535  126.819 1.00 26.01 ?  91   TYR B CD1   1 
ATOM   9769  C CD2   . TYR B 1 93   ? -12.646 47.257  126.321 1.00 29.69 ?  91   TYR B CD2   1 
ATOM   9770  C CE1   . TYR B 1 93   ? -11.879 49.199  128.132 1.00 29.39 ?  91   TYR B CE1   1 
ATOM   9771  C CE2   . TYR B 1 93   ? -12.377 46.911  127.634 1.00 31.92 ?  91   TYR B CE2   1 
ATOM   9772  C CZ    . TYR B 1 93   ? -11.988 47.885  128.531 1.00 28.22 ?  91   TYR B CZ    1 
ATOM   9773  O OH    . TYR B 1 93   ? -11.720 47.540  129.837 1.00 29.77 ?  91   TYR B OH    1 
ATOM   9774  N N     . SER B 1 94   ? -15.600 49.752  122.248 1.00 24.73 ?  92   SER B N     1 
ATOM   9775  C CA    . SER B 1 94   ? -15.972 50.433  121.010 1.00 28.30 ?  92   SER B CA    1 
ATOM   9776  C C     . SER B 1 94   ? -14.803 50.454  120.031 1.00 25.48 ?  92   SER B C     1 
ATOM   9777  O O     . SER B 1 94   ? -14.486 51.477  119.426 1.00 26.31 ?  92   SER B O     1 
ATOM   9778  C CB    . SER B 1 94   ? -16.483 51.847  121.288 1.00 26.02 ?  92   SER B CB    1 
ATOM   9779  O OG    . SER B 1 94   ? -17.630 51.790  122.121 1.00 30.57 ?  92   SER B OG    1 
ATOM   9780  N N     . LEU B 1 95   ? -14.142 49.315  119.891 1.00 20.92 ?  93   LEU B N     1 
ATOM   9781  C CA    . LEU B 1 95   ? -12.986 49.236  119.016 1.00 21.25 ?  93   LEU B CA    1 
ATOM   9782  C C     . LEU B 1 95   ? -13.410 49.133  117.562 1.00 22.44 ?  93   LEU B C     1 
ATOM   9783  O O     . LEU B 1 95   ? -14.376 48.443  117.229 1.00 24.90 ?  93   LEU B O     1 
ATOM   9784  C CB    . LEU B 1 95   ? -12.132 48.023  119.369 1.00 23.99 ?  93   LEU B CB    1 
ATOM   9785  C CG    . LEU B 1 95   ? -11.639 47.931  120.807 1.00 20.87 ?  93   LEU B CG    1 
ATOM   9786  C CD1   . LEU B 1 95   ? -10.745 46.713  120.963 1.00 22.37 ?  93   LEU B CD1   1 
ATOM   9787  C CD2   . LEU B 1 95   ? -10.926 49.206  121.239 1.00 22.28 ?  93   LEU B CD2   1 
ATOM   9788  N N     . SER B 1 96   ? -12.649 49.787  116.686 1.00 19.46 ?  94   SER B N     1 
ATOM   9789  C CA    . SER B 1 96   ? -12.744 49.491  115.273 1.00 20.91 ?  94   SER B CA    1 
ATOM   9790  C C     . SER B 1 96   ? -12.069 48.150  114.992 1.00 19.15 ?  94   SER B C     1 
ATOM   9791  O O     . SER B 1 96   ? -11.383 47.580  115.850 1.00 19.39 ?  94   SER B O     1 
ATOM   9792  C CB    . SER B 1 96   ? -12.058 50.581  114.464 1.00 22.22 ?  94   SER B CB    1 
ATOM   9793  O OG    . SER B 1 96   ? -10.674 50.549  114.763 1.00 19.86 ?  94   SER B OG    1 
ATOM   9794  N N     . SER B 1 97   ? -12.243 47.647  113.769 1.00 18.55 ?  95   SER B N     1 
ATOM   9795  C CA    . SER B 1 97   ? -11.593 46.392  113.402 1.00 17.00 ?  95   SER B CA    1 
ATOM   9796  C C     . SER B 1 97   ? -10.079 46.510  113.521 1.00 18.29 ?  95   SER B C     1 
ATOM   9797  O O     . SER B 1 97   ? -9.421  45.643  114.108 1.00 17.40 ?  95   SER B O     1 
ATOM   9798  C CB    . SER B 1 97   ? -11.985 45.983  111.979 1.00 25.51 ?  95   SER B CB    1 
ATOM   9799  O OG    . SER B 1 97   ? -13.335 45.569  111.950 1.00 30.95 ?  95   SER B OG    1 
ATOM   9800  N N     . GLN B 1 98   ? -9.507  47.587  112.975 1.00 18.74 ?  96   GLN B N     1 
ATOM   9801  C CA    . GLN B 1 98   ? -8.058  47.756  113.053 1.00 16.46 ?  96   GLN B CA    1 
ATOM   9802  C C     . GLN B 1 98   ? -7.598  47.901  114.500 1.00 16.03 ?  96   GLN B C     1 
ATOM   9803  O O     . GLN B 1 98   ? -6.518  47.416  114.852 1.00 15.43 ?  96   GLN B O     1 
ATOM   9804  C CB    . GLN B 1 98   ? -7.603  48.964  112.226 1.00 15.15 ?  96   GLN B CB    1 
ATOM   9805  C CG    . GLN B 1 98   ? -7.638  48.745  110.724 1.00 16.96 ?  96   GLN B CG    1 
ATOM   9806  C CD    . GLN B 1 98   ? -6.682  47.678  110.280 1.00 17.53 ?  96   GLN B CD    1 
ATOM   9807  O OE1   . GLN B 1 98   ? -6.978  46.483  110.357 1.00 19.66 ?  96   GLN B OE1   1 
ATOM   9808  N NE2   . GLN B 1 98   ? -5.522  48.098  109.787 1.00 18.19 ?  96   GLN B NE2   1 
ATOM   9809  N N     . GLU B 1 99   ? -8.400  48.554  115.357 1.00 14.73 ?  97   GLU B N     1 
ATOM   9810  C CA    . GLU B 1 99   ? -8.048  48.639  116.773 1.00 15.76 ?  97   GLU B CA    1 
ATOM   9811  C C     . GLU B 1 99   ? -8.084  47.262  117.417 1.00 19.66 ?  97   GLU B C     1 
ATOM   9812  O O     . GLU B 1 99   ? -7.193  46.914  118.199 1.00 18.30 ?  97   GLU B O     1 
ATOM   9813  C CB    . GLU B 1 99   ? -8.989  49.605  117.501 1.00 17.71 ?  97   GLU B CB    1 
ATOM   9814  C CG    . GLU B 1 99   ? -8.660  51.072  117.203 1.00 18.75 ?  97   GLU B CG    1 
ATOM   9815  C CD    . GLU B 1 99   ? -9.727  52.039  117.652 1.00 19.55 ?  97   GLU B CD    1 
ATOM   9816  O OE1   . GLU B 1 99   ? -10.745 51.595  118.235 1.00 21.45 ?  97   GLU B OE1   1 
ATOM   9817  O OE2   . GLU B 1 99   ? -9.536  53.262  117.477 1.00 20.54 ?  97   GLU B OE2   1 
ATOM   9818  N N     . GLY B 1 100  ? -9.099  46.459  117.091 1.00 16.76 ?  98   GLY B N     1 
ATOM   9819  C CA    . GLY B 1 100  ? -9.130  45.096  117.602 1.00 18.52 ?  98   GLY B CA    1 
ATOM   9820  C C     . GLY B 1 100  ? -7.915  44.289  117.174 1.00 16.80 ?  98   GLY B C     1 
ATOM   9821  O O     . GLY B 1 100  ? -7.293  43.603  117.998 1.00 16.71 ?  98   GLY B O     1 
ATOM   9822  N N     . VAL B 1 101  ? -7.542  44.380  115.893 1.00 15.15 ?  99   VAL B N     1 
ATOM   9823  C CA    . VAL B 1 101  ? -6.378  43.640  115.405 1.00 16.54 ?  99   VAL B CA    1 
ATOM   9824  C C     . VAL B 1 101  ? -5.110  44.131  116.093 1.00 17.20 ?  99   VAL B C     1 
ATOM   9825  O O     . VAL B 1 101  ? -4.296  43.334  116.576 1.00 16.56 ?  99   VAL B O     1 
ATOM   9826  C CB    . VAL B 1 101  ? -6.271  43.743  113.872 1.00 16.55 ?  99   VAL B CB    1 
ATOM   9827  C CG1   . VAL B 1 101  ? -4.976  43.121  113.403 1.00 16.32 ?  99   VAL B CG1   1 
ATOM   9828  C CG2   . VAL B 1 101  ? -7.457  43.051  113.234 1.00 16.66 ?  99   VAL B CG2   1 
ATOM   9829  N N     . ALA B 1 102  ? -4.940  45.452  116.172 1.00 14.37 ?  100  ALA B N     1 
ATOM   9830  C CA    . ALA B 1 102  ? -3.755  46.024  116.807 1.00 17.06 ?  100  ALA B CA    1 
ATOM   9831  C C     . ALA B 1 102  ? -3.641  45.598  118.263 1.00 17.71 ?  100  ALA B C     1 
ATOM   9832  O O     . ALA B 1 102  ? -2.541  45.301  118.744 1.00 15.95 ?  100  ALA B O     1 
ATOM   9833  C CB    . ALA B 1 102  ? -3.785  47.552  116.712 1.00 15.59 ?  100  ALA B CB    1 
ATOM   9834  N N     . LEU B 1 103  ? -4.766  45.585  118.981 1.00 14.40 ?  101  LEU B N     1 
ATOM   9835  C CA    . LEU B 1 103  ? -4.763  45.209  120.394 1.00 14.85 ?  101  LEU B CA    1 
ATOM   9836  C C     . LEU B 1 103  ? -4.326  43.765  120.574 1.00 18.13 ?  101  LEU B C     1 
ATOM   9837  O O     . LEU B 1 103  ? -3.583  43.445  121.512 1.00 19.43 ?  101  LEU B O     1 
ATOM   9838  C CB    . LEU B 1 103  ? -6.153  45.429  120.986 1.00 16.99 ?  101  LEU B CB    1 
ATOM   9839  C CG    . LEU B 1 103  ? -6.345  44.939  122.409 1.00 17.24 ?  101  LEU B CG    1 
ATOM   9840  C CD1   . LEU B 1 103  ? -5.453  45.764  123.311 1.00 20.27 ?  101  LEU B CD1   1 
ATOM   9841  C CD2   . LEU B 1 103  ? -7.808  45.070  122.802 1.00 18.43 ?  101  LEU B CD2   1 
ATOM   9842  N N     . MET B 1 104  ? -4.803  42.878  119.710 1.00 16.21 ?  102  MET B N     1 
ATOM   9843  C CA    . MET B 1 104  ? -4.410  41.478  119.822 1.00 17.81 ?  102  MET B CA    1 
ATOM   9844  C C     . MET B 1 104  ? -2.945  41.281  119.468 1.00 18.48 ?  102  MET B C     1 
ATOM   9845  O O     . MET B 1 104  ? -2.274  40.449  120.087 1.00 18.09 ?  102  MET B O     1 
ATOM   9846  C CB    . MET B 1 104  ? -5.324  40.609  118.957 1.00 19.04 ?  102  MET B CB    1 
ATOM   9847  C CG    . MET B 1 104  ? -6.803  40.703  119.391 1.00 20.27 ?  102  MET B CG    1 
ATOM   9848  S SD    . MET B 1 104  ? -7.098  40.192  121.118 1.00 27.35 ?  102  MET B SD    1 
ATOM   9849  C CE    . MET B 1 104  ? -6.776  38.437  120.993 1.00 28.74 ?  102  MET B CE    1 
ATOM   9850  N N     . CYS B 1 105  ? -2.421  42.056  118.514 1.00 15.95 ?  103  CYS B N     1 
ATOM   9851  C CA    . CYS B 1 105  ? -0.985  42.019  118.237 1.00 15.19 ?  103  CYS B CA    1 
ATOM   9852  C C     . CYS B 1 105  ? -0.187  42.464  119.455 1.00 18.18 ?  103  CYS B C     1 
ATOM   9853  O O     . CYS B 1 105  ? 0.823   41.844  119.810 1.00 18.58 ?  103  CYS B O     1 
ATOM   9854  C CB    . CYS B 1 105  ? -0.648  42.900  117.036 1.00 18.33 ?  103  CYS B CB    1 
ATOM   9855  S SG    . CYS B 1 105  ? -1.267  42.282  115.481 1.00 17.42 ?  103  CYS B SG    1 
ATOM   9856  N N     . LEU B 1 106  ? -0.612  43.558  120.098 1.00 16.69 ?  104  LEU B N     1 
ATOM   9857  C CA    . LEU B 1 106  ? 0.042   44.006  121.323 1.00 16.87 ?  104  LEU B CA    1 
ATOM   9858  C C     . LEU B 1 106  ? -0.027  42.926  122.389 1.00 19.80 ?  104  LEU B C     1 
ATOM   9859  O O     . LEU B 1 106  ? 0.974   42.626  123.056 1.00 19.46 ?  104  LEU B O     1 
ATOM   9860  C CB    . LEU B 1 106  ? -0.609  45.293  121.830 1.00 18.13 ?  104  LEU B CB    1 
ATOM   9861  C CG    . LEU B 1 106  ? -0.129  45.748  123.209 1.00 19.64 ?  104  LEU B CG    1 
ATOM   9862  C CD1   . LEU B 1 106  ? 1.337   46.137  123.153 1.00 21.54 ?  104  LEU B CD1   1 
ATOM   9863  C CD2   . LEU B 1 106  ? -0.985  46.889  123.761 1.00 21.44 ?  104  LEU B CD2   1 
ATOM   9864  N N     . ALA B 1 107  ? -1.207  42.327  122.559 1.00 16.23 ?  105  ALA B N     1 
ATOM   9865  C CA    . ALA B 1 107  ? -1.359  41.271  123.557 1.00 18.54 ?  105  ALA B CA    1 
ATOM   9866  C C     . ALA B 1 107  ? -0.429  40.101  123.260 1.00 19.82 ?  105  ALA B C     1 
ATOM   9867  O O     . ALA B 1 107  ? 0.230   39.588  124.174 1.00 20.73 ?  105  ALA B O     1 
ATOM   9868  C CB    . ALA B 1 107  ? -2.812  40.802  123.610 1.00 21.41 ?  105  ALA B CB    1 
ATOM   9869  N N     . GLU B 1 108  ? -0.355  39.680  121.991 1.00 17.96 ?  106  GLU B N     1 
ATOM   9870  C CA    . GLU B 1 108  ? 0.572   38.619  121.591 1.00 18.70 ?  106  GLU B CA    1 
ATOM   9871  C C     . GLU B 1 108  ? 2.001   38.960  121.994 1.00 22.39 ?  106  GLU B C     1 
ATOM   9872  O O     . GLU B 1 108  ? 2.714   38.122  122.556 1.00 22.71 ?  106  GLU B O     1 
ATOM   9873  C CB    . GLU B 1 108  ? 0.481   38.378  120.077 1.00 19.32 ?  106  GLU B CB    1 
ATOM   9874  C CG    . GLU B 1 108  ? 1.595   37.488  119.532 1.00 21.78 ?  106  GLU B CG    1 
ATOM   9875  C CD    . GLU B 1 108  ? 1.745   37.541  118.023 1.00 24.07 ?  106  GLU B CD    1 
ATOM   9876  O OE1   . GLU B 1 108  ? 0.833   38.061  117.343 1.00 21.90 ?  106  GLU B OE1   1 
ATOM   9877  O OE2   . GLU B 1 108  ? 2.795   37.067  117.516 1.00 24.61 ?  106  GLU B OE2   1 
ATOM   9878  N N     . ALA B 1 109  ? 2.437   40.193  121.722 1.00 19.59 ?  107  ALA B N     1 
ATOM   9879  C CA    . ALA B 1 109  ? 3.801   40.575  122.066 1.00 24.11 ?  107  ALA B CA    1 
ATOM   9880  C C     . ALA B 1 109  ? 4.016   40.572  123.576 1.00 23.01 ?  107  ALA B C     1 
ATOM   9881  O O     . ALA B 1 109  ? 5.075   40.144  124.055 1.00 24.73 ?  107  ALA B O     1 
ATOM   9882  C CB    . ALA B 1 109  ? 4.131   41.945  121.476 1.00 22.06 ?  107  ALA B CB    1 
ATOM   9883  N N     . LEU B 1 110  ? 3.024   41.041  124.346 1.00 18.82 ?  108  LEU B N     1 
ATOM   9884  C CA    . LEU B 1 110  ? 3.163   41.049  125.800 1.00 22.62 ?  108  LEU B CA    1 
ATOM   9885  C C     . LEU B 1 110  ? 3.221   39.632  126.362 1.00 24.47 ?  108  LEU B C     1 
ATOM   9886  O O     . LEU B 1 110  ? 3.877   39.397  127.384 1.00 27.85 ?  108  LEU B O     1 
ATOM   9887  C CB    . LEU B 1 110  ? 2.015   41.837  126.446 1.00 21.64 ?  108  LEU B CB    1 
ATOM   9888  C CG    . LEU B 1 110  ? 2.109   43.358  126.274 1.00 22.83 ?  108  LEU B CG    1 
ATOM   9889  C CD1   . LEU B 1 110  ? 0.785   44.044  126.574 1.00 24.81 ?  108  LEU B CD1   1 
ATOM   9890  C CD2   . LEU B 1 110  ? 3.215   43.918  127.156 1.00 26.33 ?  108  LEU B CD2   1 
ATOM   9891  N N     . LEU B 1 111  ? 2.574   38.676  125.703 1.00 25.32 ?  109  LEU B N     1 
ATOM   9892  C CA    . LEU B 1 111  ? 2.613   37.301  126.182 1.00 26.45 ?  109  LEU B CA    1 
ATOM   9893  C C     . LEU B 1 111  ? 3.931   36.602  125.868 1.00 26.53 ?  109  LEU B C     1 
ATOM   9894  O O     . LEU B 1 111  ? 4.179   35.518  126.409 1.00 31.14 ?  109  LEU B O     1 
ATOM   9895  C CB    . LEU B 1 111  ? 1.442   36.511  125.603 1.00 28.22 ?  109  LEU B CB    1 
ATOM   9896  C CG    . LEU B 1 111  ? 0.094   36.940  126.192 1.00 22.79 ?  109  LEU B CG    1 
ATOM   9897  C CD1   . LEU B 1 111  ? -1.054  36.251  125.467 1.00 24.06 ?  109  LEU B CD1   1 
ATOM   9898  C CD2   . LEU B 1 111  ? 0.032   36.666  127.692 1.00 27.66 ?  109  LEU B CD2   1 
ATOM   9899  N N     . ARG B 1 112  ? 4.788   37.202  125.040 1.00 24.92 ?  110  ARG B N     1 
ATOM   9900  C CA    . ARG B 1 112  ? 6.138   36.693  124.839 1.00 28.17 ?  110  ARG B CA    1 
ATOM   9901  C C     . ARG B 1 112  ? 7.047   36.996  126.025 1.00 31.80 ?  110  ARG B C     1 
ATOM   9902  O O     . ARG B 1 112  ? 8.154   36.448  126.097 1.00 34.36 ?  110  ARG B O     1 
ATOM   9903  C CB    . ARG B 1 112  ? 6.723   37.268  123.544 1.00 26.91 ?  110  ARG B CB    1 
ATOM   9904  C CG    . ARG B 1 112  ? 5.977   36.832  122.276 1.00 27.10 ?  110  ARG B CG    1 
ATOM   9905  C CD    . ARG B 1 112  ? 6.288   37.724  121.067 1.00 31.14 ?  110  ARG B CD    1 
ATOM   9906  N NE    . ARG B 1 112  ? 7.665   37.598  120.606 1.00 41.77 ?  110  ARG B NE    1 
ATOM   9907  C CZ    . ARG B 1 112  ? 8.064   36.786  119.636 1.00 39.96 ?  110  ARG B CZ    1 
ATOM   9908  N NH1   . ARG B 1 112  ? 7.215   35.991  119.005 1.00 40.97 ?  110  ARG B NH1   1 
ATOM   9909  N NH2   . ARG B 1 112  ? 9.348   36.773  119.285 1.00 43.31 ?  110  ARG B NH2   1 
ATOM   9910  N N     . ILE B 1 113  ? 6.610   37.846  126.947 1.00 26.89 ?  111  ILE B N     1 
ATOM   9911  C CA    . ILE B 1 113  ? 7.290   38.046  128.223 1.00 30.11 ?  111  ILE B CA    1 
ATOM   9912  C C     . ILE B 1 113  ? 6.774   36.969  129.180 1.00 34.91 ?  111  ILE B C     1 
ATOM   9913  O O     . ILE B 1 113  ? 5.596   37.026  129.571 1.00 35.02 ?  111  ILE B O     1 
ATOM   9914  C CB    . ILE B 1 113  ? 7.042   39.451  128.781 1.00 32.24 ?  111  ILE B CB    1 
ATOM   9915  C CG1   . ILE B 1 113  ? 7.530   40.507  127.790 1.00 28.89 ?  111  ILE B CG1   1 
ATOM   9916  C CG2   . ILE B 1 113  ? 7.720   39.627  130.143 1.00 33.99 ?  111  ILE B CG2   1 
ATOM   9917  C CD1   . ILE B 1 113  ? 7.093   41.914  128.139 1.00 34.75 ?  111  ILE B CD1   1 
ATOM   9918  N N     . PRO B 1 114  ? 7.598   35.990  129.566 1.00 34.34 ?  112  PRO B N     1 
ATOM   9919  C CA    . PRO B 1 114  ? 7.073   34.885  130.388 1.00 36.89 ?  112  PRO B CA    1 
ATOM   9920  C C     . PRO B 1 114  ? 6.734   35.284  131.812 1.00 35.10 ?  112  PRO B C     1 
ATOM   9921  O O     . PRO B 1 114  ? 5.812   34.706  132.403 1.00 40.20 ?  112  PRO B O     1 
ATOM   9922  C CB    . PRO B 1 114  ? 8.211   33.856  130.353 1.00 34.22 ?  112  PRO B CB    1 
ATOM   9923  C CG    . PRO B 1 114  ? 9.438   34.663  130.075 1.00 37.22 ?  112  PRO B CG    1 
ATOM   9924  C CD    . PRO B 1 114  ? 8.997   35.775  129.167 1.00 36.27 ?  112  PRO B CD    1 
ATOM   9925  N N     . ASP B 1 115  ? 7.448   36.245  132.388 1.00 34.12 ?  113  ASP B N     1 
ATOM   9926  C CA    . ASP B 1 115  ? 7.252   36.606  133.785 1.00 41.19 ?  113  ASP B CA    1 
ATOM   9927  C C     . ASP B 1 115  ? 6.055   37.543  133.917 1.00 38.77 ?  113  ASP B C     1 
ATOM   9928  O O     . ASP B 1 115  ? 6.093   38.673  133.422 1.00 36.28 ?  113  ASP B O     1 
ATOM   9929  C CB    . ASP B 1 115  ? 8.518   37.256  134.335 1.00 38.12 ?  113  ASP B CB    1 
ATOM   9930  C CG    . ASP B 1 115  ? 8.346   37.755  135.747 1.00 41.46 ?  113  ASP B CG    1 
ATOM   9931  O OD1   . ASP B 1 115  ? 7.831   36.993  136.594 1.00 46.53 ?  113  ASP B OD1   1 
ATOM   9932  O OD2   . ASP B 1 115  ? 8.732   38.909  136.018 1.00 43.49 ?  113  ASP B OD2   1 
ATOM   9933  N N     . THR B 1 116  ? 5.004   37.076  134.599 1.00 37.67 ?  114  THR B N     1 
ATOM   9934  C CA    . THR B 1 116  ? 3.797   37.883  134.771 1.00 39.39 ?  114  THR B CA    1 
ATOM   9935  C C     . THR B 1 116  ? 4.109   39.237  135.401 1.00 40.59 ?  114  THR B C     1 
ATOM   9936  O O     . THR B 1 116  ? 3.578   40.267  134.970 1.00 38.64 ?  114  THR B O     1 
ATOM   9937  C CB    . THR B 1 116  ? 2.775   37.128  135.623 1.00 44.90 ?  114  THR B CB    1 
ATOM   9938  O OG1   . THR B 1 116  ? 2.503   35.852  135.033 1.00 47.55 ?  114  THR B OG1   1 
ATOM   9939  C CG2   . THR B 1 116  ? 1.478   37.913  135.722 1.00 42.32 ?  114  THR B CG2   1 
ATOM   9940  N N     . ALA B 1 117  ? 4.969   39.258  136.421 1.00 41.19 ?  115  ALA B N     1 
ATOM   9941  C CA    . ALA B 1 117  ? 5.246   40.508  137.118 1.00 38.65 ?  115  ALA B CA    1 
ATOM   9942  C C     . ALA B 1 117  ? 5.984   41.496  136.223 1.00 36.15 ?  115  ALA B C     1 
ATOM   9943  O O     . ALA B 1 117  ? 5.720   42.703  136.277 1.00 40.76 ?  115  ALA B O     1 
ATOM   9944  C CB    . ALA B 1 117  ? 6.043   40.231  138.394 1.00 37.84 ?  115  ALA B CB    1 
ATOM   9945  N N     . THR B 1 118  ? 6.923   41.011  135.405 1.00 37.07 ?  116  THR B N     1 
ATOM   9946  C CA    . THR B 1 118  ? 7.598   41.893  134.457 1.00 35.32 ?  116  THR B CA    1 
ATOM   9947  C C     . THR B 1 118  ? 6.620   42.416  133.414 1.00 35.10 ?  116  THR B C     1 
ATOM   9948  O O     . THR B 1 118  ? 6.653   43.600  133.057 1.00 36.12 ?  116  THR B O     1 
ATOM   9949  C CB    . THR B 1 118  ? 8.755   41.159  133.776 1.00 35.57 ?  116  THR B CB    1 
ATOM   9950  O OG1   . THR B 1 118  ? 9.618   40.596  134.772 1.00 42.94 ?  116  THR B OG1   1 
ATOM   9951  C CG2   . THR B 1 118  ? 9.565   42.107  132.906 1.00 34.85 ?  116  THR B CG2   1 
ATOM   9952  N N     . ARG B 1 119  ? 5.745   41.539  132.915 1.00 35.09 ?  117  ARG B N     1 
ATOM   9953  C CA    . ARG B 1 119  ? 4.759   41.933  131.913 1.00 32.78 ?  117  ARG B CA    1 
ATOM   9954  C C     . ARG B 1 119  ? 3.818   43.000  132.459 1.00 34.64 ?  117  ARG B C     1 
ATOM   9955  O O     . ARG B 1 119  ? 3.629   44.056  131.842 1.00 30.97 ?  117  ARG B O     1 
ATOM   9956  C CB    . ARG B 1 119  ? 3.972   40.705  131.465 1.00 30.58 ?  117  ARG B CB    1 
ATOM   9957  C CG    . ARG B 1 119  ? 2.981   40.959  130.337 1.00 26.65 ?  117  ARG B CG    1 
ATOM   9958  C CD    . ARG B 1 119  ? 2.014   39.806  130.260 1.00 30.48 ?  117  ARG B CD    1 
ATOM   9959  N NE    . ARG B 1 119  ? 2.709   38.545  130.034 1.00 31.55 ?  117  ARG B NE    1 
ATOM   9960  C CZ    . ARG B 1 119  ? 2.345   37.384  130.562 1.00 36.16 ?  117  ARG B CZ    1 
ATOM   9961  N NH1   . ARG B 1 119  ? 1.296   37.286  131.364 1.00 34.33 ?  117  ARG B NH1   1 
ATOM   9962  N NH2   . ARG B 1 119  ? 3.055   36.296  130.285 1.00 34.31 ?  117  ARG B NH2   1 
ATOM   9963  N N     . ASP B 1 120  ? 3.216   42.737  133.623 1.00 34.50 ?  118  ASP B N     1 
ATOM   9964  C CA    . ASP B 1 120  ? 2.277   43.688  134.210 1.00 37.79 ?  118  ASP B CA    1 
ATOM   9965  C C     . ASP B 1 120  ? 2.949   45.011  134.548 1.00 34.14 ?  118  ASP B C     1 
ATOM   9966  O O     . ASP B 1 120  ? 2.325   46.071  134.423 1.00 32.66 ?  118  ASP B O     1 
ATOM   9967  C CB    . ASP B 1 120  ? 1.631   43.082  135.455 1.00 35.43 ?  118  ASP B CB    1 
ATOM   9968  C CG    . ASP B 1 120  ? 0.770   41.868  135.137 1.00 42.10 ?  118  ASP B CG    1 
ATOM   9969  O OD1   . ASP B 1 120  ? 0.462   41.651  133.943 1.00 39.77 ?  118  ASP B OD1   1 
ATOM   9970  O OD2   . ASP B 1 120  ? 0.398   41.132  136.077 1.00 46.54 ?  118  ASP B OD2   1 
ATOM   9971  N N     . ALA B 1 121  ? 4.218   44.977  134.965 1.00 35.32 ?  119  ALA B N     1 
ATOM   9972  C CA    . ALA B 1 121  ? 4.929   46.223  135.233 1.00 38.55 ?  119  ALA B CA    1 
ATOM   9973  C C     . ALA B 1 121  ? 5.138   47.023  133.955 1.00 37.97 ?  119  ALA B C     1 
ATOM   9974  O O     . ALA B 1 121  ? 4.994   48.250  133.958 1.00 35.17 ?  119  ALA B O     1 
ATOM   9975  C CB    . ALA B 1 121  ? 6.267   45.936  135.915 1.00 37.89 ?  119  ALA B CB    1 
ATOM   9976  N N     . LEU B 1 122  ? 5.478   46.343  132.854 1.00 32.96 ?  120  LEU B N     1 
ATOM   9977  C CA    . LEU B 1 122  ? 5.670   47.029  131.580 1.00 35.63 ?  120  LEU B CA    1 
ATOM   9978  C C     . LEU B 1 122  ? 4.370   47.657  131.099 1.00 35.30 ?  120  LEU B C     1 
ATOM   9979  O O     . LEU B 1 122  ? 4.370   48.768  130.555 1.00 34.08 ?  120  LEU B O     1 
ATOM   9980  C CB    . LEU B 1 122  ? 6.209   46.054  130.533 1.00 33.24 ?  120  LEU B CB    1 
ATOM   9981  C CG    . LEU B 1 122  ? 6.485   46.671  129.162 1.00 32.43 ?  120  LEU B CG    1 
ATOM   9982  C CD1   . LEU B 1 122  ? 7.690   47.597  129.232 1.00 38.20 ?  120  LEU B CD1   1 
ATOM   9983  C CD2   . LEU B 1 122  ? 6.681   45.598  128.103 1.00 32.26 ?  120  LEU B CD2   1 
ATOM   9984  N N     . ILE B 1 123  ? 3.252   46.954  131.297 1.00 29.94 ?  121  ILE B N     1 
ATOM   9985  C CA    . ILE B 1 123  ? 1.945   47.479  130.913 1.00 33.67 ?  121  ILE B CA    1 
ATOM   9986  C C     . ILE B 1 123  ? 1.630   48.743  131.698 1.00 34.58 ?  121  ILE B C     1 
ATOM   9987  O O     . ILE B 1 123  ? 1.273   49.781  131.125 1.00 36.23 ?  121  ILE B O     1 
ATOM   9988  C CB    . ILE B 1 123  ? 0.860   46.407  131.122 1.00 29.20 ?  121  ILE B CB    1 
ATOM   9989  C CG1   . ILE B 1 123  ? 1.053   45.260  130.131 1.00 28.38 ?  121  ILE B CG1   1 
ATOM   9990  C CG2   . ILE B 1 123  ? -0.535  47.015  131.010 1.00 28.78 ?  121  ILE B CG2   1 
ATOM   9991  C CD1   . ILE B 1 123  ? 0.185   44.067  130.417 1.00 28.12 ?  121  ILE B CD1   1 
ATOM   9992  N N     . ARG B 1 124  ? 1.770   48.678  133.027 1.00 35.10 ?  122  ARG B N     1 
ATOM   9993  C CA    . ARG B 1 124  ? 1.342   49.785  133.876 1.00 37.63 ?  122  ARG B CA    1 
ATOM   9994  C C     . ARG B 1 124  ? 2.249   50.998  133.716 1.00 40.91 ?  122  ARG B C     1 
ATOM   9995  O O     . ARG B 1 124  ? 1.773   52.140  133.700 1.00 44.48 ?  122  ARG B O     1 
ATOM   9996  C CB    . ARG B 1 124  ? 1.300   49.339  135.338 1.00 39.88 ?  122  ARG B CB    1 
ATOM   9997  N N     . ASP B 1 125  ? 3.552   50.779  133.578 1.00 40.36 ?  123  ASP B N     1 
ATOM   9998  C CA    . ASP B 1 125  ? 4.506   51.873  133.664 1.00 44.25 ?  123  ASP B CA    1 
ATOM   9999  C C     . ASP B 1 125  ? 5.061   52.321  132.315 1.00 40.53 ?  123  ASP B C     1 
ATOM   10000 O O     . ASP B 1 125  ? 5.705   53.372  132.254 1.00 44.64 ?  123  ASP B O     1 
ATOM   10001 C CB    . ASP B 1 125  ? 5.656   51.477  134.597 1.00 48.97 ?  123  ASP B CB    1 
ATOM   10002 C CG    . ASP B 1 125  ? 5.158   50.915  135.922 1.00 49.24 ?  123  ASP B CG    1 
ATOM   10003 O OD1   . ASP B 1 125  ? 4.128   51.407  136.436 1.00 47.22 ?  123  ASP B OD1   1 
ATOM   10004 O OD2   . ASP B 1 125  ? 5.789   49.973  136.447 1.00 53.92 ?  123  ASP B OD2   1 
ATOM   10005 N N     . LYS B 1 126  ? 4.821   51.579  131.236 1.00 39.03 ?  124  LYS B N     1 
ATOM   10006 C CA    . LYS B 1 126  ? 5.341   51.994  129.939 1.00 39.61 ?  124  LYS B CA    1 
ATOM   10007 C C     . LYS B 1 126  ? 4.261   52.014  128.862 1.00 42.62 ?  124  LYS B C     1 
ATOM   10008 O O     . LYS B 1 126  ? 4.079   53.027  128.178 1.00 48.90 ?  124  LYS B O     1 
ATOM   10009 C CB    . LYS B 1 126  ? 6.488   51.078  129.509 1.00 43.80 ?  124  LYS B CB    1 
ATOM   10010 N N     . ILE B 1 127  ? 3.540   50.901  128.702 1.00 36.10 ?  125  ILE B N     1 
ATOM   10011 C CA    . ILE B 1 127  ? 2.625   50.767  127.571 1.00 37.11 ?  125  ILE B CA    1 
ATOM   10012 C C     . ILE B 1 127  ? 1.400   51.658  127.744 1.00 38.38 ?  125  ILE B C     1 
ATOM   10013 O O     . ILE B 1 127  ? 0.931   52.276  126.780 1.00 35.32 ?  125  ILE B O     1 
ATOM   10014 C CB    . ILE B 1 127  ? 2.215   49.296  127.382 1.00 32.36 ?  125  ILE B CB    1 
ATOM   10015 C CG1   . ILE B 1 127  ? 3.434   48.372  127.464 1.00 32.29 ?  125  ILE B CG1   1 
ATOM   10016 C CG2   . ILE B 1 127  ? 1.496   49.123  126.045 1.00 29.82 ?  125  ILE B CG2   1 
ATOM   10017 C CD1   . ILE B 1 127  ? 4.411   48.558  126.340 1.00 36.95 ?  125  ILE B CD1   1 
ATOM   10018 N N     . ALA B 1 128  ? 0.845   51.721  128.957 1.00 37.24 ?  126  ALA B N     1 
ATOM   10019 C CA    . ALA B 1 128  ? -0.413  52.431  129.167 1.00 35.05 ?  126  ALA B CA    1 
ATOM   10020 C C     . ALA B 1 128  ? -0.293  53.926  128.905 1.00 42.67 ?  126  ALA B C     1 
ATOM   10021 O O     . ALA B 1 128  ? -1.306  54.579  128.630 1.00 38.84 ?  126  ALA B O     1 
ATOM   10022 C CB    . ALA B 1 128  ? -0.926  52.188  130.587 1.00 39.09 ?  126  ALA B CB    1 
ATOM   10023 N N     . ASP B 1 129  ? 0.913   54.479  128.972 1.00 50.47 ?  127  ASP B N     1 
ATOM   10024 C CA    . ASP B 1 129  ? 1.120   55.897  128.713 1.00 57.17 ?  127  ASP B CA    1 
ATOM   10025 C C     . ASP B 1 129  ? 1.346   56.140  127.228 1.00 56.77 ?  127  ASP B C     1 
ATOM   10026 O O     . ASP B 1 129  ? 2.455   55.965  126.728 1.00 62.72 ?  127  ASP B O     1 
ATOM   10027 C CB    . ASP B 1 129  ? 2.306   56.427  129.522 1.00 61.93 ?  127  ASP B CB    1 
ATOM   10028 C CG    . ASP B 1 129  ? 2.042   56.421  131.015 1.00 65.16 ?  127  ASP B CG    1 
ATOM   10029 O OD1   . ASP B 1 129  ? 1.027   57.009  131.448 1.00 66.80 ?  127  ASP B OD1   1 
ATOM   10030 O OD2   . ASP B 1 129  ? 2.846   55.820  131.758 1.00 66.65 ?  127  ASP B OD2   1 
ATOM   10031 N N     . ASN B 1 131  ? 3.193   55.301  124.667 1.00 55.34 ?  129  ASN B N     1 
ATOM   10032 C CA    . ASN B 1 131  ? 4.624   55.267  124.372 1.00 55.40 ?  129  ASN B CA    1 
ATOM   10033 C C     . ASN B 1 131  ? 5.074   53.836  124.117 1.00 51.87 ?  129  ASN B C     1 
ATOM   10034 O O     . ASN B 1 131  ? 6.214   53.469  124.406 1.00 53.48 ?  129  ASN B O     1 
ATOM   10035 C CB    . ASN B 1 131  ? 5.433   55.880  125.519 1.00 49.71 ?  129  ASN B CB    1 
ATOM   10036 N N     . TRP B 1 132  ? 4.159   53.033  123.568 1.00 46.10 ?  130  TRP B N     1 
ATOM   10037 C CA    . TRP B 1 132  ? 4.438   51.617  123.342 1.00 43.06 ?  130  TRP B CA    1 
ATOM   10038 C C     . TRP B 1 132  ? 5.551   51.406  122.325 1.00 45.12 ?  130  TRP B C     1 
ATOM   10039 O O     . TRP B 1 132  ? 6.228   50.373  122.360 1.00 47.35 ?  130  TRP B O     1 
ATOM   10040 C CB    . TRP B 1 132  ? 3.167   50.905  122.876 1.00 36.70 ?  130  TRP B CB    1 
ATOM   10041 C CG    . TRP B 1 132  ? 2.590   51.465  121.595 1.00 35.56 ?  130  TRP B CG    1 
ATOM   10042 C CD1   . TRP B 1 132  ? 1.683   52.479  121.477 1.00 36.24 ?  130  TRP B CD1   1 
ATOM   10043 C CD2   . TRP B 1 132  ? 2.893   51.042  120.259 1.00 30.92 ?  130  TRP B CD2   1 
ATOM   10044 N NE1   . TRP B 1 132  ? 1.398   52.709  120.151 1.00 30.65 ?  130  TRP B NE1   1 
ATOM   10045 C CE2   . TRP B 1 132  ? 2.131   51.844  119.382 1.00 30.11 ?  130  TRP B CE2   1 
ATOM   10046 C CE3   . TRP B 1 132  ? 3.736   50.067  119.720 1.00 31.36 ?  130  TRP B CE3   1 
ATOM   10047 C CZ2   . TRP B 1 132  ? 2.181   51.694  118.001 1.00 26.83 ?  130  TRP B CZ2   1 
ATOM   10048 C CZ3   . TRP B 1 132  ? 3.788   49.921  118.348 1.00 25.87 ?  130  TRP B CZ3   1 
ATOM   10049 C CH2   . TRP B 1 132  ? 3.009   50.732  117.502 1.00 27.46 ?  130  TRP B CH2   1 
ATOM   10050 N N     . LYS B 1 133  ? 5.752   52.367  121.416 1.00 46.42 ?  131  LYS B N     1 
ATOM   10051 C CA    . LYS B 1 133  ? 6.665   52.156  120.295 1.00 47.27 ?  131  LYS B CA    1 
ATOM   10052 C C     . LYS B 1 133  ? 8.091   51.886  120.761 1.00 55.32 ?  131  LYS B C     1 
ATOM   10053 O O     . LYS B 1 133  ? 8.821   51.125  120.115 1.00 57.82 ?  131  LYS B O     1 
ATOM   10054 C CB    . LYS B 1 133  ? 6.630   53.366  119.355 1.00 45.35 ?  131  LYS B CB    1 
ATOM   10055 C CG    . LYS B 1 133  ? 5.246   53.695  118.798 1.00 45.27 ?  131  LYS B CG    1 
ATOM   10056 C CD    . LYS B 1 133  ? 5.311   54.781  117.724 1.00 45.39 ?  131  LYS B CD    1 
ATOM   10057 C CE    . LYS B 1 133  ? 3.950   54.998  117.063 1.00 40.76 ?  131  LYS B CE    1 
ATOM   10058 N NZ    . LYS B 1 133  ? 4.049   55.163  115.578 1.00 39.77 ?  131  LYS B NZ    1 
ATOM   10059 N N     . SER B 1 134  ? 8.502   52.484  121.877 1.00 57.69 ?  132  SER B N     1 
ATOM   10060 C CA    . SER B 1 134  ? 9.870   52.366  122.379 1.00 58.20 ?  132  SER B CA    1 
ATOM   10061 C C     . SER B 1 134  ? 9.999   51.310  123.471 1.00 61.25 ?  132  SER B C     1 
ATOM   10062 O O     . SER B 1 134  ? 10.715  51.524  124.453 1.00 58.76 ?  132  SER B O     1 
ATOM   10063 C CB    . SER B 1 134  ? 10.357  53.720  122.886 1.00 58.35 ?  132  SER B CB    1 
ATOM   10064 N N     . HIS B 1 135  ? 9.336   50.159  123.329 1.00 62.67 ?  133  HIS B N     1 
ATOM   10065 C CA    . HIS B 1 135  ? 9.365   49.150  124.385 1.00 62.31 ?  133  HIS B CA    1 
ATOM   10066 C C     . HIS B 1 135  ? 9.091   47.734  123.883 1.00 59.64 ?  133  HIS B C     1 
ATOM   10067 O O     . HIS B 1 135  ? 9.496   46.761  124.528 1.00 63.92 ?  133  HIS B O     1 
ATOM   10068 C CB    . HIS B 1 135  ? 8.351   49.496  125.481 1.00 57.86 ?  133  HIS B CB    1 
ATOM   10069 C CG    . HIS B 1 135  ? 8.824   50.544  126.439 1.00 62.20 ?  133  HIS B CG    1 
ATOM   10070 N ND1   . HIS B 1 135  ? 8.277   51.808  126.490 1.00 61.64 ?  133  HIS B ND1   1 
ATOM   10071 C CD2   . HIS B 1 135  ? 9.797   50.517  127.380 1.00 65.67 ?  133  HIS B CD2   1 
ATOM   10072 C CE1   . HIS B 1 135  ? 8.889   52.513  127.425 1.00 65.06 ?  133  HIS B CE1   1 
ATOM   10073 N NE2   . HIS B 1 135  ? 9.815   51.753  127.980 1.00 65.79 ?  133  HIS B NE2   1 
ATOM   10074 N N     . LEU B 1 136  ? 8.398   47.595  122.763 1.00 58.02 ?  134  LEU B N     1 
ATOM   10075 C CA    . LEU B 1 136  ? 8.029   46.249  122.328 1.00 53.69 ?  134  LEU B CA    1 
ATOM   10076 C C     . LEU B 1 136  ? 8.350   45.971  120.868 1.00 55.07 ?  134  LEU B C     1 
ATOM   10077 O O     . LEU B 1 136  ? 8.789   44.863  120.544 1.00 50.64 ?  134  LEU B O     1 
ATOM   10078 C CB    . LEU B 1 136  ? 6.534   46.005  122.580 1.00 44.23 ?  134  LEU B CB    1 
ATOM   10079 C CG    . LEU B 1 136  ? 6.141   45.571  123.989 1.00 41.39 ?  134  LEU B CG    1 
ATOM   10080 C CD1   . LEU B 1 136  ? 4.657   45.318  124.034 1.00 34.48 ?  134  LEU B CD1   1 
ATOM   10081 C CD2   . LEU B 1 136  ? 6.905   44.324  124.403 1.00 38.16 ?  134  LEU B CD2   1 
ATOM   10082 N N     . GLY B 1 137  ? 8.123   46.932  119.976 1.00 55.61 ?  135  GLY B N     1 
ATOM   10083 C CA    . GLY B 1 137  ? 8.484   46.755  118.585 1.00 53.71 ?  135  GLY B CA    1 
ATOM   10084 C C     . GLY B 1 137  ? 9.985   46.813  118.373 1.00 56.76 ?  135  GLY B C     1 
ATOM   10085 O O     . GLY B 1 137  ? 10.734  46.052  118.992 1.00 57.34 ?  135  GLY B O     1 
ATOM   10086 N N     . GLY B 1 138  ? 10.434  47.720  117.515 1.00 55.93 ?  136  GLY B N     1 
ATOM   10087 C CA    . GLY B 1 138  ? 11.856  47.866  117.276 1.00 56.95 ?  136  GLY B CA    1 
ATOM   10088 C C     . GLY B 1 138  ? 12.370  46.897  116.229 1.00 51.06 ?  136  GLY B C     1 
ATOM   10089 O O     . GLY B 1 138  ? 12.115  47.085  115.034 1.00 51.45 ?  136  GLY B O     1 
ATOM   10090 N N     . SER B 1 139  ? 13.078  45.852  116.667 1.00 42.44 ?  137  SER B N     1 
ATOM   10091 C CA    . SER B 1 139  ? 13.612  44.892  115.703 1.00 39.61 ?  137  SER B CA    1 
ATOM   10092 C C     . SER B 1 139  ? 12.501  44.066  115.065 1.00 38.67 ?  137  SER B C     1 
ATOM   10093 O O     . SER B 1 139  ? 12.565  43.757  113.871 1.00 37.20 ?  137  SER B O     1 
ATOM   10094 C CB    . SER B 1 139  ? 14.641  43.988  116.376 1.00 40.56 ?  137  SER B CB    1 
ATOM   10095 O OG    . SER B 1 139  ? 15.782  44.736  116.761 1.00 43.05 ?  137  SER B OG    1 
ATOM   10096 N N     . ARG B 1 140  ? 11.479  43.702  115.839 1.00 34.63 ?  138  ARG B N     1 
ATOM   10097 C CA    . ARG B 1 140  ? 10.341  42.930  115.350 1.00 35.70 ?  138  ARG B CA    1 
ATOM   10098 C C     . ARG B 1 140  ? 9.093   43.800  115.428 1.00 32.72 ?  138  ARG B C     1 
ATOM   10099 O O     . ARG B 1 140  ? 8.752   44.302  116.504 1.00 33.32 ?  138  ARG B O     1 
ATOM   10100 C CB    . ARG B 1 140  ? 10.155  41.647  116.166 1.00 36.17 ?  138  ARG B CB    1 
ATOM   10101 C CG    . ARG B 1 140  ? 8.888   40.849  115.840 1.00 39.38 ?  138  ARG B CG    1 
ATOM   10102 C CD    . ARG B 1 140  ? 8.684   39.709  116.839 1.00 43.35 ?  138  ARG B CD    1 
ATOM   10103 N NE    . ARG B 1 140  ? 7.494   38.909  116.561 1.00 44.20 ?  138  ARG B NE    1 
ATOM   10104 C CZ    . ARG B 1 140  ? 6.285   39.154  117.054 1.00 44.16 ?  138  ARG B CZ    1 
ATOM   10105 N NH1   . ARG B 1 140  ? 6.057   40.187  117.852 1.00 40.84 ?  138  ARG B NH1   1 
ATOM   10106 N NH2   . ARG B 1 140  ? 5.276   38.344  116.734 1.00 41.18 ?  138  ARG B NH2   1 
ATOM   10107 N N     . SER B 1 141  ? 8.432   43.995  114.288 1.00 27.92 ?  139  SER B N     1 
ATOM   10108 C CA    . SER B 1 141  ? 7.167   44.714  114.283 1.00 25.05 ?  139  SER B CA    1 
ATOM   10109 C C     . SER B 1 141  ? 6.184   44.035  115.227 1.00 24.89 ?  139  SER B C     1 
ATOM   10110 O O     . SER B 1 141  ? 6.120   42.806  115.310 1.00 24.73 ?  139  SER B O     1 
ATOM   10111 C CB    . SER B 1 141  ? 6.583   44.765  112.868 1.00 24.65 ?  139  SER B CB    1 
ATOM   10112 O OG    . SER B 1 141  ? 5.264   45.306  112.866 1.00 23.41 ?  139  SER B OG    1 
ATOM   10113 N N     . LEU B 1 142  ? 5.448   44.849  115.985 1.00 21.36 ?  140  LEU B N     1 
ATOM   10114 C CA    A LEU B 1 142  ? 4.360   44.308  116.791 0.30 21.31 ?  140  LEU B CA    1 
ATOM   10115 C CA    B LEU B 1 142  ? 4.358   44.318  116.789 0.70 21.25 ?  140  LEU B CA    1 
ATOM   10116 C C     . LEU B 1 142  ? 3.351   43.565  115.934 1.00 20.02 ?  140  LEU B C     1 
ATOM   10117 O O     . LEU B 1 142  ? 2.651   42.674  116.429 1.00 18.54 ?  140  LEU B O     1 
ATOM   10118 C CB    A LEU B 1 142  ? 3.640   45.424  117.548 0.30 22.86 ?  140  LEU B CB    1 
ATOM   10119 C CB    B LEU B 1 142  ? 3.665   45.470  117.502 0.70 22.89 ?  140  LEU B CB    1 
ATOM   10120 C CG    A LEU B 1 142  ? 4.266   45.989  118.815 0.30 24.28 ?  140  LEU B CG    1 
ATOM   10121 C CG    B LEU B 1 142  ? 3.124   45.193  118.884 0.70 22.16 ?  140  LEU B CG    1 
ATOM   10122 C CD1   A LEU B 1 142  ? 3.200   46.696  119.628 0.30 23.75 ?  140  LEU B CD1   1 
ATOM   10123 C CD1   B LEU B 1 142  ? 4.279   45.042  119.829 0.70 23.93 ?  140  LEU B CD1   1 
ATOM   10124 C CD2   A LEU B 1 142  ? 4.899   44.881  119.617 0.30 27.18 ?  140  LEU B CD2   1 
ATOM   10125 C CD2   B LEU B 1 142  ? 2.288   46.367  119.276 0.70 23.83 ?  140  LEU B CD2   1 
ATOM   10126 N N     . PHE B 1 143  ? 3.261   43.917  114.657 1.00 17.97 ?  141  PHE B N     1 
ATOM   10127 C CA    . PHE B 1 143  ? 2.163   43.497  113.803 1.00 17.81 ?  141  PHE B CA    1 
ATOM   10128 C C     . PHE B 1 143  ? 2.535   42.382  112.822 1.00 17.48 ?  141  PHE B C     1 
ATOM   10129 O O     . PHE B 1 143  ? 1.795   42.149  111.863 1.00 16.95 ?  141  PHE B O     1 
ATOM   10130 C CB    . PHE B 1 143  ? 1.621   44.732  113.072 1.00 16.70 ?  141  PHE B CB    1 
ATOM   10131 C CG    . PHE B 1 143  ? 1.325   45.879  113.992 1.00 17.46 ?  141  PHE B CG    1 
ATOM   10132 C CD1   . PHE B 1 143  ? 0.408   45.734  115.025 1.00 16.52 ?  141  PHE B CD1   1 
ATOM   10133 C CD2   . PHE B 1 143  ? 1.970   47.104  113.848 1.00 18.29 ?  141  PHE B CD2   1 
ATOM   10134 C CE1   . PHE B 1 143  ? 0.137   46.775  115.898 1.00 17.51 ?  141  PHE B CE1   1 
ATOM   10135 C CE2   . PHE B 1 143  ? 1.712   48.147  114.713 1.00 17.29 ?  141  PHE B CE2   1 
ATOM   10136 C CZ    . PHE B 1 143  ? 0.793   47.995  115.744 1.00 17.63 ?  141  PHE B CZ    1 
ATOM   10137 N N     . VAL B 1 144  ? 3.614   41.634  113.092 1.00 18.36 ?  142  VAL B N     1 
ATOM   10138 C CA    . VAL B 1 144  ? 4.073   40.570  112.192 1.00 17.17 ?  142  VAL B CA    1 
ATOM   10139 C C     . VAL B 1 144  ? 2.963   39.568  111.889 1.00 18.78 ?  142  VAL B C     1 
ATOM   10140 O O     . VAL B 1 144  ? 2.824   39.098  110.751 1.00 19.82 ?  142  VAL B O     1 
ATOM   10141 C CB    . VAL B 1 144  ? 5.311   39.875  112.791 1.00 20.86 ?  142  VAL B CB    1 
ATOM   10142 C CG1   . VAL B 1 144  ? 5.682   38.641  111.989 1.00 25.58 ?  142  VAL B CG1   1 
ATOM   10143 C CG2   . VAL B 1 144  ? 6.468   40.837  112.826 1.00 24.91 ?  142  VAL B CG2   1 
ATOM   10144 N N     . ASN B 1 145  ? 2.150   39.228  112.893 1.00 19.62 ?  143  ASN B N     1 
ATOM   10145 C CA    . ASN B 1 145  ? 1.091   38.241  112.730 1.00 18.00 ?  143  ASN B CA    1 
ATOM   10146 C C     . ASN B 1 145  ? -0.288  38.875  112.591 1.00 18.24 ?  143  ASN B C     1 
ATOM   10147 O O     . ASN B 1 145  ? -1.297  38.210  112.849 1.00 18.65 ?  143  ASN B O     1 
ATOM   10148 C CB    . ASN B 1 145  ? 1.109   37.255  113.897 1.00 18.19 ?  143  ASN B CB    1 
ATOM   10149 C CG    . ASN B 1 145  ? 2.252   36.274  113.790 1.00 23.91 ?  143  ASN B CG    1 
ATOM   10150 O OD1   . ASN B 1 145  ? 2.487   35.692  112.720 1.00 25.60 ?  143  ASN B OD1   1 
ATOM   10151 N ND2   . ASN B 1 145  ? 2.986   36.096  114.879 1.00 22.57 ?  143  ASN B ND2   1 
ATOM   10152 N N     . ALA B 1 146  ? -0.353  40.137  112.163 1.00 17.44 ?  144  ALA B N     1 
ATOM   10153 C CA    . ALA B 1 146  ? -1.641  40.815  112.094 1.00 18.13 ?  144  ALA B CA    1 
ATOM   10154 C C     . ALA B 1 146  ? -2.590  40.200  111.071 1.00 18.12 ?  144  ALA B C     1 
ATOM   10155 O O     . ALA B 1 146  ? -3.807  40.357  111.208 1.00 19.42 ?  144  ALA B O     1 
ATOM   10156 C CB    . ALA B 1 146  ? -1.441  42.303  111.797 1.00 17.11 ?  144  ALA B CB    1 
ATOM   10157 N N     . ALA B 1 147  ? -2.079  39.523  110.040 1.00 18.49 ?  145  ALA B N     1 
ATOM   10158 C CA    . ALA B 1 147  ? -2.993  38.853  109.119 1.00 17.81 ?  145  ALA B CA    1 
ATOM   10159 C C     . ALA B 1 147  ? -3.772  37.765  109.841 1.00 20.82 ?  145  ALA B C     1 
ATOM   10160 O O     . ALA B 1 147  ? -4.964  37.562  109.582 1.00 20.61 ?  145  ALA B O     1 
ATOM   10161 C CB    . ALA B 1 147  ? -2.229  38.269  107.935 1.00 19.16 ?  145  ALA B CB    1 
ATOM   10162 N N     . THR B 1 148  ? -3.120  37.072  110.775 1.00 18.55 ?  146  THR B N     1 
ATOM   10163 C CA    . THR B 1 148  ? -3.805  36.041  111.540 1.00 22.30 ?  146  THR B CA    1 
ATOM   10164 C C     . THR B 1 148  ? -4.854  36.656  112.459 1.00 19.62 ?  146  THR B C     1 
ATOM   10165 O O     . THR B 1 148  ? -6.016  36.234  112.468 1.00 21.72 ?  146  THR B O     1 
ATOM   10166 C CB    . THR B 1 148  ? -2.787  35.230  112.340 1.00 22.97 ?  146  THR B CB    1 
ATOM   10167 O OG1   . THR B 1 148  ? -1.860  34.627  111.430 1.00 24.19 ?  146  THR B OG1   1 
ATOM   10168 C CG2   . THR B 1 148  ? -3.482  34.147  113.153 1.00 25.64 ?  146  THR B CG2   1 
ATOM   10169 N N     . TRP B 1 149  ? -4.464  37.671  113.233 1.00 18.89 ?  147  TRP B N     1 
ATOM   10170 C CA    . TRP B 1 149  ? -5.431  38.339  114.091 1.00 18.81 ?  147  TRP B CA    1 
ATOM   10171 C C     . TRP B 1 149  ? -6.521  39.034  113.284 1.00 19.16 ?  147  TRP B C     1 
ATOM   10172 O O     . TRP B 1 149  ? -7.650  39.175  113.764 1.00 19.46 ?  147  TRP B O     1 
ATOM   10173 C CB    . TRP B 1 149  ? -4.716  39.329  115.009 1.00 19.26 ?  147  TRP B CB    1 
ATOM   10174 C CG    . TRP B 1 149  ? -3.813  38.640  115.989 1.00 17.80 ?  147  TRP B CG    1 
ATOM   10175 C CD1   . TRP B 1 149  ? -2.454  38.731  116.057 1.00 18.54 ?  147  TRP B CD1   1 
ATOM   10176 C CD2   . TRP B 1 149  ? -4.209  37.717  117.007 1.00 20.21 ?  147  TRP B CD2   1 
ATOM   10177 N NE1   . TRP B 1 149  ? -1.978  37.943  117.087 1.00 17.66 ?  147  TRP B NE1   1 
ATOM   10178 C CE2   . TRP B 1 149  ? -3.040  37.303  117.672 1.00 21.19 ?  147  TRP B CE2   1 
ATOM   10179 C CE3   . TRP B 1 149  ? -5.441  37.209  117.426 1.00 22.61 ?  147  TRP B CE3   1 
ATOM   10180 C CZ2   . TRP B 1 149  ? -3.066  36.407  118.741 1.00 22.05 ?  147  TRP B CZ2   1 
ATOM   10181 C CZ3   . TRP B 1 149  ? -5.467  36.316  118.491 1.00 24.67 ?  147  TRP B CZ3   1 
ATOM   10182 C CH2   . TRP B 1 149  ? -4.287  35.928  119.134 1.00 24.13 ?  147  TRP B CH2   1 
ATOM   10183 N N     . GLY B 1 150  ? -6.211  39.469  112.063 1.00 18.53 ?  148  GLY B N     1 
ATOM   10184 C CA    . GLY B 1 150  ? -7.255  40.005  111.201 1.00 18.88 ?  148  GLY B CA    1 
ATOM   10185 C C     . GLY B 1 150  ? -8.349  38.994  110.919 1.00 20.96 ?  148  GLY B C     1 
ATOM   10186 O O     . GLY B 1 150  ? -9.542  39.319  110.958 1.00 22.05 ?  148  GLY B O     1 
ATOM   10187 N N     . LEU B 1 151  ? -7.960  37.748  110.648 1.00 20.92 ?  149  LEU B N     1 
ATOM   10188 C CA    . LEU B 1 151  ? -8.944  36.679  110.515 1.00 22.97 ?  149  LEU B CA    1 
ATOM   10189 C C     . LEU B 1 151  ? -9.750  36.513  111.795 1.00 24.55 ?  149  LEU B C     1 
ATOM   10190 O O     . LEU B 1 151  ? -10.980 36.405  111.756 1.00 26.69 ?  149  LEU B O     1 
ATOM   10191 C CB    . LEU B 1 151  ? -8.246  35.370  110.156 1.00 28.62 ?  149  LEU B CB    1 
ATOM   10192 C CG    . LEU B 1 151  ? -8.180  35.022  108.679 1.00 27.65 ?  149  LEU B CG    1 
ATOM   10193 C CD1   . LEU B 1 151  ? -7.415  33.728  108.528 1.00 25.98 ?  149  LEU B CD1   1 
ATOM   10194 C CD2   . LEU B 1 151  ? -9.583  34.897  108.118 1.00 26.75 ?  149  LEU B CD2   1 
ATOM   10195 N N     . VAL B 1 152  ? -9.074  36.490  112.947 1.00 24.23 ?  150  VAL B N     1 
ATOM   10196 C CA    . VAL B 1 152  ? -9.783  36.279  114.209 1.00 26.13 ?  150  VAL B CA    1 
ATOM   10197 C C     . VAL B 1 152  ? -10.800 37.388  114.454 1.00 26.26 ?  150  VAL B C     1 
ATOM   10198 O O     . VAL B 1 152  ? -11.934 37.128  114.873 1.00 29.26 ?  150  VAL B O     1 
ATOM   10199 C CB    . VAL B 1 152  ? -8.789  36.169  115.381 1.00 24.49 ?  150  VAL B CB    1 
ATOM   10200 C CG1   . VAL B 1 152  ? -9.537  36.118  116.704 1.00 27.18 ?  150  VAL B CG1   1 
ATOM   10201 C CG2   . VAL B 1 152  ? -7.905  34.950  115.220 1.00 27.36 ?  150  VAL B CG2   1 
ATOM   10202 N N     . VAL B 1 153  ? -10.421 38.638  114.179 1.00 22.90 ?  151  VAL B N     1 
ATOM   10203 C CA    . VAL B 1 153  ? -11.253 39.780  114.549 1.00 23.10 ?  151  VAL B CA    1 
ATOM   10204 C C     . VAL B 1 153  ? -12.351 40.026  113.522 1.00 23.31 ?  151  VAL B C     1 
ATOM   10205 O O     . VAL B 1 153  ? -13.497 40.312  113.887 1.00 24.85 ?  151  VAL B O     1 
ATOM   10206 C CB    . VAL B 1 153  ? -10.367 41.027  114.736 1.00 21.36 ?  151  VAL B CB    1 
ATOM   10207 C CG1   . VAL B 1 153  ? -11.213 42.280  114.923 1.00 24.14 ?  151  VAL B CG1   1 
ATOM   10208 C CG2   . VAL B 1 153  ? -9.432  40.828  115.914 1.00 22.07 ?  151  VAL B CG2   1 
ATOM   10209 N N     . THR B 1 154  ? -12.018 39.933  112.231 1.00 23.21 ?  152  THR B N     1 
ATOM   10210 C CA    . THR B 1 154  ? -12.915 40.336  111.155 1.00 23.10 ?  152  THR B CA    1 
ATOM   10211 C C     . THR B 1 154  ? -13.441 39.179  110.322 1.00 28.04 ?  152  THR B C     1 
ATOM   10212 O O     . THR B 1 154  ? -14.426 39.360  109.599 1.00 31.00 ?  152  THR B O     1 
ATOM   10213 C CB    . THR B 1 154  ? -12.205 41.313  110.199 1.00 25.23 ?  152  THR B CB    1 
ATOM   10214 O OG1   . THR B 1 154  ? -11.328 40.586  109.328 1.00 24.90 ?  152  THR B OG1   1 
ATOM   10215 C CG2   . THR B 1 154  ? -11.391 42.336  110.983 1.00 29.90 ?  152  THR B CG2   1 
ATOM   10216 N N     . GLY B 1 155  ? -12.803 38.015  110.380 1.00 24.21 ?  153  GLY B N     1 
ATOM   10217 C CA    . GLY B 1 155  ? -13.137 36.923  109.492 1.00 23.76 ?  153  GLY B CA    1 
ATOM   10218 C C     . GLY B 1 155  ? -12.603 37.064  108.087 1.00 26.87 ?  153  GLY B C     1 
ATOM   10219 O O     . GLY B 1 155  ? -12.814 36.159  107.269 1.00 31.29 ?  153  GLY B O     1 
ATOM   10220 N N     . LYS B 1 156  ? -11.923 38.163  107.773 1.00 25.77 ?  154  LYS B N     1 
ATOM   10221 C CA    . LYS B 1 156  ? -11.354 38.380  106.453 1.00 25.43 ?  154  LYS B CA    1 
ATOM   10222 C C     . LYS B 1 156  ? -9.838  38.256  106.522 1.00 24.30 ?  154  LYS B C     1 
ATOM   10223 O O     . LYS B 1 156  ? -9.214  38.610  107.531 1.00 22.69 ?  154  LYS B O     1 
ATOM   10224 C CB    . LYS B 1 156  ? -11.754 39.749  105.894 1.00 31.79 ?  154  LYS B CB    1 
ATOM   10225 N N     . LEU B 1 157  ? -9.255  37.714  105.457 1.00 25.47 ?  155  LEU B N     1 
ATOM   10226 C CA    . LEU B 1 157  ? -7.813  37.591  105.335 1.00 24.38 ?  155  LEU B CA    1 
ATOM   10227 C C     . LEU B 1 157  ? -7.289  38.718  104.457 1.00 26.41 ?  155  LEU B C     1 
ATOM   10228 O O     . LEU B 1 157  ? -7.810  38.954  103.363 1.00 27.05 ?  155  LEU B O     1 
ATOM   10229 C CB    . LEU B 1 157  ? -7.418  36.236  104.744 1.00 26.89 ?  155  LEU B CB    1 
ATOM   10230 C CG    . LEU B 1 157  ? -5.914  36.030  104.555 1.00 27.26 ?  155  LEU B CG    1 
ATOM   10231 C CD1   . LEU B 1 157  ? -5.193  36.055  105.896 1.00 26.31 ?  155  LEU B CD1   1 
ATOM   10232 C CD2   . LEU B 1 157  ? -5.631  34.733  103.809 1.00 29.29 ?  155  LEU B CD2   1 
ATOM   10233 N N     . THR B 1 158  ? -6.279  39.422  104.952 1.00 27.60 ?  156  THR B N     1 
ATOM   10234 C CA    . THR B 1 158  ? -5.512  40.375  104.165 1.00 26.47 ?  156  THR B CA    1 
ATOM   10235 C C     . THR B 1 158  ? -4.076  39.877  104.133 1.00 28.53 ?  156  THR B C     1 
ATOM   10236 O O     . THR B 1 158  ? -3.485  39.641  105.190 1.00 30.00 ?  156  THR B O     1 
ATOM   10237 C CB    . THR B 1 158  ? -5.598  41.780  104.773 1.00 33.19 ?  156  THR B CB    1 
ATOM   10238 O OG1   . THR B 1 158  ? -6.966  42.088  105.083 1.00 33.47 ?  156  THR B OG1   1 
ATOM   10239 C CG2   . THR B 1 158  ? -5.051  42.820  103.803 1.00 35.80 ?  156  THR B CG2   1 
ATOM   10240 N N     . SER B 1 159  ? -3.515  39.723  102.925 1.00 25.17 ?  157  SER B N     1 
ATOM   10241 C CA    . SER B 1 159  ? -2.253  38.998  102.759 1.00 24.04 ?  157  SER B CA    1 
ATOM   10242 C C     . SER B 1 159  ? -1.074  39.722  103.408 1.00 26.28 ?  157  SER B C     1 
ATOM   10243 O O     . SER B 1 159  ? -0.155  39.080  103.931 1.00 25.44 ?  157  SER B O     1 
ATOM   10244 C CB    . SER B 1 159  ? -1.974  38.763  101.274 1.00 28.23 ?  157  SER B CB    1 
ATOM   10245 O OG    . SER B 1 159  ? -2.037  39.980  100.545 1.00 28.83 ?  157  SER B OG    1 
ATOM   10246 N N     . THR B 1 160  ? -1.046  41.045  103.341 1.00 23.69 ?  158  THR B N     1 
ATOM   10247 C CA    . THR B 1 160  ? -0.007  41.811  104.010 1.00 20.83 ?  158  THR B CA    1 
ATOM   10248 C C     . THR B 1 160  ? -0.667  42.755  105.002 1.00 19.47 ?  158  THR B C     1 
ATOM   10249 O O     . THR B 1 160  ? -1.889  42.911  105.037 1.00 23.08 ?  158  THR B O     1 
ATOM   10250 C CB    . THR B 1 160  ? 0.853   42.597  103.012 1.00 21.34 ?  158  THR B CB    1 
ATOM   10251 O OG1   . THR B 1 160  ? 0.002   43.458  102.256 1.00 25.06 ?  158  THR B OG1   1 
ATOM   10252 C CG2   . THR B 1 160  ? 1.600   41.658  102.076 1.00 28.81 ?  158  THR B CG2   1 
ATOM   10253 N N     . VAL B 1 161  ? 0.169   43.392  105.812 1.00 15.19 ?  159  VAL B N     1 
ATOM   10254 C CA    . VAL B 1 161  ? -0.260  44.096  107.014 1.00 17.77 ?  159  VAL B CA    1 
ATOM   10255 C C     . VAL B 1 161  ? -0.102  45.591  106.792 1.00 15.96 ?  159  VAL B C     1 
ATOM   10256 O O     . VAL B 1 161  ? 0.988   46.048  106.441 1.00 14.49 ?  159  VAL B O     1 
ATOM   10257 C CB    . VAL B 1 161  ? 0.581   43.626  108.215 1.00 20.33 ?  159  VAL B CB    1 
ATOM   10258 C CG1   . VAL B 1 161  ? 0.350   44.475  109.430 1.00 21.31 ?  159  VAL B CG1   1 
ATOM   10259 C CG2   . VAL B 1 161  ? 0.313   42.145  108.493 1.00 22.85 ?  159  VAL B CG2   1 
ATOM   10260 N N     . ASN B 1 162  ? -1.163  46.366  107.042 1.00 15.34 ?  160  ASN B N     1 
ATOM   10261 C CA    . ASN B 1 162  ? -1.003  47.818  106.998 1.00 14.76 ?  160  ASN B CA    1 
ATOM   10262 C C     . ASN B 1 162  ? -0.502  48.272  108.363 1.00 12.85 ?  160  ASN B C     1 
ATOM   10263 O O     . ASN B 1 162  ? -1.271  48.648  109.261 1.00 14.26 ?  160  ASN B O     1 
ATOM   10264 C CB    . ASN B 1 162  ? -2.290  48.524  106.598 1.00 15.49 ?  160  ASN B CB    1 
ATOM   10265 C CG    . ASN B 1 162  ? -2.084  50.021  106.415 1.00 15.48 ?  160  ASN B CG    1 
ATOM   10266 O OD1   . ASN B 1 162  ? -1.135  50.587  106.942 1.00 15.09 ?  160  ASN B OD1   1 
ATOM   10267 N ND2   . ASN B 1 162  ? -2.979  50.666  105.676 1.00 19.35 ?  160  ASN B ND2   1 
ATOM   10268 N N     . ASP B 1 163  ? 0.825   48.255  108.516 1.00 13.80 ?  161  ASP B N     1 
ATOM   10269 C CA    . ASP B 1 163  ? 1.414   48.531  109.814 1.00 14.46 ?  161  ASP B CA    1 
ATOM   10270 C C     . ASP B 1 163  ? 1.313   50.002  110.213 1.00 14.71 ?  161  ASP B C     1 
ATOM   10271 O O     . ASP B 1 163  ? 1.394   50.307  111.403 1.00 14.87 ?  161  ASP B O     1 
ATOM   10272 C CB    . ASP B 1 163  ? 2.868   48.034  109.859 1.00 15.58 ?  161  ASP B CB    1 
ATOM   10273 C CG    . ASP B 1 163  ? 3.724   48.517  108.689 1.00 17.65 ?  161  ASP B CG    1 
ATOM   10274 O OD1   . ASP B 1 163  ? 3.265   48.522  107.529 1.00 16.48 ?  161  ASP B OD1   1 
ATOM   10275 O OD2   . ASP B 1 163  ? 4.899   48.855  108.944 1.00 20.99 ?  161  ASP B OD2   1 
ATOM   10276 N N     . ARG B 1 164  ? 1.110   50.923  109.265 1.00 13.73 ?  162  ARG B N     1 
ATOM   10277 C CA    . ARG B 1 164  ? 0.870   52.305  109.661 1.00 13.83 ?  162  ARG B CA    1 
ATOM   10278 C C     . ARG B 1 164  ? -0.544  52.495  110.199 1.00 13.05 ?  162  ARG B C     1 
ATOM   10279 O O     . ARG B 1 164  ? -0.754  53.247  111.157 1.00 13.73 ?  162  ARG B O     1 
ATOM   10280 C CB    . ARG B 1 164  ? 1.122   53.260  108.489 1.00 13.74 ?  162  ARG B CB    1 
ATOM   10281 C CG    . ARG B 1 164  ? 2.586   53.324  108.035 1.00 14.17 ?  162  ARG B CG    1 
ATOM   10282 C CD    . ARG B 1 164  ? 3.571   53.361  109.204 1.00 18.39 ?  162  ARG B CD    1 
ATOM   10283 N NE    . ARG B 1 164  ? 3.344   54.457  110.133 1.00 24.58 ?  162  ARG B NE    1 
ATOM   10284 C CZ    . ARG B 1 164  ? 3.776   54.469  111.387 1.00 28.19 ?  162  ARG B CZ    1 
ATOM   10285 N NH1   . ARG B 1 164  ? 4.440   53.441  111.900 1.00 27.61 ?  162  ARG B NH1   1 
ATOM   10286 N NH2   . ARG B 1 164  ? 3.533   55.533  112.145 1.00 26.82 ?  162  ARG B NH2   1 
ATOM   10287 N N     . SER B 1 165  ? -1.521  51.823  109.574 1.00 13.75 ?  163  SER B N     1 
ATOM   10288 C CA    . SER B 1 165  ? -2.887  51.868  110.087 1.00 12.21 ?  163  SER B CA    1 
ATOM   10289 C C     . SER B 1 165  ? -2.979  51.219  111.462 1.00 12.49 ?  163  SER B C     1 
ATOM   10290 O O     . SER B 1 165  ? -3.671  51.727  112.344 1.00 12.91 ?  163  SER B O     1 
ATOM   10291 C CB    . SER B 1 165  ? -3.823  51.164  109.105 1.00 13.24 ?  163  SER B CB    1 
ATOM   10292 O OG    . SER B 1 165  ? -5.119  51.019  109.658 1.00 15.22 ?  163  SER B OG    1 
ATOM   10293 N N     . LEU B 1 166  ? -2.294  50.089  111.647 1.00 13.49 ?  164  LEU B N     1 
ATOM   10294 C CA    . LEU B 1 166  ? -2.325  49.411  112.941 1.00 13.03 ?  164  LEU B CA    1 
ATOM   10295 C C     . LEU B 1 166  ? -1.595  50.217  114.010 1.00 13.46 ?  164  LEU B C     1 
ATOM   10296 O O     . LEU B 1 166  ? -2.049  50.285  115.158 1.00 14.32 ?  164  LEU B O     1 
ATOM   10297 C CB    . LEU B 1 166  ? -1.729  48.010  112.808 1.00 13.84 ?  164  LEU B CB    1 
ATOM   10298 C CG    . LEU B 1 166  ? -2.621  47.066  111.995 1.00 15.98 ?  164  LEU B CG    1 
ATOM   10299 C CD1   . LEU B 1 166  ? -1.888  45.804  111.647 1.00 16.36 ?  164  LEU B CD1   1 
ATOM   10300 C CD2   . LEU B 1 166  ? -3.919  46.736  112.719 1.00 15.33 ?  164  LEU B CD2   1 
ATOM   10301 N N     . ALA B 1 167  ? -0.466  50.846  113.658 1.00 13.55 ?  165  ALA B N     1 
ATOM   10302 C CA    . ALA B 1 167  ? 0.204   51.693  114.642 1.00 14.83 ?  165  ALA B CA    1 
ATOM   10303 C C     . ALA B 1 167  ? -0.681  52.863  115.050 1.00 14.49 ?  165  ALA B C     1 
ATOM   10304 O O     . ALA B 1 167  ? -0.769  53.208  116.232 1.00 16.44 ?  165  ALA B O     1 
ATOM   10305 C CB    . ALA B 1 167  ? 1.534   52.201  114.098 1.00 16.11 ?  165  ALA B CB    1 
ATOM   10306 N N     . ALA B 1 168  ? -1.341  53.486  114.070 1.00 14.28 ?  166  ALA B N     1 
ATOM   10307 C CA    . ALA B 1 168  ? -2.268  54.567  114.377 1.00 13.75 ?  166  ALA B CA    1 
ATOM   10308 C C     . ALA B 1 168  ? -3.401  54.081  115.274 1.00 14.08 ?  166  ALA B C     1 
ATOM   10309 O O     . ALA B 1 168  ? -3.776  54.749  116.243 1.00 15.11 ?  166  ALA B O     1 
ATOM   10310 C CB    . ALA B 1 168  ? -2.819  55.146  113.068 1.00 15.04 ?  166  ALA B CB    1 
ATOM   10311 N N     . ALA B 1 169  ? -3.944  52.900  114.963 1.00 13.87 ?  167  ALA B N     1 
ATOM   10312 C CA    . ALA B 1 169  ? -5.055  52.353  115.737 1.00 14.21 ?  167  ALA B CA    1 
ATOM   10313 C C     . ALA B 1 169  ? -4.631  51.999  117.159 1.00 14.62 ?  167  ALA B C     1 
ATOM   10314 O O     . ALA B 1 169  ? -5.396  52.204  118.105 1.00 15.91 ?  167  ALA B O     1 
ATOM   10315 C CB    . ALA B 1 169  ? -5.616  51.119  115.039 1.00 14.27 ?  167  ALA B CB    1 
ATOM   10316 N N     . LEU B 1 170  ? -3.426  51.445  117.325 1.00 16.28 ?  168  LEU B N     1 
ATOM   10317 C CA    . LEU B 1 170  ? -2.986  51.086  118.669 1.00 14.82 ?  168  LEU B CA    1 
ATOM   10318 C C     . LEU B 1 170  ? -2.750  52.331  119.518 1.00 15.03 ?  168  LEU B C     1 
ATOM   10319 O O     . LEU B 1 170  ? -3.140  52.380  120.690 1.00 15.67 ?  168  LEU B O     1 
ATOM   10320 C CB    . LEU B 1 170  ? -1.728  50.230  118.593 1.00 16.26 ?  168  LEU B CB    1 
ATOM   10321 C CG    . LEU B 1 170  ? -1.251  49.701  119.947 1.00 16.26 ?  168  LEU B CG    1 
ATOM   10322 C CD1   . LEU B 1 170  ? -2.313  48.810  120.569 1.00 18.70 ?  168  LEU B CD1   1 
ATOM   10323 C CD2   . LEU B 1 170  ? 0.023   48.938  119.728 1.00 18.70 ?  168  LEU B CD2   1 
ATOM   10324 N N     . THR B 1 171  ? -2.124  53.353  118.936 1.00 15.20 ?  169  THR B N     1 
ATOM   10325 C CA    . THR B 1 171  ? -1.966  54.620  119.642 1.00 15.48 ?  169  THR B CA    1 
ATOM   10326 C C     . THR B 1 171  ? -3.320  55.197  120.035 1.00 15.78 ?  169  THR B C     1 
ATOM   10327 O O     . THR B 1 171  ? -3.513  55.652  121.169 1.00 16.33 ?  169  THR B O     1 
ATOM   10328 C CB    . THR B 1 171  ? -1.203  55.610  118.763 1.00 17.58 ?  169  THR B CB    1 
ATOM   10329 O OG1   . THR B 1 171  ? 0.114   55.105  118.506 1.00 21.28 ?  169  THR B OG1   1 
ATOM   10330 C CG2   . THR B 1 171  ? -1.105  56.956  119.439 1.00 18.68 ?  169  THR B CG2   1 
ATOM   10331 N N     . ARG B 1 172  ? -4.277  55.164  119.104 1.00 15.62 ?  170  ARG B N     1 
ATOM   10332 C CA    . ARG B 1 172  ? -5.593  55.717  119.381 1.00 16.06 ?  170  ARG B CA    1 
ATOM   10333 C C     . ARG B 1 172  ? -6.264  54.980  120.528 1.00 16.44 ?  170  ARG B C     1 
ATOM   10334 O O     . ARG B 1 172  ? -6.801  55.602  121.448 1.00 17.05 ?  170  ARG B O     1 
ATOM   10335 C CB    . ARG B 1 172  ? -6.462  55.644  118.126 1.00 16.84 ?  170  ARG B CB    1 
ATOM   10336 C CG    . ARG B 1 172  ? -7.665  56.561  118.216 1.00 16.25 ?  170  ARG B CG    1 
ATOM   10337 C CD    . ARG B 1 172  ? -8.574  56.396  116.987 1.00 16.02 ?  170  ARG B CD    1 
ATOM   10338 N NE    . ARG B 1 172  ? -7.845  56.507  115.728 1.00 15.48 ?  170  ARG B NE    1 
ATOM   10339 C CZ    . ARG B 1 172  ? -7.538  55.476  114.950 1.00 14.98 ?  170  ARG B CZ    1 
ATOM   10340 N NH1   . ARG B 1 172  ? -7.892  54.243  115.264 1.00 16.08 ?  170  ARG B NH1   1 
ATOM   10341 N NH2   . ARG B 1 172  ? -6.861  55.686  113.825 1.00 14.55 ?  170  ARG B NH2   1 
ATOM   10342 N N     . LEU B 1 173  ? -6.249  53.641  120.483 1.00 17.30 ?  171  LEU B N     1 
ATOM   10343 C CA    . LEU B 1 173  ? -7.000  52.909  121.497 1.00 16.57 ?  171  LEU B CA    1 
ATOM   10344 C C     . LEU B 1 173  ? -6.349  53.018  122.871 1.00 16.95 ?  171  LEU B C     1 
ATOM   10345 O O     . LEU B 1 173  ? -7.055  53.051  123.880 1.00 18.34 ?  171  LEU B O     1 
ATOM   10346 C CB    . LEU B 1 173  ? -7.172  51.444  121.086 1.00 16.87 ?  171  LEU B CB    1 
ATOM   10347 C CG    . LEU B 1 173  ? -6.005  50.446  121.085 1.00 17.93 ?  171  LEU B CG    1 
ATOM   10348 C CD1   . LEU B 1 173  ? -5.920  49.785  122.478 1.00 18.93 ?  171  LEU B CD1   1 
ATOM   10349 C CD2   . LEU B 1 173  ? -6.208  49.398  120.052 1.00 19.98 ?  171  LEU B CD2   1 
ATOM   10350 N N     . ILE B 1 174  ? -5.017  53.070  122.934 1.00 18.40 ?  172  ILE B N     1 
ATOM   10351 C CA    . ILE B 1 174  ? -4.369  53.194  124.238 1.00 17.11 ?  172  ILE B CA    1 
ATOM   10352 C C     . ILE B 1 174  ? -4.567  54.592  124.807 1.00 19.16 ?  172  ILE B C     1 
ATOM   10353 O O     . ILE B 1 174  ? -4.830  54.759  126.005 1.00 20.26 ?  172  ILE B O     1 
ATOM   10354 C CB    . ILE B 1 174  ? -2.877  52.837  124.139 1.00 16.76 ?  172  ILE B CB    1 
ATOM   10355 C CG1   . ILE B 1 174  ? -2.694  51.361  123.807 1.00 17.71 ?  172  ILE B CG1   1 
ATOM   10356 C CG2   . ILE B 1 174  ? -2.182  53.150  125.463 1.00 19.01 ?  172  ILE B CG2   1 
ATOM   10357 C CD1   . ILE B 1 174  ? -1.258  50.964  123.524 1.00 19.36 ?  172  ILE B CD1   1 
ATOM   10358 N N     . SER B 1 175  ? -4.415  55.622  123.967 1.00 18.73 ?  173  SER B N     1 
ATOM   10359 C CA    . SER B 1 175  ? -4.649  56.979  124.438 1.00 18.98 ?  173  SER B CA    1 
ATOM   10360 C C     . SER B 1 175  ? -6.103  57.190  124.845 1.00 18.42 ?  173  SER B C     1 
ATOM   10361 O O     . SER B 1 175  ? -6.387  58.054  125.679 1.00 21.81 ?  173  SER B O     1 
ATOM   10362 C CB    . SER B 1 175  ? -4.234  57.992  123.365 1.00 21.52 ?  173  SER B CB    1 
ATOM   10363 O OG    . SER B 1 175  ? -2.835  57.939  123.143 1.00 24.82 ?  173  SER B OG    1 
ATOM   10364 N N     . ARG B 1 176  ? -7.032  56.424  124.264 1.00 18.30 ?  174  ARG B N     1 
ATOM   10365 C CA    . ARG B 1 176  ? -8.444  56.567  124.613 1.00 18.81 ?  174  ARG B CA    1 
ATOM   10366 C C     . ARG B 1 176  ? -8.809  55.772  125.869 1.00 21.47 ?  174  ARG B C     1 
ATOM   10367 O O     . ARG B 1 176  ? -9.529  56.277  126.735 1.00 22.52 ?  174  ARG B O     1 
ATOM   10368 C CB    . ARG B 1 176  ? -9.304  56.128  123.417 1.00 20.67 ?  174  ARG B CB    1 
ATOM   10369 C CG    . ARG B 1 176  ? -10.808 56.402  123.561 1.00 21.86 ?  174  ARG B CG    1 
ATOM   10370 C CD    . ARG B 1 176  ? -11.521 56.072  122.225 1.00 20.03 ?  174  ARG B CD    1 
ATOM   10371 N NE    . ARG B 1 176  ? -11.680 54.640  121.988 1.00 22.91 ?  174  ARG B NE    1 
ATOM   10372 C CZ    . ARG B 1 176  ? -11.140 53.941  120.991 1.00 22.48 ?  174  ARG B CZ    1 
ATOM   10373 N NH1   . ARG B 1 176  ? -10.431 54.516  120.008 1.00 19.33 ?  174  ARG B NH1   1 
ATOM   10374 N NH2   . ARG B 1 176  ? -11.325 52.623  120.956 1.00 27.23 ?  174  ARG B NH2   1 
ATOM   10375 N N     . CYS B 1 177  ? -8.326  54.527  125.980 1.00 20.46 ?  175  CYS B N     1 
ATOM   10376 C CA    . CYS B 1 177  ? -8.830  53.602  126.985 1.00 22.17 ?  175  CYS B CA    1 
ATOM   10377 C C     . CYS B 1 177  ? -7.792  53.144  127.998 1.00 25.19 ?  175  CYS B C     1 
ATOM   10378 O O     . CYS B 1 177  ? -8.179  52.603  129.041 1.00 25.30 ?  175  CYS B O     1 
ATOM   10379 C CB    . CYS B 1 177  ? -9.435  52.357  126.316 1.00 22.47 ?  175  CYS B CB    1 
ATOM   10380 S SG    . CYS B 1 177  ? -10.706 52.735  125.065 1.00 29.26 ?  175  CYS B SG    1 
ATOM   10381 N N     . GLY B 1 178  ? -6.501  53.314  127.722 1.00 23.47 ?  176  GLY B N     1 
ATOM   10382 C CA    . GLY B 1 178  ? -5.519  53.088  128.773 1.00 23.58 ?  176  GLY B CA    1 
ATOM   10383 C C     . GLY B 1 178  ? -5.313  51.630  129.165 1.00 22.44 ?  176  GLY B C     1 
ATOM   10384 O O     . GLY B 1 178  ? -5.581  50.693  128.414 1.00 22.64 ?  176  GLY B O     1 
ATOM   10385 N N     . GLU B 1 179  ? -4.804  51.458  130.384 1.00 23.29 ?  177  GLU B N     1 
ATOM   10386 C CA    . GLU B 1 179  ? -4.494  50.121  130.883 1.00 23.87 ?  177  GLU B CA    1 
ATOM   10387 C C     . GLU B 1 179  ? -5.671  49.151  130.857 1.00 21.48 ?  177  GLU B C     1 
ATOM   10388 O O     . GLU B 1 179  ? -5.443  47.970  130.546 1.00 22.41 ?  177  GLU B O     1 
ATOM   10389 C CB    . GLU B 1 179  ? -3.928  50.222  132.313 1.00 24.81 ?  177  GLU B CB    1 
ATOM   10390 C CG    . GLU B 1 179  ? -3.447  48.887  132.904 1.00 30.80 ?  177  GLU B CG    1 
ATOM   10391 C CD    . GLU B 1 179  ? -4.524  48.135  133.693 1.00 37.02 ?  177  GLU B CD    1 
ATOM   10392 O OE1   . GLU B 1 179  ? -5.594  48.724  133.975 1.00 37.31 ?  177  GLU B OE1   1 
ATOM   10393 O OE2   . GLU B 1 179  ? -4.294  46.949  134.040 1.00 40.16 ?  177  GLU B OE2   1 
ATOM   10394 N N     . PRO B 1 180  ? -6.912  49.537  131.187 1.00 22.68 ?  178  PRO B N     1 
ATOM   10395 C CA    . PRO B 1 180  ? -7.979  48.520  131.213 1.00 23.97 ?  178  PRO B CA    1 
ATOM   10396 C C     . PRO B 1 180  ? -8.151  47.774  129.895 1.00 23.60 ?  178  PRO B C     1 
ATOM   10397 O O     . PRO B 1 180  ? -8.366  46.555  129.907 1.00 25.25 ?  178  PRO B O     1 
ATOM   10398 C CB    . PRO B 1 180  ? -9.221  49.337  131.589 1.00 25.55 ?  178  PRO B CB    1 
ATOM   10399 C CG    . PRO B 1 180  ? -8.673  50.427  132.467 1.00 25.24 ?  178  PRO B CG    1 
ATOM   10400 C CD    . PRO B 1 180  ? -7.362  50.803  131.799 1.00 25.76 ?  178  PRO B CD    1 
ATOM   10401 N N     . VAL B 1 181  ? -8.045  48.449  128.746 1.00 21.82 ?  179  VAL B N     1 
ATOM   10402 C CA    . VAL B 1 181  ? -8.215  47.712  127.498 1.00 23.59 ?  179  VAL B CA    1 
ATOM   10403 C C     . VAL B 1 181  ? -7.002  46.825  127.207 1.00 19.63 ?  179  VAL B C     1 
ATOM   10404 O O     . VAL B 1 181  ? -7.140  45.751  126.605 1.00 21.47 ?  179  VAL B O     1 
ATOM   10405 C CB    . VAL B 1 181  ? -8.512  48.677  126.328 1.00 22.56 ?  179  VAL B CB    1 
ATOM   10406 C CG1   . VAL B 1 181  ? -7.263  49.442  125.878 1.00 19.62 ?  179  VAL B CG1   1 
ATOM   10407 C CG2   . VAL B 1 181  ? -9.115  47.918  125.153 1.00 24.21 ?  179  VAL B CG2   1 
ATOM   10408 N N     . ILE B 1 182  ? -5.800  47.250  127.615 1.00 20.71 ?  180  ILE B N     1 
ATOM   10409 C CA    . ILE B 1 182  ? -4.623  46.400  127.436 1.00 19.51 ?  180  ILE B CA    1 
ATOM   10410 C C     . ILE B 1 182  ? -4.764  45.138  128.275 1.00 21.84 ?  180  ILE B C     1 
ATOM   10411 O O     . ILE B 1 182  ? -4.487  44.023  127.810 1.00 21.96 ?  180  ILE B O     1 
ATOM   10412 C CB    . ILE B 1 182  ? -3.339  47.176  127.791 1.00 20.26 ?  180  ILE B CB    1 
ATOM   10413 C CG1   . ILE B 1 182  ? -3.163  48.391  126.876 1.00 21.67 ?  180  ILE B CG1   1 
ATOM   10414 C CG2   . ILE B 1 182  ? -2.109  46.257  127.696 1.00 21.16 ?  180  ILE B CG2   1 
ATOM   10415 C CD1   . ILE B 1 182  ? -2.144  49.398  127.403 1.00 22.42 ?  180  ILE B CD1   1 
ATOM   10416 N N     . ARG B 1 183  ? -5.211  45.302  129.523 1.00 23.12 ?  181  ARG B N     1 
ATOM   10417 C CA    . ARG B 1 183  ? -5.469  44.170  130.407 1.00 25.29 ?  181  ARG B CA    1 
ATOM   10418 C C     . ARG B 1 183  ? -6.442  43.183  129.777 1.00 26.07 ?  181  ARG B C     1 
ATOM   10419 O O     . ARG B 1 183  ? -6.166  41.980  129.700 1.00 26.22 ?  181  ARG B O     1 
ATOM   10420 C CB    . ARG B 1 183  ? -6.016  44.691  131.733 1.00 25.98 ?  181  ARG B CB    1 
ATOM   10421 C CG    . ARG B 1 183  ? -6.292  43.637  132.781 1.00 30.92 ?  181  ARG B CG    1 
ATOM   10422 C CD    . ARG B 1 183  ? -5.001  43.188  133.409 1.00 35.50 ?  181  ARG B CD    1 
ATOM   10423 N NE    . ARG B 1 183  ? -4.484  41.993  132.762 1.00 31.38 ?  181  ARG B NE    1 
ATOM   10424 C CZ    . ARG B 1 183  ? -3.197  41.686  132.683 1.00 36.22 ?  181  ARG B CZ    1 
ATOM   10425 N NH1   . ARG B 1 183  ? -2.261  42.502  133.145 1.00 34.07 ?  181  ARG B NH1   1 
ATOM   10426 N NH2   . ARG B 1 183  ? -2.841  40.531  132.131 1.00 31.97 ?  181  ARG B NH2   1 
ATOM   10427 N N     . ARG B 1 184  ? -7.585  43.683  129.300 1.00 24.90 ?  182  ARG B N     1 
ATOM   10428 C CA    . ARG B 1 184  ? -8.575  42.815  128.668 1.00 26.49 ?  182  ARG B CA    1 
ATOM   10429 C C     . ARG B 1 184  ? -8.018  42.134  127.422 1.00 26.12 ?  182  ARG B C     1 
ATOM   10430 O O     . ARG B 1 184  ? -8.309  40.960  127.165 1.00 26.67 ?  182  ARG B O     1 
ATOM   10431 C CB    . ARG B 1 184  ? -9.832  43.620  128.337 1.00 26.51 ?  182  ARG B CB    1 
ATOM   10432 C CG    . ARG B 1 184  ? -10.655 43.994  129.558 1.00 31.23 ?  182  ARG B CG    1 
ATOM   10433 C CD    . ARG B 1 184  ? -11.711 42.939  129.856 1.00 34.31 ?  182  ARG B CD    1 
ATOM   10434 N NE    . ARG B 1 184  ? -12.891 43.086  129.008 1.00 33.02 ?  182  ARG B NE    1 
ATOM   10435 C CZ    . ARG B 1 184  ? -13.305 42.188  128.125 1.00 33.99 ?  182  ARG B CZ    1 
ATOM   10436 N NH1   . ARG B 1 184  ? -12.650 41.053  127.931 1.00 34.20 ?  182  ARG B NH1   1 
ATOM   10437 N NH2   . ARG B 1 184  ? -14.407 42.431  127.419 1.00 33.03 ?  182  ARG B NH2   1 
ATOM   10438 N N     . GLY B 1 185  ? -7.220  42.849  126.626 1.00 22.02 ?  183  GLY B N     1 
ATOM   10439 C CA    . GLY B 1 185  ? -6.633  42.226  125.451 1.00 21.16 ?  183  GLY B CA    1 
ATOM   10440 C C     . GLY B 1 185  ? -5.658  41.119  125.806 1.00 23.10 ?  183  GLY B C     1 
ATOM   10441 O O     . GLY B 1 185  ? -5.668  40.053  125.188 1.00 22.33 ?  183  GLY B O     1 
ATOM   10442 N N     . VAL B 1 186  ? -4.810  41.354  126.816 1.00 22.33 ?  184  VAL B N     1 
ATOM   10443 C CA    . VAL B 1 186  ? -3.835  40.347  127.235 1.00 24.97 ?  184  VAL B CA    1 
ATOM   10444 C C     . VAL B 1 186  ? -4.546  39.098  127.740 1.00 23.94 ?  184  VAL B C     1 
ATOM   10445 O O     . VAL B 1 186  ? -4.200  37.971  127.365 1.00 23.95 ?  184  VAL B O     1 
ATOM   10446 C CB    . VAL B 1 186  ? -2.890  40.926  128.303 1.00 24.57 ?  184  VAL B CB    1 
ATOM   10447 C CG1   . VAL B 1 186  ? -2.111  39.807  129.006 1.00 24.12 ?  184  VAL B CG1   1 
ATOM   10448 C CG2   . VAL B 1 186  ? -1.944  41.921  127.663 1.00 23.02 ?  184  VAL B CG2   1 
ATOM   10449 N N     . ASP B 1 187  ? -5.566  39.284  128.577 1.00 24.65 ?  185  ASP B N     1 
ATOM   10450 C CA    . ASP B 1 187  ? -6.299  38.142  129.111 1.00 26.06 ?  185  ASP B CA    1 
ATOM   10451 C C     . ASP B 1 187  ? -7.016  37.383  128.006 1.00 26.82 ?  185  ASP B C     1 
ATOM   10452 O O     . ASP B 1 187  ? -7.063  36.148  128.025 1.00 27.76 ?  185  ASP B O     1 
ATOM   10453 C CB    . ASP B 1 187  ? -7.286  38.611  130.176 1.00 25.24 ?  185  ASP B CB    1 
ATOM   10454 C CG    . ASP B 1 187  ? -6.587  39.194  131.405 1.00 31.15 ?  185  ASP B CG    1 
ATOM   10455 O OD1   . ASP B 1 187  ? -5.375  38.937  131.576 1.00 33.94 ?  185  ASP B OD1   1 
ATOM   10456 O OD2   . ASP B 1 187  ? -7.235  39.910  132.197 1.00 31.16 ?  185  ASP B OD2   1 
ATOM   10457 N N     . MET B 1 188  ? -7.559  38.104  127.020 1.00 26.06 ?  186  MET B N     1 
ATOM   10458 C CA    . MET B 1 188  ? -8.271  37.460  125.919 1.00 25.53 ?  186  MET B CA    1 
ATOM   10459 C C     . MET B 1 188  ? -7.324  36.640  125.047 1.00 25.84 ?  186  MET B C     1 
ATOM   10460 O O     . MET B 1 188  ? -7.629  35.496  124.683 1.00 28.47 ?  186  MET B O     1 
ATOM   10461 C CB    . MET B 1 188  ? -8.995  38.517  125.088 1.00 25.62 ?  186  MET B CB    1 
ATOM   10462 C CG    . MET B 1 188  ? -9.817  37.965  123.944 1.00 31.41 ?  186  MET B CG    1 
ATOM   10463 S SD    . MET B 1 188  ? -11.118 36.870  124.537 1.00 39.87 ?  186  MET B SD    1 
ATOM   10464 C CE    . MET B 1 188  ? -11.858 37.870  125.834 1.00 38.91 ?  186  MET B CE    1 
ATOM   10465 N N     . ALA B 1 189  ? -6.178  37.214  124.679 1.00 25.93 ?  187  ALA B N     1 
ATOM   10466 C CA    . ALA B 1 189  ? -5.217  36.469  123.876 1.00 25.50 ?  187  ALA B CA    1 
ATOM   10467 C C     . ALA B 1 189  ? -4.663  35.281  124.648 1.00 25.34 ?  187  ALA B C     1 
ATOM   10468 O O     . ALA B 1 189  ? -4.425  34.215  124.069 1.00 26.05 ?  187  ALA B O     1 
ATOM   10469 C CB    . ALA B 1 189  ? -4.087  37.390  123.418 1.00 25.43 ?  187  ALA B CB    1 
ATOM   10470 N N     . MET B 1 190  ? -4.446  35.449  125.952 1.00 23.42 ?  188  MET B N     1 
ATOM   10471 C CA    . MET B 1 190  ? -3.960  34.338  126.766 1.00 25.73 ?  188  MET B CA    1 
ATOM   10472 C C     . MET B 1 190  ? -4.923  33.157  126.713 1.00 27.83 ?  188  MET B C     1 
ATOM   10473 O O     . MET B 1 190  ? -4.502  32.007  126.530 1.00 28.32 ?  188  MET B O     1 
ATOM   10474 C CB    . MET B 1 190  ? -3.757  34.805  128.203 1.00 26.84 ?  188  MET B CB    1 
ATOM   10475 C CG    . MET B 1 190  ? -3.024  33.814  129.080 1.00 31.01 ?  188  MET B CG    1 
ATOM   10476 S SD    . MET B 1 190  ? -2.969  34.357  130.800 1.00 37.28 ?  188  MET B SD    1 
ATOM   10477 C CE    . MET B 1 190  ? -2.043  35.884  130.668 1.00 28.80 ?  188  MET B CE    1 
ATOM   10478 N N     . ARG B 1 191  ? -6.224  33.428  126.848 1.00 26.03 ?  189  ARG B N     1 
ATOM   10479 C CA    . ARG B 1 191  ? -7.221  32.365  126.777 1.00 28.25 ?  189  ARG B CA    1 
ATOM   10480 C C     . ARG B 1 191  ? -7.249  31.727  125.391 1.00 27.38 ?  189  ARG B C     1 
ATOM   10481 O O     . ARG B 1 191  ? -7.216  30.497  125.259 1.00 28.31 ?  189  ARG B O     1 
ATOM   10482 C CB    . ARG B 1 191  ? -8.597  32.922  127.147 1.00 30.18 ?  189  ARG B CB    1 
ATOM   10483 C CG    . ARG B 1 191  ? -9.675  31.865  127.313 1.00 37.40 ?  189  ARG B CG    1 
ATOM   10484 C CD    . ARG B 1 191  ? -10.991 32.477  127.787 1.00 43.54 ?  189  ARG B CD    1 
ATOM   10485 N NE    . ARG B 1 191  ? -11.687 33.205  126.729 1.00 47.58 ?  189  ARG B NE    1 
ATOM   10486 C CZ    . ARG B 1 191  ? -12.878 33.776  126.868 1.00 48.85 ?  189  ARG B CZ    1 
ATOM   10487 N NH1   . ARG B 1 191  ? -13.535 33.734  128.017 1.00 53.36 ?  189  ARG B NH1   1 
ATOM   10488 N NH2   . ARG B 1 191  ? -13.426 34.399  125.828 1.00 51.11 ?  189  ARG B NH2   1 
ATOM   10489 N N     . MET B 1 192  ? -7.309  32.548  124.339 1.00 26.16 ?  190  MET B N     1 
ATOM   10490 C CA    . MET B 1 192  ? -7.422  31.993  122.995 1.00 26.23 ?  190  MET B CA    1 
ATOM   10491 C C     . MET B 1 192  ? -6.201  31.153  122.650 1.00 24.57 ?  190  MET B C     1 
ATOM   10492 O O     . MET B 1 192  ? -6.325  30.035  122.135 1.00 25.63 ?  190  MET B O     1 
ATOM   10493 C CB    . MET B 1 192  ? -7.618  33.113  121.970 1.00 26.92 ?  190  MET B CB    1 
ATOM   10494 C CG    . MET B 1 192  ? -8.868  33.932  122.220 1.00 28.36 ?  190  MET B CG    1 
ATOM   10495 S SD    . MET B 1 192  ? -9.165  35.162  120.943 1.00 40.16 ?  190  MET B SD    1 
ATOM   10496 C CE    . MET B 1 192  ? -9.603  34.082  119.592 1.00 32.86 ?  190  MET B CE    1 
ATOM   10497 N N     . MET B 1 193  ? -5.008  31.673  122.934 1.00 24.05 ?  191  MET B N     1 
ATOM   10498 C CA    . MET B 1 193  ? -3.791  30.972  122.550 1.00 24.77 ?  191  MET B CA    1 
ATOM   10499 C C     . MET B 1 193  ? -3.424  29.845  123.506 1.00 28.32 ?  191  MET B C     1 
ATOM   10500 O O     . MET B 1 193  ? -2.597  28.994  123.150 1.00 27.41 ?  191  MET B O     1 
ATOM   10501 C CB    . MET B 1 193  ? -2.632  31.964  122.453 1.00 26.32 ?  191  MET B CB    1 
ATOM   10502 C CG    . MET B 1 193  ? -2.810  32.969  121.336 1.00 27.35 ?  191  MET B CG    1 
ATOM   10503 S SD    . MET B 1 193  ? -1.251  33.766  120.921 1.00 38.44 ?  191  MET B SD    1 
ATOM   10504 C CE    . MET B 1 193  ? -1.323  35.153  122.010 1.00 28.92 ?  191  MET B CE    1 
ATOM   10505 N N     . GLY B 1 194  ? -4.020  29.806  124.692 1.00 25.74 ?  192  GLY B N     1 
ATOM   10506 C CA    . GLY B 1 194  ? -3.690  28.769  125.648 1.00 27.82 ?  192  GLY B CA    1 
ATOM   10507 C C     . GLY B 1 194  ? -4.743  27.687  125.769 1.00 29.14 ?  192  GLY B C     1 
ATOM   10508 O O     . GLY B 1 194  ? -4.442  26.575  126.219 1.00 28.00 ?  192  GLY B O     1 
ATOM   10509 N N     . GLU B 1 195  ? -5.982  27.994  125.374 1.00 25.55 ?  193  GLU B N     1 
ATOM   10510 C CA    . GLU B 1 195  ? -7.112  27.104  125.630 1.00 26.05 ?  193  GLU B CA    1 
ATOM   10511 C C     . GLU B 1 195  ? -8.038  26.889  124.447 1.00 25.47 ?  193  GLU B C     1 
ATOM   10512 O O     . GLU B 1 195  ? -8.796  25.914  124.463 1.00 25.50 ?  193  GLU B O     1 
ATOM   10513 C CB    . GLU B 1 195  ? -7.957  27.627  126.801 1.00 29.48 ?  193  GLU B CB    1 
ATOM   10514 C CG    . GLU B 1 195  ? -7.190  27.779  128.092 1.00 33.89 ?  193  GLU B CG    1 
ATOM   10515 C CD    . GLU B 1 195  ? -7.985  28.519  129.146 1.00 39.49 ?  193  GLU B CD    1 
ATOM   10516 O OE1   . GLU B 1 195  ? -9.234  28.505  129.077 1.00 42.80 ?  193  GLU B OE1   1 
ATOM   10517 O OE2   . GLU B 1 195  ? -7.353  29.122  130.037 1.00 45.16 ?  193  GLU B OE2   1 
ATOM   10518 N N     . GLN B 1 196  ? -8.016  27.749  123.431 1.00 27.33 ?  194  GLN B N     1 
ATOM   10519 C CA    . GLN B 1 196  ? -8.912  27.624  122.289 1.00 26.26 ?  194  GLN B CA    1 
ATOM   10520 C C     . GLN B 1 196  ? -8.185  27.133  121.043 1.00 26.52 ?  194  GLN B C     1 
ATOM   10521 O O     . GLN B 1 196  ? -8.569  26.113  120.461 1.00 27.50 ?  194  GLN B O     1 
ATOM   10522 C CB    . GLN B 1 196  ? -9.607  28.967  122.025 1.00 27.63 ?  194  GLN B CB    1 
ATOM   10523 C CG    . GLN B 1 196  ? -10.540 28.974  120.822 1.00 35.10 ?  194  GLN B CG    1 
ATOM   10524 C CD    . GLN B 1 196  ? -11.160 30.343  120.598 1.00 35.73 ?  194  GLN B CD    1 
ATOM   10525 O OE1   . GLN B 1 196  ? -11.257 31.152  121.529 1.00 43.06 ?  194  GLN B OE1   1 
ATOM   10526 N NE2   . GLN B 1 196  ? -11.575 30.614  119.366 1.00 40.63 ?  194  GLN B NE2   1 
ATOM   10527 N N     . PHE B 1 197  ? -7.129  27.826  120.620 1.00 25.09 ?  195  PHE B N     1 
ATOM   10528 C CA    . PHE B 1 197  ? -6.374  27.374  119.459 1.00 24.15 ?  195  PHE B CA    1 
ATOM   10529 C C     . PHE B 1 197  ? -5.559  26.124  119.761 1.00 23.33 ?  195  PHE B C     1 
ATOM   10530 O O     . PHE B 1 197  ? -5.143  25.427  118.827 1.00 25.84 ?  195  PHE B O     1 
ATOM   10531 C CB    . PHE B 1 197  ? -5.465  28.498  118.962 1.00 26.78 ?  195  PHE B CB    1 
ATOM   10532 C CG    . PHE B 1 197  ? -6.217  29.718  118.497 1.00 26.65 ?  195  PHE B CG    1 
ATOM   10533 C CD1   . PHE B 1 197  ? -7.405  29.585  117.792 1.00 31.69 ?  195  PHE B CD1   1 
ATOM   10534 C CD2   . PHE B 1 197  ? -5.741  30.992  118.772 1.00 30.29 ?  195  PHE B CD2   1 
ATOM   10535 C CE1   . PHE B 1 197  ? -8.103  30.699  117.358 1.00 32.35 ?  195  PHE B CE1   1 
ATOM   10536 C CE2   . PHE B 1 197  ? -6.443  32.117  118.341 1.00 28.27 ?  195  PHE B CE2   1 
ATOM   10537 C CZ    . PHE B 1 197  ? -7.621  31.964  117.636 1.00 33.78 ?  195  PHE B CZ    1 
ATOM   10538 N N     . VAL B 1 198  ? -5.310  25.844  121.039 1.00 23.88 ?  196  VAL B N     1 
ATOM   10539 C CA    . VAL B 1 198  ? -4.678  24.609  121.480 1.00 23.39 ?  196  VAL B CA    1 
ATOM   10540 C C     . VAL B 1 198  ? -5.465  24.089  122.669 1.00 22.09 ?  196  VAL B C     1 
ATOM   10541 O O     . VAL B 1 198  ? -6.062  24.856  123.433 1.00 25.01 ?  196  VAL B O     1 
ATOM   10542 C CB    . VAL B 1 198  ? -3.184  24.777  121.868 1.00 23.52 ?  196  VAL B CB    1 
ATOM   10543 C CG1   . VAL B 1 198  ? -2.352  25.260  120.694 1.00 24.29 ?  196  VAL B CG1   1 
ATOM   10544 C CG2   . VAL B 1 198  ? -3.028  25.698  123.087 1.00 25.23 ?  196  VAL B CG2   1 
ATOM   10545 N N     . THR B 1 199  ? -5.456  22.770  122.833 1.00 22.59 ?  197  THR B N     1 
ATOM   10546 C CA    . THR B 1 199  ? -6.012  22.191  124.049 1.00 22.07 ?  197  THR B CA    1 
ATOM   10547 C C     . THR B 1 199  ? -5.116  22.477  125.244 1.00 23.07 ?  197  THR B C     1 
ATOM   10548 O O     . THR B 1 199  ? -5.601  22.630  126.373 1.00 26.01 ?  197  THR B O     1 
ATOM   10549 C CB    . THR B 1 199  ? -6.207  20.692  123.847 1.00 21.81 ?  197  THR B CB    1 
ATOM   10550 O OG1   . THR B 1 199  ? -6.983  20.497  122.658 1.00 25.92 ?  197  THR B OG1   1 
ATOM   10551 C CG2   . THR B 1 199  ? -6.951  20.085  125.016 1.00 26.57 ?  197  THR B CG2   1 
ATOM   10552 N N     . GLY B 1 200  ? -3.817  22.565  125.007 1.00 22.89 ?  198  GLY B N     1 
ATOM   10553 C CA    . GLY B 1 200  ? -2.875  22.954  126.030 1.00 23.15 ?  198  GLY B CA    1 
ATOM   10554 C C     . GLY B 1 200  ? -1.542  23.269  125.394 1.00 19.88 ?  198  GLY B C     1 
ATOM   10555 O O     . GLY B 1 200  ? -1.277  22.901  124.245 1.00 21.36 ?  198  GLY B O     1 
ATOM   10556 N N     . GLU B 1 201  ? -0.701  23.959  126.165 1.00 25.51 ?  199  GLU B N     1 
ATOM   10557 C CA    . GLU B 1 201  ? 0.620   24.318  125.660 1.00 25.46 ?  199  GLU B CA    1 
ATOM   10558 C C     . GLU B 1 201  ? 1.548   23.113  125.615 1.00 23.09 ?  199  GLU B C     1 
ATOM   10559 O O     . GLU B 1 201  ? 2.374   22.998  124.698 1.00 25.92 ?  199  GLU B O     1 
ATOM   10560 C CB    . GLU B 1 201  ? 1.231   25.413  126.528 1.00 28.58 ?  199  GLU B CB    1 
ATOM   10561 C CG    . GLU B 1 201  ? 2.462   26.031  125.906 1.00 31.91 ?  199  GLU B CG    1 
ATOM   10562 C CD    . GLU B 1 201  ? 3.230   26.902  126.872 1.00 35.48 ?  199  GLU B CD    1 
ATOM   10563 O OE1   . GLU B 1 201  ? 2.870   26.932  128.070 1.00 35.94 ?  199  GLU B OE1   1 
ATOM   10564 O OE2   . GLU B 1 201  ? 4.198   27.553  126.425 1.00 40.00 ?  199  GLU B OE2   1 
ATOM   10565 N N     . THR B 1 202  ? 1.408   22.206  126.573 1.00 22.79 ?  200  THR B N     1 
ATOM   10566 C CA    . THR B 1 202  ? 2.184   20.979  126.679 1.00 22.75 ?  200  THR B CA    1 
ATOM   10567 C C     . THR B 1 202  ? 1.237   19.786  126.691 1.00 26.31 ?  200  THR B C     1 
ATOM   10568 O O     . THR B 1 202  ? 0.038   19.923  126.942 1.00 25.08 ?  200  THR B O     1 
ATOM   10569 C CB    . THR B 1 202  ? 3.028   20.966  127.958 1.00 25.87 ?  200  THR B CB    1 
ATOM   10570 O OG1   . THR B 1 202  ? 2.159   20.945  129.100 1.00 25.77 ?  200  THR B OG1   1 
ATOM   10571 C CG2   . THR B 1 202  ? 3.907   22.204  128.042 1.00 31.45 ?  200  THR B CG2   1 
ATOM   10572 N N     . ILE B 1 203  ? 1.798   18.596  126.472 1.00 22.84 ?  201  ILE B N     1 
ATOM   10573 C CA    . ILE B 1 203  ? 0.959   17.403  126.508 1.00 26.35 ?  201  ILE B CA    1 
ATOM   10574 C C     . ILE B 1 203  ? 0.421   17.159  127.914 1.00 23.94 ?  201  ILE B C     1 
ATOM   10575 O O     . ILE B 1 203  ? -0.703  16.669  128.071 1.00 23.57 ?  201  ILE B O     1 
ATOM   10576 C CB    . ILE B 1 203  ? 1.718   16.179  125.960 1.00 23.60 ?  201  ILE B CB    1 
ATOM   10577 C CG1   . ILE B 1 203  ? 0.745   15.022  125.687 1.00 23.13 ?  201  ILE B CG1   1 
ATOM   10578 C CG2   . ILE B 1 203  ? 2.801   15.737  126.925 1.00 22.43 ?  201  ILE B CG2   1 
ATOM   10579 C CD1   . ILE B 1 203  ? -0.270  15.327  124.588 1.00 22.06 ?  201  ILE B CD1   1 
ATOM   10580 N N     . ARG B 1 204  ? 1.183   17.508  128.962 1.00 21.52 ?  202  ARG B N     1 
ATOM   10581 C CA    . ARG B 1 204  ? 0.664   17.349  130.316 1.00 25.92 ?  202  ARG B CA    1 
ATOM   10582 C C     . ARG B 1 204  ? -0.583  18.200  130.521 1.00 23.54 ?  202  ARG B C     1 
ATOM   10583 O O     . ARG B 1 204  ? -1.571  17.746  131.112 1.00 27.16 ?  202  ARG B O     1 
ATOM   10584 C CB    . ARG B 1 204  ? 1.741   17.711  131.344 1.00 26.03 ?  202  ARG B CB    1 
ATOM   10585 C CG    . ARG B 1 204  ? 1.359   17.383  132.779 1.00 31.53 ?  202  ARG B CG    1 
ATOM   10586 C CD    . ARG B 1 204  ? 2.500   17.687  133.750 1.00 35.40 ?  202  ARG B CD    1 
ATOM   10587 N NE    . ARG B 1 204  ? 2.888   19.089  133.669 1.00 34.06 ?  202  ARG B NE    1 
ATOM   10588 C CZ    . ARG B 1 204  ? 2.263   20.071  134.303 1.00 43.38 ?  202  ARG B CZ    1 
ATOM   10589 N NH1   . ARG B 1 204  ? 1.254   19.831  135.124 1.00 44.68 ?  202  ARG B NH1   1 
ATOM   10590 N NH2   . ARG B 1 204  ? 2.651   21.327  134.099 1.00 43.14 ?  202  ARG B NH2   1 
ATOM   10591 N N     . GLU B 1 205  ? -0.563  19.434  130.025 1.00 24.20 ?  203  GLU B N     1 
ATOM   10592 C CA    . GLU B 1 205  ? -1.710  20.310  130.210 1.00 24.73 ?  203  GLU B CA    1 
ATOM   10593 C C     . GLU B 1 205  ? -2.883  19.850  129.358 1.00 25.10 ?  203  GLU B C     1 
ATOM   10594 O O     . GLU B 1 205  ? -4.027  19.820  129.829 1.00 25.91 ?  203  GLU B O     1 
ATOM   10595 C CB    . GLU B 1 205  ? -1.300  21.739  129.880 1.00 25.94 ?  203  GLU B CB    1 
ATOM   10596 C CG    . GLU B 1 205  ? -2.352  22.795  130.042 1.00 31.58 ?  203  GLU B CG    1 
ATOM   10597 C CD    . GLU B 1 205  ? -1.760  24.178  129.844 1.00 35.65 ?  203  GLU B CD    1 
ATOM   10598 O OE1   . GLU B 1 205  ? -1.222  24.741  130.824 1.00 43.93 ?  203  GLU B OE1   1 
ATOM   10599 O OE2   . GLU B 1 205  ? -1.798  24.684  128.703 1.00 35.70 ?  203  GLU B OE2   1 
ATOM   10600 N N     . ALA B 1 206  ? -2.608  19.458  128.116 1.00 23.29 ?  204  ALA B N     1 
ATOM   10601 C CA    . ALA B 1 206  ? -3.662  18.964  127.237 1.00 21.35 ?  204  ALA B CA    1 
ATOM   10602 C C     . ALA B 1 206  ? -4.325  17.724  127.814 1.00 24.46 ?  204  ALA B C     1 
ATOM   10603 O O     . ALA B 1 206  ? -5.555  17.611  127.793 1.00 23.81 ?  204  ALA B O     1 
ATOM   10604 C CB    . ALA B 1 206  ? -3.091  18.662  125.854 1.00 19.46 ?  204  ALA B CB    1 
ATOM   10605 N N     . LEU B 1 207  ? -3.527  16.791  128.353 1.00 23.52 ?  205  LEU B N     1 
ATOM   10606 C CA    . LEU B 1 207  ? -4.098  15.560  128.897 1.00 25.75 ?  205  LEU B CA    1 
ATOM   10607 C C     . LEU B 1 207  ? -4.976  15.852  130.099 1.00 27.74 ?  205  LEU B C     1 
ATOM   10608 O O     . LEU B 1 207  ? -6.029  15.227  130.274 1.00 29.64 ?  205  LEU B O     1 
ATOM   10609 C CB    . LEU B 1 207  ? -2.992  14.574  129.282 1.00 25.84 ?  205  LEU B CB    1 
ATOM   10610 C CG    . LEU B 1 207  ? -2.268  13.874  128.131 1.00 25.54 ?  205  LEU B CG    1 
ATOM   10611 C CD1   . LEU B 1 207  ? -0.999  13.178  128.621 1.00 27.74 ?  205  LEU B CD1   1 
ATOM   10612 C CD2   . LEU B 1 207  ? -3.191  12.884  127.420 1.00 26.06 ?  205  LEU B CD2   1 
ATOM   10613 N N     . LYS B 1 208  ? -4.560  16.801  130.940 1.00 26.40 ?  206  LYS B N     1 
ATOM   10614 C CA    . LYS B 1 208  ? -5.345  17.119  132.126 1.00 28.52 ?  206  LYS B CA    1 
ATOM   10615 C C     . LYS B 1 208  ? -6.686  17.734  131.746 1.00 27.33 ?  206  LYS B C     1 
ATOM   10616 O O     . LYS B 1 208  ? -7.710  17.445  132.376 1.00 29.82 ?  206  LYS B O     1 
ATOM   10617 C CB    . LYS B 1 208  ? -4.552  18.057  133.039 1.00 32.44 ?  206  LYS B CB    1 
ATOM   10618 C CG    . LYS B 1 208  ? -5.061  18.096  134.463 1.00 40.11 ?  206  LYS B CG    1 
ATOM   10619 C CD    . LYS B 1 208  ? -4.132  18.890  135.373 1.00 47.51 ?  206  LYS B CD    1 
ATOM   10620 C CE    . LYS B 1 208  ? -4.234  20.385  135.115 1.00 48.28 ?  206  LYS B CE    1 
ATOM   10621 N NZ    . LYS B 1 208  ? -3.468  21.163  136.130 1.00 51.03 ?  206  LYS B NZ    1 
ATOM   10622 N N     . ARG B 1 209  ? -6.703  18.570  130.713 1.00 27.99 ?  207  ARG B N     1 
ATOM   10623 C CA    . ARG B 1 209  ? -7.923  19.231  130.272 1.00 27.14 ?  207  ARG B CA    1 
ATOM   10624 C C     . ARG B 1 209  ? -8.823  18.329  129.443 1.00 29.53 ?  207  ARG B C     1 
ATOM   10625 O O     . ARG B 1 209  ? -9.949  18.728  129.130 1.00 32.42 ?  207  ARG B O     1 
ATOM   10626 C CB    . ARG B 1 209  ? -7.573  20.477  129.467 1.00 26.97 ?  207  ARG B CB    1 
ATOM   10627 C CG    . ARG B 1 209  ? -6.819  21.500  130.291 1.00 28.80 ?  207  ARG B CG    1 
ATOM   10628 C CD    . ARG B 1 209  ? -6.348  22.637  129.417 1.00 26.79 ?  207  ARG B CD    1 
ATOM   10629 N NE    . ARG B 1 209  ? -5.760  23.716  130.201 1.00 34.75 ?  207  ARG B NE    1 
ATOM   10630 C CZ    . ARG B 1 209  ? -5.216  24.802  129.671 1.00 37.51 ?  207  ARG B CZ    1 
ATOM   10631 N NH1   . ARG B 1 209  ? -5.154  24.971  128.359 1.00 31.60 ?  207  ARG B NH1   1 
ATOM   10632 N NH2   . ARG B 1 209  ? -4.722  25.739  130.477 1.00 37.12 ?  207  ARG B NH2   1 
ATOM   10633 N N     . SER B 1 210  ? -8.361  17.129  129.096 1.00 26.19 ?  208  SER B N     1 
ATOM   10634 C CA    . SER B 1 210  ? -9.138  16.212  128.273 1.00 27.94 ?  208  SER B CA    1 
ATOM   10635 C C     . SER B 1 210  ? -10.068 15.331  129.087 1.00 28.29 ?  208  SER B C     1 
ATOM   10636 O O     . SER B 1 210  ? -10.999 14.747  128.524 1.00 28.49 ?  208  SER B O     1 
ATOM   10637 C CB    . SER B 1 210  ? -8.202  15.320  127.458 1.00 25.65 ?  208  SER B CB    1 
ATOM   10638 O OG    . SER B 1 210  ? -7.411  16.092  126.566 1.00 26.92 ?  208  SER B OG    1 
ATOM   10639 N N     . LYS B 1 211  ? -9.838  15.218  130.394 1.00 28.00 ?  209  LYS B N     1 
ATOM   10640 C CA    . LYS B 1 211  ? -10.622 14.291  131.203 1.00 27.84 ?  209  LYS B CA    1 
ATOM   10641 C C     . LYS B 1 211  ? -12.095 14.670  131.211 1.00 29.57 ?  209  LYS B C     1 
ATOM   10642 O O     . LYS B 1 211  ? -12.964 13.794  131.202 1.00 29.50 ?  209  LYS B O     1 
ATOM   10643 C CB    . LYS B 1 211  ? -10.073 14.255  132.624 1.00 29.59 ?  209  LYS B CB    1 
ATOM   10644 C CG    . LYS B 1 211  ? -8.575  14.070  132.679 1.00 35.07 ?  209  LYS B CG    1 
ATOM   10645 C CD    . LYS B 1 211  ? -8.164  12.723  132.124 1.00 34.65 ?  209  LYS B CD    1 
ATOM   10646 C CE    . LYS B 1 211  ? -6.657  12.528  132.250 1.00 42.41 ?  209  LYS B CE    1 
ATOM   10647 N NZ    . LYS B 1 211  ? -6.194  11.237  131.666 1.00 40.40 ?  209  LYS B NZ    1 
ATOM   10648 N N     . GLU B 1 212  ? -12.393 15.971  131.195 1.00 27.71 ?  210  GLU B N     1 
ATOM   10649 C CA    . GLU B 1 212  ? -13.773 16.428  131.334 1.00 31.57 ?  210  GLU B CA    1 
ATOM   10650 C C     . GLU B 1 212  ? -14.655 15.878  130.220 1.00 31.72 ?  210  GLU B C     1 
ATOM   10651 O O     . GLU B 1 212  ? -15.709 15.288  130.479 1.00 31.48 ?  210  GLU B O     1 
ATOM   10652 C CB    . GLU B 1 212  ? -13.811 17.956  131.348 1.00 35.81 ?  210  GLU B CB    1 
ATOM   10653 C CG    . GLU B 1 212  ? -15.202 18.556  131.210 1.00 43.19 ?  210  GLU B CG    1 
ATOM   10654 C CD    . GLU B 1 212  ? -15.175 20.070  131.155 1.00 48.93 ?  210  GLU B CD    1 
ATOM   10655 O OE1   . GLU B 1 212  ? -14.246 20.669  131.735 1.00 55.15 ?  210  GLU B OE1   1 
ATOM   10656 O OE2   . GLU B 1 212  ? -16.074 20.663  130.523 1.00 56.96 ?  210  GLU B OE2   1 
ATOM   10657 N N     . LEU B 1 213  ? -14.231 16.053  128.970 1.00 30.63 ?  211  LEU B N     1 
ATOM   10658 C CA    . LEU B 1 213  ? -15.045 15.584  127.858 1.00 30.88 ?  211  LEU B CA    1 
ATOM   10659 C C     . LEU B 1 213  ? -14.903 14.081  127.647 1.00 29.34 ?  211  LEU B C     1 
ATOM   10660 O O     . LEU B 1 213  ? -15.837 13.442  127.150 1.00 29.14 ?  211  LEU B O     1 
ATOM   10661 C CB    . LEU B 1 213  ? -14.699 16.362  126.583 1.00 25.69 ?  211  LEU B CB    1 
ATOM   10662 C CG    . LEU B 1 213  ? -15.115 17.842  126.601 1.00 31.22 ?  211  LEU B CG    1 
ATOM   10663 C CD1   . LEU B 1 213  ? -14.845 18.545  125.277 1.00 32.99 ?  211  LEU B CD1   1 
ATOM   10664 C CD2   . LEU B 1 213  ? -16.579 17.994  126.988 1.00 37.04 ?  211  LEU B CD2   1 
ATOM   10665 N N     . GLU B 1 214  ? -13.776 13.486  128.044 1.00 25.25 ?  212  GLU B N     1 
ATOM   10666 C CA    . GLU B 1 214  ? -13.667 12.033  127.962 1.00 23.50 ?  212  GLU B CA    1 
ATOM   10667 C C     . GLU B 1 214  ? -14.696 11.357  128.856 1.00 28.73 ?  212  GLU B C     1 
ATOM   10668 O O     . GLU B 1 214  ? -15.225 10.293  128.511 1.00 29.89 ?  212  GLU B O     1 
ATOM   10669 C CB    . GLU B 1 214  ? -12.260 11.576  128.335 1.00 25.24 ?  212  GLU B CB    1 
ATOM   10670 C CG    . GLU B 1 214  ? -11.258 11.806  127.228 1.00 25.73 ?  212  GLU B CG    1 
ATOM   10671 C CD    . GLU B 1 214  ? -9.892  11.262  127.575 1.00 29.18 ?  212  GLU B CD    1 
ATOM   10672 O OE1   . GLU B 1 214  ? -9.606  11.076  128.776 1.00 30.30 ?  212  GLU B OE1   1 
ATOM   10673 O OE2   . GLU B 1 214  ? -9.099  11.037  126.638 1.00 26.62 ?  212  GLU B OE2   1 
ATOM   10674 N N     . GLU B 1 215  ? -14.981 11.953  130.016 1.00 29.05 ?  213  GLU B N     1 
ATOM   10675 C CA    . GLU B 1 215  ? -15.985 11.394  130.912 1.00 32.35 ?  213  GLU B CA    1 
ATOM   10676 C C     . GLU B 1 215  ? -17.396 11.501  130.343 1.00 32.67 ?  213  GLU B C     1 
ATOM   10677 O O     . GLU B 1 215  ? -18.290 10.773  130.792 1.00 34.06 ?  213  GLU B O     1 
ATOM   10678 C CB    . GLU B 1 215  ? -15.897 12.079  132.278 1.00 33.81 ?  213  GLU B CB    1 
ATOM   10679 C CG    . GLU B 1 215  ? -14.624 11.730  133.046 1.00 38.86 ?  213  GLU B CG    1 
ATOM   10680 C CD    . GLU B 1 215  ? -14.423 12.584  134.288 1.00 49.72 ?  213  GLU B CD    1 
ATOM   10681 O OE1   . GLU B 1 215  ? -15.422 12.882  134.979 1.00 49.65 ?  213  GLU B OE1   1 
ATOM   10682 O OE2   . GLU B 1 215  ? -13.261 12.959  134.570 1.00 48.32 ?  213  GLU B OE2   1 
ATOM   10683 N N     . LYS B 1 216  ? -17.614 12.376  129.365 1.00 32.76 ?  214  LYS B N     1 
ATOM   10684 C CA    . LYS B 1 216  ? -18.898 12.460  128.680 1.00 32.74 ?  214  LYS B CA    1 
ATOM   10685 C C     . LYS B 1 216  ? -18.992 11.546  127.463 1.00 37.24 ?  214  LYS B C     1 
ATOM   10686 O O     . LYS B 1 216  ? -20.083 11.405  126.901 1.00 34.20 ?  214  LYS B O     1 
ATOM   10687 C CB    . LYS B 1 216  ? -19.177 13.899  128.244 1.00 33.26 ?  214  LYS B CB    1 
ATOM   10688 C CG    . LYS B 1 216  ? -19.311 14.892  129.388 1.00 36.72 ?  214  LYS B CG    1 
ATOM   10689 C CD    . LYS B 1 216  ? -19.538 16.291  128.839 1.00 43.42 ?  214  LYS B CD    1 
ATOM   10690 C CE    . LYS B 1 216  ? -19.530 17.343  129.939 1.00 48.84 ?  214  LYS B CE    1 
ATOM   10691 N NZ    . LYS B 1 216  ? -19.516 18.727  129.370 1.00 54.90 ?  214  LYS B NZ    1 
ATOM   10692 N N     . GLY B 1 217  ? -17.890 10.921  127.044 1.00 31.28 ?  215  GLY B N     1 
ATOM   10693 C CA    . GLY B 1 217  ? -17.908 10.016  125.912 1.00 31.26 ?  215  GLY B CA    1 
ATOM   10694 C C     . GLY B 1 217  ? -17.110 10.480  124.710 1.00 30.17 ?  215  GLY B C     1 
ATOM   10695 O O     . GLY B 1 217  ? -17.127 9.798   123.676 1.00 30.01 ?  215  GLY B O     1 
ATOM   10696 N N     . PHE B 1 218  ? -16.442 11.625  124.795 1.00 26.36 ?  216  PHE B N     1 
ATOM   10697 C CA    . PHE B 1 218  ? -15.516 12.023  123.748 1.00 25.02 ?  216  PHE B CA    1 
ATOM   10698 C C     . PHE B 1 218  ? -14.204 11.262  123.892 1.00 26.07 ?  216  PHE B C     1 
ATOM   10699 O O     . PHE B 1 218  ? -13.873 10.731  124.954 1.00 26.84 ?  216  PHE B O     1 
ATOM   10700 C CB    . PHE B 1 218  ? -15.221 13.525  123.799 1.00 24.60 ?  216  PHE B CB    1 
ATOM   10701 C CG    . PHE B 1 218  ? -16.376 14.401  123.404 1.00 26.00 ?  216  PHE B CG    1 
ATOM   10702 C CD1   . PHE B 1 218  ? -17.384 14.696  124.314 1.00 26.45 ?  216  PHE B CD1   1 
ATOM   10703 C CD2   . PHE B 1 218  ? -16.436 14.962  122.132 1.00 26.05 ?  216  PHE B CD2   1 
ATOM   10704 C CE1   . PHE B 1 218  ? -18.442 15.516  123.955 1.00 31.12 ?  216  PHE B CE1   1 
ATOM   10705 C CE2   . PHE B 1 218  ? -17.495 15.785  121.764 1.00 25.87 ?  216  PHE B CE2   1 
ATOM   10706 C CZ    . PHE B 1 218  ? -18.501 16.059  122.690 1.00 25.67 ?  216  PHE B CZ    1 
ATOM   10707 N N     . SER B 1 219  ? -13.448 11.225  122.797 1.00 23.62 ?  217  SER B N     1 
ATOM   10708 C CA    . SER B 1 219  ? -12.077 10.736  122.811 1.00 23.00 ?  217  SER B CA    1 
ATOM   10709 C C     . SER B 1 219  ? -11.199 11.808  122.175 1.00 21.61 ?  217  SER B C     1 
ATOM   10710 O O     . SER B 1 219  ? -11.689 12.858  121.748 1.00 20.36 ?  217  SER B O     1 
ATOM   10711 C CB    . SER B 1 219  ? -11.951 9.386   122.092 1.00 21.62 ?  217  SER B CB    1 
ATOM   10712 O OG    . SER B 1 219  ? -12.299 9.522   120.719 1.00 24.64 ?  217  SER B OG    1 
ATOM   10713 N N     . TYR B 1 220  ? -9.889  11.555  122.116 1.00 22.80 ?  218  TYR B N     1 
ATOM   10714 C CA    . TYR B 1 220  ? -8.945  12.581  121.691 1.00 19.88 ?  218  TYR B CA    1 
ATOM   10715 C C     . TYR B 1 220  ? -7.918  12.008  120.728 1.00 19.32 ?  218  TYR B C     1 
ATOM   10716 O O     . TYR B 1 220  ? -7.559  10.831  120.799 1.00 19.70 ?  218  TYR B O     1 
ATOM   10717 C CB    . TYR B 1 220  ? -8.218  13.208  122.902 1.00 19.95 ?  218  TYR B CB    1 
ATOM   10718 C CG    . TYR B 1 220  ? -9.017  14.309  123.554 1.00 20.75 ?  218  TYR B CG    1 
ATOM   10719 C CD1   . TYR B 1 220  ? -9.995  14.023  124.503 1.00 23.45 ?  218  TYR B CD1   1 
ATOM   10720 C CD2   . TYR B 1 220  ? -8.815  15.631  123.202 1.00 19.37 ?  218  TYR B CD2   1 
ATOM   10721 C CE1   . TYR B 1 220  ? -10.740 15.027  125.086 1.00 22.84 ?  218  TYR B CE1   1 
ATOM   10722 C CE2   . TYR B 1 220  ? -9.553  16.645  123.788 1.00 20.92 ?  218  TYR B CE2   1 
ATOM   10723 C CZ    . TYR B 1 220  ? -10.521 16.332  124.723 1.00 20.75 ?  218  TYR B CZ    1 
ATOM   10724 O OH    . TYR B 1 220  ? -11.263 17.337  125.308 1.00 27.04 ?  218  TYR B OH    1 
ATOM   10725 N N     . SER B 1 221  ? -7.436  12.874  119.839 1.00 18.66 ?  219  SER B N     1 
ATOM   10726 C CA    . SER B 1 221  ? -6.256  12.621  119.020 1.00 18.67 ?  219  SER B CA    1 
ATOM   10727 C C     . SER B 1 221  ? -5.404  13.876  119.076 1.00 17.72 ?  219  SER B C     1 
ATOM   10728 O O     . SER B 1 221  ? -5.865  14.947  118.678 1.00 18.40 ?  219  SER B O     1 
ATOM   10729 C CB    . SER B 1 221  ? -6.633  12.299  117.577 1.00 19.39 ?  219  SER B CB    1 
ATOM   10730 O OG    . SER B 1 221  ? -5.470  12.092  116.799 1.00 20.33 ?  219  SER B OG    1 
ATOM   10731 N N     . TYR B 1 222  ? -4.175  13.762  119.578 1.00 17.80 ?  220  TYR B N     1 
ATOM   10732 C CA    . TYR B 1 222  ? -3.362  14.951  119.813 1.00 17.30 ?  220  TYR B CA    1 
ATOM   10733 C C     . TYR B 1 222  ? -2.521  15.306  118.595 1.00 19.98 ?  220  TYR B C     1 
ATOM   10734 O O     . TYR B 1 222  ? -1.878  14.440  117.990 1.00 19.30 ?  220  TYR B O     1 
ATOM   10735 C CB    . TYR B 1 222  ? -2.485  14.759  121.056 1.00 17.62 ?  220  TYR B CB    1 
ATOM   10736 C CG    . TYR B 1 222  ? -3.355  14.627  122.285 1.00 18.21 ?  220  TYR B CG    1 
ATOM   10737 C CD1   . TYR B 1 222  ? -3.982  15.739  122.824 1.00 19.43 ?  220  TYR B CD1   1 
ATOM   10738 C CD2   . TYR B 1 222  ? -3.627  13.378  122.847 1.00 18.79 ?  220  TYR B CD2   1 
ATOM   10739 C CE1   . TYR B 1 222  ? -4.819  15.621  123.937 1.00 18.78 ?  220  TYR B CE1   1 
ATOM   10740 C CE2   . TYR B 1 222  ? -4.456  13.252  123.949 1.00 19.93 ?  220  TYR B CE2   1 
ATOM   10741 C CZ    . TYR B 1 222  ? -5.050  14.373  124.480 1.00 19.87 ?  220  TYR B CZ    1 
ATOM   10742 O OH    . TYR B 1 222  ? -5.891  14.241  125.552 1.00 20.06 ?  220  TYR B OH    1 
ATOM   10743 N N     . ASP B 1 223  ? -2.558  16.585  118.236 1.00 19.78 ?  221  ASP B N     1 
ATOM   10744 C CA    . ASP B 1 223  ? -1.856  17.158  117.087 1.00 22.73 ?  221  ASP B CA    1 
ATOM   10745 C C     . ASP B 1 223  ? -0.723  18.003  117.656 1.00 24.99 ?  221  ASP B C     1 
ATOM   10746 O O     . ASP B 1 223  ? -0.955  19.110  118.152 1.00 22.47 ?  221  ASP B O     1 
ATOM   10747 C CB    . ASP B 1 223  ? -2.830  17.978  116.246 1.00 22.85 ?  221  ASP B CB    1 
ATOM   10748 C CG    . ASP B 1 223  ? -2.147  18.820  115.182 1.00 28.99 ?  221  ASP B CG    1 
ATOM   10749 O OD1   . ASP B 1 223  ? -0.976  18.551  114.853 1.00 28.03 ?  221  ASP B OD1   1 
ATOM   10750 O OD2   . ASP B 1 223  ? -2.800  19.766  114.687 1.00 32.54 ?  221  ASP B OD2   1 
ATOM   10751 N N     . MET B 1 224  ? 0.497   17.474  117.610 1.00 24.67 ?  222  MET B N     1 
ATOM   10752 C CA    . MET B 1 224  ? 1.636   18.146  118.212 1.00 26.20 ?  222  MET B CA    1 
ATOM   10753 C C     . MET B 1 224  ? 2.186   19.298  117.358 1.00 31.07 ?  222  MET B C     1 
ATOM   10754 O O     . MET B 1 224  ? 3.269   19.802  117.662 1.00 38.60 ?  222  MET B O     1 
ATOM   10755 C CB    . MET B 1 224  ? 2.730   17.121  118.522 1.00 29.04 ?  222  MET B CB    1 
ATOM   10756 C CG    . MET B 1 224  ? 2.243   15.962  119.405 1.00 26.96 ?  222  MET B CG    1 
ATOM   10757 S SD    . MET B 1 224  ? 1.500   16.484  120.971 1.00 30.00 ?  222  MET B SD    1 
ATOM   10758 C CE    . MET B 1 224  ? 2.848   17.396  121.694 1.00 24.70 ?  222  MET B CE    1 
ATOM   10759 N N     . LEU B 1 225  ? 1.455   19.729  116.331 1.00 34.65 ?  223  LEU B N     1 
ATOM   10760 C CA    . LEU B 1 225  ? 1.725   20.994  115.634 1.00 33.36 ?  223  LEU B CA    1 
ATOM   10761 C C     . LEU B 1 225  ? 3.135   21.037  115.042 1.00 42.02 ?  223  LEU B C     1 
ATOM   10762 O O     . LEU B 1 225  ? 3.852   22.031  115.162 1.00 45.82 ?  223  LEU B O     1 
ATOM   10763 C CB    . LEU B 1 225  ? 1.484   22.194  116.554 1.00 30.30 ?  223  LEU B CB    1 
ATOM   10764 C CG    . LEU B 1 225  ? -0.002  22.446  116.856 1.00 30.75 ?  223  LEU B CG    1 
ATOM   10765 C CD1   . LEU B 1 225  ? -0.202  23.751  117.600 1.00 28.50 ?  223  LEU B CD1   1 
ATOM   10766 C CD2   . LEU B 1 225  ? -0.823  22.421  115.578 1.00 28.51 ?  223  LEU B CD2   1 
ATOM   10767 N N     . GLY B 1 226  ? 3.531   19.955  114.393 1.00 40.26 ?  224  GLY B N     1 
ATOM   10768 C CA    . GLY B 1 226  ? 4.778   19.919  113.650 1.00 37.73 ?  224  GLY B CA    1 
ATOM   10769 C C     . GLY B 1 226  ? 4.494   19.623  112.193 1.00 30.13 ?  224  GLY B C     1 
ATOM   10770 O O     . GLY B 1 226  ? 3.663   18.768  111.886 1.00 31.00 ?  224  GLY B O     1 
ATOM   10771 N N     . GLU B 1 227  ? 5.175   20.344  111.303 1.00 29.58 ?  225  GLU B N     1 
ATOM   10772 C CA    . GLU B 1 227  ? 5.056   20.041  109.889 1.00 27.62 ?  225  GLU B CA    1 
ATOM   10773 C C     . GLU B 1 227  ? 6.162   20.731  109.113 1.00 23.80 ?  225  GLU B C     1 
ATOM   10774 O O     . GLU B 1 227  ? 6.786   21.687  109.586 1.00 24.22 ?  225  GLU B O     1 
ATOM   10775 C CB    . GLU B 1 227  ? 3.691   20.442  109.321 1.00 28.67 ?  225  GLU B CB    1 
ATOM   10776 C CG    . GLU B 1 227  ? 3.430   21.925  109.205 1.00 27.10 ?  225  GLU B CG    1 
ATOM   10777 C CD    . GLU B 1 227  ? 1.994   22.202  108.788 1.00 27.65 ?  225  GLU B CD    1 
ATOM   10778 O OE1   . GLU B 1 227  ? 1.115   22.182  109.676 1.00 28.38 ?  225  GLU B OE1   1 
ATOM   10779 O OE2   . GLU B 1 227  ? 1.746   22.406  107.574 1.00 27.69 ?  225  GLU B OE2   1 
ATOM   10780 N N     . ALA B 1 228  ? 6.397   20.210  107.911 1.00 19.41 ?  226  ALA B N     1 
ATOM   10781 C CA    . ALA B 1 228  ? 7.273   20.828  106.923 1.00 19.90 ?  226  ALA B CA    1 
ATOM   10782 C C     . ALA B 1 228  ? 8.661   21.111  107.503 1.00 20.28 ?  226  ALA B C     1 
ATOM   10783 O O     . ALA B 1 228  ? 9.109   22.257  107.561 1.00 23.06 ?  226  ALA B O     1 
ATOM   10784 C CB    . ALA B 1 228  ? 6.631   22.104  106.376 1.00 24.82 ?  226  ALA B CB    1 
ATOM   10785 N N     . ALA B 1 229  ? 9.339   20.043  107.933 1.00 17.90 ?  227  ALA B N     1 
ATOM   10786 C CA    . ALA B 1 229  ? 10.745  20.158  108.313 1.00 16.32 ?  227  ALA B CA    1 
ATOM   10787 C C     . ALA B 1 229  ? 11.544  20.777  107.172 1.00 15.79 ?  227  ALA B C     1 
ATOM   10788 O O     . ALA B 1 229  ? 11.378  20.398  106.008 1.00 19.43 ?  227  ALA B O     1 
ATOM   10789 C CB    . ALA B 1 229  ? 11.319  18.784  108.667 1.00 17.14 ?  227  ALA B CB    1 
ATOM   10790 N N     . THR B 1 230  ? 12.382  21.759  107.516 1.00 17.54 ?  228  THR B N     1 
ATOM   10791 C CA    . THR B 1 230  ? 13.281  22.395  106.559 1.00 19.72 ?  228  THR B CA    1 
ATOM   10792 C C     . THR B 1 230  ? 14.682  21.805  106.596 1.00 16.10 ?  228  THR B C     1 
ATOM   10793 O O     . THR B 1 230  ? 15.352  21.740  105.560 1.00 17.28 ?  228  THR B O     1 
ATOM   10794 C CB    . THR B 1 230  ? 13.379  23.902  106.841 1.00 20.83 ?  228  THR B CB    1 
ATOM   10795 O OG1   . THR B 1 230  ? 12.067  24.469  106.879 1.00 24.87 ?  228  THR B OG1   1 
ATOM   10796 C CG2   . THR B 1 230  ? 14.190  24.616  105.754 1.00 19.89 ?  228  THR B CG2   1 
ATOM   10797 N N     . THR B 1 231  ? 15.137  21.367  107.767 1.00 15.74 ?  229  THR B N     1 
ATOM   10798 C CA    . THR B 1 231  ? 16.476  20.836  107.927 1.00 15.22 ?  229  THR B CA    1 
ATOM   10799 C C     . THR B 1 231  ? 16.416  19.460  108.565 1.00 18.19 ?  229  THR B C     1 
ATOM   10800 O O     . THR B 1 231  ? 15.399  19.058  109.135 1.00 16.55 ?  229  THR B O     1 
ATOM   10801 C CB    . THR B 1 231  ? 17.335  21.741  108.804 1.00 16.43 ?  229  THR B CB    1 
ATOM   10802 O OG1   . THR B 1 231  ? 16.861  21.656  110.158 1.00 18.08 ?  229  THR B OG1   1 
ATOM   10803 C CG2   . THR B 1 231  ? 17.274  23.189  108.323 1.00 18.29 ?  229  THR B CG2   1 
ATOM   10804 N N     . ALA B 1 232  ? 17.553  18.764  108.506 1.00 15.88 ?  230  ALA B N     1 
ATOM   10805 C CA    . ALA B 1 232  ? 17.679  17.492  109.210 1.00 17.37 ?  230  ALA B CA    1 
ATOM   10806 C C     . ALA B 1 232  ? 17.399  17.652  110.699 1.00 17.70 ?  230  ALA B C     1 
ATOM   10807 O O     . ALA B 1 232  ? 16.705  16.823  111.300 1.00 19.47 ?  230  ALA B O     1 
ATOM   10808 C CB    . ALA B 1 232  ? 19.070  16.906  108.984 1.00 16.60 ?  230  ALA B CB    1 
ATOM   10809 N N     . ALA B 1 233  ? 17.925  18.715  111.311 1.00 17.46 ?  231  ALA B N     1 
ATOM   10810 C CA    . ALA B 1 233  ? 17.727  18.914  112.745 1.00 16.79 ?  231  ALA B CA    1 
ATOM   10811 C C     . ALA B 1 233  ? 16.256  19.131  113.078 1.00 17.13 ?  231  ALA B C     1 
ATOM   10812 O O     . ALA B 1 233  ? 15.787  18.699  114.142 1.00 17.52 ?  231  ALA B O     1 
ATOM   10813 C CB    . ALA B 1 233  ? 18.564  20.100  113.234 1.00 17.01 ?  231  ALA B CB    1 
ATOM   10814 N N     . ASP B 1 234  ? 15.519  19.820  112.196 1.00 17.12 ?  232  ASP B N     1 
ATOM   10815 C CA    . ASP B 1 234  ? 14.077  19.986  112.392 1.00 17.59 ?  232  ASP B CA    1 
ATOM   10816 C C     . ASP B 1 234  ? 13.385  18.634  112.441 1.00 15.99 ?  232  ASP B C     1 
ATOM   10817 O O     . ASP B 1 234  ? 12.558  18.369  113.323 1.00 16.68 ?  232  ASP B O     1 
ATOM   10818 C CB    . ASP B 1 234  ? 13.439  20.776  111.247 1.00 16.63 ?  232  ASP B CB    1 
ATOM   10819 C CG    . ASP B 1 234  ? 13.800  22.237  111.213 1.00 21.86 ?  232  ASP B CG    1 
ATOM   10820 O OD1   . ASP B 1 234  ? 14.170  22.821  112.250 1.00 23.48 ?  232  ASP B OD1   1 
ATOM   10821 O OD2   . ASP B 1 234  ? 13.649  22.808  110.099 1.00 21.89 ?  232  ASP B OD2   1 
ATOM   10822 N N     . ALA B 1 235  ? 13.688  17.782  111.462 1.00 15.31 ?  233  ALA B N     1 
ATOM   10823 C CA    . ALA B 1 235  ? 13.007  16.507  111.340 1.00 16.00 ?  233  ALA B CA    1 
ATOM   10824 C C     . ALA B 1 235  ? 13.342  15.613  112.517 1.00 16.14 ?  233  ALA B C     1 
ATOM   10825 O O     . ALA B 1 235  ? 12.476  14.898  113.026 1.00 17.24 ?  233  ALA B O     1 
ATOM   10826 C CB    . ALA B 1 235  ? 13.393  15.831  110.026 1.00 16.44 ?  233  ALA B CB    1 
ATOM   10827 N N     . GLU B 1 236  ? 14.596  15.648  112.966 1.00 16.14 ?  234  GLU B N     1 
ATOM   10828 C CA    . GLU B 1 236  ? 14.983  14.833  114.110 1.00 18.83 ?  234  GLU B CA    1 
ATOM   10829 C C     . GLU B 1 236  ? 14.279  15.303  115.375 1.00 17.84 ?  234  GLU B C     1 
ATOM   10830 O O     . GLU B 1 236  ? 13.830  14.481  116.185 1.00 18.77 ?  234  GLU B O     1 
ATOM   10831 C CB    . GLU B 1 236  ? 16.501  14.856  114.282 1.00 18.79 ?  234  GLU B CB    1 
ATOM   10832 C CG    . GLU B 1 236  ? 16.979  13.880  115.344 1.00 22.46 ?  234  GLU B CG    1 
ATOM   10833 C CD    . GLU B 1 236  ? 18.487  13.807  115.436 1.00 31.68 ?  234  GLU B CD    1 
ATOM   10834 O OE1   . GLU B 1 236  ? 19.169  14.689  114.859 1.00 32.17 ?  234  GLU B OE1   1 
ATOM   10835 O OE2   . GLU B 1 236  ? 18.983  12.864  116.093 1.00 31.43 ?  234  GLU B OE2   1 
ATOM   10836 N N     . ARG B 1 237  ? 14.143  16.622  115.547 1.00 15.82 ?  235  ARG B N     1 
ATOM   10837 C CA    . ARG B 1 237  ? 13.432  17.141  116.707 1.00 17.82 ?  235  ARG B CA    1 
ATOM   10838 C C     . ARG B 1 237  ? 11.955  16.766  116.662 1.00 17.13 ?  235  ARG B C     1 
ATOM   10839 O O     . ARG B 1 237  ? 11.393  16.323  117.668 1.00 17.55 ?  235  ARG B O     1 
ATOM   10840 C CB    . ARG B 1 237  ? 13.587  18.654  116.799 1.00 19.19 ?  235  ARG B CB    1 
ATOM   10841 C CG    . ARG B 1 237  ? 12.833  19.195  117.973 1.00 19.57 ?  235  ARG B CG    1 
ATOM   10842 C CD    . ARG B 1 237  ? 12.633  20.675  117.915 1.00 23.05 ?  235  ARG B CD    1 
ATOM   10843 N NE    . ARG B 1 237  ? 11.945  21.094  119.127 1.00 27.62 ?  235  ARG B NE    1 
ATOM   10844 C CZ    . ARG B 1 237  ? 11.935  22.332  119.596 1.00 27.52 ?  235  ARG B CZ    1 
ATOM   10845 N NH1   . ARG B 1 237  ? 12.555  23.316  118.961 1.00 30.88 ?  235  ARG B NH1   1 
ATOM   10846 N NH2   . ARG B 1 237  ? 11.297  22.586  120.734 1.00 26.44 ?  235  ARG B NH2   1 
ATOM   10847 N N     . TYR B 1 238  ? 11.303  16.936  115.505 1.00 17.07 ?  236  TYR B N     1 
ATOM   10848 C CA    . TYR B 1 238  ? 9.900   16.534  115.406 1.00 17.59 ?  236  TYR B CA    1 
ATOM   10849 C C     . TYR B 1 238  ? 9.737   15.056  115.733 1.00 17.10 ?  236  TYR B C     1 
ATOM   10850 O O     . TYR B 1 238  ? 8.799   14.670  116.440 1.00 17.22 ?  236  TYR B O     1 
ATOM   10851 C CB    . TYR B 1 238  ? 9.344   16.834  114.014 1.00 17.06 ?  236  TYR B CB    1 
ATOM   10852 C CG    . TYR B 1 238  ? 9.088   18.298  113.735 1.00 19.19 ?  236  TYR B CG    1 
ATOM   10853 C CD1   . TYR B 1 238  ? 8.558   19.138  114.708 1.00 25.82 ?  236  TYR B CD1   1 
ATOM   10854 C CD2   . TYR B 1 238  ? 9.392   18.837  112.494 1.00 19.99 ?  236  TYR B CD2   1 
ATOM   10855 C CE1   . TYR B 1 238  ? 8.325   20.482  114.437 1.00 30.55 ?  236  TYR B CE1   1 
ATOM   10856 C CE2   . TYR B 1 238  ? 9.164   20.174  112.212 1.00 21.44 ?  236  TYR B CE2   1 
ATOM   10857 C CZ    . TYR B 1 238  ? 8.635   20.991  113.185 1.00 29.34 ?  236  TYR B CZ    1 
ATOM   10858 O OH    . TYR B 1 238  ? 8.416   22.317  112.886 1.00 33.16 ?  236  TYR B OH    1 
ATOM   10859 N N     . TYR B 1 239  ? 10.657  14.217  115.251 1.00 16.31 ?  237  TYR B N     1 
ATOM   10860 C CA    . TYR B 1 239  ? 10.608  12.791  115.564 1.00 16.16 ?  237  TYR B CA    1 
ATOM   10861 C C     . TYR B 1 239  ? 10.691  12.548  117.068 1.00 17.97 ?  237  TYR B C     1 
ATOM   10862 O O     . TYR B 1 239  ? 9.884   11.805  117.641 1.00 17.58 ?  237  TYR B O     1 
ATOM   10863 C CB    . TYR B 1 239  ? 11.745  12.078  114.838 1.00 17.13 ?  237  TYR B CB    1 
ATOM   10864 C CG    . TYR B 1 239  ? 11.961  10.644  115.226 1.00 17.89 ?  237  TYR B CG    1 
ATOM   10865 C CD1   . TYR B 1 239  ? 10.935  9.713   115.149 1.00 21.75 ?  237  TYR B CD1   1 
ATOM   10866 C CD2   . TYR B 1 239  ? 13.207  10.215  115.650 1.00 26.79 ?  237  TYR B CD2   1 
ATOM   10867 C CE1   . TYR B 1 239  ? 11.144  8.397   115.495 1.00 21.08 ?  237  TYR B CE1   1 
ATOM   10868 C CE2   . TYR B 1 239  ? 13.428  8.907   116.004 1.00 31.51 ?  237  TYR B CE2   1 
ATOM   10869 C CZ    . TYR B 1 239  ? 12.395  8.000   115.926 1.00 30.77 ?  237  TYR B CZ    1 
ATOM   10870 O OH    . TYR B 1 239  ? 12.635  6.694   116.287 1.00 34.21 ?  237  TYR B OH    1 
ATOM   10871 N N     . ARG B 1 240  ? 11.665  13.168  117.733 1.00 17.22 ?  238  ARG B N     1 
ATOM   10872 C CA    . ARG B 1 240  ? 11.803  12.947  119.166 1.00 18.15 ?  238  ARG B CA    1 
ATOM   10873 C C     . ARG B 1 240  ? 10.622  13.523  119.942 1.00 16.71 ?  238  ARG B C     1 
ATOM   10874 O O     . ARG B 1 240  ? 10.212  12.952  120.957 1.00 20.20 ?  238  ARG B O     1 
ATOM   10875 C CB    . ARG B 1 240  ? 13.120  13.549  119.659 1.00 19.09 ?  238  ARG B CB    1 
ATOM   10876 C CG    . ARG B 1 240  ? 14.360  12.877  119.094 1.00 22.16 ?  238  ARG B CG    1 
ATOM   10877 C CD    . ARG B 1 240  ? 14.469  11.428  119.540 1.00 25.34 ?  238  ARG B CD    1 
ATOM   10878 N NE    . ARG B 1 240  ? 15.486  10.725  118.770 1.00 27.52 ?  238  ARG B NE    1 
ATOM   10879 C CZ    . ARG B 1 240  ? 15.709  9.419   118.827 1.00 35.97 ?  238  ARG B CZ    1 
ATOM   10880 N NH1   . ARG B 1 240  ? 15.000  8.630   119.618 1.00 37.26 ?  238  ARG B NH1   1 
ATOM   10881 N NH2   . ARG B 1 240  ? 16.668  8.892   118.071 1.00 37.69 ?  238  ARG B NH2   1 
ATOM   10882 N N     . ASP B 1 241  ? 10.054  14.637  119.468 1.00 17.53 ?  239  ASP B N     1 
ATOM   10883 C CA    . ASP B 1 241  ? 8.874   15.209  120.112 1.00 18.50 ?  239  ASP B CA    1 
ATOM   10884 C C     . ASP B 1 241  ? 7.657   14.295  119.968 1.00 16.51 ?  239  ASP B C     1 
ATOM   10885 O O     . ASP B 1 241  ? 6.872   14.157  120.909 1.00 17.79 ?  239  ASP B O     1 
ATOM   10886 C CB    . ASP B 1 241  ? 8.576   16.604  119.547 1.00 19.69 ?  239  ASP B CB    1 
ATOM   10887 C CG    . ASP B 1 241  ? 9.569   17.677  120.021 1.00 20.91 ?  239  ASP B CG    1 
ATOM   10888 O OD1   . ASP B 1 241  ? 10.316  17.455  120.999 1.00 25.69 ?  239  ASP B OD1   1 
ATOM   10889 O OD2   . ASP B 1 241  ? 9.585   18.761  119.389 1.00 25.88 ?  239  ASP B OD2   1 
ATOM   10890 N N     . TYR B 1 242  ? 7.483   13.654  118.807 1.00 16.93 ?  240  TYR B N     1 
ATOM   10891 C CA    . TYR B 1 242  ? 6.406   12.674  118.662 1.00 16.61 ?  240  TYR B CA    1 
ATOM   10892 C C     . TYR B 1 242  ? 6.604   11.478  119.588 1.00 17.57 ?  240  TYR B C     1 
ATOM   10893 O O     . TYR B 1 242  ? 5.652   10.999  120.223 1.00 17.61 ?  240  TYR B O     1 
ATOM   10894 C CB    . TYR B 1 242  ? 6.342   12.181  117.222 1.00 16.33 ?  240  TYR B CB    1 
ATOM   10895 C CG    . TYR B 1 242  ? 5.697   13.094  116.202 1.00 15.80 ?  240  TYR B CG    1 
ATOM   10896 C CD1   . TYR B 1 242  ? 4.580   13.877  116.503 1.00 17.49 ?  240  TYR B CD1   1 
ATOM   10897 C CD2   . TYR B 1 242  ? 6.194   13.137  114.916 1.00 17.80 ?  240  TYR B CD2   1 
ATOM   10898 C CE1   . TYR B 1 242  ? 3.987   14.686  115.520 1.00 19.72 ?  240  TYR B CE1   1 
ATOM   10899 C CE2   . TYR B 1 242  ? 5.624   13.929  113.942 1.00 18.91 ?  240  TYR B CE2   1 
ATOM   10900 C CZ    . TYR B 1 242  ? 4.530   14.704  114.236 1.00 16.29 ?  240  TYR B CZ    1 
ATOM   10901 O OH    . TYR B 1 242  ? 3.997   15.460  113.200 1.00 18.21 ?  240  TYR B OH    1 
ATOM   10902 N N     . GLU B 1 243  ? 7.836   10.966  119.656 1.00 17.38 ?  241  GLU B N     1 
ATOM   10903 C CA    . GLU B 1 243  ? 8.153   9.841   120.530 1.00 18.31 ?  241  GLU B CA    1 
ATOM   10904 C C     . GLU B 1 243  ? 7.802   10.152  121.978 1.00 18.53 ?  241  GLU B C     1 
ATOM   10905 O O     . GLU B 1 243  ? 7.188   9.335   122.675 1.00 18.87 ?  241  GLU B O     1 
ATOM   10906 C CB    . GLU B 1 243  ? 9.641   9.508   120.396 1.00 22.07 ?  241  GLU B CB    1 
ATOM   10907 C CG    . GLU B 1 243  ? 10.129  8.372   121.265 1.00 25.13 ?  241  GLU B CG    1 
ATOM   10908 C CD    . GLU B 1 243  ? 11.616  8.137   121.108 1.00 29.84 ?  241  GLU B CD    1 
ATOM   10909 O OE1   . GLU B 1 243  ? 12.351  9.121   120.892 1.00 30.72 ?  241  GLU B OE1   1 
ATOM   10910 O OE2   . GLU B 1 243  ? 12.049  6.973   121.188 1.00 36.22 ?  241  GLU B OE2   1 
ATOM   10911 N N     . SER B 1 244  ? 8.202   11.335  122.450 1.00 18.14 ?  242  SER B N     1 
ATOM   10912 C CA    . SER B 1 244  ? 7.932   11.720  123.829 1.00 18.49 ?  242  SER B CA    1 
ATOM   10913 C C     . SER B 1 244  ? 6.435   11.878  124.068 1.00 18.58 ?  242  SER B C     1 
ATOM   10914 O O     . SER B 1 244  ? 5.921   11.454  125.108 1.00 19.09 ?  242  SER B O     1 
ATOM   10915 C CB    . SER B 1 244  ? 8.691   13.010  124.145 1.00 18.30 ?  242  SER B CB    1 
ATOM   10916 O OG    . SER B 1 244  ? 8.342   13.523  125.406 1.00 22.59 ?  242  SER B OG    1 
ATOM   10917 N N     . ALA B 1 245  ? 5.711   12.437  123.088 1.00 18.11 ?  243  ALA B N     1 
ATOM   10918 C CA    . ALA B 1 245  ? 4.265   12.581  123.231 1.00 18.20 ?  243  ALA B CA    1 
ATOM   10919 C C     . ALA B 1 245  ? 3.569   11.222  123.267 1.00 18.67 ?  243  ALA B C     1 
ATOM   10920 O O     . ALA B 1 245  ? 2.624   11.027  124.040 1.00 19.13 ?  243  ALA B O     1 
ATOM   10921 C CB    . ALA B 1 245  ? 3.707   13.439  122.097 1.00 17.71 ?  243  ALA B CB    1 
ATOM   10922 N N     . ILE B 1 246  ? 4.026   10.265  122.455 1.00 18.66 ?  244  ILE B N     1 
ATOM   10923 C CA    . ILE B 1 246  ? 3.403   8.941   122.478 1.00 21.01 ?  244  ILE B CA    1 
ATOM   10924 C C     . ILE B 1 246  ? 3.563   8.293   123.851 1.00 20.83 ?  244  ILE B C     1 
ATOM   10925 O O     . ILE B 1 246  ? 2.631   7.665   124.371 1.00 20.82 ?  244  ILE B O     1 
ATOM   10926 C CB    . ILE B 1 246  ? 3.968   8.057   121.351 1.00 19.03 ?  244  ILE B CB    1 
ATOM   10927 C CG1   . ILE B 1 246  ? 3.473   8.548   119.994 1.00 18.47 ?  244  ILE B CG1   1 
ATOM   10928 C CG2   . ILE B 1 246  ? 3.554   6.610   121.552 1.00 20.43 ?  244  ILE B CG2   1 
ATOM   10929 C CD1   . ILE B 1 246  ? 4.184   7.893   118.808 1.00 18.83 ?  244  ILE B CD1   1 
ATOM   10930 N N     . HIS B 1 247  ? 4.726   8.462   124.486 1.00 19.89 ?  245  HIS B N     1 
ATOM   10931 C CA    . HIS B 1 247  ? 4.874   7.918   125.829 1.00 20.84 ?  245  HIS B CA    1 
ATOM   10932 C C     . HIS B 1 247  ? 3.865   8.538   126.782 1.00 20.75 ?  245  HIS B C     1 
ATOM   10933 O O     . HIS B 1 247  ? 3.262   7.836   127.599 1.00 21.58 ?  245  HIS B O     1 
ATOM   10934 C CB    . HIS B 1 247  ? 6.289   8.149   126.355 1.00 22.62 ?  245  HIS B CB    1 
ATOM   10935 C CG    . HIS B 1 247  ? 7.298   7.196   125.807 1.00 22.22 ?  245  HIS B CG    1 
ATOM   10936 N ND1   . HIS B 1 247  ? 7.294   5.852   126.119 1.00 22.65 ?  245  HIS B ND1   1 
ATOM   10937 C CD2   . HIS B 1 247  ? 8.361   7.393   124.994 1.00 23.32 ?  245  HIS B CD2   1 
ATOM   10938 C CE1   . HIS B 1 247  ? 8.298   5.259   125.497 1.00 25.05 ?  245  HIS B CE1   1 
ATOM   10939 N NE2   . HIS B 1 247  ? 8.966   6.173   124.815 1.00 26.59 ?  245  HIS B NE2   1 
ATOM   10940 N N     . ALA B 1 248  ? 3.683   9.858   126.701 1.00 20.30 ?  246  ALA B N     1 
ATOM   10941 C CA    . ALA B 1 248  ? 2.748   10.530  127.593 1.00 20.51 ?  246  ALA B CA    1 
ATOM   10942 C C     . ALA B 1 248  ? 1.315   10.109  127.290 1.00 20.67 ?  246  ALA B C     1 
ATOM   10943 O O     . ALA B 1 248  ? 0.545   9.798   128.204 1.00 23.11 ?  246  ALA B O     1 
ATOM   10944 C CB    . ALA B 1 248  ? 2.906   12.048  127.472 1.00 22.05 ?  246  ALA B CB    1 
ATOM   10945 N N     . ILE B 1 249  ? 0.951   10.080  126.008 1.00 20.61 ?  247  ILE B N     1 
ATOM   10946 C CA    . ILE B 1 249  ? -0.409  9.707   125.632 1.00 20.65 ?  247  ILE B CA    1 
ATOM   10947 C C     . ILE B 1 249  ? -0.662  8.237   125.932 1.00 21.96 ?  247  ILE B C     1 
ATOM   10948 O O     . ILE B 1 249  ? -1.746  7.865   126.394 1.00 21.48 ?  247  ILE B O     1 
ATOM   10949 C CB    . ILE B 1 249  ? -0.655  10.030  124.146 1.00 19.79 ?  247  ILE B CB    1 
ATOM   10950 C CG1   . ILE B 1 249  ? -0.557  11.535  123.889 1.00 19.22 ?  247  ILE B CG1   1 
ATOM   10951 C CG2   . ILE B 1 249  ? -2.019  9.474   123.694 1.00 20.01 ?  247  ILE B CG2   1 
ATOM   10952 C CD1   . ILE B 1 249  ? -0.337  11.894  122.406 1.00 18.58 ?  247  ILE B CD1   1 
ATOM   10953 N N     . GLY B 1 250  ? 0.330   7.380   125.679 1.00 21.23 ?  248  GLY B N     1 
ATOM   10954 C CA    . GLY B 1 250  ? 0.162   5.963   125.944 1.00 21.72 ?  248  GLY B CA    1 
ATOM   10955 C C     . GLY B 1 250  ? 0.004   5.655   127.421 1.00 23.56 ?  248  GLY B C     1 
ATOM   10956 O O     . GLY B 1 250  ? -0.826  4.827   127.811 1.00 24.00 ?  248  GLY B O     1 
ATOM   10957 N N     . LYS B 1 251  ? 0.807   6.300   128.269 1.00 22.39 ?  249  LYS B N     1 
ATOM   10958 C CA    . LYS B 1 251  ? 0.631   6.104   129.703 1.00 25.47 ?  249  LYS B CA    1 
ATOM   10959 C C     . LYS B 1 251  ? -0.735  6.598   130.154 1.00 25.00 ?  249  LYS B C     1 
ATOM   10960 O O     . LYS B 1 251  ? -1.401  5.944   130.969 1.00 26.75 ?  249  LYS B O     1 
ATOM   10961 C CB    . LYS B 1 251  ? 1.745   6.813   130.473 1.00 28.06 ?  249  LYS B CB    1 
ATOM   10962 C CG    . LYS B 1 251  ? 3.068   6.064   130.500 1.00 35.15 ?  249  LYS B CG    1 
ATOM   10963 C CD    . LYS B 1 251  ? 2.938   4.712   131.202 1.00 35.69 ?  249  LYS B CD    1 
ATOM   10964 C CE    . LYS B 1 251  ? 4.300   4.157   131.605 1.00 43.59 ?  249  LYS B CE    1 
ATOM   10965 N NZ    . LYS B 1 251  ? 5.298   4.217   130.499 1.00 42.56 ?  249  LYS B NZ    1 
ATOM   10966 N N     . ALA B 1 252  ? -1.174  7.742   129.620 1.00 24.98 ?  250  ALA B N     1 
ATOM   10967 C CA    . ALA B 1 252  ? -2.467  8.296   130.006 1.00 23.62 ?  250  ALA B CA    1 
ATOM   10968 C C     . ALA B 1 252  ? -3.604  7.402   129.540 1.00 24.06 ?  250  ALA B C     1 
ATOM   10969 O O     . ALA B 1 252  ? -4.610  7.256   130.242 1.00 27.61 ?  250  ALA B O     1 
ATOM   10970 C CB    . ALA B 1 252  ? -2.635  9.704   129.434 1.00 25.68 ?  250  ALA B CB    1 
ATOM   10971 N N     . SER B 1 253  ? -3.462  6.803   128.352 1.00 22.87 ?  251  SER B N     1 
ATOM   10972 C CA    . SER B 1 253  ? -4.486  5.882   127.868 1.00 23.20 ?  251  SER B CA    1 
ATOM   10973 C C     . SER B 1 253  ? -4.739  4.767   128.874 1.00 25.13 ?  251  SER B C     1 
ATOM   10974 O O     . SER B 1 253  ? -5.890  4.373   129.093 1.00 25.99 ?  251  SER B O     1 
ATOM   10975 C CB    . SER B 1 253  ? -4.077  5.303   126.519 1.00 25.44 ?  251  SER B CB    1 
ATOM   10976 O OG    . SER B 1 253  ? -5.057  4.389   126.060 1.00 24.80 ?  251  SER B OG    1 
ATOM   10977 N N     . ALA B 1 254  ? -3.677  4.253   129.500 1.00 24.30 ?  252  ALA B N     1 
ATOM   10978 C CA    . ALA B 1 254  ? -3.784  3.273   130.587 1.00 28.89 ?  252  ALA B CA    1 
ATOM   10979 C C     . ALA B 1 254  ? -4.651  2.080   130.187 1.00 25.62 ?  252  ALA B C     1 
ATOM   10980 O O     . ALA B 1 254  ? -5.523  1.638   130.937 1.00 27.00 ?  252  ALA B O     1 
ATOM   10981 C CB    . ALA B 1 254  ? -4.310  3.923   131.870 1.00 27.65 ?  252  ALA B CB    1 
ATOM   10982 N N     . GLY B 1 255  ? -4.423  1.570   128.978 1.00 27.67 ?  253  GLY B N     1 
ATOM   10983 C CA    . GLY B 1 255  ? -5.085  0.357   128.537 1.00 28.79 ?  253  GLY B CA    1 
ATOM   10984 C C     . GLY B 1 255  ? -6.508  0.512   128.046 1.00 28.24 ?  253  GLY B C     1 
ATOM   10985 O O     . GLY B 1 255  ? -7.198  -0.501  127.886 1.00 30.79 ?  253  GLY B O     1 
ATOM   10986 N N     . ARG B 1 256  ? -6.979  1.737   127.806 1.00 26.31 ?  254  ARG B N     1 
ATOM   10987 C CA    . ARG B 1 256  ? -8.337  1.931   127.306 1.00 26.88 ?  254  ARG B CA    1 
ATOM   10988 C C     . ARG B 1 256  ? -8.513  1.488   125.862 1.00 27.12 ?  254  ARG B C     1 
ATOM   10989 O O     . ARG B 1 256  ? -9.657  1.363   125.409 1.00 29.31 ?  254  ARG B O     1 
ATOM   10990 C CB    . ARG B 1 256  ? -8.751  3.397   127.440 1.00 24.90 ?  254  ARG B CB    1 
ATOM   10991 C CG    . ARG B 1 256  ? -9.201  3.771   128.858 1.00 26.85 ?  254  ARG B CG    1 
ATOM   10992 C CD    . ARG B 1 256  ? -9.514  5.243   128.964 1.00 27.63 ?  254  ARG B CD    1 
ATOM   10993 N NE    . ARG B 1 256  ? -8.296  6.046   128.983 1.00 25.75 ?  254  ARG B NE    1 
ATOM   10994 C CZ    . ARG B 1 256  ? -8.264  7.365   128.863 1.00 28.81 ?  254  ARG B CZ    1 
ATOM   10995 N NH1   . ARG B 1 256  ? -9.364  8.067   128.636 1.00 28.53 ?  254  ARG B NH1   1 
ATOM   10996 N NH2   . ARG B 1 256  ? -7.097  8.000   128.975 1.00 28.73 ?  254  ARG B NH2   1 
ATOM   10997 N N     . GLY B 1 257  ? -7.425  1.249   125.133 1.00 24.59 ?  255  GLY B N     1 
ATOM   10998 C CA    . GLY B 1 257  ? -7.528  0.806   123.755 1.00 24.31 ?  255  GLY B CA    1 
ATOM   10999 C C     . GLY B 1 257  ? -7.675  1.958   122.786 1.00 25.41 ?  255  GLY B C     1 
ATOM   11000 O O     . GLY B 1 257  ? -7.737  3.134   123.157 1.00 25.74 ?  255  GLY B O     1 
ATOM   11001 N N     . ILE B 1 258  ? -7.762  1.599   121.502 1.00 26.15 ?  256  ILE B N     1 
ATOM   11002 C CA    . ILE B 1 258  ? -7.682  2.599   120.438 1.00 24.90 ?  256  ILE B CA    1 
ATOM   11003 C C     . ILE B 1 258  ? -8.987  3.356   120.209 1.00 24.83 ?  256  ILE B C     1 
ATOM   11004 O O     . ILE B 1 258  ? -8.968  4.417   119.571 1.00 25.52 ?  256  ILE B O     1 
ATOM   11005 C CB    . ILE B 1 258  ? -7.223  1.961   119.114 1.00 27.54 ?  256  ILE B CB    1 
ATOM   11006 C CG1   . ILE B 1 258  ? -8.212  0.892   118.655 1.00 25.97 ?  256  ILE B CG1   1 
ATOM   11007 C CG2   . ILE B 1 258  ? -5.822  1.358   119.256 1.00 25.73 ?  256  ILE B CG2   1 
ATOM   11008 C CD1   . ILE B 1 258  ? -7.843  0.261   117.329 1.00 28.30 ?  256  ILE B CD1   1 
ATOM   11009 N N     . TYR B 1 259  ? -10.120 2.858   120.707 1.00 26.26 ?  257  TYR B N     1 
ATOM   11010 C CA    . TYR B 1 259  ? -11.394 3.541   120.492 1.00 23.03 ?  257  TYR B CA    1 
ATOM   11011 C C     . TYR B 1 259  ? -11.753 4.474   121.646 1.00 26.00 ?  257  TYR B C     1 
ATOM   11012 O O     . TYR B 1 259  ? -12.009 5.663   121.428 1.00 24.08 ?  257  TYR B O     1 
ATOM   11013 C CB    . TYR B 1 259  ? -12.504 2.505   120.255 1.00 26.62 ?  257  TYR B CB    1 
ATOM   11014 C CG    . TYR B 1 259  ? -12.138 1.538   119.153 1.00 25.71 ?  257  TYR B CG    1 
ATOM   11015 C CD1   . TYR B 1 259  ? -12.043 1.969   117.834 1.00 26.86 ?  257  TYR B CD1   1 
ATOM   11016 C CD2   . TYR B 1 259  ? -11.859 0.204   119.428 1.00 28.51 ?  257  TYR B CD2   1 
ATOM   11017 C CE1   . TYR B 1 259  ? -11.686 1.102   116.821 1.00 26.23 ?  257  TYR B CE1   1 
ATOM   11018 C CE2   . TYR B 1 259  ? -11.498 -0.670  118.420 1.00 27.08 ?  257  TYR B CE2   1 
ATOM   11019 C CZ    . TYR B 1 259  ? -11.414 -0.210  117.116 1.00 29.42 ?  257  TYR B CZ    1 
ATOM   11020 O OH    . TYR B 1 259  ? -11.056 -1.057  116.096 1.00 31.36 ?  257  TYR B OH    1 
ATOM   11021 N N     . GLU B 1 260  ? -11.760 3.970   122.880 1.00 25.91 ?  258  GLU B N     1 
ATOM   11022 C CA    . GLU B 1 260  ? -12.048 4.850   124.007 1.00 26.97 ?  258  GLU B CA    1 
ATOM   11023 C C     . GLU B 1 260  ? -10.845 5.732   124.330 1.00 25.40 ?  258  GLU B C     1 
ATOM   11024 O O     . GLU B 1 260  ? -11.008 6.897   124.710 1.00 28.52 ?  258  GLU B O     1 
ATOM   11025 C CB    . GLU B 1 260  ? -12.465 4.029   125.232 1.00 26.98 ?  258  GLU B CB    1 
ATOM   11026 C CG    . GLU B 1 260  ? -12.868 4.871   126.433 1.00 33.92 ?  258  GLU B CG    1 
ATOM   11027 C CD    . GLU B 1 260  ? -12.995 4.044   127.698 1.00 34.52 ?  258  GLU B CD    1 
ATOM   11028 O OE1   . GLU B 1 260  ? -13.117 2.801   127.582 1.00 39.15 ?  258  GLU B OE1   1 
ATOM   11029 O OE2   . GLU B 1 260  ? -12.964 4.628   128.809 1.00 33.21 ?  258  GLU B OE2   1 
ATOM   11030 N N     . GLY B 1 261  ? -9.639  5.201   124.160 1.00 26.83 ?  259  GLY B N     1 
ATOM   11031 C CA    . GLY B 1 261  ? -8.446  5.885   124.594 1.00 28.01 ?  259  GLY B CA    1 
ATOM   11032 C C     . GLY B 1 261  ? -7.949  6.872   123.567 1.00 24.02 ?  259  GLY B C     1 
ATOM   11033 O O     . GLY B 1 261  ? -8.332  6.856   122.386 1.00 22.80 ?  259  GLY B O     1 
ATOM   11034 N N     . PRO B 1 262  ? -7.066  7.759   124.009 1.00 21.63 ?  260  PRO B N     1 
ATOM   11035 C CA    . PRO B 1 262  ? -6.551  8.802   123.121 1.00 20.85 ?  260  PRO B CA    1 
ATOM   11036 C C     . PRO B 1 262  ? -5.500  8.263   122.165 1.00 20.49 ?  260  PRO B C     1 
ATOM   11037 O O     . PRO B 1 262  ? -4.900  7.207   122.380 1.00 23.70 ?  260  PRO B O     1 
ATOM   11038 C CB    . PRO B 1 262  ? -5.935  9.813   124.099 1.00 21.42 ?  260  PRO B CB    1 
ATOM   11039 C CG    . PRO B 1 262  ? -5.474  8.950   125.232 1.00 22.52 ?  260  PRO B CG    1 
ATOM   11040 C CD    . PRO B 1 262  ? -6.552  7.903   125.385 1.00 23.12 ?  260  PRO B CD    1 
ATOM   11041 N N     . GLY B 1 263  ? -5.282  9.026   121.096 1.00 21.93 ?  261  GLY B N     1 
ATOM   11042 C CA    . GLY B 1 263  ? -4.266  8.703   120.114 1.00 19.43 ?  261  GLY B CA    1 
ATOM   11043 C C     . GLY B 1 263  ? -3.461  9.924   119.732 1.00 18.77 ?  261  GLY B C     1 
ATOM   11044 O O     . GLY B 1 263  ? -3.629  10.991  120.328 1.00 19.47 ?  261  GLY B O     1 
ATOM   11045 N N     . ILE B 1 264  ? -2.593  9.780   118.738 1.00 18.36 ?  262  ILE B N     1 
ATOM   11046 C CA    . ILE B 1 264  ? -1.768  10.875  118.248 1.00 18.15 ?  262  ILE B CA    1 
ATOM   11047 C C     . ILE B 1 264  ? -1.928  10.973  116.737 1.00 19.29 ?  262  ILE B C     1 
ATOM   11048 O O     . ILE B 1 264  ? -2.242  9.984   116.063 1.00 18.20 ?  262  ILE B O     1 
ATOM   11049 C CB    . ILE B 1 264  ? -0.284  10.680  118.654 1.00 21.25 ?  262  ILE B CB    1 
ATOM   11050 C CG1   . ILE B 1 264  ? 0.513   11.969  118.500 1.00 17.32 ?  262  ILE B CG1   1 
ATOM   11051 C CG2   . ILE B 1 264  ? 0.372   9.548   117.858 1.00 20.08 ?  262  ILE B CG2   1 
ATOM   11052 C CD1   . ILE B 1 264  ? 1.944   11.831  118.974 1.00 18.32 ?  262  ILE B CD1   1 
ATOM   11053 N N     . SER B 1 265  ? -1.752  12.189  116.210 1.00 16.74 ?  263  SER B N     1 
ATOM   11054 C CA    . SER B 1 265  ? -1.717  12.446  114.774 1.00 16.25 ?  263  SER B CA    1 
ATOM   11055 C C     . SER B 1 265  ? -0.358  13.020  114.413 1.00 18.21 ?  263  SER B C     1 
ATOM   11056 O O     . SER B 1 265  ? 0.212   13.807  115.175 1.00 22.09 ?  263  SER B O     1 
ATOM   11057 C CB    . SER B 1 265  ? -2.817  13.411  114.344 1.00 19.75 ?  263  SER B CB    1 
ATOM   11058 O OG    . SER B 1 265  ? -4.090  12.789  114.402 1.00 21.72 ?  263  SER B OG    1 
ATOM   11059 N N     . ILE B 1 266  ? 0.178   12.583  113.272 1.00 15.58 ?  264  ILE B N     1 
ATOM   11060 C CA    . ILE B 1 266  ? 1.480   13.034  112.800 1.00 15.72 ?  264  ILE B CA    1 
ATOM   11061 C C     . ILE B 1 266  ? 1.348   13.502  111.360 1.00 16.07 ?  264  ILE B C     1 
ATOM   11062 O O     . ILE B 1 266  ? 0.429   13.124  110.634 1.00 15.68 ?  264  ILE B O     1 
ATOM   11063 C CB    . ILE B 1 266  ? 2.562   11.939  112.891 1.00 16.75 ?  264  ILE B CB    1 
ATOM   11064 C CG1   . ILE B 1 266  ? 2.258   10.817  111.888 1.00 17.36 ?  264  ILE B CG1   1 
ATOM   11065 C CG2   . ILE B 1 266  ? 2.692   11.422  114.325 1.00 16.78 ?  264  ILE B CG2   1 
ATOM   11066 C CD1   . ILE B 1 266  ? 3.362   9.788   111.755 1.00 19.84 ?  264  ILE B CD1   1 
ATOM   11067 N N     . LYS B 1 267  ? 2.297   14.335  110.945 1.00 15.18 ?  265  LYS B N     1 
ATOM   11068 C CA    . LYS B 1 267  ? 2.438   14.706  109.545 1.00 13.85 ?  265  LYS B CA    1 
ATOM   11069 C C     . LYS B 1 267  ? 3.763   14.172  109.030 1.00 14.38 ?  265  LYS B C     1 
ATOM   11070 O O     . LYS B 1 267  ? 4.809   14.421  109.634 1.00 15.89 ?  265  LYS B O     1 
ATOM   11071 C CB    . LYS B 1 267  ? 2.352   16.226  109.363 1.00 17.84 ?  265  LYS B CB    1 
ATOM   11072 C CG    . LYS B 1 267  ? 0.934   16.777  109.486 1.00 20.08 ?  265  LYS B CG    1 
ATOM   11073 C CD    . LYS B 1 267  ? 0.906   18.284  109.287 1.00 25.12 ?  265  LYS B CD    1 
ATOM   11074 C CE    . LYS B 1 267  ? -0.510  18.827  109.285 1.00 25.59 ?  265  LYS B CE    1 
ATOM   11075 N NZ    . LYS B 1 267  ? -1.239  18.478  110.536 1.00 28.87 ?  265  LYS B NZ    1 
ATOM   11076 N N     . LEU B 1 268  ? 3.724   13.452  107.899 1.00 15.61 ?  266  LEU B N     1 
ATOM   11077 C CA    . LEU B 1 268  ? 4.963   12.908  107.355 1.00 14.69 ?  266  LEU B CA    1 
ATOM   11078 C C     . LEU B 1 268  ? 5.947   14.012  106.968 1.00 14.82 ?  266  LEU B C     1 
ATOM   11079 O O     . LEU B 1 268  ? 7.163   13.814  107.094 1.00 14.76 ?  266  LEU B O     1 
ATOM   11080 C CB    . LEU B 1 268  ? 4.666   11.995  106.162 1.00 14.86 ?  266  LEU B CB    1 
ATOM   11081 C CG    . LEU B 1 268  ? 3.809   10.766  106.499 1.00 15.44 ?  266  LEU B CG    1 
ATOM   11082 C CD1   . LEU B 1 268  ? 3.676   9.906   105.262 1.00 16.27 ?  266  LEU B CD1   1 
ATOM   11083 C CD2   . LEU B 1 268  ? 4.392   9.964   107.650 1.00 17.45 ?  266  LEU B CD2   1 
ATOM   11084 N N     . SER B 1 269  ? 5.454   15.191  106.557 1.00 15.10 ?  267  SER B N     1 
ATOM   11085 C CA    . SER B 1 269  ? 6.359   16.288  106.204 1.00 13.98 ?  267  SER B CA    1 
ATOM   11086 C C     . SER B 1 269  ? 7.172   16.779  107.401 1.00 13.91 ?  267  SER B C     1 
ATOM   11087 O O     . SER B 1 269  ? 8.196   17.442  107.202 1.00 16.16 ?  267  SER B O     1 
ATOM   11088 C CB    . SER B 1 269  ? 5.583   17.461  105.595 1.00 16.32 ?  267  SER B CB    1 
ATOM   11089 O OG    . SER B 1 269  ? 4.802   18.099  106.591 1.00 16.44 ?  267  SER B OG    1 
ATOM   11090 N N     . ALA B 1 270  ? 6.746   16.471  108.625 1.00 13.38 ?  268  ALA B N     1 
ATOM   11091 C CA    . ALA B 1 270  ? 7.525   16.822  109.804 1.00 14.25 ?  268  ALA B CA    1 
ATOM   11092 C C     . ALA B 1 270  ? 8.728   15.916  109.986 1.00 14.95 ?  268  ALA B C     1 
ATOM   11093 O O     . ALA B 1 270  ? 9.668   16.289  110.692 1.00 14.96 ?  268  ALA B O     1 
ATOM   11094 C CB    . ALA B 1 270  ? 6.656   16.748  111.070 1.00 15.62 ?  268  ALA B CB    1 
ATOM   11095 N N     . LEU B 1 271  ? 8.730   14.741  109.364 1.00 14.57 ?  269  LEU B N     1 
ATOM   11096 C CA    . LEU B 1 271  ? 9.705   13.718  109.702 1.00 13.95 ?  269  LEU B CA    1 
ATOM   11097 C C     . LEU B 1 271  ? 10.847  13.624  108.704 1.00 13.86 ?  269  LEU B C     1 
ATOM   11098 O O     . LEU B 1 271  ? 11.757  12.807  108.904 1.00 17.14 ?  269  LEU B O     1 
ATOM   11099 C CB    . LEU B 1 271  ? 9.012   12.364  109.841 1.00 15.39 ?  269  LEU B CB    1 
ATOM   11100 C CG    . LEU B 1 271  ? 8.088   12.298  111.055 1.00 15.96 ?  269  LEU B CG    1 
ATOM   11101 C CD1   . LEU B 1 271  ? 7.312   10.992  110.988 1.00 20.57 ?  269  LEU B CD1   1 
ATOM   11102 C CD2   . LEU B 1 271  ? 8.859   12.387  112.360 1.00 17.16 ?  269  LEU B CD2   1 
ATOM   11103 N N     . HIS B 1 272  ? 10.838  14.457  107.662 1.00 16.24 ?  270  HIS B N     1 
ATOM   11104 C CA    . HIS B 1 272  ? 11.951  14.451  106.736 1.00 16.07 ?  270  HIS B CA    1 
ATOM   11105 C C     . HIS B 1 272  ? 11.963  15.777  106.007 1.00 14.25 ?  270  HIS B C     1 
ATOM   11106 O O     . HIS B 1 272  ? 10.889  16.277  105.651 1.00 16.11 ?  270  HIS B O     1 
ATOM   11107 C CB    . HIS B 1 272  ? 11.833  13.300  105.737 1.00 15.71 ?  270  HIS B CB    1 
ATOM   11108 C CG    . HIS B 1 272  ? 13.122  12.987  105.060 1.00 18.81 ?  270  HIS B CG    1 
ATOM   11109 N ND1   . HIS B 1 272  ? 13.594  13.712  103.988 1.00 18.60 ?  270  HIS B ND1   1 
ATOM   11110 C CD2   . HIS B 1 272  ? 14.062  12.053  105.331 1.00 20.66 ?  270  HIS B CD2   1 
ATOM   11111 C CE1   . HIS B 1 272  ? 14.766  13.226  103.618 1.00 22.01 ?  270  HIS B CE1   1 
ATOM   11112 N NE2   . HIS B 1 272  ? 15.070  12.216  104.413 1.00 22.63 ?  270  HIS B NE2   1 
ATOM   11113 N N     . PRO B 1 273  ? 13.134  16.366  105.754 1.00 14.21 ?  271  PRO B N     1 
ATOM   11114 C CA    . PRO B 1 273  ? 13.171  17.650  105.046 1.00 14.18 ?  271  PRO B CA    1 
ATOM   11115 C C     . PRO B 1 273  ? 12.923  17.550  103.543 1.00 14.59 ?  271  PRO B C     1 
ATOM   11116 O O     . PRO B 1 273  ? 12.690  18.589  102.917 1.00 16.30 ?  271  PRO B O     1 
ATOM   11117 C CB    . PRO B 1 273  ? 14.592  18.163  105.344 1.00 16.88 ?  271  PRO B CB    1 
ATOM   11118 C CG    . PRO B 1 273  ? 15.384  16.942  105.564 1.00 18.98 ?  271  PRO B CG    1 
ATOM   11119 C CD    . PRO B 1 273  ? 14.460  15.981  106.271 1.00 15.79 ?  271  PRO B CD    1 
ATOM   11120 N N     . ARG B 1 274  ? 12.954  16.353  102.948 1.00 14.94 ?  272  ARG B N     1 
ATOM   11121 C CA    . ARG B 1 274  ? 12.741  16.174  101.511 1.00 14.50 ?  272  ARG B CA    1 
ATOM   11122 C C     . ARG B 1 274  ? 11.636  15.152  101.268 1.00 15.18 ?  272  ARG B C     1 
ATOM   11123 O O     . ARG B 1 274  ? 11.814  14.155  100.573 1.00 16.52 ?  272  ARG B O     1 
ATOM   11124 C CB    . ARG B 1 274  ? 14.034  15.759  100.805 1.00 15.42 ?  272  ARG B CB    1 
ATOM   11125 C CG    . ARG B 1 274  ? 15.172  16.785  100.911 1.00 16.90 ?  272  ARG B CG    1 
ATOM   11126 C CD    . ARG B 1 274  ? 14.800  18.141  100.295 1.00 15.57 ?  272  ARG B CD    1 
ATOM   11127 N NE    . ARG B 1 274  ? 14.269  18.028  98.938  1.00 16.90 ?  272  ARG B NE    1 
ATOM   11128 C CZ    . ARG B 1 274  ? 15.017  17.913  97.845  1.00 16.11 ?  272  ARG B CZ    1 
ATOM   11129 N NH1   . ARG B 1 274  ? 16.338  17.841  97.913  1.00 16.54 ?  272  ARG B NH1   1 
ATOM   11130 N NH2   . ARG B 1 274  ? 14.424  17.869  96.651  1.00 15.69 ?  272  ARG B NH2   1 
ATOM   11131 N N     . TYR B 1 275  ? 10.475  15.380  101.877 1.00 15.34 ?  273  TYR B N     1 
ATOM   11132 C CA    . TYR B 1 275  ? 9.330   14.483  101.723 1.00 17.02 ?  273  TYR B CA    1 
ATOM   11133 C C     . TYR B 1 275  ? 8.648   14.803  100.396 1.00 16.58 ?  273  TYR B C     1 
ATOM   11134 O O     . TYR B 1 275  ? 7.790   15.677  100.305 1.00 15.42 ?  273  TYR B O     1 
ATOM   11135 C CB    . TYR B 1 275  ? 8.385   14.626  102.913 1.00 15.27 ?  273  TYR B CB    1 
ATOM   11136 C CG    . TYR B 1 275  ? 7.118   13.809  102.793 1.00 14.26 ?  273  TYR B CG    1 
ATOM   11137 C CD1   . TYR B 1 275  ? 7.165   12.459  102.462 1.00 15.93 ?  273  TYR B CD1   1 
ATOM   11138 C CD2   . TYR B 1 275  ? 5.882   14.388  103.012 1.00 15.31 ?  273  TYR B CD2   1 
ATOM   11139 C CE1   . TYR B 1 275  ? 6.017   11.710  102.343 1.00 15.37 ?  273  TYR B CE1   1 
ATOM   11140 C CE2   . TYR B 1 275  ? 4.712   13.643  102.892 1.00 14.69 ?  273  TYR B CE2   1 
ATOM   11141 C CZ    . TYR B 1 275  ? 4.792   12.313  102.546 1.00 15.95 ?  273  TYR B CZ    1 
ATOM   11142 O OH    . TYR B 1 275  ? 3.641   11.576  102.423 1.00 17.05 ?  273  TYR B OH    1 
ATOM   11143 N N     . SER B 1 276  ? 9.048   14.098  99.336  1.00 13.87 ?  274  SER B N     1 
ATOM   11144 C CA    . SER B 1 276  ? 8.477   14.334  98.013  1.00 13.87 ?  274  SER B CA    1 
ATOM   11145 C C     . SER B 1 276  ? 8.726   13.123  97.132  1.00 14.53 ?  274  SER B C     1 
ATOM   11146 O O     . SER B 1 276  ? 9.644   12.336  97.376  1.00 16.02 ?  274  SER B O     1 
ATOM   11147 C CB    . SER B 1 276  ? 9.089   15.567  97.361  1.00 19.31 ?  274  SER B CB    1 
ATOM   11148 O OG    . SER B 1 276  ? 10.435  15.291  97.024  1.00 21.25 ?  274  SER B OG    1 
ATOM   11149 N N     . ARG B 1 277  ? 7.899   12.991  96.094  1.00 15.59 ?  275  ARG B N     1 
ATOM   11150 C CA    . ARG B 1 277  ? 8.088   11.894  95.154  1.00 15.55 ?  275  ARG B CA    1 
ATOM   11151 C C     . ARG B 1 277  ? 9.462   11.936  94.495  1.00 14.70 ?  275  ARG B C     1 
ATOM   11152 O O     . ARG B 1 277  ? 10.040  10.875  94.213  1.00 15.77 ?  275  ARG B O     1 
ATOM   11153 C CB    . ARG B 1 277  ? 6.986   11.913  94.097  1.00 13.70 ?  275  ARG B CB    1 
ATOM   11154 C CG    . ARG B 1 277  ? 7.160   10.912  92.940  1.00 14.86 ?  275  ARG B CG    1 
ATOM   11155 C CD    . ARG B 1 277  ? 7.174   9.451   93.416  1.00 14.92 ?  275  ARG B CD    1 
ATOM   11156 N NE    . ARG B 1 277  ? 7.320   8.526   92.290  1.00 15.29 ?  275  ARG B NE    1 
ATOM   11157 C CZ    . ARG B 1 277  ? 8.481   8.178   91.756  1.00 17.57 ?  275  ARG B CZ    1 
ATOM   11158 N NH1   . ARG B 1 277  ? 9.623   8.697   92.187  1.00 17.65 ?  275  ARG B NH1   1 
ATOM   11159 N NH2   . ARG B 1 277  ? 8.501   7.263   90.790  1.00 17.11 ?  275  ARG B NH2   1 
ATOM   11160 N N     . ALA B 1 278  ? 10.011  13.133  94.265  1.00 15.14 ?  276  ALA B N     1 
ATOM   11161 C CA    . ALA B 1 278  ? 11.322  13.209  93.630  1.00 16.37 ?  276  ALA B CA    1 
ATOM   11162 C C     . ALA B 1 278  ? 12.397  12.582  94.499  1.00 16.74 ?  276  ALA B C     1 
ATOM   11163 O O     . ALA B 1 278  ? 13.416  12.113  93.983  1.00 17.69 ?  276  ALA B O     1 
ATOM   11164 C CB    . ALA B 1 278  ? 11.679  14.661  93.305  1.00 17.02 ?  276  ALA B CB    1 
ATOM   11165 N N     . GLN B 1 279  ? 12.184  12.548  95.814  1.00 15.35 ?  277  GLN B N     1 
ATOM   11166 C CA    . GLN B 1 279  ? 13.139  11.963  96.743  1.00 13.73 ?  277  GLN B CA    1 
ATOM   11167 C C     . GLN B 1 279  ? 12.600  10.678  97.363  1.00 15.07 ?  277  GLN B C     1 
ATOM   11168 O O     . GLN B 1 279  ? 12.918  10.354  98.512  1.00 15.89 ?  277  GLN B O     1 
ATOM   11169 C CB    . GLN B 1 279  ? 13.513  12.973  97.831  1.00 18.05 ?  277  GLN B CB    1 
ATOM   11170 C CG    . GLN B 1 279  ? 14.105  14.253  97.275  1.00 18.17 ?  277  GLN B CG    1 
ATOM   11171 C CD    . GLN B 1 279  ? 15.411  14.000  96.540  1.00 22.14 ?  277  GLN B CD    1 
ATOM   11172 O OE1   . GLN B 1 279  ? 16.161  13.077  96.877  1.00 25.86 ?  277  GLN B OE1   1 
ATOM   11173 N NE2   . GLN B 1 279  ? 15.673  14.791  95.505  1.00 17.78 ?  277  GLN B NE2   1 
ATOM   11174 N N     . ALA B 1 280  ? 11.817  9.920   96.589  1.00 16.39 ?  278  ALA B N     1 
ATOM   11175 C CA    . ALA B 1 280  ? 11.141  8.740   97.120  1.00 16.04 ?  278  ALA B CA    1 
ATOM   11176 C C     . ALA B 1 280  ? 12.105  7.770   97.793  1.00 17.16 ?  278  ALA B C     1 
ATOM   11177 O O     . ALA B 1 280  ? 11.781  7.199   98.837  1.00 17.24 ?  278  ALA B O     1 
ATOM   11178 C CB    . ALA B 1 280  ? 10.378  8.032   95.998  1.00 18.75 ?  278  ALA B CB    1 
ATOM   11179 N N     . ALA B 1 281  ? 13.287  7.561   97.204  1.00 17.44 ?  279  ALA B N     1 
ATOM   11180 C CA    . ALA B 1 281  ? 14.242  6.623   97.790  1.00 20.12 ?  279  ALA B CA    1 
ATOM   11181 C C     . ALA B 1 281  ? 14.668  7.066   99.183  1.00 20.68 ?  279  ALA B C     1 
ATOM   11182 O O     . ALA B 1 281  ? 14.749  6.244   100.103 1.00 20.13 ?  279  ALA B O     1 
ATOM   11183 C CB    . ALA B 1 281  ? 15.456  6.467   96.875  1.00 22.95 ?  279  ALA B CB    1 
ATOM   11184 N N     . ARG B 1 282  ? 14.945  8.362   99.361  1.00 18.65 ?  280  ARG B N     1 
ATOM   11185 C CA    . ARG B 1 282  ? 15.285  8.868   100.689 1.00 17.65 ?  280  ARG B CA    1 
ATOM   11186 C C     . ARG B 1 282  ? 14.105  8.774   101.639 1.00 17.33 ?  280  ARG B C     1 
ATOM   11187 O O     . ARG B 1 282  ? 14.294  8.557   102.842 1.00 18.11 ?  280  ARG B O     1 
ATOM   11188 C CB    . ARG B 1 282  ? 15.763  10.319  100.611 1.00 19.11 ?  280  ARG B CB    1 
ATOM   11189 C CG    . ARG B 1 282  ? 17.117  10.519  99.925  1.00 19.49 ?  280  ARG B CG    1 
ATOM   11190 C CD    . ARG B 1 282  ? 17.667  11.926  100.211 1.00 18.43 ?  280  ARG B CD    1 
ATOM   11191 N NE    . ARG B 1 282  ? 17.936  12.129  101.633 1.00 19.85 ?  280  ARG B NE    1 
ATOM   11192 C CZ    . ARG B 1 282  ? 18.098  13.315  102.200 1.00 22.03 ?  280  ARG B CZ    1 
ATOM   11193 N NH1   . ARG B 1 282  ? 18.004  14.434  101.499 1.00 21.27 ?  280  ARG B NH1   1 
ATOM   11194 N NH2   . ARG B 1 282  ? 18.347  13.381  103.507 1.00 22.42 ?  280  ARG B NH2   1 
ATOM   11195 N N     . VAL B 1 283  ? 12.888  8.970   101.129 1.00 16.31 ?  281  VAL B N     1 
ATOM   11196 C CA    . VAL B 1 283  ? 11.707  8.868   101.976 1.00 16.96 ?  281  VAL B CA    1 
ATOM   11197 C C     . VAL B 1 283  ? 11.563  7.450   102.509 1.00 17.92 ?  281  VAL B C     1 
ATOM   11198 O O     . VAL B 1 283  ? 11.372  7.236   103.710 1.00 18.32 ?  281  VAL B O     1 
ATOM   11199 C CB    . VAL B 1 283  ? 10.457  9.321   101.203 1.00 16.19 ?  281  VAL B CB    1 
ATOM   11200 C CG1   . VAL B 1 283  ? 9.190   8.918   101.954 1.00 18.28 ?  281  VAL B CG1   1 
ATOM   11201 C CG2   . VAL B 1 283  ? 10.511  10.831  100.987 1.00 17.56 ?  281  VAL B CG2   1 
ATOM   11202 N N     . MET B 1 284  ? 11.680  6.452   101.627 1.00 17.72 ?  282  MET B N     1 
ATOM   11203 C CA    . MET B 1 284  ? 11.540  5.072   102.083 1.00 16.94 ?  282  MET B CA    1 
ATOM   11204 C C     . MET B 1 284  ? 12.710  4.636   102.961 1.00 20.21 ?  282  MET B C     1 
ATOM   11205 O O     . MET B 1 284  ? 12.544  3.770   103.834 1.00 22.15 ?  282  MET B O     1 
ATOM   11206 C CB    . MET B 1 284  ? 11.410  4.129   100.885 1.00 18.24 ?  282  MET B CB    1 
ATOM   11207 C CG    . MET B 1 284  ? 10.236  4.425   99.973  1.00 21.47 ?  282  MET B CG    1 
ATOM   11208 S SD    . MET B 1 284  ? 8.650   4.381   100.821 1.00 22.36 ?  282  MET B SD    1 
ATOM   11209 C CE    . MET B 1 284  ? 8.510   2.656   101.262 1.00 24.95 ?  282  MET B CE    1 
ATOM   11210 N N     . GLY B 1 285  ? 13.889  5.209   102.748 1.00 20.07 ?  283  GLY B N     1 
ATOM   11211 C CA    . GLY B 1 285  ? 15.063  4.771   103.476 1.00 20.06 ?  283  GLY B CA    1 
ATOM   11212 C C     . GLY B 1 285  ? 15.252  5.463   104.812 1.00 20.70 ?  283  GLY B C     1 
ATOM   11213 O O     . GLY B 1 285  ? 15.856  4.903   105.737 1.00 23.62 ?  283  GLY B O     1 
ATOM   11214 N N     . GLU B 1 286  ? 14.730  6.681   104.927 1.00 19.57 ?  284  GLU B N     1 
ATOM   11215 C CA    . GLU B 1 286  ? 14.987  7.535   106.079 1.00 18.06 ?  284  GLU B CA    1 
ATOM   11216 C C     . GLU B 1 286  ? 13.732  7.963   106.822 1.00 20.01 ?  284  GLU B C     1 
ATOM   11217 O O     . GLU B 1 286  ? 13.738  7.989   108.057 1.00 23.00 ?  284  GLU B O     1 
ATOM   11218 C CB    . GLU B 1 286  ? 15.758  8.785   105.637 1.00 20.22 ?  284  GLU B CB    1 
ATOM   11219 C CG    . GLU B 1 286  ? 17.074  8.475   104.912 1.00 19.90 ?  284  GLU B CG    1 
ATOM   11220 C CD    . GLU B 1 286  ? 17.648  9.697   104.216 1.00 24.13 ?  284  GLU B CD    1 
ATOM   11221 O OE1   . GLU B 1 286  ? 17.420  10.820  104.708 1.00 25.29 ?  284  GLU B OE1   1 
ATOM   11222 O OE2   . GLU B 1 286  ? 18.318  9.539   103.174 1.00 26.43 ?  284  GLU B OE2   1 
ATOM   11223 N N     . LEU B 1 287  ? 12.664  8.315   106.106 1.00 19.74 ?  285  LEU B N     1 
ATOM   11224 C CA    . LEU B 1 287  ? 11.420  8.701   106.760 1.00 19.21 ?  285  LEU B CA    1 
ATOM   11225 C C     . LEU B 1 287  ? 10.689  7.478   107.301 1.00 18.69 ?  285  LEU B C     1 
ATOM   11226 O O     . LEU B 1 287  ? 10.285  7.457   108.468 1.00 19.33 ?  285  LEU B O     1 
ATOM   11227 C CB    . LEU B 1 287  ? 10.531  9.488   105.786 1.00 16.66 ?  285  LEU B CB    1 
ATOM   11228 C CG    . LEU B 1 287  ? 9.511   10.491  106.351 1.00 19.54 ?  285  LEU B CG    1 
ATOM   11229 C CD1   . LEU B 1 287  ? 8.890   11.320  105.256 1.00 17.44 ?  285  LEU B CD1   1 
ATOM   11230 C CD2   . LEU B 1 287  ? 8.412   9.783   107.130 1.00 19.77 ?  285  LEU B CD2   1 
ATOM   11231 N N     . LEU B 1 288  ? 10.505  6.454   106.465 1.00 19.83 ?  286  LEU B N     1 
ATOM   11232 C CA    . LEU B 1 288  ? 9.757   5.265   106.871 1.00 19.74 ?  286  LEU B CA    1 
ATOM   11233 C C     . LEU B 1 288  ? 10.241  4.656   108.182 1.00 21.14 ?  286  LEU B C     1 
ATOM   11234 O O     . LEU B 1 288  ? 9.396   4.362   109.041 1.00 19.89 ?  286  LEU B O     1 
ATOM   11235 C CB    . LEU B 1 288  ? 9.793   4.230   105.737 1.00 20.57 ?  286  LEU B CB    1 
ATOM   11236 C CG    . LEU B 1 288  ? 9.245   2.840   106.057 1.00 24.41 ?  286  LEU B CG    1 
ATOM   11237 C CD1   . LEU B 1 288  ? 7.797   2.923   106.529 1.00 23.83 ?  286  LEU B CD1   1 
ATOM   11238 C CD2   . LEU B 1 288  ? 9.353   1.959   104.821 1.00 29.35 ?  286  LEU B CD2   1 
ATOM   11239 N N     . PRO B 1 289  ? 11.542  4.447   108.417 1.00 20.27 ?  287  PRO B N     1 
ATOM   11240 C CA    . PRO B 1 289  ? 11.945  3.864   109.709 1.00 20.98 ?  287  PRO B CA    1 
ATOM   11241 C C     . PRO B 1 289  ? 11.544  4.711   110.904 1.00 20.09 ?  287  PRO B C     1 
ATOM   11242 O O     . PRO B 1 289  ? 11.332  4.168   111.999 1.00 23.19 ?  287  PRO B O     1 
ATOM   11243 C CB    . PRO B 1 289  ? 13.469  3.752   109.574 1.00 23.83 ?  287  PRO B CB    1 
ATOM   11244 C CG    . PRO B 1 289  ? 13.691  3.635   108.094 1.00 23.78 ?  287  PRO B CG    1 
ATOM   11245 C CD    . PRO B 1 289  ? 12.686  4.558   107.493 1.00 23.19 ?  287  PRO B CD    1 
ATOM   11246 N N     . ARG B 1 290  ? 11.449  6.030   110.730 1.00 19.38 ?  288  ARG B N     1 
ATOM   11247 C CA    . ARG B 1 290  ? 10.980  6.878   111.816 1.00 18.92 ?  288  ARG B CA    1 
ATOM   11248 C C     . ARG B 1 290  ? 9.509   6.616   112.105 1.00 16.79 ?  288  ARG B C     1 
ATOM   11249 O O     . ARG B 1 290  ? 9.117   6.459   113.269 1.00 19.14 ?  288  ARG B O     1 
ATOM   11250 C CB    . ARG B 1 290  ? 11.222  8.350   111.480 1.00 20.35 ?  288  ARG B CB    1 
ATOM   11251 C CG    . ARG B 1 290  ? 12.676  8.736   111.616 1.00 22.89 ?  288  ARG B CG    1 
ATOM   11252 C CD    . ARG B 1 290  ? 12.925  10.151  111.139 1.00 25.93 ?  288  ARG B CD    1 
ATOM   11253 N NE    . ARG B 1 290  ? 14.268  10.584  111.504 1.00 28.21 ?  288  ARG B NE    1 
ATOM   11254 C CZ    . ARG B 1 290  ? 14.839  11.699  111.071 1.00 26.26 ?  288  ARG B CZ    1 
ATOM   11255 N NH1   . ARG B 1 290  ? 14.214  12.522  110.243 1.00 26.63 ?  288  ARG B NH1   1 
ATOM   11256 N NH2   . ARG B 1 290  ? 16.071  11.991  111.471 1.00 26.99 ?  288  ARG B NH2   1 
ATOM   11257 N N     . VAL B 1 291  ? 8.679   6.545   111.056 1.00 18.56 ?  289  VAL B N     1 
ATOM   11258 C CA    . VAL B 1 291  ? 7.270   6.236   111.282 1.00 18.69 ?  289  VAL B CA    1 
ATOM   11259 C C     . VAL B 1 291  ? 7.120   4.849   111.897 1.00 18.16 ?  289  VAL B C     1 
ATOM   11260 O O     . VAL B 1 291  ? 6.309   4.650   112.808 1.00 18.50 ?  289  VAL B O     1 
ATOM   11261 C CB    . VAL B 1 291  ? 6.453   6.357   109.984 1.00 16.83 ?  289  VAL B CB    1 
ATOM   11262 C CG1   . VAL B 1 291  ? 4.975   6.181   110.297 1.00 20.96 ?  289  VAL B CG1   1 
ATOM   11263 C CG2   . VAL B 1 291  ? 6.685   7.700   109.337 1.00 21.35 ?  289  VAL B CG2   1 
ATOM   11264 N N     . LYS B 1 292  ? 7.888   3.868   111.408 1.00 17.65 ?  290  LYS B N     1 
ATOM   11265 C CA    . LYS B 1 292  ? 7.814   2.529   111.987 1.00 20.38 ?  290  LYS B CA    1 
ATOM   11266 C C     . LYS B 1 292  ? 8.113   2.557   113.482 1.00 20.12 ?  290  LYS B C     1 
ATOM   11267 O O     . LYS B 1 292  ? 7.407   1.922   114.274 1.00 21.17 ?  290  LYS B O     1 
ATOM   11268 C CB    . LYS B 1 292  ? 8.776   1.594   111.252 1.00 20.36 ?  290  LYS B CB    1 
ATOM   11269 C CG    . LYS B 1 292  ? 9.189   0.345   112.010 1.00 30.69 ?  290  LYS B CG    1 
ATOM   11270 C CD    . LYS B 1 292  ? 8.050   -0.611  112.218 1.00 32.11 ?  290  LYS B CD    1 
ATOM   11271 C CE    . LYS B 1 292  ? 8.542   -1.851  112.974 1.00 31.53 ?  290  LYS B CE    1 
ATOM   11272 N NZ    . LYS B 1 292  ? 9.599   -2.598  112.212 1.00 28.09 ?  290  LYS B NZ    1 
ATOM   11273 N N     . ALA B 1 293  ? 9.135   3.315   113.892 1.00 19.71 ?  291  ALA B N     1 
ATOM   11274 C CA    . ALA B 1 293  ? 9.481   3.371   115.310 1.00 21.82 ?  291  ALA B CA    1 
ATOM   11275 C C     . ALA B 1 293  ? 8.363   4.000   116.134 1.00 20.68 ?  291  ALA B C     1 
ATOM   11276 O O     . ALA B 1 293  ? 8.064   3.537   117.245 1.00 22.32 ?  291  ALA B O     1 
ATOM   11277 C CB    . ALA B 1 293  ? 10.789  4.135   115.506 1.00 21.74 ?  291  ALA B CB    1 
ATOM   11278 N N     . LEU B 1 294  ? 7.754   5.072   115.624 1.00 19.35 ?  292  LEU B N     1 
ATOM   11279 C CA    . LEU B 1 294  ? 6.624   5.680   116.317 1.00 18.95 ?  292  LEU B CA    1 
ATOM   11280 C C     . LEU B 1 294  ? 5.433   4.732   116.375 1.00 20.41 ?  292  LEU B C     1 
ATOM   11281 O O     . LEU B 1 294  ? 4.750   4.654   117.401 1.00 20.18 ?  292  LEU B O     1 
ATOM   11282 C CB    . LEU B 1 294  ? 6.232   6.988   115.629 1.00 17.58 ?  292  LEU B CB    1 
ATOM   11283 C CG    . LEU B 1 294  ? 7.328   8.050   115.574 1.00 18.94 ?  292  LEU B CG    1 
ATOM   11284 C CD1   . LEU B 1 294  ? 6.872   9.212   114.734 1.00 17.35 ?  292  LEU B CD1   1 
ATOM   11285 C CD2   . LEU B 1 294  ? 7.692   8.509   116.975 1.00 20.50 ?  292  LEU B CD2   1 
ATOM   11286 N N     . ALA B 1 295  ? 5.171   4.003   115.282 1.00 20.65 ?  293  ALA B N     1 
ATOM   11287 C CA    . ALA B 1 295  ? 4.066   3.045   115.275 1.00 20.01 ?  293  ALA B CA    1 
ATOM   11288 C C     . ALA B 1 295  ? 4.308   1.911   116.260 1.00 21.41 ?  293  ALA B C     1 
ATOM   11289 O O     . ALA B 1 295  ? 3.371   1.431   116.908 1.00 22.58 ?  293  ALA B O     1 
ATOM   11290 C CB    . ALA B 1 295  ? 3.861   2.485   113.866 1.00 19.45 ?  293  ALA B CB    1 
ATOM   11291 N N     . LEU B 1 296  ? 5.560   1.469   116.389 1.00 19.95 ?  294  LEU B N     1 
ATOM   11292 C CA    . LEU B 1 296  ? 5.871   0.405   117.336 1.00 22.67 ?  294  LEU B CA    1 
ATOM   11293 C C     . LEU B 1 296  ? 5.600   0.857   118.767 1.00 22.64 ?  294  LEU B C     1 
ATOM   11294 O O     . LEU B 1 296  ? 5.088   0.085   119.586 1.00 24.10 ?  294  LEU B O     1 
ATOM   11295 C CB    . LEU B 1 296  ? 7.324   -0.033  117.159 1.00 25.41 ?  294  LEU B CB    1 
ATOM   11296 C CG    . LEU B 1 296  ? 7.798   -1.247  117.954 1.00 30.73 ?  294  LEU B CG    1 
ATOM   11297 C CD1   . LEU B 1 296  ? 6.980   -2.464  117.564 1.00 32.33 ?  294  LEU B CD1   1 
ATOM   11298 C CD2   . LEU B 1 296  ? 9.281   -1.499  117.717 1.00 33.46 ?  294  LEU B CD2   1 
ATOM   11299 N N     . LEU B 1 297  ? 5.916   2.116   119.081 1.00 20.44 ?  295  LEU B N     1 
ATOM   11300 C CA    A LEU B 1 297  ? 5.600   2.640   120.405 0.48 22.59 ?  295  LEU B CA    1 
ATOM   11301 C CA    B LEU B 1 297  ? 5.599   2.642   120.406 0.52 22.59 ?  295  LEU B CA    1 
ATOM   11302 C C     . LEU B 1 297  ? 4.093   2.752   120.607 1.00 20.75 ?  295  LEU B C     1 
ATOM   11303 O O     . LEU B 1 297  ? 3.575   2.392   121.674 1.00 22.00 ?  295  LEU B O     1 
ATOM   11304 C CB    A LEU B 1 297  ? 6.275   3.995   120.607 0.48 20.79 ?  295  LEU B CB    1 
ATOM   11305 C CB    B LEU B 1 297  ? 6.267   4.002   120.611 0.52 20.78 ?  295  LEU B CB    1 
ATOM   11306 C CG    A LEU B 1 297  ? 6.384   4.459   122.057 0.48 21.71 ?  295  LEU B CG    1 
ATOM   11307 C CG    B LEU B 1 297  ? 7.796   4.019   120.573 0.52 22.57 ?  295  LEU B CG    1 
ATOM   11308 C CD1   A LEU B 1 297  ? 7.108   3.421   122.900 0.48 22.81 ?  295  LEU B CD1   1 
ATOM   11309 C CD1   B LEU B 1 297  ? 8.306   5.440   120.720 0.52 20.72 ?  295  LEU B CD1   1 
ATOM   11310 C CD2   A LEU B 1 297  ? 7.093   5.808   122.114 0.48 22.97 ?  295  LEU B CD2   1 
ATOM   11311 C CD2   B LEU B 1 297  ? 8.389   3.114   121.643 0.52 23.38 ?  295  LEU B CD2   1 
ATOM   11312 N N     . ALA B 1 298  ? 3.374   3.233   119.588 1.00 22.08 ?  296  ALA B N     1 
ATOM   11313 C CA    . ALA B 1 298  ? 1.922   3.335   119.675 1.00 21.03 ?  296  ALA B CA    1 
ATOM   11314 C C     . ALA B 1 298  ? 1.291   1.968   119.882 1.00 23.10 ?  296  ALA B C     1 
ATOM   11315 O O     . ALA B 1 298  ? 0.355   1.823   120.676 1.00 23.41 ?  296  ALA B O     1 
ATOM   11316 C CB    . ALA B 1 298  ? 1.359   3.992   118.413 1.00 19.82 ?  296  ALA B CB    1 
ATOM   11317 N N     . LYS B 1 299  ? 1.794   0.953   119.178 1.00 21.24 ?  297  LYS B N     1 
ATOM   11318 C CA    . LYS B 1 299  ? 1.300   -0.405  119.386 1.00 25.17 ?  297  LYS B CA    1 
ATOM   11319 C C     . LYS B 1 299  ? 1.539   -0.864  120.812 1.00 25.49 ?  297  LYS B C     1 
ATOM   11320 O O     . LYS B 1 299  ? 0.661   -1.479  121.437 1.00 27.87 ?  297  LYS B O     1 
ATOM   11321 C CB    . LYS B 1 299  ? 1.974   -1.376  118.423 1.00 22.74 ?  297  LYS B CB    1 
ATOM   11322 C CG    . LYS B 1 299  ? 1.744   -2.824  118.827 1.00 26.75 ?  297  LYS B CG    1 
ATOM   11323 C CD    . LYS B 1 299  ? 2.428   -3.824  117.933 1.00 32.15 ?  297  LYS B CD    1 
ATOM   11324 C CE    . LYS B 1 299  ? 2.149   -5.231  118.448 1.00 33.98 ?  297  LYS B CE    1 
ATOM   11325 N NZ    . LYS B 1 299  ? 2.603   -6.273  117.488 1.00 38.75 ?  297  LYS B NZ    1 
ATOM   11326 N N     . ASN B 1 300  ? 2.729   -0.587  121.343 1.00 24.04 ?  298  ASN B N     1 
ATOM   11327 C CA    . ASN B 1 300  ? 3.059   -1.092  122.666 1.00 24.78 ?  298  ASN B CA    1 
ATOM   11328 C C     . ASN B 1 300  ? 2.130   -0.524  123.724 1.00 24.90 ?  298  ASN B C     1 
ATOM   11329 O O     . ASN B 1 300  ? 1.838   -1.201  124.711 1.00 27.40 ?  298  ASN B O     1 
ATOM   11330 C CB    . ASN B 1 300  ? 4.522   -0.795  122.993 1.00 30.28 ?  298  ASN B CB    1 
ATOM   11331 C CG    . ASN B 1 300  ? 5.482   -1.570  122.095 1.00 38.49 ?  298  ASN B CG    1 
ATOM   11332 O OD1   . ASN B 1 300  ? 5.127   -2.615  121.541 1.00 44.16 ?  298  ASN B OD1   1 
ATOM   11333 N ND2   . ASN B 1 300  ? 6.699   -1.053  121.938 1.00 40.31 ?  298  ASN B ND2   1 
ATOM   11334 N N     . TYR B 1 301  ? 1.634   0.695   123.525 1.00 23.09 ?  299  TYR B N     1 
ATOM   11335 C CA    . TYR B 1 301  ? 0.646   1.273   124.427 1.00 24.48 ?  299  TYR B CA    1 
ATOM   11336 C C     . TYR B 1 301  ? -0.783  1.025   123.956 1.00 23.07 ?  299  TYR B C     1 
ATOM   11337 O O     . TYR B 1 301  ? -1.724  1.380   124.673 1.00 24.35 ?  299  TYR B O     1 
ATOM   11338 C CB    . TYR B 1 301  ? 0.872   2.782   124.581 1.00 22.42 ?  299  TYR B CB    1 
ATOM   11339 C CG    . TYR B 1 301  ? 2.124   3.196   125.339 1.00 22.33 ?  299  TYR B CG    1 
ATOM   11340 C CD1   . TYR B 1 301  ? 2.207   3.059   126.718 1.00 23.32 ?  299  TYR B CD1   1 
ATOM   11341 C CD2   . TYR B 1 301  ? 3.201   3.771   124.671 1.00 22.40 ?  299  TYR B CD2   1 
ATOM   11342 C CE1   . TYR B 1 301  ? 3.338   3.461   127.403 1.00 24.07 ?  299  TYR B CE1   1 
ATOM   11343 C CE2   . TYR B 1 301  ? 4.341   4.178   125.350 1.00 21.76 ?  299  TYR B CE2   1 
ATOM   11344 C CZ    . TYR B 1 301  ? 4.400   4.023   126.713 1.00 22.31 ?  299  TYR B CZ    1 
ATOM   11345 O OH    . TYR B 1 301  ? 5.526   4.415   127.396 1.00 25.94 ?  299  TYR B OH    1 
ATOM   11346 N N     . ASP B 1 302  ? -0.948  0.420   122.780 1.00 22.95 ?  300  ASP B N     1 
ATOM   11347 C CA    . ASP B 1 302  ? -2.237  0.211   122.110 1.00 23.61 ?  300  ASP B CA    1 
ATOM   11348 C C     . ASP B 1 302  ? -3.043  1.510   122.015 1.00 24.39 ?  300  ASP B C     1 
ATOM   11349 O O     . ASP B 1 302  ? -4.165  1.630   122.512 1.00 24.17 ?  300  ASP B O     1 
ATOM   11350 C CB    . ASP B 1 302  ? -3.039  -0.905  122.790 1.00 25.41 ?  300  ASP B CB    1 
ATOM   11351 C CG    . ASP B 1 302  ? -4.128  -1.460  121.886 1.00 28.45 ?  300  ASP B CG    1 
ATOM   11352 O OD1   . ASP B 1 302  ? -3.892  -1.559  120.658 1.00 27.14 ?  300  ASP B OD1   1 
ATOM   11353 O OD2   . ASP B 1 302  ? -5.212  -1.799  122.401 1.00 32.94 ?  300  ASP B OD2   1 
ATOM   11354 N N     . ILE B 1 303  ? -2.440  2.498   121.355 1.00 21.83 ?  301  ILE B N     1 
ATOM   11355 C CA    . ILE B 1 303  ? -3.108  3.750   121.034 1.00 21.33 ?  301  ILE B CA    1 
ATOM   11356 C C     . ILE B 1 303  ? -3.147  3.897   119.514 1.00 22.21 ?  301  ILE B C     1 
ATOM   11357 O O     . ILE B 1 303  ? -2.434  3.216   118.780 1.00 20.75 ?  301  ILE B O     1 
ATOM   11358 C CB    . ILE B 1 303  ? -2.431  4.979   121.682 1.00 20.96 ?  301  ILE B CB    1 
ATOM   11359 C CG1   . ILE B 1 303  ? -1.082  5.278   121.012 1.00 21.51 ?  301  ILE B CG1   1 
ATOM   11360 C CG2   . ILE B 1 303  ? -2.283  4.783   123.190 1.00 21.52 ?  301  ILE B CG2   1 
ATOM   11361 C CD1   . ILE B 1 303  ? -0.492  6.626   121.410 1.00 21.13 ?  301  ILE B CD1   1 
ATOM   11362 N N     . GLY B 1 304  ? -3.987  4.819   119.053 1.00 20.43 ?  302  GLY B N     1 
ATOM   11363 C CA    . GLY B 1 304  ? -4.038  5.129   117.637 1.00 19.89 ?  302  GLY B CA    1 
ATOM   11364 C C     . GLY B 1 304  ? -2.909  6.063   117.221 1.00 19.24 ?  302  GLY B C     1 
ATOM   11365 O O     . GLY B 1 304  ? -2.508  6.961   117.959 1.00 21.28 ?  302  GLY B O     1 
ATOM   11366 N N     . LEU B 1 305  ? -2.398  5.837   116.014 1.00 18.89 ?  303  LEU B N     1 
ATOM   11367 C CA    . LEU B 1 305  ? -1.407  6.718   115.401 1.00 18.26 ?  303  LEU B CA    1 
ATOM   11368 C C     . LEU B 1 305  ? -1.907  7.021   114.000 1.00 18.74 ?  303  LEU B C     1 
ATOM   11369 O O     . LEU B 1 305  ? -1.961  6.124   113.155 1.00 19.08 ?  303  LEU B O     1 
ATOM   11370 C CB    . LEU B 1 305  ? -0.019  6.079   115.374 1.00 20.34 ?  303  LEU B CB    1 
ATOM   11371 C CG    . LEU B 1 305  ? 1.090   6.961   114.786 1.00 21.68 ?  303  LEU B CG    1 
ATOM   11372 C CD1   . LEU B 1 305  ? 2.405   6.774   115.507 1.00 26.82 ?  303  LEU B CD1   1 
ATOM   11373 C CD2   . LEU B 1 305  ? 1.263   6.677   113.310 1.00 22.67 ?  303  LEU B CD2   1 
ATOM   11374 N N     . ASN B 1 306  ? -2.267  8.276   113.760 1.00 17.39 ?  304  ASN B N     1 
ATOM   11375 C CA    . ASN B 1 306  ? -2.906  8.700   112.524 1.00 18.02 ?  304  ASN B CA    1 
ATOM   11376 C C     . ASN B 1 306  ? -1.925  9.476   111.659 1.00 17.83 ?  304  ASN B C     1 
ATOM   11377 O O     . ASN B 1 306  ? -1.251  10.385  112.151 1.00 16.73 ?  304  ASN B O     1 
ATOM   11378 C CB    . ASN B 1 306  ? -4.114  9.582   112.826 1.00 17.74 ?  304  ASN B CB    1 
ATOM   11379 C CG    . ASN B 1 306  ? -4.671  10.216  111.586 1.00 20.17 ?  304  ASN B CG    1 
ATOM   11380 O OD1   . ASN B 1 306  ? -4.348  11.371  111.244 1.00 20.20 ?  304  ASN B OD1   1 
ATOM   11381 N ND2   . ASN B 1 306  ? -5.484  9.460   110.873 1.00 18.71 ?  304  ASN B ND2   1 
ATOM   11382 N N     . ILE B 1 307  ? -1.888  9.160   110.366 1.00 16.18 ?  305  ILE B N     1 
ATOM   11383 C CA    . ILE B 1 307  ? -1.117  9.937   109.395 1.00 17.47 ?  305  ILE B CA    1 
ATOM   11384 C C     . ILE B 1 307  ? -2.031  10.978  108.751 1.00 16.45 ?  305  ILE B C     1 
ATOM   11385 O O     . ILE B 1 307  ? -2.941  10.640  107.988 1.00 15.58 ?  305  ILE B O     1 
ATOM   11386 C CB    . ILE B 1 307  ? -0.476  9.034   108.336 1.00 16.08 ?  305  ILE B CB    1 
ATOM   11387 C CG1   . ILE B 1 307  ? 0.502   8.076   109.023 1.00 20.72 ?  305  ILE B CG1   1 
ATOM   11388 C CG2   . ILE B 1 307  ? 0.198   9.887   107.255 1.00 16.87 ?  305  ILE B CG2   1 
ATOM   11389 C CD1   . ILE B 1 307  ? 0.973   6.949   108.141 1.00 21.11 ?  305  ILE B CD1   1 
ATOM   11390 N N     . ASP B 1 308  ? -1.784  12.251  109.056 1.00 15.10 ?  306  ASP B N     1 
ATOM   11391 C CA    . ASP B 1 308  ? -2.544  13.342  108.458 1.00 16.62 ?  306  ASP B CA    1 
ATOM   11392 C C     . ASP B 1 308  ? -2.276  13.411  106.957 1.00 16.27 ?  306  ASP B C     1 
ATOM   11393 O O     . ASP B 1 308  ? -1.201  13.045  106.480 1.00 16.40 ?  306  ASP B O     1 
ATOM   11394 C CB    . ASP B 1 308  ? -2.169  14.684  109.102 1.00 16.76 ?  306  ASP B CB    1 
ATOM   11395 C CG    . ASP B 1 308  ? -2.711  14.856  110.526 1.00 20.17 ?  306  ASP B CG    1 
ATOM   11396 O OD1   . ASP B 1 308  ? -3.505  14.013  111.013 1.00 17.26 ?  306  ASP B OD1   1 
ATOM   11397 O OD2   . ASP B 1 308  ? -2.328  15.860  111.165 1.00 21.90 ?  306  ASP B OD2   1 
ATOM   11398 N N     . ALA B 1 309  ? -3.264  13.891  106.200 1.00 14.11 ?  307  ALA B N     1 
ATOM   11399 C CA    . ALA B 1 309  ? -3.114  14.058  104.761 1.00 13.95 ?  307  ALA B CA    1 
ATOM   11400 C C     . ALA B 1 309  ? -2.730  15.492  104.419 1.00 13.98 ?  307  ALA B C     1 
ATOM   11401 O O     . ALA B 1 309  ? -3.262  16.442  104.991 1.00 14.92 ?  307  ALA B O     1 
ATOM   11402 C CB    . ALA B 1 309  ? -4.400  13.679  104.035 1.00 14.40 ?  307  ALA B CB    1 
ATOM   11403 N N     . GLU B 1 310  ? -1.801  15.645  103.478 1.00 12.78 ?  308  GLU B N     1 
ATOM   11404 C CA    . GLU B 1 310  ? -1.257  16.966  103.182 1.00 12.66 ?  308  GLU B CA    1 
ATOM   11405 C C     . GLU B 1 310  ? -1.511  17.319  101.717 1.00 12.96 ?  308  GLU B C     1 
ATOM   11406 O O     . GLU B 1 310  ? -2.637  17.147  101.249 1.00 12.58 ?  308  GLU B O     1 
ATOM   11407 C CB    . GLU B 1 310  ? 0.235   17.004  103.566 1.00 12.22 ?  308  GLU B CB    1 
ATOM   11408 C CG    . GLU B 1 310  ? 0.454   16.689  105.053 1.00 17.08 ?  308  GLU B CG    1 
ATOM   11409 C CD    . GLU B 1 310  ? 1.898   16.841  105.510 1.00 17.17 ?  308  GLU B CD    1 
ATOM   11410 O OE1   . GLU B 1 310  ? 2.364   17.998  105.639 1.00 18.33 ?  308  GLU B OE1   1 
ATOM   11411 O OE2   . GLU B 1 310  ? 2.551   15.806  105.762 1.00 16.35 ?  308  GLU B OE2   1 
ATOM   11412 N N     . GLU B 1 311  ? -0.510  17.830  100.993 1.00 13.27 ?  309  GLU B N     1 
ATOM   11413 C CA    . GLU B 1 311  ? -0.746  18.285  99.626  1.00 13.16 ?  309  GLU B CA    1 
ATOM   11414 C C     . GLU B 1 311  ? -1.031  17.115  98.680  1.00 12.13 ?  309  GLU B C     1 
ATOM   11415 O O     . GLU B 1 311  ? -0.675  15.960  98.939  1.00 13.69 ?  309  GLU B O     1 
ATOM   11416 C CB    . GLU B 1 311  ? 0.464   19.072  99.107  1.00 12.51 ?  309  GLU B CB    1 
ATOM   11417 C CG    . GLU B 1 311  ? 0.788   20.350  99.904  1.00 17.20 ?  309  GLU B CG    1 
ATOM   11418 C CD    . GLU B 1 311  ? 1.709   20.124  101.095 1.00 18.37 ?  309  GLU B CD    1 
ATOM   11419 O OE1   . GLU B 1 311  ? 1.937   18.965  101.498 1.00 15.22 ?  309  GLU B OE1   1 
ATOM   11420 O OE2   . GLU B 1 311  ? 2.229   21.136  101.631 1.00 23.17 ?  309  GLU B OE2   1 
ATOM   11421 N N     . ALA B 1 312  ? -1.686  17.435  97.561  1.00 12.27 ?  310  ALA B N     1 
ATOM   11422 C CA    . ALA B 1 312  ? -2.100  16.396  96.624  1.00 13.26 ?  310  ALA B CA    1 
ATOM   11423 C C     . ALA B 1 312  ? -0.916  15.603  96.080  1.00 14.01 ?  310  ALA B C     1 
ATOM   11424 O O     . ALA B 1 312  ? -1.046  14.390  95.862  1.00 13.11 ?  310  ALA B O     1 
ATOM   11425 C CB    . ALA B 1 312  ? -2.901  17.006  95.464  1.00 14.05 ?  310  ALA B CB    1 
ATOM   11426 N N     . ASP B 1 313  ? 0.257   16.242  95.903  1.00 13.17 ?  311  ASP B N     1 
ATOM   11427 C CA    . ASP B 1 313  ? 1.394   15.514  95.337  1.00 12.82 ?  311  ASP B CA    1 
ATOM   11428 C C     . ASP B 1 313  ? 2.121   14.642  96.358  1.00 14.22 ?  311  ASP B C     1 
ATOM   11429 O O     . ASP B 1 313  ? 3.130   14.017  96.007  1.00 14.97 ?  311  ASP B O     1 
ATOM   11430 C CB    . ASP B 1 313  ? 2.385   16.465  94.631  1.00 13.51 ?  311  ASP B CB    1 
ATOM   11431 C CG    . ASP B 1 313  ? 3.005   17.508  95.539  1.00 17.87 ?  311  ASP B CG    1 
ATOM   11432 O OD1   . ASP B 1 313  ? 2.857   17.463  96.779  1.00 16.01 ?  311  ASP B OD1   1 
ATOM   11433 O OD2   . ASP B 1 313  ? 3.689   18.402  94.978  1.00 20.95 ?  311  ASP B OD2   1 
ATOM   11434 N N     . ARG B 1 314  ? 1.598   14.530  97.576  1.00 12.39 ?  312  ARG B N     1 
ATOM   11435 C CA    . ARG B 1 314  ? 2.129   13.607  98.572  1.00 13.52 ?  312  ARG B CA    1 
ATOM   11436 C C     . ARG B 1 314  ? 1.200   12.433  98.844  1.00 13.12 ?  312  ARG B C     1 
ATOM   11437 O O     . ARG B 1 314  ? 1.601   11.496  99.544  1.00 14.41 ?  312  ARG B O     1 
ATOM   11438 C CB    . ARG B 1 314  ? 2.430   14.360  99.877  1.00 13.85 ?  312  ARG B CB    1 
ATOM   11439 C CG    . ARG B 1 314  ? 3.719   15.195  99.751  1.00 14.16 ?  312  ARG B CG    1 
ATOM   11440 C CD    . ARG B 1 314  ? 3.773   16.328  100.772 1.00 16.89 ?  312  ARG B CD    1 
ATOM   11441 N NE    . ARG B 1 314  ? 5.131   16.835  100.940 1.00 16.61 ?  312  ARG B NE    1 
ATOM   11442 C CZ    . ARG B 1 314  ? 5.455   17.851  101.728 1.00 15.34 ?  312  ARG B CZ    1 
ATOM   11443 N NH1   . ARG B 1 314  ? 4.525   18.590  102.314 1.00 15.64 ?  312  ARG B NH1   1 
ATOM   11444 N NH2   . ARG B 1 314  ? 6.746   18.123  101.947 1.00 17.43 ?  312  ARG B NH2   1 
ATOM   11445 N N     . LEU B 1 315  ? -0.006  12.439  98.272  1.00 13.75 ?  313  LEU B N     1 
ATOM   11446 C CA    . LEU B 1 315  ? -0.985  11.396  98.562  1.00 13.13 ?  313  LEU B CA    1 
ATOM   11447 C C     . LEU B 1 315  ? -0.439  10.015  98.223  1.00 16.35 ?  313  LEU B C     1 
ATOM   11448 O O     . LEU B 1 315  ? -0.386  9.120   99.078  1.00 15.13 ?  313  LEU B O     1 
ATOM   11449 C CB    . LEU B 1 315  ? -2.279  11.682  97.795  1.00 13.08 ?  313  LEU B CB    1 
ATOM   11450 C CG    . LEU B 1 315  ? -3.554  11.005  98.315  1.00 13.60 ?  313  LEU B CG    1 
ATOM   11451 C CD1   . LEU B 1 315  ? -4.738  11.510  97.503  1.00 15.46 ?  313  LEU B CD1   1 
ATOM   11452 C CD2   . LEU B 1 315  ? -3.505  9.474   98.275  1.00 18.83 ?  313  LEU B CD2   1 
ATOM   11453 N N     . GLU B 1 316  ? -0.049  9.808   96.965  1.00 15.12 ?  314  GLU B N     1 
ATOM   11454 C CA    . GLU B 1 316  ? 0.290   8.448   96.565  1.00 15.11 ?  314  GLU B CA    1 
ATOM   11455 C C     . GLU B 1 316  ? 1.593   7.996   97.213  1.00 16.33 ?  314  GLU B C     1 
ATOM   11456 O O     . GLU B 1 316  ? 1.723   6.820   97.579  1.00 17.12 ?  314  GLU B O     1 
ATOM   11457 C CB    . GLU B 1 316  ? 0.317   8.357   95.034  1.00 16.88 ?  314  GLU B CB    1 
ATOM   11458 C CG    . GLU B 1 316  ? -1.095  8.452   94.470  1.00 15.38 ?  314  GLU B CG    1 
ATOM   11459 C CD    . GLU B 1 316  ? -1.176  8.330   92.954  1.00 18.34 ?  314  GLU B CD    1 
ATOM   11460 O OE1   . GLU B 1 316  ? -0.508  7.445   92.381  1.00 17.78 ?  314  GLU B OE1   1 
ATOM   11461 O OE2   . GLU B 1 316  ? -1.933  9.105   92.338  1.00 18.91 ?  314  GLU B OE2   1 
ATOM   11462 N N     . LEU B 1 317  ? 2.541   8.918   97.410  1.00 14.88 ?  315  LEU B N     1 
ATOM   11463 C CA    . LEU B 1 317  ? 3.764   8.582   98.135  1.00 17.57 ?  315  LEU B CA    1 
ATOM   11464 C C     . LEU B 1 317  ? 3.452   8.058   99.532  1.00 17.56 ?  315  LEU B C     1 
ATOM   11465 O O     . LEU B 1 317  ? 4.027   7.051   99.973  1.00 17.96 ?  315  LEU B O     1 
ATOM   11466 C CB    . LEU B 1 317  ? 4.669   9.809   98.218  1.00 17.11 ?  315  LEU B CB    1 
ATOM   11467 C CG    . LEU B 1 317  ? 5.988   9.611   98.958  1.00 17.95 ?  315  LEU B CG    1 
ATOM   11468 C CD1   . LEU B 1 317  ? 6.733   8.402   98.422  1.00 20.88 ?  315  LEU B CD1   1 
ATOM   11469 C CD2   . LEU B 1 317  ? 6.819   10.867  98.795  1.00 21.09 ?  315  LEU B CD2   1 
ATOM   11470 N N     . SER B 1 318  ? 2.519   8.711   100.237 1.00 15.75 ?  316  SER B N     1 
ATOM   11471 C CA    . SER B 1 318  ? 2.169   8.255   101.579 1.00 15.02 ?  316  SER B CA    1 
ATOM   11472 C C     . SER B 1 318  ? 1.603   6.840   101.567 1.00 14.96 ?  316  SER B C     1 
ATOM   11473 O O     . SER B 1 318  ? 1.782   6.100   102.541 1.00 16.75 ?  316  SER B O     1 
ATOM   11474 C CB    . SER B 1 318  ? 1.185   9.222   102.251 1.00 15.91 ?  316  SER B CB    1 
ATOM   11475 O OG    . SER B 1 318  ? -0.127  9.138   101.718 1.00 15.97 ?  316  SER B OG    1 
ATOM   11476 N N     . LEU B 1 319  ? 0.964   6.430   100.463 1.00 16.19 ?  317  LEU B N     1 
ATOM   11477 C CA    . LEU B 1 319  ? 0.429   5.073   100.391 1.00 16.23 ?  317  LEU B CA    1 
ATOM   11478 C C     . LEU B 1 319  ? 1.536   4.032   100.410 1.00 17.34 ?  317  LEU B C     1 
ATOM   11479 O O     . LEU B 1 319  ? 1.330   2.924   100.914 1.00 19.28 ?  317  LEU B O     1 
ATOM   11480 C CB    . LEU B 1 319  ? -0.427  4.899   99.137  1.00 17.57 ?  317  LEU B CB    1 
ATOM   11481 C CG    . LEU B 1 319  ? -1.688  5.758   99.032  1.00 16.40 ?  317  LEU B CG    1 
ATOM   11482 C CD1   . LEU B 1 319  ? -2.359  5.513   97.669  1.00 15.66 ?  317  LEU B CD1   1 
ATOM   11483 C CD2   . LEU B 1 319  ? -2.648  5.491   100.190 1.00 18.57 ?  317  LEU B CD2   1 
ATOM   11484 N N     . ASP B 1 320  ? 2.710   4.359   99.872  1.00 16.94 ?  318  ASP B N     1 
ATOM   11485 C CA    . ASP B 1 320  ? 3.808   3.399   99.909  1.00 19.56 ?  318  ASP B CA    1 
ATOM   11486 C C     . ASP B 1 320  ? 4.303   3.174   101.326 1.00 19.47 ?  318  ASP B C     1 
ATOM   11487 O O     . ASP B 1 320  ? 4.776   2.077   101.648 1.00 20.86 ?  318  ASP B O     1 
ATOM   11488 C CB    . ASP B 1 320  ? 4.946   3.869   99.009  1.00 19.02 ?  318  ASP B CB    1 
ATOM   11489 C CG    . ASP B 1 320  ? 4.624   3.682   97.541  1.00 21.14 ?  318  ASP B CG    1 
ATOM   11490 O OD1   . ASP B 1 320  ? 4.351   2.533   97.141  1.00 21.99 ?  318  ASP B OD1   1 
ATOM   11491 O OD2   . ASP B 1 320  ? 4.606   4.679   96.795  1.00 23.43 ?  318  ASP B OD2   1 
ATOM   11492 N N     . LEU B 1 321  ? 4.204   4.189   102.187 1.00 17.67 ?  319  LEU B N     1 
ATOM   11493 C CA    . LEU B 1 321  ? 4.555   3.984   103.588 1.00 17.89 ?  319  LEU B CA    1 
ATOM   11494 C C     . LEU B 1 321  ? 3.485   3.173   104.307 1.00 18.82 ?  319  LEU B C     1 
ATOM   11495 O O     . LEU B 1 321  ? 3.801   2.254   105.069 1.00 20.92 ?  319  LEU B O     1 
ATOM   11496 C CB    . LEU B 1 321  ? 4.768   5.330   104.278 1.00 18.90 ?  319  LEU B CB    1 
ATOM   11497 C CG    . LEU B 1 321  ? 6.112   6.002   103.996 1.00 18.18 ?  319  LEU B CG    1 
ATOM   11498 C CD1   . LEU B 1 321  ? 6.027   6.890   102.774 1.00 21.01 ?  319  LEU B CD1   1 
ATOM   11499 C CD2   . LEU B 1 321  ? 6.568   6.794   105.205 1.00 24.46 ?  319  LEU B CD2   1 
ATOM   11500 N N     . LEU B 1 322  ? 2.214   3.495   104.058 1.00 18.52 ?  320  LEU B N     1 
ATOM   11501 C CA    . LEU B 1 322  ? 1.116   2.749   104.662 1.00 19.46 ?  320  LEU B CA    1 
ATOM   11502 C C     . LEU B 1 322  ? 1.206   1.269   104.324 1.00 20.12 ?  320  LEU B C     1 
ATOM   11503 O O     . LEU B 1 322  ? 1.018   0.411   105.198 1.00 19.47 ?  320  LEU B O     1 
ATOM   11504 C CB    . LEU B 1 322  ? -0.213  3.323   104.178 1.00 17.84 ?  320  LEU B CB    1 
ATOM   11505 C CG    . LEU B 1 322  ? -1.458  2.706   104.809 1.00 19.09 ?  320  LEU B CG    1 
ATOM   11506 C CD1   . LEU B 1 322  ? -1.479  2.987   106.306 1.00 19.66 ?  320  LEU B CD1   1 
ATOM   11507 C CD2   . LEU B 1 322  ? -2.724  3.234   104.134 1.00 18.39 ?  320  LEU B CD2   1 
ATOM   11508 N N     . GLU B 1 323  ? 1.487   0.959   103.055 1.00 21.26 ?  321  GLU B N     1 
ATOM   11509 C CA    . GLU B 1 323  ? 1.646   -0.426  102.620 1.00 20.88 ?  321  GLU B CA    1 
ATOM   11510 C C     . GLU B 1 323  ? 2.669   -1.164  103.477 1.00 21.98 ?  321  GLU B C     1 
ATOM   11511 O O     . GLU B 1 323  ? 2.386   -2.248  104.005 1.00 23.42 ?  321  GLU B O     1 
ATOM   11512 C CB    . GLU B 1 323  ? 2.052   -0.458  101.142 1.00 21.41 ?  321  GLU B CB    1 
ATOM   11513 C CG    . GLU B 1 323  ? 2.392   -1.860  100.612 1.00 26.22 ?  321  GLU B CG    1 
ATOM   11514 C CD    . GLU B 1 323  ? 1.214   -2.560  99.951  1.00 29.45 ?  321  GLU B CD    1 
ATOM   11515 O OE1   . GLU B 1 323  ? 0.178   -1.910  99.726  1.00 27.56 ?  321  GLU B OE1   1 
ATOM   11516 O OE2   . GLU B 1 323  ? 1.326   -3.770  99.651  1.00 28.52 ?  321  GLU B OE2   1 
ATOM   11517 N N     . VAL B 1 324  ? 3.859   -0.574  103.650 1.00 19.96 ?  322  VAL B N     1 
ATOM   11518 C CA    . VAL B 1 324  ? 4.917   -1.243  104.406 1.00 19.78 ?  322  VAL B CA    1 
ATOM   11519 C C     . VAL B 1 324  ? 4.515   -1.413  105.866 1.00 22.32 ?  322  VAL B C     1 
ATOM   11520 O O     . VAL B 1 324  ? 4.757   -2.463  106.466 1.00 23.40 ?  322  VAL B O     1 
ATOM   11521 C CB    . VAL B 1 324  ? 6.247   -0.474  104.281 1.00 23.37 ?  322  VAL B CB    1 
ATOM   11522 C CG1   . VAL B 1 324  ? 7.304   -1.094  105.202 1.00 25.37 ?  322  VAL B CG1   1 
ATOM   11523 C CG2   . VAL B 1 324  ? 6.729   -0.463  102.839 1.00 25.02 ?  322  VAL B CG2   1 
ATOM   11524 N N     . LEU B 1 325  ? 3.902   -0.388  106.460 1.00 20.64 ?  323  LEU B N     1 
ATOM   11525 C CA    . LEU B 1 325  ? 3.540   -0.468  107.872 1.00 21.46 ?  323  LEU B CA    1 
ATOM   11526 C C     . LEU B 1 325  ? 2.493   -1.551  108.118 1.00 20.48 ?  323  LEU B C     1 
ATOM   11527 O O     . LEU B 1 325  ? 2.565   -2.280  109.114 1.00 23.28 ?  323  LEU B O     1 
ATOM   11528 C CB    . LEU B 1 325  ? 3.041   0.890   108.361 1.00 21.46 ?  323  LEU B CB    1 
ATOM   11529 C CG    . LEU B 1 325  ? 4.111   1.984   108.341 1.00 22.76 ?  323  LEU B CG    1 
ATOM   11530 C CD1   . LEU B 1 325  ? 3.473   3.343   108.497 1.00 23.16 ?  323  LEU B CD1   1 
ATOM   11531 C CD2   . LEU B 1 325  ? 5.148   1.758   109.433 1.00 21.83 ?  323  LEU B CD2   1 
ATOM   11532 N N     . CYS B 1 326  ? 1.511   -1.673  107.221 1.00 22.11 ?  324  CYS B N     1 
ATOM   11533 C CA    . CYS B 1 326  ? 0.452   -2.654  107.426 1.00 20.77 ?  324  CYS B CA    1 
ATOM   11534 C C     . CYS B 1 326  ? 0.935   -4.088  107.238 1.00 21.47 ?  324  CYS B C     1 
ATOM   11535 O O     . CYS B 1 326  ? 0.324   -5.008  107.791 1.00 24.07 ?  324  CYS B O     1 
ATOM   11536 C CB    . CYS B 1 326  ? -0.717  -2.375  106.485 1.00 23.93 ?  324  CYS B CB    1 
ATOM   11537 S SG    . CYS B 1 326  ? -1.637  -0.889  106.928 1.00 24.25 ?  324  CYS B SG    1 
ATOM   11538 N N     . LEU B 1 327  ? 2.015   -4.295  106.483 1.00 20.84 ?  325  LEU B N     1 
ATOM   11539 C CA    . LEU B 1 327  ? 2.579   -5.622  106.256 1.00 23.72 ?  325  LEU B CA    1 
ATOM   11540 C C     . LEU B 1 327  ? 3.748   -5.936  107.183 1.00 24.67 ?  325  LEU B C     1 
ATOM   11541 O O     . LEU B 1 327  ? 4.300   -7.041  107.116 1.00 23.74 ?  325  LEU B O     1 
ATOM   11542 C CB    . LEU B 1 327  ? 3.019   -5.758  104.792 1.00 21.59 ?  325  LEU B CB    1 
ATOM   11543 C CG    . LEU B 1 327  ? 1.863   -5.726  103.787 1.00 25.72 ?  325  LEU B CG    1 
ATOM   11544 C CD1   . LEU B 1 327  ? 2.366   -5.515  102.363 1.00 27.58 ?  325  LEU B CD1   1 
ATOM   11545 C CD2   . LEU B 1 327  ? 1.059   -6.988  103.870 1.00 32.76 ?  325  LEU B CD2   1 
ATOM   11546 N N     . ASP B 1 328  ? 4.128   -5.007  108.057 1.00 25.55 ?  326  ASP B N     1 
ATOM   11547 C CA    . ASP B 1 328  ? 5.259   -5.211  108.958 1.00 25.80 ?  326  ASP B CA    1 
ATOM   11548 C C     . ASP B 1 328  ? 4.809   -6.053  110.149 1.00 21.90 ?  326  ASP B C     1 
ATOM   11549 O O     . ASP B 1 328  ? 4.045   -5.581  110.997 1.00 24.77 ?  326  ASP B O     1 
ATOM   11550 C CB    . ASP B 1 328  ? 5.812   -3.859  109.411 1.00 26.18 ?  326  ASP B CB    1 
ATOM   11551 C CG    . ASP B 1 328  ? 7.147   -3.975  110.147 1.00 30.15 ?  326  ASP B CG    1 
ATOM   11552 O OD1   . ASP B 1 328  ? 7.389   -4.998  110.821 1.00 26.88 ?  326  ASP B OD1   1 
ATOM   11553 O OD2   . ASP B 1 328  ? 7.954   -3.018  110.062 1.00 33.31 ?  326  ASP B OD2   1 
ATOM   11554 N N     . GLY B 1 329  ? 5.303   -7.293  110.232 1.00 24.64 ?  327  GLY B N     1 
ATOM   11555 C CA    . GLY B 1 329  ? 4.920   -8.184  111.318 1.00 24.53 ?  327  GLY B CA    1 
ATOM   11556 C C     . GLY B 1 329  ? 5.245   -7.680  112.716 1.00 23.31 ?  327  GLY B C     1 
ATOM   11557 O O     . GLY B 1 329  ? 4.653   -8.159  113.689 1.00 26.81 ?  327  GLY B O     1 
ATOM   11558 N N     . ASP B 1 330  ? 6.160   -6.717  112.845 1.00 25.44 ?  328  ASP B N     1 
ATOM   11559 C CA    . ASP B 1 330  ? 6.416   -6.136  114.158 1.00 26.30 ?  328  ASP B CA    1 
ATOM   11560 C C     . ASP B 1 330  ? 5.202   -5.395  114.703 1.00 27.45 ?  328  ASP B C     1 
ATOM   11561 O O     . ASP B 1 330  ? 5.134   -5.155  115.913 1.00 29.04 ?  328  ASP B O     1 
ATOM   11562 C CB    . ASP B 1 330  ? 7.618   -5.185  114.103 1.00 26.55 ?  328  ASP B CB    1 
ATOM   11563 C CG    . ASP B 1 330  ? 8.937   -5.912  113.887 1.00 33.00 ?  328  ASP B CG    1 
ATOM   11564 O OD1   . ASP B 1 330  ? 8.990   -7.143  114.107 1.00 32.56 ?  328  ASP B OD1   1 
ATOM   11565 O OD2   . ASP B 1 330  ? 9.931   -5.248  113.516 1.00 30.45 ?  328  ASP B OD2   1 
ATOM   11566 N N     . LEU B 1 331  ? 4.247   -5.029  113.842 1.00 23.21 ?  329  LEU B N     1 
ATOM   11567 C CA    . LEU B 1 331  ? 3.026   -4.349  114.256 1.00 23.38 ?  329  LEU B CA    1 
ATOM   11568 C C     . LEU B 1 331  ? 1.823   -5.284  114.298 1.00 23.21 ?  329  LEU B C     1 
ATOM   11569 O O     . LEU B 1 331  ? 0.682   -4.811  114.340 1.00 23.84 ?  329  LEU B O     1 
ATOM   11570 C CB    . LEU B 1 331  ? 2.750   -3.160  113.336 1.00 23.87 ?  329  LEU B CB    1 
ATOM   11571 C CG    . LEU B 1 331  ? 3.889   -2.145  113.326 1.00 21.14 ?  329  LEU B CG    1 
ATOM   11572 C CD1   . LEU B 1 331  ? 3.624   -1.057  112.295 1.00 22.70 ?  329  LEU B CD1   1 
ATOM   11573 C CD2   . LEU B 1 331  ? 4.093   -1.556  114.729 1.00 24.26 ?  329  LEU B CD2   1 
ATOM   11574 N N     . SER B 1 332  ? 2.070   -6.594  114.304 1.00 25.55 ?  330  SER B N     1 
ATOM   11575 C CA    . SER B 1 332  ? 1.021   -7.610  114.271 1.00 25.01 ?  330  SER B CA    1 
ATOM   11576 C C     . SER B 1 332  ? -0.089  -7.345  115.280 1.00 26.47 ?  330  SER B C     1 
ATOM   11577 O O     . SER B 1 332  ? 0.168   -7.123  116.469 1.00 27.96 ?  330  SER B O     1 
ATOM   11578 C CB    . SER B 1 332  ? 1.637   -8.980  114.543 1.00 27.46 ?  330  SER B CB    1 
ATOM   11579 O OG    . SER B 1 332  ? 0.654   -9.990  114.430 1.00 30.77 ?  330  SER B OG    1 
ATOM   11580 N N     . GLY B 1 333  ? -1.333  -7.401  114.802 1.00 25.88 ?  331  GLY B N     1 
ATOM   11581 C CA    . GLY B 1 333  ? -2.499  -7.315  115.658 1.00 28.35 ?  331  GLY B CA    1 
ATOM   11582 C C     . GLY B 1 333  ? -2.873  -5.919  116.100 1.00 28.66 ?  331  GLY B C     1 
ATOM   11583 O O     . GLY B 1 333  ? -3.923  -5.746  116.733 1.00 30.20 ?  331  GLY B O     1 
ATOM   11584 N N     . TRP B 1 334  ? -2.055  -4.923  115.790 1.00 25.99 ?  332  TRP B N     1 
ATOM   11585 C CA    . TRP B 1 334  ? -2.324  -3.548  116.183 1.00 27.28 ?  332  TRP B CA    1 
ATOM   11586 C C     . TRP B 1 334  ? -3.283  -2.918  115.185 1.00 23.44 ?  332  TRP B C     1 
ATOM   11587 O O     . TRP B 1 334  ? -2.974  -2.821  113.991 1.00 25.79 ?  332  TRP B O     1 
ATOM   11588 C CB    . TRP B 1 334  ? -1.012  -2.777  116.252 1.00 27.32 ?  332  TRP B CB    1 
ATOM   11589 C CG    . TRP B 1 334  ? -1.148  -1.323  116.531 1.00 25.61 ?  332  TRP B CG    1 
ATOM   11590 C CD1   . TRP B 1 334  ? -1.692  -0.748  117.644 1.00 24.76 ?  332  TRP B CD1   1 
ATOM   11591 C CD2   . TRP B 1 334  ? -0.674  -0.253  115.711 1.00 23.96 ?  332  TRP B CD2   1 
ATOM   11592 N NE1   . TRP B 1 334  ? -1.608  0.627   117.551 1.00 21.54 ?  332  TRP B NE1   1 
ATOM   11593 C CE2   . TRP B 1 334  ? -0.983  0.955   116.377 1.00 22.57 ?  332  TRP B CE2   1 
ATOM   11594 C CE3   . TRP B 1 334  ? -0.026  -0.195  114.472 1.00 22.13 ?  332  TRP B CE3   1 
ATOM   11595 C CZ2   . TRP B 1 334  ? -0.668  2.207   115.841 1.00 21.76 ?  332  TRP B CZ2   1 
ATOM   11596 C CZ3   . TRP B 1 334  ? 0.290   1.049   113.941 1.00 25.75 ?  332  TRP B CZ3   1 
ATOM   11597 C CH2   . TRP B 1 334  ? -0.029  2.235   114.630 1.00 25.66 ?  332  TRP B CH2   1 
ATOM   11598 N N     . ASN B 1 335  ? -4.458  -2.507  115.652 1.00 24.10 ?  333  ASN B N     1 
ATOM   11599 C CA    . ASN B 1 335  ? -5.442  -1.900  114.765 1.00 22.78 ?  333  ASN B CA    1 
ATOM   11600 C C     . ASN B 1 335  ? -5.470  -0.380  114.878 1.00 24.96 ?  333  ASN B C     1 
ATOM   11601 O O     . ASN B 1 335  ? -6.433  0.253   114.432 1.00 23.85 ?  333  ASN B O     1 
ATOM   11602 C CB    . ASN B 1 335  ? -6.830  -2.478  115.036 1.00 25.58 ?  333  ASN B CB    1 
ATOM   11603 C CG    . ASN B 1 335  ? -6.927  -3.944  114.663 1.00 27.94 ?  333  ASN B CG    1 
ATOM   11604 O OD1   . ASN B 1 335  ? -6.241  -4.410  113.758 1.00 26.99 ?  333  ASN B OD1   1 
ATOM   11605 N ND2   . ASN B 1 335  ? -7.772  -4.678  115.369 1.00 28.06 ?  333  ASN B ND2   1 
ATOM   11606 N N     . GLY B 1 336  ? -4.433  0.217   115.456 1.00 22.25 ?  334  GLY B N     1 
ATOM   11607 C CA    . GLY B 1 336  ? -4.402  1.656   115.622 1.00 22.06 ?  334  GLY B CA    1 
ATOM   11608 C C     . GLY B 1 336  ? -3.775  2.457   114.512 1.00 20.00 ?  334  GLY B C     1 
ATOM   11609 O O     . GLY B 1 336  ? -3.677  3.681   114.642 1.00 20.07 ?  334  GLY B O     1 
ATOM   11610 N N     . MET B 1 337  ? -3.349  1.836   113.413 1.00 21.23 ?  335  MET B N     1 
ATOM   11611 C CA    . MET B 1 337  ? -2.842  2.605   112.284 1.00 20.59 ?  335  MET B CA    1 
ATOM   11612 C C     . MET B 1 337  ? -3.972  3.423   111.676 1.00 21.84 ?  335  MET B C     1 
ATOM   11613 O O     . MET B 1 337  ? -4.979  2.860   111.224 1.00 20.87 ?  335  MET B O     1 
ATOM   11614 C CB    . MET B 1 337  ? -2.237  1.678   111.236 1.00 21.81 ?  335  MET B CB    1 
ATOM   11615 C CG    . MET B 1 337  ? -1.613  2.400   110.043 1.00 24.34 ?  335  MET B CG    1 
ATOM   11616 S SD    . MET B 1 337  ? -0.020  3.101   110.463 1.00 34.24 ?  335  MET B SD    1 
ATOM   11617 C CE    . MET B 1 337  ? -0.426  4.842   110.584 1.00 25.88 ?  335  MET B CE    1 
ATOM   11618 N N     . GLY B 1 338  ? -3.801  4.745   111.653 1.00 22.33 ?  336  GLY B N     1 
ATOM   11619 C CA    . GLY B 1 338  ? -4.790  5.661   111.112 1.00 19.22 ?  336  GLY B CA    1 
ATOM   11620 C C     . GLY B 1 338  ? -4.291  6.394   109.876 1.00 19.36 ?  336  GLY B C     1 
ATOM   11621 O O     . GLY B 1 338  ? -3.096  6.670   109.734 1.00 18.55 ?  336  GLY B O     1 
ATOM   11622 N N     . PHE B 1 339  ? -5.216  6.726   108.978 1.00 17.50 ?  337  PHE B N     1 
ATOM   11623 C CA    . PHE B 1 339  ? -4.839  7.321   107.700 1.00 16.66 ?  337  PHE B CA    1 
ATOM   11624 C C     . PHE B 1 339  ? -5.965  8.214   107.207 1.00 16.44 ?  337  PHE B C     1 
ATOM   11625 O O     . PHE B 1 339  ? -7.116  7.776   107.147 1.00 17.31 ?  337  PHE B O     1 
ATOM   11626 C CB    . PHE B 1 339  ? -4.540  6.231   106.664 1.00 18.17 ?  337  PHE B CB    1 
ATOM   11627 C CG    . PHE B 1 339  ? -3.845  6.737   105.431 1.00 16.71 ?  337  PHE B CG    1 
ATOM   11628 C CD1   . PHE B 1 339  ? -2.465  6.852   105.387 1.00 18.00 ?  337  PHE B CD1   1 
ATOM   11629 C CD2   . PHE B 1 339  ? -4.575  7.090   104.307 1.00 17.35 ?  337  PHE B CD2   1 
ATOM   11630 C CE1   . PHE B 1 339  ? -1.821  7.312   104.228 1.00 17.26 ?  337  PHE B CE1   1 
ATOM   11631 C CE2   . PHE B 1 339  ? -3.940  7.537   103.145 1.00 19.32 ?  337  PHE B CE2   1 
ATOM   11632 C CZ    . PHE B 1 339  ? -2.559  7.657   103.116 1.00 16.52 ?  337  PHE B CZ    1 
ATOM   11633 N N     . VAL B 1 340  ? -5.642  9.451   106.872 1.00 16.74 ?  338  VAL B N     1 
ATOM   11634 C CA    . VAL B 1 340  ? -6.619  10.433  106.408 1.00 15.64 ?  338  VAL B CA    1 
ATOM   11635 C C     . VAL B 1 340  ? -6.774  10.338  104.899 1.00 16.82 ?  338  VAL B C     1 
ATOM   11636 O O     . VAL B 1 340  ? -5.785  10.209  104.169 1.00 16.24 ?  338  VAL B O     1 
ATOM   11637 C CB    . VAL B 1 340  ? -6.184  11.858  106.811 1.00 15.20 ?  338  VAL B CB    1 
ATOM   11638 C CG1   . VAL B 1 340  ? -7.153  12.897  106.263 1.00 17.30 ?  338  VAL B CG1   1 
ATOM   11639 C CG2   . VAL B 1 340  ? -6.017  11.969  108.330 1.00 15.86 ?  338  VAL B CG2   1 
ATOM   11640 N N     . VAL B 1 341  ? -8.012  10.433  104.418 1.00 15.52 ?  339  VAL B N     1 
ATOM   11641 C CA    A VAL B 1 341  ? -8.279  10.608  102.996 0.59 15.31 ?  339  VAL B CA    1 
ATOM   11642 C CA    B VAL B 1 341  ? -8.285  10.604  102.995 0.41 15.31 ?  339  VAL B CA    1 
ATOM   11643 C C     . VAL B 1 341  ? -9.164  11.837  102.820 1.00 15.07 ?  339  VAL B C     1 
ATOM   11644 O O     . VAL B 1 341  ? -10.109 12.058  103.596 1.00 15.90 ?  339  VAL B O     1 
ATOM   11645 C CB    A VAL B 1 341  ? -8.922  9.356   102.366 0.59 15.94 ?  339  VAL B CB    1 
ATOM   11646 C CB    B VAL B 1 341  ? -8.936  9.350   102.368 0.41 15.95 ?  339  VAL B CB    1 
ATOM   11647 C CG1   A VAL B 1 341  ? -8.757  9.404   100.862 0.59 17.56 ?  339  VAL B CG1   1 
ATOM   11648 C CG1   B VAL B 1 341  ? -7.990  8.160   102.452 0.41 16.19 ?  339  VAL B CG1   1 
ATOM   11649 C CG2   A VAL B 1 341  ? -8.283  8.101   102.907 0.59 16.56 ?  339  VAL B CG2   1 
ATOM   11650 C CG2   B VAL B 1 341  ? -10.265 9.033   103.025 0.41 16.81 ?  339  VAL B CG2   1 
ATOM   11651 N N     . GLN B 1 342  ? -8.841  12.646  101.812 1.00 14.97 ?  340  GLN B N     1 
ATOM   11652 C CA    . GLN B 1 342  ? -9.461  13.952  101.569 1.00 16.11 ?  340  GLN B CA    1 
ATOM   11653 C C     . GLN B 1 342  ? -10.535 13.834  100.485 1.00 14.32 ?  340  GLN B C     1 
ATOM   11654 O O     . GLN B 1 342  ? -10.228 13.606  99.307  1.00 14.13 ?  340  GLN B O     1 
ATOM   11655 C CB    . GLN B 1 342  ? -8.395  14.977  101.171 1.00 13.85 ?  340  GLN B CB    1 
ATOM   11656 C CG    . GLN B 1 342  ? -7.348  15.242  102.254 1.00 13.55 ?  340  GLN B CG    1 
ATOM   11657 C CD    . GLN B 1 342  ? -5.987  15.609  101.661 1.00 13.62 ?  340  GLN B CD    1 
ATOM   11658 O OE1   . GLN B 1 342  ? -5.525  14.965  100.722 1.00 14.02 ?  340  GLN B OE1   1 
ATOM   11659 N NE2   . GLN B 1 342  ? -5.339  16.640  102.219 1.00 12.85 ?  340  GLN B NE2   1 
ATOM   11660 N N     . ALA B 1 343  ? -11.792 14.052  100.880 1.00 14.63 ?  341  ALA B N     1 
ATOM   11661 C CA    . ALA B 1 343  ? -12.902 13.915  99.950  1.00 14.90 ?  341  ALA B CA    1 
ATOM   11662 C C     . ALA B 1 343  ? -12.938 15.012  98.896  1.00 14.93 ?  341  ALA B C     1 
ATOM   11663 O O     . ALA B 1 343  ? -13.593 14.823  97.866  1.00 15.01 ?  341  ALA B O     1 
ATOM   11664 C CB    . ALA B 1 343  ? -14.215 13.892  100.720 1.00 15.30 ?  341  ALA B CB    1 
ATOM   11665 N N     . TYR B 1 344  ? -12.236 16.139  99.090  1.00 14.88 ?  342  TYR B N     1 
ATOM   11666 C CA    . TYR B 1 344  ? -12.188 17.093  97.981  1.00 15.08 ?  342  TYR B CA    1 
ATOM   11667 C C     . TYR B 1 344  ? -11.289 16.625  96.855  1.00 13.57 ?  342  TYR B C     1 
ATOM   11668 O O     . TYR B 1 344  ? -11.237 17.291  95.809  1.00 14.91 ?  342  TYR B O     1 
ATOM   11669 C CB    . TYR B 1 344  ? -11.772 18.508  98.448  1.00 15.30 ?  342  TYR B CB    1 
ATOM   11670 C CG    . TYR B 1 344  ? -10.337 18.805  98.888  1.00 13.69 ?  342  TYR B CG    1 
ATOM   11671 C CD1   . TYR B 1 344  ? -9.349  17.830  98.958  1.00 13.26 ?  342  TYR B CD1   1 
ATOM   11672 C CD2   . TYR B 1 344  ? -9.999  20.095  99.270  1.00 12.43 ?  342  TYR B CD2   1 
ATOM   11673 C CE1   . TYR B 1 344  ? -8.041  18.149  99.373  1.00 12.47 ?  342  TYR B CE1   1 
ATOM   11674 C CE2   . TYR B 1 344  ? -8.731  20.421  99.700  1.00 13.20 ?  342  TYR B CE2   1 
ATOM   11675 C CZ    . TYR B 1 344  ? -7.751  19.459  99.756  1.00 12.34 ?  342  TYR B CZ    1 
ATOM   11676 O OH    . TYR B 1 344  ? -6.491  19.828  100.181 1.00 13.23 ?  342  TYR B OH    1 
ATOM   11677 N N     . GLY B 1 345  ? -10.604 15.497  97.032  1.00 13.60 ?  343  GLY B N     1 
ATOM   11678 C CA    . GLY B 1 345  ? -9.703  14.988  96.012  1.00 14.68 ?  343  GLY B CA    1 
ATOM   11679 C C     . GLY B 1 345  ? -10.397 13.995  95.093  1.00 14.95 ?  343  GLY B C     1 
ATOM   11680 O O     . GLY B 1 345  ? -11.180 13.153  95.535  1.00 14.81 ?  343  GLY B O     1 
ATOM   11681 N N     . LYS B 1 346  ? -10.057 14.083  93.804  1.00 15.08 ?  344  LYS B N     1 
ATOM   11682 C CA    . LYS B 1 346  ? -10.692 13.230  92.800  1.00 13.98 ?  344  LYS B CA    1 
ATOM   11683 C C     . LYS B 1 346  ? -10.317 11.767  92.963  1.00 15.19 ?  344  LYS B C     1 
ATOM   11684 O O     . LYS B 1 346  ? -11.033 10.897  92.467  1.00 16.29 ?  344  LYS B O     1 
ATOM   11685 C CB    . LYS B 1 346  ? -10.322 13.701  91.390  1.00 15.31 ?  344  LYS B CB    1 
ATOM   11686 C CG    . LYS B 1 346  ? -10.811 15.102  91.101  1.00 15.26 ?  344  LYS B CG    1 
ATOM   11687 C CD    . LYS B 1 346  ? -10.284 15.625  89.774  1.00 16.20 ?  344  LYS B CD    1 
ATOM   11688 C CE    . LYS B 1 346  ? -10.955 16.946  89.437  1.00 16.23 ?  344  LYS B CE    1 
ATOM   11689 N NZ    . LYS B 1 346  ? -10.448 17.542  88.158  1.00 16.76 ?  344  LYS B NZ    1 
ATOM   11690 N N     . ARG B 1 347  ? -9.211  11.475  93.631  1.00 13.80 ?  345  ARG B N     1 
ATOM   11691 C CA    . ARG B 1 347  ? -8.794  10.089  93.792  1.00 15.76 ?  345  ARG B CA    1 
ATOM   11692 C C     . ARG B 1 347  ? -9.425  9.406   94.993  1.00 16.59 ?  345  ARG B C     1 
ATOM   11693 O O     . ARG B 1 347  ? -9.285  8.183   95.124  1.00 16.68 ?  345  ARG B O     1 
ATOM   11694 C CB    . ARG B 1 347  ? -7.272  10.022  93.904  1.00 15.11 ?  345  ARG B CB    1 
ATOM   11695 C CG    . ARG B 1 347  ? -6.592  10.394  92.599  1.00 15.01 ?  345  ARG B CG    1 
ATOM   11696 C CD    . ARG B 1 347  ? -5.119  10.676  92.807  1.00 13.58 ?  345  ARG B CD    1 
ATOM   11697 N NE    . ARG B 1 347  ? -4.891  11.947  93.489  1.00 12.97 ?  345  ARG B NE    1 
ATOM   11698 C CZ    . ARG B 1 347  ? -3.705  12.305  93.961  1.00 14.71 ?  345  ARG B CZ    1 
ATOM   11699 N NH1   . ARG B 1 347  ? -2.643  11.530  93.809  1.00 15.69 ?  345  ARG B NH1   1 
ATOM   11700 N NH2   . ARG B 1 347  ? -3.581  13.460  94.613  1.00 14.09 ?  345  ARG B NH2   1 
ATOM   11701 N N     . CYS B 1 348  ? -10.130 10.156  95.843  1.00 14.87 ?  346  CYS B N     1 
ATOM   11702 C CA    . CYS B 1 348  ? -10.569 9.651   97.146  1.00 16.00 ?  346  CYS B CA    1 
ATOM   11703 C C     . CYS B 1 348  ? -11.238 8.277   97.107  1.00 18.67 ?  346  CYS B C     1 
ATOM   11704 O O     . CYS B 1 348  ? -10.791 7.384   97.844  1.00 18.34 ?  346  CYS B O     1 
ATOM   11705 C CB    . CYS B 1 348  ? -11.480 10.696  97.808  1.00 15.30 ?  346  CYS B CB    1 
ATOM   11706 S SG    . CYS B 1 348  ? -11.793 10.376  99.581  1.00 22.01 ?  346  CYS B SG    1 
ATOM   11707 N N     . PRO B 1 349  ? -12.273 8.018   96.295  1.00 16.77 ?  347  PRO B N     1 
ATOM   11708 C CA    . PRO B 1 349  ? -12.884 6.674   96.350  1.00 19.66 ?  347  PRO B CA    1 
ATOM   11709 C C     . PRO B 1 349  ? -11.927 5.569   95.928  1.00 19.85 ?  347  PRO B C     1 
ATOM   11710 O O     . PRO B 1 349  ? -12.005 4.444   96.445  1.00 19.13 ?  347  PRO B O     1 
ATOM   11711 C CB    . PRO B 1 349  ? -14.084 6.783   95.398  1.00 21.26 ?  347  PRO B CB    1 
ATOM   11712 C CG    . PRO B 1 349  ? -13.778 7.924   94.512  1.00 18.12 ?  347  PRO B CG    1 
ATOM   11713 C CD    . PRO B 1 349  ? -12.919 8.879   95.287  1.00 18.21 ?  347  PRO B CD    1 
ATOM   11714 N N     . PHE B 1 350  ? -11.002 5.873   95.024  1.00 18.13 ?  348  PHE B N     1 
ATOM   11715 C CA    . PHE B 1 350  ? -10.049 4.871   94.576  1.00 18.16 ?  348  PHE B CA    1 
ATOM   11716 C C     . PHE B 1 350  ? -8.981  4.623   95.627  1.00 19.52 ?  348  PHE B C     1 
ATOM   11717 O O     . PHE B 1 350  ? -8.540  3.482   95.802  1.00 19.52 ?  348  PHE B O     1 
ATOM   11718 C CB    . PHE B 1 350  ? -9.460  5.321   93.241  1.00 17.36 ?  348  PHE B CB    1 
ATOM   11719 C CG    . PHE B 1 350  ? -10.515 5.705   92.258  1.00 18.74 ?  348  PHE B CG    1 
ATOM   11720 C CD1   . PHE B 1 350  ? -11.214 4.727   91.582  1.00 22.45 ?  348  PHE B CD1   1 
ATOM   11721 C CD2   . PHE B 1 350  ? -10.852 7.035   92.060  1.00 18.72 ?  348  PHE B CD2   1 
ATOM   11722 C CE1   . PHE B 1 350  ? -12.224 5.058   90.694  1.00 24.40 ?  348  PHE B CE1   1 
ATOM   11723 C CE2   . PHE B 1 350  ? -11.863 7.379   91.171  1.00 19.73 ?  348  PHE B CE2   1 
ATOM   11724 C CZ    . PHE B 1 350  ? -12.550 6.384   90.490  1.00 22.36 ?  348  PHE B CZ    1 
ATOM   11725 N N     . VAL B 1 351  ? -8.579  5.675   96.345  1.00 17.65 ?  349  VAL B N     1 
ATOM   11726 C CA    . VAL B 1 351  ? -7.700  5.499   97.495  1.00 16.05 ?  349  VAL B CA    1 
ATOM   11727 C C     . VAL B 1 351  ? -8.370  4.622   98.546  1.00 18.91 ?  349  VAL B C     1 
ATOM   11728 O O     . VAL B 1 351  ? -7.734  3.748   99.146  1.00 19.39 ?  349  VAL B O     1 
ATOM   11729 C CB    . VAL B 1 351  ? -7.304  6.875   98.065  1.00 15.53 ?  349  VAL B CB    1 
ATOM   11730 C CG1   . VAL B 1 351  ? -6.492  6.722   99.358  1.00 18.10 ?  349  VAL B CG1   1 
ATOM   11731 C CG2   . VAL B 1 351  ? -6.514  7.663   97.028  1.00 16.33 ?  349  VAL B CG2   1 
ATOM   11732 N N     . LEU B 1 352  ? -9.666  4.833   98.782  1.00 18.51 ?  350  LEU B N     1 
ATOM   11733 C CA    . LEU B 1 352  ? -10.374 4.015   99.757  1.00 20.91 ?  350  LEU B CA    1 
ATOM   11734 C C     . LEU B 1 352  ? -10.436 2.556   99.323  1.00 19.22 ?  350  LEU B C     1 
ATOM   11735 O O     . LEU B 1 352  ? -10.288 1.656   100.158 1.00 21.86 ?  350  LEU B O     1 
ATOM   11736 C CB    . LEU B 1 352  ? -11.774 4.572   99.988  1.00 20.88 ?  350  LEU B CB    1 
ATOM   11737 C CG    . LEU B 1 352  ? -11.785 5.893   100.756 1.00 20.39 ?  350  LEU B CG    1 
ATOM   11738 C CD1   . LEU B 1 352  ? -13.209 6.392   100.854 1.00 21.03 ?  350  LEU B CD1   1 
ATOM   11739 C CD2   . LEU B 1 352  ? -11.177 5.703   102.152 1.00 22.34 ?  350  LEU B CD2   1 
ATOM   11740 N N     . ASP B 1 353  ? -10.654 2.303   98.022  1.00 19.12 ?  351  ASP B N     1 
ATOM   11741 C CA    . ASP B 1 353  ? -10.608 0.930   97.517  1.00 21.35 ?  351  ASP B CA    1 
ATOM   11742 C C     . ASP B 1 353  ? -9.262  0.287   97.821  1.00 21.57 ?  351  ASP B C     1 
ATOM   11743 O O     . ASP B 1 353  ? -9.195  -0.886  98.225  1.00 22.41 ?  351  ASP B O     1 
ATOM   11744 C CB    . ASP B 1 353  ? -10.857 0.904   96.003  1.00 21.51 ?  351  ASP B CB    1 
ATOM   11745 C CG    . ASP B 1 353  ? -12.296 1.237   95.625  1.00 23.89 ?  351  ASP B CG    1 
ATOM   11746 O OD1   . ASP B 1 353  ? -13.206 1.041   96.458  1.00 26.77 ?  351  ASP B OD1   1 
ATOM   11747 O OD2   . ASP B 1 353  ? -12.504 1.680   94.473  1.00 25.20 ?  351  ASP B OD2   1 
ATOM   11748 N N     . PHE B 1 354  ? -8.177  1.042   97.614  1.00 19.02 ?  352  PHE B N     1 
ATOM   11749 C CA    . PHE B 1 354  ? -6.843  0.541   97.927  1.00 18.11 ?  352  PHE B CA    1 
ATOM   11750 C C     . PHE B 1 354  ? -6.685  0.248   99.419  1.00 19.70 ?  352  PHE B C     1 
ATOM   11751 O O     . PHE B 1 354  ? -6.133  -0.792  99.795  1.00 20.71 ?  352  PHE B O     1 
ATOM   11752 C CB    . PHE B 1 354  ? -5.785  1.548   97.468  1.00 19.63 ?  352  PHE B CB    1 
ATOM   11753 C CG    . PHE B 1 354  ? -4.410  1.234   97.982  1.00 18.37 ?  352  PHE B CG    1 
ATOM   11754 C CD1   . PHE B 1 354  ? -3.612  0.315   97.326  1.00 22.11 ?  352  PHE B CD1   1 
ATOM   11755 C CD2   . PHE B 1 354  ? -3.929  1.838   99.141  1.00 21.39 ?  352  PHE B CD2   1 
ATOM   11756 C CE1   . PHE B 1 354  ? -2.349  -0.000  97.808  1.00 21.26 ?  352  PHE B CE1   1 
ATOM   11757 C CE2   . PHE B 1 354  ? -2.671  1.525   99.631  1.00 20.82 ?  352  PHE B CE2   1 
ATOM   11758 C CZ    . PHE B 1 354  ? -1.880  0.602   98.956  1.00 23.07 ?  352  PHE B CZ    1 
ATOM   11759 N N     . ILE B 1 355  ? -7.165  1.150   100.282 1.00 19.91 ?  353  ILE B N     1 
ATOM   11760 C CA    . ILE B 1 355  ? -6.959  0.991   101.724 1.00 19.96 ?  353  ILE B CA    1 
ATOM   11761 C C     . ILE B 1 355  ? -7.776  -0.177  102.250 1.00 21.22 ?  353  ILE B C     1 
ATOM   11762 O O     . ILE B 1 355  ? -7.293  -0.972  103.065 1.00 22.03 ?  353  ILE B O     1 
ATOM   11763 C CB    . ILE B 1 355  ? -7.308  2.292   102.473 1.00 19.09 ?  353  ILE B CB    1 
ATOM   11764 C CG1   . ILE B 1 355  ? -6.316  3.396   102.115 1.00 22.06 ?  353  ILE B CG1   1 
ATOM   11765 C CG2   . ILE B 1 355  ? -7.363  2.061   103.996 1.00 21.52 ?  353  ILE B CG2   1 
ATOM   11766 C CD1   . ILE B 1 355  ? -6.724  4.755   102.640 1.00 20.61 ?  353  ILE B CD1   1 
ATOM   11767 N N     . ILE B 1 356  ? -9.030  -0.294  101.800 1.00 19.78 ?  354  ILE B N     1 
ATOM   11768 C CA    . ILE B 1 356  ? -9.881  -1.399  102.229 1.00 23.21 ?  354  ILE B CA    1 
ATOM   11769 C C     . ILE B 1 356  ? -9.266  -2.729  101.816 1.00 21.85 ?  354  ILE B C     1 
ATOM   11770 O O     . ILE B 1 356  ? -9.257  -3.696  102.592 1.00 23.15 ?  354  ILE B O     1 
ATOM   11771 C CB    . ILE B 1 356  ? -11.301 -1.225  101.655 1.00 22.01 ?  354  ILE B CB    1 
ATOM   11772 C CG1   . ILE B 1 356  ? -12.023 -0.080  102.364 1.00 21.86 ?  354  ILE B CG1   1 
ATOM   11773 C CG2   . ILE B 1 356  ? -12.097 -2.517  101.770 1.00 23.26 ?  354  ILE B CG2   1 
ATOM   11774 C CD1   . ILE B 1 356  ? -13.256 0.419   101.624 1.00 23.39 ?  354  ILE B CD1   1 
ATOM   11775 N N     . ASP B 1 357  ? -8.741  -2.799  100.590 1.00 22.68 ?  355  ASP B N     1 
ATOM   11776 C CA    . ASP B 1 357  ? -8.095  -4.029  100.143 1.00 23.69 ?  355  ASP B CA    1 
ATOM   11777 C C     . ASP B 1 357  ? -6.817  -4.303  100.927 1.00 25.95 ?  355  ASP B C     1 
ATOM   11778 O O     . ASP B 1 357  ? -6.528  -5.458  101.256 1.00 24.80 ?  355  ASP B O     1 
ATOM   11779 C CB    . ASP B 1 357  ? -7.797  -3.962  98.649  1.00 24.79 ?  355  ASP B CB    1 
ATOM   11780 C CG    . ASP B 1 357  ? -6.937  -5.114  98.182  1.00 25.27 ?  355  ASP B CG    1 
ATOM   11781 O OD1   . ASP B 1 357  ? -7.485  -6.223  97.981  1.00 27.03 ?  355  ASP B OD1   1 
ATOM   11782 O OD2   . ASP B 1 357  ? -5.712  -4.917  98.024  1.00 24.25 ?  355  ASP B OD2   1 
ATOM   11783 N N     . LEU B 1 358  ? -6.040  -3.256  101.237 1.00 23.20 ?  356  LEU B N     1 
ATOM   11784 C CA    . LEU B 1 358  ? -4.838  -3.438  102.052 1.00 22.63 ?  356  LEU B CA    1 
ATOM   11785 C C     . LEU B 1 358  ? -5.185  -3.992  103.429 1.00 24.72 ?  356  LEU B C     1 
ATOM   11786 O O     . LEU B 1 358  ? -4.487  -4.869  103.956 1.00 24.47 ?  356  LEU B O     1 
ATOM   11787 C CB    . LEU B 1 358  ? -4.094  -2.104  102.179 1.00 20.11 ?  356  LEU B CB    1 
ATOM   11788 C CG    . LEU B 1 358  ? -2.912  -2.076  103.154 1.00 19.32 ?  356  LEU B CG    1 
ATOM   11789 C CD1   . LEU B 1 358  ? -1.841  -3.064  102.742 1.00 23.65 ?  356  LEU B CD1   1 
ATOM   11790 C CD2   . LEU B 1 358  ? -2.335  -0.658  103.236 1.00 19.97 ?  356  LEU B CD2   1 
ATOM   11791 N N     . ALA B 1 359  ? -6.268  -3.494  104.023 1.00 21.72 ?  357  ALA B N     1 
ATOM   11792 C CA    . ALA B 1 359  ? -6.702  -3.977  105.326 1.00 23.23 ?  357  ALA B CA    1 
ATOM   11793 C C     . ALA B 1 359  ? -7.073  -5.452  105.266 1.00 25.67 ?  357  ALA B C     1 
ATOM   11794 O O     . ALA B 1 359  ? -6.671  -6.236  106.135 1.00 25.05 ?  357  ALA B O     1 
ATOM   11795 C CB    . ALA B 1 359  ? -7.880  -3.136  105.814 1.00 25.10 ?  357  ALA B CB    1 
ATOM   11796 N N     . ARG B 1 360  ? -7.834  -5.838  104.239 1.00 28.37 ?  358  ARG B N     1 
ATOM   11797 C CA    . ARG B 1 360  ? -8.196  -7.240  104.040 1.00 29.49 ?  358  ARG B CA    1 
ATOM   11798 C C     . ARG B 1 360  ? -6.960  -8.108  103.867 1.00 24.75 ?  358  ARG B C     1 
ATOM   11799 O O     . ARG B 1 360  ? -6.840  -9.171  104.492 1.00 28.94 ?  358  ARG B O     1 
ATOM   11800 C CB    . ARG B 1 360  ? -9.098  -7.373  102.815 1.00 29.23 ?  358  ARG B CB    1 
ATOM   11801 C CG    . ARG B 1 360  ? -10.509 -6.885  102.999 1.00 30.95 ?  358  ARG B CG    1 
ATOM   11802 C CD    . ARG B 1 360  ? -11.342 -7.322  101.798 1.00 39.33 ?  358  ARG B CD    1 
ATOM   11803 N NE    . ARG B 1 360  ? -12.279 -6.288  101.384 1.00 41.76 ?  358  ARG B NE    1 
ATOM   11804 C CZ    . ARG B 1 360  ? -13.472 -6.103  101.928 1.00 39.91 ?  358  ARG B CZ    1 
ATOM   11805 N NH1   . ARG B 1 360  ? -13.914 -6.876  102.906 1.00 46.52 ?  358  ARG B NH1   1 
ATOM   11806 N NH2   . ARG B 1 360  ? -14.243 -5.118  101.477 1.00 41.73 ?  358  ARG B NH2   1 
ATOM   11807 N N     . ARG B 1 361  ? -6.048  -7.677  102.995 1.00 27.41 ?  359  ARG B N     1 
ATOM   11808 C CA    . ARG B 1 361  ? -4.819  -8.411  102.715 1.00 30.14 ?  359  ARG B CA    1 
ATOM   11809 C C     . ARG B 1 361  ? -3.996  -8.629  103.972 1.00 30.94 ?  359  ARG B C     1 
ATOM   11810 O O     . ARG B 1 361  ? -3.418  -9.702  104.166 1.00 25.52 ?  359  ARG B O     1 
ATOM   11811 C CB    . ARG B 1 361  ? -3.966  -7.641  101.707 1.00 31.71 ?  359  ARG B CB    1 
ATOM   11812 C CG    . ARG B 1 361  ? -4.410  -7.670  100.272 1.00 37.97 ?  359  ARG B CG    1 
ATOM   11813 C CD    . ARG B 1 361  ? -3.292  -7.104  99.425  1.00 30.51 ?  359  ARG B CD    1 
ATOM   11814 N NE    . ARG B 1 361  ? -3.218  -5.645  99.448  1.00 24.09 ?  359  ARG B NE    1 
ATOM   11815 C CZ    . ARG B 1 361  ? -2.086  -4.961  99.524  1.00 23.82 ?  359  ARG B CZ    1 
ATOM   11816 N NH1   . ARG B 1 361  ? -0.935  -5.557  99.802  1.00 26.96 ?  359  ARG B NH1   1 
ATOM   11817 N NH2   . ARG B 1 361  ? -2.105  -3.647  99.315  1.00 22.64 ?  359  ARG B NH2   1 
ATOM   11818 N N     . SER B 1 362  ? -3.892  -7.601  104.811 1.00 27.62 ?  360  SER B N     1 
ATOM   11819 C CA    . SER B 1 362  ? -2.894  -7.563  105.868 1.00 25.53 ?  360  SER B CA    1 
ATOM   11820 C C     . SER B 1 362  ? -3.420  -7.983  107.230 1.00 25.01 ?  360  SER B C     1 
ATOM   11821 O O     . SER B 1 362  ? -2.625  -8.078  108.170 1.00 25.71 ?  360  SER B O     1 
ATOM   11822 C CB    . SER B 1 362  ? -2.313  -6.151  105.984 1.00 27.60 ?  360  SER B CB    1 
ATOM   11823 O OG    . SER B 1 362  ? -3.334  -5.248  106.359 1.00 24.01 ?  360  SER B OG    1 
ATOM   11824 N N     . GLY B 1 363  ? -4.721  -8.215  107.378 1.00 24.87 ?  361  GLY B N     1 
ATOM   11825 C CA    . GLY B 1 363  ? -5.230  -8.555  108.693 1.00 25.85 ?  361  GLY B CA    1 
ATOM   11826 C C     . GLY B 1 363  ? -5.122  -7.420  109.686 1.00 25.05 ?  361  GLY B C     1 
ATOM   11827 O O     . GLY B 1 363  ? -4.966  -7.658  110.891 1.00 28.13 ?  361  GLY B O     1 
ATOM   11828 N N     . ARG B 1 364  ? -5.183  -6.187  109.198 1.00 24.51 ?  362  ARG B N     1 
ATOM   11829 C CA    . ARG B 1 364  ? -5.164  -4.984  110.015 1.00 28.29 ?  362  ARG B CA    1 
ATOM   11830 C C     . ARG B 1 364  ? -6.480  -4.259  109.815 1.00 27.08 ?  362  ARG B C     1 
ATOM   11831 O O     . ARG B 1 364  ? -6.894  -4.029  108.675 1.00 29.03 ?  362  ARG B O     1 
ATOM   11832 C CB    . ARG B 1 364  ? -4.027  -4.045  109.609 1.00 24.98 ?  362  ARG B CB    1 
ATOM   11833 C CG    . ARG B 1 364  ? -2.640  -4.615  109.742 1.00 27.40 ?  362  ARG B CG    1 
ATOM   11834 C CD    . ARG B 1 364  ? -2.208  -4.700  111.196 1.00 25.95 ?  362  ARG B CD    1 
ATOM   11835 N NE    . ARG B 1 364  ? -0.912  -5.356  111.275 1.00 26.63 ?  362  ARG B NE    1 
ATOM   11836 C CZ    . ARG B 1 364  ? 0.245   -4.758  111.033 1.00 21.81 ?  362  ARG B CZ    1 
ATOM   11837 N NH1   . ARG B 1 364  ? 0.319   -3.449  110.819 1.00 22.99 ?  362  ARG B NH1   1 
ATOM   11838 N NH2   . ARG B 1 364  ? 1.356   -5.492  111.000 1.00 24.64 ?  362  ARG B NH2   1 
ATOM   11839 N N     . ARG B 1 365  ? -7.139  -3.895  110.901 1.00 23.77 ?  363  ARG B N     1 
ATOM   11840 C CA    . ARG B 1 365  ? -8.225  -2.935  110.777 1.00 23.83 ?  363  ARG B CA    1 
ATOM   11841 C C     . ARG B 1 365  ? -7.621  -1.539  110.762 1.00 22.26 ?  363  ARG B C     1 
ATOM   11842 O O     . ARG B 1 365  ? -6.969  -1.135  111.727 1.00 25.37 ?  363  ARG B O     1 
ATOM   11843 C CB    . ARG B 1 365  ? -9.228  -3.087  111.911 1.00 23.99 ?  363  ARG B CB    1 
ATOM   11844 C CG    . ARG B 1 365  ? -10.512 -2.310  111.650 1.00 26.87 ?  363  ARG B CG    1 
ATOM   11845 C CD    . ARG B 1 365  ? -11.584 -2.646  112.678 1.00 29.02 ?  363  ARG B CD    1 
ATOM   11846 N NE    . ARG B 1 365  ? -12.861 -2.046  112.309 1.00 29.60 ?  363  ARG B NE    1 
ATOM   11847 C CZ    . ARG B 1 365  ? -13.589 -1.270  113.098 1.00 29.56 ?  363  ARG B CZ    1 
ATOM   11848 N NH1   . ARG B 1 365  ? -13.224 -1.013  114.345 1.00 28.91 ?  363  ARG B NH1   1 
ATOM   11849 N NH2   . ARG B 1 365  ? -14.721 -0.749  112.630 1.00 27.69 ?  363  ARG B NH2   1 
ATOM   11850 N N     . ILE B 1 366  ? -7.781  -0.826  109.656 1.00 21.85 ?  364  ILE B N     1 
ATOM   11851 C CA    . ILE B 1 366  ? -7.160  0.484   109.484 1.00 21.30 ?  364  ILE B CA    1 
ATOM   11852 C C     . ILE B 1 366  ? -8.169  1.553   109.867 1.00 23.08 ?  364  ILE B C     1 
ATOM   11853 O O     . ILE B 1 366  ? -9.328  1.507   109.435 1.00 22.91 ?  364  ILE B O     1 
ATOM   11854 C CB    . ILE B 1 366  ? -6.670  0.669   108.040 1.00 20.05 ?  364  ILE B CB    1 
ATOM   11855 C CG1   . ILE B 1 366  ? -5.641  -0.415  107.711 1.00 21.23 ?  364  ILE B CG1   1 
ATOM   11856 C CG2   . ILE B 1 366  ? -6.095  2.082   107.837 1.00 19.72 ?  364  ILE B CG2   1 
ATOM   11857 C CD1   . ILE B 1 366  ? -5.174  -0.422  106.267 1.00 22.72 ?  364  ILE B CD1   1 
ATOM   11858 N N     . MET B 1 367  ? -7.741  2.512   110.692 1.00 21.56 ?  365  MET B N     1 
ATOM   11859 C CA    . MET B 1 367  ? -8.587  3.649   111.031 1.00 20.26 ?  365  MET B CA    1 
ATOM   11860 C C     . MET B 1 367  ? -8.501  4.645   109.892 1.00 23.85 ?  365  MET B C     1 
ATOM   11861 O O     . MET B 1 367  ? -7.401  5.056   109.522 1.00 21.32 ?  365  MET B O     1 
ATOM   11862 C CB    . MET B 1 367  ? -8.145  4.294   112.345 1.00 21.07 ?  365  MET B CB    1 
ATOM   11863 C CG    . MET B 1 367  ? -8.029  3.298   113.494 1.00 22.63 ?  365  MET B CG    1 
ATOM   11864 S SD    . MET B 1 367  ? -7.470  3.948   115.115 1.00 24.82 ?  365  MET B SD    1 
ATOM   11865 C CE    . MET B 1 367  ? -9.005  4.249   115.996 1.00 32.73 ?  365  MET B CE    1 
ATOM   11866 N N     . VAL B 1 368  ? -9.638  4.992   109.296 1.00 20.68 ?  366  VAL B N     1 
ATOM   11867 C CA    . VAL B 1 368  ? -9.656  5.872   108.134 1.00 18.25 ?  366  VAL B CA    1 
ATOM   11868 C C     . VAL B 1 368  ? -10.400 7.138   108.509 1.00 18.99 ?  366  VAL B C     1 
ATOM   11869 O O     . VAL B 1 368  ? -11.611 7.109   108.759 1.00 20.79 ?  366  VAL B O     1 
ATOM   11870 C CB    . VAL B 1 368  ? -10.290 5.211   106.906 1.00 19.57 ?  366  VAL B CB    1 
ATOM   11871 C CG1   . VAL B 1 368  ? -10.293 6.189   105.749 1.00 20.38 ?  366  VAL B CG1   1 
ATOM   11872 C CG2   . VAL B 1 368  ? -9.514  3.955   106.542 1.00 21.89 ?  366  VAL B CG2   1 
ATOM   11873 N N     . ARG B 1 369  ? -9.681  8.254   108.552 1.00 17.49 ?  367  ARG B N     1 
ATOM   11874 C CA    . ARG B 1 369  ? -10.302 9.539   108.832 1.00 17.27 ?  367  ARG B CA    1 
ATOM   11875 C C     . ARG B 1 369  ? -10.696 10.160  107.505 1.00 18.23 ?  367  ARG B C     1 
ATOM   11876 O O     . ARG B 1 369  ? -9.833  10.508  106.696 1.00 17.92 ?  367  ARG B O     1 
ATOM   11877 C CB    . ARG B 1 369  ? -9.366  10.473  109.592 1.00 18.67 ?  367  ARG B CB    1 
ATOM   11878 C CG    . ARG B 1 369  ? -10.056 11.767  109.942 1.00 18.53 ?  367  ARG B CG    1 
ATOM   11879 C CD    . ARG B 1 369  ? -9.076  12.848  110.291 1.00 19.34 ?  367  ARG B CD    1 
ATOM   11880 N NE    . ARG B 1 369  ? -8.397  12.557  111.542 1.00 19.41 ?  367  ARG B NE    1 
ATOM   11881 C CZ    . ARG B 1 369  ? -7.206  13.035  111.876 1.00 19.43 ?  367  ARG B CZ    1 
ATOM   11882 N NH1   . ARG B 1 369  ? -6.517  13.816  111.054 1.00 19.22 ?  367  ARG B NH1   1 
ATOM   11883 N NH2   . ARG B 1 369  ? -6.696  12.719  113.065 1.00 19.02 ?  367  ARG B NH2   1 
ATOM   11884 N N     . LEU B 1 370  ? -11.995 10.300  107.283 1.00 17.09 ?  368  LEU B N     1 
ATOM   11885 C CA    . LEU B 1 370  ? -12.492 10.976  106.094 1.00 17.83 ?  368  LEU B CA    1 
ATOM   11886 C C     . LEU B 1 370  ? -12.662 12.455  106.408 1.00 16.68 ?  368  LEU B C     1 
ATOM   11887 O O     . LEU B 1 370  ? -13.406 12.824  107.326 1.00 18.81 ?  368  LEU B O     1 
ATOM   11888 C CB    . LEU B 1 370  ? -13.811 10.358  105.639 1.00 18.01 ?  368  LEU B CB    1 
ATOM   11889 C CG    . LEU B 1 370  ? -14.363 10.918  104.331 1.00 17.40 ?  368  LEU B CG    1 
ATOM   11890 C CD1   . LEU B 1 370  ? -13.476 10.570  103.148 1.00 20.84 ?  368  LEU B CD1   1 
ATOM   11891 C CD2   . LEU B 1 370  ? -15.775 10.378  104.102 1.00 17.47 ?  368  LEU B CD2   1 
ATOM   11892 N N     . VAL B 1 371  ? -11.933 13.295  105.679 1.00 15.81 ?  369  VAL B N     1 
ATOM   11893 C CA    . VAL B 1 371  ? -12.022 14.739  105.803 1.00 16.86 ?  369  VAL B CA    1 
ATOM   11894 C C     . VAL B 1 371  ? -12.396 15.295  104.446 1.00 17.01 ?  369  VAL B C     1 
ATOM   11895 O O     . VAL B 1 371  ? -12.312 14.609  103.425 1.00 17.61 ?  369  VAL B O     1 
ATOM   11896 C CB    . VAL B 1 371  ? -10.708 15.376  106.295 1.00 15.05 ?  369  VAL B CB    1 
ATOM   11897 C CG1   . VAL B 1 371  ? -10.243 14.728  107.578 1.00 15.40 ?  369  VAL B CG1   1 
ATOM   11898 C CG2   . VAL B 1 371  ? -9.632  15.279  105.210 1.00 15.72 ?  369  VAL B CG2   1 
ATOM   11899 N N     . LYS B 1 372  ? -12.749 16.577  104.424 1.00 14.87 ?  370  LYS B N     1 
ATOM   11900 C CA    . LYS B 1 372  ? -12.937 17.210  103.125 1.00 14.50 ?  370  LYS B CA    1 
ATOM   11901 C C     . LYS B 1 372  ? -11.604 17.670  102.532 1.00 13.93 ?  370  LYS B C     1 
ATOM   11902 O O     . LYS B 1 372  ? -11.231 17.232  101.441 1.00 16.64 ?  370  LYS B O     1 
ATOM   11903 C CB    . LYS B 1 372  ? -13.980 18.322  103.238 1.00 16.61 ?  370  LYS B CB    1 
ATOM   11904 C CG    . LYS B 1 372  ? -15.349 17.681  103.461 1.00 16.90 ?  370  LYS B CG    1 
ATOM   11905 C CD    . LYS B 1 372  ? -16.498 18.654  103.524 1.00 17.95 ?  370  LYS B CD    1 
ATOM   11906 C CE    . LYS B 1 372  ? -17.734 17.940  104.049 1.00 19.77 ?  370  LYS B CE    1 
ATOM   11907 N NZ    . LYS B 1 372  ? -18.851 18.905  104.204 1.00 19.70 ?  370  LYS B NZ    1 
ATOM   11908 N N     . GLY B 1 373  ? -10.851 18.509  103.239 1.00 14.18 ?  371  GLY B N     1 
ATOM   11909 C CA    . GLY B 1 373  ? -9.481  18.797  102.826 1.00 13.67 ?  371  GLY B CA    1 
ATOM   11910 C C     . GLY B 1 373  ? -9.056  20.215  103.142 1.00 14.35 ?  371  GLY B C     1 
ATOM   11911 O O     . GLY B 1 373  ? -9.876  21.131  103.050 1.00 15.39 ?  371  GLY B O     1 
ATOM   11912 N N     . ALA B 1 374  ? -7.798  20.423  103.532 1.00 12.72 ?  372  ALA B N     1 
ATOM   11913 C CA    . ALA B 1 374  ? -7.389  21.688  104.126 1.00 12.41 ?  372  ALA B CA    1 
ATOM   11914 C C     . ALA B 1 374  ? -6.591  22.591  103.206 1.00 13.78 ?  372  ALA B C     1 
ATOM   11915 O O     . ALA B 1 374  ? -6.242  23.708  103.619 1.00 14.87 ?  372  ALA B O     1 
ATOM   11916 C CB    . ALA B 1 374  ? -6.553  21.445  105.383 1.00 12.55 ?  372  ALA B CB    1 
ATOM   11917 N N     . TYR B 1 375  ? -6.291  22.157  101.979 1.00 12.15 ?  373  TYR B N     1 
ATOM   11918 C CA    . TYR B 1 375  ? -5.327  22.862  101.140 1.00 11.35 ?  373  TYR B CA    1 
ATOM   11919 C C     . TYR B 1 375  ? -5.938  23.362  99.842  1.00 14.02 ?  373  TYR B C     1 
ATOM   11920 O O     . TYR B 1 375  ? -5.224  23.543  98.861  1.00 12.84 ?  373  TYR B O     1 
ATOM   11921 C CB    . TYR B 1 375  ? -4.122  21.972  100.828 1.00 13.96 ?  373  TYR B CB    1 
ATOM   11922 C CG    . TYR B 1 375  ? -3.440  21.419  102.053 1.00 13.74 ?  373  TYR B CG    1 
ATOM   11923 C CD1   . TYR B 1 375  ? -3.981  20.338  102.750 1.00 13.59 ?  373  TYR B CD1   1 
ATOM   11924 C CD2   . TYR B 1 375  ? -2.254  21.980  102.532 1.00 15.83 ?  373  TYR B CD2   1 
ATOM   11925 C CE1   . TYR B 1 375  ? -3.376  19.847  103.882 1.00 15.65 ?  373  TYR B CE1   1 
ATOM   11926 C CE2   . TYR B 1 375  ? -1.634  21.478  103.643 1.00 18.30 ?  373  TYR B CE2   1 
ATOM   11927 C CZ    . TYR B 1 375  ? -2.196  20.411  104.316 1.00 16.58 ?  373  TYR B CZ    1 
ATOM   11928 O OH    . TYR B 1 375  ? -1.579  19.915  105.441 1.00 20.46 ?  373  TYR B OH    1 
ATOM   11929 N N     . TRP B 1 376  ? -7.243  23.625  99.827  1.00 12.67 ?  374  TRP B N     1 
ATOM   11930 C CA    . TRP B 1 376  ? -7.941  23.808  98.559  1.00 12.04 ?  374  TRP B CA    1 
ATOM   11931 C C     . TRP B 1 376  ? -7.348  24.947  97.725  1.00 13.19 ?  374  TRP B C     1 
ATOM   11932 O O     . TRP B 1 376  ? -6.998  24.750  96.554  1.00 12.31 ?  374  TRP B O     1 
ATOM   11933 C CB    . TRP B 1 376  ? -9.435  24.036  98.811  1.00 14.27 ?  374  TRP B CB    1 
ATOM   11934 C CG    . TRP B 1 376  ? -10.178 24.183  97.535  1.00 13.09 ?  374  TRP B CG    1 
ATOM   11935 C CD1   . TRP B 1 376  ? -10.543 23.180  96.682  1.00 12.82 ?  374  TRP B CD1   1 
ATOM   11936 C CD2   . TRP B 1 376  ? -10.623 25.405  96.935  1.00 14.99 ?  374  TRP B CD2   1 
ATOM   11937 N NE1   . TRP B 1 376  ? -11.195 23.705  95.584  1.00 13.92 ?  374  TRP B NE1   1 
ATOM   11938 C CE2   . TRP B 1 376  ? -11.243 25.069  95.711  1.00 15.55 ?  374  TRP B CE2   1 
ATOM   11939 C CE3   . TRP B 1 376  ? -10.557 26.751  97.314  1.00 18.53 ?  374  TRP B CE3   1 
ATOM   11940 C CZ2   . TRP B 1 376  ? -11.802 26.024  94.869  1.00 16.22 ?  374  TRP B CZ2   1 
ATOM   11941 C CZ3   . TRP B 1 376  ? -11.114 27.706  96.474  1.00 19.49 ?  374  TRP B CZ3   1 
ATOM   11942 C CH2   . TRP B 1 376  ? -11.731 27.336  95.262  1.00 18.08 ?  374  TRP B CH2   1 
ATOM   11943 N N     . ASP B 1 377  ? -7.239  26.154  98.290  1.00 13.92 ?  375  ASP B N     1 
ATOM   11944 C CA    . ASP B 1 377  ? -6.819  27.265  97.444  1.00 14.38 ?  375  ASP B CA    1 
ATOM   11945 C C     . ASP B 1 377  ? -5.382  27.087  96.960  1.00 11.98 ?  375  ASP B C     1 
ATOM   11946 O O     . ASP B 1 377  ? -5.055  27.510  95.842  1.00 13.48 ?  375  ASP B O     1 
ATOM   11947 C CB    . ASP B 1 377  ? -7.027  28.630  98.135  1.00 18.65 ?  375  ASP B CB    1 
ATOM   11948 C CG    . ASP B 1 377  ? -6.399  28.734  99.509  1.00 23.75 ?  375  ASP B CG    1 
ATOM   11949 O OD1   . ASP B 1 377  ? -5.428  28.023  99.822  1.00 28.27 ?  375  ASP B OD1   1 
ATOM   11950 O OD2   . ASP B 1 377  ? -6.907  29.568  100.295 1.00 27.77 ?  375  ASP B OD2   1 
ATOM   11951 N N     . ALA B 1 378  ? -4.535  26.418  97.744  1.00 12.86 ?  376  ALA B N     1 
ATOM   11952 C CA    . ALA B 1 378  ? -3.171  26.152  97.298  1.00 11.03 ?  376  ALA B CA    1 
ATOM   11953 C C     . ALA B 1 378  ? -3.146  25.142  96.158  1.00 13.06 ?  376  ALA B C     1 
ATOM   11954 O O     . ALA B 1 378  ? -2.286  25.232  95.264  1.00 13.30 ?  376  ALA B O     1 
ATOM   11955 C CB    . ALA B 1 378  ? -2.329  25.651  98.477  1.00 13.74 ?  376  ALA B CB    1 
ATOM   11956 N N     . GLU B 1 379  ? -4.058  24.169  96.175  1.00 12.21 ?  377  GLU B N     1 
ATOM   11957 C CA    . GLU B 1 379  ? -4.106  23.214  95.071  1.00 11.33 ?  377  GLU B CA    1 
ATOM   11958 C C     . GLU B 1 379  ? -4.548  23.889  93.785  1.00 11.80 ?  377  GLU B C     1 
ATOM   11959 O O     . GLU B 1 379  ? -4.030  23.565  92.711  1.00 12.42 ?  377  GLU B O     1 
ATOM   11960 C CB    . GLU B 1 379  ? -5.031  22.032  95.381  1.00 12.28 ?  377  GLU B CB    1 
ATOM   11961 C CG    . GLU B 1 379  ? -4.630  21.231  96.633  1.00 14.71 ?  377  GLU B CG    1 
ATOM   11962 C CD    . GLU B 1 379  ? -3.302  20.468  96.516  1.00 15.16 ?  377  GLU B CD    1 
ATOM   11963 O OE1   . GLU B 1 379  ? -2.675  20.436  95.420  1.00 15.00 ?  377  GLU B OE1   1 
ATOM   11964 O OE2   . GLU B 1 379  ? -2.889  19.876  97.546  1.00 14.56 ?  377  GLU B OE2   1 
ATOM   11965 N N     . ILE B 1 380  ? -5.484  24.838  93.859  1.00 11.05 ?  378  ILE B N     1 
ATOM   11966 C CA    . ILE B 1 380  ? -5.875  25.558  92.648  1.00 10.86 ?  378  ILE B CA    1 
ATOM   11967 C C     . ILE B 1 380  ? -4.690  26.330  92.087  1.00 12.09 ?  378  ILE B C     1 
ATOM   11968 O O     . ILE B 1 380  ? -4.384  26.255  90.883  1.00 11.55 ?  378  ILE B O     1 
ATOM   11969 C CB    . ILE B 1 380  ? -7.065  26.489  92.932  1.00 11.81 ?  378  ILE B CB    1 
ATOM   11970 C CG1   . ILE B 1 380  ? -8.242  25.701  93.515  1.00 13.13 ?  378  ILE B CG1   1 
ATOM   11971 C CG2   . ILE B 1 380  ? -7.433  27.271  91.674  1.00 13.78 ?  378  ILE B CG2   1 
ATOM   11972 C CD1   . ILE B 1 380  ? -8.789  24.601  92.596  1.00 13.65 ?  378  ILE B CD1   1 
ATOM   11973 N N     . LYS B 1 381  ? -3.999  27.079  92.952  1.00 11.19 ?  379  LYS B N     1 
ATOM   11974 C CA    . LYS B 1 381  ? -2.859  27.872  92.501  1.00 11.23 ?  379  LYS B CA    1 
ATOM   11975 C C     . LYS B 1 381  ? -1.787  26.984  91.882  1.00 12.36 ?  379  LYS B C     1 
ATOM   11976 O O     . LYS B 1 381  ? -1.257  27.293  90.807  1.00 12.43 ?  379  LYS B O     1 
ATOM   11977 C CB    . LYS B 1 381  ? -2.269  28.678  93.655  1.00 11.09 ?  379  LYS B CB    1 
ATOM   11978 C CG    . LYS B 1 381  ? -1.071  29.511  93.225  1.00 12.40 ?  379  LYS B CG    1 
ATOM   11979 C CD    . LYS B 1 381  ? -0.620  30.426  94.370  1.00 10.81 ?  379  LYS B CD    1 
ATOM   11980 C CE    . LYS B 1 381  ? 0.466   31.382  93.879  1.00 13.54 ?  379  LYS B CE    1 
ATOM   11981 N NZ    . LYS B 1 381  ? 0.978   32.251  94.996  1.00 11.80 ?  379  LYS B NZ    1 
ATOM   11982 N N     . ARG B 1 382  ? -1.460  25.863  92.544  1.00 10.87 ?  380  ARG B N     1 
ATOM   11983 C CA    . ARG B 1 382  ? -0.358  25.029  92.060  1.00 13.04 ?  380  ARG B CA    1 
ATOM   11984 C C     . ARG B 1 382  ? -0.657  24.452  90.681  1.00 11.74 ?  380  ARG B C     1 
ATOM   11985 O O     . ARG B 1 382  ? 0.218   24.442  89.804  1.00 11.75 ?  380  ARG B O     1 
ATOM   11986 C CB    . ARG B 1 382  ? -0.079  23.898  93.055  1.00 13.94 ?  380  ARG B CB    1 
ATOM   11987 C CG    . ARG B 1 382  ? 1.195   23.116  92.757  1.00 20.35 ?  380  ARG B CG    1 
ATOM   11988 C CD    . ARG B 1 382  ? 2.412   23.944  93.121  1.00 28.86 ?  380  ARG B CD    1 
ATOM   11989 N NE    . ARG B 1 382  ? 3.172   24.372  91.953  1.00 33.40 ?  380  ARG B NE    1 
ATOM   11990 C CZ    . ARG B 1 382  ? 4.108   25.314  91.971  1.00 34.04 ?  380  ARG B CZ    1 
ATOM   11991 N NH1   . ARG B 1 382  ? 4.384   25.998  93.074  1.00 34.64 ?  380  ARG B NH1   1 
ATOM   11992 N NH2   . ARG B 1 382  ? 4.787   25.577  90.855  1.00 29.55 ?  380  ARG B NH2   1 
ATOM   11993 N N     . ALA B 1 383  ? -1.875  23.959  90.469  1.00 11.38 ?  381  ALA B N     1 
ATOM   11994 C CA    . ALA B 1 383  ? -2.220  23.379  89.172  1.00 10.87 ?  381  ALA B CA    1 
ATOM   11995 C C     . ALA B 1 383  ? -2.164  24.427  88.069  1.00 11.78 ?  381  ALA B C     1 
ATOM   11996 O O     . ALA B 1 383  ? -1.696  24.146  86.959  1.00 11.46 ?  381  ALA B O     1 
ATOM   11997 C CB    . ALA B 1 383  ? -3.602  22.732  89.243  1.00 11.85 ?  381  ALA B CB    1 
ATOM   11998 N N     . GLN B 1 384  ? -2.615  25.647  88.361  1.00 11.42 ?  382  GLN B N     1 
ATOM   11999 C CA    . GLN B 1 384  ? -2.528  26.729  87.386  1.00 10.28 ?  382  GLN B CA    1 
ATOM   12000 C C     . GLN B 1 384  ? -1.080  27.085  87.078  1.00 11.68 ?  382  GLN B C     1 
ATOM   12001 O O     . GLN B 1 384  ? -0.715  27.235  85.904  1.00 13.09 ?  382  GLN B O     1 
ATOM   12002 C CB    . GLN B 1 384  ? -3.290  27.958  87.884  1.00 11.74 ?  382  GLN B CB    1 
ATOM   12003 C CG    . GLN B 1 384  ? -4.816  27.777  87.885  1.00 11.14 ?  382  GLN B CG    1 
ATOM   12004 C CD    . GLN B 1 384  ? -5.544  29.038  88.266  1.00 11.21 ?  382  GLN B CD    1 
ATOM   12005 O OE1   . GLN B 1 384  ? -4.962  29.929  88.875  1.00 14.47 ?  382  GLN B OE1   1 
ATOM   12006 N NE2   . GLN B 1 384  ? -6.833  29.109  87.935  1.00 11.14 ?  382  GLN B NE2   1 
ATOM   12007 N N     . LEU B 1 385  ? -0.243  27.238  88.112  1.00 10.73 ?  383  LEU B N     1 
ATOM   12008 C CA    . LEU B 1 385  ? 1.166   27.570  87.883  1.00 9.88  ?  383  LEU B CA    1 
ATOM   12009 C C     . LEU B 1 385  ? 1.853   26.519  87.030  1.00 11.50 ?  383  LEU B C     1 
ATOM   12010 O O     . LEU B 1 385  ? 2.679   26.853  86.165  1.00 13.37 ?  383  LEU B O     1 
ATOM   12011 C CB    . LEU B 1 385  ? 1.921   27.705  89.205  1.00 11.85 ?  383  LEU B CB    1 
ATOM   12012 C CG    . LEU B 1 385  ? 1.596   28.936  90.038  1.00 15.15 ?  383  LEU B CG    1 
ATOM   12013 C CD1   . LEU B 1 385  ? 2.317   28.828  91.355  1.00 15.79 ?  383  LEU B CD1   1 
ATOM   12014 C CD2   . LEU B 1 385  ? 2.039   30.183  89.297  1.00 18.97 ?  383  LEU B CD2   1 
ATOM   12015 N N     . ASP B 1 386  ? 1.524   25.250  87.250  1.00 12.10 ?  384  ASP B N     1 
ATOM   12016 C CA    . ASP B 1 386  ? 2.223   24.153  86.588  1.00 11.55 ?  384  ASP B CA    1 
ATOM   12017 C C     . ASP B 1 386  ? 1.613   23.787  85.243  1.00 13.73 ?  384  ASP B C     1 
ATOM   12018 O O     . ASP B 1 386  ? 2.129   22.889  84.564  1.00 13.76 ?  384  ASP B O     1 
ATOM   12019 C CB    . ASP B 1 386  ? 2.259   22.929  87.512  1.00 13.88 ?  384  ASP B CB    1 
ATOM   12020 C CG    . ASP B 1 386  ? 3.198   23.126  88.708  1.00 18.06 ?  384  ASP B CG    1 
ATOM   12021 O OD1   . ASP B 1 386  ? 3.912   24.159  88.764  1.00 17.98 ?  384  ASP B OD1   1 
ATOM   12022 O OD2   . ASP B 1 386  ? 3.228   22.239  89.595  1.00 19.89 ?  384  ASP B OD2   1 
ATOM   12023 N N     . GLY B 1 387  ? 0.540   24.459  84.834  1.00 11.83 ?  385  GLY B N     1 
ATOM   12024 C CA    . GLY B 1 387  ? -0.043  24.225  83.521  1.00 12.89 ?  385  GLY B CA    1 
ATOM   12025 C C     . GLY B 1 387  ? -0.575  22.822  83.344  1.00 13.45 ?  385  GLY B C     1 
ATOM   12026 O O     . GLY B 1 387  ? -0.470  22.252  82.252  1.00 15.36 ?  385  GLY B O     1 
ATOM   12027 N N     . LEU B 1 388  ? -1.136  22.239  84.396  1.00 12.38 ?  386  LEU B N     1 
ATOM   12028 C CA    . LEU B 1 388  ? -1.516  20.838  84.295  1.00 13.51 ?  386  LEU B CA    1 
ATOM   12029 C C     . LEU B 1 388  ? -2.940  20.684  83.751  1.00 16.39 ?  386  LEU B C     1 
ATOM   12030 O O     . LEU B 1 388  ? -3.683  21.650  83.584  1.00 14.53 ?  386  LEU B O     1 
ATOM   12031 C CB    . LEU B 1 388  ? -1.334  20.155  85.651  1.00 13.61 ?  386  LEU B CB    1 
ATOM   12032 C CG    . LEU B 1 388  ? 0.108   20.208  86.170  1.00 15.15 ?  386  LEU B CG    1 
ATOM   12033 C CD1   . LEU B 1 388  ? 0.267   19.482  87.503  1.00 18.65 ?  386  LEU B CD1   1 
ATOM   12034 C CD2   . LEU B 1 388  ? 1.097   19.624  85.146  1.00 16.73 ?  386  LEU B CD2   1 
ATOM   12035 N N     . ALA B 1 389  ? -3.304  19.435  83.436  1.00 15.30 ?  387  ALA B N     1 
ATOM   12036 C CA    . ALA B 1 389  ? -4.502  19.182  82.639  1.00 17.91 ?  387  ALA B CA    1 
ATOM   12037 C C     . ALA B 1 389  ? -5.767  19.628  83.357  1.00 17.58 ?  387  ALA B C     1 
ATOM   12038 O O     . ALA B 1 389  ? -6.718  20.110  82.730  1.00 19.38 ?  387  ALA B O     1 
ATOM   12039 C CB    . ALA B 1 389  ? -4.591  17.692  82.292  1.00 19.61 ?  387  ALA B CB    1 
ATOM   12040 N N     . ASP B 1 390  ? -5.796  19.471  84.670  1.00 15.44 ?  388  ASP B N     1 
ATOM   12041 C CA    . ASP B 1 390  ? -6.970  19.786  85.466  1.00 15.58 ?  388  ASP B CA    1 
ATOM   12042 C C     . ASP B 1 390  ? -6.480  19.877  86.904  1.00 13.27 ?  388  ASP B C     1 
ATOM   12043 O O     . ASP B 1 390  ? -5.296  19.671  87.186  1.00 14.33 ?  388  ASP B O     1 
ATOM   12044 C CB    . ASP B 1 390  ? -8.061  18.720  85.275  1.00 15.60 ?  388  ASP B CB    1 
ATOM   12045 C CG    . ASP B 1 390  ? -9.476  19.259  85.459  1.00 18.92 ?  388  ASP B CG    1 
ATOM   12046 O OD1   . ASP B 1 390  ? -9.739  19.996  86.435  1.00 16.75 ?  388  ASP B OD1   1 
ATOM   12047 O OD2   . ASP B 1 390  ? -10.339 18.917  84.613  1.00 20.34 ?  388  ASP B OD2   1 
ATOM   12048 N N     . PHE B 1 391  ? -7.397  20.177  87.804  1.00 13.52 ?  389  PHE B N     1 
ATOM   12049 C CA    . PHE B 1 391  ? -7.107  20.198  89.226  1.00 12.82 ?  389  PHE B CA    1 
ATOM   12050 C C     . PHE B 1 391  ? -7.188  18.793  89.815  1.00 11.43 ?  389  PHE B C     1 
ATOM   12051 O O     . PHE B 1 391  ? -7.889  17.928  89.282  1.00 13.69 ?  389  PHE B O     1 
ATOM   12052 C CB    . PHE B 1 391  ? -8.095  21.123  89.930  1.00 14.39 ?  389  PHE B CB    1 
ATOM   12053 C CG    . PHE B 1 391  ? -8.083  22.499  89.355  1.00 11.69 ?  389  PHE B CG    1 
ATOM   12054 C CD1   . PHE B 1 391  ? -7.040  23.361  89.653  1.00 12.18 ?  389  PHE B CD1   1 
ATOM   12055 C CD2   . PHE B 1 391  ? -9.061  22.916  88.465  1.00 12.81 ?  389  PHE B CD2   1 
ATOM   12056 C CE1   . PHE B 1 391  ? -6.980  24.623  89.095  1.00 11.49 ?  389  PHE B CE1   1 
ATOM   12057 C CE2   . PHE B 1 391  ? -9.007  24.186  87.906  1.00 13.47 ?  389  PHE B CE2   1 
ATOM   12058 C CZ    . PHE B 1 391  ? -7.973  25.040  88.219  1.00 11.55 ?  389  PHE B CZ    1 
ATOM   12059 N N     . PRO B 1 392  ? -6.457  18.543  90.902  1.00 12.32 ?  390  PRO B N     1 
ATOM   12060 C CA    . PRO B 1 392  ? -6.576  17.270  91.620  1.00 11.46 ?  390  PRO B CA    1 
ATOM   12061 C C     . PRO B 1 392  ? -7.645  17.299  92.697  1.00 13.35 ?  390  PRO B C     1 
ATOM   12062 O O     . PRO B 1 392  ? -7.799  16.326  93.443  1.00 13.64 ?  390  PRO B O     1 
ATOM   12063 C CB    . PRO B 1 392  ? -5.186  17.124  92.246  1.00 13.91 ?  390  PRO B CB    1 
ATOM   12064 C CG    . PRO B 1 392  ? -4.814  18.568  92.611  1.00 14.16 ?  390  PRO B CG    1 
ATOM   12065 C CD    . PRO B 1 392  ? -5.399  19.407  91.457  1.00 12.66 ?  390  PRO B CD    1 
ATOM   12066 N N     . VAL B 1 393  ? -8.341  18.421  92.799  1.00 12.95 ?  391  VAL B N     1 
ATOM   12067 C CA    . VAL B 1 393  ? -9.438  18.611  93.729  1.00 12.43 ?  391  VAL B CA    1 
ATOM   12068 C C     . VAL B 1 393  ? -10.631 19.138  92.947  1.00 12.40 ?  391  VAL B C     1 
ATOM   12069 O O     . VAL B 1 393  ? -10.494 19.657  91.834  1.00 13.29 ?  391  VAL B O     1 
ATOM   12070 C CB    . VAL B 1 393  ? -9.066  19.580  94.876  1.00 11.99 ?  391  VAL B CB    1 
ATOM   12071 C CG1   . VAL B 1 393  ? -7.925  19.018  95.704  1.00 13.58 ?  391  VAL B CG1   1 
ATOM   12072 C CG2   . VAL B 1 393  ? -8.677  20.946  94.304  1.00 12.64 ?  391  VAL B CG2   1 
ATOM   12073 N N     . PHE B 1 394  ? -11.811 19.018  93.560  1.00 13.04 ?  392  PHE B N     1 
ATOM   12074 C CA    . PHE B 1 394  ? -13.003 19.622  92.981  1.00 13.38 ?  392  PHE B CA    1 
ATOM   12075 C C     . PHE B 1 394  ? -12.917 21.142  93.071  1.00 13.68 ?  392  PHE B C     1 
ATOM   12076 O O     . PHE B 1 394  ? -12.144 21.703  93.852  1.00 15.40 ?  392  PHE B O     1 
ATOM   12077 C CB    . PHE B 1 394  ? -14.244 19.086  93.689  1.00 13.64 ?  392  PHE B CB    1 
ATOM   12078 C CG    . PHE B 1 394  ? -14.381 17.610  93.538  1.00 15.24 ?  392  PHE B CG    1 
ATOM   12079 C CD1   . PHE B 1 394  ? -14.574 17.071  92.265  1.00 14.91 ?  392  PHE B CD1   1 
ATOM   12080 C CD2   . PHE B 1 394  ? -14.240 16.752  94.622  1.00 15.52 ?  392  PHE B CD2   1 
ATOM   12081 C CE1   . PHE B 1 394  ? -14.655 15.719  92.084  1.00 16.09 ?  392  PHE B CE1   1 
ATOM   12082 C CE2   . PHE B 1 394  ? -14.317 15.379  94.441  1.00 15.45 ?  392  PHE B CE2   1 
ATOM   12083 C CZ    . PHE B 1 394  ? -14.538 14.866  93.165  1.00 15.79 ?  392  PHE B CZ    1 
ATOM   12084 N N     . THR B 1 395  ? -13.709 21.815  92.231  1.00 15.20 ?  393  THR B N     1 
ATOM   12085 C CA    . THR B 1 395  ? -13.737 23.273  92.202  1.00 14.26 ?  393  THR B CA    1 
ATOM   12086 C C     . THR B 1 395  ? -15.049 23.867  92.697  1.00 15.58 ?  393  THR B C     1 
ATOM   12087 O O     . THR B 1 395  ? -15.107 25.080  92.897  1.00 16.64 ?  393  THR B O     1 
ATOM   12088 C CB    . THR B 1 395  ? -13.461 23.828  90.789  1.00 15.14 ?  393  THR B CB    1 
ATOM   12089 O OG1   . THR B 1 395  ? -14.434 23.342  89.860  1.00 14.92 ?  393  THR B OG1   1 
ATOM   12090 C CG2   . THR B 1 395  ? -12.055 23.470  90.296  1.00 14.35 ?  393  THR B CG2   1 
ATOM   12091 N N     . ARG B 1 396  ? -16.096 23.065  92.866  1.00 15.05 ?  394  ARG B N     1 
ATOM   12092 C CA    . ARG B 1 396  ? -17.326 23.498  93.518  1.00 16.53 ?  394  ARG B CA    1 
ATOM   12093 C C     . ARG B 1 396  ? -17.440 22.810  94.868  1.00 18.12 ?  394  ARG B C     1 
ATOM   12094 O O     . ARG B 1 396  ? -17.238 21.595  94.970  1.00 17.85 ?  394  ARG B O     1 
ATOM   12095 C CB    . ARG B 1 396  ? -18.553 23.178  92.670  1.00 16.53 ?  394  ARG B CB    1 
ATOM   12096 C CG    . ARG B 1 396  ? -18.559 23.852  91.322  1.00 17.63 ?  394  ARG B CG    1 
ATOM   12097 C CD    . ARG B 1 396  ? -19.919 23.678  90.679  1.00 20.13 ?  394  ARG B CD    1 
ATOM   12098 N NE    . ARG B 1 396  ? -19.907 24.197  89.321  1.00 22.19 ?  394  ARG B NE    1 
ATOM   12099 C CZ    . ARG B 1 396  ? -20.778 25.073  88.836  1.00 24.13 ?  394  ARG B CZ    1 
ATOM   12100 N NH1   . ARG B 1 396  ? -21.787 25.519  89.567  1.00 30.26 ?  394  ARG B NH1   1 
ATOM   12101 N NH2   . ARG B 1 396  ? -20.635 25.506  87.584  1.00 23.03 ?  394  ARG B NH2   1 
ATOM   12102 N N     . LYS B 1 397  ? -17.788 23.587  95.896  1.00 19.38 ?  395  LYS B N     1 
ATOM   12103 C CA    . LYS B 1 397  ? -17.832 23.052  97.250  1.00 18.45 ?  395  LYS B CA    1 
ATOM   12104 C C     . LYS B 1 397  ? -18.849 21.920  97.379  1.00 15.72 ?  395  LYS B C     1 
ATOM   12105 O O     . LYS B 1 397  ? -18.595 20.930  98.075  1.00 17.94 ?  395  LYS B O     1 
ATOM   12106 C CB    . LYS B 1 397  ? -18.130 24.180  98.234  1.00 18.96 ?  395  LYS B CB    1 
ATOM   12107 C CG    . LYS B 1 397  ? -17.780 23.857  99.660  1.00 20.66 ?  395  LYS B CG    1 
ATOM   12108 C CD    . LYS B 1 397  ? -18.979 23.325  100.399 1.00 23.26 ?  395  LYS B CD    1 
ATOM   12109 C CE    . LYS B 1 397  ? -18.632 23.040  101.845 1.00 23.42 ?  395  LYS B CE    1 
ATOM   12110 N NZ    . LYS B 1 397  ? -19.829 22.490  102.541 1.00 21.99 ?  395  LYS B NZ    1 
ATOM   12111 N N     . ILE B 1 398  ? -19.995 22.021  96.694  1.00 16.86 ?  396  ILE B N     1 
ATOM   12112 C CA    . ILE B 1 398  ? -20.974 20.936  96.781  1.00 19.96 ?  396  ILE B CA    1 
ATOM   12113 C C     . ILE B 1 398  ? -20.446 19.637  96.183  1.00 17.80 ?  396  ILE B C     1 
ATOM   12114 O O     . ILE B 1 398  ? -20.920 18.556  96.548  1.00 18.64 ?  396  ILE B O     1 
ATOM   12115 C CB    . ILE B 1 398  ? -22.328 21.304  96.122  1.00 25.75 ?  396  ILE B CB    1 
ATOM   12116 C CG1   . ILE B 1 398  ? -22.154 21.681  94.651  1.00 22.78 ?  396  ILE B CG1   1 
ATOM   12117 C CG2   . ILE B 1 398  ? -23.045 22.388  96.921  1.00 32.75 ?  396  ILE B CG2   1 
ATOM   12118 C CD1   . ILE B 1 398  ? -23.473 22.039  93.957  1.00 34.02 ?  396  ILE B CD1   1 
ATOM   12119 N N     . HIS B 1 399  ? -19.479 19.706  95.259  1.00 19.44 ?  397  HIS B N     1 
ATOM   12120 C CA    . HIS B 1 399  ? -18.901 18.469  94.743  1.00 19.09 ?  397  HIS B CA    1 
ATOM   12121 C C     . HIS B 1 399  ? -18.125 17.739  95.827  1.00 17.34 ?  397  HIS B C     1 
ATOM   12122 O O     . HIS B 1 399  ? -18.200 16.510  95.937  1.00 17.59 ?  397  HIS B O     1 
ATOM   12123 C CB    . HIS B 1 399  ? -18.003 18.771  93.550  1.00 15.57 ?  397  HIS B CB    1 
ATOM   12124 C CG    . HIS B 1 399  ? -18.750 19.276  92.355  1.00 16.07 ?  397  HIS B CG    1 
ATOM   12125 N ND1   . HIS B 1 399  ? -18.118 19.835  91.266  1.00 17.62 ?  397  HIS B ND1   1 
ATOM   12126 C CD2   . HIS B 1 399  ? -20.075 19.298  92.076  1.00 20.85 ?  397  HIS B CD2   1 
ATOM   12127 C CE1   . HIS B 1 399  ? -19.023 20.185  90.368  1.00 19.46 ?  397  HIS B CE1   1 
ATOM   12128 N NE2   . HIS B 1 399  ? -20.217 19.871  90.834  1.00 21.42 ?  397  HIS B NE2   1 
ATOM   12129 N N     . THR B 1 400  ? -17.363 18.485  96.629  1.00 16.46 ?  398  THR B N     1 
ATOM   12130 C CA    . THR B 1 400  ? -16.676 17.885  97.766  1.00 16.97 ?  398  THR B CA    1 
ATOM   12131 C C     . THR B 1 400  ? -17.664 17.265  98.741  1.00 15.33 ?  398  THR B C     1 
ATOM   12132 O O     . THR B 1 400  ? -17.424 16.174  99.270  1.00 16.78 ?  398  THR B O     1 
ATOM   12133 C CB    . THR B 1 400  ? -15.813 18.946  98.448  1.00 16.35 ?  398  THR B CB    1 
ATOM   12134 O OG1   . THR B 1 400  ? -14.764 19.341  97.544  1.00 14.88 ?  398  THR B OG1   1 
ATOM   12135 C CG2   . THR B 1 400  ? -15.201 18.400  99.727  1.00 15.37 ?  398  THR B CG2   1 
ATOM   12136 N N     . ASP B 1 401  ? -18.793 17.930  98.973  1.00 17.92 ?  399  ASP B N     1 
ATOM   12137 C CA    . ASP B 1 401  ? -19.789 17.376  99.885  1.00 17.02 ?  399  ASP B CA    1 
ATOM   12138 C C     . ASP B 1 401  ? -20.354 16.061  99.353  1.00 16.65 ?  399  ASP B C     1 
ATOM   12139 O O     . ASP B 1 401  ? -20.536 15.104  100.112 1.00 19.25 ?  399  ASP B O     1 
ATOM   12140 C CB    . ASP B 1 401  ? -20.914 18.385  100.114 1.00 20.16 ?  399  ASP B CB    1 
ATOM   12141 C CG    . ASP B 1 401  ? -20.473 19.590  100.926 1.00 24.91 ?  399  ASP B CG    1 
ATOM   12142 O OD1   . ASP B 1 401  ? -19.502 19.473  101.710 1.00 21.15 ?  399  ASP B OD1   1 
ATOM   12143 O OD2   . ASP B 1 401  ? -21.095 20.664  100.773 1.00 23.02 ?  399  ASP B OD2   1 
ATOM   12144 N N     . VAL B 1 402  ? -20.630 15.992  98.045  1.00 20.10 ?  400  VAL B N     1 
ATOM   12145 C CA    . VAL B 1 402  ? -21.141 14.753  97.466  1.00 20.10 ?  400  VAL B CA    1 
ATOM   12146 C C     . VAL B 1 402  ? -20.084 13.662  97.544  1.00 18.75 ?  400  VAL B C     1 
ATOM   12147 O O     . VAL B 1 402  ? -20.375 12.522  97.934  1.00 19.63 ?  400  VAL B O     1 
ATOM   12148 C CB    . VAL B 1 402  ? -21.610 14.995  96.018  1.00 21.18 ?  400  VAL B CB    1 
ATOM   12149 C CG1   . VAL B 1 402  ? -21.987 13.679  95.332  1.00 22.56 ?  400  VAL B CG1   1 
ATOM   12150 C CG2   . VAL B 1 402  ? -22.775 15.968  96.007  1.00 24.59 ?  400  VAL B CG2   1 
ATOM   12151 N N     . SER B 1 403  ? -18.838 14.000  97.183  1.00 17.51 ?  401  SER B N     1 
ATOM   12152 C CA    . SER B 1 403  ? -17.725 13.062  97.309  1.00 18.95 ?  401  SER B CA    1 
ATOM   12153 C C     . SER B 1 403  ? -17.628 12.489  98.722  1.00 17.07 ?  401  SER B C     1 
ATOM   12154 O O     . SER B 1 403  ? -17.473 11.275  98.900  1.00 18.48 ?  401  SER B O     1 
ATOM   12155 C CB    . SER B 1 403  ? -16.423 13.772  96.918  1.00 15.63 ?  401  SER B CB    1 
ATOM   12156 O OG    . SER B 1 403  ? -15.295 12.939  97.105  1.00 18.69 ?  401  SER B OG    1 
ATOM   12157 N N     . TYR B 1 404  ? -17.750 13.348  99.737  1.00 19.34 ?  402  TYR B N     1 
ATOM   12158 C CA    . TYR B 1 404  ? -17.674 12.896  101.124 1.00 18.85 ?  402  TYR B CA    1 
ATOM   12159 C C     . TYR B 1 404  ? -18.756 11.866  101.436 1.00 20.88 ?  402  TYR B C     1 
ATOM   12160 O O     . TYR B 1 404  ? -18.480 10.818  102.027 1.00 19.71 ?  402  TYR B O     1 
ATOM   12161 C CB    . TYR B 1 404  ? -17.792 14.103  102.055 1.00 17.55 ?  402  TYR B CB    1 
ATOM   12162 C CG    . TYR B 1 404  ? -17.399 13.859  103.499 1.00 17.98 ?  402  TYR B CG    1 
ATOM   12163 C CD1   . TYR B 1 404  ? -18.282 13.277  104.398 1.00 19.62 ?  402  TYR B CD1   1 
ATOM   12164 C CD2   . TYR B 1 404  ? -16.158 14.248  103.967 1.00 18.47 ?  402  TYR B CD2   1 
ATOM   12165 C CE1   . TYR B 1 404  ? -17.932 13.073  105.718 1.00 20.57 ?  402  TYR B CE1   1 
ATOM   12166 C CE2   . TYR B 1 404  ? -15.799 14.046  105.296 1.00 18.19 ?  402  TYR B CE2   1 
ATOM   12167 C CZ    . TYR B 1 404  ? -16.699 13.461  106.162 1.00 19.96 ?  402  TYR B CZ    1 
ATOM   12168 O OH    . TYR B 1 404  ? -16.370 13.242  107.486 1.00 21.38 ?  402  TYR B OH    1 
ATOM   12169 N N     . ILE B 1 405  ? -19.997 12.144  101.029 1.00 20.29 ?  403  ILE B N     1 
ATOM   12170 C CA    . ILE B 1 405  ? -21.104 11.248  101.342 1.00 21.56 ?  403  ILE B CA    1 
ATOM   12171 C C     . ILE B 1 405  ? -20.941 9.923   100.606 1.00 21.25 ?  403  ILE B C     1 
ATOM   12172 O O     . ILE B 1 405  ? -21.158 8.850   101.183 1.00 22.00 ?  403  ILE B O     1 
ATOM   12173 C CB    . ILE B 1 405  ? -22.440 11.946  101.026 1.00 21.72 ?  403  ILE B CB    1 
ATOM   12174 C CG1   . ILE B 1 405  ? -22.608 13.166  101.937 1.00 26.99 ?  403  ILE B CG1   1 
ATOM   12175 C CG2   . ILE B 1 405  ? -23.604 11.017  101.255 1.00 22.02 ?  403  ILE B CG2   1 
ATOM   12176 C CD1   . ILE B 1 405  ? -23.801 14.040  101.605 1.00 32.76 ?  403  ILE B CD1   1 
ATOM   12177 N N     . ALA B 1 406  ? -20.507 9.978   99.341  1.00 20.05 ?  404  ALA B N     1 
ATOM   12178 C CA    . ALA B 1 406  ? -20.248 8.761   98.576  1.00 22.14 ?  404  ALA B CA    1 
ATOM   12179 C C     . ALA B 1 406  ? -19.150 7.918   99.213  1.00 20.17 ?  404  ALA B C     1 
ATOM   12180 O O     . ALA B 1 406  ? -19.257 6.686   99.284  1.00 22.15 ?  404  ALA B O     1 
ATOM   12181 C CB    . ALA B 1 406  ? -19.867 9.125   97.138  1.00 21.40 ?  404  ALA B CB    1 
ATOM   12182 N N     . CYS B 1 407  ? -18.078 8.566   99.675  1.00 19.39 ?  405  CYS B N     1 
ATOM   12183 C CA    . CYS B 1 407  ? -16.978 7.838   100.294 1.00 23.23 ?  405  CYS B CA    1 
ATOM   12184 C C     . CYS B 1 407  ? -17.369 7.298   101.665 1.00 19.58 ?  405  CYS B C     1 
ATOM   12185 O O     . CYS B 1 407  ? -16.907 6.223   102.070 1.00 22.19 ?  405  CYS B O     1 
ATOM   12186 C CB    . CYS B 1 407  ? -15.763 8.753   100.382 1.00 21.75 ?  405  CYS B CB    1 
ATOM   12187 S SG    . CYS B 1 407  ? -15.026 9.047   98.747  1.00 25.32 ?  405  CYS B SG    1 
ATOM   12188 N N     . ALA B 1 408  ? -18.239 8.010   102.375 1.00 20.44 ?  406  ALA B N     1 
ATOM   12189 C CA    . ALA B 1 408  ? -18.805 7.474   103.608 1.00 20.34 ?  406  ALA B CA    1 
ATOM   12190 C C     . ALA B 1 408  ? -19.597 6.192   103.351 1.00 21.62 ?  406  ALA B C     1 
ATOM   12191 O O     . ALA B 1 408  ? -19.518 5.239   104.135 1.00 24.43 ?  406  ALA B O     1 
ATOM   12192 C CB    . ALA B 1 408  ? -19.684 8.531   104.274 1.00 23.70 ?  406  ALA B CB    1 
ATOM   12193 N N     . ALA B 1 409  ? -20.347 6.136   102.244 1.00 24.36 ?  407  ALA B N     1 
ATOM   12194 C CA    . ALA B 1 409  ? -21.096 4.919   101.944 1.00 25.38 ?  407  ALA B CA    1 
ATOM   12195 C C     . ALA B 1 409  ? -20.156 3.740   101.723 1.00 24.50 ?  407  ALA B C     1 
ATOM   12196 O O     . ALA B 1 409  ? -20.407 2.631   102.215 1.00 27.96 ?  407  ALA B O     1 
ATOM   12197 C CB    . ALA B 1 409  ? -21.991 5.138   100.725 1.00 23.80 ?  407  ALA B CB    1 
ATOM   12198 N N     . LYS B 1 410  ? -19.055 3.973   101.006 1.00 20.88 ?  408  LYS B N     1 
ATOM   12199 C CA    . LYS B 1 410  ? -18.049 2.936   100.802 1.00 25.42 ?  408  LYS B CA    1 
ATOM   12200 C C     . LYS B 1 410  ? -17.458 2.468   102.131 1.00 26.00 ?  408  LYS B C     1 
ATOM   12201 O O     . LYS B 1 410  ? -17.321 1.262   102.375 1.00 25.08 ?  408  LYS B O     1 
ATOM   12202 C CB    . LYS B 1 410  ? -16.963 3.468   99.865  1.00 25.06 ?  408  LYS B CB    1 
ATOM   12203 C CG    . LYS B 1 410  ? -15.899 2.459   99.474  1.00 25.85 ?  408  LYS B CG    1 
ATOM   12204 C CD    . LYS B 1 410  ? -14.843 3.084   98.577  1.00 27.21 ?  408  LYS B CD    1 
ATOM   12205 C CE    . LYS B 1 410  ? -15.400 3.521   97.223  1.00 28.45 ?  408  LYS B CE    1 
ATOM   12206 N NZ    . LYS B 1 410  ? -15.610 2.379   96.270  1.00 29.62 ?  408  LYS B NZ    1 
ATOM   12207 N N     . LEU B 1 411  ? -17.115 3.410   103.015 1.00 25.15 ?  409  LEU B N     1 
ATOM   12208 C CA    . LEU B 1 411  ? -16.476 3.040   104.274 1.00 24.42 ?  409  LEU B CA    1 
ATOM   12209 C C     . LEU B 1 411  ? -17.421 2.249   105.167 1.00 24.17 ?  409  LEU B C     1 
ATOM   12210 O O     . LEU B 1 411  ? -17.014 1.263   105.795 1.00 25.37 ?  409  LEU B O     1 
ATOM   12211 C CB    . LEU B 1 411  ? -15.979 4.290   104.999 1.00 22.75 ?  409  LEU B CB    1 
ATOM   12212 C CG    . LEU B 1 411  ? -14.657 4.838   104.465 1.00 23.64 ?  409  LEU B CG    1 
ATOM   12213 C CD1   . LEU B 1 411  ? -14.447 6.268   104.915 1.00 24.31 ?  409  LEU B CD1   1 
ATOM   12214 C CD2   . LEU B 1 411  ? -13.506 3.958   104.917 1.00 26.00 ?  409  LEU B CD2   1 
ATOM   12215 N N     . LEU B 1 412  ? -18.690 2.659   105.228 1.00 25.61 ?  410  LEU B N     1 
ATOM   12216 C CA    . LEU B 1 412  ? -19.656 1.991   106.090 1.00 27.47 ?  410  LEU B CA    1 
ATOM   12217 C C     . LEU B 1 412  ? -19.983 0.577   105.628 1.00 29.80 ?  410  LEU B C     1 
ATOM   12218 O O     . LEU B 1 412  ? -20.497 -0.212  106.427 1.00 30.60 ?  410  LEU B O     1 
ATOM   12219 C CB    . LEU B 1 412  ? -20.927 2.836   106.191 1.00 26.90 ?  410  LEU B CB    1 
ATOM   12220 C CG    . LEU B 1 412  ? -20.745 4.077   107.076 1.00 28.04 ?  410  LEU B CG    1 
ATOM   12221 C CD1   . LEU B 1 412  ? -21.868 5.092   106.888 1.00 32.48 ?  410  LEU B CD1   1 
ATOM   12222 C CD2   . LEU B 1 412  ? -20.622 3.669   108.539 1.00 28.55 ?  410  LEU B CD2   1 
ATOM   12223 N N     . ALA B 1 413  ? -19.692 0.234   104.377 1.00 28.95 ?  411  ALA B N     1 
ATOM   12224 C CA    . ALA B 1 413  ? -19.862 -1.131  103.895 1.00 30.35 ?  411  ALA B CA    1 
ATOM   12225 C C     . ALA B 1 413  ? -18.656 -2.016  104.187 1.00 31.24 ?  411  ALA B C     1 
ATOM   12226 O O     . ALA B 1 413  ? -18.677 -3.199  103.833 1.00 32.81 ?  411  ALA B O     1 
ATOM   12227 C CB    . ALA B 1 413  ? -20.146 -1.131  102.384 1.00 26.78 ?  411  ALA B CB    1 
ATOM   12228 N N     . ALA B 1 414  ? -17.611 -1.483  104.832 1.00 27.51 ?  412  ALA B N     1 
ATOM   12229 C CA    . ALA B 1 414  ? -16.367 -2.222  105.025 1.00 27.58 ?  412  ALA B CA    1 
ATOM   12230 C C     . ALA B 1 414  ? -15.893 -2.163  106.475 1.00 28.73 ?  412  ALA B C     1 
ATOM   12231 O O     . ALA B 1 414  ? -14.693 -2.257  106.739 1.00 27.98 ?  412  ALA B O     1 
ATOM   12232 C CB    . ALA B 1 414  ? -15.273 -1.702  104.091 1.00 29.04 ?  412  ALA B CB    1 
ATOM   12233 N N     . THR B 1 415  ? -16.819 -2.039  107.428 1.00 29.29 ?  413  THR B N     1 
ATOM   12234 C CA    . THR B 1 415  ? -16.432 -1.817  108.818 1.00 27.06 ?  413  THR B CA    1 
ATOM   12235 C C     . THR B 1 415  ? -15.775 -3.026  109.473 1.00 30.31 ?  413  THR B C     1 
ATOM   12236 O O     . THR B 1 415  ? -15.222 -2.878  110.567 1.00 30.70 ?  413  THR B O     1 
ATOM   12237 C CB    . THR B 1 415  ? -17.639 -1.371  109.646 1.00 29.22 ?  413  THR B CB    1 
ATOM   12238 O OG1   . THR B 1 415  ? -18.694 -2.336  109.527 1.00 33.80 ?  413  THR B OG1   1 
ATOM   12239 C CG2   . THR B 1 415  ? -18.125 -0.009  109.158 1.00 26.69 ?  413  THR B CG2   1 
ATOM   12240 N N     . ASP B 1 416  ? -15.819 -4.208  108.851 1.00 27.41 ?  414  ASP B N     1 
ATOM   12241 C CA    . ASP B 1 416  ? -15.046 -5.331  109.368 1.00 27.10 ?  414  ASP B CA    1 
ATOM   12242 C C     . ASP B 1 416  ? -13.552 -5.047  109.294 1.00 31.93 ?  414  ASP B C     1 
ATOM   12243 O O     . ASP B 1 416  ? -12.796 -5.383  110.218 1.00 34.83 ?  414  ASP B O     1 
ATOM   12244 C CB    . ASP B 1 416  ? -15.379 -6.609  108.591 1.00 34.98 ?  414  ASP B CB    1 
ATOM   12245 C CG    . ASP B 1 416  ? -16.626 -7.312  109.109 1.00 41.95 ?  414  ASP B CG    1 
ATOM   12246 O OD1   . ASP B 1 416  ? -17.220 -6.846  110.106 1.00 43.38 ?  414  ASP B OD1   1 
ATOM   12247 O OD2   . ASP B 1 416  ? -17.007 -8.344  108.512 1.00 45.99 ?  414  ASP B OD2   1 
ATOM   12248 N N     . VAL B 1 417  ? -13.105 -4.408  108.213 1.00 28.37 ?  415  VAL B N     1 
ATOM   12249 C CA    . VAL B 1 417  ? -11.677 -4.216  107.983 1.00 29.62 ?  415  VAL B CA    1 
ATOM   12250 C C     . VAL B 1 417  ? -11.222 -2.766  108.103 1.00 25.00 ?  415  VAL B C     1 
ATOM   12251 O O     . VAL B 1 417  ? -10.004 -2.527  108.128 1.00 31.62 ?  415  VAL B O     1 
ATOM   12252 C CB    . VAL B 1 417  ? -11.246 -4.797  106.620 1.00 29.25 ?  415  VAL B CB    1 
ATOM   12253 C CG1   . VAL B 1 417  ? -11.497 -6.308  106.598 1.00 31.26 ?  415  VAL B CG1   1 
ATOM   12254 C CG2   . VAL B 1 417  ? -11.985 -4.110  105.492 1.00 26.58 ?  415  VAL B CG2   1 
ATOM   12255 N N     . VAL B 1 418  ? -12.128 -1.791  108.174 1.00 25.60 ?  416  VAL B N     1 
ATOM   12256 C CA    . VAL B 1 418  ? -11.714 -0.414  108.436 1.00 25.53 ?  416  VAL B CA    1 
ATOM   12257 C C     . VAL B 1 418  ? -12.609 0.205   109.499 1.00 24.97 ?  416  VAL B C     1 
ATOM   12258 O O     . VAL B 1 418  ? -13.766 -0.188  109.682 1.00 26.66 ?  416  VAL B O     1 
ATOM   12259 C CB    . VAL B 1 418  ? -11.694 0.493   107.173 1.00 21.74 ?  416  VAL B CB    1 
ATOM   12260 C CG1   . VAL B 1 418  ? -10.639 0.030   106.175 1.00 24.03 ?  416  VAL B CG1   1 
ATOM   12261 C CG2   . VAL B 1 418  ? -13.069 0.575   106.508 1.00 24.97 ?  416  VAL B CG2   1 
ATOM   12262 N N     . PHE B 1 419  ? -12.055 1.186   110.212 1.00 21.64 ?  417  PHE B N     1 
ATOM   12263 C CA    . PHE B 1 419  ? -12.783 1.924   111.238 1.00 21.97 ?  417  PHE B CA    1 
ATOM   12264 C C     . PHE B 1 419  ? -13.027 3.334   110.722 1.00 22.99 ?  417  PHE B C     1 
ATOM   12265 O O     . PHE B 1 419  ? -12.100 4.165   110.718 1.00 21.01 ?  417  PHE B O     1 
ATOM   12266 C CB    . PHE B 1 419  ? -11.989 1.952   112.546 1.00 21.93 ?  417  PHE B CB    1 
ATOM   12267 C CG    . PHE B 1 419  ? -12.619 2.780   113.622 1.00 25.54 ?  417  PHE B CG    1 
ATOM   12268 C CD1   . PHE B 1 419  ? -13.874 2.468   114.112 1.00 24.79 ?  417  PHE B CD1   1 
ATOM   12269 C CD2   . PHE B 1 419  ? -11.940 3.852   114.171 1.00 23.83 ?  417  PHE B CD2   1 
ATOM   12270 C CE1   . PHE B 1 419  ? -14.452 3.221   115.117 1.00 26.32 ?  417  PHE B CE1   1 
ATOM   12271 C CE2   . PHE B 1 419  ? -12.508 4.609   115.191 1.00 24.80 ?  417  PHE B CE2   1 
ATOM   12272 C CZ    . PHE B 1 419  ? -13.766 4.297   115.661 1.00 23.25 ?  417  PHE B CZ    1 
ATOM   12273 N N     . PRO B 1 420  ? -14.224 3.650   110.238 1.00 20.81 ?  418  PRO B N     1 
ATOM   12274 C CA    . PRO B 1 420  ? -14.433 4.964   109.626 1.00 20.55 ?  418  PRO B CA    1 
ATOM   12275 C C     . PRO B 1 420  ? -14.528 6.059   110.674 1.00 21.81 ?  418  PRO B C     1 
ATOM   12276 O O     . PRO B 1 420  ? -15.202 5.919   111.694 1.00 20.69 ?  418  PRO B O     1 
ATOM   12277 C CB    . PRO B 1 420  ? -15.751 4.799   108.854 1.00 23.57 ?  418  PRO B CB    1 
ATOM   12278 C CG    . PRO B 1 420  ? -15.973 3.307   108.765 1.00 24.62 ?  418  PRO B CG    1 
ATOM   12279 C CD    . PRO B 1 420  ? -15.383 2.766   110.043 1.00 21.47 ?  418  PRO B CD    1 
ATOM   12280 N N     . GLN B 1 421  ? -13.831 7.162   110.416 1.00 22.66 ?  419  GLN B N     1 
ATOM   12281 C CA    . GLN B 1 421  ? -13.816 8.300   111.328 1.00 21.75 ?  419  GLN B CA    1 
ATOM   12282 C C     . GLN B 1 421  ? -14.217 9.524   110.522 1.00 22.82 ?  419  GLN B C     1 
ATOM   12283 O O     . GLN B 1 421  ? -13.450 9.993   109.676 1.00 19.72 ?  419  GLN B O     1 
ATOM   12284 C CB    . GLN B 1 421  ? -12.438 8.479   111.971 1.00 20.94 ?  419  GLN B CB    1 
ATOM   12285 C CG    . GLN B 1 421  ? -11.921 7.207   112.609 1.00 20.32 ?  419  GLN B CG    1 
ATOM   12286 C CD    . GLN B 1 421  ? -10.432 7.253   112.868 1.00 19.10 ?  419  GLN B CD    1 
ATOM   12287 O OE1   . GLN B 1 421  ? -9.628  7.337   111.937 1.00 19.49 ?  419  GLN B OE1   1 
ATOM   12288 N NE2   . GLN B 1 421  ? -10.055 7.202   114.137 1.00 19.51 ?  419  GLN B NE2   1 
ATOM   12289 N N     . PHE B 1 422  ? -15.412 10.038  110.775 1.00 21.16 ?  420  PHE B N     1 
ATOM   12290 C CA    . PHE B 1 422  ? -15.998 11.072  109.927 1.00 21.07 ?  420  PHE B CA    1 
ATOM   12291 C C     . PHE B 1 422  ? -15.721 12.440  110.543 1.00 18.29 ?  420  PHE B C     1 
ATOM   12292 O O     . PHE B 1 422  ? -16.447 12.902  111.426 1.00 20.99 ?  420  PHE B O     1 
ATOM   12293 C CB    . PHE B 1 422  ? -17.486 10.809  109.725 1.00 20.97 ?  420  PHE B CB    1 
ATOM   12294 C CG    . PHE B 1 422  ? -17.765 9.500   109.042 1.00 23.69 ?  420  PHE B CG    1 
ATOM   12295 C CD1   . PHE B 1 422  ? -17.325 9.277   107.745 1.00 24.18 ?  420  PHE B CD1   1 
ATOM   12296 C CD2   . PHE B 1 422  ? -18.447 8.490   109.694 1.00 24.38 ?  420  PHE B CD2   1 
ATOM   12297 C CE1   . PHE B 1 422  ? -17.567 8.068   107.116 1.00 23.39 ?  420  PHE B CE1   1 
ATOM   12298 C CE2   . PHE B 1 422  ? -18.693 7.272   109.064 1.00 23.46 ?  420  PHE B CE2   1 
ATOM   12299 C CZ    . PHE B 1 422  ? -18.255 7.068   107.773 1.00 24.01 ?  420  PHE B CZ    1 
ATOM   12300 N N     . ALA B 1 423  ? -14.662 13.086  110.069 1.00 18.59 ?  421  ALA B N     1 
ATOM   12301 C CA    . ALA B 1 423  ? -14.245 14.394  110.559 1.00 17.77 ?  421  ALA B CA    1 
ATOM   12302 C C     . ALA B 1 423  ? -14.995 15.483  109.807 1.00 18.27 ?  421  ALA B C     1 
ATOM   12303 O O     . ALA B 1 423  ? -14.729 15.715  108.623 1.00 20.53 ?  421  ALA B O     1 
ATOM   12304 C CB    . ALA B 1 423  ? -12.741 14.570  110.365 1.00 18.71 ?  421  ALA B CB    1 
ATOM   12305 N N     . THR B 1 424  ? -15.915 16.163  110.485 1.00 20.71 ?  422  THR B N     1 
ATOM   12306 C CA    . THR B 1 424  ? -16.617 17.265  109.840 1.00 19.46 ?  422  THR B CA    1 
ATOM   12307 C C     . THR B 1 424  ? -17.322 18.112  110.886 1.00 20.01 ?  422  THR B C     1 
ATOM   12308 O O     . THR B 1 424  ? -17.777 17.607  111.915 1.00 21.99 ?  422  THR B O     1 
ATOM   12309 C CB    . THR B 1 424  ? -17.646 16.764  108.812 1.00 22.01 ?  422  THR B CB    1 
ATOM   12310 O OG1   . THR B 1 424  ? -18.266 17.888  108.173 1.00 22.07 ?  422  THR B OG1   1 
ATOM   12311 C CG2   . THR B 1 424  ? -18.724 15.925  109.492 1.00 22.56 ?  422  THR B CG2   1 
ATOM   12312 N N     . HIS B 1 425  ? -17.419 19.408  110.599 1.00 21.00 ?  423  HIS B N     1 
ATOM   12313 C CA    . HIS B 1 425  ? -18.209 20.320  111.419 1.00 20.45 ?  423  HIS B CA    1 
ATOM   12314 C C     . HIS B 1 425  ? -19.551 20.647  110.784 1.00 19.54 ?  423  HIS B C     1 
ATOM   12315 O O     . HIS B 1 425  ? -20.296 21.476  111.317 1.00 22.89 ?  423  HIS B O     1 
ATOM   12316 C CB    . HIS B 1 425  ? -17.420 21.604  111.675 1.00 17.59 ?  423  HIS B CB    1 
ATOM   12317 C CG    . HIS B 1 425  ? -16.135 21.363  112.398 1.00 19.39 ?  423  HIS B CG    1 
ATOM   12318 N ND1   . HIS B 1 425  ? -14.934 21.894  111.980 1.00 19.56 ?  423  HIS B ND1   1 
ATOM   12319 C CD2   . HIS B 1 425  ? -15.860 20.623  113.498 1.00 23.38 ?  423  HIS B CD2   1 
ATOM   12320 C CE1   . HIS B 1 425  ? -13.976 21.503  112.805 1.00 23.47 ?  423  HIS B CE1   1 
ATOM   12321 N NE2   . HIS B 1 425  ? -14.511 20.731  113.731 1.00 21.61 ?  423  HIS B NE2   1 
ATOM   12322 N N     . ASN B 1 426  ? -19.872 20.001  109.663 1.00 21.71 ?  424  ASN B N     1 
ATOM   12323 C CA    . ASN B 1 426  ? -21.063 20.294  108.876 1.00 21.72 ?  424  ASN B CA    1 
ATOM   12324 C C     . ASN B 1 426  ? -22.201 19.399  109.358 1.00 20.28 ?  424  ASN B C     1 
ATOM   12325 O O     . ASN B 1 426  ? -22.147 18.175  109.202 1.00 23.21 ?  424  ASN B O     1 
ATOM   12326 C CB    . ASN B 1 426  ? -20.763 20.069  107.395 1.00 20.41 ?  424  ASN B CB    1 
ATOM   12327 C CG    . ASN B 1 426  ? -21.909 20.471  106.489 1.00 21.16 ?  424  ASN B CG    1 
ATOM   12328 O OD1   . ASN B 1 426  ? -23.079 20.178  106.764 1.00 22.64 ?  424  ASN B OD1   1 
ATOM   12329 N ND2   . ASN B 1 426  ? -21.577 21.159  105.397 1.00 24.13 ?  424  ASN B ND2   1 
ATOM   12330 N N     . ALA B 1 427  ? -23.232 20.014  109.952 1.00 23.22 ?  425  ALA B N     1 
ATOM   12331 C CA    . ALA B 1 427  ? -24.333 19.249  110.533 1.00 25.14 ?  425  ALA B CA    1 
ATOM   12332 C C     . ALA B 1 427  ? -25.143 18.512  109.476 1.00 24.71 ?  425  ALA B C     1 
ATOM   12333 O O     . ALA B 1 427  ? -25.687 17.436  109.757 1.00 24.22 ?  425  ALA B O     1 
ATOM   12334 C CB    . ALA B 1 427  ? -25.243 20.172  111.342 1.00 27.95 ?  425  ALA B CB    1 
ATOM   12335 N N     . GLN B 1 428  ? -25.248 19.076  108.271 1.00 25.37 ?  426  GLN B N     1 
ATOM   12336 C CA    . GLN B 1 428  ? -25.939 18.380  107.189 1.00 24.52 ?  426  GLN B CA    1 
ATOM   12337 C C     . GLN B 1 428  ? -25.169 17.129  106.782 1.00 25.82 ?  426  GLN B C     1 
ATOM   12338 O O     . GLN B 1 428  ? -25.755 16.048  106.634 1.00 25.03 ?  426  GLN B O     1 
ATOM   12339 C CB    . GLN B 1 428  ? -26.141 19.330  106.007 1.00 25.97 ?  426  GLN B CB    1 
ATOM   12340 C CG    . GLN B 1 428  ? -27.148 18.872  104.962 1.00 28.57 ?  426  GLN B CG    1 
ATOM   12341 C CD    . GLN B 1 428  ? -26.609 17.776  104.066 1.00 28.25 ?  426  GLN B CD    1 
ATOM   12342 O OE1   . GLN B 1 428  ? -25.414 17.737  103.767 1.00 29.31 ?  426  GLN B OE1   1 
ATOM   12343 N NE2   . GLN B 1 428  ? -27.489 16.871  103.639 1.00 31.07 ?  426  GLN B NE2   1 
ATOM   12344 N N     . THR B 1 429  ? -23.844 17.254  106.638 1.00 24.63 ?  427  THR B N     1 
ATOM   12345 C CA    . THR B 1 429  ? -22.995 16.095  106.370 1.00 25.71 ?  427  THR B CA    1 
ATOM   12346 C C     . THR B 1 429  ? -23.128 15.053  107.473 1.00 23.65 ?  427  THR B C     1 
ATOM   12347 O O     . THR B 1 429  ? -23.308 13.857  107.204 1.00 25.27 ?  427  THR B O     1 
ATOM   12348 C CB    . THR B 1 429  ? -21.530 16.533  106.245 1.00 24.06 ?  427  THR B CB    1 
ATOM   12349 O OG1   . THR B 1 429  ? -21.396 17.518  105.213 1.00 23.00 ?  427  THR B OG1   1 
ATOM   12350 C CG2   . THR B 1 429  ? -20.647 15.347  105.901 1.00 24.89 ?  427  THR B CG2   1 
ATOM   12351 N N     . LEU B 1 430  ? -23.010 15.494  108.729 1.00 24.04 ?  428  LEU B N     1 
ATOM   12352 C CA    . LEU B 1 430  ? -23.112 14.590  109.869 1.00 24.80 ?  428  LEU B CA    1 
ATOM   12353 C C     . LEU B 1 430  ? -24.430 13.822  109.850 1.00 25.55 ?  428  LEU B C     1 
ATOM   12354 O O     . LEU B 1 430  ? -24.450 12.601  110.026 1.00 25.41 ?  428  LEU B O     1 
ATOM   12355 C CB    . LEU B 1 430  ? -22.970 15.396  111.163 1.00 26.02 ?  428  LEU B CB    1 
ATOM   12356 C CG    . LEU B 1 430  ? -22.793 14.766  112.545 1.00 24.06 ?  428  LEU B CG    1 
ATOM   12357 C CD1   . LEU B 1 430  ? -22.442 15.870  113.515 1.00 25.90 ?  428  LEU B CD1   1 
ATOM   12358 C CD2   . LEU B 1 430  ? -24.031 14.018  113.037 1.00 27.37 ?  428  LEU B CD2   1 
ATOM   12359 N N     . ALA B 1 431  ? -25.541 14.526  109.631 1.00 24.70 ?  429  ALA B N     1 
ATOM   12360 C CA    . ALA B 1 431  ? -26.851 13.885  109.704 1.00 28.54 ?  429  ALA B CA    1 
ATOM   12361 C C     . ALA B 1 431  ? -27.025 12.848  108.600 1.00 26.68 ?  429  ALA B C     1 
ATOM   12362 O O     . ALA B 1 431  ? -27.530 11.744  108.848 1.00 29.25 ?  429  ALA B O     1 
ATOM   12363 C CB    . ALA B 1 431  ? -27.949 14.944  109.630 1.00 26.96 ?  429  ALA B CB    1 
ATOM   12364 N N     . ALA B 1 432  ? -26.592 13.178  107.378 1.00 26.70 ?  430  ALA B N     1 
ATOM   12365 C CA    . ALA B 1 432  ? -26.663 12.223  106.276 1.00 23.19 ?  430  ALA B CA    1 
ATOM   12366 C C     . ALA B 1 432  ? -25.962 10.920  106.635 1.00 27.91 ?  430  ALA B C     1 
ATOM   12367 O O     . ALA B 1 432  ? -26.492 9.831   106.390 1.00 27.65 ?  430  ALA B O     1 
ATOM   12368 C CB    . ALA B 1 432  ? -26.053 12.839  105.014 1.00 27.16 ?  430  ALA B CB    1 
ATOM   12369 N N     . ILE B 1 433  ? -24.772 11.011  107.233 1.00 30.55 ?  431  ILE B N     1 
ATOM   12370 C CA    . ILE B 1 433  ? -24.020 9.810   107.579 1.00 26.73 ?  431  ILE B CA    1 
ATOM   12371 C C     . ILE B 1 433  ? -24.626 9.118   108.794 1.00 27.87 ?  431  ILE B C     1 
ATOM   12372 O O     . ILE B 1 433  ? -24.657 7.885   108.862 1.00 28.95 ?  431  ILE B O     1 
ATOM   12373 C CB    . ILE B 1 433  ? -22.538 10.168  107.798 1.00 26.43 ?  431  ILE B CB    1 
ATOM   12374 C CG1   . ILE B 1 433  ? -21.935 10.683  106.492 1.00 28.07 ?  431  ILE B CG1   1 
ATOM   12375 C CG2   . ILE B 1 433  ? -21.763 8.966   108.317 1.00 29.78 ?  431  ILE B CG2   1 
ATOM   12376 C CD1   . ILE B 1 433  ? -20.552 11.226  106.652 1.00 26.94 ?  431  ILE B CD1   1 
ATOM   12377 N N     . TYR B 1 434  ? -25.110 9.894   109.766 1.00 28.91 ?  432  TYR B N     1 
ATOM   12378 C CA    . TYR B 1 434  ? -25.748 9.310   110.943 1.00 26.77 ?  432  TYR B CA    1 
ATOM   12379 C C     . TYR B 1 434  ? -26.898 8.386   110.550 1.00 28.90 ?  432  TYR B C     1 
ATOM   12380 O O     . TYR B 1 434  ? -27.020 7.271   111.073 1.00 29.16 ?  432  TYR B O     1 
ATOM   12381 C CB    . TYR B 1 434  ? -26.216 10.429  111.881 1.00 27.95 ?  432  TYR B CB    1 
ATOM   12382 C CG    . TYR B 1 434  ? -27.120 9.973   113.009 1.00 30.10 ?  432  TYR B CG    1 
ATOM   12383 C CD1   . TYR B 1 434  ? -26.628 9.199   114.062 1.00 27.16 ?  432  TYR B CD1   1 
ATOM   12384 C CD2   . TYR B 1 434  ? -28.466 10.327  113.027 1.00 31.53 ?  432  TYR B CD2   1 
ATOM   12385 C CE1   . TYR B 1 434  ? -27.464 8.781   115.098 1.00 31.11 ?  432  TYR B CE1   1 
ATOM   12386 C CE2   . TYR B 1 434  ? -29.303 9.918   114.054 1.00 33.56 ?  432  TYR B CE2   1 
ATOM   12387 C CZ    . TYR B 1 434  ? -28.796 9.148   115.083 1.00 33.56 ?  432  TYR B CZ    1 
ATOM   12388 O OH    . TYR B 1 434  ? -29.625 8.741   116.098 1.00 36.43 ?  432  TYR B OH    1 
ATOM   12389 N N     . HIS B 1 435  ? -27.719 8.803   109.590 1.00 31.74 ?  433  HIS B N     1 
ATOM   12390 C CA    . HIS B 1 435  ? -28.823 7.953   109.162 1.00 33.49 ?  433  HIS B CA    1 
ATOM   12391 C C     . HIS B 1 435  ? -28.379 6.888   108.164 1.00 30.90 ?  433  HIS B C     1 
ATOM   12392 O O     . HIS B 1 435  ? -28.941 5.785   108.152 1.00 33.78 ?  433  HIS B O     1 
ATOM   12393 C CB    . HIS B 1 435  ? -29.938 8.825   108.593 1.00 30.39 ?  433  HIS B CB    1 
ATOM   12394 C CG    . HIS B 1 435  ? -30.665 9.602   109.644 1.00 30.67 ?  433  HIS B CG    1 
ATOM   12395 N ND1   . HIS B 1 435  ? -31.712 9.070   110.366 1.00 31.42 ?  433  HIS B ND1   1 
ATOM   12396 C CD2   . HIS B 1 435  ? -30.474 10.854  110.124 1.00 30.43 ?  433  HIS B CD2   1 
ATOM   12397 C CE1   . HIS B 1 435  ? -32.146 9.967   111.233 1.00 34.16 ?  433  HIS B CE1   1 
ATOM   12398 N NE2   . HIS B 1 435  ? -31.416 11.060  111.103 1.00 30.75 ?  433  HIS B NE2   1 
ATOM   12399 N N     . MET B 1 436  ? -27.361 7.186   107.350 1.00 31.38 ?  434  MET B N     1 
ATOM   12400 C CA    . MET B 1 436  ? -26.807 6.190   106.437 1.00 27.81 ?  434  MET B CA    1 
ATOM   12401 C C     . MET B 1 436  ? -26.290 4.970   107.192 1.00 34.34 ?  434  MET B C     1 
ATOM   12402 O O     . MET B 1 436  ? -26.391 3.836   106.705 1.00 33.48 ?  434  MET B O     1 
ATOM   12403 C CB    . MET B 1 436  ? -25.683 6.819   105.611 1.00 31.12 ?  434  MET B CB    1 
ATOM   12404 C CG    . MET B 1 436  ? -24.942 5.842   104.719 1.00 29.28 ?  434  MET B CG    1 
ATOM   12405 S SD    . MET B 1 436  ? -23.539 6.629   103.912 1.00 33.28 ?  434  MET B SD    1 
ATOM   12406 C CE    . MET B 1 436  ? -24.392 7.829   102.892 1.00 29.66 ?  434  MET B CE    1 
ATOM   12407 N N     . ALA B 1 437  ? -25.723 5.184   108.382 1.00 28.81 ?  435  ALA B N     1 
ATOM   12408 C CA    . ALA B 1 437  ? -25.114 4.083   109.121 1.00 32.08 ?  435  ALA B CA    1 
ATOM   12409 C C     . ALA B 1 437  ? -26.144 3.123   109.706 1.00 35.82 ?  435  ALA B C     1 
ATOM   12410 O O     . ALA B 1 437  ? -25.812 1.958   109.959 1.00 35.69 ?  435  ALA B O     1 
ATOM   12411 C CB    . ALA B 1 437  ? -24.220 4.632   110.232 1.00 33.86 ?  435  ALA B CB    1 
ATOM   12412 N N     . GLY B 1 438  ? -27.370 3.579   109.937 1.00 34.81 ?  436  GLY B N     1 
ATOM   12413 C CA    . GLY B 1 438  ? -28.424 2.721   110.450 1.00 37.66 ?  436  GLY B CA    1 
ATOM   12414 C C     . GLY B 1 438  ? -28.596 2.836   111.954 1.00 42.41 ?  436  GLY B C     1 
ATOM   12415 O O     . GLY B 1 438  ? -27.937 3.622   112.643 1.00 40.45 ?  436  GLY B O     1 
ATOM   12416 N N     . LYS B 1 439  ? -29.516 2.015   112.464 1.00 44.37 ?  437  LYS B N     1 
ATOM   12417 C CA    . LYS B 1 439  ? -29.857 2.055   113.882 1.00 44.38 ?  437  LYS B CA    1 
ATOM   12418 C C     . LYS B 1 439  ? -28.910 1.213   114.729 1.00 44.23 ?  437  LYS B C     1 
ATOM   12419 O O     . LYS B 1 439  ? -28.720 1.507   115.915 1.00 47.81 ?  437  LYS B O     1 
ATOM   12420 C CB    . LYS B 1 439  ? -31.303 1.585   114.091 1.00 47.52 ?  437  LYS B CB    1 
ATOM   12421 N N     . ASP B 1 440  ? -28.324 0.166   114.155 1.00 40.77 ?  438  ASP B N     1 
ATOM   12422 C CA    . ASP B 1 440  ? -27.439 -0.716  114.905 1.00 48.07 ?  438  ASP B CA    1 
ATOM   12423 C C     . ASP B 1 440  ? -26.097 -0.028  115.104 1.00 43.42 ?  438  ASP B C     1 
ATOM   12424 O O     . ASP B 1 440  ? -25.394 0.254   114.128 1.00 43.96 ?  438  ASP B O     1 
ATOM   12425 C CB    . ASP B 1 440  ? -27.257 -2.041  114.170 1.00 50.14 ?  438  ASP B CB    1 
ATOM   12426 C CG    . ASP B 1 440  ? -28.529 -2.874  114.138 1.00 56.81 ?  438  ASP B CG    1 
ATOM   12427 O OD1   . ASP B 1 440  ? -29.338 -2.782  115.091 1.00 55.06 ?  438  ASP B OD1   1 
ATOM   12428 O OD2   . ASP B 1 440  ? -28.717 -3.630  113.160 1.00 62.01 ?  438  ASP B OD2   1 
ATOM   12429 N N     . PHE B 1 441  ? -25.747 0.265   116.357 1.00 38.77 ?  439  PHE B N     1 
ATOM   12430 C CA    . PHE B 1 441  ? -24.471 0.911   116.630 1.00 40.81 ?  439  PHE B CA    1 
ATOM   12431 C C     . PHE B 1 441  ? -23.843 0.377   117.908 1.00 39.85 ?  439  PHE B C     1 
ATOM   12432 O O     . PHE B 1 441  ? -24.532 0.101   118.893 1.00 40.50 ?  439  PHE B O     1 
ATOM   12433 C CB    . PHE B 1 441  ? -24.599 2.434   116.744 1.00 36.24 ?  439  PHE B CB    1 
ATOM   12434 C CG    . PHE B 1 441  ? -23.278 3.121   116.952 1.00 33.98 ?  439  PHE B CG    1 
ATOM   12435 C CD1   . PHE B 1 441  ? -22.487 3.465   115.864 1.00 36.08 ?  439  PHE B CD1   1 
ATOM   12436 C CD2   . PHE B 1 441  ? -22.812 3.393   118.233 1.00 33.36 ?  439  PHE B CD2   1 
ATOM   12437 C CE1   . PHE B 1 441  ? -21.266 4.077   116.047 1.00 30.97 ?  439  PHE B CE1   1 
ATOM   12438 C CE2   . PHE B 1 441  ? -21.587 4.005   118.422 1.00 35.62 ?  439  PHE B CE2   1 
ATOM   12439 C CZ    . PHE B 1 441  ? -20.814 4.343   117.325 1.00 33.19 ?  439  PHE B CZ    1 
ATOM   12440 N N     . HIS B 1 442  ? -22.520 0.257   117.871 1.00 37.22 ?  440  HIS B N     1 
ATOM   12441 C CA    . HIS B 1 442  ? -21.685 -0.035  119.024 1.00 38.45 ?  440  HIS B CA    1 
ATOM   12442 C C     . HIS B 1 442  ? -20.401 0.764   118.872 1.00 34.01 ?  440  HIS B C     1 
ATOM   12443 O O     . HIS B 1 442  ? -19.940 0.993   117.753 1.00 33.00 ?  440  HIS B O     1 
ATOM   12444 C CB    . HIS B 1 442  ? -21.357 -1.525  119.112 1.00 44.93 ?  440  HIS B CB    1 
ATOM   12445 C CG    . HIS B 1 442  ? -20.698 -2.066  117.878 1.00 47.60 ?  440  HIS B CG    1 
ATOM   12446 N ND1   . HIS B 1 442  ? -19.343 -1.954  117.645 1.00 44.35 ?  440  HIS B ND1   1 
ATOM   12447 C CD2   . HIS B 1 442  ? -21.213 -2.705  116.800 1.00 49.37 ?  440  HIS B CD2   1 
ATOM   12448 C CE1   . HIS B 1 442  ? -19.050 -2.511  116.482 1.00 46.38 ?  440  HIS B CE1   1 
ATOM   12449 N NE2   . HIS B 1 442  ? -20.167 -2.975  115.950 1.00 49.99 ?  440  HIS B NE2   1 
ATOM   12450 N N     . VAL B 1 443  ? -19.821 1.189   119.995 1.00 33.78 ?  441  VAL B N     1 
ATOM   12451 C CA    . VAL B 1 443  ? -18.527 1.859   119.919 1.00 29.10 ?  441  VAL B CA    1 
ATOM   12452 C C     . VAL B 1 443  ? -17.520 0.910   119.290 1.00 35.09 ?  441  VAL B C     1 
ATOM   12453 O O     . VAL B 1 443  ? -17.441 -0.272  119.646 1.00 34.25 ?  441  VAL B O     1 
ATOM   12454 C CB    . VAL B 1 443  ? -18.074 2.340   121.304 1.00 32.48 ?  441  VAL B CB    1 
ATOM   12455 C CG1   . VAL B 1 443  ? -16.601 2.732   121.269 1.00 29.75 ?  441  VAL B CG1   1 
ATOM   12456 C CG2   . VAL B 1 443  ? -18.926 3.521   121.744 1.00 33.11 ?  441  VAL B CG2   1 
ATOM   12457 N N     . GLY B 1 444  ? -16.766 1.418   118.323 1.00 29.97 ?  442  GLY B N     1 
ATOM   12458 C CA    . GLY B 1 444  ? -15.866 0.607   117.535 1.00 29.09 ?  442  GLY B CA    1 
ATOM   12459 C C     . GLY B 1 444  ? -16.346 0.363   116.123 1.00 30.59 ?  442  GLY B C     1 
ATOM   12460 O O     . GLY B 1 444  ? -15.551 -0.084  115.287 1.00 27.57 ?  442  GLY B O     1 
ATOM   12461 N N     . LYS B 1 445  ? -17.619 0.634   115.830 1.00 29.98 ?  443  LYS B N     1 
ATOM   12462 C CA    . LYS B 1 445  ? -18.098 0.516   114.458 1.00 29.28 ?  443  LYS B CA    1 
ATOM   12463 C C     . LYS B 1 445  ? -17.597 1.681   113.612 1.00 26.56 ?  443  LYS B C     1 
ATOM   12464 O O     . LYS B 1 445  ? -16.951 1.477   112.581 1.00 28.40 ?  443  LYS B O     1 
ATOM   12465 C CB    . LYS B 1 445  ? -19.627 0.437   114.427 1.00 32.97 ?  443  LYS B CB    1 
ATOM   12466 C CG    . LYS B 1 445  ? -20.153 -0.154  113.124 1.00 35.70 ?  443  LYS B CG    1 
ATOM   12467 C CD    . LYS B 1 445  ? -21.102 0.780   112.399 1.00 42.05 ?  443  LYS B CD    1 
ATOM   12468 C CE    . LYS B 1 445  ? -22.535 0.578   112.859 1.00 43.29 ?  443  LYS B CE    1 
ATOM   12469 N NZ    . LYS B 1 445  ? -23.511 1.165   111.888 1.00 46.38 ?  443  LYS B NZ    1 
ATOM   12470 N N     . TYR B 1 446  ? -17.880 2.908   114.047 1.00 26.76 ?  444  TYR B N     1 
ATOM   12471 C CA    . TYR B 1 446  ? -17.381 4.119   113.405 1.00 24.73 ?  444  TYR B CA    1 
ATOM   12472 C C     . TYR B 1 446  ? -17.435 5.227   114.445 1.00 25.35 ?  444  TYR B C     1 
ATOM   12473 O O     . TYR B 1 446  ? -18.010 5.062   115.522 1.00 26.17 ?  444  TYR B O     1 
ATOM   12474 C CB    . TYR B 1 446  ? -18.195 4.479   112.154 1.00 27.16 ?  444  TYR B CB    1 
ATOM   12475 C CG    . TYR B 1 446  ? -19.552 5.107   112.423 1.00 28.78 ?  444  TYR B CG    1 
ATOM   12476 C CD1   . TYR B 1 446  ? -19.692 6.487   112.548 1.00 28.10 ?  444  TYR B CD1   1 
ATOM   12477 C CD2   . TYR B 1 446  ? -20.695 4.322   112.517 1.00 29.58 ?  444  TYR B CD2   1 
ATOM   12478 C CE1   . TYR B 1 446  ? -20.926 7.063   112.788 1.00 31.39 ?  444  TYR B CE1   1 
ATOM   12479 C CE2   . TYR B 1 446  ? -21.936 4.886   112.758 1.00 30.61 ?  444  TYR B CE2   1 
ATOM   12480 C CZ    . TYR B 1 446  ? -22.043 6.258   112.892 1.00 30.75 ?  444  TYR B CZ    1 
ATOM   12481 O OH    . TYR B 1 446  ? -23.275 6.826   113.120 1.00 37.17 ?  444  TYR B OH    1 
ATOM   12482 N N     . GLU B 1 447  ? -16.823 6.361   114.124 1.00 23.12 ?  445  GLU B N     1 
ATOM   12483 C CA    . GLU B 1 447  ? -16.940 7.509   115.005 1.00 23.86 ?  445  GLU B CA    1 
ATOM   12484 C C     . GLU B 1 447  ? -16.962 8.767   114.156 1.00 22.48 ?  445  GLU B C     1 
ATOM   12485 O O     . GLU B 1 447  ? -16.660 8.737   112.963 1.00 22.05 ?  445  GLU B O     1 
ATOM   12486 C CB    . GLU B 1 447  ? -15.793 7.564   116.015 1.00 21.42 ?  445  GLU B CB    1 
ATOM   12487 C CG    . GLU B 1 447  ? -14.435 7.801   115.354 1.00 20.71 ?  445  GLU B CG    1 
ATOM   12488 C CD    . GLU B 1 447  ? -13.277 7.803   116.330 1.00 20.66 ?  445  GLU B CD    1 
ATOM   12489 O OE1   . GLU B 1 447  ? -13.430 7.339   117.476 1.00 24.86 ?  445  GLU B OE1   1 
ATOM   12490 O OE2   . GLU B 1 447  ? -12.199 8.295   115.926 1.00 21.03 ?  445  GLU B OE2   1 
ATOM   12491 N N     . PHE B 1 448  ? -17.367 9.866   114.781 1.00 22.05 ?  446  PHE B N     1 
ATOM   12492 C CA    . PHE B 1 448  ? -17.182 11.204  114.243 1.00 20.65 ?  446  PHE B CA    1 
ATOM   12493 C C     . PHE B 1 448  ? -15.923 11.818  114.838 1.00 19.72 ?  446  PHE B C     1 
ATOM   12494 O O     . PHE B 1 448  ? -15.372 11.314  115.821 1.00 21.12 ?  446  PHE B O     1 
ATOM   12495 C CB    . PHE B 1 448  ? -18.386 12.087  114.555 1.00 25.79 ?  446  PHE B CB    1 
ATOM   12496 C CG    . PHE B 1 448  ? -19.642 11.656  113.879 1.00 23.75 ?  446  PHE B CG    1 
ATOM   12497 C CD1   . PHE B 1 448  ? -19.864 11.973  112.551 1.00 25.14 ?  446  PHE B CD1   1 
ATOM   12498 C CD2   . PHE B 1 448  ? -20.610 10.945  114.569 1.00 25.53 ?  446  PHE B CD2   1 
ATOM   12499 C CE1   . PHE B 1 448  ? -21.026 11.576  111.914 1.00 25.38 ?  446  PHE B CE1   1 
ATOM   12500 C CE2   . PHE B 1 448  ? -21.777 10.542  113.936 1.00 26.43 ?  446  PHE B CE2   1 
ATOM   12501 C CZ    . PHE B 1 448  ? -21.984 10.869  112.605 1.00 27.64 ?  446  PHE B CZ    1 
ATOM   12502 N N     . GLN B 1 449  ? -15.451 12.897  114.207 1.00 20.78 ?  447  GLN B N     1 
ATOM   12503 C CA    . GLN B 1 449  ? -14.312 13.648  114.712 1.00 20.64 ?  447  GLN B CA    1 
ATOM   12504 C C     . GLN B 1 449  ? -14.532 15.134  114.484 1.00 18.23 ?  447  GLN B C     1 
ATOM   12505 O O     . GLN B 1 449  ? -15.250 15.544  113.566 1.00 18.64 ?  447  GLN B O     1 
ATOM   12506 C CB    . GLN B 1 449  ? -12.989 13.231  114.050 1.00 18.80 ?  447  GLN B CB    1 
ATOM   12507 C CG    . GLN B 1 449  ? -12.663 11.757  114.163 1.00 22.10 ?  447  GLN B CG    1 
ATOM   12508 C CD    . GLN B 1 449  ? -11.193 11.484  113.967 1.00 18.19 ?  447  GLN B CD    1 
ATOM   12509 O OE1   . GLN B 1 449  ? -10.475 12.318  113.431 1.00 21.84 ?  447  GLN B OE1   1 
ATOM   12510 N NE2   . GLN B 1 449  ? -10.734 10.322  114.409 1.00 19.06 ?  447  GLN B NE2   1 
ATOM   12511 N N     . CYS B 1 450  ? -13.889 15.941  115.323 1.00 18.16 ?  448  CYS B N     1 
ATOM   12512 C CA    . CYS B 1 450  ? -13.986 17.385  115.211 1.00 17.85 ?  448  CYS B CA    1 
ATOM   12513 C C     . CYS B 1 450  ? -12.708 18.021  115.737 1.00 17.35 ?  448  CYS B C     1 
ATOM   12514 O O     . CYS B 1 450  ? -11.871 17.370  116.372 1.00 18.90 ?  448  CYS B O     1 
ATOM   12515 C CB    . CYS B 1 450  ? -15.198 17.924  115.986 1.00 18.70 ?  448  CYS B CB    1 
ATOM   12516 S SG    . CYS B 1 450  ? -15.029 17.909  117.791 1.00 22.38 ?  448  CYS B SG    1 
ATOM   12517 N N     . LEU B 1 451  ? -12.602 19.319  115.507 1.00 17.51 ?  449  LEU B N     1 
ATOM   12518 C CA    . LEU B 1 451  ? -11.473 20.111  115.977 1.00 19.46 ?  449  LEU B CA    1 
ATOM   12519 C C     . LEU B 1 451  ? -11.763 20.703  117.351 1.00 21.74 ?  449  LEU B C     1 
ATOM   12520 O O     . LEU B 1 451  ? -12.861 21.200  117.605 1.00 23.67 ?  449  LEU B O     1 
ATOM   12521 C CB    . LEU B 1 451  ? -11.174 21.231  114.985 1.00 18.22 ?  449  LEU B CB    1 
ATOM   12522 C CG    . LEU B 1 451  ? -9.992  22.142  115.288 1.00 20.64 ?  449  LEU B CG    1 
ATOM   12523 C CD1   . LEU B 1 451  ? -8.685  21.355  115.254 1.00 24.32 ?  449  LEU B CD1   1 
ATOM   12524 C CD2   . LEU B 1 451  ? -9.962  23.287  114.287 1.00 23.11 ?  449  LEU B CD2   1 
ATOM   12525 N N     . HIS B 1 452  ? -10.772 20.632  118.239 1.00 19.00 ?  450  HIS B N     1 
ATOM   12526 C CA    . HIS B 1 452  ? -10.857 21.301  119.529 1.00 22.84 ?  450  HIS B CA    1 
ATOM   12527 C C     . HIS B 1 452  ? -11.184 22.778  119.358 1.00 22.46 ?  450  HIS B C     1 
ATOM   12528 O O     . HIS B 1 452  ? -10.625 23.454  118.494 1.00 23.82 ?  450  HIS B O     1 
ATOM   12529 C CB    . HIS B 1 452  ? -9.526  21.160  120.266 1.00 21.10 ?  450  HIS B CB    1 
ATOM   12530 C CG    . HIS B 1 452  ? -9.436  22.015  121.491 1.00 23.38 ?  450  HIS B CG    1 
ATOM   12531 N ND1   . HIS B 1 452  ? -9.935  21.615  122.710 1.00 22.89 ?  450  HIS B ND1   1 
ATOM   12532 C CD2   . HIS B 1 452  ? -8.949  23.266  121.674 1.00 21.98 ?  450  HIS B CD2   1 
ATOM   12533 C CE1   . HIS B 1 452  ? -9.741  22.575  123.598 1.00 24.55 ?  450  HIS B CE1   1 
ATOM   12534 N NE2   . HIS B 1 452  ? -9.152  23.590  122.994 1.00 21.82 ?  450  HIS B NE2   1 
ATOM   12535 N N     . GLY B 1 453  ? -12.061 23.290  120.220 1.00 28.70 ?  451  GLY B N     1 
ATOM   12536 C CA    . GLY B 1 453  ? -12.347 24.715  120.198 1.00 26.00 ?  451  GLY B CA    1 
ATOM   12537 C C     . GLY B 1 453  ? -13.073 25.174  118.956 1.00 33.75 ?  451  GLY B C     1 
ATOM   12538 O O     . GLY B 1 453  ? -12.967 26.345  118.571 1.00 35.19 ?  451  GLY B O     1 
ATOM   12539 N N     . MET B 1 454  ? -13.797 24.271  118.307 1.00 27.71 ?  452  MET B N     1 
ATOM   12540 C CA    . MET B 1 454  ? -14.515 24.588  117.085 1.00 25.86 ?  452  MET B CA    1 
ATOM   12541 C C     . MET B 1 454  ? -15.704 23.654  116.959 1.00 25.25 ?  452  MET B C     1 
ATOM   12542 O O     . MET B 1 454  ? -16.833 24.096  116.728 1.00 25.24 ?  452  MET B O     1 
ATOM   12543 C CB    . MET B 1 454  ? -13.587 24.454  115.874 1.00 22.53 ?  452  MET B CB    1 
ATOM   12544 C CG    . MET B 1 454  ? -14.291 24.493  114.535 1.00 25.17 ?  452  MET B CG    1 
ATOM   12545 S SD    . MET B 1 454  ? -15.102 26.072  114.283 1.00 31.21 ?  452  MET B SD    1 
ATOM   12546 C CE    . MET B 1 454  ? -13.693 27.179  114.383 1.00 34.45 ?  452  MET B CE    1 
ATOM   12547 N N     . GLY B 1 455  ? -15.456 22.359  117.135 1.00 21.46 ?  453  GLY B N     1 
ATOM   12548 C CA    . GLY B 1 455  ? -16.472 21.351  116.932 1.00 22.98 ?  453  GLY B CA    1 
ATOM   12549 C C     . GLY B 1 455  ? -17.319 20.999  118.127 1.00 27.54 ?  453  GLY B C     1 
ATOM   12550 O O     . GLY B 1 455  ? -18.328 20.309  117.967 1.00 26.87 ?  453  GLY B O     1 
ATOM   12551 N N     . GLU B 1 456  ? -16.942 21.424  119.331 1.00 27.17 ?  454  GLU B N     1 
ATOM   12552 C CA    . GLU B 1 456  ? -17.689 20.989  120.507 1.00 26.20 ?  454  GLU B CA    1 
ATOM   12553 C C     . GLU B 1 456  ? -19.142 21.454  120.513 1.00 27.11 ?  454  GLU B C     1 
ATOM   12554 O O     . GLU B 1 456  ? -20.007 20.649  120.894 1.00 28.49 ?  454  GLU B O     1 
ATOM   12555 C CB    . GLU B 1 456  ? -16.962 21.434  121.780 1.00 30.78 ?  454  GLU B CB    1 
ATOM   12556 C CG    . GLU B 1 456  ? -15.615 20.760  121.963 1.00 31.86 ?  454  GLU B CG    1 
ATOM   12557 C CD    . GLU B 1 456  ? -14.469 21.636  121.509 1.00 35.24 ?  454  GLU B CD    1 
ATOM   12558 O OE1   . GLU B 1 456  ? -14.695 22.498  120.625 1.00 33.94 ?  454  GLU B OE1   1 
ATOM   12559 O OE2   . GLU B 1 456  ? -13.350 21.471  122.045 1.00 32.46 ?  454  GLU B OE2   1 
ATOM   12560 N N     . PRO B 1 457  ? -19.488 22.685  120.117 1.00 28.54 ?  455  PRO B N     1 
ATOM   12561 C CA    . PRO B 1 457  ? -20.916 23.045  120.090 1.00 30.41 ?  455  PRO B CA    1 
ATOM   12562 C C     . PRO B 1 457  ? -21.773 22.076  119.292 1.00 31.04 ?  455  PRO B C     1 
ATOM   12563 O O     . PRO B 1 457  ? -22.888 21.754  119.720 1.00 32.23 ?  455  PRO B O     1 
ATOM   12564 C CB    . PRO B 1 457  ? -20.904 24.446  119.471 1.00 29.72 ?  455  PRO B CB    1 
ATOM   12565 C CG    . PRO B 1 457  ? -19.597 25.011  119.889 1.00 32.85 ?  455  PRO B CG    1 
ATOM   12566 C CD    . PRO B 1 457  ? -18.632 23.861  119.865 1.00 28.43 ?  455  PRO B CD    1 
ATOM   12567 N N     . LEU B 1 458  ? -21.278 21.588  118.151 1.00 27.02 ?  456  LEU B N     1 
ATOM   12568 C CA    . LEU B 1 458  ? -22.043 20.622  117.368 1.00 29.53 ?  456  LEU B CA    1 
ATOM   12569 C C     . LEU B 1 458  ? -22.069 19.259  118.047 1.00 26.80 ?  456  LEU B C     1 
ATOM   12570 O O     . LEU B 1 458  ? -23.129 18.639  118.181 1.00 28.97 ?  456  LEU B O     1 
ATOM   12571 C CB    . LEU B 1 458  ? -21.461 20.504  115.956 1.00 23.91 ?  456  LEU B CB    1 
ATOM   12572 C CG    . LEU B 1 458  ? -22.031 19.383  115.072 1.00 24.40 ?  456  LEU B CG    1 
ATOM   12573 C CD1   . LEU B 1 458  ? -23.555 19.473  114.940 1.00 29.29 ?  456  LEU B CD1   1 
ATOM   12574 C CD2   . LEU B 1 458  ? -21.376 19.372  113.693 1.00 25.09 ?  456  LEU B CD2   1 
ATOM   12575 N N     . TYR B 1 459  ? -20.912 18.765  118.478 1.00 24.86 ?  457  TYR B N     1 
ATOM   12576 C CA    . TYR B 1 459  ? -20.874 17.394  118.957 1.00 25.56 ?  457  TYR B CA    1 
ATOM   12577 C C     . TYR B 1 459  ? -21.349 17.255  120.398 1.00 26.77 ?  457  TYR B C     1 
ATOM   12578 O O     . TYR B 1 459  ? -21.610 16.129  120.840 1.00 26.60 ?  457  TYR B O     1 
ATOM   12579 C CB    . TYR B 1 459  ? -19.469 16.832  118.735 1.00 26.69 ?  457  TYR B CB    1 
ATOM   12580 C CG    . TYR B 1 459  ? -19.294 16.505  117.267 1.00 22.88 ?  457  TYR B CG    1 
ATOM   12581 C CD1   . TYR B 1 459  ? -19.765 15.306  116.763 1.00 23.16 ?  457  TYR B CD1   1 
ATOM   12582 C CD2   . TYR B 1 459  ? -18.716 17.411  116.376 1.00 23.76 ?  457  TYR B CD2   1 
ATOM   12583 C CE1   . TYR B 1 459  ? -19.653 14.993  115.433 1.00 21.94 ?  457  TYR B CE1   1 
ATOM   12584 C CE2   . TYR B 1 459  ? -18.599 17.102  115.017 1.00 23.11 ?  457  TYR B CE2   1 
ATOM   12585 C CZ    . TYR B 1 459  ? -19.058 15.882  114.559 1.00 20.78 ?  457  TYR B CZ    1 
ATOM   12586 O OH    . TYR B 1 459  ? -18.953 15.557  113.223 1.00 24.25 ?  457  TYR B OH    1 
ATOM   12587 N N     . GLU B 1 460  ? -21.510 18.375  121.114 1.00 26.45 ?  458  GLU B N     1 
ATOM   12588 C CA    . GLU B 1 460  ? -22.303 18.372  122.341 1.00 28.72 ?  458  GLU B CA    1 
ATOM   12589 C C     . GLU B 1 460  ? -23.702 17.840  122.089 1.00 32.05 ?  458  GLU B C     1 
ATOM   12590 O O     . GLU B 1 460  ? -24.344 17.312  123.008 1.00 31.44 ?  458  GLU B O     1 
ATOM   12591 C CB    . GLU B 1 460  ? -22.406 19.785  122.915 1.00 31.87 ?  458  GLU B CB    1 
ATOM   12592 C CG    . GLU B 1 460  ? -21.274 20.213  123.816 1.00 34.72 ?  458  GLU B CG    1 
ATOM   12593 C CD    . GLU B 1 460  ? -21.365 21.692  124.156 1.00 47.72 ?  458  GLU B CD    1 
ATOM   12594 O OE1   . GLU B 1 460  ? -22.322 22.352  123.685 1.00 44.33 ?  458  GLU B OE1   1 
ATOM   12595 O OE2   . GLU B 1 460  ? -20.483 22.195  124.884 1.00 51.12 ?  458  GLU B OE2   1 
ATOM   12596 N N     . GLU B 1 461  ? -24.198 18.004  120.864 1.00 31.07 ?  459  GLU B N     1 
ATOM   12597 C CA    . GLU B 1 461  ? -25.522 17.552  120.462 1.00 31.48 ?  459  GLU B CA    1 
ATOM   12598 C C     . GLU B 1 461  ? -25.512 16.165  119.838 1.00 34.98 ?  459  GLU B C     1 
ATOM   12599 O O     . GLU B 1 461  ? -26.527 15.753  119.265 1.00 31.99 ?  459  GLU B O     1 
ATOM   12600 C CB    . GLU B 1 461  ? -26.133 18.549  119.477 1.00 29.23 ?  459  GLU B CB    1 
ATOM   12601 C CG    . GLU B 1 461  ? -26.099 19.986  119.955 1.00 26.61 ?  459  GLU B CG    1 
ATOM   12602 C CD    . GLU B 1 461  ? -26.952 20.170  121.205 1.00 32.39 ?  459  GLU B CD    1 
ATOM   12603 O OE1   . GLU B 1 461  ? -27.906 19.382  121.383 1.00 35.22 ?  459  GLU B OE1   1 
ATOM   12604 O OE2   . GLU B 1 461  ? -26.666 21.082  122.009 1.00 37.78 ?  459  GLU B OE2   1 
ATOM   12605 N N     . VAL B 1 462  ? -24.399 15.438  119.941 1.00 28.81 ?  460  VAL B N     1 
ATOM   12606 C CA    . VAL B 1 462  ? -24.238 14.154  119.268 1.00 28.86 ?  460  VAL B CA    1 
ATOM   12607 C C     . VAL B 1 462  ? -23.827 13.096  120.281 1.00 33.41 ?  460  VAL B C     1 
ATOM   12608 O O     . VAL B 1 462  ? -24.429 12.016  120.349 1.00 29.46 ?  460  VAL B O     1 
ATOM   12609 C CB    . VAL B 1 462  ? -23.210 14.262  118.123 1.00 27.57 ?  460  VAL B CB    1 
ATOM   12610 C CG1   . VAL B 1 462  ? -22.942 12.895  117.505 1.00 28.70 ?  460  VAL B CG1   1 
ATOM   12611 C CG2   . VAL B 1 462  ? -23.694 15.242  117.064 1.00 28.02 ?  460  VAL B CG2   1 
ATOM   12612 N N     . VAL B 1 463  ? -22.798 13.403  121.072 1.00 29.93 ?  461  VAL B N     1 
ATOM   12613 C CA    . VAL B 1 463  ? -22.256 12.447  122.032 1.00 27.63 ?  461  VAL B CA    1 
ATOM   12614 C C     . VAL B 1 463  ? -23.207 12.309  123.210 1.00 30.63 ?  461  VAL B C     1 
ATOM   12615 O O     . VAL B 1 463  ? -23.694 13.307  123.761 1.00 32.80 ?  461  VAL B O     1 
ATOM   12616 C CB    . VAL B 1 463  ? -20.863 12.887  122.506 1.00 28.52 ?  461  VAL B CB    1 
ATOM   12617 C CG1   . VAL B 1 463  ? -20.344 11.935  123.594 1.00 29.63 ?  461  VAL B CG1   1 
ATOM   12618 C CG2   . VAL B 1 463  ? -19.888 12.968  121.321 1.00 26.20 ?  461  VAL B CG2   1 
ATOM   12619 N N     . GLY B 1 464  ? -23.470 11.072  123.600 1.00 29.57 ?  462  GLY B N     1 
ATOM   12620 C CA    . GLY B 1 464  ? -24.216 10.791  124.811 1.00 30.86 ?  462  GLY B CA    1 
ATOM   12621 C C     . GLY B 1 464  ? -25.546 10.127  124.542 1.00 35.73 ?  462  GLY B C     1 
ATOM   12622 O O     . GLY B 1 464  ? -26.163 10.331  123.497 1.00 34.82 ?  462  GLY B O     1 
ATOM   12623 N N     . ARG B 1 465  ? -26.005 9.322   125.510 1.00 38.76 ?  463  ARG B N     1 
ATOM   12624 C CA    . ARG B 1 465  ? -27.279 8.627   125.352 1.00 39.00 ?  463  ARG B CA    1 
ATOM   12625 C C     . ARG B 1 465  ? -28.440 9.604   125.204 1.00 41.11 ?  463  ARG B C     1 
ATOM   12626 O O     . ARG B 1 465  ? -29.453 9.274   124.576 1.00 44.28 ?  463  ARG B O     1 
ATOM   12627 C CB    . ARG B 1 465  ? -27.514 7.684   126.530 1.00 43.48 ?  463  ARG B CB    1 
ATOM   12628 N N     . GLY B 1 466  ? -28.313 10.808  125.761 1.00 38.91 ?  464  GLY B N     1 
ATOM   12629 C CA    . GLY B 1 466  ? -29.336 11.826  125.605 1.00 37.36 ?  464  GLY B CA    1 
ATOM   12630 C C     . GLY B 1 466  ? -29.339 12.550  124.279 1.00 41.15 ?  464  GLY B C     1 
ATOM   12631 O O     . GLY B 1 466  ? -30.223 13.378  124.043 1.00 40.66 ?  464  GLY B O     1 
ATOM   12632 N N     . LYS B 1 467  ? -28.366 12.267  123.405 1.00 38.07 ?  465  LYS B N     1 
ATOM   12633 C CA    . LYS B 1 467  ? -28.276 12.936  122.112 1.00 33.69 ?  465  LYS B CA    1 
ATOM   12634 C C     . LYS B 1 467  ? -28.425 11.864  121.041 1.00 29.82 ?  465  LYS B C     1 
ATOM   12635 O O     . LYS B 1 467  ? -29.434 11.164  121.024 1.00 36.16 ?  465  LYS B O     1 
ATOM   12636 C CB    . LYS B 1 467  ? -26.998 13.757  122.009 1.00 33.29 ?  465  LYS B CB    1 
ATOM   12637 C CG    . LYS B 1 467  ? -26.863 14.813  123.097 1.00 37.59 ?  465  LYS B CG    1 
ATOM   12638 C CD    . LYS B 1 467  ? -27.873 15.935  122.902 1.00 36.71 ?  465  LYS B CD    1 
ATOM   12639 C CE    . LYS B 1 467  ? -27.758 16.973  124.004 1.00 40.14 ?  465  LYS B CE    1 
ATOM   12640 N NZ    . LYS B 1 467  ? -28.633 18.151  123.736 1.00 39.21 ?  465  LYS B NZ    1 
ATOM   12641 N N     . LEU B 1 468  ? -27.454 11.728  120.137 1.00 29.93 ?  466  LEU B N     1 
ATOM   12642 C CA    . LEU B 1 468  ? -27.466 10.684  119.124 1.00 29.20 ?  466  LEU B CA    1 
ATOM   12643 C C     . LEU B 1 468  ? -26.720 9.432   119.564 1.00 31.43 ?  466  LEU B C     1 
ATOM   12644 O O     . LEU B 1 468  ? -26.740 8.432   118.841 1.00 31.05 ?  466  LEU B O     1 
ATOM   12645 C CB    . LEU B 1 468  ? -26.870 11.220  117.817 1.00 31.42 ?  466  LEU B CB    1 
ATOM   12646 C CG    . LEU B 1 468  ? -27.504 12.507  117.282 1.00 30.57 ?  466  LEU B CG    1 
ATOM   12647 C CD1   . LEU B 1 468  ? -26.923 12.892  115.928 1.00 32.47 ?  466  LEU B CD1   1 
ATOM   12648 C CD2   . LEU B 1 468  ? -29.017 12.346  117.198 1.00 33.96 ?  466  LEU B CD2   1 
ATOM   12649 N N     . ASP B 1 469  ? -26.068 9.470   120.728 1.00 31.35 ?  467  ASP B N     1 
ATOM   12650 C CA    . ASP B 1 469  ? -25.322 8.337   121.274 1.00 32.57 ?  467  ASP B CA    1 
ATOM   12651 C C     . ASP B 1 469  ? -24.276 7.852   120.279 1.00 30.39 ?  467  ASP B C     1 
ATOM   12652 O O     . ASP B 1 469  ? -24.128 6.656   120.012 1.00 31.01 ?  467  ASP B O     1 
ATOM   12653 C CB    . ASP B 1 469  ? -26.262 7.207   121.698 1.00 35.12 ?  467  ASP B CB    1 
ATOM   12654 C CG    . ASP B 1 469  ? -25.643 6.292   122.738 1.00 38.06 ?  467  ASP B CG    1 
ATOM   12655 O OD1   . ASP B 1 469  ? -24.596 6.654   123.315 1.00 37.66 ?  467  ASP B OD1   1 
ATOM   12656 O OD2   . ASP B 1 469  ? -26.201 5.202   122.977 1.00 41.65 ?  467  ASP B OD2   1 
ATOM   12657 N N     . ARG B 1 470  ? -23.544 8.811   119.721 1.00 31.62 ?  468  ARG B N     1 
ATOM   12658 C CA    . ARG B 1 470  ? -22.457 8.540   118.803 1.00 29.19 ?  468  ARG B CA    1 
ATOM   12659 C C     . ARG B 1 470  ? -21.190 9.217   119.307 1.00 27.49 ?  468  ARG B C     1 
ATOM   12660 O O     . ARG B 1 470  ? -21.237 10.359  119.780 1.00 29.64 ?  468  ARG B O     1 
ATOM   12661 C CB    . ARG B 1 470  ? -22.787 9.036   117.385 1.00 29.78 ?  468  ARG B CB    1 
ATOM   12662 C CG    . ARG B 1 470  ? -23.990 8.337   116.744 1.00 28.53 ?  468  ARG B CG    1 
ATOM   12663 C CD    . ARG B 1 470  ? -23.751 6.840   116.579 1.00 28.74 ?  468  ARG B CD    1 
ATOM   12664 N NE    . ARG B 1 470  ? -24.877 6.172   115.933 1.00 31.78 ?  468  ARG B NE    1 
ATOM   12665 C CZ    . ARG B 1 470  ? -25.860 5.558   116.579 1.00 34.03 ?  468  ARG B CZ    1 
ATOM   12666 N NH1   . ARG B 1 470  ? -25.890 5.502   117.902 1.00 34.41 ?  468  ARG B NH1   1 
ATOM   12667 N NH2   . ARG B 1 470  ? -26.836 4.983   115.881 1.00 37.05 ?  468  ARG B NH2   1 
ATOM   12668 N N     . PRO B 1 471  ? -20.051 8.543   119.215 1.00 27.68 ?  469  PRO B N     1 
ATOM   12669 C CA    . PRO B 1 471  ? -18.816 9.093   119.774 1.00 23.84 ?  469  PRO B CA    1 
ATOM   12670 C C     . PRO B 1 471  ? -18.186 10.110  118.839 1.00 24.37 ?  469  PRO B C     1 
ATOM   12671 O O     . PRO B 1 471  ? -18.463 10.159  117.639 1.00 24.60 ?  469  PRO B O     1 
ATOM   12672 C CB    . PRO B 1 471  ? -17.918 7.862   119.926 1.00 26.41 ?  469  PRO B CB    1 
ATOM   12673 C CG    . PRO B 1 471  ? -18.385 6.943   118.860 1.00 30.37 ?  469  PRO B CG    1 
ATOM   12674 C CD    . PRO B 1 471  ? -19.862 7.188   118.680 1.00 29.65 ?  469  PRO B CD    1 
ATOM   12675 N N     . CYS B 1 472  ? -17.330 10.938  119.425 1.00 23.18 ?  470  CYS B N     1 
ATOM   12676 C CA    . CYS B 1 472  ? -16.585 11.935  118.675 1.00 22.93 ?  470  CYS B CA    1 
ATOM   12677 C C     . CYS B 1 472  ? -15.174 12.033  119.235 1.00 23.48 ?  470  CYS B C     1 
ATOM   12678 O O     . CYS B 1 472  ? -14.995 12.204  120.446 1.00 23.27 ?  470  CYS B O     1 
ATOM   12679 C CB    . CYS B 1 472  ? -17.264 13.303  118.736 1.00 22.29 ?  470  CYS B CB    1 
ATOM   12680 S SG    . CYS B 1 472  ? -16.381 14.529  117.770 1.00 25.58 ?  470  CYS B SG    1 
ATOM   12681 N N     . ARG B 1 473  ? -14.182 11.920  118.353 1.00 22.66 ?  471  ARG B N     1 
ATOM   12682 C CA    . ARG B 1 473  ? -12.789 12.131  118.719 1.00 21.00 ?  471  ARG B CA    1 
ATOM   12683 C C     . ARG B 1 473  ? -12.401 13.568  118.411 1.00 20.79 ?  471  ARG B C     1 
ATOM   12684 O O     . ARG B 1 473  ? -12.575 14.039  117.285 1.00 21.62 ?  471  ARG B O     1 
ATOM   12685 C CB    . ARG B 1 473  ? -11.863 11.173  117.974 1.00 19.66 ?  471  ARG B CB    1 
ATOM   12686 C CG    . ARG B 1 473  ? -10.417 11.179  118.497 1.00 19.44 ?  471  ARG B CG    1 
ATOM   12687 C CD    . ARG B 1 473  ? -9.612  10.076  117.806 1.00 19.74 ?  471  ARG B CD    1 
ATOM   12688 N NE    . ARG B 1 473  ? -10.299 8.790   117.924 1.00 23.03 ?  471  ARG B NE    1 
ATOM   12689 C CZ    . ARG B 1 473  ? -10.203 7.978   118.969 1.00 23.36 ?  471  ARG B CZ    1 
ATOM   12690 N NH1   . ARG B 1 473  ? -9.362  8.226   119.966 1.00 22.77 ?  471  ARG B NH1   1 
ATOM   12691 N NH2   . ARG B 1 473  ? -10.981 6.897   119.028 1.00 21.18 ?  471  ARG B NH2   1 
ATOM   12692 N N     . ILE B 1 474  ? -11.864 14.250  119.415 1.00 20.49 ?  472  ILE B N     1 
ATOM   12693 C CA    . ILE B 1 474  ? -11.466 15.646  119.297 1.00 18.71 ?  472  ILE B CA    1 
ATOM   12694 C C     . ILE B 1 474  ? -10.014 15.695  118.845 1.00 20.04 ?  472  ILE B C     1 
ATOM   12695 O O     . ILE B 1 474  ? -9.141  15.119  119.501 1.00 19.46 ?  472  ILE B O     1 
ATOM   12696 C CB    . ILE B 1 474  ? -11.644 16.378  120.634 1.00 21.13 ?  472  ILE B CB    1 
ATOM   12697 C CG1   . ILE B 1 474  ? -13.120 16.392  121.026 1.00 20.37 ?  472  ILE B CG1   1 
ATOM   12698 C CG2   . ILE B 1 474  ? -11.089 17.793  120.544 1.00 23.63 ?  472  ILE B CG2   1 
ATOM   12699 C CD1   . ILE B 1 474  ? -13.351 16.829  122.460 1.00 25.02 ?  472  ILE B CD1   1 
ATOM   12700 N N     . TYR B 1 475  ? -9.767  16.372  117.727 1.00 19.09 ?  473  TYR B N     1 
ATOM   12701 C CA    . TYR B 1 475  ? -8.423  16.628  117.216 1.00 17.51 ?  473  TYR B CA    1 
ATOM   12702 C C     . TYR B 1 475  ? -7.870  17.801  118.015 1.00 18.81 ?  473  TYR B C     1 
ATOM   12703 O O     . TYR B 1 475  ? -8.367  18.926  117.901 1.00 21.48 ?  473  TYR B O     1 
ATOM   12704 C CB    . TYR B 1 475  ? -8.509  16.916  115.718 1.00 19.48 ?  473  TYR B CB    1 
ATOM   12705 C CG    . TYR B 1 475  ? -7.220  17.044  114.932 1.00 22.58 ?  473  TYR B CG    1 
ATOM   12706 C CD1   . TYR B 1 475  ? -6.442  15.931  114.620 1.00 21.22 ?  473  TYR B CD1   1 
ATOM   12707 C CD2   . TYR B 1 475  ? -6.825  18.272  114.438 1.00 32.49 ?  473  TYR B CD2   1 
ATOM   12708 C CE1   . TYR B 1 475  ? -5.274  16.056  113.870 1.00 20.86 ?  473  TYR B CE1   1 
ATOM   12709 C CE2   . TYR B 1 475  ? -5.669  18.402  113.691 1.00 36.61 ?  473  TYR B CE2   1 
ATOM   12710 C CZ    . TYR B 1 475  ? -4.900  17.292  113.417 1.00 26.22 ?  473  TYR B CZ    1 
ATOM   12711 O OH    . TYR B 1 475  ? -3.747  17.444  112.673 1.00 34.40 ?  473  TYR B OH    1 
ATOM   12712 N N     . ALA B 1 476  ? -6.865  17.542  118.845 1.00 17.95 ?  474  ALA B N     1 
ATOM   12713 C CA    . ALA B 1 476  ? -6.443  18.498  119.866 1.00 21.64 ?  474  ALA B CA    1 
ATOM   12714 C C     . ALA B 1 476  ? -5.037  19.027  119.622 1.00 18.47 ?  474  ALA B C     1 
ATOM   12715 O O     . ALA B 1 476  ? -4.050  18.324  119.903 1.00 19.90 ?  474  ALA B O     1 
ATOM   12716 C CB    . ALA B 1 476  ? -6.530  17.837  121.240 1.00 21.31 ?  474  ALA B CB    1 
ATOM   12717 N N     . PRO B 1 477  ? -4.888  20.258  119.131 1.00 19.92 ?  475  PRO B N     1 
ATOM   12718 C CA    . PRO B 1 477  ? -3.544  20.818  118.956 1.00 21.67 ?  475  PRO B CA    1 
ATOM   12719 C C     . PRO B 1 477  ? -2.865  21.045  120.293 1.00 19.97 ?  475  PRO B C     1 
ATOM   12720 O O     . PRO B 1 477  ? -3.493  21.422  121.285 1.00 19.96 ?  475  PRO B O     1 
ATOM   12721 C CB    . PRO B 1 477  ? -3.798  22.144  118.231 1.00 19.49 ?  475  PRO B CB    1 
ATOM   12722 C CG    . PRO B 1 477  ? -5.187  22.024  117.659 1.00 20.93 ?  475  PRO B CG    1 
ATOM   12723 C CD    . PRO B 1 477  ? -5.930  21.173  118.639 1.00 18.98 ?  475  PRO B CD    1 
ATOM   12724 N N     . VAL B 1 478  ? -1.556  20.815  120.311 1.00 18.58 ?  476  VAL B N     1 
ATOM   12725 C CA    . VAL B 1 478  ? -0.748  20.967  121.509 1.00 17.42 ?  476  VAL B CA    1 
ATOM   12726 C C     . VAL B 1 478  ? 0.516   21.702  121.101 1.00 20.39 ?  476  VAL B C     1 
ATOM   12727 O O     . VAL B 1 478  ? 1.226   21.250  120.197 1.00 23.75 ?  476  VAL B O     1 
ATOM   12728 C CB    . VAL B 1 478  ? -0.401  19.614  122.154 1.00 17.63 ?  476  VAL B CB    1 
ATOM   12729 C CG1   . VAL B 1 478  ? 0.431   19.823  123.405 1.00 24.49 ?  476  VAL B CG1   1 
ATOM   12730 C CG2   . VAL B 1 478  ? -1.679  18.817  122.456 1.00 22.01 ?  476  VAL B CG2   1 
ATOM   12731 N N     . GLY B 1 479  ? 0.784   22.835  121.734 1.00 24.02 ?  477  GLY B N     1 
ATOM   12732 C CA    . GLY B 1 479  ? 2.013   23.533  121.429 1.00 24.00 ?  477  GLY B CA    1 
ATOM   12733 C C     . GLY B 1 479  ? 2.022   24.948  121.951 1.00 22.99 ?  477  GLY B C     1 
ATOM   12734 O O     . GLY B 1 479  ? 1.022   25.472  122.461 1.00 23.83 ?  477  GLY B O     1 
ATOM   12735 N N     . THR B 1 480  ? 3.199   25.556  121.810 1.00 28.77 ?  478  THR B N     1 
ATOM   12736 C CA    . THR B 1 480  ? 3.469   26.925  122.208 1.00 30.86 ?  478  THR B CA    1 
ATOM   12737 C C     . THR B 1 480  ? 2.803   27.908  121.250 1.00 26.44 ?  478  THR B C     1 
ATOM   12738 O O     . THR B 1 480  ? 2.279   27.543  120.196 1.00 26.16 ?  478  THR B O     1 
ATOM   12739 C CB    . THR B 1 480  ? 4.975   27.183  122.220 1.00 29.06 ?  478  THR B CB    1 
ATOM   12740 O OG1   . THR B 1 480  ? 5.480   27.045  120.886 1.00 32.99 ?  478  THR B OG1   1 
ATOM   12741 C CG2   . THR B 1 480  ? 5.674   26.184  123.121 1.00 30.19 ?  478  THR B CG2   1 
ATOM   12742 N N     . HIS B 1 481  ? 2.847   29.185  121.631 1.00 31.48 ?  479  HIS B N     1 
ATOM   12743 C CA    . HIS B 1 481  ? 2.303   30.229  120.770 1.00 29.90 ?  479  HIS B CA    1 
ATOM   12744 C C     . HIS B 1 481  ? 2.957   30.217  119.396 1.00 29.02 ?  479  HIS B C     1 
ATOM   12745 O O     . HIS B 1 481  ? 2.267   30.309  118.375 1.00 29.08 ?  479  HIS B O     1 
ATOM   12746 C CB    . HIS B 1 481  ? 2.474   31.591  121.436 1.00 27.94 ?  479  HIS B CB    1 
ATOM   12747 C CG    . HIS B 1 481  ? 1.630   31.768  122.654 1.00 31.73 ?  479  HIS B CG    1 
ATOM   12748 N ND1   . HIS B 1 481  ? 1.523   32.971  123.320 1.00 34.06 ?  479  HIS B ND1   1 
ATOM   12749 C CD2   . HIS B 1 481  ? 0.847   30.893  123.328 1.00 29.29 ?  479  HIS B CD2   1 
ATOM   12750 C CE1   . HIS B 1 481  ? 0.709   32.829  124.350 1.00 36.64 ?  479  HIS B CE1   1 
ATOM   12751 N NE2   . HIS B 1 481  ? 0.288   31.577  124.380 1.00 33.84 ?  479  HIS B NE2   1 
ATOM   12752 N N     . GLU B 1 482  ? 4.285   30.086  119.346 1.00 32.08 ?  480  GLU B N     1 
ATOM   12753 C CA    . GLU B 1 482  ? 4.983   30.125  118.065 1.00 26.86 ?  480  GLU B CA    1 
ATOM   12754 C C     . GLU B 1 482  ? 4.503   29.016  117.141 1.00 30.53 ?  480  GLU B C     1 
ATOM   12755 O O     . GLU B 1 482  ? 4.248   29.250  115.952 1.00 29.59 ?  480  GLU B O     1 
ATOM   12756 C CB    . GLU B 1 482  ? 6.495   30.024  118.277 1.00 38.67 ?  480  GLU B CB    1 
ATOM   12757 C CG    . GLU B 1 482  ? 7.280   29.854  116.976 1.00 41.03 ?  480  GLU B CG    1 
ATOM   12758 C CD    . GLU B 1 482  ? 8.763   29.594  117.199 1.00 52.66 ?  480  GLU B CD    1 
ATOM   12759 O OE1   . GLU B 1 482  ? 9.224   29.693  118.358 1.00 56.71 ?  480  GLU B OE1   1 
ATOM   12760 O OE2   . GLU B 1 482  ? 9.467   29.288  116.210 1.00 54.55 ?  480  GLU B OE2   1 
ATOM   12761 N N     . THR B 1 483  ? 4.362   27.796  117.672 1.00 28.75 ?  481  THR B N     1 
ATOM   12762 C CA    . THR B 1 483  ? 3.988   26.671  116.821 1.00 30.60 ?  481  THR B CA    1 
ATOM   12763 C C     . THR B 1 483  ? 2.543   26.778  116.359 1.00 27.55 ?  481  THR B C     1 
ATOM   12764 O O     . THR B 1 483  ? 2.219   26.380  115.236 1.00 29.20 ?  481  THR B O     1 
ATOM   12765 C CB    . THR B 1 483  ? 4.204   25.345  117.550 1.00 30.18 ?  481  THR B CB    1 
ATOM   12766 O OG1   . THR B 1 483  ? 3.227   25.210  118.591 1.00 36.72 ?  481  THR B OG1   1 
ATOM   12767 C CG2   . THR B 1 483  ? 5.594   25.298  118.155 1.00 28.43 ?  481  THR B CG2   1 
ATOM   12768 N N     . LEU B 1 484  ? 1.650   27.283  117.215 1.00 27.65 ?  482  LEU B N     1 
ATOM   12769 C CA    . LEU B 1 484  ? 0.253   27.373  116.804 1.00 26.87 ?  482  LEU B CA    1 
ATOM   12770 C C     . LEU B 1 484  ? 0.046   28.494  115.792 1.00 26.04 ?  482  LEU B C     1 
ATOM   12771 O O     . LEU B 1 484  ? -0.779  28.364  114.880 1.00 25.64 ?  482  LEU B O     1 
ATOM   12772 C CB    . LEU B 1 484  ? -0.653  27.548  118.030 1.00 28.16 ?  482  LEU B CB    1 
ATOM   12773 C CG    . LEU B 1 484  ? -0.764  28.875  118.785 1.00 27.73 ?  482  LEU B CG    1 
ATOM   12774 C CD1   . LEU B 1 484  ? -1.816  29.786  118.158 1.00 28.29 ?  482  LEU B CD1   1 
ATOM   12775 C CD2   . LEU B 1 484  ? -1.088  28.638  120.253 1.00 31.82 ?  482  LEU B CD2   1 
ATOM   12776 N N     . LEU B 1 485  ? 0.809   29.583  115.911 1.00 27.49 ?  483  LEU B N     1 
ATOM   12777 C CA    . LEU B 1 485  ? 0.642   30.702  114.992 1.00 25.84 ?  483  LEU B CA    1 
ATOM   12778 C C     . LEU B 1 485  ? 1.157   30.390  113.592 1.00 29.21 ?  483  LEU B C     1 
ATOM   12779 O O     . LEU B 1 485  ? 0.772   31.076  112.640 1.00 26.83 ?  483  LEU B O     1 
ATOM   12780 C CB    . LEU B 1 485  ? 1.351   31.940  115.552 1.00 26.19 ?  483  LEU B CB    1 
ATOM   12781 C CG    . LEU B 1 485  ? 0.671   32.668  116.712 1.00 27.38 ?  483  LEU B CG    1 
ATOM   12782 C CD1   . LEU B 1 485  ? 1.554   33.781  117.232 1.00 28.14 ?  483  LEU B CD1   1 
ATOM   12783 C CD2   . LEU B 1 485  ? -0.673  33.224  116.268 1.00 28.19 ?  483  LEU B CD2   1 
ATOM   12784 N N     . ALA B 1 486  ? 1.988   29.355  113.442 1.00 25.54 ?  484  ALA B N     1 
ATOM   12785 C CA    . ALA B 1 486  ? 2.685   29.133  112.178 1.00 26.80 ?  484  ALA B CA    1 
ATOM   12786 C C     . ALA B 1 486  ? 1.721   28.822  111.036 1.00 27.39 ?  484  ALA B C     1 
ATOM   12787 O O     . ALA B 1 486  ? 1.920   29.283  109.907 1.00 33.84 ?  484  ALA B O     1 
ATOM   12788 C CB    . ALA B 1 486  ? 3.707   28.006  112.335 1.00 29.60 ?  484  ALA B CB    1 
ATOM   12789 N N     . TYR B 1 487  ? 0.674   28.038  111.304 1.00 27.56 ?  485  TYR B N     1 
ATOM   12790 C CA    . TYR B 1 487  ? -0.278  27.652  110.267 1.00 27.22 ?  485  TYR B CA    1 
ATOM   12791 C C     . TYR B 1 487  ? -1.711  27.876  110.727 1.00 30.23 ?  485  TYR B C     1 
ATOM   12792 O O     . TYR B 1 487  ? -2.644  27.239  110.217 1.00 27.05 ?  485  TYR B O     1 
ATOM   12793 C CB    . TYR B 1 487  ? -0.056  26.201  109.836 1.00 29.34 ?  485  TYR B CB    1 
ATOM   12794 C CG    . TYR B 1 487  ? 1.275   26.012  109.139 1.00 30.32 ?  485  TYR B CG    1 
ATOM   12795 C CD1   . TYR B 1 487  ? 1.441   26.389  107.808 1.00 33.78 ?  485  TYR B CD1   1 
ATOM   12796 C CD2   . TYR B 1 487  ? 2.376   25.503  109.823 1.00 33.23 ?  485  TYR B CD2   1 
ATOM   12797 C CE1   . TYR B 1 487  ? 2.660   26.239  107.165 1.00 34.90 ?  485  TYR B CE1   1 
ATOM   12798 C CE2   . TYR B 1 487  ? 3.599   25.352  109.189 1.00 34.61 ?  485  TYR B CE2   1 
ATOM   12799 C CZ    . TYR B 1 487  ? 3.735   25.720  107.864 1.00 40.28 ?  485  TYR B CZ    1 
ATOM   12800 O OH    . TYR B 1 487  ? 4.952   25.567  107.237 1.00 46.91 ?  485  TYR B OH    1 
ATOM   12801 N N     . LEU B 1 488  ? -1.902  28.793  111.681 1.00 28.97 ?  486  LEU B N     1 
ATOM   12802 C CA    . LEU B 1 488  ? -3.250  29.100  112.142 1.00 24.66 ?  486  LEU B CA    1 
ATOM   12803 C C     . LEU B 1 488  ? -4.121  29.649  111.015 1.00 24.49 ?  486  LEU B C     1 
ATOM   12804 O O     . LEU B 1 488  ? -5.334  29.420  111.008 1.00 26.36 ?  486  LEU B O     1 
ATOM   12805 C CB    . LEU B 1 488  ? -3.203  30.080  113.319 1.00 25.47 ?  486  LEU B CB    1 
ATOM   12806 C CG    . LEU B 1 488  ? -4.579  30.375  113.939 1.00 25.60 ?  486  LEU B CG    1 
ATOM   12807 C CD1   . LEU B 1 488  ? -5.332  29.077  114.245 1.00 30.09 ?  486  LEU B CD1   1 
ATOM   12808 C CD2   . LEU B 1 488  ? -4.475  31.249  115.184 1.00 25.67 ?  486  LEU B CD2   1 
ATOM   12809 N N     . VAL B 1 489  ? -3.533  30.361  110.047 1.00 23.33 ?  487  VAL B N     1 
ATOM   12810 C CA    . VAL B 1 489  ? -4.336  30.883  108.941 1.00 21.99 ?  487  VAL B CA    1 
ATOM   12811 C C     . VAL B 1 489  ? -5.019  29.749  108.192 1.00 25.31 ?  487  VAL B C     1 
ATOM   12812 O O     . VAL B 1 489  ? -6.219  29.812  107.907 1.00 23.49 ?  487  VAL B O     1 
ATOM   12813 C CB    . VAL B 1 489  ? -3.478  31.742  107.993 1.00 20.79 ?  487  VAL B CB    1 
ATOM   12814 C CG1   . VAL B 1 489  ? -4.223  31.981  106.667 1.00 22.64 ?  487  VAL B CG1   1 
ATOM   12815 C CG2   . VAL B 1 489  ? -3.120  33.070  108.667 1.00 27.04 ?  487  VAL B CG2   1 
ATOM   12816 N N     . ARG B 1 490  ? -4.267  28.698  107.847 1.00 24.61 ?  488  ARG B N     1 
ATOM   12817 C CA    . ARG B 1 490  ? -4.876  27.583  107.127 1.00 26.00 ?  488  ARG B CA    1 
ATOM   12818 C C     . ARG B 1 490  ? -5.993  26.953  107.950 1.00 25.11 ?  488  ARG B C     1 
ATOM   12819 O O     . ARG B 1 490  ? -7.036  26.571  107.405 1.00 24.84 ?  488  ARG B O     1 
ATOM   12820 C CB    . ARG B 1 490  ? -3.816  26.542  106.751 1.00 24.38 ?  488  ARG B CB    1 
ATOM   12821 C CG    . ARG B 1 490  ? -4.368  25.327  105.996 1.00 25.61 ?  488  ARG B CG    1 
ATOM   12822 C CD    . ARG B 1 490  ? -3.275  24.284  105.797 1.00 26.56 ?  488  ARG B CD    1 
ATOM   12823 N NE    . ARG B 1 490  ? -2.891  23.655  107.056 1.00 27.79 ?  488  ARG B NE    1 
ATOM   12824 C CZ    . ARG B 1 490  ? -1.648  23.316  107.377 1.00 28.55 ?  488  ARG B CZ    1 
ATOM   12825 N NH1   . ARG B 1 490  ? -0.624  23.615  106.589 1.00 24.26 ?  488  ARG B NH1   1 
ATOM   12826 N NH2   . ARG B 1 490  ? -1.427  22.664  108.516 1.00 27.70 ?  488  ARG B NH2   1 
ATOM   12827 N N     . ARG B 1 491  ? -5.806  26.877  109.272 1.00 27.07 ?  489  ARG B N     1 
ATOM   12828 C CA    . ARG B 1 491  ? -6.829  26.297  110.135 1.00 24.21 ?  489  ARG B CA    1 
ATOM   12829 C C     . ARG B 1 491  ? -8.065  27.181  110.215 1.00 28.77 ?  489  ARG B C     1 
ATOM   12830 O O     . ARG B 1 491  ? -9.193  26.671  110.253 1.00 28.77 ?  489  ARG B O     1 
ATOM   12831 C CB    . ARG B 1 491  ? -6.273  26.065  111.537 1.00 28.96 ?  489  ARG B CB    1 
ATOM   12832 C CG    . ARG B 1 491  ? -7.253  25.330  112.431 1.00 33.11 ?  489  ARG B CG    1 
ATOM   12833 C CD    . ARG B 1 491  ? -6.948  23.843  112.439 1.00 35.09 ?  489  ARG B CD    1 
ATOM   12834 N NE    . ARG B 1 491  ? -5.879  23.566  113.388 1.00 40.03 ?  489  ARG B NE    1 
ATOM   12835 C CZ    . ARG B 1 491  ? -5.224  22.419  113.477 1.00 38.67 ?  489  ARG B CZ    1 
ATOM   12836 N NH1   . ARG B 1 491  ? -5.490  21.406  112.666 1.00 38.33 ?  489  ARG B NH1   1 
ATOM   12837 N NH2   . ARG B 1 491  ? -4.273  22.287  114.399 1.00 35.71 ?  489  ARG B NH2   1 
ATOM   12838 N N     . LEU B 1 492  ? -7.877  28.505  110.264 1.00 25.69 ?  490  LEU B N     1 
ATOM   12839 C CA    . LEU B 1 492  ? -9.022  29.409  110.341 1.00 26.88 ?  490  LEU B CA    1 
ATOM   12840 C C     . LEU B 1 492  ? -9.825  29.419  109.045 1.00 28.63 ?  490  LEU B C     1 
ATOM   12841 O O     . LEU B 1 492  ? -11.058 29.532  109.080 1.00 30.74 ?  490  LEU B O     1 
ATOM   12842 C CB    . LEU B 1 492  ? -8.554  30.823  110.696 1.00 30.86 ?  490  LEU B CB    1 
ATOM   12843 C CG    . LEU B 1 492  ? -7.923  30.964  112.083 1.00 29.09 ?  490  LEU B CG    1 
ATOM   12844 C CD1   . LEU B 1 492  ? -7.262  32.334  112.261 1.00 32.04 ?  490  LEU B CD1   1 
ATOM   12845 C CD2   . LEU B 1 492  ? -8.972  30.733  113.163 1.00 30.15 ?  490  LEU B CD2   1 
ATOM   12846 N N     . LEU B 1 493  ? -9.152  29.278  107.899 1.00 28.06 ?  491  LEU B N     1 
ATOM   12847 C CA    . LEU B 1 493  ? -9.862  29.222  106.625 1.00 25.31 ?  491  LEU B CA    1 
ATOM   12848 C C     . LEU B 1 493  ? -10.717 27.965  106.500 1.00 29.13 ?  491  LEU B C     1 
ATOM   12849 O O     . LEU B 1 493  ? -11.721 27.979  105.778 1.00 30.23 ?  491  LEU B O     1 
ATOM   12850 C CB    . LEU B 1 493  ? -8.864  29.296  105.464 1.00 27.92 ?  491  LEU B CB    1 
ATOM   12851 C CG    . LEU B 1 493  ? -8.679  30.664  104.806 1.00 32.93 ?  491  LEU B CG    1 
ATOM   12852 C CD1   . LEU B 1 493  ? -8.406  31.707  105.862 1.00 34.71 ?  491  LEU B CD1   1 
ATOM   12853 C CD2   . LEU B 1 493  ? -7.558  30.649  103.769 1.00 29.93 ?  491  LEU B CD2   1 
ATOM   12854 N N     . GLU B 1 494  ? -10.329 26.870  107.172 1.00 29.14 ?  492  GLU B N     1 
ATOM   12855 C CA    . GLU B 1 494  ? -11.096 25.624  107.088 1.00 26.96 ?  492  GLU B CA    1 
ATOM   12856 C C     . GLU B 1 494  ? -12.565 25.850  107.410 1.00 30.36 ?  492  GLU B C     1 
ATOM   12857 O O     . GLU B 1 494  ? -13.451 25.344  106.708 1.00 29.36 ?  492  GLU B O     1 
ATOM   12858 C CB    . GLU B 1 494  ? -10.516 24.568  108.038 1.00 27.12 ?  492  GLU B CB    1 
ATOM   12859 C CG    . GLU B 1 494  ? -9.171  23.967  107.606 1.00 24.53 ?  492  GLU B CG    1 
ATOM   12860 C CD    . GLU B 1 494  ? -8.533  23.144  108.713 1.00 30.18 ?  492  GLU B CD    1 
ATOM   12861 O OE1   . GLU B 1 494  ? -9.222  22.833  109.715 1.00 33.19 ?  492  GLU B OE1   1 
ATOM   12862 O OE2   . GLU B 1 494  ? -7.337  22.812  108.592 1.00 36.03 ?  492  GLU B OE2   1 
ATOM   12863 N N     . ASN B 1 495  ? -12.844 26.619  108.464 1.00 28.09 ?  493  ASN B N     1 
ATOM   12864 C CA    . ASN B 1 495  ? -14.210 26.870  108.900 1.00 31.76 ?  493  ASN B CA    1 
ATOM   12865 C C     . ASN B 1 495  ? -14.613 28.338  108.792 1.00 34.32 ?  493  ASN B C     1 
ATOM   12866 O O     . ASN B 1 495  ? -15.697 28.707  109.268 1.00 32.64 ?  493  ASN B O     1 
ATOM   12867 C CB    . ASN B 1 495  ? -14.394 26.369  110.338 1.00 27.91 ?  493  ASN B CB    1 
ATOM   12868 C CG    . ASN B 1 495  ? -14.057 24.886  110.484 1.00 30.48 ?  493  ASN B CG    1 
ATOM   12869 O OD1   . ASN B 1 495  ? -14.767 24.019  109.954 1.00 27.50 ?  493  ASN B OD1   1 
ATOM   12870 N ND2   . ASN B 1 495  ? -12.959 24.592  111.187 1.00 27.29 ?  493  ASN B ND2   1 
ATOM   12871 N N     . GLY B 1 496  ? -13.792 29.182  108.163 1.00 36.57 ?  494  GLY B N     1 
ATOM   12872 C CA    . GLY B 1 496  ? -14.078 30.605  108.113 1.00 36.90 ?  494  GLY B CA    1 
ATOM   12873 C C     . GLY B 1 496  ? -14.313 31.209  106.738 1.00 39.35 ?  494  GLY B C     1 
ATOM   12874 O O     . GLY B 1 496  ? -14.474 32.430  106.623 1.00 40.26 ?  494  GLY B O     1 
ATOM   12875 N N     . ALA B 1 497  ? -14.340 30.385  105.689 1.00 35.75 ?  495  ALA B N     1 
ATOM   12876 C CA    . ALA B 1 497  ? -14.600 30.884  104.348 1.00 34.68 ?  495  ALA B CA    1 
ATOM   12877 C C     . ALA B 1 497  ? -16.103 31.010  104.103 1.00 34.45 ?  495  ALA B C     1 
ATOM   12878 O O     . ALA B 1 497  ? -16.929 30.448  104.824 1.00 34.99 ?  495  ALA B O     1 
ATOM   12879 C CB    . ALA B 1 497  ? -13.970 29.971  103.297 1.00 32.95 ?  495  ALA B CB    1 
ATOM   12880 N N     . ASN B 1 498  ? -16.453 31.748  103.046 1.00 35.14 ?  496  ASN B N     1 
ATOM   12881 C CA    . ASN B 1 498  ? -17.853 32.084  102.802 1.00 33.52 ?  496  ASN B CA    1 
ATOM   12882 C C     . ASN B 1 498  ? -18.717 30.844  102.582 1.00 36.17 ?  496  ASN B C     1 
ATOM   12883 O O     . ASN B 1 498  ? -19.903 30.839  102.934 1.00 33.38 ?  496  ASN B O     1 
ATOM   12884 C CB    . ASN B 1 498  ? -17.952 33.027  101.603 1.00 38.84 ?  496  ASN B CB    1 
ATOM   12885 C CG    . ASN B 1 498  ? -19.379 33.240  101.145 1.00 45.64 ?  496  ASN B CG    1 
ATOM   12886 O OD1   . ASN B 1 498  ? -19.860 32.561  100.236 1.00 46.39 ?  496  ASN B OD1   1 
ATOM   12887 N ND2   . ASN B 1 498  ? -20.069 34.184  101.778 1.00 52.00 ?  496  ASN B ND2   1 
ATOM   12888 N N     . SER B 1 499  ? -18.153 29.794  102.002 1.00 31.14 ?  497  SER B N     1 
ATOM   12889 C CA    . SER B 1 499  ? -18.875 28.552  101.771 1.00 29.23 ?  497  SER B CA    1 
ATOM   12890 C C     . SER B 1 499  ? -18.750 27.567  102.927 1.00 24.84 ?  497  SER B C     1 
ATOM   12891 O O     . SER B 1 499  ? -19.341 26.484  102.861 1.00 30.54 ?  497  SER B O     1 
ATOM   12892 C CB    . SER B 1 499  ? -18.368 27.895  100.485 1.00 34.61 ?  497  SER B CB    1 
ATOM   12893 O OG    . SER B 1 499  ? -16.975 27.663  100.594 1.00 34.79 ?  497  SER B OG    1 
ATOM   12894 N N     . SER B 1 500  ? -17.997 27.907  103.972 1.00 26.63 ?  498  SER B N     1 
ATOM   12895 C CA    . SER B 1 500  ? -17.816 27.000  105.099 1.00 23.47 ?  498  SER B CA    1 
ATOM   12896 C C     . SER B 1 500  ? -19.087 26.917  105.928 1.00 25.47 ?  498  SER B C     1 
ATOM   12897 O O     . SER B 1 500  ? -19.772 27.921  106.133 1.00 28.64 ?  498  SER B O     1 
ATOM   12898 C CB    . SER B 1 500  ? -16.666 27.464  105.991 1.00 29.08 ?  498  SER B CB    1 
ATOM   12899 O OG    . SER B 1 500  ? -15.430 27.391  105.307 1.00 30.58 ?  498  SER B OG    1 
ATOM   12900 N N     . PHE B 1 501  ? -19.398 25.709  106.403 1.00 22.07 ?  499  PHE B N     1 
ATOM   12901 C CA    . PHE B 1 501  ? -20.586 25.535  107.238 1.00 23.49 ?  499  PHE B CA    1 
ATOM   12902 C C     . PHE B 1 501  ? -20.533 26.424  108.477 1.00 30.52 ?  499  PHE B C     1 
ATOM   12903 O O     . PHE B 1 501  ? -21.538 27.045  108.843 1.00 26.36 ?  499  PHE B O     1 
ATOM   12904 C CB    . PHE B 1 501  ? -20.738 24.065  107.637 1.00 23.71 ?  499  PHE B CB    1 
ATOM   12905 C CG    . PHE B 1 501  ? -21.933 23.791  108.507 1.00 24.63 ?  499  PHE B CG    1 
ATOM   12906 C CD1   . PHE B 1 501  ? -21.836 23.883  109.886 1.00 29.02 ?  499  PHE B CD1   1 
ATOM   12907 C CD2   . PHE B 1 501  ? -23.146 23.427  107.944 1.00 28.04 ?  499  PHE B CD2   1 
ATOM   12908 C CE1   . PHE B 1 501  ? -22.935 23.628  110.689 1.00 27.59 ?  499  PHE B CE1   1 
ATOM   12909 C CE2   . PHE B 1 501  ? -24.252 23.167  108.747 1.00 26.98 ?  499  PHE B CE2   1 
ATOM   12910 C CZ    . PHE B 1 501  ? -24.141 23.270  110.113 1.00 28.32 ?  499  PHE B CZ    1 
ATOM   12911 N N     . VAL B 1 502  ? -19.375 26.502  109.137 1.00 27.02 ?  500  VAL B N     1 
ATOM   12912 C CA    . VAL B 1 502  ? -19.305 27.236  110.399 1.00 29.43 ?  500  VAL B CA    1 
ATOM   12913 C C     . VAL B 1 502  ? -19.542 28.727  110.170 1.00 34.30 ?  500  VAL B C     1 
ATOM   12914 O O     . VAL B 1 502  ? -20.184 29.400  110.987 1.00 37.78 ?  500  VAL B O     1 
ATOM   12915 C CB    . VAL B 1 502  ? -17.962 26.958  111.102 1.00 31.18 ?  500  VAL B CB    1 
ATOM   12916 C CG1   . VAL B 1 502  ? -17.798 27.845  112.327 1.00 34.08 ?  500  VAL B CG1   1 
ATOM   12917 C CG2   . VAL B 1 502  ? -17.880 25.492  111.513 1.00 28.39 ?  500  VAL B CG2   1 
ATOM   12918 N N     . HIS B 1 503  ? -19.059 29.260  109.044 1.00 28.51 ?  501  HIS B N     1 
ATOM   12919 C CA    . HIS B 1 503  ? -19.302 30.666  108.726 1.00 33.89 ?  501  HIS B CA    1 
ATOM   12920 C C     . HIS B 1 503  ? -20.766 30.911  108.374 1.00 34.47 ?  501  HIS B C     1 
ATOM   12921 O O     . HIS B 1 503  ? -21.359 31.907  108.810 1.00 32.41 ?  501  HIS B O     1 
ATOM   12922 C CB    . HIS B 1 503  ? -18.389 31.106  107.578 1.00 36.08 ?  501  HIS B CB    1 
ATOM   12923 C CG    . HIS B 1 503  ? -18.599 32.524  107.138 1.00 37.12 ?  501  HIS B CG    1 
ATOM   12924 N ND1   . HIS B 1 503  ? -19.494 32.874  106.149 1.00 39.07 ?  501  HIS B ND1   1 
ATOM   12925 C CD2   . HIS B 1 503  ? -18.024 33.680  107.549 1.00 40.20 ?  501  HIS B CD2   1 
ATOM   12926 C CE1   . HIS B 1 503  ? -19.462 34.182  105.970 1.00 36.96 ?  501  HIS B CE1   1 
ATOM   12927 N NE2   . HIS B 1 503  ? -18.578 34.695  106.807 1.00 38.68 ?  501  HIS B NE2   1 
ATOM   12928 N N     . ARG B 1 504  ? -21.372 30.005  107.604 1.00 29.01 ?  502  ARG B N     1 
ATOM   12929 C CA    . ARG B 1 504  ? -22.756 30.190  107.180 1.00 31.82 ?  502  ARG B CA    1 
ATOM   12930 C C     . ARG B 1 504  ? -23.730 30.102  108.347 1.00 36.01 ?  502  ARG B C     1 
ATOM   12931 O O     . ARG B 1 504  ? -24.768 30.775  108.339 1.00 34.37 ?  502  ARG B O     1 
ATOM   12932 C CB    . ARG B 1 504  ? -23.118 29.157  106.117 1.00 32.50 ?  502  ARG B CB    1 
ATOM   12933 C CG    . ARG B 1 504  ? -22.430 29.409  104.796 1.00 34.01 ?  502  ARG B CG    1 
ATOM   12934 C CD    . ARG B 1 504  ? -22.441 28.184  103.899 1.00 31.50 ?  502  ARG B CD    1 
ATOM   12935 N NE    . ARG B 1 504  ? -23.773 27.634  103.676 1.00 34.36 ?  502  ARG B NE    1 
ATOM   12936 C CZ    . ARG B 1 504  ? -24.704 28.185  102.907 1.00 29.96 ?  502  ARG B CZ    1 
ATOM   12937 N NH1   . ARG B 1 504  ? -24.532 29.374  102.352 1.00 37.46 ?  502  ARG B NH1   1 
ATOM   12938 N NH2   . ARG B 1 504  ? -25.837 27.524  102.687 1.00 36.80 ?  502  ARG B NH2   1 
ATOM   12939 N N     . ILE B 1 505  ? -23.427 29.281  109.353 1.00 28.76 ?  503  ILE B N     1 
ATOM   12940 C CA    . ILE B 1 505  ? -24.356 29.161  110.464 1.00 31.96 ?  503  ILE B CA    1 
ATOM   12941 C C     . ILE B 1 505  ? -24.298 30.393  111.360 1.00 35.12 ?  503  ILE B C     1 
ATOM   12942 O O     . ILE B 1 505  ? -25.271 30.695  112.057 1.00 31.31 ?  503  ILE B O     1 
ATOM   12943 C CB    . ILE B 1 505  ? -24.087 27.854  111.231 1.00 29.43 ?  503  ILE B CB    1 
ATOM   12944 C CG1   . ILE B 1 505  ? -25.223 27.589  112.215 1.00 37.78 ?  503  ILE B CG1   1 
ATOM   12945 C CG2   . ILE B 1 505  ? -22.766 27.920  111.942 1.00 31.78 ?  503  ILE B CG2   1 
ATOM   12946 C CD1   . ILE B 1 505  ? -25.466 26.129  112.497 1.00 38.08 ?  503  ILE B CD1   1 
ATOM   12947 N N     . ASN B 1 506  ? -23.199 31.142  111.330 1.00 32.86 ?  504  ASN B N     1 
ATOM   12948 C CA    . ASN B 1 506  ? -23.113 32.423  112.016 1.00 36.71 ?  504  ASN B CA    1 
ATOM   12949 C C     . ASN B 1 506  ? -23.609 33.581  111.160 1.00 38.04 ?  504  ASN B C     1 
ATOM   12950 O O     . ASN B 1 506  ? -23.501 34.738  111.577 1.00 39.56 ?  504  ASN B O     1 
ATOM   12951 C CB    . ASN B 1 506  ? -21.674 32.684  112.468 1.00 39.17 ?  504  ASN B CB    1 
ATOM   12952 C CG    . ASN B 1 506  ? -21.291 31.865  113.682 1.00 46.10 ?  504  ASN B CG    1 
ATOM   12953 O OD1   . ASN B 1 506  ? -22.035 31.806  114.663 1.00 53.02 ?  504  ASN B OD1   1 
ATOM   12954 N ND2   . ASN B 1 506  ? -20.134 31.215  113.619 1.00 49.74 ?  504  ASN B ND2   1 
ATOM   12955 N N     . ASP B 1 507  ? -24.142 33.295  109.974 1.00 40.65 ?  505  ASP B N     1 
ATOM   12956 C CA    . ASP B 1 507  ? -24.690 34.320  109.101 1.00 39.59 ?  505  ASP B CA    1 
ATOM   12957 C C     . ASP B 1 507  ? -26.206 34.304  109.212 1.00 45.10 ?  505  ASP B C     1 
ATOM   12958 O O     . ASP B 1 507  ? -26.837 33.336  108.761 1.00 42.89 ?  505  ASP B O     1 
ATOM   12959 C CB    . ASP B 1 507  ? -24.256 34.076  107.656 1.00 40.12 ?  505  ASP B CB    1 
ATOM   12960 C CG    . ASP B 1 507  ? -24.684 35.187  106.712 1.00 43.90 ?  505  ASP B CG    1 
ATOM   12961 O OD1   . ASP B 1 507  ? -25.512 36.041  107.095 1.00 44.74 ?  505  ASP B OD1   1 
ATOM   12962 O OD2   . ASP B 1 507  ? -24.177 35.205  105.573 1.00 46.00 ?  505  ASP B OD2   1 
ATOM   12963 N N     . PRO B 1 508  ? -26.834 35.335  109.785 1.00 48.60 ?  506  PRO B N     1 
ATOM   12964 C CA    . PRO B 1 508  ? -28.300 35.325  109.913 1.00 48.96 ?  506  PRO B CA    1 
ATOM   12965 C C     . PRO B 1 508  ? -29.032 35.448  108.585 1.00 49.70 ?  506  PRO B C     1 
ATOM   12966 O O     . PRO B 1 508  ? -30.245 35.198  108.546 1.00 52.63 ?  506  PRO B O     1 
ATOM   12967 C CB    . PRO B 1 508  ? -28.580 36.534  110.814 1.00 52.20 ?  506  PRO B CB    1 
ATOM   12968 C CG    . PRO B 1 508  ? -27.445 37.462  110.539 1.00 53.83 ?  506  PRO B CG    1 
ATOM   12969 C CD    . PRO B 1 508  ? -26.241 36.580  110.305 1.00 47.79 ?  506  PRO B CD    1 
ATOM   12970 N N     . LYS B 1 509  ? -28.344 35.821  107.506 1.00 47.96 ?  507  LYS B N     1 
ATOM   12971 C CA    . LYS B 1 509  ? -28.945 35.884  106.179 1.00 49.37 ?  507  LYS B CA    1 
ATOM   12972 C C     . LYS B 1 509  ? -29.014 34.520  105.491 1.00 49.43 ?  507  LYS B C     1 
ATOM   12973 O O     . LYS B 1 509  ? -29.415 34.452  104.323 1.00 55.03 ?  507  LYS B O     1 
ATOM   12974 C CB    . LYS B 1 509  ? -28.173 36.873  105.302 1.00 46.22 ?  507  LYS B CB    1 
ATOM   12975 N N     . VAL B 1 510  ? -28.633 33.445  106.177 1.00 46.83 ?  508  VAL B N     1 
ATOM   12976 C CA    . VAL B 1 510  ? -28.711 32.087  105.649 1.00 42.94 ?  508  VAL B CA    1 
ATOM   12977 C C     . VAL B 1 510  ? -29.739 31.328  106.474 1.00 42.76 ?  508  VAL B C     1 
ATOM   12978 O O     . VAL B 1 510  ? -29.618 31.241  107.703 1.00 42.39 ?  508  VAL B O     1 
ATOM   12979 C CB    . VAL B 1 510  ? -27.344 31.382  105.683 1.00 41.14 ?  508  VAL B CB    1 
ATOM   12980 C CG1   . VAL B 1 510  ? -27.466 29.946  105.176 1.00 38.03 ?  508  VAL B CG1   1 
ATOM   12981 C CG2   . VAL B 1 510  ? -26.318 32.164  104.870 1.00 37.93 ?  508  VAL B CG2   1 
ATOM   12982 N N     . SER B 1 511  ? -30.748 30.776  105.807 1.00 40.14 ?  509  SER B N     1 
ATOM   12983 C CA    . SER B 1 511  ? -31.823 30.099  106.514 1.00 37.62 ?  509  SER B CA    1 
ATOM   12984 C C     . SER B 1 511  ? -31.419 28.677  106.889 1.00 39.93 ?  509  SER B C     1 
ATOM   12985 O O     . SER B 1 511  ? -30.481 28.098  106.335 1.00 39.09 ?  509  SER B O     1 
ATOM   12986 C CB    . SER B 1 511  ? -33.093 30.062  105.664 1.00 42.40 ?  509  SER B CB    1 
ATOM   12987 O OG    . SER B 1 511  ? -32.998 29.078  104.647 1.00 46.75 ?  509  SER B OG    1 
ATOM   12988 N N     . ILE B 1 512  ? -32.151 28.110  107.849 1.00 35.79 ?  510  ILE B N     1 
ATOM   12989 C CA    . ILE B 1 512  ? -31.946 26.702  108.172 1.00 39.17 ?  510  ILE B CA    1 
ATOM   12990 C C     . ILE B 1 512  ? -32.302 25.833  106.972 1.00 42.62 ?  510  ILE B C     1 
ATOM   12991 O O     . ILE B 1 512  ? -31.666 24.798  106.734 1.00 38.57 ?  510  ILE B O     1 
ATOM   12992 C CB    . ILE B 1 512  ? -32.745 26.320  109.433 1.00 40.52 ?  510  ILE B CB    1 
ATOM   12993 C CG1   . ILE B 1 512  ? -32.237 27.132  110.628 1.00 41.04 ?  510  ILE B CG1   1 
ATOM   12994 C CG2   . ILE B 1 512  ? -32.628 24.829  109.726 1.00 38.35 ?  510  ILE B CG2   1 
ATOM   12995 C CD1   . ILE B 1 512  ? -32.871 26.760  111.945 1.00 43.43 ?  510  ILE B CD1   1 
ATOM   12996 N N     . ASP B 1 513  ? -33.292 26.254  106.177 1.00 39.40 ?  511  ASP B N     1 
ATOM   12997 C CA    . ASP B 1 513  ? -33.612 25.549  104.938 1.00 43.04 ?  511  ASP B CA    1 
ATOM   12998 C C     . ASP B 1 513  ? -32.392 25.452  104.031 1.00 41.42 ?  511  ASP B C     1 
ATOM   12999 O O     . ASP B 1 513  ? -32.085 24.380  103.494 1.00 38.80 ?  511  ASP B O     1 
ATOM   13000 C CB    . ASP B 1 513  ? -34.759 26.252  104.209 1.00 45.71 ?  511  ASP B CB    1 
ATOM   13001 C CG    . ASP B 1 513  ? -36.123 25.863  104.747 1.00 50.82 ?  511  ASP B CG    1 
ATOM   13002 O OD1   . ASP B 1 513  ? -36.288 24.709  105.203 1.00 53.42 ?  511  ASP B OD1   1 
ATOM   13003 O OD2   . ASP B 1 513  ? -37.037 26.712  104.707 1.00 53.26 ?  511  ASP B OD2   1 
ATOM   13004 N N     . GLU B 1 514  ? -31.687 26.570  103.841 1.00 38.22 ?  512  GLU B N     1 
ATOM   13005 C CA    . GLU B 1 514  ? -30.492 26.549  103.006 1.00 38.41 ?  512  GLU B CA    1 
ATOM   13006 C C     . GLU B 1 514  ? -29.410 25.651  103.597 1.00 37.40 ?  512  GLU B C     1 
ATOM   13007 O O     . GLU B 1 514  ? -28.677 24.993  102.853 1.00 36.00 ?  512  GLU B O     1 
ATOM   13008 C CB    . GLU B 1 514  ? -29.957 27.970  102.814 1.00 41.70 ?  512  GLU B CB    1 
ATOM   13009 C CG    . GLU B 1 514  ? -30.953 28.943  102.189 1.00 43.35 ?  512  GLU B CG    1 
ATOM   13010 C CD    . GLU B 1 514  ? -30.416 30.366  102.118 1.00 47.68 ?  512  GLU B CD    1 
ATOM   13011 O OE1   . GLU B 1 514  ? -29.472 30.614  101.338 1.00 56.06 ?  512  GLU B OE1   1 
ATOM   13012 O OE2   . GLU B 1 514  ? -30.933 31.238  102.850 1.00 48.75 ?  512  GLU B OE2   1 
ATOM   13013 N N     . LEU B 1 515  ? -29.304 25.592  104.926 1.00 35.56 ?  513  LEU B N     1 
ATOM   13014 C CA    . LEU B 1 515  ? -28.240 24.817  105.551 1.00 33.27 ?  513  LEU B CA    1 
ATOM   13015 C C     . LEU B 1 515  ? -28.493 23.316  105.511 1.00 35.59 ?  513  LEU B C     1 
ATOM   13016 O O     . LEU B 1 515  ? -27.532 22.538  105.573 1.00 34.01 ?  513  LEU B O     1 
ATOM   13017 C CB    . LEU B 1 515  ? -28.049 25.265  107.000 1.00 30.01 ?  513  LEU B CB    1 
ATOM   13018 C CG    . LEU B 1 515  ? -27.391 26.634  107.163 1.00 31.44 ?  513  LEU B CG    1 
ATOM   13019 C CD1   . LEU B 1 515  ? -27.555 27.134  108.590 1.00 33.27 ?  513  LEU B CD1   1 
ATOM   13020 C CD2   . LEU B 1 515  ? -25.922 26.560  106.792 1.00 32.73 ?  513  LEU B CD2   1 
ATOM   13021 N N     . ILE B 1 516  ? -29.752 22.890  105.411 1.00 32.27 ?  514  ILE B N     1 
ATOM   13022 C CA    . ILE B 1 516  ? -30.086 21.470  105.347 1.00 30.82 ?  514  ILE B CA    1 
ATOM   13023 C C     . ILE B 1 516  ? -30.328 21.008  103.914 1.00 32.49 ?  514  ILE B C     1 
ATOM   13024 O O     . ILE B 1 516  ? -30.732 19.861  103.699 1.00 35.31 ?  514  ILE B O     1 
ATOM   13025 C CB    . ILE B 1 516  ? -31.296 21.132  106.234 1.00 36.04 ?  514  ILE B CB    1 
ATOM   13026 C CG1   . ILE B 1 516  ? -32.587 21.701  105.640 1.00 35.52 ?  514  ILE B CG1   1 
ATOM   13027 C CG2   . ILE B 1 516  ? -31.081 21.654  107.647 1.00 38.67 ?  514  ILE B CG2   1 
ATOM   13028 C CD1   . ILE B 1 516  ? -33.826 21.338  106.436 1.00 43.12 ?  514  ILE B CD1   1 
ATOM   13029 N N     . ALA B 1 517  ? -30.100 21.877  102.932 1.00 32.90 ?  515  ALA B N     1 
ATOM   13030 C CA    . ALA B 1 517  ? -30.187 21.470  101.535 1.00 36.04 ?  515  ALA B CA    1 
ATOM   13031 C C     . ALA B 1 517  ? -29.266 20.283  101.272 1.00 33.29 ?  515  ALA B C     1 
ATOM   13032 O O     . ALA B 1 517  ? -28.147 20.219  101.787 1.00 33.14 ?  515  ALA B O     1 
ATOM   13033 C CB    . ALA B 1 517  ? -29.820 22.638  100.620 1.00 34.16 ?  515  ALA B CB    1 
ATOM   13034 N N     . ASP B 1 518  ? -29.758 19.324  100.483 1.00 31.18 ?  516  ASP B N     1 
ATOM   13035 C CA    . ASP B 1 518  ? -29.033 18.086  100.231 1.00 31.30 ?  516  ASP B CA    1 
ATOM   13036 C C     . ASP B 1 518  ? -28.096 18.303  99.051  1.00 30.37 ?  516  ASP B C     1 
ATOM   13037 O O     . ASP B 1 518  ? -28.574 18.451  97.918  1.00 28.57 ?  516  ASP B O     1 
ATOM   13038 C CB    . ASP B 1 518  ? -30.005 16.948  99.945  1.00 29.57 ?  516  ASP B CB    1 
ATOM   13039 C CG    . ASP B 1 518  ? -29.317 15.597  99.794  1.00 35.72 ?  516  ASP B CG    1 
ATOM   13040 O OD1   . ASP B 1 518  ? -28.072 15.543  99.720  1.00 30.56 ?  516  ASP B OD1   1 
ATOM   13041 O OD2   . ASP B 1 518  ? -30.030 14.572  99.746  1.00 35.84 ?  516  ASP B OD2   1 
ATOM   13042 N N     . PRO B 1 519  ? -26.777 18.317  99.253  1.00 26.82 ?  517  PRO B N     1 
ATOM   13043 C CA    . PRO B 1 519  ? -25.864 18.506  98.115  1.00 29.25 ?  517  PRO B CA    1 
ATOM   13044 C C     . PRO B 1 519  ? -26.053 17.477  97.016  1.00 29.66 ?  517  PRO B C     1 
ATOM   13045 O O     . PRO B 1 519  ? -25.851 17.800  95.838  1.00 27.93 ?  517  PRO B O     1 
ATOM   13046 C CB    . PRO B 1 519  ? -24.470 18.389  98.753  1.00 29.15 ?  517  PRO B CB    1 
ATOM   13047 C CG    . PRO B 1 519  ? -24.686 18.530  100.223 1.00 28.18 ?  517  PRO B CG    1 
ATOM   13048 C CD    . PRO B 1 519  ? -26.065 18.074  100.520 1.00 28.30 ?  517  PRO B CD    1 
ATOM   13049 N N     . VAL B 1 520  ? -26.442 16.248  97.370  1.00 27.44 ?  518  VAL B N     1 
ATOM   13050 C CA    . VAL B 1 520  ? -26.557 15.183  96.380  1.00 26.51 ?  518  VAL B CA    1 
ATOM   13051 C C     . VAL B 1 520  ? -27.666 15.500  95.389  1.00 30.62 ?  518  VAL B C     1 
ATOM   13052 O O     . VAL B 1 520  ? -27.501 15.336  94.173  1.00 29.41 ?  518  VAL B O     1 
ATOM   13053 C CB    . VAL B 1 520  ? -26.789 13.826  97.071  1.00 30.11 ?  518  VAL B CB    1 
ATOM   13054 C CG1   . VAL B 1 520  ? -26.899 12.715  96.031  1.00 29.33 ?  518  VAL B CG1   1 
ATOM   13055 C CG2   . VAL B 1 520  ? -25.663 13.532  98.063  1.00 29.21 ?  518  VAL B CG2   1 
ATOM   13056 N N     . GLU B 1 521  ? -28.803 15.980  95.888  1.00 29.67 ?  519  GLU B N     1 
ATOM   13057 C CA    . GLU B 1 521  ? -29.915 16.298  95.001  1.00 29.20 ?  519  GLU B CA    1 
ATOM   13058 C C     . GLU B 1 521  ? -29.699 17.609  94.261  1.00 32.41 ?  519  GLU B C     1 
ATOM   13059 O O     . GLU B 1 521  ? -30.235 17.787  93.162  1.00 34.11 ?  519  GLU B O     1 
ATOM   13060 C CB    . GLU B 1 521  ? -31.226 16.351  95.788  1.00 33.64 ?  519  GLU B CB    1 
ATOM   13061 C CG    . GLU B 1 521  ? -31.613 15.026  96.412  1.00 33.37 ?  519  GLU B CG    1 
ATOM   13062 C CD    . GLU B 1 521  ? -31.670 13.894  95.396  1.00 38.02 ?  519  GLU B CD    1 
ATOM   13063 O OE1   . GLU B 1 521  ? -32.104 14.131  94.246  1.00 39.08 ?  519  GLU B OE1   1 
ATOM   13064 O OE2   . GLU B 1 521  ? -31.278 12.761  95.747  1.00 40.95 ?  519  GLU B OE2   1 
ATOM   13065 N N     . VAL B 1 522  ? -28.937 18.536  94.836  1.00 32.79 ?  520  VAL B N     1 
ATOM   13066 C CA    . VAL B 1 522  ? -28.625 19.764  94.114  1.00 30.18 ?  520  VAL B CA    1 
ATOM   13067 C C     . VAL B 1 522  ? -27.736 19.456  92.915  1.00 33.03 ?  520  VAL B C     1 
ATOM   13068 O O     . VAL B 1 522  ? -28.001 19.904  91.794  1.00 32.83 ?  520  VAL B O     1 
ATOM   13069 C CB    . VAL B 1 522  ? -27.974 20.796  95.052  1.00 29.41 ?  520  VAL B CB    1 
ATOM   13070 C CG1   . VAL B 1 522  ? -27.582 22.033  94.276  1.00 32.47 ?  520  VAL B CG1   1 
ATOM   13071 C CG2   . VAL B 1 522  ? -28.923 21.148  96.187  1.00 35.21 ?  520  VAL B CG2   1 
ATOM   13072 N N     . VAL B 1 523  ? -26.677 18.670  93.132  1.00 26.93 ?  521  VAL B N     1 
ATOM   13073 C CA    . VAL B 1 523  ? -25.802 18.272  92.033  1.00 27.16 ?  521  VAL B CA    1 
ATOM   13074 C C     . VAL B 1 523  ? -26.573 17.465  90.995  1.00 29.61 ?  521  VAL B C     1 
ATOM   13075 O O     . VAL B 1 523  ? -26.379 17.640  89.785  1.00 27.57 ?  521  VAL B O     1 
ATOM   13076 C CB    . VAL B 1 523  ? -24.590 17.486  92.568  1.00 26.72 ?  521  VAL B CB    1 
ATOM   13077 C CG1   . VAL B 1 523  ? -23.827 16.836  91.416  1.00 25.08 ?  521  VAL B CG1   1 
ATOM   13078 C CG2   . VAL B 1 523  ? -23.679 18.403  93.374  1.00 27.22 ?  521  VAL B CG2   1 
ATOM   13079 N N     . ARG B 1 524  ? -27.452 16.565  91.448  1.00 28.80 ?  522  ARG B N     1 
ATOM   13080 C CA    . ARG B 1 524  ? -28.170 15.695  90.519  1.00 29.71 ?  522  ARG B CA    1 
ATOM   13081 C C     . ARG B 1 524  ? -28.999 16.499  89.532  1.00 33.54 ?  522  ARG B C     1 
ATOM   13082 O O     . ARG B 1 524  ? -29.137 16.102  88.367  1.00 33.90 ?  522  ARG B O     1 
ATOM   13083 C CB    . ARG B 1 524  ? -29.071 14.720  91.286  1.00 28.27 ?  522  ARG B CB    1 
ATOM   13084 C CG    . ARG B 1 524  ? -29.690 13.625  90.416  1.00 33.01 ?  522  ARG B CG    1 
ATOM   13085 C CD    . ARG B 1 524  ? -30.836 12.888  91.116  1.00 35.21 ?  522  ARG B CD    1 
ATOM   13086 N NE    . ARG B 1 524  ? -30.441 12.293  92.388  1.00 37.00 ?  522  ARG B NE    1 
ATOM   13087 C CZ    . ARG B 1 524  ? -29.744 11.170  92.508  1.00 33.27 ?  522  ARG B CZ    1 
ATOM   13088 N NH1   . ARG B 1 524  ? -29.324 10.499  91.447  1.00 35.61 ?  522  ARG B NH1   1 
ATOM   13089 N NH2   . ARG B 1 524  ? -29.450 10.715  93.723  1.00 35.47 ?  522  ARG B NH2   1 
ATOM   13090 N N     . ALA B 1 525  ? -29.531 17.641  89.962  1.00 31.95 ?  523  ALA B N     1 
ATOM   13091 C CA    . ALA B 1 525  ? -30.469 18.412  89.158  1.00 32.38 ?  523  ALA B CA    1 
ATOM   13092 C C     . ALA B 1 525  ? -29.805 19.506  88.333  1.00 34.68 ?  523  ALA B C     1 
ATOM   13093 O O     . ALA B 1 525  ? -30.510 20.265  87.659  1.00 37.51 ?  523  ALA B O     1 
ATOM   13094 C CB    . ALA B 1 525  ? -31.547 19.025  90.060  1.00 29.68 ?  523  ALA B CB    1 
ATOM   13095 N N     . MET B 1 526  ? -28.478 19.605  88.357  1.00 32.28 ?  524  MET B N     1 
ATOM   13096 C CA    A MET B 1 526  ? -27.790 20.610  87.564  0.55 33.94 ?  524  MET B CA    1 
ATOM   13097 C CA    B MET B 1 526  ? -27.808 20.619  87.564  0.45 33.94 ?  524  MET B CA    1 
ATOM   13098 C C     . MET B 1 526  ? -27.862 20.247  86.081  1.00 33.95 ?  524  MET B C     1 
ATOM   13099 O O     . MET B 1 526  ? -27.891 19.066  85.727  1.00 29.18 ?  524  MET B O     1 
ATOM   13100 C CB    A MET B 1 526  ? -26.332 20.729  88.002  0.55 33.18 ?  524  MET B CB    1 
ATOM   13101 C CB    B MET B 1 526  ? -26.362 20.787  88.025  0.45 33.19 ?  524  MET B CB    1 
ATOM   13102 C CG    A MET B 1 526  ? -26.161 21.326  89.385  0.55 34.66 ?  524  MET B CG    1 
ATOM   13103 C CG    B MET B 1 526  ? -26.249 21.129  89.505  0.45 34.45 ?  524  MET B CG    1 
ATOM   13104 S SD    A MET B 1 526  ? -26.827 22.999  89.472  0.55 39.92 ?  524  MET B SD    1 
ATOM   13105 S SD    B MET B 1 526  ? -24.608 21.653  90.037  0.45 34.09 ?  524  MET B SD    1 
ATOM   13106 C CE    A MET B 1 526  ? -25.755 23.854  88.323  0.55 34.97 ?  524  MET B CE    1 
ATOM   13107 C CE    B MET B 1 526  ? -24.547 23.327  89.408  0.45 34.58 ?  524  MET B CE    1 
ATOM   13108 N N     . PRO B 1 527  ? -27.898 21.247  85.193  1.00 35.61 ?  525  PRO B N     1 
ATOM   13109 C CA    . PRO B 1 527  ? -27.990 20.935  83.754  1.00 36.50 ?  525  PRO B CA    1 
ATOM   13110 C C     . PRO B 1 527  ? -26.810 20.133  83.237  1.00 33.30 ?  525  PRO B C     1 
ATOM   13111 O O     . PRO B 1 527  ? -26.973 19.286  82.349  1.00 31.52 ?  525  PRO B O     1 
ATOM   13112 C CB    . PRO B 1 527  ? -28.063 22.324  83.106  1.00 38.44 ?  525  PRO B CB    1 
ATOM   13113 C CG    . PRO B 1 527  ? -27.402 23.228  84.082  1.00 36.79 ?  525  PRO B CG    1 
ATOM   13114 C CD    . PRO B 1 527  ? -27.793 22.695  85.435  1.00 37.60 ?  525  PRO B CD    1 
ATOM   13115 N N     . VAL B 1 528  ? -25.618 20.382  83.772  1.00 33.31 ?  526  VAL B N     1 
ATOM   13116 C CA    . VAL B 1 528  ? -24.422 19.608  83.464  1.00 28.36 ?  526  VAL B CA    1 
ATOM   13117 C C     . VAL B 1 528  ? -23.864 19.138  84.799  1.00 26.34 ?  526  VAL B C     1 
ATOM   13118 O O     . VAL B 1 528  ? -23.286 19.933  85.549  1.00 29.39 ?  526  VAL B O     1 
ATOM   13119 C CB    . VAL B 1 528  ? -23.386 20.423  82.678  1.00 29.63 ?  526  VAL B CB    1 
ATOM   13120 C CG1   . VAL B 1 528  ? -22.083 19.647  82.526  1.00 28.50 ?  526  VAL B CG1   1 
ATOM   13121 C CG2   . VAL B 1 528  ? -23.934 20.792  81.305  1.00 30.57 ?  526  VAL B CG2   1 
ATOM   13122 N N     . VAL B 1 529  ? -24.059 17.857  85.109  1.00 25.76 ?  527  VAL B N     1 
ATOM   13123 C CA    . VAL B 1 529  ? -23.601 17.328  86.386  1.00 22.78 ?  527  VAL B CA    1 
ATOM   13124 C C     . VAL B 1 529  ? -22.083 17.404  86.457  1.00 23.00 ?  527  VAL B C     1 
ATOM   13125 O O     . VAL B 1 529  ? -21.368 16.940  85.558  1.00 23.69 ?  527  VAL B O     1 
ATOM   13126 C CB    . VAL B 1 529  ? -24.098 15.890  86.585  1.00 25.70 ?  527  VAL B CB    1 
ATOM   13127 C CG1   . VAL B 1 529  ? -23.466 15.284  87.829  1.00 24.04 ?  527  VAL B CG1   1 
ATOM   13128 C CG2   . VAL B 1 529  ? -25.617 15.860  86.681  1.00 26.87 ?  527  VAL B CG2   1 
ATOM   13129 N N     . GLY B 1 530  ? -21.580 18.004  87.533  1.00 22.66 ?  528  GLY B N     1 
ATOM   13130 C CA    . GLY B 1 530  ? -20.151 18.051  87.743  1.00 21.28 ?  528  GLY B CA    1 
ATOM   13131 C C     . GLY B 1 530  ? -19.406 19.138  87.009  1.00 20.68 ?  528  GLY B C     1 
ATOM   13132 O O     . GLY B 1 530  ? -18.183 19.064  86.911  1.00 20.43 ?  528  GLY B O     1 
ATOM   13133 N N     . ALA B 1 531  ? -20.092 20.148  86.478  1.00 19.02 ?  529  ALA B N     1 
ATOM   13134 C CA    . ALA B 1 531  ? -19.383 21.195  85.755  1.00 20.96 ?  529  ALA B CA    1 
ATOM   13135 C C     . ALA B 1 531  ? -18.443 21.953  86.683  1.00 18.86 ?  529  ALA B C     1 
ATOM   13136 O O     . ALA B 1 531  ? -18.748 22.174  87.858  1.00 20.30 ?  529  ALA B O     1 
ATOM   13137 C CB    . ALA B 1 531  ? -20.371 22.160  85.103  1.00 22.77 ?  529  ALA B CB    1 
ATOM   13138 N N     . LYS B 1 532  ? -17.285 22.331  86.142  1.00 19.08 ?  530  LYS B N     1 
ATOM   13139 C CA    . LYS B 1 532  ? -16.308 23.150  86.851  1.00 17.28 ?  530  LYS B CA    1 
ATOM   13140 C C     . LYS B 1 532  ? -16.939 24.462  87.302  1.00 19.33 ?  530  LYS B C     1 
ATOM   13141 O O     . LYS B 1 532  ? -17.847 24.998  86.660  1.00 18.64 ?  530  LYS B O     1 
ATOM   13142 C CB    . LYS B 1 532  ? -15.108 23.415  85.923  1.00 18.63 ?  530  LYS B CB    1 
ATOM   13143 C CG    . LYS B 1 532  ? -14.074 24.435  86.383  1.00 22.82 ?  530  LYS B CG    1 
ATOM   13144 C CD    . LYS B 1 532  ? -13.045 24.689  85.274  1.00 22.36 ?  530  LYS B CD    1 
ATOM   13145 C CE    . LYS B 1 532  ? -13.615 25.514  84.129  1.00 18.67 ?  530  LYS B CE    1 
ATOM   13146 N NZ    . LYS B 1 532  ? -14.063 26.867  84.572  1.00 20.25 ?  530  LYS B NZ    1 
ATOM   13147 N N     . HIS B 1 533  ? -16.456 24.977  88.426  1.00 16.68 ?  531  HIS B N     1 
ATOM   13148 C CA    . HIS B 1 533  ? -16.850 26.308  88.859  1.00 16.20 ?  531  HIS B CA    1 
ATOM   13149 C C     . HIS B 1 533  ? -16.637 27.311  87.730  1.00 17.53 ?  531  HIS B C     1 
ATOM   13150 O O     . HIS B 1 533  ? -15.595 27.311  87.073  1.00 17.84 ?  531  HIS B O     1 
ATOM   13151 C CB    . HIS B 1 533  ? -16.032 26.689  90.096  1.00 16.84 ?  531  HIS B CB    1 
ATOM   13152 C CG    . HIS B 1 533  ? -16.606 27.832  90.867  1.00 19.16 ?  531  HIS B CG    1 
ATOM   13153 N ND1   . HIS B 1 533  ? -16.662 29.115  90.361  1.00 19.35 ?  531  HIS B ND1   1 
ATOM   13154 C CD2   . HIS B 1 533  ? -17.136 27.892  92.111  1.00 25.69 ?  531  HIS B CD2   1 
ATOM   13155 C CE1   . HIS B 1 533  ? -17.215 29.913  91.257  1.00 26.82 ?  531  HIS B CE1   1 
ATOM   13156 N NE2   . HIS B 1 533  ? -17.511 29.196  92.327  1.00 31.60 ?  531  HIS B NE2   1 
ATOM   13157 N N     . ASP B 1 534  ? -17.645 28.156  87.484  1.00 19.66 ?  532  ASP B N     1 
ATOM   13158 C CA    . ASP B 1 534  ? -17.554 29.115  86.387  1.00 23.00 ?  532  ASP B CA    1 
ATOM   13159 C C     . ASP B 1 534  ? -16.461 30.154  86.585  1.00 21.94 ?  532  ASP B C     1 
ATOM   13160 O O     . ASP B 1 534  ? -16.005 30.749  85.602  1.00 23.53 ?  532  ASP B O     1 
ATOM   13161 C CB    . ASP B 1 534  ? -18.882 29.846  86.204  1.00 21.28 ?  532  ASP B CB    1 
ATOM   13162 C CG    . ASP B 1 534  ? -19.980 28.944  85.699  1.00 40.21 ?  532  ASP B CG    1 
ATOM   13163 O OD1   . ASP B 1 534  ? -19.710 28.144  84.774  1.00 41.94 ?  532  ASP B OD1   1 
ATOM   13164 O OD2   . ASP B 1 534  ? -21.111 29.037  86.231  1.00 45.11 ?  532  ASP B OD2   1 
ATOM   13165 N N     . ARG B 1 535  ? -16.041 30.402  87.822  1.00 18.00 ?  533  ARG B N     1 
ATOM   13166 C CA    . ARG B 1 535  ? -15.106 31.477  88.119  1.00 18.74 ?  533  ARG B CA    1 
ATOM   13167 C C     . ARG B 1 535  ? -13.689 30.986  88.390  1.00 17.67 ?  533  ARG B C     1 
ATOM   13168 O O     . ARG B 1 535  ? -12.850 31.778  88.833  1.00 21.01 ?  533  ARG B O     1 
ATOM   13169 C CB    . ARG B 1 535  ? -15.605 32.294  89.314  1.00 25.33 ?  533  ARG B CB    1 
ATOM   13170 C CG    . ARG B 1 535  ? -16.841 33.137  89.028  1.00 29.24 ?  533  ARG B CG    1 
ATOM   13171 C CD    . ARG B 1 535  ? -17.260 33.941  90.252  1.00 36.74 ?  533  ARG B CD    1 
ATOM   13172 N N     . ILE B 1 536  ? -13.403 29.704  88.161  1.00 15.38 ?  534  ILE B N     1 
ATOM   13173 C CA    . ILE B 1 536  ? -12.057 29.162  88.309  1.00 14.84 ?  534  ILE B CA    1 
ATOM   13174 C C     . ILE B 1 536  ? -11.598 28.682  86.944  1.00 15.06 ?  534  ILE B C     1 
ATOM   13175 O O     . ILE B 1 536  ? -12.245 27.820  86.337  1.00 16.07 ?  534  ILE B O     1 
ATOM   13176 C CB    . ILE B 1 536  ? -12.001 28.022  89.328  1.00 15.53 ?  534  ILE B CB    1 
ATOM   13177 C CG1   . ILE B 1 536  ? -12.393 28.566  90.699  1.00 18.92 ?  534  ILE B CG1   1 
ATOM   13178 C CG2   . ILE B 1 536  ? -10.579 27.428  89.355  1.00 16.51 ?  534  ILE B CG2   1 
ATOM   13179 C CD1   . ILE B 1 536  ? -12.568 27.499  91.720  1.00 25.28 ?  534  ILE B CD1   1 
ATOM   13180 N N     . ALA B 1 537  ? -10.491 29.238  86.461  1.00 15.08 ?  535  ALA B N     1 
ATOM   13181 C CA    . ALA B 1 537  ? -10.007 28.876  85.136  1.00 14.02 ?  535  ALA B CA    1 
ATOM   13182 C C     . ALA B 1 537  ? -9.189  27.591  85.192  1.00 12.66 ?  535  ALA B C     1 
ATOM   13183 O O     . ALA B 1 537  ? -8.302  27.448  86.038  1.00 13.79 ?  535  ALA B O     1 
ATOM   13184 C CB    . ALA B 1 537  ? -9.161  30.012  84.555  1.00 14.68 ?  535  ALA B CB    1 
ATOM   13185 N N     . LEU B 1 538  ? -9.466  26.671  84.265  1.00 13.75 ?  536  LEU B N     1 
ATOM   13186 C CA    . LEU B 1 538  ? -8.538  25.576  84.027  1.00 11.91 ?  536  LEU B CA    1 
ATOM   13187 C C     . LEU B 1 538  ? -7.175  26.159  83.677  1.00 13.39 ?  536  LEU B C     1 
ATOM   13188 O O     . LEU B 1 538  ? -7.096  27.240  83.093  1.00 14.15 ?  536  LEU B O     1 
ATOM   13189 C CB    . LEU B 1 538  ? -9.012  24.688  82.878  1.00 14.08 ?  536  LEU B CB    1 
ATOM   13190 C CG    . LEU B 1 538  ? -10.198 23.776  83.165  1.00 15.51 ?  536  LEU B CG    1 
ATOM   13191 C CD1   . LEU B 1 538  ? -10.661 23.168  81.850  1.00 20.37 ?  536  LEU B CD1   1 
ATOM   13192 C CD2   . LEU B 1 538  ? -9.834  22.672  84.149  1.00 15.93 ?  536  LEU B CD2   1 
ATOM   13193 N N     . PRO B 1 539  ? -6.084  25.477  84.034  1.00 12.35 ?  537  PRO B N     1 
ATOM   13194 C CA    . PRO B 1 539  ? -4.755  26.019  83.717  1.00 11.66 ?  537  PRO B CA    1 
ATOM   13195 C C     . PRO B 1 539  ? -4.598  26.370  82.242  1.00 12.97 ?  537  PRO B C     1 
ATOM   13196 O O     . PRO B 1 539  ? -4.009  27.416  81.924  1.00 13.00 ?  537  PRO B O     1 
ATOM   13197 C CB    . PRO B 1 539  ? -3.808  24.903  84.193  1.00 12.35 ?  537  PRO B CB    1 
ATOM   13198 C CG    . PRO B 1 539  ? -4.577  24.223  85.288  1.00 13.47 ?  537  PRO B CG    1 
ATOM   13199 C CD    . PRO B 1 539  ? -6.016  24.256  84.860  1.00 13.46 ?  537  PRO B CD    1 
ATOM   13200 N N     . ALA B 1 540  ? -5.151  25.559  81.337  1.00 13.52 ?  538  ALA B N     1 
ATOM   13201 C CA    . ALA B 1 540  ? -5.018  25.856  79.916  1.00 13.85 ?  538  ALA B CA    1 
ATOM   13202 C C     . ALA B 1 540  ? -5.715  27.148  79.535  1.00 18.57 ?  538  ALA B C     1 
ATOM   13203 O O     . ALA B 1 540  ? -5.367  27.747  78.510  1.00 16.91 ?  538  ALA B O     1 
ATOM   13204 C CB    . ALA B 1 540  ? -5.577  24.709  79.077  1.00 16.98 ?  538  ALA B CB    1 
ATOM   13205 N N     . GLU B 1 541  ? -6.682  27.590  80.339  1.00 14.61 ?  539  GLU B N     1 
ATOM   13206 C CA    . GLU B 1 541  ? -7.535  28.716  79.980  1.00 15.88 ?  539  GLU B CA    1 
ATOM   13207 C C     . GLU B 1 541  ? -7.239  29.969  80.806  1.00 13.72 ?  539  GLU B C     1 
ATOM   13208 O O     . GLU B 1 541  ? -8.048  30.902  80.817  1.00 16.05 ?  539  GLU B O     1 
ATOM   13209 C CB    . GLU B 1 541  ? -9.002  28.279  80.085  1.00 18.14 ?  539  GLU B CB    1 
ATOM   13210 C CG    . GLU B 1 541  ? -9.261  27.021  79.214  1.00 21.34 ?  539  GLU B CG    1 
ATOM   13211 C CD    . GLU B 1 541  ? -10.693 26.473  79.219  1.00 28.65 ?  539  GLU B CD    1 
ATOM   13212 O OE1   . GLU B 1 541  ? -11.562 26.994  79.945  1.00 30.09 ?  539  GLU B OE1   1 
ATOM   13213 O OE2   . GLU B 1 541  ? -10.943 25.496  78.476  1.00 30.82 ?  539  GLU B OE2   1 
ATOM   13214 N N     . LEU B 1 542  ? -6.057  30.038  81.436  1.00 12.58 ?  540  LEU B N     1 
ATOM   13215 C CA    . LEU B 1 542  ? -5.685  31.194  82.264  1.00 14.85 ?  540  LEU B CA    1 
ATOM   13216 C C     . LEU B 1 542  ? -5.795  32.523  81.537  1.00 15.71 ?  540  LEU B C     1 
ATOM   13217 O O     . LEU B 1 542  ? -6.048  33.558  82.168  1.00 17.59 ?  540  LEU B O     1 
ATOM   13218 C CB    . LEU B 1 542  ? -4.246  31.081  82.748  1.00 19.12 ?  540  LEU B CB    1 
ATOM   13219 C CG    . LEU B 1 542  ? -3.915  30.328  84.013  1.00 21.42 ?  540  LEU B CG    1 
ATOM   13220 C CD1   . LEU B 1 542  ? -2.500  30.657  84.460  1.00 14.17 ?  540  LEU B CD1   1 
ATOM   13221 C CD2   . LEU B 1 542  ? -4.926  30.629  85.104  1.00 16.66 ?  540  LEU B CD2   1 
ATOM   13222 N N     . PHE B 1 543  ? -5.552  32.529  80.228  1.00 13.93 ?  541  PHE B N     1 
ATOM   13223 C CA    . PHE B 1 543  ? -5.502  33.758  79.447  1.00 14.23 ?  541  PHE B CA    1 
ATOM   13224 C C     . PHE B 1 543  ? -6.744  33.922  78.587  1.00 14.41 ?  541  PHE B C     1 
ATOM   13225 O O     . PHE B 1 543  ? -6.797  34.819  77.735  1.00 16.93 ?  541  PHE B O     1 
ATOM   13226 C CB    . PHE B 1 543  ? -4.221  33.776  78.612  1.00 14.11 ?  541  PHE B CB    1 
ATOM   13227 C CG    . PHE B 1 543  ? -3.002  33.469  79.425  1.00 14.56 ?  541  PHE B CG    1 
ATOM   13228 C CD1   . PHE B 1 543  ? -2.705  34.235  80.546  1.00 16.78 ?  541  PHE B CD1   1 
ATOM   13229 C CD2   . PHE B 1 543  ? -2.174  32.396  79.106  1.00 12.24 ?  541  PHE B CD2   1 
ATOM   13230 C CE1   . PHE B 1 543  ? -1.591  33.961  81.324  1.00 14.67 ?  541  PHE B CE1   1 
ATOM   13231 C CE2   . PHE B 1 543  ? -1.044  32.111  79.885  1.00 14.54 ?  541  PHE B CE2   1 
ATOM   13232 C CZ    . PHE B 1 543  ? -0.753  32.902  80.996  1.00 16.15 ?  541  PHE B CZ    1 
ATOM   13233 N N     . GLY B 1 544  ? -7.747  33.079  78.806  1.00 15.05 ?  542  GLY B N     1 
ATOM   13234 C CA    . GLY B 1 544  ? -9.009  33.222  78.099  1.00 15.64 ?  542  GLY B CA    1 
ATOM   13235 C C     . GLY B 1 544  ? -8.843  33.180  76.592  1.00 17.55 ?  542  GLY B C     1 
ATOM   13236 O O     . GLY B 1 544  ? -8.117  32.347  76.037  1.00 18.98 ?  542  GLY B O     1 
ATOM   13237 N N     . ASP B 1 545  ? -9.539  34.098  75.914  1.00 20.13 ?  543  ASP B N     1 
ATOM   13238 C CA    . ASP B 1 545  ? -9.586  34.093  74.457  1.00 20.49 ?  543  ASP B CA    1 
ATOM   13239 C C     . ASP B 1 545  ? -8.271  34.522  73.828  1.00 19.54 ?  543  ASP B C     1 
ATOM   13240 O O     . ASP B 1 545  ? -8.082  34.307  72.624  1.00 22.14 ?  543  ASP B O     1 
ATOM   13241 C CB    . ASP B 1 545  ? -10.688 35.028  73.943  1.00 23.39 ?  543  ASP B CB    1 
ATOM   13242 C CG    . ASP B 1 545  ? -12.083 34.567  74.311  1.00 36.32 ?  543  ASP B CG    1 
ATOM   13243 O OD1   . ASP B 1 545  ? -12.269 33.373  74.647  1.00 35.25 ?  543  ASP B OD1   1 
ATOM   13244 O OD2   . ASP B 1 545  ? -13.004 35.413  74.236  1.00 46.05 ?  543  ASP B OD2   1 
ATOM   13245 N N     . ALA B 1 546  ? -7.367  35.122  74.607  1.00 18.51 ?  544  ALA B N     1 
ATOM   13246 C CA    . ALA B 1 546  ? -6.166  35.715  74.027  1.00 18.26 ?  544  ALA B CA    1 
ATOM   13247 C C     . ALA B 1 546  ? -5.221  34.656  73.479  1.00 18.65 ?  544  ALA B C     1 
ATOM   13248 O O     . ALA B 1 546  ? -4.680  34.812  72.379  1.00 17.46 ?  544  ALA B O     1 
ATOM   13249 C CB    . ALA B 1 546  ? -5.442  36.565  75.068  1.00 17.44 ?  544  ALA B CB    1 
ATOM   13250 N N     . ARG B 1 547  ? -5.001  33.586  74.231  1.00 14.21 ?  545  ARG B N     1 
ATOM   13251 C CA    . ARG B 1 547  ? -4.078  32.537  73.834  1.00 14.75 ?  545  ARG B CA    1 
ATOM   13252 C C     . ARG B 1 547  ? -4.257  31.355  74.762  1.00 14.58 ?  545  ARG B C     1 
ATOM   13253 O O     . ARG B 1 547  ? -4.840  31.468  75.845  1.00 14.37 ?  545  ARG B O     1 
ATOM   13254 C CB    . ARG B 1 547  ? -2.626  33.008  73.856  1.00 18.12 ?  545  ARG B CB    1 
ATOM   13255 C CG    . ARG B 1 547  ? -2.168  33.492  75.173  1.00 17.33 ?  545  ARG B CG    1 
ATOM   13256 C CD    . ARG B 1 547  ? -0.718  33.936  75.032  1.00 20.52 ?  545  ARG B CD    1 
ATOM   13257 N NE    . ARG B 1 547  ? -0.355  34.692  76.211  1.00 21.16 ?  545  ARG B NE    1 
ATOM   13258 C CZ    . ARG B 1 547  ? 0.417   34.240  77.191  1.00 17.79 ?  545  ARG B CZ    1 
ATOM   13259 N NH1   . ARG B 1 547  ? 1.030   33.069  77.105  1.00 15.27 ?  545  ARG B NH1   1 
ATOM   13260 N NH2   . ARG B 1 547  ? 0.570   34.983  78.278  1.00 19.09 ?  545  ARG B NH2   1 
ATOM   13261 N N     . THR B 1 548  ? -3.765  30.217  74.305  1.00 12.81 ?  546  THR B N     1 
ATOM   13262 C CA    . THR B 1 548  ? -3.806  28.978  75.058  1.00 11.40 ?  546  THR B CA    1 
ATOM   13263 C C     . THR B 1 548  ? -2.535  28.870  75.887  1.00 10.58 ?  546  THR B C     1 
ATOM   13264 O O     . THR B 1 548  ? -1.427  28.995  75.361  1.00 11.88 ?  546  THR B O     1 
ATOM   13265 C CB    . THR B 1 548  ? -3.929  27.800  74.101  1.00 11.70 ?  546  THR B CB    1 
ATOM   13266 O OG1   . THR B 1 548  ? -5.140  27.948  73.348  1.00 17.28 ?  546  THR B OG1   1 
ATOM   13267 C CG2   . THR B 1 548  ? -3.951  26.486  74.853  1.00 14.09 ?  546  THR B CG2   1 
ATOM   13268 N N     . ASN B 1 549  ? -2.691  28.652  77.187  1.00 11.66 ?  547  ASN B N     1 
ATOM   13269 C CA    . ASN B 1 549  ? -1.534  28.489  78.048  1.00 10.49 ?  547  ASN B CA    1 
ATOM   13270 C C     . ASN B 1 549  ? -0.785  27.212  77.671  1.00 11.80 ?  547  ASN B C     1 
ATOM   13271 O O     . ASN B 1 549  ? -1.387  26.221  77.254  1.00 13.76 ?  547  ASN B O     1 
ATOM   13272 C CB    . ASN B 1 549  ? -2.011  28.449  79.504  1.00 11.34 ?  547  ASN B CB    1 
ATOM   13273 C CG    . ASN B 1 549  ? -0.893  28.568  80.497  1.00 10.48 ?  547  ASN B CG    1 
ATOM   13274 O OD1   . ASN B 1 549  ? 0.233   28.945  80.172  1.00 12.58 ?  547  ASN B OD1   1 
ATOM   13275 N ND2   . ASN B 1 549  ? -1.220  28.281  81.771  1.00 11.71 ?  547  ASN B ND2   1 
ATOM   13276 N N     . SER B 1 550  ? 0.545   27.255  77.763  1.00 10.25 ?  548  SER B N     1 
ATOM   13277 C CA    . SER B 1 550  ? 1.297   26.022  77.590  1.00 11.95 ?  548  SER B CA    1 
ATOM   13278 C C     . SER B 1 550  ? 0.959   25.035  78.699  1.00 13.70 ?  548  SER B C     1 
ATOM   13279 O O     . SER B 1 550  ? 0.540   25.416  79.797  1.00 12.68 ?  548  SER B O     1 
ATOM   13280 C CB    . SER B 1 550  ? 2.797   26.300  77.592  1.00 11.57 ?  548  SER B CB    1 
ATOM   13281 O OG    . SER B 1 550  ? 3.188   26.891  78.826  1.00 12.10 ?  548  SER B OG    1 
ATOM   13282 N N     . ALA B 1 551  ? 1.131   23.754  78.395  1.00 13.09 ?  549  ALA B N     1 
ATOM   13283 C CA    . ALA B 1 551  ? 0.890   22.687  79.354  1.00 14.15 ?  549  ALA B CA    1 
ATOM   13284 C C     . ALA B 1 551  ? 2.201   22.100  79.838  1.00 14.99 ?  549  ALA B C     1 
ATOM   13285 O O     . ALA B 1 551  ? 3.149   21.942  79.064  1.00 13.87 ?  549  ALA B O     1 
ATOM   13286 C CB    . ALA B 1 551  ? 0.035   21.591  78.749  1.00 14.17 ?  549  ALA B CB    1 
ATOM   13287 N N     . GLY B 1 552  ? 2.252   21.781  81.122  1.00 14.73 ?  550  GLY B N     1 
ATOM   13288 C CA    . GLY B 1 552  ? 3.388   21.127  81.722  1.00 14.15 ?  550  GLY B CA    1 
ATOM   13289 C C     . GLY B 1 552  ? 3.173   19.632  81.841  1.00 13.38 ?  550  GLY B C     1 
ATOM   13290 O O     . GLY B 1 552  ? 2.351   19.034  81.137  1.00 15.84 ?  550  GLY B O     1 
ATOM   13291 N N     . LEU B 1 553  ? 3.926   19.023  82.754  1.00 14.63 ?  551  LEU B N     1 
ATOM   13292 C CA    . LEU B 1 553  ? 3.885   17.589  83.014  1.00 15.55 ?  551  LEU B CA    1 
ATOM   13293 C C     . LEU B 1 553  ? 3.976   17.402  84.515  1.00 15.12 ?  551  LEU B C     1 
ATOM   13294 O O     . LEU B 1 553  ? 4.747   18.100  85.167  1.00 17.19 ?  551  LEU B O     1 
ATOM   13295 C CB    . LEU B 1 553  ? 5.054   16.840  82.341  1.00 16.18 ?  551  LEU B CB    1 
ATOM   13296 C CG    . LEU B 1 553  ? 5.033   16.816  80.813  1.00 17.29 ?  551  LEU B CG    1 
ATOM   13297 C CD1   . LEU B 1 553  ? 6.341   16.257  80.281  1.00 19.17 ?  551  LEU B CD1   1 
ATOM   13298 C CD2   . LEU B 1 553  ? 3.850   16.001  80.313  1.00 21.50 ?  551  LEU B CD2   1 
ATOM   13299 N N     . ASP B 1 554  ? 3.207   16.455  85.049  1.00 15.08 ?  552  ASP B N     1 
ATOM   13300 C CA    . ASP B 1 554  ? 3.117   16.239  86.496  1.00 15.73 ?  552  ASP B CA    1 
ATOM   13301 C C     . ASP B 1 554  ? 4.126   15.168  86.892  1.00 14.33 ?  552  ASP B C     1 
ATOM   13302 O O     . ASP B 1 554  ? 3.892   13.974  86.679  1.00 14.87 ?  552  ASP B O     1 
ATOM   13303 C CB    . ASP B 1 554  ? 1.701   15.834  86.887  1.00 16.33 ?  552  ASP B CB    1 
ATOM   13304 C CG    . ASP B 1 554  ? 1.536   15.642  88.389  1.00 15.67 ?  552  ASP B CG    1 
ATOM   13305 O OD1   . ASP B 1 554  ? 2.506   15.859  89.149  1.00 17.79 ?  552  ASP B OD1   1 
ATOM   13306 O OD2   . ASP B 1 554  ? 0.410   15.287  88.798  1.00 18.43 ?  552  ASP B OD2   1 
ATOM   13307 N N     . LEU B 1 555  ? 5.242   15.595  87.479  1.00 13.77 ?  553  LEU B N     1 
ATOM   13308 C CA    . LEU B 1 555  ? 6.299   14.669  87.865  1.00 15.88 ?  553  LEU B CA    1 
ATOM   13309 C C     . LEU B 1 555  ? 5.987   13.938  89.171  1.00 17.70 ?  553  LEU B C     1 
ATOM   13310 O O     . LEU B 1 555  ? 6.860   13.247  89.705  1.00 16.39 ?  553  LEU B O     1 
ATOM   13311 C CB    . LEU B 1 555  ? 7.636   15.416  87.954  1.00 15.30 ?  553  LEU B CB    1 
ATOM   13312 C CG    . LEU B 1 555  ? 8.137   16.039  86.636  1.00 14.96 ?  553  LEU B CG    1 
ATOM   13313 C CD1   . LEU B 1 555  ? 9.507   16.663  86.832  1.00 17.24 ?  553  LEU B CD1   1 
ATOM   13314 C CD2   . LEU B 1 555  ? 8.169   15.001  85.503  1.00 19.14 ?  553  LEU B CD2   1 
ATOM   13315 N N     . SER B 1 556  ? 4.768   14.078  89.702  1.00 14.96 ?  554  SER B N     1 
ATOM   13316 C CA    . SER B 1 556  ? 4.287   13.215  90.777  1.00 15.89 ?  554  SER B CA    1 
ATOM   13317 C C     . SER B 1 556  ? 3.350   12.125  90.268  1.00 15.56 ?  554  SER B C     1 
ATOM   13318 O O     . SER B 1 556  ? 2.897   11.286  91.057  1.00 16.92 ?  554  SER B O     1 
ATOM   13319 C CB    . SER B 1 556  ? 3.571   14.047  91.855  1.00 16.74 ?  554  SER B CB    1 
ATOM   13320 O OG    . SER B 1 556  ? 2.285   14.441  91.395  1.00 16.52 ?  554  SER B OG    1 
ATOM   13321 N N     . ASN B 1 557  ? 3.049   12.109  88.974  1.00 15.32 ?  555  ASN B N     1 
ATOM   13322 C CA    . ASN B 1 557  ? 2.122   11.150  88.394  1.00 15.83 ?  555  ASN B CA    1 
ATOM   13323 C C     . ASN B 1 557  ? 2.904   9.956   87.852  1.00 17.89 ?  555  ASN B C     1 
ATOM   13324 O O     . ASN B 1 557  ? 3.743   10.122  86.963  1.00 17.27 ?  555  ASN B O     1 
ATOM   13325 C CB    . ASN B 1 557  ? 1.316   11.849  87.301  1.00 16.16 ?  555  ASN B CB    1 
ATOM   13326 C CG    . ASN B 1 557  ? 0.286   10.954  86.667  1.00 16.23 ?  555  ASN B CG    1 
ATOM   13327 O OD1   . ASN B 1 557  ? 0.606   9.878   86.176  1.00 16.60 ?  555  ASN B OD1   1 
ATOM   13328 N ND2   . ASN B 1 557  ? -0.968  11.395  86.667  1.00 17.54 ?  555  ASN B ND2   1 
ATOM   13329 N N     . GLU B 1 558  ? 2.638   8.757   88.385  1.00 16.27 ?  556  GLU B N     1 
ATOM   13330 C CA    . GLU B 1 558  ? 3.420   7.591   87.963  1.00 17.48 ?  556  GLU B CA    1 
ATOM   13331 C C     . GLU B 1 558  ? 3.232   7.261   86.490  1.00 18.25 ?  556  GLU B C     1 
ATOM   13332 O O     . GLU B 1 558  ? 4.167   6.751   85.864  1.00 19.73 ?  556  GLU B O     1 
ATOM   13333 C CB    . GLU B 1 558  ? 3.078   6.348   88.788  1.00 21.23 ?  556  GLU B CB    1 
ATOM   13334 C CG    . GLU B 1 558  ? 3.486   6.385   90.259  1.00 19.05 ?  556  GLU B CG    1 
ATOM   13335 C CD    . GLU B 1 558  ? 4.995   6.480   90.536  1.00 20.99 ?  556  GLU B CD    1 
ATOM   13336 O OE1   . GLU B 1 558  ? 5.841   6.270   89.643  1.00 19.72 ?  556  GLU B OE1   1 
ATOM   13337 O OE2   . GLU B 1 558  ? 5.337   6.780   91.690  1.00 20.03 ?  556  GLU B OE2   1 
ATOM   13338 N N     . GLU B 1 559  ? 2.046   7.503   85.919  1.00 16.56 ?  557  GLU B N     1 
ATOM   13339 C CA    . GLU B 1 559  ? 1.877   7.265   84.482  1.00 17.62 ?  557  GLU B CA    1 
ATOM   13340 C C     . GLU B 1 559  ? 2.798   8.183   83.693  1.00 16.47 ?  557  GLU B C     1 
ATOM   13341 O O     . GLU B 1 559  ? 3.483   7.756   82.755  1.00 17.57 ?  557  GLU B O     1 
ATOM   13342 C CB    . GLU B 1 559  ? 0.423   7.492   84.041  1.00 20.26 ?  557  GLU B CB    1 
ATOM   13343 C CG    . GLU B 1 559  ? -0.617  6.503   84.540  1.00 25.34 ?  557  GLU B CG    1 
ATOM   13344 C CD    . GLU B 1 559  ? -2.030  6.861   84.069  1.00 31.50 ?  557  GLU B CD    1 
ATOM   13345 O OE1   . GLU B 1 559  ? -2.169  7.636   83.099  1.00 36.32 ?  557  GLU B OE1   1 
ATOM   13346 O OE2   . GLU B 1 559  ? -3.008  6.370   84.670  1.00 29.16 ?  557  GLU B OE2   1 
ATOM   13347 N N     . THR B 1 560  ? 2.832   9.454   84.079  1.00 15.72 ?  558  THR B N     1 
ATOM   13348 C CA    . THR B 1 560  ? 3.700   10.418  83.427  1.00 16.38 ?  558  THR B CA    1 
ATOM   13349 C C     . THR B 1 560  ? 5.166   10.047  83.591  1.00 16.63 ?  558  THR B C     1 
ATOM   13350 O O     . THR B 1 560  ? 5.942   10.137  82.635  1.00 16.82 ?  558  THR B O     1 
ATOM   13351 C CB    . THR B 1 560  ? 3.430   11.803  84.006  1.00 16.49 ?  558  THR B CB    1 
ATOM   13352 O OG1   . THR B 1 560  ? 2.045   12.118  83.805  1.00 17.42 ?  558  THR B OG1   1 
ATOM   13353 C CG2   . THR B 1 560  ? 4.320   12.850  83.347  1.00 18.60 ?  558  THR B CG2   1 
ATOM   13354 N N     . LEU B 1 561  ? 5.576   9.645   84.798  1.00 14.57 ?  559  LEU B N     1 
ATOM   13355 C CA    . LEU B 1 561  ? 6.980   9.296   84.988  1.00 15.58 ?  559  LEU B CA    1 
ATOM   13356 C C     . LEU B 1 561  ? 7.359   8.088   84.145  1.00 17.45 ?  559  LEU B C     1 
ATOM   13357 O O     . LEU B 1 561  ? 8.461   8.033   83.585  1.00 17.36 ?  559  LEU B O     1 
ATOM   13358 C CB    . LEU B 1 561  ? 7.273   9.035   86.466  1.00 16.58 ?  559  LEU B CB    1 
ATOM   13359 C CG    . LEU B 1 561  ? 7.164   10.285  87.349  1.00 14.85 ?  559  LEU B CG    1 
ATOM   13360 C CD1   . LEU B 1 561  ? 7.337   9.917   88.819  1.00 15.95 ?  559  LEU B CD1   1 
ATOM   13361 C CD2   . LEU B 1 561  ? 8.189   11.337  86.949  1.00 16.18 ?  559  LEU B CD2   1 
ATOM   13362 N N     . ALA B 1 562  ? 6.463   7.109   84.043  1.00 17.65 ?  560  ALA B N     1 
ATOM   13363 C CA    . ALA B 1 562  ? 6.781   5.914   83.271  1.00 17.03 ?  560  ALA B CA    1 
ATOM   13364 C C     . ALA B 1 562  ? 6.881   6.232   81.785  1.00 20.42 ?  560  ALA B C     1 
ATOM   13365 O O     . ALA B 1 562  ? 7.802   5.760   81.104  1.00 19.99 ?  560  ALA B O     1 
ATOM   13366 C CB    . ALA B 1 562  ? 5.740   4.832   83.539  1.00 18.33 ?  560  ALA B CB    1 
ATOM   13367 N N     . SER B 1 563  ? 5.958   7.047   81.266  1.00 18.54 ?  561  SER B N     1 
ATOM   13368 C CA    . SER B 1 563  ? 6.011   7.394   79.848  1.00 17.63 ?  561  SER B CA    1 
ATOM   13369 C C     . SER B 1 563  ? 7.179   8.330   79.555  1.00 19.59 ?  561  SER B C     1 
ATOM   13370 O O     . SER B 1 563  ? 7.830   8.209   78.508  1.00 20.53 ?  561  SER B O     1 
ATOM   13371 C CB    . SER B 1 563  ? 4.685   8.008   79.403  1.00 20.08 ?  561  SER B CB    1 
ATOM   13372 O OG    . SER B 1 563  ? 4.473   9.251   80.025  1.00 23.37 ?  561  SER B OG    1 
ATOM   13373 N N     . LEU B 1 564  ? 7.476   9.252   80.473  1.00 17.54 ?  562  LEU B N     1 
ATOM   13374 C CA    A LEU B 1 564  ? 8.634   10.120  80.290  0.48 18.50 ?  562  LEU B CA    1 
ATOM   13375 C CA    B LEU B 1 564  ? 8.640   10.117  80.296  0.52 18.49 ?  562  LEU B CA    1 
ATOM   13376 C C     . LEU B 1 564  ? 9.930   9.313   80.273  1.00 21.44 ?  562  LEU B C     1 
ATOM   13377 O O     . LEU B 1 564  ? 10.814  9.570   79.447  1.00 20.21 ?  562  LEU B O     1 
ATOM   13378 C CB    A LEU B 1 564  ? 8.662   11.189  81.386  0.48 20.41 ?  562  LEU B CB    1 
ATOM   13379 C CB    B LEU B 1 564  ? 8.705   11.166  81.403  0.52 20.42 ?  562  LEU B CB    1 
ATOM   13380 C CG    A LEU B 1 564  ? 9.690   12.314  81.265  0.48 19.22 ?  562  LEU B CG    1 
ATOM   13381 C CG    B LEU B 1 564  ? 8.009   12.493  81.150  0.52 19.66 ?  562  LEU B CG    1 
ATOM   13382 C CD1   A LEU B 1 564  ? 9.567   13.018  79.917  0.48 18.17 ?  562  LEU B CD1   1 
ATOM   13383 C CD1   B LEU B 1 564  ? 8.331   13.421  82.289  0.52 16.72 ?  562  LEU B CD1   1 
ATOM   13384 C CD2   A LEU B 1 564  ? 9.549   13.314  82.413  0.48 18.12 ?  562  LEU B CD2   1 
ATOM   13385 C CD2   B LEU B 1 564  ? 8.436   13.105  79.826  0.52 18.29 ?  562  LEU B CD2   1 
ATOM   13386 N N     . THR B 1 565  ? 10.066  8.344   81.186  1.00 19.96 ?  563  THR B N     1 
ATOM   13387 C CA    . THR B 1 565  ? 11.256  7.494   81.188  1.00 17.85 ?  563  THR B CA    1 
ATOM   13388 C C     . THR B 1 565  ? 11.505  6.910   79.802  1.00 20.93 ?  563  THR B C     1 
ATOM   13389 O O     . THR B 1 565  ? 12.631  6.942   79.292  1.00 20.23 ?  563  THR B O     1 
ATOM   13390 C CB    . THR B 1 565  ? 11.107  6.369   82.218  1.00 19.25 ?  563  THR B CB    1 
ATOM   13391 O OG1   . THR B 1 565  ? 10.999  6.932   83.534  1.00 19.92 ?  563  THR B OG1   1 
ATOM   13392 C CG2   . THR B 1 565  ? 12.319  5.443   82.177  1.00 23.63 ?  563  THR B CG2   1 
ATOM   13393 N N     . GLU B 1 566  ? 10.454  6.409   79.159  1.00 19.68 ?  564  GLU B N     1 
ATOM   13394 C CA    . GLU B 1 566  ? 10.646  5.768   77.862  1.00 21.41 ?  564  GLU B CA    1 
ATOM   13395 C C     . GLU B 1 566  ? 10.952  6.793   76.777  1.00 21.62 ?  564  GLU B C     1 
ATOM   13396 O O     . GLU B 1 566  ? 11.820  6.562   75.924  1.00 21.35 ?  564  GLU B O     1 
ATOM   13397 C CB    . GLU B 1 566  ? 9.420   4.930   77.503  1.00 24.36 ?  564  GLU B CB    1 
ATOM   13398 C CG    . GLU B 1 566  ? 9.207   3.726   78.435  1.00 28.39 ?  564  GLU B CG    1 
ATOM   13399 C CD    . GLU B 1 566  ? 10.499  2.969   78.759  1.00 35.56 ?  564  GLU B CD    1 
ATOM   13400 O OE1   . GLU B 1 566  ? 11.269  2.644   77.824  1.00 38.75 ?  564  GLU B OE1   1 
ATOM   13401 O OE2   . GLU B 1 566  ? 10.740  2.689   79.958  1.00 36.24 ?  564  GLU B OE2   1 
ATOM   13402 N N     . ALA B 1 567  ? 10.252  7.926   76.785  1.00 19.30 ?  565  ALA B N     1 
ATOM   13403 C CA    . ALA B 1 567  ? 10.521  8.952   75.783  1.00 17.84 ?  565  ALA B CA    1 
ATOM   13404 C C     . ALA B 1 567  ? 11.927  9.524   75.943  1.00 21.30 ?  565  ALA B C     1 
ATOM   13405 O O     . ALA B 1 567  ? 12.600  9.814   74.946  1.00 19.32 ?  565  ALA B O     1 
ATOM   13406 C CB    . ALA B 1 567  ? 9.468   10.058  75.870  1.00 20.22 ?  565  ALA B CB    1 
ATOM   13407 N N     . LEU B 1 568  ? 12.392  9.684   77.185  1.00 17.56 ?  566  LEU B N     1 
ATOM   13408 C CA    . LEU B 1 568  ? 13.737  10.204  77.413  1.00 18.54 ?  566  LEU B CA    1 
ATOM   13409 C C     . LEU B 1 568  ? 14.792  9.204   76.949  1.00 20.90 ?  566  LEU B C     1 
ATOM   13410 O O     . LEU B 1 568  ? 15.756  9.574   76.265  1.00 19.74 ?  566  LEU B O     1 
ATOM   13411 C CB    . LEU B 1 568  ? 13.923  10.540  78.892  1.00 18.38 ?  566  LEU B CB    1 
ATOM   13412 C CG    . LEU B 1 568  ? 13.064  11.687  79.446  1.00 19.33 ?  566  LEU B CG    1 
ATOM   13413 C CD1   . LEU B 1 568  ? 13.215  11.792  80.955  1.00 22.92 ?  566  LEU B CD1   1 
ATOM   13414 C CD2   . LEU B 1 568  ? 13.402  13.008  78.785  1.00 20.05 ?  566  LEU B CD2   1 
ATOM   13415 N N     . ARG B 1 569  ? 14.640  7.931   77.335  1.00 18.04 ?  567  ARG B N     1 
ATOM   13416 C CA    . ARG B 1 569  ? 15.511  6.879   76.816  1.00 20.78 ?  567  ARG B CA    1 
ATOM   13417 C C     . ARG B 1 569  ? 15.552  6.905   75.294  1.00 21.14 ?  567  ARG B C     1 
ATOM   13418 O O     . ARG B 1 569  ? 16.627  6.844   74.686  1.00 21.76 ?  567  ARG B O     1 
ATOM   13419 C CB    . ARG B 1 569  ? 15.031  5.512   77.306  1.00 21.33 ?  567  ARG B CB    1 
ATOM   13420 C CG    . ARG B 1 569  ? 15.281  5.239   78.766  1.00 28.73 ?  567  ARG B CG    1 
ATOM   13421 C CD    . ARG B 1 569  ? 14.817  3.838   79.142  1.00 33.32 ?  567  ARG B CD    1 
ATOM   13422 N NE    . ARG B 1 569  ? 14.988  3.586   80.569  1.00 37.60 ?  567  ARG B NE    1 
ATOM   13423 C CZ    . ARG B 1 569  ? 14.361  2.629   81.240  1.00 39.45 ?  567  ARG B CZ    1 
ATOM   13424 N NH1   . ARG B 1 569  ? 13.484  1.834   80.649  1.00 43.94 ?  567  ARG B NH1   1 
ATOM   13425 N NH2   . ARG B 1 569  ? 14.616  2.470   82.536  1.00 43.04 ?  567  ARG B NH2   1 
ATOM   13426 N N     . GLU B 1 570  ? 14.380  7.006   74.663  1.00 17.80 ?  568  GLU B N     1 
ATOM   13427 C CA    . GLU B 1 570  ? 14.321  6.971   73.207  1.00 19.74 ?  568  GLU B CA    1 
ATOM   13428 C C     . GLU B 1 570  ? 15.008  8.183   72.594  1.00 20.53 ?  568  GLU B C     1 
ATOM   13429 O O     . GLU B 1 570  ? 15.629  8.068   71.531  1.00 23.32 ?  568  GLU B O     1 
ATOM   13430 C CB    . GLU B 1 570  ? 12.865  6.878   72.751  1.00 21.57 ?  568  GLU B CB    1 
ATOM   13431 C CG    . GLU B 1 570  ? 12.253  5.493   72.970  1.00 27.73 ?  568  GLU B CG    1 
ATOM   13432 C CD    . GLU B 1 570  ? 10.728  5.505   72.960  1.00 34.93 ?  568  GLU B CD    1 
ATOM   13433 O OE1   . GLU B 1 570  ? 10.135  6.533   72.570  1.00 33.80 ?  568  GLU B OE1   1 
ATOM   13434 O OE2   . GLU B 1 570  ? 10.123  4.482   73.353  1.00 40.63 ?  568  GLU B OE2   1 
ATOM   13435 N N     . SER B 1 571  ? 14.917  9.348   73.251  1.00 19.42 ?  569  SER B N     1 
ATOM   13436 C CA    . SER B 1 571  ? 15.550  10.553  72.722  1.00 19.67 ?  569  SER B CA    1 
ATOM   13437 C C     . SER B 1 571  ? 17.063  10.403  72.671  1.00 21.87 ?  569  SER B C     1 
ATOM   13438 O O     . SER B 1 571  ? 17.714  10.942  71.766  1.00 22.49 ?  569  SER B O     1 
ATOM   13439 C CB    . SER B 1 571  ? 15.162  11.774  73.569  1.00 20.17 ?  569  SER B CB    1 
ATOM   13440 O OG    . SER B 1 571  ? 15.882  11.817  74.799  1.00 21.47 ?  569  SER B OG    1 
ATOM   13441 N N     . ALA B 1 572  ? 17.636  9.658   73.615  1.00 20.12 ?  570  ALA B N     1 
ATOM   13442 C CA    . ALA B 1 572  ? 19.080  9.485   73.646  1.00 21.49 ?  570  ALA B CA    1 
ATOM   13443 C C     . ALA B 1 572  ? 19.577  8.565   72.536  1.00 24.53 ?  570  ALA B C     1 
ATOM   13444 O O     . ALA B 1 572  ? 20.770  8.591   72.217  1.00 27.09 ?  570  ALA B O     1 
ATOM   13445 C CB    . ALA B 1 572  ? 19.511  8.956   75.014  1.00 22.66 ?  570  ALA B CB    1 
ATOM   13446 N N     . ALA B 1 573  ? 18.694  7.762   71.936  1.00 21.54 ?  571  ALA B N     1 
ATOM   13447 C CA    . ALA B 1 573  ? 19.078  6.882   70.841  1.00 22.91 ?  571  ALA B CA    1 
ATOM   13448 C C     . ALA B 1 573  ? 19.030  7.575   69.486  1.00 21.96 ?  571  ALA B C     1 
ATOM   13449 O O     . ALA B 1 573  ? 19.511  7.004   68.497  1.00 25.30 ?  571  ALA B O     1 
ATOM   13450 C CB    . ALA B 1 573  ? 18.183  5.638   70.811  1.00 25.16 ?  571  ALA B CB    1 
ATOM   13451 N N     . MET B 1 574  ? 18.479  8.783   69.426  1.00 20.99 ?  572  MET B N     1 
ATOM   13452 C CA    . MET B 1 574  ? 18.372  9.518   68.176  1.00 21.37 ?  572  MET B CA    1 
ATOM   13453 C C     . MET B 1 574  ? 19.711  10.141  67.810  1.00 21.60 ?  572  MET B C     1 
ATOM   13454 O O     . MET B 1 574  ? 20.514  10.486  68.682  1.00 22.24 ?  572  MET B O     1 
ATOM   13455 C CB    . MET B 1 574  ? 17.306  10.611  68.296  1.00 21.63 ?  572  MET B CB    1 
ATOM   13456 C CG    . MET B 1 574  ? 15.884  10.078  68.479  1.00 22.25 ?  572  MET B CG    1 
ATOM   13457 S SD    . MET B 1 574  ? 14.761  11.363  69.077  1.00 25.28 ?  572  MET B SD    1 
ATOM   13458 C CE    . MET B 1 574  ? 13.218  10.445  69.153  1.00 26.34 ?  572  MET B CE    1 
ATOM   13459 N N     . LYS B 1 575  ? 19.952  10.283  66.508  1.00 19.16 ?  573  LYS B N     1 
ATOM   13460 C CA    . LYS B 1 575  ? 21.135  10.988  66.026  1.00 17.74 ?  573  LYS B CA    1 
ATOM   13461 C C     . LYS B 1 575  ? 20.827  12.482  65.957  1.00 18.71 ?  573  LYS B C     1 
ATOM   13462 O O     . LYS B 1 575  ? 20.121  12.942  65.052  1.00 18.88 ?  573  LYS B O     1 
ATOM   13463 C CB    . LYS B 1 575  ? 21.572  10.447  64.669  1.00 20.40 ?  573  LYS B CB    1 
ATOM   13464 C CG    . LYS B 1 575  ? 22.769  11.174  64.074  1.00 21.77 ?  573  LYS B CG    1 
ATOM   13465 C CD    . LYS B 1 575  ? 23.205  10.506  62.789  1.00 24.88 ?  573  LYS B CD    1 
ATOM   13466 C CE    . LYS B 1 575  ? 24.362  11.261  62.150  1.00 34.46 ?  573  LYS B CE    1 
ATOM   13467 N NZ    . LYS B 1 575  ? 25.427  11.551  63.158  1.00 37.34 ?  573  LYS B NZ    1 
ATOM   13468 N N     . TRP B 1 576  ? 21.382  13.243  66.898  1.00 18.04 ?  574  TRP B N     1 
ATOM   13469 C CA    . TRP B 1 576  ? 21.198  14.685  66.979  1.00 15.85 ?  574  TRP B CA    1 
ATOM   13470 C C     . TRP B 1 576  ? 22.346  15.403  66.291  1.00 15.54 ?  574  TRP B C     1 
ATOM   13471 O O     . TRP B 1 576  ? 23.517  15.170  66.617  1.00 18.23 ?  574  TRP B O     1 
ATOM   13472 C CB    . TRP B 1 576  ? 21.123  15.136  68.436  1.00 15.19 ?  574  TRP B CB    1 
ATOM   13473 C CG    . TRP B 1 576  ? 19.964  14.585  69.189  1.00 16.44 ?  574  TRP B CG    1 
ATOM   13474 C CD1   . TRP B 1 576  ? 19.996  13.627  70.165  1.00 21.41 ?  574  TRP B CD1   1 
ATOM   13475 C CD2   . TRP B 1 576  ? 18.597  14.958  69.034  1.00 15.18 ?  574  TRP B CD2   1 
ATOM   13476 N NE1   . TRP B 1 576  ? 18.722  13.393  70.638  1.00 19.70 ?  574  TRP B NE1   1 
ATOM   13477 C CE2   . TRP B 1 576  ? 17.848  14.203  69.958  1.00 18.39 ?  574  TRP B CE2   1 
ATOM   13478 C CE3   . TRP B 1 576  ? 17.934  15.872  68.214  1.00 14.84 ?  574  TRP B CE3   1 
ATOM   13479 C CZ2   . TRP B 1 576  ? 16.462  14.325  70.069  1.00 19.93 ?  574  TRP B CZ2   1 
ATOM   13480 C CZ3   . TRP B 1 576  ? 16.558  15.992  68.324  1.00 17.44 ?  574  TRP B CZ3   1 
ATOM   13481 C CH2   . TRP B 1 576  ? 15.839  15.227  69.256  1.00 21.91 ?  574  TRP B CH2   1 
ATOM   13482 N N     . THR B 1 577  ? 22.011  16.280  65.348  1.00 16.06 ?  575  THR B N     1 
ATOM   13483 C CA    . THR B 1 577  ? 23.014  17.055  64.634  1.00 15.82 ?  575  THR B CA    1 
ATOM   13484 C C     . THR B 1 577  ? 22.591  18.515  64.577  1.00 16.25 ?  575  THR B C     1 
ATOM   13485 O O     . THR B 1 577  ? 21.418  18.864  64.748  1.00 16.51 ?  575  THR B O     1 
ATOM   13486 C CB    . THR B 1 577  ? 23.208  16.546  63.213  1.00 17.70 ?  575  THR B CB    1 
ATOM   13487 O OG1   . THR B 1 577  ? 21.988  16.770  62.497  1.00 19.34 ?  575  THR B OG1   1 
ATOM   13488 C CG2   . THR B 1 577  ? 23.529  15.075  63.210  1.00 19.00 ?  575  THR B CG2   1 
ATOM   13489 N N     . ALA B 1 578  ? 23.570  19.378  64.330  1.00 16.02 ?  576  ALA B N     1 
ATOM   13490 C CA    . ALA B 1 578  ? 23.315  20.787  64.070  1.00 13.04 ?  576  ALA B CA    1 
ATOM   13491 C C     . ALA B 1 578  ? 24.258  21.202  62.955  1.00 14.50 ?  576  ALA B C     1 
ATOM   13492 O O     . ALA B 1 578  ? 25.463  20.953  63.048  1.00 17.24 ?  576  ALA B O     1 
ATOM   13493 C CB    . ALA B 1 578  ? 23.535  21.650  65.322  1.00 15.24 ?  576  ALA B CB    1 
ATOM   13494 N N     . LEU B 1 579  ? 23.713  21.789  61.898  1.00 15.22 ?  577  LEU B N     1 
ATOM   13495 C CA    . LEU B 1 579  ? 24.461  22.145  60.702  1.00 14.97 ?  577  LEU B CA    1 
ATOM   13496 C C     . LEU B 1 579  ? 24.219  23.606  60.370  1.00 13.41 ?  577  LEU B C     1 
ATOM   13497 O O     . LEU B 1 579  ? 23.208  24.183  60.784  1.00 12.95 ?  577  LEU B O     1 
ATOM   13498 C CB    . LEU B 1 579  ? 24.018  21.289  59.506  1.00 18.81 ?  577  LEU B CB    1 
ATOM   13499 C CG    . LEU B 1 579  ? 23.830  19.793  59.731  1.00 22.54 ?  577  LEU B CG    1 
ATOM   13500 C CD1   . LEU B 1 579  ? 23.173  19.133  58.503  1.00 21.55 ?  577  LEU B CD1   1 
ATOM   13501 C CD2   . LEU B 1 579  ? 25.163  19.180  60.039  1.00 23.22 ?  577  LEU B CD2   1 
ATOM   13502 N N     . PRO B 1 580  ? 25.106  24.227  59.594  1.00 14.74 ?  578  PRO B N     1 
ATOM   13503 C CA    . PRO B 1 580  ? 24.766  25.530  59.020  1.00 13.93 ?  578  PRO B CA    1 
ATOM   13504 C C     . PRO B 1 580  ? 23.671  25.329  57.986  1.00 13.61 ?  578  PRO B C     1 
ATOM   13505 O O     . PRO B 1 580  ? 23.916  24.793  56.900  1.00 15.30 ?  578  PRO B O     1 
ATOM   13506 C CB    . PRO B 1 580  ? 26.083  26.014  58.394  1.00 14.40 ?  578  PRO B CB    1 
ATOM   13507 C CG    . PRO B 1 580  ? 27.153  25.066  58.913  1.00 16.15 ?  578  PRO B CG    1 
ATOM   13508 C CD    . PRO B 1 580  ? 26.436  23.774  59.165  1.00 16.40 ?  578  PRO B CD    1 
ATOM   13509 N N     . GLN B 1 581  ? 22.451  25.689  58.346  1.00 14.06 ?  579  GLN B N     1 
ATOM   13510 C CA    . GLN B 1 581  ? 21.277  25.475  57.498  1.00 14.40 ?  579  GLN B CA    1 
ATOM   13511 C C     . GLN B 1 581  ? 20.992  26.786  56.788  1.00 13.89 ?  579  GLN B C     1 
ATOM   13512 O O     . GLN B 1 581  ? 20.313  27.666  57.318  1.00 15.85 ?  579  GLN B O     1 
ATOM   13513 C CB    . GLN B 1 581  ? 20.079  25.029  58.329  1.00 15.02 ?  579  GLN B CB    1 
ATOM   13514 C CG    . GLN B 1 581  ? 20.285  23.727  59.039  1.00 16.44 ?  579  GLN B CG    1 
ATOM   13515 C CD    . GLN B 1 581  ? 20.294  22.523  58.115  1.00 20.43 ?  579  GLN B CD    1 
ATOM   13516 O OE1   . GLN B 1 581  ? 20.058  22.628  56.900  1.00 20.36 ?  579  GLN B OE1   1 
ATOM   13517 N NE2   . GLN B 1 581  ? 20.569  21.360  58.691  1.00 24.98 ?  579  GLN B NE2   1 
ATOM   13518 N N     . LEU B 1 582  ? 21.536  26.923  55.582  1.00 15.84 ?  580  LEU B N     1 
ATOM   13519 C CA    . LEU B 1 582  ? 21.270  28.102  54.775  1.00 15.85 ?  580  LEU B CA    1 
ATOM   13520 C C     . LEU B 1 582  ? 20.030  27.868  53.916  1.00 16.12 ?  580  LEU B C     1 
ATOM   13521 O O     . LEU B 1 582  ? 19.476  26.769  53.873  1.00 19.01 ?  580  LEU B O     1 
ATOM   13522 C CB    . LEU B 1 582  ? 22.486  28.455  53.914  1.00 17.33 ?  580  LEU B CB    1 
ATOM   13523 C CG    . LEU B 1 582  ? 23.640  29.196  54.623  1.00 20.01 ?  580  LEU B CG    1 
ATOM   13524 C CD1   . LEU B 1 582  ? 24.298  28.382  55.744  1.00 21.13 ?  580  LEU B CD1   1 
ATOM   13525 C CD2   . LEU B 1 582  ? 24.690  29.622  53.615  1.00 26.02 ?  580  LEU B CD2   1 
ATOM   13526 N N     . ALA B 1 583  ? 19.583  28.933  53.246  1.00 16.82 ?  581  ALA B N     1 
ATOM   13527 C CA    . ALA B 1 583  ? 18.360  28.851  52.452  1.00 17.88 ?  581  ALA B CA    1 
ATOM   13528 C C     . ALA B 1 583  ? 18.462  27.782  51.372  1.00 21.74 ?  581  ALA B C     1 
ATOM   13529 O O     . ALA B 1 583  ? 17.455  27.163  51.012  1.00 26.09 ?  581  ALA B O     1 
ATOM   13530 C CB    . ALA B 1 583  ? 18.056  30.211  51.820  1.00 20.63 ?  581  ALA B CB    1 
ATOM   13531 N N     . THR B 1 584  ? 19.665  27.542  50.865  1.00 15.72 ?  582  THR B N     1 
ATOM   13532 C CA    . THR B 1 584  ? 19.923  26.606  49.780  1.00 19.79 ?  582  THR B CA    1 
ATOM   13533 C C     . THR B 1 584  ? 20.255  25.203  50.268  1.00 19.14 ?  582  THR B C     1 
ATOM   13534 O O     . THR B 1 584  ? 20.538  24.324  49.445  1.00 21.77 ?  582  THR B O     1 
ATOM   13535 C CB    . THR B 1 584  ? 21.081  27.119  48.923  1.00 20.62 ?  582  THR B CB    1 
ATOM   13536 O OG1   . THR B 1 584  ? 22.134  27.563  49.792  1.00 24.65 ?  582  THR B OG1   1 
ATOM   13537 C CG2   . THR B 1 584  ? 20.623  28.278  48.058  1.00 29.56 ?  582  THR B CG2   1 
ATOM   13538 N N     . GLY B 1 585  ? 20.270  24.976  51.573  1.00 18.83 ?  583  GLY B N     1 
ATOM   13539 C CA    . GLY B 1 585  ? 20.624  23.682  52.101  1.00 17.00 ?  583  GLY B CA    1 
ATOM   13540 C C     . GLY B 1 585  ? 21.734  23.788  53.124  1.00 16.65 ?  583  GLY B C     1 
ATOM   13541 O O     . GLY B 1 585  ? 22.262  24.876  53.393  1.00 19.84 ?  583  GLY B O     1 
ATOM   13542 N N     . PRO B 1 586  ? 22.080  22.658  53.744  1.00 16.66 ?  584  PRO B N     1 
ATOM   13543 C CA    . PRO B 1 586  ? 23.172  22.662  54.723  1.00 15.90 ?  584  PRO B CA    1 
ATOM   13544 C C     . PRO B 1 586  ? 24.518  22.857  54.053  1.00 18.51 ?  584  PRO B C     1 
ATOM   13545 O O     . PRO B 1 586  ? 24.797  22.303  52.986  1.00 20.83 ?  584  PRO B O     1 
ATOM   13546 C CB    . PRO B 1 586  ? 23.081  21.279  55.374  1.00 18.14 ?  584  PRO B CB    1 
ATOM   13547 C CG    . PRO B 1 586  ? 22.467  20.420  54.315  1.00 22.31 ?  584  PRO B CG    1 
ATOM   13548 C CD    . PRO B 1 586  ? 21.480  21.319  53.596  1.00 20.49 ?  584  PRO B CD    1 
ATOM   13549 N N     . ALA B 1 587  ? 25.358  23.637  54.712  1.00 16.33 ?  585  ALA B N     1 
ATOM   13550 C CA    . ALA B 1 587  ? 26.707  23.922  54.254  1.00 16.94 ?  585  ALA B CA    1 
ATOM   13551 C C     . ALA B 1 587  ? 27.707  23.024  54.962  1.00 16.94 ?  585  ALA B C     1 
ATOM   13552 O O     . ALA B 1 587  ? 27.481  22.574  56.092  1.00 17.98 ?  585  ALA B O     1 
ATOM   13553 C CB    . ALA B 1 587  ? 27.054  25.391  54.517  1.00 19.13 ?  585  ALA B CB    1 
ATOM   13554 N N     . ALA B 1 588  ? 28.833  22.786  54.292  1.00 18.63 ?  586  ALA B N     1 
ATOM   13555 C CA    . ALA B 1 588  ? 29.934  22.065  54.910  1.00 18.01 ?  586  ALA B CA    1 
ATOM   13556 C C     . ALA B 1 588  ? 30.640  22.939  55.940  1.00 18.03 ?  586  ALA B C     1 
ATOM   13557 O O     . ALA B 1 588  ? 30.615  24.169  55.869  1.00 22.49 ?  586  ALA B O     1 
ATOM   13558 C CB    . ALA B 1 588  ? 30.939  21.625  53.850  1.00 18.87 ?  586  ALA B CB    1 
ATOM   13559 N N     . GLY B 1 589  ? 31.292  22.294  56.894  1.00 19.81 ?  587  GLY B N     1 
ATOM   13560 C CA    . GLY B 1 589  ? 32.079  23.051  57.845  1.00 20.81 ?  587  GLY B CA    1 
ATOM   13561 C C     . GLY B 1 589  ? 32.853  22.138  58.767  1.00 22.28 ?  587  GLY B C     1 
ATOM   13562 O O     . GLY B 1 589  ? 32.928  20.928  58.558  1.00 24.15 ?  587  GLY B O     1 
ATOM   13563 N N     . GLU B 1 590  ? 33.427  22.745  59.808  1.00 23.12 ?  588  GLU B N     1 
ATOM   13564 C CA    . GLU B 1 590  ? 34.205  22.000  60.790  1.00 23.52 ?  588  GLU B CA    1 
ATOM   13565 C C     . GLU B 1 590  ? 33.270  21.344  61.793  1.00 22.42 ?  588  GLU B C     1 
ATOM   13566 O O     . GLU B 1 590  ? 32.421  22.010  62.387  1.00 22.14 ?  588  GLU B O     1 
ATOM   13567 C CB    . GLU B 1 590  ? 35.180  22.927  61.514  1.00 28.80 ?  588  GLU B CB    1 
ATOM   13568 C CG    . GLU B 1 590  ? 36.399  23.294  60.708  1.00 35.82 ?  588  GLU B CG    1 
ATOM   13569 C CD    . GLU B 1 590  ? 37.308  22.106  60.465  1.00 40.01 ?  588  GLU B CD    1 
ATOM   13570 O OE1   . GLU B 1 590  ? 37.743  21.468  61.452  1.00 41.99 ?  588  GLU B OE1   1 
ATOM   13571 O OE2   . GLU B 1 590  ? 37.574  21.803  59.283  1.00 49.41 ?  588  GLU B OE2   1 
ATOM   13572 N N     . THR B 1 591  ? 33.435  20.045  61.995  1.00 20.97 ?  589  THR B N     1 
ATOM   13573 C CA    . THR B 1 591  ? 32.514  19.267  62.811  1.00 20.54 ?  589  THR B CA    1 
ATOM   13574 C C     . THR B 1 591  ? 33.180  18.804  64.101  1.00 22.35 ?  589  THR B C     1 
ATOM   13575 O O     . THR B 1 591  ? 34.358  18.423  64.107  1.00 23.95 ?  589  THR B O     1 
ATOM   13576 C CB    . THR B 1 591  ? 31.997  18.072  62.015  1.00 19.84 ?  589  THR B CB    1 
ATOM   13577 O OG1   . THR B 1 591  ? 31.333  18.559  60.840  1.00 24.44 ?  589  THR B OG1   1 
ATOM   13578 C CG2   . THR B 1 591  ? 31.023  17.254  62.828  1.00 23.40 ?  589  THR B CG2   1 
ATOM   13579 N N     . ARG B 1 592  ? 32.418  18.856  65.193  1.00 20.09 ?  590  ARG B N     1 
ATOM   13580 C CA    . ARG B 1 592  ? 32.894  18.378  66.480  1.00 18.95 ?  590  ARG B CA    1 
ATOM   13581 C C     . ARG B 1 592  ? 31.722  17.820  67.270  1.00 20.18 ?  590  ARG B C     1 
ATOM   13582 O O     . ARG B 1 592  ? 30.557  18.066  66.948  1.00 21.09 ?  590  ARG B O     1 
ATOM   13583 C CB    . ARG B 1 592  ? 33.585  19.488  67.271  1.00 25.91 ?  590  ARG B CB    1 
ATOM   13584 C CG    . ARG B 1 592  ? 32.652  20.591  67.672  1.00 23.63 ?  590  ARG B CG    1 
ATOM   13585 C CD    . ARG B 1 592  ? 33.168  21.341  68.877  1.00 29.59 ?  590  ARG B CD    1 
ATOM   13586 N NE    . ARG B 1 592  ? 32.345  22.511  69.145  1.00 29.19 ?  590  ARG B NE    1 
ATOM   13587 C CZ    . ARG B 1 592  ? 31.322  22.525  69.983  1.00 27.67 ?  590  ARG B CZ    1 
ATOM   13588 N NH1   . ARG B 1 592  ? 30.964  21.441  70.657  1.00 24.53 ?  590  ARG B NH1   1 
ATOM   13589 N NH2   . ARG B 1 592  ? 30.645  23.657  70.156  1.00 30.06 ?  590  ARG B NH2   1 
ATOM   13590 N N     . THR B 1 593  ? 32.043  17.058  68.307  1.00 22.00 ?  591  THR B N     1 
ATOM   13591 C CA    . THR B 1 593  ? 31.015  16.475  69.145  1.00 20.36 ?  591  THR B CA    1 
ATOM   13592 C C     . THR B 1 593  ? 30.526  17.479  70.183  1.00 20.52 ?  591  THR B C     1 
ATOM   13593 O O     . THR B 1 593  ? 31.216  18.437  70.548  1.00 22.01 ?  591  THR B O     1 
ATOM   13594 C CB    . THR B 1 593  ? 31.540  15.233  69.852  1.00 22.01 ?  591  THR B CB    1 
ATOM   13595 O OG1   . THR B 1 593  ? 32.661  15.601  70.664  1.00 26.32 ?  591  THR B OG1   1 
ATOM   13596 C CG2   . THR B 1 593  ? 31.975  14.196  68.831  1.00 27.19 ?  591  THR B CG2   1 
ATOM   13597 N N     . VAL B 1 594  ? 29.302  17.240  70.648  1.00 19.24 ?  592  VAL B N     1 
ATOM   13598 C CA    . VAL B 1 594  ? 28.672  17.980  71.732  1.00 19.12 ?  592  VAL B CA    1 
ATOM   13599 C C     . VAL B 1 594  ? 28.541  17.022  72.906  1.00 21.12 ?  592  VAL B C     1 
ATOM   13600 O O     . VAL B 1 594  ? 27.937  15.951  72.770  1.00 19.88 ?  592  VAL B O     1 
ATOM   13601 C CB    . VAL B 1 594  ? 27.300  18.521  71.300  1.00 18.84 ?  592  VAL B CB    1 
ATOM   13602 C CG1   . VAL B 1 594  ? 26.642  19.303  72.429  1.00 19.37 ?  592  VAL B CG1   1 
ATOM   13603 C CG2   . VAL B 1 594  ? 27.435  19.365  70.020  1.00 19.83 ?  592  VAL B CG2   1 
ATOM   13604 N N     . LEU B 1 595  ? 29.127  17.386  74.049  1.00 21.73 ?  593  LEU B N     1 
ATOM   13605 C CA    . LEU B 1 595  ? 29.207  16.505  75.206  1.00 21.33 ?  593  LEU B CA    1 
ATOM   13606 C C     . LEU B 1 595  ? 28.268  16.961  76.321  1.00 18.42 ?  593  LEU B C     1 
ATOM   13607 O O     . LEU B 1 595  ? 27.995  18.155  76.484  1.00 21.44 ?  593  LEU B O     1 
ATOM   13608 C CB    . LEU B 1 595  ? 30.643  16.444  75.740  1.00 22.67 ?  593  LEU B CB    1 
ATOM   13609 C CG    . LEU B 1 595  ? 31.701  16.032  74.715  1.00 22.13 ?  593  LEU B CG    1 
ATOM   13610 C CD1   . LEU B 1 595  ? 33.066  16.051  75.379  1.00 24.66 ?  593  LEU B CD1   1 
ATOM   13611 C CD2   . LEU B 1 595  ? 31.399  14.660  74.129  1.00 22.73 ?  593  LEU B CD2   1 
ATOM   13612 N N     . ASN B 1 596  ? 27.777  15.995  77.086  1.00 16.48 ?  594  ASN B N     1 
ATOM   13613 C CA    . ASN B 1 596  ? 26.929  16.266  78.252  1.00 16.99 ?  594  ASN B CA    1 
ATOM   13614 C C     . ASN B 1 596  ? 27.747  16.965  79.335  1.00 17.51 ?  594  ASN B C     1 
ATOM   13615 O O     . ASN B 1 596  ? 28.736  16.393  79.805  1.00 17.52 ?  594  ASN B O     1 
ATOM   13616 C CB    . ASN B 1 596  ? 26.368  14.927  78.749  1.00 17.90 ?  594  ASN B CB    1 
ATOM   13617 C CG    . ASN B 1 596  ? 25.323  15.061  79.851  1.00 18.12 ?  594  ASN B CG    1 
ATOM   13618 O OD1   . ASN B 1 596  ? 25.300  16.014  80.627  1.00 18.97 ?  594  ASN B OD1   1 
ATOM   13619 N ND2   . ASN B 1 596  ? 24.447  14.066  79.922  1.00 22.06 ?  594  ASN B ND2   1 
ATOM   13620 N N     . PRO B 1 597  ? 27.377  18.178  79.770  1.00 15.63 ?  595  PRO B N     1 
ATOM   13621 C CA    . PRO B 1 597  ? 28.163  18.854  80.820  1.00 17.37 ?  595  PRO B CA    1 
ATOM   13622 C C     . PRO B 1 597  ? 28.200  18.085  82.118  1.00 17.96 ?  595  PRO B C     1 
ATOM   13623 O O     . PRO B 1 597  ? 29.131  18.283  82.909  1.00 19.85 ?  595  PRO B O     1 
ATOM   13624 C CB    . PRO B 1 597  ? 27.462  20.209  80.994  1.00 17.58 ?  595  PRO B CB    1 
ATOM   13625 C CG    . PRO B 1 597  ? 26.147  20.073  80.310  1.00 20.73 ?  595  PRO B CG    1 
ATOM   13626 C CD    . PRO B 1 597  ? 26.274  19.012  79.265  1.00 17.08 ?  595  PRO B CD    1 
ATOM   13627 N N     . GLY B 1 598  ? 27.225  17.207  82.359  1.00 17.87 ?  596  GLY B N     1 
ATOM   13628 C CA    . GLY B 1 598  ? 27.208  16.406  83.568  1.00 19.56 ?  596  GLY B CA    1 
ATOM   13629 C C     . GLY B 1 598  ? 28.030  15.141  83.497  1.00 20.48 ?  596  GLY B C     1 
ATOM   13630 O O     . GLY B 1 598  ? 28.237  14.486  84.523  1.00 21.37 ?  596  GLY B O     1 
ATOM   13631 N N     . ASP B 1 599  ? 28.519  14.796  82.309  1.00 18.75 ?  597  ASP B N     1 
ATOM   13632 C CA    . ASP B 1 599  ? 29.293  13.578  82.099  1.00 21.56 ?  597  ASP B CA    1 
ATOM   13633 C C     . ASP B 1 599  ? 29.855  13.634  80.691  1.00 21.25 ?  597  ASP B C     1 
ATOM   13634 O O     . ASP B 1 599  ? 29.151  13.303  79.734  1.00 20.30 ?  597  ASP B O     1 
ATOM   13635 C CB    . ASP B 1 599  ? 28.417  12.335  82.280  1.00 21.59 ?  597  ASP B CB    1 
ATOM   13636 C CG    . ASP B 1 599  ? 29.206  11.037  82.228  1.00 27.01 ?  597  ASP B CG    1 
ATOM   13637 O OD1   . ASP B 1 599  ? 30.344  11.032  81.705  1.00 23.87 ?  597  ASP B OD1   1 
ATOM   13638 O OD2   . ASP B 1 599  ? 28.678  10.014  82.714  1.00 29.21 ?  597  ASP B OD2   1 
ATOM   13639 N N     . HIS B 1 600  ? 31.106  14.070  80.550  1.00 21.85 ?  598  HIS B N     1 
ATOM   13640 C CA    . HIS B 1 600  ? 31.671  14.272  79.224  1.00 22.33 ?  598  HIS B CA    1 
ATOM   13641 C C     . HIS B 1 600  ? 31.833  12.973  78.438  1.00 22.25 ?  598  HIS B C     1 
ATOM   13642 O O     . HIS B 1 600  ? 32.112  13.035  77.238  1.00 25.12 ?  598  HIS B O     1 
ATOM   13643 C CB    . HIS B 1 600  ? 33.012  15.005  79.340  1.00 24.18 ?  598  HIS B CB    1 
ATOM   13644 C CG    . HIS B 1 600  ? 32.874  16.464  79.658  1.00 26.63 ?  598  HIS B CG    1 
ATOM   13645 N ND1   . HIS B 1 600  ? 33.960  17.304  79.798  1.00 27.48 ?  598  HIS B ND1   1 
ATOM   13646 C CD2   . HIS B 1 600  ? 31.777  17.230  79.870  1.00 19.92 ?  598  HIS B CD2   1 
ATOM   13647 C CE1   . HIS B 1 600  ? 33.537  18.524  80.078  1.00 28.66 ?  598  HIS B CE1   1 
ATOM   13648 N NE2   . HIS B 1 600  ? 32.216  18.506  80.128  1.00 24.22 ?  598  HIS B NE2   1 
ATOM   13649 N N     . ARG B 1 601  ? 31.657  11.809  79.072  1.00 23.31 ?  599  ARG B N     1 
ATOM   13650 C CA    . ARG B 1 601  ? 31.651  10.543  78.349  1.00 24.46 ?  599  ARG B CA    1 
ATOM   13651 C C     . ARG B 1 601  ? 30.385  10.346  77.524  1.00 24.79 ?  599  ARG B C     1 
ATOM   13652 O O     . ARG B 1 601  ? 30.358  9.462   76.657  1.00 25.77 ?  599  ARG B O     1 
ATOM   13653 C CB    . ARG B 1 601  ? 31.801  9.386   79.333  1.00 24.62 ?  599  ARG B CB    1 
ATOM   13654 C CG    . ARG B 1 601  ? 33.032  9.492   80.200  1.00 29.16 ?  599  ARG B CG    1 
ATOM   13655 C CD    . ARG B 1 601  ? 32.983  8.498   81.347  1.00 29.03 ?  599  ARG B CD    1 
ATOM   13656 N NE    . ARG B 1 601  ? 31.789  8.686   82.161  1.00 30.32 ?  599  ARG B NE    1 
ATOM   13657 C CZ    . ARG B 1 601  ? 31.459  7.925   83.194  1.00 30.85 ?  599  ARG B CZ    1 
ATOM   13658 N NH1   . ARG B 1 601  ? 32.214  6.901   83.564  1.00 34.03 ?  599  ARG B NH1   1 
ATOM   13659 N NH2   . ARG B 1 601  ? 30.340  8.191   83.865  1.00 30.24 ?  599  ARG B NH2   1 
ATOM   13660 N N     . ASP B 1 602  ? 29.345  11.136  77.778  1.00 23.05 ?  600  ASP B N     1 
ATOM   13661 C CA    . ASP B 1 602  ? 28.067  11.014  77.082  1.00 24.66 ?  600  ASP B CA    1 
ATOM   13662 C C     . ASP B 1 602  ? 28.089  11.980  75.905  1.00 23.78 ?  600  ASP B C     1 
ATOM   13663 O O     . ASP B 1 602  ? 27.937  13.192  76.080  1.00 23.84 ?  600  ASP B O     1 
ATOM   13664 C CB    . ASP B 1 602  ? 26.919  11.308  78.041  1.00 24.22 ?  600  ASP B CB    1 
ATOM   13665 C CG    . ASP B 1 602  ? 25.556  11.160  77.393  1.00 25.99 ?  600  ASP B CG    1 
ATOM   13666 O OD1   . ASP B 1 602  ? 25.448  10.438  76.384  1.00 26.75 ?  600  ASP B OD1   1 
ATOM   13667 O OD2   . ASP B 1 602  ? 24.593  11.779  77.901  1.00 28.16 ?  600  ASP B OD2   1 
ATOM   13668 N N     . VAL B 1 603  ? 28.292  11.444  74.704  1.00 25.06 ?  601  VAL B N     1 
ATOM   13669 C CA    . VAL B 1 603  ? 28.270  12.243  73.483  1.00 23.01 ?  601  VAL B CA    1 
ATOM   13670 C C     . VAL B 1 603  ? 26.816  12.460  73.088  1.00 22.01 ?  601  VAL B C     1 
ATOM   13671 O O     . VAL B 1 603  ? 26.088  11.507  72.791  1.00 26.69 ?  601  VAL B O     1 
ATOM   13672 C CB    . VAL B 1 603  ? 29.062  11.561  72.358  1.00 23.15 ?  601  VAL B CB    1 
ATOM   13673 C CG1   . VAL B 1 603  ? 29.044  12.423  71.096  1.00 22.05 ?  601  VAL B CG1   1 
ATOM   13674 C CG2   . VAL B 1 603  ? 30.492  11.281  72.805  1.00 25.78 ?  601  VAL B CG2   1 
ATOM   13675 N N     . VAL B 1 604  ? 26.377  13.712  73.119  1.00 18.19 ?  602  VAL B N     1 
ATOM   13676 C CA    . VAL B 1 604  ? 24.981  14.003  72.833  1.00 18.01 ?  602  VAL B CA    1 
ATOM   13677 C C     . VAL B 1 604  ? 24.729  14.112  71.337  1.00 19.61 ?  602  VAL B C     1 
ATOM   13678 O O     . VAL B 1 604  ? 23.686  13.662  70.855  1.00 19.16 ?  602  VAL B O     1 
ATOM   13679 C CB    . VAL B 1 604  ? 24.550  15.283  73.565  1.00 16.25 ?  602  VAL B CB    1 
ATOM   13680 C CG1   . VAL B 1 604  ? 23.076  15.536  73.379  1.00 16.54 ?  602  VAL B CG1   1 
ATOM   13681 C CG2   . VAL B 1 604  ? 24.882  15.171  75.063  1.00 17.69 ?  602  VAL B CG2   1 
ATOM   13682 N N     . GLY B 1 605  ? 25.680  14.642  70.580  1.00 17.33 ?  603  GLY B N     1 
ATOM   13683 C CA    . GLY B 1 605  ? 25.451  14.845  69.163  1.00 17.49 ?  603  GLY B CA    1 
ATOM   13684 C C     . GLY B 1 605  ? 26.676  15.451  68.527  1.00 18.86 ?  603  GLY B C     1 
ATOM   13685 O O     . GLY B 1 605  ? 27.755  15.481  69.120  1.00 20.19 ?  603  GLY B O     1 
ATOM   13686 N N     . SER B 1 606  ? 26.482  15.971  67.324  1.00 16.89 ?  604  SER B N     1 
ATOM   13687 C CA    A SER B 1 606  ? 27.564  16.523  66.518  0.36 19.07 ?  604  SER B CA    1 
ATOM   13688 C CA    B SER B 1 606  ? 27.558  16.516  66.511  0.36 19.07 ?  604  SER B CA    1 
ATOM   13689 C CA    C SER B 1 606  ? 27.570  16.535  66.540  0.28 19.08 ?  604  SER B CA    1 
ATOM   13690 C C     . SER B 1 606  ? 27.124  17.853  65.929  1.00 19.09 ?  604  SER B C     1 
ATOM   13691 O O     . SER B 1 606  ? 25.984  17.995  65.476  1.00 19.37 ?  604  SER B O     1 
ATOM   13692 C CB    A SER B 1 606  ? 27.979  15.565  65.387  0.36 21.17 ?  604  SER B CB    1 
ATOM   13693 C CB    B SER B 1 606  ? 27.927  15.538  65.391  0.36 21.17 ?  604  SER B CB    1 
ATOM   13694 C CB    C SER B 1 606  ? 28.029  15.578  65.435  0.28 21.17 ?  604  SER B CB    1 
ATOM   13695 O OG    A SER B 1 606  ? 28.712  14.457  65.886  0.36 22.34 ?  604  SER B OG    1 
ATOM   13696 O OG    B SER B 1 606  ? 28.557  16.200  64.318  0.36 19.28 ?  604  SER B OG    1 
ATOM   13697 O OG    C SER B 1 606  ? 27.011  15.403  64.471  0.28 19.04 ?  604  SER B OG    1 
ATOM   13698 N N     . VAL B 1 607  ? 28.022  18.832  65.941  1.00 17.00 ?  605  VAL B N     1 
ATOM   13699 C CA    . VAL B 1 607  ? 27.727  20.145  65.382  1.00 16.29 ?  605  VAL B CA    1 
ATOM   13700 C C     . VAL B 1 607  ? 28.736  20.447  64.287  1.00 16.66 ?  605  VAL B C     1 
ATOM   13701 O O     . VAL B 1 607  ? 29.939  20.202  64.448  1.00 17.33 ?  605  VAL B O     1 
ATOM   13702 C CB    . VAL B 1 607  ? 27.727  21.257  66.448  1.00 15.32 ?  605  VAL B CB    1 
ATOM   13703 C CG1   . VAL B 1 607  ? 29.044  21.307  67.219  1.00 18.20 ?  605  VAL B CG1   1 
ATOM   13704 C CG2   . VAL B 1 607  ? 27.424  22.623  65.801  1.00 14.68 ?  605  VAL B CG2   1 
ATOM   13705 N N     . THR B 1 608  ? 28.236  20.956  63.171  1.00 17.34 ?  606  THR B N     1 
ATOM   13706 C CA    . THR B 1 608  ? 29.063  21.453  62.084  1.00 16.93 ?  606  THR B CA    1 
ATOM   13707 C C     . THR B 1 608  ? 28.950  22.969  62.122  1.00 16.36 ?  606  THR B C     1 
ATOM   13708 O O     . THR B 1 608  ? 27.847  23.513  62.014  1.00 16.64 ?  606  THR B O     1 
ATOM   13709 C CB    . THR B 1 608  ? 28.589  20.887  60.749  1.00 17.03 ?  606  THR B CB    1 
ATOM   13710 O OG1   . THR B 1 608  ? 28.741  19.463  60.778  1.00 19.41 ?  606  THR B OG1   1 
ATOM   13711 C CG2   . THR B 1 608  ? 29.403  21.456  59.597  1.00 18.48 ?  606  THR B CG2   1 
ATOM   13712 N N     . GLU B 1 609  ? 30.076  23.646  62.309  1.00 17.93 ?  607  GLU B N     1 
ATOM   13713 C CA    . GLU B 1 609  ? 30.043  25.075  62.558  1.00 17.79 ?  607  GLU B CA    1 
ATOM   13714 C C     . GLU B 1 609  ? 30.255  25.861  61.265  1.00 18.41 ?  607  GLU B C     1 
ATOM   13715 O O     . GLU B 1 609  ? 30.779  25.353  60.272  1.00 19.41 ?  607  GLU B O     1 
ATOM   13716 C CB    . GLU B 1 609  ? 31.057  25.440  63.650  1.00 22.79 ?  607  GLU B CB    1 
ATOM   13717 C CG    . GLU B 1 609  ? 30.577  24.857  64.988  1.00 24.00 ?  607  GLU B CG    1 
ATOM   13718 C CD    . GLU B 1 609  ? 31.462  25.171  66.177  1.00 26.96 ?  607  GLU B CD    1 
ATOM   13719 O OE1   . GLU B 1 609  ? 32.700  25.233  66.008  1.00 30.46 ?  607  GLU B OE1   1 
ATOM   13720 O OE2   . GLU B 1 609  ? 30.910  25.333  67.286  1.00 26.48 ?  607  GLU B OE2   1 
ATOM   13721 N N     . THR B 1 610  ? 29.788  27.107  61.291  1.00 18.95 ?  608  THR B N     1 
ATOM   13722 C CA    . THR B 1 610  ? 29.624  27.937  60.103  1.00 16.47 ?  608  THR B CA    1 
ATOM   13723 C C     . THR B 1 610  ? 30.907  28.705  59.803  1.00 16.96 ?  608  THR B C     1 
ATOM   13724 O O     . THR B 1 610  ? 31.472  29.338  60.695  1.00 21.38 ?  608  THR B O     1 
ATOM   13725 C CB    . THR B 1 610  ? 28.480  28.934  60.311  1.00 16.77 ?  608  THR B CB    1 
ATOM   13726 O OG1   . THR B 1 610  ? 27.316  28.257  60.807  1.00 16.55 ?  608  THR B OG1   1 
ATOM   13727 C CG2   . THR B 1 610  ? 28.129  29.629  58.996  1.00 16.50 ?  608  THR B CG2   1 
ATOM   13728 N N     . SER B 1 611  ? 31.358  28.668  58.555  1.00 18.31 ?  609  SER B N     1 
ATOM   13729 C CA    . SER B 1 611  ? 32.454  29.548  58.180  1.00 19.96 ?  609  SER B CA    1 
ATOM   13730 C C     . SER B 1 611  ? 31.964  30.993  58.128  1.00 19.62 ?  609  SER B C     1 
ATOM   13731 O O     . SER B 1 611  ? 30.774  31.263  57.932  1.00 19.61 ?  609  SER B O     1 
ATOM   13732 C CB    . SER B 1 611  ? 33.028  29.138  56.827  1.00 22.61 ?  609  SER B CB    1 
ATOM   13733 O OG    . SER B 1 611  ? 32.147  29.469  55.770  1.00 20.89 ?  609  SER B OG    1 
ATOM   13734 N N     . GLU B 1 612  ? 32.893  31.939  58.312  1.00 22.33 ?  610  GLU B N     1 
ATOM   13735 C CA    . GLU B 1 612  ? 32.511  33.347  58.218  1.00 22.24 ?  610  GLU B CA    1 
ATOM   13736 C C     . GLU B 1 612  ? 31.986  33.682  56.824  1.00 24.15 ?  610  GLU B C     1 
ATOM   13737 O O     . GLU B 1 612  ? 31.028  34.458  56.683  1.00 20.21 ?  610  GLU B O     1 
ATOM   13738 C CB    . GLU B 1 612  ? 33.694  34.249  58.585  1.00 28.94 ?  610  GLU B CB    1 
ATOM   13739 C CG    . GLU B 1 612  ? 34.081  34.182  60.050  1.00 31.39 ?  610  GLU B CG    1 
ATOM   13740 C CD    . GLU B 1 612  ? 35.221  35.128  60.406  1.00 38.54 ?  610  GLU B CD    1 
ATOM   13741 O OE1   . GLU B 1 612  ? 35.166  36.313  60.012  1.00 43.35 ?  610  GLU B OE1   1 
ATOM   13742 O OE2   . GLU B 1 612  ? 36.170  34.683  61.082  1.00 43.71 ?  610  GLU B OE2   1 
ATOM   13743 N N     . GLU B 1 613  ? 32.591  33.098  55.788  1.00 25.48 ?  611  GLU B N     1 
ATOM   13744 C CA    . GLU B 1 613  ? 32.099  33.283  54.424  1.00 23.22 ?  611  GLU B CA    1 
ATOM   13745 C C     . GLU B 1 613  ? 30.637  32.851  54.299  1.00 21.86 ?  611  GLU B C     1 
ATOM   13746 O O     . GLU B 1 613  ? 29.820  33.560  53.703  1.00 23.17 ?  611  GLU B O     1 
ATOM   13747 C CB    . GLU B 1 613  ? 32.989  32.510  53.446  1.00 26.68 ?  611  GLU B CB    1 
ATOM   13748 C CG    . GLU B 1 613  ? 32.477  32.439  52.014  1.00 28.22 ?  611  GLU B CG    1 
ATOM   13749 C CD    . GLU B 1 613  ? 33.406  31.644  51.105  1.00 42.09 ?  611  GLU B CD    1 
ATOM   13750 O OE1   . GLU B 1 613  ? 34.628  31.911  51.112  1.00 43.51 ?  611  GLU B OE1   1 
ATOM   13751 O OE2   . GLU B 1 613  ? 32.915  30.739  50.396  1.00 44.76 ?  611  GLU B OE2   1 
ATOM   13752 N N     . ASP B 1 614  ? 30.291  31.686  54.857  1.00 21.42 ?  612  ASP B N     1 
ATOM   13753 C CA    . ASP B 1 614  ? 28.908  31.217  54.780  1.00 20.64 ?  612  ASP B CA    1 
ATOM   13754 C C     . ASP B 1 614  ? 27.971  32.050  55.644  1.00 20.59 ?  612  ASP B C     1 
ATOM   13755 O O     . ASP B 1 614  ? 26.786  32.184  55.318  1.00 17.93 ?  612  ASP B O     1 
ATOM   13756 C CB    . ASP B 1 614  ? 28.827  29.740  55.165  1.00 18.83 ?  612  ASP B CB    1 
ATOM   13757 C CG    . ASP B 1 614  ? 29.268  28.818  54.029  1.00 23.23 ?  612  ASP B CG    1 
ATOM   13758 O OD1   . ASP B 1 614  ? 29.242  29.246  52.848  1.00 27.76 ?  612  ASP B OD1   1 
ATOM   13759 O OD2   . ASP B 1 614  ? 29.631  27.659  54.309  1.00 26.05 ?  612  ASP B OD2   1 
ATOM   13760 N N     . ALA B 1 615  ? 28.466  32.602  56.751  1.00 18.54 ?  613  ALA B N     1 
ATOM   13761 C CA    . ALA B 1 615  ? 27.657  33.542  57.515  1.00 17.61 ?  613  ALA B CA    1 
ATOM   13762 C C     . ALA B 1 615  ? 27.269  34.737  56.654  1.00 18.62 ?  613  ALA B C     1 
ATOM   13763 O O     . ALA B 1 615  ? 26.099  35.143  56.619  1.00 17.06 ?  613  ALA B O     1 
ATOM   13764 C CB    . ALA B 1 615  ? 28.410  33.989  58.770  1.00 18.89 ?  613  ALA B CB    1 
ATOM   13765 N N     . ARG B 1 616  ? 28.240  35.314  55.939  1.00 19.00 ?  614  ARG B N     1 
ATOM   13766 C CA    . ARG B 1 616  ? 27.915  36.439  55.070  1.00 20.86 ?  614  ARG B CA    1 
ATOM   13767 C C     . ARG B 1 616  ? 26.965  36.017  53.958  1.00 18.87 ?  614  ARG B C     1 
ATOM   13768 O O     . ARG B 1 616  ? 26.038  36.761  53.617  1.00 18.82 ?  614  ARG B O     1 
ATOM   13769 C CB    . ARG B 1 616  ? 29.195  37.052  54.502  1.00 20.73 ?  614  ARG B CB    1 
ATOM   13770 C CG    . ARG B 1 616  ? 29.973  37.820  55.576  1.00 23.73 ?  614  ARG B CG    1 
ATOM   13771 C CD    . ARG B 1 616  ? 31.157  38.576  54.990  1.00 32.43 ?  614  ARG B CD    1 
ATOM   13772 N NE    . ARG B 1 616  ? 32.265  37.682  54.685  1.00 36.19 ?  614  ARG B NE    1 
ATOM   13773 C CZ    . ARG B 1 616  ? 33.165  37.287  55.574  1.00 34.26 ?  614  ARG B CZ    1 
ATOM   13774 N NH1   . ARG B 1 616  ? 33.120  37.698  56.832  1.00 38.53 ?  614  ARG B NH1   1 
ATOM   13775 N NH2   . ARG B 1 616  ? 34.125  36.451  55.196  1.00 35.15 ?  614  ARG B NH2   1 
ATOM   13776 N N     . ARG B 1 617  ? 27.165  34.821  53.391  1.00 19.85 ?  615  ARG B N     1 
ATOM   13777 C CA    . ARG B 1 617  ? 26.259  34.331  52.355  1.00 19.01 ?  615  ARG B CA    1 
ATOM   13778 C C     . ARG B 1 617  ? 24.835  34.234  52.882  1.00 17.00 ?  615  ARG B C     1 
ATOM   13779 O O     . ARG B 1 617  ? 23.878  34.626  52.201  1.00 18.06 ?  615  ARG B O     1 
ATOM   13780 C CB    . ARG B 1 617  ? 26.741  32.969  51.846  1.00 21.30 ?  615  ARG B CB    1 
ATOM   13781 C CG    . ARG B 1 617  ? 25.931  32.412  50.690  1.00 26.05 ?  615  ARG B CG    1 
ATOM   13782 C CD    . ARG B 1 617  ? 26.745  31.395  49.904  1.00 30.97 ?  615  ARG B CD    1 
ATOM   13783 N NE    . ARG B 1 617  ? 26.911  30.125  50.603  1.00 29.13 ?  615  ARG B NE    1 
ATOM   13784 C CZ    . ARG B 1 617  ? 26.026  29.136  50.571  1.00 34.62 ?  615  ARG B CZ    1 
ATOM   13785 N NH1   . ARG B 1 617  ? 24.868  29.266  49.940  1.00 32.96 ?  615  ARG B NH1   1 
ATOM   13786 N NH2   . ARG B 1 617  ? 26.304  27.994  51.196  1.00 34.04 ?  615  ARG B NH2   1 
ATOM   13787 N N     . ALA B 1 618  ? 24.681  33.716  54.098  1.00 16.20 ?  616  ALA B N     1 
ATOM   13788 C CA    . ALA B 1 618  ? 23.356  33.597  54.689  1.00 15.47 ?  616  ALA B CA    1 
ATOM   13789 C C     . ALA B 1 618  ? 22.664  34.951  54.787  1.00 15.93 ?  616  ALA B C     1 
ATOM   13790 O O     . ALA B 1 618  ? 21.455  35.054  54.555  1.00 15.67 ?  616  ALA B O     1 
ATOM   13791 C CB    . ALA B 1 618  ? 23.471  32.946  56.065  1.00 14.93 ?  616  ALA B CB    1 
ATOM   13792 N N     . VAL B 1 619  ? 23.394  36.005  55.157  1.00 17.20 ?  617  VAL B N     1 
ATOM   13793 C CA    . VAL B 1 619  ? 22.727  37.300  55.268  1.00 15.54 ?  617  VAL B CA    1 
ATOM   13794 C C     . VAL B 1 619  ? 22.263  37.776  53.896  1.00 17.40 ?  617  VAL B C     1 
ATOM   13795 O O     . VAL B 1 619  ? 21.154  38.312  53.751  1.00 18.45 ?  617  VAL B O     1 
ATOM   13796 C CB    . VAL B 1 619  ? 23.624  38.338  55.969  1.00 17.10 ?  617  VAL B CB    1 
ATOM   13797 C CG1   . VAL B 1 619  ? 22.895  39.675  56.065  1.00 19.36 ?  617  VAL B CG1   1 
ATOM   13798 C CG2   . VAL B 1 619  ? 23.987  37.865  57.372  1.00 17.38 ?  617  VAL B CG2   1 
ATOM   13799 N N     . ARG B 1 620  ? 23.082  37.561  52.866  1.00 17.26 ?  618  ARG B N     1 
ATOM   13800 C CA    . ARG B 1 620  ? 22.659  37.907  51.513  1.00 18.58 ?  618  ARG B CA    1 
ATOM   13801 C C     . ARG B 1 620  ? 21.427  37.112  51.102  1.00 18.14 ?  618  ARG B C     1 
ATOM   13802 O O     . ARG B 1 620  ? 20.495  37.667  50.509  1.00 18.29 ?  618  ARG B O     1 
ATOM   13803 C CB    . ARG B 1 620  ? 23.809  37.694  50.530  1.00 23.25 ?  618  ARG B CB    1 
ATOM   13804 C CG    . ARG B 1 620  ? 25.016  38.589  50.813  1.00 28.66 ?  618  ARG B CG    1 
ATOM   13805 C CD    . ARG B 1 620  ? 25.970  38.639  49.625  1.00 35.16 ?  618  ARG B CD    1 
ATOM   13806 N NE    . ARG B 1 620  ? 26.251  37.309  49.098  1.00 38.08 ?  618  ARG B NE    1 
ATOM   13807 C CZ    . ARG B 1 620  ? 27.225  36.520  49.532  1.00 33.56 ?  618  ARG B CZ    1 
ATOM   13808 N NH1   . ARG B 1 620  ? 28.052  36.905  50.491  1.00 32.41 ?  618  ARG B NH1   1 
ATOM   13809 N NH2   . ARG B 1 620  ? 27.373  35.314  48.988  1.00 37.11 ?  618  ARG B NH2   1 
ATOM   13810 N N     . LEU B 1 621  ? 21.379  35.818  51.442  1.00 17.09 ?  619  LEU B N     1 
ATOM   13811 C CA    . LEU B 1 621  ? 20.197  35.027  51.112  1.00 19.00 ?  619  LEU B CA    1 
ATOM   13812 C C     . LEU B 1 621  ? 18.969  35.544  51.851  1.00 19.24 ?  619  LEU B C     1 
ATOM   13813 O O     . LEU B 1 621  ? 17.866  35.578  51.290  1.00 18.77 ?  619  LEU B O     1 
ATOM   13814 C CB    . LEU B 1 621  ? 20.434  33.552  51.439  1.00 19.88 ?  619  LEU B CB    1 
ATOM   13815 C CG    . LEU B 1 621  ? 21.464  32.806  50.583  1.00 19.09 ?  619  LEU B CG    1 
ATOM   13816 C CD1   . LEU B 1 621  ? 21.742  31.429  51.147  1.00 19.52 ?  619  LEU B CD1   1 
ATOM   13817 C CD2   . LEU B 1 621  ? 20.962  32.690  49.145  1.00 23.40 ?  619  LEU B CD2   1 
ATOM   13818 N N     . ALA B 1 622  ? 19.142  35.940  53.116  1.00 16.16 ?  620  ALA B N     1 
ATOM   13819 C CA    . ALA B 1 622  ? 18.029  36.508  53.873  1.00 13.79 ?  620  ALA B CA    1 
ATOM   13820 C C     . ALA B 1 622  ? 17.547  37.810  53.247  1.00 16.72 ?  620  ALA B C     1 
ATOM   13821 O O     . ALA B 1 622  ? 16.338  38.045  53.142  1.00 16.11 ?  620  ALA B O     1 
ATOM   13822 C CB    . ALA B 1 622  ? 18.440  36.728  55.331  1.00 15.15 ?  620  ALA B CB    1 
ATOM   13823 N N     . ALA B 1 623  ? 18.473  38.662  52.803  1.00 16.28 ?  621  ALA B N     1 
ATOM   13824 C CA    . ALA B 1 623  ? 18.065  39.905  52.155  1.00 16.70 ?  621  ALA B CA    1 
ATOM   13825 C C     . ALA B 1 623  ? 17.282  39.629  50.877  1.00 16.42 ?  621  ALA B C     1 
ATOM   13826 O O     . ALA B 1 623  ? 16.252  40.267  50.619  1.00 17.79 ?  621  ALA B O     1 
ATOM   13827 C CB    . ALA B 1 623  ? 19.291  40.765  51.850  1.00 17.66 ?  621  ALA B CB    1 
ATOM   13828 N N     . ASP B 1 624  ? 17.741  38.668  50.069  1.00 18.07 ?  622  ASP B N     1 
ATOM   13829 C CA    . ASP B 1 624  ? 17.040  38.373  48.819  1.00 20.00 ?  622  ASP B CA    1 
ATOM   13830 C C     . ASP B 1 624  ? 15.603  37.946  49.081  1.00 21.66 ?  622  ASP B C     1 
ATOM   13831 O O     . ASP B 1 624  ? 14.698  38.282  48.309  1.00 26.15 ?  622  ASP B O     1 
ATOM   13832 C CB    . ASP B 1 624  ? 17.771  37.281  48.036  1.00 23.02 ?  622  ASP B CB    1 
ATOM   13833 C CG    . ASP B 1 624  ? 19.128  37.720  47.534  1.00 30.12 ?  622  ASP B CG    1 
ATOM   13834 O OD1   . ASP B 1 624  ? 19.370  38.943  47.424  1.00 34.08 ?  622  ASP B OD1   1 
ATOM   13835 O OD2   . ASP B 1 624  ? 19.957  36.829  47.241  1.00 32.83 ?  622  ASP B OD2   1 
ATOM   13836 N N     . ALA B 1 625  ? 15.374  37.209  50.160  1.00 20.31 ?  623  ALA B N     1 
ATOM   13837 C CA    . ALA B 1 625  ? 14.053  36.687  50.480  1.00 27.72 ?  623  ALA B CA    1 
ATOM   13838 C C     . ALA B 1 625  ? 13.233  37.609  51.372  1.00 22.67 ?  623  ALA B C     1 
ATOM   13839 O O     . ALA B 1 625  ? 12.061  37.313  51.634  1.00 21.23 ?  623  ALA B O     1 
ATOM   13840 C CB    . ALA B 1 625  ? 14.181  35.327  51.166  1.00 30.28 ?  623  ALA B CB    1 
ATOM   13841 N N     . ALA B 1 626  ? 13.804  38.709  51.847  1.00 18.04 ?  624  ALA B N     1 
ATOM   13842 C CA    . ALA B 1 626  ? 13.066  39.563  52.775  1.00 17.87 ?  624  ALA B CA    1 
ATOM   13843 C C     . ALA B 1 626  ? 11.726  40.043  52.220  1.00 17.82 ?  624  ALA B C     1 
ATOM   13844 O O     . ALA B 1 626  ? 10.733  39.997  52.969  1.00 17.60 ?  624  ALA B O     1 
ATOM   13845 C CB    . ALA B 1 626  ? 13.954  40.738  53.206  1.00 15.66 ?  624  ALA B CB    1 
ATOM   13846 N N     . PRO B 1 627  ? 11.602  40.474  50.956  1.00 17.47 ?  625  PRO B N     1 
ATOM   13847 C CA    . PRO B 1 627  ? 10.279  40.929  50.489  1.00 18.78 ?  625  PRO B CA    1 
ATOM   13848 C C     . PRO B 1 627  ? 9.217   39.837  50.484  1.00 18.84 ?  625  PRO B C     1 
ATOM   13849 O O     . PRO B 1 627  ? 8.043   40.116  50.782  1.00 18.27 ?  625  PRO B O     1 
ATOM   13850 C CB    . PRO B 1 627  ? 10.569  41.452  49.071  1.00 22.04 ?  625  PRO B CB    1 
ATOM   13851 C CG    . PRO B 1 627  ? 12.012  41.818  49.089  1.00 23.76 ?  625  PRO B CG    1 
ATOM   13852 C CD    . PRO B 1 627  ? 12.668  40.811  49.991  1.00 20.51 ?  625  PRO B CD    1 
ATOM   13853 N N     . ASP B 1 628  ? 9.583   38.596  50.150  1.00 18.82 ?  626  ASP B N     1 
ATOM   13854 C CA    . ASP B 1 628  ? 8.576   37.539  50.097  1.00 20.42 ?  626  ASP B CA    1 
ATOM   13855 C C     . ASP B 1 628  ? 8.054   37.210  51.488  1.00 18.24 ?  626  ASP B C     1 
ATOM   13856 O O     . ASP B 1 628  ? 6.866   36.917  51.658  1.00 19.89 ?  626  ASP B O     1 
ATOM   13857 C CB    . ASP B 1 628  ? 9.135   36.279  49.439  1.00 20.62 ?  626  ASP B CB    1 
ATOM   13858 C CG    . ASP B 1 628  ? 9.534   36.495  47.994  1.00 28.14 ?  626  ASP B CG    1 
ATOM   13859 O OD1   . ASP B 1 628  ? 8.942   37.368  47.323  1.00 27.25 ?  626  ASP B OD1   1 
ATOM   13860 O OD2   . ASP B 1 628  ? 10.454  35.790  47.537  1.00 33.13 ?  626  ASP B OD2   1 
ATOM   13861 N N     . TRP B 1 629  ? 8.928   37.244  52.495  1.00 16.91 ?  627  TRP B N     1 
ATOM   13862 C CA    . TRP B 1 629  ? 8.470   36.961  53.848  1.00 15.45 ?  627  TRP B CA    1 
ATOM   13863 C C     . TRP B 1 629  ? 7.645   38.121  54.396  1.00 15.32 ?  627  TRP B C     1 
ATOM   13864 O O     . TRP B 1 629  ? 6.598   37.905  55.019  1.00 15.35 ?  627  TRP B O     1 
ATOM   13865 C CB    . TRP B 1 629  ? 9.669   36.636  54.744  1.00 13.97 ?  627  TRP B CB    1 
ATOM   13866 C CG    . TRP B 1 629  ? 9.240   36.338  56.147  1.00 12.93 ?  627  TRP B CG    1 
ATOM   13867 C CD1   . TRP B 1 629  ? 9.602   37.026  57.272  1.00 13.34 ?  627  TRP B CD1   1 
ATOM   13868 C CD2   . TRP B 1 629  ? 8.351   35.297  56.574  1.00 13.19 ?  627  TRP B CD2   1 
ATOM   13869 N NE1   . TRP B 1 629  ? 8.998   36.473  58.372  1.00 13.27 ?  627  TRP B NE1   1 
ATOM   13870 C CE2   . TRP B 1 629  ? 8.223   35.412  57.977  1.00 11.88 ?  627  TRP B CE2   1 
ATOM   13871 C CE3   . TRP B 1 629  ? 7.637   34.284  55.912  1.00 15.84 ?  627  TRP B CE3   1 
ATOM   13872 C CZ2   . TRP B 1 629  ? 7.401   34.555  58.735  1.00 13.68 ?  627  TRP B CZ2   1 
ATOM   13873 C CZ3   . TRP B 1 629  ? 6.824   33.429  56.672  1.00 14.93 ?  627  TRP B CZ3   1 
ATOM   13874 C CH2   . TRP B 1 629  ? 6.718   33.571  58.067  1.00 16.03 ?  627  TRP B CH2   1 
ATOM   13875 N N     . ALA B 1 630  ? 8.075   39.359  54.137  1.00 14.22 ?  628  ALA B N     1 
ATOM   13876 C CA    . ALA B 1 630  ? 7.271   40.507  54.550  1.00 14.87 ?  628  ALA B CA    1 
ATOM   13877 C C     . ALA B 1 630  ? 5.872   40.458  53.939  1.00 17.80 ?  628  ALA B C     1 
ATOM   13878 O O     . ALA B 1 630  ? 4.903   40.910  54.567  1.00 17.21 ?  628  ALA B O     1 
ATOM   13879 C CB    . ALA B 1 630  ? 7.987   41.803  54.167  1.00 15.89 ?  628  ALA B CB    1 
ATOM   13880 N N     . ALA B 1 631  ? 5.737   39.881  52.741  1.00 17.41 ?  629  ALA B N     1 
ATOM   13881 C CA    . ALA B 1 631  ? 4.436   39.828  52.083  1.00 15.27 ?  629  ALA B CA    1 
ATOM   13882 C C     . ALA B 1 631  ? 3.520   38.728  52.612  1.00 17.98 ?  629  ALA B C     1 
ATOM   13883 O O     . ALA B 1 631  ? 2.333   38.708  52.258  1.00 20.18 ?  629  ALA B O     1 
ATOM   13884 C CB    . ALA B 1 631  ? 4.615   39.662  50.564  1.00 17.81 ?  629  ALA B CB    1 
ATOM   13885 N N     . VAL B 1 632  ? 4.011   37.824  53.453  1.00 16.41 ?  630  VAL B N     1 
ATOM   13886 C CA    . VAL B 1 632  ? 3.116   36.886  54.128  1.00 15.43 ?  630  VAL B CA    1 
ATOM   13887 C C     . VAL B 1 632  ? 2.311   37.692  55.142  1.00 16.38 ?  630  VAL B C     1 
ATOM   13888 O O     . VAL B 1 632  ? 2.912   38.376  55.991  1.00 17.16 ?  630  VAL B O     1 
ATOM   13889 C CB    . VAL B 1 632  ? 3.898   35.749  54.804  1.00 16.07 ?  630  VAL B CB    1 
ATOM   13890 C CG1   . VAL B 1 632  ? 2.951   34.809  55.540  1.00 16.21 ?  630  VAL B CG1   1 
ATOM   13891 C CG2   . VAL B 1 632  ? 4.729   35.004  53.782  1.00 18.25 ?  630  VAL B CG2   1 
ATOM   13892 N N     . PRO B 1 633  ? 0.980   37.648  55.108  1.00 14.69 ?  631  PRO B N     1 
ATOM   13893 C CA    . PRO B 1 633  ? 0.200   38.510  55.990  1.00 15.11 ?  631  PRO B CA    1 
ATOM   13894 C C     . PRO B 1 633  ? 0.517   38.224  57.451  1.00 15.15 ?  631  PRO B C     1 
ATOM   13895 O O     . PRO B 1 633  ? 0.777   37.070  57.830  1.00 14.28 ?  631  PRO B O     1 
ATOM   13896 C CB    . PRO B 1 633  ? -1.250  38.145  55.653  1.00 17.70 ?  631  PRO B CB    1 
ATOM   13897 C CG    . PRO B 1 633  ? -1.184  37.695  54.240  1.00 19.85 ?  631  PRO B CG    1 
ATOM   13898 C CD    . PRO B 1 633  ? 0.130   36.977  54.106  1.00 15.84 ?  631  PRO B CD    1 
ATOM   13899 N N     . PRO B 1 634  ? 0.488   39.251  58.297  1.00 15.54 ?  632  PRO B N     1 
ATOM   13900 C CA    . PRO B 1 634  ? 0.787   39.038  59.731  1.00 15.26 ?  632  PRO B CA    1 
ATOM   13901 C C     . PRO B 1 634  ? 0.010   37.905  60.368  1.00 13.89 ?  632  PRO B C     1 
ATOM   13902 O O     . PRO B 1 634  ? 0.595   37.138  61.137  1.00 12.59 ?  632  PRO B O     1 
ATOM   13903 C CB    . PRO B 1 634  ? 0.427   40.388  60.369  1.00 14.65 ?  632  PRO B CB    1 
ATOM   13904 C CG    . PRO B 1 634  ? 0.651   41.380  59.258  1.00 20.66 ?  632  PRO B CG    1 
ATOM   13905 C CD    . PRO B 1 634  ? 0.282   40.673  57.967  1.00 18.39 ?  632  PRO B CD    1 
ATOM   13906 N N     . SER B 1 635  ? -1.284  37.767  60.078  1.00 15.46 ?  633  SER B N     1 
ATOM   13907 C CA    . SER B 1 635  ? -2.045  36.676  60.683  1.00 17.92 ?  633  SER B CA    1 
ATOM   13908 C C     . SER B 1 635  ? -1.523  35.313  60.239  1.00 16.11 ?  633  SER B C     1 
ATOM   13909 O O     . SER B 1 635  ? -1.600  34.346  61.004  1.00 14.55 ?  633  SER B O     1 
ATOM   13910 C CB    . SER B 1 635  ? -3.529  36.809  60.331  1.00 22.33 ?  633  SER B CB    1 
ATOM   13911 O OG    . SER B 1 635  ? -3.704  36.808  58.931  1.00 27.27 ?  633  SER B OG    1 
ATOM   13912 N N     . GLU B 1 636  ? -0.998  35.207  59.013  1.00 14.45 ?  634  GLU B N     1 
ATOM   13913 C CA    . GLU B 1 636  ? -0.457  33.926  58.570  1.00 13.56 ?  634  GLU B CA    1 
ATOM   13914 C C     . GLU B 1 636  ? 0.926   33.675  59.170  1.00 14.77 ?  634  GLU B C     1 
ATOM   13915 O O     . GLU B 1 636  ? 1.259   32.534  59.517  1.00 12.33 ?  634  GLU B O     1 
ATOM   13916 C CB    . GLU B 1 636  ? -0.420  33.866  57.039  1.00 14.93 ?  634  GLU B CB    1 
ATOM   13917 C CG    . GLU B 1 636  ? 0.231   32.596  56.500  1.00 19.86 ?  634  GLU B CG    1 
ATOM   13918 C CD    . GLU B 1 636  ? -0.445  31.315  56.980  1.00 25.32 ?  634  GLU B CD    1 
ATOM   13919 O OE1   . GLU B 1 636  ? -1.669  31.323  57.260  1.00 25.24 ?  634  GLU B OE1   1 
ATOM   13920 O OE2   . GLU B 1 636  ? 0.262   30.289  57.082  1.00 25.70 ?  634  GLU B OE2   1 
ATOM   13921 N N     . ARG B 1 637  ? 1.744   34.721  59.310  1.00 12.02 ?  635  ARG B N     1 
ATOM   13922 C CA    . ARG B 1 637  ? 2.990   34.544  60.048  1.00 12.09 ?  635  ARG B CA    1 
ATOM   13923 C C     . ARG B 1 637  ? 2.693   34.103  61.472  1.00 12.27 ?  635  ARG B C     1 
ATOM   13924 O O     . ARG B 1 637  ? 3.362   33.209  62.014  1.00 11.58 ?  635  ARG B O     1 
ATOM   13925 C CB    . ARG B 1 637  ? 3.815   35.836  60.029  1.00 11.70 ?  635  ARG B CB    1 
ATOM   13926 C CG    . ARG B 1 637  ? 4.106   36.318  58.620  1.00 12.57 ?  635  ARG B CG    1 
ATOM   13927 C CD    . ARG B 1 637  ? 5.128   37.440  58.606  1.00 12.36 ?  635  ARG B CD    1 
ATOM   13928 N NE    . ARG B 1 637  ? 4.723   38.594  59.394  1.00 13.40 ?  635  ARG B NE    1 
ATOM   13929 C CZ    . ARG B 1 637  ? 4.564   39.823  58.916  1.00 14.89 ?  635  ARG B CZ    1 
ATOM   13930 N NH1   . ARG B 1 637  ? 4.547   40.068  57.611  1.00 18.57 ?  635  ARG B NH1   1 
ATOM   13931 N NH2   . ARG B 1 637  ? 4.423   40.835  59.768  1.00 15.57 ?  635  ARG B NH2   1 
ATOM   13932 N N     . ALA B 1 638  ? 1.666   34.701  62.083  1.00 11.32 ?  636  ALA B N     1 
ATOM   13933 C CA    . ALA B 1 638  ? 1.277   34.307  63.430  1.00 10.96 ?  636  ALA B CA    1 
ATOM   13934 C C     . ALA B 1 638  ? 0.808   32.860  63.466  1.00 10.47 ?  636  ALA B C     1 
ATOM   13935 O O     . ALA B 1 638  ? 1.055   32.143  64.444  1.00 11.41 ?  636  ALA B O     1 
ATOM   13936 C CB    . ALA B 1 638  ? 0.181   35.236  63.954  1.00 12.38 ?  636  ALA B CB    1 
ATOM   13937 N N     . ALA B 1 639  ? 0.107   32.420  62.422  1.00 11.87 ?  637  ALA B N     1 
ATOM   13938 C CA    . ALA B 1 639  ? -0.345  31.034  62.372  1.00 11.21 ?  637  ALA B CA    1 
ATOM   13939 C C     . ALA B 1 639  ? 0.828   30.061  62.320  1.00 11.00 ?  637  ALA B C     1 
ATOM   13940 O O     . ALA B 1 639  ? 0.746   28.965  62.886  1.00 12.32 ?  637  ALA B O     1 
ATOM   13941 C CB    . ALA B 1 639  ? -1.271  30.832  61.172  1.00 11.42 ?  637  ALA B CB    1 
ATOM   13942 N N     . CYS B 1 640  ? 1.936   30.454  61.681  1.00 11.51 ?  638  CYS B N     1 
ATOM   13943 C CA    . CYS B 1 640  ? 3.143   29.631  61.726  1.00 11.11 ?  638  CYS B CA    1 
ATOM   13944 C C     . CYS B 1 640  ? 3.652   29.473  63.150  1.00 10.61 ?  638  CYS B C     1 
ATOM   13945 O O     . CYS B 1 640  ? 4.023   28.369  63.565  1.00 11.06 ?  638  CYS B O     1 
ATOM   13946 C CB    . CYS B 1 640  ? 4.251   30.230  60.866  1.00 11.62 ?  638  CYS B CB    1 
ATOM   13947 S SG    . CYS B 1 640  ? 3.954   30.179  59.103  1.00 13.43 ?  638  CYS B SG    1 
ATOM   13948 N N     . LEU B 1 641  ? 3.715   30.578  63.903  1.00 9.75  ?  639  LEU B N     1 
ATOM   13949 C CA    . LEU B 1 641  ? 4.145   30.491  65.298  1.00 8.90  ?  639  LEU B CA    1 
ATOM   13950 C C     . LEU B 1 641  ? 3.231   29.572  66.100  1.00 10.45 ?  639  LEU B C     1 
ATOM   13951 O O     . LEU B 1 641  ? 3.709   28.735  66.879  1.00 11.00 ?  639  LEU B O     1 
ATOM   13952 C CB    . LEU B 1 641  ? 4.163   31.882  65.928  1.00 12.18 ?  639  LEU B CB    1 
ATOM   13953 C CG    . LEU B 1 641  ? 5.434   32.713  65.777  1.00 11.73 ?  639  LEU B CG    1 
ATOM   13954 C CD1   . LEU B 1 641  ? 5.829   32.949  64.310  1.00 13.86 ?  639  LEU B CD1   1 
ATOM   13955 C CD2   . LEU B 1 641  ? 5.304   34.023  66.526  1.00 11.27 ?  639  LEU B CD2   1 
ATOM   13956 N N     . ASP B 1 642  ? 1.908   29.715  65.922  1.00 10.11 ?  640  ASP B N     1 
ATOM   13957 C CA    . ASP B 1 642  ? 0.983   28.852  66.652  1.00 10.62 ?  640  ASP B CA    1 
ATOM   13958 C C     . ASP B 1 642  ? 1.164   27.385  66.273  1.00 9.76  ?  640  ASP B C     1 
ATOM   13959 O O     . ASP B 1 642  ? 1.093   26.507  67.140  1.00 11.82 ?  640  ASP B O     1 
ATOM   13960 C CB    . ASP B 1 642  ? -0.466  29.280  66.412  1.00 11.98 ?  640  ASP B CB    1 
ATOM   13961 C CG    . ASP B 1 642  ? -0.884  30.471  67.250  1.00 11.81 ?  640  ASP B CG    1 
ATOM   13962 O OD1   . ASP B 1 642  ? -0.255  30.748  68.291  1.00 11.60 ?  640  ASP B OD1   1 
ATOM   13963 O OD2   . ASP B 1 642  ? -1.877  31.123  66.862  1.00 15.67 ?  640  ASP B OD2   1 
ATOM   13964 N N     . ARG B 1 643  ? 1.410   27.093  64.989  1.00 10.74 ?  641  ARG B N     1 
ATOM   13965 C CA    . ARG B 1 643  ? 1.665   25.705  64.609  1.00 10.71 ?  641  ARG B CA    1 
ATOM   13966 C C     . ARG B 1 643  ? 2.939   25.187  65.254  1.00 11.28 ?  641  ARG B C     1 
ATOM   13967 O O     . ARG B 1 643  ? 2.989   24.040  65.720  1.00 10.93 ?  641  ARG B O     1 
ATOM   13968 C CB    . ARG B 1 643  ? 1.744   25.563  63.089  1.00 10.80 ?  641  ARG B CB    1 
ATOM   13969 C CG    . ARG B 1 643  ? 0.373   25.519  62.415  1.00 13.30 ?  641  ARG B CG    1 
ATOM   13970 C CD    . ARG B 1 643  ? 0.492   25.200  60.926  1.00 15.93 ?  641  ARG B CD    1 
ATOM   13971 N NE    . ARG B 1 643  ? 1.132   26.283  60.187  1.00 15.11 ?  641  ARG B NE    1 
ATOM   13972 C CZ    . ARG B 1 643  ? 0.473   27.278  59.614  1.00 15.92 ?  641  ARG B CZ    1 
ATOM   13973 N NH1   . ARG B 1 643  ? -0.846  27.359  59.682  1.00 16.98 ?  641  ARG B NH1   1 
ATOM   13974 N NH2   . ARG B 1 643  ? 1.153   28.217  58.960  1.00 18.52 ?  641  ARG B NH2   1 
ATOM   13975 N N     . ALA B 1 644  ? 3.972   26.034  65.332  1.00 10.34 ?  642  ALA B N     1 
ATOM   13976 C CA    . ALA B 1 644  ? 5.209   25.603  65.966  1.00 11.77 ?  642  ALA B CA    1 
ATOM   13977 C C     . ALA B 1 644  ? 4.994   25.315  67.447  1.00 12.08 ?  642  ALA B C     1 
ATOM   13978 O O     . ALA B 1 644  ? 5.555   24.352  67.987  1.00 11.44 ?  642  ALA B O     1 
ATOM   13979 C CB    . ALA B 1 644  ? 6.286   26.663  65.767  1.00 10.43 ?  642  ALA B CB    1 
ATOM   13980 N N     . ALA B 1 645  ? 4.147   26.120  68.110  1.00 10.72 ?  643  ALA B N     1 
ATOM   13981 C CA    . ALA B 1 645  ? 3.859   25.879  69.520  1.00 10.84 ?  643  ALA B CA    1 
ATOM   13982 C C     . ALA B 1 645  ? 3.168   24.539  69.726  1.00 11.35 ?  643  ALA B C     1 
ATOM   13983 O O     . ALA B 1 645  ? 3.477   23.826  70.691  1.00 11.40 ?  643  ALA B O     1 
ATOM   13984 C CB    . ALA B 1 645  ? 3.007   27.016  70.089  1.00 11.31 ?  643  ALA B CB    1 
ATOM   13985 N N     . GLU B 1 646  ? 2.243   24.175  68.821  1.00 10.97 ?  644  GLU B N     1 
ATOM   13986 C CA    . GLU B 1 646  ? 1.588   22.873  68.922  1.00 12.35 ?  644  GLU B CA    1 
ATOM   13987 C C     . GLU B 1 646  ? 2.599   21.748  68.789  1.00 13.75 ?  644  GLU B C     1 
ATOM   13988 O O     . GLU B 1 646  ? 2.502   20.730  69.482  1.00 13.21 ?  644  GLU B O     1 
ATOM   13989 C CB    . GLU B 1 646  ? 0.518   22.710  67.843  1.00 13.36 ?  644  GLU B CB    1 
ATOM   13990 C CG    . GLU B 1 646  ? -0.664  23.624  67.949  1.00 17.16 ?  644  GLU B CG    1 
ATOM   13991 C CD    . GLU B 1 646  ? -1.424  23.436  69.237  1.00 23.54 ?  644  GLU B CD    1 
ATOM   13992 O OE1   . GLU B 1 646  ? -1.698  22.275  69.607  1.00 32.15 ?  644  GLU B OE1   1 
ATOM   13993 O OE2   . GLU B 1 646  ? -1.728  24.452  69.889  1.00 24.85 ?  644  GLU B OE2   1 
ATOM   13994 N N     . LEU B 1 647  ? 3.562   21.901  67.874  1.00 12.40 ?  645  LEU B N     1 
ATOM   13995 C CA    . LEU B 1 647  ? 4.558   20.849  67.691  1.00 12.73 ?  645  LEU B CA    1 
ATOM   13996 C C     . LEU B 1 647  ? 5.457   20.723  68.907  1.00 12.51 ?  645  LEU B C     1 
ATOM   13997 O O     . LEU B 1 647  ? 5.784   19.604  69.329  1.00 14.15 ?  645  LEU B O     1 
ATOM   13998 C CB    . LEU B 1 647  ? 5.398   21.117  66.443  1.00 12.68 ?  645  LEU B CB    1 
ATOM   13999 C CG    . LEU B 1 647  ? 4.628   21.047  65.135  1.00 12.36 ?  645  LEU B CG    1 
ATOM   14000 C CD1   . LEU B 1 647  ? 5.568   21.360  63.968  1.00 13.75 ?  645  LEU B CD1   1 
ATOM   14001 C CD2   . LEU B 1 647  ? 3.970   19.685  64.952  1.00 17.05 ?  645  LEU B CD2   1 
ATOM   14002 N N     . MET B 1 648  ? 5.876   21.854  69.477  1.00 11.51 ?  646  MET B N     1 
ATOM   14003 C CA    . MET B 1 648  ? 6.714   21.790  70.673  1.00 11.14 ?  646  MET B CA    1 
ATOM   14004 C C     . MET B 1 648  ? 5.956   21.187  71.848  1.00 12.79 ?  646  MET B C     1 
ATOM   14005 O O     . MET B 1 648  ? 6.536   20.462  72.662  1.00 14.41 ?  646  MET B O     1 
ATOM   14006 C CB    . MET B 1 648  ? 7.255   23.168  71.050  1.00 12.93 ?  646  MET B CB    1 
ATOM   14007 C CG    . MET B 1 648  ? 8.308   23.688  70.083  1.00 13.82 ?  646  MET B CG    1 
ATOM   14008 S SD    . MET B 1 648  ? 9.151   25.102  70.826  1.00 13.59 ?  646  MET B SD    1 
ATOM   14009 C CE    . MET B 1 648  ? 10.189  25.577  69.449  1.00 13.47 ?  646  MET B CE    1 
ATOM   14010 N N     . GLN B 1 649  ? 4.657   21.469  71.953  1.00 12.70 ?  647  GLN B N     1 
ATOM   14011 C CA    . GLN B 1 649  ? 3.873   20.860  73.021  1.00 14.14 ?  647  GLN B CA    1 
ATOM   14012 C C     . GLN B 1 649  ? 3.800   19.349  72.849  1.00 13.52 ?  647  GLN B C     1 
ATOM   14013 O O     . GLN B 1 649  ? 3.969   18.596  73.818  1.00 15.65 ?  647  GLN B O     1 
ATOM   14014 C CB    . GLN B 1 649  ? 2.469   21.463  73.043  1.00 13.34 ?  647  GLN B CB    1 
ATOM   14015 C CG    . GLN B 1 649  ? 1.606   20.992  74.221  1.00 14.04 ?  647  GLN B CG    1 
ATOM   14016 C CD    . GLN B 1 649  ? 2.025   21.647  75.522  1.00 11.84 ?  647  GLN B CD    1 
ATOM   14017 O OE1   . GLN B 1 649  ? 1.695   22.805  75.772  1.00 13.55 ?  647  GLN B OE1   1 
ATOM   14018 N NE2   . GLN B 1 649  ? 2.795   20.921  76.343  1.00 13.12 ?  647  GLN B NE2   1 
ATOM   14019 N N     . ALA B 1 650  ? 3.560   18.888  71.622  1.00 13.07 ?  648  ALA B N     1 
ATOM   14020 C CA    . ALA B 1 650  ? 3.398   17.461  71.370  1.00 12.32 ?  648  ALA B CA    1 
ATOM   14021 C C     . ALA B 1 650  ? 4.716   16.720  71.502  1.00 16.08 ?  648  ALA B C     1 
ATOM   14022 O O     . ALA B 1 650  ? 4.743   15.572  71.958  1.00 20.34 ?  648  ALA B O     1 
ATOM   14023 C CB    . ALA B 1 650  ? 2.813   17.241  69.979  1.00 15.79 ?  648  ALA B CB    1 
ATOM   14024 N N     . ARG B 1 651  ? 5.821   17.379  71.177  1.00 14.87 ?  649  ARG B N     1 
ATOM   14025 C CA    . ARG B 1 651  ? 7.134   16.760  71.241  1.00 13.36 ?  649  ARG B CA    1 
ATOM   14026 C C     . ARG B 1 651  ? 7.889   17.108  72.511  1.00 15.90 ?  649  ARG B C     1 
ATOM   14027 O O     . ARG B 1 651  ? 9.091   16.836  72.597  1.00 16.82 ?  649  ARG B O     1 
ATOM   14028 C CB    . ARG B 1 651  ? 7.926   17.163  69.999  1.00 15.12 ?  649  ARG B CB    1 
ATOM   14029 C CG    . ARG B 1 651  ? 7.188   16.700  68.776  1.00 15.23 ?  649  ARG B CG    1 
ATOM   14030 C CD    . ARG B 1 651  ? 7.816   17.133  67.486  1.00 17.07 ?  649  ARG B CD    1 
ATOM   14031 N NE    . ARG B 1 651  ? 6.907   16.795  66.403  1.00 17.52 ?  649  ARG B NE    1 
ATOM   14032 C CZ    . ARG B 1 651  ? 7.065   17.200  65.152  1.00 17.79 ?  649  ARG B CZ    1 
ATOM   14033 N NH1   . ARG B 1 651  ? 8.114   17.925  64.792  1.00 18.33 ?  649  ARG B NH1   1 
ATOM   14034 N NH2   . ARG B 1 651  ? 6.139   16.890  64.250  1.00 17.88 ?  649  ARG B NH2   1 
ATOM   14035 N N     . MET B 1 652  ? 7.209   17.681  73.513  1.00 13.49 ?  650  MET B N     1 
ATOM   14036 C CA    . MET B 1 652  ? 7.894   18.102  74.736  1.00 14.78 ?  650  MET B CA    1 
ATOM   14037 C C     . MET B 1 652  ? 8.766   17.014  75.352  1.00 15.58 ?  650  MET B C     1 
ATOM   14038 O O     . MET B 1 652  ? 9.919   17.312  75.694  1.00 16.59 ?  650  MET B O     1 
ATOM   14039 C CB    . MET B 1 652  ? 6.873   18.636  75.754  1.00 14.42 ?  650  MET B CB    1 
ATOM   14040 C CG    . MET B 1 652  ? 7.503   18.969  77.099  1.00 14.16 ?  650  MET B CG    1 
ATOM   14041 S SD    . MET B 1 652  ? 6.338   19.652  78.297  1.00 17.01 ?  650  MET B SD    1 
ATOM   14042 C CE    . MET B 1 652  ? 6.099   21.303  77.680  1.00 15.79 ?  650  MET B CE    1 
ATOM   14043 N N     . PRO B 1 653  ? 8.318   15.761  75.509  1.00 15.40 ?  651  PRO B N     1 
ATOM   14044 C CA    . PRO B 1 653  ? 9.199   14.767  76.150  1.00 17.25 ?  651  PRO B CA    1 
ATOM   14045 C C     . PRO B 1 653  ? 10.526  14.574  75.433  1.00 16.73 ?  651  PRO B C     1 
ATOM   14046 O O     . PRO B 1 653  ? 11.569  14.458  76.088  1.00 19.01 ?  651  PRO B O     1 
ATOM   14047 C CB    . PRO B 1 653  ? 8.348   13.487  76.130  1.00 16.21 ?  651  PRO B CB    1 
ATOM   14048 C CG    . PRO B 1 653  ? 6.930   13.989  76.145  1.00 18.11 ?  651  PRO B CG    1 
ATOM   14049 C CD    . PRO B 1 653  ? 6.986   15.198  75.229  1.00 17.38 ?  651  PRO B CD    1 
ATOM   14050 N N     . THR B 1 654  ? 10.519  14.543  74.100  1.00 15.94 ?  652  THR B N     1 
ATOM   14051 C CA    . THR B 1 654  ? 11.769  14.404  73.356  1.00 15.93 ?  652  THR B CA    1 
ATOM   14052 C C     . THR B 1 654  ? 12.649  15.643  73.507  1.00 20.36 ?  652  THR B C     1 
ATOM   14053 O O     . THR B 1 654  ? 13.872  15.529  73.686  1.00 18.70 ?  652  THR B O     1 
ATOM   14054 C CB    . THR B 1 654  ? 11.450  14.122  71.887  1.00 17.83 ?  652  THR B CB    1 
ATOM   14055 O OG1   . THR B 1 654  ? 10.661  12.930  71.802  1.00 19.64 ?  652  THR B OG1   1 
ATOM   14056 C CG2   . THR B 1 654  ? 12.718  13.937  71.075  1.00 19.25 ?  652  THR B CG2   1 
ATOM   14057 N N     . LEU B 1 655  ? 12.045  16.834  73.454  1.00 15.68 ?  653  LEU B N     1 
ATOM   14058 C CA    . LEU B 1 655  ? 12.804  18.064  73.664  1.00 16.37 ?  653  LEU B CA    1 
ATOM   14059 C C     . LEU B 1 655  ? 13.436  18.090  75.048  1.00 16.58 ?  653  LEU B C     1 
ATOM   14060 O O     . LEU B 1 655  ? 14.569  18.562  75.209  1.00 17.67 ?  653  LEU B O     1 
ATOM   14061 C CB    . LEU B 1 655  ? 11.902  19.284  73.477  1.00 16.47 ?  653  LEU B CB    1 
ATOM   14062 C CG    . LEU B 1 655  ? 11.307  19.490  72.084  1.00 16.88 ?  653  LEU B CG    1 
ATOM   14063 C CD1   . LEU B 1 655  ? 10.305  20.624  72.083  1.00 17.10 ?  653  LEU B CD1   1 
ATOM   14064 C CD2   . LEU B 1 655  ? 12.419  19.754  71.078  1.00 19.12 ?  653  LEU B CD2   1 
ATOM   14065 N N     . LEU B 1 656  ? 12.725  17.573  76.058  1.00 17.42 ?  654  LEU B N     1 
ATOM   14066 C CA    . LEU B 1 656  ? 13.289  17.485  77.409  1.00 18.15 ?  654  LEU B CA    1 
ATOM   14067 C C     . LEU B 1 656  ? 14.568  16.663  77.428  1.00 18.95 ?  654  LEU B C     1 
ATOM   14068 O O     . LEU B 1 656  ? 15.554  17.044  78.073  1.00 18.86 ?  654  LEU B O     1 
ATOM   14069 C CB    . LEU B 1 656  ? 12.285  16.848  78.375  1.00 19.79 ?  654  LEU B CB    1 
ATOM   14070 C CG    . LEU B 1 656  ? 10.924  17.489  78.562  1.00 19.63 ?  654  LEU B CG    1 
ATOM   14071 C CD1   . LEU B 1 656  ? 10.141  16.724  79.622  1.00 21.12 ?  654  LEU B CD1   1 
ATOM   14072 C CD2   . LEU B 1 656  ? 11.069  18.943  78.926  1.00 20.15 ?  654  LEU B CD2   1 
ATOM   14073 N N     . GLY B 1 657  ? 14.547  15.493  76.787  1.00 19.54 ?  655  GLY B N     1 
ATOM   14074 C CA    . GLY B 1 657  ? 15.725  14.645  76.781  1.00 20.96 ?  655  GLY B CA    1 
ATOM   14075 C C     . GLY B 1 657  ? 16.935  15.364  76.234  1.00 18.86 ?  655  GLY B C     1 
ATOM   14076 O O     . GLY B 1 657  ? 18.041  15.230  76.759  1.00 19.30 ?  655  GLY B O     1 
ATOM   14077 N N     . LEU B 1 658  ? 16.732  16.174  75.196  1.00 17.12 ?  656  LEU B N     1 
ATOM   14078 C CA    . LEU B 1 658  ? 17.854  16.870  74.593  1.00 17.87 ?  656  LEU B CA    1 
ATOM   14079 C C     . LEU B 1 658  ? 18.313  18.041  75.455  1.00 20.09 ?  656  LEU B C     1 
ATOM   14080 O O     . LEU B 1 658  ? 19.521  18.260  75.615  1.00 18.94 ?  656  LEU B O     1 
ATOM   14081 C CB    . LEU B 1 658  ? 17.469  17.314  73.182  1.00 17.08 ?  656  LEU B CB    1 
ATOM   14082 C CG    . LEU B 1 658  ? 18.570  17.992  72.377  1.00 17.94 ?  656  LEU B CG    1 
ATOM   14083 C CD1   . LEU B 1 658  ? 19.780  17.084  72.224  1.00 17.21 ?  656  LEU B CD1   1 
ATOM   14084 C CD2   . LEU B 1 658  ? 17.999  18.386  71.025  1.00 16.80 ?  656  LEU B CD2   1 
ATOM   14085 N N     . ILE B 1 659  ? 17.375  18.776  76.054  1.00 16.96 ?  657  ILE B N     1 
ATOM   14086 C CA    . ILE B 1 659  ? 17.754  19.880  76.930  1.00 13.30 ?  657  ILE B CA    1 
ATOM   14087 C C     . ILE B 1 659  ? 18.489  19.357  78.154  1.00 16.43 ?  657  ILE B C     1 
ATOM   14088 O O     . ILE B 1 659  ? 19.489  19.940  78.595  1.00 18.36 ?  657  ILE B O     1 
ATOM   14089 C CB    . ILE B 1 659  ? 16.518  20.711  77.331  1.00 16.06 ?  657  ILE B CB    1 
ATOM   14090 C CG1   . ILE B 1 659  ? 15.982  21.449  76.109  1.00 15.01 ?  657  ILE B CG1   1 
ATOM   14091 C CG2   . ILE B 1 659  ? 16.860  21.700  78.454  1.00 18.23 ?  657  ILE B CG2   1 
ATOM   14092 C CD1   . ILE B 1 659  ? 14.538  21.889  76.278  1.00 15.89 ?  657  ILE B CD1   1 
ATOM   14093 N N     . ILE B 1 660  ? 18.000  18.256  78.731  1.00 15.62 ?  658  ILE B N     1 
ATOM   14094 C CA    . ILE B 1 660  ? 18.667  17.669  79.894  1.00 14.48 ?  658  ILE B CA    1 
ATOM   14095 C C     . ILE B 1 660  ? 20.116  17.324  79.564  1.00 14.61 ?  658  ILE B C     1 
ATOM   14096 O O     . ILE B 1 660  ? 21.040  17.646  80.325  1.00 17.40 ?  658  ILE B O     1 
ATOM   14097 C CB    . ILE B 1 660  ? 17.898  16.425  80.369  1.00 17.35 ?  658  ILE B CB    1 
ATOM   14098 C CG1   . ILE B 1 660  ? 16.589  16.835  81.045  1.00 17.99 ?  658  ILE B CG1   1 
ATOM   14099 C CG2   . ILE B 1 660  ? 18.779  15.555  81.275  1.00 17.44 ?  658  ILE B CG2   1 
ATOM   14100 C CD1   . ILE B 1 660  ? 15.660  15.664  81.283  1.00 19.09 ?  658  ILE B CD1   1 
ATOM   14101 N N     . ARG B 1 661  ? 20.340  16.655  78.428  1.00 14.97 ?  659  ARG B N     1 
ATOM   14102 C CA    . ARG B 1 661  ? 21.666  16.103  78.160  1.00 15.38 ?  659  ARG B CA    1 
ATOM   14103 C C     . ARG B 1 661  ? 22.613  17.139  77.570  1.00 16.43 ?  659  ARG B C     1 
ATOM   14104 O O     . ARG B 1 661  ? 23.799  17.156  77.908  1.00 17.17 ?  659  ARG B O     1 
ATOM   14105 C CB    . ARG B 1 661  ? 21.554  14.883  77.248  1.00 18.31 ?  659  ARG B CB    1 
ATOM   14106 C CG    . ARG B 1 661  ? 21.058  13.666  78.001  1.00 21.07 ?  659  ARG B CG    1 
ATOM   14107 C CD    . ARG B 1 661  ? 20.882  12.446  77.120  1.00 26.09 ?  659  ARG B CD    1 
ATOM   14108 N NE    . ARG B 1 661  ? 22.110  12.035  76.452  1.00 23.88 ?  659  ARG B NE    1 
ATOM   14109 C CZ    . ARG B 1 661  ? 22.228  11.876  75.141  1.00 23.81 ?  659  ARG B CZ    1 
ATOM   14110 N NH1   . ARG B 1 661  ? 21.212  12.093  74.324  1.00 23.87 ?  659  ARG B NH1   1 
ATOM   14111 N NH2   . ARG B 1 661  ? 23.388  11.464  74.637  1.00 24.78 ?  659  ARG B NH2   1 
ATOM   14112 N N     . GLU B 1 662  ? 22.128  18.014  76.692  1.00 15.30 ?  660  GLU B N     1 
ATOM   14113 C CA    . GLU B 1 662  ? 23.029  18.981  76.077  1.00 16.49 ?  660  GLU B CA    1 
ATOM   14114 C C     . GLU B 1 662  ? 23.286  20.176  76.992  1.00 16.41 ?  660  GLU B C     1 
ATOM   14115 O O     . GLU B 1 662  ? 24.423  20.650  77.103  1.00 17.26 ?  660  GLU B O     1 
ATOM   14116 C CB    . GLU B 1 662  ? 22.460  19.443  74.730  1.00 17.07 ?  660  GLU B CB    1 
ATOM   14117 C CG    . GLU B 1 662  ? 23.310  20.531  74.086  1.00 18.32 ?  660  GLU B CG    1 
ATOM   14118 C CD    . GLU B 1 662  ? 22.757  21.068  72.774  1.00 17.47 ?  660  GLU B CD    1 
ATOM   14119 O OE1   . GLU B 1 662  ? 21.547  21.337  72.666  1.00 18.01 ?  660  GLU B OE1   1 
ATOM   14120 O OE2   . GLU B 1 662  ? 23.571  21.234  71.851  1.00 18.07 ?  660  GLU B OE2   1 
ATOM   14121 N N     . ALA B 1 663  ? 22.261  20.670  77.672  1.00 15.68 ?  661  ALA B N     1 
ATOM   14122 C CA    . ALA B 1 663  ? 22.404  21.893  78.444  1.00 14.59 ?  661  ALA B CA    1 
ATOM   14123 C C     . ALA B 1 663  ? 22.587  21.640  79.933  1.00 14.60 ?  661  ALA B C     1 
ATOM   14124 O O     . ALA B 1 663  ? 22.820  22.594  80.682  1.00 16.79 ?  661  ALA B O     1 
ATOM   14125 C CB    . ALA B 1 663  ? 21.190  22.797  78.206  1.00 15.84 ?  661  ALA B CB    1 
ATOM   14126 N N     . GLY B 1 664  ? 22.499  20.389  80.368  1.00 14.86 ?  662  GLY B N     1 
ATOM   14127 C CA    . GLY B 1 664  ? 22.743  20.056  81.755  1.00 16.32 ?  662  GLY B CA    1 
ATOM   14128 C C     . GLY B 1 664  ? 21.605  20.365  82.698  1.00 16.90 ?  662  GLY B C     1 
ATOM   14129 O O     . GLY B 1 664  ? 21.841  20.537  83.897  1.00 17.83 ?  662  GLY B O     1 
ATOM   14130 N N     . LYS B 1 665  ? 20.374  20.438  82.202  1.00 16.32 ?  663  LYS B N     1 
ATOM   14131 C CA    . LYS B 1 665  ? 19.245  20.858  83.023  1.00 15.45 ?  663  LYS B CA    1 
ATOM   14132 C C     . LYS B 1 665  ? 18.525  19.668  83.633  1.00 12.45 ?  663  LYS B C     1 
ATOM   14133 O O     . LYS B 1 665  ? 18.558  18.551  83.119  1.00 16.31 ?  663  LYS B O     1 
ATOM   14134 C CB    . LYS B 1 665  ? 18.241  21.669  82.206  1.00 16.53 ?  663  LYS B CB    1 
ATOM   14135 C CG    . LYS B 1 665  ? 18.794  22.945  81.670  1.00 17.02 ?  663  LYS B CG    1 
ATOM   14136 C CD    . LYS B 1 665  ? 17.683  23.970  81.478  1.00 17.66 ?  663  LYS B CD    1 
ATOM   14137 C CE    . LYS B 1 665  ? 18.293  25.294  81.089  1.00 21.07 ?  663  LYS B CE    1 
ATOM   14138 N NZ    . LYS B 1 665  ? 17.285  26.391  81.037  1.00 17.25 ?  663  LYS B NZ    1 
ATOM   14139 N N     . SER B 1 666  ? 17.847  19.938  84.748  1.00 16.32 ?  664  SER B N     1 
ATOM   14140 C CA    . SER B 1 666  ? 16.932  18.964  85.320  1.00 17.13 ?  664  SER B CA    1 
ATOM   14141 C C     . SER B 1 666  ? 15.677  18.857  84.457  1.00 16.76 ?  664  SER B C     1 
ATOM   14142 O O     . SER B 1 666  ? 15.343  19.772  83.702  1.00 16.93 ?  664  SER B O     1 
ATOM   14143 C CB    . SER B 1 666  ? 16.539  19.379  86.738  1.00 19.90 ?  664  SER B CB    1 
ATOM   14144 O OG    . SER B 1 666  ? 15.761  20.573  86.681  1.00 19.88 ?  664  SER B OG    1 
ATOM   14145 N N     . ALA B 1 667  ? 14.972  17.726  84.578  1.00 16.60 ?  665  ALA B N     1 
ATOM   14146 C CA    . ALA B 1 667  ? 13.711  17.572  83.850  1.00 16.50 ?  665  ALA B CA    1 
ATOM   14147 C C     . ALA B 1 667  ? 12.717  18.653  84.248  1.00 16.29 ?  665  ALA B C     1 
ATOM   14148 O O     . ALA B 1 667  ? 12.008  19.204  83.399  1.00 15.26 ?  665  ALA B O     1 
ATOM   14149 C CB    . ALA B 1 667  ? 13.120  16.180  84.096  1.00 20.72 ?  665  ALA B CB    1 
ATOM   14150 N N     . LEU B 1 668  ? 12.665  18.981  85.536  1.00 15.69 ?  666  LEU B N     1 
ATOM   14151 C CA    . LEU B 1 668  ? 11.784  20.039  86.009  1.00 15.25 ?  666  LEU B CA    1 
ATOM   14152 C C     . LEU B 1 668  ? 12.042  21.352  85.276  1.00 14.42 ?  666  LEU B C     1 
ATOM   14153 O O     . LEU B 1 668  ? 11.113  22.000  84.770  1.00 15.49 ?  666  LEU B O     1 
ATOM   14154 C CB    . LEU B 1 668  ? 11.990  20.210  87.508  1.00 21.46 ?  666  LEU B CB    1 
ATOM   14155 C CG    . LEU B 1 668  ? 10.951  21.063  88.199  1.00 22.47 ?  666  LEU B CG    1 
ATOM   14156 C CD1   . LEU B 1 668  ? 9.611   20.339  88.176  1.00 28.92 ?  666  LEU B CD1   1 
ATOM   14157 C CD2   . LEU B 1 668  ? 11.409  21.322  89.626  1.00 30.41 ?  666  LEU B CD2   1 
ATOM   14158 N N     . ASN B 1 669  ? 13.309  21.763  85.204  1.00 14.29 ?  667  ASN B N     1 
ATOM   14159 C CA    . ASN B 1 669  ? 13.609  23.028  84.546  1.00 13.92 ?  667  ASN B CA    1 
ATOM   14160 C C     . ASN B 1 669  ? 13.459  22.904  83.037  1.00 13.51 ?  667  ASN B C     1 
ATOM   14161 O O     . ASN B 1 669  ? 13.114  23.886  82.368  1.00 14.22 ?  667  ASN B O     1 
ATOM   14162 C CB    . ASN B 1 669  ? 15.020  23.482  84.900  1.00 15.24 ?  667  ASN B CB    1 
ATOM   14163 C CG    . ASN B 1 669  ? 15.136  23.943  86.330  1.00 16.39 ?  667  ASN B CG    1 
ATOM   14164 O OD1   . ASN B 1 669  ? 14.210  24.553  86.874  1.00 20.24 ?  667  ASN B OD1   1 
ATOM   14165 N ND2   . ASN B 1 669  ? 16.262  23.651  86.949  1.00 17.91 ?  667  ASN B ND2   1 
ATOM   14166 N N     . ALA B 1 670  ? 13.718  21.715  82.483  1.00 13.54 ?  668  ALA B N     1 
ATOM   14167 C CA    . ALA B 1 670  ? 13.547  21.541  81.043  1.00 13.46 ?  668  ALA B CA    1 
ATOM   14168 C C     . ALA B 1 670  ? 12.084  21.674  80.647  1.00 12.70 ?  668  ALA B C     1 
ATOM   14169 O O     . ALA B 1 670  ? 11.767  22.251  79.596  1.00 12.25 ?  668  ALA B O     1 
ATOM   14170 C CB    . ALA B 1 670  ? 14.106  20.191  80.594  1.00 15.18 ?  668  ALA B CB    1 
ATOM   14171 N N     . ILE B 1 671  ? 11.172  21.143  81.473  1.00 12.37 ?  669  ILE B N     1 
ATOM   14172 C CA    . ILE B 1 671  ? 9.742   21.310  81.208  1.00 12.95 ?  669  ILE B CA    1 
ATOM   14173 C C     . ILE B 1 671  ? 9.381   22.786  81.184  1.00 13.88 ?  669  ILE B C     1 
ATOM   14174 O O     . ILE B 1 671  ? 8.693   23.256  80.274  1.00 13.49 ?  669  ILE B O     1 
ATOM   14175 C CB    . ILE B 1 671  ? 8.902   20.557  82.257  1.00 12.81 ?  669  ILE B CB    1 
ATOM   14176 C CG1   . ILE B 1 671  ? 9.072   19.050  82.079  1.00 16.09 ?  669  ILE B CG1   1 
ATOM   14177 C CG2   . ILE B 1 671  ? 7.446   20.957  82.135  1.00 15.92 ?  669  ILE B CG2   1 
ATOM   14178 C CD1   . ILE B 1 671  ? 8.557   18.229  83.245  1.00 19.42 ?  669  ILE B CD1   1 
ATOM   14179 N N     . ALA B 1 672  ? 9.813   23.531  82.200  1.00 12.63 ?  670  ALA B N     1 
ATOM   14180 C CA    . ALA B 1 672  ? 9.507   24.954  82.236  1.00 13.63 ?  670  ALA B CA    1 
ATOM   14181 C C     . ALA B 1 672  ? 10.089  25.677  81.032  1.00 14.66 ?  670  ALA B C     1 
ATOM   14182 O O     . ALA B 1 672  ? 9.482   26.625  80.534  1.00 14.94 ?  670  ALA B O     1 
ATOM   14183 C CB    . ALA B 1 672  ? 10.030  25.565  83.536  1.00 15.11 ?  670  ALA B CB    1 
ATOM   14184 N N     . GLU B 1 673  ? 11.252  25.239  80.543  1.00 13.50 ?  671  GLU B N     1 
ATOM   14185 C CA    . GLU B 1 673  ? 11.846  25.896  79.388  1.00 13.52 ?  671  GLU B CA    1 
ATOM   14186 C C     . GLU B 1 673  ? 11.037  25.648  78.124  1.00 12.33 ?  671  GLU B C     1 
ATOM   14187 O O     . GLU B 1 673  ? 10.798  26.584  77.351  1.00 12.52 ?  671  GLU B O     1 
ATOM   14188 C CB    . GLU B 1 673  ? 13.285  25.437  79.179  1.00 14.66 ?  671  GLU B CB    1 
ATOM   14189 C CG    . GLU B 1 673  ? 13.810  25.965  77.866  1.00 17.83 ?  671  GLU B CG    1 
ATOM   14190 C CD    . GLU B 1 673  ? 15.285  26.244  77.860  1.00 16.41 ?  671  GLU B CD    1 
ATOM   14191 O OE1   . GLU B 1 673  ? 16.022  25.668  78.691  1.00 17.88 ?  671  GLU B OE1   1 
ATOM   14192 O OE2   . GLU B 1 673  ? 15.709  27.038  76.991  1.00 13.23 ?  671  GLU B OE2   1 
ATOM   14193 N N     . VAL B 1 674  ? 10.610  24.402  77.892  1.00 10.80 ?  672  VAL B N     1 
ATOM   14194 C CA    . VAL B 1 674  ? 9.765   24.134  76.731  1.00 11.39 ?  672  VAL B CA    1 
ATOM   14195 C C     . VAL B 1 674  ? 8.454   24.899  76.845  1.00 11.73 ?  672  VAL B C     1 
ATOM   14196 O O     . VAL B 1 674  ? 7.980   25.484  75.866  1.00 11.00 ?  672  VAL B O     1 
ATOM   14197 C CB    . VAL B 1 674  ? 9.533   22.621  76.545  1.00 10.76 ?  672  VAL B CB    1 
ATOM   14198 C CG1   . VAL B 1 674  ? 8.682   22.368  75.312  1.00 11.19 ?  672  VAL B CG1   1 
ATOM   14199 C CG2   . VAL B 1 674  ? 10.865  21.897  76.383  1.00 12.53 ?  672  VAL B CG2   1 
ATOM   14200 N N     . ARG B 1 675  ? 7.870   24.948  78.049  1.00 11.04 ?  673  ARG B N     1 
ATOM   14201 C CA    . ARG B 1 675  ? 6.666   25.758  78.243  1.00 11.78 ?  673  ARG B CA    1 
ATOM   14202 C C     . ARG B 1 675  ? 6.899   27.216  77.854  1.00 9.90  ?  673  ARG B C     1 
ATOM   14203 O O     . ARG B 1 675  ? 6.059   27.823  77.183  1.00 10.50 ?  673  ARG B O     1 
ATOM   14204 C CB    . ARG B 1 675  ? 6.190   25.696  79.691  1.00 11.79 ?  673  ARG B CB    1 
ATOM   14205 C CG    . ARG B 1 675  ? 5.543   24.397  80.101  1.00 12.25 ?  673  ARG B CG    1 
ATOM   14206 C CD    . ARG B 1 675  ? 4.851   24.564  81.451  1.00 11.03 ?  673  ARG B CD    1 
ATOM   14207 N NE    . ARG B 1 675  ? 3.688   25.429  81.310  1.00 12.23 ?  673  ARG B NE    1 
ATOM   14208 C CZ    . ARG B 1 675  ? 3.070   26.032  82.316  1.00 12.04 ?  673  ARG B CZ    1 
ATOM   14209 N NH1   . ARG B 1 675  ? 3.517   25.933  83.560  1.00 14.98 ?  673  ARG B NH1   1 
ATOM   14210 N NH2   . ARG B 1 675  ? 1.979   26.752  82.066  1.00 12.07 ?  673  ARG B NH2   1 
ATOM   14211 N N     . GLU B 1 676  ? 8.044   27.777  78.235  1.00 10.72 ?  674  GLU B N     1 
ATOM   14212 C CA    . GLU B 1 676  ? 8.318   29.179  77.933  1.00 10.83 ?  674  GLU B CA    1 
ATOM   14213 C C     . GLU B 1 676  ? 8.468   29.397  76.430  1.00 11.00 ?  674  GLU B C     1 
ATOM   14214 O O     . GLU B 1 676  ? 7.993   30.406  75.893  1.00 10.41 ?  674  GLU B O     1 
ATOM   14215 C CB    . GLU B 1 676  ? 9.569   29.631  78.677  1.00 11.34 ?  674  GLU B CB    1 
ATOM   14216 C CG    . GLU B 1 676  ? 9.889   31.101  78.483  1.00 14.19 ?  674  GLU B CG    1 
ATOM   14217 C CD    . GLU B 1 676  ? 10.998  31.598  79.394  1.00 23.81 ?  674  GLU B CD    1 
ATOM   14218 O OE1   . GLU B 1 676  ? 11.262  30.972  80.454  1.00 25.71 ?  674  GLU B OE1   1 
ATOM   14219 O OE2   . GLU B 1 676  ? 11.602  32.635  79.058  1.00 26.59 ?  674  GLU B OE2   1 
ATOM   14220 N N     . ALA B 1 677  ? 9.099   28.450  75.727  1.00 9.98  ?  675  ALA B N     1 
ATOM   14221 C CA    . ALA B 1 677  ? 9.189   28.560  74.273  1.00 9.82  ?  675  ALA B CA    1 
ATOM   14222 C C     . ALA B 1 677  ? 7.805   28.554  73.633  1.00 9.87  ?  675  ALA B C     1 
ATOM   14223 O O     . ALA B 1 677  ? 7.516   29.366  72.742  1.00 9.84  ?  675  ALA B O     1 
ATOM   14224 C CB    . ALA B 1 677  ? 10.035  27.417  73.720  1.00 11.28 ?  675  ALA B CB    1 
ATOM   14225 N N     . ILE B 1 678  ? 6.942   27.637  74.074  1.00 9.90  ?  676  ILE B N     1 
ATOM   14226 C CA    . ILE B 1 678  ? 5.559   27.598  73.595  1.00 9.30  ?  676  ILE B CA    1 
ATOM   14227 C C     . ILE B 1 678  ? 4.863   28.919  73.894  1.00 9.85  ?  676  ILE B C     1 
ATOM   14228 O O     . ILE B 1 678  ? 4.165   29.478  73.035  1.00 9.92  ?  676  ILE B O     1 
ATOM   14229 C CB    . ILE B 1 678  ? 4.819   26.405  74.236  1.00 9.69  ?  676  ILE B CB    1 
ATOM   14230 C CG1   . ILE B 1 678  ? 5.412   25.078  73.767  1.00 10.58 ?  676  ILE B CG1   1 
ATOM   14231 C CG2   . ILE B 1 678  ? 3.275   26.466  74.034  1.00 11.81 ?  676  ILE B CG2   1 
ATOM   14232 C CD1   . ILE B 1 678  ? 5.101   23.932  74.702  1.00 10.90 ?  676  ILE B CD1   1 
ATOM   14233 N N     . ASP B 1 679  ? 5.056   29.447  75.110  1.00 8.85  ?  677  ASP B N     1 
ATOM   14234 C CA    . ASP B 1 679  ? 4.388   30.690  75.478  1.00 10.91 ?  677  ASP B CA    1 
ATOM   14235 C C     . ASP B 1 679  ? 4.864   31.862  74.625  1.00 9.02  ?  677  ASP B C     1 
ATOM   14236 O O     . ASP B 1 679  ? 4.047   32.692  74.206  1.00 10.17 ?  677  ASP B O     1 
ATOM   14237 C CB    . ASP B 1 679  ? 4.609   31.002  76.959  1.00 10.67 ?  677  ASP B CB    1 
ATOM   14238 C CG    . ASP B 1 679  ? 3.913   30.010  77.897  1.00 12.03 ?  677  ASP B CG    1 
ATOM   14239 O OD1   . ASP B 1 679  ? 2.886   29.417  77.517  1.00 14.84 ?  677  ASP B OD1   1 
ATOM   14240 O OD2   . ASP B 1 679  ? 4.398   29.871  79.043  1.00 14.63 ?  677  ASP B OD2   1 
ATOM   14241 N N     . PHE B 1 680  ? 6.177   31.966  74.364  1.00 9.48  ?  678  PHE B N     1 
ATOM   14242 C CA    . PHE B 1 680  ? 6.661   33.024  73.473  1.00 8.65  ?  678  PHE B CA    1 
ATOM   14243 C C     . PHE B 1 680  ? 5.982   32.931  72.107  1.00 9.74  ?  678  PHE B C     1 
ATOM   14244 O O     . PHE B 1 680  ? 5.546   33.945  71.546  1.00 10.08 ?  678  PHE B O     1 
ATOM   14245 C CB    . PHE B 1 680  ? 8.179   32.941  73.269  1.00 8.38  ?  678  PHE B CB    1 
ATOM   14246 C CG    . PHE B 1 680  ? 9.012   33.578  74.350  1.00 9.05  ?  678  PHE B CG    1 
ATOM   14247 C CD1   . PHE B 1 680  ? 8.794   34.878  74.761  1.00 10.13 ?  678  PHE B CD1   1 
ATOM   14248 C CD2   . PHE B 1 680  ? 10.061  32.872  74.905  1.00 10.87 ?  678  PHE B CD2   1 
ATOM   14249 C CE1   . PHE B 1 680  ? 9.599   35.465  75.739  1.00 12.00 ?  678  PHE B CE1   1 
ATOM   14250 C CE2   . PHE B 1 680  ? 10.868  33.436  75.883  1.00 12.48 ?  678  PHE B CE2   1 
ATOM   14251 C CZ    . PHE B 1 680  ? 10.630  34.734  76.310  1.00 10.84 ?  678  PHE B CZ    1 
ATOM   14252 N N     . LEU B 1 681  ? 5.952   31.725  71.529  1.00 8.83  ?  679  LEU B N     1 
ATOM   14253 C CA    . LEU B 1 681  ? 5.337   31.549  70.215  1.00 8.98  ?  679  LEU B CA    1 
ATOM   14254 C C     . LEU B 1 681  ? 3.897   32.037  70.217  1.00 9.08  ?  679  LEU B C     1 
ATOM   14255 O O     . LEU B 1 681  ? 3.489   32.812  69.340  1.00 10.53 ?  679  LEU B O     1 
ATOM   14256 C CB    . LEU B 1 681  ? 5.411   30.079  69.802  1.00 10.12 ?  679  LEU B CB    1 
ATOM   14257 C CG    . LEU B 1 681  ? 6.826   29.596  69.471  1.00 9.21  ?  679  LEU B CG    1 
ATOM   14258 C CD1   . LEU B 1 681  ? 6.858   28.065  69.526  1.00 10.37 ?  679  LEU B CD1   1 
ATOM   14259 C CD2   . LEU B 1 681  ? 7.278   30.101  68.094  1.00 11.56 ?  679  LEU B CD2   1 
ATOM   14260 N N     . ARG B 1 682  ? 3.114   31.614  71.217  1.00 8.33  ?  680  ARG B N     1 
ATOM   14261 C CA    . ARG B 1 682  ? 1.697   31.962  71.228  1.00 9.38  ?  680  ARG B CA    1 
ATOM   14262 C C     . ARG B 1 682  ? 1.472   33.412  71.613  1.00 9.61  ?  680  ARG B C     1 
ATOM   14263 O O     . ARG B 1 682  ? 0.525   34.032  71.109  1.00 10.39 ?  680  ARG B O     1 
ATOM   14264 C CB    . ARG B 1 682  ? 0.938   31.033  72.163  1.00 10.16 ?  680  ARG B CB    1 
ATOM   14265 C CG    . ARG B 1 682  ? 0.799   29.630  71.601  1.00 10.66 ?  680  ARG B CG    1 
ATOM   14266 C CD    . ARG B 1 682  ? 0.193   28.715  72.643  1.00 10.27 ?  680  ARG B CD    1 
ATOM   14267 N NE    . ARG B 1 682  ? -0.041  27.382  72.105  1.00 10.36 ?  680  ARG B NE    1 
ATOM   14268 C CZ    . ARG B 1 682  ? -0.266  26.322  72.869  1.00 11.47 ?  680  ARG B CZ    1 
ATOM   14269 N NH1   . ARG B 1 682  ? -0.328  26.425  74.190  1.00 12.64 ?  680  ARG B NH1   1 
ATOM   14270 N NH2   . ARG B 1 682  ? -0.398  25.128  72.296  1.00 14.12 ?  680  ARG B NH2   1 
ATOM   14271 N N     . TYR B 1 683  ? 2.304   33.956  72.504  1.00 9.81  ?  681  TYR B N     1 
ATOM   14272 C CA    . TYR B 1 683  ? 2.153   35.350  72.902  1.00 10.17 ?  681  TYR B CA    1 
ATOM   14273 C C     . TYR B 1 683  ? 2.501   36.292  71.754  1.00 9.74  ?  681  TYR B C     1 
ATOM   14274 O O     . TYR B 1 683  ? 1.748   37.227  71.471  1.00 9.70  ?  681  TYR B O     1 
ATOM   14275 C CB    . TYR B 1 683  ? 3.016   35.635  74.133  1.00 9.94  ?  681  TYR B CB    1 
ATOM   14276 C CG    . TYR B 1 683  ? 2.980   37.087  74.544  1.00 9.54  ?  681  TYR B CG    1 
ATOM   14277 C CD1   . TYR B 1 683  ? 1.941   37.574  75.328  1.00 10.67 ?  681  TYR B CD1   1 
ATOM   14278 C CD2   . TYR B 1 683  ? 3.992   37.955  74.170  1.00 9.77  ?  681  TYR B CD2   1 
ATOM   14279 C CE1   . TYR B 1 683  ? 1.900   38.912  75.696  1.00 12.25 ?  681  TYR B CE1   1 
ATOM   14280 C CE2   . TYR B 1 683  ? 3.965   39.294  74.530  1.00 10.06 ?  681  TYR B CE2   1 
ATOM   14281 C CZ    . TYR B 1 683  ? 2.917   39.760  75.301  1.00 11.02 ?  681  TYR B CZ    1 
ATOM   14282 O OH    . TYR B 1 683  ? 2.853   41.091  75.666  1.00 14.02 ?  681  TYR B OH    1 
ATOM   14283 N N     . TYR B 1 684  ? 3.643   36.073  71.085  1.00 9.78  ?  682  TYR B N     1 
ATOM   14284 C CA    . TYR B 1 684  ? 3.968   36.972  69.979  1.00 8.99  ?  682  TYR B CA    1 
ATOM   14285 C C     . TYR B 1 684  ? 2.990   36.798  68.821  1.00 10.35 ?  682  TYR B C     1 
ATOM   14286 O O     . TYR B 1 684  ? 2.694   37.768  68.113  1.00 10.69 ?  682  TYR B O     1 
ATOM   14287 C CB    . TYR B 1 684  ? 5.414   36.769  69.515  1.00 9.88  ?  682  TYR B CB    1 
ATOM   14288 C CG    . TYR B 1 684  ? 6.439   37.152  70.562  1.00 9.28  ?  682  TYR B CG    1 
ATOM   14289 C CD1   . TYR B 1 684  ? 6.279   38.305  71.333  1.00 10.25 ?  682  TYR B CD1   1 
ATOM   14290 C CD2   . TYR B 1 684  ? 7.557   36.359  70.788  1.00 9.75  ?  682  TYR B CD2   1 
ATOM   14291 C CE1   . TYR B 1 684  ? 7.215   38.657  72.311  1.00 10.78 ?  682  TYR B CE1   1 
ATOM   14292 C CE2   . TYR B 1 684  ? 8.493   36.703  71.753  1.00 10.29 ?  682  TYR B CE2   1 
ATOM   14293 C CZ    . TYR B 1 684  ? 8.310   37.842  72.510  1.00 10.50 ?  682  TYR B CZ    1 
ATOM   14294 O OH    . TYR B 1 684  ? 9.243   38.167  73.479  1.00 10.19 ?  682  TYR B OH    1 
ATOM   14295 N N     . ALA B 1 685  ? 2.444   35.592  68.638  1.00 9.52  ?  683  ALA B N     1 
ATOM   14296 C CA    . ALA B 1 685  ? 1.379   35.407  67.651  1.00 9.52  ?  683  ALA B CA    1 
ATOM   14297 C C     . ALA B 1 685  ? 0.157   36.261  67.990  1.00 9.95  ?  683  ALA B C     1 
ATOM   14298 O O     . ALA B 1 685  ? -0.397  36.945  67.119  1.00 10.35 ?  683  ALA B O     1 
ATOM   14299 C CB    . ALA B 1 685  ? 0.991   33.930  67.570  1.00 10.20 ?  683  ALA B CB    1 
ATOM   14300 N N     . GLU B 1 686  ? -0.299  36.212  69.245  1.00 9.23  ?  684  GLU B N     1 
ATOM   14301 C CA    . GLU B 1 686  ? -1.473  36.994  69.614  1.00 12.57 ?  684  GLU B CA    1 
ATOM   14302 C C     . GLU B 1 686  ? -1.187  38.487  69.536  1.00 11.58 ?  684  GLU B C     1 
ATOM   14303 O O     . GLU B 1 686  ? -2.008  39.246  69.014  1.00 11.41 ?  684  GLU B O     1 
ATOM   14304 C CB    . GLU B 1 686  ? -1.947  36.617  71.009  1.00 14.30 ?  684  GLU B CB    1 
ATOM   14305 C CG    . GLU B 1 686  ? -3.084  37.538  71.500  1.00 15.02 ?  684  GLU B CG    1 
ATOM   14306 C CD    . GLU B 1 686  ? -4.379  37.453  70.676  1.00 20.82 ?  684  GLU B CD    1 
ATOM   14307 O OE1   . GLU B 1 686  ? -4.527  36.547  69.824  1.00 18.51 ?  684  GLU B OE1   1 
ATOM   14308 O OE2   . GLU B 1 686  ? -5.278  38.303  70.896  1.00 21.39 ?  684  GLU B OE2   1 
ATOM   14309 N N     . GLN B 1 687  ? -0.013  38.923  70.009  1.00 9.73  ?  685  GLN B N     1 
ATOM   14310 C CA    . GLN B 1 687  ? 0.314   40.344  69.914  1.00 9.10  ?  685  GLN B CA    1 
ATOM   14311 C C     . GLN B 1 687  ? 0.335   40.806  68.462  1.00 11.20 ?  685  GLN B C     1 
ATOM   14312 O O     . GLN B 1 687  ? -0.112  41.916  68.163  1.00 12.30 ?  685  GLN B O     1 
ATOM   14313 C CB    . GLN B 1 687  ? 1.651   40.642  70.590  1.00 11.30 ?  685  GLN B CB    1 
ATOM   14314 C CG    . GLN B 1 687  ? 1.614   40.448  72.116  1.00 11.16 ?  685  GLN B CG    1 
ATOM   14315 C CD    . GLN B 1 687  ? 0.615   41.361  72.798  1.00 12.48 ?  685  GLN B CD    1 
ATOM   14316 O OE1   . GLN B 1 687  ? 0.649   42.568  72.622  1.00 13.75 ?  685  GLN B OE1   1 
ATOM   14317 N NE2   . GLN B 1 687  ? -0.301  40.775  73.562  1.00 17.71 ?  685  GLN B NE2   1 
ATOM   14318 N N     . THR B 1 688  ? 0.817   39.955  67.542  1.00 9.91  ?  686  THR B N     1 
ATOM   14319 C CA    . THR B 1 688  ? 0.767   40.280  66.114  1.00 10.41 ?  686  THR B CA    1 
ATOM   14320 C C     . THR B 1 688  ? -0.671  40.461  65.643  1.00 9.97  ?  686  THR B C     1 
ATOM   14321 O O     . THR B 1 688  ? -1.002  41.450  64.974  1.00 12.94 ?  686  THR B O     1 
ATOM   14322 C CB    . THR B 1 688  ? 1.461   39.173  65.318  1.00 10.99 ?  686  THR B CB    1 
ATOM   14323 O OG1   . THR B 1 688  ? 2.860   39.175  65.632  1.00 11.39 ?  686  THR B OG1   1 
ATOM   14324 C CG2   . THR B 1 688  ? 1.257   39.383  63.814  1.00 12.66 ?  686  THR B CG2   1 
ATOM   14325 N N     . ARG B 1 689  ? -1.540  39.512  65.986  1.00 10.40 ?  687  ARG B N     1 
ATOM   14326 C CA    . ARG B 1 689  ? -2.940  39.606  65.569  1.00 10.64 ?  687  ARG B CA    1 
ATOM   14327 C C     . ARG B 1 689  ? -3.624  40.852  66.129  1.00 12.32 ?  687  ARG B C     1 
ATOM   14328 O O     . ARG B 1 689  ? -4.574  41.361  65.514  1.00 14.92 ?  687  ARG B O     1 
ATOM   14329 C CB    . ARG B 1 689  ? -3.706  38.355  65.993  1.00 13.00 ?  687  ARG B CB    1 
ATOM   14330 C CG    . ARG B 1 689  ? -3.386  37.112  65.152  1.00 13.53 ?  687  ARG B CG    1 
ATOM   14331 C CD    . ARG B 1 689  ? -4.279  35.947  65.536  1.00 13.59 ?  687  ARG B CD    1 
ATOM   14332 N NE    . ARG B 1 689  ? -4.128  35.518  66.921  1.00 14.63 ?  687  ARG B NE    1 
ATOM   14333 C CZ    . ARG B 1 689  ? -3.392  34.483  67.313  1.00 14.08 ?  687  ARG B CZ    1 
ATOM   14334 N NH1   . ARG B 1 689  ? -2.706  33.749  66.445  1.00 13.36 ?  687  ARG B NH1   1 
ATOM   14335 N NH2   . ARG B 1 689  ? -3.350  34.169  68.602  1.00 14.59 ?  687  ARG B NH2   1 
ATOM   14336 N N     . ARG B 1 690  ? -3.168  41.354  67.282  1.00 11.47 ?  688  ARG B N     1 
ATOM   14337 C CA    A ARG B 1 690  ? -3.736  42.565  67.869  0.64 11.83 ?  688  ARG B CA    1 
ATOM   14338 C CA    B ARG B 1 690  ? -3.741  42.562  67.862  0.36 11.87 ?  688  ARG B CA    1 
ATOM   14339 C C     . ARG B 1 690  ? -3.217  43.853  67.241  1.00 12.11 ?  688  ARG B C     1 
ATOM   14340 O O     . ARG B 1 690  ? -3.860  44.899  67.400  1.00 12.95 ?  688  ARG B O     1 
ATOM   14341 C CB    A ARG B 1 690  ? -3.440  42.627  69.376  0.64 11.89 ?  688  ARG B CB    1 
ATOM   14342 C CB    B ARG B 1 690  ? -3.468  42.598  69.370  0.36 11.94 ?  688  ARG B CB    1 
ATOM   14343 C CG    A ARG B 1 690  ? -4.113  41.561  70.236  0.64 13.68 ?  688  ARG B CG    1 
ATOM   14344 C CG    B ARG B 1 690  ? -4.179  41.520  70.167  0.36 13.73 ?  688  ARG B CG    1 
ATOM   14345 C CD    A ARG B 1 690  ? -5.626  41.809  70.437  0.64 15.81 ?  688  ARG B CD    1 
ATOM   14346 C CD    B ARG B 1 690  ? -5.695  41.705  70.111  0.36 15.86 ?  688  ARG B CD    1 
ATOM   14347 N NE    A ARG B 1 690  ? -5.905  43.088  71.086  0.64 14.85 ?  688  ARG B NE    1 
ATOM   14348 N NE    B ARG B 1 690  ? -6.065  43.095  70.352  0.36 16.33 ?  688  ARG B NE    1 
ATOM   14349 C CZ    A ARG B 1 690  ? -6.521  44.108  70.504  0.64 15.39 ?  688  ARG B CZ    1 
ATOM   14350 C CZ    B ARG B 1 690  ? -6.130  43.654  71.551  0.36 15.48 ?  688  ARG B CZ    1 
ATOM   14351 N NH1   A ARG B 1 690  ? -7.031  44.005  69.284  0.64 15.49 ?  688  ARG B NH1   1 
ATOM   14352 N NH1   B ARG B 1 690  ? -5.898  42.958  72.651  0.36 16.44 ?  688  ARG B NH1   1 
ATOM   14353 N NH2   A ARG B 1 690  ? -6.654  45.253  71.171  0.64 13.52 ?  688  ARG B NH2   1 
ATOM   14354 N NH2   B ARG B 1 690  ? -6.424  44.949  71.648  0.36 14.05 ?  688  ARG B NH2   1 
ATOM   14355 N N     . THR B 1 691  ? -2.048  43.828  66.565  1.00 10.72 ?  689  THR B N     1 
ATOM   14356 C CA    . THR B 1 691  ? -1.407  45.097  66.220  1.00 12.83 ?  689  THR B CA    1 
ATOM   14357 C C     . THR B 1 691  ? -1.002  45.279  64.764  1.00 14.14 ?  689  THR B C     1 
ATOM   14358 O O     . THR B 1 691  ? -1.181  46.373  64.240  1.00 15.53 ?  689  THR B O     1 
ATOM   14359 C CB    . THR B 1 691  ? -0.144  45.321  67.087  1.00 13.31 ?  689  THR B CB    1 
ATOM   14360 O OG1   . THR B 1 691  ? 0.773   44.221  66.933  1.00 13.14 ?  689  THR B OG1   1 
ATOM   14361 C CG2   . THR B 1 691  ? -0.515  45.469  68.555  1.00 13.52 ?  689  THR B CG2   1 
ATOM   14362 N N     . LEU B 1 692  ? -0.388  44.285  64.117  1.00 12.86 ?  690  LEU B N     1 
ATOM   14363 C CA    . LEU B 1 692  ? 0.393   44.596  62.917  1.00 13.13 ?  690  LEU B CA    1 
ATOM   14364 C C     . LEU B 1 692  ? -0.476  44.763  61.669  1.00 13.27 ?  690  LEU B C     1 
ATOM   14365 O O     . LEU B 1 692  ? -1.295  43.900  61.340  1.00 15.81 ?  690  LEU B O     1 
ATOM   14366 C CB    . LEU B 1 692  ? 1.458   43.528  62.662  1.00 12.31 ?  690  LEU B CB    1 
ATOM   14367 C CG    . LEU B 1 692  ? 2.547   43.454  63.732  1.00 12.40 ?  690  LEU B CG    1 
ATOM   14368 C CD1   . LEU B 1 692  ? 3.643   42.517  63.225  1.00 14.05 ?  690  LEU B CD1   1 
ATOM   14369 C CD2   . LEU B 1 692  ? 3.126   44.837  64.013  1.00 15.85 ?  690  LEU B CD2   1 
ATOM   14370 N N     . GLY B 1 693  ? -0.259  45.873  60.966  1.00 13.20 ?  691  GLY B N     1 
ATOM   14371 C CA    . GLY B 1 693  ? -0.961  46.189  59.743  1.00 15.12 ?  691  GLY B CA    1 
ATOM   14372 C C     . GLY B 1 693  ? 0.005   46.619  58.656  1.00 15.41 ?  691  GLY B C     1 
ATOM   14373 O O     . GLY B 1 693  ? 1.228   46.571  58.832  1.00 15.74 ?  691  GLY B O     1 
ATOM   14374 N N     . PRO B 1 694  ? -0.529  47.067  57.515  1.00 18.18 ?  692  PRO B N     1 
ATOM   14375 C CA    . PRO B 1 694  ? 0.342   47.310  56.347  1.00 16.15 ?  692  PRO B CA    1 
ATOM   14376 C C     . PRO B 1 694  ? 1.406   48.363  56.578  1.00 18.36 ?  692  PRO B C     1 
ATOM   14377 O O     . PRO B 1 694  ? 2.493   48.277  55.986  1.00 21.13 ?  692  PRO B O     1 
ATOM   14378 C CB    . PRO B 1 694  ? -0.644  47.752  55.254  1.00 20.13 ?  692  PRO B CB    1 
ATOM   14379 C CG    . PRO B 1 694  ? -1.981  47.255  55.698  1.00 20.94 ?  692  PRO B CG    1 
ATOM   14380 C CD    . PRO B 1 694  ? -1.960  47.211  57.206  1.00 18.01 ?  692  PRO B CD    1 
ATOM   14381 N N     . GLY B 1 695  ? 1.138   49.353  57.422  1.00 17.34 ?  693  GLY B N     1 
ATOM   14382 C CA    . GLY B 1 695  ? 2.087   50.415  57.675  1.00 17.78 ?  693  GLY B CA    1 
ATOM   14383 C C     . GLY B 1 695  ? 3.165   50.120  58.693  1.00 17.23 ?  693  GLY B C     1 
ATOM   14384 O O     . GLY B 1 695  ? 3.979   51.004  58.980  1.00 20.76 ?  693  GLY B O     1 
ATOM   14385 N N     . HIS B 1 696  ? 3.204   48.913  59.260  1.00 16.95 ?  694  HIS B N     1 
ATOM   14386 C CA    . HIS B 1 696  ? 4.252   48.551  60.213  1.00 13.75 ?  694  HIS B CA    1 
ATOM   14387 C C     . HIS B 1 696  ? 5.244   47.651  59.485  1.00 17.68 ?  694  HIS B C     1 
ATOM   14388 O O     . HIS B 1 696  ? 5.228   46.429  59.608  1.00 18.99 ?  694  HIS B O     1 
ATOM   14389 C CB    . HIS B 1 696  ? 3.659   47.872  61.451  1.00 13.83 ?  694  HIS B CB    1 
ATOM   14390 C CG    . HIS B 1 696  ? 2.503   48.618  62.039  1.00 12.87 ?  694  HIS B CG    1 
ATOM   14391 N ND1   . HIS B 1 696  ? 1.231   48.090  62.090  1.00 13.65 ?  694  HIS B ND1   1 
ATOM   14392 C CD2   . HIS B 1 696  ? 2.419   49.860  62.572  1.00 14.45 ?  694  HIS B CD2   1 
ATOM   14393 C CE1   . HIS B 1 696  ? 0.414   48.975  62.633  1.00 14.48 ?  694  HIS B CE1   1 
ATOM   14394 N NE2   . HIS B 1 696  ? 1.108   50.058  62.930  1.00 15.27 ?  694  HIS B NE2   1 
ATOM   14395 N N     . GLY B 1 697  ? 6.112   48.280  58.699  1.00 17.29 ?  695  GLY B N     1 
ATOM   14396 C CA    . GLY B 1 697  ? 7.012   47.547  57.838  1.00 17.62 ?  695  GLY B CA    1 
ATOM   14397 C C     . GLY B 1 697  ? 8.154   46.901  58.590  1.00 16.21 ?  695  GLY B C     1 
ATOM   14398 O O     . GLY B 1 697  ? 8.599   47.393  59.626  1.00 16.19 ?  695  GLY B O     1 
ATOM   14399 N N     . PRO B 1 698  ? 8.653   45.779  58.085  1.00 16.34 ?  696  PRO B N     1 
ATOM   14400 C CA    . PRO B 1 698  ? 9.745   45.092  58.777  1.00 15.80 ?  696  PRO B CA    1 
ATOM   14401 C C     . PRO B 1 698  ? 11.073  45.816  58.614  1.00 15.42 ?  696  PRO B C     1 
ATOM   14402 O O     . PRO B 1 698  ? 11.263  46.661  57.735  1.00 18.08 ?  696  PRO B O     1 
ATOM   14403 C CB    . PRO B 1 698  ? 9.780   43.715  58.103  1.00 20.00 ?  696  PRO B CB    1 
ATOM   14404 C CG    . PRO B 1 698  ? 9.293   43.990  56.735  1.00 23.20 ?  696  PRO B CG    1 
ATOM   14405 C CD    . PRO B 1 698  ? 8.171   45.001  56.933  1.00 20.71 ?  696  PRO B CD    1 
ATOM   14406 N N     . LEU B 1 699  ? 12.012  45.463  59.493  1.00 13.41 ?  697  LEU B N     1 
ATOM   14407 C CA    . LEU B 1 699  ? 13.364  46.010  59.390  1.00 13.51 ?  697  LEU B CA    1 
ATOM   14408 C C     . LEU B 1 699  ? 14.123  45.392  58.223  1.00 15.20 ?  697  LEU B C     1 
ATOM   14409 O O     . LEU B 1 699  ? 14.807  46.096  57.474  1.00 14.95 ?  697  LEU B O     1 
ATOM   14410 C CB    . LEU B 1 699  ? 14.138  45.759  60.682  1.00 14.14 ?  697  LEU B CB    1 
ATOM   14411 C CG    . LEU B 1 699  ? 13.579  46.373  61.968  1.00 14.61 ?  697  LEU B CG    1 
ATOM   14412 C CD1   . LEU B 1 699  ? 14.415  45.981  63.171  1.00 15.62 ?  697  LEU B CD1   1 
ATOM   14413 C CD2   . LEU B 1 699  ? 13.521  47.885  61.800  1.00 19.62 ?  697  LEU B CD2   1 
ATOM   14414 N N     . GLY B 1 700  ? 14.026  44.077  58.073  1.00 12.94 ?  698  GLY B N     1 
ATOM   14415 C CA    . GLY B 1 700  ? 14.882  43.327  57.186  1.00 12.71 ?  698  GLY B CA    1 
ATOM   14416 C C     . GLY B 1 700  ? 15.546  42.199  57.946  1.00 14.29 ?  698  GLY B C     1 
ATOM   14417 O O     . GLY B 1 700  ? 15.105  41.820  59.035  1.00 13.99 ?  698  GLY B O     1 
ATOM   14418 N N     . PRO B 1 701  ? 16.636  41.660  57.409  1.00 13.42 ?  699  PRO B N     1 
ATOM   14419 C CA    . PRO B 1 701  ? 17.309  40.529  58.070  1.00 13.26 ?  699  PRO B CA    1 
ATOM   14420 C C     . PRO B 1 701  ? 17.712  40.872  59.499  1.00 13.28 ?  699  PRO B C     1 
ATOM   14421 O O     . PRO B 1 701  ? 18.357  41.891  59.752  1.00 14.85 ?  699  PRO B O     1 
ATOM   14422 C CB    . PRO B 1 701  ? 18.534  40.285  57.181  1.00 13.77 ?  699  PRO B CB    1 
ATOM   14423 C CG    . PRO B 1 701  ? 18.112  40.821  55.832  1.00 16.08 ?  699  PRO B CG    1 
ATOM   14424 C CD    . PRO B 1 701  ? 17.300  42.039  56.147  1.00 13.24 ?  699  PRO B CD    1 
ATOM   14425 N N     . ILE B 1 702  ? 17.302  40.026  60.447  1.00 11.81 ?  700  ILE B N     1 
ATOM   14426 C CA    A ILE B 1 702  ? 17.633  40.215  61.854  0.53 11.15 ?  700  ILE B CA    1 
ATOM   14427 C CA    B ILE B 1 702  ? 17.613  40.202  61.864  0.47 11.16 ?  700  ILE B CA    1 
ATOM   14428 C C     . ILE B 1 702  ? 18.534  39.078  62.304  1.00 12.86 ?  700  ILE B C     1 
ATOM   14429 O O     . ILE B 1 702  ? 18.247  37.904  62.049  1.00 12.47 ?  700  ILE B O     1 
ATOM   14430 C CB    A ILE B 1 702  ? 16.372  40.309  62.726  0.53 11.67 ?  700  ILE B CB    1 
ATOM   14431 C CB    B ILE B 1 702  ? 16.344  40.210  62.733  0.47 11.68 ?  700  ILE B CB    1 
ATOM   14432 C CG1   A ILE B 1 702  ? 15.671  41.646  62.468  0.53 12.71 ?  700  ILE B CG1   1 
ATOM   14433 C CG1   B ILE B 1 702  ? 15.367  41.295  62.274  0.47 13.15 ?  700  ILE B CG1   1 
ATOM   14434 C CG2   A ILE B 1 702  ? 16.732  40.150  64.214  0.53 12.06 ?  700  ILE B CG2   1 
ATOM   14435 C CG2   B ILE B 1 702  ? 16.713  40.367  64.221  0.47 12.10 ?  700  ILE B CG2   1 
ATOM   14436 C CD1   A ILE B 1 702  ? 14.407  41.848  63.274  0.53 11.81 ?  700  ILE B CD1   1 
ATOM   14437 C CD1   B ILE B 1 702  ? 15.854  42.697  62.461  0.47 12.76 ?  700  ILE B CD1   1 
ATOM   14438 N N     . VAL B 1 703  ? 19.620  39.432  62.973  1.00 12.38 ?  701  VAL B N     1 
ATOM   14439 C CA    . VAL B 1 703  ? 20.550  38.462  63.532  1.00 11.55 ?  701  VAL B CA    1 
ATOM   14440 C C     . VAL B 1 703  ? 20.147  38.205  64.977  1.00 13.32 ?  701  VAL B C     1 
ATOM   14441 O O     . VAL B 1 703  ? 20.092  39.136  65.787  1.00 12.84 ?  701  VAL B O     1 
ATOM   14442 C CB    . VAL B 1 703  ? 21.994  38.980  63.439  1.00 11.84 ?  701  VAL B CB    1 
ATOM   14443 C CG1   . VAL B 1 703  ? 22.928  38.092  64.234  1.00 14.63 ?  701  VAL B CG1   1 
ATOM   14444 C CG2   . VAL B 1 703  ? 22.415  39.054  61.970  1.00 14.04 ?  701  VAL B CG2   1 
ATOM   14445 N N     . CYS B 1 704  ? 19.830  36.955  65.299  1.00 10.90 ?  702  CYS B N     1 
ATOM   14446 C CA    . CYS B 1 704  ? 19.399  36.581  66.641  1.00 10.20 ?  702  CYS B CA    1 
ATOM   14447 C C     . CYS B 1 704  ? 20.486  35.741  67.279  1.00 12.09 ?  702  CYS B C     1 
ATOM   14448 O O     . CYS B 1 704  ? 20.760  34.635  66.822  1.00 12.44 ?  702  CYS B O     1 
ATOM   14449 C CB    . CYS B 1 704  ? 18.080  35.806  66.614  1.00 10.92 ?  702  CYS B CB    1 
ATOM   14450 S SG    . CYS B 1 704  ? 16.689  36.718  65.927  1.00 12.25 ?  702  CYS B SG    1 
ATOM   14451 N N     . ILE B 1 705  ? 21.087  36.263  68.351  1.00 12.87 ?  703  ILE B N     1 
ATOM   14452 C CA    . ILE B 1 705  ? 22.184  35.595  69.044  1.00 11.91 ?  703  ILE B CA    1 
ATOM   14453 C C     . ILE B 1 705  ? 21.670  35.234  70.428  1.00 12.79 ?  703  ILE B C     1 
ATOM   14454 O O     . ILE B 1 705  ? 21.269  36.118  71.195  1.00 11.86 ?  703  ILE B O     1 
ATOM   14455 C CB    . ILE B 1 705  ? 23.436  36.479  69.117  1.00 11.71 ?  703  ILE B CB    1 
ATOM   14456 C CG1   . ILE B 1 705  ? 23.951  36.762  67.706  1.00 14.82 ?  703  ILE B CG1   1 
ATOM   14457 C CG2   . ILE B 1 705  ? 24.511  35.824  70.003  1.00 14.49 ?  703  ILE B CG2   1 
ATOM   14458 C CD1   . ILE B 1 705  ? 24.975  37.893  67.642  1.00 16.66 ?  703  ILE B CD1   1 
ATOM   14459 N N     . SER B 1 706  ? 21.688  33.942  70.740  1.00 12.27 ?  704  SER B N     1 
ATOM   14460 C CA    . SER B 1 706  ? 21.004  33.402  71.900  1.00 13.93 ?  704  SER B CA    1 
ATOM   14461 C C     . SER B 1 706  ? 21.990  32.739  72.854  1.00 13.45 ?  704  SER B C     1 
ATOM   14462 O O     . SER B 1 706  ? 23.090  32.325  72.453  1.00 13.54 ?  704  SER B O     1 
ATOM   14463 C CB    . SER B 1 706  ? 19.925  32.398  71.466  1.00 13.63 ?  704  SER B CB    1 
ATOM   14464 O OG    . SER B 1 706  ? 20.487  31.394  70.655  1.00 13.33 ?  704  SER B OG    1 
ATOM   14465 N N     . PRO B 1 707  ? 21.626  32.638  74.125  1.00 12.68 ?  705  PRO B N     1 
ATOM   14466 C CA    . PRO B 1 707  ? 22.532  32.138  75.159  1.00 13.91 ?  705  PRO B CA    1 
ATOM   14467 C C     . PRO B 1 707  ? 22.422  30.627  75.346  1.00 13.76 ?  705  PRO B C     1 
ATOM   14468 O O     . PRO B 1 707  ? 21.494  29.972  74.865  1.00 15.26 ?  705  PRO B O     1 
ATOM   14469 C CB    . PRO B 1 707  ? 22.025  32.880  76.408  1.00 14.67 ?  705  PRO B CB    1 
ATOM   14470 C CG    . PRO B 1 707  ? 20.572  32.931  76.205  1.00 16.42 ?  705  PRO B CG    1 
ATOM   14471 C CD    . PRO B 1 707  ? 20.373  33.151  74.713  1.00 13.99 ?  705  PRO B CD    1 
ATOM   14472 N N     . TRP B 1 708  ? 23.384  30.081  76.090  1.00 12.78 ?  706  TRP B N     1 
ATOM   14473 C CA    . TRP B 1 708  ? 23.372  28.655  76.373  1.00 13.45 ?  706  TRP B CA    1 
ATOM   14474 C C     . TRP B 1 708  ? 22.521  28.301  77.578  1.00 13.12 ?  706  TRP B C     1 
ATOM   14475 O O     . TRP B 1 708  ? 22.255  27.117  77.788  1.00 15.24 ?  706  TRP B O     1 
ATOM   14476 C CB    . TRP B 1 708  ? 24.800  28.129  76.594  1.00 13.75 ?  706  TRP B CB    1 
ATOM   14477 C CG    . TRP B 1 708  ? 25.569  28.954  77.575  1.00 15.16 ?  706  TRP B CG    1 
ATOM   14478 C CD1   . TRP B 1 708  ? 26.484  29.924  77.286  1.00 17.62 ?  706  TRP B CD1   1 
ATOM   14479 C CD2   . TRP B 1 708  ? 25.481  28.895  79.005  1.00 14.80 ?  706  TRP B CD2   1 
ATOM   14480 N NE1   . TRP B 1 708  ? 26.969  30.479  78.452  1.00 17.49 ?  706  TRP B NE1   1 
ATOM   14481 C CE2   . TRP B 1 708  ? 26.358  29.871  79.516  1.00 17.74 ?  706  TRP B CE2   1 
ATOM   14482 C CE3   . TRP B 1 708  ? 24.740  28.118  79.904  1.00 14.96 ?  706  TRP B CE3   1 
ATOM   14483 C CZ2   . TRP B 1 708  ? 26.519  30.084  80.888  1.00 16.95 ?  706  TRP B CZ2   1 
ATOM   14484 C CZ3   . TRP B 1 708  ? 24.897  28.342  81.268  1.00 15.99 ?  706  TRP B CZ3   1 
ATOM   14485 C CH2   . TRP B 1 708  ? 25.769  29.319  81.741  1.00 16.04 ?  706  TRP B CH2   1 
ATOM   14486 N N     . ASN B 1 709  ? 22.104  29.284  78.385  1.00 13.66 ?  707  ASN B N     1 
ATOM   14487 C CA    . ASN B 1 709  ? 21.395  28.934  79.606  1.00 14.80 ?  707  ASN B CA    1 
ATOM   14488 C C     . ASN B 1 709  ? 19.899  28.767  79.405  1.00 14.87 ?  707  ASN B C     1 
ATOM   14489 O O     . ASN B 1 709  ? 19.257  28.109  80.227  1.00 16.47 ?  707  ASN B O     1 
ATOM   14490 C CB    . ASN B 1 709  ? 21.680  29.967  80.709  1.00 15.29 ?  707  ASN B CB    1 
ATOM   14491 C CG    . ASN B 1 709  ? 21.075  31.329  80.428  1.00 16.75 ?  707  ASN B CG    1 
ATOM   14492 O OD1   . ASN B 1 709  ? 20.794  31.690  79.289  1.00 17.10 ?  707  ASN B OD1   1 
ATOM   14493 N ND2   . ASN B 1 709  ? 20.870  32.102  81.483  1.00 15.53 ?  707  ASN B ND2   1 
ATOM   14494 N N     . PHE B 1 710  ? 19.336  29.333  78.341  1.00 13.69 ?  708  PHE B N     1 
ATOM   14495 C CA    . PHE B 1 710  ? 17.964  29.052  77.904  1.00 12.80 ?  708  PHE B CA    1 
ATOM   14496 C C     . PHE B 1 710  ? 18.027  28.775  76.418  1.00 13.10 ?  708  PHE B C     1 
ATOM   14497 O O     . PHE B 1 710  ? 17.542  29.561  75.586  1.00 12.33 ?  708  PHE B O     1 
ATOM   14498 C CB    . PHE B 1 710  ? 17.007  30.193  78.240  1.00 13.17 ?  708  PHE B CB    1 
ATOM   14499 C CG    . PHE B 1 710  ? 16.697  30.251  79.695  1.00 16.37 ?  708  PHE B CG    1 
ATOM   14500 C CD1   . PHE B 1 710  ? 15.668  29.475  80.220  1.00 18.10 ?  708  PHE B CD1   1 
ATOM   14501 C CD2   . PHE B 1 710  ? 17.482  30.998  80.551  1.00 17.23 ?  708  PHE B CD2   1 
ATOM   14502 C CE1   . PHE B 1 710  ? 15.389  29.490  81.574  1.00 21.22 ?  708  PHE B CE1   1 
ATOM   14503 C CE2   . PHE B 1 710  ? 17.205  31.009  81.921  1.00 17.67 ?  708  PHE B CE2   1 
ATOM   14504 C CZ    . PHE B 1 710  ? 16.159  30.253  82.416  1.00 16.50 ?  708  PHE B CZ    1 
ATOM   14505 N N     . PRO B 1 711  ? 18.620  27.636  76.056  1.00 12.96 ?  709  PRO B N     1 
ATOM   14506 C CA    . PRO B 1 711  ? 18.977  27.381  74.656  1.00 12.61 ?  709  PRO B CA    1 
ATOM   14507 C C     . PRO B 1 711  ? 17.803  27.042  73.774  1.00 11.98 ?  709  PRO B C     1 
ATOM   14508 O O     . PRO B 1 711  ? 17.994  26.970  72.558  1.00 12.80 ?  709  PRO B O     1 
ATOM   14509 C CB    . PRO B 1 711  ? 19.938  26.197  74.769  1.00 16.20 ?  709  PRO B CB    1 
ATOM   14510 C CG    . PRO B 1 711  ? 19.389  25.445  75.950  1.00 13.82 ?  709  PRO B CG    1 
ATOM   14511 C CD    . PRO B 1 711  ? 18.983  26.502  76.927  1.00 13.66 ?  709  PRO B CD    1 
ATOM   14512 N N     . LEU B 1 712  ? 16.615  26.820  74.331  1.00 11.72 ?  710  LEU B N     1 
ATOM   14513 C CA    . LEU B 1 712  ? 15.402  26.751  73.528  1.00 11.74 ?  710  LEU B CA    1 
ATOM   14514 C C     . LEU B 1 712  ? 14.495  27.946  73.741  1.00 12.06 ?  710  LEU B C     1 
ATOM   14515 O O     . LEU B 1 712  ? 13.981  28.512  72.773  1.00 12.65 ?  710  LEU B O     1 
ATOM   14516 C CB    . LEU B 1 712  ? 14.615  25.468  73.835  1.00 12.22 ?  710  LEU B CB    1 
ATOM   14517 C CG    . LEU B 1 712  ? 13.335  25.294  73.002  1.00 11.75 ?  710  LEU B CG    1 
ATOM   14518 C CD1   . LEU B 1 712  ? 13.645  25.054  71.536  1.00 12.89 ?  710  LEU B CD1   1 
ATOM   14519 C CD2   . LEU B 1 712  ? 12.516  24.140  73.589  1.00 14.94 ?  710  LEU B CD2   1 
ATOM   14520 N N     . ALA B 1 713  ? 14.297  28.372  74.986  1.00 11.07 ?  711  ALA B N     1 
ATOM   14521 C CA    . ALA B 1 713  ? 13.279  29.385  75.236  1.00 11.60 ?  711  ALA B CA    1 
ATOM   14522 C C     . ALA B 1 713  ? 13.697  30.752  74.711  1.00 11.18 ?  711  ALA B C     1 
ATOM   14523 O O     . ALA B 1 713  ? 12.916  31.414  74.023  1.00 11.80 ?  711  ALA B O     1 
ATOM   14524 C CB    . ALA B 1 713  ? 12.958  29.444  76.728  1.00 12.48 ?  711  ALA B CB    1 
ATOM   14525 N N     . ILE B 1 714  ? 14.902  31.215  75.051  1.00 12.68 ?  712  ILE B N     1 
ATOM   14526 C CA    . ILE B 1 714  ? 15.308  32.536  74.571  1.00 12.74 ?  712  ILE B CA    1 
ATOM   14527 C C     . ILE B 1 714  ? 15.651  32.470  73.091  1.00 12.20 ?  712  ILE B C     1 
ATOM   14528 O O     . ILE B 1 714  ? 15.353  33.398  72.325  1.00 13.04 ?  712  ILE B O     1 
ATOM   14529 C CB    . ILE B 1 714  ? 16.465  33.098  75.416  1.00 12.10 ?  712  ILE B CB    1 
ATOM   14530 C CG1   . ILE B 1 714  ? 15.929  33.423  76.810  1.00 12.46 ?  712  ILE B CG1   1 
ATOM   14531 C CG2   . ILE B 1 714  ? 17.013  34.369  74.785  1.00 14.37 ?  712  ILE B CG2   1 
ATOM   14532 C CD1   . ILE B 1 714  ? 16.941  34.004  77.757  1.00 17.12 ?  712  ILE B CD1   1 
ATOM   14533 N N     . PHE B 1 715  ? 16.239  31.353  72.657  1.00 11.49 ?  713  PHE B N     1 
ATOM   14534 C CA    . PHE B 1 715  ? 16.419  31.087  71.235  1.00 11.85 ?  713  PHE B CA    1 
ATOM   14535 C C     . PHE B 1 715  ? 15.109  31.282  70.472  1.00 10.91 ?  713  PHE B C     1 
ATOM   14536 O O     . PHE B 1 715  ? 15.041  32.060  69.509  1.00 11.82 ?  713  PHE B O     1 
ATOM   14537 C CB    . PHE B 1 715  ? 16.946  29.665  71.068  1.00 12.32 ?  713  PHE B CB    1 
ATOM   14538 C CG    . PHE B 1 715  ? 17.127  29.249  69.636  1.00 12.07 ?  713  PHE B CG    1 
ATOM   14539 C CD1   . PHE B 1 715  ? 18.269  29.600  68.939  1.00 13.16 ?  713  PHE B CD1   1 
ATOM   14540 C CD2   . PHE B 1 715  ? 16.146  28.510  68.993  1.00 12.46 ?  713  PHE B CD2   1 
ATOM   14541 C CE1   . PHE B 1 715  ? 18.433  29.211  67.613  1.00 15.37 ?  713  PHE B CE1   1 
ATOM   14542 C CE2   . PHE B 1 715  ? 16.296  28.120  67.672  1.00 13.80 ?  713  PHE B CE2   1 
ATOM   14543 C CZ    . PHE B 1 715  ? 17.445  28.469  66.981  1.00 13.89 ?  713  PHE B CZ    1 
ATOM   14544 N N     . THR B 1 716  ? 14.043  30.627  70.941  1.00 12.00 ?  714  THR B N     1 
ATOM   14545 C CA    . THR B 1 716  ? 12.748  30.680  70.266  1.00 12.00 ?  714  THR B CA    1 
ATOM   14546 C C     . THR B 1 716  ? 12.107  32.055  70.376  1.00 10.88 ?  714  THR B C     1 
ATOM   14547 O O     . THR B 1 716  ? 11.527  32.547  69.403  1.00 10.73 ?  714  THR B O     1 
ATOM   14548 C CB    . THR B 1 716  ? 11.809  29.619  70.849  1.00 11.87 ?  714  THR B CB    1 
ATOM   14549 O OG1   . THR B 1 716  ? 12.378  28.324  70.634  1.00 13.83 ?  714  THR B OG1   1 
ATOM   14550 C CG2   . THR B 1 716  ? 10.433  29.672  70.180  1.00 13.18 ?  714  THR B CG2   1 
ATOM   14551 N N     . GLY B 1 717  ? 12.170  32.677  71.556  1.00 10.11 ?  715  GLY B N     1 
ATOM   14552 C CA    . GLY B 1 717  ? 11.514  33.966  71.746  1.00 10.97 ?  715  GLY B CA    1 
ATOM   14553 C C     . GLY B 1 717  ? 12.041  35.033  70.801  1.00 10.34 ?  715  GLY B C     1 
ATOM   14554 O O     . GLY B 1 717  ? 11.266  35.736  70.145  1.00 11.33 ?  715  GLY B O     1 
ATOM   14555 N N     . GLN B 1 718  ? 13.368  35.166  70.714  1.00 10.28 ?  716  GLN B N     1 
ATOM   14556 C CA    . GLN B 1 718  ? 13.930  36.198  69.849  1.00 10.29 ?  716  GLN B CA    1 
ATOM   14557 C C     . GLN B 1 718  ? 13.557  35.928  68.400  1.00 11.19 ?  716  GLN B C     1 
ATOM   14558 O O     . GLN B 1 718  ? 13.101  36.824  67.684  1.00 11.07 ?  716  GLN B O     1 
ATOM   14559 C CB    . GLN B 1 718  ? 15.458  36.264  70.006  1.00 11.71 ?  716  GLN B CB    1 
ATOM   14560 C CG    . GLN B 1 718  ? 15.919  36.691  71.420  1.00 12.49 ?  716  GLN B CG    1 
ATOM   14561 C CD    . GLN B 1 718  ? 17.418  36.838  71.548  1.00 13.34 ?  716  GLN B CD    1 
ATOM   14562 O OE1   . GLN B 1 718  ? 17.891  37.745  72.243  1.00 13.58 ?  716  GLN B OE1   1 
ATOM   14563 N NE2   . GLN B 1 718  ? 18.176  35.946  70.904  1.00 12.27 ?  716  GLN B NE2   1 
ATOM   14564 N N     . ILE B 1 719  ? 13.727  34.679  67.966  1.00 10.16 ?  717  ILE B N     1 
ATOM   14565 C CA    . ILE B 1 719  ? 13.472  34.315  66.576  1.00 11.06 ?  717  ILE B CA    1 
ATOM   14566 C C     . ILE B 1 719  ? 12.005  34.496  66.232  1.00 10.36 ?  717  ILE B C     1 
ATOM   14567 O O     . ILE B 1 719  ? 11.667  35.033  65.167  1.00 10.90 ?  717  ILE B O     1 
ATOM   14568 C CB    . ILE B 1 719  ? 13.934  32.869  66.318  1.00 10.62 ?  717  ILE B CB    1 
ATOM   14569 C CG1   . ILE B 1 719  ? 15.454  32.816  66.361  1.00 11.19 ?  717  ILE B CG1   1 
ATOM   14570 C CG2   . ILE B 1 719  ? 13.355  32.343  65.005  1.00 15.66 ?  717  ILE B CG2   1 
ATOM   14571 C CD1   . ILE B 1 719  ? 15.971  31.417  66.404  1.00 18.33 ?  717  ILE B CD1   1 
ATOM   14572 N N     . ALA B 1 720  ? 11.115  34.031  67.112  1.00 11.04 ?  718  ALA B N     1 
ATOM   14573 C CA    . ALA B 1 720  ? 9.686   34.110  66.832  1.00 9.99  ?  718  ALA B CA    1 
ATOM   14574 C C     . ALA B 1 720  ? 9.231   35.555  66.693  1.00 10.41 ?  718  ALA B C     1 
ATOM   14575 O O     . ALA B 1 720  ? 8.451   35.886  65.793  1.00 11.11 ?  718  ALA B O     1 
ATOM   14576 C CB    . ALA B 1 720  ? 8.899   33.403  67.933  1.00 10.14 ?  718  ALA B CB    1 
ATOM   14577 N N     . ALA B 1 721  ? 9.705   36.432  67.574  1.00 10.34 ?  719  ALA B N     1 
ATOM   14578 C CA    . ALA B 1 721  ? 9.324   37.837  67.486  1.00 9.70  ?  719  ALA B CA    1 
ATOM   14579 C C     . ALA B 1 721  ? 9.819   38.466  66.191  1.00 10.83 ?  719  ALA B C     1 
ATOM   14580 O O     . ALA B 1 721  ? 9.060   39.141  65.484  1.00 10.58 ?  719  ALA B O     1 
ATOM   14581 C CB    . ALA B 1 721  ? 9.884   38.580  68.698  1.00 11.43 ?  719  ALA B CB    1 
ATOM   14582 N N     . ALA B 1 722  ? 11.085  38.228  65.847  1.00 10.07 ?  720  ALA B N     1 
ATOM   14583 C CA    . ALA B 1 722  ? 11.612  38.790  64.607  1.00 9.82  ?  720  ALA B CA    1 
ATOM   14584 C C     . ALA B 1 722  ? 10.839  38.279  63.391  1.00 10.32 ?  720  ALA B C     1 
ATOM   14585 O O     . ALA B 1 722  ? 10.462  39.064  62.513  1.00 10.79 ?  720  ALA B O     1 
ATOM   14586 C CB    . ALA B 1 722  ? 13.105  38.470  64.472  1.00 9.24  ?  720  ALA B CB    1 
ATOM   14587 N N     . LEU B 1 723  ? 10.579  36.966  63.337  1.00 10.43 ?  721  LEU B N     1 
ATOM   14588 C CA    . LEU B 1 723  ? 9.870   36.385  62.197  1.00 11.08 ?  721  LEU B CA    1 
ATOM   14589 C C     . LEU B 1 723  ? 8.469   36.949  62.072  1.00 11.10 ?  721  LEU B C     1 
ATOM   14590 O O     . LEU B 1 723  ? 8.023   37.309  60.971  1.00 11.27 ?  721  LEU B O     1 
ATOM   14591 C CB    . LEU B 1 723  ? 9.793   34.865  62.352  1.00 10.88 ?  721  LEU B CB    1 
ATOM   14592 C CG    . LEU B 1 723  ? 11.082  34.086  62.118  1.00 11.75 ?  721  LEU B CG    1 
ATOM   14593 C CD1   . LEU B 1 723  ? 10.821  32.660  62.539  1.00 12.72 ?  721  LEU B CD1   1 
ATOM   14594 C CD2   . LEU B 1 723  ? 11.483  34.186  60.651  1.00 11.97 ?  721  LEU B CD2   1 
ATOM   14595 N N     . VAL B 1 724  ? 7.734   36.989  63.183  1.00 9.98  ?  722  VAL B N     1 
ATOM   14596 C CA    . VAL B 1 724  ? 6.331   37.345  63.070  1.00 10.21 ?  722  VAL B CA    1 
ATOM   14597 C C     . VAL B 1 724  ? 6.171   38.827  62.770  1.00 10.79 ?  722  VAL B C     1 
ATOM   14598 O O     . VAL B 1 724  ? 5.165   39.234  62.168  1.00 10.67 ?  722  VAL B O     1 
ATOM   14599 C CB    . VAL B 1 724  ? 5.563   36.908  64.333  1.00 11.17 ?  722  VAL B CB    1 
ATOM   14600 C CG1   . VAL B 1 724  ? 5.736   37.901  65.506  1.00 10.83 ?  722  VAL B CG1   1 
ATOM   14601 C CG2   . VAL B 1 724  ? 4.106   36.685  64.004  1.00 10.25 ?  722  VAL B CG2   1 
ATOM   14602 N N     . ALA B 1 725  ? 7.163   39.643  63.133  1.00 10.92 ?  723  ALA B N     1 
ATOM   14603 C CA    . ALA B 1 725  ? 7.177   41.036  62.707  1.00 10.13 ?  723  ALA B CA    1 
ATOM   14604 C C     . ALA B 1 725  ? 7.533   41.194  61.238  1.00 13.26 ?  723  ALA B C     1 
ATOM   14605 O O     . ALA B 1 725  ? 7.560   42.329  60.760  1.00 14.96 ?  723  ALA B O     1 
ATOM   14606 C CB    . ALA B 1 725  ? 8.153   41.835  63.576  1.00 11.38 ?  723  ALA B CB    1 
ATOM   14607 N N     . GLY B 1 726  ? 7.795   40.102  60.520  1.00 11.02 ?  724  GLY B N     1 
ATOM   14608 C CA    . GLY B 1 726  ? 8.002   40.154  59.082  1.00 11.60 ?  724  GLY B CA    1 
ATOM   14609 C C     . GLY B 1 726  ? 9.446   40.166  58.636  1.00 13.44 ?  724  GLY B C     1 
ATOM   14610 O O     . GLY B 1 726  ? 9.710   40.485  57.470  1.00 13.66 ?  724  GLY B O     1 
ATOM   14611 N N     . ASN B 1 727  ? 10.386  39.826  59.517  1.00 11.78 ?  725  ASN B N     1 
ATOM   14612 C CA    . ASN B 1 727  ? 11.822  39.859  59.248  1.00 11.66 ?  725  ASN B CA    1 
ATOM   14613 C C     . ASN B 1 727  ? 12.366  38.457  59.047  1.00 12.06 ?  725  ASN B C     1 
ATOM   14614 O O     . ASN B 1 727  ? 12.077  37.578  59.867  1.00 12.96 ?  725  ASN B O     1 
ATOM   14615 C CB    . ASN B 1 727  ? 12.569  40.504  60.410  1.00 11.93 ?  725  ASN B CB    1 
ATOM   14616 C CG    . ASN B 1 727  ? 12.019  41.871  60.780  1.00 13.24 ?  725  ASN B CG    1 
ATOM   14617 O OD1   . ASN B 1 727  ? 12.278  42.864  60.089  1.00 12.97 ?  725  ASN B OD1   1 
ATOM   14618 N ND2   . ASN B 1 727  ? 11.267  41.937  61.883  1.00 13.07 ?  725  ASN B ND2   1 
ATOM   14619 N N     . PRO B 1 728  ? 13.163  38.197  58.015  1.00 11.84 ?  726  PRO B N     1 
ATOM   14620 C CA    . PRO B 1 728  ? 13.889  36.923  57.962  1.00 10.93 ?  726  PRO B CA    1 
ATOM   14621 C C     . PRO B 1 728  ? 15.004  36.944  58.992  1.00 13.19 ?  726  PRO B C     1 
ATOM   14622 O O     . PRO B 1 728  ? 15.502  38.011  59.360  1.00 12.79 ?  726  PRO B O     1 
ATOM   14623 C CB    . PRO B 1 728  ? 14.430  36.881  56.532  1.00 13.86 ?  726  PRO B CB    1 
ATOM   14624 C CG    . PRO B 1 728  ? 14.672  38.344  56.195  1.00 14.23 ?  726  PRO B CG    1 
ATOM   14625 C CD    . PRO B 1 728  ? 13.616  39.142  56.975  1.00 12.16 ?  726  PRO B CD    1 
ATOM   14626 N N     . VAL B 1 729  ? 15.365  35.758  59.486  1.00 10.24 ?  727  VAL B N     1 
ATOM   14627 C CA    . VAL B 1 729  ? 16.216  35.629  60.671  1.00 10.60 ?  727  VAL B CA    1 
ATOM   14628 C C     . VAL B 1 729  ? 17.458  34.796  60.379  1.00 12.62 ?  727  VAL B C     1 
ATOM   14629 O O     . VAL B 1 729  ? 17.391  33.744  59.733  1.00 12.74 ?  727  VAL B O     1 
ATOM   14630 C CB    . VAL B 1 729  ? 15.419  35.005  61.835  1.00 11.21 ?  727  VAL B CB    1 
ATOM   14631 C CG1   . VAL B 1 729  ? 16.361  34.546  62.962  1.00 12.68 ?  727  VAL B CG1   1 
ATOM   14632 C CG2   . VAL B 1 729  ? 14.434  35.989  62.362  1.00 12.10 ?  727  VAL B CG2   1 
ATOM   14633 N N     . LEU B 1 730  ? 18.601  35.269  60.878  1.00 10.96 ?  728  LEU B N     1 
ATOM   14634 C CA    . LEU B 1 730  ? 19.843  34.505  60.934  1.00 11.79 ?  728  LEU B CA    1 
ATOM   14635 C C     . LEU B 1 730  ? 20.030  34.128  62.391  1.00 13.11 ?  728  LEU B C     1 
ATOM   14636 O O     . LEU B 1 730  ? 20.284  35.004  63.225  1.00 13.25 ?  728  LEU B O     1 
ATOM   14637 C CB    . LEU B 1 730  ? 21.039  35.315  60.445  1.00 14.23 ?  728  LEU B CB    1 
ATOM   14638 C CG    . LEU B 1 730  ? 21.058  35.871  59.025  1.00 14.17 ?  728  LEU B CG    1 
ATOM   14639 C CD1   . LEU B 1 730  ? 20.652  34.773  58.042  1.00 15.38 ?  728  LEU B CD1   1 
ATOM   14640 C CD2   . LEU B 1 730  ? 20.167  37.096  58.866  1.00 15.84 ?  728  LEU B CD2   1 
ATOM   14641 N N     . ALA B 1 731  ? 19.873  32.848  62.710  1.00 11.50 ?  729  ALA B N     1 
ATOM   14642 C CA    . ALA B 1 731  ? 19.879  32.388  64.098  1.00 11.32 ?  729  ALA B CA    1 
ATOM   14643 C C     . ALA B 1 731  ? 21.262  31.840  64.438  1.00 13.64 ?  729  ALA B C     1 
ATOM   14644 O O     . ALA B 1 731  ? 21.691  30.837  63.868  1.00 14.09 ?  729  ALA B O     1 
ATOM   14645 C CB    . ALA B 1 731  ? 18.791  31.334  64.310  1.00 14.29 ?  729  ALA B CB    1 
ATOM   14646 N N     . LYS B 1 732  ? 21.968  32.517  65.351  1.00 12.88 ?  730  LYS B N     1 
ATOM   14647 C CA    . LYS B 1 732  ? 23.300  32.101  65.782  1.00 14.97 ?  730  LYS B CA    1 
ATOM   14648 C C     . LYS B 1 732  ? 23.207  31.622  67.223  1.00 13.39 ?  730  LYS B C     1 
ATOM   14649 O O     . LYS B 1 732  ? 23.200  32.444  68.154  1.00 15.15 ?  730  LYS B O     1 
ATOM   14650 C CB    . LYS B 1 732  ? 24.308  33.248  65.652  1.00 15.07 ?  730  LYS B CB    1 
ATOM   14651 C CG    . LYS B 1 732  ? 25.736  32.825  65.269  1.00 18.17 ?  730  LYS B CG    1 
ATOM   14652 C CD    . LYS B 1 732  ? 26.400  31.933  66.311  1.00 19.00 ?  730  LYS B CD    1 
ATOM   14653 C CE    . LYS B 1 732  ? 26.705  32.695  67.589  1.00 18.37 ?  730  LYS B CE    1 
ATOM   14654 N NZ    . LYS B 1 732  ? 27.360  31.798  68.585  1.00 20.49 ?  730  LYS B NZ    1 
ATOM   14655 N N     . PRO B 1 733  ? 23.116  30.320  67.455  1.00 11.98 ?  731  PRO B N     1 
ATOM   14656 C CA    . PRO B 1 733  ? 22.972  29.807  68.817  1.00 13.24 ?  731  PRO B CA    1 
ATOM   14657 C C     . PRO B 1 733  ? 24.307  29.804  69.531  1.00 12.20 ?  731  PRO B C     1 
ATOM   14658 O O     . PRO B 1 733  ? 25.378  29.879  68.924  1.00 14.59 ?  731  PRO B O     1 
ATOM   14659 C CB    . PRO B 1 733  ? 22.480  28.374  68.601  1.00 14.30 ?  731  PRO B CB    1 
ATOM   14660 C CG    . PRO B 1 733  ? 23.098  27.981  67.289  1.00 14.52 ?  731  PRO B CG    1 
ATOM   14661 C CD    . PRO B 1 733  ? 23.133  29.241  66.452  1.00 15.16 ?  731  PRO B CD    1 
ATOM   14662 N N     . ALA B 1 734  ? 24.222  29.716  70.855  1.00 13.32 ?  732  ALA B N     1 
ATOM   14663 C CA    . ALA B 1 734  ? 25.435  29.594  71.652  1.00 13.75 ?  732  ALA B CA    1 
ATOM   14664 C C     . ALA B 1 734  ? 26.269  28.403  71.197  1.00 15.58 ?  732  ALA B C     1 
ATOM   14665 O O     . ALA B 1 734  ? 25.741  27.349  70.819  1.00 14.96 ?  732  ALA B O     1 
ATOM   14666 C CB    . ALA B 1 734  ? 25.085  29.435  73.133  1.00 13.74 ?  732  ALA B CB    1 
ATOM   14667 N N     . GLU B 1 735  ? 27.593  28.582  71.227  1.00 14.21 ?  733  GLU B N     1 
ATOM   14668 C CA    . GLU B 1 735  ? 28.508  27.510  70.849  1.00 14.64 ?  733  GLU B CA    1 
ATOM   14669 C C     . GLU B 1 735  ? 28.249  26.232  71.644  1.00 15.37 ?  733  GLU B C     1 
ATOM   14670 O O     . GLU B 1 735  ? 28.394  25.123  71.120  1.00 15.18 ?  733  GLU B O     1 
ATOM   14671 C CB    . GLU B 1 735  ? 29.950  27.992  71.040  1.00 17.49 ?  733  GLU B CB    1 
ATOM   14672 C CG    . GLU B 1 735  ? 31.002  27.023  70.593  1.00 24.67 ?  733  GLU B CG    1 
ATOM   14673 C CD    . GLU B 1 735  ? 32.395  27.617  70.658  1.00 27.96 ?  733  GLU B CD    1 
ATOM   14674 O OE1   . GLU B 1 735  ? 32.532  28.770  71.127  1.00 27.87 ?  733  GLU B OE1   1 
ATOM   14675 O OE2   . GLU B 1 735  ? 33.341  26.928  70.221  1.00 34.36 ?  733  GLU B OE2   1 
ATOM   14676 N N     . GLU B 1 736  ? 27.854  26.370  72.911  1.00 15.63 ?  734  GLU B N     1 
ATOM   14677 C CA    . GLU B 1 736  ? 27.688  25.221  73.787  1.00 14.55 ?  734  GLU B CA    1 
ATOM   14678 C C     . GLU B 1 736  ? 26.431  24.396  73.502  1.00 15.45 ?  734  GLU B C     1 
ATOM   14679 O O     . GLU B 1 736  ? 26.386  23.213  73.858  1.00 17.72 ?  734  GLU B O     1 
ATOM   14680 C CB    . GLU B 1 736  ? 27.660  25.709  75.242  1.00 15.64 ?  734  GLU B CB    1 
ATOM   14681 C CG    . GLU B 1 736  ? 28.957  26.404  75.691  1.00 19.90 ?  734  GLU B CG    1 
ATOM   14682 C CD    . GLU B 1 736  ? 28.983  27.925  75.445  1.00 20.95 ?  734  GLU B CD    1 
ATOM   14683 O OE1   . GLU B 1 736  ? 28.138  28.475  74.698  1.00 18.25 ?  734  GLU B OE1   1 
ATOM   14684 O OE2   . GLU B 1 736  ? 29.880  28.582  76.029  1.00 25.06 ?  734  GLU B OE2   1 
ATOM   14685 N N     . THR B 1 737  ? 25.396  24.983  72.906  1.00 15.55 ?  735  THR B N     1 
ATOM   14686 C CA    . THR B 1 737  ? 24.077  24.347  72.838  1.00 15.31 ?  735  THR B CA    1 
ATOM   14687 C C     . THR B 1 737  ? 23.477  24.431  71.436  1.00 14.29 ?  735  THR B C     1 
ATOM   14688 O O     . THR B 1 737  ? 22.356  24.909  71.251  1.00 15.24 ?  735  THR B O     1 
ATOM   14689 C CB    . THR B 1 737  ? 23.131  24.977  73.864  1.00 13.03 ?  735  THR B CB    1 
ATOM   14690 O OG1   . THR B 1 737  ? 23.081  26.404  73.689  1.00 14.26 ?  735  THR B OG1   1 
ATOM   14691 C CG2   . THR B 1 737  ? 23.577  24.661  75.281  1.00 13.87 ?  735  THR B CG2   1 
ATOM   14692 N N     . PRO B 1 738  ? 24.175  23.928  70.421  1.00 14.60 ?  736  PRO B N     1 
ATOM   14693 C CA    . PRO B 1 738  ? 23.628  24.033  69.062  1.00 13.74 ?  736  PRO B CA    1 
ATOM   14694 C C     . PRO B 1 738  ? 22.545  23.019  68.749  1.00 13.39 ?  736  PRO B C     1 
ATOM   14695 O O     . PRO B 1 738  ? 21.765  23.256  67.814  1.00 13.39 ?  736  PRO B O     1 
ATOM   14696 C CB    . PRO B 1 738  ? 24.852  23.786  68.184  1.00 15.01 ?  736  PRO B CB    1 
ATOM   14697 C CG    . PRO B 1 738  ? 25.652  22.806  69.002  1.00 15.33 ?  736  PRO B CG    1 
ATOM   14698 C CD    . PRO B 1 738  ? 25.522  23.329  70.416  1.00 13.59 ?  736  PRO B CD    1 
ATOM   14699 N N     . LEU B 1 739  ? 22.488  21.891  69.464  1.00 13.69 ?  737  LEU B N     1 
ATOM   14700 C CA    . LEU B 1 739  ? 21.603  20.819  69.020  1.00 12.94 ?  737  LEU B CA    1 
ATOM   14701 C C     . LEU B 1 739  ? 20.149  21.178  69.269  1.00 12.10 ?  737  LEU B C     1 
ATOM   14702 O O     . LEU B 1 739  ? 19.292  20.961  68.400  1.00 12.67 ?  737  LEU B O     1 
ATOM   14703 C CB    . LEU B 1 739  ? 21.956  19.506  69.718  1.00 13.51 ?  737  LEU B CB    1 
ATOM   14704 C CG    . LEU B 1 739  ? 23.405  19.061  69.555  1.00 14.01 ?  737  LEU B CG    1 
ATOM   14705 C CD1   . LEU B 1 739  ? 23.674  17.854  70.450  1.00 15.35 ?  737  LEU B CD1   1 
ATOM   14706 C CD2   . LEU B 1 739  ? 23.702  18.715  68.092  1.00 16.03 ?  737  LEU B CD2   1 
ATOM   14707 N N     . ILE B 1 740  ? 19.843  21.737  70.441  1.00 13.19 ?  738  ILE B N     1 
ATOM   14708 C CA    . ILE B 1 740  ? 18.459  22.113  70.690  1.00 12.82 ?  738  ILE B CA    1 
ATOM   14709 C C     . ILE B 1 740  ? 18.045  23.263  69.775  1.00 12.68 ?  738  ILE B C     1 
ATOM   14710 O O     . ILE B 1 740  ? 16.882  23.345  69.361  1.00 12.95 ?  738  ILE B O     1 
ATOM   14711 C CB    . ILE B 1 740  ? 18.255  22.449  72.182  1.00 14.26 ?  738  ILE B CB    1 
ATOM   14712 C CG1   . ILE B 1 740  ? 16.771  22.707  72.483  1.00 14.61 ?  738  ILE B CG1   1 
ATOM   14713 C CG2   . ILE B 1 740  ? 19.069  23.671  72.575  1.00 15.76 ?  738  ILE B CG2   1 
ATOM   14714 C CD1   . ILE B 1 740  ? 15.878  21.503  72.235  1.00 16.26 ?  738  ILE B CD1   1 
ATOM   14715 N N     . ALA B 1 741  ? 18.976  24.163  69.441  1.00 13.47 ?  739  ALA B N     1 
ATOM   14716 C CA    . ALA B 1 741  ? 18.676  25.213  68.468  1.00 14.45 ?  739  ALA B CA    1 
ATOM   14717 C C     . ALA B 1 741  ? 18.314  24.616  67.115  1.00 12.54 ?  739  ALA B C     1 
ATOM   14718 O O     . ALA B 1 741  ? 17.350  25.059  66.466  1.00 12.50 ?  739  ALA B O     1 
ATOM   14719 C CB    . ALA B 1 741  ? 19.869  26.156  68.325  1.00 15.79 ?  739  ALA B CB    1 
ATOM   14720 N N     . ALA B 1 742  ? 19.109  23.638  66.649  1.00 11.89 ?  740  ALA B N     1 
ATOM   14721 C CA    . ALA B 1 742  ? 18.805  22.986  65.380  1.00 11.81 ?  740  ALA B CA    1 
ATOM   14722 C C     . ALA B 1 742  ? 17.413  22.368  65.408  1.00 13.13 ?  740  ALA B C     1 
ATOM   14723 O O     . ALA B 1 742  ? 16.681  22.427  64.415  1.00 12.96 ?  740  ALA B O     1 
ATOM   14724 C CB    . ALA B 1 742  ? 19.857  21.926  65.051  1.00 12.54 ?  740  ALA B CB    1 
ATOM   14725 N N     . GLU B 1 743  ? 17.026  21.787  66.546  1.00 12.86 ?  741  GLU B N     1 
ATOM   14726 C CA    . GLU B 1 743  ? 15.702  21.183  66.656  1.00 13.31 ?  741  GLU B CA    1 
ATOM   14727 C C     . GLU B 1 743  ? 14.610  22.246  66.636  1.00 12.67 ?  741  GLU B C     1 
ATOM   14728 O O     . GLU B 1 743  ? 13.552  22.047  66.014  1.00 12.84 ?  741  GLU B O     1 
ATOM   14729 C CB    . GLU B 1 743  ? 15.640  20.338  67.930  1.00 15.22 ?  741  GLU B CB    1 
ATOM   14730 C CG    . GLU B 1 743  ? 14.301  19.670  68.182  1.00 14.34 ?  741  GLU B CG    1 
ATOM   14731 C CD    . GLU B 1 743  ? 13.941  18.584  67.177  1.00 17.58 ?  741  GLU B CD    1 
ATOM   14732 O OE1   . GLU B 1 743  ? 14.788  18.176  66.343  1.00 16.66 ?  741  GLU B OE1   1 
ATOM   14733 O OE2   . GLU B 1 743  ? 12.772  18.133  67.211  1.00 20.57 ?  741  GLU B OE2   1 
ATOM   14734 N N     . GLY B 1 744  ? 14.857  23.390  67.278  1.00 12.13 ?  742  GLY B N     1 
ATOM   14735 C CA    . GLY B 1 744  ? 13.918  24.497  67.191  1.00 12.59 ?  742  GLY B CA    1 
ATOM   14736 C C     . GLY B 1 744  ? 13.716  24.974  65.764  1.00 10.84 ?  742  GLY B C     1 
ATOM   14737 O O     . GLY B 1 744  ? 12.594  25.271  65.354  1.00 12.44 ?  742  GLY B O     1 
ATOM   14738 N N     . VAL B 1 745  ? 14.800  25.063  64.993  1.00 11.12 ?  743  VAL B N     1 
ATOM   14739 C CA    . VAL B 1 745  ? 14.661  25.464  63.593  1.00 11.59 ?  743  VAL B CA    1 
ATOM   14740 C C     . VAL B 1 745  ? 13.899  24.408  62.797  1.00 12.45 ?  743  VAL B C     1 
ATOM   14741 O O     . VAL B 1 745  ? 13.066  24.748  61.943  1.00 13.72 ?  743  VAL B O     1 
ATOM   14742 C CB    . VAL B 1 745  ? 16.043  25.756  62.983  1.00 12.55 ?  743  VAL B CB    1 
ATOM   14743 C CG1   . VAL B 1 745  ? 15.942  25.889  61.459  1.00 12.04 ?  743  VAL B CG1   1 
ATOM   14744 C CG2   . VAL B 1 745  ? 16.604  27.031  63.576  1.00 14.07 ?  743  VAL B CG2   1 
ATOM   14745 N N     . ARG B 1 746  ? 14.164  23.116  63.049  1.00 10.97 ?  744  ARG B N     1 
ATOM   14746 C CA    . ARG B 1 746  ? 13.391  22.074  62.373  1.00 12.37 ?  744  ARG B CA    1 
ATOM   14747 C C     . ARG B 1 746  ? 11.899  22.268  62.610  1.00 11.63 ?  744  ARG B C     1 
ATOM   14748 O O     . ARG B 1 746  ? 11.089  22.124  61.687  1.00 13.05 ?  744  ARG B O     1 
ATOM   14749 C CB    . ARG B 1 746  ? 13.790  20.678  62.865  1.00 13.62 ?  744  ARG B CB    1 
ATOM   14750 C CG    . ARG B 1 746  ? 15.178  20.219  62.478  1.00 13.90 ?  744  ARG B CG    1 
ATOM   14751 C CD    . ARG B 1 746  ? 15.383  18.809  63.023  1.00 14.46 ?  744  ARG B CD    1 
ATOM   14752 N NE    . ARG B 1 746  ? 16.768  18.420  62.847  1.00 15.83 ?  744  ARG B NE    1 
ATOM   14753 C CZ    . ARG B 1 746  ? 17.688  18.457  63.799  1.00 12.90 ?  744  ARG B CZ    1 
ATOM   14754 N NH1   . ARG B 1 746  ? 17.361  18.636  65.077  1.00 13.90 ?  744  ARG B NH1   1 
ATOM   14755 N NH2   . ARG B 1 746  ? 18.966  18.348  63.457  1.00 16.87 ?  744  ARG B NH2   1 
ATOM   14756 N N     . ILE B 1 747  ? 11.523  22.583  63.850  1.00 10.66 ?  745  ILE B N     1 
ATOM   14757 C CA    . ILE B 1 747  ? 10.111  22.694  64.200  1.00 10.43 ?  745  ILE B CA    1 
ATOM   14758 C C     . ILE B 1 747  ? 9.496   23.933  63.568  1.00 11.47 ?  745  ILE B C     1 
ATOM   14759 O O     . ILE B 1 747  ? 8.385   23.878  63.018  1.00 11.65 ?  745  ILE B O     1 
ATOM   14760 C CB    . ILE B 1 747  ? 9.954   22.677  65.728  1.00 10.60 ?  745  ILE B CB    1 
ATOM   14761 C CG1   . ILE B 1 747  ? 10.118  21.231  66.214  1.00 11.39 ?  745  ILE B CG1   1 
ATOM   14762 C CG2   . ILE B 1 747  ? 8.598   23.245  66.130  1.00 12.61 ?  745  ILE B CG2   1 
ATOM   14763 C CD1   . ILE B 1 747  ? 10.295  21.100  67.721  1.00 14.27 ?  745  ILE B CD1   1 
ATOM   14764 N N     . LEU B 1 748  ? 10.215  25.056  63.597  1.00 11.50 ?  746  LEU B N     1 
ATOM   14765 C CA    . LEU B 1 748  ? 9.681   26.263  62.972  1.00 12.02 ?  746  LEU B CA    1 
ATOM   14766 C C     . LEU B 1 748  ? 9.541   26.094  61.464  1.00 10.97 ?  746  LEU B C     1 
ATOM   14767 O O     . LEU B 1 748  ? 8.558   26.556  60.878  1.00 11.10 ?  746  LEU B O     1 
ATOM   14768 C CB    . LEU B 1 748  ? 10.557  27.471  63.309  1.00 12.26 ?  746  LEU B CB    1 
ATOM   14769 C CG    . LEU B 1 748  ? 10.268  28.093  64.677  1.00 14.75 ?  746  LEU B CG    1 
ATOM   14770 C CD1   . LEU B 1 748  ? 11.493  28.916  65.134  1.00 14.92 ?  746  LEU B CD1   1 
ATOM   14771 C CD2   . LEU B 1 748  ? 9.030   28.937  64.609  1.00 15.39 ?  746  LEU B CD2   1 
ATOM   14772 N N     . ARG B 1 749  ? 10.497  25.409  60.818  1.00 10.91 ?  747  ARG B N     1 
ATOM   14773 C CA    . ARG B 1 749  ? 10.350  25.163  59.387  1.00 10.85 ?  747  ARG B CA    1 
ATOM   14774 C C     . ARG B 1 749  ? 9.186   24.225  59.111  1.00 10.98 ?  747  ARG B C     1 
ATOM   14775 O O     . ARG B 1 749  ? 8.413   24.453  58.170  1.00 12.69 ?  747  ARG B O     1 
ATOM   14776 C CB    . ARG B 1 749  ? 11.656  24.616  58.818  1.00 13.01 ?  747  ARG B CB    1 
ATOM   14777 C CG    . ARG B 1 749  ? 12.718  25.695  58.645  1.00 15.05 ?  747  ARG B CG    1 
ATOM   14778 C CD    . ARG B 1 749  ? 13.887  25.165  57.835  1.00 17.69 ?  747  ARG B CD    1 
ATOM   14779 N NE    . ARG B 1 749  ? 14.963  26.138  57.714  1.00 15.13 ?  747  ARG B NE    1 
ATOM   14780 C CZ    . ARG B 1 749  ? 16.015  25.940  56.935  1.00 20.62 ?  747  ARG B CZ    1 
ATOM   14781 N NH1   . ARG B 1 749  ? 16.122  24.846  56.198  1.00 20.02 ?  747  ARG B NH1   1 
ATOM   14782 N NH2   . ARG B 1 749  ? 16.979  26.855  56.896  1.00 21.15 ?  747  ARG B NH2   1 
ATOM   14783 N N     . GLU B 1 750  ? 9.028   23.182  59.933  1.00 11.39 ?  748  GLU B N     1 
ATOM   14784 C CA    . GLU B 1 750  ? 7.913   22.260  59.745  1.00 12.96 ?  748  GLU B CA    1 
ATOM   14785 C C     . GLU B 1 750  ? 6.584   22.988  59.871  1.00 11.45 ?  748  GLU B C     1 
ATOM   14786 O O     . GLU B 1 750  ? 5.614   22.654  59.174  1.00 13.36 ?  748  GLU B O     1 
ATOM   14787 C CB    . GLU B 1 750  ? 7.998   21.132  60.778  1.00 13.40 ?  748  GLU B CB    1 
ATOM   14788 C CG    . GLU B 1 750  ? 6.922   20.089  60.611  1.00 15.00 ?  748  GLU B CG    1 
ATOM   14789 C CD    . GLU B 1 750  ? 7.131   18.882  61.501  1.00 16.47 ?  748  GLU B CD    1 
ATOM   14790 O OE1   . GLU B 1 750  ? 8.213   18.758  62.107  1.00 18.71 ?  748  GLU B OE1   1 
ATOM   14791 O OE2   . GLU B 1 750  ? 6.192   18.067  61.602  1.00 23.83 ?  748  GLU B OE2   1 
ATOM   14792 N N     . ALA B 1 751  ? 6.548   24.014  60.718  1.00 11.62 ?  749  ALA B N     1 
ATOM   14793 C CA    . ALA B 1 751  ? 5.357   24.800  60.996  1.00 10.34 ?  749  ALA B CA    1 
ATOM   14794 C C     . ALA B 1 751  ? 5.039   25.815  59.912  1.00 11.54 ?  749  ALA B C     1 
ATOM   14795 O O     . ALA B 1 751  ? 3.992   26.469  59.982  1.00 14.40 ?  749  ALA B O     1 
ATOM   14796 C CB    . ALA B 1 751  ? 5.524   25.534  62.319  1.00 12.18 ?  749  ALA B CB    1 
ATOM   14797 N N     . GLY B 1 752  ? 5.910   25.985  58.922  1.00 11.31 ?  750  GLY B N     1 
ATOM   14798 C CA    . GLY B 1 752  ? 5.623   26.884  57.821  1.00 13.52 ?  750  GLY B CA    1 
ATOM   14799 C C     . GLY B 1 752  ? 6.626   27.993  57.613  1.00 12.35 ?  750  GLY B C     1 
ATOM   14800 O O     . GLY B 1 752  ? 6.484   28.744  56.639  1.00 14.42 ?  750  GLY B O     1 
ATOM   14801 N N     . ILE B 1 753  ? 7.630   28.171  58.466  1.00 11.99 ?  751  ILE B N     1 
ATOM   14802 C CA    . ILE B 1 753  ? 8.611   29.220  58.203  1.00 12.72 ?  751  ILE B CA    1 
ATOM   14803 C C     . ILE B 1 753  ? 9.513   28.778  57.056  1.00 13.85 ?  751  ILE B C     1 
ATOM   14804 O O     . ILE B 1 753  ? 10.170  27.735  57.149  1.00 15.13 ?  751  ILE B O     1 
ATOM   14805 C CB    . ILE B 1 753  ? 9.445   29.539  59.447  1.00 10.38 ?  751  ILE B CB    1 
ATOM   14806 C CG1   . ILE B 1 753  ? 8.555   29.875  60.659  1.00 11.83 ?  751  ILE B CG1   1 
ATOM   14807 C CG2   . ILE B 1 753  ? 10.407  30.670  59.117  1.00 12.98 ?  751  ILE B CG2   1 
ATOM   14808 C CD1   . ILE B 1 753  ? 7.692   31.145  60.507  1.00 13.76 ?  751  ILE B CD1   1 
ATOM   14809 N N     . PRO B 1 754  ? 9.573   29.535  55.958  1.00 14.52 ?  752  PRO B N     1 
ATOM   14810 C CA    . PRO B 1 754  ? 10.406  29.134  54.820  1.00 17.27 ?  752  PRO B CA    1 
ATOM   14811 C C     . PRO B 1 754  ? 11.885  29.078  55.171  1.00 16.69 ?  752  PRO B C     1 
ATOM   14812 O O     . PRO B 1 754  ? 12.381  29.824  56.023  1.00 14.63 ?  752  PRO B O     1 
ATOM   14813 C CB    . PRO B 1 754  ? 10.129  30.222  53.775  1.00 18.29 ?  752  PRO B CB    1 
ATOM   14814 C CG    . PRO B 1 754  ? 8.862   30.897  54.215  1.00 19.29 ?  752  PRO B CG    1 
ATOM   14815 C CD    . PRO B 1 754  ? 8.812   30.770  55.706  1.00 13.97 ?  752  PRO B CD    1 
ATOM   14816 N N     . ALA B 1 755  ? 12.599  28.187  54.478  1.00 17.67 ?  753  ALA B N     1 
ATOM   14817 C CA    . ALA B 1 755  ? 14.027  28.039  54.733  1.00 16.26 ?  753  ALA B CA    1 
ATOM   14818 C C     . ALA B 1 755  ? 14.762  29.360  54.547  1.00 16.24 ?  753  ALA B C     1 
ATOM   14819 O O     . ALA B 1 755  ? 15.674  29.684  55.313  1.00 17.59 ?  753  ALA B O     1 
ATOM   14820 C CB    . ALA B 1 755  ? 14.619  26.963  53.824  1.00 21.39 ?  753  ALA B CB    1 
ATOM   14821 N N     . SER B 1 756  ? 14.352  30.162  53.564  1.00 15.26 ?  754  SER B N     1 
ATOM   14822 C CA    . SER B 1 756  ? 15.011  31.442  53.358  1.00 16.44 ?  754  SER B CA    1 
ATOM   14823 C C     . SER B 1 756  ? 14.702  32.447  54.455  1.00 15.69 ?  754  SER B C     1 
ATOM   14824 O O     . SER B 1 756  ? 15.435  33.432  54.598  1.00 16.01 ?  754  SER B O     1 
ATOM   14825 C CB    . SER B 1 756  ? 14.615  32.019  52.009  1.00 19.18 ?  754  SER B CB    1 
ATOM   14826 O OG    . SER B 1 756  ? 13.223  32.235  51.960  1.00 21.22 ?  754  SER B OG    1 
ATOM   14827 N N     . ALA B 1 757  ? 13.626  32.241  55.216  1.00 12.78 ?  755  ALA B N     1 
ATOM   14828 C CA    . ALA B 1 757  ? 13.290  33.137  56.310  1.00 11.77 ?  755  ALA B CA    1 
ATOM   14829 C C     . ALA B 1 757  ? 13.928  32.741  57.632  1.00 11.19 ?  755  ALA B C     1 
ATOM   14830 O O     . ALA B 1 757  ? 13.928  33.556  58.559  1.00 12.97 ?  755  ALA B O     1 
ATOM   14831 C CB    . ALA B 1 757  ? 11.761  33.234  56.461  1.00 12.63 ?  755  ALA B CB    1 
ATOM   14832 N N     . LEU B 1 758  ? 14.488  31.532  57.748  1.00 10.79 ?  756  LEU B N     1 
ATOM   14833 C CA    . LEU B 1 758  ? 15.079  31.093  59.014  1.00 11.99 ?  756  LEU B CA    1 
ATOM   14834 C C     . LEU B 1 758  ? 16.269  30.199  58.700  1.00 13.41 ?  756  LEU B C     1 
ATOM   14835 O O     . LEU B 1 758  ? 16.104  29.029  58.346  1.00 12.30 ?  756  LEU B O     1 
ATOM   14836 C CB    . LEU B 1 758  ? 14.069  30.373  59.891  1.00 11.87 ?  756  LEU B CB    1 
ATOM   14837 C CG    . LEU B 1 758  ? 14.624  29.853  61.232  1.00 11.06 ?  756  LEU B CG    1 
ATOM   14838 C CD1   . LEU B 1 758  ? 15.269  30.979  62.069  1.00 13.53 ?  756  LEU B CD1   1 
ATOM   14839 C CD2   . LEU B 1 758  ? 13.503  29.175  62.033  1.00 13.56 ?  756  LEU B CD2   1 
ATOM   14840 N N     . GLN B 1 759  ? 17.460  30.751  58.874  1.00 12.95 ?  757  GLN B N     1 
ATOM   14841 C CA    . GLN B 1 759  ? 18.708  30.040  58.656  1.00 11.55 ?  757  GLN B CA    1 
ATOM   14842 C C     . GLN B 1 759  ? 19.428  29.880  59.988  1.00 11.87 ?  757  GLN B C     1 
ATOM   14843 O O     . GLN B 1 759  ? 19.422  30.796  60.815  1.00 13.95 ?  757  GLN B O     1 
ATOM   14844 C CB    . GLN B 1 759  ? 19.566  30.801  57.652  1.00 12.94 ?  757  GLN B CB    1 
ATOM   14845 C CG    . GLN B 1 759  ? 18.930  30.854  56.256  1.00 14.16 ?  757  GLN B CG    1 
ATOM   14846 C CD    . GLN B 1 759  ? 19.720  31.706  55.302  1.00 12.28 ?  757  GLN B CD    1 
ATOM   14847 O OE1   . GLN B 1 759  ? 20.546  31.207  54.538  1.00 14.96 ?  757  GLN B OE1   1 
ATOM   14848 N NE2   . GLN B 1 759  ? 19.481  33.006  55.344  1.00 14.16 ?  757  GLN B NE2   1 
ATOM   14849 N N     . LEU B 1 760  ? 20.021  28.705  60.207  1.00 12.61 ?  758  LEU B N     1 
ATOM   14850 C CA    . LEU B 1 760  ? 20.762  28.401  61.429  1.00 13.03 ?  758  LEU B CA    1 
ATOM   14851 C C     . LEU B 1 760  ? 22.262  28.432  61.145  1.00 13.81 ?  758  LEU B C     1 
ATOM   14852 O O     . LEU B 1 760  ? 22.737  27.762  60.225  1.00 13.22 ?  758  LEU B O     1 
ATOM   14853 C CB    . LEU B 1 760  ? 20.375  27.027  61.979  1.00 14.09 ?  758  LEU B CB    1 
ATOM   14854 C CG    . LEU B 1 760  ? 21.089  26.662  63.285  1.00 13.02 ?  758  LEU B CG    1 
ATOM   14855 C CD1   . LEU B 1 760  ? 20.398  27.356  64.464  1.00 15.24 ?  758  LEU B CD1   1 
ATOM   14856 C CD2   . LEU B 1 760  ? 21.157  25.145  63.501  1.00 15.99 ?  758  LEU B CD2   1 
ATOM   14857 N N     . LEU B 1 761  ? 23.014  29.180  61.961  1.00 12.37 ?  759  LEU B N     1 
ATOM   14858 C CA    . LEU B 1 761  ? 24.459  29.329  61.778  1.00 13.23 ?  759  LEU B CA    1 
ATOM   14859 C C     . LEU B 1 761  ? 25.158  28.973  63.082  1.00 13.46 ?  759  LEU B C     1 
ATOM   14860 O O     . LEU B 1 761  ? 25.459  29.858  63.889  1.00 15.21 ?  759  LEU B O     1 
ATOM   14861 C CB    . LEU B 1 761  ? 24.828  30.755  61.361  1.00 15.66 ?  759  LEU B CB    1 
ATOM   14862 C CG    . LEU B 1 761  ? 24.332  31.326  60.019  1.00 15.35 ?  759  LEU B CG    1 
ATOM   14863 C CD1   . LEU B 1 761  ? 24.404  30.316  58.869  1.00 16.12 ?  759  LEU B CD1   1 
ATOM   14864 C CD2   . LEU B 1 761  ? 22.932  31.870  60.154  1.00 17.34 ?  759  LEU B CD2   1 
ATOM   14865 N N     . PRO B 1 762  ? 25.413  27.694  63.333  1.00 13.80 ?  760  PRO B N     1 
ATOM   14866 C CA    . PRO B 1 762  ? 26.125  27.328  64.564  1.00 15.82 ?  760  PRO B CA    1 
ATOM   14867 C C     . PRO B 1 762  ? 27.555  27.823  64.516  1.00 16.36 ?  760  PRO B C     1 
ATOM   14868 O O     . PRO B 1 762  ? 28.159  27.952  63.446  1.00 16.64 ?  760  PRO B O     1 
ATOM   14869 C CB    . PRO B 1 762  ? 26.077  25.794  64.580  1.00 13.64 ?  760  PRO B CB    1 
ATOM   14870 C CG    . PRO B 1 762  ? 25.043  25.413  63.537  1.00 14.32 ?  760  PRO B CG    1 
ATOM   14871 C CD    . PRO B 1 762  ? 25.031  26.519  62.534  1.00 14.51 ?  760  PRO B CD    1 
ATOM   14872 N N     . GLY B 1 763  ? 28.105  28.091  65.694  1.00 15.14 ?  761  GLY B N     1 
ATOM   14873 C CA    . GLY B 1 763  ? 29.514  28.410  65.799  1.00 17.82 ?  761  GLY B CA    1 
ATOM   14874 C C     . GLY B 1 763  ? 29.776  29.360  66.952  1.00 15.99 ?  761  GLY B C     1 
ATOM   14875 O O     . GLY B 1 763  ? 28.924  29.580  67.812  1.00 19.13 ?  761  GLY B O     1 
ATOM   14876 N N     . ASP B 1 764  ? 30.985  29.929  66.938  1.00 22.78 ?  762  ASP B N     1 
ATOM   14877 C CA    . ASP B 1 764  ? 31.462  30.738  68.051  1.00 23.70 ?  762  ASP B CA    1 
ATOM   14878 C C     . ASP B 1 764  ? 31.144  32.214  67.814  1.00 28.41 ?  762  ASP B C     1 
ATOM   14879 O O     . ASP B 1 764  ? 30.350  32.575  66.939  1.00 21.51 ?  762  ASP B O     1 
ATOM   14880 C CB    . ASP B 1 764  ? 32.956  30.496  68.296  1.00 26.22 ?  762  ASP B CB    1 
ATOM   14881 C CG    . ASP B 1 764  ? 33.848  30.891  67.110  1.00 29.23 ?  762  ASP B CG    1 
ATOM   14882 O OD1   . ASP B 1 764  ? 33.428  31.690  66.247  1.00 27.83 ?  762  ASP B OD1   1 
ATOM   14883 O OD2   . ASP B 1 764  ? 34.997  30.387  67.042  1.00 35.40 ?  762  ASP B OD2   1 
ATOM   14884 N N     . GLY B 1 765  ? 31.770  33.091  68.603  1.00 23.76 ?  763  GLY B N     1 
ATOM   14885 C CA    . GLY B 1 765  ? 31.479  34.510  68.501  1.00 23.40 ?  763  GLY B CA    1 
ATOM   14886 C C     . GLY B 1 765  ? 31.969  35.155  67.223  1.00 22.17 ?  763  GLY B C     1 
ATOM   14887 O O     . GLY B 1 765  ? 31.481  36.231  66.864  1.00 24.70 ?  763  GLY B O     1 
ATOM   14888 N N     . ARG B 1 766  ? 32.937  34.539  66.536  1.00 23.43 ?  764  ARG B N     1 
ATOM   14889 C CA    . ARG B 1 766  ? 33.345  35.057  65.234  1.00 24.12 ?  764  ARG B CA    1 
ATOM   14890 C C     . ARG B 1 766  ? 32.231  34.897  64.202  1.00 20.52 ?  764  ARG B C     1 
ATOM   14891 O O     . ARG B 1 766  ? 32.083  35.745  63.313  1.00 22.97 ?  764  ARG B O     1 
ATOM   14892 C CB    . ARG B 1 766  ? 34.621  34.361  64.762  1.00 29.86 ?  764  ARG B CB    1 
ATOM   14893 C CG    . ARG B 1 766  ? 35.736  34.377  65.798  1.00 32.10 ?  764  ARG B CG    1 
ATOM   14894 C CD    . ARG B 1 766  ? 36.987  33.693  65.280  1.00 42.30 ?  764  ARG B CD    1 
ATOM   14895 N NE    . ARG B 1 766  ? 37.710  34.526  64.326  1.00 54.55 ?  764  ARG B NE    1 
ATOM   14896 C CZ    . ARG B 1 766  ? 38.803  35.222  64.615  1.00 57.67 ?  764  ARG B CZ    1 
ATOM   14897 N NH1   . ARG B 1 766  ? 39.337  35.200  65.826  1.00 58.60 ?  764  ARG B NH1   1 
ATOM   14898 N NH2   . ARG B 1 766  ? 39.379  35.952  63.663  1.00 59.56 ?  764  ARG B NH2   1 
ATOM   14899 N N     . VAL B 1 767  ? 31.450  33.820  64.302  1.00 20.83 ?  765  VAL B N     1 
ATOM   14900 C CA    . VAL B 1 767  ? 30.268  33.679  63.453  1.00 19.74 ?  765  VAL B CA    1 
ATOM   14901 C C     . VAL B 1 767  ? 29.269  34.783  63.768  1.00 17.67 ?  765  VAL B C     1 
ATOM   14902 O O     . VAL B 1 767  ? 28.735  35.445  62.869  1.00 19.41 ?  765  VAL B O     1 
ATOM   14903 C CB    . VAL B 1 767  ? 29.636  32.285  63.626  1.00 17.05 ?  765  VAL B CB    1 
ATOM   14904 C CG1   . VAL B 1 767  ? 28.417  32.148  62.713  1.00 17.54 ?  765  VAL B CG1   1 
ATOM   14905 C CG2   . VAL B 1 767  ? 30.642  31.196  63.314  1.00 19.65 ?  765  VAL B CG2   1 
ATOM   14906 N N     . GLY B 1 768  ? 28.999  34.999  65.057  1.00 17.94 ?  766  GLY B N     1 
ATOM   14907 C CA    . GLY B 1 768  ? 28.113  36.083  65.441  1.00 19.47 ?  766  GLY B CA    1 
ATOM   14908 C C     . GLY B 1 768  ? 28.593  37.432  64.935  1.00 18.35 ?  766  GLY B C     1 
ATOM   14909 O O     . GLY B 1 768  ? 27.801  38.239  64.442  1.00 17.50 ?  766  GLY B O     1 
ATOM   14910 N N     . ALA B 1 769  ? 29.897  37.695  65.047  1.00 21.24 ?  767  ALA B N     1 
ATOM   14911 C CA    . ALA B 1 769  ? 30.417  38.989  64.620  1.00 19.33 ?  767  ALA B CA    1 
ATOM   14912 C C     . ALA B 1 769  ? 30.296  39.170  63.111  1.00 20.48 ?  767  ALA B C     1 
ATOM   14913 O O     . ALA B 1 769  ? 29.988  40.272  62.638  1.00 21.36 ?  767  ALA B O     1 
ATOM   14914 C CB    . ALA B 1 769  ? 31.868  39.147  65.073  1.00 22.16 ?  767  ALA B CB    1 
ATOM   14915 N N     . ALA B 1 770  ? 30.517  38.100  62.342  1.00 19.19 ?  768  ALA B N     1 
ATOM   14916 C CA    . ALA B 1 770  ? 30.375  38.195  60.894  1.00 18.77 ?  768  ALA B CA    1 
ATOM   14917 C C     . ALA B 1 770  ? 28.930  38.477  60.499  1.00 19.26 ?  768  ALA B C     1 
ATOM   14918 O O     . ALA B 1 770  ? 28.668  39.204  59.530  1.00 20.61 ?  768  ALA B O     1 
ATOM   14919 C CB    . ALA B 1 770  ? 30.876  36.910  60.236  1.00 21.73 ?  768  ALA B CB    1 
ATOM   14920 N N     . LEU B 1 771  ? 27.973  37.901  61.226  1.00 17.78 ?  769  LEU B N     1 
ATOM   14921 C CA    . LEU B 1 771  ? 26.579  38.207  60.934  1.00 18.18 ?  769  LEU B CA    1 
ATOM   14922 C C     . LEU B 1 771  ? 26.258  39.662  61.264  1.00 17.59 ?  769  LEU B C     1 
ATOM   14923 O O     . LEU B 1 771  ? 25.593  40.348  60.483  1.00 18.33 ?  769  LEU B O     1 
ATOM   14924 C CB    . LEU B 1 771  ? 25.658  37.258  61.706  1.00 15.09 ?  769  LEU B CB    1 
ATOM   14925 C CG    . LEU B 1 771  ? 25.729  35.776  61.319  1.00 15.43 ?  769  LEU B CG    1 
ATOM   14926 C CD1   . LEU B 1 771  ? 25.005  34.893  62.330  1.00 16.67 ?  769  LEU B CD1   1 
ATOM   14927 C CD2   . LEU B 1 771  ? 25.179  35.554  59.906  1.00 16.55 ?  769  LEU B CD2   1 
ATOM   14928 N N     . VAL B 1 772  ? 26.717  40.144  62.424  1.00 15.82 ?  770  VAL B N     1 
ATOM   14929 C CA    . VAL B 1 772  ? 26.410  41.506  62.854  1.00 16.47 ?  770  VAL B CA    1 
ATOM   14930 C C     . VAL B 1 772  ? 26.986  42.527  61.879  1.00 19.85 ?  770  VAL B C     1 
ATOM   14931 O O     . VAL B 1 772  ? 26.347  43.543  61.571  1.00 20.80 ?  770  VAL B O     1 
ATOM   14932 C CB    . VAL B 1 772  ? 26.931  41.728  64.283  1.00 16.57 ?  770  VAL B CB    1 
ATOM   14933 C CG1   . VAL B 1 772  ? 26.932  43.212  64.640  1.00 17.37 ?  770  VAL B CG1   1 
ATOM   14934 C CG2   . VAL B 1 772  ? 26.087  40.932  65.263  1.00 14.57 ?  770  VAL B CG2   1 
ATOM   14935 N N     . ALA B 1 773  ? 28.192  42.266  61.367  1.00 19.27 ?  771  ALA B N     1 
ATOM   14936 C CA    . ALA B 1 773  ? 28.874  43.217  60.497  1.00 19.51 ?  771  ALA B CA    1 
ATOM   14937 C C     . ALA B 1 773  ? 28.372  43.200  59.054  1.00 23.66 ?  771  ALA B C     1 
ATOM   14938 O O     . ALA B 1 773  ? 28.697  44.124  58.299  1.00 23.83 ?  771  ALA B O     1 
ATOM   14939 C CB    . ALA B 1 773  ? 30.378  42.943  60.523  1.00 20.28 ?  771  ALA B CB    1 
ATOM   14940 N N     . ALA B 1 774  ? 27.598  42.191  58.657  1.00 18.75 ?  772  ALA B N     1 
ATOM   14941 C CA    . ALA B 1 774  ? 27.155  42.066  57.271  1.00 19.49 ?  772  ALA B CA    1 
ATOM   14942 C C     . ALA B 1 774  ? 26.310  43.261  56.839  1.00 19.93 ?  772  ALA B C     1 
ATOM   14943 O O     . ALA B 1 774  ? 25.495  43.791  57.604  1.00 23.21 ?  772  ALA B O     1 
ATOM   14944 C CB    . ALA B 1 774  ? 26.365  40.769  57.086  1.00 22.19 ?  772  ALA B CB    1 
ATOM   14945 N N     . ALA B 1 775  ? 26.496  43.667  55.576  1.00 25.53 ?  773  ALA B N     1 
ATOM   14946 C CA    . ALA B 1 775  ? 25.913  44.915  55.092  1.00 21.50 ?  773  ALA B CA    1 
ATOM   14947 C C     . ALA B 1 775  ? 24.393  44.918  55.151  1.00 20.50 ?  773  ALA B C     1 
ATOM   14948 O O     . ALA B 1 775  ? 23.789  45.965  55.391  1.00 25.12 ?  773  ALA B O     1 
ATOM   14949 C CB    . ALA B 1 775  ? 26.376  45.181  53.658  1.00 31.64 ?  773  ALA B CB    1 
ATOM   14950 N N     . GLU B 1 776  ? 23.756  43.771  54.938  1.00 20.50 ?  774  GLU B N     1 
ATOM   14951 C CA    . GLU B 1 776  ? 22.307  43.720  54.862  1.00 18.47 ?  774  GLU B CA    1 
ATOM   14952 C C     . GLU B 1 776  ? 21.638  43.514  56.216  1.00 17.94 ?  774  GLU B C     1 
ATOM   14953 O O     . GLU B 1 776  ? 20.407  43.531  56.285  1.00 18.25 ?  774  GLU B O     1 
ATOM   14954 C CB    . GLU B 1 776  ? 21.868  42.614  53.899  1.00 20.31 ?  774  GLU B CB    1 
ATOM   14955 C CG    . GLU B 1 776  ? 22.423  42.748  52.488  1.00 24.73 ?  774  GLU B CG    1 
ATOM   14956 C CD    . GLU B 1 776  ? 23.756  42.018  52.298  1.00 29.42 ?  774  GLU B CD    1 
ATOM   14957 O OE1   . GLU B 1 776  ? 24.334  41.507  53.291  1.00 25.92 ?  774  GLU B OE1   1 
ATOM   14958 O OE2   . GLU B 1 776  ? 24.235  41.955  51.143  1.00 32.47 ?  774  GLU B OE2   1 
ATOM   14959 N N     . THR B 1 777  ? 22.403  43.325  57.287  1.00 17.20 ?  775  THR B N     1 
ATOM   14960 C CA    . THR B 1 777  ? 21.801  43.145  58.603  1.00 15.06 ?  775  THR B CA    1 
ATOM   14961 C C     . THR B 1 777  ? 21.078  44.415  59.039  1.00 16.35 ?  775  THR B C     1 
ATOM   14962 O O     . THR B 1 777  ? 21.650  45.512  59.005  1.00 17.79 ?  775  THR B O     1 
ATOM   14963 C CB    . THR B 1 777  ? 22.880  42.758  59.606  1.00 16.07 ?  775  THR B CB    1 
ATOM   14964 O OG1   . THR B 1 777  ? 23.362  41.446  59.280  1.00 19.22 ?  775  THR B OG1   1 
ATOM   14965 C CG2   . THR B 1 777  ? 22.332  42.762  61.025  1.00 15.55 ?  775  THR B CG2   1 
ATOM   14966 N N     . ALA B 1 778  ? 19.806  44.261  59.434  1.00 13.46 ?  776  ALA B N     1 
ATOM   14967 C CA    . ALA B 1 778  ? 18.914  45.378  59.715  1.00 14.66 ?  776  ALA B CA    1 
ATOM   14968 C C     . ALA B 1 778  ? 18.518  45.446  61.184  1.00 14.38 ?  776  ALA B C     1 
ATOM   14969 O O     . ALA B 1 778  ? 17.791  46.367  61.590  1.00 14.76 ?  776  ALA B O     1 
ATOM   14970 C CB    . ALA B 1 778  ? 17.651  45.277  58.845  1.00 14.61 ?  776  ALA B CB    1 
ATOM   14971 N N     . GLY B 1 779  ? 18.991  44.511  61.995  1.00 13.61 ?  777  GLY B N     1 
ATOM   14972 C CA    . GLY B 1 779  ? 18.686  44.522  63.414  1.00 14.23 ?  777  GLY B CA    1 
ATOM   14973 C C     . GLY B 1 779  ? 19.370  43.343  64.069  1.00 13.53 ?  777  GLY B C     1 
ATOM   14974 O O     . GLY B 1 779  ? 19.699  42.345  63.419  1.00 13.28 ?  777  GLY B O     1 
ATOM   14975 N N     . VAL B 1 780  ? 19.600  43.485  65.371  1.00 11.20 ?  778  VAL B N     1 
ATOM   14976 C CA    . VAL B 1 780  ? 20.269  42.449  66.156  1.00 12.00 ?  778  VAL B CA    1 
ATOM   14977 C C     . VAL B 1 780  ? 19.516  42.261  67.462  1.00 12.66 ?  778  VAL B C     1 
ATOM   14978 O O     . VAL B 1 780  ? 19.161  43.235  68.137  1.00 12.86 ?  778  VAL B O     1 
ATOM   14979 C CB    . VAL B 1 780  ? 21.750  42.778  66.435  1.00 12.85 ?  778  VAL B CB    1 
ATOM   14980 C CG1   . VAL B 1 780  ? 22.379  41.680  67.262  1.00 14.00 ?  778  VAL B CG1   1 
ATOM   14981 C CG2   . VAL B 1 780  ? 22.541  42.963  65.128  1.00 12.59 ?  778  VAL B CG2   1 
ATOM   14982 N N     . MET B 1 781  ? 19.250  41.005  67.804  1.00 11.93 ?  779  MET B N     1 
ATOM   14983 C CA    . MET B 1 781  ? 18.672  40.626  69.087  1.00 12.52 ?  779  MET B CA    1 
ATOM   14984 C C     . MET B 1 781  ? 19.705  39.763  69.780  1.00 12.21 ?  779  MET B C     1 
ATOM   14985 O O     . MET B 1 781  ? 20.098  38.714  69.251  1.00 13.09 ?  779  MET B O     1 
ATOM   14986 C CB    . MET B 1 781  ? 17.355  39.878  68.892  1.00 12.01 ?  779  MET B CB    1 
ATOM   14987 C CG    . MET B 1 781  ? 16.373  40.677  68.073  1.00 13.21 ?  779  MET B CG    1 
ATOM   14988 S SD    . MET B 1 781  ? 14.889  39.726  67.707  1.00 13.60 ?  779  MET B SD    1 
ATOM   14989 C CE    . MET B 1 781  ? 14.003  39.913  69.240  1.00 12.91 ?  779  MET B CE    1 
ATOM   14990 N N     . PHE B 1 782  ? 20.197  40.232  70.928  1.00 13.19 ?  780  PHE B N     1 
ATOM   14991 C CA    . PHE B 1 782  ? 21.317  39.608  71.606  1.00 11.40 ?  780  PHE B CA    1 
ATOM   14992 C C     . PHE B 1 782  ? 20.998  39.412  73.077  1.00 13.08 ?  780  PHE B C     1 
ATOM   14993 O O     . PHE B 1 782  ? 20.549  40.347  73.747  1.00 15.69 ?  780  PHE B O     1 
ATOM   14994 C CB    . PHE B 1 782  ? 22.579  40.467  71.483  1.00 13.42 ?  780  PHE B CB    1 
ATOM   14995 C CG    . PHE B 1 782  ? 23.728  39.976  72.329  1.00 14.74 ?  780  PHE B CG    1 
ATOM   14996 C CD1   . PHE B 1 782  ? 24.528  38.930  71.890  1.00 15.43 ?  780  PHE B CD1   1 
ATOM   14997 C CD2   . PHE B 1 782  ? 24.003  40.563  73.556  1.00 16.94 ?  780  PHE B CD2   1 
ATOM   14998 C CE1   . PHE B 1 782  ? 25.580  38.466  72.647  1.00 18.83 ?  780  PHE B CE1   1 
ATOM   14999 C CE2   . PHE B 1 782  ? 25.067  40.112  74.323  1.00 16.96 ?  780  PHE B CE2   1 
ATOM   15000 C CZ    . PHE B 1 782  ? 25.858  39.060  73.869  1.00 18.28 ?  780  PHE B CZ    1 
ATOM   15001 N N     . THR B 1 783  ? 21.205  38.201  73.569  1.00 12.51 ?  781  THR B N     1 
ATOM   15002 C CA    . THR B 1 783  ? 21.144  37.925  74.999  1.00 13.74 ?  781  THR B CA    1 
ATOM   15003 C C     . THR B 1 783  ? 22.468  37.298  75.404  1.00 15.76 ?  781  THR B C     1 
ATOM   15004 O O     . THR B 1 783  ? 22.842  36.240  74.886  1.00 16.84 ?  781  THR B O     1 
ATOM   15005 C CB    . THR B 1 783  ? 19.952  37.015  75.332  1.00 13.63 ?  781  THR B CB    1 
ATOM   15006 O OG1   . THR B 1 783  ? 18.739  37.642  74.886  1.00 15.51 ?  781  THR B OG1   1 
ATOM   15007 C CG2   . THR B 1 783  ? 19.860  36.792  76.830  1.00 16.70 ?  781  THR B CG2   1 
ATOM   15008 N N     . GLY B 1 784  ? 23.197  37.975  76.293  1.00 13.85 ?  782  GLY B N     1 
ATOM   15009 C CA    . GLY B 1 784  ? 24.530  37.519  76.662  1.00 16.61 ?  782  GLY B CA    1 
ATOM   15010 C C     . GLY B 1 784  ? 25.252  38.562  77.497  1.00 16.13 ?  782  GLY B C     1 
ATOM   15011 O O     . GLY B 1 784  ? 24.622  39.372  78.177  1.00 17.11 ?  782  GLY B O     1 
ATOM   15012 N N     . SER B 1 785  ? 26.580  38.534  77.422  1.00 18.57 ?  783  SER B N     1 
ATOM   15013 C CA    . SER B 1 785  ? 27.389  39.372  78.307  1.00 19.80 ?  783  SER B CA    1 
ATOM   15014 C C     . SER B 1 785  ? 27.374  40.842  77.890  1.00 22.11 ?  783  SER B C     1 
ATOM   15015 O O     . SER B 1 785  ? 27.192  41.184  76.719  1.00 18.90 ?  783  SER B O     1 
ATOM   15016 C CB    . SER B 1 785  ? 28.834  38.881  78.337  1.00 20.33 ?  783  SER B CB    1 
ATOM   15017 O OG    . SER B 1 785  ? 29.486  39.118  77.101  1.00 21.81 ?  783  SER B OG    1 
ATOM   15018 N N     . THR B 1 786  ? 27.603  41.725  78.867  1.00 19.73 ?  784  THR B N     1 
ATOM   15019 C CA    A THR B 1 786  ? 27.693  43.153  78.562  0.72 19.78 ?  784  THR B CA    1 
ATOM   15020 C CA    B THR B 1 786  ? 27.687  43.149  78.557  0.28 19.80 ?  784  THR B CA    1 
ATOM   15021 C C     . THR B 1 786  ? 28.867  43.448  77.637  1.00 19.50 ?  784  THR B C     1 
ATOM   15022 O O     . THR B 1 786  ? 28.773  44.313  76.755  1.00 21.63 ?  784  THR B O     1 
ATOM   15023 C CB    A THR B 1 786  ? 27.828  43.977  79.851  0.72 21.46 ?  784  THR B CB    1 
ATOM   15024 C CB    B THR B 1 786  ? 27.788  43.961  79.850  0.28 21.45 ?  784  THR B CB    1 
ATOM   15025 O OG1   A THR B 1 786  ? 29.074  43.671  80.491  0.72 27.37 ?  784  THR B OG1   1 
ATOM   15026 O OG1   B THR B 1 786  ? 28.301  45.267  79.557  0.28 20.43 ?  784  THR B OG1   1 
ATOM   15027 C CG2   A THR B 1 786  ? 26.689  43.702  80.799  0.72 18.43 ?  784  THR B CG2   1 
ATOM   15028 C CG2   B THR B 1 786  ? 28.701  43.265  80.849  0.28 25.30 ?  784  THR B CG2   1 
ATOM   15029 N N     . GLU B 1 787  ? 29.992  42.743  77.824  1.00 19.19 ?  785  GLU B N     1 
ATOM   15030 C CA    . GLU B 1 787  ? 31.163  42.990  76.990  1.00 21.52 ?  785  GLU B CA    1 
ATOM   15031 C C     . GLU B 1 787  ? 30.853  42.725  75.521  1.00 19.84 ?  785  GLU B C     1 
ATOM   15032 O O     . GLU B 1 787  ? 31.185  43.538  74.651  1.00 22.38 ?  785  GLU B O     1 
ATOM   15033 C CB    . GLU B 1 787  ? 32.338  42.130  77.459  1.00 23.71 ?  785  GLU B CB    1 
ATOM   15034 N N     . VAL B 1 788  ? 30.199  41.594  75.224  1.00 21.07 ?  786  VAL B N     1 
ATOM   15035 C CA    . VAL B 1 788  ? 29.900  41.283  73.830  1.00 19.66 ?  786  VAL B CA    1 
ATOM   15036 C C     . VAL B 1 788  ? 28.834  42.228  73.297  1.00 16.68 ?  786  VAL B C     1 
ATOM   15037 O O     . VAL B 1 788  ? 28.919  42.694  72.159  1.00 19.31 ?  786  VAL B O     1 
ATOM   15038 C CB    . VAL B 1 788  ? 29.491  39.805  73.676  1.00 19.95 ?  786  VAL B CB    1 
ATOM   15039 C CG1   . VAL B 1 788  ? 29.002  39.533  72.263  1.00 17.88 ?  786  VAL B CG1   1 
ATOM   15040 C CG2   . VAL B 1 788  ? 30.690  38.905  73.992  1.00 26.07 ?  786  VAL B CG2   1 
ATOM   15041 N N     . ALA B 1 789  ? 27.831  42.551  74.119  1.00 17.48 ?  787  ALA B N     1 
ATOM   15042 C CA    . ALA B 1 789  ? 26.810  43.500  73.685  1.00 17.51 ?  787  ALA B CA    1 
ATOM   15043 C C     . ALA B 1 789  ? 27.431  44.837  73.299  1.00 16.46 ?  787  ALA B C     1 
ATOM   15044 O O     . ALA B 1 789  ? 27.025  45.459  72.306  1.00 16.67 ?  787  ALA B O     1 
ATOM   15045 C CB    . ALA B 1 789  ? 25.772  43.689  74.786  1.00 16.00 ?  787  ALA B CB    1 
ATOM   15046 N N     . ARG B 1 790  ? 28.422  45.297  74.076  1.00 18.40 ?  788  ARG B N     1 
ATOM   15047 C CA    . ARG B 1 790  ? 29.102  46.545  73.743  1.00 18.11 ?  788  ARG B CA    1 
ATOM   15048 C C     . ARG B 1 790  ? 29.835  46.441  72.410  1.00 19.34 ?  788  ARG B C     1 
ATOM   15049 O O     . ARG B 1 790  ? 29.839  47.392  71.622  1.00 20.16 ?  788  ARG B O     1 
ATOM   15050 C CB    . ARG B 1 790  ? 30.074  46.926  74.868  1.00 23.41 ?  788  ARG B CB    1 
ATOM   15051 C CG    . ARG B 1 790  ? 30.592  48.356  74.821  1.00 31.68 ?  788  ARG B CG    1 
ATOM   15052 C CD    . ARG B 1 790  ? 31.340  48.709  76.111  1.00 30.51 ?  788  ARG B CD    1 
ATOM   15053 N NE    . ARG B 1 790  ? 30.539  48.398  77.288  1.00 30.65 ?  788  ARG B NE    1 
ATOM   15054 C CZ    . ARG B 1 790  ? 29.598  49.190  77.786  1.00 37.12 ?  788  ARG B CZ    1 
ATOM   15055 N NH1   . ARG B 1 790  ? 29.325  50.368  77.242  1.00 34.11 ?  788  ARG B NH1   1 
ATOM   15056 N NH2   . ARG B 1 790  ? 28.909  48.787  78.853  1.00 38.23 ?  788  ARG B NH2   1 
ATOM   15057 N N     . LEU B 1 791  ? 30.469  45.298  72.139  1.00 18.59 ?  789  LEU B N     1 
ATOM   15058 C CA    . LEU B 1 791  ? 31.150  45.131  70.858  1.00 18.45 ?  789  LEU B CA    1 
ATOM   15059 C C     . LEU B 1 791  ? 30.159  45.157  69.703  1.00 17.99 ?  789  LEU B C     1 
ATOM   15060 O O     . LEU B 1 791  ? 30.424  45.753  68.655  1.00 19.44 ?  789  LEU B O     1 
ATOM   15061 C CB    . LEU B 1 791  ? 31.947  43.828  70.852  1.00 20.72 ?  789  LEU B CB    1 
ATOM   15062 C CG    . LEU B 1 791  ? 33.102  43.770  71.852  1.00 24.60 ?  789  LEU B CG    1 
ATOM   15063 C CD1   . LEU B 1 791  ? 33.750  42.402  71.791  1.00 26.54 ?  789  LEU B CD1   1 
ATOM   15064 C CD2   . LEU B 1 791  ? 34.120  44.868  71.573  1.00 27.36 ?  789  LEU B CD2   1 
ATOM   15065 N N     . ILE B 1 792  ? 29.003  44.528  69.888  1.00 17.58 ?  790  ILE B N     1 
ATOM   15066 C CA    . ILE B 1 792  ? 27.967  44.534  68.860  1.00 16.79 ?  790  ILE B CA    1 
ATOM   15067 C C     . ILE B 1 792  ? 27.470  45.953  68.612  1.00 17.74 ?  790  ILE B C     1 
ATOM   15068 O O     . ILE B 1 792  ? 27.305  46.385  67.462  1.00 18.61 ?  790  ILE B O     1 
ATOM   15069 C CB    . ILE B 1 792  ? 26.820  43.602  69.284  1.00 14.88 ?  790  ILE B CB    1 
ATOM   15070 C CG1   . ILE B 1 792  ? 27.315  42.154  69.261  1.00 15.09 ?  790  ILE B CG1   1 
ATOM   15071 C CG2   . ILE B 1 792  ? 25.601  43.792  68.391  1.00 15.06 ?  790  ILE B CG2   1 
ATOM   15072 C CD1   . ILE B 1 792  ? 26.307  41.150  69.762  1.00 17.67 ?  790  ILE B CD1   1 
ATOM   15073 N N     . GLN B 1 793  ? 27.194  46.685  69.693  1.00 17.46 ?  791  GLN B N     1 
ATOM   15074 C CA    . GLN B 1 793  ? 26.741  48.068  69.581  1.00 16.16 ?  791  GLN B CA    1 
ATOM   15075 C C     . GLN B 1 793  ? 27.728  48.920  68.781  1.00 17.21 ?  791  GLN B C     1 
ATOM   15076 O O     . GLN B 1 793  ? 27.319  49.722  67.930  1.00 17.99 ?  791  GLN B O     1 
ATOM   15077 C CB    . GLN B 1 793  ? 26.545  48.638  70.984  1.00 19.00 ?  791  GLN B CB    1 
ATOM   15078 C CG    . GLN B 1 793  ? 25.947  50.036  71.067  1.00 22.26 ?  791  GLN B CG    1 
ATOM   15079 C CD    . GLN B 1 793  ? 26.282  50.714  72.390  1.00 30.84 ?  791  GLN B CD    1 
ATOM   15080 O OE1   . GLN B 1 793  ? 27.353  50.484  72.973  1.00 33.82 ?  791  GLN B OE1   1 
ATOM   15081 N NE2   . GLN B 1 793  ? 25.364  51.544  72.879  1.00 33.28 ?  791  GLN B NE2   1 
ATOM   15082 N N     . ALA B 1 794  ? 29.029  48.755  69.032  1.00 19.25 ?  792  ALA B N     1 
ATOM   15083 C CA    . ALA B 1 794  ? 30.024  49.539  68.303  1.00 20.54 ?  792  ALA B CA    1 
ATOM   15084 C C     . ALA B 1 794  ? 30.040  49.171  66.823  1.00 20.18 ?  792  ALA B C     1 
ATOM   15085 O O     . ALA B 1 794  ? 30.167  50.049  65.958  1.00 22.91 ?  792  ALA B O     1 
ATOM   15086 C CB    . ALA B 1 794  ? 31.411  49.349  68.922  1.00 24.19 ?  792  ALA B CB    1 
ATOM   15087 N N     . GLN B 1 795  ? 29.900  47.881  66.507  1.00 20.05 ?  793  GLN B N     1 
ATOM   15088 C CA    . GLN B 1 795  ? 29.877  47.485  65.103  1.00 20.05 ?  793  GLN B CA    1 
ATOM   15089 C C     . GLN B 1 795  ? 28.661  48.068  64.395  1.00 17.05 ?  793  GLN B C     1 
ATOM   15090 O O     . GLN B 1 795  ? 28.772  48.572  63.268  1.00 19.44 ?  793  GLN B O     1 
ATOM   15091 C CB    . GLN B 1 795  ? 29.902  45.957  64.986  1.00 23.19 ?  793  GLN B CB    1 
ATOM   15092 C CG    . GLN B 1 795  ? 29.903  45.429  63.548  1.00 28.36 ?  793  GLN B CG    1 
ATOM   15093 C CD    . GLN B 1 795  ? 31.091  45.898  62.726  1.00 35.00 ?  793  GLN B CD    1 
ATOM   15094 O OE1   . GLN B 1 795  ? 32.239  45.581  63.035  1.00 35.38 ?  793  GLN B OE1   1 
ATOM   15095 N NE2   . GLN B 1 795  ? 30.816  46.649  61.662  1.00 33.98 ?  793  GLN B NE2   1 
ATOM   15096 N N     . LEU B 1 796  ? 27.493  48.020  65.043  1.00 16.57 ?  794  LEU B N     1 
ATOM   15097 C CA    . LEU B 1 796  ? 26.272  48.506  64.408  1.00 16.41 ?  794  LEU B CA    1 
ATOM   15098 C C     . LEU B 1 796  ? 26.308  50.013  64.195  1.00 18.68 ?  794  LEU B C     1 
ATOM   15099 O O     . LEU B 1 796  ? 25.737  50.518  63.223  1.00 20.16 ?  794  LEU B O     1 
ATOM   15100 C CB    . LEU B 1 796  ? 25.055  48.139  65.252  1.00 16.30 ?  794  LEU B CB    1 
ATOM   15101 C CG    . LEU B 1 796  ? 24.644  46.667  65.311  1.00 15.77 ?  794  LEU B CG    1 
ATOM   15102 C CD1   . LEU B 1 796  ? 23.401  46.484  66.154  1.00 16.11 ?  794  LEU B CD1   1 
ATOM   15103 C CD2   . LEU B 1 796  ? 24.431  46.116  63.910  1.00 16.16 ?  794  LEU B CD2   1 
ATOM   15104 N N     . ALA B 1 797  ? 26.965  50.745  65.095  1.00 20.27 ?  795  ALA B N     1 
ATOM   15105 C CA    . ALA B 1 797  ? 26.984  52.194  64.977  1.00 23.03 ?  795  ALA B CA    1 
ATOM   15106 C C     . ALA B 1 797  ? 27.803  52.672  63.787  1.00 23.93 ?  795  ALA B C     1 
ATOM   15107 O O     . ALA B 1 797  ? 27.708  53.846  63.424  1.00 27.30 ?  795  ALA B O     1 
ATOM   15108 C CB    . ALA B 1 797  ? 27.519  52.818  66.264  1.00 24.95 ?  795  ALA B CB    1 
ATOM   15109 N N     . ASP B 1 798  ? 28.596  51.804  63.168  1.00 21.13 ?  796  ASP B N     1 
ATOM   15110 C CA    . ASP B 1 798  ? 29.312  52.225  61.978  1.00 26.75 ?  796  ASP B CA    1 
ATOM   15111 C C     . ASP B 1 798  ? 28.428  52.290  60.742  1.00 25.47 ?  796  ASP B C     1 
ATOM   15112 O O     . ASP B 1 798  ? 28.853  52.862  59.730  1.00 28.43 ?  796  ASP B O     1 
ATOM   15113 C CB    . ASP B 1 798  ? 30.480  51.288  61.713  1.00 23.39 ?  796  ASP B CB    1 
ATOM   15114 C CG    . ASP B 1 798  ? 31.542  51.938  60.865  1.00 33.18 ?  796  ASP B CG    1 
ATOM   15115 O OD1   . ASP B 1 798  ? 32.013  53.030  61.254  1.00 35.53 ?  796  ASP B OD1   1 
ATOM   15116 O OD2   . ASP B 1 798  ? 31.891  51.368  59.813  1.00 33.84 ?  796  ASP B OD2   1 
ATOM   15117 N N     . ARG B 1 799  ? 27.221  51.734  60.805  1.00 24.37 ?  797  ARG B N     1 
ATOM   15118 C CA    . ARG B 1 799  ? 26.327  51.613  59.663  1.00 25.39 ?  797  ARG B CA    1 
ATOM   15119 C C     . ARG B 1 799  ? 25.003  52.303  59.968  1.00 21.88 ?  797  ARG B C     1 
ATOM   15120 O O     . ARG B 1 799  ? 24.706  52.655  61.113  1.00 21.02 ?  797  ARG B O     1 
ATOM   15121 C CB    . ARG B 1 799  ? 26.070  50.137  59.304  1.00 28.24 ?  797  ARG B CB    1 
ATOM   15122 C CG    . ARG B 1 799  ? 27.325  49.296  59.054  1.00 33.04 ?  797  ARG B CG    1 
ATOM   15123 C CD    . ARG B 1 799  ? 26.998  47.887  58.521  1.00 36.15 ?  797  ARG B CD    1 
ATOM   15124 N NE    . ARG B 1 799  ? 26.370  47.012  59.510  1.00 36.00 ?  797  ARG B NE    1 
ATOM   15125 C CZ    . ARG B 1 799  ? 25.118  46.570  59.449  1.00 35.52 ?  797  ARG B CZ    1 
ATOM   15126 N NH1   . ARG B 1 799  ? 24.314  46.896  58.449  1.00 28.52 ?  797  ARG B NH1   1 
ATOM   15127 N NH2   . ARG B 1 799  ? 24.660  45.776  60.415  1.00 28.67 ?  797  ARG B NH2   1 
ATOM   15128 N N     . LEU B 1 800  ? 24.207  52.490  58.916  1.00 21.96 ?  798  LEU B N     1 
ATOM   15129 C CA    . LEU B 1 800  ? 22.828  52.952  59.022  1.00 21.11 ?  798  LEU B CA    1 
ATOM   15130 C C     . LEU B 1 800  ? 21.924  52.021  58.226  1.00 21.81 ?  798  LEU B C     1 
ATOM   15131 O O     . LEU B 1 800  ? 22.369  51.328  57.308  1.00 23.78 ?  798  LEU B O     1 
ATOM   15132 C CB    . LEU B 1 800  ? 22.657  54.389  58.502  1.00 24.96 ?  798  LEU B CB    1 
ATOM   15133 C CG    . LEU B 1 800  ? 23.279  55.518  59.319  1.00 24.83 ?  798  LEU B CG    1 
ATOM   15134 C CD1   . LEU B 1 800  ? 23.198  56.831  58.533  1.00 26.23 ?  798  LEU B CD1   1 
ATOM   15135 C CD2   . LEU B 1 800  ? 22.615  55.631  60.685  1.00 23.42 ?  798  LEU B CD2   1 
ATOM   15136 N N     . SER B 1 801  ? 20.642  52.016  58.600  1.00 22.36 ?  799  SER B N     1 
ATOM   15137 C CA    . SER B 1 801  ? 19.618  51.256  57.907  1.00 24.55 ?  799  SER B CA    1 
ATOM   15138 C C     . SER B 1 801  ? 19.406  51.814  56.507  1.00 27.20 ?  799  SER B C     1 
ATOM   15139 O O     . SER B 1 801  ? 19.864  52.914  56.189  1.00 26.33 ?  799  SER B O     1 
ATOM   15140 C CB    . SER B 1 801  ? 18.310  51.318  58.691  1.00 23.98 ?  799  SER B CB    1 
ATOM   15141 O OG    . SER B 1 801  ? 17.695  52.586  58.512  1.00 26.18 ?  799  SER B OG    1 
ATOM   15142 N N     . PRO B 1 802  ? 18.697  51.077  55.644  1.00 26.47 ?  800  PRO B N     1 
ATOM   15143 C CA    . PRO B 1 802  ? 18.357  51.638  54.325  1.00 30.63 ?  800  PRO B CA    1 
ATOM   15144 C C     . PRO B 1 802  ? 17.666  52.990  54.406  1.00 24.70 ?  800  PRO B C     1 
ATOM   15145 O O     . PRO B 1 802  ? 17.844  53.828  53.515  1.00 30.90 ?  800  PRO B O     1 
ATOM   15146 C CB    . PRO B 1 802  ? 17.443  50.565  53.723  1.00 27.50 ?  800  PRO B CB    1 
ATOM   15147 C CG    . PRO B 1 802  ? 17.924  49.289  54.342  1.00 28.46 ?  800  PRO B CG    1 
ATOM   15148 C CD    . PRO B 1 802  ? 18.358  49.643  55.742  1.00 29.46 ?  800  PRO B CD    1 
ATOM   15149 N N     . ALA B 1 803  ? 16.905  53.240  55.466  1.00 27.04 ?  801  ALA B N     1 
ATOM   15150 C CA    . ALA B 1 803  ? 16.244  54.522  55.656  1.00 24.88 ?  801  ALA B CA    1 
ATOM   15151 C C     . ALA B 1 803  ? 17.144  55.558  56.324  1.00 26.07 ?  801  ALA B C     1 
ATOM   15152 O O     . ALA B 1 803  ? 16.673  56.655  56.637  1.00 28.49 ?  801  ALA B O     1 
ATOM   15153 C CB    . ALA B 1 803  ? 14.964  54.331  56.468  1.00 28.18 ?  801  ALA B CB    1 
ATOM   15154 N N     . GLY B 1 804  ? 18.418  55.240  56.545  1.00 23.14 ?  802  GLY B N     1 
ATOM   15155 C CA    . GLY B 1 804  ? 19.333  56.195  57.154  1.00 23.46 ?  802  GLY B CA    1 
ATOM   15156 C C     . GLY B 1 804  ? 19.114  56.396  58.638  1.00 23.45 ?  802  GLY B C     1 
ATOM   15157 O O     . GLY B 1 804  ? 19.246  57.522  59.139  1.00 23.37 ?  802  GLY B O     1 
ATOM   15158 N N     . ARG B 1 805  ? 18.787  55.334  59.354  1.00 21.69 ?  803  ARG B N     1 
ATOM   15159 C CA    . ARG B 1 805  ? 18.477  55.391  60.771  1.00 20.91 ?  803  ARG B CA    1 
ATOM   15160 C C     . ARG B 1 805  ? 19.308  54.354  61.506  1.00 19.09 ?  803  ARG B C     1 
ATOM   15161 O O     . ARG B 1 805  ? 19.783  53.388  60.900  1.00 19.04 ?  803  ARG B O     1 
ATOM   15162 C CB    . ARG B 1 805  ? 16.980  55.147  61.009  1.00 20.75 ?  803  ARG B CB    1 
ATOM   15163 C CG    . ARG B 1 805  ? 16.086  56.173  60.327  1.00 25.45 ?  803  ARG B CG    1 
ATOM   15164 C CD    . ARG B 1 805  ? 16.203  57.538  61.003  1.00 25.03 ?  803  ARG B CD    1 
ATOM   15165 N NE    . ARG B 1 805  ? 15.285  58.529  60.445  1.00 29.06 ?  803  ARG B NE    1 
ATOM   15166 C CZ    . ARG B 1 805  ? 15.627  59.451  59.552  1.00 27.58 ?  803  ARG B CZ    1 
ATOM   15167 N NH1   . ARG B 1 805  ? 16.852  59.512  59.054  1.00 25.81 ?  803  ARG B NH1   1 
ATOM   15168 N NH2   . ARG B 1 805  ? 14.719  60.343  59.158  1.00 28.14 ?  803  ARG B NH2   1 
ATOM   15169 N N     . PRO B 1 806  ? 19.525  54.537  62.807  1.00 18.43 ?  804  PRO B N     1 
ATOM   15170 C CA    . PRO B 1 806  ? 20.292  53.540  63.560  1.00 15.88 ?  804  PRO B CA    1 
ATOM   15171 C C     . PRO B 1 806  ? 19.687  52.148  63.428  1.00 16.51 ?  804  PRO B C     1 
ATOM   15172 O O     . PRO B 1 806  ? 18.466  51.975  63.408  1.00 17.84 ?  804  PRO B O     1 
ATOM   15173 C CB    . PRO B 1 806  ? 20.211  54.051  65.004  1.00 18.07 ?  804  PRO B CB    1 
ATOM   15174 C CG    . PRO B 1 806  ? 20.032  55.533  64.853  1.00 20.27 ?  804  PRO B CG    1 
ATOM   15175 C CD    . PRO B 1 806  ? 19.168  55.701  63.640  1.00 18.72 ?  804  PRO B CD    1 
ATOM   15176 N N     . ILE B 1 807  ? 20.566  51.154  63.355  1.00 16.82 ?  805  ILE B N     1 
ATOM   15177 C CA    A ILE B 1 807  ? 20.194  49.739  63.328  0.27 16.76 ?  805  ILE B CA    1 
ATOM   15178 C CA    B ILE B 1 807  ? 20.156  49.754  63.321  0.73 16.73 ?  805  ILE B CA    1 
ATOM   15179 C C     . ILE B 1 807  ? 19.796  49.317  64.737  1.00 16.13 ?  805  ILE B C     1 
ATOM   15180 O O     . ILE B 1 807  ? 20.624  49.435  65.649  1.00 18.09 ?  805  ILE B O     1 
ATOM   15181 C CB    A ILE B 1 807  ? 21.357  48.871  62.823  0.27 16.66 ?  805  ILE B CB    1 
ATOM   15182 C CB    B ILE B 1 807  ? 21.261  48.876  62.723  0.73 16.60 ?  805  ILE B CB    1 
ATOM   15183 C CG1   A ILE B 1 807  ? 21.882  49.386  61.482  0.27 19.25 ?  805  ILE B CG1   1 
ATOM   15184 C CG1   B ILE B 1 807  ? 21.511  49.288  61.270  0.73 18.69 ?  805  ILE B CG1   1 
ATOM   15185 C CG2   A ILE B 1 807  ? 20.934  47.412  62.717  0.27 17.94 ?  805  ILE B CG2   1 
ATOM   15186 C CG2   B ILE B 1 807  ? 20.884  47.405  62.815  0.73 18.02 ?  805  ILE B CG2   1 
ATOM   15187 C CD1   A ILE B 1 807  ? 20.995  49.052  60.319  0.27 18.81 ?  805  ILE B CD1   1 
ATOM   15188 C CD1   B ILE B 1 807  ? 22.807  48.773  60.711  0.73 20.72 ?  805  ILE B CD1   1 
ATOM   15189 N N     . PRO B 1 808  ? 18.578  48.810  64.965  1.00 16.55 ?  806  PRO B N     1 
ATOM   15190 C CA    . PRO B 1 808  ? 18.157  48.473  66.333  1.00 14.52 ?  806  PRO B CA    1 
ATOM   15191 C C     . PRO B 1 808  ? 18.940  47.319  66.925  1.00 14.84 ?  806  PRO B C     1 
ATOM   15192 O O     . PRO B 1 808  ? 19.258  46.335  66.246  1.00 15.84 ?  806  PRO B O     1 
ATOM   15193 C CB    . PRO B 1 808  ? 16.682  48.086  66.165  1.00 15.82 ?  806  PRO B CB    1 
ATOM   15194 C CG    . PRO B 1 808  ? 16.246  48.742  64.924  1.00 21.55 ?  806  PRO B CG    1 
ATOM   15195 C CD    . PRO B 1 808  ? 17.452  48.715  64.019  1.00 15.64 ?  806  PRO B CD    1 
ATOM   15196 N N     . LEU B 1 809  ? 19.260  47.457  68.206  1.00 15.92 ?  807  LEU B N     1 
ATOM   15197 C CA    . LEU B 1 809  ? 19.851  46.396  69.008  1.00 15.23 ?  807  LEU B CA    1 
ATOM   15198 C C     . LEU B 1 809  ? 18.951  46.185  70.210  1.00 15.14 ?  807  LEU B C     1 
ATOM   15199 O O     . LEU B 1 809  ? 18.706  47.129  70.969  1.00 16.31 ?  807  LEU B O     1 
ATOM   15200 C CB    . LEU B 1 809  ? 21.262  46.769  69.467  1.00 16.04 ?  807  LEU B CB    1 
ATOM   15201 C CG    . LEU B 1 809  ? 21.938  45.812  70.453  1.00 15.81 ?  807  LEU B CG    1 
ATOM   15202 C CD1   . LEU B 1 809  ? 22.077  44.428  69.828  1.00 17.96 ?  807  LEU B CD1   1 
ATOM   15203 C CD2   . LEU B 1 809  ? 23.313  46.336  70.913  1.00 17.91 ?  807  LEU B CD2   1 
ATOM   15204 N N     . ILE B 1 810  ? 18.452  44.965  70.381  1.00 12.19 ?  808  ILE B N     1 
ATOM   15205 C CA    . ILE B 1 810  ? 17.796  44.578  71.624  1.00 13.48 ?  808  ILE B CA    1 
ATOM   15206 C C     . ILE B 1 810  ? 18.782  43.701  72.367  1.00 14.42 ?  808  ILE B C     1 
ATOM   15207 O O     . ILE B 1 810  ? 19.135  42.615  71.893  1.00 15.97 ?  808  ILE B O     1 
ATOM   15208 C CB    . ILE B 1 810  ? 16.480  43.831  71.397  1.00 14.79 ?  808  ILE B CB    1 
ATOM   15209 C CG1   . ILE B 1 810  ? 15.515  44.662  70.564  1.00 16.03 ?  808  ILE B CG1   1 
ATOM   15210 C CG2   . ILE B 1 810  ? 15.852  43.484  72.745  1.00 17.96 ?  808  ILE B CG2   1 
ATOM   15211 C CD1   . ILE B 1 810  ? 14.182  43.941  70.352  1.00 19.27 ?  808  ILE B CD1   1 
ATOM   15212 N N     . ALA B 1 811  ? 19.267  44.172  73.508  1.00 16.26 ?  809  ALA B N     1 
ATOM   15213 C CA    . ALA B 1 811  ? 20.289  43.447  74.244  1.00 17.04 ?  809  ALA B CA    1 
ATOM   15214 C C     . ALA B 1 811  ? 19.796  43.234  75.668  1.00 17.06 ?  809  ALA B C     1 
ATOM   15215 O O     . ALA B 1 811  ? 19.335  44.175  76.324  1.00 20.40 ?  809  ALA B O     1 
ATOM   15216 C CB    . ALA B 1 811  ? 21.618  44.191  74.227  1.00 16.95 ?  809  ALA B CB    1 
ATOM   15217 N N     . GLU B 1 812  ? 19.842  41.994  76.123  1.00 14.79 ?  810  GLU B N     1 
ATOM   15218 C CA    . GLU B 1 812  ? 19.565  41.662  77.515  1.00 15.91 ?  810  GLU B CA    1 
ATOM   15219 C C     . GLU B 1 812  ? 20.863  41.124  78.098  1.00 16.15 ?  810  GLU B C     1 
ATOM   15220 O O     . GLU B 1 812  ? 21.412  40.150  77.576  1.00 15.22 ?  810  GLU B O     1 
ATOM   15221 C CB    . GLU B 1 812  ? 18.439  40.635  77.624  1.00 19.23 ?  810  GLU B CB    1 
ATOM   15222 N N     . THR B 1 813  ? 21.367  41.765  79.172  1.00 15.05 ?  811  THR B N     1 
ATOM   15223 C CA    . THR B 1 813  ? 22.738  41.548  79.613  1.00 17.23 ?  811  THR B CA    1 
ATOM   15224 C C     . THR B 1 813  ? 22.872  41.301  81.118  1.00 18.70 ?  811  THR B C     1 
ATOM   15225 O O     . THR B 1 813  ? 23.933  41.575  81.696  1.00 23.73 ?  811  THR B O     1 
ATOM   15226 C CB    . THR B 1 813  ? 23.627  42.725  79.199  1.00 17.58 ?  811  THR B CB    1 
ATOM   15227 O OG1   . THR B 1 813  ? 23.014  43.957  79.588  1.00 16.63 ?  811  THR B OG1   1 
ATOM   15228 C CG2   . THR B 1 813  ? 23.819  42.752  77.688  1.00 20.97 ?  811  THR B CG2   1 
ATOM   15229 N N     . GLY B 1 814  ? 21.852  40.760  81.764  1.00 19.85 ?  812  GLY B N     1 
ATOM   15230 C CA    . GLY B 1 814  ? 22.056  40.199  83.099  1.00 20.71 ?  812  GLY B CA    1 
ATOM   15231 C C     . GLY B 1 814  ? 21.813  41.152  84.254  1.00 18.16 ?  812  GLY B C     1 
ATOM   15232 O O     . GLY B 1 814  ? 21.242  42.231  84.121  1.00 18.95 ?  812  GLY B O     1 
ATOM   15233 N N     . GLY B 1 815  ? 22.261  40.724  85.429  1.00 18.37 ?  813  GLY B N     1 
ATOM   15234 C CA    . GLY B 1 815  ? 21.926  41.473  86.626  1.00 17.68 ?  813  GLY B CA    1 
ATOM   15235 C C     . GLY B 1 815  ? 22.743  41.002  87.808  1.00 20.27 ?  813  GLY B C     1 
ATOM   15236 O O     . GLY B 1 815  ? 23.390  39.953  87.770  1.00 28.12 ?  813  GLY B O     1 
ATOM   15237 N N     . GLN B 1 816  ? 22.709  41.804  88.868  1.00 18.27 ?  814  GLN B N     1 
ATOM   15238 C CA    . GLN B 1 816  ? 23.368  41.487  90.135  1.00 17.35 ?  814  GLN B CA    1 
ATOM   15239 C C     . GLN B 1 816  ? 22.267  41.509  91.190  1.00 14.34 ?  814  GLN B C     1 
ATOM   15240 O O     . GLN B 1 816  ? 22.154  42.459  91.971  1.00 17.79 ?  814  GLN B O     1 
ATOM   15241 C CB    . GLN B 1 816  ? 24.471  42.486  90.447  1.00 20.18 ?  814  GLN B CB    1 
ATOM   15242 C CG    . GLN B 1 816  ? 25.345  42.071  91.592  1.00 22.98 ?  814  GLN B CG    1 
ATOM   15243 C CD    . GLN B 1 816  ? 26.223  40.899  91.233  1.00 27.51 ?  814  GLN B CD    1 
ATOM   15244 O OE1   . GLN B 1 816  ? 25.762  39.755  91.190  1.00 26.65 ?  814  GLN B OE1   1 
ATOM   15245 N NE2   . GLN B 1 816  ? 27.500  41.173  90.956  1.00 30.26 ?  814  GLN B NE2   1 
ATOM   15246 N N     . ASN B 1 817  ? 21.448  40.461  91.194  1.00 12.57 ?  815  ASN B N     1 
ATOM   15247 C CA    . ASN B 1 817  ? 20.097  40.552  91.730  1.00 11.56 ?  815  ASN B CA    1 
ATOM   15248 C C     . ASN B 1 817  ? 20.079  40.315  93.226  1.00 12.56 ?  815  ASN B C     1 
ATOM   15249 O O     . ASN B 1 817  ? 20.659  39.341  93.717  1.00 13.54 ?  815  ASN B O     1 
ATOM   15250 C CB    . ASN B 1 817  ? 19.193  39.546  91.035  1.00 11.40 ?  815  ASN B CB    1 
ATOM   15251 C CG    . ASN B 1 817  ? 19.327  39.621  89.543  1.00 13.41 ?  815  ASN B CG    1 
ATOM   15252 O OD1   . ASN B 1 817  ? 19.137  40.693  88.947  1.00 12.09 ?  815  ASN B OD1   1 
ATOM   15253 N ND2   . ASN B 1 817  ? 19.698  38.506  88.933  1.00 14.02 ?  815  ASN B ND2   1 
ATOM   15254 N N     . ALA B 1 818  ? 19.383  41.196  93.939  1.00 13.07 ?  816  ALA B N     1 
ATOM   15255 C CA    . ALA B 1 818  ? 19.312  41.141  95.390  1.00 11.93 ?  816  ALA B CA    1 
ATOM   15256 C C     . ALA B 1 818  ? 17.924  40.720  95.850  1.00 11.77 ?  816  ALA B C     1 
ATOM   15257 O O     . ALA B 1 818  ? 16.922  40.889  95.145  1.00 11.76 ?  816  ALA B O     1 
ATOM   15258 C CB    . ALA B 1 818  ? 19.646  42.503  95.999  1.00 14.13 ?  816  ALA B CB    1 
ATOM   15259 N N     . MET B 1 819  ? 17.880  40.174  97.062  1.00 11.73 ?  817  MET B N     1 
ATOM   15260 C CA    . MET B 1 819  ? 16.638  39.972  97.793  1.00 10.86 ?  817  MET B CA    1 
ATOM   15261 C C     . MET B 1 819  ? 16.818  40.565  99.175  1.00 11.96 ?  817  MET B C     1 
ATOM   15262 O O     . MET B 1 819  ? 17.801  40.255  99.851  1.00 14.13 ?  817  MET B O     1 
ATOM   15263 C CB    . MET B 1 819  ? 16.268  38.496  97.914  1.00 12.26 ?  817  MET B CB    1 
ATOM   15264 C CG    . MET B 1 819  ? 15.017  38.254  98.767  1.00 12.58 ?  817  MET B CG    1 
ATOM   15265 S SD    . MET B 1 819  ? 14.665  36.497  99.019  1.00 15.96 ?  817  MET B SD    1 
ATOM   15266 C CE    . MET B 1 819  ? 14.086  36.032  97.384  1.00 16.44 ?  817  MET B CE    1 
ATOM   15267 N N     . ILE B 1 820  ? 15.875  41.406  99.590  1.00 12.44 ?  818  ILE B N     1 
ATOM   15268 C CA    . ILE B 1 820  ? 15.890  42.006  100.919 1.00 12.32 ?  818  ILE B CA    1 
ATOM   15269 C C     . ILE B 1 820  ? 14.835  41.309  101.762 1.00 11.50 ?  818  ILE B C     1 
ATOM   15270 O O     . ILE B 1 820  ? 13.697  41.116  101.315 1.00 12.90 ?  818  ILE B O     1 
ATOM   15271 C CB    . ILE B 1 820  ? 15.645  43.523  100.851 1.00 11.98 ?  818  ILE B CB    1 
ATOM   15272 C CG1   . ILE B 1 820  ? 16.770  44.189  100.038 1.00 14.86 ?  818  ILE B CG1   1 
ATOM   15273 C CG2   . ILE B 1 820  ? 15.474  44.101  102.290 1.00 13.13 ?  818  ILE B CG2   1 
ATOM   15274 C CD1   . ILE B 1 820  ? 16.586  45.691  99.814  1.00 16.75 ?  818  ILE B CD1   1 
ATOM   15275 N N     . VAL B 1 821  ? 15.224  40.914  102.976 1.00 13.48 ?  819  VAL B N     1 
ATOM   15276 C CA    . VAL B 1 821  ? 14.382  40.168  103.905 1.00 12.82 ?  819  VAL B CA    1 
ATOM   15277 C C     . VAL B 1 821  ? 14.383  40.930  105.223 1.00 14.28 ?  819  VAL B C     1 
ATOM   15278 O O     . VAL B 1 821  ? 15.453  41.195  105.778 1.00 15.89 ?  819  VAL B O     1 
ATOM   15279 C CB    . VAL B 1 821  ? 14.923  38.740  104.125 1.00 14.04 ?  819  VAL B CB    1 
ATOM   15280 C CG1   . VAL B 1 821  ? 14.053  37.972  105.117 1.00 16.17 ?  819  VAL B CG1   1 
ATOM   15281 C CG2   . VAL B 1 821  ? 15.015  37.994  102.791 1.00 14.37 ?  819  VAL B CG2   1 
ATOM   15282 N N     . ASP B 1 822  ? 13.200  41.264  105.738 1.00 13.21 ?  820  ASP B N     1 
ATOM   15283 C CA    . ASP B 1 822  ? 13.166  41.906  107.046 1.00 14.57 ?  820  ASP B CA    1 
ATOM   15284 C C     . ASP B 1 822  ? 12.719  40.906  108.113 1.00 16.60 ?  820  ASP B C     1 
ATOM   15285 O O     . ASP B 1 822  ? 12.493  39.724  107.851 1.00 16.17 ?  820  ASP B O     1 
ATOM   15286 C CB    . ASP B 1 822  ? 12.318  43.192  107.017 1.00 15.02 ?  820  ASP B CB    1 
ATOM   15287 C CG    . ASP B 1 822  ? 10.806  42.956  106.979 1.00 14.44 ?  820  ASP B CG    1 
ATOM   15288 O OD1   . ASP B 1 822  ? 10.306  41.828  107.166 1.00 16.57 ?  820  ASP B OD1   1 
ATOM   15289 O OD2   . ASP B 1 822  ? 10.103  43.974  106.739 1.00 18.79 ?  820  ASP B OD2   1 
ATOM   15290 N N     . SER B 1 823  ? 12.614  41.391  109.350 1.00 17.02 ?  821  SER B N     1 
ATOM   15291 C CA    . SER B 1 823  ? 12.319  40.492  110.456 1.00 18.39 ?  821  SER B CA    1 
ATOM   15292 C C     . SER B 1 823  ? 10.864  40.043  110.505 1.00 18.99 ?  821  SER B C     1 
ATOM   15293 O O     . SER B 1 823  ? 10.524  39.199  111.346 1.00 20.86 ?  821  SER B O     1 
ATOM   15294 C CB    . SER B 1 823  ? 12.696  41.157  111.781 1.00 20.01 ?  821  SER B CB    1 
ATOM   15295 O OG    . SER B 1 823  ? 11.933  42.336  111.998 1.00 22.42 ?  821  SER B OG    1 
ATOM   15296 N N     . SER B 1 824  ? 9.993   40.580  109.649 1.00 15.19 ?  822  SER B N     1 
ATOM   15297 C CA    . SER B 1 824  ? 8.612   40.109  109.619 1.00 15.94 ?  822  SER B CA    1 
ATOM   15298 C C     . SER B 1 824  ? 8.420   38.920  108.691 1.00 18.42 ?  822  SER B C     1 
ATOM   15299 O O     . SER B 1 824  ? 7.368   38.277  108.734 1.00 18.49 ?  822  SER B O     1 
ATOM   15300 C CB    . SER B 1 824  ? 7.652   41.238  109.198 1.00 16.12 ?  822  SER B CB    1 
ATOM   15301 O OG    . SER B 1 824  ? 7.765   41.551  107.811 1.00 14.49 ?  822  SER B OG    1 
ATOM   15302 N N     . ALA B 1 825  ? 9.401   38.624  107.848 1.00 15.78 ?  823  ALA B N     1 
ATOM   15303 C CA    . ALA B 1 825  ? 9.257   37.546  106.880 1.00 17.03 ?  823  ALA B CA    1 
ATOM   15304 C C     . ALA B 1 825  ? 9.265   36.190  107.583 1.00 17.08 ?  823  ALA B C     1 
ATOM   15305 O O     . ALA B 1 825  ? 9.868   36.020  108.648 1.00 20.52 ?  823  ALA B O     1 
ATOM   15306 C CB    . ALA B 1 825  ? 10.382  37.628  105.845 1.00 17.16 ?  823  ALA B CB    1 
ATOM   15307 N N     . LEU B 1 826  ? 8.567   35.224  106.989 1.00 18.20 ?  824  LEU B N     1 
ATOM   15308 C CA    . LEU B 1 826  ? 8.549   33.866  107.518 1.00 19.97 ?  824  LEU B CA    1 
ATOM   15309 C C     . LEU B 1 826  ? 9.788   33.127  107.025 1.00 20.53 ?  824  LEU B C     1 
ATOM   15310 O O     . LEU B 1 826  ? 9.974   32.961  105.816 1.00 20.53 ?  824  LEU B O     1 
ATOM   15311 C CB    . LEU B 1 826  ? 7.276   33.138  107.097 1.00 23.55 ?  824  LEU B CB    1 
ATOM   15312 C CG    . LEU B 1 826  ? 7.020   31.760  107.716 1.00 26.80 ?  824  LEU B CG    1 
ATOM   15313 C CD1   . LEU B 1 826  ? 7.183   31.795  109.230 1.00 29.26 ?  824  LEU B CD1   1 
ATOM   15314 C CD2   . LEU B 1 826  ? 5.616   31.296  107.344 1.00 32.97 ?  824  LEU B CD2   1 
ATOM   15315 N N     . ALA B 1 827  ? 10.625  32.672  107.961 1.00 20.27 ?  825  ALA B N     1 
ATOM   15316 C CA    . ALA B 1 827  ? 11.943  32.150  107.604 1.00 17.03 ?  825  ALA B CA    1 
ATOM   15317 C C     . ALA B 1 827  ? 11.843  30.952  106.666 1.00 20.32 ?  825  ALA B C     1 
ATOM   15318 O O     . ALA B 1 827  ? 12.616  30.844  105.706 1.00 17.83 ?  825  ALA B O     1 
ATOM   15319 C CB    . ALA B 1 827  ? 12.717  31.775  108.870 1.00 19.87 ?  825  ALA B CB    1 
ATOM   15320 N N     . GLU B 1 828  ? 10.911  30.035  106.934 1.00 20.20 ?  826  GLU B N     1 
ATOM   15321 C CA    . GLU B 1 828  ? 10.768  28.858  106.080 1.00 22.50 ?  826  GLU B CA    1 
ATOM   15322 C C     . GLU B 1 828  ? 10.449  29.248  104.643 1.00 20.58 ?  826  GLU B C     1 
ATOM   15323 O O     . GLU B 1 828  ? 10.979  28.646  103.700 1.00 18.18 ?  826  GLU B O     1 
ATOM   15324 C CB    . GLU B 1 828  ? 9.685   27.933  106.636 1.00 24.29 ?  826  GLU B CB    1 
ATOM   15325 C CG    . GLU B 1 828  ? 10.111  27.147  107.866 1.00 29.10 ?  826  GLU B CG    1 
ATOM   15326 C CD    . GLU B 1 828  ? 10.098  27.947  109.172 1.00 32.57 ?  826  GLU B CD    1 
ATOM   15327 O OE1   . GLU B 1 828  ? 9.711   29.141  109.178 1.00 30.07 ?  826  GLU B OE1   1 
ATOM   15328 O OE2   . GLU B 1 828  ? 10.483  27.363  110.213 1.00 34.65 ?  826  GLU B OE2   1 
ATOM   15329 N N     . GLN B 1 829  ? 9.580   30.245  104.458 1.00 17.16 ?  827  GLN B N     1 
ATOM   15330 C CA    . GLN B 1 829  ? 9.254   30.731  103.118 1.00 18.12 ?  827  GLN B CA    1 
ATOM   15331 C C     . GLN B 1 829  ? 10.464  31.368  102.460 1.00 17.33 ?  827  GLN B C     1 
ATOM   15332 O O     . GLN B 1 829  ? 10.746  31.120  101.279 1.00 15.51 ?  827  GLN B O     1 
ATOM   15333 C CB    . GLN B 1 829  ? 8.124   31.757  103.186 1.00 23.63 ?  827  GLN B CB    1 
ATOM   15334 C CG    . GLN B 1 829  ? 6.728   31.211  103.311 1.00 29.31 ?  827  GLN B CG    1 
ATOM   15335 C CD    . GLN B 1 829  ? 5.694   32.327  103.196 1.00 33.53 ?  827  GLN B CD    1 
ATOM   15336 O OE1   . GLN B 1 829  ? 6.025   33.513  103.336 1.00 28.91 ?  827  GLN B OE1   1 
ATOM   15337 N NE2   . GLN B 1 829  ? 4.442   31.957  102.937 1.00 31.26 ?  827  GLN B NE2   1 
ATOM   15338 N N     . VAL B 1 830  ? 11.163  32.228  103.201 1.00 16.56 ?  828  VAL B N     1 
ATOM   15339 C CA    . VAL B 1 830  ? 12.390  32.839  102.704 1.00 14.22 ?  828  VAL B CA    1 
ATOM   15340 C C     . VAL B 1 830  ? 13.357  31.768  102.224 1.00 15.01 ?  828  VAL B C     1 
ATOM   15341 O O     . VAL B 1 830  ? 13.903  31.845  101.120 1.00 15.42 ?  828  VAL B O     1 
ATOM   15342 C CB    . VAL B 1 830  ? 13.038  33.709  103.797 1.00 16.01 ?  828  VAL B CB    1 
ATOM   15343 C CG1   . VAL B 1 830  ? 14.398  34.202  103.339 1.00 17.83 ?  828  VAL B CG1   1 
ATOM   15344 C CG2   . VAL B 1 830  ? 12.103  34.876  104.177 1.00 17.71 ?  828  VAL B CG2   1 
ATOM   15345 N N     . VAL B 1 831  ? 13.614  30.764  103.068 1.00 16.42 ?  829  VAL B N     1 
ATOM   15346 C CA    . VAL B 1 831  ? 14.658  29.803  102.738 1.00 14.13 ?  829  VAL B CA    1 
ATOM   15347 C C     . VAL B 1 831  ? 14.289  29.018  101.484 1.00 14.92 ?  829  VAL B C     1 
ATOM   15348 O O     . VAL B 1 831  ? 15.130  28.829  100.594 1.00 15.34 ?  829  VAL B O     1 
ATOM   15349 C CB    . VAL B 1 831  ? 14.941  28.895  103.950 1.00 15.12 ?  829  VAL B CB    1 
ATOM   15350 C CG1   . VAL B 1 831  ? 15.762  27.687  103.521 1.00 18.04 ?  829  VAL B CG1   1 
ATOM   15351 C CG2   . VAL B 1 831  ? 15.684  29.695  105.025 1.00 17.06 ?  829  VAL B CG2   1 
ATOM   15352 N N     . GLY B 1 832  ? 13.029  28.590  101.360 1.00 15.40 ?  830  GLY B N     1 
ATOM   15353 C CA    . GLY B 1 832  ? 12.622  27.913  100.138 1.00 13.87 ?  830  GLY B CA    1 
ATOM   15354 C C     . GLY B 1 832  ? 12.804  28.785  98.912  1.00 16.17 ?  830  GLY B C     1 
ATOM   15355 O O     . GLY B 1 832  ? 13.288  28.325  97.874  1.00 15.56 ?  830  GLY B O     1 
ATOM   15356 N N     . ASP B 1 833  ? 12.460  30.066  99.027  1.00 15.86 ?  831  ASP B N     1 
ATOM   15357 C CA    . ASP B 1 833  ? 12.579  30.938  97.859  1.00 14.33 ?  831  ASP B CA    1 
ATOM   15358 C C     . ASP B 1 833  ? 14.031  31.284  97.559  1.00 15.17 ?  831  ASP B C     1 
ATOM   15359 O O     . ASP B 1 833  ? 14.373  31.556  96.403  1.00 16.11 ?  831  ASP B O     1 
ATOM   15360 C CB    . ASP B 1 833  ? 11.755  32.214  98.061  1.00 13.78 ?  831  ASP B CB    1 
ATOM   15361 C CG    . ASP B 1 833  ? 10.265  31.945  98.054  1.00 15.10 ?  831  ASP B CG    1 
ATOM   15362 O OD1   . ASP B 1 833  ? 9.844   30.858  97.604  1.00 17.51 ?  831  ASP B OD1   1 
ATOM   15363 O OD2   . ASP B 1 833  ? 9.493   32.817  98.516  1.00 17.06 ?  831  ASP B OD2   1 
ATOM   15364 N N     . VAL B 1 834  ? 14.894  31.292  98.577  1.00 13.88 ?  832  VAL B N     1 
ATOM   15365 C CA    . VAL B 1 834  ? 16.310  31.564  98.358  1.00 12.74 ?  832  VAL B CA    1 
ATOM   15366 C C     . VAL B 1 834  ? 16.985  30.367  97.704  1.00 13.06 ?  832  VAL B C     1 
ATOM   15367 O O     . VAL B 1 834  ? 17.777  30.514  96.760  1.00 16.06 ?  832  VAL B O     1 
ATOM   15368 C CB    . VAL B 1 834  ? 16.987  31.938  99.689  1.00 13.54 ?  832  VAL B CB    1 
ATOM   15369 C CG1   . VAL B 1 834  ? 18.511  31.895  99.551  1.00 16.57 ?  832  VAL B CG1   1 
ATOM   15370 C CG2   . VAL B 1 834  ? 16.543  33.330  100.102 1.00 15.09 ?  832  VAL B CG2   1 
ATOM   15371 N N     . ILE B 1 835  ? 16.709  29.167  98.222  1.00 13.93 ?  833  ILE B N     1 
ATOM   15372 C CA    . ILE B 1 835  ? 17.296  27.951  97.664  1.00 15.73 ?  833  ILE B CA    1 
ATOM   15373 C C     . ILE B 1 835  ? 16.950  27.839  96.187  1.00 15.95 ?  833  ILE B C     1 
ATOM   15374 O O     . ILE B 1 835  ? 17.816  27.568  95.346  1.00 17.49 ?  833  ILE B O     1 
ATOM   15375 C CB    . ILE B 1 835  ? 16.823  26.717  98.455  1.00 16.52 ?  833  ILE B CB    1 
ATOM   15376 C CG1   . ILE B 1 835  ? 17.396  26.704  99.877  1.00 20.35 ?  833  ILE B CG1   1 
ATOM   15377 C CG2   . ILE B 1 835  ? 17.185  25.417  97.723  1.00 21.42 ?  833  ILE B CG2   1 
ATOM   15378 C CD1   . ILE B 1 835  ? 18.828  26.236  99.982  1.00 23.20 ?  833  ILE B CD1   1 
ATOM   15379 N N     . THR B 1 836  ? 15.688  28.082  95.842  1.00 15.31 ?  834  THR B N     1 
ATOM   15380 C CA    A THR B 1 836  ? 15.279  28.059  94.442  0.64 15.46 ?  834  THR B CA    1 
ATOM   15381 C CA    B THR B 1 836  ? 15.304  28.043  94.433  0.36 15.49 ?  834  THR B CA    1 
ATOM   15382 C C     . THR B 1 836  ? 15.970  29.166  93.652  1.00 16.12 ?  834  THR B C     1 
ATOM   15383 O O     . THR B 1 836  ? 16.581  28.921  92.609  1.00 16.38 ?  834  THR B O     1 
ATOM   15384 C CB    A THR B 1 836  ? 13.757  28.206  94.357  0.64 17.47 ?  834  THR B CB    1 
ATOM   15385 C CB    B THR B 1 836  ? 13.785  28.127  94.266  0.36 17.51 ?  834  THR B CB    1 
ATOM   15386 O OG1   A THR B 1 836  ? 13.128  27.159  95.109  0.64 20.26 ?  834  THR B OG1   1 
ATOM   15387 O OG1   B THR B 1 836  ? 13.301  29.353  94.823  0.36 16.78 ?  834  THR B OG1   1 
ATOM   15388 C CG2   A THR B 1 836  ? 13.297  28.130  92.915  0.64 16.50 ?  834  THR B CG2   1 
ATOM   15389 C CG2   B THR B 1 836  ? 13.094  26.943  94.916  0.36 19.97 ?  834  THR B CG2   1 
ATOM   15390 N N     . SER B 1 837  ? 15.879  30.407  94.143  1.00 14.29 ?  835  SER B N     1 
ATOM   15391 C CA    . SER B 1 837  ? 16.354  31.545  93.363  1.00 12.57 ?  835  SER B CA    1 
ATOM   15392 C C     . SER B 1 837  ? 17.853  31.506  93.138  1.00 13.04 ?  835  SER B C     1 
ATOM   15393 O O     . SER B 1 837  ? 18.332  31.957  92.094  1.00 14.17 ?  835  SER B O     1 
ATOM   15394 C CB    . SER B 1 837  ? 15.978  32.858  94.038  1.00 13.23 ?  835  SER B CB    1 
ATOM   15395 O OG    . SER B 1 837  ? 14.578  32.988  94.142  1.00 12.69 ?  835  SER B OG    1 
ATOM   15396 N N     . ALA B 1 838  ? 18.614  31.046  94.126  1.00 12.88 ?  836  ALA B N     1 
ATOM   15397 C CA    . ALA B 1 838  ? 20.063  31.098  94.016  1.00 13.69 ?  836  ALA B CA    1 
ATOM   15398 C C     . ALA B 1 838  ? 20.657  29.885  93.316  1.00 14.39 ?  836  ALA B C     1 
ATOM   15399 O O     . ALA B 1 838  ? 21.684  30.021  92.651  1.00 15.94 ?  836  ALA B O     1 
ATOM   15400 C CB    . ALA B 1 838  ? 20.698  31.230  95.411  1.00 16.42 ?  836  ALA B CB    1 
ATOM   15401 N N     . PHE B 1 839  ? 20.057  28.703  93.460  1.00 13.48 ?  837  PHE B N     1 
ATOM   15402 C CA    . PHE B 1 839  ? 20.725  27.477  93.046  1.00 15.12 ?  837  PHE B CA    1 
ATOM   15403 C C     . PHE B 1 839  ? 19.990  26.686  91.977  1.00 16.31 ?  837  PHE B C     1 
ATOM   15404 O O     . PHE B 1 839  ? 20.595  25.780  91.386  1.00 16.98 ?  837  PHE B O     1 
ATOM   15405 C CB    . PHE B 1 839  ? 20.973  26.572  94.262  1.00 16.06 ?  837  PHE B CB    1 
ATOM   15406 C CG    . PHE B 1 839  ? 21.724  27.257  95.371  1.00 16.60 ?  837  PHE B CG    1 
ATOM   15407 C CD1   . PHE B 1 839  ? 22.945  27.882  95.132  1.00 17.77 ?  837  PHE B CD1   1 
ATOM   15408 C CD2   . PHE B 1 839  ? 21.187  27.317  96.649  1.00 19.03 ?  837  PHE B CD2   1 
ATOM   15409 C CE1   . PHE B 1 839  ? 23.634  28.522  96.147  1.00 16.90 ?  837  PHE B CE1   1 
ATOM   15410 C CE2   . PHE B 1 839  ? 21.871  27.969  97.678  1.00 20.00 ?  837  PHE B CE2   1 
ATOM   15411 C CZ    . PHE B 1 839  ? 23.097  28.565  97.431  1.00 20.15 ?  837  PHE B CZ    1 
ATOM   15412 N N     . ASP B 1 840  ? 18.723  26.985  91.712  1.00 14.34 ?  838  ASP B N     1 
ATOM   15413 C CA    . ASP B 1 840  ? 18.046  26.398  90.561  1.00 14.51 ?  838  ASP B CA    1 
ATOM   15414 C C     . ASP B 1 840  ? 18.877  26.634  89.308  1.00 15.14 ?  838  ASP B C     1 
ATOM   15415 O O     . ASP B 1 840  ? 19.440  27.714  89.112  1.00 14.66 ?  838  ASP B O     1 
ATOM   15416 C CB    . ASP B 1 840  ? 16.643  27.018  90.421  1.00 15.96 ?  838  ASP B CB    1 
ATOM   15417 C CG    . ASP B 1 840  ? 15.873  26.512  89.215  1.00 16.36 ?  838  ASP B CG    1 
ATOM   15418 O OD1   . ASP B 1 840  ? 16.197  26.912  88.067  1.00 17.43 ?  838  ASP B OD1   1 
ATOM   15419 O OD2   . ASP B 1 840  ? 14.922  25.730  89.427  1.00 18.12 ?  838  ASP B OD2   1 
ATOM   15420 N N     . SER B 1 841  ? 18.962  25.607  88.464  1.00 16.00 ?  839  SER B N     1 
ATOM   15421 C CA    . SER B 1 841  ? 19.743  25.681  87.225  1.00 16.36 ?  839  SER B CA    1 
ATOM   15422 C C     . SER B 1 841  ? 21.203  26.012  87.501  1.00 15.18 ?  839  SER B C     1 
ATOM   15423 O O     . SER B 1 841  ? 21.866  26.657  86.681  1.00 15.85 ?  839  SER B O     1 
ATOM   15424 C CB    . SER B 1 841  ? 19.143  26.704  86.261  1.00 15.29 ?  839  SER B CB    1 
ATOM   15425 O OG    . SER B 1 841  ? 17.827  26.311  85.937  1.00 17.24 ?  839  SER B OG    1 
ATOM   15426 N N     . ALA B 1 842  ? 21.698  25.580  88.669  1.00 14.45 ?  840  ALA B N     1 
ATOM   15427 C CA    . ALA B 1 842  ? 23.062  25.857  89.127  1.00 14.01 ?  840  ALA B CA    1 
ATOM   15428 C C     . ALA B 1 842  ? 23.370  27.351  89.091  1.00 13.43 ?  840  ALA B C     1 
ATOM   15429 O O     . ALA B 1 842  ? 24.499  27.765  88.808  1.00 15.35 ?  840  ALA B O     1 
ATOM   15430 C CB    . ALA B 1 842  ? 24.096  25.060  88.317  1.00 16.73 ?  840  ALA B CB    1 
ATOM   15431 N N     . GLY B 1 843  ? 22.360  28.171  89.378  1.00 13.20 ?  841  GLY B N     1 
ATOM   15432 C CA    . GLY B 1 843  ? 22.555  29.609  89.376  1.00 15.45 ?  841  GLY B CA    1 
ATOM   15433 C C     . GLY B 1 843  ? 22.823  30.216  88.018  1.00 15.06 ?  841  GLY B C     1 
ATOM   15434 O O     . GLY B 1 843  ? 23.258  31.374  87.935  1.00 15.86 ?  841  GLY B O     1 
ATOM   15435 N N     . GLN B 1 844  ? 22.593  29.467  86.947  1.00 13.84 ?  842  GLN B N     1 
ATOM   15436 C CA    . GLN B 1 844  ? 22.870  29.955  85.595  1.00 15.05 ?  842  GLN B CA    1 
ATOM   15437 C C     . GLN B 1 844  ? 21.653  30.621  84.966  1.00 15.13 ?  842  GLN B C     1 
ATOM   15438 O O     . GLN B 1 844  ? 21.295  30.353  83.821  1.00 18.55 ?  842  GLN B O     1 
ATOM   15439 C CB    . GLN B 1 844  ? 23.372  28.803  84.736  1.00 14.69 ?  842  GLN B CB    1 
ATOM   15440 C CG    . GLN B 1 844  ? 24.665  28.203  85.265  1.00 15.32 ?  842  GLN B CG    1 
ATOM   15441 C CD    . GLN B 1 844  ? 25.152  27.056  84.417  1.00 15.13 ?  842  GLN B CD    1 
ATOM   15442 O OE1   . GLN B 1 844  ? 26.341  26.965  84.110  1.00 14.19 ?  842  GLN B OE1   1 
ATOM   15443 N NE2   . GLN B 1 844  ? 24.241  26.166  84.036  1.00 17.01 ?  842  GLN B NE2   1 
ATOM   15444 N N     . ARG B 1 845  ? 20.953  31.439  85.735  1.00 14.32 ?  843  ARG B N     1 
ATOM   15445 C CA    . ARG B 1 845  ? 19.884  32.300  85.249  1.00 12.63 ?  843  ARG B CA    1 
ATOM   15446 C C     . ARG B 1 845  ? 20.340  33.741  85.409  1.00 14.39 ?  843  ARG B C     1 
ATOM   15447 O O     . ARG B 1 845  ? 20.916  34.100  86.440  1.00 14.16 ?  843  ARG B O     1 
ATOM   15448 C CB    . ARG B 1 845  ? 18.592  32.094  86.050  1.00 12.98 ?  843  ARG B CB    1 
ATOM   15449 C CG    . ARG B 1 845  ? 17.972  30.705  85.982  1.00 13.65 ?  843  ARG B CG    1 
ATOM   15450 C CD    . ARG B 1 845  ? 16.706  30.670  86.834  1.00 14.63 ?  843  ARG B CD    1 
ATOM   15451 N NE    . ARG B 1 845  ? 16.018  29.382  86.799  1.00 16.50 ?  843  ARG B NE    1 
ATOM   15452 C CZ    . ARG B 1 845  ? 14.899  29.144  86.123  1.00 15.26 ?  843  ARG B CZ    1 
ATOM   15453 N NH1   . ARG B 1 845  ? 14.310  30.090  85.400  1.00 16.34 ?  843  ARG B NH1   1 
ATOM   15454 N NH2   . ARG B 1 845  ? 14.345  27.935  86.190  1.00 17.08 ?  843  ARG B NH2   1 
ATOM   15455 N N     . CYS B 1 846  ? 20.073  34.588  84.415  1.00 14.51 ?  844  CYS B N     1 
ATOM   15456 C CA    . CYS B 1 846  ? 20.386  36.000  84.625  1.00 15.75 ?  844  CYS B CA    1 
ATOM   15457 C C     . CYS B 1 846  ? 19.543  36.606  85.739  1.00 12.28 ?  844  CYS B C     1 
ATOM   15458 O O     . CYS B 1 846  ? 19.925  37.646  86.295  1.00 16.87 ?  844  CYS B O     1 
ATOM   15459 C CB    . CYS B 1 846  ? 20.194  36.796  83.341  1.00 18.26 ?  844  CYS B CB    1 
ATOM   15460 S SG    . CYS B 1 846  ? 21.414  36.331  82.102  1.00 24.46 ?  844  CYS B SG    1 
ATOM   15461 N N     . SER B 1 847  ? 18.410  35.974  86.056  1.00 12.47 ?  845  SER B N     1 
ATOM   15462 C CA    . SER B 1 847  ? 17.502  36.357  87.130  1.00 11.01 ?  845  SER B CA    1 
ATOM   15463 C C     . SER B 1 847  ? 17.937  35.847  88.499  1.00 11.15 ?  845  SER B C     1 
ATOM   15464 O O     . SER B 1 847  ? 17.284  36.174  89.494  1.00 12.44 ?  845  SER B O     1 
ATOM   15465 C CB    . SER B 1 847  ? 16.121  35.792  86.831  1.00 12.50 ?  845  SER B CB    1 
ATOM   15466 O OG    . SER B 1 847  ? 16.272  34.387  86.644  1.00 12.94 ?  845  SER B OG    1 
ATOM   15467 N N     . ALA B 1 848  ? 18.993  35.038  88.571  1.00 12.49 ?  846  ALA B N     1 
ATOM   15468 C CA    . ALA B 1 848  ? 19.288  34.310  89.798  1.00 12.99 ?  846  ALA B CA    1 
ATOM   15469 C C     . ALA B 1 848  ? 19.605  35.263  90.939  1.00 11.16 ?  846  ALA B C     1 
ATOM   15470 O O     . ALA B 1 848  ? 20.141  36.359  90.746  1.00 13.69 ?  846  ALA B O     1 
ATOM   15471 C CB    . ALA B 1 848  ? 20.465  33.359  89.591  1.00 12.61 ?  846  ALA B CB    1 
ATOM   15472 N N     . LEU B 1 849  ? 19.279  34.815  92.149  1.00 12.59 ?  847  LEU B N     1 
ATOM   15473 C CA    . LEU B 1 849  ? 19.576  35.582  93.351  1.00 12.18 ?  847  LEU B CA    1 
ATOM   15474 C C     . LEU B 1 849  ? 21.072  35.549  93.630  1.00 14.55 ?  847  LEU B C     1 
ATOM   15475 O O     . LEU B 1 849  ? 21.642  34.472  93.819  1.00 15.03 ?  847  LEU B O     1 
ATOM   15476 C CB    . LEU B 1 849  ? 18.797  35.004  94.528  1.00 12.37 ?  847  LEU B CB    1 
ATOM   15477 C CG    . LEU B 1 849  ? 19.149  35.648  95.873  1.00 12.17 ?  847  LEU B CG    1 
ATOM   15478 C CD1   . LEU B 1 849  ? 18.824  37.127  95.848  1.00 14.82 ?  847  LEU B CD1   1 
ATOM   15479 C CD2   . LEU B 1 849  ? 18.419  34.936  96.981  1.00 14.03 ?  847  LEU B CD2   1 
ATOM   15480 N N     . ARG B 1 850  ? 21.706  36.722  93.643  1.00 13.68 ?  848  ARG B N     1 
ATOM   15481 C CA    . ARG B 1 850  ? 23.143  36.828  93.867  1.00 13.69 ?  848  ARG B CA    1 
ATOM   15482 C C     . ARG B 1 850  ? 23.504  37.359  95.244  1.00 14.28 ?  848  ARG B C     1 
ATOM   15483 O O     . ARG B 1 850  ? 24.550  36.985  95.791  1.00 14.25 ?  848  ARG B O     1 
ATOM   15484 C CB    . ARG B 1 850  ? 23.781  37.732  92.807  1.00 16.02 ?  848  ARG B CB    1 
ATOM   15485 C CG    . ARG B 1 850  ? 23.404  37.333  91.383  1.00 14.52 ?  848  ARG B CG    1 
ATOM   15486 C CD    . ARG B 1 850  ? 23.796  35.894  91.099  1.00 14.56 ?  848  ARG B CD    1 
ATOM   15487 N NE    . ARG B 1 850  ? 23.681  35.588  89.680  1.00 15.12 ?  848  ARG B NE    1 
ATOM   15488 C CZ    . ARG B 1 850  ? 23.814  34.373  89.174  1.00 15.52 ?  848  ARG B CZ    1 
ATOM   15489 N NH1   . ARG B 1 850  ? 24.060  33.328  89.947  1.00 14.09 ?  848  ARG B NH1   1 
ATOM   15490 N NH2   . ARG B 1 850  ? 23.697  34.205  87.857  1.00 16.35 ?  848  ARG B NH2   1 
ATOM   15491 N N     . VAL B 1 851  ? 22.670  38.216  95.823  1.00 14.13 ?  849  VAL B N     1 
ATOM   15492 C CA    . VAL B 1 851  ? 22.970  38.844  97.106  1.00 14.98 ?  849  VAL B CA    1 
ATOM   15493 C C     . VAL B 1 851  ? 21.704  38.796  97.949  1.00 14.97 ?  849  VAL B C     1 
ATOM   15494 O O     . VAL B 1 851  ? 20.707  39.449  97.619  1.00 13.79 ?  849  VAL B O     1 
ATOM   15495 C CB    . VAL B 1 851  ? 23.449  40.292  96.964  1.00 17.22 ?  849  VAL B CB    1 
ATOM   15496 C CG1   . VAL B 1 851  ? 23.893  40.805  98.335  1.00 18.37 ?  849  VAL B CG1   1 
ATOM   15497 C CG2   . VAL B 1 851  ? 24.576  40.397  95.966  1.00 23.18 ?  849  VAL B CG2   1 
ATOM   15498 N N     . LEU B 1 852  ? 21.733  38.005  99.010  1.00 14.87 ?  850  LEU B N     1 
ATOM   15499 C CA    . LEU B 1 852  ? 20.663  37.966  99.993  1.00 11.83 ?  850  LEU B CA    1 
ATOM   15500 C C     . LEU B 1 852  ? 20.982  38.956  101.109 1.00 14.05 ?  850  LEU B C     1 
ATOM   15501 O O     . LEU B 1 852  ? 22.070  38.904  101.687 1.00 15.28 ?  850  LEU B O     1 
ATOM   15502 C CB    . LEU B 1 852  ? 20.535  36.547  100.545 1.00 15.34 ?  850  LEU B CB    1 
ATOM   15503 C CG    . LEU B 1 852  ? 19.515  36.360  101.656 1.00 14.19 ?  850  LEU B CG    1 
ATOM   15504 C CD1   . LEU B 1 852  ? 18.101  36.682  101.175 1.00 15.53 ?  850  LEU B CD1   1 
ATOM   15505 C CD2   . LEU B 1 852  ? 19.579  34.925  102.165 1.00 17.81 ?  850  LEU B CD2   1 
ATOM   15506 N N     . CYS B 1 853  ? 20.045  39.859  101.394 1.00 12.58 ?  851  CYS B N     1 
ATOM   15507 C CA    . CYS B 1 853  ? 20.231  40.919  102.387 1.00 13.61 ?  851  CYS B CA    1 
ATOM   15508 C C     . CYS B 1 853  ? 19.297  40.651  103.557 1.00 13.29 ?  851  CYS B C     1 
ATOM   15509 O O     . CYS B 1 853  ? 18.074  40.765  103.418 1.00 14.36 ?  851  CYS B O     1 
ATOM   15510 C CB    . CYS B 1 853  ? 19.942  42.286  101.778 1.00 13.65 ?  851  CYS B CB    1 
ATOM   15511 S SG    . CYS B 1 853  ? 20.839  42.602  100.246 1.00 16.52 ?  851  CYS B SG    1 
ATOM   15512 N N     . LEU B 1 854  ? 19.877  40.326  104.717 1.00 12.71 ?  852  LEU B N     1 
ATOM   15513 C CA    . LEU B 1 854  ? 19.122  39.877  105.879 1.00 14.40 ?  852  LEU B CA    1 
ATOM   15514 C C     . LEU B 1 854  ? 19.162  40.929  106.977 1.00 15.95 ?  852  LEU B C     1 
ATOM   15515 O O     . LEU B 1 854  ? 20.245  41.365  107.377 1.00 16.33 ?  852  LEU B O     1 
ATOM   15516 C CB    . LEU B 1 854  ? 19.699  38.570  106.424 1.00 14.34 ?  852  LEU B CB    1 
ATOM   15517 C CG    . LEU B 1 854  ? 19.662  37.376  105.472 1.00 15.45 ?  852  LEU B CG    1 
ATOM   15518 C CD1   . LEU B 1 854  ? 20.332  36.192  106.137 1.00 15.50 ?  852  LEU B CD1   1 
ATOM   15519 C CD2   . LEU B 1 854  ? 18.211  37.048  105.124 1.00 17.19 ?  852  LEU B CD2   1 
ATOM   15520 N N     . GLN B 1 855  ? 17.989  41.314  107.480 1.00 14.17 ?  853  GLN B N     1 
ATOM   15521 C CA    . GLN B 1 855  ? 17.957  42.198  108.637 1.00 13.59 ?  853  GLN B CA    1 
ATOM   15522 C C     . GLN B 1 855  ? 18.705  41.556  109.799 1.00 16.43 ?  853  GLN B C     1 
ATOM   15523 O O     . GLN B 1 855  ? 18.544  40.362  110.074 1.00 16.03 ?  853  GLN B O     1 
ATOM   15524 C CB    . GLN B 1 855  ? 16.514  42.514  109.037 1.00 16.14 ?  853  GLN B CB    1 
ATOM   15525 C CG    . GLN B 1 855  ? 16.415  43.706  109.981 1.00 17.58 ?  853  GLN B CG    1 
ATOM   15526 C CD    . GLN B 1 855  ? 15.013  43.933  110.510 1.00 19.35 ?  853  GLN B CD    1 
ATOM   15527 O OE1   . GLN B 1 855  ? 14.042  43.910  109.754 1.00 20.99 ?  853  GLN B OE1   1 
ATOM   15528 N NE2   . GLN B 1 855  ? 14.903  44.181  111.816 1.00 21.31 ?  853  GLN B NE2   1 
ATOM   15529 N N     . GLU B 1 856  ? 19.531  42.367  110.470 1.00 16.35 ?  854  GLU B N     1 
ATOM   15530 C CA    . GLU B 1 856  ? 20.510  41.842  111.426 1.00 18.55 ?  854  GLU B CA    1 
ATOM   15531 C C     . GLU B 1 856  ? 19.860  40.942  112.470 1.00 19.36 ?  854  GLU B C     1 
ATOM   15532 O O     . GLU B 1 856  ? 20.399  39.878  112.810 1.00 19.37 ?  854  GLU B O     1 
ATOM   15533 C CB    . GLU B 1 856  ? 21.245  43.006  112.098 1.00 22.01 ?  854  GLU B CB    1 
ATOM   15534 C CG    . GLU B 1 856  ? 22.101  42.604  113.293 1.00 22.97 ?  854  GLU B CG    1 
ATOM   15535 C CD    . GLU B 1 856  ? 23.252  41.711  112.892 1.00 29.59 ?  854  GLU B CD    1 
ATOM   15536 O OE1   . GLU B 1 856  ? 23.705  41.815  111.734 1.00 27.22 ?  854  GLU B OE1   1 
ATOM   15537 O OE2   . GLU B 1 856  ? 23.704  40.900  113.730 1.00 25.59 ?  854  GLU B OE2   1 
ATOM   15538 N N     . ASP B 1 857  ? 18.683  41.335  112.961 1.00 19.15 ?  855  ASP B N     1 
ATOM   15539 C CA    . ASP B 1 857  ? 18.012  40.633  114.051 1.00 21.50 ?  855  ASP B CA    1 
ATOM   15540 C C     . ASP B 1 857  ? 17.621  39.203  113.703 1.00 19.67 ?  855  ASP B C     1 
ATOM   15541 O O     . ASP B 1 857  ? 17.440  38.390  114.614 1.00 22.64 ?  855  ASP B O     1 
ATOM   15542 C CB    . ASP B 1 857  ? 16.761  41.406  114.474 1.00 25.61 ?  855  ASP B CB    1 
ATOM   15543 N N     . VAL B 1 858  ? 17.467  38.868  112.420 1.00 14.24 ?  856  VAL B N     1 
ATOM   15544 C CA    . VAL B 1 858  ? 17.052  37.528  112.026 1.00 17.95 ?  856  VAL B CA    1 
ATOM   15545 C C     . VAL B 1 858  ? 18.102  36.816  111.196 1.00 14.04 ?  856  VAL B C     1 
ATOM   15546 O O     . VAL B 1 858  ? 17.867  35.681  110.772 1.00 17.65 ?  856  VAL B O     1 
ATOM   15547 C CB    . VAL B 1 858  ? 15.702  37.531  111.274 1.00 17.66 ?  856  VAL B CB    1 
ATOM   15548 C CG1   . VAL B 1 858  ? 14.574  37.975  112.193 1.00 21.33 ?  856  VAL B CG1   1 
ATOM   15549 C CG2   . VAL B 1 858  ? 15.755  38.402  110.001 1.00 18.20 ?  856  VAL B CG2   1 
ATOM   15550 N N     . ALA B 1 859  ? 19.259  37.440  110.962 1.00 16.06 ?  857  ALA B N     1 
ATOM   15551 C CA    . ALA B 1 859  ? 20.218  36.883  110.007 1.00 16.25 ?  857  ALA B CA    1 
ATOM   15552 C C     . ALA B 1 859  ? 20.767  35.526  110.453 1.00 15.92 ?  857  ALA B C     1 
ATOM   15553 O O     . ALA B 1 859  ? 20.860  34.596  109.644 1.00 17.48 ?  857  ALA B O     1 
ATOM   15554 C CB    . ALA B 1 859  ? 21.358  37.875  109.761 1.00 18.19 ?  857  ALA B CB    1 
ATOM   15555 N N     . ASP B 1 860  ? 21.132  35.381  111.734 1.00 19.98 ?  858  ASP B N     1 
ATOM   15556 C CA    . ASP B 1 860  ? 21.719  34.116  112.163 1.00 18.71 ?  858  ASP B CA    1 
ATOM   15557 C C     . ASP B 1 860  ? 20.726  32.967  112.061 1.00 18.02 ?  858  ASP B C     1 
ATOM   15558 O O     . ASP B 1 860  ? 21.085  31.877  111.599 1.00 20.84 ?  858  ASP B O     1 
ATOM   15559 C CB    . ASP B 1 860  ? 22.261  34.233  113.589 1.00 19.72 ?  858  ASP B CB    1 
ATOM   15560 C CG    . ASP B 1 860  ? 23.447  35.158  113.682 1.00 26.67 ?  858  ASP B CG    1 
ATOM   15561 O OD1   . ASP B 1 860  ? 24.244  35.201  112.717 1.00 27.23 ?  858  ASP B OD1   1 
ATOM   15562 O OD2   . ASP B 1 860  ? 23.590  35.840  114.715 1.00 29.84 ?  858  ASP B OD2   1 
ATOM   15563 N N     . ARG B 1 861  ? 19.477  33.177  112.490 1.00 17.31 ?  859  ARG B N     1 
ATOM   15564 C CA    A ARG B 1 861  ? 18.476  32.116  112.409 0.47 18.80 ?  859  ARG B CA    1 
ATOM   15565 C CA    B ARG B 1 861  ? 18.486  32.106  112.408 0.53 18.79 ?  859  ARG B CA    1 
ATOM   15566 C C     . ARG B 1 861  ? 18.191  31.725  110.961 1.00 17.80 ?  859  ARG B C     1 
ATOM   15567 O O     . ARG B 1 861  ? 18.086  30.536  110.636 1.00 18.16 ?  859  ARG B O     1 
ATOM   15568 C CB    A ARG B 1 861  ? 17.194  32.564  113.111 0.47 20.54 ?  859  ARG B CB    1 
ATOM   15569 C CB    B ARG B 1 861  ? 17.191  32.505  113.118 0.53 20.54 ?  859  ARG B CB    1 
ATOM   15570 C CG    A ARG B 1 861  ? 16.115  31.502  113.182 0.47 22.90 ?  859  ARG B CG    1 
ATOM   15571 C CG    B ARG B 1 861  ? 16.035  31.571  112.777 0.53 24.32 ?  859  ARG B CG    1 
ATOM   15572 C CD    A ARG B 1 861  ? 15.047  31.867  114.210 0.47 28.08 ?  859  ARG B CD    1 
ATOM   15573 C CD    B ARG B 1 861  ? 15.156  31.219  113.959 0.53 28.59 ?  859  ARG B CD    1 
ATOM   15574 N NE    A ARG B 1 861  ? 14.704  33.284  114.191 0.47 27.09 ?  859  ARG B NE    1 
ATOM   15575 N NE    B ARG B 1 861  ? 14.195  30.186  113.592 0.53 27.70 ?  859  ARG B NE    1 
ATOM   15576 C CZ    A ARG B 1 861  ? 13.845  33.838  113.346 0.47 26.89 ?  859  ARG B CZ    1 
ATOM   15577 C CZ    B ARG B 1 861  ? 13.066  30.420  112.938 0.53 27.56 ?  859  ARG B CZ    1 
ATOM   15578 N NH1   A ARG B 1 861  ? 13.247  33.129  112.403 0.47 28.37 ?  859  ARG B NH1   1 
ATOM   15579 N NH1   B ARG B 1 861  ? 12.721  31.644  112.573 0.53 25.17 ?  859  ARG B NH1   1 
ATOM   15580 N NH2   A ARG B 1 861  ? 13.579  35.136  113.451 0.47 28.84 ?  859  ARG B NH2   1 
ATOM   15581 N NH2   B ARG B 1 861  ? 12.264  29.402  112.643 0.53 28.20 ?  859  ARG B NH2   1 
ATOM   15582 N N     . ILE B 1 862  ? 18.055  32.711  110.075 1.00 17.47 ?  860  ILE B N     1 
ATOM   15583 C CA    . ILE B 1 862  ? 17.815  32.381  108.674 1.00 15.76 ?  860  ILE B CA    1 
ATOM   15584 C C     . ILE B 1 862  ? 19.031  31.683  108.072 1.00 15.36 ?  860  ILE B C     1 
ATOM   15585 O O     . ILE B 1 862  ? 18.888  30.722  107.308 1.00 16.58 ?  860  ILE B O     1 
ATOM   15586 C CB    . ILE B 1 862  ? 17.418  33.645  107.891 1.00 15.47 ?  860  ILE B CB    1 
ATOM   15587 C CG1   . ILE B 1 862  ? 16.005  34.065  108.309 1.00 19.86 ?  860  ILE B CG1   1 
ATOM   15588 C CG2   . ILE B 1 862  ? 17.465  33.388  106.384 1.00 15.82 ?  860  ILE B CG2   1 
ATOM   15589 C CD1   . ILE B 1 862  ? 15.592  35.432  107.800 1.00 19.85 ?  860  ILE B CD1   1 
ATOM   15590 N N     . LEU B 1 863  ? 20.244  32.131  108.413 1.00 16.82 ?  861  LEU B N     1 
ATOM   15591 C CA    . LEU B 1 863  ? 21.437  31.483  107.862 1.00 18.57 ?  861  LEU B CA    1 
ATOM   15592 C C     . LEU B 1 863  ? 21.539  30.026  108.296 1.00 18.93 ?  861  LEU B C     1 
ATOM   15593 O O     . LEU B 1 863  ? 21.903  29.158  107.495 1.00 17.47 ?  861  LEU B O     1 
ATOM   15594 C CB    . LEU B 1 863  ? 22.697  32.246  108.265 1.00 19.21 ?  861  LEU B CB    1 
ATOM   15595 C CG    . LEU B 1 863  ? 23.050  33.416  107.353 1.00 23.62 ?  861  LEU B CG    1 
ATOM   15596 C CD1   . LEU B 1 863  ? 24.067  34.324  108.027 1.00 27.51 ?  861  LEU B CD1   1 
ATOM   15597 C CD2   . LEU B 1 863  ? 23.578  32.905  106.014 1.00 24.61 ?  861  LEU B CD2   1 
ATOM   15598 N N     . THR B 1 864  ? 21.242  29.739  109.564 1.00 17.87 ?  862  THR B N     1 
ATOM   15599 C CA    . THR B 1 864  ? 21.232  28.352  110.032 1.00 18.42 ?  862  THR B CA    1 
ATOM   15600 C C     . THR B 1 864  ? 20.263  27.508  109.218 1.00 17.65 ?  862  THR B C     1 
ATOM   15601 O O     . THR B 1 864  ? 20.598  26.409  108.754 1.00 18.02 ?  862  THR B O     1 
ATOM   15602 C CB    . THR B 1 864  ? 20.847  28.306  111.511 1.00 22.39 ?  862  THR B CB    1 
ATOM   15603 O OG1   . THR B 1 864  ? 21.888  28.901  112.282 1.00 23.83 ?  862  THR B OG1   1 
ATOM   15604 C CG2   . THR B 1 864  ? 20.620  26.862  111.988 1.00 23.26 ?  862  THR B CG2   1 
ATOM   15605 N N     . MET B 1 865  ? 19.041  28.007  109.042 1.00 16.25 ?  863  MET B N     1 
ATOM   15606 C CA    . MET B 1 865  ? 18.047  27.264  108.282 1.00 17.24 ?  863  MET B CA    1 
ATOM   15607 C C     . MET B 1 865  ? 18.470  27.102  106.826 1.00 15.12 ?  863  MET B C     1 
ATOM   15608 O O     . MET B 1 865  ? 18.295  26.031  106.230 1.00 17.68 ?  863  MET B O     1 
ATOM   15609 C CB    . MET B 1 865  ? 16.706  27.984  108.370 1.00 16.84 ?  863  MET B CB    1 
ATOM   15610 C CG    . MET B 1 865  ? 15.557  27.160  107.918 1.00 17.32 ?  863  MET B CG    1 
ATOM   15611 S SD    . MET B 1 865  ? 14.032  28.111  108.013 1.00 23.88 ?  863  MET B SD    1 
ATOM   15612 C CE    . MET B 1 865  ? 14.003  28.507  109.754 1.00 23.51 ?  863  MET B CE    1 
ATOM   15613 N N     . LEU B 1 866  ? 19.048  28.156  106.248 1.00 14.73 ?  864  LEU B N     1 
ATOM   15614 C CA    . LEU B 1 866  ? 19.484  28.108  104.856 1.00 15.90 ?  864  LEU B CA    1 
ATOM   15615 C C     . LEU B 1 866  ? 20.573  27.064  104.663 1.00 15.96 ?  864  LEU B C     1 
ATOM   15616 O O     . LEU B 1 866  ? 20.526  26.264  103.726 1.00 15.23 ?  864  LEU B O     1 
ATOM   15617 C CB    . LEU B 1 866  ? 19.981  29.488  104.436 1.00 15.91 ?  864  LEU B CB    1 
ATOM   15618 C CG    . LEU B 1 866  ? 20.413  29.630  102.984 1.00 20.29 ?  864  LEU B CG    1 
ATOM   15619 C CD1   . LEU B 1 866  ? 19.221  29.343  102.079 1.00 21.13 ?  864  LEU B CD1   1 
ATOM   15620 C CD2   . LEU B 1 866  ? 20.921  31.055  102.787 1.00 19.45 ?  864  LEU B CD2   1 
ATOM   15621 N N     . LYS B 1 867  ? 21.551  27.036  105.568 1.00 15.50 ?  865  LYS B N     1 
ATOM   15622 C CA    . LYS B 1 867  ? 22.616  26.049  105.449 1.00 15.49 ?  865  LYS B CA    1 
ATOM   15623 C C     . LYS B 1 867  ? 22.071  24.639  105.642 1.00 15.89 ?  865  LYS B C     1 
ATOM   15624 O O     . LYS B 1 867  ? 22.463  23.715  104.918 1.00 15.67 ?  865  LYS B O     1 
ATOM   15625 C CB    . LYS B 1 867  ? 23.739  26.367  106.441 1.00 17.71 ?  865  LYS B CB    1 
ATOM   15626 C CG    . LYS B 1 867  ? 24.452  27.681  106.113 1.00 19.83 ?  865  LYS B CG    1 
ATOM   15627 C CD    . LYS B 1 867  ? 25.500  28.029  107.159 1.00 23.93 ?  865  LYS B CD    1 
ATOM   15628 C CE    . LYS B 1 867  ? 26.093  29.406  106.909 1.00 24.53 ?  865  LYS B CE    1 
ATOM   15629 N NZ    . LYS B 1 867  ? 26.949  29.850  108.051 1.00 26.15 ?  865  LYS B NZ    1 
ATOM   15630 N N     . GLY B 1 868  ? 21.121  24.465  106.565 1.00 17.62 ?  866  GLY B N     1 
ATOM   15631 C CA    . GLY B 1 868  ? 20.483  23.161  106.715 1.00 16.82 ?  866  GLY B CA    1 
ATOM   15632 C C     . GLY B 1 868  ? 19.766  22.697  105.460 1.00 18.25 ?  866  GLY B C     1 
ATOM   15633 O O     . GLY B 1 868  ? 19.860  21.527  105.073 1.00 19.26 ?  866  GLY B O     1 
ATOM   15634 N N     . ALA B 1 869  ? 19.037  23.606  104.807 1.00 17.66 ?  867  ALA B N     1 
ATOM   15635 C CA    . ALA B 1 869  ? 18.345  23.276  103.567 1.00 16.82 ?  867  ALA B CA    1 
ATOM   15636 C C     . ALA B 1 869  ? 19.336  22.971  102.453 1.00 15.01 ?  867  ALA B C     1 
ATOM   15637 O O     . ALA B 1 869  ? 19.104  22.069  101.635 1.00 16.08 ?  867  ALA B O     1 
ATOM   15638 C CB    . ALA B 1 869  ? 17.426  24.433  103.170 1.00 16.91 ?  867  ALA B CB    1 
ATOM   15639 N N     . LEU B 1 870  ? 20.440  23.723  102.407 1.00 14.43 ?  868  LEU B N     1 
ATOM   15640 C CA    . LEU B 1 870  ? 21.467  23.514  101.389 1.00 15.69 ?  868  LEU B CA    1 
ATOM   15641 C C     . LEU B 1 870  ? 21.984  22.086  101.417 1.00 17.76 ?  868  LEU B C     1 
ATOM   15642 O O     . LEU B 1 870  ? 22.199  21.466  100.369 1.00 18.60 ?  868  LEU B O     1 
ATOM   15643 C CB    . LEU B 1 870  ? 22.621  24.491  101.630 1.00 17.78 ?  868  LEU B CB    1 
ATOM   15644 C CG    . LEU B 1 870  ? 23.764  24.532  100.621 1.00 21.95 ?  868  LEU B CG    1 
ATOM   15645 C CD1   . LEU B 1 870  ? 23.421  25.520  99.528  1.00 27.08 ?  868  LEU B CD1   1 
ATOM   15646 C CD2   . LEU B 1 870  ? 25.074  24.892  101.302 1.00 25.87 ?  868  LEU B CD2   1 
ATOM   15647 N N     . HIS B 1 871  ? 22.198  21.545  102.610 1.00 15.29 ?  869  HIS B N     1 
ATOM   15648 C CA    . HIS B 1 871  ? 22.810  20.224  102.694 1.00 17.89 ?  869  HIS B CA    1 
ATOM   15649 C C     . HIS B 1 871  ? 21.858  19.087  102.335 1.00 19.96 ?  869  HIS B C     1 
ATOM   15650 O O     . HIS B 1 871  ? 22.306  17.937  102.234 1.00 21.91 ?  869  HIS B O     1 
ATOM   15651 C CB    . HIS B 1 871  ? 23.412  20.046  104.084 1.00 23.04 ?  869  HIS B CB    1 
ATOM   15652 C CG    . HIS B 1 871  ? 24.684  20.816  104.258 1.00 26.68 ?  869  HIS B CG    1 
ATOM   15653 N ND1   . HIS B 1 871  ? 25.833  20.514  103.553 1.00 26.89 ?  869  HIS B ND1   1 
ATOM   15654 C CD2   . HIS B 1 871  ? 24.980  21.899  105.013 1.00 27.38 ?  869  HIS B CD2   1 
ATOM   15655 C CE1   . HIS B 1 871  ? 26.786  21.365  103.886 1.00 29.06 ?  869  HIS B CE1   1 
ATOM   15656 N NE2   . HIS B 1 871  ? 26.294  22.217  104.769 1.00 31.80 ?  869  HIS B NE2   1 
ATOM   15657 N N     . GLU B 1 872  ? 20.586  19.381  102.086 1.00 15.75 ?  870  GLU B N     1 
ATOM   15658 C CA    . GLU B 1 872  ? 19.635  18.380  101.636 1.00 16.79 ?  870  GLU B CA    1 
ATOM   15659 C C     . GLU B 1 872  ? 19.503  18.332  100.124 1.00 17.70 ?  870  GLU B C     1 
ATOM   15660 O O     . GLU B 1 872  ? 18.693  17.546  99.628  1.00 17.01 ?  870  GLU B O     1 
ATOM   15661 C CB    . GLU B 1 872  ? 18.272  18.644  102.268 1.00 16.78 ?  870  GLU B CB    1 
ATOM   15662 C CG    . GLU B 1 872  ? 18.332  18.625  103.772 1.00 18.87 ?  870  GLU B CG    1 
ATOM   15663 C CD    . GLU B 1 872  ? 18.680  17.259  104.320 1.00 21.20 ?  870  GLU B CD    1 
ATOM   15664 O OE1   . GLU B 1 872  ? 18.421  16.245  103.629 1.00 23.06 ?  870  GLU B OE1   1 
ATOM   15665 O OE2   . GLU B 1 872  ? 19.202  17.193  105.448 1.00 24.00 ?  870  GLU B OE2   1 
ATOM   15666 N N     . LEU B 1 873  ? 20.247  19.168  99.390  1.00 16.65 ?  871  LEU B N     1 
ATOM   15667 C CA    . LEU B 1 873  ? 20.190  19.149  97.934  1.00 15.77 ?  871  LEU B CA    1 
ATOM   15668 C C     . LEU B 1 873  ? 21.033  18.021  97.368  1.00 17.09 ?  871  LEU B C     1 
ATOM   15669 O O     . LEU B 1 873  ? 22.074  17.657  97.918  1.00 18.92 ?  871  LEU B O     1 
ATOM   15670 C CB    . LEU B 1 873  ? 20.682  20.467  97.337  1.00 16.23 ?  871  LEU B CB    1 
ATOM   15671 C CG    . LEU B 1 873  ? 19.934  21.724  97.761  1.00 22.15 ?  871  LEU B CG    1 
ATOM   15672 C CD1   . LEU B 1 873  ? 20.564  22.959  97.102  1.00 19.17 ?  871  LEU B CD1   1 
ATOM   15673 C CD2   . LEU B 1 873  ? 18.451  21.617  97.411  1.00 19.60 ?  871  LEU B CD2   1 
ATOM   15674 N N     . HIS B 1 874  ? 20.576  17.490  96.241  1.00 16.98 ?  872  HIS B N     1 
ATOM   15675 C CA    . HIS B 1 874  ? 21.265  16.422  95.530  1.00 17.61 ?  872  HIS B CA    1 
ATOM   15676 C C     . HIS B 1 874  ? 21.842  16.989  94.238  1.00 16.63 ?  872  HIS B C     1 
ATOM   15677 O O     . HIS B 1 874  ? 21.095  17.506  93.400  1.00 16.52 ?  872  HIS B O     1 
ATOM   15678 C CB    . HIS B 1 874  ? 20.303  15.272  95.234  1.00 17.30 ?  872  HIS B CB    1 
ATOM   15679 C CG    . HIS B 1 874  ? 20.933  14.118  94.515  1.00 20.78 ?  872  HIS B CG    1 
ATOM   15680 N ND1   . HIS B 1 874  ? 22.295  13.913  94.479  1.00 30.62 ?  872  HIS B ND1   1 
ATOM   15681 C CD2   . HIS B 1 874  ? 20.383  13.114  93.794  1.00 24.34 ?  872  HIS B CD2   1 
ATOM   15682 C CE1   . HIS B 1 874  ? 22.559  12.828  93.771  1.00 28.93 ?  872  HIS B CE1   1 
ATOM   15683 N NE2   . HIS B 1 874  ? 21.416  12.325  93.341  1.00 24.99 ?  872  HIS B NE2   1 
ATOM   15684 N N     . ILE B 1 875  ? 23.157  16.873  94.069  1.00 18.35 ?  873  ILE B N     1 
ATOM   15685 C CA    . ILE B 1 875  ? 23.865  17.427  92.919  1.00 17.50 ?  873  ILE B CA    1 
ATOM   15686 C C     . ILE B 1 875  ? 24.393  16.274  92.079  1.00 21.47 ?  873  ILE B C     1 
ATOM   15687 O O     . ILE B 1 875  ? 25.084  15.390  92.597  1.00 22.44 ?  873  ILE B O     1 
ATOM   15688 C CB    . ILE B 1 875  ? 25.014  18.355  93.343  1.00 20.55 ?  873  ILE B CB    1 
ATOM   15689 C CG1   . ILE B 1 875  ? 24.483  19.649  93.954  1.00 26.86 ?  873  ILE B CG1   1 
ATOM   15690 C CG2   . ILE B 1 875  ? 25.888  18.684  92.143  1.00 20.44 ?  873  ILE B CG2   1 
ATOM   15691 C CD1   . ILE B 1 875  ? 24.115  19.533  95.404  1.00 30.95 ?  873  ILE B CD1   1 
ATOM   15692 N N     . GLY B 1 876  ? 24.075  16.279  90.788  1.00 17.61 ?  874  GLY B N     1 
ATOM   15693 C CA    . GLY B 1 876  ? 24.588  15.223  89.935  1.00 19.94 ?  874  GLY B CA    1 
ATOM   15694 C C     . GLY B 1 876  ? 24.113  15.363  88.505  1.00 19.42 ?  874  GLY B C     1 
ATOM   15695 O O     . GLY B 1 876  ? 23.476  16.355  88.125  1.00 16.52 ?  874  GLY B O     1 
ATOM   15696 N N     . ARG B 1 877  ? 24.449  14.343  87.710  1.00 20.35 ?  875  ARG B N     1 
ATOM   15697 C CA    . ARG B 1 877  ? 23.990  14.276  86.329  1.00 19.26 ?  875  ARG B CA    1 
ATOM   15698 C C     . ARG B 1 877  ? 22.468  14.267  86.311  1.00 18.43 ?  875  ARG B C     1 
ATOM   15699 O O     . ARG B 1 877  ? 21.836  13.531  87.071  1.00 21.37 ?  875  ARG B O     1 
ATOM   15700 C CB    . ARG B 1 877  ? 24.544  13.024  85.643  1.00 21.08 ?  875  ARG B CB    1 
ATOM   15701 C CG    . ARG B 1 877  ? 24.360  13.035  84.132  1.00 21.45 ?  875  ARG B CG    1 
ATOM   15702 C CD    . ARG B 1 877  ? 25.061  11.845  83.483  1.00 26.35 ?  875  ARG B CD    1 
ATOM   15703 N NE    . ARG B 1 877  ? 24.163  10.715  83.306  1.00 30.37 ?  875  ARG B NE    1 
ATOM   15704 C CZ    . ARG B 1 877  ? 24.513  9.571   82.735  1.00 34.74 ?  875  ARG B CZ    1 
ATOM   15705 N NH1   . ARG B 1 877  ? 25.746  9.364   82.302  1.00 28.73 ?  875  ARG B NH1   1 
ATOM   15706 N NH2   . ARG B 1 877  ? 23.600  8.613   82.592  1.00 31.49 ?  875  ARG B NH2   1 
ATOM   15707 N N     . THR B 1 878  ? 21.880  15.082  85.442  1.00 17.80 ?  876  THR B N     1 
ATOM   15708 C CA    . THR B 1 878  ? 20.472  15.439  85.563  1.00 17.43 ?  876  THR B CA    1 
ATOM   15709 C C     . THR B 1 878  ? 19.506  14.462  84.891  1.00 20.28 ?  876  THR B C     1 
ATOM   15710 O O     . THR B 1 878  ? 18.340  14.816  84.689  1.00 20.89 ?  876  THR B O     1 
ATOM   15711 C CB    . THR B 1 878  ? 20.242  16.849  85.016  1.00 18.64 ?  876  THR B CB    1 
ATOM   15712 O OG1   . THR B 1 878  ? 20.811  16.968  83.709  1.00 20.36 ?  876  THR B OG1   1 
ATOM   15713 C CG2   . THR B 1 878  ? 20.886  17.871  85.923  1.00 20.50 ?  876  THR B CG2   1 
ATOM   15714 N N     . ASP B 1 879  ? 19.915  13.232  84.589  1.00 21.64 ?  877  ASP B N     1 
ATOM   15715 C CA    . ASP B 1 879  ? 18.937  12.277  84.080  1.00 19.66 ?  877  ASP B CA    1 
ATOM   15716 C C     . ASP B 1 879  ? 18.345  11.411  85.187  1.00 22.00 ?  877  ASP B C     1 
ATOM   15717 O O     . ASP B 1 879  ? 17.882  10.293  84.930  1.00 20.82 ?  877  ASP B O     1 
ATOM   15718 C CB    . ASP B 1 879  ? 19.537  11.427  82.957  1.00 24.52 ?  877  ASP B CB    1 
ATOM   15719 C CG    . ASP B 1 879  ? 20.709  10.592  83.409  1.00 25.90 ?  877  ASP B CG    1 
ATOM   15720 O OD1   . ASP B 1 879  ? 21.411  10.985  84.370  1.00 28.85 ?  877  ASP B OD1   1 
ATOM   15721 O OD2   . ASP B 1 879  ? 20.931  9.532   82.778  1.00 27.57 ?  877  ASP B OD2   1 
ATOM   15722 N N     . ARG B 1 880  ? 18.322  11.928  86.415  1.00 20.29 ?  878  ARG B N     1 
ATOM   15723 C CA    . ARG B 1 880  ? 17.599  11.316  87.523  1.00 18.87 ?  878  ARG B CA    1 
ATOM   15724 C C     . ARG B 1 880  ? 16.697  12.371  88.151  1.00 19.28 ?  878  ARG B C     1 
ATOM   15725 O O     . ARG B 1 880  ? 17.144  13.489  88.425  1.00 19.07 ?  878  ARG B O     1 
ATOM   15726 C CB    . ARG B 1 880  ? 18.558  10.742  88.568  1.00 21.80 ?  878  ARG B CB    1 
ATOM   15727 C CG    . ARG B 1 880  ? 19.430  9.629   88.010  1.00 24.08 ?  878  ARG B CG    1 
ATOM   15728 C CD    . ARG B 1 880  ? 20.233  8.939   89.095  1.00 32.83 ?  878  ARG B CD    1 
ATOM   15729 N NE    . ARG B 1 880  ? 21.198  8.031   88.489  1.00 46.23 ?  878  ARG B NE    1 
ATOM   15730 C CZ    . ARG B 1 880  ? 21.756  6.999   89.107  1.00 45.79 ?  878  ARG B CZ    1 
ATOM   15731 N NH1   . ARG B 1 880  ? 21.462  6.704   90.363  1.00 49.71 ?  878  ARG B NH1   1 
ATOM   15732 N NH2   . ARG B 1 880  ? 22.624  6.239   88.444  1.00 46.62 ?  878  ARG B NH2   1 
ATOM   15733 N N     . LEU B 1 881  ? 15.429  12.004  88.369  1.00 17.39 ?  879  LEU B N     1 
ATOM   15734 C CA    . LEU B 1 881  ? 14.457  12.915  88.972  1.00 16.84 ?  879  LEU B CA    1 
ATOM   15735 C C     . LEU B 1 881  ? 14.919  13.433  90.331  1.00 17.72 ?  879  LEU B C     1 
ATOM   15736 O O     . LEU B 1 881  ? 14.547  14.543  90.735  1.00 17.79 ?  879  LEU B O     1 
ATOM   15737 C CB    . LEU B 1 881  ? 13.120  12.193  89.113  1.00 19.33 ?  879  LEU B CB    1 
ATOM   15738 C CG    . LEU B 1 881  ? 11.931  12.962  89.688  1.00 17.24 ?  879  LEU B CG    1 
ATOM   15739 C CD1   . LEU B 1 881  ? 11.430  13.940  88.642  1.00 18.11 ?  879  LEU B CD1   1 
ATOM   15740 C CD2   . LEU B 1 881  ? 10.849  11.979  90.087  1.00 18.06 ?  879  LEU B CD2   1 
ATOM   15741 N N     . SER B 1 882  ? 15.730  12.653  91.046  1.00 15.89 ?  880  SER B N     1 
ATOM   15742 C CA    . SER B 1 882  ? 16.176  13.035  92.377  1.00 15.07 ?  880  SER B CA    1 
ATOM   15743 C C     . SER B 1 882  ? 17.220  14.140  92.373  1.00 16.83 ?  880  SER B C     1 
ATOM   15744 O O     . SER B 1 882  ? 17.582  14.618  93.449  1.00 18.13 ?  880  SER B O     1 
ATOM   15745 C CB    . SER B 1 882  ? 16.745  11.815  93.093  1.00 18.27 ?  880  SER B CB    1 
ATOM   15746 O OG    . SER B 1 882  ? 17.904  11.357  92.414  1.00 22.30 ?  880  SER B OG    1 
ATOM   15747 N N     . VAL B 1 883  ? 17.729  14.550  91.220  1.00 16.77 ?  881  VAL B N     1 
ATOM   15748 C CA    . VAL B 1 883  ? 18.767  15.575  91.202  1.00 16.61 ?  881  VAL B CA    1 
ATOM   15749 C C     . VAL B 1 883  ? 18.125  16.951  91.281  1.00 16.47 ?  881  VAL B C     1 
ATOM   15750 O O     . VAL B 1 883  ? 17.212  17.269  90.512  1.00 17.91 ?  881  VAL B O     1 
ATOM   15751 C CB    . VAL B 1 883  ? 19.646  15.444  89.951  1.00 17.62 ?  881  VAL B CB    1 
ATOM   15752 C CG1   . VAL B 1 883  ? 20.533  16.673  89.800  1.00 18.08 ?  881  VAL B CG1   1 
ATOM   15753 C CG2   . VAL B 1 883  ? 20.485  14.184  90.055  1.00 18.93 ?  881  VAL B CG2   1 
ATOM   15754 N N     . ASP B 1 884  ? 18.617  17.772  92.207  1.00 15.35 ?  882  ASP B N     1 
ATOM   15755 C CA    . ASP B 1 884  ? 18.141  19.139  92.378  1.00 14.98 ?  882  ASP B CA    1 
ATOM   15756 C C     . ASP B 1 884  ? 18.976  20.152  91.617  1.00 20.73 ?  882  ASP B C     1 
ATOM   15757 O O     . ASP B 1 884  ? 18.438  21.155  91.137  1.00 19.23 ?  882  ASP B O     1 
ATOM   15758 C CB    . ASP B 1 884  ? 18.167  19.517  93.855  1.00 16.08 ?  882  ASP B CB    1 
ATOM   15759 C CG    . ASP B 1 884  ? 17.363  18.574  94.701  1.00 18.32 ?  882  ASP B CG    1 
ATOM   15760 O OD1   . ASP B 1 884  ? 16.154  18.436  94.425  1.00 18.52 ?  882  ASP B OD1   1 
ATOM   15761 O OD2   . ASP B 1 884  ? 17.944  17.969  95.624  1.00 17.89 ?  882  ASP B OD2   1 
ATOM   15762 N N     . VAL B 1 885  ? 20.288  19.946  91.555  1.00 17.80 ?  883  VAL B N     1 
ATOM   15763 C CA    . VAL B 1 885  ? 21.213  20.884  90.928  1.00 17.55 ?  883  VAL B CA    1 
ATOM   15764 C C     . VAL B 1 885  ? 22.146  20.085  90.036  1.00 14.99 ?  883  VAL B C     1 
ATOM   15765 O O     . VAL B 1 885  ? 22.781  19.132  90.498  1.00 16.51 ?  883  VAL B O     1 
ATOM   15766 C CB    . VAL B 1 885  ? 22.015  21.685  91.969  1.00 20.19 ?  883  VAL B CB    1 
ATOM   15767 C CG1   . VAL B 1 885  ? 22.964  22.671  91.279  1.00 22.50 ?  883  VAL B CG1   1 
ATOM   15768 C CG2   . VAL B 1 885  ? 21.069  22.430  92.914  1.00 21.47 ?  883  VAL B CG2   1 
ATOM   15769 N N     . GLY B 1 886  ? 22.209  20.460  88.760  1.00 15.46 ?  884  GLY B N     1 
ATOM   15770 C CA    . GLY B 1 886  ? 23.091  19.825  87.817  1.00 15.69 ?  884  GLY B CA    1 
ATOM   15771 C C     . GLY B 1 886  ? 24.395  20.573  87.647  1.00 15.30 ?  884  GLY B C     1 
ATOM   15772 O O     . GLY B 1 886  ? 24.789  21.402  88.477  1.00 15.28 ?  884  GLY B O     1 
ATOM   15773 N N     . PRO B 1 887  ? 25.079  20.298  86.541  1.00 15.17 ?  885  PRO B N     1 
ATOM   15774 C CA    . PRO B 1 887  ? 26.397  20.890  86.293  1.00 15.85 ?  885  PRO B CA    1 
ATOM   15775 C C     . PRO B 1 887  ? 26.309  22.324  85.779  1.00 15.14 ?  885  PRO B C     1 
ATOM   15776 O O     . PRO B 1 887  ? 25.272  22.775  85.284  1.00 15.11 ?  885  PRO B O     1 
ATOM   15777 C CB    . PRO B 1 887  ? 26.982  19.965  85.217  1.00 15.19 ?  885  PRO B CB    1 
ATOM   15778 C CG    . PRO B 1 887  ? 25.750  19.532  84.434  1.00 15.53 ?  885  PRO B CG    1 
ATOM   15779 C CD    . PRO B 1 887  ? 24.670  19.359  85.483  1.00 16.07 ?  885  PRO B CD    1 
ATOM   15780 N N     . VAL B 1 888  ? 27.449  23.030  85.877  1.00 15.12 ?  886  VAL B N     1 
ATOM   15781 C CA    . VAL B 1 888  ? 27.631  24.251  85.098  1.00 14.58 ?  886  VAL B CA    1 
ATOM   15782 C C     . VAL B 1 888  ? 28.064  23.875  83.682  1.00 13.99 ?  886  VAL B C     1 
ATOM   15783 O O     . VAL B 1 888  ? 28.457  22.742  83.404  1.00 15.44 ?  886  VAL B O     1 
ATOM   15784 C CB    . VAL B 1 888  ? 28.618  25.227  85.764  1.00 15.21 ?  886  VAL B CB    1 
ATOM   15785 C CG1   . VAL B 1 888  ? 28.102  25.624  87.146  1.00 15.79 ?  886  VAL B CG1   1 
ATOM   15786 C CG2   . VAL B 1 888  ? 30.009  24.637  85.868  1.00 18.02 ?  886  VAL B CG2   1 
ATOM   15787 N N     . ILE B 1 889  ? 27.957  24.838  82.767  1.00 14.92 ?  887  ILE B N     1 
ATOM   15788 C CA    . ILE B 1 889  ? 27.891  24.488  81.346  1.00 14.96 ?  887  ILE B CA    1 
ATOM   15789 C C     . ILE B 1 889  ? 29.239  24.000  80.802  1.00 15.52 ?  887  ILE B C     1 
ATOM   15790 O O     . ILE B 1 889  ? 29.277  23.115  79.938  1.00 16.01 ?  887  ILE B O     1 
ATOM   15791 C CB    . ILE B 1 889  ? 27.340  25.684  80.549  1.00 15.79 ?  887  ILE B CB    1 
ATOM   15792 C CG1   . ILE B 1 889  ? 27.134  25.314  79.070  1.00 15.48 ?  887  ILE B CG1   1 
ATOM   15793 C CG2   . ILE B 1 889  ? 28.216  26.923  80.729  1.00 16.55 ?  887  ILE B CG2   1 
ATOM   15794 C CD1   . ILE B 1 889  ? 26.031  24.307  78.846  1.00 17.08 ?  887  ILE B CD1   1 
ATOM   15795 N N     . THR B 1 890  ? 30.357  24.558  81.279  1.00 17.23 ?  888  THR B N     1 
ATOM   15796 C CA    . THR B 1 890  ? 31.683  24.231  80.747  1.00 16.03 ?  888  THR B CA    1 
ATOM   15797 C C     . THR B 1 890  ? 32.713  24.233  81.864  1.00 17.31 ?  888  THR B C     1 
ATOM   15798 O O     . THR B 1 890  ? 32.489  24.781  82.946  1.00 17.67 ?  888  THR B O     1 
ATOM   15799 C CB    . THR B 1 890  ? 32.179  25.227  79.684  1.00 19.84 ?  888  THR B CB    1 
ATOM   15800 O OG1   . THR B 1 890  ? 32.219  26.547  80.236  1.00 18.64 ?  888  THR B OG1   1 
ATOM   15801 C CG2   . THR B 1 890  ? 31.294  25.223  78.445  1.00 17.97 ?  888  THR B CG2   1 
ATOM   15802 N N     . SER B 1 891  ? 33.885  23.653  81.563  1.00 18.67 ?  889  SER B N     1 
ATOM   15803 C CA    . SER B 1 891  ? 35.017  23.761  82.484  1.00 17.54 ?  889  SER B CA    1 
ATOM   15804 C C     . SER B 1 891  ? 35.488  25.207  82.635  1.00 23.55 ?  889  SER B C     1 
ATOM   15805 O O     . SER B 1 891  ? 35.925  25.600  83.724  1.00 21.74 ?  889  SER B O     1 
ATOM   15806 C CB    . SER B 1 891  ? 36.170  22.863  82.015  1.00 22.03 ?  889  SER B CB    1 
ATOM   15807 O OG    . SER B 1 891  ? 36.624  23.243  80.731  1.00 33.34 ?  889  SER B OG    1 
ATOM   15808 N N     . GLU B 1 892  ? 35.419  26.011  81.569  1.00 20.91 ?  890  GLU B N     1 
ATOM   15809 C CA    . GLU B 1 892  ? 35.796  27.418  81.686  1.00 20.86 ?  890  GLU B CA    1 
ATOM   15810 C C     . GLU B 1 892  ? 34.869  28.155  82.641  1.00 23.58 ?  890  GLU B C     1 
ATOM   15811 O O     . GLU B 1 892  ? 35.321  28.965  83.458  1.00 24.42 ?  890  GLU B O     1 
ATOM   15812 C CB    . GLU B 1 892  ? 35.789  28.091  80.314  1.00 26.21 ?  890  GLU B CB    1 
ATOM   15813 N N     . ALA B 1 893  ? 33.567  27.893  82.549  1.00 20.14 ?  891  ALA B N     1 
ATOM   15814 C CA    . ALA B 1 893  ? 32.634  28.500  83.489  1.00 19.60 ?  891  ALA B CA    1 
ATOM   15815 C C     . ALA B 1 893  ? 32.958  28.072  84.911  1.00 22.75 ?  891  ALA B C     1 
ATOM   15816 O O     . ALA B 1 893  ? 32.984  28.902  85.828  1.00 21.93 ?  891  ALA B O     1 
ATOM   15817 C CB    . ALA B 1 893  ? 31.200  28.118  83.118  1.00 19.65 ?  891  ALA B CB    1 
ATOM   15818 N N     . LYS B 1 894  ? 33.214  26.777  85.106  1.00 20.27 ?  892  LYS B N     1 
ATOM   15819 C CA    . LYS B 1 894  ? 33.561  26.269  86.429  1.00 20.19 ?  892  LYS B CA    1 
ATOM   15820 C C     . LYS B 1 894  ? 34.813  26.950  86.972  1.00 24.10 ?  892  LYS B C     1 
ATOM   15821 O O     . LYS B 1 894  ? 34.844  27.390  88.129  1.00 23.65 ?  892  LYS B O     1 
ATOM   15822 C CB    . LYS B 1 894  ? 33.742  24.751  86.367  1.00 19.41 ?  892  LYS B CB    1 
ATOM   15823 C CG    . LYS B 1 894  ? 34.260  24.124  87.651  1.00 21.04 ?  892  LYS B CG    1 
ATOM   15824 C CD    . LYS B 1 894  ? 34.309  22.605  87.539  1.00 21.69 ?  892  LYS B CD    1 
ATOM   15825 C CE    . LYS B 1 894  ? 34.889  21.981  88.808  1.00 30.75 ?  892  LYS B CE    1 
ATOM   15826 N NZ    . LYS B 1 894  ? 34.805  20.495  88.802  1.00 37.35 ?  892  LYS B NZ    1 
ATOM   15827 N N     . ASP B 1 895  ? 35.852  27.074  86.143  1.00 21.34 ?  893  ASP B N     1 
ATOM   15828 C CA    . ASP B 1 895  ? 37.086  27.699  86.610  1.00 23.81 ?  893  ASP B CA    1 
ATOM   15829 C C     . ASP B 1 895  ? 36.864  29.155  87.009  1.00 23.78 ?  893  ASP B C     1 
ATOM   15830 O O     . ASP B 1 895  ? 37.443  29.631  87.996  1.00 27.70 ?  893  ASP B O     1 
ATOM   15831 C CB    . ASP B 1 895  ? 38.165  27.606  85.532  1.00 26.67 ?  893  ASP B CB    1 
ATOM   15832 C CG    . ASP B 1 895  ? 38.664  26.196  85.331  1.00 27.67 ?  893  ASP B CG    1 
ATOM   15833 O OD1   . ASP B 1 895  ? 38.360  25.324  86.173  1.00 31.44 ?  893  ASP B OD1   1 
ATOM   15834 O OD2   . ASP B 1 895  ? 39.362  25.962  84.320  1.00 31.94 ?  893  ASP B OD2   1 
ATOM   15835 N N     . ASN B 1 896  ? 36.056  29.886  86.240  1.00 23.29 ?  894  ASN B N     1 
ATOM   15836 C CA    . ASN B 1 896  ? 35.812  31.290  86.543  1.00 23.48 ?  894  ASN B CA    1 
ATOM   15837 C C     . ASN B 1 896  ? 35.034  31.447  87.847  1.00 24.19 ?  894  ASN B C     1 
ATOM   15838 O O     . ASN B 1 896  ? 35.333  32.342  88.648  1.00 25.41 ?  894  ASN B O     1 
ATOM   15839 C CB    . ASN B 1 896  ? 35.070  31.952  85.383  1.00 26.29 ?  894  ASN B CB    1 
ATOM   15840 C CG    . ASN B 1 896  ? 34.857  33.431  85.599  1.00 34.91 ?  894  ASN B CG    1 
ATOM   15841 O OD1   . ASN B 1 896  ? 33.776  33.864  86.001  1.00 37.70 ?  894  ASN B OD1   1 
ATOM   15842 N ND2   . ASN B 1 896  ? 35.896  34.219  85.344  1.00 42.55 ?  894  ASN B ND2   1 
ATOM   15843 N N     . ILE B 1 897  ? 34.040  30.583  88.076  1.00 21.73 ?  895  ILE B N     1 
ATOM   15844 C CA    . ILE B 1 897  ? 33.282  30.605  89.327  1.00 24.88 ?  895  ILE B CA    1 
ATOM   15845 C C     . ILE B 1 897  ? 34.185  30.249  90.499  1.00 27.23 ?  895  ILE B C     1 
ATOM   15846 O O     . ILE B 1 897  ? 34.147  30.897  91.553  1.00 21.94 ?  895  ILE B O     1 
ATOM   15847 C CB    . ILE B 1 897  ? 32.075  29.647  89.240  1.00 19.95 ?  895  ILE B CB    1 
ATOM   15848 C CG1   . ILE B 1 897  ? 31.083  30.108  88.172  1.00 20.66 ?  895  ILE B CG1   1 
ATOM   15849 C CG2   . ILE B 1 897  ? 31.368  29.495  90.603  1.00 21.40 ?  895  ILE B CG2   1 
ATOM   15850 C CD1   . ILE B 1 897  ? 30.164  28.995  87.723  1.00 18.62 ?  895  ILE B CD1   1 
ATOM   15851 N N     . GLU B 1 898  ? 35.007  29.211  90.338  1.00 24.64 ?  896  GLU B N     1 
ATOM   15852 C CA    . GLU B 1 898  ? 35.888  28.794  91.423  1.00 26.74 ?  896  GLU B CA    1 
ATOM   15853 C C     . GLU B 1 898  ? 36.974  29.824  91.703  1.00 29.30 ?  896  GLU B C     1 
ATOM   15854 O O     . GLU B 1 898  ? 37.374  29.988  92.862  1.00 27.68 ?  896  GLU B O     1 
ATOM   15855 C CB    . GLU B 1 898  ? 36.489  27.426  91.102  1.00 25.90 ?  896  GLU B CB    1 
ATOM   15856 C CG    . GLU B 1 898  ? 35.496  26.293  91.325  1.00 25.70 ?  896  GLU B CG    1 
ATOM   15857 C CD    . GLU B 1 898  ? 36.011  24.946  90.876  1.00 34.04 ?  896  GLU B CD    1 
ATOM   15858 O OE1   . GLU B 1 898  ? 37.034  24.899  90.157  1.00 36.96 ?  896  GLU B OE1   1 
ATOM   15859 O OE2   . GLU B 1 898  ? 35.385  23.932  91.250  1.00 39.27 ?  896  GLU B OE2   1 
ATOM   15860 N N     . LYS B 1 899  ? 37.450  30.544  90.678  1.00 26.74 ?  897  LYS B N     1 
ATOM   15861 C CA    . LYS B 1 899  ? 38.399  31.621  90.944  1.00 27.39 ?  897  LYS B CA    1 
ATOM   15862 C C     . LYS B 1 899  ? 37.801  32.655  91.887  1.00 29.91 ?  897  LYS B C     1 
ATOM   15863 O O     . LYS B 1 899  ? 38.515  33.214  92.725  1.00 32.44 ?  897  LYS B O     1 
ATOM   15864 C CB    . LYS B 1 899  ? 38.845  32.293  89.644  1.00 31.07 ?  897  LYS B CB    1 
ATOM   15865 C CG    . LYS B 1 899  ? 39.828  33.444  89.871  1.00 36.56 ?  897  LYS B CG    1 
ATOM   15866 C CD    . LYS B 1 899  ? 40.484  33.935  88.587  1.00 40.16 ?  897  LYS B CD    1 
ATOM   15867 C CE    . LYS B 1 899  ? 39.665  35.021  87.905  1.00 45.85 ?  897  LYS B CE    1 
ATOM   15868 N NZ    . LYS B 1 899  ? 40.510  35.852  86.988  1.00 48.57 ?  897  LYS B NZ    1 
ATOM   15869 N N     . HIS B 1 900  ? 36.493  32.905  91.780  1.00 25.19 ?  898  HIS B N     1 
ATOM   15870 C CA    . HIS B 1 900  ? 35.840  33.851  92.679  1.00 27.12 ?  898  HIS B CA    1 
ATOM   15871 C C     . HIS B 1 900  ? 35.696  33.275  94.084  1.00 27.71 ?  898  HIS B C     1 
ATOM   15872 O O     . HIS B 1 900  ? 35.958  33.965  95.078  1.00 26.63 ?  898  HIS B O     1 
ATOM   15873 C CB    . HIS B 1 900  ? 34.473  34.242  92.115  1.00 24.95 ?  898  HIS B CB    1 
ATOM   15874 C CG    . HIS B 1 900  ? 33.643  35.052  93.059  1.00 24.68 ?  898  HIS B CG    1 
ATOM   15875 N ND1   . HIS B 1 900  ? 33.849  36.399  93.260  1.00 23.73 ?  898  HIS B ND1   1 
ATOM   15876 C CD2   . HIS B 1 900  ? 32.612  34.702  93.864  1.00 23.99 ?  898  HIS B CD2   1 
ATOM   15877 C CE1   . HIS B 1 900  ? 32.968  36.850  94.137  1.00 21.62 ?  898  HIS B CE1   1 
ATOM   15878 N NE2   . HIS B 1 900  ? 32.211  35.839  94.523  1.00 24.16 ?  898  HIS B NE2   1 
ATOM   15879 N N     . ILE B 1 901  ? 35.259  32.018  94.187  1.00 25.37 ?  899  ILE B N     1 
ATOM   15880 C CA    . ILE B 1 901  ? 35.025  31.409  95.496  1.00 24.60 ?  899  ILE B CA    1 
ATOM   15881 C C     . ILE B 1 901  ? 36.318  31.359  96.296  1.00 30.22 ?  899  ILE B C     1 
ATOM   15882 O O     . ILE B 1 901  ? 36.334  31.644  97.500  1.00 27.66 ?  899  ILE B O     1 
ATOM   15883 C CB    . ILE B 1 901  ? 34.412  30.005  95.340  1.00 25.84 ?  899  ILE B CB    1 
ATOM   15884 C CG1   . ILE B 1 901  ? 33.046  30.081  94.651  1.00 22.62 ?  899  ILE B CG1   1 
ATOM   15885 C CG2   . ILE B 1 901  ? 34.295  29.314  96.697  1.00 25.84 ?  899  ILE B CG2   1 
ATOM   15886 C CD1   . ILE B 1 901  ? 32.375  28.725  94.491  1.00 23.53 ?  899  ILE B CD1   1 
ATOM   15887 N N     . GLU B 1 902  ? 37.423  31.006  95.639  1.00 28.71 ?  900  GLU B N     1 
ATOM   15888 C CA    . GLU B 1 902  ? 38.705  30.949  96.337  1.00 27.04 ?  900  GLU B CA    1 
ATOM   15889 C C     . GLU B 1 902  ? 39.209  32.340  96.692  1.00 31.99 ?  900  GLU B C     1 
ATOM   15890 O O     . GLU B 1 902  ? 39.810  32.532  97.754  1.00 36.24 ?  900  GLU B O     1 
ATOM   15891 C CB    . GLU B 1 902  ? 39.731  30.204  95.485  1.00 34.12 ?  900  GLU B CB    1 
ATOM   15892 C CG    . GLU B 1 902  ? 39.418  28.733  95.364  1.00 35.59 ?  900  GLU B CG    1 
ATOM   15893 C CD    . GLU B 1 902  ? 39.131  28.113  96.712  1.00 39.72 ?  900  GLU B CD    1 
ATOM   15894 O OE1   . GLU B 1 902  ? 40.005  28.213  97.600  1.00 40.90 ?  900  GLU B OE1   1 
ATOM   15895 O OE2   . GLU B 1 902  ? 38.030  27.547  96.888  1.00 39.88 ?  900  GLU B OE2   1 
ATOM   15896 N N     . ARG B 1 903  ? 38.986  33.321  95.817  1.00 28.55 ?  901  ARG B N     1 
ATOM   15897 C CA    . ARG B 1 903  ? 39.358  34.692  96.141  1.00 34.05 ?  901  ARG B CA    1 
ATOM   15898 C C     . ARG B 1 903  ? 38.606  35.187  97.373  1.00 36.50 ?  901  ARG B C     1 
ATOM   15899 O O     . ARG B 1 903  ? 39.182  35.874  98.226  1.00 34.81 ?  901  ARG B O     1 
ATOM   15900 C CB    . ARG B 1 903  ? 39.092  35.600  94.941  1.00 35.87 ?  901  ARG B CB    1 
ATOM   15901 C CG    . ARG B 1 903  ? 39.670  36.999  95.055  1.00 40.46 ?  901  ARG B CG    1 
ATOM   15902 C CD    . ARG B 1 903  ? 38.829  37.969  94.250  1.00 48.07 ?  901  ARG B CD    1 
ATOM   15903 N NE    . ARG B 1 903  ? 39.387  39.315  94.216  1.00 59.52 ?  901  ARG B NE    1 
ATOM   15904 C CZ    . ARG B 1 903  ? 38.661  40.422  94.115  1.00 57.04 ?  901  ARG B CZ    1 
ATOM   15905 N NH1   . ARG B 1 903  ? 37.338  40.382  94.085  1.00 56.47 ?  901  ARG B NH1   1 
ATOM   15906 N NH2   . ARG B 1 903  ? 39.278  41.598  94.050  1.00 58.70 ?  901  ARG B NH2   1 
ATOM   15907 N N     . MET B 1 904  ? 37.320  34.833  97.493  1.00 35.18 ?  902  MET B N     1 
ATOM   15908 C CA    . MET B 1 904  ? 36.552  35.191  98.685  1.00 34.58 ?  902  MET B CA    1 
ATOM   15909 C C     . MET B 1 904  ? 37.039  34.414  99.902  1.00 37.21 ?  902  MET B C     1 
ATOM   15910 O O     . MET B 1 904  ? 37.186  34.976  100.998 1.00 32.22 ?  902  MET B O     1 
ATOM   15911 C CB    . MET B 1 904  ? 35.058  34.930  98.458  1.00 29.54 ?  902  MET B CB    1 
ATOM   15912 C CG    . MET B 1 904  ? 34.423  35.742  97.341  1.00 32.60 ?  902  MET B CG    1 
ATOM   15913 S SD    . MET B 1 904  ? 34.479  37.518  97.636  1.00 36.46 ?  902  MET B SD    1 
ATOM   15914 C CE    . MET B 1 904  ? 35.748  38.012  96.467  1.00 37.12 ?  902  MET B CE    1 
ATOM   15915 N N     . ARG B 1 905  ? 37.268  33.110  99.731  1.00 37.32 ?  903  ARG B N     1 
ATOM   15916 C CA    . ARG B 1 905  ? 37.754  32.290  100.834 1.00 35.22 ?  903  ARG B CA    1 
ATOM   15917 C C     . ARG B 1 905  ? 39.118  32.764  101.313 1.00 38.35 ?  903  ARG B C     1 
ATOM   15918 O O     . ARG B 1 905  ? 39.403  32.744  102.516 1.00 40.76 ?  903  ARG B O     1 
ATOM   15919 C CB    . ARG B 1 905  ? 37.822  30.823  100.411 1.00 37.81 ?  903  ARG B CB    1 
ATOM   15920 C CG    . ARG B 1 905  ? 37.795  29.863  101.579 1.00 39.48 ?  903  ARG B CG    1 
ATOM   15921 C CD    . ARG B 1 905  ? 38.231  28.476  101.167 1.00 42.22 ?  903  ARG B CD    1 
ATOM   15922 N NE    . ARG B 1 905  ? 37.393  27.916  100.115 1.00 32.02 ?  903  ARG B NE    1 
ATOM   15923 C CZ    . ARG B 1 905  ? 36.330  27.155  100.333 1.00 34.12 ?  903  ARG B CZ    1 
ATOM   15924 N NH1   . ARG B 1 905  ? 35.908  26.894  101.560 1.00 33.31 ?  903  ARG B NH1   1 
ATOM   15925 N NH2   . ARG B 1 905  ? 35.679  26.637  99.295  1.00 29.83 ?  903  ARG B NH2   1 
ATOM   15926 N N     . GLY B 1 906  ? 39.972  33.202  100.385 1.00 35.54 ?  904  GLY B N     1 
ATOM   15927 C CA    . GLY B 1 906  ? 41.270  33.726  100.759 1.00 42.31 ?  904  GLY B CA    1 
ATOM   15928 C C     . GLY B 1 906  ? 41.198  34.964  101.621 1.00 39.62 ?  904  GLY B C     1 
ATOM   15929 O O     . GLY B 1 906  ? 42.133  35.235  102.379 1.00 36.15 ?  904  GLY B O     1 
ATOM   15930 N N     . LEU B 1 907  ? 40.103  35.718  101.531 1.00 38.05 ?  905  LEU B N     1 
ATOM   15931 C CA    . LEU B 1 907  ? 39.902  36.914  102.336 1.00 37.84 ?  905  LEU B CA    1 
ATOM   15932 C C     . LEU B 1 907  ? 39.286  36.605  103.696 1.00 32.67 ?  905  LEU B C     1 
ATOM   15933 O O     . LEU B 1 907  ? 38.970  37.534  104.443 1.00 43.33 ?  905  LEU B O     1 
ATOM   15934 C CB    . LEU B 1 907  ? 39.027  37.916  101.572 1.00 40.15 ?  905  LEU B CB    1 
ATOM   15935 C CG    . LEU B 1 907  ? 39.568  38.392  100.217 1.00 39.74 ?  905  LEU B CG    1 
ATOM   15936 C CD1   . LEU B 1 907  ? 38.568  39.268  99.467  1.00 41.63 ?  905  LEU B CD1   1 
ATOM   15937 C CD2   . LEU B 1 907  ? 40.896  39.115  100.388 1.00 41.41 ?  905  LEU B CD2   1 
ATOM   15938 N N     . GLY B 1 908  ? 39.106  35.327  104.027 1.00 35.73 ?  906  GLY B N     1 
ATOM   15939 C CA    . GLY B 1 908  ? 38.594  34.924  105.320 1.00 32.90 ?  906  GLY B CA    1 
ATOM   15940 C C     . GLY B 1 908  ? 37.091  34.959  105.467 1.00 37.65 ?  906  GLY B C     1 
ATOM   15941 O O     . GLY B 1 908  ? 36.595  34.875  106.598 1.00 35.78 ?  906  GLY B O     1 
ATOM   15942 N N     . ARG B 1 909  ? 36.350  35.075  104.369 1.00 35.85 ?  907  ARG B N     1 
ATOM   15943 C CA    . ARG B 1 909  ? 34.898  35.129  104.439 1.00 25.70 ?  907  ARG B CA    1 
ATOM   15944 C C     . ARG B 1 909  ? 34.344  33.723  104.626 1.00 26.96 ?  907  ARG B C     1 
ATOM   15945 O O     . ARG B 1 909  ? 34.922  32.747  104.136 1.00 31.18 ?  907  ARG B O     1 
ATOM   15946 C CB    . ARG B 1 909  ? 34.363  35.798  103.178 1.00 31.03 ?  907  ARG B CB    1 
ATOM   15947 C CG    . ARG B 1 909  ? 35.154  37.072  102.940 1.00 36.59 ?  907  ARG B CG    1 
ATOM   15948 C CD    . ARG B 1 909  ? 34.751  37.854  101.730 1.00 39.10 ?  907  ARG B CD    1 
ATOM   15949 N NE    . ARG B 1 909  ? 35.059  39.266  101.936 1.00 43.76 ?  907  ARG B NE    1 
ATOM   15950 C CZ    . ARG B 1 909  ? 35.241  40.150  100.964 1.00 46.20 ?  907  ARG B CZ    1 
ATOM   15951 N NH1   . ARG B 1 909  ? 35.190  39.797  99.689  1.00 41.36 ?  907  ARG B NH1   1 
ATOM   15952 N NH2   . ARG B 1 909  ? 35.485  41.419  101.280 1.00 39.74 ?  907  ARG B NH2   1 
ATOM   15953 N N     . LYS B 1 910  ? 33.257  33.614  105.387 1.00 23.03 ?  908  LYS B N     1 
ATOM   15954 C CA    . LYS B 1 910  ? 32.683  32.304  105.669 1.00 26.34 ?  908  LYS B CA    1 
ATOM   15955 C C     . LYS B 1 910  ? 32.055  31.729  104.404 1.00 28.36 ?  908  LYS B C     1 
ATOM   15956 O O     . LYS B 1 910  ? 31.212  32.374  103.769 1.00 26.76 ?  908  LYS B O     1 
ATOM   15957 C CB    . LYS B 1 910  ? 31.637  32.391  106.783 1.00 27.06 ?  908  LYS B CB    1 
ATOM   15958 C CG    . LYS B 1 910  ? 32.176  32.730  108.167 1.00 34.36 ?  908  LYS B CG    1 
ATOM   15959 C CD    . LYS B 1 910  ? 31.083  32.597  109.233 1.00 39.12 ?  908  LYS B CD    1 
ATOM   15960 C CE    . LYS B 1 910  ? 30.421  31.217  109.186 1.00 39.20 ?  908  LYS B CE    1 
ATOM   15961 N NZ    . LYS B 1 910  ? 29.576  30.928  110.391 1.00 45.26 ?  908  LYS B NZ    1 
ATOM   15962 N N     . VAL B 1 911  ? 32.468  30.512  104.046 1.00 27.16 ?  909  VAL B N     1 
ATOM   15963 C CA    . VAL B 1 911  ? 32.044  29.828  102.826 1.00 22.00 ?  909  VAL B CA    1 
ATOM   15964 C C     . VAL B 1 911  ? 31.481  28.470  103.225 1.00 25.58 ?  909  VAL B C     1 
ATOM   15965 O O     . VAL B 1 911  ? 32.191  27.654  103.828 1.00 29.77 ?  909  VAL B O     1 
ATOM   15966 C CB    . VAL B 1 911  ? 33.208  29.658  101.836 1.00 25.33 ?  909  VAL B CB    1 
ATOM   15967 C CG1   . VAL B 1 911  ? 32.757  28.912  100.592 1.00 24.91 ?  909  VAL B CG1   1 
ATOM   15968 C CG2   . VAL B 1 911  ? 33.810  31.007  101.470 1.00 25.61 ?  909  VAL B CG2   1 
ATOM   15969 N N     . GLU B 1 912  ? 30.211  28.237  102.910 1.00 24.37 ?  910  GLU B N     1 
ATOM   15970 C CA    . GLU B 1 912  ? 29.535  26.960  103.114 1.00 25.95 ?  910  GLU B CA    1 
ATOM   15971 C C     . GLU B 1 912  ? 29.332  26.284  101.761 1.00 28.56 ?  910  GLU B C     1 
ATOM   15972 O O     . GLU B 1 912  ? 28.837  26.914  100.820 1.00 22.94 ?  910  GLU B O     1 
ATOM   15973 C CB    . GLU B 1 912  ? 28.180  27.170  103.797 1.00 28.11 ?  910  GLU B CB    1 
ATOM   15974 C CG    . GLU B 1 912  ? 27.481  25.893  104.248 1.00 25.80 ?  910  GLU B CG    1 
ATOM   15975 C CD    . GLU B 1 912  ? 27.992  25.408  105.590 1.00 28.57 ?  910  GLU B CD    1 
ATOM   15976 O OE1   . GLU B 1 912  ? 28.711  26.179  106.258 1.00 31.08 ?  910  GLU B OE1   1 
ATOM   15977 O OE2   . GLU B 1 912  ? 27.687  24.259  105.974 1.00 31.55 ?  910  GLU B OE2   1 
ATOM   15978 N N     . GLN B 1 913  ? 29.691  25.003  101.663 1.00 25.94 ?  911  GLN B N     1 
ATOM   15979 C CA    . GLN B 1 913  ? 29.531  24.267  100.414 1.00 24.13 ?  911  GLN B CA    1 
ATOM   15980 C C     . GLN B 1 913  ? 29.016  22.862  100.694 1.00 28.79 ?  911  GLN B C     1 
ATOM   15981 O O     . GLN B 1 913  ? 29.416  22.232  101.677 1.00 28.68 ?  911  GLN B O     1 
ATOM   15982 C CB    . GLN B 1 913  ? 30.858  24.185  99.643  1.00 24.34 ?  911  GLN B CB    1 
ATOM   15983 C CG    . GLN B 1 913  ? 31.315  25.485  99.009  1.00 27.17 ?  911  GLN B CG    1 
ATOM   15984 C CD    . GLN B 1 913  ? 32.530  25.305  98.117  1.00 30.63 ?  911  GLN B CD    1 
ATOM   15985 O OE1   . GLN B 1 913  ? 33.546  24.754  98.542  1.00 31.64 ?  911  GLN B OE1   1 
ATOM   15986 N NE2   . GLN B 1 913  ? 32.430  25.767  96.872  1.00 24.83 ?  911  GLN B NE2   1 
ATOM   15987 N N     . ILE B 1 914  ? 28.129  22.368  99.828  1.00 26.65 ?  912  ILE B N     1 
ATOM   15988 C CA    . ILE B 1 914  ? 27.771  20.955  99.870  1.00 26.63 ?  912  ILE B CA    1 
ATOM   15989 C C     . ILE B 1 914  ? 28.931  20.122  99.343  1.00 33.45 ?  912  ILE B C     1 
ATOM   15990 O O     . ILE B 1 914  ? 29.620  20.512  98.391  1.00 30.18 ?  912  ILE B O     1 
ATOM   15991 C CB    . ILE B 1 914  ? 26.506  20.679  99.043  1.00 34.18 ?  912  ILE B CB    1 
ATOM   15992 C CG1   . ILE B 1 914  ? 25.570  21.877  99.068  1.00 31.27 ?  912  ILE B CG1   1 
ATOM   15993 C CG2   . ILE B 1 914  ? 25.789  19.434  99.565  1.00 33.78 ?  912  ILE B CG2   1 
ATOM   15994 C CD1   . ILE B 1 914  ? 24.363  21.680  98.191  1.00 26.95 ?  912  ILE B CD1   1 
ATOM   15995 N N     . GLY B 1 915  ? 29.150  18.962  99.956  1.00 31.29 ?  913  GLY B N     1 
ATOM   15996 C CA    . GLY B 1 915  ? 30.105  18.018  99.404  1.00 33.10 ?  913  GLY B CA    1 
ATOM   15997 C C     . GLY B 1 915  ? 29.532  17.335  98.174  1.00 33.18 ?  913  GLY B C     1 
ATOM   15998 O O     . GLY B 1 915  ? 28.376  16.911  98.154  1.00 38.66 ?  913  GLY B O     1 
ATOM   15999 N N     . LEU B 1 916  ? 30.351  17.245  97.126  1.00 30.15 ?  914  LEU B N     1 
ATOM   16000 C CA    . LEU B 1 916  ? 29.939  16.623  95.873  1.00 32.09 ?  914  LEU B CA    1 
ATOM   16001 C C     . LEU B 1 916  ? 30.330  15.150  95.849  1.00 35.36 ?  914  LEU B C     1 
ATOM   16002 O O     . LEU B 1 916  ? 31.411  14.772  96.315  1.00 35.26 ?  914  LEU B O     1 
ATOM   16003 C CB    . LEU B 1 916  ? 30.572  17.340  94.678  1.00 31.04 ?  914  LEU B CB    1 
ATOM   16004 C CG    . LEU B 1 916  ? 30.251  18.822  94.481  1.00 31.14 ?  914  LEU B CG    1 
ATOM   16005 C CD1   . LEU B 1 916  ? 30.895  19.325  93.198  1.00 33.46 ?  914  LEU B CD1   1 
ATOM   16006 C CD2   . LEU B 1 916  ? 28.744  19.064  94.469  1.00 31.94 ?  914  LEU B CD2   1 
ATOM   16007 N N     . ALA B 1 917  ? 29.443  14.321  95.305  1.00 27.80 ?  915  ALA B N     1 
ATOM   16008 C CA    . ALA B 1 917  ? 29.718  12.902  95.149  1.00 29.13 ?  915  ALA B CA    1 
ATOM   16009 C C     . ALA B 1 917  ? 30.791  12.685  94.087  1.00 32.28 ?  915  ALA B C     1 
ATOM   16010 O O     . ALA B 1 917  ? 30.999  13.512  93.195  1.00 31.86 ?  915  ALA B O     1 
ATOM   16011 C CB    . ALA B 1 917  ? 28.441  12.147  94.776  1.00 34.79 ?  915  ALA B CB    1 
ATOM   16012 N N     . SER B 1 918  ? 31.486  11.552  94.191  1.00 33.27 ?  916  SER B N     1 
ATOM   16013 C CA    . SER B 1 918  ? 32.581  11.288  93.263  1.00 36.69 ?  916  SER B CA    1 
ATOM   16014 C C     . SER B 1 918  ? 32.098  11.133  91.825  1.00 31.36 ?  916  SER B C     1 
ATOM   16015 O O     . SER B 1 918  ? 32.889  11.334  90.898  1.00 32.32 ?  916  SER B O     1 
ATOM   16016 C CB    . SER B 1 918  ? 33.351  10.041  93.693  1.00 39.47 ?  916  SER B CB    1 
ATOM   16017 O OG    . SER B 1 918  ? 32.520  8.898   93.621  1.00 45.02 ?  916  SER B OG    1 
ATOM   16018 N N     . GLU B 1 919  ? 30.817  10.802  91.620  1.00 35.20 ?  917  GLU B N     1 
ATOM   16019 C CA    . GLU B 1 919  ? 30.287  10.661  90.265  1.00 33.52 ?  917  GLU B CA    1 
ATOM   16020 C C     . GLU B 1 919  ? 30.290  11.977  89.500  1.00 30.91 ?  917  GLU B C     1 
ATOM   16021 O O     . GLU B 1 919  ? 30.130  11.966  88.273  1.00 29.42 ?  917  GLU B O     1 
ATOM   16022 C CB    . GLU B 1 919  ? 28.858  10.105  90.292  1.00 30.96 ?  917  GLU B CB    1 
ATOM   16023 C CG    . GLU B 1 919  ? 28.749  8.624   90.625  1.00 41.44 ?  917  GLU B CG    1 
ATOM   16024 C CD    . GLU B 1 919  ? 28.808  8.347   92.120  1.00 49.27 ?  917  GLU B CD    1 
ATOM   16025 O OE1   . GLU B 1 919  ? 28.760  9.316   92.912  1.00 43.06 ?  917  GLU B OE1   1 
ATOM   16026 O OE2   . GLU B 1 919  ? 28.899  7.159   92.503  1.00 49.76 ?  917  GLU B OE2   1 
ATOM   16027 N N     . THR B 1 920  ? 30.447  13.108  90.189  1.00 28.49 ?  918  THR B N     1 
ATOM   16028 C CA    . THR B 1 920  ? 30.468  14.395  89.512  1.00 27.01 ?  918  THR B CA    1 
ATOM   16029 C C     . THR B 1 920  ? 31.787  14.675  88.802  1.00 25.70 ?  918  THR B C     1 
ATOM   16030 O O     . THR B 1 920  ? 31.826  15.575  87.959  1.00 24.94 ?  918  THR B O     1 
ATOM   16031 C CB    . THR B 1 920  ? 30.168  15.530  90.501  1.00 26.81 ?  918  THR B CB    1 
ATOM   16032 O OG1   . THR B 1 920  ? 31.149  15.533  91.551  1.00 26.47 ?  918  THR B OG1   1 
ATOM   16033 C CG2   . THR B 1 920  ? 28.782  15.366  91.105  1.00 26.96 ?  918  THR B CG2   1 
ATOM   16034 N N     . GLY B 1 921  ? 32.858  13.934  89.110  1.00 23.88 ?  919  GLY B N     1 
ATOM   16035 C CA    . GLY B 1 921  ? 34.145  14.196  88.491  1.00 27.54 ?  919  GLY B CA    1 
ATOM   16036 C C     . GLY B 1 921  ? 34.164  14.057  86.981  1.00 28.10 ?  919  GLY B C     1 
ATOM   16037 O O     . GLY B 1 921  ? 35.048  14.623  86.329  1.00 25.84 ?  919  GLY B O     1 
ATOM   16038 N N     . VAL B 1 922  ? 33.218  13.311  86.402  1.00 23.25 ?  920  VAL B N     1 
ATOM   16039 C CA    . VAL B 1 922  ? 33.207  13.155  84.948  1.00 23.11 ?  920  VAL B CA    1 
ATOM   16040 C C     . VAL B 1 922  ? 32.535  14.326  84.249  1.00 23.29 ?  920  VAL B C     1 
ATOM   16041 O O     . VAL B 1 922  ? 32.620  14.424  83.020  1.00 23.63 ?  920  VAL B O     1 
ATOM   16042 C CB    . VAL B 1 922  ? 32.536  11.837  84.520  1.00 24.31 ?  920  VAL B CB    1 
ATOM   16043 C CG1   . VAL B 1 922  ? 33.389  10.653  84.942  1.00 27.76 ?  920  VAL B CG1   1 
ATOM   16044 C CG2   . VAL B 1 922  ? 31.134  11.719  85.099  1.00 24.14 ?  920  VAL B CG2   1 
ATOM   16045 N N     . GLY B 1 923  ? 31.907  15.228  84.997  1.00 21.85 ?  921  GLY B N     1 
ATOM   16046 C CA    . GLY B 1 923  ? 31.320  16.437  84.444  1.00 20.23 ?  921  GLY B CA    1 
ATOM   16047 C C     . GLY B 1 923  ? 31.914  17.694  85.055  1.00 18.00 ?  921  GLY B C     1 
ATOM   16048 O O     . GLY B 1 923  ? 32.956  17.622  85.711  1.00 22.98 ?  921  GLY B O     1 
ATOM   16049 N N     . THR B 1 924  ? 31.272  18.849  84.861  1.00 18.46 ?  922  THR B N     1 
ATOM   16050 C CA    . THR B 1 924  ? 31.768  20.134  85.358  1.00 17.52 ?  922  THR B CA    1 
ATOM   16051 C C     . THR B 1 924  ? 30.755  20.670  86.369  1.00 16.74 ?  922  THR B C     1 
ATOM   16052 O O     . THR B 1 924  ? 29.789  21.334  85.995  1.00 18.13 ?  922  THR B O     1 
ATOM   16053 C CB    . THR B 1 924  ? 31.998  21.127  84.211  1.00 17.20 ?  922  THR B CB    1 
ATOM   16054 O OG1   . THR B 1 924  ? 30.844  21.162  83.366  1.00 18.23 ?  922  THR B OG1   1 
ATOM   16055 C CG2   . THR B 1 924  ? 33.180  20.701  83.373  1.00 19.24 ?  922  THR B CG2   1 
ATOM   16056 N N     . PHE B 1 925  ? 30.977  20.379  87.652  1.00 18.43 ?  923  PHE B N     1 
ATOM   16057 C CA    . PHE B 1 925  ? 30.058  20.772  88.717  1.00 17.82 ?  923  PHE B CA    1 
ATOM   16058 C C     . PHE B 1 925  ? 30.713  21.765  89.668  1.00 18.38 ?  923  PHE B C     1 
ATOM   16059 O O     . PHE B 1 925  ? 31.897  21.638  89.999  1.00 20.34 ?  923  PHE B O     1 
ATOM   16060 C CB    . PHE B 1 925  ? 29.585  19.559  89.528  1.00 18.46 ?  923  PHE B CB    1 
ATOM   16061 C CG    . PHE B 1 925  ? 28.723  18.597  88.753  1.00 18.51 ?  923  PHE B CG    1 
ATOM   16062 C CD1   . PHE B 1 925  ? 29.289  17.649  87.913  1.00 19.53 ?  923  PHE B CD1   1 
ATOM   16063 C CD2   . PHE B 1 925  ? 27.335  18.646  88.861  1.00 16.82 ?  923  PHE B CD2   1 
ATOM   16064 C CE1   . PHE B 1 925  ? 28.495  16.762  87.208  1.00 17.58 ?  923  PHE B CE1   1 
ATOM   16065 C CE2   . PHE B 1 925  ? 26.540  17.762  88.152  1.00 18.51 ?  923  PHE B CE2   1 
ATOM   16066 C CZ    . PHE B 1 925  ? 27.115  16.817  87.335  1.00 19.31 ?  923  PHE B CZ    1 
ATOM   16067 N N     . VAL B 1 926  ? 29.928  22.737  90.119  1.00 18.95 ?  924  VAL B N     1 
ATOM   16068 C CA    . VAL B 1 926  ? 30.292  23.618  91.221  1.00 19.82 ?  924  VAL B CA    1 
ATOM   16069 C C     . VAL B 1 926  ? 29.268  23.391  92.323  1.00 21.28 ?  924  VAL B C     1 
ATOM   16070 O O     . VAL B 1 926  ? 28.067  23.450  92.052  1.00 20.20 ?  924  VAL B O     1 
ATOM   16071 C CB    . VAL B 1 926  ? 30.311  25.102  90.814  1.00 18.04 ?  924  VAL B CB    1 
ATOM   16072 C CG1   . VAL B 1 926  ? 30.579  25.999  92.038  1.00 18.29 ?  924  VAL B CG1   1 
ATOM   16073 C CG2   . VAL B 1 926  ? 31.344  25.343  89.728  1.00 19.75 ?  924  VAL B CG2   1 
ATOM   16074 N N     . PRO B 1 927  ? 29.679  23.125  93.558  1.00 20.34 ?  925  PRO B N     1 
ATOM   16075 C CA    . PRO B 1 927  ? 28.700  22.886  94.619  1.00 22.27 ?  925  PRO B CA    1 
ATOM   16076 C C     . PRO B 1 927  ? 27.951  24.159  94.950  1.00 20.31 ?  925  PRO B C     1 
ATOM   16077 O O     . PRO B 1 927  ? 28.538  25.253  94.936  1.00 19.94 ?  925  PRO B O     1 
ATOM   16078 C CB    . PRO B 1 927  ? 29.564  22.434  95.806  1.00 22.93 ?  925  PRO B CB    1 
ATOM   16079 C CG    . PRO B 1 927  ? 30.896  23.064  95.553  1.00 24.34 ?  925  PRO B CG    1 
ATOM   16080 C CD    . PRO B 1 927  ? 31.064  23.010  94.049  1.00 19.55 ?  925  PRO B CD    1 
ATOM   16081 N N     . PRO B 1 928  ? 26.652  24.066  95.227  1.00 22.02 ?  926  PRO B N     1 
ATOM   16082 C CA    . PRO B 1 928  ? 25.950  25.216  95.791  1.00 20.99 ?  926  PRO B CA    1 
ATOM   16083 C C     . PRO B 1 928  ? 26.720  25.760  96.982  1.00 19.98 ?  926  PRO B C     1 
ATOM   16084 O O     . PRO B 1 928  ? 27.126  25.010  97.876  1.00 23.82 ?  926  PRO B O     1 
ATOM   16085 C CB    . PRO B 1 928  ? 24.595  24.634  96.189  1.00 19.41 ?  926  PRO B CB    1 
ATOM   16086 C CG    . PRO B 1 928  ? 24.363  23.563  95.154  1.00 25.05 ?  926  PRO B CG    1 
ATOM   16087 C CD    . PRO B 1 928  ? 25.734  22.954  94.926  1.00 23.94 ?  926  PRO B CD    1 
ATOM   16088 N N     . THR B 1 929  ? 26.948  27.073  96.963  1.00 16.80 ?  927  THR B N     1 
ATOM   16089 C CA    . THR B 1 929  ? 27.871  27.760  97.853  1.00 20.13 ?  927  THR B CA    1 
ATOM   16090 C C     . THR B 1 929  ? 27.188  28.976  98.455  1.00 22.09 ?  927  THR B C     1 
ATOM   16091 O O     . THR B 1 929  ? 26.484  29.704  97.756  1.00 19.55 ?  927  THR B O     1 
ATOM   16092 C CB    . THR B 1 929  ? 29.131  28.204  97.094  1.00 22.69 ?  927  THR B CB    1 
ATOM   16093 O OG1   . THR B 1 929  ? 29.757  27.058  96.509  1.00 20.89 ?  927  THR B OG1   1 
ATOM   16094 C CG2   . THR B 1 929  ? 30.116  28.906  98.008  1.00 20.94 ?  927  THR B CG2   1 
ATOM   16095 N N     . ILE B 1 930  ? 27.418  29.201  99.749  1.00 21.68 ?  928  ILE B N     1 
ATOM   16096 C CA    . ILE B 1 930  ? 26.939  30.386  100.452 1.00 22.50 ?  928  ILE B CA    1 
ATOM   16097 C C     . ILE B 1 930  ? 28.162  31.143  100.956 1.00 19.82 ?  928  ILE B C     1 
ATOM   16098 O O     . ILE B 1 930  ? 29.004  30.569  101.664 1.00 23.00 ?  928  ILE B O     1 
ATOM   16099 C CB    . ILE B 1 930  ? 26.002  30.019  101.615 1.00 19.30 ?  928  ILE B CB    1 
ATOM   16100 C CG1   . ILE B 1 930  ? 24.758  29.284  101.107 1.00 22.32 ?  928  ILE B CG1   1 
ATOM   16101 C CG2   . ILE B 1 930  ? 25.620  31.270  102.404 1.00 23.55 ?  928  ILE B CG2   1 
ATOM   16102 C CD1   . ILE B 1 930  ? 23.881  28.728  102.228 1.00 22.32 ?  928  ILE B CD1   1 
ATOM   16103 N N     . ILE B 1 931  ? 28.272  32.418  100.592 1.00 19.79 ?  929  ILE B N     1 
ATOM   16104 C CA    . ILE B 1 931  ? 29.405  33.259  100.971 1.00 20.45 ?  929  ILE B CA    1 
ATOM   16105 C C     . ILE B 1 931  ? 28.883  34.451  101.762 1.00 22.76 ?  929  ILE B C     1 
ATOM   16106 O O     . ILE B 1 931  ? 28.095  35.247  101.243 1.00 23.02 ?  929  ILE B O     1 
ATOM   16107 C CB    . ILE B 1 931  ? 30.203  33.744  99.752  1.00 19.99 ?  929  ILE B CB    1 
ATOM   16108 C CG1   . ILE B 1 931  ? 30.735  32.556  98.952  1.00 21.72 ?  929  ILE B CG1   1 
ATOM   16109 C CG2   . ILE B 1 931  ? 31.359  34.641  100.189 1.00 29.14 ?  929  ILE B CG2   1 
ATOM   16110 C CD1   . ILE B 1 931  ? 31.604  32.977  97.775  1.00 24.01 ?  929  ILE B CD1   1 
ATOM   16111 N N     . GLU B 1 932  ? 29.341  34.600  103.003 1.00 21.39 ?  930  GLU B N     1 
ATOM   16112 C CA    . GLU B 1 932  ? 28.922  35.732  103.825 1.00 21.77 ?  930  GLU B CA    1 
ATOM   16113 C C     . GLU B 1 932  ? 29.888  36.894  103.616 1.00 22.53 ?  930  GLU B C     1 
ATOM   16114 O O     . GLU B 1 932  ? 31.099  36.750  103.839 1.00 25.15 ?  930  GLU B O     1 
ATOM   16115 C CB    . GLU B 1 932  ? 28.835  35.323  105.297 1.00 22.11 ?  930  GLU B CB    1 
ATOM   16116 C CG    . GLU B 1 932  ? 27.732  34.295  105.538 1.00 25.48 ?  930  GLU B CG    1 
ATOM   16117 C CD    . GLU B 1 932  ? 27.804  33.633  106.898 1.00 30.99 ?  930  GLU B CD    1 
ATOM   16118 O OE1   . GLU B 1 932  ? 27.953  34.355  107.910 1.00 27.13 ?  930  GLU B OE1   1 
ATOM   16119 O OE2   . GLU B 1 932  ? 27.700  32.385  106.949 1.00 28.79 ?  930  GLU B OE2   1 
ATOM   16120 N N     . LEU B 1 933  ? 29.347  38.042  103.210 1.00 20.93 ?  931  LEU B N     1 
ATOM   16121 C CA    . LEU B 1 933  ? 30.091  39.265  102.940 1.00 20.91 ?  931  LEU B CA    1 
ATOM   16122 C C     . LEU B 1 933  ? 29.761  40.342  103.968 1.00 29.77 ?  931  LEU B C     1 
ATOM   16123 O O     . LEU B 1 933  ? 28.711  40.312  104.620 1.00 24.55 ?  931  LEU B O     1 
ATOM   16124 C CB    . LEU B 1 933  ? 29.767  39.825  101.547 1.00 25.35 ?  931  LEU B CB    1 
ATOM   16125 C CG    . LEU B 1 933  ? 29.922  38.942  100.309 1.00 26.57 ?  931  LEU B CG    1 
ATOM   16126 C CD1   . LEU B 1 933  ? 29.543  39.743  99.070  1.00 27.37 ?  931  LEU B CD1   1 
ATOM   16127 C CD2   . LEU B 1 933  ? 31.345  38.416  100.201 1.00 29.81 ?  931  LEU B CD2   1 
ATOM   16128 N N     . GLU B 1 934  ? 30.652  41.335  104.054 1.00 29.83 ?  932  GLU B N     1 
ATOM   16129 C CA    . GLU B 1 934  ? 30.433  42.487  104.926 1.00 30.00 ?  932  GLU B CA    1 
ATOM   16130 C C     . GLU B 1 934  ? 29.473  43.493  104.293 1.00 35.45 ?  932  GLU B C     1 
ATOM   16131 O O     . GLU B 1 934  ? 28.455  43.856  104.894 1.00 35.27 ?  932  GLU B O     1 
ATOM   16132 C CB    . GLU B 1 934  ? 31.773  43.154  105.264 1.00 34.25 ?  932  GLU B CB    1 
ATOM   16133 N N     . LYS B 1 935  ? 29.778  43.956  103.079 1.00 33.72 ?  933  LYS B N     1 
ATOM   16134 C CA    . LYS B 1 935  ? 28.941  44.932  102.394 1.00 33.74 ?  933  LYS B CA    1 
ATOM   16135 C C     . LYS B 1 935  ? 28.739  44.514  100.943 1.00 32.07 ?  933  LYS B C     1 
ATOM   16136 O O     . LYS B 1 935  ? 29.499  43.715  100.392 1.00 31.00 ?  933  LYS B O     1 
ATOM   16137 C CB    . LYS B 1 935  ? 29.536  46.352  102.471 1.00 38.05 ?  933  LYS B CB    1 
ATOM   16138 C CG    . LYS B 1 935  ? 30.985  46.481  102.027 1.00 39.10 ?  933  LYS B CG    1 
ATOM   16139 C CD    . LYS B 1 935  ? 31.574  47.822  102.454 1.00 36.46 ?  933  LYS B CD    1 
ATOM   16140 N N     . LEU B 1 936  ? 27.687  45.065  100.329 1.00 33.43 ?  934  LEU B N     1 
ATOM   16141 C CA    . LEU B 1 936  ? 27.356  44.685  98.959  1.00 32.12 ?  934  LEU B CA    1 
ATOM   16142 C C     . LEU B 1 936  ? 28.491  45.011  97.995  1.00 33.82 ?  934  LEU B C     1 
ATOM   16143 O O     . LEU B 1 936  ? 28.733  44.253  97.051  1.00 33.41 ?  934  LEU B O     1 
ATOM   16144 C CB    . LEU B 1 936  ? 26.056  45.366  98.520  1.00 30.76 ?  934  LEU B CB    1 
ATOM   16145 C CG    . LEU B 1 936  ? 25.202  44.583  97.519  1.00 29.24 ?  934  LEU B CG    1 
ATOM   16146 C CD1   . LEU B 1 936  ? 23.724  44.844  97.766  1.00 32.18 ?  934  LEU B CD1   1 
ATOM   16147 C CD2   . LEU B 1 936  ? 25.571  44.942  96.091  1.00 36.71 ?  934  LEU B CD2   1 
ATOM   16148 N N     . SER B 1 937  ? 29.213  46.111  98.226  1.00 33.16 ?  935  SER B N     1 
ATOM   16149 C CA    . SER B 1 937  ? 30.303  46.492  97.331  1.00 36.19 ?  935  SER B CA    1 
ATOM   16150 C C     . SER B 1 937  ? 31.484  45.523  97.379  1.00 34.93 ?  935  SER B C     1 
ATOM   16151 O O     . SER B 1 937  ? 32.398  45.649  96.555  1.00 37.23 ?  935  SER B O     1 
ATOM   16152 C CB    . SER B 1 937  ? 30.780  47.911  97.652  1.00 38.73 ?  935  SER B CB    1 
ATOM   16153 O OG    . SER B 1 937  ? 31.349  47.976  98.946  1.00 39.82 ?  935  SER B OG    1 
ATOM   16154 N N     . ASP B 1 938  ? 31.490  44.565  98.312  1.00 31.41 ?  936  ASP B N     1 
ATOM   16155 C CA    . ASP B 1 938  ? 32.488  43.500  98.288  1.00 33.06 ?  936  ASP B CA    1 
ATOM   16156 C C     . ASP B 1 938  ? 32.312  42.576  97.088  1.00 36.78 ?  936  ASP B C     1 
ATOM   16157 O O     . ASP B 1 938  ? 33.249  41.851  96.736  1.00 33.61 ?  936  ASP B O     1 
ATOM   16158 C CB    . ASP B 1 938  ? 32.419  42.675  99.574  1.00 32.81 ?  936  ASP B CB    1 
ATOM   16159 C CG    . ASP B 1 938  ? 32.895  43.442  100.794 1.00 39.93 ?  936  ASP B CG    1 
ATOM   16160 O OD1   . ASP B 1 938  ? 33.510  44.523  100.632 1.00 36.53 ?  936  ASP B OD1   1 
ATOM   16161 O OD2   . ASP B 1 938  ? 32.654  42.950  101.917 1.00 38.55 ?  936  ASP B OD2   1 
ATOM   16162 N N     . LEU B 1 939  ? 31.130  42.573  96.475  1.00 33.78 ?  937  LEU B N     1 
ATOM   16163 C CA    . LEU B 1 939  ? 30.863  41.807  95.263  1.00 29.94 ?  937  LEU B CA    1 
ATOM   16164 C C     . LEU B 1 939  ? 31.092  42.721  94.067  1.00 31.17 ?  937  LEU B C     1 
ATOM   16165 O O     . LEU B 1 939  ? 30.332  43.670  93.845  1.00 34.28 ?  937  LEU B O     1 
ATOM   16166 C CB    . LEU B 1 939  ? 29.438  41.261  95.276  1.00 31.57 ?  937  LEU B CB    1 
ATOM   16167 C CG    . LEU B 1 939  ? 29.034  40.490  94.025  1.00 29.08 ?  937  LEU B CG    1 
ATOM   16168 C CD1   . LEU B 1 939  ? 29.993  39.333  93.783  1.00 28.43 ?  937  LEU B CD1   1 
ATOM   16169 C CD2   . LEU B 1 939  ? 27.614  39.986  94.186  1.00 30.70 ?  937  LEU B CD2   1 
ATOM   16170 N N     . GLN B 1 940  ? 32.131  42.432  93.288  1.00 31.95 ?  938  GLN B N     1 
ATOM   16171 C CA    . GLN B 1 940  ? 32.627  43.367  92.290  1.00 36.62 ?  938  GLN B CA    1 
ATOM   16172 C C     . GLN B 1 940  ? 32.451  42.889  90.857  1.00 42.73 ?  938  GLN B C     1 
ATOM   16173 O O     . GLN B 1 940  ? 32.835  43.612  89.932  1.00 43.81 ?  938  GLN B O     1 
ATOM   16174 C CB    . GLN B 1 940  ? 34.105  43.678  92.564  1.00 43.24 ?  938  GLN B CB    1 
ATOM   16175 C CG    . GLN B 1 940  ? 34.294  44.810  93.571  1.00 42.00 ?  938  GLN B CG    1 
ATOM   16176 C CD    . GLN B 1 940  ? 35.507  44.626  94.465  1.00 50.83 ?  938  GLN B CD    1 
ATOM   16177 O OE1   . GLN B 1 940  ? 36.502  44.010  94.075  1.00 53.31 ?  938  GLN B OE1   1 
ATOM   16178 N NE2   . GLN B 1 940  ? 35.425  45.163  95.678  1.00 50.33 ?  938  GLN B NE2   1 
ATOM   16179 N N     . ARG B 1 941  ? 31.879  41.707  90.641  1.00 35.18 ?  939  ARG B N     1 
ATOM   16180 C CA    . ARG B 1 941  ? 31.588  41.269  89.283  1.00 37.81 ?  939  ARG B CA    1 
ATOM   16181 C C     . ARG B 1 941  ? 30.514  40.194  89.328  1.00 35.87 ?  939  ARG B C     1 
ATOM   16182 O O     . ARG B 1 941  ? 30.198  39.650  90.389  1.00 29.36 ?  939  ARG B O     1 
ATOM   16183 C CB    . ARG B 1 941  ? 32.843  40.753  88.569  1.00 38.37 ?  939  ARG B CB    1 
ATOM   16184 C CG    . ARG B 1 941  ? 33.419  39.465  89.126  1.00 38.87 ?  939  ARG B CG    1 
ATOM   16185 C CD    . ARG B 1 941  ? 34.412  38.883  88.123  1.00 40.90 ?  939  ARG B CD    1 
ATOM   16186 N NE    . ARG B 1 941  ? 35.139  37.724  88.631  1.00 44.68 ?  939  ARG B NE    1 
ATOM   16187 C CZ    . ARG B 1 941  ? 34.791  36.462  88.416  1.00 39.56 ?  939  ARG B CZ    1 
ATOM   16188 N NH1   . ARG B 1 941  ? 33.694  36.150  87.740  1.00 41.09 ?  939  ARG B NH1   1 
ATOM   16189 N NH2   . ARG B 1 941  ? 35.563  35.487  88.893  1.00 35.82 ?  939  ARG B NH2   1 
ATOM   16190 N N     . GLU B 1 942  ? 29.950  39.901  88.158  1.00 36.91 ?  940  GLU B N     1 
ATOM   16191 C CA    . GLU B 1 942  ? 28.935  38.862  88.078  1.00 37.66 ?  940  GLU B CA    1 
ATOM   16192 C C     . GLU B 1 942  ? 29.604  37.498  88.179  1.00 30.84 ?  940  GLU B C     1 
ATOM   16193 O O     . GLU B 1 942  ? 30.639  37.249  87.552  1.00 33.99 ?  940  GLU B O     1 
ATOM   16194 C CB    . GLU B 1 942  ? 28.133  38.978  86.780  1.00 41.72 ?  940  GLU B CB    1 
ATOM   16195 C CG    . GLU B 1 942  ? 26.768  38.274  86.834  1.00 40.98 ?  940  GLU B CG    1 
ATOM   16196 C CD    . GLU B 1 942  ? 25.971  38.401  85.538  1.00 46.59 ?  940  GLU B CD    1 
ATOM   16197 O OE1   . GLU B 1 942  ? 26.593  38.599  84.470  1.00 49.03 ?  940  GLU B OE1   1 
ATOM   16198 O OE2   . GLU B 1 942  ? 24.722  38.302  85.584  1.00 41.09 ?  940  GLU B OE2   1 
ATOM   16199 N N     . VAL B 1 943  ? 29.034  36.631  89.005  1.00 23.55 ?  941  VAL B N     1 
ATOM   16200 C CA    . VAL B 1 943  ? 29.520  35.271  89.202  1.00 23.21 ?  941  VAL B CA    1 
ATOM   16201 C C     . VAL B 1 943  ? 28.373  34.357  88.803  1.00 22.46 ?  941  VAL B C     1 
ATOM   16202 O O     . VAL B 1 943  ? 27.414  34.174  89.563  1.00 19.94 ?  941  VAL B O     1 
ATOM   16203 C CB    . VAL B 1 943  ? 29.967  35.017  90.645  1.00 24.98 ?  941  VAL B CB    1 
ATOM   16204 C CG1   . VAL B 1 943  ? 30.469  33.582  90.809  1.00 23.84 ?  941  VAL B CG1   1 
ATOM   16205 C CG2   . VAL B 1 943  ? 31.046  36.022  91.031  1.00 26.20 ?  941  VAL B CG2   1 
ATOM   16206 N N     . PHE B 1 944  ? 28.469  33.781  87.606  1.00 19.43 ?  942  PHE B N     1 
ATOM   16207 C CA    . PHE B 1 944  ? 27.325  33.149  86.953  1.00 16.85 ?  942  PHE B CA    1 
ATOM   16208 C C     . PHE B 1 944  ? 27.298  31.660  87.293  1.00 19.43 ?  942  PHE B C     1 
ATOM   16209 O O     . PHE B 1 944  ? 27.520  30.778  86.460  1.00 20.13 ?  942  PHE B O     1 
ATOM   16210 C CB    . PHE B 1 944  ? 27.390  33.390  85.449  1.00 19.75 ?  942  PHE B CB    1 
ATOM   16211 C CG    . PHE B 1 944  ? 26.062  33.319  84.770  1.00 18.93 ?  942  PHE B CG    1 
ATOM   16212 C CD1   . PHE B 1 944  ? 25.128  34.332  84.948  1.00 20.09 ?  942  PHE B CD1   1 
ATOM   16213 C CD2   . PHE B 1 944  ? 25.736  32.245  83.949  1.00 19.09 ?  942  PHE B CD2   1 
ATOM   16214 C CE1   . PHE B 1 944  ? 23.883  34.283  84.318  1.00 17.86 ?  942  PHE B CE1   1 
ATOM   16215 C CE2   . PHE B 1 944  ? 24.488  32.193  83.317  1.00 19.52 ?  942  PHE B CE2   1 
ATOM   16216 C CZ    . PHE B 1 944  ? 23.563  33.214  83.510  1.00 20.12 ?  942  PHE B CZ    1 
ATOM   16217 N N     . GLY B 1 945  ? 27.021  31.386  88.564  1.00 17.62 ?  943  GLY B N     1 
ATOM   16218 C CA    . GLY B 1 945  ? 27.000  30.027  89.050  1.00 16.96 ?  943  GLY B CA    1 
ATOM   16219 C C     . GLY B 1 945  ? 26.215  29.939  90.339  1.00 17.40 ?  943  GLY B C     1 
ATOM   16220 O O     . GLY B 1 945  ? 25.572  30.906  90.754  1.00 18.17 ?  943  GLY B O     1 
ATOM   16221 N N     . PRO B 1 946  ? 26.269  28.782  91.013  1.00 15.41 ?  944  PRO B N     1 
ATOM   16222 C CA    . PRO B 1 946  ? 25.433  28.575  92.223  1.00 14.89 ?  944  PRO B CA    1 
ATOM   16223 C C     . PRO B 1 946  ? 26.102  29.151  93.467  1.00 17.02 ?  944  PRO B C     1 
ATOM   16224 O O     . PRO B 1 946  ? 26.499  28.444  94.394  1.00 18.92 ?  944  PRO B O     1 
ATOM   16225 C CB    . PRO B 1 946  ? 25.297  27.053  92.270  1.00 16.72 ?  944  PRO B CB    1 
ATOM   16226 C CG    . PRO B 1 946  ? 26.625  26.558  91.701  1.00 18.08 ?  944  PRO B CG    1 
ATOM   16227 C CD    . PRO B 1 946  ? 27.034  27.576  90.639  1.00 18.55 ?  944  PRO B CD    1 
ATOM   16228 N N     . VAL B 1 947  ? 26.247  30.472  93.483  1.00 16.20 ?  945  VAL B N     1 
ATOM   16229 C CA    . VAL B 1 947  ? 27.034  31.161  94.500  1.00 18.38 ?  945  VAL B CA    1 
ATOM   16230 C C     . VAL B 1 947  ? 26.182  32.284  95.064  1.00 21.02 ?  945  VAL B C     1 
ATOM   16231 O O     . VAL B 1 947  ? 25.990  33.318  94.412  1.00 18.38 ?  945  VAL B O     1 
ATOM   16232 C CB    . VAL B 1 947  ? 28.354  31.707  93.950  1.00 18.78 ?  945  VAL B CB    1 
ATOM   16233 C CG1   . VAL B 1 947  ? 29.155  32.386  95.056  1.00 21.78 ?  945  VAL B CG1   1 
ATOM   16234 C CG2   . VAL B 1 947  ? 29.185  30.586  93.331  1.00 22.89 ?  945  VAL B CG2   1 
ATOM   16235 N N     . LEU B 1 948  ? 25.685  32.088  96.273  1.00 18.60 ?  946  LEU B N     1 
ATOM   16236 C CA    . LEU B 1 948  ? 24.882  33.087  96.954  1.00 16.90 ?  946  LEU B CA    1 
ATOM   16237 C C     . LEU B 1 948  ? 25.749  33.876  97.919  1.00 21.06 ?  946  LEU B C     1 
ATOM   16238 O O     . LEU B 1 948  ? 26.447  33.289  98.749  1.00 20.92 ?  946  LEU B O     1 
ATOM   16239 C CB    . LEU B 1 948  ? 23.749  32.420  97.714  1.00 15.61 ?  946  LEU B CB    1 
ATOM   16240 C CG    . LEU B 1 948  ? 22.913  33.376  98.560  1.00 17.99 ?  946  LEU B CG    1 
ATOM   16241 C CD1   . LEU B 1 948  ? 22.088  34.262  97.637  1.00 16.48 ?  946  LEU B CD1   1 
ATOM   16242 C CD2   . LEU B 1 948  ? 22.035  32.573  99.487  1.00 20.28 ?  946  LEU B CD2   1 
ATOM   16243 N N     . HIS B 1 949  ? 25.692  35.196  97.818  1.00 16.55 ?  947  HIS B N     1 
ATOM   16244 C CA    . HIS B 1 949  ? 26.346  36.078  98.773  1.00 16.55 ?  947  HIS B CA    1 
ATOM   16245 C C     . HIS B 1 949  ? 25.310  36.595  99.758  1.00 17.84 ?  947  HIS B C     1 
ATOM   16246 O O     . HIS B 1 949  ? 24.171  36.882  99.383  1.00 18.39 ?  947  HIS B O     1 
ATOM   16247 C CB    . HIS B 1 949  ? 27.040  37.228  98.054  1.00 19.53 ?  947  HIS B CB    1 
ATOM   16248 C CG    . HIS B 1 949  ? 27.968  36.764  96.977  1.00 21.15 ?  947  HIS B CG    1 
ATOM   16249 N ND1   . HIS B 1 949  ? 27.520  36.387  95.726  1.00 19.71 ?  947  HIS B ND1   1 
ATOM   16250 C CD2   . HIS B 1 949  ? 29.307  36.568  96.974  1.00 23.17 ?  947  HIS B CD2   1 
ATOM   16251 C CE1   . HIS B 1 949  ? 28.550  35.997  94.995  1.00 21.47 ?  947  HIS B CE1   1 
ATOM   16252 N NE2   . HIS B 1 949  ? 29.644  36.094  95.728  1.00 21.88 ?  947  HIS B NE2   1 
ATOM   16253 N N     . VAL B 1 950  ? 25.701  36.701  101.023 1.00 18.15 ?  948  VAL B N     1 
ATOM   16254 C CA    . VAL B 1 950  ? 24.777  37.119  102.067 1.00 19.20 ?  948  VAL B CA    1 
ATOM   16255 C C     . VAL B 1 950  ? 25.372  38.314  102.794 1.00 19.76 ?  948  VAL B C     1 
ATOM   16256 O O     . VAL B 1 950  ? 26.529  38.263  103.231 1.00 22.91 ?  948  VAL B O     1 
ATOM   16257 C CB    . VAL B 1 950  ? 24.484  35.985  103.065 1.00 19.16 ?  948  VAL B CB    1 
ATOM   16258 C CG1   . VAL B 1 950  ? 23.510  36.474  104.142 1.00 19.85 ?  948  VAL B CG1   1 
ATOM   16259 C CG2   . VAL B 1 950  ? 23.956  34.746  102.361 1.00 19.82 ?  948  VAL B CG2   1 
ATOM   16260 N N     . ILE B 1 951  ? 24.583  39.382  102.934 1.00 15.95 ?  949  ILE B N     1 
ATOM   16261 C CA    . ILE B 1 951  ? 24.975  40.529  103.746 1.00 16.83 ?  949  ILE B CA    1 
ATOM   16262 C C     . ILE B 1 951  ? 23.895  40.781  104.786 1.00 17.17 ?  949  ILE B C     1 
ATOM   16263 O O     . ILE B 1 951  ? 22.751  40.340  104.655 1.00 17.74 ?  949  ILE B O     1 
ATOM   16264 C CB    . ILE B 1 951  ? 25.225  41.802  102.923 1.00 19.81 ?  949  ILE B CB    1 
ATOM   16265 C CG1   . ILE B 1 951  ? 23.946  42.239  102.214 1.00 18.84 ?  949  ILE B CG1   1 
ATOM   16266 C CG2   . ILE B 1 951  ? 26.349  41.575  101.921 1.00 24.98 ?  949  ILE B CG2   1 
ATOM   16267 C CD1   . ILE B 1 951  ? 24.099  43.504  101.414 1.00 28.42 ?  949  ILE B CD1   1 
ATOM   16268 N N     . ARG B 1 952  ? 24.285  41.494  105.841 1.00 16.92 ?  950  ARG B N     1 
ATOM   16269 C CA    . ARG B 1 952  ? 23.394  41.826  106.943 1.00 18.18 ?  950  ARG B CA    1 
ATOM   16270 C C     . ARG B 1 952  ? 23.190  43.335  106.969 1.00 16.76 ?  950  ARG B C     1 
ATOM   16271 O O     . ARG B 1 952  ? 24.105  44.097  106.647 1.00 21.34 ?  950  ARG B O     1 
ATOM   16272 C CB    . ARG B 1 952  ? 23.989  41.344  108.286 1.00 19.26 ?  950  ARG B CB    1 
ATOM   16273 C CG    . ARG B 1 952  ? 24.450  39.888  108.280 1.00 20.52 ?  950  ARG B CG    1 
ATOM   16274 C CD    . ARG B 1 952  ? 25.443  39.584  109.412 1.00 25.20 ?  950  ARG B CD    1 
ATOM   16275 N NE    . ARG B 1 952  ? 24.787  39.456  110.709 1.00 26.02 ?  950  ARG B NE    1 
ATOM   16276 C CZ    . ARG B 1 952  ? 24.510  38.304  111.306 1.00 26.41 ?  950  ARG B CZ    1 
ATOM   16277 N NH1   . ARG B 1 952  ? 24.822  37.142  110.753 1.00 24.54 ?  950  ARG B NH1   1 
ATOM   16278 N NH2   . ARG B 1 952  ? 23.907  38.318  112.493 1.00 25.15 ?  950  ARG B NH2   1 
ATOM   16279 N N     . TYR B 1 953  ? 21.991  43.782  107.359 1.00 16.39 ?  951  TYR B N     1 
ATOM   16280 C CA    . TYR B 1 953  ? 21.738  45.218  107.447 1.00 16.63 ?  951  TYR B CA    1 
ATOM   16281 C C     . TYR B 1 953  ? 20.896  45.542  108.677 1.00 17.03 ?  951  TYR B C     1 
ATOM   16282 O O     . TYR B 1 953  ? 20.065  44.743  109.112 1.00 16.51 ?  951  TYR B O     1 
ATOM   16283 C CB    . TYR B 1 953  ? 21.037  45.757  106.178 1.00 17.31 ?  951  TYR B CB    1 
ATOM   16284 C CG    . TYR B 1 953  ? 19.579  45.353  106.052 1.00 16.06 ?  951  TYR B CG    1 
ATOM   16285 C CD1   . TYR B 1 953  ? 19.218  44.108  105.543 1.00 16.08 ?  951  TYR B CD1   1 
ATOM   16286 C CD2   . TYR B 1 953  ? 18.567  46.204  106.472 1.00 14.89 ?  951  TYR B CD2   1 
ATOM   16287 C CE1   . TYR B 1 953  ? 17.885  43.727  105.445 1.00 16.86 ?  951  TYR B CE1   1 
ATOM   16288 C CE2   . TYR B 1 953  ? 17.231  45.835  106.365 1.00 16.00 ?  951  TYR B CE2   1 
ATOM   16289 C CZ    . TYR B 1 953  ? 16.894  44.596  105.853 1.00 16.15 ?  951  TYR B CZ    1 
ATOM   16290 O OH    . TYR B 1 953  ? 15.569  44.235  105.784 1.00 17.20 ?  951  TYR B OH    1 
ATOM   16291 N N     . ARG B 1 954  ? 21.121  46.733  109.229 1.00 20.05 ?  952  ARG B N     1 
ATOM   16292 C CA    . ARG B 1 954  ? 20.265  47.260  110.285 1.00 21.39 ?  952  ARG B CA    1 
ATOM   16293 C C     . ARG B 1 954  ? 19.043  47.914  109.662 1.00 19.84 ?  952  ARG B C     1 
ATOM   16294 O O     . ARG B 1 954  ? 19.152  48.579  108.628 1.00 20.10 ?  952  ARG B O     1 
ATOM   16295 C CB    . ARG B 1 954  ? 21.025  48.283  111.135 1.00 27.30 ?  952  ARG B CB    1 
ATOM   16296 C CG    . ARG B 1 954  ? 22.372  47.808  111.646 1.00 29.39 ?  952  ARG B CG    1 
ATOM   16297 C CD    . ARG B 1 954  ? 22.236  46.631  112.617 1.00 37.86 ?  952  ARG B CD    1 
ATOM   16298 N NE    . ARG B 1 954  ? 21.283  46.896  113.690 1.00 43.65 ?  952  ARG B NE    1 
ATOM   16299 C CZ    . ARG B 1 954  ? 21.542  47.623  114.771 1.00 46.46 ?  952  ARG B CZ    1 
ATOM   16300 N NH1   . ARG B 1 954  ? 22.726  48.184  114.962 1.00 47.79 ?  952  ARG B NH1   1 
ATOM   16301 N NH2   . ARG B 1 954  ? 20.586  47.797  115.681 1.00 47.17 ?  952  ARG B NH2   1 
ATOM   16302 N N     . ARG B 1 955  ? 17.872  47.721  110.286 1.00 22.23 ?  953  ARG B N     1 
ATOM   16303 C CA    . ARG B 1 955  ? 16.634  48.189  109.658 1.00 24.44 ?  953  ARG B CA    1 
ATOM   16304 C C     . ARG B 1 955  ? 16.655  49.692  109.401 1.00 23.92 ?  953  ARG B C     1 
ATOM   16305 O O     . ARG B 1 955  ? 16.105  50.154  108.395 1.00 22.58 ?  953  ARG B O     1 
ATOM   16306 C CB    . ARG B 1 955  ? 15.415  47.813  110.507 1.00 27.10 ?  953  ARG B CB    1 
ATOM   16307 C CG    . ARG B 1 955  ? 14.045  48.243  109.925 1.00 28.01 ?  953  ARG B CG    1 
ATOM   16308 C CD    . ARG B 1 955  ? 13.872  47.872  108.436 1.00 29.01 ?  953  ARG B CD    1 
ATOM   16309 N NE    . ARG B 1 955  ? 12.594  48.310  107.875 1.00 30.50 ?  953  ARG B NE    1 
ATOM   16310 C CZ    . ARG B 1 955  ? 12.322  49.553  107.491 1.00 33.32 ?  953  ARG B CZ    1 
ATOM   16311 N NH1   . ARG B 1 955  ? 13.213  50.526  107.607 1.00 29.31 ?  953  ARG B NH1   1 
ATOM   16312 N NH2   . ARG B 1 955  ? 11.123  49.828  106.980 1.00 28.38 ?  953  ARG B NH2   1 
ATOM   16313 N N     . ASP B 1 956  ? 17.299  50.471  110.273 1.00 24.29 ?  954  ASP B N     1 
ATOM   16314 C CA    . ASP B 1 956  ? 17.387  51.905  110.025 1.00 25.35 ?  954  ASP B CA    1 
ATOM   16315 C C     . ASP B 1 956  ? 18.225  52.245  108.804 1.00 23.83 ?  954  ASP B C     1 
ATOM   16316 O O     . ASP B 1 956  ? 18.213  53.401  108.369 1.00 26.74 ?  954  ASP B O     1 
ATOM   16317 C CB    . ASP B 1 956  ? 17.959  52.618  111.250 1.00 27.77 ?  954  ASP B CB    1 
ATOM   16318 C CG    . ASP B 1 956  ? 17.088  52.454  112.474 1.00 39.67 ?  954  ASP B CG    1 
ATOM   16319 O OD1   . ASP B 1 956  ? 15.852  52.381  112.307 1.00 42.62 ?  954  ASP B OD1   1 
ATOM   16320 O OD2   . ASP B 1 956  ? 17.637  52.394  113.598 1.00 46.50 ?  954  ASP B OD2   1 
ATOM   16321 N N     . ASP B 1 957  ? 18.960  51.283  108.252 1.00 21.09 ?  955  ASP B N     1 
ATOM   16322 C CA    . ASP B 1 957  ? 19.787  51.513  107.077 1.00 23.46 ?  955  ASP B CA    1 
ATOM   16323 C C     . ASP B 1 957  ? 19.148  50.968  105.808 1.00 19.60 ?  955  ASP B C     1 
ATOM   16324 O O     . ASP B 1 957  ? 19.830  50.846  104.787 1.00 19.77 ?  955  ASP B O     1 
ATOM   16325 C CB    . ASP B 1 957  ? 21.171  50.885  107.270 1.00 24.26 ?  955  ASP B CB    1 
ATOM   16326 C CG    . ASP B 1 957  ? 22.041  51.656  108.250 1.00 33.86 ?  955  ASP B CG    1 
ATOM   16327 O OD1   . ASP B 1 957  ? 21.958  52.904  108.286 1.00 31.47 ?  955  ASP B OD1   1 
ATOM   16328 O OD2   . ASP B 1 957  ? 22.820  51.003  108.980 1.00 36.87 ?  955  ASP B OD2   1 
ATOM   16329 N N     . LEU B 1 958  ? 17.857  50.633  105.858 1.00 17.33 ?  956  LEU B N     1 
ATOM   16330 C CA    . LEU B 1 958  ? 17.195  50.028  104.704 1.00 15.00 ?  956  LEU B CA    1 
ATOM   16331 C C     . LEU B 1 958  ? 17.278  50.917  103.470 1.00 18.89 ?  956  LEU B C     1 
ATOM   16332 O O     . LEU B 1 958  ? 17.575  50.434  102.371 1.00 16.08 ?  956  LEU B O     1 
ATOM   16333 C CB    . LEU B 1 958  ? 15.740  49.727  105.038 1.00 16.79 ?  956  LEU B CB    1 
ATOM   16334 C CG    . LEU B 1 958  ? 14.928  49.134  103.892 1.00 16.48 ?  956  LEU B CG    1 
ATOM   16335 C CD1   . LEU B 1 958  ? 15.507  47.786  103.468 1.00 18.51 ?  956  LEU B CD1   1 
ATOM   16336 C CD2   . LEU B 1 958  ? 13.492  49.018  104.315 1.00 18.55 ?  956  LEU B CD2   1 
ATOM   16337 N N     . ASP B 1 959  ? 17.021  52.217  103.623 1.00 17.60 ?  957  ASP B N     1 
ATOM   16338 C CA    . ASP B 1 959  ? 17.044  53.092  102.457 1.00 18.61 ?  957  ASP B CA    1 
ATOM   16339 C C     . ASP B 1 959  ? 18.433  53.138  101.835 1.00 16.51 ?  957  ASP B C     1 
ATOM   16340 O O     . ASP B 1 959  ? 18.570  53.142  100.601 1.00 17.53 ?  957  ASP B O     1 
ATOM   16341 C CB    . ASP B 1 959  ? 16.572  54.495  102.838 1.00 18.41 ?  957  ASP B CB    1 
ATOM   16342 C CG    . ASP B 1 959  ? 16.190  55.326  101.633 1.00 17.91 ?  957  ASP B CG    1 
ATOM   16343 O OD1   . ASP B 1 959  ? 15.409  54.828  100.783 1.00 17.52 ?  957  ASP B OD1   1 
ATOM   16344 O OD2   . ASP B 1 959  ? 16.649  56.482  101.538 1.00 18.31 ?  957  ASP B OD2   1 
ATOM   16345 N N     . ARG B 1 960  ? 19.474  53.176  102.672 1.00 17.87 ?  958  ARG B N     1 
ATOM   16346 C CA    . ARG B 1 960  ? 20.841  53.160  102.167 1.00 19.20 ?  958  ARG B CA    1 
ATOM   16347 C C     . ARG B 1 960  ? 21.153  51.840  101.472 1.00 20.29 ?  958  ARG B C     1 
ATOM   16348 O O     . ARG B 1 960  ? 21.886  51.815  100.476 1.00 20.58 ?  958  ARG B O     1 
ATOM   16349 C CB    . ARG B 1 960  ? 21.809  53.416  103.318 1.00 21.86 ?  958  ARG B CB    1 
ATOM   16350 C CG    . ARG B 1 960  ? 23.276  53.253  102.989 1.00 28.05 ?  958  ARG B CG    1 
ATOM   16351 C CD    . ARG B 1 960  ? 24.088  53.704  104.192 1.00 36.89 ?  958  ARG B CD    1 
ATOM   16352 N NE    . ARG B 1 960  ? 25.433  53.146  104.221 1.00 49.44 ?  958  ARG B NE    1 
ATOM   16353 C CZ    . ARG B 1 960  ? 26.174  53.056  105.317 1.00 56.32 ?  958  ARG B CZ    1 
ATOM   16354 N NH1   . ARG B 1 960  ? 25.713  53.448  106.496 1.00 51.43 ?  958  ARG B NH1   1 
ATOM   16355 N NH2   . ARG B 1 960  ? 27.404  52.557  105.231 1.00 55.37 ?  958  ARG B NH2   1 
ATOM   16356 N N     . LEU B 1 961  ? 20.617  50.734  101.990 1.00 16.14 ?  959  LEU B N     1 
ATOM   16357 C CA    . LEU B 1 961  ? 20.822  49.441  101.347 1.00 16.97 ?  959  LEU B CA    1 
ATOM   16358 C C     . LEU B 1 961  ? 20.196  49.407  99.955  1.00 16.69 ?  959  LEU B C     1 
ATOM   16359 O O     . LEU B 1 961  ? 20.796  48.881  99.009  1.00 17.85 ?  959  LEU B O     1 
ATOM   16360 C CB    . LEU B 1 961  ? 20.248  48.332  102.222 1.00 15.24 ?  959  LEU B CB    1 
ATOM   16361 C CG    . LEU B 1 961  ? 20.162  46.947  101.573 1.00 16.93 ?  959  LEU B CG    1 
ATOM   16362 C CD1   . LEU B 1 961  ? 21.548  46.407  101.256 1.00 21.22 ?  959  LEU B CD1   1 
ATOM   16363 C CD2   . LEU B 1 961  ? 19.402  45.980  102.442 1.00 15.71 ?  959  LEU B CD2   1 
ATOM   16364 N N     . VAL B 1 962  ? 18.991  49.965  99.806  1.00 14.62 ?  960  VAL B N     1 
ATOM   16365 C CA    . VAL B 1 962  ? 18.392  50.067  98.480  1.00 14.61 ?  960  VAL B CA    1 
ATOM   16366 C C     . VAL B 1 962  ? 19.292  50.871  97.551  1.00 16.53 ?  960  VAL B C     1 
ATOM   16367 O O     . VAL B 1 962  ? 19.463  50.512  96.382  1.00 16.75 ?  960  VAL B O     1 
ATOM   16368 C CB    . VAL B 1 962  ? 16.979  50.670  98.578  1.00 15.73 ?  960  VAL B CB    1 
ATOM   16369 C CG1   . VAL B 1 962  ? 16.430  50.960  97.187  1.00 19.01 ?  960  VAL B CG1   1 
ATOM   16370 C CG2   . VAL B 1 962  ? 16.055  49.720  99.333  1.00 15.87 ?  960  VAL B CG2   1 
ATOM   16371 N N     . ASP B 1 963  ? 19.892  51.957  98.056  1.00 16.17 ?  961  ASP B N     1 
ATOM   16372 C CA    . ASP B 1 963  ? 20.898  52.690  97.285  1.00 19.66 ?  961  ASP B CA    1 
ATOM   16373 C C     . ASP B 1 963  ? 22.042  51.779  96.877  1.00 20.67 ?  961  ASP B C     1 
ATOM   16374 O O     . ASP B 1 963  ? 22.501  51.814  95.728  1.00 24.27 ?  961  ASP B O     1 
ATOM   16375 C CB    . ASP B 1 963  ? 21.465  53.850  98.104  1.00 20.68 ?  961  ASP B CB    1 
ATOM   16376 C CG    . ASP B 1 963  ? 20.543  55.029  98.174  1.00 27.03 ?  961  ASP B CG    1 
ATOM   16377 O OD1   . ASP B 1 963  ? 19.574  55.088  97.395  1.00 29.79 ?  961  ASP B OD1   1 
ATOM   16378 O OD2   . ASP B 1 963  ? 20.805  55.911  99.025  1.00 28.97 ?  961  ASP B OD2   1 
ATOM   16379 N N     . ASP B 1 964  ? 22.541  50.982  97.825  1.00 20.35 ?  962  ASP B N     1 
ATOM   16380 C CA    . ASP B 1 964  ? 23.645  50.071  97.537  1.00 21.60 ?  962  ASP B CA    1 
ATOM   16381 C C     . ASP B 1 964  ? 23.279  49.099  96.424  1.00 24.29 ?  962  ASP B C     1 
ATOM   16382 O O     . ASP B 1 964  ? 24.105  48.807  95.554  1.00 22.46 ?  962  ASP B O     1 
ATOM   16383 C CB    . ASP B 1 964  ? 24.053  49.298  98.797  1.00 22.18 ?  962  ASP B CB    1 
ATOM   16384 C CG    . ASP B 1 964  ? 24.761  50.167  99.829  1.00 28.08 ?  962  ASP B CG    1 
ATOM   16385 O OD1   . ASP B 1 964  ? 25.109  51.331  99.515  1.00 26.74 ?  962  ASP B OD1   1 
ATOM   16386 O OD2   . ASP B 1 964  ? 24.967  49.664  100.960 1.00 30.43 ?  962  ASP B OD2   1 
ATOM   16387 N N     . VAL B 1 965  ? 22.038  48.604  96.423  1.00 17.68 ?  963  VAL B N     1 
ATOM   16388 C CA    . VAL B 1 965  ? 21.613  47.678  95.372  1.00 16.07 ?  963  VAL B CA    1 
ATOM   16389 C C     . VAL B 1 965  ? 21.559  48.388  94.026  1.00 18.56 ?  963  VAL B C     1 
ATOM   16390 O O     . VAL B 1 965  ? 22.021  47.849  93.010  1.00 20.82 ?  963  VAL B O     1 
ATOM   16391 C CB    . VAL B 1 965  ? 20.257  47.041  95.730  1.00 15.86 ?  963  VAL B CB    1 
ATOM   16392 C CG1   . VAL B 1 965  ? 19.734  46.215  94.558  1.00 14.81 ?  963  VAL B CG1   1 
ATOM   16393 C CG2   . VAL B 1 965  ? 20.383  46.165  96.957  1.00 17.71 ?  963  VAL B CG2   1 
ATOM   16394 N N     . ASN B 1 966  ? 20.997  49.599  93.991  1.00 16.75 ?  964  ASN B N     1 
ATOM   16395 C CA    . ASN B 1 966  ? 20.901  50.348  92.744  1.00 19.41 ?  964  ASN B CA    1 
ATOM   16396 C C     . ASN B 1 966  ? 22.274  50.762  92.236  1.00 21.79 ?  964  ASN B C     1 
ATOM   16397 O O     . ASN B 1 966  ? 22.443  50.980  91.031  1.00 24.09 ?  964  ASN B O     1 
ATOM   16398 C CB    . ASN B 1 966  ? 20.034  51.594  92.928  1.00 18.41 ?  964  ASN B CB    1 
ATOM   16399 C CG    . ASN B 1 966  ? 18.564  51.270  93.159  1.00 19.01 ?  964  ASN B CG    1 
ATOM   16400 O OD1   . ASN B 1 966  ? 18.081  50.216  92.759  1.00 18.74 ?  964  ASN B OD1   1 
ATOM   16401 N ND2   . ASN B 1 966  ? 17.850  52.190  93.782  1.00 17.78 ?  964  ASN B ND2   1 
ATOM   16402 N N     . ALA B 1 967  ? 23.256  50.873  93.139  1.00 22.39 ?  965  ALA B N     1 
ATOM   16403 C CA    . ALA B 1 967  ? 24.560  51.431  92.802  1.00 22.47 ?  965  ALA B CA    1 
ATOM   16404 C C     . ALA B 1 967  ? 25.364  50.541  91.871  1.00 25.30 ?  965  ALA B C     1 
ATOM   16405 O O     . ALA B 1 967  ? 26.317  51.029  91.251  1.00 27.67 ?  965  ALA B O     1 
ATOM   16406 C CB    . ALA B 1 967  ? 25.368  51.689  94.076  1.00 23.46 ?  965  ALA B CB    1 
ATOM   16407 N N     . THR B 1 968  ? 25.040  49.250  91.780  1.00 21.61 ?  966  THR B N     1 
ATOM   16408 C CA    . THR B 1 968  ? 25.763  48.395  90.849  1.00 21.82 ?  966  THR B CA    1 
ATOM   16409 C C     . THR B 1 968  ? 25.542  48.825  89.408  1.00 26.15 ?  966  THR B C     1 
ATOM   16410 O O     . THR B 1 968  ? 26.367  48.500  88.548  1.00 25.32 ?  966  THR B O     1 
ATOM   16411 C CB    . THR B 1 968  ? 25.352  46.926  91.001  1.00 23.66 ?  966  THR B CB    1 
ATOM   16412 O OG1   . THR B 1 968  ? 24.060  46.716  90.401  1.00 21.18 ?  966  THR B OG1   1 
ATOM   16413 C CG2   . THR B 1 968  ? 25.307  46.521  92.470  1.00 24.14 ?  966  THR B CG2   1 
ATOM   16414 N N     . GLY B 1 969  ? 24.462  49.566  89.131  1.00 22.85 ?  967  GLY B N     1 
ATOM   16415 C CA    . GLY B 1 969  ? 24.102  49.935  87.780  1.00 23.83 ?  967  GLY B CA    1 
ATOM   16416 C C     . GLY B 1 969  ? 23.210  48.935  87.080  1.00 22.40 ?  967  GLY B C     1 
ATOM   16417 O O     . GLY B 1 969  ? 22.656  49.260  86.023  1.00 21.07 ?  967  GLY B O     1 
ATOM   16418 N N     . TYR B 1 970  ? 23.069  47.733  87.631  1.00 20.12 ?  968  TYR B N     1 
ATOM   16419 C CA    . TYR B 1 970  ? 22.163  46.723  87.112  1.00 16.20 ?  968  TYR B CA    1 
ATOM   16420 C C     . TYR B 1 970  ? 20.761  46.963  87.653  1.00 18.82 ?  968  TYR B C     1 
ATOM   16421 O O     . TYR B 1 970  ? 20.554  47.706  88.617  1.00 19.84 ?  968  TYR B O     1 
ATOM   16422 C CB    . TYR B 1 970  ? 22.642  45.324  87.498  1.00 19.18 ?  968  TYR B CB    1 
ATOM   16423 C CG    . TYR B 1 970  ? 23.906  44.905  86.800  1.00 20.50 ?  968  TYR B CG    1 
ATOM   16424 C CD1   . TYR B 1 970  ? 23.862  44.358  85.525  1.00 23.46 ?  968  TYR B CD1   1 
ATOM   16425 C CD2   . TYR B 1 970  ? 25.136  45.026  87.426  1.00 25.00 ?  968  TYR B CD2   1 
ATOM   16426 C CE1   . TYR B 1 970  ? 25.028  43.968  84.874  1.00 28.21 ?  968  TYR B CE1   1 
ATOM   16427 C CE2   . TYR B 1 970  ? 26.298  44.635  86.790  1.00 28.47 ?  968  TYR B CE2   1 
ATOM   16428 C CZ    . TYR B 1 970  ? 26.236  44.109  85.519  1.00 31.48 ?  968  TYR B CZ    1 
ATOM   16429 O OH    . TYR B 1 970  ? 27.396  43.717  84.890  1.00 37.17 ?  968  TYR B OH    1 
ATOM   16430 N N     . GLY B 1 971  ? 19.791  46.311  87.028  1.00 14.68 ?  969  GLY B N     1 
ATOM   16431 C CA    . GLY B 1 971  ? 18.423  46.440  87.487  1.00 15.34 ?  969  GLY B CA    1 
ATOM   16432 C C     . GLY B 1 971  ? 17.542  45.418  86.817  1.00 13.45 ?  969  GLY B C     1 
ATOM   16433 O O     . GLY B 1 971  ? 16.617  45.793  86.087  1.00 14.64 ?  969  GLY B O     1 
ATOM   16434 N N     . LEU B 1 972  ? 17.821  44.132  87.047  1.00 13.29 ?  970  LEU B N     1 
ATOM   16435 C CA    . LEU B 1 972  ? 17.055  43.065  86.408  1.00 12.89 ?  970  LEU B CA    1 
ATOM   16436 C C     . LEU B 1 972  ? 15.981  42.533  87.355  1.00 11.39 ?  970  LEU B C     1 
ATOM   16437 O O     . LEU B 1 972  ? 14.847  43.011  87.299  1.00 13.62 ?  970  LEU B O     1 
ATOM   16438 C CB    . LEU B 1 972  ? 17.984  41.952  85.916  1.00 13.05 ?  970  LEU B CB    1 
ATOM   16439 C CG    . LEU B 1 972  ? 17.321  40.918  85.001  1.00 13.54 ?  970  LEU B CG    1 
ATOM   16440 C CD1   . LEU B 1 972  ? 16.497  41.573  83.885  1.00 16.96 ?  970  LEU B CD1   1 
ATOM   16441 C CD2   . LEU B 1 972  ? 18.374  39.967  84.428  1.00 15.30 ?  970  LEU B CD2   1 
ATOM   16442 N N     . THR B 1 973  ? 16.303  41.559  88.208  1.00 10.85 ?  971  THR B N     1 
ATOM   16443 C CA    . THR B 1 973  ? 15.312  41.043  89.147  1.00 10.80 ?  971  THR B CA    1 
ATOM   16444 C C     . THR B 1 973  ? 15.627  41.529  90.554  1.00 12.20 ?  971  THR B C     1 
ATOM   16445 O O     . THR B 1 973  ? 16.762  41.881  90.877  1.00 12.51 ?  971  THR B O     1 
ATOM   16446 C CB    . THR B 1 973  ? 15.242  39.513  89.137  1.00 10.82 ?  971  THR B CB    1 
ATOM   16447 O OG1   . THR B 1 973  ? 16.523  38.974  89.480  1.00 11.30 ?  971  THR B OG1   1 
ATOM   16448 C CG2   . THR B 1 973  ? 14.807  39.018  87.763  1.00 12.25 ?  971  THR B CG2   1 
ATOM   16449 N N     . PHE B 1 974  ? 14.589  41.537  91.386  1.00 10.44 ?  972  PHE B N     1 
ATOM   16450 C CA    . PHE B 1 974  ? 14.719  41.987  92.762  1.00 10.14 ?  972  PHE B CA    1 
ATOM   16451 C C     . PHE B 1 974  ? 13.616  41.338  93.571  1.00 11.36 ?  972  PHE B C     1 
ATOM   16452 O O     . PHE B 1 974  ? 12.459  41.327  93.137  1.00 11.21 ?  972  PHE B O     1 
ATOM   16453 C CB    . PHE B 1 974  ? 14.601  43.508  92.873  1.00 11.74 ?  972  PHE B CB    1 
ATOM   16454 C CG    . PHE B 1 974  ? 14.544  43.989  94.289  1.00 11.18 ?  972  PHE B CG    1 
ATOM   16455 C CD1   . PHE B 1 974  ? 15.711  44.131  95.005  1.00 12.59 ?  972  PHE B CD1   1 
ATOM   16456 C CD2   . PHE B 1 974  ? 13.332  44.301  94.890  1.00 12.06 ?  972  PHE B CD2   1 
ATOM   16457 C CE1   . PHE B 1 974  ? 15.693  44.565  96.327  1.00 13.46 ?  972  PHE B CE1   1 
ATOM   16458 C CE2   . PHE B 1 974  ? 13.298  44.737  96.210  1.00 11.40 ?  972  PHE B CE2   1 
ATOM   16459 C CZ    . PHE B 1 974  ? 14.478  44.863  96.929  1.00 13.71 ?  972  PHE B CZ    1 
ATOM   16460 N N     . GLY B 1 975  ? 13.962  40.843  94.756  1.00 11.26 ?  973  GLY B N     1 
ATOM   16461 C CA    . GLY B 1 975  ? 12.987  40.253  95.654  1.00 11.48 ?  973  GLY B CA    1 
ATOM   16462 C C     . GLY B 1 975  ? 12.906  40.972  96.988  1.00 10.97 ?  973  GLY B C     1 
ATOM   16463 O O     . GLY B 1 975  ? 13.895  41.504  97.488  1.00 11.93 ?  973  GLY B O     1 
ATOM   16464 N N     . LEU B 1 976  ? 11.703  40.980  97.557  1.00 11.94 ?  974  LEU B N     1 
ATOM   16465 C CA    . LEU B 1 976  ? 11.459  41.539  98.880  1.00 11.71 ?  974  LEU B CA    1 
ATOM   16466 C C     . LEU B 1 976  ? 10.559  40.585  99.631  1.00 10.76 ?  974  LEU B C     1 
ATOM   16467 O O     . LEU B 1 976  ? 9.487   40.226  99.137  1.00 12.10 ?  974  LEU B O     1 
ATOM   16468 C CB    . LEU B 1 976  ? 10.793  42.912  98.803  1.00 12.83 ?  974  LEU B CB    1 
ATOM   16469 C CG    . LEU B 1 976  ? 10.374  43.557  100.131 1.00 12.65 ?  974  LEU B CG    1 
ATOM   16470 C CD1   . LEU B 1 976  ? 11.579  43.878  100.987 1.00 14.65 ?  974  LEU B CD1   1 
ATOM   16471 C CD2   . LEU B 1 976  ? 9.548   44.803  99.839  1.00 15.65 ?  974  LEU B CD2   1 
ATOM   16472 N N     . HIS B 1 977  ? 10.999  40.177  100.825 1.00 12.58 ?  975  HIS B N     1 
ATOM   16473 C CA    . HIS B 1 977  ? 10.196  39.363  101.728 1.00 11.43 ?  975  HIS B CA    1 
ATOM   16474 C C     . HIS B 1 977  ? 9.912   40.189  102.974 1.00 12.64 ?  975  HIS B C     1 
ATOM   16475 O O     . HIS B 1 977  ? 10.823  40.498  103.750 1.00 13.13 ?  975  HIS B O     1 
ATOM   16476 C CB    . HIS B 1 977  ? 10.915  38.065  102.096 1.00 14.03 ?  975  HIS B CB    1 
ATOM   16477 C CG    . HIS B 1 977  ? 10.553  36.899  101.235 1.00 15.93 ?  975  HIS B CG    1 
ATOM   16478 N ND1   . HIS B 1 977  ? 9.664   35.926  101.640 1.00 21.85 ?  975  HIS B ND1   1 
ATOM   16479 C CD2   . HIS B 1 977  ? 10.960  36.547  99.993  1.00 21.20 ?  975  HIS B CD2   1 
ATOM   16480 C CE1   . HIS B 1 977  ? 9.551   35.016  100.688 1.00 19.35 ?  975  HIS B CE1   1 
ATOM   16481 N NE2   . HIS B 1 977  ? 10.325  35.370  99.681  1.00 21.25 ?  975  HIS B NE2   1 
ATOM   16482 N N     . THR B 1 978  ? 8.646   40.518  103.166 1.00 12.19 ?  976  THR B N     1 
ATOM   16483 C CA    . THR B 1 978  ? 8.155   41.294  104.294 1.00 11.86 ?  976  THR B CA    1 
ATOM   16484 C C     . THR B 1 978  ? 6.651   41.146  104.325 1.00 12.00 ?  976  THR B C     1 
ATOM   16485 O O     . THR B 1 978  ? 6.015   40.946  103.288 1.00 13.86 ?  976  THR B O     1 
ATOM   16486 C CB    . THR B 1 978  ? 8.517   42.777  104.183 1.00 12.69 ?  976  THR B CB    1 
ATOM   16487 O OG1   . THR B 1 978  ? 7.958   43.483  105.294 1.00 14.74 ?  976  THR B OG1   1 
ATOM   16488 C CG2   . THR B 1 978  ? 7.942   43.376  102.921 1.00 16.06 ?  976  THR B CG2   1 
ATOM   16489 N N     . ARG B 1 979  ? 6.089   41.257  105.521 1.00 13.54 ?  977  ARG B N     1 
ATOM   16490 C CA    . ARG B 1 979  ? 4.645   41.306  105.667 1.00 14.05 ?  977  ARG B CA    1 
ATOM   16491 C C     . ARG B 1 979  ? 4.106   42.720  105.773 1.00 13.97 ?  977  ARG B C     1 
ATOM   16492 O O     . ARG B 1 979  ? 2.891   42.890  105.857 1.00 17.19 ?  977  ARG B O     1 
ATOM   16493 C CB    . ARG B 1 979  ? 4.220   40.511  106.896 1.00 16.89 ?  977  ARG B CB    1 
ATOM   16494 C CG    . ARG B 1 979  ? 4.485   39.043  106.702 1.00 21.67 ?  977  ARG B CG    1 
ATOM   16495 C CD    . ARG B 1 979  ? 4.182   38.293  107.951 1.00 25.98 ?  977  ARG B CD    1 
ATOM   16496 N NE    . ARG B 1 979  ? 4.235   36.858  107.728 1.00 27.91 ?  977  ARG B NE    1 
ATOM   16497 C CZ    . ARG B 1 979  ? 3.912   35.961  108.648 1.00 31.04 ?  977  ARG B CZ    1 
ATOM   16498 N NH1   . ARG B 1 979  ? 3.536   36.330  109.866 1.00 26.74 ?  977  ARG B NH1   1 
ATOM   16499 N NH2   . ARG B 1 979  ? 3.963   34.667  108.338 1.00 30.51 ?  977  ARG B NH2   1 
ATOM   16500 N N     . LEU B 1 980  ? 4.968   43.731  105.766 1.00 12.76 ?  978  LEU B N     1 
ATOM   16501 C CA    . LEU B 1 980  ? 4.585   45.078  106.183 1.00 13.88 ?  978  LEU B CA    1 
ATOM   16502 C C     . LEU B 1 980  ? 4.389   45.977  104.969 1.00 13.52 ?  978  LEU B C     1 
ATOM   16503 O O     . LEU B 1 980  ? 5.324   46.186  104.188 1.00 14.41 ?  978  LEU B O     1 
ATOM   16504 C CB    . LEU B 1 980  ? 5.645   45.672  107.106 1.00 13.95 ?  978  LEU B CB    1 
ATOM   16505 C CG    . LEU B 1 980  ? 6.044   44.744  108.246 1.00 14.99 ?  978  LEU B CG    1 
ATOM   16506 C CD1   . LEU B 1 980  ? 7.169   45.380  109.064 1.00 16.92 ?  978  LEU B CD1   1 
ATOM   16507 C CD2   . LEU B 1 980  ? 4.828   44.456  109.097 1.00 15.43 ?  978  LEU B CD2   1 
ATOM   16508 N N     . ASP B 1 981  ? 3.188   46.554  104.848 1.00 13.63 ?  979  ASP B N     1 
ATOM   16509 C CA    . ASP B 1 981  ? 2.882   47.417  103.707 1.00 13.65 ?  979  ASP B CA    1 
ATOM   16510 C C     . ASP B 1 981  ? 3.786   48.639  103.619 1.00 13.78 ?  979  ASP B C     1 
ATOM   16511 O O     . ASP B 1 981  ? 4.076   49.092  102.510 1.00 13.57 ?  979  ASP B O     1 
ATOM   16512 C CB    . ASP B 1 981  ? 1.435   47.902  103.758 1.00 13.94 ?  979  ASP B CB    1 
ATOM   16513 C CG    . ASP B 1 981  ? 0.437   46.821  103.447 1.00 16.51 ?  979  ASP B CG    1 
ATOM   16514 O OD1   . ASP B 1 981  ? 0.797   45.794  102.852 1.00 17.05 ?  979  ASP B OD1   1 
ATOM   16515 O OD2   . ASP B 1 981  ? -0.737  47.028  103.811 1.00 19.32 ?  979  ASP B OD2   1 
ATOM   16516 N N     . GLU B 1 982  ? 4.204   49.222  104.750 1.00 13.20 ?  980  GLU B N     1 
ATOM   16517 C CA    . GLU B 1 982  ? 5.072   50.395  104.657 1.00 13.54 ?  980  GLU B CA    1 
ATOM   16518 C C     . GLU B 1 982  ? 6.420   50.023  104.055 1.00 13.48 ?  980  GLU B C     1 
ATOM   16519 O O     . GLU B 1 982  ? 6.982   50.775  103.252 1.00 14.77 ?  980  GLU B O     1 
ATOM   16520 C CB    . GLU B 1 982  ? 5.264   51.054  106.026 1.00 14.46 ?  980  GLU B CB    1 
ATOM   16521 C CG    . GLU B 1 982  ? 6.297   52.176  105.991 1.00 18.38 ?  980  GLU B CG    1 
ATOM   16522 C CD    . GLU B 1 982  ? 6.755   52.623  107.363 1.00 23.74 ?  980  GLU B CD    1 
ATOM   16523 O OE1   . GLU B 1 982  ? 7.061   51.751  108.209 1.00 30.26 ?  980  GLU B OE1   1 
ATOM   16524 O OE2   . GLU B 1 982  ? 6.821   53.845  107.592 1.00 23.27 ?  980  GLU B OE2   1 
ATOM   16525 N N     . THR B 1 983  ? 6.955   48.860  104.430 1.00 13.14 ?  981  THR B N     1 
ATOM   16526 C CA    . THR B 1 983  ? 8.219   48.414  103.856 1.00 13.26 ?  981  THR B CA    1 
ATOM   16527 C C     . THR B 1 983  ? 8.070   48.094  102.371 1.00 11.92 ?  981  THR B C     1 
ATOM   16528 O O     . THR B 1 983  ? 8.953   48.425  101.572 1.00 14.18 ?  981  THR B O     1 
ATOM   16529 C CB    . THR B 1 983  ? 8.727   47.210  104.639 1.00 14.04 ?  981  THR B CB    1 
ATOM   16530 O OG1   . THR B 1 983  ? 8.949   47.633  105.988 1.00 16.54 ?  981  THR B OG1   1 
ATOM   16531 C CG2   . THR B 1 983  ? 10.047  46.709  104.052 1.00 15.69 ?  981  THR B CG2   1 
ATOM   16532 N N     . ILE B 1 984  ? 6.954   47.475  101.981 1.00 11.43 ?  982  ILE B N     1 
ATOM   16533 C CA    . ILE B 1 984  ? 6.709   47.213  100.563 1.00 13.06 ?  982  ILE B CA    1 
ATOM   16534 C C     . ILE B 1 984  ? 6.667   48.518  99.772  1.00 11.98 ?  982  ILE B C     1 
ATOM   16535 O O     . ILE B 1 984  ? 7.309   48.643  98.723  1.00 12.71 ?  982  ILE B O     1 
ATOM   16536 C CB    . ILE B 1 984  ? 5.419   46.398  100.383 1.00 12.96 ?  982  ILE B CB    1 
ATOM   16537 C CG1   . ILE B 1 984  ? 5.592   45.015  101.007 1.00 16.56 ?  982  ILE B CG1   1 
ATOM   16538 C CG2   . ILE B 1 984  ? 5.076   46.265  98.887  1.00 14.95 ?  982  ILE B CG2   1 
ATOM   16539 C CD1   . ILE B 1 984  ? 4.315   44.199  101.052 1.00 17.90 ?  982  ILE B CD1   1 
ATOM   16540 N N     . ALA B 1 985  ? 5.943   49.522  100.277 1.00 13.29 ?  983  ALA B N     1 
ATOM   16541 C CA    . ALA B 1 985  ? 5.832   50.780  99.535  1.00 14.50 ?  983  ALA B CA    1 
ATOM   16542 C C     . ALA B 1 985  ? 7.175   51.486  99.452  1.00 14.38 ?  983  ALA B C     1 
ATOM   16543 O O     . ALA B 1 985  ? 7.556   51.996  98.390  1.00 14.09 ?  983  ALA B O     1 
ATOM   16544 C CB    . ALA B 1 985  ? 4.794   51.692  100.184 1.00 14.43 ?  983  ALA B CB    1 
ATOM   16545 N N     . HIS B 1 986  ? 7.900   51.527  100.566 1.00 13.42 ?  984  HIS B N     1 
ATOM   16546 C CA    . HIS B 1 986  ? 9.216   52.156  100.587 1.00 14.09 ?  984  HIS B CA    1 
ATOM   16547 C C     . HIS B 1 986  ? 10.146  51.484  99.587  1.00 13.32 ?  984  HIS B C     1 
ATOM   16548 O O     . HIS B 1 986  ? 10.689  52.127  98.683  1.00 15.46 ?  984  HIS B O     1 
ATOM   16549 C CB    . HIS B 1 986  ? 9.794   52.080  102.004 1.00 14.99 ?  984  HIS B CB    1 
ATOM   16550 C CG    . HIS B 1 986  ? 11.192  52.607  102.139 1.00 16.30 ?  984  HIS B CG    1 
ATOM   16551 N ND1   . HIS B 1 986  ? 11.809  52.734  103.364 1.00 22.81 ?  984  HIS B ND1   1 
ATOM   16552 C CD2   . HIS B 1 986  ? 12.090  53.043  101.220 1.00 17.61 ?  984  HIS B CD2   1 
ATOM   16553 C CE1   . HIS B 1 986  ? 13.024  53.228  103.195 1.00 19.57 ?  984  HIS B CE1   1 
ATOM   16554 N NE2   . HIS B 1 986  ? 13.228  53.406  101.903 1.00 19.33 ?  984  HIS B NE2   1 
ATOM   16555 N N     . VAL B 1 987  ? 10.335  50.179  99.730  1.00 12.03 ?  985  VAL B N     1 
ATOM   16556 C CA    . VAL B 1 987  ? 11.326  49.496  98.901  1.00 13.50 ?  985  VAL B CA    1 
ATOM   16557 C C     . VAL B 1 987  ? 10.926  49.509  97.428  1.00 14.35 ?  985  VAL B C     1 
ATOM   16558 O O     . VAL B 1 987  ? 11.765  49.762  96.554  1.00 16.16 ?  985  VAL B O     1 
ATOM   16559 C CB    . VAL B 1 987  ? 11.554  48.068  99.416  1.00 12.84 ?  985  VAL B CB    1 
ATOM   16560 C CG1   . VAL B 1 987  ? 12.415  47.280  98.432  1.00 17.68 ?  985  VAL B CG1   1 
ATOM   16561 C CG2   . VAL B 1 987  ? 12.210  48.113  100.794 1.00 13.79 ?  985  VAL B CG2   1 
ATOM   16562 N N     . THR B 1 988  ? 9.664   49.222  97.110  1.00 12.33 ?  986  THR B N     1 
ATOM   16563 C CA    . THR B 1 988  ? 9.338   49.169  95.685  1.00 12.94 ?  986  THR B CA    1 
ATOM   16564 C C     . THR B 1 988  ? 9.345   50.557  95.047  1.00 15.65 ?  986  THR B C     1 
ATOM   16565 O O     . THR B 1 988  ? 9.568   50.669  93.834  1.00 21.11 ?  986  THR B O     1 
ATOM   16566 C CB    . THR B 1 988  ? 7.997   48.466  95.442  1.00 17.32 ?  986  THR B CB    1 
ATOM   16567 O OG1   . THR B 1 988  ? 6.944   49.193  96.058  1.00 19.20 ?  986  THR B OG1   1 
ATOM   16568 C CG2   . THR B 1 988  ? 8.035   47.027  95.954  1.00 20.12 ?  986  THR B CG2   1 
ATOM   16569 N N     . SER B 1 989  ? 9.151   51.619  95.827  1.00 15.70 ?  987  SER B N     1 
ATOM   16570 C CA    . SER B 1 989  ? 9.234   52.959  95.254  1.00 18.03 ?  987  SER B CA    1 
ATOM   16571 C C     . SER B 1 989  ? 10.670  53.398  94.997  1.00 20.29 ?  987  SER B C     1 
ATOM   16572 O O     . SER B 1 989  ? 10.887  54.276  94.156  1.00 27.23 ?  987  SER B O     1 
ATOM   16573 C CB    . SER B 1 989  ? 8.532   53.984  96.160  1.00 19.76 ?  987  SER B CB    1 
ATOM   16574 O OG    . SER B 1 989  ? 9.261   54.262  97.347  1.00 25.45 ?  987  SER B OG    1 
ATOM   16575 N N     . ARG B 1 990  ? 11.653  52.805  95.679  1.00 15.66 ?  988  ARG B N     1 
ATOM   16576 C CA    . ARG B 1 990  ? 13.033  53.274  95.609  1.00 17.26 ?  988  ARG B CA    1 
ATOM   16577 C C     . ARG B 1 990  ? 13.944  52.352  94.822  1.00 16.17 ?  988  ARG B C     1 
ATOM   16578 O O     . ARG B 1 990  ? 14.969  52.808  94.314  1.00 17.56 ?  988  ARG B O     1 
ATOM   16579 C CB    . ARG B 1 990  ? 13.618  53.456  97.019  1.00 18.14 ?  988  ARG B CB    1 
ATOM   16580 C CG    . ARG B 1 990  ? 12.795  54.339  97.976  1.00 25.01 ?  988  ARG B CG    1 
ATOM   16581 C CD    . ARG B 1 990  ? 13.056  55.816  97.763  1.00 24.35 ?  988  ARG B CD    1 
ATOM   16582 N NE    . ARG B 1 990  ? 14.211  56.308  98.510  1.00 19.68 ?  988  ARG B NE    1 
ATOM   16583 C CZ    . ARG B 1 990  ? 14.657  57.553  98.427  1.00 18.51 ?  988  ARG B CZ    1 
ATOM   16584 N NH1   . ARG B 1 990  ? 14.105  58.428  97.603  1.00 21.51 ?  988  ARG B NH1   1 
ATOM   16585 N NH2   . ARG B 1 990  ? 15.682  57.929  99.185  1.00 19.46 ?  988  ARG B NH2   1 
ATOM   16586 N N     . ILE B 1 991  ? 13.601  51.068  94.709  1.00 14.90 ?  989  ILE B N     1 
ATOM   16587 C CA    . ILE B 1 991  ? 14.423  50.146  93.938  1.00 15.43 ?  989  ILE B CA    1 
ATOM   16588 C C     . ILE B 1 991  ? 14.259  50.447  92.452  1.00 15.28 ?  989  ILE B C     1 
ATOM   16589 O O     . ILE B 1 991  ? 13.193  50.882  91.998  1.00 17.01 ?  989  ILE B O     1 
ATOM   16590 C CB    . ILE B 1 991  ? 14.025  48.695  94.269  1.00 13.79 ?  989  ILE B CB    1 
ATOM   16591 C CG1   . ILE B 1 991  ? 15.088  47.715  93.773  1.00 16.88 ?  989  ILE B CG1   1 
ATOM   16592 C CG2   . ILE B 1 991  ? 12.627  48.364  93.716  1.00 17.91 ?  989  ILE B CG2   1 
ATOM   16593 C CD1   . ILE B 1 991  ? 16.361  47.816  94.601  1.00 20.48 ?  989  ILE B CD1   1 
ATOM   16594 N N     . LYS B 1 992  ? 15.328  50.240  91.690  1.00 14.53 ?  990  LYS B N     1 
ATOM   16595 C CA    . LYS B 1 992  ? 15.320  50.491  90.246  1.00 16.46 ?  990  LYS B CA    1 
ATOM   16596 C C     . LYS B 1 992  ? 15.635  49.182  89.532  1.00 18.80 ?  990  LYS B C     1 
ATOM   16597 O O     . LYS B 1 992  ? 16.776  48.931  89.147  1.00 22.64 ?  990  LYS B O     1 
ATOM   16598 C CB    . LYS B 1 992  ? 16.336  51.594  89.864  1.00 18.86 ?  990  LYS B CB    1 
ATOM   16599 C CG    . LYS B 1 992  ? 16.042  52.961  90.465  1.00 20.22 ?  990  LYS B CG    1 
ATOM   16600 C CD    . LYS B 1 992  ? 14.769  53.561  89.899  1.00 31.28 ?  990  LYS B CD    1 
ATOM   16601 C CE    . LYS B 1 992  ? 14.669  55.049  90.213  1.00 38.01 ?  990  LYS B CE    1 
ATOM   16602 N NZ    . LYS B 1 992  ? 13.385  55.628  89.728  1.00 48.92 ?  990  LYS B NZ    1 
ATOM   16603 N N     . ALA B 1 993  ? 14.625  48.334  89.377  1.00 15.85 ?  991  ALA B N     1 
ATOM   16604 C CA    . ALA B 1 993  ? 14.801  47.061  88.692  1.00 13.72 ?  991  ALA B CA    1 
ATOM   16605 C C     . ALA B 1 993  ? 13.560  46.760  87.874  1.00 13.20 ?  991  ALA B C     1 
ATOM   16606 O O     . ALA B 1 993  ? 12.463  47.225  88.194  1.00 14.95 ?  991  ALA B O     1 
ATOM   16607 C CB    . ALA B 1 993  ? 15.063  45.905  89.659  1.00 14.82 ?  991  ALA B CB    1 
ATOM   16608 N N     . GLY B 1 994  ? 13.742  45.949  86.830  1.00 12.04 ?  992  GLY B N     1 
ATOM   16609 C CA    . GLY B 1 994  ? 12.657  45.719  85.884  1.00 11.07 ?  992  GLY B CA    1 
ATOM   16610 C C     . GLY B 1 994  ? 11.654  44.661  86.292  1.00 10.51 ?  992  GLY B C     1 
ATOM   16611 O O     . GLY B 1 994  ? 10.512  44.708  85.831  1.00 10.76 ?  992  GLY B O     1 
ATOM   16612 N N     . ASN B 1 995  ? 12.045  43.711  87.142  1.00 9.89  ?  993  ASN B N     1 
ATOM   16613 C CA    . ASN B 1 995  ? 11.192  42.595  87.549  1.00 10.38 ?  993  ASN B CA    1 
ATOM   16614 C C     . ASN B 1 995  ? 11.281  42.484  89.059  1.00 10.51 ?  993  ASN B C     1 
ATOM   16615 O O     . ASN B 1 995  ? 12.295  42.024  89.589  1.00 12.30 ?  993  ASN B O     1 
ATOM   16616 C CB    . ASN B 1 995  ? 11.617  41.295  86.868  1.00 10.43 ?  993  ASN B CB    1 
ATOM   16617 C CG    . ASN B 1 995  ? 11.097  41.200  85.451  1.00 12.22 ?  993  ASN B CG    1 
ATOM   16618 O OD1   . ASN B 1 995  ? 11.714  41.701  84.510  1.00 11.46 ?  993  ASN B OD1   1 
ATOM   16619 N ND2   . ASN B 1 995  ? 9.943   40.579  85.297  1.00 12.86 ?  993  ASN B ND2   1 
ATOM   16620 N N     . LEU B 1 996  ? 10.215  42.901  89.728  1.00 9.60  ?  994  LEU B N     1 
ATOM   16621 C CA    . LEU B 1 996  ? 10.122  42.895  91.182  1.00 9.06  ?  994  LEU B CA    1 
ATOM   16622 C C     . LEU B 1 996  ? 9.271   41.712  91.613  1.00 12.56 ?  994  LEU B C     1 
ATOM   16623 O O     . LEU B 1 996  ? 8.280   41.373  90.954  1.00 12.03 ?  994  LEU B O     1 
ATOM   16624 C CB    . LEU B 1 996  ? 9.495   44.191  91.702  1.00 11.25 ?  994  LEU B CB    1 
ATOM   16625 C CG    . LEU B 1 996  ? 10.046  45.476  91.084  1.00 12.14 ?  994  LEU B CG    1 
ATOM   16626 C CD1   . LEU B 1 996  ? 9.291   46.665  91.696  1.00 15.64 ?  994  LEU B CD1   1 
ATOM   16627 C CD2   . LEU B 1 996  ? 11.544  45.610  91.315  1.00 15.60 ?  994  LEU B CD2   1 
ATOM   16628 N N     . TYR B 1 997  ? 9.653   41.089  92.722  1.00 10.73 ?  995  TYR B N     1 
ATOM   16629 C CA    . TYR B 1 997  ? 8.945   39.929  93.244  1.00 9.95  ?  995  TYR B CA    1 
ATOM   16630 C C     . TYR B 1 997  ? 8.764   40.104  94.739  1.00 11.24 ?  995  TYR B C     1 
ATOM   16631 O O     . TYR B 1 997  ? 9.741   40.354  95.453  1.00 10.95 ?  995  TYR B O     1 
ATOM   16632 C CB    . TYR B 1 997  ? 9.721   38.644  92.965  1.00 10.62 ?  995  TYR B CB    1 
ATOM   16633 C CG    . TYR B 1 997  ? 9.877   38.361  91.484  1.00 10.24 ?  995  TYR B CG    1 
ATOM   16634 C CD1   . TYR B 1 997  ? 8.852   37.760  90.766  1.00 13.07 ?  995  TYR B CD1   1 
ATOM   16635 C CD2   . TYR B 1 997  ? 11.022  38.744  90.801  1.00 11.44 ?  995  TYR B CD2   1 
ATOM   16636 C CE1   . TYR B 1 997  ? 8.985   37.493  89.395  1.00 12.73 ?  995  TYR B CE1   1 
ATOM   16637 C CE2   . TYR B 1 997  ? 11.159  38.488  89.415  1.00 12.26 ?  995  TYR B CE2   1 
ATOM   16638 C CZ    . TYR B 1 997  ? 10.131  37.866  88.740  1.00 12.88 ?  995  TYR B CZ    1 
ATOM   16639 O OH    . TYR B 1 997  ? 10.228  37.594  87.381  1.00 13.01 ?  995  TYR B OH    1 
ATOM   16640 N N     . ILE B 1 998  ? 7.533   39.961  95.210  1.00 9.85  ?  996  ILE B N     1 
ATOM   16641 C CA    . ILE B 1 998  ? 7.202   40.195  96.611  1.00 10.89 ?  996  ILE B CA    1 
ATOM   16642 C C     . ILE B 1 998  ? 6.722   38.884  97.231  1.00 10.34 ?  996  ILE B C     1 
ATOM   16643 O O     . ILE B 1 998  ? 5.696   38.323  96.818  1.00 11.22 ?  996  ILE B O     1 
ATOM   16644 C CB    . ILE B 1 998  ? 6.137   41.286  96.762  1.00 11.49 ?  996  ILE B CB    1 
ATOM   16645 C CG1   . ILE B 1 998  ? 6.540   42.582  96.050  1.00 16.78 ?  996  ILE B CG1   1 
ATOM   16646 C CG2   . ILE B 1 998  ? 5.883   41.577  98.245  1.00 12.78 ?  996  ILE B CG2   1 
ATOM   16647 C CD1   . ILE B 1 998  ? 7.840   43.112  96.423  1.00 19.82 ?  996  ILE B CD1   1 
ATOM   16648 N N     . ASN B 1 999  ? 7.469   38.410  98.238  1.00 10.58 ?  997  ASN B N     1 
ATOM   16649 C CA    . ASN B 1 999  ? 7.104   37.232  99.029  1.00 10.66 ?  997  ASN B CA    1 
ATOM   16650 C C     . ASN B 1 999  ? 7.033   35.969  98.176  1.00 10.24 ?  997  ASN B C     1 
ATOM   16651 O O     . ASN B 1 999  ? 6.201   35.094  98.407  1.00 12.21 ?  997  ASN B O     1 
ATOM   16652 C CB    . ASN B 1 999  ? 5.799   37.462  99.795  1.00 12.20 ?  997  ASN B CB    1 
ATOM   16653 C CG    . ASN B 1 999  ? 5.975   38.486  100.892 1.00 10.19 ?  997  ASN B CG    1 
ATOM   16654 O OD1   . ASN B 1 999  ? 7.062   38.610  101.456 1.00 12.73 ?  997  ASN B OD1   1 
ATOM   16655 N ND2   . ASN B 1 999  ? 4.924   39.237  101.192 1.00 11.37 ?  997  ASN B ND2   1 
ATOM   16656 N N     . ARG B 1 1000 ? 7.945   35.869  97.207  1.00 10.72 ?  998  ARG B N     1 
ATOM   16657 C CA    . ARG B 1 1000 ? 8.085   34.693  96.351  1.00 9.81  ?  998  ARG B CA    1 
ATOM   16658 C C     . ARG B 1 1000 ? 9.513   34.667  95.825  1.00 12.29 ?  998  ARG B C     1 
ATOM   16659 O O     . ARG B 1 1000 ? 10.317  35.554  96.119  1.00 13.86 ?  998  ARG B O     1 
ATOM   16660 C CB    . ARG B 1 1000 ? 7.063   34.700  95.202  1.00 11.76 ?  998  ARG B CB    1 
ATOM   16661 C CG    . ARG B 1 1000 ? 7.005   36.010  94.452  1.00 11.14 ?  998  ARG B CG    1 
ATOM   16662 C CD    . ARG B 1 1000 ? 6.495   35.783  93.028  1.00 11.26 ?  998  ARG B CD    1 
ATOM   16663 N NE    . ARG B 1 1000 ? 7.493   35.040  92.276  1.00 10.96 ?  998  ARG B NE    1 
ATOM   16664 C CZ    . ARG B 1 1000 ? 7.357   34.687  91.008  1.00 11.38 ?  998  ARG B CZ    1 
ATOM   16665 N NH1   . ARG B 1 1000 ? 6.275   35.010  90.309  1.00 11.93 ?  998  ARG B NH1   1 
ATOM   16666 N NH2   . ARG B 1 1000 ? 8.335   34.007  90.420  1.00 12.74 ?  998  ARG B NH2   1 
ATOM   16667 N N     . ASN B 1 1001 ? 9.832   33.634  95.043  1.00 11.72 ?  999  ASN B N     1 
ATOM   16668 C CA    . ASN B 1 1001 ? 11.154  33.586  94.443  1.00 11.27 ?  999  ASN B CA    1 
ATOM   16669 C C     . ASN B 1 1001 ? 11.244  34.601  93.298  1.00 11.31 ?  999  ASN B C     1 
ATOM   16670 O O     . ASN B 1 1001 ? 10.254  35.229  92.907  1.00 11.74 ?  999  ASN B O     1 
ATOM   16671 C CB    . ASN B 1 1001 ? 11.494  32.154  93.988  1.00 11.13 ?  999  ASN B CB    1 
ATOM   16672 C CG    . ASN B 1 1001 ? 10.704  31.685  92.773  1.00 15.65 ?  999  ASN B CG    1 
ATOM   16673 O OD1   . ASN B 1 1001 ? 10.537  32.402  91.797  1.00 13.32 ?  999  ASN B OD1   1 
ATOM   16674 N ND2   . ASN B 1 1001 ? 10.255  30.437  92.825  1.00 19.18 ?  999  ASN B ND2   1 
ATOM   16675 N N     . ILE B 1 1002 ? 12.453  34.789  92.781  1.00 11.06 ?  1000 ILE B N     1 
ATOM   16676 C CA    . ILE B 1 1002 ? 12.689  35.857  91.817  1.00 10.65 ?  1000 ILE B CA    1 
ATOM   16677 C C     . ILE B 1 1002 ? 13.005  35.303  90.427  1.00 11.93 ?  1000 ILE B C     1 
ATOM   16678 O O     . ILE B 1 1002 ? 13.520  36.034  89.585  1.00 11.68 ?  1000 ILE B O     1 
ATOM   16679 C CB    . ILE B 1 1002 ? 13.774  36.841  92.298  1.00 10.88 ?  1000 ILE B CB    1 
ATOM   16680 C CG1   . ILE B 1 1002 ? 15.192  36.230  92.323  1.00 11.34 ?  1000 ILE B CG1   1 
ATOM   16681 C CG2   . ILE B 1 1002 ? 13.389  37.405  93.675  1.00 12.79 ?  1000 ILE B CG2   1 
ATOM   16682 C CD1   . ILE B 1 1002 ? 16.265  37.274  92.647  1.00 13.53 ?  1000 ILE B CD1   1 
ATOM   16683 N N     . ILE B 1 1003 ? 12.709  34.025  90.173  1.00 12.55 ?  1001 ILE B N     1 
ATOM   16684 C CA    . ILE B 1 1003 ? 13.080  33.382  88.916  1.00 12.34 ?  1001 ILE B CA    1 
ATOM   16685 C C     . ILE B 1 1003 ? 11.841  32.881  88.173  1.00 11.54 ?  1001 ILE B C     1 
ATOM   16686 O O     . ILE B 1 1003 ? 10.725  32.855  88.693  1.00 12.45 ?  1001 ILE B O     1 
ATOM   16687 C CB    . ILE B 1 1003 ? 14.068  32.221  89.117  1.00 13.95 ?  1001 ILE B CB    1 
ATOM   16688 C CG1   . ILE B 1 1003 ? 13.469  31.139  90.022  1.00 14.98 ?  1001 ILE B CG1   1 
ATOM   16689 C CG2   . ILE B 1 1003 ? 15.384  32.740  89.669  1.00 13.70 ?  1001 ILE B CG2   1 
ATOM   16690 C CD1   . ILE B 1 1003 ? 14.276  29.837  89.983  1.00 18.35 ?  1001 ILE B CD1   1 
ATOM   16691 N N     . GLY B 1 1004 ? 12.063  32.473  86.931  1.00 12.92 ?  1002 GLY B N     1 
ATOM   16692 C CA    . GLY B 1 1004 ? 10.991  31.884  86.148  1.00 12.19 ?  1002 GLY B CA    1 
ATOM   16693 C C     . GLY B 1 1004 ? 9.904   32.847  85.716  1.00 12.73 ?  1002 GLY B C     1 
ATOM   16694 O O     . GLY B 1 1004 ? 8.721   32.503  85.789  1.00 14.41 ?  1002 GLY B O     1 
ATOM   16695 N N     . ALA B 1 1005 ? 10.279  34.049  85.274  1.00 11.72 ?  1003 ALA B N     1 
ATOM   16696 C CA    . ALA B 1 1005 ? 9.304   34.992  84.737  1.00 11.91 ?  1003 ALA B CA    1 
ATOM   16697 C C     . ALA B 1 1005 ? 8.463   34.332  83.652  1.00 13.41 ?  1003 ALA B C     1 
ATOM   16698 O O     . ALA B 1 1005 ? 8.974   33.592  82.804  1.00 16.56 ?  1003 ALA B O     1 
ATOM   16699 C CB    . ALA B 1 1005 ? 10.005  36.226  84.175  1.00 11.98 ?  1003 ALA B CB    1 
ATOM   16700 N N     . VAL B 1 1006 ? 7.167   34.601  83.701  1.00 11.11 ?  1004 VAL B N     1 
ATOM   16701 C CA    . VAL B 1 1006 ? 6.180   33.970  82.832  1.00 10.79 ?  1004 VAL B CA    1 
ATOM   16702 C C     . VAL B 1 1006 ? 5.797   34.950  81.733  1.00 10.61 ?  1004 VAL B C     1 
ATOM   16703 O O     . VAL B 1 1006 ? 5.415   36.096  82.014  1.00 10.15 ?  1004 VAL B O     1 
ATOM   16704 C CB    . VAL B 1 1006 ? 4.948   33.525  83.642  1.00 10.70 ?  1004 VAL B CB    1 
ATOM   16705 C CG1   . VAL B 1 1006 ? 3.809   33.087  82.723  1.00 12.07 ?  1004 VAL B CG1   1 
ATOM   16706 C CG2   . VAL B 1 1006 ? 5.331   32.402  84.612  1.00 11.95 ?  1004 VAL B CG2   1 
ATOM   16707 N N     . VAL B 1 1007 ? 5.913   34.493  80.476  1.00 10.26 ?  1005 VAL B N     1 
ATOM   16708 C CA    . VAL B 1 1007 ? 5.587   35.303  79.306  1.00 11.02 ?  1005 VAL B CA    1 
ATOM   16709 C C     . VAL B 1 1007 ? 4.199   35.915  79.449  1.00 10.74 ?  1005 VAL B C     1 
ATOM   16710 O O     . VAL B 1 1007 ? 3.229   35.226  79.777  1.00 10.39 ?  1005 VAL B O     1 
ATOM   16711 C CB    . VAL B 1 1007 ? 5.666   34.425  78.045  1.00 10.15 ?  1005 VAL B CB    1 
ATOM   16712 C CG1   . VAL B 1 1007 ? 5.127   35.172  76.851  1.00 11.99 ?  1005 VAL B CG1   1 
ATOM   16713 C CG2   . VAL B 1 1007 ? 7.103   33.964  77.790  1.00 12.02 ?  1005 VAL B CG2   1 
ATOM   16714 N N     . GLY B 1 1008 ? 4.104   37.228  79.216  1.00 10.63 ?  1006 GLY B N     1 
ATOM   16715 C CA    . GLY B 1 1008 ? 2.833   37.932  79.262  1.00 10.71 ?  1006 GLY B CA    1 
ATOM   16716 C C     . GLY B 1 1008 ? 2.236   38.107  80.640  1.00 10.85 ?  1006 GLY B C     1 
ATOM   16717 O O     . GLY B 1 1008 ? 1.134   38.669  80.754  1.00 12.97 ?  1006 GLY B O     1 
ATOM   16718 N N     . VAL B 1 1009 ? 2.916   37.635  81.677  1.00 11.01 ?  1007 VAL B N     1 
ATOM   16719 C CA    . VAL B 1 1009 ? 2.469   37.758  83.058  1.00 10.44 ?  1007 VAL B CA    1 
ATOM   16720 C C     . VAL B 1 1009 ? 3.486   38.530  83.888  1.00 10.52 ?  1007 VAL B C     1 
ATOM   16721 O O     . VAL B 1 1009 ? 3.138   39.506  84.568  1.00 12.16 ?  1007 VAL B O     1 
ATOM   16722 C CB    . VAL B 1 1009 ? 2.196   36.371  83.678  1.00 10.77 ?  1007 VAL B CB    1 
ATOM   16723 C CG1   . VAL B 1 1009 ? 1.641   36.526  85.079  1.00 11.54 ?  1007 VAL B CG1   1 
ATOM   16724 C CG2   . VAL B 1 1009 ? 1.194   35.604  82.833  1.00 11.48 ?  1007 VAL B CG2   1 
ATOM   16725 N N     . GLN B 1 1010 ? 4.767   38.133  83.808  1.00 10.22 ?  1008 GLN B N     1 
ATOM   16726 C CA    . GLN B 1 1010 ? 5.899   38.981  84.201  1.00 9.48  ?  1008 GLN B CA    1 
ATOM   16727 C C     . GLN B 1 1010 ? 6.782   39.199  82.978  1.00 12.30 ?  1008 GLN B C     1 
ATOM   16728 O O     . GLN B 1 1010 ? 7.821   38.539  82.831  1.00 12.50 ?  1008 GLN B O     1 
ATOM   16729 C CB    . GLN B 1 1010 ? 6.725   38.394  85.348  1.00 10.90 ?  1008 GLN B CB    1 
ATOM   16730 C CG    . GLN B 1 1010 ? 5.915   38.062  86.581  1.00 10.90 ?  1008 GLN B CG    1 
ATOM   16731 C CD    . GLN B 1 1010 ? 5.527   36.601  86.654  1.00 11.20 ?  1008 GLN B CD    1 
ATOM   16732 O OE1   . GLN B 1 1010 ? 6.209   35.727  86.122  1.00 11.85 ?  1008 GLN B OE1   1 
ATOM   16733 N NE2   . GLN B 1 1010 ? 4.408   36.331  87.300  1.00 11.44 ?  1008 GLN B NE2   1 
ATOM   16734 N N     . PRO B 1 1011 ? 6.395   40.106  82.076  1.00 10.88 ?  1009 PRO B N     1 
ATOM   16735 C CA    . PRO B 1 1011 ? 7.307   40.510  80.991  1.00 12.11 ?  1009 PRO B CA    1 
ATOM   16736 C C     . PRO B 1 1011 ? 8.691   40.806  81.549  1.00 12.20 ?  1009 PRO B C     1 
ATOM   16737 O O     . PRO B 1 1011 ? 8.830   41.478  82.579  1.00 11.30 ?  1009 PRO B O     1 
ATOM   16738 C CB    . PRO B 1 1011 ? 6.645   41.770  80.428  1.00 12.54 ?  1009 PRO B CB    1 
ATOM   16739 C CG    . PRO B 1 1011 ? 5.175   41.575  80.710  1.00 11.99 ?  1009 PRO B CG    1 
ATOM   16740 C CD    . PRO B 1 1011 ? 5.148   40.895  82.075  1.00 12.21 ?  1009 PRO B CD    1 
ATOM   16741 N N     . PHE B 1 1012 ? 9.717   40.290  80.880  1.00 9.99  ?  1010 PHE B N     1 
ATOM   16742 C CA    . PHE B 1 1012 ? 11.027  40.122  81.499  1.00 11.10 ?  1010 PHE B CA    1 
ATOM   16743 C C     . PHE B 1 1012 ? 12.063  41.043  80.875  1.00 11.30 ?  1010 PHE B C     1 
ATOM   16744 O O     . PHE B 1 1012 ? 12.258  41.050  79.653  1.00 12.19 ?  1010 PHE B O     1 
ATOM   16745 C CB    . PHE B 1 1012 ? 11.499  38.673  81.379  1.00 11.38 ?  1010 PHE B CB    1 
ATOM   16746 C CG    . PHE B 1 1012 ? 12.767  38.409  82.121  1.00 10.48 ?  1010 PHE B CG    1 
ATOM   16747 C CD1   . PHE B 1 1012 ? 12.759  38.332  83.497  1.00 14.16 ?  1010 PHE B CD1   1 
ATOM   16748 C CD2   . PHE B 1 1012 ? 13.970  38.295  81.449  1.00 14.12 ?  1010 PHE B CD2   1 
ATOM   16749 C CE1   . PHE B 1 1012 ? 13.937  38.096  84.193  1.00 12.54 ?  1010 PHE B CE1   1 
ATOM   16750 C CE2   . PHE B 1 1012 ? 15.160  38.069  82.137  1.00 15.40 ?  1010 PHE B CE2   1 
ATOM   16751 C CZ    . PHE B 1 1012 ? 15.140  37.982  83.518  1.00 15.13 ?  1010 PHE B CZ    1 
ATOM   16752 N N     . GLY B 1 1013 ? 12.737  41.793  81.714  1.00 11.64 ?  1011 GLY B N     1 
ATOM   16753 C CA    . GLY B 1 1013 ? 13.851  42.605  81.265  1.00 11.94 ?  1011 GLY B CA    1 
ATOM   16754 C C     . GLY B 1 1013 ? 14.038  43.781  82.197  1.00 12.09 ?  1011 GLY B C     1 
ATOM   16755 O O     . GLY B 1 1013 ? 13.122  44.247  82.872  1.00 12.22 ?  1011 GLY B O     1 
ATOM   16756 N N     . GLY B 1 1014 ? 15.260  44.289  82.225  1.00 14.64 ?  1012 GLY B N     1 
ATOM   16757 C CA    . GLY B 1 1014 ? 15.572  45.411  83.081  1.00 14.13 ?  1012 GLY B CA    1 
ATOM   16758 C C     . GLY B 1 1014 ? 16.183  46.582  82.363  1.00 19.49 ?  1012 GLY B C     1 
ATOM   16759 O O     . GLY B 1 1014 ? 16.078  46.712  81.137  1.00 23.56 ?  1012 GLY B O     1 
ATOM   16760 N N     . ARG B 1 1015 ? 16.862  47.415  83.137  1.00 18.84 ?  1013 ARG B N     1 
ATOM   16761 C CA    . ARG B 1 1015 ? 17.331  48.730  82.739  1.00 25.10 ?  1013 ARG B CA    1 
ATOM   16762 C C     . ARG B 1 1015 ? 18.817  48.838  83.058  1.00 20.50 ?  1013 ARG B C     1 
ATOM   16763 O O     . ARG B 1 1015 ? 19.418  47.915  83.609  1.00 17.00 ?  1013 ARG B O     1 
ATOM   16764 C CB    . ARG B 1 1015 ? 16.532  49.815  83.472  1.00 24.01 ?  1013 ARG B CB    1 
ATOM   16765 C CG    . ARG B 1 1015 ? 16.417  49.546  84.971  1.00 25.86 ?  1013 ARG B CG    1 
ATOM   16766 C CD    . ARG B 1 1015 ? 16.310  50.825  85.791  1.00 29.48 ?  1013 ARG B CD    1 
ATOM   16767 N NE    . ARG B 1 1015 ? 17.543  51.604  85.732  1.00 34.09 ?  1013 ARG B NE    1 
ATOM   16768 C CZ    . ARG B 1 1015 ? 18.626  51.359  86.458  1.00 34.69 ?  1013 ARG B CZ    1 
ATOM   16769 N NH1   . ARG B 1 1015 ? 18.664  50.367  87.338  1.00 27.82 ?  1013 ARG B NH1   1 
ATOM   16770 N NH2   . ARG B 1 1015 ? 19.699  52.131  86.300  1.00 38.58 ?  1013 ARG B NH2   1 
ATOM   16771 N N     . GLY B 1 1016 ? 19.410  49.980  82.715  1.00 17.64 ?  1014 GLY B N     1 
ATOM   16772 C CA    . GLY B 1 1016 ? 20.816  50.186  83.032  1.00 20.06 ?  1014 GLY B CA    1 
ATOM   16773 C C     . GLY B 1 1016 ? 21.706  49.144  82.375  1.00 19.03 ?  1014 GLY B C     1 
ATOM   16774 O O     . GLY B 1 1016 ? 21.560  48.821  81.188  1.00 20.49 ?  1014 GLY B O     1 
ATOM   16775 N N     . LEU B 1 1017 ? 22.637  48.593  83.153  1.00 18.58 ?  1015 LEU B N     1 
ATOM   16776 C CA    . LEU B 1 1017 ? 23.543  47.572  82.653  1.00 19.82 ?  1015 LEU B CA    1 
ATOM   16777 C C     . LEU B 1 1017 ? 22.845  46.252  82.365  1.00 18.43 ?  1015 LEU B C     1 
ATOM   16778 O O     . LEU B 1 1017 ? 23.494  45.327  81.864  1.00 19.16 ?  1015 LEU B O     1 
ATOM   16779 C CB    . LEU B 1 1017 ? 24.685  47.349  83.651  1.00 22.10 ?  1015 LEU B CB    1 
ATOM   16780 C CG    . LEU B 1 1017 ? 25.598  48.556  83.878  1.00 22.58 ?  1015 LEU B CG    1 
ATOM   16781 C CD1   . LEU B 1 1017 ? 26.550  48.289  85.034  1.00 21.66 ?  1015 LEU B CD1   1 
ATOM   16782 C CD2   . LEU B 1 1017 ? 26.370  48.857  82.603  1.00 24.65 ?  1015 LEU B CD2   1 
ATOM   16783 N N     . SER B 1 1018 ? 21.556  46.125  82.685  1.00 15.33 ?  1016 SER B N     1 
ATOM   16784 C CA    . SER B 1 1018 ? 20.829  44.895  82.410  1.00 15.34 ?  1016 SER B CA    1 
ATOM   16785 C C     . SER B 1 1018 ? 20.266  44.833  80.999  1.00 14.97 ?  1016 SER B C     1 
ATOM   16786 O O     . SER B 1 1018 ? 19.824  43.762  80.581  1.00 16.53 ?  1016 SER B O     1 
ATOM   16787 C CB    . SER B 1 1018 ? 19.683  44.717  83.409  1.00 13.90 ?  1016 SER B CB    1 
ATOM   16788 O OG    . SER B 1 1018 ? 20.217  44.567  84.714  1.00 17.30 ?  1016 SER B OG    1 
ATOM   16789 N N     . GLY B 1 1019 ? 20.227  45.937  80.277  1.00 17.22 ?  1017 GLY B N     1 
ATOM   16790 C CA    . GLY B 1 1019 ? 19.892  45.851  78.869  1.00 21.62 ?  1017 GLY B CA    1 
ATOM   16791 C C     . GLY B 1 1019 ? 19.185  47.086  78.355  1.00 17.68 ?  1017 GLY B C     1 
ATOM   16792 O O     . GLY B 1 1019 ? 18.980  48.069  79.062  1.00 18.42 ?  1017 GLY B O     1 
ATOM   16793 N N     . THR B 1 1020 ? 18.805  46.995  77.078  1.00 16.27 ?  1018 THR B N     1 
ATOM   16794 C CA    . THR B 1 1020 ? 18.167  48.085  76.357  1.00 18.54 ?  1018 THR B CA    1 
ATOM   16795 C C     . THR B 1 1020 ? 16.655  48.102  76.508  1.00 17.18 ?  1018 THR B C     1 
ATOM   16796 O O     . THR B 1 1020 ? 16.029  49.149  76.288  1.00 18.41 ?  1018 THR B O     1 
ATOM   16797 C CB    . THR B 1 1020 ? 18.478  47.954  74.867  1.00 16.04 ?  1018 THR B CB    1 
ATOM   16798 O OG1   . THR B 1 1020 ? 17.979  46.684  74.422  1.00 15.13 ?  1018 THR B OG1   1 
ATOM   16799 C CG2   . THR B 1 1020 ? 19.980  47.986  74.606  1.00 18.75 ?  1018 THR B CG2   1 
ATOM   16800 N N     . GLY B 1 1021 ? 16.053  46.964  76.817  1.00 14.61 ?  1019 GLY B N     1 
ATOM   16801 C CA    . GLY B 1 1021 ? 14.641  46.778  76.578  1.00 13.79 ?  1019 GLY B CA    1 
ATOM   16802 C C     . GLY B 1 1021 ? 14.364  46.786  75.085  1.00 15.82 ?  1019 GLY B C     1 
ATOM   16803 O O     . GLY B 1 1021 ? 15.281  46.880  74.265  1.00 15.21 ?  1019 GLY B O     1 
ATOM   16804 N N     . PRO B 1 1022 ? 13.102  46.665  74.702  1.00 11.57 ?  1020 PRO B N     1 
ATOM   16805 C CA    . PRO B 1 1022 ? 11.935  46.450  75.562  1.00 11.92 ?  1020 PRO B CA    1 
ATOM   16806 C C     . PRO B 1 1022 ? 11.915  45.045  76.156  1.00 12.67 ?  1020 PRO B C     1 
ATOM   16807 O O     . PRO B 1 1022 ? 12.692  44.169  75.763  1.00 13.19 ?  1020 PRO B O     1 
ATOM   16808 C CB    . PRO B 1 1022 ? 10.763  46.685  74.601  1.00 13.77 ?  1020 PRO B CB    1 
ATOM   16809 C CG    . PRO B 1 1022 ? 11.294  46.249  73.273  1.00 15.85 ?  1020 PRO B CG    1 
ATOM   16810 C CD    . PRO B 1 1022 ? 12.726  46.715  73.276  1.00 13.97 ?  1020 PRO B CD    1 
ATOM   16811 N N     . LYS B 1 1023 ? 11.009  44.823  77.106  1.00 11.30 ?  1021 LYS B N     1 
ATOM   16812 C CA    . LYS B 1 1023 ? 10.916  43.526  77.768  1.00 11.31 ?  1021 LYS B CA    1 
ATOM   16813 C C     . LYS B 1 1023 ? 10.468  42.439  76.803  1.00 10.75 ?  1021 LYS B C     1 
ATOM   16814 O O     . LYS B 1 1023 ? 9.501   42.609  76.053  1.00 11.49 ?  1021 LYS B O     1 
ATOM   16815 C CB    . LYS B 1 1023 ? 9.912   43.588  78.913  1.00 11.08 ?  1021 LYS B CB    1 
ATOM   16816 C CG    . LYS B 1 1023 ? 10.397  44.341  80.140  1.00 10.91 ?  1021 LYS B CG    1 
ATOM   16817 C CD    . LYS B 1 1023 ? 9.241   44.455  81.095  1.00 10.76 ?  1021 LYS B CD    1 
ATOM   16818 C CE    . LYS B 1 1023 ? 9.664   44.934  82.475  1.00 11.54 ?  1021 LYS B CE    1 
ATOM   16819 N NZ    . LYS B 1 1023 ? 10.397  43.844  83.203  1.00 10.65 ?  1021 LYS B NZ    1 
ATOM   16820 N N     . ALA B 1 1024 ? 11.139  41.298  76.879  1.00 12.34 ?  1022 ALA B N     1 
ATOM   16821 C CA    . ALA B 1 1024 ? 10.673  40.079  76.235  1.00 10.74 ?  1022 ALA B CA    1 
ATOM   16822 C C     . ALA B 1 1024 ? 9.394   39.581  76.885  1.00 11.13 ?  1022 ALA B C     1 
ATOM   16823 O O     . ALA B 1 1024 ? 9.213   39.694  78.096  1.00 13.26 ?  1022 ALA B O     1 
ATOM   16824 C CB    . ALA B 1 1024 ? 11.742  38.993  76.332  1.00 12.02 ?  1022 ALA B CB    1 
ATOM   16825 N N     . GLY B 1 1025 ? 8.500   39.022  76.072  1.00 9.43  ?  1023 GLY B N     1 
ATOM   16826 C CA    . GLY B 1 1025 ? 7.250   38.559  76.631  1.00 10.10 ?  1023 GLY B CA    1 
ATOM   16827 C C     . GLY B 1 1025 ? 6.354   39.679  77.084  1.00 10.11 ?  1023 GLY B C     1 
ATOM   16828 O O     . GLY B 1 1025 ? 5.476   39.463  77.917  1.00 11.65 ?  1023 GLY B O     1 
ATOM   16829 N N     . GLY B 1 1026 ? 6.540   40.874  76.533  1.00 11.50 ?  1024 GLY B N     1 
ATOM   16830 C CA    . GLY B 1 1026 ? 5.736   42.023  76.875  1.00 10.36 ?  1024 GLY B CA    1 
ATOM   16831 C C     . GLY B 1 1026 ? 5.270   42.731  75.624  1.00 9.84  ?  1024 GLY B C     1 
ATOM   16832 O O     . GLY B 1 1026 ? 5.663   42.396  74.501  1.00 10.22 ?  1024 GLY B O     1 
ATOM   16833 N N     . PRO B 1 1027 ? 4.428   43.744  75.800  1.00 9.28  ?  1025 PRO B N     1 
ATOM   16834 C CA    . PRO B 1 1027 ? 3.671   44.292  74.663  1.00 8.20  ?  1025 PRO B CA    1 
ATOM   16835 C C     . PRO B 1 1027 ? 4.433   45.305  73.831  1.00 10.92 ?  1025 PRO B C     1 
ATOM   16836 O O     . PRO B 1 1027 ? 3.920   45.698  72.772  1.00 10.89 ?  1025 PRO B O     1 
ATOM   16837 C CB    . PRO B 1 1027 ? 2.448   44.931  75.344  1.00 12.65 ?  1025 PRO B CB    1 
ATOM   16838 C CG    . PRO B 1 1027 ? 2.962   45.291  76.724  1.00 12.37 ?  1025 PRO B CG    1 
ATOM   16839 C CD    . PRO B 1 1027 ? 3.935   44.214  77.106  1.00 10.84 ?  1025 PRO B CD    1 
ATOM   16840 N N     . LEU B 1 1028 ? 5.612   45.749  74.259  1.00 11.60 ?  1026 LEU B N     1 
ATOM   16841 C CA    . LEU B 1 1028 ? 6.393   46.677  73.446  1.00 9.79  ?  1026 LEU B CA    1 
ATOM   16842 C C     . LEU B 1 1028 ? 7.409   45.976  72.559  1.00 11.61 ?  1026 LEU B C     1 
ATOM   16843 O O     . LEU B 1 1028 ? 8.069   46.645  71.758  1.00 12.42 ?  1026 LEU B O     1 
ATOM   16844 C CB    . LEU B 1 1028 ? 7.120   47.694  74.339  1.00 11.58 ?  1026 LEU B CB    1 
ATOM   16845 C CG    . LEU B 1 1028 ? 6.165   48.585  75.132  1.00 14.33 ?  1026 LEU B CG    1 
ATOM   16846 C CD1   . LEU B 1 1028 ? 6.936   49.448  76.100  1.00 16.90 ?  1026 LEU B CD1   1 
ATOM   16847 C CD2   . LEU B 1 1028 ? 5.382   49.445  74.197  1.00 21.09 ?  1026 LEU B CD2   1 
ATOM   16848 N N     . TYR B 1 1029 ? 7.550   44.657  72.694  1.00 10.28 ?  1027 TYR B N     1 
ATOM   16849 C CA    . TYR B 1 1029 ? 8.660   43.944  72.067  1.00 10.55 ?  1027 TYR B CA    1 
ATOM   16850 C C     . TYR B 1 1029 ? 8.584   44.006  70.550  1.00 11.81 ?  1027 TYR B C     1 
ATOM   16851 O O     . TYR B 1 1029 ? 9.571   44.356  69.887  1.00 10.77 ?  1027 TYR B O     1 
ATOM   16852 C CB    . TYR B 1 1029 ? 8.644   42.502  72.542  1.00 10.70 ?  1027 TYR B CB    1 
ATOM   16853 C CG    . TYR B 1 1029 ? 9.952   41.746  72.468  1.00 11.43 ?  1027 TYR B CG    1 
ATOM   16854 C CD1   . TYR B 1 1029 ? 11.049  42.100  73.254  1.00 9.95  ?  1027 TYR B CD1   1 
ATOM   16855 C CD2   . TYR B 1 1029 ? 10.071  40.626  71.650  1.00 10.65 ?  1027 TYR B CD2   1 
ATOM   16856 C CE1   . TYR B 1 1029 ? 12.228  41.368  73.217  1.00 10.21 ?  1027 TYR B CE1   1 
ATOM   16857 C CE2   . TYR B 1 1029 ? 11.243  39.886  71.616  1.00 10.74 ?  1027 TYR B CE2   1 
ATOM   16858 C CZ    . TYR B 1 1029 ? 12.316  40.255  72.393  1.00 10.62 ?  1027 TYR B CZ    1 
ATOM   16859 O OH    . TYR B 1 1029 ? 13.454  39.475  72.356  1.00 12.83 ?  1027 TYR B OH    1 
ATOM   16860 N N     . LEU B 1 1030 ? 7.435   43.636  69.977  1.00 10.77 ?  1028 LEU B N     1 
ATOM   16861 C CA    . LEU B 1 1030 ? 7.359   43.544  68.521  1.00 9.65  ?  1028 LEU B CA    1 
ATOM   16862 C C     . LEU B 1 1030 ? 7.552   44.904  67.873  1.00 10.68 ?  1028 LEU B C     1 
ATOM   16863 O O     . LEU B 1 1030 ? 8.076   44.993  66.751  1.00 11.38 ?  1028 LEU B O     1 
ATOM   16864 C CB    . LEU B 1 1030 ? 6.022   42.949  68.097  1.00 11.69 ?  1028 LEU B CB    1 
ATOM   16865 C CG    . LEU B 1 1030 ? 5.768   41.499  68.521  1.00 11.14 ?  1028 LEU B CG    1 
ATOM   16866 C CD1   . LEU B 1 1030 ? 4.445   41.008  67.934  1.00 13.64 ?  1028 LEU B CD1   1 
ATOM   16867 C CD2   . LEU B 1 1030 ? 6.932   40.598  68.064  1.00 13.20 ?  1028 LEU B CD2   1 
ATOM   16868 N N     . GLY B 1 1031 ? 7.179   45.977  68.569  1.00 12.15 ?  1029 GLY B N     1 
ATOM   16869 C CA    . GLY B 1 1031 ? 7.272   47.294  67.968  1.00 11.87 ?  1029 GLY B CA    1 
ATOM   16870 C C     . GLY B 1 1031 ? 8.689   47.735  67.676  1.00 11.31 ?  1029 GLY B C     1 
ATOM   16871 O O     . GLY B 1 1031 ? 8.899   48.651  66.864  1.00 13.98 ?  1029 GLY B O     1 
ATOM   16872 N N     . ARG B 1 1032 ? 9.670   47.124  68.335  1.00 11.32 ?  1030 ARG B N     1 
ATOM   16873 C CA    . ARG B 1 1032 ? 11.068  47.418  68.087  1.00 12.09 ?  1030 ARG B CA    1 
ATOM   16874 C C     . ARG B 1 1032 ? 11.582  46.760  66.816  1.00 12.14 ?  1030 ARG B C     1 
ATOM   16875 O O     . ARG B 1 1032 ? 12.674  47.109  66.346  1.00 13.12 ?  1030 ARG B O     1 
ATOM   16876 C CB    . ARG B 1 1032 ? 11.890  46.949  69.296  1.00 14.40 ?  1030 ARG B CB    1 
ATOM   16877 C CG    . ARG B 1 1032 ? 13.310  47.448  69.325  1.00 15.59 ?  1030 ARG B CG    1 
ATOM   16878 C CD    . ARG B 1 1032 ? 13.378  48.942  69.618  1.00 18.95 ?  1030 ARG B CD    1 
ATOM   16879 N NE    . ARG B 1 1032 ? 14.764  49.359  69.801  1.00 20.43 ?  1030 ARG B NE    1 
ATOM   16880 C CZ    . ARG B 1 1032 ? 15.389  50.258  69.053  1.00 19.86 ?  1030 ARG B CZ    1 
ATOM   16881 N NH1   . ARG B 1 1032 ? 14.765  50.901  68.075  1.00 21.99 ?  1030 ARG B NH1   1 
ATOM   16882 N NH2   . ARG B 1 1032 ? 16.671  50.519  69.292  1.00 21.50 ?  1030 ARG B NH2   1 
ATOM   16883 N N     . LEU B 1 1033 ? 10.812  45.830  66.249  1.00 11.96 ?  1031 LEU B N     1 
ATOM   16884 C CA    . LEU B 1 1033 ? 11.267  44.988  65.149  1.00 11.02 ?  1031 LEU B CA    1 
ATOM   16885 C C     . LEU B 1 1033 ? 10.587  45.359  63.840  1.00 12.44 ?  1031 LEU B C     1 
ATOM   16886 O O     . LEU B 1 1033 ? 10.638  44.589  62.870  1.00 12.78 ?  1031 LEU B O     1 
ATOM   16887 C CB    . LEU B 1 1033 ? 11.026  43.518  65.499  1.00 11.45 ?  1031 LEU B CB    1 
ATOM   16888 C CG    . LEU B 1 1033 ? 11.650  43.100  66.838  1.00 12.87 ?  1031 LEU B CG    1 
ATOM   16889 C CD1   . LEU B 1 1033 ? 11.300  41.655  67.200  1.00 14.21 ?  1031 LEU B CD1   1 
ATOM   16890 C CD2   . LEU B 1 1033 ? 13.148  43.310  66.825  1.00 17.87 ?  1031 LEU B CD2   1 
ATOM   16891 N N     . VAL B 1 1034 ? 9.941   46.527  63.804  1.00 11.83 ?  1032 VAL B N     1 
ATOM   16892 C CA    . VAL B 1 1034 ? 9.355   47.110  62.608  1.00 14.01 ?  1032 VAL B CA    1 
ATOM   16893 C C     . VAL B 1 1034 ? 9.836   48.559  62.548  1.00 14.57 ?  1032 VAL B C     1 
ATOM   16894 O O     . VAL B 1 1034 ? 10.336  49.103  63.535  1.00 14.97 ?  1032 VAL B O     1 
ATOM   16895 C CB    . VAL B 1 1034 ? 7.807   47.018  62.629  1.00 13.69 ?  1032 VAL B CB    1 
ATOM   16896 C CG1   . VAL B 1 1034 ? 7.355   45.562  62.513  1.00 14.35 ?  1032 VAL B CG1   1 
ATOM   16897 C CG2   . VAL B 1 1034 ? 7.266   47.634  63.920  1.00 14.31 ?  1032 VAL B CG2   1 
ATOM   16898 N N     . THR B 1 1035 ? 9.715   49.183  61.364  1.00 15.60 ?  1033 THR B N     1 
ATOM   16899 C CA    . THR B 1 1035 ? 10.233  50.543  61.232  1.00 16.50 ?  1033 THR B CA    1 
ATOM   16900 C C     . THR B 1 1035 ? 9.258   51.590  61.743  1.00 17.46 ?  1033 THR B C     1 
ATOM   16901 O O     . THR B 1 1035 ? 9.683   52.702  62.071  1.00 19.96 ?  1033 THR B O     1 
ATOM   16902 C CB    . THR B 1 1035 ? 10.595  50.861  59.779  1.00 21.11 ?  1033 THR B CB    1 
ATOM   16903 O OG1   . THR B 1 1035 ? 9.503   50.511  58.928  1.00 23.46 ?  1033 THR B OG1   1 
ATOM   16904 C CG2   . THR B 1 1035 ? 11.847  50.087  59.358  1.00 19.79 ?  1033 THR B CG2   1 
ATOM   16905 N N     . THR B 1 1036 ? 7.973   51.253  61.832  1.00 15.76 ?  1034 THR B N     1 
ATOM   16906 C CA    . THR B 1 1036 ? 6.952   52.108  62.430  1.00 18.27 ?  1034 THR B CA    1 
ATOM   16907 C C     . THR B 1 1036 ? 6.223   51.271  63.468  1.00 16.27 ?  1034 THR B C     1 
ATOM   16908 O O     . THR B 1 1036 ? 5.586   50.275  63.116  1.00 16.93 ?  1034 THR B O     1 
ATOM   16909 C CB    . THR B 1 1036 ? 5.963   52.621  61.384  1.00 20.53 ?  1034 THR B CB    1 
ATOM   16910 O OG1   . THR B 1 1036 ? 6.680   53.212  60.296  1.00 22.96 ?  1034 THR B OG1   1 
ATOM   16911 C CG2   . THR B 1 1036 ? 5.020   53.646  62.000  1.00 22.85 ?  1034 THR B CG2   1 
ATOM   16912 N N     . ALA B 1 1037 ? 6.334   51.662  64.753  1.00 14.84 ?  1035 ALA B N     1 
ATOM   16913 C CA    . ALA B 1 1037 ? 5.772   50.843  65.827  1.00 14.09 ?  1035 ALA B CA    1 
ATOM   16914 C C     . ALA B 1 1037 ? 4.253   50.997  65.899  1.00 14.47 ?  1035 ALA B C     1 
ATOM   16915 O O     . ALA B 1 1037 ? 3.734   52.111  65.747  1.00 15.62 ?  1035 ALA B O     1 
ATOM   16916 C CB    . ALA B 1 1037 ? 6.378   51.238  67.156  1.00 15.65 ?  1035 ALA B CB    1 
ATOM   16917 N N     . PRO B 1 1038 ? 3.526   49.911  66.147  1.00 11.23 ?  1036 PRO B N     1 
ATOM   16918 C CA    . PRO B 1 1038 ? 2.082   50.010  66.369  1.00 12.05 ?  1036 PRO B CA    1 
ATOM   16919 C C     . PRO B 1 1038 ? 1.784   50.457  67.796  1.00 12.04 ?  1036 PRO B C     1 
ATOM   16920 O O     . PRO B 1 1038 ? 2.662   50.558  68.651  1.00 12.52 ?  1036 PRO B O     1 
ATOM   16921 C CB    . PRO B 1 1038 ? 1.594   48.575  66.139  1.00 13.81 ?  1036 PRO B CB    1 
ATOM   16922 C CG    . PRO B 1 1038 ? 2.750   47.737  66.620  1.00 15.19 ?  1036 PRO B CG    1 
ATOM   16923 C CD    . PRO B 1 1038 ? 3.993   48.510  66.225  1.00 13.10 ?  1036 PRO B CD    1 
ATOM   16924 N N     . VAL B 1 1039 ? 0.504   50.697  68.043  1.00 12.46 ?  1037 VAL B N     1 
ATOM   16925 C CA    . VAL B 1 1039 ? 0.013   50.987  69.391  1.00 12.77 ?  1037 VAL B CA    1 
ATOM   16926 C C     . VAL B 1 1039 ? -0.259  49.646  70.070  1.00 11.88 ?  1037 VAL B C     1 
ATOM   16927 O O     . VAL B 1 1039 ? -1.158  48.918  69.631  1.00 12.37 ?  1037 VAL B O     1 
ATOM   16928 C CB    . VAL B 1 1039 ? -1.252  51.849  69.347  1.00 13.22 ?  1037 VAL B CB    1 
ATOM   16929 C CG1   . VAL B 1 1039 ? -1.739  52.096  70.774  1.00 14.72 ?  1037 VAL B CG1   1 
ATOM   16930 C CG2   . VAL B 1 1039 ? -0.954  53.156  68.621  1.00 16.22 ?  1037 VAL B CG2   1 
ATOM   16931 N N     . PRO B 1 1040 ? 0.485   49.274  71.105  1.00 13.09 ?  1038 PRO B N     1 
ATOM   16932 C CA    . PRO B 1 1040 ? 0.252   47.965  71.720  1.00 12.14 ?  1038 PRO B CA    1 
ATOM   16933 C C     . PRO B 1 1040 ? -1.106  47.896  72.401  1.00 11.58 ?  1038 PRO B C     1 
ATOM   16934 O O     . PRO B 1 1040 ? -1.680  48.931  72.786  1.00 12.00 ?  1038 PRO B O     1 
ATOM   16935 C CB    . PRO B 1 1040 ? 1.404   47.837  72.741  1.00 15.30 ?  1038 PRO B CB    1 
ATOM   16936 C CG    . PRO B 1 1040 ? 2.398   48.845  72.341  1.00 16.39 ?  1038 PRO B CG    1 
ATOM   16937 C CD    . PRO B 1 1040 ? 1.631   49.972  71.699  1.00 13.75 ?  1038 PRO B CD    1 
ATOM   16938 N N     . PRO B 1 1041 ? -1.639  46.691  72.600  1.00 11.54 ?  1039 PRO B N     1 
ATOM   16939 C CA    . PRO B 1 1041 ? -2.864  46.540  73.393  1.00 12.00 ?  1039 PRO B CA    1 
ATOM   16940 C C     . PRO B 1 1041 ? -2.693  47.185  74.760  1.00 12.47 ?  1039 PRO B C     1 
ATOM   16941 O O     . PRO B 1 1041 ? -1.627  47.086  75.376  1.00 13.31 ?  1039 PRO B O     1 
ATOM   16942 C CB    . PRO B 1 1041 ? -3.031  45.023  73.511  1.00 14.88 ?  1039 PRO B CB    1 
ATOM   16943 C CG    . PRO B 1 1041 ? -2.165  44.452  72.416  1.00 16.15 ?  1039 PRO B CG    1 
ATOM   16944 C CD    . PRO B 1 1041 ? -1.050  45.393  72.211  1.00 14.47 ?  1039 PRO B CD    1 
ATOM   16945 N N     . GLN B 1 1042 ? -3.746  47.874  75.206  1.00 12.27 ?  1040 GLN B N     1 
ATOM   16946 C CA    . GLN B 1 1042 ? -3.847  48.468  76.532  1.00 12.78 ?  1040 GLN B CA    1 
ATOM   16947 C C     . GLN B 1 1042 ? -2.856  49.596  76.773  1.00 13.26 ?  1040 GLN B C     1 
ATOM   16948 O O     . GLN B 1 1042 ? -2.711  50.048  77.923  1.00 13.97 ?  1040 GLN B O     1 
ATOM   16949 C CB    . GLN B 1 1042 ? -3.672  47.407  77.625  1.00 17.30 ?  1040 GLN B CB    1 
ATOM   16950 C CG    . GLN B 1 1042 ? -4.612  46.230  77.499  1.00 22.05 ?  1040 GLN B CG    1 
ATOM   16951 C CD    . GLN B 1 1042 ? -4.424  45.270  78.662  1.00 27.31 ?  1040 GLN B CD    1 
ATOM   16952 O OE1   . GLN B 1 1042 ? -5.280  45.171  79.526  1.00 31.99 ?  1040 GLN B OE1   1 
ATOM   16953 N NE2   . GLN B 1 1042 ? -3.279  44.589  78.701  1.00 33.13 ?  1040 GLN B NE2   1 
ATOM   16954 N N     . HIS B 1 1043 ? -2.167  50.069  75.735  1.00 11.91 ?  1041 HIS B N     1 
ATOM   16955 C CA    . HIS B 1 1043 ? -1.050  51.000  75.898  1.00 11.56 ?  1041 HIS B CA    1 
ATOM   16956 C C     . HIS B 1 1043 ? -1.554  52.435  75.791  1.00 12.79 ?  1041 HIS B C     1 
ATOM   16957 O O     . HIS B 1 1043 ? -1.657  53.009  74.702  1.00 14.20 ?  1041 HIS B O     1 
ATOM   16958 C CB    . HIS B 1 1043 ? 0.018   50.688  74.861  1.00 12.12 ?  1041 HIS B CB    1 
ATOM   16959 C CG    . HIS B 1 1043 ? 1.228   51.569  74.930  1.00 14.65 ?  1041 HIS B CG    1 
ATOM   16960 N ND1   . HIS B 1 1043 ? 2.344   51.261  75.684  1.00 12.84 ?  1041 HIS B ND1   1 
ATOM   16961 C CD2   . HIS B 1 1043 ? 1.498   52.748  74.321  1.00 13.84 ?  1041 HIS B CD2   1 
ATOM   16962 C CE1   . HIS B 1 1043 ? 3.250   52.211  75.529  1.00 12.36 ?  1041 HIS B CE1   1 
ATOM   16963 N NE2   . HIS B 1 1043 ? 2.764   53.121  74.701  1.00 12.83 ?  1041 HIS B NE2   1 
ATOM   16964 N N     . SER B 1 1044 ? -1.885  53.020  76.939  1.00 11.23 ?  1042 SER B N     1 
ATOM   16965 C CA    . SER B 1 1044 ? -2.328  54.404  77.018  1.00 12.32 ?  1042 SER B CA    1 
ATOM   16966 C C     . SER B 1 1044 ? -2.244  54.832  78.473  1.00 11.74 ?  1042 SER B C     1 
ATOM   16967 O O     . SER B 1 1044 ? -2.069  54.006  79.370  1.00 13.03 ?  1042 SER B O     1 
ATOM   16968 C CB    . SER B 1 1044 ? -3.760  54.578  76.498  1.00 13.31 ?  1042 SER B CB    1 
ATOM   16969 O OG    . SER B 1 1044 ? -4.688  53.961  77.375  1.00 12.06 ?  1042 SER B OG    1 
ATOM   16970 N N     . SER B 1 1045 ? -2.423  56.129  78.700  1.00 11.81 ?  1043 SER B N     1 
ATOM   16971 C CA    . SER B 1 1045 ? -2.473  56.661  80.056  1.00 12.38 ?  1043 SER B CA    1 
ATOM   16972 C C     . SER B 1 1045 ? -3.337  57.908  80.075  1.00 11.53 ?  1043 SER B C     1 
ATOM   16973 O O     . SER B 1 1045 ? -3.272  58.714  79.146  1.00 12.70 ?  1043 SER B O     1 
ATOM   16974 C CB    . SER B 1 1045 ? -1.068  57.006  80.547  1.00 12.32 ?  1043 SER B CB    1 
ATOM   16975 O OG    . SER B 1 1045 ? -1.133  57.613  81.825  1.00 12.90 ?  1043 SER B OG    1 
ATOM   16976 N N     . VAL B 1 1046 ? -4.134  58.075  81.141  1.00 12.36 ?  1044 VAL B N     1 
ATOM   16977 C CA    . VAL B 1 1046 ? -4.928  59.296  81.277  1.00 14.24 ?  1044 VAL B CA    1 
ATOM   16978 C C     . VAL B 1 1046 ? -4.141  60.435  81.891  1.00 12.18 ?  1044 VAL B C     1 
ATOM   16979 O O     . VAL B 1 1046 ? -4.655  61.557  81.957  1.00 14.36 ?  1044 VAL B O     1 
ATOM   16980 C CB    . VAL B 1 1046 ? -6.208  59.116  82.123  1.00 14.87 ?  1044 VAL B CB    1 
ATOM   16981 C CG1   . VAL B 1 1046 ? -7.140  58.120  81.437  1.00 17.15 ?  1044 VAL B CG1   1 
ATOM   16982 C CG2   . VAL B 1 1046 ? -5.875  58.675  83.547  1.00 15.62 ?  1044 VAL B CG2   1 
ATOM   16983 N N     . HIS B 1 1047 ? -2.917  60.182  82.328  1.00 14.10 ?  1045 HIS B N     1 
ATOM   16984 C CA    . HIS B 1 1047 ? -2.128  61.189  83.015  1.00 13.43 ?  1045 HIS B CA    1 
ATOM   16985 C C     . HIS B 1 1047 ? -1.290  62.004  82.037  1.00 12.39 ?  1045 HIS B C     1 
ATOM   16986 O O     . HIS B 1 1047 ? -0.824  61.495  81.014  1.00 15.17 ?  1045 HIS B O     1 
ATOM   16987 C CB    . HIS B 1 1047 ? -1.271  60.491  84.060  1.00 15.38 ?  1045 HIS B CB    1 
ATOM   16988 C CG    . HIS B 1 1047 ? -2.106  59.678  85.004  1.00 18.24 ?  1045 HIS B CG    1 
ATOM   16989 N ND1   . HIS B 1 1047 ? -2.994  60.248  85.896  1.00 21.29 ?  1045 HIS B ND1   1 
ATOM   16990 C CD2   . HIS B 1 1047 ? -2.262  58.337  85.121  1.00 22.41 ?  1045 HIS B CD2   1 
ATOM   16991 C CE1   . HIS B 1 1047 ? -3.625  59.292  86.554  1.00 21.88 ?  1045 HIS B CE1   1 
ATOM   16992 N NE2   . HIS B 1 1047 ? -3.201  58.123  86.100  1.00 20.02 ?  1045 HIS B NE2   1 
ATOM   16993 N N     . THR B 1 1048 ? -1.129  63.284  82.345  1.00 14.05 ?  1046 THR B N     1 
ATOM   16994 C CA    . THR B 1 1048 ? -0.315  64.176  81.530  1.00 13.27 ?  1046 THR B CA    1 
ATOM   16995 C C     . THR B 1 1048 ? 0.800   64.740  82.401  1.00 12.92 ?  1046 THR B C     1 
ATOM   16996 O O     . THR B 1 1048 ? 0.546   65.253  83.494  1.00 15.25 ?  1046 THR B O     1 
ATOM   16997 C CB    . THR B 1 1048 ? -1.149  65.308  80.937  1.00 15.66 ?  1046 THR B CB    1 
ATOM   16998 O OG1   . THR B 1 1048 ? -2.314  64.762  80.296  1.00 16.60 ?  1046 THR B OG1   1 
ATOM   16999 C CG2   . THR B 1 1048 ? -0.327  66.082  79.889  1.00 16.77 ?  1046 THR B CG2   1 
ATOM   17000 N N     . ASP B 1 1049 ? 2.032   64.633  81.915  1.00 12.90 ?  1047 ASP B N     1 
ATOM   17001 C CA    . ASP B 1 1049 ? 3.151   65.113  82.703  1.00 14.00 ?  1047 ASP B CA    1 
ATOM   17002 C C     . ASP B 1 1049 ? 3.017   66.622  82.918  1.00 14.98 ?  1047 ASP B C     1 
ATOM   17003 O O     . ASP B 1 1049 ? 2.752   67.363  81.960  1.00 15.69 ?  1047 ASP B O     1 
ATOM   17004 C CB    . ASP B 1 1049 ? 4.453   64.755  82.000  1.00 11.76 ?  1047 ASP B CB    1 
ATOM   17005 C CG    . ASP B 1 1049 ? 5.668   65.214  82.763  1.00 14.24 ?  1047 ASP B CG    1 
ATOM   17006 O OD1   . ASP B 1 1049 ? 5.987   66.423  82.672  1.00 15.17 ?  1047 ASP B OD1   1 
ATOM   17007 O OD2   . ASP B 1 1049 ? 6.273   64.386  83.471  1.00 14.88 ?  1047 ASP B OD2   1 
ATOM   17008 N N     . PRO B 1 1050 ? 3.152   67.110  84.153  1.00 14.86 ?  1048 PRO B N     1 
ATOM   17009 C CA    . PRO B 1 1050 ? 2.899   68.537  84.412  1.00 15.56 ?  1048 PRO B CA    1 
ATOM   17010 C C     . PRO B 1 1050 ? 3.993   69.444  83.887  1.00 16.46 ?  1048 PRO B C     1 
ATOM   17011 O O     . PRO B 1 1050 ? 3.719   70.613  83.578  1.00 17.21 ?  1048 PRO B O     1 
ATOM   17012 C CB    . PRO B 1 1050 ? 2.802   68.602  85.943  1.00 19.15 ?  1048 PRO B CB    1 
ATOM   17013 C CG    . PRO B 1 1050 ? 3.619   67.450  86.407  1.00 17.27 ?  1048 PRO B CG    1 
ATOM   17014 C CD    . PRO B 1 1050 ? 3.396   66.355  85.390  1.00 15.34 ?  1048 PRO B CD    1 
ATOM   17015 N N     . VAL B 1 1051 ? 5.225   68.939  83.779  1.00 17.77 ?  1049 VAL B N     1 
ATOM   17016 C CA    . VAL B 1 1051 ? 6.299   69.744  83.202  1.00 16.83 ?  1049 VAL B CA    1 
ATOM   17017 C C     . VAL B 1 1051 ? 6.114   69.873  81.696  1.00 15.69 ?  1049 VAL B C     1 
ATOM   17018 O O     . VAL B 1 1051 ? 6.347   70.944  81.122  1.00 16.39 ?  1049 VAL B O     1 
ATOM   17019 C CB    . VAL B 1 1051 ? 7.668   69.151  83.572  1.00 16.98 ?  1049 VAL B CB    1 
ATOM   17020 C CG1   . VAL B 1 1051 ? 8.782   70.008  82.975  1.00 16.12 ?  1049 VAL B CG1   1 
ATOM   17021 C CG2   . VAL B 1 1051 ? 7.810   69.069  85.086  1.00 19.64 ?  1049 VAL B CG2   1 
ATOM   17022 N N     . LEU B 1 1052 ? 5.663   68.801  81.033  1.00 13.56 ?  1050 LEU B N     1 
ATOM   17023 C CA    . LEU B 1 1052 ? 5.247   68.902  79.635  1.00 12.69 ?  1050 LEU B CA    1 
ATOM   17024 C C     . LEU B 1 1052 ? 4.201   69.996  79.461  1.00 16.75 ?  1050 LEU B C     1 
ATOM   17025 O O     . LEU B 1 1052 ? 4.281   70.803  78.528  1.00 15.33 ?  1050 LEU B O     1 
ATOM   17026 C CB    . LEU B 1 1052 ? 4.708   67.554  79.132  1.00 12.97 ?  1050 LEU B CB    1 
ATOM   17027 C CG    . LEU B 1 1052 ? 4.187   67.400  77.687  1.00 12.77 ?  1050 LEU B CG    1 
ATOM   17028 C CD1   . LEU B 1 1052 ? 2.785   67.991  77.459  1.00 15.60 ?  1050 LEU B CD1   1 
ATOM   17029 C CD2   . LEU B 1 1052 ? 5.197   67.939  76.659  1.00 13.75 ?  1050 LEU B CD2   1 
ATOM   17030 N N     . LEU B 1 1053 ? 3.197   70.024  80.344  1.00 15.24 ?  1051 LEU B N     1 
ATOM   17031 C CA    . LEU B 1 1053 ? 2.158   71.043  80.240  1.00 18.04 ?  1051 LEU B CA    1 
ATOM   17032 C C     . LEU B 1 1053 ? 2.743   72.442  80.364  1.00 17.38 ?  1051 LEU B C     1 
ATOM   17033 O O     . LEU B 1 1053 ? 2.381   73.346  79.601  1.00 18.54 ?  1051 LEU B O     1 
ATOM   17034 C CB    . LEU B 1 1053 ? 1.087   70.818  81.314  1.00 17.16 ?  1051 LEU B CB    1 
ATOM   17035 C CG    . LEU B 1 1053 ? 0.181   69.609  81.064  1.00 19.67 ?  1051 LEU B CG    1 
ATOM   17036 C CD1   . LEU B 1 1053 ? -0.698  69.352  82.279  1.00 19.21 ?  1051 LEU B CD1   1 
ATOM   17037 C CD2   . LEU B 1 1053 ? -0.650  69.826  79.820  1.00 21.62 ?  1051 LEU B CD2   1 
ATOM   17038 N N     . ASP B 1 1054 ? 3.656   72.636  81.316  1.00 16.81 ?  1052 ASP B N     1 
ATOM   17039 C CA    . ASP B 1 1054 ? 4.281   73.944  81.477  1.00 19.95 ?  1052 ASP B CA    1 
ATOM   17040 C C     . ASP B 1 1054 ? 5.096   74.317  80.244  1.00 17.23 ?  1052 ASP B C     1 
ATOM   17041 O O     . ASP B 1 1054 ? 5.146   75.489  79.851  1.00 19.97 ?  1052 ASP B O     1 
ATOM   17042 C CB    . ASP B 1 1054 ? 5.158   73.944  82.724  1.00 18.82 ?  1052 ASP B CB    1 
ATOM   17043 C CG    . ASP B 1 1054 ? 4.350   73.948  83.999  1.00 24.83 ?  1052 ASP B CG    1 
ATOM   17044 O OD1   . ASP B 1 1054 ? 3.130   74.193  83.919  1.00 22.88 ?  1052 ASP B OD1   1 
ATOM   17045 O OD2   . ASP B 1 1054 ? 4.934   73.722  85.081  1.00 24.86 ?  1052 ASP B OD2   1 
ATOM   17046 N N     . PHE B 1 1055 ? 5.736   73.330  79.620  1.00 17.11 ?  1053 PHE B N     1 
ATOM   17047 C CA    . PHE B 1 1055 ? 6.509   73.583  78.405  1.00 16.41 ?  1053 PHE B CA    1 
ATOM   17048 C C     . PHE B 1 1055 ? 5.605   74.019  77.263  1.00 18.70 ?  1053 PHE B C     1 
ATOM   17049 O O     . PHE B 1 1055 ? 5.941   74.939  76.507  1.00 18.36 ?  1053 PHE B O     1 
ATOM   17050 C CB    . PHE B 1 1055 ? 7.301   72.322  78.039  1.00 16.60 ?  1053 PHE B CB    1 
ATOM   17051 C CG    . PHE B 1 1055 ? 8.190   72.469  76.821  1.00 14.23 ?  1053 PHE B CG    1 
ATOM   17052 C CD1   . PHE B 1 1055 ? 9.151   73.464  76.764  1.00 19.51 ?  1053 PHE B CD1   1 
ATOM   17053 C CD2   . PHE B 1 1055 ? 8.077   71.589  75.763  1.00 14.83 ?  1053 PHE B CD2   1 
ATOM   17054 C CE1   . PHE B 1 1055 ? 9.974   73.589  75.654  1.00 17.73 ?  1053 PHE B CE1   1 
ATOM   17055 C CE2   . PHE B 1 1055 ? 8.904   71.707  74.641  1.00 17.12 ?  1053 PHE B CE2   1 
ATOM   17056 C CZ    . PHE B 1 1055 ? 9.851   72.715  74.597  1.00 18.36 ?  1053 PHE B CZ    1 
ATOM   17057 N N     . ALA B 1 1056 ? 4.433   73.395  77.145  1.00 17.08 ?  1054 ALA B N     1 
ATOM   17058 C CA    . ALA B 1 1056 ? 3.514   73.755  76.074  1.00 16.76 ?  1054 ALA B CA    1 
ATOM   17059 C C     . ALA B 1 1056 ? 3.014   75.185  76.235  1.00 18.04 ?  1054 ALA B C     1 
ATOM   17060 O O     . ALA B 1 1056 ? 2.881   75.914  75.247  1.00 20.54 ?  1054 ALA B O     1 
ATOM   17061 C CB    . ALA B 1 1056 ? 2.339   72.773  76.037  1.00 17.19 ?  1054 ALA B CB    1 
ATOM   17062 N N     . LYS B 1 1057 ? 2.725   75.599  77.473  1.00 19.14 ?  1055 LYS B N     1 
ATOM   17063 C CA    . LYS B 1 1057 ? 2.300   76.977  77.708  1.00 22.20 ?  1055 LYS B CA    1 
ATOM   17064 C C     . LYS B 1 1057 ? 3.413   77.958  77.362  1.00 25.37 ?  1055 LYS B C     1 
ATOM   17065 O O     . LYS B 1 1057 ? 3.160   79.018  76.776  1.00 25.40 ?  1055 LYS B O     1 
ATOM   17066 C CB    . LYS B 1 1057 ? 1.865   77.156  79.159  1.00 21.91 ?  1055 LYS B CB    1 
ATOM   17067 C CG    . LYS B 1 1057 ? 0.499   76.577  79.459  1.00 25.80 ?  1055 LYS B CG    1 
ATOM   17068 C CD    . LYS B 1 1057 ? 0.078   76.857  80.876  1.00 23.66 ?  1055 LYS B CD    1 
ATOM   17069 C CE    . LYS B 1 1057 ? 1.038   76.255  81.880  1.00 24.67 ?  1055 LYS B CE    1 
ATOM   17070 N NZ    . LYS B 1 1057 ? 0.444   76.317  83.243  1.00 27.86 ?  1055 LYS B NZ    1 
ATOM   17071 N N     . TRP B 1 1058 ? 4.654   77.623  77.727  1.00 22.46 ?  1056 TRP B N     1 
ATOM   17072 C CA    . TRP B 1 1058 ? 5.787   78.476  77.375  1.00 25.07 ?  1056 TRP B CA    1 
ATOM   17073 C C     . TRP B 1 1058 ? 5.924   78.600  75.864  1.00 23.47 ?  1056 TRP B C     1 
ATOM   17074 O O     . TRP B 1 1058 ? 6.152   79.700  75.340  1.00 24.67 ?  1056 TRP B O     1 
ATOM   17075 C CB    . TRP B 1 1058 ? 7.064   77.919  78.006  1.00 23.37 ?  1056 TRP B CB    1 
ATOM   17076 C CG    . TRP B 1 1058 ? 8.341   78.638  77.649  1.00 26.33 ?  1056 TRP B CG    1 
ATOM   17077 C CD1   . TRP B 1 1058 ? 8.822   79.790  78.202  1.00 31.90 ?  1056 TRP B CD1   1 
ATOM   17078 C CD2   . TRP B 1 1058 ? 9.315   78.217  76.689  1.00 23.65 ?  1056 TRP B CD2   1 
ATOM   17079 N NE1   . TRP B 1 1058 ? 10.028  80.125  77.629  1.00 29.32 ?  1056 TRP B NE1   1 
ATOM   17080 C CE2   . TRP B 1 1058 ? 10.354  79.174  76.698  1.00 27.23 ?  1056 TRP B CE2   1 
ATOM   17081 C CE3   . TRP B 1 1058 ? 9.407   77.131  75.816  1.00 26.35 ?  1056 TRP B CE3   1 
ATOM   17082 C CZ2   . TRP B 1 1058 ? 11.472  79.072  75.866  1.00 27.44 ?  1056 TRP B CZ2   1 
ATOM   17083 C CZ3   . TRP B 1 1058 ? 10.515  77.037  74.981  1.00 27.80 ?  1056 TRP B CZ3   1 
ATOM   17084 C CH2   . TRP B 1 1058 ? 11.531  78.002  75.016  1.00 28.67 ?  1056 TRP B CH2   1 
ATOM   17085 N N     . LEU B 1 1059 ? 5.759   77.490  75.138  1.00 21.35 ?  1057 LEU B N     1 
ATOM   17086 C CA    . LEU B 1 1059 ? 5.767   77.564  73.680  1.00 22.67 ?  1057 LEU B CA    1 
ATOM   17087 C C     . LEU B 1 1059 ? 4.611   78.416  73.159  1.00 30.28 ?  1057 LEU B C     1 
ATOM   17088 O O     . LEU B 1 1059 ? 4.783   79.176  72.196  1.00 27.61 ?  1057 LEU B O     1 
ATOM   17089 C CB    . LEU B 1 1059 ? 5.714   76.163  73.071  1.00 21.27 ?  1057 LEU B CB    1 
ATOM   17090 C CG    . LEU B 1 1059 ? 6.956   75.300  73.304  1.00 21.62 ?  1057 LEU B CG    1 
ATOM   17091 C CD1   . LEU B 1 1059 ? 6.664   73.886  72.869  1.00 20.25 ?  1057 LEU B CD1   1 
ATOM   17092 C CD2   . LEU B 1 1059 ? 8.176   75.844  72.558  1.00 24.16 ?  1057 LEU B CD2   1 
ATOM   17093 N N     . ASP B 1 1060 ? 3.425   78.295  73.775  1.00 27.39 ?  1058 ASP B N     1 
ATOM   17094 C CA    . ASP B 1 1060 ? 2.297   79.160  73.419  1.00 27.72 ?  1058 ASP B CA    1 
ATOM   17095 C C     . ASP B 1 1060 ? 2.686   80.630  73.530  1.00 29.89 ?  1058 ASP B C     1 
ATOM   17096 O O     . ASP B 1 1060 ? 2.379   81.436  72.643  1.00 36.25 ?  1058 ASP B O     1 
ATOM   17097 C CB    . ASP B 1 1060 ? 1.086   78.893  74.327  1.00 30.63 ?  1058 ASP B CB    1 
ATOM   17098 C CG    . ASP B 1 1060 ? 0.311   77.625  73.972  1.00 29.23 ?  1058 ASP B CG    1 
ATOM   17099 O OD1   . ASP B 1 1060 ? 0.274   77.217  72.789  1.00 28.66 ?  1058 ASP B OD1   1 
ATOM   17100 O OD2   . ASP B 1 1060 ? -0.303  77.048  74.905  1.00 28.54 ?  1058 ASP B OD2   1 
ATOM   17101 N N     . GLY B 1 1061 ? 3.339   81.001  74.636  1.00 28.95 ?  1059 GLY B N     1 
ATOM   17102 C CA    . GLY B 1 1061 ? 3.669   82.398  74.862  1.00 30.52 ?  1059 GLY B CA    1 
ATOM   17103 C C     . GLY B 1 1061 ? 4.639   82.952  73.840  1.00 33.07 ?  1059 GLY B C     1 
ATOM   17104 O O     . GLY B 1 1061 ? 4.643   84.156  73.571  1.00 34.20 ?  1059 GLY B O     1 
ATOM   17105 N N     . LYS B 1 1062 ? 5.461   82.091  73.250  1.00 33.00 ?  1060 LYS B N     1 
ATOM   17106 C CA    . LYS B 1 1062 ? 6.418   82.501  72.233  1.00 32.76 ?  1060 LYS B CA    1 
ATOM   17107 C C     . LYS B 1 1062 ? 5.840   82.481  70.825  1.00 38.09 ?  1060 LYS B C     1 
ATOM   17108 O O     . LYS B 1 1062 ? 6.554   82.824  69.877  1.00 38.82 ?  1060 LYS B O     1 
ATOM   17109 C CB    . LYS B 1 1062 ? 7.651   81.597  72.276  1.00 33.03 ?  1060 LYS B CB    1 
ATOM   17110 C CG    . LYS B 1 1062 ? 8.462   81.710  73.541  1.00 32.59 ?  1060 LYS B CG    1 
ATOM   17111 C CD    . LYS B 1 1062 ? 9.349   80.490  73.684  1.00 29.63 ?  1060 LYS B CD    1 
ATOM   17112 C CE    . LYS B 1 1062 ? 10.091  80.175  72.396  1.00 32.72 ?  1060 LYS B CE    1 
ATOM   17113 N NZ    . LYS B 1 1062 ? 11.284  81.031  72.205  1.00 33.26 ?  1060 LYS B NZ    1 
ATOM   17114 N N     . GLY B 1 1063 ? 4.580   82.081  70.664  1.00 36.13 ?  1061 GLY B N     1 
ATOM   17115 C CA    . GLY B 1 1063 ? 4.011   81.952  69.338  1.00 31.13 ?  1061 GLY B CA    1 
ATOM   17116 C C     . GLY B 1 1063 ? 4.507   80.765  68.549  1.00 37.98 ?  1061 GLY B C     1 
ATOM   17117 O O     . GLY B 1 1063 ? 4.344   80.733  67.326  1.00 36.64 ?  1061 GLY B O     1 
ATOM   17118 N N     . ALA B 1 1064 ? 5.109   79.776  69.216  1.00 32.93 ?  1062 ALA B N     1 
ATOM   17119 C CA    . ALA B 1 1064 ? 5.619   78.579  68.548  1.00 32.74 ?  1062 ALA B CA    1 
ATOM   17120 C C     . ALA B 1 1064 ? 4.481   77.568  68.402  1.00 33.80 ?  1062 ALA B C     1 
ATOM   17121 O O     . ALA B 1 1064 ? 4.439   76.523  69.053  1.00 30.14 ?  1062 ALA B O     1 
ATOM   17122 C CB    . ALA B 1 1064 ? 6.795   77.999  69.322  1.00 27.95 ?  1062 ALA B CB    1 
ATOM   17123 N N     . ARG B 1 1065 ? 3.555   77.892  67.492  1.00 33.25 ?  1063 ARG B N     1 
ATOM   17124 C CA    . ARG B 1 1065 ? 2.258   77.214  67.456  1.00 27.96 ?  1063 ARG B CA    1 
ATOM   17125 C C     . ARG B 1 1065 ? 2.394   75.744  67.072  1.00 28.03 ?  1063 ARG B C     1 
ATOM   17126 O O     . ARG B 1 1065 ? 1.802   74.870  67.719  1.00 32.44 ?  1063 ARG B O     1 
ATOM   17127 C CB    . ARG B 1 1065 ? 1.314   77.943  66.492  1.00 32.09 ?  1063 ARG B CB    1 
ATOM   17128 N N     . ALA B 1 1066 ? 3.158   75.448  66.017  1.00 28.42 ?  1064 ALA B N     1 
ATOM   17129 C CA    . ALA B 1 1066 ? 3.357   74.057  65.616  1.00 28.28 ?  1064 ALA B CA    1 
ATOM   17130 C C     . ALA B 1 1066 ? 4.005   73.243  66.731  1.00 27.11 ?  1064 ALA B C     1 
ATOM   17131 O O     . ALA B 1 1066 ? 3.644   72.081  66.951  1.00 25.70 ?  1064 ALA B O     1 
ATOM   17132 C CB    . ALA B 1 1066 ? 4.207   73.992  64.345  1.00 28.40 ?  1064 ALA B CB    1 
ATOM   17133 N N     . GLU B 1 1067 ? 4.972   73.834  67.438  1.00 27.13 ?  1065 GLU B N     1 
ATOM   17134 C CA    . GLU B 1 1067 ? 5.666   73.096  68.491  1.00 24.57 ?  1065 GLU B CA    1 
ATOM   17135 C C     . GLU B 1 1067 ? 4.785   72.922  69.725  1.00 23.48 ?  1065 GLU B C     1 
ATOM   17136 O O     . GLU B 1 1067 ? 4.814   71.865  70.364  1.00 22.58 ?  1065 GLU B O     1 
ATOM   17137 C CB    . GLU B 1 1067 ? 6.977   73.799  68.857  1.00 24.30 ?  1065 GLU B CB    1 
ATOM   17138 C CG    . GLU B 1 1067 ? 8.093   73.646  67.816  1.00 25.06 ?  1065 GLU B CG    1 
ATOM   17139 C CD    . GLU B 1 1067 ? 7.950   74.609  66.651  1.00 29.78 ?  1065 GLU B CD    1 
ATOM   17140 O OE1   . GLU B 1 1067 ? 7.058   75.489  66.699  1.00 32.75 ?  1065 GLU B OE1   1 
ATOM   17141 O OE2   . GLU B 1 1067 ? 8.738   74.494  65.689  1.00 29.71 ?  1065 GLU B OE2   1 
ATOM   17142 N N     . ALA B 1 1068 ? 4.006   73.945  70.088  1.00 23.21 ?  1066 ALA B N     1 
ATOM   17143 C CA    . ALA B 1 1068 ? 3.107   73.795  71.232  1.00 22.71 ?  1066 ALA B CA    1 
ATOM   17144 C C     . ALA B 1 1068 ? 2.062   72.719  70.967  1.00 26.10 ?  1066 ALA B C     1 
ATOM   17145 O O     . ALA B 1 1068 ? 1.729   71.930  71.863  1.00 18.96 ?  1066 ALA B O     1 
ATOM   17146 C CB    . ALA B 1 1068 ? 2.435   75.125  71.568  1.00 23.47 ?  1066 ALA B CB    1 
ATOM   17147 N N     . GLU B 1 1069 ? 1.526   72.681  69.744  1.00 23.56 ?  1067 GLU B N     1 
ATOM   17148 C CA    . GLU B 1 1069 ? 0.621   71.604  69.356  1.00 23.03 ?  1067 GLU B CA    1 
ATOM   17149 C C     . GLU B 1 1069 ? 1.315   70.249  69.423  1.00 25.13 ?  1067 GLU B C     1 
ATOM   17150 O O     . GLU B 1 1069 ? 0.739   69.268  69.913  1.00 21.84 ?  1067 GLU B O     1 
ATOM   17151 C CB    . GLU B 1 1069 ? 0.079   71.865  67.947  1.00 25.74 ?  1067 GLU B CB    1 
ATOM   17152 C CG    . GLU B 1 1069 ? -0.634  70.682  67.289  1.00 29.89 ?  1067 GLU B CG    1 
ATOM   17153 C CD    . GLU B 1 1069 ? -2.064  70.468  67.788  1.00 34.67 ?  1067 GLU B CD    1 
ATOM   17154 O OE1   . GLU B 1 1069 ? -2.499  71.170  68.729  1.00 34.43 ?  1067 GLU B OE1   1 
ATOM   17155 O OE2   . GLU B 1 1069 ? -2.758  69.591  67.228  1.00 41.26 ?  1067 GLU B OE2   1 
ATOM   17156 N N     . ALA B 1 1070 ? 2.557   70.177  68.939  1.00 21.84 ?  1068 ALA B N     1 
ATOM   17157 C CA    . ALA B 1 1070 ? 3.305   68.930  69.019  1.00 23.35 ?  1068 ALA B CA    1 
ATOM   17158 C C     . ALA B 1 1070 ? 3.509   68.514  70.468  1.00 18.87 ?  1068 ALA B C     1 
ATOM   17159 O O     . ALA B 1 1070 ? 3.428   67.324  70.795  1.00 19.23 ?  1068 ALA B O     1 
ATOM   17160 C CB    . ALA B 1 1070 ? 4.649   69.074  68.307  1.00 27.59 ?  1068 ALA B CB    1 
ATOM   17161 N N     . ALA B 1 1071 ? 3.762   69.484  71.350  1.00 17.77 ?  1069 ALA B N     1 
ATOM   17162 C CA    . ALA B 1 1071 ? 3.959   69.171  72.762  1.00 15.45 ?  1069 ALA B CA    1 
ATOM   17163 C C     . ALA B 1 1071 ? 2.680   68.633  73.384  1.00 18.83 ?  1069 ALA B C     1 
ATOM   17164 O O     . ALA B 1 1071 ? 2.712   67.640  74.118  1.00 17.06 ?  1069 ALA B O     1 
ATOM   17165 C CB    . ALA B 1 1071 ? 4.439   70.408  73.519  1.00 18.21 ?  1069 ALA B CB    1 
ATOM   17166 N N     . ARG B 1 1072 ? 1.541   69.271  73.097  1.00 17.95 ?  1070 ARG B N     1 
ATOM   17167 C CA    A ARG B 1 1072 ? 0.283   68.776  73.645  0.51 17.89 ?  1070 ARG B CA    1 
ATOM   17168 C CA    B ARG B 1 1072 ? 0.270   68.784  73.629  0.49 17.90 ?  1070 ARG B CA    1 
ATOM   17169 C C     . ARG B 1 1072 ? -0.034  67.381  73.118  1.00 20.31 ?  1070 ARG B C     1 
ATOM   17170 O O     . ARG B 1 1072 ? -0.507  66.520  73.873  1.00 17.59 ?  1070 ARG B O     1 
ATOM   17171 C CB    A ARG B 1 1072 ? -0.847  69.764  73.339  0.51 19.59 ?  1070 ARG B CB    1 
ATOM   17172 C CB    B ARG B 1 1072 ? -0.862  69.753  73.263  0.49 19.57 ?  1070 ARG B CB    1 
ATOM   17173 C CG    A ARG B 1 1072 ? -0.632  71.108  74.024  0.51 21.53 ?  1070 ARG B CG    1 
ATOM   17174 C CG    B ARG B 1 1072 ? -0.852  71.063  74.055  0.49 21.47 ?  1070 ARG B CG    1 
ATOM   17175 C CD    A ARG B 1 1072 ? -1.874  71.990  74.056  0.51 22.00 ?  1070 ARG B CD    1 
ATOM   17176 C CD    B ARG B 1 1072 ? -2.073  71.936  73.743  0.49 21.71 ?  1070 ARG B CD    1 
ATOM   17177 N NE    A ARG B 1 1072 ? -1.547  73.300  74.606  0.51 21.40 ?  1070 ARG B NE    1 
ATOM   17178 N NE    B ARG B 1 1072 ? -2.141  72.312  72.336  0.49 23.42 ?  1070 ARG B NE    1 
ATOM   17179 C CZ    A ARG B 1 1072 ? -1.370  73.545  75.896  0.51 20.21 ?  1070 ARG B CZ    1 
ATOM   17180 C CZ    B ARG B 1 1072 ? -1.718  73.468  71.841  0.49 21.45 ?  1070 ARG B CZ    1 
ATOM   17181 N NH1   A ARG B 1 1072 ? -1.548  72.604  76.811  0.51 22.30 ?  1070 ARG B NH1   1 
ATOM   17182 N NH1   B ARG B 1 1072 ? -1.232  74.420  72.621  0.49 20.99 ?  1070 ARG B NH1   1 
ATOM   17183 N NH2   A ARG B 1 1072 ? -0.999  74.762  76.280  0.51 21.53 ?  1070 ARG B NH2   1 
ATOM   17184 N NH2   B ARG B 1 1072 ? -1.774  73.670  70.526  0.49 19.88 ?  1070 ARG B NH2   1 
ATOM   17185 N N     . ASN B 1 1073 ? 0.240   67.126  71.837  1.00 17.64 ?  1071 ASN B N     1 
ATOM   17186 C CA    . ASN B 1 1073 ? -0.009  65.799  71.290  1.00 18.21 ?  1071 ASN B CA    1 
ATOM   17187 C C     . ASN B 1 1073 ? 0.899   64.756  71.928  1.00 19.70 ?  1071 ASN B C     1 
ATOM   17188 O O     . ASN B 1 1073 ? 0.459   63.633  72.192  1.00 18.93 ?  1071 ASN B O     1 
ATOM   17189 C CB    . ASN B 1 1073 ? 0.151   65.820  69.773  1.00 21.14 ?  1071 ASN B CB    1 
ATOM   17190 C CG    . ASN B 1 1073 ? -0.959  66.590  69.097  1.00 28.12 ?  1071 ASN B CG    1 
ATOM   17191 O OD1   . ASN B 1 1073 ? -2.031  66.784  69.676  1.00 29.47 ?  1071 ASN B OD1   1 
ATOM   17192 N ND2   . ASN B 1 1073 ? -0.712  67.035  67.871  1.00 30.33 ?  1071 ASN B ND2   1 
ATOM   17193 N N     . ALA B 1 1074 ? 2.158   65.113  72.206  1.00 17.96 ?  1072 ALA B N     1 
ATOM   17194 C CA    . ALA B 1 1074 ? 3.039   64.195  72.928  1.00 17.53 ?  1072 ALA B CA    1 
ATOM   17195 C C     . ALA B 1 1074 ? 2.512   63.921  74.330  1.00 16.00 ?  1072 ALA B C     1 
ATOM   17196 O O     . ALA B 1 1074 ? 2.531   62.774  74.790  1.00 14.74 ?  1072 ALA B O     1 
ATOM   17197 C CB    . ALA B 1 1074 ? 4.456   64.760  72.997  1.00 16.93 ?  1072 ALA B CB    1 
ATOM   17198 N N     . GLY B 1 1075 ? 2.033   64.959  75.022  1.00 13.63 ?  1073 GLY B N     1 
ATOM   17199 C CA    . GLY B 1 1075 ? 1.503   64.752  76.365  1.00 16.73 ?  1073 GLY B CA    1 
ATOM   17200 C C     . GLY B 1 1075 ? 0.352   63.768  76.385  1.00 19.55 ?  1073 GLY B C     1 
ATOM   17201 O O     . GLY B 1 1075 ? 0.246   62.934  77.292  1.00 18.43 ?  1073 GLY B O     1 
ATOM   17202 N N     . SER B 1 1076 ? -0.518  63.840  75.375  1.00 19.11 ?  1074 SER B N     1 
ATOM   17203 C CA    . SER B 1 1076 ? -1.646  62.918  75.323  1.00 18.75 ?  1074 SER B CA    1 
ATOM   17204 C C     . SER B 1 1076 ? -1.203  61.528  74.888  1.00 19.87 ?  1074 SER B C     1 
ATOM   17205 O O     . SER B 1 1076 ? -1.650  60.525  75.463  1.00 23.22 ?  1074 SER B O     1 
ATOM   17206 C CB    . SER B 1 1076 ? -2.715  63.470  74.386  1.00 21.02 ?  1074 SER B CB    1 
ATOM   17207 O OG    . SER B 1 1076 ? -3.299  64.625  74.957  1.00 23.79 ?  1074 SER B OG    1 
ATOM   17208 N N     . SER B 1 1077 ? -0.301  61.462  73.895  1.00 18.15 ?  1075 SER B N     1 
ATOM   17209 C CA    . SER B 1 1077 ? 0.186   60.214  73.302  1.00 21.97 ?  1075 SER B CA    1 
ATOM   17210 C C     . SER B 1 1077 ? 0.970   59.364  74.293  1.00 17.96 ?  1075 SER B C     1 
ATOM   17211 O O     . SER B 1 1077 ? 0.949   58.127  74.215  1.00 21.45 ?  1075 SER B O     1 
ATOM   17212 C CB    . SER B 1 1077 ? 1.084   60.547  72.102  1.00 21.53 ?  1075 SER B CB    1 
ATOM   17213 O OG    . SER B 1 1077 ? 1.788   59.420  71.626  1.00 31.15 ?  1075 SER B OG    1 
ATOM   17214 N N     . SER B 1 1078 ? 1.666   60.010  75.216  1.00 13.87 ?  1076 SER B N     1 
ATOM   17215 C CA    . SER B 1 1078 ? 2.525   59.311  76.152  1.00 12.92 ?  1076 SER B CA    1 
ATOM   17216 C C     . SER B 1 1078 ? 1.729   58.317  76.985  1.00 12.95 ?  1076 SER B C     1 
ATOM   17217 O O     . SER B 1 1078 ? 0.623   58.623  77.447  1.00 14.24 ?  1076 SER B O     1 
ATOM   17218 C CB    . SER B 1 1078 ? 3.190   60.329  77.071  1.00 13.79 ?  1076 SER B CB    1 
ATOM   17219 O OG    . SER B 1 1078 ? 3.858   59.685  78.146  1.00 11.98 ?  1076 SER B OG    1 
ATOM   17220 N N     . ALA B 1 1079 ? 2.311   57.137  77.207  1.00 12.53 ?  1077 ALA B N     1 
ATOM   17221 C CA    . ALA B 1 1079 ? 1.702   56.163  78.102  1.00 10.54 ?  1077 ALA B CA    1 
ATOM   17222 C C     . ALA B 1 1079 ? 2.323   56.178  79.486  1.00 11.96 ?  1077 ALA B C     1 
ATOM   17223 O O     . ALA B 1 1079 ? 2.082   55.254  80.262  1.00 11.87 ?  1077 ALA B O     1 
ATOM   17224 C CB    . ALA B 1 1079 ? 1.774   54.755  77.511  1.00 13.10 ?  1077 ALA B CB    1 
ATOM   17225 N N     . LEU B 1 1080 ? 3.119   57.197  79.806  1.00 11.30 ?  1078 LEU B N     1 
ATOM   17226 C CA    . LEU B 1 1080 ? 3.624   57.356  81.162  1.00 10.03 ?  1078 LEU B CA    1 
ATOM   17227 C C     . LEU B 1 1080 ? 2.478   57.287  82.156  1.00 9.56  ?  1078 LEU B C     1 
ATOM   17228 O O     . LEU B 1 1080 ? 1.499   58.017  82.029  1.00 11.23 ?  1078 LEU B O     1 
ATOM   17229 C CB    . LEU B 1 1080 ? 4.340   58.700  81.304  1.00 9.94  ?  1078 LEU B CB    1 
ATOM   17230 C CG    . LEU B 1 1080 ? 4.819   59.107  82.698  1.00 10.78 ?  1078 LEU B CG    1 
ATOM   17231 C CD1   . LEU B 1 1080 ? 5.931   58.177  83.161  1.00 12.76 ?  1078 LEU B CD1   1 
ATOM   17232 C CD2   . LEU B 1 1080 ? 5.229   60.571  82.712  1.00 12.84 ?  1078 LEU B CD2   1 
ATOM   17233 N N     . GLY B 1 1081 ? 2.626   56.436  83.174  1.00 11.25 ?  1079 GLY B N     1 
ATOM   17234 C CA    . GLY B 1 1081 ? 1.581   56.292  84.169  1.00 12.78 ?  1079 GLY B CA    1 
ATOM   17235 C C     . GLY B 1 1081 ? 0.648   55.121  83.967  1.00 13.32 ?  1079 GLY B C     1 
ATOM   17236 O O     . GLY B 1 1081 ? -0.246  54.909  84.807  1.00 14.37 ?  1079 GLY B O     1 
ATOM   17237 N N     . LEU B 1 1082 ? 0.799   54.387  82.867  1.00 11.94 ?  1080 LEU B N     1 
ATOM   17238 C CA    A LEU B 1 1082 ? 0.065   53.146  82.674  0.58 10.98 ?  1080 LEU B CA    1 
ATOM   17239 C CA    B LEU B 1 1082 ? 0.054   53.153  82.683  0.42 11.00 ?  1080 LEU B CA    1 
ATOM   17240 C C     . LEU B 1 1082 ? 0.272   52.241  83.880  1.00 12.73 ?  1080 LEU B C     1 
ATOM   17241 O O     . LEU B 1 1082 ? 1.390   52.102  84.378  1.00 12.66 ?  1080 LEU B O     1 
ATOM   17242 C CB    A LEU B 1 1082 ? 0.547   52.467  81.387  0.58 11.87 ?  1080 LEU B CB    1 
ATOM   17243 C CB    B LEU B 1 1082 ? 0.497   52.463  81.393  0.42 11.88 ?  1080 LEU B CB    1 
ATOM   17244 C CG    A LEU B 1 1082 ? -0.002  51.108  80.933  0.58 11.13 ?  1080 LEU B CG    1 
ATOM   17245 C CG    B LEU B 1 1082 ? -0.166  51.118  81.087  0.42 11.28 ?  1080 LEU B CG    1 
ATOM   17246 C CD1   A LEU B 1 1082 ? 0.215   50.948  79.433  0.58 11.82 ?  1080 LEU B CD1   1 
ATOM   17247 C CD1   B LEU B 1 1082 ? -1.676  51.276  81.030  0.42 13.00 ?  1080 LEU B CD1   1 
ATOM   17248 C CD2   A LEU B 1 1082 ? 0.653   49.961  81.688  0.58 12.23 ?  1080 LEU B CD2   1 
ATOM   17249 C CD2   B LEU B 1 1082 ? 0.366   50.561  79.783  0.42 12.11 ?  1080 LEU B CD2   1 
ATOM   17250 N N     . ASP B 1 1083 ? -0.814  51.620  84.344  1.00 13.90 ?  1081 ASP B N     1 
ATOM   17251 C CA    . ASP B 1 1083 ? -0.763  50.809  85.561  1.00 16.42 ?  1081 ASP B CA    1 
ATOM   17252 C C     . ASP B 1 1083 ? -1.817  49.715  85.405  1.00 15.08 ?  1081 ASP B C     1 
ATOM   17253 O O     . ASP B 1 1083 ? -3.007  49.973  85.611  1.00 18.93 ?  1081 ASP B O     1 
ATOM   17254 C CB    . ASP B 1 1083 ? -1.011  51.696  86.775  1.00 16.66 ?  1081 ASP B CB    1 
ATOM   17255 C CG    . ASP B 1 1083 ? -0.962  50.947  88.095  1.00 25.72 ?  1081 ASP B CG    1 
ATOM   17256 O OD1   . ASP B 1 1083 ? -0.500  49.791  88.126  1.00 28.58 ?  1081 ASP B OD1   1 
ATOM   17257 O OD2   . ASP B 1 1083 ? -1.391  51.539  89.111  1.00 33.08 ?  1081 ASP B OD2   1 
ATOM   17258 N N     . LEU B 1 1084 ? -1.368  48.509  85.053  1.00 14.11 ?  1082 LEU B N     1 
ATOM   17259 C CA    . LEU B 1 1084 ? -2.228  47.412  84.627  1.00 15.92 ?  1082 LEU B CA    1 
ATOM   17260 C C     . LEU B 1 1084 ? -2.017  46.208  85.531  1.00 15.21 ?  1082 LEU B C     1 
ATOM   17261 O O     . LEU B 1 1084 ? -0.911  45.982  86.021  1.00 14.73 ?  1082 LEU B O     1 
ATOM   17262 C CB    . LEU B 1 1084 ? -1.924  46.986  83.176  1.00 16.88 ?  1082 LEU B CB    1 
ATOM   17263 C CG    . LEU B 1 1084 ? -2.248  47.921  82.017  1.00 18.96 ?  1082 LEU B CG    1 
ATOM   17264 C CD1   . LEU B 1 1084 ? -1.799  47.303  80.710  1.00 18.78 ?  1082 LEU B CD1   1 
ATOM   17265 C CD2   . LEU B 1 1084 ? -3.744  48.231  82.011  1.00 22.48 ?  1082 LEU B CD2   1 
ATOM   17266 N N     . GLU B 1 1085 ? -3.081  45.430  85.742  1.00 14.05 ?  1083 GLU B N     1 
ATOM   17267 C CA    . GLU B 1 1085 ? -2.946  44.075  86.263  1.00 13.25 ?  1083 GLU B CA    1 
ATOM   17268 C C     . GLU B 1 1085 ? -3.118  43.075  85.125  1.00 13.76 ?  1083 GLU B C     1 
ATOM   17269 O O     . GLU B 1 1085 ? -4.114  43.123  84.396  1.00 18.64 ?  1083 GLU B O     1 
ATOM   17270 C CB    . GLU B 1 1085 ? -3.955  43.780  87.372  1.00 13.01 ?  1083 GLU B CB    1 
ATOM   17271 C CG    . GLU B 1 1085 ? -3.697  42.380  87.936  1.00 15.93 ?  1083 GLU B CG    1 
ATOM   17272 C CD    . GLU B 1 1085 ? -4.545  42.010  89.145  1.00 18.80 ?  1083 GLU B CD    1 
ATOM   17273 O OE1   . GLU B 1 1085 ? -5.140  42.910  89.793  1.00 21.62 ?  1083 GLU B OE1   1 
ATOM   17274 O OE2   . GLU B 1 1085 ? -4.601  40.793  89.452  1.00 20.89 ?  1083 GLU B OE2   1 
ATOM   17275 N N     . LEU B 1 1086 ? -2.135  42.203  84.952  1.00 11.42 ?  1084 LEU B N     1 
ATOM   17276 C CA    . LEU B 1 1086 ? -2.116  41.205  83.886  1.00 12.61 ?  1084 LEU B CA    1 
ATOM   17277 C C     . LEU B 1 1086 ? -2.748  39.898  84.360  1.00 16.51 ?  1084 LEU B C     1 
ATOM   17278 O O     . LEU B 1 1086 ? -2.527  39.480  85.504  1.00 16.17 ?  1084 LEU B O     1 
ATOM   17279 C CB    . LEU B 1 1086 ? -0.691  40.933  83.423  1.00 13.40 ?  1084 LEU B CB    1 
ATOM   17280 C CG    . LEU B 1 1086 ? 0.097   42.140  82.915  1.00 13.75 ?  1084 LEU B CG    1 
ATOM   17281 C CD1   . LEU B 1 1086 ? 1.498   41.749  82.479  1.00 15.39 ?  1084 LEU B CD1   1 
ATOM   17282 C CD2   . LEU B 1 1086 ? -0.658  42.847  81.785  1.00 17.50 ?  1084 LEU B CD2   1 
ATOM   17283 N N     . PRO B 1 1087 ? -3.536  39.254  83.502  1.00 13.29 ?  1085 PRO B N     1 
ATOM   17284 C CA    . PRO B 1 1087 ? -4.149  37.971  83.876  1.00 15.59 ?  1085 PRO B CA    1 
ATOM   17285 C C     . PRO B 1 1087 ? -3.098  36.914  84.159  1.00 13.75 ?  1085 PRO B C     1 
ATOM   17286 O O     . PRO B 1 1087 ? -2.105  36.788  83.442  1.00 16.38 ?  1085 PRO B O     1 
ATOM   17287 C CB    . PRO B 1 1087 ? -4.980  37.596  82.643  1.00 19.21 ?  1085 PRO B CB    1 
ATOM   17288 C CG    . PRO B 1 1087 ? -5.135  38.831  81.868  1.00 18.74 ?  1085 PRO B CG    1 
ATOM   17289 C CD    . PRO B 1 1087 ? -3.956  39.705  82.163  1.00 14.62 ?  1085 PRO B CD    1 
ATOM   17290 N N     . GLY B 1 1088 ? -3.330  36.137  85.208  1.00 14.43 ?  1086 GLY B N     1 
ATOM   17291 C CA    . GLY B 1 1088 ? -2.407  35.111  85.624  1.00 14.77 ?  1086 GLY B CA    1 
ATOM   17292 C C     . GLY B 1 1088 ? -3.062  34.158  86.607  1.00 11.14 ?  1086 GLY B C     1 
ATOM   17293 O O     . GLY B 1 1088 ? -4.293  34.073  86.706  1.00 14.44 ?  1086 GLY B O     1 
ATOM   17294 N N     . PRO B 1 1089 ? -2.244  33.439  87.369  1.00 13.96 ?  1087 PRO B N     1 
ATOM   17295 C CA    . PRO B 1 1089 ? -2.776  32.464  88.327  1.00 13.38 ?  1087 PRO B CA    1 
ATOM   17296 C C     . PRO B 1 1089 ? -3.428  33.131  89.525  1.00 13.24 ?  1087 PRO B C     1 
ATOM   17297 O O     . PRO B 1 1089 ? -3.117  34.272  89.885  1.00 14.52 ?  1087 PRO B O     1 
ATOM   17298 C CB    . PRO B 1 1089 ? -1.524  31.691  88.757  1.00 15.45 ?  1087 PRO B CB    1 
ATOM   17299 C CG    . PRO B 1 1089 ? -0.409  32.710  88.604  1.00 18.37 ?  1087 PRO B CG    1 
ATOM   17300 C CD    . PRO B 1 1089 ? -0.773  33.500  87.384  1.00 17.37 ?  1087 PRO B CD    1 
ATOM   17301 N N     . VAL B 1 1090 ? -4.353  32.391  90.149  1.00 12.53 ?  1088 VAL B N     1 
ATOM   17302 C CA    . VAL B 1 1090 ? -4.870  32.832  91.445  1.00 12.38 ?  1088 VAL B CA    1 
ATOM   17303 C C     . VAL B 1 1090 ? -3.733  32.892  92.468  1.00 14.05 ?  1088 VAL B C     1 
ATOM   17304 O O     . VAL B 1 1090 ? -2.692  32.244  92.335  1.00 13.67 ?  1088 VAL B O     1 
ATOM   17305 C CB    . VAL B 1 1090 ? -5.996  31.930  91.964  1.00 14.53 ?  1088 VAL B CB    1 
ATOM   17306 C CG1   . VAL B 1 1090 ? -7.148  31.906  90.980  1.00 14.51 ?  1088 VAL B CG1   1 
ATOM   17307 C CG2   . VAL B 1 1090 ? -5.474  30.526  92.240  1.00 15.42 ?  1088 VAL B CG2   1 
ATOM   17308 N N     . GLY B 1 1091 ? -3.953  33.678  93.516  1.00 14.04 ?  1089 GLY B N     1 
ATOM   17309 C CA    . GLY B 1 1091 ? -2.958  33.771  94.573  1.00 12.72 ?  1089 GLY B CA    1 
ATOM   17310 C C     . GLY B 1 1091 ? -1.762  34.619  94.233  1.00 12.96 ?  1089 GLY B C     1 
ATOM   17311 O O     . GLY B 1 1091 ? -0.758  34.587  94.967  1.00 12.06 ?  1089 GLY B O     1 
ATOM   17312 N N     . GLU B 1 1092 ? -1.834  35.356  93.129  1.00 13.79 ?  1090 GLU B N     1 
ATOM   17313 C CA    . GLU B 1 1092 ? -0.778  36.241  92.684  1.00 12.60 ?  1090 GLU B CA    1 
ATOM   17314 C C     . GLU B 1 1092 ? -1.412  37.467  92.063  1.00 12.69 ?  1090 GLU B C     1 
ATOM   17315 O O     . GLU B 1 1092 ? -2.479  37.384  91.445  1.00 13.93 ?  1090 GLU B O     1 
ATOM   17316 C CB    . GLU B 1 1092 ? 0.114   35.559  91.653  1.00 15.67 ?  1090 GLU B CB    1 
ATOM   17317 C CG    . GLU B 1 1092 ? 1.556   35.912  91.703  1.00 19.82 ?  1090 GLU B CG    1 
ATOM   17318 C CD    . GLU B 1 1092 ? 2.356   34.947  90.847  1.00 19.15 ?  1090 GLU B CD    1 
ATOM   17319 O OE1   . GLU B 1 1092 ? 2.158   34.967  89.616  1.00 17.96 ?  1090 GLU B OE1   1 
ATOM   17320 O OE2   . GLU B 1 1092 ? 3.140   34.147  91.407  1.00 21.56 ?  1090 GLU B OE2   1 
ATOM   17321 N N     . ARG B 1 1093 ? -0.752  38.601  92.236  1.00 11.67 ?  1091 ARG B N     1 
ATOM   17322 C CA    . ARG B 1 1093 ? -1.128  39.838  91.567  1.00 11.63 ?  1091 ARG B CA    1 
ATOM   17323 C C     . ARG B 1 1093 ? 0.061   40.273  90.730  1.00 10.74 ?  1091 ARG B C     1 
ATOM   17324 O O     . ARG B 1 1093 ? 1.154   40.493  91.263  1.00 11.66 ?  1091 ARG B O     1 
ATOM   17325 C CB    . ARG B 1 1093 ? -1.518  40.921  92.567  1.00 16.54 ?  1091 ARG B CB    1 
ATOM   17326 C CG    . ARG B 1 1093 ? -1.957  42.208  91.923  1.00 23.23 ?  1091 ARG B CG    1 
ATOM   17327 C CD    . ARG B 1 1093 ? -2.481  43.198  92.949  1.00 27.89 ?  1091 ARG B CD    1 
ATOM   17328 N NE    . ARG B 1 1093 ? -3.415  42.552  93.863  1.00 28.94 ?  1091 ARG B NE    1 
ATOM   17329 C CZ    . ARG B 1 1093 ? -3.207  42.401  95.164  1.00 26.83 ?  1091 ARG B CZ    1 
ATOM   17330 N NH1   . ARG B 1 1093 ? -2.119  42.879  95.753  1.00 33.28 ?  1091 ARG B NH1   1 
ATOM   17331 N NH2   . ARG B 1 1093 ? -4.120  41.765  95.895  1.00 29.54 ?  1091 ARG B NH2   1 
ATOM   17332 N N     . ASN B 1 1094 ? -0.143  40.377  89.424  1.00 9.69  ?  1092 ASN B N     1 
ATOM   17333 C CA    . ASN B 1 1094 ? 0.951   40.622  88.490  1.00 10.27 ?  1092 ASN B CA    1 
ATOM   17334 C C     . ASN B 1 1094 ? 0.698   41.953  87.810  1.00 12.37 ?  1092 ASN B C     1 
ATOM   17335 O O     . ASN B 1 1094 ? -0.289  42.106  87.082  1.00 12.79 ?  1092 ASN B O     1 
ATOM   17336 C CB    . ASN B 1 1094 ? 1.060   39.472  87.500  1.00 11.22 ?  1092 ASN B CB    1 
ATOM   17337 C CG    . ASN B 1 1094 ? 1.642   38.245  88.157  1.00 10.79 ?  1092 ASN B CG    1 
ATOM   17338 O OD1   . ASN B 1 1094 ? 2.812   38.247  88.518  1.00 12.34 ?  1092 ASN B OD1   1 
ATOM   17339 N ND2   . ASN B 1 1094 ? 0.826   37.225  88.372  1.00 13.27 ?  1092 ASN B ND2   1 
ATOM   17340 N N     . LEU B 1 1095 ? 1.558   42.920  88.091  1.00 11.58 ?  1093 LEU B N     1 
ATOM   17341 C CA    . LEU B 1 1095 ? 1.329   44.308  87.721  1.00 11.02 ?  1093 LEU B CA    1 
ATOM   17342 C C     . LEU B 1 1095 ? 2.357   44.739  86.689  1.00 10.83 ?  1093 LEU B C     1 
ATOM   17343 O O     . LEU B 1 1095 ? 3.498   44.277  86.698  1.00 12.33 ?  1093 LEU B O     1 
ATOM   17344 C CB    . LEU B 1 1095 ? 1.402   45.222  88.948  1.00 12.84 ?  1093 LEU B CB    1 
ATOM   17345 C CG    . LEU B 1 1095 ? 0.544   44.710  90.113  1.00 16.98 ?  1093 LEU B CG    1 
ATOM   17346 C CD1   . LEU B 1 1095 ? 0.831   45.491  91.394  1.00 23.05 ?  1093 LEU B CD1   1 
ATOM   17347 C CD2   . LEU B 1 1095 ? -0.910  44.782  89.734  1.00 18.02 ?  1093 LEU B CD2   1 
ATOM   17348 N N     . TYR B 1 1096 ? 1.942   45.656  85.819  1.00 10.81 ?  1094 TYR B N     1 
ATOM   17349 C CA    . TYR B 1 1096 ? 2.782   46.151  84.734  1.00 11.20 ?  1094 TYR B CA    1 
ATOM   17350 C C     . TYR B 1 1096 ? 2.579   47.655  84.652  1.00 11.50 ?  1094 TYR B C     1 
ATOM   17351 O O     . TYR B 1 1096 ? 1.446   48.126  84.522  1.00 11.65 ?  1094 TYR B O     1 
ATOM   17352 C CB    . TYR B 1 1096 ? 2.416   45.453  83.413  1.00 9.54  ?  1094 TYR B CB    1 
ATOM   17353 C CG    . TYR B 1 1096 ? 3.092   45.980  82.178  1.00 10.47 ?  1094 TYR B CG    1 
ATOM   17354 C CD1   . TYR B 1 1096 ? 4.326   45.503  81.775  1.00 10.44 ?  1094 TYR B CD1   1 
ATOM   17355 C CD2   . TYR B 1 1096 ? 2.467   46.932  81.391  1.00 12.69 ?  1094 TYR B CD2   1 
ATOM   17356 C CE1   . TYR B 1 1096 ? 4.938   45.974  80.605  1.00 10.91 ?  1094 TYR B CE1   1 
ATOM   17357 C CE2   . TYR B 1 1096 ? 3.066   47.398  80.226  1.00 12.86 ?  1094 TYR B CE2   1 
ATOM   17358 C CZ    . TYR B 1 1096 ? 4.294   46.915  79.846  1.00 12.41 ?  1094 TYR B CZ    1 
ATOM   17359 O OH    . TYR B 1 1096 ? 4.877   47.377  78.685  1.00 12.83 ?  1094 TYR B OH    1 
ATOM   17360 N N     . THR B 1 1097 ? 3.669   48.411  84.754  1.00 9.84  ?  1095 THR B N     1 
ATOM   17361 C CA    . THR B 1 1097 ? 3.581   49.861  84.875  1.00 10.00 ?  1095 THR B CA    1 
ATOM   17362 C C     . THR B 1 1097 ? 4.626   50.524  83.991  1.00 10.93 ?  1095 THR B C     1 
ATOM   17363 O O     . THR B 1 1097 ? 5.672   49.943  83.711  1.00 12.35 ?  1095 THR B O     1 
ATOM   17364 C CB    . THR B 1 1097 ? 3.778   50.323  86.324  1.00 12.73 ?  1095 THR B CB    1 
ATOM   17365 O OG1   . THR B 1 1097 ? 5.030   49.845  86.822  1.00 15.96 ?  1095 THR B OG1   1 
ATOM   17366 C CG2   . THR B 1 1097 ? 2.699   49.752  87.203  1.00 14.09 ?  1095 THR B CG2   1 
ATOM   17367 N N     . LEU B 1 1098 ? 4.319   51.735  83.526  1.00 10.88 ?  1096 LEU B N     1 
ATOM   17368 C CA    . LEU B 1 1098 ? 5.256   52.511  82.717  1.00 9.96  ?  1096 LEU B CA    1 
ATOM   17369 C C     . LEU B 1 1098 ? 5.678   53.775  83.458  1.00 10.02 ?  1096 LEU B C     1 
ATOM   17370 O O     . LEU B 1 1098 ? 4.839   54.594  83.859  1.00 11.05 ?  1096 LEU B O     1 
ATOM   17371 C CB    . LEU B 1 1098 ? 4.653   52.862  81.353  1.00 8.95  ?  1096 LEU B CB    1 
ATOM   17372 C CG    . LEU B 1 1098 ? 4.337   51.658  80.462  1.00 9.31  ?  1096 LEU B CG    1 
ATOM   17373 C CD1   . LEU B 1 1098 ? 3.730   52.178  79.155  1.00 10.73 ?  1096 LEU B CD1   1 
ATOM   17374 C CD2   . LEU B 1 1098 ? 5.527   50.775  80.193  1.00 11.37 ?  1096 LEU B CD2   1 
ATOM   17375 N N     . HIS B 1 1099 ? 6.986   53.930  83.615  1.00 11.88 ?  1097 HIS B N     1 
ATOM   17376 C CA    . HIS B 1 1099 ? 7.619   55.013  84.342  1.00 11.03 ?  1097 HIS B CA    1 
ATOM   17377 C C     . HIS B 1 1099 ? 8.530   55.804  83.414  1.00 11.78 ?  1097 HIS B C     1 
ATOM   17378 O O     . HIS B 1 1099 ? 8.821   55.398  82.297  1.00 13.08 ?  1097 HIS B O     1 
ATOM   17379 C CB    . HIS B 1 1099 ? 8.459   54.468  85.494  1.00 11.90 ?  1097 HIS B CB    1 
ATOM   17380 C CG    . HIS B 1 1099 ? 7.692   53.616  86.441  1.00 12.47 ?  1097 HIS B CG    1 
ATOM   17381 N ND1   . HIS B 1 1099 ? 7.283   54.072  87.673  1.00 17.36 ?  1097 HIS B ND1   1 
ATOM   17382 C CD2   . HIS B 1 1099 ? 7.253   52.340  86.339  1.00 15.67 ?  1097 HIS B CD2   1 
ATOM   17383 C CE1   . HIS B 1 1099 ? 6.633   53.105  88.300  1.00 18.33 ?  1097 HIS B CE1   1 
ATOM   17384 N NE2   . HIS B 1 1099 ? 6.610   52.042  87.516  1.00 16.13 ?  1097 HIS B NE2   1 
ATOM   17385 N N     . ALA B 1 1100 ? 8.994   56.945  83.912  1.00 13.60 ?  1098 ALA B N     1 
ATOM   17386 C CA    . ALA B 1 1100 ? 10.038  57.664  83.196  1.00 14.44 ?  1098 ALA B CA    1 
ATOM   17387 C C     . ALA B 1 1100 ? 11.304  56.821  83.145  1.00 14.85 ?  1098 ALA B C     1 
ATOM   17388 O O     . ALA B 1 1100 ? 11.568  56.019  84.046  1.00 16.59 ?  1098 ALA B O     1 
ATOM   17389 C CB    . ALA B 1 1100 ? 10.337  58.995  83.886  1.00 16.63 ?  1098 ALA B CB    1 
ATOM   17390 N N     . ARG B 1 1101 ? 12.099  57.011  82.079  1.00 15.81 ?  1099 ARG B N     1 
ATOM   17391 C CA    . ARG B 1 1101 ? 13.374  56.293  81.962  1.00 16.90 ?  1099 ARG B CA    1 
ATOM   17392 C C     . ARG B 1 1101 ? 14.478  56.915  82.809  1.00 18.25 ?  1099 ARG B C     1 
ATOM   17393 O O     . ARG B 1 1101 ? 15.290  56.192  83.402  1.00 19.31 ?  1099 ARG B O     1 
ATOM   17394 C CB    . ARG B 1 1101 ? 13.829  56.234  80.503  1.00 19.52 ?  1099 ARG B CB    1 
ATOM   17395 C CG    . ARG B 1 1101 ? 13.091  55.238  79.658  1.00 19.76 ?  1099 ARG B CG    1 
ATOM   17396 C CD    . ARG B 1 1101 ? 13.671  55.113  78.253  1.00 21.93 ?  1099 ARG B CD    1 
ATOM   17397 N NE    . ARG B 1 1101 ? 14.750  54.137  78.121  1.00 25.05 ?  1099 ARG B NE    1 
ATOM   17398 C CZ    . ARG B 1 1101 ? 14.578  52.862  77.788  1.00 28.15 ?  1099 ARG B CZ    1 
ATOM   17399 N NH1   . ARG B 1 1101 ? 13.371  52.334  77.676  1.00 23.66 ?  1099 ARG B NH1   1 
ATOM   17400 N NH2   . ARG B 1 1101 ? 15.645  52.095  77.564  1.00 24.75 ?  1099 ARG B NH2   1 
ATOM   17401 N N     . GLY B 1 1102 ? 14.548  58.241  82.867  1.00 14.82 ?  1100 GLY B N     1 
ATOM   17402 C CA    . GLY B 1 1102 ? 15.672  58.902  83.501  1.00 16.67 ?  1100 GLY B CA    1 
ATOM   17403 C C     . GLY B 1 1102 ? 16.040  60.186  82.783  1.00 14.51 ?  1100 GLY B C     1 
ATOM   17404 O O     . GLY B 1 1102 ? 15.180  61.023  82.506  1.00 16.62 ?  1100 GLY B O     1 
ATOM   17405 N N     . ARG B 1 1103 ? 17.319  60.376  82.496  1.00 15.24 ?  1101 ARG B N     1 
ATOM   17406 C CA    . ARG B 1 1103 ? 17.782  61.567  81.793  1.00 14.60 ?  1101 ARG B CA    1 
ATOM   17407 C C     . ARG B 1 1103 ? 18.101  61.200  80.350  1.00 13.76 ?  1101 ARG B C     1 
ATOM   17408 O O     . ARG B 1 1103 ? 18.926  60.321  80.099  1.00 15.33 ?  1101 ARG B O     1 
ATOM   17409 C CB    . ARG B 1 1103 ? 19.007  62.171  82.482  1.00 14.21 ?  1101 ARG B CB    1 
ATOM   17410 C CG    . ARG B 1 1103 ? 19.407  63.510  81.834  1.00 17.11 ?  1101 ARG B CG    1 
ATOM   17411 C CD    . ARG B 1 1103 ? 20.402  64.356  82.657  1.00 21.23 ?  1101 ARG B CD    1 
ATOM   17412 N NE    . ARG B 1 1103 ? 19.971  64.627  84.028  1.00 24.63 ?  1101 ARG B NE    1 
ATOM   17413 C CZ    . ARG B 1 1103 ? 19.403  65.748  84.462  1.00 27.93 ?  1101 ARG B CZ    1 
ATOM   17414 N NH1   . ARG B 1 1103 ? 19.131  66.765  83.647  1.00 22.31 ?  1101 ARG B NH1   1 
ATOM   17415 N NH2   . ARG B 1 1103 ? 19.099  65.855  85.753  1.00 25.58 ?  1101 ARG B NH2   1 
ATOM   17416 N N     . ILE B 1 1104 ? 17.438  61.860  79.408  1.00 11.70 ?  1102 ILE B N     1 
ATOM   17417 C CA    . ILE B 1 1104 ? 17.591  61.559  77.990  1.00 12.87 ?  1102 ILE B CA    1 
ATOM   17418 C C     . ILE B 1 1104 ? 18.614  62.517  77.402  1.00 12.49 ?  1102 ILE B C     1 
ATOM   17419 O O     . ILE B 1 1104 ? 18.518  63.732  77.599  1.00 13.01 ?  1102 ILE B O     1 
ATOM   17420 C CB    . ILE B 1 1104 ? 16.249  61.685  77.244  1.00 13.20 ?  1102 ILE B CB    1 
ATOM   17421 C CG1   . ILE B 1 1104 ? 15.141  60.891  77.961  1.00 12.95 ?  1102 ILE B CG1   1 
ATOM   17422 C CG2   . ILE B 1 1104 ? 16.396  61.241  75.792  1.00 14.16 ?  1102 ILE B CG2   1 
ATOM   17423 C CD1   . ILE B 1 1104 ? 15.395  59.410  78.020  1.00 14.89 ?  1102 ILE B CD1   1 
ATOM   17424 N N     . LEU B 1 1105 ? 19.585  61.981  76.671  1.00 11.99 ?  1103 LEU B N     1 
ATOM   17425 C CA    . LEU B 1 1105 ? 20.532  62.813  75.939  1.00 12.68 ?  1103 LEU B CA    1 
ATOM   17426 C C     . LEU B 1 1105 ? 19.866  63.361  74.677  1.00 13.81 ?  1103 LEU B C     1 
ATOM   17427 O O     . LEU B 1 1105 ? 19.387  62.594  73.842  1.00 13.19 ?  1103 LEU B O     1 
ATOM   17428 C CB    . LEU B 1 1105 ? 21.773  61.993  75.587  1.00 13.45 ?  1103 LEU B CB    1 
ATOM   17429 C CG    . LEU B 1 1105 ? 22.826  62.678  74.712  1.00 14.67 ?  1103 LEU B CG    1 
ATOM   17430 C CD1   . LEU B 1 1105 ? 23.436  63.873  75.427  1.00 14.68 ?  1103 LEU B CD1   1 
ATOM   17431 C CD2   . LEU B 1 1105 ? 23.877  61.666  74.259  1.00 18.30 ?  1103 LEU B CD2   1 
ATOM   17432 N N     . LEU B 1 1106 ? 19.837  64.681  74.541  1.00 12.70 ?  1104 LEU B N     1 
ATOM   17433 C CA    . LEU B 1 1106 ? 19.253  65.347  73.385  1.00 13.20 ?  1104 LEU B CA    1 
ATOM   17434 C C     . LEU B 1 1106 ? 20.371  65.906  72.520  1.00 13.93 ?  1104 LEU B C     1 
ATOM   17435 O O     . LEU B 1 1106 ? 21.223  66.662  73.007  1.00 15.08 ?  1104 LEU B O     1 
ATOM   17436 C CB    . LEU B 1 1106 ? 18.314  66.476  73.814  1.00 14.17 ?  1104 LEU B CB    1 
ATOM   17437 C CG    . LEU B 1 1106 ? 16.840  66.131  73.933  1.00 18.30 ?  1104 LEU B CG    1 
ATOM   17438 C CD1   . LEU B 1 1106 ? 16.594  64.801  74.609  1.00 17.44 ?  1104 LEU B CD1   1 
ATOM   17439 C CD2   . LEU B 1 1106 ? 16.164  67.290  74.645  1.00 15.86 ?  1104 LEU B CD2   1 
ATOM   17440 N N     . VAL B 1 1107 ? 20.364  65.527  71.250  1.00 15.11 ?  1105 VAL B N     1 
ATOM   17441 C CA    . VAL B 1 1107 ? 21.370  65.996  70.300  1.00 14.77 ?  1105 VAL B CA    1 
ATOM   17442 C C     . VAL B 1 1107 ? 20.613  66.678  69.168  1.00 15.44 ?  1105 VAL B C     1 
ATOM   17443 O O     . VAL B 1 1107 ? 20.419  66.086  68.096  1.00 17.27 ?  1105 VAL B O     1 
ATOM   17444 C CB    . VAL B 1 1107 ? 22.266  64.845  69.808  1.00 14.68 ?  1105 VAL B CB    1 
ATOM   17445 C CG1   . VAL B 1 1107 ? 23.417  65.384  68.994  1.00 17.25 ?  1105 VAL B CG1   1 
ATOM   17446 C CG2   . VAL B 1 1107 ? 22.792  64.031  70.993  1.00 15.70 ?  1105 VAL B CG2   1 
ATOM   17447 N N     . PRO B 1 1108 ? 20.160  67.909  69.372  1.00 14.96 ?  1106 PRO B N     1 
ATOM   17448 C CA    . PRO B 1 1108 ? 19.413  68.616  68.334  1.00 15.48 ?  1106 PRO B CA    1 
ATOM   17449 C C     . PRO B 1 1108 ? 20.336  69.224  67.298  1.00 17.79 ?  1106 PRO B C     1 
ATOM   17450 O O     . PRO B 1 1108 ? 21.535  69.416  67.520  1.00 19.58 ?  1106 PRO B O     1 
ATOM   17451 C CB    . PRO B 1 1108 ? 18.699  69.722  69.115  1.00 16.84 ?  1106 PRO B CB    1 
ATOM   17452 C CG    . PRO B 1 1108 ? 19.641  70.013  70.252  1.00 16.19 ?  1106 PRO B CG    1 
ATOM   17453 C CD    . PRO B 1 1108 ? 20.226  68.675  70.632  1.00 16.42 ?  1106 PRO B CD    1 
ATOM   17454 N N     . ALA B 1 1109 ? 19.734  69.558  66.164  1.00 16.38 ?  1107 ALA B N     1 
ATOM   17455 C CA    . ALA B 1 1109 ? 20.377  70.359  65.127  1.00 18.39 ?  1107 ALA B CA    1 
ATOM   17456 C C     . ALA B 1 1109 ? 19.735  71.727  64.959  1.00 22.96 ?  1107 ALA B C     1 
ATOM   17457 O O     . ALA B 1 1109 ? 20.436  72.709  64.704  1.00 23.50 ?  1107 ALA B O     1 
ATOM   17458 C CB    . ALA B 1 1109 ? 20.343  69.612  63.784  1.00 20.64 ?  1107 ALA B CB    1 
ATOM   17459 N N     . THR B 1 1110 ? 18.413  71.815  65.115  1.00 21.60 ?  1108 THR B N     1 
ATOM   17460 C CA    . THR B 1 1110 ? 17.662  73.046  64.906  1.00 18.83 ?  1108 THR B CA    1 
ATOM   17461 C C     . THR B 1 1110 ? 16.822  73.346  66.140  1.00 19.74 ?  1108 THR B C     1 
ATOM   17462 O O     . THR B 1 1110 ? 16.530  72.454  66.942  1.00 17.81 ?  1108 THR B O     1 
ATOM   17463 C CB    . THR B 1 1110 ? 16.742  72.952  63.671  1.00 22.25 ?  1108 THR B CB    1 
ATOM   17464 O OG1   . THR B 1 1110 ? 15.699  71.992  63.908  1.00 21.71 ?  1108 THR B OG1   1 
ATOM   17465 C CG2   . THR B 1 1110 ? 17.535  72.531  62.434  1.00 22.75 ?  1108 THR B CG2   1 
ATOM   17466 N N     . GLU B 1 1111 ? 16.423  74.619  66.268  1.00 23.26 ?  1109 GLU B N     1 
ATOM   17467 C CA    . GLU B 1 1111 ? 15.576  75.035  67.385  1.00 21.30 ?  1109 GLU B CA    1 
ATOM   17468 C C     . GLU B 1 1111 ? 14.275  74.238  67.422  1.00 19.77 ?  1109 GLU B C     1 
ATOM   17469 O O     . GLU B 1 1111 ? 13.900  73.696  68.469  1.00 18.69 ?  1109 GLU B O     1 
ATOM   17470 C CB    . GLU B 1 1111 ? 15.281  76.531  67.295  1.00 19.69 ?  1109 GLU B CB    1 
ATOM   17471 C CG    . GLU B 1 1111 ? 14.279  77.018  68.339  1.00 21.26 ?  1109 GLU B CG    1 
ATOM   17472 C CD    . GLU B 1 1111 ? 14.082  78.519  68.280  1.00 23.78 ?  1109 GLU B CD    1 
ATOM   17473 O OE1   . GLU B 1 1111 ? 14.924  79.251  68.841  1.00 26.63 ?  1109 GLU B OE1   1 
ATOM   17474 O OE2   . GLU B 1 1111 ? 13.097  78.962  67.652  1.00 29.54 ?  1109 GLU B OE2   1 
ATOM   17475 N N     . SER B 1 1112 ? 13.563  74.166  66.293  1.00 21.06 ?  1110 SER B N     1 
ATOM   17476 C CA    . SER B 1 1112 ? 12.341  73.361  66.248  1.00 19.61 ?  1110 SER B CA    1 
ATOM   17477 C C     . SER B 1 1112 ? 12.617  71.908  66.618  1.00 18.87 ?  1110 SER B C     1 
ATOM   17478 O O     . SER B 1 1112 ? 11.828  71.282  67.339  1.00 18.74 ?  1110 SER B O     1 
ATOM   17479 C CB    . SER B 1 1112 ? 11.696  73.436  64.861  1.00 21.79 ?  1110 SER B CB    1 
ATOM   17480 O OG    . SER B 1 1112 ? 10.485  72.686  64.825  1.00 22.48 ?  1110 SER B OG    1 
ATOM   17481 N N     . GLY B 1 1113 ? 13.727  71.354  66.127  1.00 18.16 ?  1111 GLY B N     1 
ATOM   17482 C CA    . GLY B 1 1113 ? 14.088  69.993  66.491  1.00 17.06 ?  1111 GLY B CA    1 
ATOM   17483 C C     . GLY B 1 1113 ? 14.271  69.831  67.987  1.00 17.31 ?  1111 GLY B C     1 
ATOM   17484 O O     . GLY B 1 1113 ? 13.813  68.846  68.573  1.00 16.79 ?  1111 GLY B O     1 
ATOM   17485 N N     . LEU B 1 1114 ? 14.937  70.796  68.625  1.00 17.09 ?  1112 LEU B N     1 
ATOM   17486 C CA    . LEU B 1 1114 ? 15.098  70.760  70.075  1.00 14.57 ?  1112 LEU B CA    1 
ATOM   17487 C C     . LEU B 1 1114 ? 13.749  70.803  70.776  1.00 15.61 ?  1112 LEU B C     1 
ATOM   17488 O O     . LEU B 1 1114 ? 13.504  70.028  71.700  1.00 15.68 ?  1112 LEU B O     1 
ATOM   17489 C CB    . LEU B 1 1114 ? 15.980  71.920  70.542  1.00 17.80 ?  1112 LEU B CB    1 
ATOM   17490 C CG    . LEU B 1 1114 ? 16.133  72.185  72.047  1.00 17.56 ?  1112 LEU B CG    1 
ATOM   17491 C CD1   . LEU B 1 1114 ? 16.640  70.955  72.797  1.00 18.56 ?  1112 LEU B CD1   1 
ATOM   17492 C CD2   . LEU B 1 1114 ? 17.050  73.387  72.307  1.00 19.46 ?  1112 LEU B CD2   1 
ATOM   17493 N N     . TYR B 1 1115 ? 12.853  71.685  70.325  1.00 16.29 ?  1113 TYR B N     1 
ATOM   17494 C CA    . TYR B 1 1115 ? 11.540  71.772  70.963  1.00 16.26 ?  1113 TYR B CA    1 
ATOM   17495 C C     . TYR B 1 1115 ? 10.783  70.451  70.852  1.00 15.83 ?  1113 TYR B C     1 
ATOM   17496 O O     . TYR B 1 1115 ? 10.106  70.033  71.803  1.00 16.43 ?  1113 TYR B O     1 
ATOM   17497 C CB    . TYR B 1 1115 ? 10.729  72.911  70.336  1.00 16.11 ?  1113 TYR B CB    1 
ATOM   17498 C CG    . TYR B 1 1115 ? 11.228  74.318  70.626  1.00 18.21 ?  1113 TYR B CG    1 
ATOM   17499 C CD1   . TYR B 1 1115 ? 12.121  74.581  71.658  1.00 19.06 ?  1113 TYR B CD1   1 
ATOM   17500 C CD2   . TYR B 1 1115 ? 10.789  75.391  69.862  1.00 21.48 ?  1113 TYR B CD2   1 
ATOM   17501 C CE1   . TYR B 1 1115 ? 12.569  75.881  71.909  1.00 23.95 ?  1113 TYR B CE1   1 
ATOM   17502 C CE2   . TYR B 1 1115 ? 11.216  76.674  70.111  1.00 22.30 ?  1113 TYR B CE2   1 
ATOM   17503 C CZ    . TYR B 1 1115 ? 12.104  76.922  71.130  1.00 24.13 ?  1113 TYR B CZ    1 
ATOM   17504 O OH    . TYR B 1 1115 ? 12.529  78.220  71.354  1.00 29.21 ?  1113 TYR B OH    1 
ATOM   17505 N N     . HIS B 1 1116 ? 10.846  69.800  69.688  1.00 15.47 ?  1114 HIS B N     1 
ATOM   17506 C CA    . HIS B 1 1116 ? 10.183  68.510  69.526  1.00 14.39 ?  1114 HIS B CA    1 
ATOM   17507 C C     . HIS B 1 1116 ? 10.828  67.438  70.400  1.00 14.90 ?  1114 HIS B C     1 
ATOM   17508 O O     . HIS B 1 1116 ? 10.125  66.612  70.992  1.00 15.56 ?  1114 HIS B O     1 
ATOM   17509 C CB    . HIS B 1 1116 ? 10.206  68.070  68.064  1.00 15.69 ?  1114 HIS B CB    1 
ATOM   17510 C CG    . HIS B 1 1116 ? 9.158   68.721  67.214  1.00 17.93 ?  1114 HIS B CG    1 
ATOM   17511 N ND1   . HIS B 1 1116 ? 9.304   69.989  66.691  1.00 19.93 ?  1114 HIS B ND1   1 
ATOM   17512 C CD2   . HIS B 1 1116 ? 7.951   68.276  66.791  1.00 19.38 ?  1114 HIS B CD2   1 
ATOM   17513 C CE1   . HIS B 1 1116 ? 8.234   70.294  65.977  1.00 22.58 ?  1114 HIS B CE1   1 
ATOM   17514 N NE2   . HIS B 1 1116 ? 7.395   69.276  66.029  1.00 23.35 ?  1114 HIS B NE2   1 
ATOM   17515 N N     . GLN B 1 1117 ? 12.167  67.419  70.471  1.00 14.94 ?  1115 GLN B N     1 
ATOM   17516 C CA    . GLN B 1 1117 ? 12.856  66.458  71.328  1.00 13.74 ?  1115 GLN B CA    1 
ATOM   17517 C C     . GLN B 1 1117 ? 12.500  66.668  72.792  1.00 13.78 ?  1115 GLN B C     1 
ATOM   17518 O O     . GLN B 1 1117 ? 12.249  65.695  73.519  1.00 13.80 ?  1115 GLN B O     1 
ATOM   17519 C CB    . GLN B 1 1117 ? 14.373  66.567  71.135  1.00 13.89 ?  1115 GLN B CB    1 
ATOM   17520 C CG    . GLN B 1 1117 ? 14.877  66.124  69.790  1.00 15.36 ?  1115 GLN B CG    1 
ATOM   17521 C CD    . GLN B 1 1117 ? 16.386  66.262  69.669  1.00 16.07 ?  1115 GLN B CD    1 
ATOM   17522 O OE1   . GLN B 1 1117 ? 17.035  66.917  70.484  1.00 16.24 ?  1115 GLN B OE1   1 
ATOM   17523 N NE2   . GLN B 1 1117 ? 16.953  65.635  68.648  1.00 14.11 ?  1115 GLN B NE2   1 
ATOM   17524 N N     . LEU B 1 1118 ? 12.493  67.929  73.245  1.00 12.48 ?  1116 LEU B N     1 
ATOM   17525 C CA    . LEU B 1 1118 ? 12.094  68.240  74.613  1.00 12.88 ?  1116 LEU B CA    1 
ATOM   17526 C C     . LEU B 1 1118 ? 10.665  67.803  74.887  1.00 13.79 ?  1116 LEU B C     1 
ATOM   17527 O O     . LEU B 1 1118 ? 10.384  67.232  75.945  1.00 15.94 ?  1116 LEU B O     1 
ATOM   17528 C CB    . LEU B 1 1118 ? 12.233  69.737  74.872  1.00 14.71 ?  1116 LEU B CB    1 
ATOM   17529 C CG    . LEU B 1 1118 ? 13.622  70.227  75.231  1.00 21.07 ?  1116 LEU B CG    1 
ATOM   17530 C CD1   . LEU B 1 1118 ? 13.638  71.744  75.226  1.00 21.71 ?  1116 LEU B CD1   1 
ATOM   17531 C CD2   . LEU B 1 1118 ? 13.976  69.691  76.595  1.00 22.09 ?  1116 LEU B CD2   1 
ATOM   17532 N N     . ALA B 1 1119 ? 9.753   68.055  73.943  1.00 14.21 ?  1117 ALA B N     1 
ATOM   17533 C CA    . ALA B 1 1119 ? 8.366   67.637  74.138  1.00 14.71 ?  1117 ALA B CA    1 
ATOM   17534 C C     . ALA B 1 1119 ? 8.272   66.132  74.343  1.00 13.72 ?  1117 ALA B C     1 
ATOM   17535 O O     . ALA B 1 1119 ? 7.597   65.665  75.274  1.00 15.22 ?  1117 ALA B O     1 
ATOM   17536 C CB    . ALA B 1 1119 ? 7.506   68.077  72.953  1.00 15.85 ?  1117 ALA B CB    1 
ATOM   17537 N N     . ALA B 1 1120 ? 8.956   65.355  73.495  1.00 14.10 ?  1118 ALA B N     1 
ATOM   17538 C CA    . ALA B 1 1120 ? 8.908   63.898  73.611  1.00 12.14 ?  1118 ALA B CA    1 
ATOM   17539 C C     . ALA B 1 1120 ? 9.434   63.437  74.963  1.00 13.65 ?  1118 ALA B C     1 
ATOM   17540 O O     . ALA B 1 1120 ? 8.833   62.576  75.617  1.00 13.54 ?  1118 ALA B O     1 
ATOM   17541 C CB    . ALA B 1 1120 ? 9.727   63.247  72.495  1.00 14.12 ?  1118 ALA B CB    1 
ATOM   17542 N N     . ALA B 1 1121 ? 10.574  63.990  75.390  1.00 12.37 ?  1119 ALA B N     1 
ATOM   17543 C CA    . ALA B 1 1121 ? 11.200  63.547  76.629  1.00 11.93 ?  1119 ALA B CA    1 
ATOM   17544 C C     . ALA B 1 1121 ? 10.395  63.984  77.846  1.00 11.40 ?  1119 ALA B C     1 
ATOM   17545 O O     . ALA B 1 1121 ? 10.251  63.210  78.802  1.00 12.11 ?  1119 ALA B O     1 
ATOM   17546 C CB    . ALA B 1 1121 ? 12.634  64.078  76.707  1.00 14.81 ?  1119 ALA B CB    1 
ATOM   17547 N N     . LEU B 1 1122 ? 9.879   65.219  77.836  1.00 12.41 ?  1120 LEU B N     1 
ATOM   17548 C CA    . LEU B 1 1122 ? 9.118   65.703  78.983  1.00 11.89 ?  1120 LEU B CA    1 
ATOM   17549 C C     . LEU B 1 1122 ? 7.793   64.978  79.097  1.00 12.21 ?  1120 LEU B C     1 
ATOM   17550 O O     . LEU B 1 1122 ? 7.338   64.682  80.207  1.00 13.21 ?  1120 LEU B O     1 
ATOM   17551 C CB    . LEU B 1 1122 ? 8.867   67.204  78.887  1.00 12.50 ?  1120 LEU B CB    1 
ATOM   17552 C CG    . LEU B 1 1122 ? 10.127  68.058  78.904  1.00 12.30 ?  1120 LEU B CG    1 
ATOM   17553 C CD1   . LEU B 1 1122 ? 9.735   69.498  78.625  1.00 16.49 ?  1120 LEU B CD1   1 
ATOM   17554 C CD2   . LEU B 1 1122 ? 10.832  67.935  80.252  1.00 16.32 ?  1120 LEU B CD2   1 
ATOM   17555 N N     . ALA B 1 1123 ? 7.159   64.686  77.958  1.00 12.30 ?  1121 ALA B N     1 
ATOM   17556 C CA    . ALA B 1 1123 ? 5.863   64.012  78.000  1.00 11.65 ?  1121 ALA B CA    1 
ATOM   17557 C C     . ALA B 1 1123 ? 5.954   62.624  78.607  1.00 12.32 ?  1121 ALA B C     1 
ATOM   17558 O O     . ALA B 1 1123 ? 4.939   62.110  79.101  1.00 12.52 ?  1121 ALA B O     1 
ATOM   17559 C CB    . ALA B 1 1123 ? 5.268   63.912  76.601  1.00 12.36 ?  1121 ALA B CB    1 
ATOM   17560 N N     . THR B 1 1124 ? 7.135   62.005  78.574  1.00 11.76 ?  1122 THR B N     1 
ATOM   17561 C CA    . THR B 1 1124 ? 7.369   60.688  79.138  1.00 11.13 ?  1122 THR B CA    1 
ATOM   17562 C C     . THR B 1 1124 ? 8.070   60.763  80.496  1.00 10.03 ?  1122 THR B C     1 
ATOM   17563 O O     . THR B 1 1124 ? 8.593   59.755  80.973  1.00 11.96 ?  1122 THR B O     1 
ATOM   17564 C CB    . THR B 1 1124 ? 8.149   59.835  78.126  1.00 12.72 ?  1122 THR B CB    1 
ATOM   17565 O OG1   . THR B 1 1124 ? 9.257   60.585  77.588  1.00 11.34 ?  1122 THR B OG1   1 
ATOM   17566 C CG2   . THR B 1 1124 ? 7.220   59.441  76.958  1.00 12.85 ?  1122 THR B CG2   1 
ATOM   17567 N N     . GLY B 1 1125 ? 8.075   61.940  81.123  1.00 10.61 ?  1123 GLY B N     1 
ATOM   17568 C CA    . GLY B 1 1125 ? 8.493   62.081  82.507  1.00 11.35 ?  1123 GLY B CA    1 
ATOM   17569 C C     . GLY B 1 1125 ? 9.981   62.265  82.718  1.00 11.80 ?  1123 GLY B C     1 
ATOM   17570 O O     . GLY B 1 1125 ? 10.432  62.306  83.869  1.00 13.41 ?  1123 GLY B O     1 
ATOM   17571 N N     . ASN B 1 1126 ? 10.746  62.415  81.651  1.00 12.14 ?  1124 ASN B N     1 
ATOM   17572 C CA    . ASN B 1 1126 ? 12.197  62.407  81.750  1.00 12.64 ?  1124 ASN B CA    1 
ATOM   17573 C C     . ASN B 1 1126 ? 12.773  63.800  81.956  1.00 12.67 ?  1124 ASN B C     1 
ATOM   17574 O O     . ASN B 1 1126 ? 12.150  64.820  81.648  1.00 13.97 ?  1124 ASN B O     1 
ATOM   17575 C CB    . ASN B 1 1126 ? 12.801  61.821  80.478  1.00 11.15 ?  1124 ASN B CB    1 
ATOM   17576 C CG    . ASN B 1 1126 ? 12.346  60.398  80.222  1.00 12.62 ?  1124 ASN B CG    1 
ATOM   17577 O OD1   . ASN B 1 1126 ? 12.700  59.481  80.957  1.00 14.38 ?  1124 ASN B OD1   1 
ATOM   17578 N ND2   . ASN B 1 1126 ? 11.566  60.208  79.183  1.00 11.61 ?  1124 ASN B ND2   1 
ATOM   17579 N N     . SER B 1 1127 ? 14.004  63.821  82.472  1.00 13.44 ?  1125 SER B N     1 
ATOM   17580 C CA    . SER B 1 1127 ? 14.851  64.996  82.376  1.00 11.59 ?  1125 SER B CA    1 
ATOM   17581 C C     . SER B 1 1127 ? 15.696  64.869  81.118  1.00 13.72 ?  1125 SER B C     1 
ATOM   17582 O O     . SER B 1 1127 ? 15.673  63.845  80.441  1.00 12.26 ?  1125 SER B O     1 
ATOM   17583 C CB    . SER B 1 1127 ? 15.750  65.129  83.609  1.00 15.05 ?  1125 SER B CB    1 
ATOM   17584 O OG    . SER B 1 1127 ? 16.525  63.947  83.787  1.00 19.79 ?  1125 SER B OG    1 
ATOM   17585 N N     . VAL B 1 1128 ? 16.431  65.926  80.794  1.00 14.77 ?  1126 VAL B N     1 
ATOM   17586 C CA    . VAL B 1 1128 ? 17.238  65.910  79.581  1.00 12.41 ?  1126 VAL B CA    1 
ATOM   17587 C C     . VAL B 1 1128 ? 18.621  66.475  79.862  1.00 13.05 ?  1126 VAL B C     1 
ATOM   17588 O O     . VAL B 1 1128 ? 18.809  67.312  80.751  1.00 16.16 ?  1126 VAL B O     1 
ATOM   17589 C CB    . VAL B 1 1128 ? 16.586  66.692  78.414  1.00 13.93 ?  1126 VAL B CB    1 
ATOM   17590 C CG1   . VAL B 1 1128 ? 15.267  66.056  78.015  1.00 14.50 ?  1126 VAL B CG1   1 
ATOM   17591 C CG2   . VAL B 1 1128 ? 16.412  68.178  78.762  1.00 13.59 ?  1126 VAL B CG2   1 
ATOM   17592 N N     . ALA B 1 1129 ? 19.589  66.013  79.070  1.00 12.53 ?  1127 ALA B N     1 
ATOM   17593 C CA    . ALA B 1 1129 ? 20.882  66.668  78.919  1.00 14.73 ?  1127 ALA B CA    1 
ATOM   17594 C C     . ALA B 1 1129 ? 21.020  67.033  77.450  1.00 14.37 ?  1127 ALA B C     1 
ATOM   17595 O O     . ALA B 1 1129 ? 20.976  66.144  76.589  1.00 14.75 ?  1127 ALA B O     1 
ATOM   17596 C CB    . ALA B 1 1129 ? 22.011  65.742  79.358  1.00 16.06 ?  1127 ALA B CB    1 
ATOM   17597 N N     . ILE B 1 1130 ? 21.122  68.333  77.161  1.00 13.42 ?  1128 ILE B N     1 
ATOM   17598 C CA    . ILE B 1 1130 ? 21.157  68.833  75.794  1.00 13.98 ?  1128 ILE B CA    1 
ATOM   17599 C C     . ILE B 1 1130 ? 22.604  69.063  75.392  1.00 14.08 ?  1128 ILE B C     1 
ATOM   17600 O O     . ILE B 1 1130 ? 23.375  69.705  76.126  1.00 14.68 ?  1128 ILE B O     1 
ATOM   17601 C CB    . ILE B 1 1130 ? 20.353  70.133  75.630  1.00 13.93 ?  1128 ILE B CB    1 
ATOM   17602 C CG1   . ILE B 1 1130 ? 18.956  69.986  76.233  1.00 17.64 ?  1128 ILE B CG1   1 
ATOM   17603 C CG2   . ILE B 1 1130 ? 20.234  70.498  74.155  1.00 16.81 ?  1128 ILE B CG2   1 
ATOM   17604 C CD1   . ILE B 1 1130 ? 18.243  71.313  76.315  1.00 17.02 ?  1128 ILE B CD1   1 
ATOM   17605 N N     . ASP B 1 1131 ? 22.965  68.545  74.221  1.00 14.41 ?  1129 ASP B N     1 
ATOM   17606 C CA    . ASP B 1 1131 ? 24.301  68.744  73.665  1.00 14.88 ?  1129 ASP B CA    1 
ATOM   17607 C C     . ASP B 1 1131 ? 24.628  70.225  73.520  1.00 16.50 ?  1129 ASP B C     1 
ATOM   17608 O O     . ASP B 1 1131 ? 24.009  70.919  72.708  1.00 16.27 ?  1129 ASP B O     1 
ATOM   17609 C CB    . ASP B 1 1131 ? 24.395  68.052  72.313  1.00 14.43 ?  1129 ASP B CB    1 
ATOM   17610 C CG    . ASP B 1 1131 ? 25.766  68.177  71.690  1.00 15.12 ?  1129 ASP B CG    1 
ATOM   17611 O OD1   . ASP B 1 1131 ? 26.752  68.259  72.449  1.00 18.25 ?  1129 ASP B OD1   1 
ATOM   17612 O OD2   . ASP B 1 1131 ? 25.827  68.196  70.442  1.00 18.44 ?  1129 ASP B OD2   1 
ATOM   17613 N N     . ALA B 1 1132 ? 25.608  70.712  74.288  1.00 17.46 ?  1130 ALA B N     1 
ATOM   17614 C CA    . ALA B 1 1132 ? 25.973  72.126  74.234  1.00 16.91 ?  1130 ALA B CA    1 
ATOM   17615 C C     . ALA B 1 1132 ? 26.585  72.506  72.894  1.00 17.96 ?  1130 ALA B C     1 
ATOM   17616 O O     . ALA B 1 1132 ? 26.495  73.669  72.483  1.00 19.82 ?  1130 ALA B O     1 
ATOM   17617 C CB    . ALA B 1 1132 ? 26.931  72.465  75.375  1.00 17.55 ?  1130 ALA B CB    1 
ATOM   17618 N N     . ALA B 1 1133 ? 27.190  71.548  72.189  1.00 19.39 ?  1131 ALA B N     1 
ATOM   17619 C CA    . ALA B 1 1133 ? 27.785  71.848  70.892  1.00 20.48 ?  1131 ALA B CA    1 
ATOM   17620 C C     . ALA B 1 1133 ? 26.741  72.215  69.847  1.00 20.50 ?  1131 ALA B C     1 
ATOM   17621 O O     . ALA B 1 1133 ? 27.105  72.724  68.781  1.00 25.31 ?  1131 ALA B O     1 
ATOM   17622 C CB    . ALA B 1 1133 ? 28.618  70.659  70.410  1.00 24.82 ?  1131 ALA B CB    1 
ATOM   17623 N N     . SER B 1 1134 ? 25.456  71.988  70.131  1.00 18.09 ?  1132 SER B N     1 
ATOM   17624 C CA    . SER B 1 1134 ? 24.416  72.408  69.199  1.00 20.11 ?  1132 SER B CA    1 
ATOM   17625 C C     . SER B 1 1134 ? 24.341  73.925  69.080  1.00 20.10 ?  1132 SER B C     1 
ATOM   17626 O O     . SER B 1 1134 ? 23.830  74.432  68.077  1.00 22.04 ?  1132 SER B O     1 
ATOM   17627 C CB    . SER B 1 1134 ? 23.058  71.865  69.644  1.00 18.18 ?  1132 SER B CB    1 
ATOM   17628 O OG    . SER B 1 1134 ? 22.655  72.491  70.855  1.00 19.81 ?  1132 SER B OG    1 
ATOM   17629 N N     . GLY B 1 1135 ? 24.828  74.655  70.077  1.00 18.43 ?  1133 GLY B N     1 
ATOM   17630 C CA    . GLY B 1 1135 ? 24.765  76.104  70.043  1.00 20.99 ?  1133 GLY B CA    1 
ATOM   17631 C C     . GLY B 1 1135 ? 23.373  76.685  70.178  1.00 23.24 ?  1133 GLY B C     1 
ATOM   17632 O O     . GLY B 1 1135 ? 23.158  77.843  69.810  1.00 25.71 ?  1133 GLY B O     1 
ATOM   17633 N N     . LEU B 1 1136 ? 22.416  75.920  70.706  1.00 20.75 ?  1134 LEU B N     1 
ATOM   17634 C CA    . LEU B 1 1136 ? 21.019  76.339  70.742  1.00 23.83 ?  1134 LEU B CA    1 
ATOM   17635 C C     . LEU B 1 1136 ? 20.600  76.905  72.097  1.00 23.88 ?  1134 LEU B C     1 
ATOM   17636 O O     . LEU B 1 1136 ? 19.399  76.999  72.372  1.00 23.70 ?  1134 LEU B O     1 
ATOM   17637 C CB    . LEU B 1 1136 ? 20.112  75.168  70.353  1.00 20.33 ?  1134 LEU B CB    1 
ATOM   17638 C CG    . LEU B 1 1136 ? 20.234  74.663  68.918  1.00 21.46 ?  1134 LEU B CG    1 
ATOM   17639 C CD1   . LEU B 1 1136 ? 19.401  73.413  68.741  1.00 22.41 ?  1134 LEU B CD1   1 
ATOM   17640 C CD2   . LEU B 1 1136 ? 19.804  75.745  67.922  1.00 22.90 ?  1134 LEU B CD2   1 
ATOM   17641 N N     . GLN B 1 1137 ? 21.559  77.304  72.935  1.00 20.19 ?  1135 GLN B N     1 
ATOM   17642 C CA    . GLN B 1 1137 ? 21.245  77.730  74.299  1.00 24.26 ?  1135 GLN B CA    1 
ATOM   17643 C C     . GLN B 1 1137 ? 20.260  78.900  74.326  1.00 26.77 ?  1135 GLN B C     1 
ATOM   17644 O O     . GLN B 1 1137 ? 19.389  78.964  75.204  1.00 26.24 ?  1135 GLN B O     1 
ATOM   17645 C CB    . GLN B 1 1137 ? 22.527  78.094  75.046  1.00 24.60 ?  1135 GLN B CB    1 
ATOM   17646 C CG    . GLN B 1 1137 ? 23.375  76.889  75.436  1.00 24.76 ?  1135 GLN B CG    1 
ATOM   17647 C CD    . GLN B 1 1137 ? 24.345  76.460  74.350  1.00 24.23 ?  1135 GLN B CD    1 
ATOM   17648 O OE1   . GLN B 1 1137 ? 24.217  76.847  73.190  1.00 23.42 ?  1135 GLN B OE1   1 
ATOM   17649 N NE2   . GLN B 1 1137 ? 25.325  75.648  74.726  1.00 25.86 ?  1135 GLN B NE2   1 
ATOM   17650 N N     . ALA B 1 1138 ? 20.367  79.820  73.363  1.00 24.36 ?  1136 ALA B N     1 
ATOM   17651 C CA    . ALA B 1 1138 ? 19.468  80.971  73.328  1.00 27.09 ?  1136 ALA B CA    1 
ATOM   17652 C C     . ALA B 1 1138 ? 18.020  80.574  73.057  1.00 27.75 ?  1136 ALA B C     1 
ATOM   17653 O O     . ALA B 1 1138 ? 17.113  81.384  73.280  1.00 28.34 ?  1136 ALA B O     1 
ATOM   17654 C CB    . ALA B 1 1138 ? 19.938  81.970  72.272  1.00 28.01 ?  1136 ALA B CB    1 
ATOM   17655 N N     . SER B 1 1139 ? 17.780  79.350  72.589  1.00 23.32 ?  1137 SER B N     1 
ATOM   17656 C CA    . SER B 1 1139 ? 16.423  78.920  72.274  1.00 25.98 ?  1137 SER B CA    1 
ATOM   17657 C C     . SER B 1 1139 ? 15.604  78.617  73.520  1.00 24.84 ?  1137 SER B C     1 
ATOM   17658 O O     . SER B 1 1139 ? 14.378  78.505  73.423  1.00 28.11 ?  1137 SER B O     1 
ATOM   17659 C CB    . SER B 1 1139 ? 16.454  77.685  71.366  1.00 24.92 ?  1137 SER B CB    1 
ATOM   17660 O OG    . SER B 1 1139 ? 16.944  78.010  70.078  1.00 26.89 ?  1137 SER B OG    1 
ATOM   17661 N N     . LEU B 1 1140 ? 16.245  78.472  74.676  1.00 27.16 ?  1138 LEU B N     1 
ATOM   17662 C CA    . LEU B 1 1140 ? 15.558  78.185  75.931  1.00 25.88 ?  1138 LEU B CA    1 
ATOM   17663 C C     . LEU B 1 1140 ? 15.610  79.381  76.878  1.00 31.14 ?  1138 LEU B C     1 
ATOM   17664 O O     . LEU B 1 1140 ? 15.752  79.228  78.093  1.00 34.75 ?  1138 LEU B O     1 
ATOM   17665 C CB    . LEU B 1 1140 ? 16.138  76.943  76.605  1.00 27.88 ?  1138 LEU B CB    1 
ATOM   17666 C CG    . LEU B 1 1140 ? 15.995  75.629  75.834  1.00 26.79 ?  1138 LEU B CG    1 
ATOM   17667 C CD1   . LEU B 1 1140 ? 16.418  74.440  76.696  1.00 26.12 ?  1138 LEU B CD1   1 
ATOM   17668 C CD2   . LEU B 1 1140 ? 14.582  75.431  75.307  1.00 26.37 ?  1138 LEU B CD2   1 
ATOM   17669 N N     . LYS B 1 1141 ? 15.496  80.586  76.327  1.00 33.45 ?  1139 LYS B N     1 
ATOM   17670 C CA    . LYS B 1 1141 ? 15.477  81.784  77.153  1.00 34.10 ?  1139 LYS B CA    1 
ATOM   17671 C C     . LYS B 1 1141 ? 14.150  81.884  77.895  1.00 38.27 ?  1139 LYS B C     1 
ATOM   17672 O O     . LYS B 1 1141 ? 13.080  81.690  77.307  1.00 36.83 ?  1139 LYS B O     1 
ATOM   17673 C CB    . LYS B 1 1141 ? 15.705  83.028  76.293  1.00 37.14 ?  1139 LYS B CB    1 
ATOM   17674 N N     . ASN B 1 1142 ? 14.229  82.162  79.197  1.00 36.02 ?  1140 ASN B N     1 
ATOM   17675 C CA    . ASN B 1 1142 ? 13.058  82.419  80.036  1.00 38.68 ?  1140 ASN B CA    1 
ATOM   17676 C C     . ASN B 1 1142 ? 12.169  81.181  80.161  1.00 36.67 ?  1140 ASN B C     1 
ATOM   17677 O O     . ASN B 1 1142 ? 10.942  81.288  80.194  1.00 34.05 ?  1140 ASN B O     1 
ATOM   17678 C CB    . ASN B 1 1142 ? 12.254  83.615  79.517  1.00 41.73 ?  1140 ASN B CB    1 
ATOM   17679 C CG    . ASN B 1 1142 ? 13.107  84.862  79.350  1.00 48.73 ?  1140 ASN B CG    1 
ATOM   17680 O OD1   . ASN B 1 1142 ? 13.181  85.436  78.264  1.00 48.64 ?  1140 ASN B OD1   1 
ATOM   17681 N ND2   . ASN B 1 1142 ? 13.764  85.279  80.425  1.00 46.30 ?  1140 ASN B ND2   1 
ATOM   17682 N N     . LEU B 1 1143 ? 12.790  80.003  80.222  1.00 33.93 ?  1141 LEU B N     1 
ATOM   17683 C CA    . LEU B 1 1143 ? 12.043  78.785  80.492  1.00 30.07 ?  1141 LEU B CA    1 
ATOM   17684 C C     . LEU B 1 1143 ? 11.341  78.898  81.842  1.00 28.79 ?  1141 LEU B C     1 
ATOM   17685 O O     . LEU B 1 1143 ? 11.869  79.515  82.769  1.00 35.78 ?  1141 LEU B O     1 
ATOM   17686 C CB    . LEU B 1 1143 ? 12.972  77.574  80.523  1.00 30.70 ?  1141 LEU B CB    1 
ATOM   17687 C CG    . LEU B 1 1143 ? 13.043  76.569  79.379  1.00 32.81 ?  1141 LEU B CG    1 
ATOM   17688 C CD1   . LEU B 1 1143 ? 13.789  75.339  79.873  1.00 26.07 ?  1141 LEU B CD1   1 
ATOM   17689 C CD2   . LEU B 1 1143 ? 11.678  76.190  78.847  1.00 27.89 ?  1141 LEU B CD2   1 
ATOM   17690 N N     . PRO B 1 1144 ? 10.161  78.299  81.993  1.00 30.69 ?  1142 PRO B N     1 
ATOM   17691 C CA    . PRO B 1 1144 ? 9.596   78.159  83.338  1.00 28.20 ?  1142 PRO B CA    1 
ATOM   17692 C C     . PRO B 1 1144 ? 10.545  77.371  84.228  1.00 29.58 ?  1142 PRO B C     1 
ATOM   17693 O O     . PRO B 1 1144 ? 11.214  76.436  83.779  1.00 24.65 ?  1142 PRO B O     1 
ATOM   17694 C CB    . PRO B 1 1144 ? 8.283   77.401  83.105  1.00 28.83 ?  1142 PRO B CB    1 
ATOM   17695 C CG    . PRO B 1 1144 ? 7.969   77.589  81.662  1.00 30.47 ?  1142 PRO B CG    1 
ATOM   17696 C CD    . PRO B 1 1144 ? 9.285   77.727  80.956  1.00 30.21 ?  1142 PRO B CD    1 
ATOM   17697 N N     . GLN B 1 1145 ? 10.609  77.771  85.500  1.00 28.90 ?  1143 GLN B N     1 
ATOM   17698 C CA    . GLN B 1 1145 ? 11.470  77.082  86.453  1.00 26.62 ?  1143 GLN B CA    1 
ATOM   17699 C C     . GLN B 1 1145 ? 11.161  75.591  86.498  1.00 25.85 ?  1143 GLN B C     1 
ATOM   17700 O O     . GLN B 1 1145 ? 12.069  74.766  86.639  1.00 25.29 ?  1143 GLN B O     1 
ATOM   17701 C CB    . GLN B 1 1145 ? 11.319  77.700  87.843  1.00 27.25 ?  1143 GLN B CB    1 
ATOM   17702 N N     . THR B 1 1146 ? 9.883   75.222  86.372  1.00 27.47 ?  1144 THR B N     1 
ATOM   17703 C CA    . THR B 1 1146 ? 9.534   73.804  86.393  1.00 25.88 ?  1144 THR B CA    1 
ATOM   17704 C C     . THR B 1 1146 ? 10.223  73.053  85.263  1.00 25.54 ?  1144 THR B C     1 
ATOM   17705 O O     . THR B 1 1146 ? 10.708  71.928  85.454  1.00 26.43 ?  1144 THR B O     1 
ATOM   17706 C CB    . THR B 1 1146 ? 8.020   73.618  86.292  1.00 26.52 ?  1144 THR B CB    1 
ATOM   17707 O OG1   . THR B 1 1146 ? 7.534   74.312  85.142  1.00 29.43 ?  1144 THR B OG1   1 
ATOM   17708 C CG2   . THR B 1 1146 ? 7.330   74.145  87.535  1.00 31.74 ?  1144 THR B CG2   1 
ATOM   17709 N N     . VAL B 1 1147 ? 10.281  73.658  84.078  1.00 21.36 ?  1145 VAL B N     1 
ATOM   17710 C CA    . VAL B 1 1147 ? 10.958  73.000  82.966  1.00 16.41 ?  1145 VAL B CA    1 
ATOM   17711 C C     . VAL B 1 1147 ? 12.468  73.100  83.131  1.00 20.80 ?  1145 VAL B C     1 
ATOM   17712 O O     . VAL B 1 1147 ? 13.200  72.144  82.847  1.00 18.97 ?  1145 VAL B O     1 
ATOM   17713 C CB    . VAL B 1 1147 ? 10.494  73.588  81.621  1.00 18.17 ?  1145 VAL B CB    1 
ATOM   17714 C CG1   . VAL B 1 1147 ? 11.066  72.754  80.471  1.00 20.84 ?  1145 VAL B CG1   1 
ATOM   17715 C CG2   . VAL B 1 1147 ? 8.966   73.648  81.553  1.00 21.64 ?  1145 VAL B CG2   1 
ATOM   17716 N N     . GLY B 1 1148 ? 12.954  74.246  83.609  1.00 22.15 ?  1146 GLY B N     1 
ATOM   17717 C CA    . GLY B 1 1148 ? 14.391  74.418  83.771  1.00 22.22 ?  1146 GLY B CA    1 
ATOM   17718 C C     . GLY B 1 1148 ? 15.010  73.387  84.695  1.00 23.49 ?  1146 GLY B C     1 
ATOM   17719 O O     . GLY B 1 1148 ? 16.131  72.929  84.464  1.00 22.34 ?  1146 GLY B O     1 
ATOM   17720 N N     . LEU B 1 1149 ? 14.287  72.997  85.750  1.00 21.75 ?  1147 LEU B N     1 
ATOM   17721 C CA    . LEU B 1 1149 ? 14.812  72.012  86.685  1.00 22.20 ?  1147 LEU B CA    1 
ATOM   17722 C C     . LEU B 1 1149 ? 15.071  70.665  86.030  1.00 21.82 ?  1147 LEU B C     1 
ATOM   17723 O O     . LEU B 1 1149 ? 15.837  69.864  86.579  1.00 24.37 ?  1147 LEU B O     1 
ATOM   17724 C CB    . LEU B 1 1149 ? 13.852  71.831  87.860  1.00 29.35 ?  1147 LEU B CB    1 
ATOM   17725 C CG    . LEU B 1 1149 ? 13.639  73.096  88.692  1.00 33.62 ?  1147 LEU B CG    1 
ATOM   17726 C CD1   . LEU B 1 1149 ? 12.779  72.798  89.914  1.00 36.63 ?  1147 LEU B CD1   1 
ATOM   17727 C CD2   . LEU B 1 1149 ? 14.969  73.729  89.086  1.00 37.55 ?  1147 LEU B CD2   1 
ATOM   17728 N N     . ARG B 1 1150 ? 14.432  70.385  84.892  1.00 18.41 ?  1148 ARG B N     1 
ATOM   17729 C CA    . ARG B 1 1150 ? 14.621  69.125  84.184  1.00 17.63 ?  1148 ARG B CA    1 
ATOM   17730 C C     . ARG B 1 1150 ? 15.641  69.218  83.067  1.00 18.35 ?  1148 ARG B C     1 
ATOM   17731 O O     . ARG B 1 1150 ? 15.893  68.209  82.398  1.00 17.11 ?  1148 ARG B O     1 
ATOM   17732 C CB    . ARG B 1 1150 ? 13.300  68.636  83.591  1.00 17.53 ?  1148 ARG B CB    1 
ATOM   17733 C CG    . ARG B 1 1150 ? 12.355  68.036  84.609  1.00 20.85 ?  1148 ARG B CG    1 
ATOM   17734 C CD    . ARG B 1 1150 ? 11.594  66.929  83.954  1.00 17.58 ?  1148 ARG B CD    1 
ATOM   17735 N NE    . ARG B 1 1150 ? 10.420  66.542  84.722  1.00 19.84 ?  1148 ARG B NE    1 
ATOM   17736 C CZ    . ARG B 1 1150 ? 9.373   65.942  84.181  1.00 19.57 ?  1148 ARG B CZ    1 
ATOM   17737 N NH1   . ARG B 1 1150 ? 9.360   65.615  82.900  1.00 17.53 ?  1148 ARG B NH1   1 
ATOM   17738 N NH2   . ARG B 1 1150 ? 8.309   65.685  84.938  1.00 15.63 ?  1148 ARG B NH2   1 
ATOM   17739 N N     . VAL B 1 1151 ? 16.212  70.394  82.835  1.00 17.52 ?  1149 VAL B N     1 
ATOM   17740 C CA    . VAL B 1 1151 ? 17.088  70.643  81.695  1.00 16.56 ?  1149 VAL B CA    1 
ATOM   17741 C C     . VAL B 1 1151 ? 18.504  70.868  82.196  1.00 18.83 ?  1149 VAL B C     1 
ATOM   17742 O O     . VAL B 1 1151 ? 18.729  71.674  83.105  1.00 21.27 ?  1149 VAL B O     1 
ATOM   17743 C CB    . VAL B 1 1151 ? 16.621  71.858  80.876  1.00 19.29 ?  1149 VAL B CB    1 
ATOM   17744 C CG1   . VAL B 1 1151 ? 17.664  72.206  79.817  1.00 20.76 ?  1149 VAL B CG1   1 
ATOM   17745 C CG2   . VAL B 1 1151 ? 15.277  71.589  80.228  1.00 21.43 ?  1149 VAL B CG2   1 
ATOM   17746 N N     . SER B 1 1152 ? 19.458  70.169  81.593  1.00 16.27 ?  1150 SER B N     1 
ATOM   17747 C CA    . SER B 1 1152 ? 20.860  70.501  81.750  1.00 16.22 ?  1150 SER B CA    1 
ATOM   17748 C C     . SER B 1 1152 ? 21.483  70.535  80.367  1.00 16.70 ?  1150 SER B C     1 
ATOM   17749 O O     . SER B 1 1152 ? 20.939  69.979  79.411  1.00 18.39 ?  1150 SER B O     1 
ATOM   17750 C CB    . SER B 1 1152 ? 21.589  69.495  82.653  1.00 19.80 ?  1150 SER B CB    1 
ATOM   17751 O OG    . SER B 1 1152 ? 21.615  68.221  82.051  1.00 25.89 ?  1150 SER B OG    1 
ATOM   17752 N N     . TRP B 1 1153 ? 22.609  71.225  80.265  1.00 18.60 ?  1151 TRP B N     1 
ATOM   17753 C CA    . TRP B 1 1153 ? 23.389  71.290  79.041  1.00 18.63 ?  1151 TRP B CA    1 
ATOM   17754 C C     . TRP B 1 1153 ? 24.696  70.552  79.276  1.00 19.81 ?  1151 TRP B C     1 
ATOM   17755 O O     . TRP B 1 1153 ? 25.324  70.719  80.326  1.00 22.45 ?  1151 TRP B O     1 
ATOM   17756 C CB    . TRP B 1 1153 ? 23.651  72.744  78.638  1.00 18.85 ?  1151 TRP B CB    1 
ATOM   17757 C CG    . TRP B 1 1153 ? 22.402  73.454  78.199  1.00 19.70 ?  1151 TRP B CG    1 
ATOM   17758 C CD1   . TRP B 1 1153 ? 21.477  74.077  79.001  1.00 22.41 ?  1151 TRP B CD1   1 
ATOM   17759 C CD2   . TRP B 1 1153 ? 21.947  73.624  76.855  1.00 19.35 ?  1151 TRP B CD2   1 
ATOM   17760 N NE1   . TRP B 1 1153 ? 20.474  74.609  78.230  1.00 20.51 ?  1151 TRP B NE1   1 
ATOM   17761 C CE2   . TRP B 1 1153 ? 20.734  74.341  76.911  1.00 22.74 ?  1151 TRP B CE2   1 
ATOM   17762 C CE3   . TRP B 1 1153 ? 22.435  73.218  75.608  1.00 17.59 ?  1151 TRP B CE3   1 
ATOM   17763 C CZ2   . TRP B 1 1153 ? 20.018  74.682  75.764  1.00 21.51 ?  1151 TRP B CZ2   1 
ATOM   17764 C CZ3   . TRP B 1 1153 ? 21.722  73.552  74.471  1.00 20.82 ?  1151 TRP B CZ3   1 
ATOM   17765 C CH2   . TRP B 1 1153 ? 20.516  74.268  74.559  1.00 22.13 ?  1151 TRP B CH2   1 
ATOM   17766 N N     . SER B 1 1154 ? 25.091  69.716  78.321  1.00 15.59 ?  1152 SER B N     1 
ATOM   17767 C CA    . SER B 1 1154 ? 26.281  68.886  78.498  1.00 16.29 ?  1152 SER B CA    1 
ATOM   17768 C C     . SER B 1 1154 ? 27.351  69.232  77.473  1.00 17.12 ?  1152 SER B C     1 
ATOM   17769 O O     . SER B 1 1154 ? 27.098  69.177  76.263  1.00 16.33 ?  1152 SER B O     1 
ATOM   17770 C CB    . SER B 1 1154 ? 25.945  67.403  78.401  1.00 17.31 ?  1152 SER B CB    1 
ATOM   17771 O OG    . SER B 1 1154 ? 27.145  66.650  78.536  1.00 17.56 ?  1152 SER B OG    1 
ATOM   17772 N N     . LYS B 1 1155 ? 28.545  69.556  77.967  1.00 17.16 ?  1153 LYS B N     1 
ATOM   17773 C CA    . LYS B 1 1155 ? 29.754  69.707  77.163  1.00 16.73 ?  1153 LYS B CA    1 
ATOM   17774 C C     . LYS B 1 1155 ? 30.612  68.449  77.185  1.00 18.94 ?  1153 LYS B C     1 
ATOM   17775 O O     . LYS B 1 1155 ? 31.737  68.464  76.671  1.00 19.89 ?  1153 LYS B O     1 
ATOM   17776 C CB    . LYS B 1 1155 ? 30.585  70.898  77.659  1.00 20.94 ?  1153 LYS B CB    1 
ATOM   17777 C CG    . LYS B 1 1155 ? 29.893  72.245  77.539  1.00 24.67 ?  1153 LYS B CG    1 
ATOM   17778 C CD    . LYS B 1 1155 ? 30.764  73.365  78.114  1.00 29.18 ?  1153 LYS B CD    1 
ATOM   17779 C CE    . LYS B 1 1155 ? 30.056  74.716  78.060  1.00 38.22 ?  1153 LYS B CE    1 
ATOM   17780 N NZ    . LYS B 1 1155 ? 30.727  75.757  78.898  1.00 39.46 ?  1153 LYS B NZ    1 
ATOM   17781 N N     . ASP B 1 1156 ? 30.125  67.375  77.801  1.00 16.45 ?  1154 ASP B N     1 
ATOM   17782 C CA    . ASP B 1 1156 ? 30.944  66.184  78.039  1.00 16.50 ?  1154 ASP B CA    1 
ATOM   17783 C C     . ASP B 1 1156 ? 29.968  65.031  78.301  1.00 14.88 ?  1154 ASP B C     1 
ATOM   17784 O O     . ASP B 1 1156 ? 29.575  64.787  79.444  1.00 15.42 ?  1154 ASP B O     1 
ATOM   17785 C CB    . ASP B 1 1156 ? 31.888  66.399  79.206  1.00 17.87 ?  1154 ASP B CB    1 
ATOM   17786 C CG    . ASP B 1 1156 ? 32.913  65.293  79.342  1.00 15.92 ?  1154 ASP B CG    1 
ATOM   17787 O OD1   . ASP B 1 1156 ? 32.607  64.139  78.963  1.00 16.56 ?  1154 ASP B OD1   1 
ATOM   17788 O OD2   . ASP B 1 1156 ? 34.010  65.593  79.832  1.00 18.89 ?  1154 ASP B OD2   1 
ATOM   17789 N N     . TRP B 1 1157 ? 29.578  64.343  77.230  1.00 14.49 ?  1155 TRP B N     1 
ATOM   17790 C CA    . TRP B 1 1157 ? 28.499  63.367  77.371  1.00 13.88 ?  1155 TRP B CA    1 
ATOM   17791 C C     . TRP B 1 1157 ? 28.907  62.230  78.294  1.00 15.87 ?  1155 TRP B C     1 
ATOM   17792 O O     . TRP B 1 1157 ? 28.105  61.758  79.111  1.00 15.86 ?  1155 TRP B O     1 
ATOM   17793 C CB    . TRP B 1 1157 ? 28.083  62.792  76.020  1.00 14.50 ?  1155 TRP B CB    1 
ATOM   17794 C CG    . TRP B 1 1157 ? 27.599  63.767  75.012  1.00 14.15 ?  1155 TRP B CG    1 
ATOM   17795 C CD1   . TRP B 1 1157 ? 27.352  65.100  75.186  1.00 16.15 ?  1155 TRP B CD1   1 
ATOM   17796 C CD2   . TRP B 1 1157 ? 27.318  63.479  73.647  1.00 15.05 ?  1155 TRP B CD2   1 
ATOM   17797 N NE1   . TRP B 1 1157 ? 26.931  65.657  73.998  1.00 14.95 ?  1155 TRP B NE1   1 
ATOM   17798 C CE2   . TRP B 1 1157 ? 26.910  64.683  73.037  1.00 14.96 ?  1155 TRP B CE2   1 
ATOM   17799 C CE3   . TRP B 1 1157 ? 27.381  62.314  72.871  1.00 16.56 ?  1155 TRP B CE3   1 
ATOM   17800 C CZ2   . TRP B 1 1157 ? 26.553  64.754  71.692  1.00 15.91 ?  1155 TRP B CZ2   1 
ATOM   17801 C CZ3   . TRP B 1 1157 ? 27.030  62.384  71.551  1.00 15.49 ?  1155 TRP B CZ3   1 
ATOM   17802 C CH2   . TRP B 1 1157 ? 26.613  63.593  70.965  1.00 18.70 ?  1155 TRP B CH2   1 
ATOM   17803 N N     . ALA B 1 1158 ? 30.160  61.780  78.190  1.00 16.64 ?  1156 ALA B N     1 
ATOM   17804 C CA    . ALA B 1 1158 ? 30.559  60.617  78.969  1.00 16.42 ?  1156 ALA B CA    1 
ATOM   17805 C C     . ALA B 1 1158 ? 30.690  60.954  80.445  1.00 16.81 ?  1156 ALA B C     1 
ATOM   17806 O O     . ALA B 1 1158 ? 30.468  60.084  81.294  1.00 20.90 ?  1156 ALA B O     1 
ATOM   17807 C CB    . ALA B 1 1158 ? 31.871  60.045  78.436  1.00 14.11 ?  1156 ALA B CB    1 
ATOM   17808 N N     . ALA B 1 1159 ? 31.036  62.202  80.773  1.00 14.71 ?  1157 ALA B N     1 
ATOM   17809 C CA    . ALA B 1 1159 ? 31.146  62.600  82.171  1.00 16.54 ?  1157 ALA B CA    1 
ATOM   17810 C C     . ALA B 1 1159 ? 29.787  62.846  82.806  1.00 19.00 ?  1157 ALA B C     1 
ATOM   17811 O O     . ALA B 1 1159 ? 29.636  62.656  84.017  1.00 19.44 ?  1157 ALA B O     1 
ATOM   17812 C CB    . ALA B 1 1159 ? 32.001  63.858  82.302  1.00 18.25 ?  1157 ALA B CB    1 
ATOM   17813 N N     . ASP B 1 1160 ? 28.803  63.260  82.012  1.00 18.06 ?  1158 ASP B N     1 
ATOM   17814 C CA    . ASP B 1 1160 ? 27.505  63.688  82.511  1.00 18.16 ?  1158 ASP B CA    1 
ATOM   17815 C C     . ASP B 1 1160 ? 26.465  62.581  82.532  1.00 17.25 ?  1158 ASP B C     1 
ATOM   17816 O O     . ASP B 1 1160 ? 25.356  62.805  83.044  1.00 21.11 ?  1158 ASP B O     1 
ATOM   17817 C CB    . ASP B 1 1160 ? 26.997  64.863  81.665  1.00 17.65 ?  1158 ASP B CB    1 
ATOM   17818 C CG    . ASP B 1 1160 ? 27.831  66.110  81.858  1.00 19.69 ?  1158 ASP B CG    1 
ATOM   17819 O OD1   . ASP B 1 1160 ? 28.581  66.171  82.862  1.00 26.13 ?  1158 ASP B OD1   1 
ATOM   17820 O OD2   . ASP B 1 1160 ? 27.754  67.032  81.017  1.00 21.77 ?  1158 ASP B OD2   1 
ATOM   17821 N N     . GLY B 1 1161 ? 26.780  61.407  81.986  1.00 16.72 ?  1159 GLY B N     1 
ATOM   17822 C CA    . GLY B 1 1161 ? 25.905  60.262  82.055  1.00 16.26 ?  1159 GLY B CA    1 
ATOM   17823 C C     . GLY B 1 1161 ? 25.984  59.587  83.409  1.00 22.59 ?  1159 GLY B C     1 
ATOM   17824 O O     . GLY B 1 1161 ? 26.612  60.091  84.344  1.00 24.15 ?  1159 GLY B O     1 
ATOM   17825 N N     . PRO B 1 1162 ? 25.359  58.415  83.538  1.00 24.17 ?  1160 PRO B N     1 
ATOM   17826 C CA    . PRO B 1 1162 ? 24.676  57.652  82.491  1.00 20.14 ?  1160 PRO B CA    1 
ATOM   17827 C C     . PRO B 1 1162 ? 23.349  58.264  82.099  1.00 19.12 ?  1160 PRO B C     1 
ATOM   17828 O O     . PRO B 1 1162 ? 22.610  58.827  82.904  1.00 22.34 ?  1160 PRO B O     1 
ATOM   17829 C CB    . PRO B 1 1162 ? 24.476  56.276  83.143  1.00 25.37 ?  1160 PRO B CB    1 
ATOM   17830 C CG    . PRO B 1 1162 ? 24.274  56.604  84.590  1.00 25.94 ?  1160 PRO B CG    1 
ATOM   17831 C CD    . PRO B 1 1162 ? 25.220  57.766  84.856  1.00 27.36 ?  1160 PRO B CD    1 
ATOM   17832 N N     . PHE B 1 1163 ? 23.038  58.148  80.821  1.00 15.66 ?  1161 PHE B N     1 
ATOM   17833 C CA    . PHE B 1 1163 ? 21.746  58.549  80.302  1.00 16.00 ?  1161 PHE B CA    1 
ATOM   17834 C C     . PHE B 1 1163 ? 20.867  57.317  80.142  1.00 16.91 ?  1161 PHE B C     1 
ATOM   17835 O O     . PHE B 1 1163 ? 21.304  56.177  80.313  1.00 17.49 ?  1161 PHE B O     1 
ATOM   17836 C CB    . PHE B 1 1163 ? 21.932  59.312  78.988  1.00 15.45 ?  1161 PHE B CB    1 
ATOM   17837 C CG    . PHE B 1 1163 ? 22.844  60.492  79.119  1.00 14.09 ?  1161 PHE B CG    1 
ATOM   17838 C CD1   . PHE B 1 1163 ? 22.513  61.542  79.955  1.00 17.24 ?  1161 PHE B CD1   1 
ATOM   17839 C CD2   . PHE B 1 1163 ? 24.048  60.543  78.431  1.00 15.74 ?  1161 PHE B CD2   1 
ATOM   17840 C CE1   . PHE B 1 1163 ? 23.348  62.623  80.105  1.00 20.21 ?  1161 PHE B CE1   1 
ATOM   17841 C CE2   . PHE B 1 1163 ? 24.877  61.633  78.563  1.00 17.33 ?  1161 PHE B CE2   1 
ATOM   17842 C CZ    . PHE B 1 1163 ? 24.534  62.669  79.407  1.00 16.49 ?  1161 PHE B CZ    1 
ATOM   17843 N N     . ALA B 1 1164 ? 19.591  57.558  79.866  1.00 15.99 ?  1162 ALA B N     1 
ATOM   17844 C CA    . ALA B 1 1164 ? 18.627  56.479  79.753  1.00 17.48 ?  1162 ALA B CA    1 
ATOM   17845 C C     . ALA B 1 1164 ? 18.100  56.311  78.339  1.00 18.09 ?  1162 ALA B C     1 
ATOM   17846 O O     . ALA B 1 1164 ? 17.249  55.449  78.104  1.00 20.93 ?  1162 ALA B O     1 
ATOM   17847 C CB    . ALA B 1 1164 ? 17.466  56.722  80.726  1.00 17.39 ?  1162 ALA B CB    1 
ATOM   17848 N N     . GLY B 1 1165 ? 18.622  57.075  77.392  1.00 14.60 ?  1163 GLY B N     1 
ATOM   17849 C CA    . GLY B 1 1165 ? 18.154  57.071  76.021  1.00 14.63 ?  1163 GLY B CA    1 
ATOM   17850 C C     . GLY B 1 1165 ? 18.688  58.302  75.331  1.00 13.61 ?  1163 GLY B C     1 
ATOM   17851 O O     . GLY B 1 1165 ? 19.324  59.149  75.946  1.00 14.19 ?  1163 GLY B O     1 
ATOM   17852 N N     . ALA B 1 1166 ? 18.437  58.386  74.022  1.00 15.36 ?  1164 ALA B N     1 
ATOM   17853 C CA    . ALA B 1 1166 ? 18.952  59.522  73.270  1.00 14.84 ?  1164 ALA B CA    1 
ATOM   17854 C C     . ALA B 1 1166 ? 18.035  59.835  72.103  1.00 14.16 ?  1164 ALA B C     1 
ATOM   17855 O O     . ALA B 1 1166 ? 17.471  58.932  71.484  1.00 16.66 ?  1164 ALA B O     1 
ATOM   17856 C CB    . ALA B 1 1166 ? 20.375  59.271  72.747  1.00 14.43 ?  1164 ALA B CB    1 
ATOM   17857 N N     . LEU B 1 1167 ? 17.904  61.127  71.809  1.00 12.67 ?  1165 LEU B N     1 
ATOM   17858 C CA    . LEU B 1 1167 ? 17.182  61.615  70.642  1.00 13.52 ?  1165 LEU B CA    1 
ATOM   17859 C C     . LEU B 1 1167 ? 18.148  62.450  69.814  1.00 13.14 ?  1165 LEU B C     1 
ATOM   17860 O O     . LEU B 1 1167 ? 18.817  63.334  70.357  1.00 15.91 ?  1165 LEU B O     1 
ATOM   17861 C CB    . LEU B 1 1167 ? 15.968  62.456  71.055  1.00 14.68 ?  1165 LEU B CB    1 
ATOM   17862 C CG    . LEU B 1 1167 ? 14.962  61.781  71.988  1.00 12.99 ?  1165 LEU B CG    1 
ATOM   17863 C CD1   . LEU B 1 1167 ? 13.901  62.796  72.374  1.00 15.87 ?  1165 LEU B CD1   1 
ATOM   17864 C CD2   . LEU B 1 1167 ? 14.325  60.575  71.306  1.00 13.84 ?  1165 LEU B CD2   1 
ATOM   17865 N N     . VAL B 1 1168 ? 18.219  62.171  68.507  1.00 13.92 ?  1166 VAL B N     1 
ATOM   17866 C CA    . VAL B 1 1168 ? 19.216  62.769  67.625  1.00 15.47 ?  1166 VAL B CA    1 
ATOM   17867 C C     . VAL B 1 1168 ? 18.509  63.348  66.406  1.00 14.88 ?  1166 VAL B C     1 
ATOM   17868 O O     . VAL B 1 1168 ? 17.587  62.729  65.865  1.00 16.02 ?  1166 VAL B O     1 
ATOM   17869 C CB    . VAL B 1 1168 ? 20.268  61.721  67.205  1.00 16.06 ?  1166 VAL B CB    1 
ATOM   17870 C CG1   . VAL B 1 1168 ? 21.342  62.345  66.306  1.00 17.92 ?  1166 VAL B CG1   1 
ATOM   17871 C CG2   . VAL B 1 1168 ? 20.905  61.050  68.442  1.00 15.01 ?  1166 VAL B CG2   1 
ATOM   17872 N N     . GLU B 1 1169 ? 18.914  64.552  66.000  1.00 15.12 ?  1167 GLU B N     1 
ATOM   17873 C CA    . GLU B 1 1169 ? 18.405  65.216  64.805  1.00 16.90 ?  1167 GLU B CA    1 
ATOM   17874 C C     . GLU B 1 1169 ? 19.572  65.480  63.866  1.00 17.82 ?  1167 GLU B C     1 
ATOM   17875 O O     . GLU B 1 1169 ? 20.601  65.995  64.304  1.00 19.93 ?  1167 GLU B O     1 
ATOM   17876 C CB    . GLU B 1 1169 ? 17.729  66.543  65.166  1.00 16.98 ?  1167 GLU B CB    1 
ATOM   17877 C CG    . GLU B 1 1169 ? 17.298  67.365  63.970  1.00 17.54 ?  1167 GLU B CG    1 
ATOM   17878 C CD    . GLU B 1 1169 ? 16.865  68.773  64.328  1.00 18.21 ?  1167 GLU B CD    1 
ATOM   17879 O OE1   . GLU B 1 1169 ? 17.115  69.250  65.461  1.00 17.66 ?  1167 GLU B OE1   1 
ATOM   17880 O OE2   . GLU B 1 1169 ? 16.256  69.419  63.453  1.00 20.01 ?  1167 GLU B OE2   1 
ATOM   17881 N N     . GLY B 1 1170 ? 19.422  65.125  62.598  1.00 17.18 ?  1168 GLY B N     1 
ATOM   17882 C CA    . GLY B 1 1170 ? 20.423  65.499  61.616  1.00 18.79 ?  1168 GLY B CA    1 
ATOM   17883 C C     . GLY B 1 1170 ? 20.310  64.668  60.357  1.00 20.62 ?  1168 GLY B C     1 
ATOM   17884 O O     . GLY B 1 1170 ? 19.425  63.823  60.211  1.00 19.28 ?  1168 GLY B O     1 
ATOM   17885 N N     . ASP B 1 1171 ? 21.243  64.930  59.440  1.00 21.69 ?  1169 ASP B N     1 
ATOM   17886 C CA    . ASP B 1 1171 ? 21.300  64.158  58.208  1.00 22.93 ?  1169 ASP B CA    1 
ATOM   17887 C C     . ASP B 1 1171 ? 22.045  62.848  58.459  1.00 22.00 ?  1169 ASP B C     1 
ATOM   17888 O O     . ASP B 1 1171 ? 22.469  62.546  59.580  1.00 19.49 ?  1169 ASP B O     1 
ATOM   17889 C CB    . ASP B 1 1171 ? 21.919  64.984  57.072  1.00 23.26 ?  1169 ASP B CB    1 
ATOM   17890 C CG    . ASP B 1 1171 ? 23.389  65.350  57.299  1.00 24.79 ?  1169 ASP B CG    1 
ATOM   17891 O OD1   . ASP B 1 1171 ? 24.020  64.915  58.282  1.00 24.58 ?  1169 ASP B OD1   1 
ATOM   17892 O OD2   . ASP B 1 1171 ? 23.935  66.099  56.453  1.00 28.77 ?  1169 ASP B OD2   1 
ATOM   17893 N N     . ALA B 1 1172 ? 22.211  62.060  57.393  1.00 22.34 ?  1170 ALA B N     1 
ATOM   17894 C CA    . ALA B 1 1172 ? 22.772  60.720  57.529  1.00 23.26 ?  1170 ALA B CA    1 
ATOM   17895 C C     . ALA B 1 1172 ? 24.171  60.758  58.125  1.00 21.77 ?  1170 ALA B C     1 
ATOM   17896 O O     . ALA B 1 1172 ? 24.498  59.963  59.014  1.00 22.35 ?  1170 ALA B O     1 
ATOM   17897 C CB    . ALA B 1 1172 ? 22.791  60.021  56.169  1.00 23.59 ?  1170 ALA B CB    1 
ATOM   17898 N N     . GLU B 1 1173 ? 25.027  61.661  57.630  1.00 21.42 ?  1171 GLU B N     1 
ATOM   17899 C CA    . GLU B 1 1173 ? 26.382  61.747  58.171  1.00 21.29 ?  1171 GLU B CA    1 
ATOM   17900 C C     . GLU B 1 1173 ? 26.364  62.131  59.645  1.00 20.39 ?  1171 GLU B C     1 
ATOM   17901 O O     . GLU B 1 1173 ? 27.143  61.593  60.444  1.00 21.49 ?  1171 GLU B O     1 
ATOM   17902 C CB    . GLU B 1 1173 ? 27.213  62.750  57.368  1.00 26.54 ?  1171 GLU B CB    1 
ATOM   17903 N N     . ARG B 1 1174 ? 25.479  63.056  60.025  1.00 19.73 ?  1172 ARG B N     1 
ATOM   17904 C CA    . ARG B 1 1174 ? 25.413  63.491  61.418  1.00 18.75 ?  1172 ARG B CA    1 
ATOM   17905 C C     . ARG B 1 1174 ? 24.900  62.374  62.314  1.00 18.84 ?  1172 ARG B C     1 
ATOM   17906 O O     . ARG B 1 1174 ? 25.445  62.139  63.396  1.00 19.98 ?  1172 ARG B O     1 
ATOM   17907 C CB    . ARG B 1 1174 ? 24.532  64.736  61.532  1.00 21.83 ?  1172 ARG B CB    1 
ATOM   17908 C CG    . ARG B 1 1174 ? 24.309  65.259  62.946  1.00 21.58 ?  1172 ARG B CG    1 
ATOM   17909 C CD    . ARG B 1 1174 ? 25.614  65.613  63.636  1.00 26.07 ?  1172 ARG B CD    1 
ATOM   17910 N NE    . ARG B 1 1174 ? 25.385  66.180  64.961  1.00 24.17 ?  1172 ARG B NE    1 
ATOM   17911 C CZ    . ARG B 1 1174 ? 26.318  66.301  65.898  1.00 24.64 ?  1172 ARG B CZ    1 
ATOM   17912 N NH1   . ARG B 1 1174 ? 27.563  65.900  65.694  1.00 25.05 ?  1172 ARG B NH1   1 
ATOM   17913 N NH2   . ARG B 1 1174 ? 25.989  66.815  67.080  1.00 24.42 ?  1172 ARG B NH2   1 
ATOM   17914 N N     . ILE B 1 1175 ? 23.875  61.657  61.858  1.00 18.14 ?  1173 ILE B N     1 
ATOM   17915 C CA    . ILE B 1 1175 ? 23.306  60.578  62.658  1.00 17.98 ?  1173 ILE B CA    1 
ATOM   17916 C C     . ILE B 1 1175 ? 24.351  59.505  62.910  1.00 17.48 ?  1173 ILE B C     1 
ATOM   17917 O O     . ILE B 1 1175 ? 24.501  59.015  64.035  1.00 18.63 ?  1173 ILE B O     1 
ATOM   17918 C CB    . ILE B 1 1175 ? 22.057  59.998  61.970  1.00 18.56 ?  1173 ILE B CB    1 
ATOM   17919 C CG1   . ILE B 1 1175 ? 20.906  61.006  62.010  1.00 19.28 ?  1173 ILE B CG1   1 
ATOM   17920 C CG2   . ILE B 1 1175 ? 21.651  58.707  62.647  1.00 20.65 ?  1173 ILE B CG2   1 
ATOM   17921 C CD1   . ILE B 1 1175 ? 19.732  60.598  61.156  1.00 20.69 ?  1173 ILE B CD1   1 
ATOM   17922 N N     . ARG B 1 1176 ? 25.099  59.134  61.867  1.00 19.14 ?  1174 ARG B N     1 
ATOM   17923 C CA    A ARG B 1 1176 ? 26.125  58.111  62.033  0.59 20.43 ?  1174 ARG B CA    1 
ATOM   17924 C CA    B ARG B 1 1176 ? 26.138  58.117  62.012  0.41 20.42 ?  1174 ARG B CA    1 
ATOM   17925 C C     . ARG B 1 1176 ? 27.210  58.562  63.003  1.00 18.47 ?  1174 ARG B C     1 
ATOM   17926 O O     . ARG B 1 1176 ? 27.623  57.795  63.881  1.00 18.96 ?  1174 ARG B O     1 
ATOM   17927 C CB    A ARG B 1 1176 ? 26.727  57.743  60.678  0.59 20.42 ?  1174 ARG B CB    1 
ATOM   17928 C CB    B ARG B 1 1176 ? 26.751  57.809  60.643  0.41 20.46 ?  1174 ARG B CB    1 
ATOM   17929 C CG    A ARG B 1 1176 ? 27.863  56.754  60.788  0.59 21.86 ?  1174 ARG B CG    1 
ATOM   17930 C CG    B ARG B 1 1176 ? 27.617  56.560  60.598  0.41 22.54 ?  1174 ARG B CG    1 
ATOM   17931 C CD    A ARG B 1 1176 ? 28.409  56.366  59.423  0.59 24.35 ?  1174 ARG B CD    1 
ATOM   17932 C CD    B ARG B 1 1176 ? 28.399  56.461  59.281  0.41 24.28 ?  1174 ARG B CD    1 
ATOM   17933 N NE    A ARG B 1 1176 ? 29.548  55.468  59.567  0.59 25.16 ?  1174 ARG B NE    1 
ATOM   17934 N NE    B ARG B 1 1176 ? 27.562  56.631  58.099  0.41 26.14 ?  1174 ARG B NE    1 
ATOM   17935 C CZ    A ARG B 1 1176 ? 30.802  55.872  59.709  0.59 29.29 ?  1174 ARG B CZ    1 
ATOM   17936 C CZ    B ARG B 1 1176 ? 27.008  55.637  57.416  0.41 27.06 ?  1174 ARG B CZ    1 
ATOM   17937 N NH1   A ARG B 1 1176 ? 31.116  57.159  59.726  0.59 31.69 ?  1174 ARG B NH1   1 
ATOM   17938 N NH1   B ARG B 1 1176 ? 27.162  54.376  57.783  0.41 27.77 ?  1174 ARG B NH1   1 
ATOM   17939 N NH2   A ARG B 1 1176 ? 31.763  54.965  59.841  0.59 27.45 ?  1174 ARG B NH2   1 
ATOM   17940 N NH2   B ARG B 1 1176 ? 26.283  55.916  56.336  0.41 30.58 ?  1174 ARG B NH2   1 
ATOM   17941 N N     . ALA B 1 1177 ? 27.673  59.812  62.880  1.00 17.71 ?  1175 ALA B N     1 
ATOM   17942 C CA    . ALA B 1 1177 ? 28.701  60.307  63.793  1.00 18.51 ?  1175 ALA B CA    1 
ATOM   17943 C C     . ALA B 1 1177 ? 28.220  60.305  65.237  1.00 18.59 ?  1175 ALA B C     1 
ATOM   17944 O O     . ALA B 1 1177 ? 28.958  59.904  66.148  1.00 19.47 ?  1175 ALA B O     1 
ATOM   17945 C CB    . ALA B 1 1177 ? 29.127  61.715  63.394  1.00 20.02 ?  1175 ALA B CB    1 
ATOM   17946 N N     . VAL B 1 1178 ? 26.994  60.775  65.468  1.00 18.77 ?  1176 VAL B N     1 
ATOM   17947 C CA    . VAL B 1 1178 ? 26.471  60.813  66.828  1.00 17.63 ?  1176 VAL B CA    1 
ATOM   17948 C C     . VAL B 1 1178 ? 26.264  59.403  67.354  1.00 18.01 ?  1176 VAL B C     1 
ATOM   17949 O O     . VAL B 1 1178 ? 26.578  59.100  68.514  1.00 17.58 ?  1176 VAL B O     1 
ATOM   17950 C CB    . VAL B 1 1178 ? 25.169  61.629  66.867  1.00 18.59 ?  1176 VAL B CB    1 
ATOM   17951 C CG1   . VAL B 1 1178 ? 24.500  61.490  68.237  1.00 18.70 ?  1176 VAL B CG1   1 
ATOM   17952 C CG2   . VAL B 1 1178 ? 25.465  63.085  66.547  1.00 19.49 ?  1176 VAL B CG2   1 
ATOM   17953 N N     . ASN B 1 1179 ? 25.722  58.522  66.512  1.00 16.78 ?  1177 ASN B N     1 
ATOM   17954 C CA    . ASN B 1 1179 ? 25.487  57.148  66.931  1.00 18.21 ?  1177 ASN B CA    1 
ATOM   17955 C C     . ASN B 1 1179 ? 26.792  56.486  67.358  1.00 18.29 ?  1177 ASN B C     1 
ATOM   17956 O O     . ASN B 1 1179 ? 26.835  55.784  68.375  1.00 18.32 ?  1177 ASN B O     1 
ATOM   17957 C CB    . ASN B 1 1179 ? 24.810  56.378  65.793  1.00 19.63 ?  1177 ASN B CB    1 
ATOM   17958 C CG    . ASN B 1 1179 ? 24.052  55.156  66.274  1.00 21.38 ?  1177 ASN B CG    1 
ATOM   17959 O OD1   . ASN B 1 1179 ? 23.601  55.083  67.420  1.00 22.58 ?  1177 ASN B OD1   1 
ATOM   17960 N ND2   . ASN B 1 1179 ? 23.909  54.180  65.389  1.00 20.87 ?  1177 ASN B ND2   1 
ATOM   17961 N N     . LYS B 1 1180 ? 27.877  56.725  66.608  1.00 18.50 ?  1178 LYS B N     1 
ATOM   17962 C CA    . LYS B 1 1180 ? 29.183  56.186  66.990  1.00 18.09 ?  1178 LYS B CA    1 
ATOM   17963 C C     . LYS B 1 1180 ? 29.658  56.753  68.323  1.00 17.81 ?  1178 LYS B C     1 
ATOM   17964 O O     . LYS B 1 1180 ? 30.176  56.013  69.170  1.00 19.73 ?  1178 LYS B O     1 
ATOM   17965 C CB    . LYS B 1 1180 ? 30.213  56.471  65.900  1.00 19.98 ?  1178 LYS B CB    1 
ATOM   17966 C CG    . LYS B 1 1180 ? 29.953  55.689  64.634  1.00 21.41 ?  1178 LYS B CG    1 
ATOM   17967 C CD    . LYS B 1 1180 ? 30.975  56.035  63.555  1.00 27.89 ?  1178 LYS B CD    1 
ATOM   17968 C CE    . LYS B 1 1180 ? 32.325  55.427  63.872  1.00 31.17 ?  1178 LYS B CE    1 
ATOM   17969 N NZ    . LYS B 1 1180 ? 32.278  53.937  63.750  1.00 34.18 ?  1178 LYS B NZ    1 
ATOM   17970 N N     . ALA B 1 1181 ? 29.493  58.065  68.529  1.00 17.66 ?  1179 ALA B N     1 
ATOM   17971 C CA    . ALA B 1 1181 ? 29.878  58.667  69.801  1.00 17.30 ?  1179 ALA B CA    1 
ATOM   17972 C C     . ALA B 1 1181 ? 29.057  58.105  70.953  1.00 18.63 ?  1179 ALA B C     1 
ATOM   17973 O O     . ALA B 1 1181 ? 29.589  57.868  72.043  1.00 17.59 ?  1179 ALA B O     1 
ATOM   17974 C CB    . ALA B 1 1181 ? 29.732  60.189  69.734  1.00 17.88 ?  1179 ALA B CB    1 
ATOM   17975 N N     . ILE B 1 1182 ? 27.761  57.878  70.727  1.00 17.29 ?  1180 ILE B N     1 
ATOM   17976 C CA    . ILE B 1 1182 ? 26.925  57.323  71.782  1.00 16.80 ?  1180 ILE B CA    1 
ATOM   17977 C C     . ILE B 1 1182 ? 27.335  55.889  72.085  1.00 17.39 ?  1180 ILE B C     1 
ATOM   17978 O O     . ILE B 1 1182 ? 27.375  55.476  73.250  1.00 16.78 ?  1180 ILE B O     1 
ATOM   17979 C CB    . ILE B 1 1182 ? 25.437  57.422  71.404  1.00 17.79 ?  1180 ILE B CB    1 
ATOM   17980 C CG1   . ILE B 1 1182 ? 24.996  58.884  71.431  1.00 18.26 ?  1180 ILE B CG1   1 
ATOM   17981 C CG2   . ILE B 1 1182 ? 24.581  56.578  72.365  1.00 18.04 ?  1180 ILE B CG2   1 
ATOM   17982 C CD1   . ILE B 1 1182 ? 23.576  59.097  70.980  1.00 18.72 ?  1180 ILE B CD1   1 
ATOM   17983 N N     . ALA B 1 1183 ? 27.662  55.110  71.046  1.00 16.93 ?  1181 ALA B N     1 
ATOM   17984 C CA    . ALA B 1 1183 ? 28.088  53.736  71.280  1.00 21.38 ?  1181 ALA B CA    1 
ATOM   17985 C C     . ALA B 1 1183 ? 29.364  53.682  72.102  1.00 21.37 ?  1181 ALA B C     1 
ATOM   17986 O O     . ALA B 1 1183 ? 29.591  52.706  72.827  1.00 23.12 ?  1181 ALA B O     1 
ATOM   17987 C CB    . ALA B 1 1183 ? 28.281  52.998  69.951  1.00 20.81 ?  1181 ALA B CB    1 
ATOM   17988 N N     . ALA B 1 1184 ? 30.200  54.724  72.020  1.00 16.82 ?  1182 ALA B N     1 
ATOM   17989 C CA    . ALA B 1 1184 ? 31.441  54.770  72.788  1.00 21.07 ?  1182 ALA B CA    1 
ATOM   17990 C C     . ALA B 1 1184 ? 31.267  55.253  74.230  1.00 18.85 ?  1182 ALA B C     1 
ATOM   17991 O O     . ALA B 1 1184 ? 32.256  55.269  74.971  1.00 19.28 ?  1182 ALA B O     1 
ATOM   17992 C CB    . ALA B 1 1184 ? 32.458  55.664  72.073  1.00 21.19 ?  1182 ALA B CB    1 
ATOM   17993 N N     . LEU B 1 1185 ? 30.068  55.654  74.654  1.00 16.20 ?  1183 LEU B N     1 
ATOM   17994 C CA    . LEU B 1 1185 ? 29.909  56.119  76.029  1.00 16.30 ?  1183 LEU B CA    1 
ATOM   17995 C C     . LEU B 1 1185 ? 29.998  54.935  76.991  1.00 17.67 ?  1183 LEU B C     1 
ATOM   17996 O O     . LEU B 1 1185 ? 29.520  53.839  76.677  1.00 20.83 ?  1183 LEU B O     1 
ATOM   17997 C CB    . LEU B 1 1185 ? 28.569  56.838  76.218  1.00 18.01 ?  1183 LEU B CB    1 
ATOM   17998 C CG    . LEU B 1 1185 ? 28.319  58.080  75.362  1.00 16.36 ?  1183 LEU B CG    1 
ATOM   17999 C CD1   . LEU B 1 1185 ? 26.882  58.563  75.534  1.00 17.21 ?  1183 LEU B CD1   1 
ATOM   18000 C CD2   . LEU B 1 1185 ? 29.313  59.184  75.737  1.00 16.21 ?  1183 LEU B CD2   1 
ATOM   18001 N N     . PRO B 1 1186 ? 30.584  55.122  78.170  1.00 20.75 ?  1184 PRO B N     1 
ATOM   18002 C CA    . PRO B 1 1186 ? 30.627  54.032  79.149  1.00 22.36 ?  1184 PRO B CA    1 
ATOM   18003 C C     . PRO B 1 1186 ? 29.258  53.788  79.762  1.00 17.48 ?  1184 PRO B C     1 
ATOM   18004 O O     . PRO B 1 1186 ? 28.357  54.626  79.703  1.00 20.08 ?  1184 PRO B O     1 
ATOM   18005 C CB    . PRO B 1 1186 ? 31.620  54.537  80.201  1.00 25.43 ?  1184 PRO B CB    1 
ATOM   18006 C CG    . PRO B 1 1186 ? 31.497  56.035  80.121  1.00 25.23 ?  1184 PRO B CG    1 
ATOM   18007 C CD    . PRO B 1 1186 ? 31.227  56.352  78.675  1.00 20.08 ?  1184 PRO B CD    1 
ATOM   18008 N N     . GLY B 1 1187 ? 29.112  52.611  80.362  1.00 19.95 ?  1185 GLY B N     1 
ATOM   18009 C CA    . GLY B 1 1187 ? 27.903  52.275  81.080  1.00 20.88 ?  1185 GLY B CA    1 
ATOM   18010 C C     . GLY B 1 1187 ? 26.841  51.643  80.200  1.00 19.31 ?  1185 GLY B C     1 
ATOM   18011 O O     . GLY B 1 1187 ? 27.132  50.820  79.327  1.00 22.52 ?  1185 GLY B O     1 
ATOM   18012 N N     . PRO B 1 1188 ? 25.588  52.019  80.415  1.00 18.37 ?  1186 PRO B N     1 
ATOM   18013 C CA    . PRO B 1 1188 ? 24.486  51.314  79.743  1.00 18.02 ?  1186 PRO B CA    1 
ATOM   18014 C C     . PRO B 1 1188 ? 24.458  51.566  78.246  1.00 19.39 ?  1186 PRO B C     1 
ATOM   18015 O O     . PRO B 1 1188 ? 24.903  52.604  77.751  1.00 22.55 ?  1186 PRO B O     1 
ATOM   18016 C CB    . PRO B 1 1188 ? 23.233  51.890  80.414  1.00 20.92 ?  1186 PRO B CB    1 
ATOM   18017 C CG    . PRO B 1 1188 ? 23.661  53.240  80.891  1.00 27.68 ?  1186 PRO B CG    1 
ATOM   18018 C CD    . PRO B 1 1188 ? 25.097  53.076  81.312  1.00 23.23 ?  1186 PRO B CD    1 
ATOM   18019 N N     . LEU B 1 1189 ? 23.900  50.596  77.526  1.00 18.08 ?  1187 LEU B N     1 
ATOM   18020 C CA    . LEU B 1 1189 ? 23.712  50.720  76.085  1.00 21.27 ?  1187 LEU B CA    1 
ATOM   18021 C C     . LEU B 1 1189 ? 22.462  51.542  75.812  1.00 22.62 ?  1187 LEU B C     1 
ATOM   18022 O O     . LEU B 1 1189 ? 21.352  51.123  76.153  1.00 24.01 ?  1187 LEU B O     1 
ATOM   18023 C CB    . LEU B 1 1189 ? 23.604  49.338  75.441  1.00 22.31 ?  1187 LEU B CB    1 
ATOM   18024 C CG    . LEU B 1 1189 ? 24.916  48.631  75.102  1.00 26.52 ?  1187 LEU B CG    1 
ATOM   18025 C CD1   . LEU B 1 1189 ? 25.675  48.225  76.360  1.00 33.87 ?  1187 LEU B CD1   1 
ATOM   18026 C CD2   . LEU B 1 1189 ? 24.664  47.427  74.219  1.00 26.27 ?  1187 LEU B CD2   1 
ATOM   18027 N N     . LEU B 1 1190 ? 22.631  52.715  75.217  1.00 20.93 ?  1188 LEU B N     1 
ATOM   18028 C CA    . LEU B 1 1190 ? 21.497  53.610  75.052  1.00 18.61 ?  1188 LEU B CA    1 
ATOM   18029 C C     . LEU B 1 1190 ? 20.646  53.217  73.856  1.00 18.67 ?  1188 LEU B C     1 
ATOM   18030 O O     . LEU B 1 1190 ? 21.160  52.900  72.776  1.00 19.78 ?  1188 LEU B O     1 
ATOM   18031 C CB    . LEU B 1 1190 ? 21.959  55.052  74.879  1.00 18.18 ?  1188 LEU B CB    1 
ATOM   18032 C CG    . LEU B 1 1190 ? 22.779  55.657  76.010  1.00 17.97 ?  1188 LEU B CG    1 
ATOM   18033 C CD1   . LEU B 1 1190 ? 22.914  57.147  75.760  1.00 17.76 ?  1188 LEU B CD1   1 
ATOM   18034 C CD2   . LEU B 1 1190 ? 22.158  55.379  77.373  1.00 21.63 ?  1188 LEU B CD2   1 
ATOM   18035 N N     . LEU B 1 1191 ? 19.333  53.256  74.055  1.00 18.57 ?  1189 LEU B N     1 
ATOM   18036 C CA    . LEU B 1 1191 ? 18.383  53.153  72.958  1.00 19.00 ?  1189 LEU B CA    1 
ATOM   18037 C C     . LEU B 1 1191 ? 18.307  54.519  72.279  1.00 21.82 ?  1189 LEU B C     1 
ATOM   18038 O O     . LEU B 1 1191 ? 17.797  55.483  72.864  1.00 20.08 ?  1189 LEU B O     1 
ATOM   18039 C CB    . LEU B 1 1191 ? 17.026  52.691  73.484  1.00 18.36 ?  1189 LEU B CB    1 
ATOM   18040 C CG    . LEU B 1 1191 ? 16.037  52.056  72.498  1.00 19.55 ?  1189 LEU B CG    1 
ATOM   18041 C CD1   . LEU B 1 1191 ? 14.893  51.404  73.270  1.00 21.00 ?  1189 LEU B CD1   1 
ATOM   18042 C CD2   . LEU B 1 1191 ? 15.487  53.061  71.490  1.00 17.37 ?  1189 LEU B CD2   1 
ATOM   18043 N N     . VAL B 1 1192 ? 18.817  54.593  71.048  1.00 16.62 ?  1190 VAL B N     1 
ATOM   18044 C CA    . VAL B 1 1192 ? 18.956  55.831  70.288  1.00 19.93 ?  1190 VAL B CA    1 
ATOM   18045 C C     . VAL B 1 1192 ? 17.850  55.909  69.244  1.00 21.23 ?  1190 VAL B C     1 
ATOM   18046 O O     . VAL B 1 1192 ? 17.601  54.933  68.524  1.00 20.69 ?  1190 VAL B O     1 
ATOM   18047 C CB    . VAL B 1 1192 ? 20.338  55.900  69.618  1.00 19.67 ?  1190 VAL B CB    1 
ATOM   18048 C CG1   . VAL B 1 1192 ? 20.481  57.158  68.780  1.00 17.75 ?  1190 VAL B CG1   1 
ATOM   18049 C CG2   . VAL B 1 1192 ? 21.451  55.816  70.674  1.00 19.68 ?  1190 VAL B CG2   1 
ATOM   18050 N N     . GLN B 1 1193 ? 17.186  57.065  69.158  1.00 15.64 ?  1191 GLN B N     1 
ATOM   18051 C CA    . GLN B 1 1193 ? 16.238  57.366  68.088  1.00 13.91 ?  1191 GLN B CA    1 
ATOM   18052 C C     . GLN B 1 1193 ? 16.731  58.571  67.311  1.00 15.34 ?  1191 GLN B C     1 
ATOM   18053 O O     . GLN B 1 1193 ? 17.130  59.574  67.913  1.00 16.58 ?  1191 GLN B O     1 
ATOM   18054 C CB    . GLN B 1 1193 ? 14.855  57.669  68.640  1.00 15.72 ?  1191 GLN B CB    1 
ATOM   18055 C CG    . GLN B 1 1193 ? 14.207  56.511  69.302  1.00 17.01 ?  1191 GLN B CG    1 
ATOM   18056 C CD    . GLN B 1 1193 ? 12.749  56.797  69.550  1.00 15.16 ?  1191 GLN B CD    1 
ATOM   18057 O OE1   . GLN B 1 1193 ? 11.918  56.686  68.640  1.00 16.08 ?  1191 GLN B OE1   1 
ATOM   18058 N NE2   . GLN B 1 1193 ? 12.427  57.165  70.778  1.00 16.37 ?  1191 GLN B NE2   1 
ATOM   18059 N N     . ALA B 1 1194 ? 16.682  58.481  65.985  1.00 16.23 ?  1192 ALA B N     1 
ATOM   18060 C CA    . ALA B 1 1194 ? 17.153  59.557  65.133  1.00 15.29 ?  1192 ALA B CA    1 
ATOM   18061 C C     . ALA B 1 1194 ? 16.083  59.971  64.137  1.00 18.13 ?  1192 ALA B C     1 
ATOM   18062 O O     . ALA B 1 1194 ? 15.212  59.180  63.755  1.00 19.67 ?  1192 ALA B O     1 
ATOM   18063 C CB    . ALA B 1 1194 ? 18.418  59.140  64.379  1.00 16.59 ?  1192 ALA B CB    1 
ATOM   18064 N N     . ALA B 1 1195 ? 16.167  61.228  63.715  1.00 16.10 ?  1193 ALA B N     1 
ATOM   18065 C CA    . ALA B 1 1195 ? 15.286  61.755  62.684  1.00 18.29 ?  1193 ALA B CA    1 
ATOM   18066 C C     . ALA B 1 1195 ? 15.965  62.926  61.996  1.00 21.74 ?  1193 ALA B C     1 
ATOM   18067 O O     . ALA B 1 1195 ? 16.775  63.635  62.597  1.00 18.47 ?  1193 ALA B O     1 
ATOM   18068 C CB    . ALA B 1 1195 ? 13.941  62.205  63.267  1.00 19.36 ?  1193 ALA B CB    1 
ATOM   18069 N N     . SER B 1 1196 ? 15.634  63.117  60.726  1.00 19.62 ?  1194 SER B N     1 
ATOM   18070 C CA    . SER B 1 1196 ? 16.058  64.327  60.054  1.00 20.34 ?  1194 SER B CA    1 
ATOM   18071 C C     . SER B 1 1196 ? 15.163  65.491  60.465  1.00 19.92 ?  1194 SER B C     1 
ATOM   18072 O O     . SER B 1 1196 ? 14.050  65.306  60.974  1.00 20.77 ?  1194 SER B O     1 
ATOM   18073 C CB    . SER B 1 1196 ? 15.999  64.141  58.540  1.00 21.37 ?  1194 SER B CB    1 
ATOM   18074 O OG    . SER B 1 1196 ? 14.655  63.918  58.153  1.00 23.34 ?  1194 SER B OG    1 
ATOM   18075 N N     . SER B 1 1197 ? 15.655  66.711  60.226  1.00 20.88 ?  1195 SER B N     1 
ATOM   18076 C CA    . SER B 1 1197 ? 14.822  67.887  60.462  1.00 20.79 ?  1195 SER B CA    1 
ATOM   18077 C C     . SER B 1 1197 ? 13.534  67.802  59.658  1.00 21.22 ?  1195 SER B C     1 
ATOM   18078 O O     . SER B 1 1197 ? 12.464  68.195  60.137  1.00 21.91 ?  1195 SER B O     1 
ATOM   18079 C CB    . SER B 1 1197 ? 15.579  69.165  60.110  1.00 19.74 ?  1195 SER B CB    1 
ATOM   18080 O OG    . SER B 1 1197 ? 16.769  69.309  60.875  1.00 21.82 ?  1195 SER B OG    1 
ATOM   18081 N N     . GLY B 1 1198 ? 13.620  67.264  58.442  1.00 22.51 ?  1196 GLY B N     1 
ATOM   18082 C CA    . GLY B 1 1198 ? 12.435  67.116  57.617  1.00 24.97 ?  1196 GLY B CA    1 
ATOM   18083 C C     . GLY B 1 1198 ? 11.436  66.128  58.186  1.00 23.61 ?  1196 GLY B C     1 
ATOM   18084 O O     . GLY B 1 1198 ? 10.229  66.377  58.156  1.00 26.23 ?  1196 GLY B O     1 
ATOM   18085 N N     . GLU B 1 1199 ? 11.914  64.986  58.698  1.00 23.86 ?  1197 GLU B N     1 
ATOM   18086 C CA    . GLU B 1 1199 ? 10.986  64.030  59.297  1.00 23.47 ?  1197 GLU B CA    1 
ATOM   18087 C C     . GLU B 1 1199 ? 10.304  64.623  60.527  1.00 23.96 ?  1197 GLU B C     1 
ATOM   18088 O O     . GLU B 1 1199 ? 9.110   64.392  60.758  1.00 24.10 ?  1197 GLU B O     1 
ATOM   18089 C CB    . GLU B 1 1199 ? 11.689  62.719  59.666  1.00 25.48 ?  1197 GLU B CB    1 
ATOM   18090 C CG    . GLU B 1 1199 ? 10.673  61.655  60.108  1.00 25.71 ?  1197 GLU B CG    1 
ATOM   18091 C CD    . GLU B 1 1199 ? 11.271  60.350  60.629  1.00 33.25 ?  1197 GLU B CD    1 
ATOM   18092 O OE1   . GLU B 1 1199 ? 12.510  60.169  60.603  1.00 33.49 ?  1197 GLU B OE1   1 
ATOM   18093 O OE2   . GLU B 1 1199 ? 10.471  59.490  61.068  1.00 33.24 ?  1197 GLU B OE2   1 
ATOM   18094 N N     . ILE B 1 1200 ? 11.043  65.393  61.331  1.00 19.60 ?  1198 ILE B N     1 
ATOM   18095 C CA    . ILE B 1 1200 ? 10.432  66.027  62.497  1.00 19.04 ?  1198 ILE B CA    1 
ATOM   18096 C C     . ILE B 1 1200 ? 9.289   66.938  62.066  1.00 23.88 ?  1198 ILE B C     1 
ATOM   18097 O O     . ILE B 1 1200 ? 8.226   66.968  62.699  1.00 21.66 ?  1198 ILE B O     1 
ATOM   18098 C CB    . ILE B 1 1200 ? 11.498  66.783  63.313  1.00 18.39 ?  1198 ILE B CB    1 
ATOM   18099 C CG1   . ILE B 1 1200 ? 12.509  65.793  63.897  1.00 20.75 ?  1198 ILE B CG1   1 
ATOM   18100 C CG2   . ILE B 1 1200 ? 10.863  67.610  64.430  1.00 19.15 ?  1198 ILE B CG2   1 
ATOM   18101 C CD1   . ILE B 1 1200 ? 13.680  66.455  64.590  1.00 20.42 ?  1198 ILE B CD1   1 
ATOM   18102 N N     . ALA B 1 1201 ? 9.473   67.657  60.954  1.00 24.14 ?  1199 ALA B N     1 
ATOM   18103 C CA    . ALA B 1 1201 ? 8.439   68.568  60.473  1.00 25.31 ?  1199 ALA B CA    1 
ATOM   18104 C C     . ALA B 1 1201 ? 7.228   67.811  59.940  1.00 24.46 ?  1199 ALA B C     1 
ATOM   18105 O O     . ALA B 1 1201 ? 6.088   68.261  60.102  1.00 28.53 ?  1199 ALA B O     1 
ATOM   18106 C CB    . ALA B 1 1201 ? 9.006   69.482  59.386  1.00 26.74 ?  1199 ALA B CB    1 
ATOM   18107 N N     . ARG B 1 1202 ? 7.449   66.658  59.308  1.00 25.37 ?  1200 ARG B N     1 
ATOM   18108 C CA    . ARG B 1 1202 ? 6.373   65.979  58.598  1.00 27.02 ?  1200 ARG B CA    1 
ATOM   18109 C C     . ARG B 1 1202 ? 5.754   64.821  59.368  1.00 29.11 ?  1200 ARG B C     1 
ATOM   18110 O O     . ARG B 1 1202 ? 4.619   64.439  59.062  1.00 27.20 ?  1200 ARG B O     1 
ATOM   18111 C CB    . ARG B 1 1202 ? 6.871   65.454  57.247  1.00 30.95 ?  1200 ARG B CB    1 
ATOM   18112 C CG    . ARG B 1 1202 ? 7.852   64.308  57.361  1.00 28.19 ?  1200 ARG B CG    1 
ATOM   18113 C CD    . ARG B 1 1202 ? 8.203   63.707  56.004  1.00 35.64 ?  1200 ARG B CD    1 
ATOM   18114 N NE    . ARG B 1 1202 ? 9.145   62.603  56.148  1.00 37.29 ?  1200 ARG B NE    1 
ATOM   18115 C CZ    . ARG B 1 1202 ? 10.448  62.694  55.920  1.00 34.72 ?  1200 ARG B CZ    1 
ATOM   18116 N NH1   . ARG B 1 1202 ? 10.993  63.811  55.463  1.00 32.75 ?  1200 ARG B NH1   1 
ATOM   18117 N NH2   . ARG B 1 1202 ? 11.222  61.639  56.156  1.00 31.93 ?  1200 ARG B NH2   1 
ATOM   18118 N N     . ASN B 1 1203 ? 6.451   64.253  60.343  1.00 24.72 ?  1201 ASN B N     1 
ATOM   18119 C CA    . ASN B 1 1203 ? 5.979   63.042  61.015  1.00 26.41 ?  1201 ASN B CA    1 
ATOM   18120 C C     . ASN B 1 1203 ? 5.812   63.296  62.504  1.00 27.30 ?  1201 ASN B C     1 
ATOM   18121 O O     . ASN B 1 1203 ? 6.821   63.378  63.230  1.00 25.28 ?  1201 ASN B O     1 
ATOM   18122 C CB    . ASN B 1 1203 ? 6.953   61.886  60.770  1.00 25.11 ?  1201 ASN B CB    1 
ATOM   18123 C CG    . ASN B 1 1203 ? 6.516   60.594  61.444  1.00 24.68 ?  1201 ASN B CG    1 
ATOM   18124 O OD1   . ASN B 1 1203 ? 5.387   60.480  61.925  1.00 26.37 ?  1201 ASN B OD1   1 
ATOM   18125 N ND2   . ASN B 1 1203 ? 7.411   59.614  61.479  1.00 28.49 ?  1201 ASN B ND2   1 
ATOM   18126 N N     . PRO B 1 1204 ? 4.579   63.412  63.010  1.00 26.37 ?  1202 PRO B N     1 
ATOM   18127 C CA    . PRO B 1 1204 ? 4.391   63.609  64.459  1.00 25.86 ?  1202 PRO B CA    1 
ATOM   18128 C C     . PRO B 1 1204 ? 4.967   62.487  65.309  1.00 25.92 ?  1202 PRO B C     1 
ATOM   18129 O O     . PRO B 1 1204 ? 5.235   62.701  66.499  1.00 25.81 ?  1202 PRO B O     1 
ATOM   18130 C CB    . PRO B 1 1204 ? 2.865   63.703  64.615  1.00 30.81 ?  1202 PRO B CB    1 
ATOM   18131 C CG    . PRO B 1 1204 ? 2.289   63.189  63.316  1.00 32.81 ?  1202 PRO B CG    1 
ATOM   18132 C CD    . PRO B 1 1204 ? 3.311   63.432  62.260  1.00 30.06 ?  1202 PRO B CD    1 
ATOM   18133 N N     . ASP B 1 1205 ? 5.176   61.300  64.743  1.00 21.89 ?  1203 ASP B N     1 
ATOM   18134 C CA    . ASP B 1 1205 ? 5.783   60.192  65.465  1.00 26.14 ?  1203 ASP B CA    1 
ATOM   18135 C C     . ASP B 1 1205 ? 7.245   59.991  65.089  1.00 25.05 ?  1203 ASP B C     1 
ATOM   18136 O O     . ASP B 1 1205 ? 7.754   58.870  65.184  1.00 24.22 ?  1203 ASP B O     1 
ATOM   18137 C CB    . ASP B 1 1205 ? 5.000   58.903  65.222  1.00 23.88 ?  1203 ASP B CB    1 
ATOM   18138 C CG    . ASP B 1 1205 ? 3.574   58.972  65.748  1.00 30.55 ?  1203 ASP B CG    1 
ATOM   18139 O OD1   . ASP B 1 1205 ? 3.312   59.719  66.720  1.00 30.72 ?  1203 ASP B OD1   1 
ATOM   18140 O OD2   . ASP B 1 1205 ? 2.714   58.261  65.187  1.00 29.62 ?  1203 ASP B OD2   1 
ATOM   18141 N N     . ALA B 1 1206 ? 7.926   61.054  64.647  1.00 22.61 ?  1204 ALA B N     1 
ATOM   18142 C CA    . ALA B 1 1206 ? 9.341   60.936  64.294  1.00 22.58 ?  1204 ALA B CA    1 
ATOM   18143 C C     . ALA B 1 1206 ? 10.146  60.349  65.444  1.00 20.77 ?  1204 ALA B C     1 
ATOM   18144 O O     . ALA B 1 1206 ? 11.043  59.523  65.235  1.00 22.60 ?  1204 ALA B O     1 
ATOM   18145 C CB    . ALA B 1 1206 ? 9.901   62.300  63.893  1.00 22.54 ?  1204 ALA B CB    1 
ATOM   18146 N N     . TYR B 1 1207 ? 9.834   60.757  66.667  1.00 17.94 ?  1205 TYR B N     1 
ATOM   18147 C CA    . TYR B 1 1207 ? 10.381  60.140  67.867  1.00 18.03 ?  1205 TYR B CA    1 
ATOM   18148 C C     . TYR B 1 1207 ? 9.261   59.360  68.536  1.00 18.26 ?  1205 TYR B C     1 
ATOM   18149 O O     . TYR B 1 1207 ? 8.227   59.935  68.887  1.00 23.67 ?  1205 TYR B O     1 
ATOM   18150 C CB    . TYR B 1 1207 ? 10.959  61.188  68.816  1.00 18.64 ?  1205 TYR B CB    1 
ATOM   18151 C CG    . TYR B 1 1207 ? 12.109  61.950  68.211  1.00 14.78 ?  1205 TYR B CG    1 
ATOM   18152 C CD1   . TYR B 1 1207 ? 13.271  61.289  67.821  1.00 14.64 ?  1205 TYR B CD1   1 
ATOM   18153 C CD2   . TYR B 1 1207 ? 12.045  63.318  68.044  1.00 15.16 ?  1205 TYR B CD2   1 
ATOM   18154 C CE1   . TYR B 1 1207 ? 14.332  61.984  67.259  1.00 15.72 ?  1205 TYR B CE1   1 
ATOM   18155 C CE2   . TYR B 1 1207 ? 13.097  64.019  67.479  1.00 18.60 ?  1205 TYR B CE2   1 
ATOM   18156 C CZ    . TYR B 1 1207 ? 14.237  63.346  67.098  1.00 16.13 ?  1205 TYR B CZ    1 
ATOM   18157 O OH    . TYR B 1 1207 ? 15.283  64.038  66.543  1.00 18.62 ?  1205 TYR B OH    1 
ATOM   18158 N N     . CYS B 1 1208 ? 9.460   58.059  68.676  1.00 13.62 ?  1206 CYS B N     1 
ATOM   18159 C CA    . CYS B 1 1208 ? 8.448   57.167  69.219  1.00 15.55 ?  1206 CYS B CA    1 
ATOM   18160 C C     . CYS B 1 1208 ? 8.487   57.215  70.740  1.00 15.36 ?  1206 CYS B C     1 
ATOM   18161 O O     . CYS B 1 1208 ? 9.526   56.939  71.349  1.00 14.13 ?  1206 CYS B O     1 
ATOM   18162 C CB    . CYS B 1 1208 ? 8.692   55.746  68.719  1.00 16.35 ?  1206 CYS B CB    1 
ATOM   18163 S SG    . CYS B 1 1208 ? 7.424   54.591  69.259  1.00 20.38 ?  1206 CYS B SG    1 
ATOM   18164 N N     . LEU B 1 1209 ? 7.347   57.541  71.362  1.00 13.91 ?  1207 LEU B N     1 
ATOM   18165 C CA    . LEU B 1 1209 ? 7.330   57.624  72.820  1.00 12.64 ?  1207 LEU B CA    1 
ATOM   18166 C C     . LEU B 1 1209 ? 7.385   56.257  73.491  1.00 13.08 ?  1207 LEU B C     1 
ATOM   18167 O O     . LEU B 1 1209 ? 7.630   56.194  74.701  1.00 14.55 ?  1207 LEU B O     1 
ATOM   18168 C CB    . LEU B 1 1209 ? 6.100   58.388  73.287  1.00 13.58 ?  1207 LEU B CB    1 
ATOM   18169 C CG    . LEU B 1 1209 ? 5.936   59.789  72.704  1.00 15.00 ?  1207 LEU B CG    1 
ATOM   18170 C CD1   . LEU B 1 1209 ? 4.742   60.483  73.353  1.00 16.48 ?  1207 LEU B CD1   1 
ATOM   18171 C CD2   . LEU B 1 1209 ? 7.193   60.629  72.898  1.00 17.23 ?  1207 LEU B CD2   1 
ATOM   18172 N N     . ASN B 1 1210 ? 7.179   55.170  72.736  1.00 13.94 ?  1208 ASN B N     1 
ATOM   18173 C CA    . ASN B 1 1210 ? 7.284   53.830  73.304  1.00 16.64 ?  1208 ASN B CA    1 
ATOM   18174 C C     . ASN B 1 1210 ? 8.638   53.621  73.969  1.00 13.73 ?  1208 ASN B C     1 
ATOM   18175 O O     . ASN B 1 1210 ? 8.747   52.922  74.982  1.00 17.68 ?  1208 ASN B O     1 
ATOM   18176 C CB    . ASN B 1 1210 ? 7.079   52.762  72.217  1.00 18.73 ?  1208 ASN B CB    1 
ATOM   18177 C CG    . ASN B 1 1210 ? 5.652   52.742  71.637  1.00 20.70 ?  1208 ASN B CG    1 
ATOM   18178 O OD1   . ASN B 1 1210 ? 4.872   53.675  71.812  1.00 24.91 ?  1208 ASN B OD1   1 
ATOM   18179 N ND2   . ASN B 1 1210 ? 5.349   51.696  70.865  1.00 25.58 ?  1208 ASN B ND2   1 
ATOM   18180 N N     . TRP B 1 1211 ? 9.697   54.199  73.397  1.00 13.71 ?  1209 TRP B N     1 
ATOM   18181 C CA    . TRP B 1 1211 ? 11.053  53.913  73.847  1.00 14.01 ?  1209 TRP B CA    1 
ATOM   18182 C C     . TRP B 1 1211 ? 11.559  54.910  74.868  1.00 13.91 ?  1209 TRP B C     1 
ATOM   18183 O O     . TRP B 1 1211 ? 12.716  54.814  75.283  1.00 16.70 ?  1209 TRP B O     1 
ATOM   18184 C CB    . TRP B 1 1211 ? 12.015  53.862  72.647  1.00 16.05 ?  1209 TRP B CB    1 
ATOM   18185 C CG    . TRP B 1 1211 ? 11.385  53.162  71.482  1.00 15.79 ?  1209 TRP B CG    1 
ATOM   18186 C CD1   . TRP B 1 1211 ? 11.211  53.649  70.211  1.00 16.43 ?  1209 TRP B CD1   1 
ATOM   18187 C CD2   . TRP B 1 1211 ? 10.775  51.867  71.502  1.00 16.96 ?  1209 TRP B CD2   1 
ATOM   18188 N NE1   . TRP B 1 1211 ? 10.557  52.718  69.430  1.00 16.80 ?  1209 TRP B NE1   1 
ATOM   18189 C CE2   . TRP B 1 1211 ? 10.273  51.619  70.206  1.00 17.96 ?  1209 TRP B CE2   1 
ATOM   18190 C CE3   . TRP B 1 1211 ? 10.620  50.880  72.494  1.00 16.55 ?  1209 TRP B CE3   1 
ATOM   18191 C CZ2   . TRP B 1 1211 ? 9.622   50.430  69.873  1.00 20.62 ?  1209 TRP B CZ2   1 
ATOM   18192 C CZ3   . TRP B 1 1211 ? 9.966   49.706  72.165  1.00 18.21 ?  1209 TRP B CZ3   1 
ATOM   18193 C CH2   . TRP B 1 1211 ? 9.475   49.490  70.863  1.00 19.91 ?  1209 TRP B CH2   1 
ATOM   18194 N N     . LEU B 1 1212 ? 10.707  55.835  75.316  1.00 13.51 ?  1210 LEU B N     1 
ATOM   18195 C CA    . LEU B 1 1212 ? 11.100  56.855  76.277  1.00 13.04 ?  1210 LEU B CA    1 
ATOM   18196 C C     . LEU B 1 1212 ? 10.483  56.623  77.649  1.00 12.90 ?  1210 LEU B C     1 
ATOM   18197 O O     . LEU B 1 1212 ? 10.622  57.468  78.530  1.00 12.42 ?  1210 LEU B O     1 
ATOM   18198 C CB    . LEU B 1 1212 ? 10.736  58.247  75.735  1.00 11.63 ?  1210 LEU B CB    1 
ATOM   18199 C CG    . LEU B 1 1212 ? 11.623  58.693  74.561  1.00 11.26 ?  1210 LEU B CG    1 
ATOM   18200 C CD1   . LEU B 1 1212 ? 10.996  59.869  73.841  1.00 15.08 ?  1210 LEU B CD1   1 
ATOM   18201 C CD2   . LEU B 1 1212 ? 13.005  59.059  75.076  1.00 15.38 ?  1210 LEU B CD2   1 
ATOM   18202 N N     . VAL B 1 1213 ? 9.837   55.476  77.854  1.00 14.41 ?  1211 VAL B N     1 
ATOM   18203 C CA    . VAL B 1 1213 ? 9.326   55.070  79.155  1.00 12.54 ?  1211 VAL B CA    1 
ATOM   18204 C C     . VAL B 1 1213 ? 10.045  53.780  79.541  1.00 14.33 ?  1211 VAL B C     1 
ATOM   18205 O O     . VAL B 1 1213 ? 10.659  53.105  78.707  1.00 16.01 ?  1211 VAL B O     1 
ATOM   18206 C CB    . VAL B 1 1213 ? 7.791   54.880  79.147  1.00 13.27 ?  1211 VAL B CB    1 
ATOM   18207 C CG1   . VAL B 1 1213 ? 7.099   56.240  79.011  1.00 12.63 ?  1211 VAL B CG1   1 
ATOM   18208 C CG2   . VAL B 1 1213 ? 7.361   53.913  78.027  1.00 14.45 ?  1211 VAL B CG2   1 
ATOM   18209 N N     . GLU B 1 1214 ? 10.006  53.474  80.828  1.00 13.24 ?  1212 GLU B N     1 
ATOM   18210 C CA    . GLU B 1 1214 ? 10.601  52.261  81.372  1.00 14.09 ?  1212 GLU B CA    1 
ATOM   18211 C C     . GLU B 1 1214 ? 9.492   51.335  81.855  1.00 12.44 ?  1212 GLU B C     1 
ATOM   18212 O O     . GLU B 1 1214 ? 8.614   51.756  82.608  1.00 12.24 ?  1212 GLU B O     1 
ATOM   18213 C CB    . GLU B 1 1214 ? 11.548  52.592  82.520  1.00 17.94 ?  1212 GLU B CB    1 
ATOM   18214 C CG    . GLU B 1 1214 ? 12.230  51.364  83.101  1.00 20.75 ?  1212 GLU B CG    1 
ATOM   18215 C CD    . GLU B 1 1214 ? 13.142  51.689  84.261  1.00 33.12 ?  1212 GLU B CD    1 
ATOM   18216 O OE1   . GLU B 1 1214 ? 13.854  52.709  84.183  1.00 32.28 ?  1212 GLU B OE1   1 
ATOM   18217 O OE2   . GLU B 1 1214 ? 13.142  50.922  85.252  1.00 40.14 ?  1212 GLU B OE2   1 
ATOM   18218 N N     . GLU B 1 1215 ? 9.534   50.084  81.418  1.00 13.56 ?  1213 GLU B N     1 
ATOM   18219 C CA    . GLU B 1 1215 ? 8.591   49.079  81.892  1.00 10.95 ?  1213 GLU B CA    1 
ATOM   18220 C C     . GLU B 1 1215 ? 9.043   48.496  83.221  1.00 10.58 ?  1213 GLU B C     1 
ATOM   18221 O O     . GLU B 1 1215 ? 10.213  48.154  83.398  1.00 12.72 ?  1213 GLU B O     1 
ATOM   18222 C CB    . GLU B 1 1215 ? 8.496   47.943  80.888  1.00 12.02 ?  1213 GLU B CB    1 
ATOM   18223 C CG    . GLU B 1 1215 ? 8.118   48.343  79.475  1.00 13.78 ?  1213 GLU B CG    1 
ATOM   18224 C CD    . GLU B 1 1215 ? 8.279   47.185  78.513  1.00 12.43 ?  1213 GLU B CD    1 
ATOM   18225 O OE1   . GLU B 1 1215 ? 9.418   46.998  78.029  1.00 14.11 ?  1213 GLU B OE1   1 
ATOM   18226 O OE2   . GLU B 1 1215 ? 7.290   46.466  78.258  1.00 12.79 ?  1213 GLU B OE2   1 
ATOM   18227 N N     . VAL B 1 1216 ? 8.092   48.320  84.137  1.00 10.05 ?  1214 VAL B N     1 
ATOM   18228 C CA    . VAL B 1 1216 ? 8.346   47.621  85.392  1.00 10.13 ?  1214 VAL B CA    1 
ATOM   18229 C C     . VAL B 1 1216 ? 7.267   46.569  85.599  1.00 10.58 ?  1214 VAL B C     1 
ATOM   18230 O O     . VAL B 1 1216 ? 6.072   46.872  85.530  1.00 13.09 ?  1214 VAL B O     1 
ATOM   18231 C CB    . VAL B 1 1216 ? 8.392   48.584  86.592  1.00 11.83 ?  1214 VAL B CB    1 
ATOM   18232 C CG1   . VAL B 1 1216 ? 8.585   47.796  87.897  1.00 13.60 ?  1214 VAL B CG1   1 
ATOM   18233 C CG2   . VAL B 1 1216 ? 9.524   49.574  86.403  1.00 12.92 ?  1214 VAL B CG2   1 
ATOM   18234 N N     . SER B 1 1217 ? 7.697   45.340  85.891  1.00 9.26  ?  1215 SER B N     1 
ATOM   18235 C CA    . SER B 1 1217 ? 6.824   44.231  86.244  1.00 9.26  ?  1215 SER B CA    1 
ATOM   18236 C C     . SER B 1 1217 ? 6.965   43.956  87.730  1.00 9.70  ?  1215 SER B C     1 
ATOM   18237 O O     . SER B 1 1217 ? 8.080   43.944  88.250  1.00 11.72 ?  1215 SER B O     1 
ATOM   18238 C CB    . SER B 1 1217 ? 7.227   42.975  85.464  1.00 10.67 ?  1215 SER B CB    1 
ATOM   18239 O OG    . SER B 1 1217 ? 6.663   41.794  86.021  1.00 13.04 ?  1215 SER B OG    1 
ATOM   18240 N N     . ALA B 1 1218 ? 5.841   43.757  88.416  1.00 9.57  ?  1216 ALA B N     1 
ATOM   18241 C CA    . ALA B 1 1218 ? 5.862   43.367  89.823  1.00 10.71 ?  1216 ALA B CA    1 
ATOM   18242 C C     . ALA B 1 1218 ? 4.931   42.189  90.040  1.00 11.67 ?  1216 ALA B C     1 
ATOM   18243 O O     . ALA B 1 1218 ? 3.767   42.233  89.637  1.00 13.59 ?  1216 ALA B O     1 
ATOM   18244 C CB    . ALA B 1 1218 ? 5.457   44.529  90.737  1.00 12.26 ?  1216 ALA B CB    1 
ATOM   18245 N N     . SER B 1 1219 ? 5.441   41.137  90.680  1.00 10.47 ?  1217 SER B N     1 
ATOM   18246 C CA    . SER B 1 1219 ? 4.655   39.945  90.963  1.00 10.42 ?  1217 SER B CA    1 
ATOM   18247 C C     . SER B 1 1219 ? 4.570   39.787  92.468  1.00 9.40  ?  1217 SER B C     1 
ATOM   18248 O O     . SER B 1 1219 ? 5.600   39.607  93.123  1.00 10.82 ?  1217 SER B O     1 
ATOM   18249 C CB    . SER B 1 1219 ? 5.293   38.706  90.329  1.00 11.04 ?  1217 SER B CB    1 
ATOM   18250 O OG    . SER B 1 1219 ? 4.519   37.523  90.540  1.00 12.37 ?  1217 SER B OG    1 
ATOM   18251 N N     . ILE B 1 1220 ? 3.350   39.829  92.997  1.00 9.65  ?  1218 ILE B N     1 
ATOM   18252 C CA    . ILE B 1 1220 ? 3.097   39.798  94.438  1.00 11.36 ?  1218 ILE B CA    1 
ATOM   18253 C C     . ILE B 1 1220 ? 2.407   38.479  94.764  1.00 11.27 ?  1218 ILE B C     1 
ATOM   18254 O O     . ILE B 1 1220 ? 1.326   38.190  94.235  1.00 12.09 ?  1218 ILE B O     1 
ATOM   18255 C CB    . ILE B 1 1220 ? 2.232   40.986  94.879  1.00 15.09 ?  1218 ILE B CB    1 
ATOM   18256 C CG1   . ILE B 1 1220 ? 2.915   42.309  94.512  1.00 17.87 ?  1218 ILE B CG1   1 
ATOM   18257 C CG2   . ILE B 1 1220 ? 1.995   40.922  96.382  1.00 16.29 ?  1218 ILE B CG2   1 
ATOM   18258 C CD1   . ILE B 1 1220 ? 1.962   43.462  94.333  1.00 26.22 ?  1218 ILE B CD1   1 
ATOM   18259 N N     . ASN B 1 1221 ? 3.010   37.689  95.652  1.00 12.38 ?  1219 ASN B N     1 
ATOM   18260 C CA    . ASN B 1 1221 ? 2.381   36.454  96.121  1.00 11.66 ?  1219 ASN B CA    1 
ATOM   18261 C C     . ASN B 1 1221 ? 1.338   36.816  97.174  1.00 13.01 ?  1219 ASN B C     1 
ATOM   18262 O O     . ASN B 1 1221 ? 1.678   37.069  98.334  1.00 15.83 ?  1219 ASN B O     1 
ATOM   18263 C CB    . ASN B 1 1221 ? 3.441   35.512  96.678  1.00 12.46 ?  1219 ASN B CB    1 
ATOM   18264 C CG    . ASN B 1 1221 ? 2.850   34.280  97.311  1.00 13.42 ?  1219 ASN B CG    1 
ATOM   18265 O OD1   . ASN B 1 1221 ? 1.655   34.021  97.191  1.00 13.15 ?  1219 ASN B OD1   1 
ATOM   18266 N ND2   . ASN B 1 1221 ? 3.688   33.517  98.016  1.00 15.80 ?  1219 ASN B ND2   1 
ATOM   18267 N N     . THR B 1 1222 ? 0.057   36.815  96.790  1.00 12.63 ?  1220 THR B N     1 
ATOM   18268 C CA    . THR B 1 1222 ? -1.016  37.202  97.705  1.00 13.24 ?  1220 THR B CA    1 
ATOM   18269 C C     . THR B 1 1222 ? -1.512  36.045  98.549  1.00 16.75 ?  1220 THR B C     1 
ATOM   18270 O O     . THR B 1 1222 ? -2.414  36.239  99.373  1.00 20.17 ?  1220 THR B O     1 
ATOM   18271 C CB    . THR B 1 1222 ? -2.188  37.820  96.940  1.00 15.20 ?  1220 THR B CB    1 
ATOM   18272 O OG1   . THR B 1 1222 ? -2.693  36.883  95.979  1.00 17.05 ?  1220 THR B OG1   1 
ATOM   18273 C CG2   . THR B 1 1222 ? -1.750  39.105  96.238  1.00 16.19 ?  1220 THR B CG2   1 
ATOM   18274 N N     . ALA B 1 1223 ? -0.939  34.859  98.379  1.00 14.37 ?  1221 ALA B N     1 
ATOM   18275 C CA    . ALA B 1 1223 ? -1.214  33.719  99.230  1.00 16.45 ?  1221 ALA B CA    1 
ATOM   18276 C C     . ALA B 1 1223 ? -0.178  33.573  100.336 1.00 19.95 ?  1221 ALA B C     1 
ATOM   18277 O O     . ALA B 1 1223 ? -0.230  32.595  101.089 1.00 20.91 ?  1221 ALA B O     1 
ATOM   18278 C CB    . ALA B 1 1223 ? -1.266  32.440  98.392  1.00 17.37 ?  1221 ALA B CB    1 
ATOM   18279 N N     . ALA B 1 1224 ? 0.759   34.525  100.453 1.00 19.14 ?  1222 ALA B N     1 
ATOM   18280 C CA    . ALA B 1 1224 ? 1.919   34.321  101.317 1.00 19.62 ?  1222 ALA B CA    1 
ATOM   18281 C C     . ALA B 1 1224 ? 1.540   34.202  102.790 1.00 24.62 ?  1222 ALA B C     1 
ATOM   18282 O O     . ALA B 1 1224 ? 2.276   33.573  103.562 1.00 24.43 ?  1222 ALA B O     1 
ATOM   18283 C CB    . ALA B 1 1224 ? 2.936   35.448  101.124 1.00 21.98 ?  1222 ALA B CB    1 
ATOM   18284 N N     . ALA B 1 1225 ? 0.408   34.781  103.206 1.00 18.67 ?  1223 ALA B N     1 
ATOM   18285 C CA    . ALA B 1 1225 ? 0.028   34.694  104.613 1.00 21.71 ?  1223 ALA B CA    1 
ATOM   18286 C C     . ALA B 1 1225 ? -0.502  33.322  104.997 1.00 25.86 ?  1223 ALA B C     1 
ATOM   18287 O O     . ALA B 1 1225 ? -0.705  33.073  106.189 1.00 23.93 ?  1223 ALA B O     1 
ATOM   18288 C CB    . ALA B 1 1225 ? -1.018  35.761  104.963 1.00 23.63 ?  1223 ALA B CB    1 
ATOM   18289 N N     . GLY B 1 1226 ? -0.743  32.440  104.033 1.00 23.64 ?  1224 GLY B N     1 
ATOM   18290 C CA    . GLY B 1 1226 ? -1.205  31.090  104.315 1.00 23.14 ?  1224 GLY B CA    1 
ATOM   18291 C C     . GLY B 1 1226 ? -2.495  30.704  103.622 1.00 24.63 ?  1224 GLY B C     1 
ATOM   18292 O O     . GLY B 1 1226 ? -2.920  29.545  103.740 1.00 24.67 ?  1224 GLY B O     1 
ATOM   18293 N N     . GLY B 1 1227 ? -3.144  31.619  102.911 1.00 20.75 ?  1225 GLY B N     1 
ATOM   18294 C CA    . GLY B 1 1227 ? -4.357  31.313  102.176 1.00 20.60 ?  1225 GLY B CA    1 
ATOM   18295 C C     . GLY B 1 1227 ? -4.649  32.433  101.203 1.00 20.83 ?  1225 GLY B C     1 
ATOM   18296 O O     . GLY B 1 1227 ? -3.936  33.440  101.152 1.00 19.81 ?  1225 GLY B O     1 
ATOM   18297 N N     . ASN B 1 1228 ? -5.737  32.260  100.451 1.00 19.89 ?  1226 ASN B N     1 
ATOM   18298 C CA    . ASN B 1 1228 ? -6.107  33.144  99.344  1.00 20.84 ?  1226 ASN B CA    1 
ATOM   18299 C C     . ASN B 1 1228 ? -7.446  33.810  99.654  1.00 23.95 ?  1226 ASN B C     1 
ATOM   18300 O O     . ASN B 1 1228 ? -8.498  33.161  99.588  1.00 24.00 ?  1226 ASN B O     1 
ATOM   18301 C CB    . ASN B 1 1228 ? -6.167  32.340  98.039  1.00 22.64 ?  1226 ASN B CB    1 
ATOM   18302 C CG    . ASN B 1 1228 ? -6.485  33.198  96.813  1.00 22.56 ?  1226 ASN B CG    1 
ATOM   18303 O OD1   . ASN B 1 1228 ? -7.231  34.178  96.891  1.00 23.56 ?  1226 ASN B OD1   1 
ATOM   18304 N ND2   . ASN B 1 1228 ? -5.942  32.805  95.660  1.00 21.74 ?  1226 ASN B ND2   1 
ATOM   18305 N N     . ALA B 1 1229 ? -7.406  35.111  99.967  1.00 21.71 ?  1227 ALA B N     1 
ATOM   18306 C CA    . ALA B 1 1229 ? -8.620  35.835  100.346 1.00 25.83 ?  1227 ALA B CA    1 
ATOM   18307 C C     . ALA B 1 1229 ? -9.670  35.800  99.241  1.00 27.28 ?  1227 ALA B C     1 
ATOM   18308 O O     . ALA B 1 1229 ? -10.862 35.608  99.516  1.00 25.43 ?  1227 ALA B O     1 
ATOM   18309 C CB    . ALA B 1 1229 ? -8.274  37.283  100.702 1.00 26.87 ?  1227 ALA B CB    1 
ATOM   18310 N N     . SER B 1 1230 ? -9.250  35.982  97.985  1.00 25.39 ?  1228 SER B N     1 
ATOM   18311 C CA    . SER B 1 1230 ? -10.205 35.998  96.880  1.00 25.13 ?  1228 SER B CA    1 
ATOM   18312 C C     . SER B 1 1230 ? -10.939 34.670  96.758  1.00 28.81 ?  1228 SER B C     1 
ATOM   18313 O O     . SER B 1 1230 ? -12.157 34.643  96.528  1.00 27.86 ?  1228 SER B O     1 
ATOM   18314 C CB    . SER B 1 1230 ? -9.487  36.326  95.570  1.00 31.04 ?  1228 SER B CB    1 
ATOM   18315 O OG    . SER B 1 1230 ? -9.077  37.679  95.545  1.00 39.44 ?  1228 SER B OG    1 
ATOM   18316 N N     . LEU B 1 1231 ? -10.221 33.556  96.910  1.00 24.24 ?  1229 LEU B N     1 
ATOM   18317 C CA    . LEU B 1 1231 ? -10.855 32.248  96.786  1.00 25.07 ?  1229 LEU B CA    1 
ATOM   18318 C C     . LEU B 1 1231 ? -11.715 31.884  97.991  1.00 28.08 ?  1229 LEU B C     1 
ATOM   18319 O O     . LEU B 1 1231 ? -12.497 30.927  97.910  1.00 26.80 ?  1229 LEU B O     1 
ATOM   18320 C CB    . LEU B 1 1231 ? -9.792  31.167  96.539  1.00 23.60 ?  1229 LEU B CB    1 
ATOM   18321 C CG    . LEU B 1 1231 ? -9.663  30.765  95.059  1.00 22.97 ?  1229 LEU B CG    1 
ATOM   18322 C CD1   . LEU B 1 1231 ? -9.406  31.969  94.169  1.00 29.30 ?  1229 LEU B CD1   1 
ATOM   18323 C CD2   . LEU B 1 1231 ? -8.564  29.722  94.866  1.00 22.58 ?  1229 LEU B CD2   1 
ATOM   18324 N N     . MET B 1 1232 ? -11.624 32.629  99.096  1.00 26.65 ?  1230 MET B N     1 
ATOM   18325 C CA    . MET B 1 1232 ? -12.574 32.398  100.179 1.00 27.36 ?  1230 MET B CA    1 
ATOM   18326 C C     . MET B 1 1232 ? -14.006 32.705  99.756  1.00 30.65 ?  1230 MET B C     1 
ATOM   18327 O O     . MET B 1 1232 ? -14.947 32.200  100.380 1.00 29.45 ?  1230 MET B O     1 
ATOM   18328 C CB    . MET B 1 1232 ? -12.210 33.226  101.412 1.00 26.74 ?  1230 MET B CB    1 
ATOM   18329 C CG    . MET B 1 1232 ? -10.956 32.767  102.138 1.00 26.52 ?  1230 MET B CG    1 
ATOM   18330 S SD    . MET B 1 1232 ? -10.483 33.958  103.435 1.00 31.57 ?  1230 MET B SD    1 
ATOM   18331 C CE    . MET B 1 1232 ? -11.809 33.750  104.650 1.00 31.01 ?  1230 MET B CE    1 
ATOM   18332 N N     . ALA B 1 1233 ? -14.193 33.499  98.702  1.00 28.51 ?  1231 ALA B N     1 
ATOM   18333 C CA    . ALA B 1 1233 ? -15.522 33.821  98.195  1.00 31.71 ?  1231 ALA B CA    1 
ATOM   18334 C C     . ALA B 1 1233 ? -16.002 32.872  97.099  1.00 38.98 ?  1231 ALA B C     1 
ATOM   18335 O O     . ALA B 1 1233 ? -17.140 33.013  96.634  1.00 36.62 ?  1231 ALA B O     1 
ATOM   18336 C CB    . ALA B 1 1233 ? -15.547 35.260  97.671  1.00 35.71 ?  1231 ALA B CB    1 
ATOM   18337 N N     . ILE B 1 1234 ? -15.181 31.906  96.688  1.00 30.46 ?  1232 ILE B N     1 
ATOM   18338 C CA    . ILE B 1 1234 ? -15.491 31.025  95.563  1.00 33.03 ?  1232 ILE B CA    1 
ATOM   18339 C C     . ILE B 1 1234 ? -15.870 29.653  96.108  1.00 35.35 ?  1232 ILE B C     1 
ATOM   18340 O O     . ILE B 1 1234 ? -15.013 28.914  96.612  1.00 34.87 ?  1232 ILE B O     1 
ATOM   18341 C CB    . ILE B 1 1234 ? -14.315 30.926  94.583  1.00 29.40 ?  1232 ILE B CB    1 
ATOM   18342 C CG1   . ILE B 1 1234 ? -14.104 32.272  93.885  1.00 32.99 ?  1232 ILE B CG1   1 
ATOM   18343 C CG2   . ILE B 1 1234 ? -14.560 29.816  93.559  1.00 28.78 ?  1232 ILE B CG2   1 
ATOM   18344 C CD1   . ILE B 1 1234 ? -12.969 32.278  92.875  1.00 28.29 ?  1232 ILE B CD1   1 
ATOM   18345 N N     . GLY B 1 1235 ? -17.152 29.305  95.997  1.00 33.06 ?  1233 GLY B N     1 
ATOM   18346 C CA    . GLY B 1 1235 ? -17.643 28.002  96.410  1.00 29.36 ?  1233 GLY B CA    1 
ATOM   18347 C C     . GLY B 1 1235 ? -18.582 27.383  95.384  1.00 34.43 ?  1233 GLY B C     1 
ATOM   18348 O O     . GLY B 1 1235 ? -18.643 26.161  95.214  1.00 27.89 ?  1233 GLY B O     1 
ATOM   18349 O OXT   . GLY B 1 1235 ? -19.313 28.092  94.684  1.00 37.50 ?  1233 GLY B OXT   1 
HETATM 18350 N N     . GGL C 2 .    ? -20.942 74.345  103.594 1.00 20.38 ?  1301 GGL A N     1 
HETATM 18351 C CA    . GGL C 2 .    ? -21.718 75.220  102.742 1.00 17.58 ?  1301 GGL A CA    1 
HETATM 18352 C C     . GGL C 2 .    ? -21.877 74.611  101.387 1.00 16.15 ?  1301 GGL A C     1 
HETATM 18353 O O     . GGL C 2 .    ? -22.747 75.075  100.599 1.00 15.36 ?  1301 GGL A O     1 
HETATM 18354 C CB    . GGL C 2 .    ? -21.087 76.573  102.631 1.00 18.46 ?  1301 GGL A CB    1 
HETATM 18355 C CG    . GGL C 2 .    ? -20.798 77.119  104.006 1.00 18.59 ?  1301 GGL A CG    1 
HETATM 18356 C CD    . GGL C 2 .    ? -20.510 78.590  103.951 1.00 21.84 ?  1301 GGL A CD    1 
HETATM 18357 O OE1   . GGL C 2 .    ? -21.159 79.344  103.172 1.00 22.48 ?  1301 GGL A OE1   1 
HETATM 18358 O OE2   . GGL C 2 .    ? -19.614 79.098  104.681 1.00 26.78 -1 1301 GGL A OE2   1 
HETATM 18359 O OXT   . GGL C 2 .    ? -21.151 73.640  101.027 1.00 16.93 -1 1301 GGL A OXT   1 
HETATM 18360 S S     . SO4 D 3 .    ? -9.559  52.922  112.210 1.00 14.86 ?  1302 SO4 A S     1 
HETATM 18361 O O1    . SO4 D 3 .    ? -8.447  53.195  111.253 1.00 17.45 ?  1302 SO4 A O1    1 
HETATM 18362 O O2    . SO4 D 3 .    ? -10.600 52.083  111.565 1.00 18.95 ?  1302 SO4 A O2    1 
HETATM 18363 O O3    . SO4 D 3 .    ? -9.042  52.207  113.427 1.00 15.21 ?  1302 SO4 A O3    1 
HETATM 18364 O O4    . SO4 D 3 .    ? -10.126 54.253  112.595 1.00 18.01 ?  1302 SO4 A O4    1 
HETATM 18365 S S     . SO4 E 3 .    ? -12.606 75.278  70.986  0.76 20.39 ?  1303 SO4 A S     1 
HETATM 18366 O O1    . SO4 E 3 .    ? -12.368 73.944  70.355  0.76 25.23 ?  1303 SO4 A O1    1 
HETATM 18367 O O2    . SO4 E 3 .    ? -12.903 76.304  69.931  0.76 29.00 ?  1303 SO4 A O2    1 
HETATM 18368 O O3    . SO4 E 3 .    ? -13.805 75.154  71.863  0.76 17.72 ?  1303 SO4 A O3    1 
HETATM 18369 O O4    . SO4 E 3 .    ? -11.380 75.662  71.733  0.76 20.89 ?  1303 SO4 A O4    1 
HETATM 18370 S S     . SO4 F 3 .    ? -18.483 53.763  87.467  0.53 26.10 ?  1304 SO4 A S     1 
HETATM 18371 O O1    . SO4 F 3 .    ? -17.519 52.736  86.952  0.53 28.46 ?  1304 SO4 A O1    1 
HETATM 18372 O O2    . SO4 F 3 .    ? -19.604 53.906  86.479  0.53 20.61 ?  1304 SO4 A O2    1 
HETATM 18373 O O3    . SO4 F 3 .    ? -19.052 53.314  88.777  0.53 32.17 ?  1304 SO4 A O3    1 
HETATM 18374 O O4    . SO4 F 3 .    ? -17.776 55.070  87.657  0.53 25.34 ?  1304 SO4 A O4    1 
HETATM 18375 S S     . SO4 G 3 .    ? 12.393  75.428  127.314 0.71 29.44 ?  1305 SO4 A S     1 
HETATM 18376 O O1    . SO4 G 3 .    ? 13.158  75.886  126.104 0.71 35.12 ?  1305 SO4 A O1    1 
HETATM 18377 O O2    . SO4 G 3 .    ? 10.987  75.056  126.952 0.71 28.98 ?  1305 SO4 A O2    1 
HETATM 18378 O O3    . SO4 G 3 .    ? 13.102  74.235  127.874 0.71 31.45 ?  1305 SO4 A O3    1 
HETATM 18379 O O4    . SO4 G 3 .    ? 12.343  76.526  128.334 0.71 39.94 ?  1305 SO4 A O4    1 
HETATM 18380 S S     . SO4 H 3 .    ? 29.851  70.799  107.007 0.76 48.45 ?  1306 SO4 A S     1 
HETATM 18381 O O1    . SO4 H 3 .    ? 30.879  70.136  106.139 0.76 47.99 ?  1306 SO4 A O1    1 
HETATM 18382 O O2    . SO4 H 3 .    ? 28.620  71.084  106.206 0.76 43.26 ?  1306 SO4 A O2    1 
HETATM 18383 O O3    . SO4 H 3 .    ? 29.519  69.888  108.155 0.76 48.02 ?  1306 SO4 A O3    1 
HETATM 18384 O O4    . SO4 H 3 .    ? 30.388  72.097  107.532 0.76 50.31 ?  1306 SO4 A O4    1 
HETATM 18385 C C1    . PGE I 4 .    ? -3.536  60.813  97.445  1.00 29.21 ?  1307 PGE A C1    1 
HETATM 18386 O O1    . PGE I 4 .    ? -3.294  60.108  96.254  1.00 33.77 ?  1307 PGE A O1    1 
HETATM 18387 C C2    . PGE I 4 .    ? -2.668  62.070  97.516  1.00 28.25 ?  1307 PGE A C2    1 
HETATM 18388 O O2    . PGE I 4 .    ? -1.346  61.715  97.798  1.00 23.50 ?  1307 PGE A O2    1 
HETATM 18389 C C3    . PGE I 4 .    ? -0.488  62.806  97.975  1.00 22.27 ?  1307 PGE A C3    1 
HETATM 18390 C C4    . PGE I 4 .    ? 0.961   62.329  98.014  1.00 23.39 ?  1307 PGE A C4    1 
HETATM 18391 O O4    . PGE I 4 .    ? 1.966   58.306  96.524  1.00 41.38 ?  1307 PGE A O4    1 
HETATM 18392 C C6    . PGE I 4 .    ? 2.480   59.549  96.113  1.00 40.43 ?  1307 PGE A C6    1 
HETATM 18393 C C5    . PGE I 4 .    ? 2.303   60.587  97.223  1.00 32.84 ?  1307 PGE A C5    1 
HETATM 18394 O O3    . PGE I 4 .    ? 1.245   61.471  96.942  1.00 32.52 ?  1307 PGE A O3    1 
HETATM 18395 P PA    . FAD J 5 .    ? -38.362 43.297  83.627  1.00 16.92 ?  1308 FAD A PA    1 
HETATM 18396 O O1A   . FAD J 5 .    ? -39.275 42.137  84.121  1.00 18.68 ?  1308 FAD A O1A   1 
HETATM 18397 O O2A   . FAD J 5 .    ? -36.976 43.015  83.293  1.00 20.56 ?  1308 FAD A O2A   1 
HETATM 18398 O O5B   . FAD J 5 .    ? -38.267 44.392  84.620  1.00 17.45 ?  1308 FAD A O5B   1 
HETATM 18399 C C5B   . FAD J 5 .    ? -37.255 45.377  84.766  1.00 19.13 ?  1308 FAD A C5B   1 
HETATM 18400 C C4B   . FAD J 5 .    ? -37.763 46.414  85.771  1.00 17.27 ?  1308 FAD A C4B   1 
HETATM 18401 O O4B   . FAD J 5 .    ? -37.770 45.936  87.087  1.00 15.97 ?  1308 FAD A O4B   1 
HETATM 18402 C C3B   . FAD J 5 .    ? -36.975 47.685  85.895  1.00 15.43 ?  1308 FAD A C3B   1 
HETATM 18403 O O3B   . FAD J 5 .    ? -37.123 48.483  84.769  1.00 16.37 ?  1308 FAD A O3B   1 
HETATM 18404 C C2B   . FAD J 5 .    ? -37.473 48.242  87.172  1.00 15.61 ?  1308 FAD A C2B   1 
HETATM 18405 O O2B   . FAD J 5 .    ? -38.710 48.878  87.053  1.00 15.23 ?  1308 FAD A O2B   1 
HETATM 18406 C C1B   . FAD J 5 .    ? -37.647 47.001  87.987  1.00 14.23 ?  1308 FAD A C1B   1 
HETATM 18407 N N9A   . FAD J 5 .    ? -36.534 46.752  88.880  1.00 15.44 ?  1308 FAD A N9A   1 
HETATM 18408 C C8A   . FAD J 5 .    ? -35.227 46.399  88.569  1.00 18.46 ?  1308 FAD A C8A   1 
HETATM 18409 N N7A   . FAD J 5 .    ? -34.525 46.266  89.697  1.00 16.06 ?  1308 FAD A N7A   1 
HETATM 18410 C C5A   . FAD J 5 .    ? -35.352 46.517  90.791  1.00 15.88 ?  1308 FAD A C5A   1 
HETATM 18411 C C6A   . FAD J 5 .    ? -35.181 46.521  92.163  1.00 16.63 ?  1308 FAD A C6A   1 
HETATM 18412 N N6A   . FAD J 5 .    ? -33.918 46.199  92.754  1.00 15.59 ?  1308 FAD A N6A   1 
HETATM 18413 N N1A   . FAD J 5 .    ? -36.210 46.829  92.960  1.00 15.77 ?  1308 FAD A N1A   1 
HETATM 18414 C C2A   . FAD J 5 .    ? -37.432 47.117  92.451  1.00 15.47 ?  1308 FAD A C2A   1 
HETATM 18415 N N3A   . FAD J 5 .    ? -37.652 47.120  91.115  1.00 15.44 ?  1308 FAD A N3A   1 
HETATM 18416 C C4A   . FAD J 5 .    ? -36.644 46.829  90.275  1.00 16.50 ?  1308 FAD A C4A   1 
HETATM 18417 N N1    . FAD J 5 .    ? -41.261 53.437  82.376  1.00 14.70 ?  1308 FAD A N1    1 
HETATM 18418 C C2    . FAD J 5 .    ? -41.624 54.615  83.074  1.00 11.65 ?  1308 FAD A C2    1 
HETATM 18419 O O2    . FAD J 5 .    ? -41.123 54.889  84.272  1.00 12.91 ?  1308 FAD A O2    1 
HETATM 18420 N N3    . FAD J 5 .    ? -42.508 55.534  82.490  1.00 11.35 ?  1308 FAD A N3    1 
HETATM 18421 C C4    . FAD J 5 .    ? -43.060 55.293  81.245  1.00 12.50 ?  1308 FAD A C4    1 
HETATM 18422 O O4    . FAD J 5 .    ? -43.925 56.188  80.700  1.00 13.65 ?  1308 FAD A O4    1 
HETATM 18423 C C4X   . FAD J 5 .    ? -42.702 54.069  80.501  1.00 12.58 ?  1308 FAD A C4X   1 
HETATM 18424 N N5    . FAD J 5 .    ? -43.289 53.784  79.224  1.00 13.60 ?  1308 FAD A N5    1 
HETATM 18425 C C5X   . FAD J 5 .    ? -43.043 52.466  78.692  1.00 13.75 ?  1308 FAD A C5X   1 
HETATM 18426 C C6    . FAD J 5 .    ? -43.829 52.016  77.536  1.00 13.57 ?  1308 FAD A C6    1 
HETATM 18427 C C7    . FAD J 5 .    ? -43.618 50.728  77.033  1.00 15.49 ?  1308 FAD A C7    1 
HETATM 18428 C C7M   . FAD J 5 .    ? -44.429 50.298  75.848  1.00 15.31 ?  1308 FAD A C7M   1 
HETATM 18429 C C8    . FAD J 5 .    ? -42.672 49.844  77.628  1.00 15.05 ?  1308 FAD A C8    1 
HETATM 18430 C C8M   . FAD J 5 .    ? -42.470 48.465  77.058  1.00 18.51 ?  1308 FAD A C8M   1 
HETATM 18431 C C9    . FAD J 5 .    ? -41.922 50.270  78.737  1.00 15.43 ?  1308 FAD A C9    1 
HETATM 18432 C C9A   . FAD J 5 .    ? -42.142 51.621  79.262  1.00 13.06 ?  1308 FAD A C9A   1 
HETATM 18433 N N10   . FAD J 5 .    ? -41.372 52.057  80.379  1.00 16.10 ?  1308 FAD A N10   1 
HETATM 18434 C C10   . FAD J 5 .    ? -41.830 53.193  81.086  1.00 14.03 ?  1308 FAD A C10   1 
HETATM 18435 C "C1'" . FAD J 5 .    ? -40.178 51.318  80.849  1.00 18.18 ?  1308 FAD A "C1'" 1 
HETATM 18436 C "C2'" . FAD J 5 .    ? -40.650 50.241  81.802  1.00 17.88 ?  1308 FAD A "C2'" 1 
HETATM 18437 O "O2'" . FAD J 5 .    ? -41.137 50.824  82.944  1.00 19.18 ?  1308 FAD A "O2'" 1 
HETATM 18438 C "C3'" . FAD J 5 .    ? -39.552 49.260  82.219  1.00 20.55 ?  1308 FAD A "C3'" 1 
HETATM 18439 O "O3'" . FAD J 5 .    ? -38.477 49.965  82.748  1.00 21.24 ?  1308 FAD A "O3'" 1 
HETATM 18440 C "C4'" . FAD J 5 .    ? -39.019 48.327  81.136  1.00 22.98 ?  1308 FAD A "C4'" 1 
HETATM 18441 O "O4'" . FAD J 5 .    ? -39.955 48.074  80.134  1.00 32.61 ?  1308 FAD A "O4'" 1 
HETATM 18442 C "C5'" . FAD J 5 .    ? -38.543 47.016  81.759  1.00 25.13 ?  1308 FAD A "C5'" 1 
HETATM 18443 O "O5'" . FAD J 5 .    ? -39.548 46.308  82.458  1.00 18.62 ?  1308 FAD A "O5'" 1 
HETATM 18444 P P     . FAD J 5 .    ? -39.955 44.912  81.810  1.00 18.78 ?  1308 FAD A P     1 
HETATM 18445 O O1P   . FAD J 5 .    ? -40.121 44.980  80.267  1.00 18.79 ?  1308 FAD A O1P   1 
HETATM 18446 O O2P   . FAD J 5 .    ? -41.207 44.489  82.676  1.00 21.33 ?  1308 FAD A O2P   1 
HETATM 18447 O O3P   . FAD J 5 .    ? -38.764 43.892  82.316  1.00 17.52 ?  1308 FAD A O3P   1 
HETATM 18448 N N     . GGL K 2 .    ? 13.564  34.595  82.227  1.00 17.74 ?  1301 GGL B N     1 
HETATM 18449 C CA    . GGL K 2 .    ? 14.486  33.845  83.046  1.00 16.17 ?  1301 GGL B CA    1 
HETATM 18450 C C     . GGL K 2 .    ? 13.976  33.858  84.451  1.00 13.73 ?  1301 GGL B C     1 
HETATM 18451 O O     . GGL K 2 .    ? 13.115  34.701  84.807  1.00 13.86 ?  1301 GGL B O     1 
HETATM 18452 C CB    . GGL K 2 .    ? 15.875  34.411  82.993  1.00 17.38 ?  1301 GGL B CB    1 
HETATM 18453 C CG    . GGL K 2 .    ? 16.415  34.420  81.590  1.00 16.82 ?  1301 GGL B CG    1 
HETATM 18454 C CD    . GGL K 2 .    ? 17.910  34.586  81.545  1.00 18.81 ?  1301 GGL B CD    1 
HETATM 18455 O OE1   . GGL K 2 .    ? 18.426  35.424  80.750  1.00 19.86 -1 1301 GGL B OE1   1 
HETATM 18456 O OE2   . GGL K 2 .    ? 18.653  33.892  82.298  1.00 18.52 ?  1301 GGL B OE2   1 
HETATM 18457 O OXT   . GGL K 2 .    ? 14.410  33.025  85.293  1.00 14.94 -1 1301 GGL B OXT   1 
HETATM 18458 S S     . SO4 L 3 .    ? -7.300  47.364  74.180  1.00 12.91 ?  1302 SO4 B S     1 
HETATM 18459 O O1    . SO4 L 3 .    ? -6.075  46.622  73.740  1.00 16.65 ?  1302 SO4 B O1    1 
HETATM 18460 O O2    . SO4 L 3 .    ? -8.049  47.847  72.990  1.00 12.18 ?  1302 SO4 B O2    1 
HETATM 18461 O O3    . SO4 L 3 .    ? -8.192  46.470  74.959  1.00 17.04 ?  1302 SO4 B O3    1 
HETATM 18462 O O4    . SO4 L 3 .    ? -6.824  48.506  75.004  1.00 17.42 ?  1302 SO4 B O4    1 
HETATM 18463 S S     . SO4 M 3 .    ? -5.223  40.577  99.562  0.50 26.71 ?  1303 SO4 B S     1 
HETATM 18464 O O1    . SO4 M 3 .    ? -3.896  41.199  99.249  0.50 29.42 ?  1303 SO4 B O1    1 
HETATM 18465 O O2    . SO4 M 3 .    ? -5.763  39.935  98.320  0.50 31.01 ?  1303 SO4 B O2    1 
HETATM 18466 O O3    . SO4 M 3 .    ? -5.051  39.532  100.623 0.50 28.08 ?  1303 SO4 B O3    1 
HETATM 18467 O O4    . SO4 M 3 .    ? -6.178  41.628  100.043 0.50 30.88 ?  1303 SO4 B O4    1 
HETATM 18468 S S     . SO4 N 3 .    ? 17.915  45.320  113.754 0.63 25.87 ?  1304 SO4 B S     1 
HETATM 18469 O O1    . SO4 N 3 .    ? 17.546  44.058  113.033 0.63 20.90 ?  1304 SO4 B O1    1 
HETATM 18470 O O2    . SO4 N 3 .    ? 18.225  46.439  112.806 0.63 26.14 ?  1304 SO4 B O2    1 
HETATM 18471 O O3    . SO4 N 3 .    ? 19.103  45.042  114.625 0.63 35.62 ?  1304 SO4 B O3    1 
HETATM 18472 O O4    . SO4 N 3 .    ? 16.764  45.731  114.621 0.63 37.73 ?  1304 SO4 B O4    1 
HETATM 18473 S S     . SO4 O 3 .    ? 14.987  61.673  55.423  0.67 33.62 ?  1305 SO4 B S     1 
HETATM 18474 O O1    . SO4 O 3 .    ? 15.779  62.433  54.401  0.67 36.60 ?  1305 SO4 B O1    1 
HETATM 18475 O O2    . SO4 O 3 .    ? 14.311  60.497  54.783  0.67 43.44 ?  1305 SO4 B O2    1 
HETATM 18476 O O3    . SO4 O 3 .    ? 15.900  61.182  56.504  0.67 32.44 ?  1305 SO4 B O3    1 
HETATM 18477 O O4    . SO4 O 3 .    ? 13.952  62.589  56.004  0.67 33.74 ?  1305 SO4 B O4    1 
HETATM 18478 C C1    . PEG P 6 .    ? -7.822  30.719  72.834  1.00 31.27 ?  1306 PEG B C1    1 
HETATM 18479 O O1    . PEG P 6 .    ? -9.178  30.371  72.916  1.00 36.80 ?  1306 PEG B O1    1 
HETATM 18480 C C2    . PEG P 6 .    ? -7.350  30.516  71.395  1.00 30.83 ?  1306 PEG B C2    1 
HETATM 18481 O O2    . PEG P 6 .    ? -6.378  31.472  71.083  1.00 33.90 ?  1306 PEG B O2    1 
HETATM 18482 C C3    . PEG P 6 .    ? -5.882  31.399  69.774  1.00 32.12 ?  1306 PEG B C3    1 
HETATM 18483 C C4    . PEG P 6 .    ? -6.798  32.200  68.848  1.00 35.10 ?  1306 PEG B C4    1 
HETATM 18484 O O4    . PEG P 6 .    ? -6.310  32.162  67.535  1.00 38.44 ?  1306 PEG B O4    1 
HETATM 18485 C C1    . PGE Q 4 .    ? 2.509   53.886  87.669  1.00 29.32 ?  1307 PGE B C1    1 
HETATM 18486 O O1    . PGE Q 4 .    ? 2.001   54.427  88.857  1.00 34.55 ?  1307 PGE B O1    1 
HETATM 18487 C C2    . PGE Q 4 .    ? 3.685   54.726  87.170  1.00 27.02 ?  1307 PGE B C2    1 
HETATM 18488 O O2    . PGE Q 4 .    ? 3.334   56.079  87.052  1.00 30.52 ?  1307 PGE B O2    1 
HETATM 18489 C C3    . PGE Q 4 .    ? 4.420   56.895  86.715  1.00 23.91 ?  1307 PGE B C3    1 
HETATM 18490 C C4    . PGE Q 4 .    ? 3.954   58.330  86.486  1.00 25.38 ?  1307 PGE B C4    1 
HETATM 18491 O O4    . PGE Q 4 .    ? 0.280   59.817  88.230  1.00 37.90 ?  1307 PGE B O4    1 
HETATM 18492 C C6    . PGE Q 4 .    ? 1.562   60.349  88.431  1.00 38.78 ?  1307 PGE B C6    1 
HETATM 18493 C C5    . PGE Q 4 .    ? 2.477   59.981  87.264  1.00 34.76 ?  1307 PGE B C5    1 
HETATM 18494 O O3    . PGE Q 4 .    ? 3.087   58.742  87.504  1.00 39.16 ?  1307 PGE B O3    1 
HETATM 18495 P PA    . FAD R 5 .    ? -17.549 22.301  105.388 1.00 17.75 ?  1308 FAD B PA    1 
HETATM 18496 O O1A   . FAD R 5 .    ? -18.867 21.553  105.068 1.00 20.06 ?  1308 FAD B O1A   1 
HETATM 18497 O O2A   . FAD R 5 .    ? -17.607 23.727  105.478 1.00 18.19 ?  1308 FAD B O2A   1 
HETATM 18498 O O5B   . FAD R 5 .    ? -16.515 22.128  104.297 1.00 17.85 ?  1308 FAD B O5B   1 
HETATM 18499 C C5B   . FAD R 5 .    ? -15.464 23.037  103.993 1.00 19.57 ?  1308 FAD B C5B   1 
HETATM 18500 C C4B   . FAD R 5 .    ? -14.539 22.355  102.981 1.00 15.91 ?  1308 FAD B C4B   1 
HETATM 18501 O O4B   . FAD R 5 .    ? -15.065 22.337  101.676 1.00 16.58 ?  1308 FAD B O4B   1 
HETATM 18502 C C3B   . FAD R 5 .    ? -13.200 22.998  102.795 1.00 13.64 ?  1308 FAD B C3B   1 
HETATM 18503 O O3B   . FAD R 5 .    ? -12.332 22.820  103.853 1.00 13.90 ?  1308 FAD B O3B   1 
HETATM 18504 C C2B   . FAD R 5 .    ? -12.732 22.361  101.536 1.00 14.08 ?  1308 FAD B C2B   1 
HETATM 18505 O O2B   . FAD R 5 .    ? -12.235 21.079  101.746 1.00 15.03 ?  1308 FAD B O2B   1 
HETATM 18506 C C1B   . FAD R 5 .    ? -13.995 22.303  100.756 1.00 15.47 ?  1308 FAD B C1B   1 
HETATM 18507 N N9A   . FAD R 5 .    ? -14.181 23.386  99.806  1.00 15.18 ?  1308 FAD B N9A   1 
HETATM 18508 C C8A   . FAD R 5 .    ? -14.354 24.733  100.050 1.00 17.96 ?  1308 FAD B C8A   1 
HETATM 18509 N N7A   . FAD R 5 .    ? -14.520 25.381  98.888  1.00 16.64 ?  1308 FAD B N7A   1 
HETATM 18510 C C5A   . FAD R 5 .    ? -14.473 24.452  97.846  1.00 13.42 ?  1308 FAD B C5A   1 
HETATM 18511 C C6A   . FAD R 5 .    ? -14.607 24.538  96.467  1.00 16.20 ?  1308 FAD B C6A   1 
HETATM 18512 N N6A   . FAD R 5 .    ? -14.829 25.814  95.853  1.00 15.87 ?  1308 FAD B N6A   1 
HETATM 18513 N N1A   . FAD R 5 .    ? -14.511 23.421  95.724  1.00 14.22 ?  1308 FAD B N1A   1 
HETATM 18514 C C2A   . FAD R 5 .    ? -14.307 22.200  96.275  1.00 14.08 ?  1308 FAD B C2A   1 
HETATM 18515 N N3A   . FAD R 5 .    ? -14.193 22.079  97.637  1.00 14.46 ?  1308 FAD B N3A   1 
HETATM 18516 C C4A   . FAD R 5 .    ? -14.274 23.167  98.416  1.00 15.63 ?  1308 FAD B C4A   1 
HETATM 18517 N N1    . FAD R 5 .    ? -7.754  18.279  106.242 1.00 13.16 ?  1308 FAD B N1    1 
HETATM 18518 C C2    . FAD R 5 .    ? -6.652  17.699  105.556 1.00 14.26 ?  1308 FAD B C2    1 
HETATM 18519 O O2    . FAD R 5 .    ? -6.414  18.069  104.281 1.00 14.40 ?  1308 FAD B O2    1 
HETATM 18520 N N3    . FAD R 5 .    ? -5.810  16.745  106.141 1.00 13.28 ?  1308 FAD B N3    1 
HETATM 18521 C C4    . FAD R 5 .    ? -6.009  16.319  107.433 1.00 13.87 ?  1308 FAD B C4    1 
HETATM 18522 O O4    . FAD R 5 .    ? -5.170  15.393  107.954 1.00 15.61 ?  1308 FAD B O4    1 
HETATM 18523 C C4X   . FAD R 5 .    ? -7.144  16.907  108.178 1.00 15.64 ?  1308 FAD B C4X   1 
HETATM 18524 N N5    . FAD R 5 .    ? -7.418  16.420  109.502 1.00 16.90 ?  1308 FAD B N5    1 
HETATM 18525 C C5X   . FAD R 5 .    ? -8.649  16.879  110.090 1.00 15.21 ?  1308 FAD B C5X   1 
HETATM 18526 C C6    . FAD R 5 .    ? -9.081  16.241  111.350 1.00 14.62 ?  1308 FAD B C6    1 
HETATM 18527 C C7    . FAD R 5 .    ? -10.284 16.678  111.920 1.00 16.14 ?  1308 FAD B C7    1 
HETATM 18528 C C7M   . FAD R 5 .    ? -10.752 16.046  113.205 1.00 16.59 ?  1308 FAD B C7M   1 
HETATM 18529 C C8    . FAD R 5 .    ? -11.076 17.697  111.329 1.00 14.39 ?  1308 FAD B C8    1 
HETATM 18530 C C8M   . FAD R 5 .    ? -12.371 18.171  111.941 1.00 19.31 ?  1308 FAD B C8M   1 
HETATM 18531 C C9    . FAD R 5 .    ? -10.666 18.302  110.133 1.00 17.69 ?  1308 FAD B C9    1 
HETATM 18532 C C9A   . FAD R 5 .    ? -9.414  17.850  109.538 1.00 15.90 ?  1308 FAD B C9A   1 
HETATM 18533 N N10   . FAD R 5 .    ? -9.016  18.469  108.306 1.00 17.89 ?  1308 FAD B N10   1 
HETATM 18534 C C10   . FAD R 5 .    ? -7.960  17.846  107.591 1.00 14.49 ?  1308 FAD B C10   1 
HETATM 18535 C "C1'" . FAD R 5 .    ? -9.626  19.724  107.833 1.00 23.20 ?  1308 FAD B "C1'" 1 
HETATM 18536 C "C2'" . FAD R 5 .    ? -10.783 19.273  106.979 1.00 19.06 ?  1308 FAD B "C2'" 1 
HETATM 18537 O "O2'" . FAD R 5 .    ? -10.300 18.598  105.868 1.00 22.51 ?  1308 FAD B "O2'" 1 
HETATM 18538 C "C3'" . FAD R 5 .    ? -11.663 20.419  106.510 1.00 24.68 ?  1308 FAD B "C3'" 1 
HETATM 18539 O "O3'" . FAD R 5 .    ? -10.819 21.348  105.931 1.00 27.19 ?  1308 FAD B "O3'" 1 
HETATM 18540 C "C4'" . FAD R 5 .    ? -12.517 21.140  107.541 1.00 31.63 ?  1308 FAD B "C4'" 1 
HETATM 18541 O "O4'" . FAD R 5 .    ? -12.800 20.342  108.650 1.00 32.49 ?  1308 FAD B "O4'" 1 
HETATM 18542 C "C5'" . FAD R 5 .    ? -13.785 21.711  106.904 1.00 28.39 ?  1308 FAD B "C5'" 1 
HETATM 18543 O "O5'" . FAD R 5 .    ? -14.695 20.762  106.390 1.00 17.90 ?  1308 FAD B "O5'" 1 
HETATM 18544 P P     . FAD R 5 .    ? -16.087 20.657  107.188 1.00 19.80 ?  1308 FAD B P     1 
HETATM 18545 O O1P   . FAD R 5 .    ? -15.866 20.668  108.745 1.00 18.60 ?  1308 FAD B O1P   1 
HETATM 18546 O O2P   . FAD R 5 .    ? -16.878 19.464  106.524 1.00 24.11 ?  1308 FAD B O2P   1 
HETATM 18547 O O3P   . FAD R 5 .    ? -16.833 21.981  106.661 1.00 17.44 ?  1308 FAD B O3P   1 
HETATM 18548 O O     . HOH S 7 .    ? 16.665  57.716  104.061 1.00 20.52 ?  1401 HOH A O     1 
HETATM 18549 O O     . HOH S 7 .    ? -51.934 73.757  69.119  1.00 27.29 ?  1402 HOH A O     1 
HETATM 18550 O O     . HOH S 7 .    ? -25.529 60.613  129.080 1.00 31.64 ?  1403 HOH A O     1 
HETATM 18551 O O     . HOH S 7 .    ? -39.127 67.385  69.817  1.00 29.58 ?  1404 HOH A O     1 
HETATM 18552 O O     . HOH S 7 .    ? -30.772 50.068  105.939 1.00 23.92 ?  1405 HOH A O     1 
HETATM 18553 O O     . HOH S 7 .    ? -18.706 70.853  70.162  1.00 35.65 ?  1406 HOH A O     1 
HETATM 18554 O O     . HOH S 7 .    ? -52.967 61.343  102.912 1.00 23.56 ?  1407 HOH A O     1 
HETATM 18555 O O     . HOH S 7 .    ? -29.876 47.354  64.368  1.00 37.53 ?  1408 HOH A O     1 
HETATM 18556 O O     . HOH S 7 .    ? -47.522 75.451  67.718  1.00 29.56 ?  1409 HOH A O     1 
HETATM 18557 O O     . HOH S 7 .    ? -2.420  67.629  126.344 1.00 35.13 ?  1410 HOH A O     1 
HETATM 18558 O O     . HOH S 7 .    ? -5.046  71.443  96.829  1.00 29.81 ?  1411 HOH A O     1 
HETATM 18559 O O     . HOH S 7 .    ? -36.433 55.477  79.568  1.00 30.04 ?  1412 HOH A O     1 
HETATM 18560 O O     . HOH S 7 .    ? -4.196  79.321  105.224 1.00 24.92 ?  1413 HOH A O     1 
HETATM 18561 O O     . HOH S 7 .    ? -42.973 38.468  86.275  1.00 25.59 ?  1414 HOH A O     1 
HETATM 18562 O O     . HOH S 7 .    ? -47.519 77.391  69.777  1.00 22.36 ?  1415 HOH A O     1 
HETATM 18563 O O     . HOH S 7 .    ? -11.165 91.990  115.525 1.00 32.14 ?  1416 HOH A O     1 
HETATM 18564 O O     . HOH S 7 .    ? -0.213  82.235  114.942 1.00 29.64 ?  1417 HOH A O     1 
HETATM 18565 O O     . HOH S 7 .    ? -0.631  63.509  111.172 1.00 18.19 ?  1418 HOH A O     1 
HETATM 18566 O O     . HOH S 7 .    ? -31.325 67.147  99.745  1.00 31.75 ?  1419 HOH A O     1 
HETATM 18567 O O     . HOH S 7 .    ? -29.454 57.435  116.815 1.00 28.64 ?  1420 HOH A O     1 
HETATM 18568 O O     . HOH S 7 .    ? -5.082  70.403  77.495  1.00 36.22 ?  1421 HOH A O     1 
HETATM 18569 O O     . HOH S 7 .    ? -44.575 76.463  75.287  1.00 26.37 ?  1422 HOH A O     1 
HETATM 18570 O O     . HOH S 7 .    ? -33.265 96.044  127.389 1.00 35.59 ?  1423 HOH A O     1 
HETATM 18571 O O     . HOH S 7 .    ? -58.111 64.738  92.016  1.00 28.47 ?  1424 HOH A O     1 
HETATM 18572 O O     . HOH S 7 .    ? -24.129 65.308  131.361 1.00 33.06 ?  1425 HOH A O     1 
HETATM 18573 O O     . HOH S 7 .    ? 26.171  71.704  106.577 1.00 32.60 ?  1426 HOH A O     1 
HETATM 18574 O O     . HOH S 7 .    ? -4.297  69.435  108.041 1.00 25.45 ?  1427 HOH A O     1 
HETATM 18575 O O     . HOH S 7 .    ? -41.918 71.490  65.075  1.00 26.03 ?  1428 HOH A O     1 
HETATM 18576 O O     . HOH S 7 .    ? -47.415 34.871  88.497  1.00 33.37 ?  1429 HOH A O     1 
HETATM 18577 O O     . HOH S 7 .    ? -33.607 71.492  77.655  1.00 34.27 ?  1430 HOH A O     1 
HETATM 18578 O O     . HOH S 7 .    ? 0.035   93.139  106.049 1.00 27.72 ?  1431 HOH A O     1 
HETATM 18579 O O     . HOH S 7 .    ? -25.956 96.158  125.533 1.00 33.30 ?  1432 HOH A O     1 
HETATM 18580 O O     . HOH S 7 .    ? -59.260 37.809  77.584  1.00 33.51 ?  1433 HOH A O     1 
HETATM 18581 O O     . HOH S 7 .    ? -0.614  59.915  96.111  1.00 25.86 ?  1434 HOH A O     1 
HETATM 18582 O O     . HOH S 7 .    ? -27.818 88.214  75.977  1.00 33.31 ?  1435 HOH A O     1 
HETATM 18583 O O     . HOH S 7 .    ? -57.033 39.946  92.985  1.00 35.12 ?  1436 HOH A O     1 
HETATM 18584 O O     . HOH S 7 .    ? -6.506  68.422  93.524  1.00 22.86 ?  1437 HOH A O     1 
HETATM 18585 O O     . HOH S 7 .    ? -18.579 50.659  85.882  1.00 32.85 ?  1438 HOH A O     1 
HETATM 18586 O O     . HOH S 7 .    ? -12.875 53.848  111.835 1.00 30.21 ?  1439 HOH A O     1 
HETATM 18587 O O     . HOH S 7 .    ? -10.568 67.361  126.088 1.00 31.42 ?  1440 HOH A O     1 
HETATM 18588 O O     . HOH S 7 .    ? -38.958 37.913  89.164  1.00 33.24 ?  1441 HOH A O     1 
HETATM 18589 O O     . HOH S 7 .    ? -21.857 66.329  71.303  1.00 37.23 ?  1442 HOH A O     1 
HETATM 18590 O O     . HOH S 7 .    ? -46.038 89.439  107.289 1.00 35.30 ?  1443 HOH A O     1 
HETATM 18591 O O     . HOH S 7 .    ? 25.601  79.837  109.055 1.00 30.34 ?  1444 HOH A O     1 
HETATM 18592 O O     . HOH S 7 .    ? -30.503 62.962  92.965  1.00 28.19 ?  1445 HOH A O     1 
HETATM 18593 O O     . HOH S 7 .    ? -11.959 63.271  114.553 1.00 15.80 ?  1446 HOH A O     1 
HETATM 18594 O O     . HOH S 7 .    ? -27.264 97.069  90.141  1.00 31.90 ?  1447 HOH A O     1 
HETATM 18595 O O     . HOH S 7 .    ? -4.343  78.859  113.312 1.00 29.49 ?  1448 HOH A O     1 
HETATM 18596 O O     . HOH S 7 .    ? -55.474 32.980  72.750  1.00 31.34 ?  1449 HOH A O     1 
HETATM 18597 O O     . HOH S 7 .    ? -56.869 34.331  87.792  1.00 31.92 ?  1450 HOH A O     1 
HETATM 18598 O O     . HOH S 7 .    ? 7.559   91.294  115.218 1.00 29.44 ?  1451 HOH A O     1 
HETATM 18599 O O     . HOH S 7 .    ? -25.110 65.079  95.611  1.00 23.90 ?  1452 HOH A O     1 
HETATM 18600 O O     . HOH S 7 .    ? -7.302  50.229  77.628  1.00 23.38 ?  1453 HOH A O     1 
HETATM 18601 O O     . HOH S 7 .    ? 16.184  61.100  117.449 1.00 31.55 ?  1454 HOH A O     1 
HETATM 18602 O O     . HOH S 7 .    ? -36.935 64.412  63.866  1.00 29.07 ?  1455 HOH A O     1 
HETATM 18603 O O     . HOH S 7 .    ? -25.449 59.013  74.638  1.00 25.47 ?  1456 HOH A O     1 
HETATM 18604 O O     . HOH S 7 .    ? -52.495 47.049  69.946  1.00 27.18 ?  1457 HOH A O     1 
HETATM 18605 O O     . HOH S 7 .    ? -35.640 40.271  93.398  1.00 24.38 ?  1458 HOH A O     1 
HETATM 18606 O O     . HOH S 7 .    ? -55.474 56.281  65.669  1.00 17.06 ?  1459 HOH A O     1 
HETATM 18607 O O     . HOH S 7 .    ? -14.523 61.392  108.921 1.00 23.50 ?  1460 HOH A O     1 
HETATM 18608 O O     . HOH S 7 .    ? -19.583 72.876  98.802  1.00 13.80 ?  1461 HOH A O     1 
HETATM 18609 O O     . HOH S 7 .    ? 8.121   89.697  121.720 1.00 27.27 ?  1462 HOH A O     1 
HETATM 18610 O O     . HOH S 7 .    ? -38.073 61.745  81.955  1.00 22.55 ?  1463 HOH A O     1 
HETATM 18611 O O     . HOH S 7 .    ? -0.214  76.617  124.414 1.00 36.32 ?  1464 HOH A O     1 
HETATM 18612 O O     . HOH S 7 .    ? -5.966  53.466  111.995 1.00 13.16 ?  1465 HOH A O     1 
HETATM 18613 O O     . HOH S 7 .    ? -26.182 69.830  132.587 1.00 33.65 ?  1466 HOH A O     1 
HETATM 18614 O O     . HOH S 7 .    ? 21.697  67.912  117.819 1.00 22.71 ?  1467 HOH A O     1 
HETATM 18615 O O     . HOH S 7 .    ? -41.466 48.500  64.924  1.00 23.13 ?  1468 HOH A O     1 
HETATM 18616 O O     . HOH S 7 .    ? -32.571 80.168  100.728 1.00 20.35 ?  1469 HOH A O     1 
HETATM 18617 O O     . HOH S 7 .    ? -56.442 36.429  77.576  1.00 34.73 ?  1470 HOH A O     1 
HETATM 18618 O O     . HOH S 7 .    ? -24.625 47.766  99.480  1.00 34.43 ?  1471 HOH A O     1 
HETATM 18619 O O     . HOH S 7 .    ? -38.476 62.408  56.841  1.00 30.52 ?  1472 HOH A O     1 
HETATM 18620 O O     . HOH S 7 .    ? -38.345 48.826  77.913  1.00 23.77 ?  1473 HOH A O     1 
HETATM 18621 O O     . HOH S 7 .    ? -1.216  73.194  89.961  1.00 32.54 ?  1474 HOH A O     1 
HETATM 18622 O O     . HOH S 7 .    ? -41.823 86.029  115.155 1.00 27.69 ?  1475 HOH A O     1 
HETATM 18623 O O     . HOH S 7 .    ? -39.419 52.562  106.730 1.00 31.92 ?  1476 HOH A O     1 
HETATM 18624 O O     . HOH S 7 .    ? -23.332 57.099  85.126  1.00 23.10 ?  1477 HOH A O     1 
HETATM 18625 O O     . HOH S 7 .    ? -34.588 77.126  97.635  1.00 23.79 ?  1478 HOH A O     1 
HETATM 18626 O O     . HOH S 7 .    ? -21.409 56.645  54.342  1.00 31.15 ?  1479 HOH A O     1 
HETATM 18627 O O     . HOH S 7 .    ? -19.247 70.178  88.833  1.00 21.70 ?  1480 HOH A O     1 
HETATM 18628 O O     . HOH S 7 .    ? -63.483 43.755  83.424  1.00 32.49 ?  1481 HOH A O     1 
HETATM 18629 O O     . HOH S 7 .    ? -24.361 83.307  113.533 1.00 20.32 ?  1482 HOH A O     1 
HETATM 18630 O O     . HOH S 7 .    ? -27.039 38.367  79.265  1.00 34.07 ?  1483 HOH A O     1 
HETATM 18631 O O     . HOH S 7 .    ? -26.238 50.790  106.443 1.00 31.52 ?  1484 HOH A O     1 
HETATM 18632 O O     . HOH S 7 .    ? -10.980 69.145  135.069 1.00 31.66 ?  1485 HOH A O     1 
HETATM 18633 O O     . HOH S 7 .    ? -23.449 62.519  67.528  1.00 24.80 ?  1486 HOH A O     1 
HETATM 18634 O O     . HOH S 7 .    ? -40.244 57.120  89.078  1.00 13.16 ?  1487 HOH A O     1 
HETATM 18635 O O     . HOH S 7 .    ? -6.898  58.364  121.346 1.00 18.63 ?  1488 HOH A O     1 
HETATM 18636 O O     . HOH S 7 .    ? -10.944 49.499  111.229 1.00 19.35 ?  1489 HOH A O     1 
HETATM 18637 O O     . HOH S 7 .    ? -69.124 56.365  83.626  1.00 28.81 ?  1490 HOH A O     1 
HETATM 18638 O O     . HOH S 7 .    ? -11.972 68.594  77.434  1.00 24.22 ?  1491 HOH A O     1 
HETATM 18639 O O     . HOH S 7 .    ? -13.631 55.057  104.519 1.00 29.43 ?  1492 HOH A O     1 
HETATM 18640 O O     . HOH S 7 .    ? -20.209 54.859  108.292 1.00 27.94 ?  1493 HOH A O     1 
HETATM 18641 O O     . HOH S 7 .    ? -3.890  70.426  118.784 1.00 23.34 ?  1494 HOH A O     1 
HETATM 18642 O O     . HOH S 7 .    ? -62.419 57.150  64.531  1.00 26.31 ?  1495 HOH A O     1 
HETATM 18643 O O     . HOH S 7 .    ? -26.732 50.782  57.466  1.00 31.12 ?  1496 HOH A O     1 
HETATM 18644 O O     . HOH S 7 .    ? -39.104 73.281  91.383  1.00 26.97 ?  1497 HOH A O     1 
HETATM 18645 O O     . HOH S 7 .    ? -38.898 62.615  106.672 1.00 30.02 ?  1498 HOH A O     1 
HETATM 18646 O O     . HOH S 7 .    ? -2.515  74.329  85.494  1.00 27.25 ?  1499 HOH A O     1 
HETATM 18647 O O     . HOH S 7 .    ? -29.990 37.618  86.794  1.00 36.53 ?  1500 HOH A O     1 
HETATM 18648 O O     . HOH S 7 .    ? -49.072 56.837  105.747 1.00 33.77 ?  1501 HOH A O     1 
HETATM 18649 O O     . HOH S 7 .    ? 6.726   53.820  102.683 1.00 16.24 ?  1502 HOH A O     1 
HETATM 18650 O O     . HOH S 7 .    ? -40.009 78.613  101.432 1.00 21.57 ?  1503 HOH A O     1 
HETATM 18651 O O     . HOH S 7 .    ? 4.907   80.415  130.620 1.00 35.24 ?  1504 HOH A O     1 
HETATM 18652 O O     . HOH S 7 .    ? -43.653 80.575  90.745  1.00 26.95 ?  1505 HOH A O     1 
HETATM 18653 O O     . HOH S 7 .    ? 4.028   93.193  105.630 1.00 26.10 ?  1506 HOH A O     1 
HETATM 18654 O O     . HOH S 7 .    ? -13.481 55.346  82.505  1.00 23.10 ?  1507 HOH A O     1 
HETATM 18655 O O     . HOH S 7 .    ? -38.379 65.121  89.349  1.00 26.92 ?  1508 HOH A O     1 
HETATM 18656 O O     . HOH S 7 .    ? -9.212  88.182  100.015 1.00 32.59 ?  1509 HOH A O     1 
HETATM 18657 O O     . HOH S 7 .    ? -31.529 47.243  76.925  1.00 31.11 ?  1510 HOH A O     1 
HETATM 18658 O O     . HOH S 7 .    ? -22.514 67.480  82.337  1.00 23.75 ?  1511 HOH A O     1 
HETATM 18659 O O     . HOH S 7 .    ? -42.898 60.136  75.002  1.00 26.48 ?  1512 HOH A O     1 
HETATM 18660 O O     . HOH S 7 .    ? -35.799 76.293  93.734  1.00 27.95 ?  1513 HOH A O     1 
HETATM 18661 O O     . HOH S 7 .    ? -48.784 81.313  85.713  1.00 30.70 ?  1514 HOH A O     1 
HETATM 18662 O O     . HOH S 7 .    ? -41.567 71.860  115.592 1.00 24.56 ?  1515 HOH A O     1 
HETATM 18663 O O     . HOH S 7 .    ? -35.080 67.142  126.851 1.00 27.16 ?  1516 HOH A O     1 
HETATM 18664 O O     . HOH S 7 .    ? -46.030 86.925  112.927 1.00 37.95 ?  1517 HOH A O     1 
HETATM 18665 O O     . HOH S 7 .    ? -6.470  82.620  104.575 1.00 20.14 ?  1518 HOH A O     1 
HETATM 18666 O O     . HOH S 7 .    ? -3.203  89.914  110.529 1.00 25.53 ?  1519 HOH A O     1 
HETATM 18667 O O     . HOH S 7 .    ? -67.138 67.534  72.938  1.00 29.40 ?  1520 HOH A O     1 
HETATM 18668 O O     . HOH S 7 .    ? 12.580  74.085  92.906  1.00 30.71 ?  1521 HOH A O     1 
HETATM 18669 O O     . HOH S 7 .    ? -24.641 93.019  128.449 1.00 31.41 ?  1522 HOH A O     1 
HETATM 18670 O O     . HOH S 7 .    ? -26.426 69.037  99.893  1.00 33.84 ?  1523 HOH A O     1 
HETATM 18671 O O     . HOH S 7 .    ? -31.850 58.469  116.842 1.00 33.02 ?  1524 HOH A O     1 
HETATM 18672 O O     . HOH S 7 .    ? -17.996 59.043  87.422  1.00 22.50 ?  1525 HOH A O     1 
HETATM 18673 O O     . HOH S 7 .    ? -9.654  64.933  77.498  1.00 16.76 ?  1526 HOH A O     1 
HETATM 18674 O O     . HOH S 7 .    ? -38.100 77.875  121.745 1.00 31.87 ?  1527 HOH A O     1 
HETATM 18675 O O     . HOH S 7 .    ? -23.522 63.815  99.064  1.00 16.10 ?  1528 HOH A O     1 
HETATM 18676 O O     . HOH S 7 .    ? -32.629 75.919  96.028  1.00 29.27 ?  1529 HOH A O     1 
HETATM 18677 O O     . HOH S 7 .    ? -23.779 63.832  107.337 1.00 17.98 ?  1530 HOH A O     1 
HETATM 18678 O O     . HOH S 7 .    ? -36.083 51.491  70.413  1.00 30.19 ?  1531 HOH A O     1 
HETATM 18679 O O     . HOH S 7 .    ? -51.941 55.021  76.851  1.00 16.43 ?  1532 HOH A O     1 
HETATM 18680 O O     . HOH S 7 .    ? -22.544 96.251  131.133 1.00 39.76 ?  1533 HOH A O     1 
HETATM 18681 O O     . HOH S 7 .    ? -14.960 48.621  76.754  1.00 23.72 ?  1534 HOH A O     1 
HETATM 18682 O O     . HOH S 7 .    ? -25.262 66.826  87.323  1.00 26.54 ?  1535 HOH A O     1 
HETATM 18683 O O     . HOH S 7 .    ? -14.592 75.962  110.945 1.00 17.00 ?  1536 HOH A O     1 
HETATM 18684 O O     . HOH S 7 .    ? -27.448 53.841  110.991 1.00 23.64 ?  1537 HOH A O     1 
HETATM 18685 O O     . HOH S 7 .    ? -20.785 60.238  84.187  1.00 30.10 ?  1538 HOH A O     1 
HETATM 18686 O O     . HOH S 7 .    ? -54.800 37.408  90.865  1.00 34.35 ?  1539 HOH A O     1 
HETATM 18687 O O     . HOH S 7 .    ? -43.382 47.901  61.164  1.00 24.69 ?  1540 HOH A O     1 
HETATM 18688 O O     . HOH S 7 .    ? -41.659 27.355  71.868  1.00 35.18 ?  1541 HOH A O     1 
HETATM 18689 O O     . HOH S 7 .    ? -45.040 63.215  82.373  1.00 13.98 ?  1542 HOH A O     1 
HETATM 18690 O O     . HOH S 7 .    ? -5.353  54.483  109.504 1.00 16.80 ?  1543 HOH A O     1 
HETATM 18691 O O     . HOH S 7 .    ? -35.014 63.811  82.476  1.00 30.18 ?  1544 HOH A O     1 
HETATM 18692 O O     . HOH S 7 .    ? -51.111 69.866  101.400 1.00 18.65 ?  1545 HOH A O     1 
HETATM 18693 O O     . HOH S 7 .    ? -28.573 61.963  103.358 1.00 13.81 ?  1546 HOH A O     1 
HETATM 18694 O O     . HOH S 7 .    ? -24.134 63.465  92.745  1.00 17.25 ?  1547 HOH A O     1 
HETATM 18695 O O     . HOH S 7 .    ? -19.210 61.340  86.444  1.00 17.96 ?  1548 HOH A O     1 
HETATM 18696 O O     . HOH S 7 .    ? -12.095 77.073  104.351 1.00 26.63 ?  1549 HOH A O     1 
HETATM 18697 O O     . HOH S 7 .    ? -32.641 48.381  85.302  1.00 25.84 ?  1550 HOH A O     1 
HETATM 18698 O O     . HOH S 7 .    ? -14.971 63.961  100.664 1.00 19.92 ?  1551 HOH A O     1 
HETATM 18699 O O     . HOH S 7 .    ? -46.167 76.181  95.297  1.00 21.90 ?  1552 HOH A O     1 
HETATM 18700 O O     . HOH S 7 .    ? 14.409  60.957  95.904  1.00 26.20 ?  1553 HOH A O     1 
HETATM 18701 O O     . HOH S 7 .    ? -18.061 82.901  97.638  1.00 20.43 ?  1554 HOH A O     1 
HETATM 18702 O O     . HOH S 7 .    ? -66.017 47.638  86.613  1.00 34.00 ?  1555 HOH A O     1 
HETATM 18703 O O     . HOH S 7 .    ? -12.128 73.131  129.917 1.00 25.64 ?  1556 HOH A O     1 
HETATM 18704 O O     . HOH S 7 .    ? -70.663 61.245  86.415  1.00 28.78 ?  1557 HOH A O     1 
HETATM 18705 O O     . HOH S 7 .    ? -60.010 53.939  75.628  1.00 16.21 ?  1558 HOH A O     1 
HETATM 18706 O O     . HOH S 7 .    ? -28.960 61.834  118.150 1.00 17.51 ?  1559 HOH A O     1 
HETATM 18707 O O     . HOH S 7 .    ? -19.456 59.092  105.750 1.00 21.56 ?  1560 HOH A O     1 
HETATM 18708 O O     . HOH S 7 .    ? -41.016 71.754  118.320 1.00 30.76 ?  1561 HOH A O     1 
HETATM 18709 O O     . HOH S 7 .    ? 13.844  82.012  115.721 1.00 22.66 ?  1562 HOH A O     1 
HETATM 18710 O O     . HOH S 7 .    ? -45.239 63.447  85.221  1.00 15.79 ?  1563 HOH A O     1 
HETATM 18711 O O     . HOH S 7 .    ? 6.520   90.631  108.258 1.00 32.66 ?  1564 HOH A O     1 
HETATM 18712 O O     . HOH S 7 .    ? -58.745 65.494  95.317  1.00 24.80 ?  1565 HOH A O     1 
HETATM 18713 O O     . HOH S 7 .    ? 19.267  81.912  114.807 1.00 28.35 ?  1566 HOH A O     1 
HETATM 18714 O O     . HOH S 7 .    ? -66.335 58.651  76.765  1.00 16.60 ?  1567 HOH A O     1 
HETATM 18715 O O     . HOH S 7 .    ? -3.485  57.293  69.093  1.00 29.48 ?  1568 HOH A O     1 
HETATM 18716 O O     . HOH S 7 .    ? -1.589  57.958  97.961  1.00 25.96 ?  1569 HOH A O     1 
HETATM 18717 O O     . HOH S 7 .    ? -28.620 77.885  102.585 1.00 21.62 ?  1570 HOH A O     1 
HETATM 18718 O O     . HOH S 7 .    ? -51.222 50.234  58.301  1.00 27.86 ?  1571 HOH A O     1 
HETATM 18719 O O     . HOH S 7 .    ? 5.550   62.897  98.560  1.00 17.26 ?  1572 HOH A O     1 
HETATM 18720 O O     . HOH S 7 .    ? -60.961 59.666  91.523  1.00 18.33 ?  1573 HOH A O     1 
HETATM 18721 O O     . HOH S 7 .    ? -8.377  59.839  95.387  1.00 28.08 ?  1574 HOH A O     1 
HETATM 18722 O O     . HOH S 7 .    ? -53.257 23.879  84.248  1.00 38.97 ?  1575 HOH A O     1 
HETATM 18723 O O     . HOH S 7 .    ? -42.031 64.143  104.610 1.00 19.32 ?  1576 HOH A O     1 
HETATM 18724 O O     . HOH S 7 .    ? -37.257 80.643  79.949  1.00 16.98 ?  1577 HOH A O     1 
HETATM 18725 O O     . HOH S 7 .    ? -37.967 63.720  68.071  1.00 23.46 ?  1578 HOH A O     1 
HETATM 18726 O O     . HOH S 7 .    ? -44.748 31.348  85.607  1.00 27.72 ?  1579 HOH A O     1 
HETATM 18727 O O     . HOH S 7 .    ? -1.436  78.197  115.924 1.00 22.91 ?  1580 HOH A O     1 
HETATM 18728 O O     . HOH S 7 .    ? -57.287 45.587  72.252  1.00 20.56 ?  1581 HOH A O     1 
HETATM 18729 O O     . HOH S 7 .    ? -8.632  82.319  106.197 1.00 24.85 ?  1582 HOH A O     1 
HETATM 18730 O O     . HOH S 7 .    ? -32.748 93.049  105.035 1.00 23.17 ?  1583 HOH A O     1 
HETATM 18731 O O     . HOH S 7 .    ? -39.434 78.518  98.810  1.00 22.76 ?  1584 HOH A O     1 
HETATM 18732 O O     . HOH S 7 .    ? -25.115 89.044  100.849 1.00 20.96 ?  1585 HOH A O     1 
HETATM 18733 O O     . HOH S 7 .    ? -53.478 63.757  99.289  1.00 19.74 ?  1586 HOH A O     1 
HETATM 18734 O O     . HOH S 7 .    ? -32.275 84.352  100.572 1.00 18.12 ?  1587 HOH A O     1 
HETATM 18735 O O     . HOH S 7 .    ? -7.298  80.437  129.346 1.00 32.44 ?  1588 HOH A O     1 
HETATM 18736 O O     . HOH S 7 .    ? -31.518 71.812  83.675  1.00 30.28 ?  1589 HOH A O     1 
HETATM 18737 O O     . HOH S 7 .    ? -44.689 41.711  105.825 1.00 31.99 ?  1590 HOH A O     1 
HETATM 18738 O O     . HOH S 7 .    ? -26.717 56.419  109.266 1.00 19.87 ?  1591 HOH A O     1 
HETATM 18739 O O     . HOH S 7 .    ? -70.320 64.937  74.724  1.00 22.33 ?  1592 HOH A O     1 
HETATM 18740 O O     . HOH S 7 .    ? -13.524 59.208  123.816 1.00 21.80 ?  1593 HOH A O     1 
HETATM 18741 O O     . HOH S 7 .    ? -50.254 35.404  89.535  1.00 31.91 ?  1594 HOH A O     1 
HETATM 18742 O O     . HOH S 7 .    ? 0.377   85.340  104.275 1.00 23.10 ?  1595 HOH A O     1 
HETATM 18743 O O     . HOH S 7 .    ? -8.411  93.315  107.440 1.00 25.73 ?  1596 HOH A O     1 
HETATM 18744 O O     . HOH S 7 .    ? -6.745  54.675  106.436 1.00 26.41 ?  1597 HOH A O     1 
HETATM 18745 O O     . HOH S 7 .    ? 4.923   54.941  98.105  1.00 22.29 ?  1598 HOH A O     1 
HETATM 18746 O O     . HOH S 7 .    ? -49.709 66.705  94.974  1.00 18.52 ?  1599 HOH A O     1 
HETATM 18747 O O     . HOH S 7 .    ? -0.660  83.780  111.194 1.00 30.01 ?  1600 HOH A O     1 
HETATM 18748 O O     . HOH S 7 .    ? 12.787  67.052  94.689  1.00 28.26 ?  1601 HOH A O     1 
HETATM 18749 O O     . HOH S 7 .    ? -14.371 64.517  52.115  1.00 32.87 ?  1602 HOH A O     1 
HETATM 18750 O O     . HOH S 7 .    ? -20.997 70.826  76.698  1.00 20.54 ?  1603 HOH A O     1 
HETATM 18751 O O     . HOH S 7 .    ? -31.066 91.108  108.379 1.00 24.09 ?  1604 HOH A O     1 
HETATM 18752 O O     . HOH S 7 .    ? -23.187 72.454  103.494 1.00 20.48 ?  1605 HOH A O     1 
HETATM 18753 O O     . HOH S 7 .    ? -4.412  73.072  118.260 1.00 24.50 ?  1606 HOH A O     1 
HETATM 18754 O O     . HOH S 7 .    ? -32.537 61.876  112.938 1.00 20.45 ?  1607 HOH A O     1 
HETATM 18755 O O     . HOH S 7 .    ? -18.983 86.176  110.429 1.00 25.45 ?  1608 HOH A O     1 
HETATM 18756 O O     . HOH S 7 .    ? -65.134 59.670  93.726  1.00 33.05 ?  1609 HOH A O     1 
HETATM 18757 O O     . HOH S 7 .    ? -23.041 67.541  98.757  1.00 16.90 ?  1610 HOH A O     1 
HETATM 18758 O O     . HOH S 7 .    ? -24.804 92.925  106.230 1.00 32.09 ?  1611 HOH A O     1 
HETATM 18759 O O     . HOH S 7 .    ? -18.509 39.205  69.197  1.00 35.09 ?  1612 HOH A O     1 
HETATM 18760 O O     . HOH S 7 .    ? -21.841 46.972  58.988  1.00 26.26 ?  1613 HOH A O     1 
HETATM 18761 O O     . HOH S 7 .    ? -25.082 59.639  78.701  1.00 27.12 ?  1614 HOH A O     1 
HETATM 18762 O O     . HOH S 7 .    ? -27.754 82.363  131.209 1.00 26.75 ?  1615 HOH A O     1 
HETATM 18763 O O     . HOH S 7 .    ? -19.381 96.813  95.666  1.00 35.57 ?  1616 HOH A O     1 
HETATM 18764 O O     . HOH S 7 .    ? -41.424 90.945  99.903  1.00 23.59 ?  1617 HOH A O     1 
HETATM 18765 O O     . HOH S 7 .    ? -12.701 77.252  92.160  1.00 12.69 ?  1618 HOH A O     1 
HETATM 18766 O O     . HOH S 7 .    ? -23.463 60.425  117.091 1.00 17.13 ?  1619 HOH A O     1 
HETATM 18767 O O     . HOH S 7 .    ? 1.308   72.957  117.416 1.00 25.53 ?  1620 HOH A O     1 
HETATM 18768 O O     . HOH S 7 .    ? 14.255  86.802  111.756 1.00 30.20 ?  1621 HOH A O     1 
HETATM 18769 O O     . HOH S 7 .    ? 24.459  58.265  111.261 1.00 36.97 ?  1622 HOH A O     1 
HETATM 18770 O O     . HOH S 7 .    ? -17.735 86.981  93.238  1.00 23.30 ?  1623 HOH A O     1 
HETATM 18771 O O     . HOH S 7 .    ? 17.496  78.177  121.952 1.00 31.77 ?  1624 HOH A O     1 
HETATM 18772 O O     . HOH S 7 .    ? -10.928 49.393  50.961  1.00 36.08 ?  1625 HOH A O     1 
HETATM 18773 O O     . HOH S 7 .    ? -15.683 55.333  123.015 1.00 28.96 ?  1626 HOH A O     1 
HETATM 18774 O O     . HOH S 7 .    ? -60.862 61.435  93.697  1.00 22.18 ?  1627 HOH A O     1 
HETATM 18775 O O     . HOH S 7 .    ? -34.345 90.931  123.731 1.00 29.24 ?  1628 HOH A O     1 
HETATM 18776 O O     . HOH S 7 .    ? -22.161 54.319  87.311  1.00 25.95 ?  1629 HOH A O     1 
HETATM 18777 O O     . HOH S 7 .    ? -47.410 48.831  94.366  1.00 16.83 ?  1630 HOH A O     1 
HETATM 18778 O O     . HOH S 7 .    ? -9.395  77.777  133.374 1.00 32.70 ?  1631 HOH A O     1 
HETATM 18779 O O     . HOH S 7 .    ? -27.253 64.040  72.616  1.00 31.58 ?  1632 HOH A O     1 
HETATM 18780 O O     . HOH S 7 .    ? -0.497  77.383  118.492 1.00 24.60 ?  1633 HOH A O     1 
HETATM 18781 O O     . HOH S 7 .    ? 6.943   57.178  113.819 1.00 30.08 ?  1634 HOH A O     1 
HETATM 18782 O O     . HOH S 7 .    ? -35.968 51.553  86.565  1.00 14.65 ?  1635 HOH A O     1 
HETATM 18783 O O     . HOH S 7 .    ? -42.765 47.334  82.297  1.00 15.91 ?  1636 HOH A O     1 
HETATM 18784 O O     . HOH S 7 .    ? 10.186  62.726  114.507 1.00 23.80 ?  1637 HOH A O     1 
HETATM 18785 O O     . HOH S 7 .    ? -27.899 73.202  131.048 1.00 28.28 ?  1638 HOH A O     1 
HETATM 18786 O O     . HOH S 7 .    ? -60.192 60.563  76.780  1.00 14.97 ?  1639 HOH A O     1 
HETATM 18787 O O     . HOH S 7 .    ? -39.294 64.444  97.026  1.00 25.39 ?  1640 HOH A O     1 
HETATM 18788 O O     . HOH S 7 .    ? -64.285 73.368  79.214  1.00 25.45 ?  1641 HOH A O     1 
HETATM 18789 O O     . HOH S 7 .    ? -9.320  44.901  56.538  1.00 31.88 ?  1642 HOH A O     1 
HETATM 18790 O O     . HOH S 7 .    ? -51.274 51.651  64.925  1.00 18.27 ?  1643 HOH A O     1 
HETATM 18791 O O     . HOH S 7 .    ? -1.034  50.315  58.862  1.00 22.29 ?  1644 HOH A O     1 
HETATM 18792 O O     . HOH S 7 .    ? -1.284  83.779  119.473 1.00 23.97 ?  1645 HOH A O     1 
HETATM 18793 O O     . HOH S 7 .    ? -18.133 101.186 85.322  1.00 31.61 ?  1646 HOH A O     1 
HETATM 18794 O O     . HOH S 7 .    ? -67.610 72.446  76.149  1.00 26.05 ?  1647 HOH A O     1 
HETATM 18795 O O     . HOH S 7 .    ? -10.389 81.116  92.396  1.00 21.47 ?  1648 HOH A O     1 
HETATM 18796 O O     . HOH S 7 .    ? -12.716 81.954  73.599  1.00 31.70 ?  1649 HOH A O     1 
HETATM 18797 O O     . HOH S 7 .    ? -16.971 55.748  113.581 1.00 29.66 ?  1650 HOH A O     1 
HETATM 18798 O O     . HOH S 7 .    ? -39.113 49.418  103.864 1.00 24.17 ?  1651 HOH A O     1 
HETATM 18799 O O     . HOH S 7 .    ? -7.691  42.338  62.969  1.00 26.37 ?  1652 HOH A O     1 
HETATM 18800 O O     . HOH S 7 .    ? -48.303 85.266  102.958 1.00 36.91 ?  1653 HOH A O     1 
HETATM 18801 O O     . HOH S 7 .    ? 15.089  82.986  112.704 1.00 22.19 ?  1654 HOH A O     1 
HETATM 18802 O O     . HOH S 7 .    ? -17.930 72.897  112.456 1.00 15.99 ?  1655 HOH A O     1 
HETATM 18803 O O     . HOH S 7 .    ? -36.951 95.185  94.980  1.00 32.58 ?  1656 HOH A O     1 
HETATM 18804 O O     . HOH S 7 .    ? -61.688 55.173  68.421  1.00 16.73 ?  1657 HOH A O     1 
HETATM 18805 O O     . HOH S 7 .    ? 9.227   56.571  99.050  1.00 25.46 ?  1658 HOH A O     1 
HETATM 18806 O O     . HOH S 7 .    ? 1.848   85.861  119.617 1.00 21.13 ?  1659 HOH A O     1 
HETATM 18807 O O     . HOH S 7 .    ? -11.061 67.780  109.326 1.00 13.55 ?  1660 HOH A O     1 
HETATM 18808 O O     . HOH S 7 .    ? -44.942 58.456  56.029  1.00 23.57 ?  1661 HOH A O     1 
HETATM 18809 O O     . HOH S 7 .    ? -9.653  55.964  83.612  1.00 22.69 ?  1662 HOH A O     1 
HETATM 18810 O O     . HOH S 7 .    ? -67.378 67.843  81.411  1.00 19.48 ?  1663 HOH A O     1 
HETATM 18811 O O     . HOH S 7 .    ? -43.508 85.345  98.354  1.00 24.75 ?  1664 HOH A O     1 
HETATM 18812 O O     . HOH S 7 .    ? -52.311 73.189  106.676 1.00 28.90 ?  1665 HOH A O     1 
HETATM 18813 O O     . HOH S 7 .    ? -47.621 60.229  86.168  1.00 13.54 ?  1666 HOH A O     1 
HETATM 18814 O O     . HOH S 7 .    ? -26.861 82.691  114.406 1.00 19.86 ?  1667 HOH A O     1 
HETATM 18815 O O     . HOH S 7 .    ? -62.364 57.899  71.056  1.00 17.82 ?  1668 HOH A O     1 
HETATM 18816 O O     . HOH S 7 .    ? -0.359  69.863  97.351  1.00 31.19 ?  1669 HOH A O     1 
HETATM 18817 O O     . HOH S 7 .    ? -47.947 49.122  97.199  1.00 18.92 ?  1670 HOH A O     1 
HETATM 18818 O O     . HOH S 7 .    ? -22.101 42.687  61.732  1.00 30.61 ?  1671 HOH A O     1 
HETATM 18819 O O     . HOH S 7 .    ? -32.081 58.836  64.045  1.00 23.27 ?  1672 HOH A O     1 
HETATM 18820 O O     . HOH S 7 .    ? -20.502 91.278  98.299  1.00 27.82 ?  1673 HOH A O     1 
HETATM 18821 O O     . HOH S 7 .    ? -12.345 79.210  95.699  1.00 13.84 ?  1674 HOH A O     1 
HETATM 18822 O O     . HOH S 7 .    ? -47.253 59.879  103.292 1.00 20.92 ?  1675 HOH A O     1 
HETATM 18823 O O     . HOH S 7 .    ? 4.056   73.563  117.752 1.00 24.74 ?  1676 HOH A O     1 
HETATM 18824 O O     . HOH S 7 .    ? -56.660 55.797  96.168  1.00 16.73 ?  1677 HOH A O     1 
HETATM 18825 O O     . HOH S 7 .    ? -32.371 89.345  110.107 1.00 25.85 ?  1678 HOH A O     1 
HETATM 18826 O O     . HOH S 7 .    ? -60.367 39.619  79.792  1.00 38.19 ?  1679 HOH A O     1 
HETATM 18827 O O     . HOH S 7 .    ? -51.655 64.934  95.784  1.00 19.56 ?  1680 HOH A O     1 
HETATM 18828 O O     . HOH S 7 .    ? -5.437  77.515  96.266  1.00 22.65 ?  1681 HOH A O     1 
HETATM 18829 O O     . HOH S 7 .    ? -53.557 56.610  56.091  1.00 26.70 ?  1682 HOH A O     1 
HETATM 18830 O O     . HOH S 7 .    ? -6.166  65.137  115.587 1.00 18.48 ?  1683 HOH A O     1 
HETATM 18831 O O     . HOH S 7 .    ? -36.926 58.855  95.339  1.00 15.23 ?  1684 HOH A O     1 
HETATM 18832 O O     . HOH S 7 .    ? -20.131 78.899  71.133  1.00 20.01 ?  1685 HOH A O     1 
HETATM 18833 O O     . HOH S 7 .    ? -58.167 57.896  102.233 1.00 22.24 ?  1686 HOH A O     1 
HETATM 18834 O O     . HOH S 7 .    ? -55.647 47.283  70.981  1.00 22.58 ?  1687 HOH A O     1 
HETATM 18835 O O     . HOH S 7 .    ? -46.162 65.181  92.771  1.00 15.04 ?  1688 HOH A O     1 
HETATM 18836 O O     . HOH S 7 .    ? -38.841 36.015  83.842  1.00 31.50 ?  1689 HOH A O     1 
HETATM 18837 O O     . HOH S 7 .    ? 17.997  58.733  96.884  1.00 28.20 ?  1690 HOH A O     1 
HETATM 18838 O O     . HOH S 7 .    ? -6.297  76.153  112.530 1.00 17.33 ?  1691 HOH A O     1 
HETATM 18839 O O     . HOH S 7 .    ? -46.849 67.244  60.534  1.00 22.80 ?  1692 HOH A O     1 
HETATM 18840 O O     . HOH S 7 .    ? -18.642 60.726  68.035  1.00 20.25 ?  1693 HOH A O     1 
HETATM 18841 O O     . HOH S 7 .    ? -53.013 54.073  101.415 1.00 23.41 ?  1694 HOH A O     1 
HETATM 18842 O O     . HOH S 7 .    ? -52.958 48.270  63.698  1.00 26.51 ?  1695 HOH A O     1 
HETATM 18843 O O     . HOH S 7 .    ? -43.194 61.212  101.127 1.00 19.30 ?  1696 HOH A O     1 
HETATM 18844 O O     . HOH S 7 .    ? -43.984 75.876  115.290 1.00 26.17 ?  1697 HOH A O     1 
HETATM 18845 O O     . HOH S 7 .    ? -50.781 26.960  78.927  1.00 33.93 ?  1698 HOH A O     1 
HETATM 18846 O O     . HOH S 7 .    ? -32.265 82.643  111.428 1.00 29.38 ?  1699 HOH A O     1 
HETATM 18847 O O     . HOH S 7 .    ? -4.331  78.302  123.815 1.00 21.30 ?  1700 HOH A O     1 
HETATM 18848 O O     . HOH S 7 .    ? 16.693  71.258  120.728 1.00 21.54 ?  1701 HOH A O     1 
HETATM 18849 O O     . HOH S 7 .    ? -20.345 58.972  77.451  1.00 16.97 ?  1702 HOH A O     1 
HETATM 18850 O O     . HOH S 7 .    ? -41.993 71.022  96.447  1.00 19.97 ?  1703 HOH A O     1 
HETATM 18851 O O     . HOH S 7 .    ? -41.030 58.312  81.101  1.00 21.31 ?  1704 HOH A O     1 
HETATM 18852 O O     . HOH S 7 .    ? -43.549 77.451  68.553  1.00 22.95 ?  1705 HOH A O     1 
HETATM 18853 O O     . HOH S 7 .    ? -14.086 41.731  72.133  1.00 26.55 ?  1706 HOH A O     1 
HETATM 18854 O O     . HOH S 7 .    ? -8.996  60.106  108.374 1.00 15.45 ?  1707 HOH A O     1 
HETATM 18855 O O     . HOH S 7 .    ? 14.335  87.822  107.594 1.00 32.80 ?  1708 HOH A O     1 
HETATM 18856 O O     . HOH S 7 .    ? -7.108  41.753  67.199  1.00 23.29 ?  1709 HOH A O     1 
HETATM 18857 O O     . HOH S 7 .    ? -32.639 82.300  98.684  1.00 17.16 ?  1710 HOH A O     1 
HETATM 18858 O O     . HOH S 7 .    ? -21.236 54.536  92.095  1.00 27.52 ?  1711 HOH A O     1 
HETATM 18859 O O     . HOH S 7 .    ? -23.007 96.986  79.630  1.00 29.15 ?  1712 HOH A O     1 
HETATM 18860 O O     . HOH S 7 .    ? -57.704 53.500  97.264  1.00 23.62 ?  1713 HOH A O     1 
HETATM 18861 O O     . HOH S 7 .    ? -20.205 81.411  106.214 1.00 25.77 ?  1714 HOH A O     1 
HETATM 18862 O O     . HOH S 7 .    ? -14.949 52.912  76.588  1.00 25.92 ?  1715 HOH A O     1 
HETATM 18863 O O     . HOH S 7 .    ? -14.552 74.979  106.925 1.00 19.45 ?  1716 HOH A O     1 
HETATM 18864 O O     . HOH S 7 .    ? -2.849  55.808  101.005 1.00 22.53 ?  1717 HOH A O     1 
HETATM 18865 O O     . HOH S 7 .    ? -34.714 56.976  77.738  1.00 32.51 ?  1718 HOH A O     1 
HETATM 18866 O O     . HOH S 7 .    ? -18.480 57.373  98.471  1.00 14.72 ?  1719 HOH A O     1 
HETATM 18867 O O     . HOH S 7 .    ? 10.677  56.971  107.132 1.00 26.27 ?  1720 HOH A O     1 
HETATM 18868 O O     . HOH S 7 .    ? -1.516  79.243  101.348 1.00 27.12 ?  1721 HOH A O     1 
HETATM 18869 O O     . HOH S 7 .    ? -27.535 64.910  101.409 1.00 20.35 ?  1722 HOH A O     1 
HETATM 18870 O O     . HOH S 7 .    ? -47.365 82.422  102.596 1.00 25.05 ?  1723 HOH A O     1 
HETATM 18871 O O     . HOH S 7 .    ? 3.869   57.662  106.179 1.00 18.68 ?  1724 HOH A O     1 
HETATM 18872 O O     . HOH S 7 .    ? 14.836  55.558  112.309 1.00 33.57 ?  1725 HOH A O     1 
HETATM 18873 O O     . HOH S 7 .    ? -21.454 55.002  96.138  1.00 26.86 ?  1726 HOH A O     1 
HETATM 18874 O O     . HOH S 7 .    ? -59.718 51.606  66.927  1.00 19.20 ?  1727 HOH A O     1 
HETATM 18875 O O     . HOH S 7 .    ? -37.702 45.347  105.364 1.00 30.15 ?  1728 HOH A O     1 
HETATM 18876 O O     . HOH S 7 .    ? 16.835  68.968  119.464 1.00 22.45 ?  1729 HOH A O     1 
HETATM 18877 O O     . HOH S 7 .    ? -26.392 60.875  59.824  1.00 34.52 ?  1730 HOH A O     1 
HETATM 18878 O O     . HOH S 7 .    ? 5.813   58.329  98.642  1.00 24.14 ?  1731 HOH A O     1 
HETATM 18879 O O     . HOH S 7 .    ? 23.262  65.272  115.992 1.00 22.41 ?  1732 HOH A O     1 
HETATM 18880 O O     . HOH S 7 .    ? -32.107 82.521  76.299  1.00 17.52 ?  1733 HOH A O     1 
HETATM 18881 O O     . HOH S 7 .    ? -35.332 95.121  97.480  1.00 23.91 ?  1734 HOH A O     1 
HETATM 18882 O O     . HOH S 7 .    ? -46.924 54.273  90.767  1.00 15.29 ?  1735 HOH A O     1 
HETATM 18883 O O     . HOH S 7 .    ? 10.869  67.442  118.170 1.00 21.58 ?  1736 HOH A O     1 
HETATM 18884 O O     . HOH S 7 .    ? -25.933 62.672  111.255 1.00 19.46 ?  1737 HOH A O     1 
HETATM 18885 O O     . HOH S 7 .    ? -61.795 52.983  92.337  1.00 23.07 ?  1738 HOH A O     1 
HETATM 18886 O O     . HOH S 7 .    ? -64.205 70.794  71.665  1.00 22.64 ?  1739 HOH A O     1 
HETATM 18887 O O     . HOH S 7 .    ? -20.703 71.076  105.682 1.00 29.11 ?  1740 HOH A O     1 
HETATM 18888 O O     . HOH S 7 .    ? -9.767  63.840  97.473  1.00 17.75 ?  1741 HOH A O     1 
HETATM 18889 O O     . HOH S 7 .    ? -35.729 73.235  84.534  1.00 20.47 ?  1742 HOH A O     1 
HETATM 18890 O O     . HOH S 7 .    ? 12.373  65.249  120.205 1.00 24.48 ?  1743 HOH A O     1 
HETATM 18891 O O     . HOH S 7 .    ? -32.530 79.367  97.340  1.00 20.60 ?  1744 HOH A O     1 
HETATM 18892 O O     . HOH S 7 .    ? -62.145 70.289  83.880  1.00 18.76 ?  1745 HOH A O     1 
HETATM 18893 O O     . HOH S 7 .    ? -27.142 89.406  78.591  1.00 23.16 ?  1746 HOH A O     1 
HETATM 18894 O O     . HOH S 7 .    ? -53.047 72.564  65.245  1.00 25.42 ?  1747 HOH A O     1 
HETATM 18895 O O     . HOH S 7 .    ? -42.321 67.826  92.187  1.00 16.07 ?  1748 HOH A O     1 
HETATM 18896 O O     . HOH S 7 .    ? -8.690  80.679  75.732  1.00 26.45 ?  1749 HOH A O     1 
HETATM 18897 O O     . HOH S 7 .    ? -38.847 50.395  99.477  1.00 20.03 ?  1750 HOH A O     1 
HETATM 18898 O O     . HOH S 7 .    ? -19.878 85.167  76.524  1.00 24.02 ?  1751 HOH A O     1 
HETATM 18899 O O     . HOH S 7 .    ? -50.091 76.090  102.547 1.00 21.23 ?  1752 HOH A O     1 
HETATM 18900 O O     . HOH S 7 .    ? -32.994 60.420  74.586  1.00 28.48 ?  1753 HOH A O     1 
HETATM 18901 O O     . HOH S 7 .    ? -3.829  57.488  73.808  1.00 18.67 ?  1754 HOH A O     1 
HETATM 18902 O O     . HOH S 7 .    ? -44.646 52.197  53.950  1.00 33.75 ?  1755 HOH A O     1 
HETATM 18903 O O     . HOH S 7 .    ? -45.788 62.623  93.606  1.00 14.70 ?  1756 HOH A O     1 
HETATM 18904 O O     . HOH S 7 .    ? -33.543 78.149  74.991  1.00 22.49 ?  1757 HOH A O     1 
HETATM 18905 O O     . HOH S 7 .    ? -33.678 48.637  76.337  1.00 24.46 ?  1758 HOH A O     1 
HETATM 18906 O O     . HOH S 7 .    ? -24.459 67.641  106.430 1.00 18.93 ?  1759 HOH A O     1 
HETATM 18907 O O     . HOH S 7 .    ? -60.045 38.216  84.264  1.00 36.91 ?  1760 HOH A O     1 
HETATM 18908 O O     . HOH S 7 .    ? -19.202 59.432  71.024  1.00 16.59 ?  1761 HOH A O     1 
HETATM 18909 O O     . HOH S 7 .    ? -31.494 60.902  91.586  1.00 16.84 ?  1762 HOH A O     1 
HETATM 18910 O O     . HOH S 7 .    ? -50.795 32.514  93.384  1.00 39.24 ?  1763 HOH A O     1 
HETATM 18911 O O     . HOH S 7 .    ? -20.335 52.003  79.272  1.00 18.36 ?  1764 HOH A O     1 
HETATM 18912 O O     . HOH S 7 .    ? -54.232 55.292  69.401  1.00 16.27 ?  1765 HOH A O     1 
HETATM 18913 O O     . HOH S 7 .    ? -28.917 56.796  61.196  1.00 25.32 ?  1766 HOH A O     1 
HETATM 18914 O O     . HOH S 7 .    ? -50.027 78.141  78.366  1.00 25.00 ?  1767 HOH A O     1 
HETATM 18915 O O     . HOH S 7 .    ? -51.607 69.928  94.890  1.00 20.32 ?  1768 HOH A O     1 
HETATM 18916 O O     . HOH S 7 .    ? -2.675  53.664  105.747 1.00 21.33 ?  1769 HOH A O     1 
HETATM 18917 O O     . HOH S 7 .    ? 5.012   67.088  97.246  1.00 20.45 ?  1770 HOH A O     1 
HETATM 18918 O O     . HOH S 7 .    ? -44.597 55.669  96.182  1.00 15.16 ?  1771 HOH A O     1 
HETATM 18919 O O     . HOH S 7 .    ? -26.263 61.969  77.014  1.00 28.00 ?  1772 HOH A O     1 
HETATM 18920 O O     . HOH S 7 .    ? -48.823 54.334  62.203  1.00 21.47 ?  1773 HOH A O     1 
HETATM 18921 O O     . HOH S 7 .    ? -20.401 86.806  92.647  1.00 20.58 ?  1774 HOH A O     1 
HETATM 18922 O O     . HOH S 7 .    ? -55.793 47.343  96.023  1.00 35.83 ?  1775 HOH A O     1 
HETATM 18923 O O     . HOH S 7 .    ? -34.820 41.874  72.038  1.00 31.68 ?  1776 HOH A O     1 
HETATM 18924 O O     . HOH S 7 .    ? -1.960  77.695  122.632 1.00 27.44 ?  1777 HOH A O     1 
HETATM 18925 O O     . HOH S 7 .    ? -3.046  62.390  78.655  1.00 21.26 ?  1778 HOH A O     1 
HETATM 18926 O O     . HOH S 7 .    ? -13.939 77.986  112.483 1.00 15.96 ?  1779 HOH A O     1 
HETATM 18927 O O     . HOH S 7 .    ? -33.166 60.016  83.609  1.00 33.15 ?  1780 HOH A O     1 
HETATM 18928 O O     . HOH S 7 .    ? -46.598 29.249  91.159  1.00 36.69 ?  1781 HOH A O     1 
HETATM 18929 O O     . HOH S 7 .    ? -22.968 58.657  77.072  1.00 22.78 ?  1782 HOH A O     1 
HETATM 18930 O O     . HOH S 7 .    ? -22.813 98.543  101.551 1.00 31.79 ?  1783 HOH A O     1 
HETATM 18931 O O     . HOH S 7 .    ? -44.582 24.771  77.462  1.00 34.86 ?  1784 HOH A O     1 
HETATM 18932 O O     . HOH S 7 .    ? -17.407 54.924  79.476  1.00 23.29 ?  1785 HOH A O     1 
HETATM 18933 O O     . HOH S 7 .    ? -40.459 64.152  63.420  1.00 26.57 ?  1786 HOH A O     1 
HETATM 18934 O O     . HOH S 7 .    ? -50.718 66.557  107.484 1.00 25.54 ?  1787 HOH A O     1 
HETATM 18935 O O     . HOH S 7 .    ? -20.435 65.956  82.114  1.00 21.08 ?  1788 HOH A O     1 
HETATM 18936 O O     . HOH S 7 .    ? -48.280 64.288  97.875  1.00 19.84 ?  1789 HOH A O     1 
HETATM 18937 O O     . HOH S 7 .    ? 20.664  61.856  100.354 1.00 23.21 ?  1790 HOH A O     1 
HETATM 18938 O O     . HOH S 7 .    ? 7.700   89.015  128.472 1.00 32.77 ?  1791 HOH A O     1 
HETATM 18939 O O     . HOH S 7 .    ? -66.845 61.335  76.589  1.00 16.18 ?  1792 HOH A O     1 
HETATM 18940 O O     . HOH S 7 .    ? -26.672 50.187  97.633  1.00 22.27 ?  1793 HOH A O     1 
HETATM 18941 O O     . HOH S 7 .    ? -34.551 75.583  84.121  1.00 22.41 ?  1794 HOH A O     1 
HETATM 18942 O O     . HOH S 7 .    ? -12.982 65.915  114.027 1.00 14.86 ?  1795 HOH A O     1 
HETATM 18943 O O     . HOH S 7 .    ? -46.381 72.569  65.116  1.00 18.02 ?  1796 HOH A O     1 
HETATM 18944 O O     . HOH S 7 .    ? -38.489 40.492  72.842  1.00 23.33 ?  1797 HOH A O     1 
HETATM 18945 O O     . HOH S 7 .    ? -47.805 70.763  112.305 1.00 30.12 ?  1798 HOH A O     1 
HETATM 18946 O O     . HOH S 7 .    ? 23.027  76.895  102.797 1.00 33.91 ?  1799 HOH A O     1 
HETATM 18947 O O     . HOH S 7 .    ? -0.502  66.077  95.695  1.00 24.68 ?  1800 HOH A O     1 
HETATM 18948 O O     . HOH S 7 .    ? -4.891  59.185  119.676 1.00 17.08 ?  1801 HOH A O     1 
HETATM 18949 O O     . HOH S 7 .    ? -31.777 59.999  106.663 1.00 24.96 ?  1802 HOH A O     1 
HETATM 18950 O O     . HOH S 7 .    ? -8.976  65.191  115.258 1.00 15.94 ?  1803 HOH A O     1 
HETATM 18951 O O     . HOH S 7 .    ? -33.062 40.404  96.385  1.00 36.63 ?  1804 HOH A O     1 
HETATM 18952 O O     . HOH S 7 .    ? -28.993 75.167  103.278 1.00 22.54 ?  1805 HOH A O     1 
HETATM 18953 O O     . HOH S 7 .    ? -38.735 61.489  92.880  1.00 17.23 ?  1806 HOH A O     1 
HETATM 18954 O O     . HOH S 7 .    ? -23.265 55.223  89.619  1.00 28.09 ?  1807 HOH A O     1 
HETATM 18955 O O     . HOH S 7 .    ? -32.350 86.784  77.345  1.00 30.34 ?  1808 HOH A O     1 
HETATM 18956 O O     . HOH S 7 .    ? -63.552 53.756  73.105  1.00 21.29 ?  1809 HOH A O     1 
HETATM 18957 O O     . HOH S 7 .    ? -11.849 59.560  85.760  1.00 23.03 ?  1810 HOH A O     1 
HETATM 18958 O O     . HOH S 7 .    ? -62.570 61.624  69.052  1.00 21.83 ?  1811 HOH A O     1 
HETATM 18959 O O     . HOH S 7 .    ? -62.780 54.528  64.063  1.00 32.31 ?  1812 HOH A O     1 
HETATM 18960 O O     . HOH S 7 .    ? -24.158 60.968  64.781  1.00 21.33 ?  1813 HOH A O     1 
HETATM 18961 O O     . HOH S 7 .    ? -1.923  91.043  107.077 1.00 28.53 ?  1814 HOH A O     1 
HETATM 18962 O O     . HOH S 7 .    ? -52.804 61.952  95.739  1.00 19.36 ?  1815 HOH A O     1 
HETATM 18963 O O     . HOH S 7 .    ? -37.046 63.319  97.109  1.00 24.85 ?  1816 HOH A O     1 
HETATM 18964 O O     . HOH S 7 .    ? -47.013 66.578  94.907  1.00 17.09 ?  1817 HOH A O     1 
HETATM 18965 O O     . HOH S 7 .    ? -28.988 50.616  87.931  1.00 23.09 ?  1818 HOH A O     1 
HETATM 18966 O O     . HOH S 7 .    ? -37.857 86.113  103.085 1.00 26.15 ?  1819 HOH A O     1 
HETATM 18967 O O     . HOH S 7 .    ? -54.922 47.157  68.363  1.00 23.31 ?  1820 HOH A O     1 
HETATM 18968 O O     . HOH S 7 .    ? -7.018  70.369  95.332  1.00 19.02 ?  1821 HOH A O     1 
HETATM 18969 O O     . HOH S 7 .    ? -48.206 59.025  83.809  1.00 12.91 ?  1822 HOH A O     1 
HETATM 18970 O O     . HOH S 7 .    ? -29.188 76.527  73.770  1.00 22.15 ?  1823 HOH A O     1 
HETATM 18971 O O     . HOH S 7 .    ? 9.059   54.935  106.203 1.00 26.06 ?  1824 HOH A O     1 
HETATM 18972 O O     . HOH S 7 .    ? -61.353 68.443  69.463  1.00 21.64 ?  1825 HOH A O     1 
HETATM 18973 O O     . HOH S 7 .    ? -7.311  38.043  64.457  1.00 27.62 ?  1826 HOH A O     1 
HETATM 18974 O O     . HOH S 7 .    ? -43.469 49.500  56.702  1.00 28.15 ?  1827 HOH A O     1 
HETATM 18975 O O     . HOH S 7 .    ? -34.751 82.732  119.970 1.00 22.36 ?  1828 HOH A O     1 
HETATM 18976 O O     . HOH S 7 .    ? -2.133  78.203  76.912  1.00 25.45 ?  1829 HOH A O     1 
HETATM 18977 O O     . HOH S 7 .    ? -23.735 54.313  102.504 1.00 21.39 ?  1830 HOH A O     1 
HETATM 18978 O O     . HOH S 7 .    ? -39.600 35.177  87.283  1.00 33.28 ?  1831 HOH A O     1 
HETATM 18979 O O     . HOH S 7 .    ? 0.055   85.128  113.194 1.00 26.99 ?  1832 HOH A O     1 
HETATM 18980 O O     . HOH S 7 .    ? -5.358  90.829  121.603 1.00 29.05 ?  1833 HOH A O     1 
HETATM 18981 O O     . HOH S 7 .    ? 0.944   74.700  108.800 1.00 18.41 ?  1834 HOH A O     1 
HETATM 18982 O O     . HOH S 7 .    ? -17.834 64.834  62.918  1.00 33.98 ?  1835 HOH A O     1 
HETATM 18983 O O     . HOH S 7 .    ? 5.583   64.188  114.954 1.00 30.38 ?  1836 HOH A O     1 
HETATM 18984 O O     . HOH S 7 .    ? -66.062 64.609  82.267  1.00 18.28 ?  1837 HOH A O     1 
HETATM 18985 O O     . HOH S 7 .    ? -16.148 68.132  97.859  1.00 11.81 ?  1838 HOH A O     1 
HETATM 18986 O O     . HOH S 7 .    ? -58.520 57.532  63.907  1.00 17.40 ?  1839 HOH A O     1 
HETATM 18987 O O     . HOH S 7 .    ? -35.205 80.661  121.901 1.00 22.63 ?  1840 HOH A O     1 
HETATM 18988 O O     . HOH S 7 .    ? -49.647 47.632  98.630  1.00 21.24 ?  1841 HOH A O     1 
HETATM 18989 O O     . HOH S 7 .    ? -48.274 57.673  87.326  1.00 14.72 ?  1842 HOH A O     1 
HETATM 18990 O O     . HOH S 7 .    ? -26.235 63.692  105.885 1.00 21.18 ?  1843 HOH A O     1 
HETATM 18991 O O     . HOH S 7 .    ? 6.535   60.850  104.542 1.00 15.57 ?  1844 HOH A O     1 
HETATM 18992 O O     . HOH S 7 .    ? 1.077   62.005  112.559 1.00 27.41 ?  1845 HOH A O     1 
HETATM 18993 O O     . HOH S 7 .    ? -44.778 73.642  75.915  1.00 20.33 ?  1846 HOH A O     1 
HETATM 18994 O O     . HOH S 7 .    ? 10.222  81.352  126.806 1.00 27.85 ?  1847 HOH A O     1 
HETATM 18995 O O     . HOH S 7 .    ? -27.624 58.588  77.201  1.00 25.69 ?  1848 HOH A O     1 
HETATM 18996 O O     . HOH S 7 .    ? -46.600 55.915  88.477  1.00 14.37 ?  1849 HOH A O     1 
HETATM 18997 O O     . HOH S 7 .    ? -7.533  62.429  108.492 1.00 16.35 ?  1850 HOH A O     1 
HETATM 18998 O O     . HOH S 7 .    ? -1.524  76.609  89.059  1.00 25.53 ?  1851 HOH A O     1 
HETATM 18999 O O     . HOH S 7 .    ? -21.243 101.216 90.886  1.00 30.88 ?  1852 HOH A O     1 
HETATM 19000 O O     . HOH S 7 .    ? -50.210 49.017  101.154 1.00 23.21 ?  1853 HOH A O     1 
HETATM 19001 O O     . HOH S 7 .    ? -20.198 89.151  76.126  1.00 27.44 ?  1854 HOH A O     1 
HETATM 19002 O O     . HOH S 7 .    ? -60.437 50.207  91.814  1.00 29.69 ?  1855 HOH A O     1 
HETATM 19003 O O     . HOH S 7 .    ? -41.120 82.041  112.003 1.00 29.71 ?  1856 HOH A O     1 
HETATM 19004 O O     . HOH S 7 .    ? -24.631 59.442  122.988 1.00 30.92 ?  1857 HOH A O     1 
HETATM 19005 O O     . HOH S 7 .    ? -16.951 76.766  109.917 1.00 17.29 ?  1858 HOH A O     1 
HETATM 19006 O O     . HOH S 7 .    ? -12.565 39.896  69.314  1.00 32.59 ?  1859 HOH A O     1 
HETATM 19007 O O     . HOH S 7 .    ? -52.795 78.431  88.469  1.00 25.86 ?  1860 HOH A O     1 
HETATM 19008 O O     . HOH S 7 .    ? -42.495 55.609  106.086 1.00 32.20 ?  1861 HOH A O     1 
HETATM 19009 O O     . HOH S 7 .    ? -26.804 80.725  102.868 1.00 21.79 ?  1862 HOH A O     1 
HETATM 19010 O O     . HOH S 7 .    ? -21.645 52.878  89.789  1.00 26.50 ?  1863 HOH A O     1 
HETATM 19011 O O     . HOH S 7 .    ? -12.751 75.109  108.904 1.00 21.84 ?  1864 HOH A O     1 
HETATM 19012 O O     . HOH S 7 .    ? -5.708  67.947  78.931  1.00 28.67 ?  1865 HOH A O     1 
HETATM 19013 O O     . HOH S 7 .    ? 18.639  73.034  119.788 1.00 22.39 ?  1866 HOH A O     1 
HETATM 19014 O O     . HOH S 7 .    ? -39.331 54.042  78.678  1.00 31.16 ?  1867 HOH A O     1 
HETATM 19015 O O     . HOH S 7 .    ? -33.131 77.928  94.207  1.00 24.21 ?  1868 HOH A O     1 
HETATM 19016 O O     . HOH S 7 .    ? -11.949 88.898  130.413 1.00 30.71 ?  1869 HOH A O     1 
HETATM 19017 O O     . HOH S 7 .    ? -32.123 88.610  96.361  1.00 19.93 ?  1870 HOH A O     1 
HETATM 19018 O O     . HOH S 7 .    ? -10.822 63.018  73.819  1.00 22.35 ?  1871 HOH A O     1 
HETATM 19019 O O     . HOH S 7 .    ? -50.421 72.635  102.176 1.00 20.30 ?  1872 HOH A O     1 
HETATM 19020 O O     . HOH S 7 .    ? -18.296 49.332  80.140  1.00 26.37 ?  1873 HOH A O     1 
HETATM 19021 O O     . HOH S 7 .    ? -37.123 69.555  120.564 1.00 22.88 ?  1874 HOH A O     1 
HETATM 19022 O O     . HOH S 7 .    ? 3.842   60.301  102.345 1.00 20.47 ?  1875 HOH A O     1 
HETATM 19023 O O     . HOH S 7 .    ? -37.281 68.164  84.122  1.00 25.64 ?  1876 HOH A O     1 
HETATM 19024 O O     . HOH S 7 .    ? -16.483 64.590  67.525  1.00 26.48 ?  1877 HOH A O     1 
HETATM 19025 O O     . HOH S 7 .    ? -16.180 46.885  54.628  1.00 26.67 ?  1878 HOH A O     1 
HETATM 19026 O O     . HOH S 7 .    ? -32.586 75.213  127.902 1.00 25.80 ?  1879 HOH A O     1 
HETATM 19027 O O     . HOH S 7 .    ? -48.699 75.258  96.518  1.00 19.47 ?  1880 HOH A O     1 
HETATM 19028 O O     . HOH S 7 .    ? -18.637 79.534  128.677 1.00 20.74 ?  1881 HOH A O     1 
HETATM 19029 O O     . HOH S 7 .    ? -57.584 59.922  61.850  1.00 16.90 ?  1882 HOH A O     1 
HETATM 19030 O O     . HOH S 7 .    ? -36.567 43.780  67.602  1.00 31.96 ?  1883 HOH A O     1 
HETATM 19031 O O     . HOH S 7 .    ? -37.254 49.888  101.984 1.00 22.69 ?  1884 HOH A O     1 
HETATM 19032 O O     . HOH S 7 .    ? -38.604 70.312  82.696  1.00 18.01 ?  1885 HOH A O     1 
HETATM 19033 O O     . HOH S 7 .    ? -17.340 52.965  77.407  1.00 24.95 ?  1886 HOH A O     1 
HETATM 19034 O O     . HOH S 7 .    ? -39.574 88.885  91.750  1.00 30.73 ?  1887 HOH A O     1 
HETATM 19035 O O     . HOH S 7 .    ? -32.976 59.600  110.895 1.00 26.69 ?  1888 HOH A O     1 
HETATM 19036 O O     . HOH S 7 .    ? -65.992 71.405  81.392  1.00 23.43 ?  1889 HOH A O     1 
HETATM 19037 O O     . HOH S 7 .    ? -34.240 83.909  124.853 1.00 32.01 ?  1890 HOH A O     1 
HETATM 19038 O O     . HOH S 7 .    ? -2.418  85.237  114.891 1.00 26.15 ?  1891 HOH A O     1 
HETATM 19039 O O     . HOH S 7 .    ? -29.353 54.780  112.959 1.00 30.43 ?  1892 HOH A O     1 
HETATM 19040 O O     . HOH S 7 .    ? -25.210 88.335  80.216  1.00 19.11 ?  1893 HOH A O     1 
HETATM 19041 O O     . HOH S 7 .    ? -46.122 78.327  97.036  1.00 19.08 ?  1894 HOH A O     1 
HETATM 19042 O O     . HOH S 7 .    ? -33.679 92.331  108.089 1.00 31.15 ?  1895 HOH A O     1 
HETATM 19043 O O     . HOH S 7 .    ? -9.516  87.044  89.317  1.00 36.39 ?  1896 HOH A O     1 
HETATM 19044 O O     . HOH S 7 .    ? -25.160 69.708  104.527 1.00 26.12 ?  1897 HOH A O     1 
HETATM 19045 O O     . HOH S 7 .    ? -41.095 80.216  88.540  1.00 17.77 ?  1898 HOH A O     1 
HETATM 19046 O O     . HOH S 7 .    ? -21.194 81.639  117.425 1.00 17.81 ?  1899 HOH A O     1 
HETATM 19047 O O     . HOH S 7 .    ? -37.111 76.785  96.439  1.00 22.92 ?  1900 HOH A O     1 
HETATM 19048 O O     . HOH S 7 .    ? -33.916 52.351  83.340  1.00 22.95 ?  1901 HOH A O     1 
HETATM 19049 O O     . HOH S 7 .    ? -20.660 47.468  55.812  1.00 29.89 ?  1902 HOH A O     1 
HETATM 19050 O O     . HOH S 7 .    ? -27.146 96.384  80.583  1.00 31.99 ?  1903 HOH A O     1 
HETATM 19051 O O     . HOH S 7 .    ? -31.951 94.456  129.067 1.00 39.27 ?  1904 HOH A O     1 
HETATM 19052 O O     . HOH S 7 .    ? -48.918 61.385  57.742  1.00 20.32 ?  1905 HOH A O     1 
HETATM 19053 O O     . HOH S 7 .    ? -1.398  95.880  118.901 1.00 30.58 ?  1906 HOH A O     1 
HETATM 19054 O O     . HOH S 7 .    ? -51.418 58.814  106.161 1.00 35.04 ?  1907 HOH A O     1 
HETATM 19055 O O     . HOH S 7 .    ? -31.418 84.015  124.911 1.00 21.58 ?  1908 HOH A O     1 
HETATM 19056 O O     . HOH S 7 .    ? -39.689 76.638  94.142  1.00 20.19 ?  1909 HOH A O     1 
HETATM 19057 O O     . HOH S 7 .    ? -42.161 88.950  97.886  1.00 21.56 ?  1910 HOH A O     1 
HETATM 19058 O O     . HOH S 7 .    ? -46.827 30.321  87.036  1.00 33.22 ?  1911 HOH A O     1 
HETATM 19059 O O     . HOH S 7 .    ? -16.816 60.164  107.749 1.00 22.46 ?  1912 HOH A O     1 
HETATM 19060 O O     . HOH S 7 .    ? -60.897 46.938  89.834  1.00 25.82 ?  1913 HOH A O     1 
HETATM 19061 O O     . HOH S 7 .    ? -22.853 65.375  76.299  1.00 32.57 ?  1914 HOH A O     1 
HETATM 19062 O O     . HOH S 7 .    ? -39.278 75.157  97.253  1.00 23.50 ?  1915 HOH A O     1 
HETATM 19063 O O     . HOH S 7 .    ? -20.407 79.147  116.316 1.00 18.21 ?  1916 HOH A O     1 
HETATM 19064 O O     . HOH S 7 .    ? -3.375  82.078  98.768  1.00 22.55 ?  1917 HOH A O     1 
HETATM 19065 O O     . HOH S 7 .    ? -49.446 29.110  75.317  1.00 37.89 ?  1918 HOH A O     1 
HETATM 19066 O O     . HOH S 7 .    ? 23.021  62.700  116.879 1.00 17.86 ?  1919 HOH A O     1 
HETATM 19067 O O     . HOH S 7 .    ? -31.531 46.618  89.223  1.00 26.22 ?  1920 HOH A O     1 
HETATM 19068 O O     . HOH S 7 .    ? -6.426  70.787  107.554 1.00 25.96 ?  1921 HOH A O     1 
HETATM 19069 O O     . HOH S 7 .    ? -23.068 83.489  92.656  1.00 14.16 ?  1922 HOH A O     1 
HETATM 19070 O O     . HOH S 7 .    ? -13.543 54.092  78.363  1.00 20.96 ?  1923 HOH A O     1 
HETATM 19071 O O     . HOH S 7 .    ? -19.757 91.107  77.833  1.00 25.37 ?  1924 HOH A O     1 
HETATM 19072 O O     . HOH S 7 .    ? -61.642 61.609  63.360  1.00 34.12 ?  1925 HOH A O     1 
HETATM 19073 O O     . HOH S 7 .    ? 10.427  66.943  113.408 1.00 27.47 ?  1926 HOH A O     1 
HETATM 19074 O O     . HOH S 7 .    ? -42.113 79.702  80.844  1.00 23.90 ?  1927 HOH A O     1 
HETATM 19075 O O     . HOH S 7 .    ? -28.252 61.052  85.671  1.00 25.81 ?  1928 HOH A O     1 
HETATM 19076 O O     . HOH S 7 .    ? -26.105 94.161  79.139  1.00 24.92 ?  1929 HOH A O     1 
HETATM 19077 O O     . HOH S 7 .    ? -4.335  76.386  125.863 1.00 24.91 ?  1930 HOH A O     1 
HETATM 19078 O O     . HOH S 7 .    ? -0.320  52.614  64.050  1.00 20.13 ?  1931 HOH A O     1 
HETATM 19079 O O     . HOH S 7 .    ? -45.504 80.298  80.060  1.00 31.66 ?  1932 HOH A O     1 
HETATM 19080 O O     . HOH S 7 .    ? -35.027 66.691  102.888 1.00 19.50 ?  1933 HOH A O     1 
HETATM 19081 O O     . HOH S 7 .    ? -59.563 58.152  77.792  1.00 14.80 ?  1934 HOH A O     1 
HETATM 19082 O O     . HOH S 7 .    ? -15.083 67.057  74.132  1.00 18.22 ?  1935 HOH A O     1 
HETATM 19083 O O     . HOH S 7 .    ? -6.848  93.893  114.922 1.00 24.44 ?  1936 HOH A O     1 
HETATM 19084 O O     . HOH S 7 .    ? 11.018  60.830  116.632 1.00 28.57 ?  1937 HOH A O     1 
HETATM 19085 O O     . HOH S 7 .    ? -34.667 56.370  106.600 1.00 22.60 ?  1938 HOH A O     1 
HETATM 19086 O O     . HOH S 7 .    ? -39.895 60.995  104.627 1.00 31.02 ?  1939 HOH A O     1 
HETATM 19087 O O     . HOH S 7 .    ? -44.450 30.585  70.758  1.00 32.61 ?  1940 HOH A O     1 
HETATM 19088 O O     . HOH S 7 .    ? -4.917  93.624  119.624 1.00 31.63 ?  1941 HOH A O     1 
HETATM 19089 O O     . HOH S 7 .    ? -50.219 68.642  92.977  1.00 19.18 ?  1942 HOH A O     1 
HETATM 19090 O O     . HOH S 7 .    ? -46.966 31.457  71.670  1.00 32.07 ?  1943 HOH A O     1 
HETATM 19091 O O     . HOH S 7 .    ? -36.066 43.257  80.399  1.00 20.63 ?  1944 HOH A O     1 
HETATM 19092 O O     . HOH S 7 .    ? -4.403  54.874  62.477  1.00 28.74 ?  1945 HOH A O     1 
HETATM 19093 O O     . HOH S 7 .    ? -42.634 56.628  90.555  1.00 13.40 ?  1946 HOH A O     1 
HETATM 19094 O O     . HOH S 7 .    ? 13.724  86.591  122.149 1.00 34.00 ?  1947 HOH A O     1 
HETATM 19095 O O     . HOH S 7 .    ? -6.806  70.989  105.290 1.00 24.51 ?  1948 HOH A O     1 
HETATM 19096 O O     . HOH S 7 .    ? -33.903 70.260  101.604 1.00 26.15 ?  1949 HOH A O     1 
HETATM 19097 O O     . HOH S 7 .    ? -59.989 62.851  78.455  1.00 17.94 ?  1950 HOH A O     1 
HETATM 19098 O O     . HOH S 7 .    ? -28.457 69.427  86.789  1.00 26.23 ?  1951 HOH A O     1 
HETATM 19099 O O     . HOH S 7 .    ? -7.981  72.415  101.552 1.00 26.68 ?  1952 HOH A O     1 
HETATM 19100 O O     . HOH S 7 .    ? -37.303 51.177  61.969  1.00 26.08 ?  1953 HOH A O     1 
HETATM 19101 O O     . HOH S 7 .    ? -37.677 65.064  109.541 1.00 30.07 ?  1954 HOH A O     1 
HETATM 19102 O O     . HOH S 7 .    ? -37.278 60.527  97.436  1.00 14.65 ?  1955 HOH A O     1 
HETATM 19103 O O     . HOH S 7 .    ? -2.014  77.834  106.532 1.00 21.24 ?  1956 HOH A O     1 
HETATM 19104 O O     . HOH S 7 .    ? -21.182 58.106  98.469  1.00 18.43 ?  1957 HOH A O     1 
HETATM 19105 O O     . HOH S 7 .    ? -14.499 85.200  77.932  1.00 23.44 ?  1958 HOH A O     1 
HETATM 19106 O O     . HOH S 7 .    ? -48.447 65.870  58.743  1.00 24.60 ?  1959 HOH A O     1 
HETATM 19107 O O     . HOH S 7 .    ? -50.675 56.674  72.676  1.00 21.68 ?  1960 HOH A O     1 
HETATM 19108 O O     . HOH S 7 .    ? -27.698 90.791  117.294 1.00 24.61 ?  1961 HOH A O     1 
HETATM 19109 O O     . HOH S 7 .    ? 16.237  65.212  121.470 1.00 23.88 ?  1962 HOH A O     1 
HETATM 19110 O O     . HOH S 7 .    ? -25.367 82.815  73.452  1.00 26.83 ?  1963 HOH A O     1 
HETATM 19111 O O     . HOH S 7 .    ? 2.383   83.844  128.215 1.00 32.19 ?  1964 HOH A O     1 
HETATM 19112 O O     . HOH S 7 .    ? -36.335 39.040  86.261  1.00 32.03 ?  1965 HOH A O     1 
HETATM 19113 O O     . HOH S 7 .    ? -23.303 53.669  93.746  1.00 27.29 ?  1966 HOH A O     1 
HETATM 19114 O O     . HOH S 7 .    ? -2.251  62.290  114.479 1.00 29.26 ?  1967 HOH A O     1 
HETATM 19115 O O     . HOH S 7 .    ? -46.674 23.897  83.911  1.00 37.29 ?  1968 HOH A O     1 
HETATM 19116 O O     . HOH S 7 .    ? -45.076 60.968  86.520  1.00 13.37 ?  1969 HOH A O     1 
HETATM 19117 O O     . HOH S 7 .    ? -10.140 74.338  105.481 1.00 23.35 ?  1970 HOH A O     1 
HETATM 19118 O O     . HOH S 7 .    ? -27.997 71.043  91.068  1.00 21.36 ?  1971 HOH A O     1 
HETATM 19119 O O     . HOH S 7 .    ? -53.932 48.997  61.170  1.00 22.30 ?  1972 HOH A O     1 
HETATM 19120 O O     . HOH S 7 .    ? -30.817 86.645  103.385 1.00 17.46 ?  1973 HOH A O     1 
HETATM 19121 O O     . HOH S 7 .    ? -13.147 69.190  74.761  1.00 30.57 ?  1974 HOH A O     1 
HETATM 19122 O O     . HOH S 7 .    ? -25.251 79.363  96.260  1.00 16.41 ?  1975 HOH A O     1 
HETATM 19123 O O     . HOH S 7 .    ? 2.528   84.056  103.022 1.00 22.91 ?  1976 HOH A O     1 
HETATM 19124 O O     . HOH S 7 .    ? -23.612 86.647  74.655  1.00 26.90 ?  1977 HOH A O     1 
HETATM 19125 O O     . HOH S 7 .    ? -42.911 77.859  76.769  1.00 21.98 ?  1978 HOH A O     1 
HETATM 19126 O O     . HOH S 7 .    ? -27.608 61.909  90.027  1.00 15.74 ?  1979 HOH A O     1 
HETATM 19127 O O     . HOH S 7 .    ? -32.445 51.992  87.393  1.00 22.42 ?  1980 HOH A O     1 
HETATM 19128 O O     . HOH S 7 .    ? -12.669 64.188  130.940 1.00 29.26 ?  1981 HOH A O     1 
HETATM 19129 O O     . HOH S 7 .    ? -35.744 63.252  117.434 1.00 29.47 ?  1982 HOH A O     1 
HETATM 19130 O O     . HOH S 7 .    ? 12.451  75.747  96.303  1.00 28.82 ?  1983 HOH A O     1 
HETATM 19131 O O     . HOH S 7 .    ? -49.209 65.207  55.041  1.00 27.84 ?  1984 HOH A O     1 
HETATM 19132 O O     . HOH S 7 .    ? -40.078 61.636  95.558  1.00 18.05 ?  1985 HOH A O     1 
HETATM 19133 O O     . HOH S 7 .    ? -16.474 53.774  101.848 1.00 30.51 ?  1986 HOH A O     1 
HETATM 19134 O O     . HOH S 7 .    ? -29.743 73.327  97.189  1.00 24.77 ?  1987 HOH A O     1 
HETATM 19135 O O     . HOH S 7 .    ? -34.756 77.487  86.006  1.00 18.64 ?  1988 HOH A O     1 
HETATM 19136 O O     . HOH S 7 .    ? -30.717 81.312  124.645 1.00 22.43 ?  1989 HOH A O     1 
HETATM 19137 O O     . HOH S 7 .    ? -20.193 59.684  80.138  1.00 21.93 ?  1990 HOH A O     1 
HETATM 19138 O O     . HOH S 7 .    ? -36.416 37.146  84.668  1.00 29.57 ?  1991 HOH A O     1 
HETATM 19139 O O     . HOH S 7 .    ? -27.285 51.870  99.791  1.00 18.75 ?  1992 HOH A O     1 
HETATM 19140 O O     . HOH S 7 .    ? -27.020 62.917  87.516  1.00 19.40 ?  1993 HOH A O     1 
HETATM 19141 O O     . HOH S 7 .    ? -44.258 59.263  88.596  1.00 14.19 ?  1994 HOH A O     1 
HETATM 19142 O O     . HOH S 7 .    ? -54.640 79.338  82.077  1.00 32.60 ?  1995 HOH A O     1 
HETATM 19143 O O     . HOH S 7 .    ? -28.179 55.991  91.655  1.00 22.98 ?  1996 HOH A O     1 
HETATM 19144 O O     . HOH S 7 .    ? -34.378 69.283  77.155  1.00 26.56 ?  1997 HOH A O     1 
HETATM 19145 O O     . HOH S 7 .    ? -4.704  50.626  57.553  1.00 28.22 ?  1998 HOH A O     1 
HETATM 19146 O O     . HOH S 7 .    ? -50.346 72.824  63.633  1.00 17.51 ?  1999 HOH A O     1 
HETATM 19147 O O     . HOH S 7 .    ? -54.120 68.846  94.302  1.00 23.56 ?  2000 HOH A O     1 
HETATM 19148 O O     . HOH S 7 .    ? -10.667 63.685  116.996 1.00 16.82 ?  2001 HOH A O     1 
HETATM 19149 O O     . HOH S 7 .    ? -65.130 42.750  87.428  1.00 33.24 ?  2002 HOH A O     1 
HETATM 19150 O O     . HOH S 7 .    ? 17.678  80.225  98.448  1.00 32.83 ?  2003 HOH A O     1 
HETATM 19151 O O     . HOH S 7 .    ? -4.362  72.944  78.158  1.00 22.91 ?  2004 HOH A O     1 
HETATM 19152 O O     . HOH S 7 .    ? -25.958 88.856  117.642 1.00 22.93 ?  2005 HOH A O     1 
HETATM 19153 O O     . HOH S 7 .    ? -61.637 41.157  68.368  1.00 36.93 ?  2006 HOH A O     1 
HETATM 19154 O O     . HOH S 7 .    ? -29.197 95.009  90.258  1.00 29.24 ?  2007 HOH A O     1 
HETATM 19155 O O     . HOH S 7 .    ? 1.053   66.190  97.939  1.00 18.58 ?  2008 HOH A O     1 
HETATM 19156 O O     . HOH S 7 .    ? -33.778 45.559  85.886  1.00 26.28 ?  2009 HOH A O     1 
HETATM 19157 O O     . HOH S 7 .    ? -1.866  80.166  113.167 1.00 25.45 ?  2010 HOH A O     1 
HETATM 19158 O O     . HOH S 7 .    ? -30.134 62.405  62.958  1.00 31.34 ?  2011 HOH A O     1 
HETATM 19159 O O     . HOH S 7 .    ? -40.088 88.918  120.655 1.00 29.53 ?  2012 HOH A O     1 
HETATM 19160 O O     . HOH S 7 .    ? -39.067 71.124  85.252  1.00 20.51 ?  2013 HOH A O     1 
HETATM 19161 O O     . HOH S 7 .    ? 2.748   74.175  110.883 1.00 19.76 ?  2014 HOH A O     1 
HETATM 19162 O O     . HOH S 7 .    ? -57.134 73.400  97.180  1.00 30.56 ?  2015 HOH A O     1 
HETATM 19163 O O     . HOH S 7 .    ? -27.158 73.292  102.275 1.00 25.83 ?  2016 HOH A O     1 
HETATM 19164 O O     . HOH S 7 .    ? -54.112 72.320  69.071  1.00 22.75 ?  2017 HOH A O     1 
HETATM 19165 O O     . HOH S 7 .    ? -22.709 54.454  98.582  1.00 26.88 ?  2018 HOH A O     1 
HETATM 19166 O O     . HOH S 7 .    ? 9.486   67.875  95.246  1.00 29.02 ?  2019 HOH A O     1 
HETATM 19167 O O     . HOH S 7 .    ? -34.663 50.037  84.663  1.00 22.44 ?  2020 HOH A O     1 
HETATM 19168 O O     . HOH S 7 .    ? -8.154  77.223  93.198  1.00 18.33 ?  2021 HOH A O     1 
HETATM 19169 O O     . HOH S 7 .    ? -15.244 59.018  127.839 1.00 29.38 ?  2022 HOH A O     1 
HETATM 19170 O O     . HOH S 7 .    ? -26.146 69.993  96.838  1.00 22.68 ?  2023 HOH A O     1 
HETATM 19171 O O     . HOH S 7 .    ? -56.589 68.951  101.113 1.00 30.13 ?  2024 HOH A O     1 
HETATM 19172 O O     . HOH S 7 .    ? -5.255  72.660  108.574 1.00 26.69 ?  2025 HOH A O     1 
HETATM 19173 O O     . HOH S 7 .    ? 2.635   77.853  99.342  1.00 21.82 ?  2026 HOH A O     1 
HETATM 19174 O O     . HOH S 7 .    ? 22.694  76.058  116.589 1.00 23.81 ?  2027 HOH A O     1 
HETATM 19175 O O     . HOH S 7 .    ? 23.117  81.499  113.634 1.00 37.53 ?  2028 HOH A O     1 
HETATM 19176 O O     . HOH S 7 .    ? -25.676 59.352  115.714 1.00 20.05 ?  2029 HOH A O     1 
HETATM 19177 O O     . HOH S 7 .    ? 8.658   64.884  95.612  1.00 25.32 ?  2030 HOH A O     1 
HETATM 19178 O O     . HOH S 7 .    ? 22.919  72.747  100.077 1.00 32.53 ?  2031 HOH A O     1 
HETATM 19179 O O     . HOH S 7 .    ? -9.403  83.865  81.925  1.00 32.65 ?  2032 HOH A O     1 
HETATM 19180 O O     . HOH S 7 .    ? -17.573 88.502  108.407 1.00 27.94 ?  2033 HOH A O     1 
HETATM 19181 O O     . HOH S 7 .    ? -31.254 66.285  128.439 1.00 35.21 ?  2034 HOH A O     1 
HETATM 19182 O O     . HOH S 7 .    ? 25.670  64.247  104.027 1.00 25.25 ?  2035 HOH A O     1 
HETATM 19183 O O     . HOH S 7 .    ? -11.421 53.918  101.623 1.00 22.29 ?  2036 HOH A O     1 
HETATM 19184 O O     . HOH S 7 .    ? -43.043 77.595  79.350  1.00 21.22 ?  2037 HOH A O     1 
HETATM 19185 O O     . HOH S 7 .    ? -32.777 64.498  123.383 1.00 25.73 ?  2038 HOH A O     1 
HETATM 19186 O O     . HOH S 7 .    ? 25.132  69.328  115.511 1.00 22.85 ?  2039 HOH A O     1 
HETATM 19187 O O     . HOH S 7 .    ? -23.238 67.686  131.143 1.00 33.04 ?  2040 HOH A O     1 
HETATM 19188 O O     . HOH S 7 .    ? -31.981 38.699  100.806 1.00 37.30 ?  2041 HOH A O     1 
HETATM 19189 O O     . HOH S 7 .    ? -30.602 72.913  99.892  1.00 32.01 ?  2042 HOH A O     1 
HETATM 19190 O O     . HOH S 7 .    ? -38.216 72.846  88.204  1.00 27.79 ?  2043 HOH A O     1 
HETATM 19191 O O     . HOH S 7 .    ? -68.125 59.825  70.614  1.00 24.11 ?  2044 HOH A O     1 
HETATM 19192 O O     . HOH S 7 .    ? -34.591 54.909  72.302  1.00 26.79 ?  2045 HOH A O     1 
HETATM 19193 O O     . HOH S 7 .    ? -0.282  67.101  87.394  1.00 31.64 ?  2046 HOH A O     1 
HETATM 19194 O O     . HOH S 7 .    ? 2.139   76.385  118.371 1.00 22.44 ?  2047 HOH A O     1 
HETATM 19195 O O     . HOH S 7 .    ? -35.781 66.238  95.595  1.00 34.70 ?  2048 HOH A O     1 
HETATM 19196 O O     . HOH S 7 .    ? -64.971 70.770  84.217  1.00 31.96 ?  2049 HOH A O     1 
HETATM 19197 O O     . HOH S 7 .    ? 20.567  83.161  102.744 1.00 31.67 ?  2050 HOH A O     1 
HETATM 19198 O O     . HOH S 7 .    ? -7.645  50.889  53.953  1.00 26.86 ?  2051 HOH A O     1 
HETATM 19199 O O     . HOH S 7 .    ? -45.619 57.702  103.352 1.00 23.07 ?  2052 HOH A O     1 
HETATM 19200 O O     . HOH S 7 .    ? -22.920 47.809  84.266  1.00 26.73 ?  2053 HOH A O     1 
HETATM 19201 O O     . HOH S 7 .    ? -48.319 54.611  59.145  1.00 31.52 ?  2054 HOH A O     1 
HETATM 19202 O O     . HOH S 7 .    ? -35.821 59.955  89.766  1.00 25.48 ?  2055 HOH A O     1 
HETATM 19203 O O     . HOH S 7 .    ? -9.433  60.402  85.389  1.00 18.30 ?  2056 HOH A O     1 
HETATM 19204 O O     . HOH S 7 .    ? -38.366 39.798  75.603  1.00 25.38 ?  2057 HOH A O     1 
HETATM 19205 O O     . HOH S 7 .    ? -1.866  54.223  103.066 1.00 19.22 ?  2058 HOH A O     1 
HETATM 19206 O O     . HOH S 7 .    ? -29.000 83.999  105.637 1.00 19.84 ?  2059 HOH A O     1 
HETATM 19207 O O     . HOH S 7 .    ? -65.953 72.552  72.467  1.00 31.39 ?  2060 HOH A O     1 
HETATM 19208 O O     . HOH S 7 .    ? -25.065 69.340  75.410  1.00 25.16 ?  2061 HOH A O     1 
HETATM 19209 O O     . HOH S 7 .    ? -38.743 76.034  99.821  1.00 22.12 ?  2062 HOH A O     1 
HETATM 19210 O O     . HOH S 7 .    ? -46.003 54.937  93.317  1.00 13.76 ?  2063 HOH A O     1 
HETATM 19211 O O     . HOH S 7 .    ? -54.586 45.044  93.318  1.00 26.84 ?  2064 HOH A O     1 
HETATM 19212 O O     . HOH S 7 .    ? -16.709 95.889  91.084  1.00 34.09 ?  2065 HOH A O     1 
HETATM 19213 O O     . HOH S 7 .    ? 14.017  78.394  122.383 1.00 29.21 ?  2066 HOH A O     1 
HETATM 19214 O O     . HOH S 7 .    ? -3.342  77.269  102.869 1.00 27.94 ?  2067 HOH A O     1 
HETATM 19215 O O     . HOH S 7 .    ? 2.691   66.465  121.839 1.00 33.62 ?  2068 HOH A O     1 
HETATM 19216 O O     . HOH S 7 .    ? -17.916 85.676  78.411  1.00 20.78 ?  2069 HOH A O     1 
HETATM 19217 O O     . HOH S 7 .    ? 12.764  63.437  122.410 1.00 28.85 ?  2070 HOH A O     1 
HETATM 19218 O O     . HOH S 7 .    ? 6.880   54.992  100.117 1.00 16.08 ?  2071 HOH A O     1 
HETATM 19219 O O     . HOH S 7 .    ? -35.052 27.123  73.051  1.00 37.57 ?  2072 HOH A O     1 
HETATM 19220 O O     . HOH S 7 .    ? 18.743  62.106  95.654  1.00 30.62 ?  2073 HOH A O     1 
HETATM 19221 O O     . HOH S 7 .    ? -43.154 28.379  88.022  1.00 33.83 ?  2074 HOH A O     1 
HETATM 19222 O O     . HOH S 7 .    ? -65.250 54.992  81.765  1.00 24.00 ?  2075 HOH A O     1 
HETATM 19223 O O     . HOH S 7 .    ? -31.477 74.292  88.734  1.00 27.16 ?  2076 HOH A O     1 
HETATM 19224 O O     . HOH S 7 .    ? -31.572 91.465  81.471  1.00 24.19 ?  2077 HOH A O     1 
HETATM 19225 O O     . HOH S 7 .    ? 21.696  72.415  117.584 1.00 21.06 ?  2078 HOH A O     1 
HETATM 19226 O O     . HOH S 7 .    ? -5.296  55.568  102.515 1.00 26.77 ?  2079 HOH A O     1 
HETATM 19227 O O     . HOH S 7 .    ? -42.928 65.913  64.668  1.00 26.91 ?  2080 HOH A O     1 
HETATM 19228 O O     . HOH S 7 .    ? -10.533 64.418  126.496 1.00 29.47 ?  2081 HOH A O     1 
HETATM 19229 O O     . HOH S 7 .    ? -38.266 67.692  99.334  1.00 24.34 ?  2082 HOH A O     1 
HETATM 19230 O O     . HOH S 7 .    ? -9.354  51.797  108.813 1.00 25.71 ?  2083 HOH A O     1 
HETATM 19231 O O     . HOH S 7 .    ? -1.890  79.766  98.550  1.00 34.31 ?  2084 HOH A O     1 
HETATM 19232 O O     . HOH S 7 .    ? -47.390 77.214  93.092  1.00 22.58 ?  2085 HOH A O     1 
HETATM 19233 O O     . HOH S 7 .    ? -35.477 64.741  67.074  1.00 25.73 ?  2086 HOH A O     1 
HETATM 19234 O O     . HOH S 7 .    ? -13.115 40.846  56.626  1.00 36.08 ?  2087 HOH A O     1 
HETATM 19235 O O     . HOH S 7 .    ? -39.803 86.449  90.328  1.00 22.90 ?  2088 HOH A O     1 
HETATM 19236 O O     . HOH S 7 .    ? -22.368 76.996  71.113  1.00 18.44 ?  2089 HOH A O     1 
HETATM 19237 O O     . HOH S 7 .    ? -4.993  82.343  126.697 1.00 32.47 ?  2090 HOH A O     1 
HETATM 19238 O O     . HOH S 7 .    ? -21.792 59.175  123.714 1.00 23.71 ?  2091 HOH A O     1 
HETATM 19239 O O     . HOH S 7 .    ? -25.773 68.134  91.980  1.00 22.37 ?  2092 HOH A O     1 
HETATM 19240 O O     . HOH S 7 .    ? 12.960  88.679  117.727 1.00 27.34 ?  2093 HOH A O     1 
HETATM 19241 O O     . HOH S 7 .    ? -1.400  70.007  117.790 1.00 20.43 ?  2094 HOH A O     1 
HETATM 19242 O O     . HOH S 7 .    ? -39.209 77.965  70.700  1.00 25.09 ?  2095 HOH A O     1 
HETATM 19243 O O     . HOH S 7 .    ? 21.444  71.171  96.536  1.00 36.41 ?  2096 HOH A O     1 
HETATM 19244 O O     . HOH S 7 .    ? -31.013 95.940  106.373 1.00 27.15 ?  2097 HOH A O     1 
HETATM 19245 O O     . HOH S 7 .    ? 2.294   86.383  127.633 1.00 35.08 ?  2098 HOH A O     1 
HETATM 19246 O O     . HOH S 7 .    ? -64.698 57.821  68.009  1.00 33.51 ?  2099 HOH A O     1 
HETATM 19247 O O     . HOH S 7 .    ? -31.533 34.319  73.736  1.00 40.81 ?  2100 HOH A O     1 
HETATM 19248 O O     . HOH S 7 .    ? -29.849 58.353  80.303  1.00 21.90 ?  2101 HOH A O     1 
HETATM 19249 O O     . HOH S 7 .    ? -63.546 62.501  98.997  1.00 28.55 ?  2102 HOH A O     1 
HETATM 19250 O O     . HOH S 7 .    ? -39.353 51.892  76.865  1.00 29.68 ?  2103 HOH A O     1 
HETATM 19251 O O     . HOH S 7 .    ? -37.630 64.327  83.554  1.00 26.99 ?  2104 HOH A O     1 
HETATM 19252 O O     . HOH S 7 .    ? 10.981  85.228  126.196 1.00 25.29 ?  2105 HOH A O     1 
HETATM 19253 O O     . HOH S 7 .    ? -33.368 57.129  73.494  1.00 27.20 ?  2106 HOH A O     1 
HETATM 19254 O O     . HOH S 7 .    ? 10.826  64.658  115.953 1.00 28.44 ?  2107 HOH A O     1 
HETATM 19255 O O     . HOH S 7 .    ? -0.464  67.544  118.871 1.00 26.00 ?  2108 HOH A O     1 
HETATM 19256 O O     . HOH S 7 .    ? -30.963 59.350  82.923  1.00 30.17 ?  2109 HOH A O     1 
HETATM 19257 O O     . HOH S 7 .    ? -42.062 88.688  94.857  1.00 29.09 ?  2110 HOH A O     1 
HETATM 19258 O O     . HOH S 7 .    ? -14.046 95.621  121.709 1.00 38.65 ?  2111 HOH A O     1 
HETATM 19259 O O     . HOH S 7 .    ? -11.443 43.382  75.248  1.00 24.57 ?  2112 HOH A O     1 
HETATM 19260 O O     . HOH S 7 .    ? -6.723  80.514  79.633  1.00 29.59 ?  2113 HOH A O     1 
HETATM 19261 O O     . HOH S 7 .    ? -36.483 80.765  76.564  1.00 20.95 ?  2114 HOH A O     1 
HETATM 19262 O O     . HOH S 7 .    ? 0.306   64.135  108.593 1.00 15.57 ?  2115 HOH A O     1 
HETATM 19263 O O     . HOH S 7 .    ? -18.760 68.943  105.855 1.00 20.71 ?  2116 HOH A O     1 
HETATM 19264 O O     . HOH S 7 .    ? -11.833 83.534  75.321  1.00 36.15 ?  2117 HOH A O     1 
HETATM 19265 O O     . HOH S 7 .    ? -39.888 47.067  105.188 1.00 28.19 ?  2118 HOH A O     1 
HETATM 19266 O O     . HOH S 7 .    ? -0.182  74.178  97.229  1.00 32.15 ?  2119 HOH A O     1 
HETATM 19267 O O     . HOH S 7 .    ? -28.579 64.820  65.339  1.00 29.82 ?  2120 HOH A O     1 
HETATM 19268 O O     . HOH S 7 .    ? -21.995 67.395  74.639  1.00 32.43 ?  2121 HOH A O     1 
HETATM 19269 O O     . HOH S 7 .    ? -43.447 56.249  93.155  1.00 13.29 ?  2122 HOH A O     1 
HETATM 19270 O O     . HOH S 7 .    ? -41.641 66.971  71.323  1.00 25.38 ?  2123 HOH A O     1 
HETATM 19271 O O     . HOH S 7 .    ? -40.292 37.677  86.474  1.00 28.32 ?  2124 HOH A O     1 
HETATM 19272 O O     . HOH S 7 .    ? 2.912   64.737  114.764 1.00 25.20 ?  2125 HOH A O     1 
HETATM 19273 O O     . HOH S 7 .    ? -41.172 70.425  93.848  1.00 25.15 ?  2126 HOH A O     1 
HETATM 19274 O O     . HOH S 7 .    ? 0.002   87.258  126.047 1.00 27.84 ?  2127 HOH A O     1 
HETATM 19275 O O     . HOH S 7 .    ? -11.194 62.983  69.756  1.00 26.49 ?  2128 HOH A O     1 
HETATM 19276 O O     . HOH S 7 .    ? -0.874  74.845  117.877 1.00 30.45 ?  2129 HOH A O     1 
HETATM 19277 O O     . HOH S 7 .    ? -21.609 50.144  109.799 1.00 35.36 ?  2130 HOH A O     1 
HETATM 19278 O O     . HOH S 7 .    ? -10.822 76.946  107.630 1.00 19.09 ?  2131 HOH A O     1 
HETATM 19279 O O     . HOH S 7 .    ? -68.128 64.161  86.166  1.00 28.31 ?  2132 HOH A O     1 
HETATM 19280 O O     . HOH S 7 .    ? -36.817 71.500  122.574 1.00 31.10 ?  2133 HOH A O     1 
HETATM 19281 O O     . HOH S 7 .    ? -19.413 89.152  114.162 1.00 34.92 ?  2134 HOH A O     1 
HETATM 19282 O O     . HOH S 7 .    ? -33.432 84.297  129.685 1.00 37.35 ?  2135 HOH A O     1 
HETATM 19283 O O     . HOH S 7 .    ? -16.407 42.911  73.095  1.00 32.51 ?  2136 HOH A O     1 
HETATM 19284 O O     . HOH S 7 .    ? -63.095 67.299  67.211  1.00 25.49 ?  2137 HOH A O     1 
HETATM 19285 O O     . HOH S 7 .    ? 1.065   57.098  108.932 1.00 15.90 ?  2138 HOH A O     1 
HETATM 19286 O O     . HOH S 7 .    ? -11.786 59.791  107.706 1.00 29.16 ?  2139 HOH A O     1 
HETATM 19287 O O     . HOH S 7 .    ? 18.582  75.133  98.028  1.00 32.74 ?  2140 HOH A O     1 
HETATM 19288 O O     . HOH S 7 .    ? -27.102 79.898  70.890  1.00 30.20 ?  2141 HOH A O     1 
HETATM 19289 O O     . HOH S 7 .    ? -14.468 58.261  111.108 1.00 32.75 ?  2142 HOH A O     1 
HETATM 19290 O O     . HOH S 7 .    ? -40.719 56.235  78.902  1.00 27.32 ?  2143 HOH A O     1 
HETATM 19291 O O     . HOH S 7 .    ? -2.941  76.032  78.420  1.00 16.62 ?  2144 HOH A O     1 
HETATM 19292 O O     . HOH S 7 .    ? -6.869  92.685  120.820 1.00 30.80 ?  2145 HOH A O     1 
HETATM 19293 O O     . HOH S 7 .    ? -50.012 54.055  75.075  1.00 18.42 ?  2146 HOH A O     1 
HETATM 19294 O O     . HOH S 7 .    ? -26.775 84.322  74.982  1.00 30.40 ?  2147 HOH A O     1 
HETATM 19295 O O     . HOH S 7 .    ? -19.579 57.743  107.988 1.00 25.84 ?  2148 HOH A O     1 
HETATM 19296 O O     . HOH S 7 .    ? -31.389 78.291  91.910  1.00 23.19 ?  2149 HOH A O     1 
HETATM 19297 O O     . HOH S 7 .    ? -33.593 53.464  110.694 1.00 39.12 ?  2150 HOH A O     1 
HETATM 19298 O O     . HOH S 7 .    ? -30.454 67.811  102.383 1.00 29.88 ?  2151 HOH A O     1 
HETATM 19299 O O     . HOH S 7 .    ? -28.625 42.002  94.224  1.00 39.34 ?  2152 HOH A O     1 
HETATM 19300 O O     . HOH S 7 .    ? -14.957 68.716  66.673  1.00 35.56 ?  2153 HOH A O     1 
HETATM 19301 O O     . HOH S 7 .    ? -51.695 79.576  79.507  1.00 31.48 ?  2154 HOH A O     1 
HETATM 19302 O O     . HOH S 7 .    ? -44.500 69.541  110.007 1.00 30.54 ?  2155 HOH A O     1 
HETATM 19303 O O     . HOH S 7 .    ? -39.408 66.814  95.492  1.00 25.71 ?  2156 HOH A O     1 
HETATM 19304 O O     . HOH S 7 .    ? -5.442  47.403  56.799  1.00 31.99 ?  2157 HOH A O     1 
HETATM 19305 O O     . HOH S 7 .    ? -15.465 55.311  52.037  1.00 37.93 ?  2158 HOH A O     1 
HETATM 19306 O O     . HOH S 7 .    ? -41.658 64.181  59.367  1.00 23.01 ?  2159 HOH A O     1 
HETATM 19307 O O     . HOH S 7 .    ? -52.858 29.518  74.131  1.00 42.30 ?  2160 HOH A O     1 
HETATM 19308 O O     . HOH S 7 .    ? -62.569 59.960  96.844  1.00 24.91 ?  2161 HOH A O     1 
HETATM 19309 O O     . HOH S 7 .    ? -0.738  52.630  59.935  1.00 28.59 ?  2162 HOH A O     1 
HETATM 19310 O O     . HOH S 7 .    ? -11.195 66.696  128.742 1.00 30.92 ?  2163 HOH A O     1 
HETATM 19311 O O     . HOH S 7 .    ? 6.665   91.235  120.041 1.00 29.18 ?  2164 HOH A O     1 
HETATM 19312 O O     . HOH S 7 .    ? -3.488  55.869  96.989  1.00 34.52 ?  2165 HOH A O     1 
HETATM 19313 O O     . HOH S 7 .    ? -57.533 31.732  89.329  1.00 36.59 ?  2166 HOH A O     1 
HETATM 19314 O O     . HOH S 7 .    ? -20.726 54.678  100.108 1.00 23.11 ?  2167 HOH A O     1 
HETATM 19315 O O     . HOH S 7 .    ? 14.820  82.489  120.813 1.00 26.03 ?  2168 HOH A O     1 
HETATM 19316 O O     . HOH S 7 .    ? -9.062  41.139  70.374  1.00 28.06 ?  2169 HOH A O     1 
HETATM 19317 O O     . HOH S 7 .    ? 12.720  64.198  117.868 1.00 29.35 ?  2170 HOH A O     1 
HETATM 19318 O O     . HOH S 7 .    ? -44.091 90.637  101.135 1.00 28.49 ?  2171 HOH A O     1 
HETATM 19319 O O     . HOH S 7 .    ? 4.394   86.013  102.316 1.00 26.02 ?  2172 HOH A O     1 
HETATM 19320 O O     . HOH S 7 .    ? -28.425 67.309  94.386  1.00 37.88 ?  2173 HOH A O     1 
HETATM 19321 O O     . HOH S 7 .    ? 20.801  75.266  101.845 1.00 32.48 ?  2174 HOH A O     1 
HETATM 19322 O O     . HOH S 7 .    ? -59.627 42.251  90.783  1.00 35.82 ?  2175 HOH A O     1 
HETATM 19323 O O     . HOH S 7 .    ? -14.980 48.087  52.378  1.00 33.06 ?  2176 HOH A O     1 
HETATM 19324 O O     . HOH S 7 .    ? -31.696 41.096  99.388  1.00 30.93 ?  2177 HOH A O     1 
HETATM 19325 O O     . HOH S 7 .    ? -66.908 68.636  85.009  1.00 25.28 ?  2178 HOH A O     1 
HETATM 19326 O O     . HOH S 7 .    ? 19.470  64.283  94.471  1.00 29.09 ?  2179 HOH A O     1 
HETATM 19327 O O     . HOH S 7 .    ? -40.221 47.446  107.961 1.00 30.80 ?  2180 HOH A O     1 
HETATM 19328 O O     . HOH S 7 .    ? -66.626 64.305  88.940  1.00 28.14 ?  2181 HOH A O     1 
HETATM 19329 O O     . HOH S 7 .    ? -34.725 65.493  75.404  1.00 31.64 ?  2182 HOH A O     1 
HETATM 19330 O O     . HOH S 7 .    ? -11.843 53.232  104.266 1.00 33.26 ?  2183 HOH A O     1 
HETATM 19331 O O     . HOH S 7 .    ? -7.348  86.101  83.329  1.00 36.42 ?  2184 HOH A O     1 
HETATM 19332 O O     . HOH S 7 .    ? -37.331 82.743  122.301 1.00 28.73 ?  2185 HOH A O     1 
HETATM 19333 O O     . HOH S 7 .    ? 27.469  65.371  114.091 1.00 29.10 ?  2186 HOH A O     1 
HETATM 19334 O O     . HOH S 7 .    ? -62.512 66.739  61.278  1.00 32.60 ?  2187 HOH A O     1 
HETATM 19335 O O     . HOH S 7 .    ? -28.549 82.881  103.101 1.00 21.62 ?  2188 HOH A O     1 
HETATM 19336 O O     . HOH S 7 .    ? -19.554 54.654  119.849 1.00 31.99 ?  2189 HOH A O     1 
HETATM 19337 O O     . HOH S 7 .    ? -18.306 53.834  99.981  1.00 30.20 ?  2190 HOH A O     1 
HETATM 19338 O O     . HOH S 7 .    ? -23.645 75.972  134.937 1.00 30.46 ?  2191 HOH A O     1 
HETATM 19339 O O     . HOH S 7 .    ? -17.273 54.765  118.798 1.00 33.11 ?  2192 HOH A O     1 
HETATM 19340 O O     . HOH S 7 .    ? -61.471 69.238  92.714  1.00 37.01 ?  2193 HOH A O     1 
HETATM 19341 O O     . HOH S 7 .    ? -36.889 72.966  127.506 1.00 35.09 ?  2194 HOH A O     1 
HETATM 19342 O O     . HOH S 7 .    ? -48.324 79.985  96.665  1.00 32.34 ?  2195 HOH A O     1 
HETATM 19343 O O     . HOH S 7 .    ? -61.063 59.479  63.071  1.00 29.69 ?  2196 HOH A O     1 
HETATM 19344 O O     . HOH S 7 .    ? -35.178 75.445  127.596 1.00 28.45 ?  2197 HOH A O     1 
HETATM 19345 O O     . HOH S 7 .    ? -23.186 64.471  71.626  1.00 32.31 ?  2198 HOH A O     1 
HETATM 19346 O O     . HOH S 7 .    ? -50.806 55.000  106.070 1.00 35.06 ?  2199 HOH A O     1 
HETATM 19347 O O     . HOH S 7 .    ? -46.185 78.412  90.941  1.00 19.39 ?  2200 HOH A O     1 
HETATM 19348 O O     . HOH S 7 .    ? -24.834 97.222  123.103 1.00 41.38 ?  2201 HOH A O     1 
HETATM 19349 O O     . HOH S 7 .    ? -54.690 62.293  104.528 1.00 35.03 ?  2202 HOH A O     1 
HETATM 19350 O O     . HOH S 7 .    ? -22.425 85.129  106.219 1.00 28.94 ?  2203 HOH A O     1 
HETATM 19351 O O     . HOH S 7 .    ? 0.864   69.495  88.713  1.00 28.02 ?  2204 HOH A O     1 
HETATM 19352 O O     . HOH S 7 .    ? 16.275  64.744  118.686 1.00 28.47 ?  2205 HOH A O     1 
HETATM 19353 O O     . HOH S 7 .    ? -34.524 59.112  107.476 1.00 27.45 ?  2206 HOH A O     1 
HETATM 19354 O O     . HOH S 7 .    ? -52.100 54.974  71.217  1.00 20.41 ?  2207 HOH A O     1 
HETATM 19355 O O     . HOH S 7 .    ? -2.069  83.447  116.953 1.00 27.86 ?  2208 HOH A O     1 
HETATM 19356 O O     . HOH S 7 .    ? -62.131 68.387  90.500  1.00 35.24 ?  2209 HOH A O     1 
HETATM 19357 O O     . HOH S 7 .    ? -53.324 66.491  103.122 1.00 30.03 ?  2210 HOH A O     1 
HETATM 19358 O O     . HOH S 7 .    ? -46.506 62.825  54.797  1.00 32.40 ?  2211 HOH A O     1 
HETATM 19359 O O     . HOH S 7 .    ? -47.977 63.814  57.065  1.00 27.21 ?  2212 HOH A O     1 
HETATM 19360 O O     . HOH S 7 .    ? -26.283 74.468  134.258 1.00 32.83 ?  2213 HOH A O     1 
HETATM 19361 O O     . HOH S 7 .    ? -60.422 64.065  93.230  1.00 26.45 ?  2214 HOH A O     1 
HETATM 19362 O O     . HOH S 7 .    ? -27.267 60.506  124.041 1.00 31.37 ?  2215 HOH A O     1 
HETATM 19363 O O     . HOH S 7 .    ? -28.907 57.342  89.580  1.00 24.68 ?  2216 HOH A O     1 
HETATM 19364 O O     . HOH S 7 .    ? -64.531 50.908  74.254  1.00 33.96 ?  2217 HOH A O     1 
HETATM 19365 O O     . HOH S 7 .    ? -25.710 63.700  68.154  1.00 32.45 ?  2218 HOH A O     1 
HETATM 19366 O O     . HOH S 7 .    ? -22.709 74.250  70.643  1.00 26.15 ?  2219 HOH A O     1 
HETATM 19367 O O     . HOH S 7 .    ? -26.115 67.720  95.086  1.00 28.09 ?  2220 HOH A O     1 
HETATM 19368 O O     . HOH S 7 .    ? -64.897 62.899  69.351  1.00 29.22 ?  2221 HOH A O     1 
HETATM 19369 O O     . HOH S 7 .    ? -29.249 67.186  97.751  1.00 32.08 ?  2222 HOH A O     1 
HETATM 19370 O O     . HOH S 7 .    ? -40.235 67.769  90.261  1.00 25.71 ?  2223 HOH A O     1 
HETATM 19371 O O     . HOH S 7 .    ? -23.158 71.503  75.114  1.00 27.71 ?  2224 HOH A O     1 
HETATM 19372 O O     . HOH S 7 .    ? -15.651 57.742  107.513 1.00 30.06 ?  2225 HOH A O     1 
HETATM 19373 O O     . HOH S 7 .    ? -55.665 57.667  103.310 1.00 27.16 ?  2226 HOH A O     1 
HETATM 19374 O O     . HOH S 7 .    ? -22.542 92.122  100.036 1.00 31.25 ?  2227 HOH A O     1 
HETATM 19375 O O     . HOH S 7 .    ? -11.801 64.051  52.217  1.00 38.41 ?  2228 HOH A O     1 
HETATM 19376 O O     . HOH S 7 .    ? -34.249 60.926  87.629  1.00 28.38 ?  2229 HOH A O     1 
HETATM 19377 O O     . HOH S 7 .    ? -53.007 56.672  74.804  1.00 21.50 ?  2230 HOH A O     1 
HETATM 19378 O O     . HOH S 7 .    ? -48.138 32.866  86.947  1.00 33.68 ?  2231 HOH A O     1 
HETATM 19379 O O     . HOH S 7 .    ? -47.242 30.520  74.361  1.00 36.69 ?  2232 HOH A O     1 
HETATM 19380 O O     . HOH S 7 .    ? -21.028 86.841  108.773 1.00 32.47 ?  2233 HOH A O     1 
HETATM 19381 O O     . HOH S 7 .    ? -27.331 65.462  104.075 1.00 25.21 ?  2234 HOH A O     1 
HETATM 19382 O O     . HOH S 7 .    ? -31.267 59.014  61.362  1.00 28.97 ?  2235 HOH A O     1 
HETATM 19383 O O     . HOH S 7 .    ? 22.599  64.753  94.446  1.00 39.27 ?  2236 HOH A O     1 
HETATM 19384 O O     . HOH S 7 .    ? -21.470 61.624  82.005  1.00 31.26 ?  2237 HOH A O     1 
HETATM 19385 O O     . HOH S 7 .    ? -33.247 84.359  78.017  1.00 22.27 ?  2238 HOH A O     1 
HETATM 19386 O O     . HOH S 7 .    ? -64.276 65.188  67.219  1.00 34.25 ?  2239 HOH A O     1 
HETATM 19387 O O     . HOH S 7 .    ? -10.233 66.797  75.534  1.00 28.76 ?  2240 HOH A O     1 
HETATM 19388 O O     . HOH S 7 .    ? -27.295 92.136  77.624  1.00 30.98 ?  2241 HOH A O     1 
HETATM 19389 O O     . HOH S 7 .    ? -34.964 76.224  88.389  1.00 24.32 ?  2242 HOH A O     1 
HETATM 19390 O O     . HOH S 7 .    ? -39.556 35.482  90.203  1.00 33.40 ?  2243 HOH A O     1 
HETATM 19391 O O     . HOH S 7 .    ? -10.276 66.904  133.669 1.00 38.74 ?  2244 HOH A O     1 
HETATM 19392 O O     . HOH S 7 .    ? -52.947 47.961  59.029  1.00 32.65 ?  2245 HOH A O     1 
HETATM 19393 O O     . HOH S 7 .    ? -7.010  54.888  83.650  1.00 24.30 ?  2246 HOH A O     1 
HETATM 19394 O O     . HOH S 7 .    ? 6.779   66.763  95.200  1.00 31.32 ?  2247 HOH A O     1 
HETATM 19395 O O     . HOH S 7 .    ? -52.817 73.793  62.711  1.00 19.36 ?  2248 HOH A O     1 
HETATM 19396 O O     . HOH S 7 .    ? -35.663 73.618  87.408  1.00 27.53 ?  2249 HOH A O     1 
HETATM 19397 O O     . HOH S 7 .    ? 4.834   60.462  99.613  1.00 20.24 ?  2250 HOH A O     1 
HETATM 19398 O O     . HOH S 7 .    ? -28.087 63.950  91.856  1.00 28.16 ?  2251 HOH A O     1 
HETATM 19399 O O     . HOH S 7 .    ? -27.705 51.200  111.016 1.00 30.53 ?  2252 HOH A O     1 
HETATM 19400 O O     . HOH S 7 .    ? -30.861 82.205  101.786 1.00 19.04 ?  2253 HOH A O     1 
HETATM 19401 O O     . HOH S 7 .    ? -32.991 68.577  103.109 1.00 24.18 ?  2254 HOH A O     1 
HETATM 19402 O O     . HOH S 7 .    ? -9.336  67.060  130.899 1.00 35.08 ?  2255 HOH A O     1 
HETATM 19403 O O     . HOH S 7 .    ? -27.406 58.324  59.448  1.00 38.21 ?  2256 HOH A O     1 
HETATM 19404 O O     . HOH S 7 .    ? -10.590 78.692  93.472  1.00 15.83 ?  2257 HOH A O     1 
HETATM 19405 O O     . HOH S 7 .    ? -29.516 60.739  122.294 1.00 30.62 ?  2258 HOH A O     1 
HETATM 19406 O O     . HOH S 7 .    ? -31.626 76.506  75.285  1.00 26.81 ?  2259 HOH A O     1 
HETATM 19407 O O     . HOH S 7 .    ? -16.671 47.001  80.469  1.00 37.32 ?  2260 HOH A O     1 
HETATM 19408 O O     . HOH S 7 .    ? -31.039 48.892  87.584  1.00 26.21 ?  2261 HOH A O     1 
HETATM 19409 O O     . HOH S 7 .    ? -25.911 100.749 92.571  1.00 36.71 ?  2262 HOH A O     1 
HETATM 19410 O O     . HOH S 7 .    ? -63.421 61.076  94.678  1.00 31.80 ?  2263 HOH A O     1 
HETATM 19411 O O     . HOH S 7 .    ? -2.695  56.671  71.571  1.00 27.59 ?  2264 HOH A O     1 
HETATM 19412 O O     . HOH S 7 .    ? 17.004  84.061  114.489 1.00 34.80 ?  2265 HOH A O     1 
HETATM 19413 O O     . HOH S 7 .    ? -46.442 56.470  55.345  1.00 29.81 ?  2266 HOH A O     1 
HETATM 19414 O O     . HOH S 7 .    ? -67.657 54.477  83.100  1.00 31.70 ?  2267 HOH A O     1 
HETATM 19415 O O     . HOH S 7 .    ? -53.149 66.531  105.831 1.00 30.19 ?  2268 HOH A O     1 
HETATM 19416 O O     . HOH S 7 .    ? -25.031 65.835  98.180  1.00 22.93 ?  2269 HOH A O     1 
HETATM 19417 O O     . HOH S 7 .    ? -30.710 47.490  72.750  1.00 35.69 ?  2270 HOH A O     1 
HETATM 19418 O O     . HOH S 7 .    ? -26.026 64.911  65.568  1.00 36.26 ?  2271 HOH A O     1 
HETATM 19419 O O     . HOH S 7 .    ? -35.462 54.870  108.758 1.00 31.17 ?  2272 HOH A O     1 
HETATM 19420 O O     . HOH S 7 .    ? -67.437 65.936  84.225  1.00 23.23 ?  2273 HOH A O     1 
HETATM 19421 O O     . HOH S 7 .    ? 12.669  88.487  120.280 1.00 30.67 ?  2274 HOH A O     1 
HETATM 19422 O O     . HOH S 7 .    ? -8.519  81.462  78.329  1.00 37.64 ?  2275 HOH A O     1 
HETATM 19423 O O     . HOH S 7 .    ? -53.652 45.544  95.970  1.00 29.81 ?  2276 HOH A O     1 
HETATM 19424 O O     . HOH S 7 .    ? 3.022   64.210  94.972  1.00 31.73 ?  2277 HOH A O     1 
HETATM 19425 O O     . HOH S 7 .    ? -39.761 69.963  119.741 1.00 31.24 ?  2278 HOH A O     1 
HETATM 19426 O O     . HOH S 7 .    ? -27.595 65.432  87.288  1.00 33.44 ?  2279 HOH A O     1 
HETATM 19427 O O     . HOH S 7 .    ? -45.779 28.577  88.635  1.00 33.74 ?  2280 HOH A O     1 
HETATM 19428 O O     . HOH S 7 .    ? 16.456  66.282  91.538  1.00 35.21 ?  2281 HOH A O     1 
HETATM 19429 O O     . HOH S 7 .    ? -49.838 59.152  56.169  1.00 29.97 ?  2282 HOH A O     1 
HETATM 19430 O O     . HOH S 7 .    ? -34.047 51.925  72.414  1.00 31.05 ?  2283 HOH A O     1 
HETATM 19431 O O     . HOH S 7 .    ? -34.642 42.660  69.420  1.00 31.92 ?  2284 HOH A O     1 
HETATM 19432 O O     . HOH S 7 .    ? 22.765  79.229  101.514 1.00 36.13 ?  2285 HOH A O     1 
HETATM 19433 O O     . HOH S 7 .    ? -52.856 64.245  101.924 1.00 24.71 ?  2286 HOH A O     1 
HETATM 19434 O O     . HOH S 7 .    ? -35.786 39.441  72.787  1.00 35.09 ?  2287 HOH A O     1 
HETATM 19435 O O     . HOH S 7 .    ? -27.606 59.370  117.755 1.00 26.39 ?  2288 HOH A O     1 
HETATM 19436 O O     . HOH S 7 .    ? -43.303 80.132  76.189  1.00 31.07 ?  2289 HOH A O     1 
HETATM 19437 O O     . HOH S 7 .    ? -37.837 63.229  115.582 1.00 32.30 ?  2290 HOH A O     1 
HETATM 19438 O O     . HOH S 7 .    ? -38.412 74.276  94.076  1.00 25.18 ?  2291 HOH A O     1 
HETATM 19439 O O     . HOH S 7 .    ? -47.393 80.846  90.439  1.00 32.37 ?  2292 HOH A O     1 
HETATM 19440 O O     . HOH S 7 .    ? -56.923 74.633  80.167  1.00 30.99 ?  2293 HOH A O     1 
HETATM 19441 O O     . HOH S 7 .    ? -35.184 38.964  95.732  1.00 37.17 ?  2294 HOH A O     1 
HETATM 19442 O O     . HOH S 7 .    ? -42.246 61.604  103.740 1.00 23.06 ?  2295 HOH A O     1 
HETATM 19443 O O     . HOH S 7 .    ? -33.955 80.888  75.373  1.00 26.04 ?  2296 HOH A O     1 
HETATM 19444 O O     . HOH S 7 .    ? -49.033 81.317  88.509  1.00 34.56 ?  2297 HOH A O     1 
HETATM 19445 O O     . HOH S 7 .    ? 20.387  61.448  97.719  1.00 30.11 ?  2298 HOH A O     1 
HETATM 19446 O O     . HOH S 7 .    ? -25.850 65.278  92.915  1.00 26.89 ?  2299 HOH A O     1 
HETATM 19447 O O     . HOH S 7 .    ? -31.862 55.072  112.146 1.00 36.23 ?  2300 HOH A O     1 
HETATM 19448 O O     . HOH S 7 .    ? -2.473  74.044  119.981 1.00 29.73 ?  2301 HOH A O     1 
HETATM 19449 O O     . HOH S 7 .    ? -54.960 78.085  86.942  1.00 34.50 ?  2302 HOH A O     1 
HETATM 19450 O O     . HOH S 7 .    ? -54.541 46.036  63.945  1.00 33.87 ?  2303 HOH A O     1 
HETATM 19451 O O     . HOH S 7 .    ? -41.988 63.578  107.189 1.00 32.82 ?  2304 HOH A O     1 
HETATM 19452 O O     . HOH S 7 .    ? 6.381   81.409  128.613 1.00 31.72 ?  2305 HOH A O     1 
HETATM 19453 O O     . HOH S 7 .    ? -13.276 52.873  80.472  1.00 33.98 ?  2306 HOH A O     1 
HETATM 19454 O O     . HOH S 7 .    ? -17.130 50.279  77.912  1.00 30.29 ?  2307 HOH A O     1 
HETATM 19455 O O     . HOH S 7 .    ? -6.202  42.112  60.407  1.00 34.50 ?  2308 HOH A O     1 
HETATM 19456 O O     . HOH S 7 .    ? -29.383 61.563  83.096  1.00 31.06 ?  2309 HOH A O     1 
HETATM 19457 O O     . HOH S 7 .    ? -23.078 91.680  104.400 1.00 31.08 ?  2310 HOH A O     1 
HETATM 19458 O O     . HOH S 7 .    ? -23.105 90.413  102.066 1.00 25.40 ?  2311 HOH A O     1 
HETATM 19459 O O     . HOH S 7 .    ? 3.628   64.782  97.560  1.00 20.31 ?  2312 HOH A O     1 
HETATM 19460 O O     . HOH S 7 .    ? -32.181 70.374  99.613  1.00 31.57 ?  2313 HOH A O     1 
HETATM 19461 O O     . HOH S 7 .    ? -25.812 62.153  103.460 1.00 24.10 ?  2314 HOH A O     1 
HETATM 19462 O O     . HOH S 7 .    ? -53.639 69.047  101.905 1.00 23.98 ?  2315 HOH A O     1 
HETATM 19463 O O     . HOH S 7 .    ? -9.097  57.806  85.505  1.00 31.71 ?  2316 HOH A O     1 
HETATM 19464 O O     . HOH S 7 .    ? -19.015 74.282  107.668 1.00 22.59 ?  2317 HOH A O     1 
HETATM 19465 O O     . HOH S 7 .    ? -18.832 74.789  110.551 1.00 18.81 ?  2318 HOH A O     1 
HETATM 19466 O O     . HOH S 7 .    ? 18.158  64.505  91.659  1.00 36.40 ?  2319 HOH A O     1 
HETATM 19467 O O     . HOH S 7 .    ? -27.317 66.621  99.457  1.00 21.56 ?  2320 HOH A O     1 
HETATM 19468 O O     . HOH S 7 .    ? 30.317  62.994  112.683 1.00 31.49 ?  2321 HOH A O     1 
HETATM 19469 O O     . HOH S 7 .    ? -70.335 61.668  73.475  1.00 26.09 ?  2322 HOH A O     1 
HETATM 19470 O O     . HOH S 7 .    ? -4.382  80.017  126.267 1.00 29.00 ?  2323 HOH A O     1 
HETATM 19471 O O     . HOH S 7 .    ? -57.302 36.835  89.378  1.00 39.18 ?  2324 HOH A O     1 
HETATM 19472 O O     . HOH S 7 .    ? -45.038 69.596  112.545 1.00 32.05 ?  2325 HOH A O     1 
HETATM 19473 O O     . HOH S 7 .    ? -36.492 37.484  88.407  1.00 37.61 ?  2326 HOH A O     1 
HETATM 19474 O O     . HOH S 7 .    ? -9.539  62.268  95.399  1.00 28.50 ?  2327 HOH A O     1 
HETATM 19475 O O     . HOH S 7 .    ? -43.430 59.966  104.756 1.00 35.84 ?  2328 HOH A O     1 
HETATM 19476 O O     . HOH S 7 .    ? -23.964 102.023 91.705  1.00 35.84 ?  2329 HOH A O     1 
HETATM 19477 O O     . HOH S 7 .    ? 13.208  61.529  117.942 1.00 32.15 ?  2330 HOH A O     1 
HETATM 19478 O O     . HOH S 7 .    ? -49.491 77.752  94.829  1.00 31.43 ?  2331 HOH A O     1 
HETATM 19479 O O     . HOH S 7 .    ? -63.074 53.387  66.658  1.00 29.10 ?  2332 HOH A O     1 
HETATM 19480 O O     . HOH S 7 .    ? -9.477  73.876  130.602 1.00 30.10 ?  2333 HOH A O     1 
HETATM 19481 O O     . HOH S 7 .    ? -48.506 56.511  56.829  1.00 27.69 ?  2334 HOH A O     1 
HETATM 19482 O O     . HOH S 7 .    ? -0.805  60.267  113.624 1.00 30.18 ?  2335 HOH A O     1 
HETATM 19483 O O     . HOH S 7 .    ? -37.100 82.701  78.215  1.00 31.75 ?  2336 HOH A O     1 
HETATM 19484 O O     . HOH S 7 .    ? -10.382 65.679  73.375  1.00 34.21 ?  2337 HOH A O     1 
HETATM 19485 O O     . HOH S 7 .    ? -52.667 73.233  103.637 1.00 28.01 ?  2338 HOH A O     1 
HETATM 19486 O O     . HOH S 7 .    ? 6.665   62.513  96.075  1.00 24.10 ?  2339 HOH A O     1 
HETATM 19487 O O     . HOH S 7 .    ? -29.009 77.606  71.166  1.00 29.08 ?  2340 HOH A O     1 
HETATM 19488 O O     . HOH S 7 .    ? -29.842 92.647  110.117 1.00 31.98 ?  2341 HOH A O     1 
HETATM 19489 O O     . HOH S 7 .    ? -32.880 58.804  85.945  1.00 29.46 ?  2342 HOH A O     1 
HETATM 19490 O O     . HOH S 7 .    ? -27.967 71.153  100.620 1.00 27.63 ?  2343 HOH A O     1 
HETATM 19491 O O     . HOH S 7 .    ? -69.356 69.539  81.224  1.00 28.96 ?  2344 HOH A O     1 
HETATM 19492 O O     . HOH S 7 .    ? -8.991  77.080  130.934 1.00 33.35 ?  2345 HOH A O     1 
HETATM 19493 O O     . HOH S 7 .    ? 0.697   58.669  115.517 1.00 33.40 ?  2346 HOH A O     1 
HETATM 19494 O O     . HOH S 7 .    ? -57.186 52.294  99.796  1.00 31.00 ?  2347 HOH A O     1 
HETATM 19495 O O     . HOH S 7 .    ? -32.762 65.626  126.020 1.00 27.38 ?  2348 HOH A O     1 
HETATM 19496 O O     . HOH S 7 .    ? -63.193 55.297  70.743  1.00 22.10 ?  2349 HOH A O     1 
HETATM 19497 O O     . HOH S 7 .    ? 23.221  70.102  117.364 1.00 24.28 ?  2350 HOH A O     1 
HETATM 19498 O O     . HOH S 7 .    ? -52.266 47.110  97.824  1.00 26.15 ?  2351 HOH A O     1 
HETATM 19499 O O     . HOH S 7 .    ? -19.114 41.011  71.382  1.00 37.93 ?  2352 HOH A O     1 
HETATM 19500 O O     . HOH S 7 .    ? -56.997 76.117  77.771  1.00 26.60 ?  2353 HOH A O     1 
HETATM 19501 O O     . HOH S 7 .    ? -55.980 45.757  66.191  1.00 34.05 ?  2354 HOH A O     1 
HETATM 19502 O O     . HOH S 7 .    ? -9.490  83.027  74.683  1.00 36.00 ?  2355 HOH A O     1 
HETATM 19503 O O     . HOH S 7 .    ? -33.001 49.874  73.697  1.00 35.33 ?  2356 HOH A O     1 
HETATM 19504 O O     . HOH S 7 .    ? -41.952 80.607  70.640  1.00 33.66 ?  2357 HOH A O     1 
HETATM 19505 O O     . HOH S 7 .    ? -13.918 46.932  78.875  1.00 38.14 ?  2358 HOH A O     1 
HETATM 19506 O O     . HOH S 7 .    ? -30.692 86.758  75.305  1.00 37.43 ?  2359 HOH A O     1 
HETATM 19507 O O     . HOH S 7 .    ? -24.926 52.071  101.330 1.00 25.18 ?  2360 HOH A O     1 
HETATM 19508 O O     . HOH S 7 .    ? -55.160 54.906  103.493 1.00 37.19 ?  2361 HOH A O     1 
HETATM 19509 O O     . HOH S 7 .    ? -22.254 68.979  133.640 1.00 36.69 ?  2362 HOH A O     1 
HETATM 19510 O O     . HOH S 7 .    ? -30.309 60.161  87.003  1.00 27.63 ?  2363 HOH A O     1 
HETATM 19511 O O     . HOH S 7 .    ? -29.675 60.017  89.622  1.00 17.87 ?  2364 HOH A O     1 
HETATM 19512 O O     . HOH S 7 .    ? -31.326 84.246  74.332  1.00 32.22 ?  2365 HOH A O     1 
HETATM 19513 O O     . HOH S 7 .    ? -21.191 52.680  102.456 1.00 27.68 ?  2366 HOH A O     1 
HETATM 19514 O O     . HOH S 7 .    ? 12.753  62.540  94.489  1.00 30.87 ?  2367 HOH A O     1 
HETATM 19515 O O     . HOH S 7 .    ? -8.945  43.068  58.831  1.00 33.95 ?  2368 HOH A O     1 
HETATM 19516 O O     . HOH S 7 .    ? -17.133 76.064  107.254 1.00 21.73 ?  2369 HOH A O     1 
HETATM 19517 O O     . HOH S 7 .    ? -12.627 61.833  106.429 1.00 28.77 ?  2370 HOH A O     1 
HETATM 19518 O O     . HOH S 7 .    ? -33.714 58.165  114.947 1.00 34.44 ?  2371 HOH A O     1 
HETATM 19519 O O     . HOH S 7 .    ? -35.802 38.806  75.190  1.00 30.55 ?  2372 HOH A O     1 
HETATM 19520 O O     . HOH S 7 .    ? -13.536 60.296  87.949  1.00 27.52 ?  2373 HOH A O     1 
HETATM 19521 O O     . HOH S 7 .    ? -2.349  84.460  97.600  1.00 32.18 ?  2374 HOH A O     1 
HETATM 19522 O O     . HOH S 7 .    ? 3.546   69.157  89.646  1.00 31.90 ?  2375 HOH A O     1 
HETATM 19523 O O     . HOH S 7 .    ? -56.860 76.486  81.852  1.00 33.19 ?  2376 HOH A O     1 
HETATM 19524 O O     . HOH S 7 .    ? -65.736 55.631  70.426  1.00 33.59 ?  2377 HOH A O     1 
HETATM 19525 O O     . HOH S 7 .    ? -23.453 51.899  98.977  1.00 31.45 ?  2378 HOH A O     1 
HETATM 19526 O O     . HOH S 7 .    ? -25.372 62.821  101.034 1.00 26.09 ?  2379 HOH A O     1 
HETATM 19527 O O     . HOH S 7 .    ? -35.282 64.222  123.294 1.00 35.34 ?  2380 HOH A O     1 
HETATM 19528 O O     . HOH S 7 .    ? -32.064 61.673  123.406 1.00 32.41 ?  2381 HOH A O     1 
HETATM 19529 O O     . HOH S 7 .    ? -55.607 52.850  101.635 1.00 29.52 ?  2382 HOH A O     1 
HETATM 19530 O O     . HOH S 7 .    ? -36.353 58.767  109.468 1.00 35.95 ?  2383 HOH A O     1 
HETATM 19531 O O     . HOH S 7 .    ? -20.632 89.383  102.875 1.00 32.16 ?  2384 HOH A O     1 
HETATM 19532 O O     . HOH S 7 .    ? -33.374 57.222  112.396 1.00 26.14 ?  2385 HOH A O     1 
HETATM 19533 O O     . HOH S 7 .    ? 11.341  64.537  94.443  1.00 32.86 ?  2386 HOH A O     1 
HETATM 19534 O O     . HOH S 7 .    ? -39.438 72.276  96.735  1.00 25.17 ?  2387 HOH A O     1 
HETATM 19535 O O     . HOH S 7 .    ? -33.687 78.652  72.198  1.00 33.01 ?  2388 HOH A O     1 
HETATM 19536 O O     . HOH S 7 .    ? 13.774  65.903  91.853  1.00 33.76 ?  2389 HOH A O     1 
HETATM 19537 O O     . HOH S 7 .    ? -37.467 34.352  91.392  1.00 37.28 ?  2390 HOH A O     1 
HETATM 19538 O O     . HOH S 7 .    ? -54.594 71.409  103.553 1.00 31.54 ?  2391 HOH A O     1 
HETATM 19539 O O     . HOH S 7 .    ? -36.834 31.815  92.172  1.00 37.09 ?  2392 HOH A O     1 
HETATM 19540 O O     . HOH S 7 .    ? -54.329 47.542  99.610  1.00 31.51 ?  2393 HOH A O     1 
HETATM 19541 O O     . HOH S 7 .    ? -34.247 81.407  72.457  1.00 32.51 ?  2394 HOH A O     1 
HETATM 19542 O O     . HOH S 7 .    ? 13.815  63.107  91.929  1.00 33.98 ?  2395 HOH A O     1 
HETATM 19543 O O     . HOH T 7 .    ? 12.884  50.990  87.454  1.00 27.19 ?  1401 HOH B O     1 
HETATM 19544 O O     . HOH T 7 .    ? 33.046  68.410  74.837  1.00 18.08 ?  1402 HOH B O     1 
HETATM 19545 O O     . HOH T 7 .    ? -11.549 27.300  82.219  1.00 21.24 ?  1403 HOH B O     1 
HETATM 19546 O O     . HOH T 7 .    ? 18.464  12.579  96.619  1.00 31.57 ?  1404 HOH B O     1 
HETATM 19547 O O     . HOH T 7 .    ? -28.203 31.923  122.633 1.00 38.95 ?  1405 HOH B O     1 
HETATM 19548 O O     . HOH T 7 .    ? -1.307  22.006  71.959  1.00 32.24 ?  1406 HOH B O     1 
HETATM 19549 O O     . HOH T 7 .    ? -4.947  22.923  108.816 1.00 32.63 ?  1407 HOH B O     1 
HETATM 19550 O O     . HOH T 7 .    ? 0.826   -10.773 112.159 1.00 26.37 ?  1408 HOH B O     1 
HETATM 19551 O O     . HOH T 7 .    ? 8.489   -1.359  108.392 1.00 33.97 ?  1409 HOH B O     1 
HETATM 19552 O O     . HOH T 7 .    ? -20.087 27.308  92.525  1.00 34.87 ?  1410 HOH B O     1 
HETATM 19553 O O     . HOH T 7 .    ? 23.777  52.995  71.751  1.00 29.51 ?  1411 HOH B O     1 
HETATM 19554 O O     . HOH T 7 .    ? 3.968   72.486  86.941  1.00 28.03 ?  1412 HOH B O     1 
HETATM 19555 O O     . HOH T 7 .    ? -10.253 -3.156  117.030 1.00 34.53 ?  1413 HOH B O     1 
HETATM 19556 O O     . HOH T 7 .    ? 2.158   16.992  113.710 1.00 28.81 ?  1414 HOH B O     1 
HETATM 19557 O O     . HOH T 7 .    ? -14.504 8.796   119.905 1.00 29.70 ?  1415 HOH B O     1 
HETATM 19558 O O     . HOH T 7 .    ? 0.795   20.312  105.996 1.00 24.59 ?  1416 HOH B O     1 
HETATM 19559 O O     . HOH T 7 .    ? 10.441  24.142  105.047 1.00 32.29 ?  1417 HOH B O     1 
HETATM 19560 O O     . HOH T 7 .    ? 1.616   57.123  88.666  1.00 26.61 ?  1418 HOH B O     1 
HETATM 19561 O O     . HOH T 7 .    ? -24.994 2.713   113.132 1.00 36.61 ?  1419 HOH B O     1 
HETATM 19562 O O     . HOH T 7 .    ? -14.538 14.366  79.687  1.00 29.78 ?  1420 HOH B O     1 
HETATM 19563 O O     . HOH T 7 .    ? -6.912  43.839  74.747  1.00 28.82 ?  1421 HOH B O     1 
HETATM 19564 O O     . HOH T 7 .    ? 0.029   40.374  99.207  1.00 27.38 ?  1422 HOH B O     1 
HETATM 19565 O O     . HOH T 7 .    ? 14.346  64.740  54.796  1.00 34.14 ?  1423 HOH B O     1 
HETATM 19566 O O     . HOH T 7 .    ? -21.216 24.856  103.170 1.00 34.15 ?  1424 HOH B O     1 
HETATM 19567 O O     . HOH T 7 .    ? 13.613  34.041  79.558  1.00 28.80 ?  1425 HOH B O     1 
HETATM 19568 O O     . HOH T 7 .    ? -2.653  4.406   86.194  1.00 22.00 ?  1426 HOH B O     1 
HETATM 19569 O O     . HOH T 7 .    ? 9.777   50.317  91.356  1.00 25.34 ?  1427 HOH B O     1 
HETATM 19570 O O     . HOH T 7 .    ? -0.558  -10.513 116.571 1.00 28.06 ?  1428 HOH B O     1 
HETATM 19571 O O     . HOH T 7 .    ? 16.849  14.196  110.535 1.00 26.02 ?  1429 HOH B O     1 
HETATM 19572 O O     . HOH T 7 .    ? 0.371   19.505  112.943 1.00 33.59 ?  1430 HOH B O     1 
HETATM 19573 O O     . HOH T 7 .    ? 32.613  18.417  58.541  1.00 27.10 ?  1431 HOH B O     1 
HETATM 19574 O O     . HOH T 7 .    ? 34.507  62.470  79.121  1.00 15.45 ?  1432 HOH B O     1 
HETATM 19575 O O     . HOH T 7 .    ? 33.231  28.977  62.483  1.00 30.15 ?  1433 HOH B O     1 
HETATM 19576 O O     . HOH T 7 .    ? 9.317   25.709  55.878  1.00 17.01 ?  1434 HOH B O     1 
HETATM 19577 O O     . HOH T 7 .    ? 7.122   32.669  99.415  1.00 26.63 ?  1435 HOH B O     1 
HETATM 19578 O O     . HOH T 7 .    ? 3.974   55.243  73.604  1.00 21.38 ?  1436 HOH B O     1 
HETATM 19579 O O     . HOH T 7 .    ? -8.284  24.267  117.912 1.00 31.99 ?  1437 HOH B O     1 
HETATM 19580 O O     . HOH T 7 .    ? 4.857   43.967  138.314 1.00 36.33 ?  1438 HOH B O     1 
HETATM 19581 O O     . HOH T 7 .    ? -6.990  11.037  129.249 1.00 31.43 ?  1439 HOH B O     1 
HETATM 19582 O O     . HOH T 7 .    ? -5.570  4.921   123.616 1.00 22.63 ?  1440 HOH B O     1 
HETATM 19583 O O     . HOH T 7 .    ? 4.916   31.321  114.615 1.00 30.29 ?  1441 HOH B O     1 
HETATM 19584 O O     . HOH T 7 .    ? 5.808   25.100  87.333  1.00 29.97 ?  1442 HOH B O     1 
HETATM 19585 O O     . HOH T 7 .    ? -9.043  23.953  77.742  1.00 30.83 ?  1443 HOH B O     1 
HETATM 19586 O O     . HOH T 7 .    ? 16.105  15.437  85.762  1.00 23.48 ?  1444 HOH B O     1 
HETATM 19587 O O     . HOH T 7 .    ? 12.847  35.060  110.772 1.00 31.84 ?  1445 HOH B O     1 
HETATM 19588 O O     . HOH T 7 .    ? 22.769  34.661  116.837 1.00 23.84 ?  1446 HOH B O     1 
HETATM 19589 O O     . HOH T 7 .    ? 29.972  26.883  56.728  1.00 21.22 ?  1447 HOH B O     1 
HETATM 19590 O O     . HOH T 7 .    ? -11.405 19.579  124.059 1.00 26.89 ?  1448 HOH B O     1 
HETATM 19591 O O     . HOH T 7 .    ? 27.460  12.609  67.161  1.00 28.95 ?  1449 HOH B O     1 
HETATM 19592 O O     . HOH T 7 .    ? 4.702   32.134  91.046  1.00 28.70 ?  1450 HOH B O     1 
HETATM 19593 O O     . HOH T 7 .    ? 35.777  41.341  97.714  1.00 35.32 ?  1451 HOH B O     1 
HETATM 19594 O O     . HOH T 7 .    ? -5.080  43.908  82.139  1.00 28.84 ?  1452 HOH B O     1 
HETATM 19595 O O     . HOH T 7 .    ? -12.831 19.476  84.967  1.00 21.62 ?  1453 HOH B O     1 
HETATM 19596 O O     . HOH T 7 .    ? 33.085  18.624  88.353  1.00 23.02 ?  1454 HOH B O     1 
HETATM 19597 O O     . HOH T 7 .    ? -6.907  52.417  108.426 1.00 27.51 ?  1455 HOH B O     1 
HETATM 19598 O O     . HOH T 7 .    ? 10.788  18.841  62.288  1.00 27.35 ?  1456 HOH B O     1 
HETATM 19599 O O     . HOH T 7 .    ? -4.472  -2.653  98.158  1.00 22.15 ?  1457 HOH B O     1 
HETATM 19600 O O     . HOH T 7 .    ? -12.060 17.868  127.907 1.00 28.34 ?  1458 HOH B O     1 
HETATM 19601 O O     . HOH T 7 .    ? -5.954  37.047  78.744  1.00 26.60 ?  1459 HOH B O     1 
HETATM 19602 O O     . HOH T 7 .    ? 5.246   69.143  64.591  1.00 35.39 ?  1460 HOH B O     1 
HETATM 19603 O O     . HOH T 7 .    ? 3.631   7.523   93.497  1.00 19.87 ?  1461 HOH B O     1 
HETATM 19604 O O     . HOH T 7 .    ? 10.896  37.898  97.086  1.00 24.29 ?  1462 HOH B O     1 
HETATM 19605 O O     . HOH T 7 .    ? -27.228 14.192  101.776 1.00 36.96 ?  1463 HOH B O     1 
HETATM 19606 O O     . HOH T 7 .    ? -7.527  -1.505  121.240 1.00 27.94 ?  1464 HOH B O     1 
HETATM 19607 O O     . HOH T 7 .    ? 5.115   65.834  69.479  1.00 30.77 ?  1465 HOH B O     1 
HETATM 19608 O O     . HOH T 7 .    ? -6.074  40.132  63.771  1.00 26.88 ?  1466 HOH B O     1 
HETATM 19609 O O     . HOH T 7 .    ? 3.268   33.572  87.711  1.00 16.53 ?  1467 HOH B O     1 
HETATM 19610 O O     . HOH T 7 .    ? 33.223  10.674  88.396  1.00 33.05 ?  1468 HOH B O     1 
HETATM 19611 O O     . HOH T 7 .    ? -9.217  45.160  110.136 1.00 25.97 ?  1469 HOH B O     1 
HETATM 19612 O O     . HOH T 7 .    ? -10.754 46.308  75.439  1.00 15.72 ?  1470 HOH B O     1 
HETATM 19613 O O     . HOH T 7 .    ? 33.769  11.930  75.547  1.00 28.59 ?  1471 HOH B O     1 
HETATM 19614 O O     . HOH T 7 .    ? 10.307  50.574  65.790  1.00 20.37 ?  1472 HOH B O     1 
HETATM 19615 O O     . HOH T 7 .    ? 27.213  37.586  91.029  1.00 29.30 ?  1473 HOH B O     1 
HETATM 19616 O O     . HOH T 7 .    ? 3.831   21.311  119.723 1.00 31.41 ?  1474 HOH B O     1 
HETATM 19617 O O     . HOH T 7 .    ? 15.612  3.789   99.823  1.00 30.89 ?  1475 HOH B O     1 
HETATM 19618 O O     . HOH T 7 .    ? -4.935  26.817  70.994  1.00 22.14 ?  1476 HOH B O     1 
HETATM 19619 O O     . HOH T 7 .    ? 2.278   30.045  55.427  1.00 26.94 ?  1477 HOH B O     1 
HETATM 19620 O O     . HOH T 7 .    ? -6.631  11.907  126.780 1.00 24.54 ?  1478 HOH B O     1 
HETATM 19621 O O     . HOH T 7 .    ? -4.749  5.672   82.838  1.00 35.54 ?  1479 HOH B O     1 
HETATM 19622 O O     . HOH T 7 .    ? 2.562   43.808  71.324  1.00 12.69 ?  1480 HOH B O     1 
HETATM 19623 O O     . HOH T 7 .    ? 1.516   12.920  103.175 1.00 17.76 ?  1481 HOH B O     1 
HETATM 19624 O O     . HOH T 7 .    ? 6.117   14.684  126.180 1.00 22.99 ?  1482 HOH B O     1 
HETATM 19625 O O     . HOH T 7 .    ? -13.945 -0.757  98.224  1.00 34.89 ?  1483 HOH B O     1 
HETATM 19626 O O     . HOH T 7 .    ? 5.898   43.901  59.363  1.00 22.45 ?  1484 HOH B O     1 
HETATM 19627 O O     . HOH T 7 .    ? -14.390 54.102  119.415 1.00 24.67 ?  1485 HOH B O     1 
HETATM 19628 O O     . HOH T 7 .    ? 22.784  45.902  77.837  1.00 30.90 ?  1486 HOH B O     1 
HETATM 19629 O O     . HOH T 7 .    ? 19.908  50.850  78.331  1.00 25.25 ?  1487 HOH B O     1 
HETATM 19630 O O     . HOH T 7 .    ? 19.810  19.368  106.791 1.00 17.57 ?  1488 HOH B O     1 
HETATM 19631 O O     . HOH T 7 .    ? -2.761  29.225  58.412  1.00 26.31 ?  1489 HOH B O     1 
HETATM 19632 O O     . HOH T 7 .    ? -5.424  -2.357  124.966 1.00 29.37 ?  1490 HOH B O     1 
HETATM 19633 O O     . HOH T 7 .    ? -0.214  73.459  79.166  1.00 24.01 ?  1491 HOH B O     1 
HETATM 19634 O O     . HOH T 7 .    ? 27.105  41.966  106.136 1.00 26.04 ?  1492 HOH B O     1 
HETATM 19635 O O     . HOH T 7 .    ? 6.996   51.172  58.459  1.00 26.16 ?  1493 HOH B O     1 
HETATM 19636 O O     . HOH T 7 .    ? 0.913   41.914  77.248  1.00 20.48 ?  1494 HOH B O     1 
HETATM 19637 O O     . HOH T 7 .    ? 4.138   41.957  85.277  1.00 16.60 ?  1495 HOH B O     1 
HETATM 19638 O O     . HOH T 7 .    ? -25.664 5.707   113.013 1.00 30.13 ?  1496 HOH B O     1 
HETATM 19639 O O     . HOH T 7 .    ? -2.400  48.703  64.478  1.00 13.93 ?  1497 HOH B O     1 
HETATM 19640 O O     . HOH T 7 .    ? 10.891  46.238  107.850 1.00 26.29 ?  1498 HOH B O     1 
HETATM 19641 O O     . HOH T 7 .    ? 26.126  54.892  78.256  1.00 24.48 ?  1499 HOH B O     1 
HETATM 19642 O O     . HOH T 7 .    ? 30.910  25.531  53.399  1.00 33.69 ?  1500 HOH B O     1 
HETATM 19643 O O     . HOH T 7 .    ? -4.394  64.188  82.005  1.00 14.83 ?  1501 HOH B O     1 
HETATM 19644 O O     . HOH T 7 .    ? -0.228  39.096  132.548 1.00 34.97 ?  1502 HOH B O     1 
HETATM 19645 O O     . HOH T 7 .    ? -6.411  50.912  73.979  1.00 11.98 ?  1503 HOH B O     1 
HETATM 19646 O O     . HOH T 7 .    ? 12.001  70.498  61.359  1.00 32.62 ?  1504 HOH B O     1 
HETATM 19647 O O     . HOH T 7 .    ? -32.878 15.028  99.529  1.00 35.46 ?  1505 HOH B O     1 
HETATM 19648 O O     . HOH T 7 .    ? 19.677  59.571  57.514  1.00 27.39 ?  1506 HOH B O     1 
HETATM 19649 O O     . HOH T 7 .    ? -5.021  36.779  90.994  1.00 23.66 ?  1507 HOH B O     1 
HETATM 19650 O O     . HOH T 7 .    ? 15.751  55.325  94.023  1.00 30.35 ?  1508 HOH B O     1 
HETATM 19651 O O     . HOH T 7 .    ? 17.142  54.765  98.402  1.00 27.20 ?  1509 HOH B O     1 
HETATM 19652 O O     . HOH T 7 .    ? -0.604  26.794  69.355  1.00 13.48 ?  1510 HOH B O     1 
HETATM 19653 O O     . HOH T 7 .    ? 21.497  29.419  72.111  1.00 14.27 ?  1511 HOH B O     1 
HETATM 19654 O O     . HOH T 7 .    ? 31.409  31.055  71.875  1.00 33.27 ?  1512 HOH B O     1 
HETATM 19655 O O     . HOH T 7 .    ? 19.170  79.244  69.322  1.00 29.80 ?  1513 HOH B O     1 
HETATM 19656 O O     . HOH T 7 .    ? 28.105  12.664  86.699  1.00 26.45 ?  1514 HOH B O     1 
HETATM 19657 O O     . HOH T 7 .    ? -4.427  18.413  99.280  1.00 13.08 ?  1515 HOH B O     1 
HETATM 19658 O O     . HOH T 7 .    ? 25.265  54.694  62.797  1.00 21.70 ?  1516 HOH B O     1 
HETATM 19659 O O     . HOH T 7 .    ? 2.253   39.106  99.947  1.00 18.36 ?  1517 HOH B O     1 
HETATM 19660 O O     . HOH T 7 .    ? 7.346   20.254  103.426 1.00 24.30 ?  1518 HOH B O     1 
HETATM 19661 O O     . HOH T 7 .    ? 15.297  21.261  89.211  1.00 23.52 ?  1519 HOH B O     1 
HETATM 19662 O O     . HOH T 7 .    ? -0.071  17.934  81.261  1.00 26.00 ?  1520 HOH B O     1 
HETATM 19663 O O     . HOH T 7 .    ? 6.228   5.295   87.195  1.00 19.41 ?  1521 HOH B O     1 
HETATM 19664 O O     . HOH T 7 .    ? 11.347  24.662  109.436 1.00 30.96 ?  1522 HOH B O     1 
HETATM 19665 O O     . HOH T 7 .    ? 11.228  5.314   123.104 1.00 29.02 ?  1523 HOH B O     1 
HETATM 19666 O O     . HOH T 7 .    ? 20.796  4.672   68.594  1.00 34.81 ?  1524 HOH B O     1 
HETATM 19667 O O     . HOH T 7 .    ? -9.422  30.407  100.023 1.00 28.33 ?  1525 HOH B O     1 
HETATM 19668 O O     . HOH T 7 .    ? 0.613   38.637  109.336 1.00 20.11 ?  1526 HOH B O     1 
HETATM 19669 O O     . HOH T 7 .    ? 15.491  54.052  67.152  1.00 29.11 ?  1527 HOH B O     1 
HETATM 19670 O O     . HOH T 7 .    ? 1.021   10.558  130.716 1.00 27.43 ?  1528 HOH B O     1 
HETATM 19671 O O     . HOH T 7 .    ? -2.386  41.804  62.578  1.00 19.48 ?  1529 HOH B O     1 
HETATM 19672 O O     . HOH T 7 .    ? -13.963 17.530  106.823 1.00 19.49 ?  1530 HOH B O     1 
HETATM 19673 O O     . HOH T 7 .    ? -10.887 1.190   123.047 1.00 24.88 ?  1531 HOH B O     1 
HETATM 19674 O O     . HOH T 7 .    ? 15.228  52.348  59.503  1.00 21.86 ?  1532 HOH B O     1 
HETATM 19675 O O     . HOH T 7 .    ? 11.653  55.492  66.267  1.00 31.39 ?  1533 HOH B O     1 
HETATM 19676 O O     . HOH T 7 .    ? 22.775  48.315  78.864  1.00 22.05 ?  1534 HOH B O     1 
HETATM 19677 O O     . HOH T 7 .    ? -5.241  51.515  76.455  1.00 16.21 ?  1535 HOH B O     1 
HETATM 19678 O O     . HOH T 7 .    ? -2.809  45.342  103.849 1.00 26.51 ?  1536 HOH B O     1 
HETATM 19679 O O     . HOH T 7 .    ? 13.527  9.930   92.446  1.00 22.29 ?  1537 HOH B O     1 
HETATM 19680 O O     . HOH T 7 .    ? 26.749  21.382  76.009  1.00 25.95 ?  1538 HOH B O     1 
HETATM 19681 O O     . HOH T 7 .    ? 26.562  36.622  108.176 1.00 26.27 ?  1539 HOH B O     1 
HETATM 19682 O O     . HOH T 7 .    ? -5.564  -7.787  117.270 1.00 25.46 ?  1540 HOH B O     1 
HETATM 19683 O O     . HOH T 7 .    ? 26.660  20.047  56.390  1.00 28.13 ?  1541 HOH B O     1 
HETATM 19684 O O     . HOH T 7 .    ? -7.078  7.962   112.443 1.00 20.94 ?  1542 HOH B O     1 
HETATM 19685 O O     . HOH T 7 .    ? 4.361   35.650  119.157 1.00 28.60 ?  1543 HOH B O     1 
HETATM 19686 O O     . HOH T 7 .    ? -5.261  9.455   116.404 1.00 22.73 ?  1544 HOH B O     1 
HETATM 19687 O O     . HOH T 7 .    ? 10.075  49.059  56.754  1.00 26.99 ?  1545 HOH B O     1 
HETATM 19688 O O     . HOH T 7 .    ? 3.672   56.286  63.656  1.00 32.22 ?  1546 HOH B O     1 
HETATM 19689 O O     . HOH T 7 .    ? 17.852  12.221  118.432 1.00 23.08 ?  1547 HOH B O     1 
HETATM 19690 O O     . HOH T 7 .    ? 22.217  45.343  91.775  1.00 19.72 ?  1548 HOH B O     1 
HETATM 19691 O O     . HOH T 7 .    ? 26.880  15.429  94.584  1.00 26.44 ?  1549 HOH B O     1 
HETATM 19692 O O     . HOH T 7 .    ? 18.833  5.341   74.918  1.00 28.18 ?  1550 HOH B O     1 
HETATM 19693 O O     . HOH T 7 .    ? 12.488  1.884   112.791 1.00 26.59 ?  1551 HOH B O     1 
HETATM 19694 O O     . HOH T 7 .    ? -13.641 53.975  123.689 1.00 29.39 ?  1552 HOH B O     1 
HETATM 19695 O O     . HOH T 7 .    ? 8.434   35.488  103.981 1.00 26.73 ?  1553 HOH B O     1 
HETATM 19696 O O     . HOH T 7 .    ? 10.890  17.722  65.345  1.00 23.02 ?  1554 HOH B O     1 
HETATM 19697 O O     . HOH T 7 .    ? 23.206  51.986  63.235  1.00 21.21 ?  1555 HOH B O     1 
HETATM 19698 O O     . HOH T 7 .    ? -10.651 10.277  131.116 1.00 32.06 ?  1556 HOH B O     1 
HETATM 19699 O O     . HOH T 7 .    ? 18.815  24.471  55.093  1.00 22.47 ?  1557 HOH B O     1 
HETATM 19700 O O     . HOH T 7 .    ? -3.002  30.886  64.436  1.00 21.97 ?  1558 HOH B O     1 
HETATM 19701 O O     . HOH T 7 .    ? 28.532  18.225  58.405  1.00 28.12 ?  1559 HOH B O     1 
HETATM 19702 O O     . HOH T 7 .    ? -5.080  -6.968  113.483 1.00 25.90 ?  1560 HOH B O     1 
HETATM 19703 O O     . HOH T 7 .    ? 7.669   56.553  88.625  1.00 28.16 ?  1561 HOH B O     1 
HETATM 19704 O O     . HOH T 7 .    ? -2.853  62.837  86.597  1.00 21.94 ?  1562 HOH B O     1 
HETATM 19705 O O     . HOH T 7 .    ? 11.971  46.348  55.163  1.00 28.20 ?  1563 HOH B O     1 
HETATM 19706 O O     . HOH T 7 .    ? 17.242  40.342  72.478  1.00 15.46 ?  1564 HOH B O     1 
HETATM 19707 O O     . HOH T 7 .    ? -0.677  16.181  113.261 1.00 29.39 ?  1565 HOH B O     1 
HETATM 19708 O O     . HOH T 7 .    ? -1.510  14.177  87.280  1.00 17.25 ?  1566 HOH B O     1 
HETATM 19709 O O     . HOH T 7 .    ? 10.703  52.661  105.813 1.00 29.70 ?  1567 HOH B O     1 
HETATM 19710 O O     . HOH T 7 .    ? 24.308  44.286  110.864 1.00 33.78 ?  1568 HOH B O     1 
HETATM 19711 O O     . HOH T 7 .    ? 7.679   65.464  64.860  1.00 23.87 ?  1569 HOH B O     1 
HETATM 19712 O O     . HOH T 7 .    ? 12.197  21.218  102.633 1.00 23.31 ?  1570 HOH B O     1 
HETATM 19713 O O     . HOH T 7 .    ? 16.278  16.179  88.237  1.00 23.93 ?  1571 HOH B O     1 
HETATM 19714 O O     . HOH T 7 .    ? 18.054  68.759  85.530  1.00 29.09 ?  1572 HOH B O     1 
HETATM 19715 O O     . HOH T 7 .    ? -1.151  55.105  73.093  1.00 26.28 ?  1573 HOH B O     1 
HETATM 19716 O O     . HOH T 7 .    ? 1.499   5.760   92.990  1.00 18.58 ?  1574 HOH B O     1 
HETATM 19717 O O     . HOH T 7 .    ? -20.859 24.689  95.615  1.00 21.60 ?  1575 HOH B O     1 
HETATM 19718 O O     . HOH T 7 .    ? 11.744  10.552  72.447  1.00 21.76 ?  1576 HOH B O     1 
HETATM 19719 O O     . HOH T 7 .    ? -13.879 28.483  99.015  1.00 33.20 ?  1577 HOH B O     1 
HETATM 19720 O O     . HOH T 7 .    ? 7.020   33.670  87.659  1.00 16.97 ?  1578 HOH B O     1 
HETATM 19721 O O     . HOH T 7 .    ? 30.956  20.821  80.680  1.00 20.63 ?  1579 HOH B O     1 
HETATM 19722 O O     . HOH T 7 .    ? 9.902   30.784  111.303 1.00 34.33 ?  1580 HOH B O     1 
HETATM 19723 O O     . HOH T 7 .    ? 2.610   11.400  95.643  1.00 15.69 ?  1581 HOH B O     1 
HETATM 19724 O O     . HOH T 7 .    ? 0.923   49.096  90.304  1.00 30.48 ?  1582 HOH B O     1 
HETATM 19725 O O     . HOH T 7 .    ? 14.252  25.486  111.869 1.00 34.83 ?  1583 HOH B O     1 
HETATM 19726 O O     . HOH T 7 .    ? 12.641  36.480  86.944  1.00 14.00 ?  1584 HOH B O     1 
HETATM 19727 O O     . HOH T 7 .    ? -16.432 3.613   94.021  1.00 34.09 ?  1585 HOH B O     1 
HETATM 19728 O O     . HOH T 7 .    ? 16.407  2.270   105.882 1.00 36.33 ?  1586 HOH B O     1 
HETATM 19729 O O     . HOH T 7 .    ? 2.805   56.951  71.985  1.00 27.07 ?  1587 HOH B O     1 
HETATM 19730 O O     . HOH T 7 .    ? -11.518 21.925  110.795 1.00 27.98 ?  1588 HOH B O     1 
HETATM 19731 O O     . HOH T 7 .    ? 17.334  28.468  112.192 1.00 26.52 ?  1589 HOH B O     1 
HETATM 19732 O O     . HOH T 7 .    ? 17.119  48.695  60.406  1.00 19.79 ?  1590 HOH B O     1 
HETATM 19733 O O     . HOH T 7 .    ? 20.803  37.436  113.884 1.00 19.64 ?  1591 HOH B O     1 
HETATM 19734 O O     . HOH T 7 .    ? -5.132  30.433  78.320  1.00 14.31 ?  1592 HOH B O     1 
HETATM 19735 O O     . HOH T 7 .    ? 9.676   -6.272  110.164 1.00 35.46 ?  1593 HOH B O     1 
HETATM 19736 O O     . HOH T 7 .    ? 1.498   13.332  106.001 1.00 14.09 ?  1594 HOH B O     1 
HETATM 19737 O O     . HOH T 7 .    ? -25.228 9.688   88.708  1.00 29.15 ?  1595 HOH B O     1 
HETATM 19738 O O     . HOH T 7 .    ? 25.618  53.637  74.567  1.00 24.14 ?  1596 HOH B O     1 
HETATM 19739 O O     . HOH T 7 .    ? -7.593  15.336  82.686  1.00 28.78 ?  1597 HOH B O     1 
HETATM 19740 O O     . HOH T 7 .    ? 4.905   22.461  123.919 1.00 25.82 ?  1598 HOH B O     1 
HETATM 19741 O O     . HOH T 7 .    ? 15.230  40.186  74.266  1.00 13.86 ?  1599 HOH B O     1 
HETATM 19742 O O     . HOH T 7 .    ? -1.975  10.919  102.570 1.00 17.08 ?  1600 HOH B O     1 
HETATM 19743 O O     . HOH T 7 .    ? -9.522  9.547   124.421 1.00 22.32 ?  1601 HOH B O     1 
HETATM 19744 O O     . HOH T 7 .    ? 6.686   7.473   76.169  1.00 27.39 ?  1602 HOH B O     1 
HETATM 19745 O O     . HOH T 7 .    ? 12.667  58.455  63.182  1.00 32.91 ?  1603 HOH B O     1 
HETATM 19746 O O     . HOH T 7 .    ? 7.867   7.118   73.929  1.00 34.32 ?  1604 HOH B O     1 
HETATM 19747 O O     . HOH T 7 .    ? 19.921  43.285  88.937  1.00 14.64 ?  1605 HOH B O     1 
HETATM 19748 O O     . HOH T 7 .    ? -1.917  25.128  80.900  1.00 20.46 ?  1606 HOH B O     1 
HETATM 19749 O O     . HOH T 7 .    ? 8.064   13.391  72.420  1.00 22.44 ?  1607 HOH B O     1 
HETATM 19750 O O     . HOH T 7 .    ? -2.248  35.479  101.968 1.00 22.50 ?  1608 HOH B O     1 
HETATM 19751 O O     . HOH T 7 .    ? -1.440  37.824  81.028  1.00 19.22 ?  1609 HOH B O     1 
HETATM 19752 O O     . HOH T 7 .    ? 6.693   5.357   93.556  1.00 20.01 ?  1610 HOH B O     1 
HETATM 19753 O O     . HOH T 7 .    ? 5.074   35.975  49.856  1.00 29.32 ?  1611 HOH B O     1 
HETATM 19754 O O     . HOH T 7 .    ? 10.152  51.344  76.681  1.00 27.79 ?  1612 HOH B O     1 
HETATM 19755 O O     . HOH T 7 .    ? 21.927  53.046  68.056  1.00 24.30 ?  1613 HOH B O     1 
HETATM 19756 O O     . HOH T 7 .    ? -5.351  39.732  73.201  1.00 22.99 ?  1614 HOH B O     1 
HETATM 19757 O O     . HOH T 7 .    ? 7.097   42.646  50.519  1.00 24.77 ?  1615 HOH B O     1 
HETATM 19758 O O     . HOH T 7 .    ? 14.672  20.450  93.370  1.00 28.59 ?  1616 HOH B O     1 
HETATM 19759 O O     . HOH T 7 .    ? -2.834  21.129  92.746  1.00 14.62 ?  1617 HOH B O     1 
HETATM 19760 O O     . HOH T 7 .    ? 6.661   82.064  76.573  1.00 31.56 ?  1618 HOH B O     1 
HETATM 19761 O O     . HOH T 7 .    ? 31.686  53.819  68.646  1.00 21.74 ?  1619 HOH B O     1 
HETATM 19762 O O     . HOH T 7 .    ? -0.748  23.637  74.930  1.00 16.62 ?  1620 HOH B O     1 
HETATM 19763 O O     . HOH T 7 .    ? 19.661  4.817   77.580  1.00 32.32 ?  1621 HOH B O     1 
HETATM 19764 O O     . HOH T 7 .    ? -12.977 8.326   125.920 1.00 31.00 ?  1622 HOH B O     1 
HETATM 19765 O O     . HOH T 7 .    ? -0.105  3.817   89.633  1.00 20.21 ?  1623 HOH B O     1 
HETATM 19766 O O     . HOH T 7 .    ? 0.672   28.537  83.962  1.00 11.90 ?  1624 HOH B O     1 
HETATM 19767 O O     . HOH T 7 .    ? 0.898   30.330  75.812  1.00 15.68 ?  1625 HOH B O     1 
HETATM 19768 O O     . HOH T 7 .    ? 14.615  40.676  78.349  1.00 15.01 ?  1626 HOH B O     1 
HETATM 19769 O O     . HOH T 7 .    ? 22.572  22.603  85.564  1.00 16.16 ?  1627 HOH B O     1 
HETATM 19770 O O     . HOH T 7 .    ? 26.825  48.757  95.557  1.00 30.45 ?  1628 HOH B O     1 
HETATM 19771 O O     . HOH T 7 .    ? 31.677  59.971  66.220  1.00 24.94 ?  1629 HOH B O     1 
HETATM 19772 O O     . HOH T 7 .    ? 1.019   30.204  101.444 1.00 29.92 ?  1630 HOH B O     1 
HETATM 19773 O O     . HOH T 7 .    ? 28.054  67.467  69.058  1.00 30.76 ?  1631 HOH B O     1 
HETATM 19774 O O     . HOH T 7 .    ? 22.264  11.429  71.903  1.00 26.19 ?  1632 HOH B O     1 
HETATM 19775 O O     . HOH T 7 .    ? 2.363   30.342  81.132  1.00 17.02 ?  1633 HOH B O     1 
HETATM 19776 O O     . HOH T 7 .    ? 16.068  48.106  71.836  1.00 16.22 ?  1634 HOH B O     1 
HETATM 19777 O O     . HOH T 7 .    ? 10.658  14.584  126.367 1.00 25.34 ?  1635 HOH B O     1 
HETATM 19778 O O     . HOH T 7 .    ? 28.609  46.955  88.584  1.00 31.54 ?  1636 HOH B O     1 
HETATM 19779 O O     . HOH T 7 .    ? 18.706  38.421  117.025 1.00 27.37 ?  1637 HOH B O     1 
HETATM 19780 O O     . HOH T 7 .    ? -0.973  55.952  123.092 1.00 30.25 ?  1638 HOH B O     1 
HETATM 19781 O O     . HOH T 7 .    ? -9.940  18.952  81.919  1.00 32.83 ?  1639 HOH B O     1 
HETATM 19782 O O     . HOH T 7 .    ? 16.428  26.690  83.631  1.00 21.06 ?  1640 HOH B O     1 
HETATM 19783 O O     . HOH T 7 .    ? 18.515  22.692  85.756  1.00 17.88 ?  1641 HOH B O     1 
HETATM 19784 O O     . HOH T 7 .    ? 11.514  32.616  82.678  1.00 19.20 ?  1642 HOH B O     1 
HETATM 19785 O O     . HOH T 7 .    ? 0.170   19.899  70.620  1.00 20.99 ?  1643 HOH B O     1 
HETATM 19786 O O     . HOH T 7 .    ? -7.893  25.468  104.885 1.00 26.34 ?  1644 HOH B O     1 
HETATM 19787 O O     . HOH T 7 .    ? 3.774   29.286  85.607  1.00 20.04 ?  1645 HOH B O     1 
HETATM 19788 O O     . HOH T 7 .    ? -10.469 32.132  90.113  1.00 18.90 ?  1646 HOH B O     1 
HETATM 19789 O O     . HOH T 7 .    ? 7.399   48.930  107.857 1.00 18.64 ?  1647 HOH B O     1 
HETATM 19790 O O     . HOH T 7 .    ? -19.627 -3.053  107.066 1.00 34.49 ?  1648 HOH B O     1 
HETATM 19791 O O     . HOH T 7 .    ? 33.746  17.872  71.716  1.00 32.97 ?  1649 HOH B O     1 
HETATM 19792 O O     . HOH T 7 .    ? -13.738 11.225  92.327  1.00 17.91 ?  1650 HOH B O     1 
HETATM 19793 O O     . HOH T 7 .    ? -3.479  10.280  85.551  1.00 19.71 ?  1651 HOH B O     1 
HETATM 19794 O O     . HOH T 7 .    ? 2.916   23.000  59.391  1.00 30.16 ?  1652 HOH B O     1 
HETATM 19795 O O     . HOH T 7 .    ? 3.315   33.468  94.045  1.00 16.08 ?  1653 HOH B O     1 
HETATM 19796 O O     . HOH T 7 .    ? 19.931  23.904  46.817  1.00 19.32 ?  1654 HOH B O     1 
HETATM 19797 O O     . HOH T 7 .    ? 28.111  29.104  84.386  1.00 16.63 ?  1655 HOH B O     1 
HETATM 19798 O O     . HOH T 7 .    ? -19.398 23.240  116.351 1.00 24.08 ?  1656 HOH B O     1 
HETATM 19799 O O     . HOH T 7 .    ? 17.976  52.371  67.654  1.00 27.51 ?  1657 HOH B O     1 
HETATM 19800 O O     . HOH T 7 .    ? 26.960  34.882  92.162  1.00 20.99 ?  1658 HOH B O     1 
HETATM 19801 O O     . HOH T 7 .    ? 34.049  37.430  62.442  1.00 28.67 ?  1659 HOH B O     1 
HETATM 19802 O O     . HOH T 7 .    ? 25.297  32.918  111.648 1.00 32.38 ?  1660 HOH B O     1 
HETATM 19803 O O     . HOH T 7 .    ? 33.815  40.527  94.288  1.00 36.32 ?  1661 HOH B O     1 
HETATM 19804 O O     . HOH T 7 .    ? 27.957  31.161  74.230  1.00 30.52 ?  1662 HOH B O     1 
HETATM 19805 O O     . HOH T 7 .    ? 11.703  49.514  89.479  1.00 19.10 ?  1663 HOH B O     1 
HETATM 19806 O O     . HOH T 7 .    ? 28.361  25.161  68.257  1.00 16.90 ?  1664 HOH B O     1 
HETATM 19807 O O     . HOH T 7 .    ? 18.193  43.433  92.613  1.00 12.69 ?  1665 HOH B O     1 
HETATM 19808 O O     . HOH T 7 .    ? 18.148  10.312  115.582 1.00 36.70 ?  1666 HOH B O     1 
HETATM 19809 O O     . HOH T 7 .    ? -2.382  42.836  59.069  1.00 26.00 ?  1667 HOH B O     1 
HETATM 19810 O O     . HOH T 7 .    ? -3.260  66.051  78.079  1.00 26.59 ?  1668 HOH B O     1 
HETATM 19811 O O     . HOH T 7 .    ? -1.568  32.434  69.996  1.00 12.26 ?  1669 HOH B O     1 
HETATM 19812 O O     . HOH T 7 .    ? 11.051  16.003  123.197 1.00 24.44 ?  1670 HOH B O     1 
HETATM 19813 O O     . HOH T 7 .    ? 21.013  62.658  85.615  1.00 35.81 ?  1671 HOH B O     1 
HETATM 19814 O O     . HOH T 7 .    ? 5.460   6.923   95.482  1.00 19.90 ?  1672 HOH B O     1 
HETATM 19815 O O     . HOH T 7 .    ? 25.136  34.781  74.573  1.00 22.64 ?  1673 HOH B O     1 
HETATM 19816 O O     . HOH T 7 .    ? 12.357  37.103  108.997 1.00 20.81 ?  1674 HOH B O     1 
HETATM 19817 O O     . HOH T 7 .    ? 1.296   14.740  83.564  1.00 18.92 ?  1675 HOH B O     1 
HETATM 19818 O O     . HOH T 7 .    ? -5.565  54.845  79.813  1.00 20.48 ?  1676 HOH B O     1 
HETATM 19819 O O     . HOH T 7 .    ? -0.500  55.946  87.329  1.00 28.74 ?  1677 HOH B O     1 
HETATM 19820 O O     . HOH T 7 .    ? 18.399  7.116   101.898 1.00 33.47 ?  1678 HOH B O     1 
HETATM 19821 O O     . HOH T 7 .    ? 9.215   61.915  86.293  1.00 19.05 ?  1679 HOH B O     1 
HETATM 19822 O O     . HOH T 7 .    ? 11.090  49.025  77.248  1.00 27.47 ?  1680 HOH B O     1 
HETATM 19823 O O     . HOH T 7 .    ? 14.692  22.296  102.957 1.00 23.80 ?  1681 HOH B O     1 
HETATM 19824 O O     . HOH T 7 .    ? -1.155  60.489  78.384  1.00 21.89 ?  1682 HOH B O     1 
HETATM 19825 O O     . HOH T 7 .    ? -6.231  -0.275  87.298  1.00 25.45 ?  1683 HOH B O     1 
HETATM 19826 O O     . HOH T 7 .    ? -21.401 14.900  83.725  1.00 27.15 ?  1684 HOH B O     1 
HETATM 19827 O O     . HOH T 7 .    ? -8.045  29.719  76.819  1.00 20.40 ?  1685 HOH B O     1 
HETATM 19828 O O     . HOH T 7 .    ? 30.692  40.197  57.967  1.00 25.66 ?  1686 HOH B O     1 
HETATM 19829 O O     . HOH T 7 .    ? -29.653 19.069  119.291 1.00 38.63 ?  1687 HOH B O     1 
HETATM 19830 O O     . HOH T 7 .    ? 20.530  34.421  79.247  1.00 20.76 ?  1688 HOH B O     1 
HETATM 19831 O O     . HOH T 7 .    ? 11.383  41.350  55.474  1.00 15.73 ?  1689 HOH B O     1 
HETATM 19832 O O     . HOH T 7 .    ? -14.794 39.798  126.121 1.00 35.87 ?  1690 HOH B O     1 
HETATM 19833 O O     . HOH T 7 .    ? 28.943  22.454  77.295  1.00 20.92 ?  1691 HOH B O     1 
HETATM 19834 O O     . HOH T 7 .    ? 16.392  53.077  64.830  1.00 22.44 ?  1692 HOH B O     1 
HETATM 19835 O O     . HOH T 7 .    ? -11.203 26.770  112.121 1.00 29.58 ?  1693 HOH B O     1 
HETATM 19836 O O     . HOH T 7 .    ? -9.716  5.387   88.134  1.00 21.33 ?  1694 HOH B O     1 
HETATM 19837 O O     . HOH T 7 .    ? -10.423 39.651  128.716 1.00 36.52 ?  1695 HOH B O     1 
HETATM 19838 O O     . HOH T 7 .    ? 5.443   55.587  105.977 1.00 22.02 ?  1696 HOH B O     1 
HETATM 19839 O O     . HOH T 7 .    ? 1.120   8.954   90.764  1.00 20.45 ?  1697 HOH B O     1 
HETATM 19840 O O     . HOH T 7 .    ? -2.966  54.598  84.585  1.00 24.65 ?  1698 HOH B O     1 
HETATM 19841 O O     . HOH T 7 .    ? 10.679  33.398  48.870  1.00 36.67 ?  1699 HOH B O     1 
HETATM 19842 O O     . HOH T 7 .    ? -4.082  24.255  71.292  1.00 31.84 ?  1700 HOH B O     1 
HETATM 19843 O O     . HOH T 7 .    ? 5.223   3.036   94.261  1.00 21.94 ?  1701 HOH B O     1 
HETATM 19844 O O     . HOH T 7 .    ? 10.635  8.511   70.728  1.00 30.74 ?  1702 HOH B O     1 
HETATM 19845 O O     . HOH T 7 .    ? -3.418  -11.719 102.298 1.00 27.08 ?  1703 HOH B O     1 
HETATM 19846 O O     . HOH T 7 .    ? 30.330  50.035  72.201  1.00 32.58 ?  1704 HOH B O     1 
HETATM 19847 O O     . HOH T 7 .    ? -15.566 47.008  115.206 1.00 26.56 ?  1705 HOH B O     1 
HETATM 19848 O O     . HOH T 7 .    ? -16.765 4.123   117.822 1.00 27.03 ?  1706 HOH B O     1 
HETATM 19849 O O     . HOH T 7 .    ? 5.744   14.839  95.749  1.00 17.00 ?  1707 HOH B O     1 
HETATM 19850 O O     . HOH T 7 .    ? -28.316 19.666  126.012 1.00 36.68 ?  1708 HOH B O     1 
HETATM 19851 O O     . HOH T 7 .    ? 12.337  53.249  62.557  1.00 25.90 ?  1709 HOH B O     1 
HETATM 19852 O O     . HOH T 7 .    ? -14.780 5.484   118.998 1.00 24.43 ?  1710 HOH B O     1 
HETATM 19853 O O     . HOH T 7 .    ? 4.714   47.416  88.080  1.00 17.30 ?  1711 HOH B O     1 
HETATM 19854 O O     . HOH T 7 .    ? 24.128  68.850  68.255  1.00 22.41 ?  1712 HOH B O     1 
HETATM 19855 O O     . HOH T 7 .    ? -8.095  1.881   93.493  1.00 20.27 ?  1713 HOH B O     1 
HETATM 19856 O O     . HOH T 7 .    ? -2.621  39.285  88.269  1.00 13.93 ?  1714 HOH B O     1 
HETATM 19857 O O     . HOH T 7 .    ? 20.615  27.016  71.604  1.00 14.43 ?  1715 HOH B O     1 
HETATM 19858 O O     . HOH T 7 .    ? 7.571   44.713  76.150  1.00 11.67 ?  1716 HOH B O     1 
HETATM 19859 O O     . HOH T 7 .    ? -4.756  10.551  101.634 1.00 16.42 ?  1717 HOH B O     1 
HETATM 19860 O O     . HOH T 7 .    ? 18.978  45.675  55.303  1.00 26.13 ?  1718 HOH B O     1 
HETATM 19861 O O     . HOH T 7 .    ? -1.447  67.181  76.380  1.00 23.20 ?  1719 HOH B O     1 
HETATM 19862 O O     . HOH T 7 .    ? 7.841   62.795  67.397  1.00 31.58 ?  1720 HOH B O     1 
HETATM 19863 O O     . HOH T 7 .    ? 27.256  17.861  62.462  1.00 22.82 ?  1721 HOH B O     1 
HETATM 19864 O O     . HOH T 7 .    ? 11.767  37.067  73.308  1.00 11.34 ?  1722 HOH B O     1 
HETATM 19865 O O     . HOH T 7 .    ? -5.081  36.889  99.829  1.00 24.71 ?  1723 HOH B O     1 
HETATM 19866 O O     . HOH T 7 .    ? 19.330  51.990  80.823  1.00 30.27 ?  1724 HOH B O     1 
HETATM 19867 O O     . HOH T 7 .    ? 19.371  15.479  64.253  1.00 16.76 ?  1725 HOH B O     1 
HETATM 19868 O O     . HOH T 7 .    ? -31.638 15.318  103.575 1.00 32.37 ?  1726 HOH B O     1 
HETATM 19869 O O     . HOH T 7 .    ? 13.916  72.284  61.815  1.00 25.54 ?  1727 HOH B O     1 
HETATM 19870 O O     . HOH T 7 .    ? -12.892 34.458  88.154  1.00 32.91 ?  1728 HOH B O     1 
HETATM 19871 O O     . HOH T 7 .    ? -8.185  12.052  98.277  1.00 15.60 ?  1729 HOH B O     1 
HETATM 19872 O O     . HOH T 7 .    ? 4.495   60.637  69.046  1.00 32.60 ?  1730 HOH B O     1 
HETATM 19873 O O     . HOH T 7 .    ? 30.380  35.034  51.430  1.00 29.97 ?  1731 HOH B O     1 
HETATM 19874 O O     . HOH T 7 .    ? -4.579  59.917  126.636 1.00 27.94 ?  1732 HOH B O     1 
HETATM 19875 O O     . HOH T 7 .    ? 3.625   19.054  61.291  1.00 28.10 ?  1733 HOH B O     1 
HETATM 19876 O O     . HOH T 7 .    ? 12.085  7.399   91.435  1.00 21.85 ?  1734 HOH B O     1 
HETATM 19877 O O     . HOH T 7 .    ? 31.886  59.164  72.885  1.00 21.12 ?  1735 HOH B O     1 
HETATM 19878 O O     . HOH T 7 .    ? 11.788  20.607  59.479  1.00 16.67 ?  1736 HOH B O     1 
HETATM 19879 O O     . HOH T 7 .    ? 6.674   16.305  122.645 1.00 23.76 ?  1737 HOH B O     1 
HETATM 19880 O O     . HOH T 7 .    ? 2.224   41.519  54.922  1.00 23.07 ?  1738 HOH B O     1 
HETATM 19881 O O     . HOH T 7 .    ? -30.777 4.728   101.138 1.00 38.78 ?  1739 HOH B O     1 
HETATM 19882 O O     . HOH T 7 .    ? 29.496  28.816  106.582 1.00 29.55 ?  1740 HOH B O     1 
HETATM 19883 O O     . HOH T 7 .    ? 13.647  26.476  83.197  1.00 22.19 ?  1741 HOH B O     1 
HETATM 19884 O O     . HOH T 7 .    ? 0.148   47.493  77.465  1.00 15.54 ?  1742 HOH B O     1 
HETATM 19885 O O     . HOH T 7 .    ? 22.943  61.631  83.741  1.00 29.94 ?  1743 HOH B O     1 
HETATM 19886 O O     . HOH T 7 .    ? 23.343  55.920  100.142 1.00 30.08 ?  1744 HOH B O     1 
HETATM 19887 O O     . HOH T 7 .    ? -28.499 4.998   102.746 1.00 35.54 ?  1745 HOH B O     1 
HETATM 19888 O O     . HOH T 7 .    ? 12.330  5.494   85.497  1.00 21.76 ?  1746 HOH B O     1 
HETATM 19889 O O     . HOH T 7 .    ? 29.903  19.829  77.603  1.00 25.57 ?  1747 HOH B O     1 
HETATM 19890 O O     . HOH T 7 .    ? -5.224  37.389  94.962  1.00 26.66 ?  1748 HOH B O     1 
HETATM 19891 O O     . HOH T 7 .    ? 21.407  53.622  84.701  1.00 37.16 ?  1749 HOH B O     1 
HETATM 19892 O O     . HOH T 7 .    ? 9.440   43.467  111.547 1.00 25.60 ?  1750 HOH B O     1 
HETATM 19893 O O     . HOH T 7 .    ? -7.038  35.113  70.183  1.00 31.89 ?  1751 HOH B O     1 
HETATM 19894 O O     . HOH T 7 .    ? 18.077  23.597  111.724 1.00 22.61 ?  1752 HOH B O     1 
HETATM 19895 O O     . HOH T 7 .    ? 19.244  54.616  94.680  1.00 26.60 ?  1753 HOH B O     1 
HETATM 19896 O O     . HOH T 7 .    ? -10.668 31.652  81.343  1.00 23.79 ?  1754 HOH B O     1 
HETATM 19897 O O     . HOH T 7 .    ? -2.676  23.765  77.139  1.00 23.19 ?  1755 HOH B O     1 
HETATM 19898 O O     . HOH T 7 .    ? -2.766  25.998  61.155  1.00 29.82 ?  1756 HOH B O     1 
HETATM 19899 O O     . HOH T 7 .    ? -8.195  35.269  81.754  1.00 28.23 ?  1757 HOH B O     1 
HETATM 19900 O O     . HOH T 7 .    ? -38.310 9.640   107.348 1.00 35.72 ?  1758 HOH B O     1 
HETATM 19901 O O     . HOH T 7 .    ? 31.219  28.545  78.581  1.00 25.03 ?  1759 HOH B O     1 
HETATM 19902 O O     . HOH T 7 .    ? -9.273  23.606  101.934 1.00 15.31 ?  1760 HOH B O     1 
HETATM 19903 O O     . HOH T 7 .    ? 13.215  25.555  97.636  1.00 28.94 ?  1761 HOH B O     1 
HETATM 19904 O O     . HOH T 7 .    ? 8.818   3.313   81.950  1.00 26.73 ?  1762 HOH B O     1 
HETATM 19905 O O     . HOH T 7 .    ? 33.030  46.087  67.741  1.00 27.98 ?  1763 HOH B O     1 
HETATM 19906 O O     . HOH T 7 .    ? -1.949  2.339   127.275 1.00 22.58 ?  1764 HOH B O     1 
HETATM 19907 O O     . HOH T 7 .    ? 33.322  17.149  90.912  1.00 32.76 ?  1765 HOH B O     1 
HETATM 19908 O O     . HOH T 7 .    ? 17.779  23.153  89.228  1.00 20.50 ?  1766 HOH B O     1 
HETATM 19909 O O     . HOH T 7 .    ? 27.147  22.632  89.556  1.00 18.10 ?  1767 HOH B O     1 
HETATM 19910 O O     . HOH T 7 .    ? 18.934  7.639   84.741  1.00 25.36 ?  1768 HOH B O     1 
HETATM 19911 O O     . HOH T 7 .    ? -10.873 52.369  129.703 1.00 32.33 ?  1769 HOH B O     1 
HETATM 19912 O O     . HOH T 7 .    ? 2.568   32.541  79.452  1.00 13.59 ?  1770 HOH B O     1 
HETATM 19913 O O     . HOH T 7 .    ? -0.761  -9.431  103.379 1.00 29.39 ?  1771 HOH B O     1 
HETATM 19914 O O     . HOH T 7 .    ? 19.713  32.347  68.018  1.00 13.75 ?  1772 HOH B O     1 
HETATM 19915 O O     . HOH T 7 .    ? 16.578  22.679  92.544  1.00 26.90 ?  1773 HOH B O     1 
HETATM 19916 O O     . HOH T 7 .    ? -13.727 11.989  95.007  1.00 17.12 ?  1774 HOH B O     1 
HETATM 19917 O O     . HOH T 7 .    ? 0.025   26.620  95.969  1.00 18.09 ?  1775 HOH B O     1 
HETATM 19918 O O     . HOH T 7 .    ? 20.811  21.465  61.465  1.00 18.39 ?  1776 HOH B O     1 
HETATM 19919 O O     . HOH T 7 .    ? 14.706  42.289  76.186  1.00 16.18 ?  1777 HOH B O     1 
HETATM 19920 O O     . HOH T 7 .    ? 13.833  81.200  70.509  1.00 34.40 ?  1778 HOH B O     1 
HETATM 19921 O O     . HOH T 7 .    ? 16.181  42.993  51.201  1.00 27.63 ?  1779 HOH B O     1 
HETATM 19922 O O     . HOH T 7 .    ? 4.046   19.159  98.646  1.00 27.66 ?  1780 HOH B O     1 
HETATM 19923 O O     . HOH T 7 .    ? 11.881  38.065  48.290  1.00 29.81 ?  1781 HOH B O     1 
HETATM 19924 O O     . HOH T 7 .    ? -2.923  -2.801  95.934  1.00 23.67 ?  1782 HOH B O     1 
HETATM 19925 O O     . HOH T 7 .    ? 22.886  67.273  65.545  1.00 24.09 ?  1783 HOH B O     1 
HETATM 19926 O O     . HOH T 7 .    ? 11.424  25.928  103.257 1.00 27.95 ?  1784 HOH B O     1 
HETATM 19927 O O     . HOH T 7 .    ? 14.657  6.243   69.658  1.00 24.90 ?  1785 HOH B O     1 
HETATM 19928 O O     . HOH T 7 .    ? -6.810  13.817  92.600  1.00 14.53 ?  1786 HOH B O     1 
HETATM 19929 O O     . HOH T 7 .    ? 5.943   27.521  89.221  1.00 33.10 ?  1787 HOH B O     1 
HETATM 19930 O O     . HOH T 7 .    ? 29.260  69.355  80.669  1.00 20.49 ?  1788 HOH B O     1 
HETATM 19931 O O     . HOH T 7 .    ? 22.206  24.361  109.758 1.00 23.32 ?  1789 HOH B O     1 
HETATM 19932 O O     . HOH T 7 .    ? 1.328   -1.197  93.940  1.00 26.09 ?  1790 HOH B O     1 
HETATM 19933 O O     . HOH T 7 .    ? 22.599  11.489  88.815  1.00 26.85 ?  1791 HOH B O     1 
HETATM 19934 O O     . HOH T 7 .    ? 2.616   5.513   81.335  1.00 24.96 ?  1792 HOH B O     1 
HETATM 19935 O O     . HOH T 7 .    ? 13.001  48.007  83.316  1.00 24.27 ?  1793 HOH B O     1 
HETATM 19936 O O     . HOH T 7 .    ? 9.784   71.154  62.597  1.00 28.79 ?  1794 HOH B O     1 
HETATM 19937 O O     . HOH T 7 .    ? 4.804   30.748  55.657  1.00 26.10 ?  1795 HOH B O     1 
HETATM 19938 O O     . HOH T 7 .    ? -9.178  -0.067  114.017 1.00 25.35 ?  1796 HOH B O     1 
HETATM 19939 O O     . HOH T 7 .    ? 23.317  32.540  92.691  1.00 16.42 ?  1797 HOH B O     1 
HETATM 19940 O O     . HOH T 7 .    ? 1.500   20.397  90.792  1.00 22.09 ?  1798 HOH B O     1 
HETATM 19941 O O     . HOH T 7 .    ? 0.007   35.997  109.864 1.00 29.65 ?  1799 HOH B O     1 
HETATM 19942 O O     . HOH T 7 .    ? 27.525  33.611  70.707  1.00 29.46 ?  1800 HOH B O     1 
HETATM 19943 O O     . HOH T 7 .    ? 8.459   22.180  85.632  1.00 23.14 ?  1801 HOH B O     1 
HETATM 19944 O O     . HOH T 7 .    ? 0.769   55.536  111.721 1.00 25.20 ?  1802 HOH B O     1 
HETATM 19945 O O     . HOH T 7 .    ? 2.841   44.358  59.400  1.00 24.64 ?  1803 HOH B O     1 
HETATM 19946 O O     . HOH T 7 .    ? -12.046 27.195  103.113 1.00 30.31 ?  1804 HOH B O     1 
HETATM 19947 O O     . HOH T 7 .    ? 5.706   -9.255  116.037 1.00 34.85 ?  1805 HOH B O     1 
HETATM 19948 O O     . HOH T 7 .    ? 33.005  28.104  53.484  1.00 30.68 ?  1806 HOH B O     1 
HETATM 19949 O O     . HOH T 7 .    ? -11.207 -2.747  97.663  1.00 25.35 ?  1807 HOH B O     1 
HETATM 19950 O O     . HOH T 7 .    ? -6.443  34.177  84.868  1.00 18.31 ?  1808 HOH B O     1 
HETATM 19951 O O     . HOH T 7 .    ? 2.398   63.243  79.404  1.00 14.68 ?  1809 HOH B O     1 
HETATM 19952 O O     . HOH T 7 .    ? 18.585  61.999  58.261  1.00 25.72 ?  1810 HOH B O     1 
HETATM 19953 O O     . HOH T 7 .    ? 31.306  52.602  66.109  1.00 27.30 ?  1811 HOH B O     1 
HETATM 19954 O O     . HOH T 7 .    ? 18.428  47.780  91.093  1.00 21.54 ?  1812 HOH B O     1 
HETATM 19955 O O     . HOH T 7 .    ? 4.921   49.202  69.600  1.00 14.51 ?  1813 HOH B O     1 
HETATM 19956 O O     . HOH T 7 .    ? 24.898  23.536  82.615  1.00 14.81 ?  1814 HOH B O     1 
HETATM 19957 O O     . HOH T 7 .    ? -22.668 19.854  89.479  1.00 31.65 ?  1815 HOH B O     1 
HETATM 19958 O O     . HOH T 7 .    ? 20.675  54.109  82.094  1.00 32.60 ?  1816 HOH B O     1 
HETATM 19959 O O     . HOH T 7 .    ? 3.071   40.644  118.313 1.00 22.52 ?  1817 HOH B O     1 
HETATM 19960 O O     . HOH T 7 .    ? 9.231   18.859  105.018 1.00 21.74 ?  1818 HOH B O     1 
HETATM 19961 O O     . HOH T 7 .    ? 12.051  11.647  122.620 1.00 25.43 ?  1819 HOH B O     1 
HETATM 19962 O O     . HOH T 7 .    ? 8.895   45.279  133.132 1.00 38.14 ?  1820 HOH B O     1 
HETATM 19963 O O     . HOH T 7 .    ? 19.607  18.593  66.935  1.00 13.50 ?  1821 HOH B O     1 
HETATM 19964 O O     . HOH T 7 .    ? 12.986  49.854  65.874  1.00 24.86 ?  1822 HOH B O     1 
HETATM 19965 O O     . HOH T 7 .    ? -4.703  42.336  109.437 1.00 28.37 ?  1823 HOH B O     1 
HETATM 19966 O O     . HOH T 7 .    ? 33.540  22.789  64.923  1.00 29.19 ?  1824 HOH B O     1 
HETATM 19967 O O     . HOH T 7 .    ? 10.509  70.227  87.673  1.00 33.59 ?  1825 HOH B O     1 
HETATM 19968 O O     . HOH T 7 .    ? 10.125  2.493   118.833 1.00 28.18 ?  1826 HOH B O     1 
HETATM 19969 O O     . HOH T 7 .    ? 17.055  43.392  80.267  1.00 22.77 ?  1827 HOH B O     1 
HETATM 19970 O O     . HOH T 7 .    ? 4.711   46.479  70.198  1.00 12.49 ?  1828 HOH B O     1 
HETATM 19971 O O     . HOH T 7 .    ? -4.201  -0.755  111.967 1.00 24.05 ?  1829 HOH B O     1 
HETATM 19972 O O     . HOH T 7 .    ? -1.309  66.788  84.932  1.00 24.27 ?  1830 HOH B O     1 
HETATM 19973 O O     . HOH T 7 .    ? -7.352  27.637  75.044  1.00 22.86 ?  1831 HOH B O     1 
HETATM 19974 O O     . HOH T 7 .    ? 1.598   40.196  115.467 1.00 20.81 ?  1832 HOH B O     1 
HETATM 19975 O O     . HOH T 7 .    ? 14.651  16.469  93.106  1.00 20.48 ?  1833 HOH B O     1 
HETATM 19976 O O     . HOH T 7 .    ? 30.971  33.874  86.037  1.00 27.33 ?  1834 HOH B O     1 
HETATM 19977 O O     . HOH T 7 .    ? 3.490   20.673  104.094 1.00 30.23 ?  1835 HOH B O     1 
HETATM 19978 O O     . HOH T 7 .    ? 0.050   11.983  94.926  1.00 14.77 ?  1836 HOH B O     1 
HETATM 19979 O O     . HOH T 7 .    ? 4.895   62.769  85.304  1.00 17.13 ?  1837 HOH B O     1 
HETATM 19980 O O     . HOH T 7 .    ? 27.136  52.325  76.073  1.00 30.19 ?  1838 HOH B O     1 
HETATM 19981 O O     . HOH T 7 .    ? 0.193   -7.767  108.293 1.00 25.32 ?  1839 HOH B O     1 
HETATM 19982 O O     . HOH T 7 .    ? 25.683  7.961   79.431  1.00 34.20 ?  1840 HOH B O     1 
HETATM 19983 O O     . HOH T 7 .    ? 23.008  72.764  65.833  1.00 30.06 ?  1841 HOH B O     1 
HETATM 19984 O O     . HOH T 7 .    ? -1.202  50.796  65.813  1.00 13.97 ?  1842 HOH B O     1 
HETATM 19985 O O     . HOH T 7 .    ? 25.317  29.463  110.306 1.00 35.48 ?  1843 HOH B O     1 
HETATM 19986 O O     . HOH T 7 .    ? -1.543  15.466  132.756 1.00 29.91 ?  1844 HOH B O     1 
HETATM 19987 O O     . HOH T 7 .    ? 2.532   70.252  65.128  1.00 33.70 ?  1845 HOH B O     1 
HETATM 19988 O O     . HOH T 7 .    ? 25.019  57.357  78.989  1.00 18.53 ?  1846 HOH B O     1 
HETATM 19989 O O     . HOH T 7 .    ? 25.751  33.234  72.415  1.00 25.95 ?  1847 HOH B O     1 
HETATM 19990 O O     . HOH T 7 .    ? -24.080 22.628  85.416  1.00 34.31 ?  1848 HOH B O     1 
HETATM 19991 O O     . HOH T 7 .    ? -7.032  34.546  130.337 1.00 33.45 ?  1849 HOH B O     1 
HETATM 19992 O O     . HOH T 7 .    ? 18.477  12.864  75.087  1.00 25.85 ?  1850 HOH B O     1 
HETATM 19993 O O     . HOH T 7 .    ? 4.612   21.581  84.776  1.00 17.36 ?  1851 HOH B O     1 
HETATM 19994 O O     . HOH T 7 .    ? 28.692  30.650  104.967 1.00 25.66 ?  1852 HOH B O     1 
HETATM 19995 O O     . HOH T 7 .    ? 20.234  52.213  70.208  1.00 25.66 ?  1853 HOH B O     1 
HETATM 19996 O O     . HOH T 7 .    ? 2.375   3.301   85.797  1.00 30.34 ?  1854 HOH B O     1 
HETATM 19997 O O     . HOH T 7 .    ? 8.338   40.542  87.909  1.00 11.94 ?  1855 HOH B O     1 
HETATM 19998 O O     . HOH T 7 .    ? -0.037  27.812  123.623 1.00 26.18 ?  1856 HOH B O     1 
HETATM 19999 O O     . HOH T 7 .    ? 12.847  16.699  90.095  1.00 23.60 ?  1857 HOH B O     1 
HETATM 20000 O O     . HOH T 7 .    ? 16.069  7.466   109.554 1.00 30.19 ?  1858 HOH B O     1 
HETATM 20001 O O     . HOH T 7 .    ? 10.850  20.014  122.055 1.00 24.45 ?  1859 HOH B O     1 
HETATM 20002 O O     . HOH T 7 .    ? 1.339   46.279  100.128 1.00 21.98 ?  1860 HOH B O     1 
HETATM 20003 O O     . HOH T 7 .    ? 2.576   48.808  77.055  1.00 16.19 ?  1861 HOH B O     1 
HETATM 20004 O O     . HOH T 7 .    ? -6.287  12.263  100.458 1.00 13.60 ?  1862 HOH B O     1 
HETATM 20005 O O     . HOH T 7 .    ? 24.758  50.903  67.978  1.00 24.78 ?  1863 HOH B O     1 
HETATM 20006 O O     . HOH T 7 .    ? 4.385   77.736  81.377  1.00 27.97 ?  1864 HOH B O     1 
HETATM 20007 O O     . HOH T 7 .    ? -1.459  4.965   93.332  1.00 18.11 ?  1865 HOH B O     1 
HETATM 20008 O O     . HOH T 7 .    ? 15.502  9.650   90.545  1.00 20.16 ?  1866 HOH B O     1 
HETATM 20009 O O     . HOH T 7 .    ? -6.641  5.980   119.892 1.00 21.09 ?  1867 HOH B O     1 
HETATM 20010 O O     . HOH T 7 .    ? -6.501  39.282  107.925 1.00 20.78 ?  1868 HOH B O     1 
HETATM 20011 O O     . HOH T 7 .    ? 23.921  25.892  51.200  1.00 23.51 ?  1869 HOH B O     1 
HETATM 20012 O O     . HOH T 7 .    ? 10.520  29.066  95.530  1.00 20.57 ?  1870 HOH B O     1 
HETATM 20013 O O     . HOH T 7 .    ? 23.796  31.193  111.991 1.00 29.68 ?  1871 HOH B O     1 
HETATM 20014 O O     . HOH T 7 .    ? 7.114   37.621  104.100 1.00 23.44 ?  1872 HOH B O     1 
HETATM 20015 O O     . HOH T 7 .    ? 16.320  45.842  55.103  1.00 25.72 ?  1873 HOH B O     1 
HETATM 20016 O O     . HOH T 7 .    ? -11.566 19.952  89.217  1.00 18.82 ?  1874 HOH B O     1 
HETATM 20017 O O     . HOH T 7 .    ? -25.172 16.190  83.117  1.00 29.71 ?  1875 HOH B O     1 
HETATM 20018 O O     . HOH T 7 .    ? 8.662   14.626  91.390  1.00 20.77 ?  1876 HOH B O     1 
HETATM 20019 O O     . HOH T 7 .    ? 11.625  17.683  96.101  1.00 28.35 ?  1877 HOH B O     1 
HETATM 20020 O O     . HOH T 7 .    ? 19.426  28.166  83.048  1.00 17.91 ?  1878 HOH B O     1 
HETATM 20021 O O     . HOH T 7 .    ? -17.037 14.532  80.600  1.00 36.21 ?  1879 HOH B O     1 
HETATM 20022 O O     . HOH T 7 .    ? 3.821   10.215  93.506  1.00 16.31 ?  1880 HOH B O     1 
HETATM 20023 O O     . HOH T 7 .    ? 20.868  47.497  57.147  1.00 30.43 ?  1881 HOH B O     1 
HETATM 20024 O O     . HOH T 7 .    ? -6.292  41.449  85.076  1.00 29.98 ?  1882 HOH B O     1 
HETATM 20025 O O     . HOH T 7 .    ? -14.685 6.548   121.690 1.00 27.45 ?  1883 HOH B O     1 
HETATM 20026 O O     . HOH T 7 .    ? 18.696  30.411  89.543  1.00 16.22 ?  1884 HOH B O     1 
HETATM 20027 O O     . HOH T 7 .    ? -15.059 26.395  102.683 1.00 27.32 ?  1885 HOH B O     1 
HETATM 20028 O O     . HOH T 7 .    ? 15.529  48.737  58.195  1.00 21.75 ?  1886 HOH B O     1 
HETATM 20029 O O     . HOH T 7 .    ? 11.473  18.466  99.031  1.00 31.29 ?  1887 HOH B O     1 
HETATM 20030 O O     . HOH T 7 .    ? 17.185  33.968  56.759  1.00 14.41 ?  1888 HOH B O     1 
HETATM 20031 O O     . HOH T 7 .    ? 11.436  34.276  52.775  1.00 27.77 ?  1889 HOH B O     1 
HETATM 20032 O O     . HOH T 7 .    ? 26.273  19.893  53.208  1.00 27.30 ?  1890 HOH B O     1 
HETATM 20033 O O     . HOH T 7 .    ? 1.642   9.306   80.154  1.00 27.60 ?  1891 HOH B O     1 
HETATM 20034 O O     . HOH T 7 .    ? -3.516  11.916  132.302 1.00 33.70 ?  1892 HOH B O     1 
HETATM 20035 O O     . HOH T 7 .    ? -4.551  55.651  82.552  1.00 22.34 ?  1893 HOH B O     1 
HETATM 20036 O O     . HOH T 7 .    ? 18.368  53.173  76.834  1.00 24.11 ?  1894 HOH B O     1 
HETATM 20037 O O     . HOH T 7 .    ? 3.894   29.587  124.237 1.00 34.56 ?  1895 HOH B O     1 
HETATM 20038 O O     . HOH T 7 .    ? -12.419 29.008  111.514 1.00 32.57 ?  1896 HOH B O     1 
HETATM 20039 O O     . HOH T 7 .    ? 5.193   42.536  71.706  1.00 10.60 ?  1897 HOH B O     1 
HETATM 20040 O O     . HOH T 7 .    ? 14.421  23.305  90.813  1.00 29.02 ?  1898 HOH B O     1 
HETATM 20041 O O     . HOH T 7 .    ? 20.680  22.577  87.648  1.00 16.80 ?  1899 HOH B O     1 
HETATM 20042 O O     . HOH T 7 .    ? -2.870  60.034  121.224 1.00 23.96 ?  1900 HOH B O     1 
HETATM 20043 O O     . HOH T 7 .    ? 8.525   30.955  81.844  1.00 23.24 ?  1901 HOH B O     1 
HETATM 20044 O O     . HOH T 7 .    ? 25.277  13.124  65.726  1.00 24.35 ?  1902 HOH B O     1 
HETATM 20045 O O     . HOH T 7 .    ? 18.348  14.894  98.664  1.00 21.26 ?  1903 HOH B O     1 
HETATM 20046 O O     . HOH T 7 .    ? 6.559   -4.529  105.713 1.00 29.47 ?  1904 HOH B O     1 
HETATM 20047 O O     . HOH T 7 .    ? 19.047  70.658  59.837  1.00 30.56 ?  1905 HOH B O     1 
HETATM 20048 O O     . HOH T 7 .    ? 8.202   24.817  106.716 1.00 35.00 ?  1906 HOH B O     1 
HETATM 20049 O O     . HOH T 7 .    ? -0.255  39.901  78.598  1.00 20.49 ?  1907 HOH B O     1 
HETATM 20050 O O     . HOH T 7 .    ? 5.646   51.185  110.612 1.00 32.18 ?  1908 HOH B O     1 
HETATM 20051 O O     . HOH T 7 .    ? 24.987  53.480  69.320  1.00 24.94 ?  1909 HOH B O     1 
HETATM 20052 O O     . HOH T 7 .    ? 24.606  62.976  55.141  1.00 30.53 ?  1910 HOH B O     1 
HETATM 20053 O O     . HOH T 7 .    ? 1.053   -8.320  110.881 1.00 26.96 ?  1911 HOH B O     1 
HETATM 20054 O O     . HOH T 7 .    ? 7.926   65.501  69.565  1.00 28.29 ?  1912 HOH B O     1 
HETATM 20055 O O     . HOH T 7 .    ? 7.873   29.787  85.906  1.00 32.48 ?  1913 HOH B O     1 
HETATM 20056 O O     . HOH T 7 .    ? -5.274  16.006  98.083  1.00 13.82 ?  1914 HOH B O     1 
HETATM 20057 O O     . HOH T 7 .    ? -0.142  19.160  95.156  1.00 18.33 ?  1915 HOH B O     1 
HETATM 20058 O O     . HOH T 7 .    ? -14.283 8.784   88.510  1.00 22.88 ?  1916 HOH B O     1 
HETATM 20059 O O     . HOH T 7 .    ? 20.372  18.526  60.941  1.00 22.16 ?  1917 HOH B O     1 
HETATM 20060 O O     . HOH T 7 .    ? 15.356  55.785  74.822  1.00 22.74 ?  1918 HOH B O     1 
HETATM 20061 O O     . HOH T 7 .    ? -29.226 16.480  118.682 1.00 33.41 ?  1919 HOH B O     1 
HETATM 20062 O O     . HOH T 7 .    ? 31.062  23.995  103.956 1.00 33.31 ?  1920 HOH B O     1 
HETATM 20063 O O     . HOH T 7 .    ? 23.639  16.691  83.426  1.00 23.50 ?  1921 HOH B O     1 
HETATM 20064 O O     . HOH T 7 .    ? -1.988  49.170  102.396 1.00 24.59 ?  1922 HOH B O     1 
HETATM 20065 O O     . HOH T 7 .    ? -10.663 25.138  103.859 1.00 28.13 ?  1923 HOH B O     1 
HETATM 20066 O O     . HOH T 7 .    ? 7.874   57.985  86.326  1.00 20.47 ?  1924 HOH B O     1 
HETATM 20067 O O     . HOH T 7 .    ? 33.506  25.867  59.591  1.00 23.78 ?  1925 HOH B O     1 
HETATM 20068 O O     . HOH T 7 .    ? -1.625  -1.390  110.436 1.00 26.20 ?  1926 HOH B O     1 
HETATM 20069 O O     . HOH T 7 .    ? 16.621  44.128  77.219  1.00 22.15 ?  1927 HOH B O     1 
HETATM 20070 O O     . HOH T 7 .    ? 9.903   18.186  102.427 1.00 22.12 ?  1928 HOH B O     1 
HETATM 20071 O O     . HOH T 7 .    ? 10.397  66.625  87.580  1.00 30.98 ?  1929 HOH B O     1 
HETATM 20072 O O     . HOH T 7 .    ? 5.700   47.909  111.765 1.00 29.18 ?  1930 HOH B O     1 
HETATM 20073 O O     . HOH T 7 .    ? -2.684  14.212  99.982  1.00 14.57 ?  1931 HOH B O     1 
HETATM 20074 O O     . HOH T 7 .    ? 4.461   18.602  125.428 1.00 21.93 ?  1932 HOH B O     1 
HETATM 20075 O O     . HOH T 7 .    ? -3.106  10.646  105.071 1.00 15.19 ?  1933 HOH B O     1 
HETATM 20076 O O     . HOH T 7 .    ? -18.387 5.372   96.895  1.00 31.31 ?  1934 HOH B O     1 
HETATM 20077 O O     . HOH T 7 .    ? -10.528 17.934  132.272 1.00 32.35 ?  1935 HOH B O     1 
HETATM 20078 O O     . HOH T 7 .    ? 33.897  33.077  70.518  1.00 32.39 ?  1936 HOH B O     1 
HETATM 20079 O O     . HOH T 7 .    ? 7.113   19.162  118.002 1.00 27.21 ?  1937 HOH B O     1 
HETATM 20080 O O     . HOH T 7 .    ? -5.182  -2.792  118.418 1.00 25.58 ?  1938 HOH B O     1 
HETATM 20081 O O     . HOH T 7 .    ? 2.820   35.291  122.132 1.00 29.10 ?  1939 HOH B O     1 
HETATM 20082 O O     . HOH T 7 .    ? 27.255  59.029  79.303  1.00 18.73 ?  1940 HOH B O     1 
HETATM 20083 O O     . HOH T 7 .    ? -0.087  25.956  113.119 1.00 34.70 ?  1941 HOH B O     1 
HETATM 20084 O O     . HOH T 7 .    ? -5.352  12.238  85.446  1.00 22.64 ?  1942 HOH B O     1 
HETATM 20085 O O     . HOH T 7 .    ? -15.574 34.063  104.536 1.00 34.52 ?  1943 HOH B O     1 
HETATM 20086 O O     . HOH T 7 .    ? 33.436  57.882  74.859  1.00 29.26 ?  1944 HOH B O     1 
HETATM 20087 O O     . HOH T 7 .    ? -2.824  18.094  107.296 1.00 22.91 ?  1945 HOH B O     1 
HETATM 20088 O O     . HOH T 7 .    ? 1.233   22.259  64.313  1.00 19.63 ?  1946 HOH B O     1 
HETATM 20089 O O     . HOH T 7 .    ? 17.459  33.589  69.260  1.00 12.76 ?  1947 HOH B O     1 
HETATM 20090 O O     . HOH T 7 .    ? -10.534 1.061   92.477  1.00 24.22 ?  1948 HOH B O     1 
HETATM 20091 O O     . HOH T 7 .    ? 32.815  8.738   75.358  1.00 35.24 ?  1949 HOH B O     1 
HETATM 20092 O O     . HOH T 7 .    ? -4.432  30.377  95.931  1.00 22.67 ?  1950 HOH B O     1 
HETATM 20093 O O     . HOH T 7 .    ? -3.485  52.242  83.476  1.00 25.83 ?  1951 HOH B O     1 
HETATM 20094 O O     . HOH T 7 .    ? -1.292  20.423  90.635  1.00 14.64 ?  1952 HOH B O     1 
HETATM 20095 O O     . HOH T 7 .    ? 37.620  36.422  90.674  1.00 36.77 ?  1953 HOH B O     1 
HETATM 20096 O O     . HOH T 7 .    ? -8.954  31.167  87.943  1.00 15.51 ?  1954 HOH B O     1 
HETATM 20097 O O     . HOH T 7 .    ? -2.051  -7.901  111.986 1.00 23.47 ?  1955 HOH B O     1 
HETATM 20098 O O     . HOH T 7 .    ? 29.560  60.220  59.699  1.00 26.23 ?  1956 HOH B O     1 
HETATM 20099 O O     . HOH T 7 .    ? -12.223 21.428  86.687  1.00 18.74 ?  1957 HOH B O     1 
HETATM 20100 O O     . HOH T 7 .    ? -0.389  3.438   131.961 1.00 36.25 ?  1958 HOH B O     1 
HETATM 20101 O O     . HOH T 7 .    ? 4.696   17.700  92.371  1.00 24.88 ?  1959 HOH B O     1 
HETATM 20102 O O     . HOH T 7 .    ? 22.731  37.097  87.284  1.00 19.55 ?  1960 HOH B O     1 
HETATM 20103 O O     . HOH T 7 .    ? 32.405  27.512  75.142  1.00 33.84 ?  1961 HOH B O     1 
HETATM 20104 O O     . HOH T 7 .    ? 2.012   27.140  94.251  1.00 27.79 ?  1962 HOH B O     1 
HETATM 20105 O O     . HOH T 7 .    ? 30.508  19.907  74.284  1.00 31.41 ?  1963 HOH B O     1 
HETATM 20106 O O     . HOH T 7 .    ? -8.143  -2.290  125.830 1.00 34.76 ?  1964 HOH B O     1 
HETATM 20107 O O     . HOH T 7 .    ? 19.959  21.824  75.025  1.00 25.32 ?  1965 HOH B O     1 
HETATM 20108 O O     . HOH T 7 .    ? -23.440 24.880  104.470 1.00 31.75 ?  1966 HOH B O     1 
HETATM 20109 O O     . HOH T 7 .    ? 15.696  56.070  64.742  1.00 19.60 ?  1967 HOH B O     1 
HETATM 20110 O O     . HOH T 7 .    ? 22.397  54.179  94.076  1.00 29.86 ?  1968 HOH B O     1 
HETATM 20111 O O     . HOH T 7 .    ? 0.830   -0.347  97.372  1.00 23.61 ?  1969 HOH B O     1 
HETATM 20112 O O     . HOH T 7 .    ? -17.079 24.735  108.380 1.00 23.63 ?  1970 HOH B O     1 
HETATM 20113 O O     . HOH T 7 .    ? 37.459  30.752  82.695  1.00 35.29 ?  1971 HOH B O     1 
HETATM 20114 O O     . HOH T 7 .    ? -3.797  45.802  108.087 1.00 21.37 ?  1972 HOH B O     1 
HETATM 20115 O O     . HOH T 7 .    ? -4.545  1.624   125.396 1.00 23.11 ?  1973 HOH B O     1 
HETATM 20116 O O     . HOH T 7 .    ? -5.849  22.768  81.605  1.00 19.85 ?  1974 HOH B O     1 
HETATM 20117 O O     . HOH T 7 .    ? 6.403   31.662  80.166  1.00 16.31 ?  1975 HOH B O     1 
HETATM 20118 O O     . HOH T 7 .    ? 9.239   30.560  89.629  1.00 23.62 ?  1976 HOH B O     1 
HETATM 20119 O O     . HOH T 7 .    ? 23.197  11.827  68.647  1.00 22.03 ?  1977 HOH B O     1 
HETATM 20120 O O     . HOH T 7 .    ? 15.907  37.809  75.446  1.00 13.88 ?  1978 HOH B O     1 
HETATM 20121 O O     . HOH T 7 .    ? -9.458  45.634  132.422 1.00 30.31 ?  1979 HOH B O     1 
HETATM 20122 O O     . HOH T 7 .    ? 34.100  22.217  79.061  1.00 24.41 ?  1980 HOH B O     1 
HETATM 20123 O O     . HOH T 7 .    ? -4.547  53.732  132.154 1.00 31.39 ?  1981 HOH B O     1 
HETATM 20124 O O     . HOH T 7 .    ? 27.692  36.376  75.848  1.00 27.52 ?  1982 HOH B O     1 
HETATM 20125 O O     . HOH T 7 .    ? -12.336 7.440   128.537 1.00 27.60 ?  1983 HOH B O     1 
HETATM 20126 O O     . HOH T 7 .    ? -3.056  33.678  63.415  1.00 18.06 ?  1984 HOH B O     1 
HETATM 20127 O O     . HOH T 7 .    ? 14.794  18.861  90.523  1.00 21.65 ?  1985 HOH B O     1 
HETATM 20128 O O     . HOH T 7 .    ? 7.857   31.554  94.640  1.00 25.44 ?  1986 HOH B O     1 
HETATM 20129 O O     . HOH T 7 .    ? 23.265  48.278  108.042 1.00 28.85 ?  1987 HOH B O     1 
HETATM 20130 O O     . HOH T 7 .    ? 26.460  27.100  67.864  1.00 16.06 ?  1988 HOH B O     1 
HETATM 20131 O O     . HOH T 7 .    ? 1.994   76.205  85.689  1.00 37.35 ?  1989 HOH B O     1 
HETATM 20132 O O     . HOH T 7 .    ? 26.273  12.392  88.836  1.00 24.95 ?  1990 HOH B O     1 
HETATM 20133 O O     . HOH T 7 .    ? 6.225   25.881  84.594  1.00 25.83 ?  1991 HOH B O     1 
HETATM 20134 O O     . HOH T 7 .    ? 26.505  39.619  53.757  1.00 23.99 ?  1992 HOH B O     1 
HETATM 20135 O O     . HOH T 7 .    ? 22.230  25.418  80.389  1.00 17.48 ?  1993 HOH B O     1 
HETATM 20136 O O     . HOH T 7 .    ? -8.107  48.037  77.562  1.00 26.18 ?  1994 HOH B O     1 
HETATM 20137 O O     . HOH T 7 .    ? -15.469 9.656   90.951  1.00 20.64 ?  1995 HOH B O     1 
HETATM 20138 O O     . HOH T 7 .    ? 18.201  22.499  61.945  1.00 18.92 ?  1996 HOH B O     1 
HETATM 20139 O O     . HOH T 7 .    ? 2.389   48.778  100.170 1.00 19.35 ?  1997 HOH B O     1 
HETATM 20140 O O     . HOH T 7 .    ? -2.721  30.431  71.605  1.00 14.87 ?  1998 HOH B O     1 
HETATM 20141 O O     . HOH T 7 .    ? -1.073  13.267  101.981 1.00 15.67 ?  1999 HOH B O     1 
HETATM 20142 O O     . HOH T 7 .    ? -4.835  44.568  109.945 1.00 23.86 ?  2000 HOH B O     1 
HETATM 20143 O O     . HOH T 7 .    ? 22.931  51.167  65.977  1.00 23.97 ?  2001 HOH B O     1 
HETATM 20144 O O     . HOH T 7 .    ? 4.895   54.773  65.755  1.00 28.83 ?  2002 HOH B O     1 
HETATM 20145 O O     . HOH T 7 .    ? -3.333  41.747  107.272 1.00 29.58 ?  2003 HOH B O     1 
HETATM 20146 O O     . HOH T 7 .    ? 4.835   57.683  69.910  1.00 23.22 ?  2004 HOH B O     1 
HETATM 20147 O O     . HOH T 7 .    ? 1.658   30.377  97.109  1.00 17.91 ?  2005 HOH B O     1 
HETATM 20148 O O     . HOH T 7 .    ? 31.015  51.695  75.284  1.00 31.87 ?  2006 HOH B O     1 
HETATM 20149 O O     . HOH T 7 .    ? -16.778 -0.937  100.552 1.00 31.10 ?  2007 HOH B O     1 
HETATM 20150 O O     . HOH T 7 .    ? 7.333   66.340  87.599  1.00 27.59 ?  2008 HOH B O     1 
HETATM 20151 O O     . HOH T 7 .    ? 9.421   67.838  55.773  1.00 35.24 ?  2009 HOH B O     1 
HETATM 20152 O O     . HOH T 7 .    ? -7.532  12.725  95.653  1.00 16.25 ?  2010 HOH B O     1 
HETATM 20153 O O     . HOH T 7 .    ? 16.161  53.428  106.126 1.00 23.08 ?  2011 HOH B O     1 
HETATM 20154 O O     . HOH T 7 .    ? 6.255   30.421  121.463 1.00 33.58 ?  2012 HOH B O     1 
HETATM 20155 O O     . HOH T 7 .    ? 14.784  57.385  72.474  1.00 21.07 ?  2013 HOH B O     1 
HETATM 20156 O O     . HOH T 7 .    ? 16.318  21.532  100.979 1.00 20.82 ?  2014 HOH B O     1 
HETATM 20157 O O     . HOH T 7 .    ? -6.001  35.368  88.679  1.00 23.53 ?  2015 HOH B O     1 
HETATM 20158 O O     . HOH T 7 .    ? 27.013  38.456  106.100 1.00 26.63 ?  2016 HOH B O     1 
HETATM 20159 O O     . HOH T 7 .    ? -16.635 21.367  83.467  1.00 24.73 ?  2017 HOH B O     1 
HETATM 20160 O O     . HOH T 7 .    ? -1.671  31.305  126.553 1.00 29.34 ?  2018 HOH B O     1 
HETATM 20161 O O     . HOH T 7 .    ? 18.373  66.887  59.182  1.00 25.59 ?  2019 HOH B O     1 
HETATM 20162 O O     . HOH T 7 .    ? -0.456  17.644  92.617  1.00 17.07 ?  2020 HOH B O     1 
HETATM 20163 O O     . HOH T 7 .    ? 8.395   15.531  93.876  1.00 26.59 ?  2021 HOH B O     1 
HETATM 20164 O O     . HOH T 7 .    ? 8.727   5.607   86.136  1.00 20.11 ?  2022 HOH B O     1 
HETATM 20165 O O     . HOH T 7 .    ? -6.345  35.346  93.628  1.00 24.04 ?  2023 HOH B O     1 
HETATM 20166 O O     . HOH T 7 .    ? 9.505   -0.781  91.432  1.00 32.34 ?  2024 HOH B O     1 
HETATM 20167 O O     . HOH T 7 .    ? 13.740  16.969  87.357  1.00 22.59 ?  2025 HOH B O     1 
HETATM 20168 O O     . HOH T 7 .    ? -20.315 23.206  113.669 1.00 25.39 ?  2026 HOH B O     1 
HETATM 20169 O O     . HOH T 7 .    ? 33.420  45.298  75.310  1.00 27.24 ?  2027 HOH B O     1 
HETATM 20170 O O     . HOH T 7 .    ? 28.220  8.549   74.319  1.00 33.09 ?  2028 HOH B O     1 
HETATM 20171 O O     . HOH T 7 .    ? 10.512  33.429  110.781 1.00 24.06 ?  2029 HOH B O     1 
HETATM 20172 O O     . HOH T 7 .    ? 31.969  62.252  75.943  1.00 16.67 ?  2030 HOH B O     1 
HETATM 20173 O O     . HOH T 7 .    ? 28.882  23.733  51.526  1.00 26.89 ?  2031 HOH B O     1 
HETATM 20174 O O     . HOH T 7 .    ? 5.330   66.642  62.943  1.00 31.66 ?  2032 HOH B O     1 
HETATM 20175 O O     . HOH T 7 .    ? 29.046  32.538  78.506  1.00 30.07 ?  2033 HOH B O     1 
HETATM 20176 O O     . HOH T 7 .    ? -1.304  17.314  83.686  1.00 24.63 ?  2034 HOH B O     1 
HETATM 20177 O O     . HOH T 7 .    ? 2.996   44.815  68.743  1.00 13.84 ?  2035 HOH B O     1 
HETATM 20178 O O     . HOH T 7 .    ? 34.336  29.010  105.734 1.00 32.25 ?  2036 HOH B O     1 
HETATM 20179 O O     . HOH T 7 .    ? 1.057   38.638  106.564 1.00 23.16 ?  2037 HOH B O     1 
HETATM 20180 O O     . HOH T 7 .    ? -34.793 12.479  112.447 1.00 34.07 ?  2038 HOH B O     1 
HETATM 20181 O O     . HOH T 7 .    ? 35.285  31.939  55.744  1.00 27.23 ?  2039 HOH B O     1 
HETATM 20182 O O     . HOH T 7 .    ? 31.418  50.801  80.468  1.00 27.99 ?  2040 HOH B O     1 
HETATM 20183 O O     . HOH T 7 .    ? 28.900  31.178  71.637  1.00 27.73 ?  2041 HOH B O     1 
HETATM 20184 O O     . HOH T 7 .    ? 9.127   28.937  99.705  1.00 25.17 ?  2042 HOH B O     1 
HETATM 20185 O O     . HOH T 7 .    ? 30.914  19.395  56.614  1.00 24.17 ?  2043 HOH B O     1 
HETATM 20186 O O     . HOH T 7 .    ? 12.063  26.400  89.332  1.00 27.70 ?  2044 HOH B O     1 
HETATM 20187 O O     . HOH T 7 .    ? -3.516  -4.910  119.520 1.00 33.70 ?  2045 HOH B O     1 
HETATM 20188 O O     . HOH T 7 .    ? 1.894   61.045  82.035  1.00 22.78 ?  2046 HOH B O     1 
HETATM 20189 O O     . HOH T 7 .    ? 20.707  62.558  54.918  1.00 29.75 ?  2047 HOH B O     1 
HETATM 20190 O O     . HOH T 7 .    ? -8.542  26.815  100.840 1.00 21.31 ?  2048 HOH B O     1 
HETATM 20191 O O     . HOH T 7 .    ? 12.922  56.793  60.245  1.00 34.06 ?  2049 HOH B O     1 
HETATM 20192 O O     . HOH T 7 .    ? 4.807   56.199  75.967  1.00 15.17 ?  2050 HOH B O     1 
HETATM 20193 O O     . HOH T 7 .    ? -2.037  36.550  88.371  1.00 15.06 ?  2051 HOH B O     1 
HETATM 20194 O O     . HOH T 7 .    ? 11.914  49.201  79.930  1.00 29.74 ?  2052 HOH B O     1 
HETATM 20195 O O     . HOH T 7 .    ? -19.908 28.402  89.351  1.00 26.67 ?  2053 HOH B O     1 
HETATM 20196 O O     . HOH T 7 .    ? -28.481 3.089   104.767 1.00 37.16 ?  2054 HOH B O     1 
HETATM 20197 O O     . HOH T 7 .    ? 9.874   53.192  66.603  1.00 18.83 ?  2055 HOH B O     1 
HETATM 20198 O O     . HOH T 7 .    ? -5.757  46.296  84.859  1.00 21.64 ?  2056 HOH B O     1 
HETATM 20199 O O     . HOH T 7 .    ? -11.035 36.187  77.365  1.00 34.91 ?  2057 HOH B O     1 
HETATM 20200 O O     . HOH T 7 .    ? 4.614   -0.124  87.886  1.00 29.42 ?  2058 HOH B O     1 
HETATM 20201 O O     . HOH T 7 .    ? 34.815  31.167  63.693  1.00 35.84 ?  2059 HOH B O     1 
HETATM 20202 O O     . HOH T 7 .    ? 28.921  65.232  63.157  1.00 27.20 ?  2060 HOH B O     1 
HETATM 20203 O O     . HOH T 7 .    ? -30.142 17.155  104.908 1.00 30.40 ?  2061 HOH B O     1 
HETATM 20204 O O     . HOH T 7 .    ? 17.860  76.666  64.694  1.00 27.85 ?  2062 HOH B O     1 
HETATM 20205 O O     . HOH T 7 .    ? -6.550  37.241  97.391  1.00 26.78 ?  2063 HOH B O     1 
HETATM 20206 O O     . HOH T 7 .    ? -8.365  23.669  126.525 1.00 28.96 ?  2064 HOH B O     1 
HETATM 20207 O O     . HOH T 7 .    ? 5.176   23.530  120.947 1.00 31.15 ?  2065 HOH B O     1 
HETATM 20208 O O     . HOH T 7 .    ? 35.607  31.121  59.168  1.00 29.15 ?  2066 HOH B O     1 
HETATM 20209 O O     . HOH T 7 .    ? 5.760   11.360  78.393  1.00 33.63 ?  2067 HOH B O     1 
HETATM 20210 O O     . HOH T 7 .    ? 5.128   42.889  56.923  1.00 26.40 ?  2068 HOH B O     1 
HETATM 20211 O O     . HOH T 7 .    ? -1.956  27.915  63.495  1.00 20.93 ?  2069 HOH B O     1 
HETATM 20212 O O     . HOH T 7 .    ? 32.780  28.475  65.083  1.00 25.32 ?  2070 HOH B O     1 
HETATM 20213 O O     . HOH T 7 .    ? -6.549  8.628   83.097  1.00 30.72 ?  2071 HOH B O     1 
HETATM 20214 O O     . HOH T 7 .    ? 23.234  51.979  84.989  1.00 33.63 ?  2072 HOH B O     1 
HETATM 20215 O O     . HOH T 7 .    ? 16.964  33.541  49.332  1.00 25.79 ?  2073 HOH B O     1 
HETATM 20216 O O     . HOH T 7 .    ? 15.232  28.760  49.867  1.00 29.56 ?  2074 HOH B O     1 
HETATM 20217 O O     . HOH T 7 .    ? 25.888  46.909  101.801 1.00 33.92 ?  2075 HOH B O     1 
HETATM 20218 O O     . HOH T 7 .    ? 2.897   31.033  99.433  1.00 20.69 ?  2076 HOH B O     1 
HETATM 20219 O O     . HOH T 7 .    ? 24.550  15.560  96.339  1.00 26.00 ?  2077 HOH B O     1 
HETATM 20220 O O     . HOH T 7 .    ? 8.318   37.217  80.218  1.00 17.00 ?  2078 HOH B O     1 
HETATM 20221 O O     . HOH T 7 .    ? -14.074 49.007  111.865 1.00 30.01 ?  2079 HOH B O     1 
HETATM 20222 O O     . HOH T 7 .    ? 11.378  45.077  110.366 1.00 31.81 ?  2080 HOH B O     1 
HETATM 20223 O O     . HOH T 7 .    ? 5.627   18.376  88.461  1.00 22.16 ?  2081 HOH B O     1 
HETATM 20224 O O     . HOH T 7 .    ? -2.866  64.514  84.424  1.00 13.97 ?  2082 HOH B O     1 
HETATM 20225 O O     . HOH T 7 .    ? 25.271  23.906  50.524  1.00 33.39 ?  2083 HOH B O     1 
HETATM 20226 O O     . HOH T 7 .    ? 27.655  10.116  85.507  1.00 33.13 ?  2084 HOH B O     1 
HETATM 20227 O O     . HOH T 7 .    ? -0.419  25.298  104.142 1.00 32.44 ?  2085 HOH B O     1 
HETATM 20228 O O     . HOH T 7 .    ? 11.482  56.238  87.015  1.00 33.39 ?  2086 HOH B O     1 
HETATM 20229 O O     . HOH T 7 .    ? -1.025  37.385  77.296  1.00 28.39 ?  2087 HOH B O     1 
HETATM 20230 O O     . HOH T 7 .    ? 23.290  72.779  82.715  1.00 26.56 ?  2088 HOH B O     1 
HETATM 20231 O O     . HOH T 7 .    ? -2.098  57.650  76.112  1.00 15.29 ?  2089 HOH B O     1 
HETATM 20232 O O     . HOH T 7 .    ? 16.215  50.884  61.786  1.00 21.40 ?  2090 HOH B O     1 
HETATM 20233 O O     . HOH T 7 .    ? 18.100  49.413  112.988 1.00 31.97 ?  2091 HOH B O     1 
HETATM 20234 O O     . HOH T 7 .    ? -4.766  -4.436  92.900  1.00 24.91 ?  2092 HOH B O     1 
HETATM 20235 O O     . HOH T 7 .    ? 7.903   77.383  86.951  1.00 36.42 ?  2093 HOH B O     1 
HETATM 20236 O O     . HOH T 7 .    ? 22.498  53.383  54.856  1.00 33.81 ?  2094 HOH B O     1 
HETATM 20237 O O     . HOH T 7 .    ? -0.323  44.795  78.308  1.00 28.97 ?  2095 HOH B O     1 
HETATM 20238 O O     . HOH T 7 .    ? 34.970  16.445  68.262  1.00 28.28 ?  2096 HOH B O     1 
HETATM 20239 O O     . HOH T 7 .    ? 22.090  13.980  81.771  1.00 28.66 ?  2097 HOH B O     1 
HETATM 20240 O O     . HOH T 7 .    ? 6.209   57.036  62.427  1.00 35.70 ?  2098 HOH B O     1 
HETATM 20241 O O     . HOH T 7 .    ? 25.301  52.428  56.125  1.00 33.05 ?  2099 HOH B O     1 
HETATM 20242 O O     . HOH T 7 .    ? 20.380  20.159  110.369 1.00 20.93 ?  2100 HOH B O     1 
HETATM 20243 O O     . HOH T 7 .    ? -0.618  -8.338  100.882 1.00 28.53 ?  2101 HOH B O     1 
HETATM 20244 O O     . HOH T 7 .    ? 4.287   25.085  129.963 1.00 31.48 ?  2102 HOH B O     1 
HETATM 20245 O O     . HOH T 7 .    ? 12.039  25.932  120.338 1.00 37.78 ?  2103 HOH B O     1 
HETATM 20246 O O     . HOH T 7 .    ? 18.182  75.906  79.670  1.00 34.58 ?  2104 HOH B O     1 
HETATM 20247 O O     . HOH T 7 .    ? 11.307  25.320  86.892  1.00 29.43 ?  2105 HOH B O     1 
HETATM 20248 O O     . HOH T 7 .    ? -5.938  15.089  95.514  1.00 15.72 ?  2106 HOH B O     1 
HETATM 20249 O O     . HOH T 7 .    ? -1.264  22.301  98.257  1.00 22.33 ?  2107 HOH B O     1 
HETATM 20250 O O     . HOH T 7 .    ? -2.890  39.909  58.714  1.00 22.15 ?  2108 HOH B O     1 
HETATM 20251 O O     . HOH T 7 .    ? 7.670   54.275  65.399  1.00 23.60 ?  2109 HOH B O     1 
HETATM 20252 O O     . HOH T 7 .    ? 4.735   -4.213  96.707  1.00 39.11 ?  2110 HOH B O     1 
HETATM 20253 O O     . HOH T 7 .    ? 34.563  12.690  81.518  1.00 33.84 ?  2111 HOH B O     1 
HETATM 20254 O O     . HOH T 7 .    ? 0.588   63.168  85.661  1.00 27.82 ?  2112 HOH B O     1 
HETATM 20255 O O     . HOH T 7 .    ? -5.626  37.152  86.873  1.00 23.74 ?  2113 HOH B O     1 
HETATM 20256 O O     . HOH T 7 .    ? 25.874  75.372  77.675  1.00 28.40 ?  2114 HOH B O     1 
HETATM 20257 O O     . HOH T 7 .    ? 14.491  8.750   94.703  1.00 22.21 ?  2115 HOH B O     1 
HETATM 20258 O O     . HOH T 7 .    ? 19.123  54.351  105.433 1.00 22.48 ?  2116 HOH B O     1 
HETATM 20259 O O     . HOH T 7 .    ? 19.543  58.531  83.383  1.00 24.90 ?  2117 HOH B O     1 
HETATM 20260 O O     . HOH T 7 .    ? -0.673  27.832  104.815 1.00 28.21 ?  2118 HOH B O     1 
HETATM 20261 O O     . HOH T 7 .    ? 6.605   16.739  116.678 1.00 24.60 ?  2119 HOH B O     1 
HETATM 20262 O O     . HOH T 7 .    ? 34.942  15.902  62.540  1.00 33.62 ?  2120 HOH B O     1 
HETATM 20263 O O     . HOH T 7 .    ? 31.373  67.020  83.661  1.00 31.98 ?  2121 HOH B O     1 
HETATM 20264 O O     . HOH T 7 .    ? -23.682 20.797  103.250 1.00 30.62 ?  2122 HOH B O     1 
HETATM 20265 O O     . HOH T 7 .    ? -2.743  -6.020  90.823  1.00 31.13 ?  2123 HOH B O     1 
HETATM 20266 O O     . HOH T 7 .    ? 13.989  75.788  63.769  1.00 28.35 ?  2124 HOH B O     1 
HETATM 20267 O O     . HOH T 7 .    ? -4.850  25.309  115.810 1.00 30.70 ?  2125 HOH B O     1 
HETATM 20268 O O     . HOH T 7 .    ? 7.594   28.216  82.298  1.00 30.53 ?  2126 HOH B O     1 
HETATM 20269 O O     . HOH T 7 .    ? 3.477   23.102  105.179 1.00 33.01 ?  2127 HOH B O     1 
HETATM 20270 O O     . HOH T 7 .    ? 6.934   35.635  110.170 1.00 33.21 ?  2128 HOH B O     1 
HETATM 20271 O O     . HOH T 7 .    ? -6.944  38.868  68.417  1.00 29.69 ?  2129 HOH B O     1 
HETATM 20272 O O     . HOH T 7 .    ? -6.257  39.603  87.196  1.00 24.38 ?  2130 HOH B O     1 
HETATM 20273 O O     . HOH T 7 .    ? 16.905  24.894  94.218  1.00 31.32 ?  2131 HOH B O     1 
HETATM 20274 O O     . HOH T 7 .    ? 18.618  34.146  46.704  1.00 34.34 ?  2132 HOH B O     1 
HETATM 20275 O O     . HOH T 7 .    ? 18.789  35.462  114.386 1.00 18.77 ?  2133 HOH B O     1 
HETATM 20276 O O     . HOH T 7 .    ? 23.288  24.189  48.125  1.00 28.69 ?  2134 HOH B O     1 
HETATM 20277 O O     . HOH T 7 .    ? 35.552  25.188  78.629  1.00 25.57 ?  2135 HOH B O     1 
HETATM 20278 O O     . HOH T 7 .    ? 11.936  28.655  84.103  1.00 26.42 ?  2136 HOH B O     1 
HETATM 20279 O O     . HOH T 7 .    ? -7.689  10.023  114.222 1.00 19.06 ?  2137 HOH B O     1 
HETATM 20280 O O     . HOH T 7 .    ? 12.693  29.205  51.170  1.00 25.24 ?  2138 HOH B O     1 
HETATM 20281 O O     . HOH T 7 .    ? 26.254  12.716  91.658  1.00 29.88 ?  2139 HOH B O     1 
HETATM 20282 O O     . HOH T 7 .    ? -3.044  22.428  80.594  1.00 21.14 ?  2140 HOH B O     1 
HETATM 20283 O O     . HOH T 7 .    ? 12.189  77.610  65.050  1.00 33.09 ?  2141 HOH B O     1 
HETATM 20284 O O     . HOH T 7 .    ? -32.285 13.851  115.536 1.00 38.89 ?  2142 HOH B O     1 
HETATM 20285 O O     . HOH T 7 .    ? -2.810  26.125  114.338 1.00 32.19 ?  2143 HOH B O     1 
HETATM 20286 O O     . HOH T 7 .    ? 29.150  22.026  73.227  1.00 28.50 ?  2144 HOH B O     1 
HETATM 20287 O O     . HOH T 7 .    ? -9.100  7.194   83.197  1.00 36.51 ?  2145 HOH B O     1 
HETATM 20288 O O     . HOH T 7 .    ? 2.257   18.439  78.122  1.00 28.95 ?  2146 HOH B O     1 
HETATM 20289 O O     . HOH T 7 .    ? 15.858  66.918  56.357  1.00 25.34 ?  2147 HOH B O     1 
HETATM 20290 O O     . HOH T 7 .    ? -15.042 18.352  81.056  1.00 29.41 ?  2148 HOH B O     1 
HETATM 20291 O O     . HOH T 7 .    ? 8.216   5.232   70.541  1.00 33.69 ?  2149 HOH B O     1 
HETATM 20292 O O     . HOH T 7 .    ? -0.562  31.276  109.868 1.00 31.65 ?  2150 HOH B O     1 
HETATM 20293 O O     . HOH T 7 .    ? -13.042 31.112  84.828  1.00 29.91 ?  2151 HOH B O     1 
HETATM 20294 O O     . HOH T 7 .    ? -15.280 18.872  83.644  1.00 23.72 ?  2152 HOH B O     1 
HETATM 20295 O O     . HOH T 7 .    ? -1.257  29.074  107.269 1.00 29.38 ?  2153 HOH B O     1 
HETATM 20296 O O     . HOH T 7 .    ? -33.726 16.461  122.758 1.00 26.86 ?  2154 HOH B O     1 
HETATM 20297 O O     . HOH T 7 .    ? 8.038   -9.714  112.665 1.00 33.82 ?  2155 HOH B O     1 
HETATM 20298 O O     . HOH T 7 .    ? 10.388  35.192  80.334  1.00 29.05 ?  2156 HOH B O     1 
HETATM 20299 O O     . HOH T 7 .    ? 21.356  26.278  82.888  1.00 18.27 ?  2157 HOH B O     1 
HETATM 20300 O O     . HOH T 7 .    ? -32.313 30.162  112.269 1.00 36.81 ?  2158 HOH B O     1 
HETATM 20301 O O     . HOH T 7 .    ? 5.399   70.564  62.077  1.00 33.08 ?  2159 HOH B O     1 
HETATM 20302 O O     . HOH T 7 .    ? 16.018  9.972   96.665  1.00 25.19 ?  2160 HOH B O     1 
HETATM 20303 O O     . HOH T 7 .    ? 5.209   76.609  86.238  1.00 33.35 ?  2161 HOH B O     1 
HETATM 20304 O O     . HOH T 7 .    ? 16.092  49.522  79.746  1.00 32.03 ?  2162 HOH B O     1 
HETATM 20305 O O     . HOH T 7 .    ? 8.928   80.249  86.451  1.00 40.55 ?  2163 HOH B O     1 
HETATM 20306 O O     . HOH T 7 .    ? -7.533  11.751  84.280  1.00 32.89 ?  2164 HOH B O     1 
HETATM 20307 O O     . HOH T 7 .    ? 17.960  74.841  82.767  1.00 31.10 ?  2165 HOH B O     1 
HETATM 20308 O O     . HOH T 7 .    ? 8.202   21.019  121.108 1.00 35.54 ?  2166 HOH B O     1 
HETATM 20309 O O     . HOH T 7 .    ? 22.735  67.599  60.242  1.00 27.43 ?  2167 HOH B O     1 
HETATM 20310 O O     . HOH T 7 .    ? -2.369  60.245  125.268 1.00 33.66 ?  2168 HOH B O     1 
HETATM 20311 O O     . HOH T 7 .    ? 21.797  11.292  80.287  1.00 34.16 ?  2169 HOH B O     1 
HETATM 20312 O O     . HOH T 7 .    ? 5.930   17.026  97.454  1.00 26.72 ?  2170 HOH B O     1 
HETATM 20313 O O     . HOH T 7 .    ? 5.882   47.993  115.702 1.00 29.80 ?  2171 HOH B O     1 
HETATM 20314 O O     . HOH T 7 .    ? -0.572  43.933  56.882  1.00 25.90 ?  2172 HOH B O     1 
HETATM 20315 O O     . HOH T 7 .    ? 18.416  63.369  55.951  1.00 29.29 ?  2173 HOH B O     1 
HETATM 20316 O O     . HOH T 7 .    ? 31.567  31.485  84.580  1.00 28.82 ?  2174 HOH B O     1 
HETATM 20317 O O     . HOH T 7 .    ? 31.039  67.670  73.635  1.00 28.58 ?  2175 HOH B O     1 
HETATM 20318 O O     . HOH T 7 .    ? 29.441  8.132   86.954  1.00 36.16 ?  2176 HOH B O     1 
HETATM 20319 O O     . HOH T 7 .    ? -1.757  -10.093 110.527 1.00 26.77 ?  2177 HOH B O     1 
HETATM 20320 O O     . HOH T 7 .    ? -2.561  69.548  76.662  1.00 34.09 ?  2178 HOH B O     1 
HETATM 20321 O O     . HOH T 7 .    ? -8.887  41.842  73.228  1.00 30.40 ?  2179 HOH B O     1 
HETATM 20322 O O     . HOH T 7 .    ? -6.970  6.711   115.019 1.00 35.26 ?  2180 HOH B O     1 
HETATM 20323 O O     . HOH T 7 .    ? 11.475  43.607  51.811  1.00 27.17 ?  2181 HOH B O     1 
HETATM 20324 O O     . HOH T 7 .    ? -2.057  2.351   84.426  1.00 37.19 ?  2182 HOH B O     1 
HETATM 20325 O O     . HOH T 7 .    ? 32.804  70.605  74.433  1.00 25.56 ?  2183 HOH B O     1 
HETATM 20326 O O     . HOH T 7 .    ? -30.333 15.866  116.156 1.00 34.23 ?  2184 HOH B O     1 
HETATM 20327 O O     . HOH T 7 .    ? -7.126  36.866  67.320  1.00 29.93 ?  2185 HOH B O     1 
HETATM 20328 O O     . HOH T 7 .    ? 4.424   -4.953  99.574  1.00 36.32 ?  2186 HOH B O     1 
HETATM 20329 O O     . HOH T 7 .    ? -22.107 7.119   86.924  1.00 37.93 ?  2187 HOH B O     1 
HETATM 20330 O O     . HOH T 7 .    ? 7.423   33.682  52.161  1.00 27.52 ?  2188 HOH B O     1 
HETATM 20331 O O     . HOH T 7 .    ? 16.384  13.835  108.081 1.00 28.59 ?  2189 HOH B O     1 
HETATM 20332 O O     . HOH T 7 .    ? 2.501   36.846  104.780 1.00 31.01 ?  2190 HOH B O     1 
HETATM 20333 O O     . HOH T 7 .    ? 15.038  51.030  57.226  1.00 28.21 ?  2191 HOH B O     1 
HETATM 20334 O O     . HOH T 7 .    ? -9.384  -7.618  115.381 1.00 32.87 ?  2192 HOH B O     1 
HETATM 20335 O O     . HOH T 7 .    ? 23.494  49.889  103.969 1.00 36.56 ?  2193 HOH B O     1 
HETATM 20336 O O     . HOH T 7 .    ? -3.039  29.641  98.101  1.00 25.24 ?  2194 HOH B O     1 
HETATM 20337 O O     . HOH T 7 .    ? 32.914  19.594  73.221  1.00 36.24 ?  2195 HOH B O     1 
HETATM 20338 O O     . HOH T 7 .    ? 16.638  56.121  96.078  1.00 30.45 ?  2196 HOH B O     1 
HETATM 20339 O O     . HOH T 7 .    ? -6.807  7.769   117.792 1.00 23.86 ?  2197 HOH B O     1 
HETATM 20340 O O     . HOH T 7 .    ? 0.043   -2.612  96.062  1.00 26.84 ?  2198 HOH B O     1 
HETATM 20341 O O     . HOH T 7 .    ? 4.938   4.073   79.921  1.00 34.12 ?  2199 HOH B O     1 
HETATM 20342 O O     . HOH T 7 .    ? 32.493  20.121  77.119  1.00 34.62 ?  2200 HOH B O     1 
HETATM 20343 O O     . HOH T 7 .    ? 33.333  15.306  65.116  1.00 33.15 ?  2201 HOH B O     1 
HETATM 20344 O O     . HOH T 7 .    ? 9.378   48.475  109.644 1.00 29.39 ?  2202 HOH B O     1 
HETATM 20345 O O     . HOH T 7 .    ? -33.360 16.056  102.133 1.00 30.58 ?  2203 HOH B O     1 
HETATM 20346 O O     . HOH T 7 .    ? 25.615  32.754  76.209  1.00 26.67 ?  2204 HOH B O     1 
HETATM 20347 O O     . HOH T 7 .    ? -6.745  2.241   86.176  1.00 29.16 ?  2205 HOH B O     1 
HETATM 20348 O O     . HOH T 7 .    ? 4.088   29.362  82.966  1.00 24.78 ?  2206 HOH B O     1 
HETATM 20349 O O     . HOH T 7 .    ? 32.929  58.421  68.137  1.00 26.62 ?  2207 HOH B O     1 
HETATM 20350 O O     . HOH T 7 .    ? 7.099   30.633  91.341  1.00 32.13 ?  2208 HOH B O     1 
HETATM 20351 O O     . HOH T 7 .    ? 19.654  45.261  90.974  1.00 18.09 ?  2209 HOH B O     1 
HETATM 20352 O O     . HOH T 7 .    ? 28.446  41.152  54.062  1.00 37.23 ?  2210 HOH B O     1 
HETATM 20353 O O     . HOH T 7 .    ? 6.781   21.718  117.111 1.00 36.56 ?  2211 HOH B O     1 
HETATM 20354 O O     . HOH T 7 .    ? 2.198   3.329   83.104  1.00 28.77 ?  2212 HOH B O     1 
HETATM 20355 O O     . HOH T 7 .    ? -3.986  14.264  133.338 1.00 31.69 ?  2213 HOH B O     1 
HETATM 20356 O O     . HOH T 7 .    ? 16.892  26.029  111.057 1.00 26.47 ?  2214 HOH B O     1 
HETATM 20357 O O     . HOH T 7 .    ? 27.268  73.569  79.492  1.00 37.14 ?  2215 HOH B O     1 
HETATM 20358 O O     . HOH T 7 .    ? 23.609  22.486  108.145 1.00 29.31 ?  2216 HOH B O     1 
HETATM 20359 O O     . HOH T 7 .    ? 25.026  9.073   86.333  1.00 35.39 ?  2217 HOH B O     1 
HETATM 20360 O O     . HOH T 7 .    ? -30.647 14.435  120.272 1.00 35.92 ?  2218 HOH B O     1 
HETATM 20361 O O     . HOH T 7 .    ? 6.497   28.814  92.427  1.00 36.06 ?  2219 HOH B O     1 
HETATM 20362 O O     . HOH T 7 .    ? 4.751   14.805  61.187  1.00 29.15 ?  2220 HOH B O     1 
HETATM 20363 O O     . HOH T 7 .    ? 30.268  71.027  73.979  1.00 28.40 ?  2221 HOH B O     1 
HETATM 20364 O O     . HOH T 7 .    ? 5.360   44.482  54.607  1.00 27.30 ?  2222 HOH B O     1 
HETATM 20365 O O     . HOH T 7 .    ? 40.710  39.413  86.424  1.00 36.58 ?  2223 HOH B O     1 
HETATM 20366 O O     . HOH T 7 .    ? 23.811  68.760  62.983  1.00 31.56 ?  2224 HOH B O     1 
HETATM 20367 O O     . HOH T 7 .    ? 20.609  24.094  84.463  1.00 17.71 ?  2225 HOH B O     1 
HETATM 20368 O O     . HOH T 7 .    ? -2.615  41.035  79.007  1.00 27.91 ?  2226 HOH B O     1 
HETATM 20369 O O     . HOH T 7 .    ? 4.899   43.433  51.945  1.00 24.50 ?  2227 HOH B O     1 
HETATM 20370 O O     . HOH T 7 .    ? -22.486 25.113  93.117  1.00 35.16 ?  2228 HOH B O     1 
HETATM 20371 O O     . HOH T 7 .    ? 21.459  18.072  111.907 1.00 33.57 ?  2229 HOH B O     1 
HETATM 20372 O O     . HOH T 7 .    ? 8.649   17.015  124.418 1.00 25.07 ?  2230 HOH B O     1 
HETATM 20373 O O     . HOH T 7 .    ? 20.688  68.540  59.425  1.00 36.01 ?  2231 HOH B O     1 
HETATM 20374 O O     . HOH T 7 .    ? 7.308   18.891  98.420  1.00 32.59 ?  2232 HOH B O     1 
HETATM 20375 O O     . HOH T 7 .    ? -2.674  51.822  102.221 1.00 22.52 ?  2233 HOH B O     1 
HETATM 20376 O O     . HOH T 7 .    ? 6.686   23.471  84.119  1.00 22.72 ?  2234 HOH B O     1 
HETATM 20377 O O     . HOH T 7 .    ? 14.596  48.006  54.338  1.00 36.59 ?  2235 HOH B O     1 
HETATM 20378 O O     . HOH T 7 .    ? 0.326   4.222   87.169  1.00 23.52 ?  2236 HOH B O     1 
HETATM 20379 O O     . HOH T 7 .    ? -2.067  25.876  65.316  1.00 26.84 ?  2237 HOH B O     1 
HETATM 20380 O O     . HOH T 7 .    ? 9.238   63.940  88.078  1.00 28.91 ?  2238 HOH B O     1 
HETATM 20381 O O     . HOH T 7 .    ? -0.128  18.650  76.615  1.00 33.38 ?  2239 HOH B O     1 
HETATM 20382 O O     . HOH T 7 .    ? 22.892  35.401  78.956  1.00 28.76 ?  2240 HOH B O     1 
HETATM 20383 O O     . HOH T 7 .    ? -34.736 14.120  114.527 1.00 37.85 ?  2241 HOH B O     1 
HETATM 20384 O O     . HOH T 7 .    ? 30.113  73.645  73.355  1.00 32.39 ?  2242 HOH B O     1 
HETATM 20385 O O     . HOH T 7 .    ? 2.397   62.037  84.567  1.00 19.79 ?  2243 HOH B O     1 
HETATM 20386 O O     . HOH T 7 .    ? -7.563  -3.322  118.857 1.00 30.43 ?  2244 HOH B O     1 
HETATM 20387 O O     . HOH T 7 .    ? 14.762  21.743  98.729  1.00 27.46 ?  2245 HOH B O     1 
HETATM 20388 O O     . HOH T 7 .    ? 13.814  24.965  102.017 1.00 24.29 ?  2246 HOH B O     1 
HETATM 20389 O O     . HOH T 7 .    ? 11.046  9.821   124.404 1.00 26.98 ?  2247 HOH B O     1 
HETATM 20390 O O     . HOH T 7 .    ? 20.229  31.535  115.806 1.00 31.53 ?  2248 HOH B O     1 
HETATM 20391 O O     . HOH T 7 .    ? 8.873   23.301  123.543 1.00 27.84 ?  2249 HOH B O     1 
HETATM 20392 O O     . HOH T 7 .    ? 5.265   31.857  88.480  1.00 22.08 ?  2250 HOH B O     1 
HETATM 20393 O O     . HOH T 7 .    ? 3.526   29.467  95.281  1.00 29.42 ?  2251 HOH B O     1 
HETATM 20394 O O     . HOH T 7 .    ? 15.132  3.504   73.428  1.00 36.94 ?  2252 HOH B O     1 
HETATM 20395 O O     . HOH T 7 .    ? -10.590 29.618  76.965  1.00 29.58 ?  2253 HOH B O     1 
HETATM 20396 O O     . HOH T 7 .    ? 5.685   30.368  99.716  1.00 36.46 ?  2254 HOH B O     1 
HETATM 20397 O O     . HOH T 7 .    ? -2.925  28.287  69.764  1.00 21.32 ?  2255 HOH B O     1 
HETATM 20398 O O     . HOH T 7 .    ? -11.266 28.615  100.707 1.00 30.16 ?  2256 HOH B O     1 
HETATM 20399 O O     . HOH T 7 .    ? -7.561  22.080  79.530  1.00 29.74 ?  2257 HOH B O     1 
HETATM 20400 O O     . HOH T 7 .    ? 32.337  74.708  75.543  1.00 37.59 ?  2258 HOH B O     1 
HETATM 20401 O O     . HOH T 7 .    ? 6.213   60.476  88.997  1.00 28.92 ?  2259 HOH B O     1 
HETATM 20402 O O     . HOH T 7 .    ? 0.000   24.003  100.267 1.00 30.41 ?  2260 HOH B O     1 
HETATM 20403 O O     . HOH T 7 .    ? -0.035  17.832  72.680  1.00 29.29 ?  2261 HOH B O     1 
HETATM 20404 O O     . HOH T 7 .    ? 6.439   -10.219 106.411 1.00 33.18 ?  2262 HOH B O     1 
HETATM 20405 O O     . HOH T 7 .    ? -17.850 6.110   94.103  1.00 30.32 ?  2263 HOH B O     1 
HETATM 20406 O O     . HOH T 7 .    ? 12.251  21.267  99.733  1.00 30.35 ?  2264 HOH B O     1 
HETATM 20407 O O     . HOH T 7 .    ? -4.090  40.151  61.388  1.00 27.15 ?  2265 HOH B O     1 
HETATM 20408 O O     . HOH T 7 .    ? 1.751   29.385  104.131 1.00 37.78 ?  2266 HOH B O     1 
HETATM 20409 O O     . HOH T 7 .    ? 12.479  18.049  93.097  1.00 28.00 ?  2267 HOH B O     1 
HETATM 20410 O O     . HOH T 7 .    ? 11.619  0.456   114.962 1.00 31.70 ?  2268 HOH B O     1 
HETATM 20411 O O     . HOH T 7 .    ? 4.769   16.025  124.451 1.00 21.65 ?  2269 HOH B O     1 
HETATM 20412 O O     . HOH T 7 .    ? 0.979   14.316  80.687  1.00 36.40 ?  2270 HOH B O     1 
HETATM 20413 O O     . HOH T 7 .    ? 6.664   1.973   80.813  1.00 37.07 ?  2271 HOH B O     1 
HETATM 20414 O O     . HOH T 7 .    ? 6.596   42.363  47.827  1.00 34.43 ?  2272 HOH B O     1 
HETATM 20415 O O     . HOH T 7 .    ? 18.666  6.941   99.492  1.00 35.46 ?  2273 HOH B O     1 
HETATM 20416 O O     . HOH T 7 .    ? 19.970  33.978  116.368 1.00 24.19 ?  2274 HOH B O     1 
HETATM 20417 O O     . HOH T 7 .    ? 8.476   47.504  111.978 1.00 35.15 ?  2275 HOH B O     1 
HETATM 20418 O O     . HOH T 7 .    ? -0.774  3.213   82.407  1.00 37.64 ?  2276 HOH B O     1 
HETATM 20419 O O     . HOH T 7 .    ? 13.164  55.739  63.899  1.00 29.40 ?  2277 HOH B O     1 
HETATM 20420 O O     . HOH T 7 .    ? 5.534   10.365  76.018  1.00 30.77 ?  2278 HOH B O     1 
HETATM 20421 O O     . HOH T 7 .    ? 34.686  25.611  57.285  1.00 25.25 ?  2279 HOH B O     1 
HETATM 20422 O O     . HOH T 7 .    ? -12.312 29.996  82.750  1.00 29.52 ?  2280 HOH B O     1 
HETATM 20423 O O     . HOH T 7 .    ? 4.357   15.463  130.347 1.00 24.41 ?  2281 HOH B O     1 
HETATM 20424 O O     . HOH T 7 .    ? 20.567  22.803  111.241 1.00 29.89 ?  2282 HOH B O     1 
HETATM 20425 O O     . HOH T 7 .    ? -24.426 7.642   86.505  1.00 34.81 ?  2283 HOH B O     1 
HETATM 20426 O O     . HOH T 7 .    ? 30.504  30.758  80.380  1.00 27.94 ?  2284 HOH B O     1 
HETATM 20427 O O     . HOH T 7 .    ? 12.363  43.768  54.405  1.00 24.18 ?  2285 HOH B O     1 
HETATM 20428 O O     . HOH T 7 .    ? 24.333  32.541  116.927 1.00 30.84 ?  2286 HOH B O     1 
HETATM 20429 O O     . HOH T 7 .    ? 4.934   31.534  93.926  1.00 27.20 ?  2287 HOH B O     1 
HETATM 20430 O O     . HOH T 7 .    ? -8.181  37.576  80.374  1.00 30.79 ?  2288 HOH B O     1 
HETATM 20431 O O     . HOH T 7 .    ? -35.449 14.257  119.012 1.00 40.00 ?  2289 HOH B O     1 
HETATM 20432 O O     . HOH T 7 .    ? 29.435  30.986  82.865  1.00 21.63 ?  2290 HOH B O     1 
HETATM 20433 O O     . HOH T 7 .    ? 16.013  69.647  56.147  1.00 36.71 ?  2291 HOH B O     1 
HETATM 20434 O O     . HOH T 7 .    ? 0.879   31.284  83.628  1.00 22.78 ?  2292 HOH B O     1 
HETATM 20435 O O     . HOH T 7 .    ? -14.645 2.335   91.028  1.00 41.39 ?  2293 HOH B O     1 
HETATM 20436 O O     . HOH T 7 .    ? -1.243  14.878  84.501  1.00 21.13 ?  2294 HOH B O     1 
HETATM 20437 O O     . HOH T 7 .    ? 34.727  27.005  61.680  1.00 29.99 ?  2295 HOH B O     1 
HETATM 20438 O O     . HOH T 7 .    ? -15.385 6.929   126.081 1.00 34.02 ?  2296 HOH B O     1 
HETATM 20439 O O     . HOH T 7 .    ? 10.690  0.393   108.428 1.00 35.62 ?  2297 HOH B O     1 
HETATM 20440 O O     . HOH T 7 .    ? 13.351  36.243  78.000  1.00 17.72 ?  2298 HOH B O     1 
HETATM 20441 O O     . HOH T 7 .    ? 18.394  8.796   97.082  1.00 32.95 ?  2299 HOH B O     1 
HETATM 20442 O O     . HOH T 7 .    ? 18.024  2.979   74.037  1.00 39.79 ?  2300 HOH B O     1 
HETATM 20443 O O     . HOH T 7 .    ? 2.147   24.909  103.734 1.00 35.54 ?  2301 HOH B O     1 
HETATM 20444 O O     . HOH T 7 .    ? 5.025   2.816   87.019  1.00 27.54 ?  2302 HOH B O     1 
HETATM 20445 O O     . HOH T 7 .    ? 5.656   29.554  87.379  1.00 23.25 ?  2303 HOH B O     1 
HETATM 20446 O O     . HOH T 7 .    ? -7.427  25.128  75.952  1.00 25.80 ?  2304 HOH B O     1 
HETATM 20447 O O     . HOH T 7 .    ? 15.734  59.694  93.923  1.00 35.95 ?  2305 HOH B O     1 
HETATM 20448 O O     . HOH T 7 .    ? 13.669  36.101  75.111  1.00 15.87 ?  2306 HOH B O     1 
HETATM 20449 O O     . HOH T 7 .    ? 15.073  43.894  53.862  1.00 25.99 ?  2307 HOH B O     1 
HETATM 20450 O O     . HOH T 7 .    ? 13.145  53.991  59.985  1.00 29.26 ?  2308 HOH B O     1 
HETATM 20451 O O     . HOH T 7 .    ? 3.095   12.865  78.271  1.00 32.01 ?  2309 HOH B O     1 
HETATM 20452 O O     . HOH T 7 .    ? 10.186  28.223  89.193  1.00 40.45 ?  2310 HOH B O     1 
HETATM 20453 O O     . HOH T 7 .    ? 9.230   3.299   84.882  1.00 28.41 ?  2311 HOH B O     1 
HETATM 20454 O O     . HOH T 7 .    ? -13.997 16.580  79.574  1.00 34.68 ?  2312 HOH B O     1 
HETATM 20455 O O     . HOH T 7 .    ? 18.398  65.967  56.411  1.00 26.82 ?  2313 HOH B O     1 
HETATM 20456 O O     . HOH T 7 .    ? 4.710   47.530  92.799  1.00 31.98 ?  2314 HOH B O     1 
HETATM 20457 O O     . HOH T 7 .    ? 21.921  19.618  108.340 1.00 25.10 ?  2315 HOH B O     1 
HETATM 20458 O O     . HOH T 7 .    ? 4.790   55.706  67.967  1.00 34.13 ?  2316 HOH B O     1 
HETATM 20459 O O     . HOH T 7 .    ? -36.673 15.947  115.314 1.00 31.41 ?  2317 HOH B O     1 
HETATM 20460 O O     . HOH T 7 .    ? 14.171  51.440  63.827  1.00 22.61 ?  2318 HOH B O     1 
HETATM 20461 O O     . HOH T 7 .    ? -1.830  25.690  102.068 1.00 29.62 ?  2319 HOH B O     1 
HETATM 20462 O O     . HOH T 7 .    ? -8.382  16.562  80.861  1.00 32.47 ?  2320 HOH B O     1 
HETATM 20463 O O     . HOH T 7 .    ? 13.911  24.359  99.540  1.00 32.62 ?  2321 HOH B O     1 
HETATM 20464 O O     . HOH T 7 .    ? 7.395   72.063  61.825  1.00 36.93 ?  2322 HOH B O     1 
HETATM 20465 O O     . HOH T 7 .    ? 8.609   19.690  124.327 1.00 27.76 ?  2323 HOH B O     1 
HETATM 20466 O O     . HOH T 7 .    ? 30.460  23.425  75.395  1.00 26.64 ?  2324 HOH B O     1 
HETATM 20467 O O     . HOH T 7 .    ? 8.611   24.303  87.502  1.00 32.29 ?  2325 HOH B O     1 
HETATM 20468 O O     . HOH T 7 .    ? 11.813  1.336   117.634 1.00 29.18 ?  2326 HOH B O     1 
HETATM 20469 O O     . HOH T 7 .    ? 30.476  64.156  71.923  1.00 32.26 ?  2327 HOH B O     1 
HETATM 20470 O O     . HOH T 7 .    ? 32.415  59.808  63.461  1.00 32.57 ?  2328 HOH B O     1 
HETATM 20471 O O     . HOH T 7 .    ? 6.726   60.838  86.239  1.00 20.79 ?  2329 HOH B O     1 
HETATM 20472 O O     . HOH T 7 .    ? -21.075 15.795  81.033  1.00 35.73 ?  2330 HOH B O     1 
HETATM 20473 O O     . HOH T 7 .    ? 3.242   49.604  93.662  1.00 36.01 ?  2331 HOH B O     1 
HETATM 20474 O O     . HOH T 7 .    ? 18.701  78.884  66.105  1.00 35.41 ?  2332 HOH B O     1 
HETATM 20475 O O     . HOH T 7 .    ? 2.222   21.675  61.852  1.00 26.43 ?  2333 HOH B O     1 
HETATM 20476 O O     . HOH T 7 .    ? 12.840  74.730  61.669  1.00 32.62 ?  2334 HOH B O     1 
HETATM 20477 O O     . HOH T 7 .    ? 9.913   28.198  85.965  1.00 30.00 ?  2335 HOH B O     1 
HETATM 20478 O O     . HOH T 7 .    ? 3.338   47.747  90.359  1.00 27.64 ?  2336 HOH B O     1 
HETATM 20479 O O     . HOH T 7 .    ? -7.910  36.741  84.675  1.00 29.82 ?  2337 HOH B O     1 
HETATM 20480 O O     . HOH T 7 .    ? -12.579 -0.984  122.964 1.00 34.52 ?  2338 HOH B O     1 
HETATM 20481 O O     . HOH T 7 .    ? 25.531  52.646  85.466  1.00 37.47 ?  2339 HOH B O     1 
HETATM 20482 O O     . HOH T 7 .    ? -25.391 12.187  87.461  1.00 31.52 ?  2340 HOH B O     1 
HETATM 20483 O O     . HOH T 7 .    ? 12.868  0.241   110.466 1.00 33.34 ?  2341 HOH B O     1 
HETATM 20484 O O     . HOH T 7 .    ? -3.143  37.456  78.805  1.00 24.99 ?  2342 HOH B O     1 
HETATM 20485 O O     . HOH T 7 .    ? -11.697 1.353   90.060  1.00 29.18 ?  2343 HOH B O     1 
HETATM 20486 O O     . HOH T 7 .    ? -16.282 7.069   92.019  1.00 27.51 ?  2344 HOH B O     1 
HETATM 20487 O O     . HOH T 7 .    ? -8.710  33.368  86.142  1.00 27.28 ?  2345 HOH B O     1 
HETATM 20488 O O     . HOH T 7 .    ? -11.296 46.993  78.194  1.00 29.89 ?  2346 HOH B O     1 
HETATM 20489 O O     . HOH T 7 .    ? -9.646  26.978  114.744 1.00 35.26 ?  2347 HOH B O     1 
HETATM 20490 O O     . HOH T 7 .    ? 8.938   44.531  51.211  1.00 36.36 ?  2348 HOH B O     1 
HETATM 20491 O O     . HOH T 7 .    ? 1.764   44.528  98.227  1.00 27.91 ?  2349 HOH B O     1 
HETATM 20492 O O     . HOH T 7 .    ? -5.228  14.090  82.178  1.00 32.48 ?  2350 HOH B O     1 
HETATM 20493 O O     . HOH T 7 .    ? 6.782   23.369  125.716 1.00 28.24 ?  2351 HOH B O     1 
HETATM 20494 O O     . HOH T 7 .    ? 15.385  38.062  78.096  1.00 16.79 ?  2352 HOH B O     1 
HETATM 20495 O O     . HOH T 7 .    ? 4.674   64.101  87.777  1.00 27.91 ?  2353 HOH B O     1 
HETATM 20496 O O     . HOH T 7 .    ? -8.448  35.110  88.453  1.00 34.62 ?  2354 HOH B O     1 
HETATM 20497 O O     . HOH T 7 .    ? -21.940 4.685   88.547  1.00 40.86 ?  2355 HOH B O     1 
HETATM 20498 O O     . HOH T 7 .    ? -0.392  28.646  97.756  1.00 20.82 ?  2356 HOH B O     1 
HETATM 20499 O O     . HOH T 7 .    ? 5.580   31.675  53.146  1.00 30.25 ?  2357 HOH B O     1 
HETATM 20500 O O     . HOH T 7 .    ? 28.796  35.834  70.916  1.00 33.92 ?  2358 HOH B O     1 
HETATM 20501 O O     . HOH T 7 .    ? -23.645 13.524  83.309  1.00 31.71 ?  2359 HOH B O     1 
HETATM 20502 O O     . HOH T 7 .    ? 0.480   19.752  65.043  1.00 29.67 ?  2360 HOH B O     1 
HETATM 20503 O O     . HOH T 7 .    ? 34.447  48.031  69.703  1.00 35.25 ?  2361 HOH B O     1 
HETATM 20504 O O     . HOH T 7 .    ? 31.277  73.676  71.006  1.00 34.85 ?  2362 HOH B O     1 
HETATM 20505 O O     . HOH T 7 .    ? 6.620   11.315  73.727  1.00 34.88 ?  2363 HOH B O     1 
HETATM 20506 O O     . HOH T 7 .    ? -18.745 21.595  81.668  1.00 35.04 ?  2364 HOH B O     1 
HETATM 20507 O O     . HOH T 7 .    ? -1.472  22.983  64.417  1.00 24.37 ?  2365 HOH B O     1 
HETATM 20508 O O     . HOH T 7 .    ? -11.133 3.027   87.935  1.00 31.29 ?  2366 HOH B O     1 
HETATM 20509 O O     . HOH T 7 .    ? 7.782   68.857  88.480  1.00 33.08 ?  2367 HOH B O     1 
HETATM 20510 O O     . HOH T 7 .    ? -9.852  34.489  91.423  1.00 35.09 ?  2368 HOH B O     1 
HETATM 20511 O O     . HOH T 7 .    ? 34.170  47.754  73.974  1.00 31.47 ?  2369 HOH B O     1 
HETATM 20512 O O     . HOH T 7 .    ? 2.068   31.640  86.027  1.00 22.78 ?  2370 HOH B O     1 
HETATM 20513 O O     . HOH T 7 .    ? 7.408   45.886  53.380  1.00 36.42 ?  2371 HOH B O     1 
HETATM 20514 O O     . HOH T 7 .    ? 32.345  24.979  51.267  1.00 37.62 ?  2372 HOH B O     1 
HETATM 20515 O O     . HOH T 7 .    ? 28.688  33.452  81.961  1.00 27.95 ?  2373 HOH B O     1 
HETATM 20516 O O     . HOH T 7 .    ? 10.048  16.878  90.728  1.00 26.18 ?  2374 HOH B O     1 
HETATM 20517 O O     . HOH T 7 .    ? -5.191  23.362  75.829  1.00 25.80 ?  2375 HOH B O     1 
HETATM 20518 O O     . HOH T 7 .    ? -2.617  23.263  62.014  1.00 32.81 ?  2376 HOH B O     1 
HETATM 20519 O O     . HOH T 7 .    ? 31.502  67.780  70.839  1.00 37.08 ?  2377 HOH B O     1 
HETATM 20520 O O     . HOH T 7 .    ? 22.279  31.130  45.918  1.00 33.21 ?  2378 HOH B O     1 
HETATM 20521 O O     . HOH T 7 .    ? 11.006  60.132  93.644  1.00 30.55 ?  2379 HOH B O     1 
HETATM 20522 O O     . HOH T 7 .    ? 22.840  28.965  44.669  1.00 39.89 ?  2380 HOH B O     1 
HETATM 20523 O O     . HOH T 7 .    ? 34.706  50.967  68.687  1.00 31.99 ?  2381 HOH B O     1 
HETATM 20524 O O     . HOH T 7 .    ? -24.969 11.898  85.019  1.00 36.14 ?  2382 HOH B O     1 
HETATM 20525 O O     . HOH T 7 .    ? 7.035   1.544   85.265  1.00 30.48 ?  2383 HOH B O     1 
HETATM 20526 O O     . HOH T 7 .    ? -5.628  21.080  77.480  1.00 36.33 ?  2384 HOH B O     1 
HETATM 20527 O O     . HOH T 7 .    ? 19.454  31.512  46.094  1.00 35.05 ?  2385 HOH B O     1 
HETATM 20528 O O     . HOH T 7 .    ? 20.539  27.548  44.205  1.00 30.28 ?  2386 HOH B O     1 
HETATM 20529 O O     . HOH T 7 .    ? -16.143 4.953   90.191  1.00 39.22 ?  2387 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . PRO A 17   ? 0.5274 0.5496 0.5682 0.1138  0.0078  -0.0818 15   PRO A N   
2     C CA  . PRO A 17   ? 0.4522 0.4827 0.4891 0.1129  0.0132  -0.0761 15   PRO A CA  
3     C C   . PRO A 17   ? 0.4355 0.4761 0.4640 0.1133  0.0169  -0.0765 15   PRO A C   
4     O O   . PRO A 17   ? 0.4155 0.4523 0.4398 0.1122  0.0154  -0.0783 15   PRO A O   
5     C CB  . PRO A 17   ? 0.5038 0.5244 0.5415 0.1090  0.0123  -0.0702 15   PRO A CB  
6     C CG  . PRO A 17   ? 0.4840 0.4919 0.5284 0.1081  0.0066  -0.0721 15   PRO A CG  
7     C CD  . PRO A 17   ? 0.4696 0.4777 0.5138 0.1105  0.0039  -0.0793 15   PRO A CD  
8     N N   . ALA A 18   ? 0.3858 0.4392 0.4119 0.1145  0.0215  -0.0745 16   ALA A N   
9     C CA  . ALA A 18   ? 0.3846 0.4487 0.4030 0.1147  0.0249  -0.0743 16   ALA A CA  
10    C C   . ALA A 18   ? 0.3701 0.4307 0.3832 0.1113  0.0264  -0.0692 16   ALA A C   
11    O O   . ALA A 18   ? 0.3628 0.4178 0.3774 0.1084  0.0270  -0.0635 16   ALA A O   
12    C CB  . ALA A 18   ? 0.3977 0.4760 0.4153 0.1159  0.0295  -0.0715 16   ALA A CB  
13    N N   . PRO A 19   ? 0.3390 0.4024 0.3456 0.1110  0.0267  -0.0709 17   PRO A N   
14    C CA  . PRO A 19   ? 0.3469 0.4066 0.3484 0.1078  0.0280  -0.0662 17   PRO A CA  
15    C C   . PRO A 19   ? 0.3293 0.3958 0.3287 0.1044  0.0327  -0.0575 17   PRO A C   
16    O O   . PRO A 19   ? 0.3258 0.4057 0.3233 0.1067  0.0365  -0.0566 17   PRO A O   
17    C CB  . PRO A 19   ? 0.3260 0.3900 0.3214 0.1086  0.0275  -0.0700 17   PRO A CB  
18    C CG  . PRO A 19   ? 0.3893 0.4536 0.3880 0.1120  0.0240  -0.0778 17   PRO A CG  
19    C CD  . PRO A 19   ? 0.3346 0.4035 0.3387 0.1138  0.0253  -0.0775 17   PRO A CD  
20    N N   . PHE A 20   ? 0.3200 0.3769 0.3202 0.0985  0.0322  -0.0507 18   PHE A N   
21    C CA  . PHE A 20   ? 0.2973 0.3573 0.2957 0.0937  0.0357  -0.0418 18   PHE A CA  
22    C C   . PHE A 20   ? 0.2935 0.3607 0.2962 0.0943  0.0383  -0.0388 18   PHE A C   
23    O O   . PHE A 20   ? 0.3149 0.3872 0.3163 0.0910  0.0415  -0.0319 18   PHE A O   
24    C CB  . PHE A 20   ? 0.2839 0.3525 0.2753 0.0931  0.0387  -0.0395 18   PHE A CB  
25    C CG  . PHE A 20   ? 0.2725 0.3345 0.2595 0.0920  0.0364  -0.0416 18   PHE A CG  
26    C CD1 . PHE A 20   ? 0.2703 0.3213 0.2568 0.0867  0.0350  -0.0371 18   PHE A CD1 
27    C CD2 . PHE A 20   ? 0.2759 0.3431 0.2593 0.0965  0.0357  -0.0484 18   PHE A CD2 
28    C CE1 . PHE A 20   ? 0.2858 0.3312 0.2685 0.0857  0.0329  -0.0390 18   PHE A CE1 
29    C CE2 . PHE A 20   ? 0.3119 0.3733 0.2913 0.0955  0.0335  -0.0504 18   PHE A CE2 
30    C CZ  . PHE A 20   ? 0.2691 0.3196 0.2484 0.0901  0.0321  -0.0456 18   PHE A CZ  
31    N N   . ALA A 21   ? 0.3146 0.3821 0.3227 0.0983  0.0367  -0.0437 19   ALA A N   
32    C CA  . ALA A 21   ? 0.3352 0.4094 0.3477 0.0990  0.0389  -0.0410 19   ALA A CA  
33    C C   . ALA A 21   ? 0.3627 0.4290 0.3786 0.0933  0.0386  -0.0338 19   ALA A C   
34    O O   . ALA A 21   ? 0.3886 0.4607 0.4075 0.0925  0.0409  -0.0297 19   ALA A O   
35    C CB  . ALA A 21   ? 0.3583 0.4342 0.3764 0.1048  0.0369  -0.0484 19   ALA A CB  
36    N N   . ASP A 22   ? 0.2953 0.3489 0.3108 0.0894  0.0357  -0.0321 20   ASP A N   
37    C CA  . ASP A 22   ? 0.3672 0.4133 0.3856 0.0842  0.0351  -0.0258 20   ASP A CA  
38    C C   . ASP A 22   ? 0.2972 0.3370 0.3110 0.0790  0.0350  -0.0215 20   ASP A C   
39    O O   . ASP A 22   ? 0.2828 0.3126 0.2981 0.0752  0.0328  -0.0188 20   ASP A O   
40    C CB  . ASP A 22   ? 0.3971 0.4336 0.4215 0.0848  0.0310  -0.0283 20   ASP A CB  
41    C CG  . ASP A 22   ? 0.5167 0.5590 0.5469 0.0889  0.0312  -0.0308 20   ASP A CG  
42    O OD1 . ASP A 22   ? 0.5648 0.6161 0.5958 0.0886  0.0346  -0.0272 20   ASP A OD1 
43    O OD2 . ASP A 22   ? 0.5671 0.6051 0.6014 0.0924  0.0279  -0.0363 20   ASP A OD2 
44    N N   . PHE A 23   ? 0.2339 0.2799 0.2421 0.0790  0.0374  -0.0206 21   PHE A N   
45    C CA  . PHE A 23   ? 0.2253 0.2653 0.2291 0.0749  0.0370  -0.0176 21   PHE A CA  
46    C C   . PHE A 23   ? 0.2019 0.2374 0.2071 0.0693  0.0376  -0.0104 21   PHE A C   
47    O O   . PHE A 23   ? 0.2102 0.2358 0.2156 0.0659  0.0352  -0.0091 21   PHE A O   
48    C CB  . PHE A 23   ? 0.2245 0.2731 0.2223 0.0760  0.0396  -0.0175 21   PHE A CB  
49    C CG  . PHE A 23   ? 0.2176 0.2608 0.2112 0.0717  0.0394  -0.0138 21   PHE A CG  
50    C CD1 . PHE A 23   ? 0.2252 0.2586 0.2175 0.0709  0.0361  -0.0167 21   PHE A CD1 
51    C CD2 . PHE A 23   ? 0.2442 0.2923 0.2358 0.0686  0.0422  -0.0074 21   PHE A CD2 
52    C CE1 . PHE A 23   ? 0.2348 0.2636 0.2235 0.0672  0.0359  -0.0136 21   PHE A CE1 
53    C CE2 . PHE A 23   ? 0.2481 0.2911 0.2363 0.0649  0.0418  -0.0043 21   PHE A CE2 
54    C CZ  . PHE A 23   ? 0.2315 0.2650 0.2181 0.0643  0.0387  -0.0075 21   PHE A CZ  
55    N N   . ALA A 24   ? 0.2218 0.2651 0.2282 0.0681  0.0407  -0.0057 22   ALA A N   
56    C CA  . ALA A 24   ? 0.2219 0.2614 0.2298 0.0628  0.0411  0.0008  22   ALA A CA  
57    C C   . ALA A 24   ? 0.2144 0.2621 0.2262 0.0624  0.0437  0.0047  22   ALA A C   
58    O O   . ALA A 24   ? 0.2062 0.2581 0.2171 0.0596  0.0459  0.0100  22   ALA A O   
59    C CB  . ALA A 24   ? 0.2729 0.3116 0.2762 0.0596  0.0421  0.0043  22   ALA A CB  
60    N N   . PRO A 25   ? 0.2440 0.2936 0.2603 0.0651  0.0432  0.0024  23   PRO A N   
61    C CA  . PRO A 25   ? 0.2169 0.2748 0.2372 0.0648  0.0456  0.0061  23   PRO A CA  
62    C C   . PRO A 25   ? 0.2103 0.2635 0.2330 0.0594  0.0454  0.0121  23   PRO A C   
63    O O   . PRO A 25   ? 0.2416 0.2847 0.2650 0.0569  0.0426  0.0121  23   PRO A O   
64    C CB  . PRO A 25   ? 0.2315 0.2899 0.2565 0.0688  0.0442  0.0016  23   PRO A CB  
65    C CG  . PRO A 25   ? 0.2564 0.3027 0.2814 0.0686  0.0402  -0.0018 23   PRO A CG  
66    C CD  . PRO A 25   ? 0.2296 0.2728 0.2486 0.0678  0.0399  -0.0030 23   PRO A CD  
67    N N   . PRO A 26   ? 0.2178 0.2783 0.2417 0.0573  0.0480  0.0173  24   PRO A N   
68    C CA  . PRO A 26   ? 0.2181 0.2743 0.2446 0.0522  0.0476  0.0227  24   PRO A CA  
69    C C   . PRO A 26   ? 0.2513 0.3045 0.2833 0.0519  0.0459  0.0225  24   PRO A C   
70    O O   . PRO A 26   ? 0.2291 0.2860 0.2638 0.0556  0.0459  0.0194  24   PRO A O   
71    C CB  . PRO A 26   ? 0.2248 0.2910 0.2522 0.0507  0.0508  0.0279  24   PRO A CB  
72    C CG  . PRO A 26   ? 0.2459 0.3231 0.2731 0.0556  0.0530  0.0253  24   PRO A CG  
73    C CD  . PRO A 26   ? 0.2599 0.3334 0.2832 0.0595  0.0515  0.0186  24   PRO A CD  
74    N N   . VAL A 27   ? 0.2100 0.2568 0.2436 0.0474  0.0445  0.0258  25   VAL A N   
75    C CA  . VAL A 27   ? 0.2414 0.2853 0.2800 0.0465  0.0427  0.0263  25   VAL A CA  
76    C C   . VAL A 27   ? 0.2331 0.2867 0.2766 0.0479  0.0447  0.0280  25   VAL A C   
77    O O   . VAL A 27   ? 0.2764 0.3305 0.3238 0.0499  0.0437  0.0263  25   VAL A O   
78    C CB  . VAL A 27   ? 0.2421 0.2793 0.2813 0.0413  0.0412  0.0298  25   VAL A CB  
79    C CG1 . VAL A 27   ? 0.2747 0.3112 0.3193 0.0400  0.0398  0.0313  25   VAL A CG1 
80    C CG2 . VAL A 27   ? 0.2483 0.2760 0.2834 0.0403  0.0389  0.0276  25   VAL A CG2 
81    N N   . ARG A 28   ? 0.2867 0.3483 0.3302 0.0468  0.0476  0.0317  26   ARG A N   
82    C CA  . ARG A 28   ? 0.2479 0.3201 0.2961 0.0479  0.0498  0.0340  26   ARG A CA  
83    C C   . ARG A 28   ? 0.3079 0.3897 0.3538 0.0487  0.0531  0.0361  26   ARG A C   
84    O O   . ARG A 28   ? 0.2624 0.3418 0.3039 0.0471  0.0534  0.0371  26   ARG A O   
85    C CB  . ARG A 28   ? 0.2879 0.3592 0.3411 0.0436  0.0492  0.0387  26   ARG A CB  
86    C CG  . ARG A 28   ? 0.2642 0.3343 0.3166 0.0389  0.0498  0.0436  26   ARG A CG  
87    C CD  . ARG A 28   ? 0.3114 0.3794 0.3690 0.0347  0.0485  0.0473  26   ARG A CD  
88    N NE  . ARG A 28   ? 0.3098 0.3672 0.3666 0.0329  0.0453  0.0454  26   ARG A NE  
89    C CZ  . ARG A 28   ? 0.3389 0.3935 0.3981 0.0339  0.0434  0.0433  26   ARG A CZ  
90    N NH1 . ARG A 28   ? 0.3622 0.4232 0.4253 0.0367  0.0441  0.0426  26   ARG A NH1 
91    N NH2 . ARG A 28   ? 0.3400 0.3855 0.3978 0.0321  0.0405  0.0420  26   ARG A NH2 
92    N N   . PRO A 29   ? 0.2638 0.3573 0.3125 0.0512  0.0556  0.0368  27   PRO A N   
93    C CA  . PRO A 29   ? 0.2642 0.3681 0.3111 0.0513  0.0588  0.0400  27   PRO A CA  
94    C C   . PRO A 29   ? 0.2385 0.3408 0.2867 0.0457  0.0590  0.0467  27   PRO A C   
95    O O   . PRO A 29   ? 0.2779 0.3766 0.3307 0.0423  0.0578  0.0496  27   PRO A O   
96    C CB  . PRO A 29   ? 0.2911 0.4077 0.3423 0.0544  0.0612  0.0402  27   PRO A CB  
97    C CG  . PRO A 29   ? 0.3092 0.4216 0.3622 0.0581  0.0591  0.0343  27   PRO A CG  
98    C CD  . PRO A 29   ? 0.2895 0.3878 0.3429 0.0546  0.0556  0.0343  27   PRO A CD  
99    N N   . GLN A 30   ? 0.2745 0.3795 0.3188 0.0448  0.0605  0.0491  28   GLN A N   
100   C CA  . GLN A 30   ? 0.2636 0.3658 0.3090 0.0396  0.0602  0.0551  28   GLN A CA  
101   C C   . GLN A 30   ? 0.2338 0.3469 0.2847 0.0377  0.0625  0.0614  28   GLN A C   
102   O O   . GLN A 30   ? 0.2634 0.3884 0.3136 0.0398  0.0654  0.0631  28   GLN A O   
103   C CB  . GLN A 30   ? 0.2499 0.3502 0.2893 0.0394  0.0605  0.0552  28   GLN A CB  
104   C CG  . GLN A 30   ? 0.2089 0.2991 0.2429 0.0415  0.0582  0.0489  28   GLN A CG  
105   C CD  . GLN A 30   ? 0.2216 0.2989 0.2568 0.0381  0.0551  0.0484  28   GLN A CD  
106   O OE1 . GLN A 30   ? 0.2287 0.3007 0.2633 0.0345  0.0541  0.0513  28   GLN A OE1 
107   N NE2 . GLN A 30   ? 0.2259 0.2985 0.2630 0.0394  0.0533  0.0447  28   GLN A NE2 
108   N N   . SER A 31   ? 0.2204 0.3301 0.2771 0.0337  0.0611  0.0650  29   SER A N   
109   C CA  . SER A 31   ? 0.2068 0.3259 0.2696 0.0311  0.0629  0.0715  29   SER A CA  
110   C C   . SER A 31   ? 0.2129 0.3352 0.2747 0.0283  0.0640  0.0773  29   SER A C   
111   O O   . SER A 31   ? 0.2284 0.3443 0.2852 0.0279  0.0631  0.0762  29   SER A O   
112   C CB  . SER A 31   ? 0.1964 0.3098 0.2656 0.0271  0.0606  0.0736  29   SER A CB  
113   O OG  . SER A 31   ? 0.1898 0.2926 0.2581 0.0233  0.0582  0.0749  29   SER A OG  
114   N N   . THR A 32   ? 0.1927 0.3253 0.2599 0.0263  0.0658  0.0837  30   THR A N   
115   C CA  . THR A 32   ? 0.1947 0.3306 0.2626 0.0230  0.0666  0.0904  30   THR A CA  
116   C C   . THR A 32   ? 0.2009 0.3236 0.2696 0.0188  0.0634  0.0915  30   THR A C   
117   O O   . THR A 32   ? 0.2011 0.3208 0.2662 0.0178  0.0631  0.0930  30   THR A O   
118   C CB  . THR A 32   ? 0.1989 0.3463 0.2737 0.0208  0.0681  0.0972  30   THR A CB  
119   O OG1 . THR A 32   ? 0.2863 0.4452 0.3592 0.0251  0.0704  0.0949  30   THR A OG1 
120   C CG2 . THR A 32   ? 0.2423 0.3900 0.3169 0.0174  0.0668  0.1028  30   THR A CG2 
121   N N   . LEU A 33   ? 0.1911 0.3059 0.2642 0.0164  0.0608  0.0904  31   LEU A N   
122   C CA  . LEU A 33   ? 0.1703 0.2730 0.2443 0.0126  0.0577  0.0907  31   LEU A CA  
123   C C   . LEU A 33   ? 0.2102 0.3033 0.2765 0.0146  0.0564  0.0849  31   LEU A C   
124   O O   . LEU A 33   ? 0.1774 0.2641 0.2421 0.0126  0.0550  0.0860  31   LEU A O   
125   C CB  . LEU A 33   ? 0.1836 0.2812 0.2636 0.0102  0.0553  0.0901  31   LEU A CB  
126   C CG  . LEU A 33   ? 0.1927 0.2975 0.2815 0.0067  0.0557  0.0967  31   LEU A CG  
127   C CD1 . LEU A 33   ? 0.2153 0.3173 0.3096 0.0054  0.0537  0.0951  31   LEU A CD1 
128   C CD2 . LEU A 33   ? 0.2425 0.3441 0.3344 0.0025  0.0543  0.1021  31   LEU A CD2 
129   N N   . ARG A 34   ? 0.1571 0.2492 0.2191 0.0186  0.0567  0.0788  32   ARG A N   
130   C CA  . ARG A 34   ? 0.1539 0.2371 0.2090 0.0204  0.0553  0.0735  32   ARG A CA  
131   C C   . ARG A 34   ? 0.1699 0.2569 0.2197 0.0219  0.0570  0.0745  32   ARG A C   
132   O O   . ARG A 34   ? 0.1970 0.2763 0.2427 0.0212  0.0556  0.0731  32   ARG A O   
133   C CB  . ARG A 34   ? 0.1998 0.2813 0.2523 0.0243  0.0551  0.0671  32   ARG A CB  
134   C CG  . ARG A 34   ? 0.1865 0.2616 0.2429 0.0228  0.0526  0.0654  32   ARG A CG  
135   C CD  . ARG A 34   ? 0.1987 0.2615 0.2531 0.0204  0.0496  0.0633  32   ARG A CD  
136   N NE  . ARG A 34   ? 0.2141 0.2711 0.2618 0.0230  0.0490  0.0584  32   ARG A NE  
137   C CZ  . ARG A 34   ? 0.2294 0.2819 0.2755 0.0251  0.0476  0.0537  32   ARG A CZ  
138   N NH1 . ARG A 34   ? 0.2279 0.2811 0.2780 0.0253  0.0468  0.0530  32   ARG A NH1 
139   N NH2 . ARG A 34   ? 0.2553 0.3023 0.2957 0.0269  0.0468  0.0497  32   ARG A NH2 
140   N N   . ARG A 35   ? 0.1683 0.2676 0.2180 0.0238  0.0600  0.0771  33   ARG A N   
141   C CA  . ARG A 35   ? 0.1854 0.2894 0.2299 0.0253  0.0616  0.0782  33   ARG A CA  
142   C C   . ARG A 35   ? 0.1714 0.2732 0.2177 0.0211  0.0608  0.0844  33   ARG A C   
143   O O   . ARG A 35   ? 0.1855 0.2852 0.2269 0.0215  0.0606  0.0842  33   ARG A O   
144   C CB  . ARG A 35   ? 0.2071 0.3261 0.2512 0.0285  0.0650  0.0795  33   ARG A CB  
145   C CG  . ARG A 35   ? 0.2178 0.3384 0.2589 0.0336  0.0655  0.0723  33   ARG A CG  
146   C CD  . ARG A 35   ? 0.2765 0.4127 0.3182 0.0370  0.0689  0.0730  33   ARG A CD  
147   N NE  . ARG A 35   ? 0.3466 0.4828 0.3860 0.0421  0.0688  0.0653  33   ARG A NE  
148   C CZ  . ARG A 35   ? 0.4083 0.5442 0.4414 0.0462  0.0689  0.0596  33   ARG A CZ  
149   N NH1 . ARG A 35   ? 0.4749 0.6120 0.5028 0.0461  0.0694  0.0606  33   ARG A NH1 
150   N NH2 . ARG A 35   ? 0.4520 0.5862 0.4842 0.0504  0.0682  0.0525  33   ARG A NH2 
151   N N   . ALA A 36   ? 0.1635 0.2658 0.2171 0.0171  0.0601  0.0898  34   ALA A N   
152   C CA  . ALA A 36   ? 0.1940 0.2931 0.2505 0.0130  0.0588  0.0955  34   ALA A CA  
153   C C   . ALA A 36   ? 0.2042 0.2895 0.2583 0.0117  0.0557  0.0919  34   ALA A C   
154   O O   . ALA A 36   ? 0.1954 0.2776 0.2484 0.0100  0.0548  0.0945  34   ALA A O   
155   C CB  . ALA A 36   ? 0.2022 0.3041 0.2681 0.0089  0.0582  0.1016  34   ALA A CB  
156   N N   . ILE A 37   ? 0.1479 0.2252 0.2012 0.0124  0.0540  0.0861  35   ILE A N   
157   C CA  . ILE A 37   ? 0.1591 0.2243 0.2093 0.0117  0.0513  0.0820  35   ILE A CA  
158   C C   . ILE A 37   ? 0.1780 0.2424 0.2203 0.0146  0.0520  0.0790  35   ILE A C   
159   O O   . ILE A 37   ? 0.1742 0.2338 0.2146 0.0133  0.0509  0.0800  35   ILE A O   
160   C CB  . ILE A 37   ? 0.1454 0.2040 0.1961 0.0122  0.0496  0.0767  35   ILE A CB  
161   C CG1 . ILE A 37   ? 0.1445 0.2029 0.2031 0.0089  0.0484  0.0796  35   ILE A CG1 
162   C CG2 . ILE A 37   ? 0.1556 0.2031 0.2021 0.0120  0.0472  0.0722  35   ILE A CG2 
163   C CD1 . ILE A 37   ? 0.1631 0.2178 0.2223 0.0098  0.0472  0.0750  35   ILE A CD1 
164   N N   . THR A 38   ? 0.1846 0.2538 0.2225 0.0187  0.0538  0.0751  36   THR A N   
165   C CA  . THR A 38   ? 0.1788 0.2468 0.2092 0.0216  0.0541  0.0714  36   THR A CA  
166   C C   . THR A 38   ? 0.1843 0.2582 0.2130 0.0211  0.0554  0.0763  36   THR A C   
167   O O   . THR A 38   ? 0.1692 0.2388 0.1933 0.0215  0.0546  0.0749  36   THR A O   
168   C CB  . THR A 38   ? 0.1576 0.2309 0.1847 0.0262  0.0557  0.0665  36   THR A CB  
169   O OG1 . THR A 38   ? 0.1760 0.2445 0.2055 0.0265  0.0544  0.0630  36   THR A OG1 
170   C CG2 . THR A 38   ? 0.1991 0.2699 0.2188 0.0293  0.0555  0.0618  36   THR A CG2 
171   N N   . ALA A 39   ? 0.1778 0.2619 0.2106 0.0200  0.0574  0.0823  37   ALA A N   
172   C CA  . ALA A 39   ? 0.1924 0.2833 0.2240 0.0194  0.0587  0.0879  37   ALA A CA  
173   C C   . ALA A 39   ? 0.2169 0.2996 0.2503 0.0158  0.0563  0.0911  37   ALA A C   
174   O O   . ALA A 39   ? 0.2140 0.2994 0.2445 0.0158  0.0566  0.0940  37   ALA A O   
175   C CB  . ALA A 39   ? 0.1987 0.3023 0.2355 0.0184  0.0611  0.0946  37   ALA A CB  
176   N N   . ALA A 40   ? 0.1873 0.2604 0.2253 0.0128  0.0537  0.0906  38   ALA A N   
177   C CA  . ALA A 40   ? 0.1919 0.2571 0.2325 0.0095  0.0512  0.0932  38   ALA A CA  
178   C C   . ALA A 40   ? 0.1782 0.2328 0.2137 0.0104  0.0491  0.0874  38   ALA A C   
179   O O   . ALA A 40   ? 0.1833 0.2313 0.2208 0.0080  0.0470  0.0888  38   ALA A O   
180   C CB  . ALA A 40   ? 0.1814 0.2427 0.2307 0.0057  0.0493  0.0959  38   ALA A CB  
181   N N   . TYR A 41   ? 0.1670 0.2201 0.1966 0.0137  0.0497  0.0809  39   TYR A N   
182   C CA  . TYR A 41   ? 0.1631 0.2060 0.1887 0.0144  0.0476  0.0750  39   TYR A CA  
183   C C   . TYR A 41   ? 0.1780 0.2168 0.2017 0.0133  0.0463  0.0766  39   TYR A C   
184   O O   . TYR A 41   ? 0.1813 0.2113 0.2065 0.0113  0.0438  0.0753  39   TYR A O   
185   C CB  . TYR A 41   ? 0.1674 0.2117 0.1868 0.0184  0.0487  0.0691  39   TYR A CB  
186   C CG  . TYR A 41   ? 0.1585 0.1933 0.1752 0.0192  0.0466  0.0627  39   TYR A CG  
187   C CD1 . TYR A 41   ? 0.1859 0.2118 0.2023 0.0172  0.0443  0.0615  39   TYR A CD1 
188   C CD2 . TYR A 41   ? 0.1660 0.2013 0.1804 0.0220  0.0471  0.0578  39   TYR A CD2 
189   C CE1 . TYR A 41   ? 0.1745 0.1928 0.1884 0.0178  0.0426  0.0561  39   TYR A CE1 
190   C CE2 . TYR A 41   ? 0.1686 0.1957 0.1808 0.0226  0.0451  0.0526  39   TYR A CE2 
191   C CZ  . TYR A 41   ? 0.1611 0.1801 0.1730 0.0204  0.0430  0.0520  39   TYR A CZ  
192   O OH  . TYR A 41   ? 0.1871 0.1989 0.1969 0.0207  0.0412  0.0473  39   TYR A OH  
193   N N   . ARG A 42   ? 0.1977 0.2432 0.2180 0.0146  0.0479  0.0793  40   ARG A N   
194   C CA  . ARG A 42   ? 0.1989 0.2413 0.2171 0.0140  0.0467  0.0809  40   ARG A CA  
195   C C   . ARG A 42   ? 0.2009 0.2510 0.2221 0.0124  0.0477  0.0888  40   ARG A C   
196   O O   . ARG A 42   ? 0.2450 0.2978 0.2626 0.0132  0.0479  0.0908  40   ARG A O   
197   C CB  . ARG A 42   ? 0.2284 0.2703 0.2385 0.0173  0.0470  0.0757  40   ARG A CB  
198   C CG  . ARG A 42   ? 0.2141 0.2467 0.2221 0.0181  0.0454  0.0686  40   ARG A CG  
199   C CD  . ARG A 42   ? 0.2598 0.2922 0.2606 0.0215  0.0456  0.0632  40   ARG A CD  
200   N NE  . ARG A 42   ? 0.2345 0.2608 0.2346 0.0223  0.0446  0.0573  40   ARG A NE  
201   C CZ  . ARG A 42   ? 0.2116 0.2287 0.2120 0.0209  0.0423  0.0545  40   ARG A CZ  
202   N NH1 . ARG A 42   ? 0.2201 0.2326 0.2212 0.0189  0.0408  0.0561  40   ARG A NH1 
203   N NH2 . ARG A 42   ? 0.2014 0.2143 0.2018 0.0215  0.0415  0.0502  40   ARG A NH2 
204   N N   . ARG A 43   ? 0.1961 0.2498 0.2242 0.0100  0.0480  0.0937  41   ARG A N   
205   C CA  . ARG A 43   ? 0.1867 0.2482 0.2189 0.0080  0.0488  0.1022  41   ARG A CA  
206   C C   . ARG A 43   ? 0.2183 0.2733 0.2525 0.0059  0.0458  0.1042  41   ARG A C   
207   O O   . ARG A 43   ? 0.2170 0.2618 0.2539 0.0042  0.0435  0.1024  41   ARG A O   
208   C CB  . ARG A 43   ? 0.1994 0.2633 0.2397 0.0055  0.0482  0.1051  41   ARG A CB  
209   C CG  . ARG A 43   ? 0.1946 0.2640 0.2405 0.0031  0.0467  0.1111  41   ARG A CG  
210   C CD  . ARG A 43   ? 0.2336 0.3074 0.2862 0.0014  0.0469  0.1134  41   ARG A CD  
211   N NE  . ARG A 43   ? 0.2354 0.3179 0.2843 0.0044  0.0503  0.1116  41   ARG A NE  
212   C CZ  . ARG A 43   ? 0.2208 0.3058 0.2734 0.0041  0.0512  0.1112  41   ARG A CZ  
213   N NH1 . ARG A 43   ? 0.2161 0.2956 0.2763 0.0008  0.0489  0.1125  41   ARG A NH1 
214   N NH2 . ARG A 43   ? 0.1978 0.2912 0.2468 0.0072  0.0543  0.1093  41   ARG A NH2 
215   N N   . PRO A 44   ? 0.2169 0.2777 0.2498 0.0060  0.0455  0.1077  42   PRO A N   
216   C CA  . PRO A 44   ? 0.2206 0.2755 0.2558 0.0041  0.0425  0.1097  42   PRO A CA  
217   C C   . PRO A 44   ? 0.2100 0.2579 0.2544 0.0004  0.0393  0.1113  42   PRO A C   
218   O O   . PRO A 44   ? 0.2225 0.2738 0.2728 -0.0012 0.0392  0.1136  42   PRO A O   
219   C CB  . PRO A 44   ? 0.2470 0.3120 0.2814 0.0044  0.0430  0.1144  42   PRO A CB  
220   C CG  . PRO A 44   ? 0.2442 0.3185 0.2717 0.0079  0.0465  0.1124  42   PRO A CG  
221   C CD  . PRO A 44   ? 0.2414 0.3146 0.2704 0.0082  0.0479  0.1096  42   PRO A CD  
222   N N   . GLU A 45   ? 0.2462 0.2844 0.2919 -0.0006 0.0367  0.1096  43   GLU A N   
223   C CA  . GLU A 45   ? 0.2423 0.2733 0.2965 -0.0037 0.0333  0.1099  43   GLU A CA  
224   C C   . GLU A 45   ? 0.2466 0.2824 0.3083 -0.0062 0.0316  0.1158  43   GLU A C   
225   O O   . GLU A 45   ? 0.2444 0.2782 0.3137 -0.0085 0.0298  0.1167  43   GLU A O   
226   C CB  . GLU A 45   ? 0.2689 0.2898 0.3225 -0.0038 0.0308  0.1069  43   GLU A CB  
227   C CG  . GLU A 45   ? 0.2549 0.2667 0.3141 -0.0056 0.0283  0.1035  43   GLU A CG  
228   C CD  . GLU A 45   ? 0.2127 0.2152 0.2690 -0.0046 0.0269  0.0986  43   GLU A CD  
229   O OE1 . GLU A 45   ? 0.2274 0.2300 0.2765 -0.0024 0.0283  0.0973  43   GLU A OE1 
230   O OE2 . GLU A 45   ? 0.2130 0.2085 0.2746 -0.0062 0.0242  0.0961  43   GLU A OE2 
231   N N   . THR A 46   ? 0.2643 0.3069 0.3244 -0.0057 0.0320  0.1200  44   THR A N   
232   C CA  . THR A 46   ? 0.2834 0.3312 0.3509 -0.0081 0.0304  0.1261  44   THR A CA  
233   C C   . THR A 46   ? 0.2941 0.3503 0.3643 -0.0086 0.0322  0.1287  44   THR A C   
234   O O   . THR A 46   ? 0.3230 0.3818 0.4010 -0.0110 0.0304  0.1332  44   THR A O   
235   C CB  . THR A 46   ? 0.2716 0.3256 0.3364 -0.0073 0.0306  0.1302  44   THR A CB  
236   O OG1 . THR A 46   ? 0.2776 0.3394 0.3335 -0.0042 0.0342  0.1290  44   THR A OG1 
237   C CG2 . THR A 46   ? 0.2557 0.3013 0.3201 -0.0075 0.0280  0.1288  44   THR A CG2 
238   N N   . GLU A 47   ? 0.2514 0.3121 0.3156 -0.0062 0.0356  0.1259  45   GLU A N   
239   C CA  . GLU A 47   ? 0.2326 0.3011 0.2994 -0.0064 0.0373  0.1277  45   GLU A CA  
240   C C   . GLU A 47   ? 0.2662 0.3282 0.3380 -0.0080 0.0362  0.1250  45   GLU A C   
241   O O   . GLU A 47   ? 0.2591 0.3255 0.3366 -0.0095 0.0362  0.1277  45   GLU A O   
242   C CB  . GLU A 47   ? 0.2649 0.3418 0.3233 -0.0028 0.0413  0.1257  45   GLU A CB  
243   C CG  . GLU A 47   ? 0.3712 0.4560 0.4240 -0.0009 0.0426  0.1279  45   GLU A CG  
244   C CD  . GLU A 47   ? 0.3683 0.4616 0.4132 0.0029  0.0463  0.1250  45   GLU A CD  
245   O OE1 . GLU A 47   ? 0.3950 0.4901 0.4401 0.0037  0.0481  0.1227  45   GLU A OE1 
246   O OE2 . GLU A 47   ? 0.5330 0.6312 0.5714 0.0052  0.0474  0.1246  45   GLU A OE2 
247   N N   . CYS A 48   ? 0.2240 0.2759 0.2939 -0.0077 0.0353  0.1198  46   CYS A N   
248   C CA  . CYS A 48   ? 0.2200 0.2661 0.2941 -0.0089 0.0344  0.1168  46   CYS A CA  
249   C C   . CYS A 48   ? 0.1708 0.2121 0.2547 -0.0124 0.0305  0.1189  46   CYS A C   
250   O O   . CYS A 48   ? 0.2005 0.2418 0.2900 -0.0139 0.0297  0.1189  46   CYS A O   
251   C CB  . CYS A 48   ? 0.2207 0.2578 0.2899 -0.0075 0.0345  0.1106  46   CYS A CB  
252   S SG  . CYS A 48   ? 0.2405 0.2816 0.2989 -0.0034 0.0388  0.1071  46   CYS A SG  
253   N N   . LEU A 49   ? 0.2328 0.2699 0.3191 -0.0134 0.0278  0.1203  47   LEU A N   
254   C CA  . LEU A 49   ? 0.2419 0.2723 0.3371 -0.0163 0.0237  0.1206  47   LEU A CA  
255   C C   . LEU A 49   ? 0.2280 0.2642 0.3318 -0.0187 0.0223  0.1262  47   LEU A C   
256   O O   . LEU A 49   ? 0.2619 0.2941 0.3728 -0.0208 0.0199  0.1252  47   LEU A O   
257   C CB  . LEU A 49   ? 0.2476 0.2717 0.3433 -0.0165 0.0210  0.1202  47   LEU A CB  
258   C CG  . LEU A 49   ? 0.2566 0.2701 0.3502 -0.0158 0.0196  0.1137  47   LEU A CG  
259   C CD1 . LEU A 49   ? 0.2657 0.2735 0.3664 -0.0177 0.0170  0.1109  47   LEU A CD1 
260   C CD2 . LEU A 49   ? 0.2600 0.2737 0.3439 -0.0130 0.0230  0.1097  47   LEU A CD2 
261   N N   . PRO A 50   ? 0.2554 0.3009 0.3593 -0.0187 0.0236  0.1319  48   PRO A N   
262   C CA  . PRO A 50   ? 0.2911 0.3417 0.4039 -0.0213 0.0218  0.1377  48   PRO A CA  
263   C C   . PRO A 50   ? 0.2567 0.3088 0.3736 -0.0223 0.0222  0.1368  48   PRO A C   
264   O O   . PRO A 50   ? 0.2495 0.2985 0.3753 -0.0249 0.0190  0.1381  48   PRO A O   
265   C CB  . PRO A 50   ? 0.2589 0.3210 0.3686 -0.0203 0.0242  0.1432  48   PRO A CB  
266   C CG  . PRO A 50   ? 0.2657 0.3254 0.3679 -0.0182 0.0250  0.1413  48   PRO A CG  
267   C CD  . PRO A 50   ? 0.2398 0.2912 0.3364 -0.0166 0.0259  0.1338  48   PRO A CD  
268   N N   . PRO A 51   ? 0.2332 0.2898 0.3443 -0.0203 0.0258  0.1346  49   PRO A N   
269   C CA  . PRO A 51   ? 0.2659 0.3237 0.3814 -0.0214 0.0258  0.1339  49   PRO A CA  
270   C C   . PRO A 51   ? 0.2341 0.2811 0.3530 -0.0226 0.0231  0.1287  49   PRO A C   
271   O O   . PRO A 51   ? 0.2855 0.3320 0.4113 -0.0245 0.0215  0.1290  49   PRO A O   
272   C CB  . PRO A 51   ? 0.2541 0.3189 0.3619 -0.0185 0.0303  0.1321  49   PRO A CB  
273   C CG  . PRO A 51   ? 0.2983 0.3612 0.3972 -0.0159 0.0320  0.1295  49   PRO A CG  
274   C CD  . PRO A 51   ? 0.2411 0.3029 0.3421 -0.0170 0.0298  0.1330  49   PRO A CD  
275   N N   . LEU A 52   ? 0.2491 0.2878 0.3635 -0.0215 0.0226  0.1238  50   LEU A N   
276   C CA  . LEU A 52   ? 0.2439 0.2727 0.3618 -0.0226 0.0197  0.1188  50   LEU A CA  
277   C C   . LEU A 52   ? 0.2338 0.2581 0.3611 -0.0253 0.0151  0.1206  50   LEU A C   
278   O O   . LEU A 52   ? 0.2384 0.2589 0.3723 -0.0271 0.0126  0.1188  50   LEU A O   
279   C CB  . LEU A 52   ? 0.2182 0.2400 0.3287 -0.0206 0.0203  0.1134  50   LEU A CB  
280   C CG  . LEU A 52   ? 0.2190 0.2438 0.3204 -0.0178 0.0245  0.1108  50   LEU A CG  
281   C CD1 . LEU A 52   ? 0.2227 0.2406 0.3174 -0.0159 0.0247  0.1062  50   LEU A CD1 
282   C CD2 . LEU A 52   ? 0.2172 0.2426 0.3202 -0.0180 0.0253  0.1085  50   LEU A CD2 
283   N N   . VAL A 53   ? 0.2626 0.2877 0.3910 -0.0256 0.0139  0.1242  51   VAL A N   
284   C CA  . VAL A 53   ? 0.3021 0.3235 0.4401 -0.0280 0.0095  0.1264  51   VAL A CA  
285   C C   . VAL A 53   ? 0.2291 0.2557 0.3754 -0.0303 0.0084  0.1306  51   VAL A C   
286   O O   . VAL A 53   ? 0.2786 0.3004 0.4331 -0.0323 0.0047  0.1295  51   VAL A O   
287   C CB  . VAL A 53   ? 0.2750 0.2980 0.4127 -0.0278 0.0088  0.1305  51   VAL A CB  
288   C CG1 . VAL A 53   ? 0.3189 0.3394 0.4676 -0.0304 0.0041  0.1338  51   VAL A CG1 
289   C CG2 . VAL A 53   ? 0.2752 0.2918 0.4060 -0.0258 0.0091  0.1259  51   VAL A CG2 
290   N N   . GLU A 54   ? 0.2589 0.2956 0.4031 -0.0299 0.0115  0.1353  52   GLU A N   
291   C CA  . GLU A 54   ? 0.2894 0.3318 0.4414 -0.0320 0.0106  0.1396  52   GLU A CA  
292   C C   . GLU A 54   ? 0.3089 0.3475 0.4633 -0.0326 0.0100  0.1351  52   GLU A C   
293   O O   . GLU A 54   ? 0.2915 0.3278 0.4549 -0.0350 0.0066  0.1358  52   GLU A O   
294   C CB  . GLU A 54   ? 0.3172 0.3718 0.4655 -0.0310 0.0144  0.1448  52   GLU A CB  
295   N N   . ALA A 55   ? 0.2620 0.2996 0.4087 -0.0306 0.0129  0.1302  53   ALA A N   
296   C CA  . ALA A 55   ? 0.2730 0.3078 0.4216 -0.0311 0.0125  0.1261  53   ALA A CA  
297   C C   . ALA A 55   ? 0.2531 0.2775 0.4068 -0.0324 0.0082  0.1213  53   ALA A C   
298   O O   . ALA A 55   ? 0.2926 0.3151 0.4518 -0.0339 0.0063  0.1194  53   ALA A O   
299   C CB  . ALA A 55   ? 0.2510 0.2873 0.3903 -0.0284 0.0166  0.1222  53   ALA A CB  
300   N N   . ALA A 56   ? 0.2785 0.2963 0.4305 -0.0319 0.0066  0.1191  54   ALA A N   
301   C CA  . ALA A 56   ? 0.2987 0.3068 0.4548 -0.0326 0.0026  0.1139  54   ALA A CA  
302   C C   . ALA A 56   ? 0.3340 0.3398 0.5007 -0.0350 -0.0020 0.1165  54   ALA A C   
303   O O   . ALA A 56   ? 0.3097 0.3079 0.4809 -0.0356 -0.0058 0.1120  54   ALA A O   
304   C CB  . ALA A 56   ? 0.2558 0.2580 0.4050 -0.0306 0.0031  0.1097  54   ALA A CB  
305   N N   . THR A 57   ? 0.3274 0.3398 0.4984 -0.0362 -0.0021 0.1235  55   THR A N   
306   C CA  . THR A 57   ? 0.3503 0.3607 0.5316 -0.0383 -0.0066 0.1265  55   THR A CA  
307   C C   . THR A 57   ? 0.3152 0.3231 0.5052 -0.0403 -0.0099 0.1246  55   THR A C   
308   O O   . THR A 57   ? 0.3499 0.3621 0.5396 -0.0408 -0.0081 0.1250  55   THR A O   
309   C CB  . THR A 57   ? 0.3567 0.3758 0.5403 -0.0392 -0.0056 0.1350  55   THR A CB  
310   O OG1 . THR A 57   ? 0.3346 0.3554 0.5108 -0.0374 -0.0033 0.1363  55   THR A OG1 
311   C CG2 . THR A 57   ? 0.3605 0.3782 0.5560 -0.0417 -0.0105 0.1389  55   THR A CG2 
312   N N   . GLN A 58   ? 0.3521 0.3529 0.5498 -0.0414 -0.0148 0.1222  56   GLN A N   
313   C CA  . GLN A 58   ? 0.3016 0.2998 0.5088 -0.0434 -0.0187 0.1206  56   GLN A CA  
314   C C   . GLN A 58   ? 0.3677 0.3648 0.5857 -0.0452 -0.0233 0.1247  56   GLN A C   
315   O O   . GLN A 58   ? 0.3744 0.3709 0.5923 -0.0447 -0.0239 0.1273  56   GLN A O   
316   C CB  . GLN A 58   ? 0.3527 0.3428 0.5591 -0.0426 -0.0207 0.1116  56   GLN A CB  
317   C CG  . GLN A 58   ? 0.3544 0.3451 0.5504 -0.0407 -0.0164 0.1073  56   GLN A CG  
318   C CD  . GLN A 58   ? 0.2885 0.2735 0.4855 -0.0407 -0.0184 0.0996  56   GLN A CD  
319   O OE1 . GLN A 58   ? 0.3254 0.3116 0.5277 -0.0422 -0.0199 0.0991  56   GLN A OE1 
320   N NE2 . GLN A 58   ? 0.3381 0.3172 0.5299 -0.0389 -0.0185 0.0935  56   GLN A NE2 
321   N N   . SER A 59   ? 0.3366 0.3334 0.5641 -0.0472 -0.0267 0.1255  57   SER A N   
322   C CA  . SER A 59   ? 0.3539 0.3499 0.5927 -0.0491 -0.0314 0.1298  57   SER A CA  
323   C C   . SER A 59   ? 0.4147 0.4020 0.6568 -0.0483 -0.0354 0.1250  57   SER A C   
324   O O   . SER A 59   ? 0.3697 0.3510 0.6068 -0.0466 -0.0354 0.1174  57   SER A O   
325   C CB  . SER A 59   ? 0.3551 0.3520 0.6036 -0.0514 -0.0344 0.1306  57   SER A CB  
326   O OG  . SER A 59   ? 0.4123 0.4024 0.6619 -0.0510 -0.0367 0.1223  57   SER A OG  
327   N N   . LYS A 60   ? 0.3608 0.3477 0.6117 -0.0496 -0.0391 0.1297  58   LYS A N   
328   C CA  . LYS A 60   ? 0.3634 0.3424 0.6189 -0.0489 -0.0434 0.1254  58   LYS A CA  
329   C C   . LYS A 60   ? 0.3726 0.3447 0.6333 -0.0488 -0.0473 0.1173  58   LYS A C   
330   O O   . LYS A 60   ? 0.3629 0.3283 0.6218 -0.0470 -0.0489 0.1101  58   LYS A O   
331   C CB  . LYS A 60   ? 0.4134 0.3937 0.6790 -0.0505 -0.0471 0.1323  58   LYS A CB  
332   C CG  . LYS A 60   ? 0.4349 0.4075 0.7062 -0.0497 -0.0518 0.1283  58   LYS A CG  
333   C CD  . LYS A 60   ? 0.4738 0.4430 0.7346 -0.0470 -0.0491 0.1233  58   LYS A CD  
334   C CE  . LYS A 60   ? 0.4688 0.4327 0.7347 -0.0463 -0.0530 0.1223  58   LYS A CE  
335   N NZ  . LYS A 60   ? 0.4897 0.4462 0.7647 -0.0461 -0.0587 0.1155  58   LYS A NZ  
336   N N   . GLU A 61   ? 0.3444 0.3183 0.6114 -0.0505 -0.0489 0.1183  59   GLU A N   
337   C CA  . GLU A 61   ? 0.3513 0.3193 0.6235 -0.0505 -0.0528 0.1106  59   GLU A CA  
338   C C   . GLU A 61   ? 0.3987 0.3640 0.6607 -0.0485 -0.0499 0.1024  59   GLU A C   
339   O O   . GLU A 61   ? 0.3557 0.3146 0.6188 -0.0472 -0.0528 0.0944  59   GLU A O   
340   C CB  . GLU A 61   ? 0.3998 0.3712 0.6799 -0.0529 -0.0545 0.1138  59   GLU A CB  
341   N N   . ILE A 62   ? 0.3408 0.3114 0.5932 -0.0481 -0.0444 0.1043  60   ILE A N   
342   C CA  . ILE A 62   ? 0.3417 0.3101 0.5847 -0.0463 -0.0417 0.0972  60   ILE A CA  
343   C C   . ILE A 62   ? 0.3465 0.3102 0.5832 -0.0440 -0.0411 0.0929  60   ILE A C   
344   O O   . ILE A 62   ? 0.3303 0.2889 0.5643 -0.0425 -0.0420 0.0848  60   ILE A O   
345   C CB  . ILE A 62   ? 0.3250 0.3004 0.5598 -0.0464 -0.0360 0.1006  60   ILE A CB  
346   C CG1 . ILE A 62   ? 0.3722 0.3510 0.6128 -0.0483 -0.0370 0.1017  60   ILE A CG1 
347   C CG2 . ILE A 62   ? 0.3349 0.3084 0.5587 -0.0442 -0.0326 0.0946  60   ILE A CG2 
348   C CD1 . ILE A 62   ? 0.3578 0.3431 0.5909 -0.0482 -0.0318 0.1037  60   ILE A CD1 
349   N N   . ARG A 63   ? 0.3221 0.2877 0.5566 -0.0436 -0.0396 0.0982  61   ARG A N   
350   C CA  . ARG A 63   ? 0.3281 0.2893 0.5567 -0.0414 -0.0390 0.0946  61   ARG A CA  
351   C C   . ARG A 63   ? 0.3638 0.3177 0.5996 -0.0407 -0.0444 0.0882  61   ARG A C   
352   O O   . ARG A 63   ? 0.3242 0.2734 0.5551 -0.0387 -0.0445 0.0812  61   ARG A O   
353   C CB  . ARG A 63   ? 0.3359 0.3010 0.5621 -0.0414 -0.0369 0.1019  61   ARG A CB  
354   C CG  . ARG A 63   ? 0.4160 0.3884 0.6332 -0.0412 -0.0311 0.1066  61   ARG A CG  
355   C CD  . ARG A 63   ? 0.4458 0.4222 0.6590 -0.0407 -0.0287 0.1128  61   ARG A CD  
356   N NE  . ARG A 63   ? 0.4384 0.4196 0.6599 -0.0428 -0.0305 0.1209  61   ARG A NE  
357   C CZ  . ARG A 63   ? 0.5181 0.4975 0.7465 -0.0434 -0.0340 0.1237  61   ARG A CZ  
358   N NH1 . ARG A 63   ? 0.5245 0.4972 0.7526 -0.0420 -0.0361 0.1191  61   ARG A NH1 
359   N NH2 . ARG A 63   ? 0.4918 0.4765 0.7279 -0.0455 -0.0354 0.1316  61   ARG A NH2 
360   N N   . ASP A 64   ? 0.3443 0.2972 0.5918 -0.0423 -0.0492 0.0906  62   ASP A N   
361   C CA  . ASP A 64   ? 0.3357 0.2819 0.5908 -0.0415 -0.0547 0.0841  62   ASP A CA  
362   C C   . ASP A 64   ? 0.3282 0.2713 0.5823 -0.0407 -0.0558 0.0752  62   ASP A C   
363   O O   . ASP A 64   ? 0.3322 0.2704 0.5853 -0.0386 -0.0578 0.0673  62   ASP A O   
364   C CB  . ASP A 64   ? 0.3374 0.2836 0.6060 -0.0435 -0.0597 0.0888  62   ASP A CB  
365   C CG  . ASP A 64   ? 0.3742 0.3228 0.6447 -0.0441 -0.0594 0.0968  62   ASP A CG  
366   O OD1 . ASP A 64   ? 0.4152 0.3646 0.6770 -0.0427 -0.0560 0.0977  62   ASP A OD1 
367   O OD2 . ASP A 64   ? 0.4646 0.4146 0.7457 -0.0460 -0.0629 0.1024  62   ASP A OD2 
368   N N   . ALA A 65   ? 0.3141 0.2607 0.5685 -0.0422 -0.0546 0.0762  63   ALA A N   
369   C CA  . ALA A 65   ? 0.3202 0.2645 0.5732 -0.0415 -0.0555 0.0680  63   ALA A CA  
370   C C   . ALA A 65   ? 0.3241 0.2675 0.5653 -0.0394 -0.0517 0.0629  63   ALA A C   
371   O O   . ALA A 65   ? 0.3345 0.2743 0.5746 -0.0379 -0.0534 0.0543  63   ALA A O   
372   C CB  . ALA A 65   ? 0.3058 0.2546 0.5610 -0.0437 -0.0546 0.0710  63   ALA A CB  
373   N N   . ALA A 66   ? 0.2762 0.2232 0.5086 -0.0392 -0.0465 0.0679  64   ALA A N   
374   C CA  . ALA A 66   ? 0.3313 0.2775 0.5525 -0.0372 -0.0428 0.0636  64   ALA A CA  
375   C C   . ALA A 66   ? 0.3650 0.3060 0.5846 -0.0350 -0.0445 0.0585  64   ALA A C   
376   O O   . ALA A 66   ? 0.3196 0.2577 0.5346 -0.0332 -0.0444 0.0510  64   ALA A O   
377   C CB  . ALA A 66   ? 0.3191 0.2707 0.5318 -0.0373 -0.0370 0.0704  64   ALA A CB  
378   N N   . ALA A 67   ? 0.3212 0.2613 0.5450 -0.0350 -0.0461 0.0626  65   ALA A N   
379   C CA  . ALA A 67   ? 0.3039 0.2391 0.5272 -0.0328 -0.0480 0.0578  65   ALA A CA  
380   C C   . ALA A 67   ? 0.3201 0.2509 0.5500 -0.0319 -0.0530 0.0490  65   ALA A C   
381   O O   . ALA A 67   ? 0.3059 0.2334 0.5320 -0.0296 -0.0536 0.0418  65   ALA A O   
382   C CB  . ALA A 67   ? 0.3437 0.2791 0.5718 -0.0333 -0.0494 0.0642  65   ALA A CB  
383   N N   . SER A 68   ? 0.3283 0.2592 0.5678 -0.0335 -0.0567 0.0492  66   SER A N   
384   C CA  . SER A 68   ? 0.3438 0.2711 0.5897 -0.0324 -0.0616 0.0405  66   SER A CA  
385   C C   . SER A 68   ? 0.3333 0.2607 0.5720 -0.0312 -0.0599 0.0328  66   SER A C   
386   O O   . SER A 68   ? 0.3450 0.2695 0.5831 -0.0290 -0.0621 0.0241  66   SER A O   
387   C CB  . SER A 68   ? 0.3668 0.2946 0.6242 -0.0345 -0.0657 0.0428  66   SER A CB  
388   O OG  . SER A 68   ? 0.4532 0.3779 0.7167 -0.0333 -0.0705 0.0340  66   SER A OG  
389   N N   . THR A 69   ? 0.3323 0.2635 0.5657 -0.0327 -0.0562 0.0357  67   THR A N   
390   C CA  . THR A 69   ? 0.3162 0.2479 0.5428 -0.0318 -0.0545 0.0290  67   THR A CA  
391   C C   . THR A 69   ? 0.3073 0.2376 0.5242 -0.0294 -0.0516 0.0256  67   THR A C   
392   O O   . THR A 69   ? 0.3123 0.2412 0.5263 -0.0277 -0.0526 0.0171  67   THR A O   
393   C CB  . THR A 69   ? 0.2876 0.2240 0.5108 -0.0339 -0.0509 0.0338  67   THR A CB  
394   O OG1 . THR A 69   ? 0.2908 0.2285 0.5233 -0.0359 -0.0540 0.0357  67   THR A OG1 
395   C CG2 . THR A 69   ? 0.2838 0.2213 0.4994 -0.0331 -0.0488 0.0277  67   THR A CG2 
396   N N   . ALA A 70   ? 0.2708 0.2018 0.4827 -0.0293 -0.0482 0.0319  68   ALA A N   
397   C CA  . ALA A 70   ? 0.2861 0.2156 0.4890 -0.0271 -0.0455 0.0292  68   ALA A CA  
398   C C   . ALA A 70   ? 0.3090 0.2344 0.5150 -0.0248 -0.0493 0.0221  68   ALA A C   
399   O O   . ALA A 70   ? 0.3007 0.2249 0.5013 -0.0227 -0.0488 0.0153  68   ALA A O   
400   C CB  . ALA A 70   ? 0.2847 0.2161 0.4822 -0.0273 -0.0415 0.0375  68   ALA A CB  
401   N N   . ARG A 71   ? 0.3110 0.2346 0.5263 -0.0251 -0.0533 0.0237  69   ARG A N   
402   C CA  . ARG A 71   ? 0.3322 0.2523 0.5515 -0.0227 -0.0573 0.0169  69   ARG A CA  
403   C C   . ARG A 71   ? 0.3100 0.2296 0.5307 -0.0214 -0.0599 0.0067  69   ARG A C   
404   O O   . ARG A 71   ? 0.3419 0.2605 0.5591 -0.0188 -0.0605 -0.0008 69   ARG A O   
405   C CB  . ARG A 71   ? 0.3245 0.2430 0.5549 -0.0236 -0.0615 0.0207  69   ARG A CB  
406   C CG  . ARG A 71   ? 0.3697 0.2849 0.6063 -0.0212 -0.0663 0.0132  69   ARG A CG  
407   C CD  . ARG A 71   ? 0.3362 0.2497 0.5836 -0.0221 -0.0703 0.0179  69   ARG A CD  
408   N NE  . ARG A 71   ? 0.4058 0.3190 0.6503 -0.0219 -0.0683 0.0239  69   ARG A NE  
409   C CZ  . ARG A 71   ? 0.3990 0.3102 0.6405 -0.0195 -0.0684 0.0200  69   ARG A CZ  
410   N NH1 . ARG A 71   ? 0.4254 0.3351 0.6661 -0.0168 -0.0703 0.0101  69   ARG A NH1 
411   N NH2 . ARG A 71   ? 0.4458 0.3569 0.6849 -0.0196 -0.0667 0.0261  69   ARG A NH2 
412   N N   . LYS A 72   ? 0.2883 0.2095 0.5136 -0.0231 -0.0615 0.0062  70   LYS A N   
413   C CA  . LYS A 72   ? 0.3093 0.2309 0.5359 -0.0219 -0.0642 -0.0034 70   LYS A CA  
414   C C   . LYS A 72   ? 0.3510 0.2743 0.5669 -0.0206 -0.0607 -0.0085 70   LYS A C   
415   O O   . LYS A 72   ? 0.3107 0.2341 0.5252 -0.0181 -0.0625 -0.0177 70   LYS A O   
416   C CB  . LYS A 72   ? 0.3418 0.2651 0.5745 -0.0242 -0.0660 -0.0020 70   LYS A CB  
417   C CG  . LYS A 72   ? 0.3220 0.2466 0.5556 -0.0232 -0.0686 -0.0119 70   LYS A CG  
418   C CD  . LYS A 72   ? 0.3679 0.2937 0.6092 -0.0254 -0.0712 -0.0105 70   LYS A CD  
419   C CE  . LYS A 72   ? 0.3975 0.3246 0.6410 -0.0239 -0.0748 -0.0210 70   LYS A CE  
420   N NZ  . LYS A 72   ? 0.6103 0.5382 0.8622 -0.0260 -0.0779 -0.0199 70   LYS A NZ  
421   N N   . LEU A 73   ? 0.3089 0.2341 0.5173 -0.0220 -0.0558 -0.0028 71   LEU A N   
422   C CA  . LEU A 73   ? 0.2947 0.2215 0.4933 -0.0210 -0.0526 -0.0070 71   LEU A CA  
423   C C   . LEU A 73   ? 0.3085 0.2335 0.5021 -0.0181 -0.0519 -0.0107 71   LEU A C   
424   O O   . LEU A 73   ? 0.2914 0.2173 0.4804 -0.0162 -0.0519 -0.0186 71   LEU A O   
425   C CB  . LEU A 73   ? 0.3184 0.2475 0.5107 -0.0230 -0.0475 0.0007  71   LEU A CB  
426   C CG  . LEU A 73   ? 0.3184 0.2505 0.5141 -0.0257 -0.0473 0.0043  71   LEU A CG  
427   C CD1 . LEU A 73   ? 0.2859 0.2206 0.4760 -0.0273 -0.0422 0.0132  71   LEU A CD1 
428   C CD2 . LEU A 73   ? 0.2735 0.2077 0.4683 -0.0257 -0.0487 -0.0035 71   LEU A CD2 
429   N N   . ILE A 74   ? 0.2660 0.1888 0.4604 -0.0178 -0.0512 -0.0051 72   ILE A N   
430   C CA  . ILE A 74   ? 0.2692 0.1904 0.4586 -0.0153 -0.0503 -0.0077 72   ILE A CA  
431   C C   . ILE A 74   ? 0.3481 0.2682 0.5425 -0.0127 -0.0548 -0.0167 72   ILE A C   
432   O O   . ILE A 74   ? 0.3165 0.2370 0.5059 -0.0102 -0.0543 -0.0231 72   ILE A O   
433   C CB  . ILE A 74   ? 0.3466 0.2664 0.5355 -0.0159 -0.0485 0.0012  72   ILE A CB  
434   C CG1 . ILE A 74   ? 0.3368 0.2587 0.5183 -0.0175 -0.0432 0.0087  72   ILE A CG1 
435   C CG2 . ILE A 74   ? 0.3359 0.2537 0.5221 -0.0132 -0.0487 -0.0018 72   ILE A CG2 
436   C CD1 . ILE A 74   ? 0.3295 0.2518 0.5118 -0.0188 -0.0416 0.0183  72   ILE A CD1 
437   N N   . GLU A 75   ? 0.3489 0.2680 0.5535 -0.0132 -0.0593 -0.0173 73   GLU A N   
438   C CA  . GLU A 75   ? 0.3676 0.2863 0.5776 -0.0106 -0.0638 -0.0264 73   GLU A CA  
439   C C   . GLU A 75   ? 0.3374 0.2593 0.5432 -0.0091 -0.0641 -0.0359 73   GLU A C   
440   O O   . GLU A 75   ? 0.3641 0.2873 0.5685 -0.0061 -0.0654 -0.0440 73   GLU A O   
441   C CB  . GLU A 75   ? 0.3422 0.2593 0.5645 -0.0116 -0.0687 -0.0250 73   GLU A CB  
442   C CG  . GLU A 75   ? 0.3850 0.2992 0.6124 -0.0124 -0.0694 -0.0174 73   GLU A CG  
443   C CD  . GLU A 75   ? 0.4496 0.3624 0.6893 -0.0139 -0.0740 -0.0146 73   GLU A CD  
444   O OE1 . GLU A 75   ? 0.4243 0.3382 0.6680 -0.0151 -0.0758 -0.0164 73   GLU A OE1 
445   O OE2 . GLU A 75   ? 0.4709 0.3815 0.7165 -0.0140 -0.0760 -0.0104 73   GLU A OE2 
446   N N   . ALA A 76   ? 0.3613 0.2854 0.5650 -0.0112 -0.0626 -0.0349 74   ALA A N   
447   C CA  . ALA A 76   ? 0.3502 0.2784 0.5493 -0.0101 -0.0626 -0.0435 74   ALA A CA  
448   C C   . ALA A 76   ? 0.3278 0.2576 0.5162 -0.0085 -0.0588 -0.0459 74   ALA A C   
449   O O   . ALA A 76   ? 0.3688 0.3020 0.5538 -0.0060 -0.0596 -0.0549 74   ALA A O   
450   C CB  . ALA A 76   ? 0.3674 0.2977 0.5669 -0.0130 -0.0620 -0.0412 74   ALA A CB  
451   N N   . LEU A 77   ? 0.3289 0.2570 0.5118 -0.0098 -0.0546 -0.0381 75   LEU A N   
452   C CA  . LEU A 77   ? 0.3333 0.2625 0.5063 -0.0084 -0.0509 -0.0398 75   LEU A CA  
453   C C   . LEU A 77   ? 0.4129 0.3417 0.5851 -0.0050 -0.0521 -0.0451 75   LEU A C   
454   O O   . LEU A 77   ? 0.4219 0.3540 0.5882 -0.0029 -0.0514 -0.0522 75   LEU A O   
455   C CB  . LEU A 77   ? 0.3467 0.2739 0.5147 -0.0102 -0.0463 -0.0298 75   LEU A CB  
456   C CG  . LEU A 77   ? 0.3780 0.3096 0.5413 -0.0124 -0.0431 -0.0248 75   LEU A CG  
457   C CD1 . LEU A 77   ? 0.3381 0.2687 0.4971 -0.0138 -0.0389 -0.0146 75   LEU A CD1 
458   C CD2 . LEU A 77   ? 0.3413 0.2801 0.4940 -0.0109 -0.0407 -0.0301 75   LEU A CD2 
459   N N   . ARG A 78   ? 0.3828 0.3082 0.5610 -0.0046 -0.0540 -0.0418 76   ARG A N   
460   C CA  . ARG A 78   ? 0.3655 0.2907 0.5436 -0.0015 -0.0553 -0.0463 76   ARG A CA  
461   C C   . ARG A 78   ? 0.3984 0.3266 0.5811 0.0010  -0.0594 -0.0565 76   ARG A C   
462   O O   . ARG A 78   ? 0.4205 0.3507 0.6010 0.0040  -0.0599 -0.0625 76   ARG A O   
463   C CB  . ARG A 78   ? 0.3398 0.2608 0.5232 -0.0020 -0.0562 -0.0392 76   ARG A CB  
464   C CG  . ARG A 78   ? 0.4094 0.3286 0.5861 -0.0033 -0.0517 -0.0305 76   ARG A CG  
465   C CD  . ARG A 78   ? 0.3296 0.2456 0.5109 -0.0038 -0.0526 -0.0239 76   ARG A CD  
466   N NE  . ARG A 78   ? 0.3619 0.2772 0.5356 -0.0039 -0.0484 -0.0178 76   ARG A NE  
467   C CZ  . ARG A 78   ? 0.3246 0.2380 0.5000 -0.0043 -0.0482 -0.0113 76   ARG A CZ  
468   N NH1 . ARG A 78   ? 0.3662 0.2779 0.5509 -0.0048 -0.0520 -0.0095 76   ARG A NH1 
469   N NH2 . ARG A 78   ? 0.3424 0.2557 0.5099 -0.0041 -0.0443 -0.0067 76   ARG A NH2 
470   N N   . GLY A 79   ? 0.3795 0.3087 0.5683 -0.0001 -0.0624 -0.0588 77   GLY A N   
471   C CA  . GLY A 79   ? 0.4542 0.3868 0.6477 0.0025  -0.0665 -0.0685 77   GLY A CA  
472   C C   . GLY A 79   ? 0.4445 0.3837 0.6307 0.0041  -0.0654 -0.0771 77   GLY A C   
473   O O   . GLY A 79   ? 0.5091 0.4524 0.6966 0.0072  -0.0679 -0.0857 77   GLY A O   
474   N N   . LYS A 80   ? 0.4742 0.4151 0.6528 0.0022  -0.0619 -0.0748 78   LYS A N   
475   C CA  . LYS A 80   ? 0.5151 0.4631 0.6862 0.0035  -0.0607 -0.0824 78   LYS A CA  
476   C C   . LYS A 80   ? 0.5145 0.4642 0.6756 0.0044  -0.0565 -0.0821 78   LYS A C   
477   O O   . LYS A 80   ? 0.5906 0.5481 0.7435 0.0055  -0.0547 -0.0869 78   LYS A O   
478   C CB  . LYS A 80   ? 0.4449 0.3950 0.6152 0.0006  -0.0604 -0.0813 78   LYS A CB  
479   C CG  . LYS A 80   ? 0.4429 0.3903 0.6090 -0.0026 -0.0563 -0.0712 78   LYS A CG  
480   C CD  . LYS A 80   ? 0.4407 0.3912 0.6071 -0.0052 -0.0563 -0.0693 78   LYS A CD  
481   C CE  . LYS A 80   ? 0.4031 0.3524 0.5650 -0.0079 -0.0518 -0.0581 78   LYS A CE  
482   N NZ  . LYS A 80   ? 0.3054 0.2579 0.4680 -0.0103 -0.0518 -0.0561 78   LYS A NZ  
483   N N   . HIS A 81   ? 0.4974 0.4418 0.6576 0.0042  -0.0545 -0.0756 79   HIS A N   
484   C CA  . HIS A 81   ? 0.6070 0.5544 0.7563 0.0053  -0.0498 -0.0736 79   HIS A CA  
485   C C   . HIS A 81   ? 0.6478 0.5995 0.7953 0.0090  -0.0510 -0.0827 79   HIS A C   
486   O O   . HIS A 81   ? 0.6506 0.6003 0.8047 0.0110  -0.0540 -0.0855 79   HIS A O   
487   C CB  . HIS A 81   ? 0.6118 0.5526 0.7612 0.0042  -0.0476 -0.0643 79   HIS A CB  
488   C CG  . HIS A 81   ? 0.7049 0.6491 0.8427 0.0052  -0.0426 -0.0612 79   HIS A CG  
489   N ND1 . HIS A 81   ? 0.7291 0.6696 0.8666 0.0064  -0.0418 -0.0587 79   HIS A ND1 
490   C CD2 . HIS A 81   ? 0.7141 0.6652 0.8408 0.0050  -0.0385 -0.0601 79   HIS A CD2 
491   C CE1 . HIS A 81   ? 0.7012 0.6461 0.8278 0.0069  -0.0374 -0.0564 79   HIS A CE1 
492   N NE2 . HIS A 81   ? 0.7583 0.7095 0.8784 0.0061  -0.0353 -0.0572 79   HIS A NE2 
493   N N   . SER A 82   ? 0.6635 0.6241 0.8004 0.0101  -0.0477 -0.0851 80   SER A N   
494   C CA  . SER A 82   ? 0.6423 0.6089 0.7757 0.0135  -0.0477 -0.0927 80   SER A CA  
495   C C   . SER A 82   ? 0.6800 0.6484 0.8034 0.0138  -0.0428 -0.0873 80   SER A C   
496   O O   . SER A 82   ? 0.6794 0.6453 0.7980 0.0114  -0.0393 -0.0785 80   SER A O   
497   C CB  . SER A 82   ? 0.6080 0.5850 0.7377 0.0146  -0.0484 -0.1006 80   SER A CB  
498   N N   . GLY A 83   ? 0.6323 0.6056 0.7530 0.0167  -0.0426 -0.0931 81   GLY A N   
499   C CA  . GLY A 83   ? 0.6318 0.6079 0.7432 0.0170  -0.0382 -0.0888 81   GLY A CA  
500   C C   . GLY A 83   ? 0.5787 0.5628 0.6795 0.0156  -0.0343 -0.0863 81   GLY A C   
501   O O   . GLY A 83   ? 0.5680 0.5594 0.6674 0.0158  -0.0352 -0.0913 81   GLY A O   
502   N N   . SER A 84   ? 0.5467 0.5297 0.6403 0.0142  -0.0302 -0.0785 82   SER A N   
503   C CA  . SER A 84   ? 0.5117 0.5014 0.5959 0.0126  -0.0266 -0.0752 82   SER A CA  
504   C C   . SER A 84   ? 0.4536 0.4541 0.5320 0.0146  -0.0258 -0.0811 82   SER A C   
505   O O   . SER A 84   ? 0.4028 0.4056 0.4838 0.0172  -0.0275 -0.0874 82   SER A O   
506   C CB  . SER A 84   ? 0.4714 0.4570 0.5499 0.0109  -0.0228 -0.0660 82   SER A CB  
507   O OG  . SER A 84   ? 0.4694 0.4558 0.5444 0.0125  -0.0213 -0.0661 82   SER A OG  
508   N N   . GLY A 85   ? 0.4078 0.4154 0.4785 0.0132  -0.0233 -0.0788 83   GLY A N   
509   C CA  . GLY A 85   ? 0.3668 0.3855 0.4313 0.0146  -0.0221 -0.0830 83   GLY A CA  
510   C C   . GLY A 85   ? 0.2963 0.3154 0.3569 0.0156  -0.0197 -0.0811 83   GLY A C   
511   O O   . GLY A 85   ? 0.2925 0.3184 0.3525 0.0179  -0.0202 -0.0870 83   GLY A O   
512   N N   . VAL A 86   ? 0.3475 0.3600 0.4054 0.0140  -0.0173 -0.0731 84   VAL A N   
513   C CA  . VAL A 86   ? 0.2948 0.3074 0.3488 0.0148  -0.0151 -0.0710 84   VAL A CA  
514   C C   . VAL A 86   ? 0.3270 0.3361 0.3873 0.0174  -0.0174 -0.0757 84   VAL A C   
515   O O   . VAL A 86   ? 0.2917 0.3059 0.3501 0.0192  -0.0169 -0.0789 84   VAL A O   
516   C CB  . VAL A 86   ? 0.3306 0.3365 0.3810 0.0126  -0.0123 -0.0618 84   VAL A CB  
517   C CG1 . VAL A 86   ? 0.3111 0.3151 0.3593 0.0136  -0.0108 -0.0600 84   VAL A CG1 
518   C CG2 . VAL A 86   ? 0.3539 0.3648 0.3973 0.0105  -0.0098 -0.0576 84   VAL A CG2 
519   N N   . GLU A 87   ? 0.3441 0.3447 0.4123 0.0175  -0.0201 -0.0763 85   GLU A N   
520   C CA  . GLU A 87   ? 0.3526 0.3493 0.4280 0.0201  -0.0229 -0.0808 85   GLU A CA  
521   C C   . GLU A 87   ? 0.3287 0.3338 0.4063 0.0229  -0.0252 -0.0908 85   GLU A C   
522   O O   . GLU A 87   ? 0.3240 0.3306 0.4034 0.0255  -0.0259 -0.0949 85   GLU A O   
523   C CB  . GLU A 87   ? 0.4457 0.4321 0.5299 0.0193  -0.0258 -0.0792 85   GLU A CB  
524   C CG  . GLU A 87   ? 0.5047 0.4827 0.5880 0.0172  -0.0239 -0.0697 85   GLU A CG  
525   C CD  . GLU A 87   ? 0.6066 0.5762 0.6982 0.0158  -0.0265 -0.0672 85   GLU A CD  
526   O OE1 . GLU A 87   ? 0.6012 0.5709 0.6996 0.0165  -0.0300 -0.0730 85   GLU A OE1 
527   O OE2 . GLU A 87   ? 0.6780 0.6413 0.7694 0.0140  -0.0250 -0.0595 85   GLU A OE2 
528   N N   . GLY A 88   ? 0.3231 0.3341 0.4007 0.0227  -0.0264 -0.0951 86   GLY A N   
529   C CA  . GLY A 88   ? 0.3021 0.3224 0.3813 0.0256  -0.0285 -0.1050 86   GLY A CA  
530   C C   . GLY A 88   ? 0.2950 0.3263 0.3664 0.0267  -0.0256 -0.1061 86   GLY A C   
531   O O   . GLY A 88   ? 0.3181 0.3561 0.3912 0.0297  -0.0269 -0.1136 86   GLY A O   
532   N N   . LEU A 89   ? 0.2889 0.3224 0.3520 0.0241  -0.0218 -0.0987 87   LEU A N   
533   C CA  . LEU A 89   ? 0.2898 0.3334 0.3457 0.0246  -0.0189 -0.0984 87   LEU A CA  
534   C C   . LEU A 89   ? 0.2493 0.2894 0.3061 0.0261  -0.0183 -0.0978 87   LEU A C   
535   O O   . LEU A 89   ? 0.2494 0.2977 0.3055 0.0285  -0.0182 -0.1029 87   LEU A O   
536   C CB  . LEU A 89   ? 0.2905 0.3358 0.3384 0.0212  -0.0155 -0.0902 87   LEU A CB  
537   C CG  . LEU A 89   ? 0.3563 0.4115 0.3964 0.0207  -0.0124 -0.0878 87   LEU A CG  
538   C CD1 . LEU A 89   ? 0.3805 0.4494 0.4195 0.0226  -0.0133 -0.0954 87   LEU A CD1 
539   C CD2 . LEU A 89   ? 0.3380 0.3926 0.3721 0.0172  -0.0099 -0.0796 87   LEU A CD2 
540   N N   . VAL A 90   ? 0.2655 0.2941 0.3242 0.0249  -0.0179 -0.0915 88   VAL A N   
541   C CA  . VAL A 90   ? 0.2512 0.2754 0.3117 0.0264  -0.0177 -0.0907 88   VAL A CA  
542   C C   . VAL A 90   ? 0.2857 0.3109 0.3538 0.0301  -0.0212 -0.0996 88   VAL A C   
543   O O   . VAL A 90   ? 0.2748 0.3043 0.3427 0.0323  -0.0209 -0.1026 88   VAL A O   
544   C CB  . VAL A 90   ? 0.2351 0.2467 0.2972 0.0245  -0.0173 -0.0829 88   VAL A CB  
545   C CG1 . VAL A 90   ? 0.2611 0.2675 0.3268 0.0263  -0.0180 -0.0826 88   VAL A CG1 
546   C CG2 . VAL A 90   ? 0.2454 0.2573 0.2995 0.0214  -0.0136 -0.0747 88   VAL A CG2 
547   N N   . GLN A 91   ? 0.2701 0.2917 0.3454 0.0308  -0.0247 -0.1042 89   GLN A N   
548   C CA  . GLN A 91   ? 0.3339 0.3560 0.4174 0.0345  -0.0285 -0.1132 89   GLN A CA  
549   C C   . GLN A 91   ? 0.2942 0.3304 0.3749 0.0371  -0.0284 -0.1215 89   GLN A C   
550   O O   . GLN A 91   ? 0.3136 0.3534 0.3968 0.0401  -0.0292 -0.1262 89   GLN A O   
551   C CB  . GLN A 91   ? 0.3565 0.3717 0.4486 0.0344  -0.0325 -0.1162 89   GLN A CB  
552   N N   . GLU A 92   ? 0.2982 0.3434 0.3737 0.0359  -0.0272 -0.1226 90   GLU A N   
553   C CA  . GLU A 92   ? 0.2972 0.3570 0.3706 0.0384  -0.0274 -0.1309 90   GLU A CA  
554   C C   . GLU A 92   ? 0.3021 0.3697 0.3702 0.0395  -0.0245 -0.1300 90   GLU A C   
555   O O   . GLU A 92   ? 0.2702 0.3462 0.3405 0.0421  -0.0256 -0.1349 90   GLU A O   
556   C CB  . GLU A 92   ? 0.3022 0.3704 0.3699 0.0365  -0.0263 -0.1305 90   GLU A CB  
557   C CG  . GLU A 92   ? 0.3328 0.4175 0.3980 0.0386  -0.0265 -0.1375 90   GLU A CG  
558   C CD  . GLU A 92   ? 0.3876 0.4809 0.4474 0.0369  -0.0257 -0.1379 90   GLU A CD  
559   O OE1 . GLU A 92   ? 0.3656 0.4517 0.4241 0.0337  -0.0252 -0.1317 90   GLU A OE1 
560   O OE2 . GLU A 92   ? 0.3815 0.4891 0.4389 0.0381  -0.0255 -0.1413 90   GLU A OE2 
561   N N   . TYR A 93   ? 0.2825 0.3477 0.3442 0.0366  -0.0209 -0.1207 91   TYR A N   
562   C CA  . TYR A 93   ? 0.2340 0.3072 0.2902 0.0369  -0.0181 -0.1190 91   TYR A CA  
563   C C   . TYR A 93   ? 0.2628 0.3271 0.3216 0.0376  -0.0178 -0.1157 91   TYR A C   
564   O O   . TYR A 93   ? 0.2451 0.3142 0.2994 0.0373  -0.0153 -0.1126 91   TYR A O   
565   C CB  . TYR A 93   ? 0.2473 0.3260 0.2945 0.0333  -0.0144 -0.1114 91   TYR A CB  
566   C CG  . TYR A 93   ? 0.2364 0.3274 0.2803 0.0331  -0.0144 -0.1152 91   TYR A CG  
567   C CD1 . TYR A 93   ? 0.2240 0.3305 0.2651 0.0350  -0.0136 -0.1204 91   TYR A CD1 
568   C CD2 . TYR A 93   ? 0.2725 0.3602 0.3164 0.0312  -0.0152 -0.1137 91   TYR A CD2 
569   C CE1 . TYR A 93   ? 0.2581 0.3767 0.2961 0.0349  -0.0137 -0.1239 91   TYR A CE1 
570   C CE2 . TYR A 93   ? 0.2806 0.3801 0.3215 0.0311  -0.0154 -0.1172 91   TYR A CE2 
571   C CZ  . TYR A 93   ? 0.2762 0.3913 0.3140 0.0329  -0.0146 -0.1222 91   TYR A CZ  
572   O OH  . TYR A 93   ? 0.2888 0.4166 0.3235 0.0329  -0.0148 -0.1256 91   TYR A OH  
573   N N   . SER A 94   ? 0.2351 0.2871 0.3014 0.0384  -0.0206 -0.1160 92   SER A N   
574   C CA  . SER A 94   ? 0.2435 0.2868 0.3131 0.0392  -0.0209 -0.1131 92   SER A CA  
575   C C   . SER A 94   ? 0.2197 0.2602 0.2822 0.0362  -0.0172 -0.1034 92   SER A C   
576   O O   . SER A 94   ? 0.2090 0.2508 0.2700 0.0369  -0.0160 -0.1018 92   SER A O   
577   C CB  . SER A 94   ? 0.2330 0.2828 0.3062 0.0433  -0.0222 -0.1206 92   SER A CB  
578   O OG  . SER A 94   ? 0.3027 0.3559 0.3821 0.0452  -0.0258 -0.1273 92   SER A OG  
579   N N   . LEU A 95   ? 0.1981 0.2351 0.2564 0.0328  -0.0157 -0.0970 93   LEU A N   
580   C CA  . LEU A 95   ? 0.2009 0.2356 0.2525 0.0299  -0.0123 -0.0882 93   LEU A CA  
581   C C   . LEU A 95   ? 0.1771 0.1993 0.2316 0.0294  -0.0127 -0.0829 93   LEU A C   
582   O O   . LEU A 95   ? 0.2212 0.2347 0.2815 0.0295  -0.0150 -0.0827 93   LEU A O   
583   C CB  . LEU A 95   ? 0.1967 0.2320 0.2431 0.0266  -0.0106 -0.0834 93   LEU A CB  
584   C CG  . LEU A 95   ? 0.1792 0.2272 0.2222 0.0266  -0.0101 -0.0874 93   LEU A CG  
585   C CD1 . LEU A 95   ? 0.2270 0.2742 0.2649 0.0232  -0.0084 -0.0812 93   LEU A CD1 
586   C CD2 . LEU A 95   ? 0.2293 0.2886 0.2681 0.0275  -0.0083 -0.0889 93   LEU A CD2 
587   N N   . SER A 96   ? 0.1559 0.1778 0.2065 0.0288  -0.0106 -0.0783 94   SER A N   
588   C CA  . SER A 96   ? 0.1573 0.1684 0.2083 0.0275  -0.0102 -0.0715 94   SER A CA  
589   C C   . SER A 96   ? 0.1815 0.1882 0.2284 0.0243  -0.0086 -0.0650 94   SER A C   
590   O O   . SER A 96   ? 0.1603 0.1726 0.2033 0.0228  -0.0074 -0.0650 94   SER A O   
591   C CB  . SER A 96   ? 0.1897 0.2023 0.2370 0.0276  -0.0084 -0.0685 94   SER A CB  
592   O OG  . SER A 96   ? 0.1631 0.1818 0.2028 0.0253  -0.0055 -0.0649 94   SER A OG  
593   N N   . SER A 97   ? 0.1782 0.1753 0.2261 0.0232  -0.0085 -0.0592 95   SER A N   
594   C CA  . SER A 97   ? 0.1709 0.1640 0.2150 0.0203  -0.0067 -0.0529 95   SER A CA  
595   C C   . SER A 97   ? 0.1660 0.1650 0.2021 0.0186  -0.0038 -0.0496 95   SER A C   
596   O O   . SER A 97   ? 0.1490 0.1501 0.1818 0.0167  -0.0027 -0.0478 95   SER A O   
597   C CB  . SER A 97   ? 0.2111 0.1944 0.2570 0.0197  -0.0069 -0.0472 95   SER A CB  
598   O OG  . SER A 97   ? 0.2914 0.2690 0.3450 0.0206  -0.0097 -0.0490 95   SER A OG  
599   N N   . GLN A 98   ? 0.1402 0.1414 0.1734 0.0190  -0.0026 -0.0486 96   GLN A N   
600   C CA  . GLN A 98   ? 0.1370 0.1432 0.1634 0.0171  -0.0001 -0.0451 96   GLN A CA  
601   C C   . GLN A 98   ? 0.1215 0.1382 0.1459 0.0169  0.0003  -0.0488 96   GLN A C   
602   O O   . GLN A 98   ? 0.1249 0.1449 0.1446 0.0147  0.0019  -0.0455 96   GLN A O   
603   C CB  . GLN A 98   ? 0.1397 0.1464 0.1641 0.0176  0.0008  -0.0435 96   GLN A CB  
604   C CG  . GLN A 98   ? 0.1501 0.1474 0.1743 0.0171  0.0011  -0.0381 96   GLN A CG  
605   C CD  . GLN A 98   ? 0.1759 0.1701 0.1955 0.0146  0.0029  -0.0324 96   GLN A CD  
606   O OE1 . GLN A 98   ? 0.1992 0.1894 0.2199 0.0137  0.0027  -0.0309 96   GLN A OE1 
607   N NE2 . GLN A 98   ? 0.1917 0.1877 0.2067 0.0134  0.0045  -0.0292 96   GLN A NE2 
608   N N   . GLU A 99   ? 0.1420 0.1644 0.1700 0.0192  -0.0013 -0.0556 97   GLU A N   
609   C CA  . GLU A 99   ? 0.1239 0.1572 0.1500 0.0192  -0.0011 -0.0594 97   GLU A CA  
610   C C   . GLU A 99   ? 0.1573 0.1895 0.1833 0.0177  -0.0015 -0.0587 97   GLU A C   
611   O O   . GLU A 99   ? 0.1405 0.1797 0.1622 0.0161  -0.0002 -0.0575 97   GLU A O   
612   C CB  . GLU A 99   ? 0.1444 0.1841 0.1748 0.0223  -0.0029 -0.0675 97   GLU A CB  
613   C CG  . GLU A 99   ? 0.1456 0.1899 0.1752 0.0236  -0.0021 -0.0683 97   GLU A CG  
614   C CD  . GLU A 99   ? 0.1612 0.2100 0.1962 0.0273  -0.0042 -0.0765 97   GLU A CD  
615   O OE1 . GLU A 99   ? 0.1730 0.2203 0.2129 0.0289  -0.0065 -0.0816 97   GLU A OE1 
616   O OE2 . GLU A 99   ? 0.1630 0.2169 0.1977 0.0286  -0.0036 -0.0778 97   GLU A OE2 
617   N N   . GLY A 100  ? 0.1436 0.1674 0.1744 0.0182  -0.0032 -0.0594 98   GLY A N   
618   C CA  . GLY A 100  ? 0.1494 0.1719 0.1804 0.0167  -0.0037 -0.0585 98   GLY A CA  
619   C C   . GLY A 100  ? 0.1299 0.1503 0.1554 0.0138  -0.0014 -0.0512 98   GLY A C   
620   O O   . GLY A 100  ? 0.1400 0.1651 0.1627 0.0123  -0.0008 -0.0503 98   GLY A O   
621   N N   . VAL A 101  ? 0.1318 0.1452 0.1560 0.0131  -0.0002 -0.0459 99   VAL A N   
622   C CA  . VAL A 101  ? 0.1406 0.1517 0.1600 0.0106  0.0019  -0.0393 99   VAL A CA  
623   C C   . VAL A 101  ? 0.1241 0.1442 0.1382 0.0095  0.0034  -0.0384 99   VAL A C   
624   O O   . VAL A 101  ? 0.1446 0.1672 0.1559 0.0076  0.0041  -0.0356 99   VAL A O   
625   C CB  . VAL A 101  ? 0.1400 0.1430 0.1589 0.0105  0.0027  -0.0348 99   VAL A CB  
626   C CG1 . VAL A 101  ? 0.1583 0.1598 0.1721 0.0083  0.0047  -0.0287 99   VAL A CG1 
627   C CG2 . VAL A 101  ? 0.1665 0.1610 0.1904 0.0112  0.0012  -0.0345 99   VAL A CG2 
628   N N   . ALA A 102  ? 0.1398 0.1655 0.1531 0.0105  0.0037  -0.0405 100  ALA A N   
629   C CA  . ALA A 102  ? 0.1366 0.1714 0.1454 0.0092  0.0050  -0.0390 100  ALA A CA  
630   C C   . ALA A 102  ? 0.1337 0.1776 0.1417 0.0087  0.0047  -0.0416 100  ALA A C   
631   O O   . ALA A 102  ? 0.1306 0.1794 0.1348 0.0066  0.0057  -0.0380 100  ALA A O   
632   C CB  . ALA A 102  ? 0.1284 0.1684 0.1373 0.0106  0.0052  -0.0415 100  ALA A CB  
633   N N   . LEU A 103  ? 0.1247 0.1711 0.1365 0.0107  0.0030  -0.0480 101  LEU A N   
634   C CA  . LEU A 103  ? 0.1202 0.1756 0.1313 0.0106  0.0023  -0.0512 101  LEU A CA  
635   C C   . LEU A 103  ? 0.1366 0.1886 0.1463 0.0084  0.0026  -0.0470 101  LEU A C   
636   O O   . LEU A 103  ? 0.1613 0.2211 0.1678 0.0069  0.0031  -0.0455 101  LEU A O   
637   C CB  . LEU A 103  ? 0.1571 0.2142 0.1734 0.0134  0.0000  -0.0593 101  LEU A CB  
638   C CG  . LEU A 103  ? 0.1310 0.1974 0.1471 0.0136  -0.0010 -0.0635 101  LEU A CG  
639   C CD1 . LEU A 103  ? 0.1726 0.2530 0.1840 0.0131  0.0004  -0.0637 101  LEU A CD1 
640   C CD2 . LEU A 103  ? 0.1621 0.2279 0.1842 0.0166  -0.0037 -0.0717 101  LEU A CD2 
641   N N   . MET A 104  ? 0.1262 0.1671 0.1385 0.0082  0.0021  -0.0449 102  MET A N   
642   C CA  . MET A 104  ? 0.1650 0.2029 0.1763 0.0063  0.0023  -0.0410 102  MET A CA  
643   C C   . MET A 104  ? 0.1722 0.2102 0.1786 0.0040  0.0042  -0.0342 102  MET A C   
644   O O   . MET A 104  ? 0.1735 0.2145 0.1780 0.0024  0.0045  -0.0316 102  MET A O   
645   C CB  . MET A 104  ? 0.1588 0.1855 0.1743 0.0066  0.0014  -0.0401 102  MET A CB  
646   C CG  . MET A 104  ? 0.1668 0.1928 0.1881 0.0086  -0.0011 -0.0466 102  MET A CG  
647   S SD  . MET A 104  ? 0.2444 0.2808 0.2665 0.0091  -0.0028 -0.0529 102  MET A SD  
648   C CE  . MET A 104  ? 0.2693 0.3022 0.2907 0.0066  -0.0025 -0.0479 102  MET A CE  
649   N N   . CYS A 105  ? 0.1536 0.1887 0.1584 0.0039  0.0054  -0.0314 103  CYS A N   
650   C CA  . CYS A 105  ? 0.1490 0.1848 0.1497 0.0017  0.0069  -0.0254 103  CYS A CA  
651   C C   . CYS A 105  ? 0.1763 0.2240 0.1742 0.0006  0.0072  -0.0254 103  CYS A C   
652   O O   . CYS A 105  ? 0.1979 0.2476 0.1934 -0.0014 0.0077  -0.0209 103  CYS A O   
653   C CB  . CYS A 105  ? 0.1620 0.1931 0.1620 0.0020  0.0077  -0.0233 103  CYS A CB  
654   S SG  . CYS A 105  ? 0.1807 0.1986 0.1828 0.0027  0.0077  -0.0213 103  CYS A SG  
655   N N   . LEU A 106  ? 0.1526 0.2086 0.1510 0.0020  0.0069  -0.0301 104  LEU A N   
656   C CA  . LEU A 106  ? 0.1920 0.2608 0.1877 0.0010  0.0072  -0.0302 104  LEU A CA  
657   C C   . LEU A 106  ? 0.1869 0.2600 0.1824 0.0003  0.0064  -0.0308 104  LEU A C   
658   O O   . LEU A 106  ? 0.2029 0.2822 0.1955 -0.0017 0.0069  -0.0268 104  LEU A O   
659   C CB  . LEU A 106  ? 0.1575 0.2350 0.1543 0.0031  0.0069  -0.0362 104  LEU A CB  
660   C CG  . LEU A 106  ? 0.1764 0.2692 0.1707 0.0025  0.0072  -0.0372 104  LEU A CG  
661   C CD1 . LEU A 106  ? 0.2201 0.3168 0.2110 -0.0003 0.0086  -0.0302 104  LEU A CD1 
662   C CD2 . LEU A 106  ? 0.1886 0.2901 0.1845 0.0052  0.0067  -0.0445 104  LEU A CD2 
663   N N   . ALA A 107  ? 0.1532 0.2232 0.1519 0.0020  0.0050  -0.0356 105  ALA A N   
664   C CA  . ALA A 107  ? 0.1785 0.2523 0.1773 0.0014  0.0041  -0.0365 105  ALA A CA  
665   C C   . ALA A 107  ? 0.2148 0.2834 0.2119 -0.0010 0.0047  -0.0296 105  ALA A C   
666   O O   . ALA A 107  ? 0.2073 0.2826 0.2023 -0.0025 0.0046  -0.0274 105  ALA A O   
667   C CB  . ALA A 107  ? 0.1807 0.2499 0.1841 0.0034  0.0022  -0.0425 105  ALA A CB  
668   N N   . GLU A 108  ? 0.1894 0.2464 0.1875 -0.0013 0.0053  -0.0262 106  GLU A N   
669   C CA  . GLU A 108  ? 0.2058 0.2576 0.2025 -0.0033 0.0059  -0.0199 106  GLU A CA  
670   C C   . GLU A 108  ? 0.2299 0.2882 0.2230 -0.0053 0.0067  -0.0150 106  GLU A C   
671   O O   . GLU A 108  ? 0.2578 0.3185 0.2497 -0.0069 0.0065  -0.0114 106  GLU A O   
672   C CB  . GLU A 108  ? 0.1991 0.2388 0.1970 -0.0029 0.0065  -0.0174 106  GLU A CB  
673   C CG  . GLU A 108  ? 0.2098 0.2437 0.2065 -0.0045 0.0072  -0.0113 106  GLU A CG  
674   C CD  . GLU A 108  ? 0.2708 0.2954 0.2675 -0.0042 0.0081  -0.0086 106  GLU A CD  
675   O OE1 . GLU A 108  ? 0.2302 0.2507 0.2286 -0.0027 0.0081  -0.0113 106  GLU A OE1 
676   O OE2 . GLU A 108  ? 0.2594 0.2810 0.2545 -0.0054 0.0087  -0.0038 106  GLU A OE2 
677   N N   . ALA A 109  ? 0.2267 0.2880 0.2185 -0.0053 0.0075  -0.0145 107  ALA A N   
678   C CA  . ALA A 109  ? 0.2451 0.3125 0.2342 -0.0075 0.0081  -0.0095 107  ALA A CA  
679   C C   . ALA A 109  ? 0.2693 0.3498 0.2568 -0.0084 0.0076  -0.0100 107  ALA A C   
680   O O   . ALA A 109  ? 0.2959 0.3801 0.2819 -0.0106 0.0076  -0.0047 107  ALA A O   
681   C CB  . ALA A 109  ? 0.2473 0.3156 0.2358 -0.0072 0.0088  -0.0095 107  ALA A CB  
682   N N   . LEU A 110  ? 0.2231 0.3111 0.2111 -0.0066 0.0071  -0.0164 108  LEU A N   
683   C CA  . LEU A 110  ? 0.2380 0.3396 0.2244 -0.0071 0.0067  -0.0174 108  LEU A CA  
684   C C   . LEU A 110  ? 0.2654 0.3660 0.2518 -0.0081 0.0058  -0.0155 108  LEU A C   
685   O O   . LEU A 110  ? 0.3029 0.4131 0.2873 -0.0098 0.0055  -0.0126 108  LEU A O   
686   C CB  . LEU A 110  ? 0.2277 0.3368 0.2151 -0.0045 0.0061  -0.0257 108  LEU A CB  
687   C CG  . LEU A 110  ? 0.2603 0.3750 0.2471 -0.0037 0.0070  -0.0274 108  LEU A CG  
688   C CD1 . LEU A 110  ? 0.2285 0.3465 0.2177 -0.0004 0.0062  -0.0363 108  LEU A CD1 
689   C CD2 . LEU A 110  ? 0.2620 0.3908 0.2456 -0.0057 0.0077  -0.0235 108  LEU A CD2 
690   N N   . LEU A 111  ? 0.2560 0.3457 0.2449 -0.0073 0.0052  -0.0168 109  LEU A N   
691   C CA  . LEU A 111  ? 0.2654 0.3536 0.2548 -0.0082 0.0043  -0.0148 109  LEU A CA  
692   C C   . LEU A 111  ? 0.3115 0.3955 0.2997 -0.0106 0.0048  -0.0068 109  LEU A C   
693   O O   . LEU A 111  ? 0.3448 0.4291 0.3332 -0.0116 0.0041  -0.0043 109  LEU A O   
694   C CB  . LEU A 111  ? 0.2423 0.3207 0.2353 -0.0066 0.0036  -0.0186 109  LEU A CB  
695   C CG  . LEU A 111  ? 0.2276 0.3104 0.2227 -0.0043 0.0024  -0.0269 109  LEU A CG  
696   C CD1 . LEU A 111  ? 0.2544 0.3262 0.2539 -0.0029 0.0015  -0.0300 109  LEU A CD1 
697   C CD2 . LEU A 111  ? 0.2438 0.3384 0.2378 -0.0045 0.0011  -0.0295 109  LEU A CD2 
698   N N   . ARG A 112  ? 0.2977 0.3779 0.2850 -0.0114 0.0058  -0.0029 110  ARG A N   
699   C CA  . ARG A 112  ? 0.3243 0.4022 0.3109 -0.0136 0.0059  0.0045  110  ARG A CA  
700   C C   . ARG A 112  ? 0.3740 0.4644 0.3585 -0.0157 0.0056  0.0081  110  ARG A C   
701   O O   . ARG A 112  ? 0.4159 0.5056 0.4003 -0.0177 0.0052  0.0144  110  ARG A O   
702   C CB  . ARG A 112  ? 0.3377 0.4074 0.3244 -0.0138 0.0068  0.0072  110  ARG A CB  
703   C CG  . ARG A 112  ? 0.2985 0.3558 0.2871 -0.0120 0.0072  0.0048  110  ARG A CG  
704   C CD  . ARG A 112  ? 0.3463 0.3974 0.3347 -0.0118 0.0080  0.0062  110  ARG A CD  
705   N NE  . ARG A 112  ? 0.3679 0.4152 0.3560 -0.0136 0.0079  0.0122  110  ARG A NE  
706   C CZ  . ARG A 112  ? 0.4014 0.4391 0.3905 -0.0133 0.0079  0.0145  110  ARG A CZ  
707   N NH1 . ARG A 112  ? 0.3869 0.4180 0.3773 -0.0117 0.0082  0.0118  110  ARG A NH1 
708   N NH2 . ARG A 112  ? 0.4101 0.4450 0.3993 -0.0148 0.0075  0.0196  110  ARG A NH2 
709   N N   . ILE A 113  ? 0.3362 0.4383 0.3193 -0.0151 0.0056  0.0043  111  ILE A N   
710   C CA  . ILE A 113  ? 0.3987 0.5148 0.3797 -0.0169 0.0053  0.0072  111  ILE A CA  
711   C C   . ILE A 113  ? 0.4146 0.5350 0.3955 -0.0168 0.0041  0.0060  111  ILE A C   
712   O O   . ILE A 113  ? 0.3992 0.5222 0.3805 -0.0148 0.0037  -0.0009 111  ILE A O   
713   C CB  . ILE A 113  ? 0.3778 0.5057 0.3573 -0.0161 0.0059  0.0032  111  ILE A CB  
714   C CG1 . ILE A 113  ? 0.3698 0.4934 0.3496 -0.0162 0.0070  0.0047  111  ILE A CG1 
715   C CG2 . ILE A 113  ? 0.3922 0.5360 0.3693 -0.0179 0.0056  0.0063  111  ILE A CG2 
716   C CD1 . ILE A 113  ? 0.3840 0.5190 0.3627 -0.0153 0.0077  0.0008  111  ILE A CD1 
717   N N   . PRO A 114  ? 0.5074 0.6288 0.4881 -0.0189 0.0033  0.0123  112  PRO A N   
718   C CA  . PRO A 114  ? 0.5265 0.6495 0.5076 -0.0187 0.0021  0.0111  112  PRO A CA  
719   C C   . PRO A 114  ? 0.4935 0.6317 0.4725 -0.0183 0.0015  0.0074  112  PRO A C   
720   O O   . PRO A 114  ? 0.4996 0.6386 0.4794 -0.0169 0.0005  0.0023  112  PRO A O   
721   C CB  . PRO A 114  ? 0.4987 0.6187 0.4804 -0.0210 0.0014  0.0195  112  PRO A CB  
722   C CG  . PRO A 114  ? 0.5605 0.6741 0.5426 -0.0222 0.0022  0.0242  112  PRO A CG  
723   C CD  . PRO A 114  ? 0.5087 0.6286 0.4893 -0.0215 0.0033  0.0206  112  PRO A CD  
724   N N   . ASP A 115  ? 0.4707 0.6216 0.4473 -0.0196 0.0018  0.0098  113  ASP A N   
725   C CA  . ASP A 115  ? 0.5044 0.6716 0.4787 -0.0193 0.0013  0.0067  113  ASP A CA  
726   C C   . ASP A 115  ? 0.4533 0.6247 0.4274 -0.0164 0.0017  -0.0027 113  ASP A C   
727   O O   . ASP A 115  ? 0.4663 0.6368 0.4404 -0.0157 0.0029  -0.0041 113  ASP A O   
728   C CB  . ASP A 115  ? 0.5275 0.7078 0.4993 -0.0219 0.0015  0.0136  113  ASP A CB  
729   C CG  . ASP A 115  ? 0.4980 0.6968 0.4670 -0.0214 0.0011  0.0101  113  ASP A CG  
730   O OD1 . ASP A 115  ? 0.5487 0.7513 0.5173 -0.0208 -0.0002 0.0076  113  ASP A OD1 
731   O OD2 . ASP A 115  ? 0.4968 0.7070 0.4639 -0.0215 0.0021  0.0098  113  ASP A OD2 
732   N N   . THR A 116  ? 0.4610 0.6374 0.4352 -0.0146 0.0005  -0.0094 114  THR A N   
733   C CA  . THR A 116  ? 0.4486 0.6275 0.4237 -0.0115 0.0004  -0.0191 114  THR A CA  
734   C C   . THR A 116  ? 0.4748 0.6688 0.4472 -0.0110 0.0013  -0.0209 114  THR A C   
735   O O   . THR A 116  ? 0.4353 0.6277 0.4086 -0.0093 0.0022  -0.0252 114  THR A O   
736   C CB  . THR A 116  ? 0.4809 0.6627 0.4571 -0.0098 -0.0015 -0.0257 114  THR A CB  
737   O OG1 . THR A 116  ? 0.4706 0.6382 0.4496 -0.0102 -0.0023 -0.0240 114  THR A OG1 
738   C CG2 . THR A 116  ? 0.4942 0.6779 0.4720 -0.0064 -0.0020 -0.0362 114  THR A CG2 
739   N N   . ALA A 117  ? 0.4557 0.6653 0.4249 -0.0126 0.0012  -0.0175 115  ALA A N   
740   C CA  . ALA A 117  ? 0.4095 0.6356 0.3761 -0.0122 0.0022  -0.0191 115  ALA A CA  
741   C C   . ALA A 117  ? 0.3720 0.5947 0.3388 -0.0135 0.0040  -0.0143 115  ALA A C   
742   O O   . ALA A 117  ? 0.4375 0.6669 0.4040 -0.0119 0.0049  -0.0187 115  ALA A O   
743   C CB  . ALA A 117  ? 0.4680 0.7114 0.4312 -0.0142 0.0018  -0.0146 115  ALA A CB  
744   N N   . THR A 118  ? 0.4121 0.6249 0.3797 -0.0163 0.0042  -0.0055 116  THR A N   
745   C CA  . THR A 118  ? 0.4284 0.6368 0.3967 -0.0176 0.0056  -0.0009 116  THR A CA  
746   C C   . THR A 118  ? 0.3800 0.5772 0.3506 -0.0148 0.0062  -0.0075 116  THR A C   
747   O O   . THR A 118  ? 0.3658 0.5672 0.3363 -0.0141 0.0073  -0.0092 116  THR A O   
748   C CB  . THR A 118  ? 0.3843 0.5821 0.3537 -0.0207 0.0053  0.0088  116  THR A CB  
749   O OG1 . THR A 118  ? 0.4784 0.6877 0.4461 -0.0235 0.0047  0.0159  116  THR A OG1 
750   C CG2 . THR A 118  ? 0.4335 0.6249 0.4042 -0.0218 0.0064  0.0127  116  THR A CG2 
751   N N   . ARG A 119  ? 0.3933 0.5765 0.3662 -0.0133 0.0054  -0.0110 117  ARG A N   
752   C CA  . ARG A 119  ? 0.3681 0.5403 0.3436 -0.0107 0.0057  -0.0171 117  ARG A CA  
753   C C   . ARG A 119  ? 0.3833 0.5658 0.3587 -0.0077 0.0057  -0.0259 117  ARG A C   
754   O O   . ARG A 119  ? 0.3295 0.5106 0.3059 -0.0064 0.0066  -0.0283 117  ARG A O   
755   C CB  . ARG A 119  ? 0.3531 0.5114 0.3311 -0.0097 0.0045  -0.0194 117  ARG A CB  
756   C CG  . ARG A 119  ? 0.3342 0.4798 0.3153 -0.0073 0.0046  -0.0243 117  ARG A CG  
757   C CD  . ARG A 119  ? 0.2832 0.4191 0.2670 -0.0062 0.0033  -0.0276 117  ARG A CD  
758   N NE  . ARG A 119  ? 0.3186 0.4485 0.3022 -0.0084 0.0031  -0.0209 117  ARG A NE  
759   C CZ  . ARG A 119  ? 0.3491 0.4785 0.3335 -0.0085 0.0018  -0.0218 117  ARG A CZ  
760   N NH1 . ARG A 119  ? 0.3398 0.4746 0.3253 -0.0066 0.0004  -0.0291 117  ARG A NH1 
761   N NH2 . ARG A 119  ? 0.3973 0.5208 0.3816 -0.0105 0.0017  -0.0154 117  ARG A NH2 
762   N N   . ASP A 120  ? 0.3735 0.5668 0.3480 -0.0065 0.0046  -0.0310 118  ASP A N   
763   C CA  . ASP A 120  ? 0.3978 0.6012 0.3725 -0.0032 0.0044  -0.0403 118  ASP A CA  
764   C C   . ASP A 120  ? 0.3933 0.6110 0.3657 -0.0036 0.0059  -0.0389 118  ASP A C   
765   O O   . ASP A 120  ? 0.3586 0.5803 0.3322 -0.0009 0.0063  -0.0455 118  ASP A O   
766   C CB  . ASP A 120  ? 0.3923 0.6053 0.3664 -0.0019 0.0027  -0.0459 118  ASP A CB  
767   C CG  . ASP A 120  ? 0.4266 0.6262 0.4036 -0.0014 0.0010  -0.0479 118  ASP A CG  
768   O OD1 . ASP A 120  ? 0.4231 0.6067 0.4032 -0.0011 0.0010  -0.0476 118  ASP A OD1 
769   O OD2 . ASP A 120  ? 0.4693 0.6749 0.4456 -0.0014 -0.0004 -0.0498 118  ASP A OD2 
770   N N   . ALA A 121  ? 0.3661 0.5920 0.3357 -0.0070 0.0068  -0.0302 119  ALA A N   
771   C CA  . ALA A 121  ? 0.4049 0.6442 0.3726 -0.0079 0.0083  -0.0276 119  ALA A CA  
772   C C   . ALA A 121  ? 0.3947 0.6237 0.3645 -0.0080 0.0095  -0.0257 119  ALA A C   
773   O O   . ALA A 121  ? 0.3895 0.6263 0.3594 -0.0066 0.0105  -0.0290 119  ALA A O   
774   C CB  . ALA A 121  ? 0.3903 0.6394 0.3557 -0.0118 0.0086  -0.0177 119  ALA A CB  
775   N N   . LEU A 122  ? 0.3852 0.5969 0.3566 -0.0096 0.0093  -0.0207 120  LEU A N   
776   C CA  . LEU A 122  ? 0.3467 0.5480 0.3200 -0.0096 0.0101  -0.0191 120  LEU A CA  
777   C C   . LEU A 122  ? 0.3989 0.5960 0.3746 -0.0057 0.0100  -0.0285 120  LEU A C   
778   O O   . LEU A 122  ? 0.3731 0.5718 0.3496 -0.0048 0.0109  -0.0298 120  LEU A O   
779   C CB  . LEU A 122  ? 0.3543 0.5382 0.3289 -0.0116 0.0098  -0.0129 120  LEU A CB  
780   C CG  . LEU A 122  ? 0.3760 0.5498 0.3521 -0.0123 0.0106  -0.0098 120  LEU A CG  
781   C CD1 . LEU A 122  ? 0.4432 0.6275 0.4182 -0.0151 0.0115  -0.0032 120  LEU A CD1 
782   C CD2 . LEU A 122  ? 0.4010 0.5573 0.3785 -0.0133 0.0100  -0.0057 120  LEU A CD2 
783   N N   . ILE A 123  ? 0.3569 0.5486 0.3341 -0.0032 0.0087  -0.0352 121  ILE A N   
784   C CA  . ILE A 123  ? 0.3347 0.5219 0.3150 0.0006  0.0081  -0.0442 121  ILE A CA  
785   C C   . ILE A 123  ? 0.3818 0.5857 0.3615 0.0028  0.0085  -0.0502 121  ILE A C   
786   O O   . ILE A 123  ? 0.3394 0.5426 0.3208 0.0047  0.0091  -0.0536 121  ILE A O   
787   C CB  . ILE A 123  ? 0.3271 0.5065 0.3097 0.0024  0.0062  -0.0497 121  ILE A CB  
788   C CG1 . ILE A 123  ? 0.3100 0.4717 0.2940 0.0007  0.0059  -0.0445 121  ILE A CG1 
789   C CG2 . ILE A 123  ? 0.3255 0.5040 0.3117 0.0065  0.0051  -0.0599 121  ILE A CG2 
790   C CD1 . ILE A 123  ? 0.3225 0.4784 0.3082 0.0015  0.0042  -0.0477 121  ILE A CD1 
791   N N   . ARG A 124  ? 0.3382 0.5577 0.3153 0.0028  0.0083  -0.0519 122  ARG A N   
792   C CA  . ARG A 124  ? 0.4350 0.6713 0.4118 0.0055  0.0085  -0.0588 122  ARG A CA  
793   C C   . ARG A 124  ? 0.4333 0.6773 0.4100 0.0038  0.0100  -0.0532 122  ARG A C   
794   O O   . ARG A 124  ? 0.4776 0.7265 0.4572 0.0063  0.0099  -0.0580 122  ARG A O   
795   C CB  . ARG A 124  ? 0.4058 0.6540 0.3827 0.0056  0.0071  -0.0602 122  ARG A CB  
796   N N   . ASP A 125  ? 0.4486 0.6935 0.4227 -0.0003 0.0112  -0.0431 123  ASP A N   
797   C CA  . ASP A 125  ? 0.5000 0.7542 0.4746 -0.0024 0.0120  -0.0371 123  ASP A CA  
798   C C   . ASP A 125  ? 0.5096 0.7547 0.4840 -0.0038 0.0136  -0.0327 123  ASP A C   
799   O O   . ASP A 125  ? 0.5609 0.8130 0.5365 -0.0048 0.0141  -0.0297 123  ASP A O   
800   C CB  . ASP A 125  ? 0.5514 0.8143 0.5244 -0.0062 0.0117  -0.0283 123  ASP A CB  
801   C CG  . ASP A 125  ? 0.5648 0.8391 0.5382 -0.0049 0.0103  -0.0322 123  ASP A CG  
802   O OD1 . ASP A 125  ? 0.5754 0.8567 0.5511 -0.0014 0.0096  -0.0407 123  ASP A OD1 
803   O OD2 . ASP A 125  ? 0.6016 0.8778 0.5734 -0.0074 0.0098  -0.0267 123  ASP A OD2 
804   N N   . LYS A 126  ? 0.4430 0.6705 0.4181 -0.0041 0.0134  -0.0317 124  LYS A N   
805   C CA  . LYS A 126  ? 0.4714 0.6881 0.4480 -0.0057 0.0140  -0.0264 124  LYS A CA  
806   C C   . LYS A 126  ? 0.4602 0.6606 0.4398 -0.0029 0.0134  -0.0317 124  LYS A C   
807   O O   . LYS A 126  ? 0.5368 0.7350 0.5180 -0.0020 0.0140  -0.0327 124  LYS A O   
808   C CB  . LYS A 126  ? 0.4824 0.6915 0.4580 -0.0099 0.0138  -0.0163 124  LYS A CB  
809   N N   . ILE A 127  ? 0.4342 0.6237 0.4149 -0.0016 0.0122  -0.0348 125  ILE A N   
810   C CA  . ILE A 127  ? 0.3710 0.5443 0.3548 0.0005  0.0115  -0.0384 125  ILE A CA  
811   C C   . ILE A 127  ? 0.4355 0.6130 0.4217 0.0046  0.0110  -0.0478 125  ILE A C   
812   O O   . ILE A 127  ? 0.3915 0.5623 0.3800 0.0060  0.0112  -0.0494 125  ILE A O   
813   C CB  . ILE A 127  ? 0.3225 0.4837 0.3070 0.0005  0.0102  -0.0386 125  ILE A CB  
814   C CG1 . ILE A 127  ? 0.4049 0.5635 0.3871 -0.0033 0.0104  -0.0298 125  ILE A CG1 
815   C CG2 . ILE A 127  ? 0.3276 0.4720 0.3152 0.0021  0.0096  -0.0406 125  ILE A CG2 
816   C CD1 . ILE A 127  ? 0.4469 0.5971 0.4291 -0.0056 0.0112  -0.0226 125  ILE A CD1 
817   N N   . ALA A 128  ? 0.3180 0.5068 0.3040 0.0068  0.0104  -0.0544 126  ALA A N   
818   C CA  . ALA A 128  ? 0.3770 0.5684 0.3662 0.0111  0.0094  -0.0644 126  ALA A CA  
819   C C   . ALA A 128  ? 0.4718 0.6741 0.4612 0.0122  0.0107  -0.0659 126  ALA A C   
820   O O   . ALA A 128  ? 0.4093 0.6075 0.4021 0.0152  0.0102  -0.0714 126  ALA A O   
821   C CB  . ALA A 128  ? 0.3473 0.5486 0.3365 0.0132  0.0081  -0.0715 126  ALA A CB  
822   N N   . ASP A 129  ? 0.6144 0.8310 0.6004 0.0098  0.0123  -0.0609 127  ASP A N   
823   C CA  . ASP A 129  ? 0.6639 0.8934 0.6504 0.0107  0.0132  -0.0621 127  ASP A CA  
824   C C   . ASP A 129  ? 0.6802 0.9026 0.6675 0.0095  0.0144  -0.0576 127  ASP A C   
825   O O   . ASP A 129  ? 0.7502 0.9812 0.7388 0.0105  0.0150  -0.0590 127  ASP A O   
826   C CB  . ASP A 129  ? 0.6611 0.9060 0.6459 0.0080  0.0133  -0.0566 127  ASP A CB  
827   N N   . GLY A 130  ? 0.6036 0.8093 0.5912 0.0072  0.0141  -0.0517 128  GLY A N   
828   C CA  . GLY A 130  ? 0.6888 0.8865 0.6777 0.0063  0.0147  -0.0479 128  GLY A CA  
829   C C   . GLY A 130  ? 0.6645 0.8441 0.6535 0.0040  0.0143  -0.0418 128  GLY A C   
830   O O   . GLY A 130  ? 0.6231 0.7900 0.6135 0.0054  0.0131  -0.0443 128  GLY A O   
831   N N   . ASN A 131  ? 0.7461 0.9248 0.7339 0.0005  0.0151  -0.0337 129  ASN A N   
832   C CA  . ASN A 131  ? 0.7183 0.8806 0.7064 -0.0014 0.0147  -0.0282 129  ASN A CA  
833   C C   . ASN A 131  ? 0.6892 0.8454 0.6756 -0.0033 0.0142  -0.0246 129  ASN A C   
834   O O   . ASN A 131  ? 0.7322 0.8965 0.7167 -0.0061 0.0145  -0.0195 129  ASN A O   
835   C CB  . ASN A 131  ? 0.7743 0.9383 0.7621 -0.0045 0.0155  -0.0212 129  ASN A CB  
836   C CG  . ASN A 131  ? 0.8363 1.0173 0.8225 -0.0071 0.0163  -0.0171 129  ASN A CG  
837   O OD1 . ASN A 131  ? 0.9052 1.0998 0.8917 -0.0060 0.0171  -0.0199 129  ASN A OD1 
838   N ND2 . ASN A 131  ? 0.8282 1.0088 0.8126 -0.0104 0.0161  -0.0103 129  ASN A ND2 
839   N N   . TRP A 132  ? 0.5906 0.7331 0.5782 -0.0018 0.0132  -0.0270 130  TRP A N   
840   C CA  . TRP A 132  ? 0.5056 0.6400 0.4921 -0.0036 0.0127  -0.0230 130  TRP A CA  
841   C C   . TRP A 132  ? 0.4907 0.6171 0.4765 -0.0068 0.0129  -0.0149 130  TRP A C   
842   O O   . TRP A 132  ? 0.5002 0.6234 0.4849 -0.0089 0.0126  -0.0103 130  TRP A O   
843   C CB  . TRP A 132  ? 0.4266 0.5487 0.4151 -0.0011 0.0117  -0.0278 130  TRP A CB  
844   C CG  . TRP A 132  ? 0.3753 0.4867 0.3660 0.0006  0.0116  -0.0293 130  TRP A CG  
845   C CD1 . TRP A 132  ? 0.3563 0.4694 0.3494 0.0035  0.0113  -0.0353 130  TRP A CD1 
846   C CD2 . TRP A 132  ? 0.3103 0.4084 0.3011 -0.0006 0.0116  -0.0246 130  TRP A CD2 
847   N NE1 . TRP A 132  ? 0.3109 0.4124 0.3055 0.0041  0.0111  -0.0342 130  TRP A NE1 
848   C CE2 . TRP A 132  ? 0.3116 0.4040 0.3046 0.0016  0.0114  -0.0279 130  TRP A CE2 
849   C CE3 . TRP A 132  ? 0.3562 0.4469 0.3456 -0.0032 0.0117  -0.0183 130  TRP A CE3 
850   C CZ2 . TRP A 132  ? 0.2721 0.3523 0.2655 0.0013  0.0113  -0.0248 130  TRP A CZ2 
851   C CZ3 . TRP A 132  ? 0.3096 0.3882 0.2996 -0.0033 0.0116  -0.0157 130  TRP A CZ3 
852   C CH2 . TRP A 132  ? 0.2986 0.3723 0.2904 -0.0012 0.0115  -0.0190 130  TRP A CH2 
853   N N   . LYS A 133  ? 0.5427 0.6658 0.5295 -0.0070 0.0133  -0.0134 131  LYS A N   
854   C CA  . LYS A 133  ? 0.5940 0.7076 0.5806 -0.0095 0.0131  -0.0068 131  LYS A CA  
855   C C   . LYS A 133  ? 0.6761 0.7973 0.6616 -0.0132 0.0131  0.0003  131  LYS A C   
856   O O   . LYS A 133  ? 0.7122 0.8257 0.6975 -0.0153 0.0126  0.0055  131  LYS A O   
857   C CB  . LYS A 133  ? 0.5377 0.6476 0.5258 -0.0088 0.0133  -0.0073 131  LYS A CB  
858   C CG  . LYS A 133  ? 0.5464 0.6509 0.5361 -0.0050 0.0131  -0.0142 131  LYS A CG  
859   C CD  . LYS A 133  ? 0.5135 0.6119 0.5045 -0.0045 0.0130  -0.0139 131  LYS A CD  
860   C CE  . LYS A 133  ? 0.4489 0.5413 0.4420 -0.0008 0.0126  -0.0202 131  LYS A CE  
861   N NZ  . LYS A 133  ? 0.3712 0.4547 0.3653 -0.0002 0.0123  -0.0193 131  LYS A NZ  
862   N N   . SER A 134  ? 0.6938 0.8302 0.6787 -0.0141 0.0138  0.0006  132  SER A N   
863   C CA  . SER A 134  ? 0.6711 0.8158 0.6554 -0.0179 0.0137  0.0080  132  SER A CA  
864   C C   . SER A 134  ? 0.6694 0.8149 0.6523 -0.0191 0.0131  0.0105  132  SER A C   
865   O O   . SER A 134  ? 0.6553 0.8040 0.6381 -0.0224 0.0126  0.0176  132  SER A O   
866   C CB  . SER A 134  ? 0.6700 0.8324 0.6540 -0.0183 0.0146  0.0076  132  SER A CB  
867   N N   . HIS A 135  ? 0.6555 0.7982 0.6377 -0.0165 0.0130  0.0050  133  HIS A N   
868   C CA  . HIS A 135  ? 0.6478 0.7934 0.6288 -0.0175 0.0124  0.0067  133  HIS A CA  
869   C C   . HIS A 135  ? 0.6691 0.7996 0.6505 -0.0170 0.0116  0.0069  133  HIS A C   
870   O O   . HIS A 135  ? 0.6547 0.7858 0.6354 -0.0183 0.0110  0.0099  133  HIS A O   
871   C CB  . HIS A 135  ? 0.6259 0.7836 0.6057 -0.0152 0.0127  0.0001  133  HIS A CB  
872   C CG  . HIS A 135  ? 0.6520 0.8265 0.6310 -0.0154 0.0136  -0.0005 133  HIS A CG  
873   N ND1 . HIS A 135  ? 0.6422 0.8198 0.6222 -0.0129 0.0143  -0.0063 133  HIS A ND1 
874   C CD2 . HIS A 135  ? 0.6461 0.8356 0.6237 -0.0179 0.0140  0.0041  133  HIS A CD2 
875   C CE1 . HIS A 135  ? 0.6484 0.8425 0.6276 -0.0136 0.0152  -0.0054 133  HIS A CE1 
876   N NE2 . HIS A 135  ? 0.6769 0.8788 0.6545 -0.0168 0.0150  0.0010  133  HIS A NE2 
877   N N   . LEU A 136  ? 0.6188 0.7366 0.6016 -0.0151 0.0116  0.0040  134  LEU A N   
878   C CA  . LEU A 136  ? 0.6244 0.7285 0.6078 -0.0145 0.0110  0.0042  134  LEU A CA  
879   C C   . LEU A 136  ? 0.6296 0.7213 0.6141 -0.0140 0.0111  0.0050  134  LEU A C   
880   O O   . LEU A 136  ? 0.6216 0.7149 0.6066 -0.0136 0.0115  0.0040  134  LEU A O   
881   C CB  . LEU A 136  ? 0.5436 0.6463 0.5273 -0.0117 0.0108  -0.0025 134  LEU A CB  
882   C CG  . LEU A 136  ? 0.5547 0.6673 0.5373 -0.0118 0.0104  -0.0039 134  LEU A CG  
883   C CD1 . LEU A 136  ? 0.4884 0.5992 0.4723 -0.0087 0.0099  -0.0116 134  LEU A CD1 
884   C CD2 . LEU A 136  ? 0.5703 0.6796 0.5524 -0.0141 0.0098  0.0020  134  LEU A CD2 
885   N N   . GLY A 137  ? 0.5728 0.6526 0.5578 -0.0140 0.0107  0.0067  135  GLY A N   
886   C CA  . GLY A 137  ? 0.5145 0.5825 0.5003 -0.0131 0.0107  0.0067  135  GLY A CA  
887   C C   . GLY A 137  ? 0.5492 0.6155 0.5353 -0.0152 0.0105  0.0116  135  GLY A C   
888   O O   . GLY A 137  ? 0.5630 0.6232 0.5497 -0.0143 0.0106  0.0106  135  GLY A O   
889   N N   . GLY A 138  ? 0.5321 0.6034 0.5182 -0.0180 0.0099  0.0171  136  GLY A N   
890   C CA  . GLY A 138  ? 0.5561 0.6255 0.5432 -0.0203 0.0093  0.0222  136  GLY A CA  
891   C C   . GLY A 138  ? 0.4999 0.5559 0.4879 -0.0202 0.0085  0.0242  136  GLY A C   
892   O O   . GLY A 138  ? 0.5265 0.5749 0.5145 -0.0187 0.0087  0.0219  136  GLY A O   
893   N N   . SER A 139  ? 0.3845 0.4378 0.3730 -0.0217 0.0076  0.0283  137  SER A N   
894   C CA  . SER A 139  ? 0.3130 0.3543 0.3025 -0.0214 0.0068  0.0299  137  SER A CA  
895   C C   . SER A 139  ? 0.3309 0.3641 0.3196 -0.0184 0.0076  0.0253  137  SER A C   
896   O O   . SER A 139  ? 0.3638 0.3874 0.3528 -0.0174 0.0074  0.0252  137  SER A O   
897   C CB  . SER A 139  ? 0.3903 0.4311 0.3811 -0.0234 0.0055  0.0350  137  SER A CB  
898   O OG  . SER A 139  ? 0.4027 0.4491 0.3952 -0.0264 0.0043  0.0403  137  SER A OG  
899   N N   . ARG A 140  ? 0.2703 0.3073 0.2580 -0.0170 0.0085  0.0216  138  ARG A N   
900   C CA  . ARG A 140  ? 0.2695 0.2994 0.2569 -0.0144 0.0091  0.0177  138  ARG A CA  
901   C C   . ARG A 140  ? 0.2791 0.3126 0.2662 -0.0126 0.0099  0.0125  138  ARG A C   
902   O O   . ARG A 140  ? 0.2703 0.3132 0.2571 -0.0127 0.0101  0.0108  138  ARG A O   
903   C CB  . ARG A 140  ? 0.3118 0.3419 0.2994 -0.0145 0.0089  0.0182  138  ARG A CB  
904   C CG  . ARG A 140  ? 0.3403 0.3653 0.3281 -0.0121 0.0095  0.0142  138  ARG A CG  
905   C CD  . ARG A 140  ? 0.3758 0.4039 0.3640 -0.0125 0.0091  0.0146  138  ARG A CD  
906   N NE  . ARG A 140  ? 0.3637 0.3870 0.3528 -0.0107 0.0095  0.0113  138  ARG A NE  
907   C CZ  . ARG A 140  ? 0.3701 0.3968 0.3597 -0.0094 0.0096  0.0067  138  ARG A CZ  
908   N NH1 . ARG A 140  ? 0.3511 0.3858 0.3401 -0.0093 0.0096  0.0041  138  ARG A NH1 
909   N NH2 . ARG A 140  ? 0.3910 0.4130 0.3821 -0.0081 0.0095  0.0045  138  ARG A NH2 
910   N N   . SER A 141  ? 0.2446 0.2711 0.2320 -0.0107 0.0102  0.0100  139  SER A N   
911   C CA  . SER A 141  ? 0.2058 0.2344 0.1935 -0.0087 0.0107  0.0050  139  SER A CA  
912   C C   . SER A 141  ? 0.2013 0.2331 0.1897 -0.0077 0.0107  0.0018  139  SER A C   
913   O O   . SER A 141  ? 0.2141 0.2419 0.2027 -0.0077 0.0106  0.0027  139  SER A O   
914   C CB  . SER A 141  ? 0.2184 0.2378 0.2066 -0.0068 0.0109  0.0035  139  SER A CB  
915   O OG  . SER A 141  ? 0.1965 0.2168 0.1858 -0.0047 0.0110  -0.0012 139  SER A OG  
916   N N   . LEU A 142  ? 0.1928 0.2321 0.1816 -0.0066 0.0108  -0.0023 140  LEU A N   
917   C CA  A LEU A 142  ? 0.1950 0.2364 0.1849 -0.0053 0.0105  -0.0064 140  LEU A CA  
918   C CA  B LEU A 142  ? 0.1951 0.2366 0.1850 -0.0053 0.0105  -0.0064 140  LEU A CA  
919   C C   . LEU A 142  ? 0.2102 0.2417 0.2019 -0.0035 0.0103  -0.0082 140  LEU A C   
920   O O   . LEU A 142  ? 0.1934 0.2242 0.1863 -0.0030 0.0098  -0.0102 140  LEU A O   
921   C CB  A LEU A 142  ? 0.1980 0.2483 0.1886 -0.0039 0.0104  -0.0115 140  LEU A CB  
922   C CB  B LEU A 142  ? 0.1981 0.2484 0.1886 -0.0039 0.0104  -0.0114 140  LEU A CB  
923   C CG  A LEU A 142  ? 0.2359 0.2991 0.2250 -0.0052 0.0106  -0.0110 140  LEU A CG  
924   C CG  B LEU A 142  ? 0.2085 0.2691 0.1989 -0.0038 0.0100  -0.0142 140  LEU A CG  
925   C CD1 A LEU A 142  ? 0.2520 0.3232 0.2423 -0.0030 0.0103  -0.0175 140  LEU A CD1 
926   C CD1 B LEU A 142  ? 0.2646 0.3339 0.2527 -0.0065 0.0103  -0.0097 140  LEU A CD1 
927   C CD2 A LEU A 142  ? 0.2738 0.3410 0.2615 -0.0072 0.0104  -0.0075 140  LEU A CD2 
928   C CD2 B LEU A 142  ? 0.2132 0.2801 0.2050 -0.0016 0.0098  -0.0203 140  LEU A CD2 
929   N N   . PHE A 143  ? 0.1630 0.1871 0.1549 -0.0028 0.0105  -0.0075 141  PHE A N   
930   C CA  . PHE A 143  ? 0.1755 0.1916 0.1694 -0.0010 0.0103  -0.0095 141  PHE A CA  
931   C C   . PHE A 143  ? 0.1861 0.1935 0.1796 -0.0014 0.0107  -0.0058 141  PHE A C   
932   O O   . PHE A 143  ? 0.1967 0.1974 0.1914 -0.0001 0.0107  -0.0063 141  PHE A O   
933   C CB  . PHE A 143  ? 0.1632 0.1784 0.1579 0.0005  0.0103  -0.0117 141  PHE A CB  
934   C CG  . PHE A 143  ? 0.1558 0.1804 0.1511 0.0011  0.0100  -0.0154 141  PHE A CG  
935   C CD1 . PHE A 143  ? 0.1573 0.1863 0.1546 0.0024  0.0093  -0.0201 141  PHE A CD1 
936   C CD2 . PHE A 143  ? 0.1660 0.1956 0.1599 0.0004  0.0104  -0.0144 141  PHE A CD2 
937   C CE1 . PHE A 143  ? 0.1590 0.1975 0.1568 0.0032  0.0091  -0.0240 141  PHE A CE1 
938   C CE2 . PHE A 143  ? 0.1593 0.1985 0.1536 0.0011  0.0103  -0.0178 141  PHE A CE2 
939   C CZ  . PHE A 143  ? 0.1466 0.1906 0.1427 0.0026  0.0097  -0.0228 141  PHE A CZ  
940   N N   . VAL A 144  ? 0.1824 0.1903 0.1744 -0.0031 0.0108  -0.0022 142  VAL A N   
941   C CA  A VAL A 144  ? 0.2033 0.2037 0.1949 -0.0033 0.0112  0.0011  142  VAL A CA  
942   C CA  B VAL A 144  ? 0.2034 0.2037 0.1951 -0.0032 0.0112  0.0010  142  VAL A CA  
943   C C   . VAL A 144  ? 0.2147 0.2102 0.2084 -0.0020 0.0112  -0.0003 142  VAL A C   
944   O O   . VAL A 144  ? 0.2133 0.2022 0.2072 -0.0013 0.0116  0.0011  142  VAL A O   
945   C CB  A VAL A 144  ? 0.2020 0.2047 0.1925 -0.0052 0.0110  0.0046  142  VAL A CB  
946   C CB  B VAL A 144  ? 0.2037 0.2058 0.1941 -0.0051 0.0111  0.0048  142  VAL A CB  
947   C CG1 A VAL A 144  ? 0.2187 0.2145 0.2095 -0.0050 0.0112  0.0071  142  VAL A CG1 
948   C CG1 B VAL A 144  ? 0.2243 0.2297 0.2133 -0.0065 0.0109  0.0070  142  VAL A CG1 
949   C CG2 A VAL A 144  ? 0.2233 0.2290 0.2124 -0.0066 0.0108  0.0071  142  VAL A CG2 
950   C CG2 B VAL A 144  ? 0.2325 0.2406 0.2235 -0.0058 0.0107  0.0039  142  VAL A CG2 
951   N N   . ASN A 145  ? 0.1992 0.1983 0.1947 -0.0018 0.0106  -0.0031 143  ASN A N   
952   C CA  . ASN A 145  ? 0.1905 0.1853 0.1886 -0.0009 0.0103  -0.0042 143  ASN A CA  
953   C C   . ASN A 145  ? 0.1960 0.1899 0.1971 0.0007  0.0096  -0.0081 143  ASN A C   
954   O O   . ASN A 145  ? 0.1916 0.1839 0.1958 0.0012  0.0089  -0.0099 143  ASN A O   
955   C CB  . ASN A 145  ? 0.1841 0.1826 0.1831 -0.0018 0.0098  -0.0044 143  ASN A CB  
956   C CG  . ASN A 145  ? 0.2408 0.2383 0.2381 -0.0031 0.0103  -0.0001 143  ASN A CG  
957   O OD1 . ASN A 145  ? 0.2556 0.2470 0.2527 -0.0029 0.0110  0.0025  143  ASN A OD1 
958   N ND2 . ASN A 145  ? 0.2524 0.2562 0.2485 -0.0044 0.0100  0.0007  143  ASN A ND2 
959   N N   . ALA A 146  ? 0.1760 0.1706 0.1764 0.0015  0.0097  -0.0094 144  ALA A N   
960   C CA  . ALA A 146  ? 0.1839 0.1778 0.1875 0.0031  0.0087  -0.0133 144  ALA A CA  
961   C C   . ALA A 146  ? 0.1860 0.1722 0.1924 0.0040  0.0085  -0.0123 144  ALA A C   
962   O O   . ALA A 146  ? 0.2002 0.1853 0.2105 0.0052  0.0072  -0.0153 144  ALA A O   
963   C CB  . ALA A 146  ? 0.1872 0.1838 0.1897 0.0039  0.0088  -0.0146 144  ALA A CB  
964   N N   . ALA A 147  ? 0.1696 0.1507 0.1744 0.0035  0.0095  -0.0081 145  ALA A N   
965   C CA  . ALA A 147  ? 0.2214 0.1964 0.2290 0.0042  0.0093  -0.0067 145  ALA A CA  
966   C C   . ALA A 147  ? 0.2177 0.1925 0.2289 0.0039  0.0085  -0.0078 145  ALA A C   
967   O O   . ALA A 147  ? 0.2339 0.2055 0.2493 0.0046  0.0074  -0.0086 145  ALA A O   
968   C CB  . ALA A 147  ? 0.2326 0.2033 0.2375 0.0039  0.0107  -0.0023 145  ALA A CB  
969   N N   . THR A 148  ? 0.1893 0.1676 0.1992 0.0028  0.0087  -0.0076 146  THR A N   
970   C CA  . THR A 148  ? 0.1927 0.1716 0.2061 0.0023  0.0077  -0.0089 146  THR A CA  
971   C C   . THR A 148  ? 0.1733 0.1553 0.1901 0.0032  0.0059  -0.0142 146  THR A C   
972   O O   . THR A 148  ? 0.1983 0.1776 0.2200 0.0037  0.0045  -0.0158 146  THR A O   
973   C CB  . THR A 148  ? 0.2374 0.2200 0.2483 0.0010  0.0083  -0.0074 146  THR A CB  
974   O OG1 . THR A 148  ? 0.2421 0.2214 0.2501 0.0005  0.0097  -0.0029 146  THR A OG1 
975   C CG2 . THR A 148  ? 0.2778 0.2609 0.2921 0.0005  0.0073  -0.0084 146  THR A CG2 
976   N N   . TRP A 149  ? 0.1812 0.1692 0.1959 0.0035  0.0057  -0.0171 147  TRP A N   
977   C CA  . TRP A 149  ? 0.1959 0.1877 0.2140 0.0047  0.0040  -0.0228 147  TRP A CA  
978   C C   . TRP A 149  ? 0.1688 0.1558 0.1907 0.0063  0.0029  -0.0244 147  TRP A C   
979   O O   . TRP A 149  ? 0.1847 0.1719 0.2115 0.0074  0.0009  -0.0287 147  TRP A O   
980   C CB  . TRP A 149  ? 0.1714 0.1717 0.1862 0.0048  0.0043  -0.0253 147  TRP A CB  
981   C CG  . TRP A 149  ? 0.1749 0.1808 0.1868 0.0032  0.0048  -0.0240 147  TRP A CG  
982   C CD1 . TRP A 149  ? 0.1934 0.2024 0.2007 0.0018  0.0062  -0.0203 147  TRP A CD1 
983   C CD2 . TRP A 149  ? 0.1771 0.1861 0.1909 0.0028  0.0036  -0.0261 147  TRP A CD2 
984   N NE1 . TRP A 149  ? 0.1954 0.2095 0.2017 0.0006  0.0060  -0.0198 147  TRP A NE1 
985   C CE2 . TRP A 149  ? 0.1960 0.2103 0.2059 0.0012  0.0045  -0.0234 147  TRP A CE2 
986   C CE3 . TRP A 149  ? 0.1890 0.1968 0.2078 0.0036  0.0017  -0.0301 147  TRP A CE3 
987   C CZ2 . TRP A 149  ? 0.1849 0.2036 0.1953 0.0005  0.0037  -0.0245 147  TRP A CZ2 
988   C CZ3 . TRP A 149  ? 0.2500 0.2621 0.2694 0.0029  0.0008  -0.0315 147  TRP A CZ3 
989   C CH2 . TRP A 149  ? 0.2653 0.2830 0.2803 0.0014  0.0019  -0.0286 147  TRP A CH2 
990   N N   . GLY A 150  ? 0.1773 0.1603 0.1975 0.0065  0.0040  -0.0212 148  GLY A N   
991   C CA  . GLY A 150  ? 0.1916 0.1696 0.2156 0.0079  0.0030  -0.0217 148  GLY A CA  
992   C C   . GLY A 150  ? 0.1987 0.1712 0.2280 0.0078  0.0017  -0.0207 148  GLY A C   
993   O O   . GLY A 150  ? 0.2124 0.1827 0.2473 0.0089  -0.0003 -0.0234 148  GLY A O   
994   N N   . LEU A 151  ? 0.2207 0.1912 0.2488 0.0063  0.0028  -0.0167 149  LEU A N   
995   C CA  . LEU A 151  ? 0.2452 0.2114 0.2787 0.0058  0.0016  -0.0155 149  LEU A CA  
996   C C   . LEU A 151  ? 0.2228 0.1916 0.2611 0.0061  -0.0007 -0.0205 149  LEU A C   
997   O O   . LEU A 151  ? 0.2700 0.2352 0.3147 0.0065  -0.0029 -0.0218 149  LEU A O   
998   C CB  . LEU A 151  ? 0.2480 0.2129 0.2791 0.0043  0.0033  -0.0106 149  LEU A CB  
999   C CG  . LEU A 151  ? 0.3097 0.2701 0.3396 0.0043  0.0047  -0.0053 149  LEU A CG  
1000  C CD1 . LEU A 151  ? 0.3149 0.2755 0.3420 0.0031  0.0065  -0.0014 149  LEU A CD1 
1001  C CD2 . LEU A 151  ? 0.2606 0.2164 0.2968 0.0045  0.0032  -0.0041 149  LEU A CD2 
1002  N N   . VAL A 152  ? 0.2164 0.1914 0.2518 0.0057  -0.0005 -0.0234 150  VAL A N   
1003  C CA  . VAL A 152  ? 0.2341 0.2125 0.2735 0.0060  -0.0027 -0.0287 150  VAL A CA  
1004  C C   . VAL A 152  ? 0.2679 0.2466 0.3116 0.0081  -0.0050 -0.0342 150  VAL A C   
1005  O O   . VAL A 152  ? 0.2717 0.2488 0.3219 0.0086  -0.0076 -0.0378 150  VAL A O   
1006  C CB  . VAL A 152  ? 0.2606 0.2469 0.2952 0.0054  -0.0019 -0.0302 150  VAL A CB  
1007  C CG1 . VAL A 152  ? 0.2831 0.2742 0.3212 0.0061  -0.0042 -0.0366 150  VAL A CG1 
1008  C CG2 . VAL A 152  ? 0.2960 0.2814 0.3276 0.0035  -0.0002 -0.0251 150  VAL A CG2 
1009  N N   . VAL A 153  ? 0.2239 0.2048 0.2646 0.0092  -0.0041 -0.0352 151  VAL A N   
1010  C CA  . VAL A 153  ? 0.2449 0.2275 0.2895 0.0114  -0.0062 -0.0411 151  VAL A CA  
1011  C C   . VAL A 153  ? 0.2298 0.2047 0.2802 0.0123  -0.0077 -0.0399 151  VAL A C   
1012  O O   . VAL A 153  ? 0.2809 0.2543 0.3381 0.0138  -0.0106 -0.0445 151  VAL A O   
1013  C CB  . VAL A 153  ? 0.2082 0.1970 0.2474 0.0122  -0.0046 -0.0425 151  VAL A CB  
1014  C CG1 . VAL A 153  ? 0.2444 0.2345 0.2876 0.0148  -0.0065 -0.0480 151  VAL A CG1 
1015  C CG2 . VAL A 153  ? 0.2182 0.2159 0.2529 0.0114  -0.0036 -0.0441 151  VAL A CG2 
1016  N N   . THR A 154  ? 0.2241 0.1940 0.2722 0.0116  -0.0061 -0.0338 152  THR A N   
1017  C CA  . THR A 154  ? 0.2629 0.2266 0.3156 0.0125  -0.0073 -0.0321 152  THR A CA  
1018  C C   . THR A 154  ? 0.2714 0.2286 0.3277 0.0111  -0.0076 -0.0267 152  THR A C   
1019  O O   . THR A 154  ? 0.2955 0.2475 0.3571 0.0117  -0.0092 -0.0253 152  THR A O   
1020  C CB  . THR A 154  ? 0.2689 0.2325 0.3167 0.0130  -0.0054 -0.0293 152  THR A CB  
1021  O OG1 . THR A 154  ? 0.2706 0.2323 0.3131 0.0114  -0.0028 -0.0230 152  THR A OG1 
1022  C CG2 . THR A 154  ? 0.3009 0.2717 0.3443 0.0140  -0.0046 -0.0334 152  THR A CG2 
1023  N N   . GLY A 155  ? 0.2441 0.2017 0.2977 0.0093  -0.0061 -0.0235 153  GLY A N   
1024  C CA  . GLY A 155  ? 0.2442 0.1967 0.3002 0.0078  -0.0058 -0.0177 153  GLY A CA  
1025  C C   . GLY A 155  ? 0.3013 0.2514 0.3531 0.0076  -0.0035 -0.0118 153  GLY A C   
1026  O O   . GLY A 155  ? 0.3024 0.2492 0.3558 0.0066  -0.0030 -0.0066 153  GLY A O   
1027  N N   . LYS A 156  ? 0.2605 0.2126 0.3071 0.0086  -0.0023 -0.0125 154  LYS A N   
1028  C CA  . LYS A 156  ? 0.2834 0.2336 0.3260 0.0086  -0.0004 -0.0076 154  LYS A CA  
1029  C C   . LYS A 156  ? 0.2716 0.2252 0.3063 0.0080  0.0023  -0.0064 154  LYS A C   
1030  O O   . LYS A 156  ? 0.2446 0.2026 0.2765 0.0081  0.0026  -0.0099 154  LYS A O   
1031  C CB  . LYS A 156  ? 0.3544 0.3035 0.3981 0.0103  -0.0014 -0.0089 154  LYS A CB  
1032  N N   . LEU A 157  ? 0.2453 0.1971 0.2766 0.0074  0.0042  -0.0014 155  LEU A N   
1033  C CA  . LEU A 157  ? 0.2425 0.1967 0.2671 0.0069  0.0064  0.0001  155  LEU A CA  
1034  C C   . LEU A 157  ? 0.2402 0.1943 0.2609 0.0079  0.0071  0.0006  155  LEU A C   
1035  O O   . LEU A 157  ? 0.3104 0.2616 0.3320 0.0085  0.0070  0.0033  155  LEU A O   
1036  C CB  . LEU A 157  ? 0.2566 0.2094 0.2799 0.0060  0.0080  0.0047  155  LEU A CB  
1037  C CG  . LEU A 157  ? 0.2478 0.2022 0.2647 0.0057  0.0101  0.0063  155  LEU A CG  
1038  C CD1 . LEU A 157  ? 0.2622 0.2204 0.2769 0.0050  0.0101  0.0035  155  LEU A CD1 
1039  C CD2 . LEU A 157  ? 0.2693 0.2224 0.2858 0.0052  0.0114  0.0105  155  LEU A CD2 
1040  N N   . THR A 158  ? 0.2662 0.2238 0.2831 0.0079  0.0077  -0.0017 156  THR A N   
1041  C CA  . THR A 158  ? 0.2973 0.2555 0.3100 0.0085  0.0085  -0.0011 156  THR A CA  
1042  C C   . THR A 158  ? 0.3070 0.2668 0.3145 0.0074  0.0101  0.0006  156  THR A C   
1043  O O   . THR A 158  ? 0.3037 0.2670 0.3102 0.0066  0.0102  -0.0012 156  THR A O   
1044  C CB  . THR A 158  ? 0.3163 0.2777 0.3298 0.0093  0.0074  -0.0053 156  THR A CB  
1045  O OG1 . THR A 158  ? 0.3409 0.3004 0.3602 0.0104  0.0055  -0.0072 156  THR A OG1 
1046  C CG2 . THR A 158  ? 0.3231 0.2850 0.3329 0.0098  0.0080  -0.0045 156  THR A CG2 
1047  N N   . SER A 159  ? 0.2810 0.2386 0.2854 0.0076  0.0112  0.0039  157  SER A N   
1048  C CA  . SER A 159  ? 0.2532 0.2114 0.2539 0.0068  0.0125  0.0057  157  SER A CA  
1049  C C   . SER A 159  ? 0.2987 0.2601 0.2963 0.0062  0.0126  0.0042  157  SER A C   
1050  O O   . SER A 159  ? 0.2931 0.2558 0.2891 0.0052  0.0131  0.0049  157  SER A O   
1051  C CB  . SER A 159  ? 0.3395 0.2951 0.3378 0.0075  0.0135  0.0088  157  SER A CB  
1052  O OG  . SER A 159  ? 0.3237 0.2789 0.3203 0.0083  0.0132  0.0085  157  SER A OG  
1053  N N   . THR A 160  ? 0.2677 0.2304 0.2646 0.0067  0.0121  0.0026  158  THR A N   
1054  C CA  . THR A 160  ? 0.2515 0.2179 0.2462 0.0059  0.0120  0.0015  158  THR A CA  
1055  C C   . THR A 160  ? 0.2295 0.2001 0.2264 0.0060  0.0112  -0.0020 158  THR A C   
1056  O O   . THR A 160  ? 0.2392 0.2089 0.2393 0.0071  0.0104  -0.0038 158  THR A O   
1057  C CB  . THR A 160  ? 0.2605 0.2258 0.2522 0.0061  0.0122  0.0026  158  THR A CB  
1058  O OG1 . THR A 160  ? 0.2921 0.2564 0.2851 0.0075  0.0116  0.0017  158  THR A OG1 
1059  C CG2 . THR A 160  ? 0.3221 0.2839 0.3116 0.0063  0.0130  0.0053  158  THR A CG2 
1060  N N   . VAL A 161  ? 0.1794 0.1548 0.1747 0.0050  0.0112  -0.0029 159  VAL A N   
1061  C CA  . VAL A 161  ? 0.1859 0.1671 0.1828 0.0050  0.0106  -0.0062 159  VAL A CA  
1062  C C   . VAL A 161  ? 0.1681 0.1521 0.1644 0.0055  0.0103  -0.0076 159  VAL A C   
1063  O O   . VAL A 161  ? 0.1609 0.1460 0.1547 0.0046  0.0107  -0.0058 159  VAL A O   
1064  C CB  . VAL A 161  ? 0.2083 0.1942 0.2038 0.0033  0.0109  -0.0058 159  VAL A CB  
1065  C CG1 . VAL A 161  ? 0.2168 0.2103 0.2133 0.0034  0.0104  -0.0092 159  VAL A CG1 
1066  C CG2 . VAL A 161  ? 0.2410 0.2244 0.2373 0.0029  0.0110  -0.0046 159  VAL A CG2 
1067  N N   . ASN A 162  ? 0.1618 0.1475 0.1611 0.0070  0.0094  -0.0110 160  ASN A N   
1068  C CA  . ASN A 162  ? 0.1556 0.1452 0.1546 0.0076  0.0092  -0.0126 160  ASN A CA  
1069  C C   . ASN A 162  ? 0.1504 0.1486 0.1490 0.0067  0.0093  -0.0146 160  ASN A C   
1070  O O   . ASN A 162  ? 0.1453 0.1479 0.1464 0.0077  0.0087  -0.0185 160  ASN A O   
1071  C CB  . ASN A 162  ? 0.1818 0.1699 0.1843 0.0097  0.0081  -0.0153 160  ASN A CB  
1072  C CG  . ASN A 162  ? 0.1817 0.1738 0.1840 0.0104  0.0079  -0.0168 160  ASN A CG  
1073  O OD1 . ASN A 162  ? 0.1692 0.1673 0.1696 0.0092  0.0084  -0.0168 160  ASN A OD1 
1074  N ND2 . ASN A 162  ? 0.2162 0.2054 0.2209 0.0122  0.0070  -0.0177 160  ASN A ND2 
1075  N N   . ASP A 163  ? 0.1398 0.1406 0.1354 0.0047  0.0100  -0.0117 161  ASP A N   
1076  C CA  . ASP A 163  ? 0.1438 0.1531 0.1388 0.0035  0.0102  -0.0126 161  ASP A CA  
1077  C C   . ASP A 163  ? 0.1286 0.1454 0.1243 0.0041  0.0101  -0.0152 161  ASP A C   
1078  O O   . ASP A 163  ? 0.1499 0.1751 0.1459 0.0038  0.0101  -0.0174 161  ASP A O   
1079  C CB  . ASP A 163  ? 0.1691 0.1789 0.1613 0.0010  0.0107  -0.0082 161  ASP A CB  
1080  C CG  . ASP A 163  ? 0.1993 0.2051 0.1899 0.0002  0.0108  -0.0051 161  ASP A CG  
1081  O OD1 . ASP A 163  ? 0.1713 0.1710 0.1622 0.0016  0.0106  -0.0052 161  ASP A OD1 
1082  O OD2 . ASP A 163  ? 0.1992 0.2082 0.1885 -0.0018 0.0108  -0.0023 161  ASP A OD2 
1083  N N   . ARG A 164  ? 0.1440 0.1586 0.1401 0.0050  0.0098  -0.0154 162  ARG A N   
1084  C CA  . ARG A 164  ? 0.1193 0.1413 0.1167 0.0059  0.0096  -0.0183 162  ARG A CA  
1085  C C   . ARG A 164  ? 0.1337 0.1575 0.1346 0.0085  0.0088  -0.0237 162  ARG A C   
1086  O O   . ARG A 164  ? 0.1408 0.1735 0.1428 0.0092  0.0088  -0.0272 162  ARG A O   
1087  C CB  . ARG A 164  ? 0.1509 0.1703 0.1480 0.0061  0.0095  -0.0169 162  ARG A CB  
1088  C CG  . ARG A 164  ? 0.1794 0.1981 0.1738 0.0036  0.0099  -0.0122 162  ARG A CG  
1089  C CD  . ARG A 164  ? 0.3061 0.3331 0.2994 0.0013  0.0103  -0.0107 162  ARG A CD  
1090  N NE  . ARG A 164  ? 0.2966 0.3342 0.2911 0.0018  0.0105  -0.0137 162  ARG A NE  
1091  C CZ  . ARG A 164  ? 0.3237 0.3697 0.3177 0.0005  0.0110  -0.0137 162  ARG A CZ  
1092  N NH1 . ARG A 164  ? 0.3899 0.4347 0.3824 -0.0013 0.0112  -0.0107 162  ARG A NH1 
1093  N NH2 . ARG A 164  ? 0.2694 0.3258 0.2645 0.0013  0.0112  -0.0168 162  ARG A NH2 
1094  N N   . SER A 165  ? 0.1313 0.1471 0.1343 0.0100  0.0081  -0.0243 163  SER A N   
1095  C CA  . SER A 165  ? 0.1337 0.1499 0.1407 0.0123  0.0069  -0.0293 163  SER A CA  
1096  C C   . SER A 165  ? 0.1137 0.1355 0.1211 0.0120  0.0069  -0.0318 163  SER A C   
1097  O O   . SER A 165  ? 0.1149 0.1428 0.1248 0.0136  0.0061  -0.0369 163  SER A O   
1098  C CB  . SER A 165  ? 0.1351 0.1412 0.1445 0.0134  0.0061  -0.0283 163  SER A CB  
1099  O OG  . SER A 165  ? 0.1521 0.1578 0.1662 0.0153  0.0046  -0.0327 163  SER A OG  
1100  N N   . LEU A 166  ? 0.1445 0.1643 0.1494 0.0099  0.0076  -0.0285 164  LEU A N   
1101  C CA  . LEU A 166  ? 0.1223 0.1476 0.1273 0.0095  0.0075  -0.0306 164  LEU A CA  
1102  C C   . LEU A 166  ? 0.1135 0.1506 0.1167 0.0088  0.0081  -0.0318 164  LEU A C   
1103  O O   . LEU A 166  ? 0.1137 0.1580 0.1180 0.0096  0.0076  -0.0360 164  LEU A O   
1104  C CB  . LEU A 166  ? 0.1239 0.1443 0.1269 0.0075  0.0080  -0.0264 164  LEU A CB  
1105  C CG  . LEU A 166  ? 0.1345 0.1449 0.1400 0.0084  0.0074  -0.0257 164  LEU A CG  
1106  C CD1 . LEU A 166  ? 0.1594 0.1653 0.1625 0.0065  0.0082  -0.0209 164  LEU A CD1 
1107  C CD2 . LEU A 166  ? 0.1429 0.1538 0.1526 0.0099  0.0059  -0.0305 164  LEU A CD2 
1108  N N   . ALA A 167  ? 0.1153 0.1550 0.1157 0.0071  0.0091  -0.0281 165  ALA A N   
1109  C CA  . ALA A 167  ? 0.1296 0.1812 0.1286 0.0062  0.0097  -0.0286 165  ALA A CA  
1110  C C   . ALA A 167  ? 0.1305 0.1889 0.1321 0.0088  0.0092  -0.0345 165  ALA A C   
1111  O O   . ALA A 167  ? 0.1398 0.2089 0.1414 0.0093  0.0093  -0.0377 165  ALA A O   
1112  C CB  . ALA A 167  ? 0.1408 0.1932 0.1372 0.0038  0.0105  -0.0232 165  ALA A CB  
1113  N N   . ALA A 168  ? 0.1204 0.1734 0.1242 0.0107  0.0086  -0.0359 166  ALA A N   
1114  C CA  . ALA A 168  ? 0.1262 0.1849 0.1333 0.0135  0.0079  -0.0418 166  ALA A CA  
1115  C C   . ALA A 168  ? 0.1195 0.1796 0.1297 0.0157  0.0066  -0.0476 166  ALA A C   
1116  O O   . ALA A 168  ? 0.1232 0.1933 0.1348 0.0174  0.0063  -0.0529 166  ALA A O   
1117  C CB  . ALA A 168  ? 0.1199 0.1709 0.1291 0.0150  0.0072  -0.0416 166  ALA A CB  
1118  N N   . ALA A 169  ? 0.1175 0.1681 0.1289 0.0157  0.0058  -0.0469 167  ALA A N   
1119  C CA  . ALA A 169  ? 0.1186 0.1694 0.1336 0.0176  0.0042  -0.0524 167  ALA A CA  
1120  C C   . ALA A 169  ? 0.1188 0.1799 0.1317 0.0167  0.0047  -0.0542 167  ALA A C   
1121  O O   . ALA A 169  ? 0.1245 0.1917 0.1400 0.0188  0.0035  -0.0606 167  ALA A O   
1122  C CB  . ALA A 169  ? 0.1226 0.1613 0.1394 0.0172  0.0034  -0.0501 167  ALA A CB  
1123  N N   . LEU A 170  ? 0.1170 0.1801 0.1254 0.0137  0.0062  -0.0487 168  LEU A N   
1124  C CA  . LEU A 170  ? 0.1173 0.1905 0.1236 0.0127  0.0065  -0.0497 168  LEU A CA  
1125  C C   . LEU A 170  ? 0.1274 0.2147 0.1330 0.0135  0.0071  -0.0529 168  LEU A C   
1126  O O   . LEU A 170  ? 0.1352 0.2319 0.1413 0.0148  0.0065  -0.0580 168  LEU A O   
1127  C CB  . LEU A 170  ? 0.1205 0.1917 0.1228 0.0092  0.0077  -0.0425 168  LEU A CB  
1128  C CG  . LEU A 170  ? 0.1368 0.2176 0.1367 0.0079  0.0080  -0.0424 168  LEU A CG  
1129  C CD1 . LEU A 170  ? 0.1446 0.2241 0.1471 0.0095  0.0065  -0.0474 168  LEU A CD1 
1130  C CD2 . LEU A 170  ? 0.1648 0.2426 0.1614 0.0046  0.0089  -0.0349 168  LEU A CD2 
1131  N N   . THR A 171  ? 0.1314 0.2208 0.1358 0.0129  0.0081  -0.0502 169  THR A N   
1132  C CA  . THR A 171  ? 0.1329 0.2360 0.1372 0.0139  0.0087  -0.0532 169  THR A CA  
1133  C C   . THR A 171  ? 0.1436 0.2497 0.1521 0.0179  0.0073  -0.0619 169  THR A C   
1134  O O   . THR A 171  ? 0.1321 0.2509 0.1408 0.0194  0.0072  -0.0669 169  THR A O   
1135  C CB  . THR A 171  ? 0.1450 0.2479 0.1483 0.0127  0.0097  -0.0491 169  THR A CB  
1136  O OG1 . THR A 171  ? 0.1867 0.2876 0.1864 0.0090  0.0108  -0.0414 169  THR A OG1 
1137  C CG2 . THR A 171  ? 0.1378 0.2550 0.1416 0.0140  0.0103  -0.0526 169  THR A CG2 
1138  N N   . ARG A 172  ? 0.1210 0.2158 0.1333 0.0199  0.0059  -0.0638 170  ARG A N   
1139  C CA  . ARG A 172  ? 0.1266 0.2230 0.1440 0.0239  0.0041  -0.0719 170  ARG A CA  
1140  C C   . ARG A 172  ? 0.1254 0.2254 0.1445 0.0252  0.0027  -0.0775 170  ARG A C   
1141  O O   . ARG A 172  ? 0.1278 0.2381 0.1488 0.0279  0.0020  -0.0846 170  ARG A O   
1142  C CB  . ARG A 172  ? 0.1235 0.2062 0.1450 0.0253  0.0027  -0.0717 170  ARG A CB  
1143  C CG  . ARG A 172  ? 0.1264 0.2103 0.1539 0.0295  0.0007  -0.0794 170  ARG A CG  
1144  C CD  . ARG A 172  ? 0.1308 0.2003 0.1628 0.0306  -0.0011 -0.0786 170  ARG A CD  
1145  N NE  . ARG A 172  ? 0.1248 0.1871 0.1540 0.0285  0.0002  -0.0713 170  ARG A NE  
1146  C CZ  . ARG A 172  ? 0.1248 0.1769 0.1521 0.0261  0.0006  -0.0653 170  ARG A CZ  
1147  N NH1 . ARG A 172  ? 0.1356 0.1829 0.1636 0.0254  -0.0002 -0.0652 170  ARG A NH1 
1148  N NH2 . ARG A 172  ? 0.1423 0.1891 0.1670 0.0245  0.0016  -0.0595 170  ARG A NH2 
1149  N N   . LEU A 173  ? 0.1288 0.2209 0.1471 0.0234  0.0023  -0.0747 171  LEU A N   
1150  C CA  . LEU A 173  ? 0.1305 0.2251 0.1510 0.0248  0.0007  -0.0803 171  LEU A CA  
1151  C C   . LEU A 173  ? 0.1278 0.2378 0.1446 0.0241  0.0017  -0.0819 171  LEU A C   
1152  O O   . LEU A 173  ? 0.1399 0.2577 0.1587 0.0265  0.0003  -0.0892 171  LEU A O   
1153  C CB  . LEU A 173  ? 0.1494 0.2319 0.1706 0.0231  -0.0001 -0.0768 171  LEU A CB  
1154  C CG  . LEU A 173  ? 0.1328 0.2142 0.1487 0.0193  0.0016  -0.0694 171  LEU A CG  
1155  C CD1 . LEU A 173  ? 0.1856 0.2756 0.2001 0.0188  0.0012  -0.0719 171  LEU A CD1 
1156  C CD2 . LEU A 173  ? 0.1677 0.2345 0.1848 0.0180  0.0013  -0.0646 171  LEU A CD2 
1157  N N   . ILE A 174  ? 0.1254 0.2403 0.1368 0.0209  0.0039  -0.0751 172  ILE A N   
1158  C CA  . ILE A 174  ? 0.1364 0.2668 0.1442 0.0200  0.0049  -0.0757 172  ILE A CA  
1159  C C   . ILE A 174  ? 0.1436 0.2877 0.1522 0.0226  0.0052  -0.0815 172  ILE A C   
1160  O O   . ILE A 174  ? 0.1552 0.3118 0.1636 0.0243  0.0047  -0.0872 172  ILE A O   
1161  C CB  . ILE A 174  ? 0.1233 0.2551 0.1259 0.0158  0.0069  -0.0664 172  ILE A CB  
1162  C CG1 . ILE A 174  ? 0.1649 0.2859 0.1666 0.0136  0.0065  -0.0620 172  ILE A CG1 
1163  C CG2 . ILE A 174  ? 0.1564 0.3062 0.1554 0.0148  0.0080  -0.0664 172  ILE A CG2 
1164  C CD1 . ILE A 174  ? 0.1789 0.2987 0.1765 0.0097  0.0081  -0.0528 172  ILE A CD1 
1165  N N   . SER A 175  ? 0.1365 0.2790 0.1462 0.0232  0.0059  -0.0802 173  SER A N   
1166  C CA  . SER A 175  ? 0.1280 0.2837 0.1388 0.0258  0.0062  -0.0856 173  SER A CA  
1167  C C   . SER A 175  ? 0.1314 0.2879 0.1476 0.0304  0.0039  -0.0959 173  SER A C   
1168  O O   . SER A 175  ? 0.1680 0.3386 0.1849 0.0330  0.0039  -0.1022 173  SER A O   
1169  C CB  . SER A 175  ? 0.1658 0.3186 0.1771 0.0254  0.0073  -0.0819 173  SER A CB  
1170  O OG  . SER A 175  ? 0.2328 0.3876 0.2395 0.0212  0.0092  -0.0731 173  SER A OG  
1171  N N   . ARG A 176  ? 0.1409 0.2831 0.1612 0.0316  0.0018  -0.0978 174  ARG A N   
1172  C CA  . ARG A 176  ? 0.1360 0.2773 0.1624 0.0359  -0.0010 -0.1074 174  ARG A CA  
1173  C C   . ARG A 176  ? 0.1809 0.3286 0.2072 0.0366  -0.0023 -0.1127 174  ARG A C   
1174  O O   . ARG A 176  ? 0.1942 0.3501 0.2239 0.0393  -0.0042 -0.1192 174  ARG A O   
1175  C CB  . ARG A 176  ? 0.1639 0.2870 0.1953 0.0365  -0.0029 -0.1065 174  ARG A CB  
1176  C CG  . ARG A 176  ? 0.1824 0.3028 0.2215 0.0411  -0.0062 -0.1160 174  ARG A CG  
1177  C CD  . ARG A 176  ? 0.1934 0.2965 0.2374 0.0413  -0.0079 -0.1134 174  ARG A CD  
1178  N NE  . ARG A 176  ? 0.1736 0.2658 0.2178 0.0390  -0.0087 -0.1097 174  ARG A NE  
1179  C CZ  . ARG A 176  ? 0.1804 0.2619 0.2220 0.0357  -0.0075 -0.1011 174  ARG A CZ  
1180  N NH1 . ARG A 176  ? 0.1580 0.2369 0.1965 0.0342  -0.0055 -0.0949 174  ARG A NH1 
1181  N NH2 . ARG A 176  ? 0.2372 0.3107 0.2794 0.0340  -0.0084 -0.0988 174  ARG A NH2 
1182  N N   . CYS A 177  ? 0.1667 0.3093 0.1900 0.0335  -0.0019 -0.1075 175  CYS A N   
1183  C CA  . CYS A 177  ? 0.2073 0.3524 0.2314 0.0341  -0.0037 -0.1122 175  CYS A CA  
1184  C C   . CYS A 177  ? 0.1954 0.3526 0.2133 0.0315  -0.0020 -0.1089 175  CYS A C   
1185  O O   . CYS A 177  ? 0.2246 0.3880 0.2428 0.0325  -0.0034 -0.1142 175  CYS A O   
1186  C CB  . CYS A 177  ? 0.2111 0.3392 0.2385 0.0329  -0.0054 -0.1097 175  CYS A CB  
1187  S SG  . CYS A 177  ? 0.2612 0.3744 0.2968 0.0359  -0.0080 -0.1131 175  CYS A SG  
1188  N N   . GLY A 178  ? 0.2012 0.3614 0.2137 0.0280  0.0007  -0.1003 176  GLY A N   
1189  C CA  . GLY A 178  ? 0.1969 0.3708 0.2039 0.0258  0.0022  -0.0974 176  GLY A CA  
1190  C C   . GLY A 178  ? 0.1915 0.3613 0.1966 0.0234  0.0016  -0.0942 176  GLY A C   
1191  O O   . GLY A 178  ? 0.1901 0.3451 0.1972 0.0224  0.0007  -0.0916 176  GLY A O   
1192  N N   . GLU A 179  ? 0.1931 0.3774 0.1942 0.0224  0.0023  -0.0940 177  GLU A N   
1193  C CA  . GLU A 179  ? 0.1829 0.3660 0.1818 0.0201  0.0018  -0.0908 177  GLU A CA  
1194  C C   . GLU A 179  ? 0.1590 0.3318 0.1625 0.0218  -0.0010 -0.0964 177  GLU A C   
1195  O O   . GLU A 179  ? 0.1999 0.3627 0.2030 0.0194  -0.0013 -0.0913 177  GLU A O   
1196  C CB  . GLU A 179  ? 0.2242 0.4268 0.2187 0.0196  0.0025  -0.0916 177  GLU A CB  
1197  C CG  . GLU A 179  ? 0.2699 0.4729 0.2613 0.0167  0.0022  -0.0867 177  GLU A CG  
1198  C CD  . GLU A 179  ? 0.3596 0.5635 0.3534 0.0189  -0.0004 -0.0946 177  GLU A CD  
1199  O OE1 . GLU A 179  ? 0.4268 0.6333 0.4252 0.0225  -0.0022 -0.1033 177  GLU A OE1 
1200  O OE2 . GLU A 179  ? 0.4385 0.6398 0.4310 0.0167  -0.0010 -0.0911 177  GLU A OE2 
1201  N N   . PRO A 180  ? 0.1606 0.3352 0.1687 0.0258  -0.0032 -0.1065 178  PRO A N   
1202  C CA  . PRO A 180  ? 0.2122 0.3767 0.2252 0.0270  -0.0061 -0.1111 178  PRO A CA  
1203  C C   . PRO A 180  ? 0.2020 0.3471 0.2178 0.0253  -0.0064 -0.1055 178  PRO A C   
1204  O O   . PRO A 180  ? 0.2203 0.3579 0.2375 0.0240  -0.0077 -0.1042 178  PRO A O   
1205  C CB  . PRO A 180  ? 0.2014 0.3695 0.2203 0.0315  -0.0085 -0.1216 178  PRO A CB  
1206  C CG  . PRO A 180  ? 0.1897 0.3749 0.2065 0.0319  -0.0073 -0.1213 178  PRO A CG  
1207  C CD  . PRO A 180  ? 0.1946 0.3811 0.2050 0.0290  -0.0037 -0.1131 178  PRO A CD  
1208  N N   . VAL A 181  ? 0.1739 0.3113 0.1905 0.0252  -0.0052 -0.1020 179  VAL A N   
1209  C CA  . VAL A 181  ? 0.1617 0.2817 0.1809 0.0236  -0.0055 -0.0967 179  VAL A CA  
1210  C C   . VAL A 181  ? 0.1875 0.3041 0.2016 0.0195  -0.0034 -0.0868 179  VAL A C   
1211  O O   . VAL A 181  ? 0.1850 0.2899 0.2006 0.0180  -0.0040 -0.0832 179  VAL A O   
1212  C CB  . VAL A 181  ? 0.1476 0.2600 0.1695 0.0250  -0.0052 -0.0962 179  VAL A CB  
1213  C CG1 . VAL A 181  ? 0.1667 0.2838 0.1835 0.0232  -0.0022 -0.0899 179  VAL A CG1 
1214  C CG2 . VAL A 181  ? 0.1879 0.2828 0.2137 0.0243  -0.0062 -0.0928 179  VAL A CG2 
1215  N N   . ILE A 182  ? 0.1669 0.2937 0.1754 0.0176  -0.0012 -0.0823 180  ILE A N   
1216  C CA  . ILE A 182  ? 0.1613 0.2856 0.1654 0.0139  0.0004  -0.0732 180  ILE A CA  
1217  C C   . ILE A 182  ? 0.1930 0.3188 0.1969 0.0130  -0.0008 -0.0740 180  ILE A C   
1218  O O   . ILE A 182  ? 0.1915 0.3080 0.1952 0.0109  -0.0008 -0.0686 180  ILE A O   
1219  C CB  . ILE A 182  ? 0.1605 0.2965 0.1595 0.0120  0.0027  -0.0685 180  ILE A CB  
1220  C CG1 . ILE A 182  ? 0.1851 0.3196 0.1847 0.0128  0.0038  -0.0678 180  ILE A CG1 
1221  C CG2 . ILE A 182  ? 0.2189 0.3519 0.2141 0.0082  0.0039  -0.0591 180  ILE A CG2 
1222  C CD1 . ILE A 182  ? 0.2154 0.3631 0.2109 0.0113  0.0058  -0.0643 180  ILE A CD1 
1223  N N   . ARG A 183  ? 0.1965 0.3344 0.2005 0.0148  -0.0021 -0.0808 181  ARG A N   
1224  C CA  . ARG A 183  ? 0.2305 0.3709 0.2345 0.0142  -0.0036 -0.0824 181  ARG A CA  
1225  C C   . ARG A 183  ? 0.2243 0.3500 0.2336 0.0147  -0.0056 -0.0838 181  ARG A C   
1226  O O   . ARG A 183  ? 0.2340 0.3545 0.2428 0.0125  -0.0058 -0.0796 181  ARG A O   
1227  C CB  . ARG A 183  ? 0.2483 0.4041 0.2524 0.0168  -0.0049 -0.0912 181  ARG A CB  
1228  C CG  . ARG A 183  ? 0.3049 0.4656 0.3086 0.0165  -0.0067 -0.0936 181  ARG A CG  
1229  C CD  . ARG A 183  ? 0.3632 0.5330 0.3607 0.0133  -0.0049 -0.0861 181  ARG A CD  
1230  N NE  . ARG A 183  ? 0.3260 0.4844 0.3232 0.0103  -0.0046 -0.0783 181  ARG A NE  
1231  C CZ  . ARG A 183  ? 0.3468 0.5068 0.3397 0.0071  -0.0027 -0.0692 181  ARG A CZ  
1232  N NH1 . ARG A 183  ? 0.3718 0.5439 0.3604 0.0061  -0.0010 -0.0660 181  ARG A NH1 
1233  N NH2 . ARG A 183  ? 0.3369 0.4861 0.3301 0.0048  -0.0027 -0.0631 181  ARG A NH2 
1234  N N   . ARG A 184  ? 0.2050 0.3242 0.2197 0.0174  -0.0072 -0.0897 182  ARG A N   
1235  C CA  . ARG A 184  ? 0.2311 0.3366 0.2515 0.0176  -0.0093 -0.0908 182  ARG A CA  
1236  C C   . ARG A 184  ? 0.2189 0.3115 0.2386 0.0150  -0.0077 -0.0817 182  ARG A C   
1237  O O   . ARG A 184  ? 0.2121 0.2966 0.2339 0.0137  -0.0086 -0.0795 182  ARG A O   
1238  C CB  . ARG A 184  ? 0.2528 0.3544 0.2797 0.0211  -0.0114 -0.0985 182  ARG A CB  
1239  C CG  . ARG A 184  ? 0.2887 0.4006 0.3184 0.0240  -0.0140 -0.1088 182  ARG A CG  
1240  C CD  . ARG A 184  ? 0.3121 0.4169 0.3478 0.0245  -0.0173 -0.1129 182  ARG A CD  
1241  N NE  . ARG A 184  ? 0.3535 0.4465 0.3970 0.0264  -0.0197 -0.1163 182  ARG A NE  
1242  C CZ  . ARG A 184  ? 0.3235 0.4023 0.3712 0.0249  -0.0205 -0.1119 182  ARG A CZ  
1243  N NH1 . ARG A 184  ? 0.2981 0.3722 0.3429 0.0217  -0.0191 -0.1044 182  ARG A NH1 
1244  N NH2 . ARG A 184  ? 0.3556 0.4251 0.4108 0.0268  -0.0228 -0.1151 182  ARG A NH2 
1245  N N   . GLY A 185  ? 0.1908 0.2816 0.2074 0.0141  -0.0054 -0.0766 183  GLY A N   
1246  C CA  . GLY A 185  ? 0.1631 0.2427 0.1785 0.0118  -0.0038 -0.0683 183  GLY A CA  
1247  C C   . GLY A 185  ? 0.2146 0.2956 0.2262 0.0089  -0.0029 -0.0623 183  GLY A C   
1248  O O   . GLY A 185  ? 0.1942 0.2656 0.2071 0.0075  -0.0029 -0.0583 183  GLY A O   
1249  N N   . VAL A 186  ? 0.2089 0.3024 0.2161 0.0080  -0.0020 -0.0615 184  VAL A N   
1250  C CA  . VAL A 186  ? 0.1856 0.2812 0.1893 0.0053  -0.0013 -0.0556 184  VAL A CA  
1251  C C   . VAL A 186  ? 0.2098 0.3030 0.2163 0.0053  -0.0033 -0.0581 184  VAL A C   
1252  O O   . VAL A 186  ? 0.2025 0.2889 0.2090 0.0035  -0.0030 -0.0529 184  VAL A O   
1253  C CB  . VAL A 186  ? 0.1824 0.2933 0.1813 0.0044  -0.0003 -0.0546 184  VAL A CB  
1254  C CG1 . VAL A 186  ? 0.2193 0.3337 0.2155 0.0020  -0.0003 -0.0497 184  VAL A CG1 
1255  C CG2 . VAL A 186  ? 0.2119 0.3240 0.2080 0.0035  0.0018  -0.0499 184  VAL A CG2 
1256  N N   . ASP A 187  ? 0.1817 0.2805 0.1911 0.0075  -0.0054 -0.0663 185  ASP A N   
1257  C CA  . ASP A 187  ? 0.2300 0.3272 0.2427 0.0076  -0.0076 -0.0693 185  ASP A CA  
1258  C C   . ASP A 187  ? 0.2462 0.3282 0.2639 0.0074  -0.0084 -0.0677 185  ASP A C   
1259  O O   . ASP A 187  ? 0.2557 0.3333 0.2747 0.0059  -0.0091 -0.0652 185  ASP A O   
1260  C CB  . ASP A 187  ? 0.2549 0.3612 0.2700 0.0103  -0.0100 -0.0791 185  ASP A CB  
1261  C CG  . ASP A 187  ? 0.2864 0.4097 0.2963 0.0103  -0.0093 -0.0805 185  ASP A CG  
1262  O OD1 . ASP A 187  ? 0.3285 0.4560 0.3333 0.0078  -0.0074 -0.0733 185  ASP A OD1 
1263  O OD2 . ASP A 187  ? 0.2997 0.4324 0.3107 0.0127  -0.0109 -0.0888 185  ASP A OD2 
1264  N N   . MET A 188  ? 0.2294 0.3037 0.2500 0.0087  -0.0083 -0.0686 186  MET A N   
1265  C CA  . MET A 188  ? 0.2107 0.2712 0.2361 0.0084  -0.0089 -0.0664 186  MET A CA  
1266  C C   . MET A 188  ? 0.2368 0.2906 0.2592 0.0058  -0.0067 -0.0574 186  MET A C   
1267  O O   . MET A 188  ? 0.2444 0.2912 0.2694 0.0047  -0.0073 -0.0548 186  MET A O   
1268  C CB  . MET A 188  ? 0.2723 0.3271 0.3011 0.0104  -0.0093 -0.0690 186  MET A CB  
1269  C CG  . MET A 188  ? 0.3200 0.3614 0.3542 0.0102  -0.0101 -0.0668 186  MET A CG  
1270  S SD  . MET A 188  ? 0.3939 0.4323 0.4356 0.0107  -0.0138 -0.0720 186  MET A SD  
1271  C CE  . MET A 188  ? 0.3578 0.4045 0.4027 0.0141  -0.0164 -0.0830 186  MET A CE  
1272  N N   . ALA A 189  ? 0.2192 0.2751 0.2365 0.0049  -0.0043 -0.0527 187  ALA A N   
1273  C CA  . ALA A 189  ? 0.2112 0.2612 0.2258 0.0028  -0.0024 -0.0447 187  ALA A CA  
1274  C C   . ALA A 189  ? 0.2036 0.2571 0.2167 0.0010  -0.0026 -0.0420 187  ALA A C   
1275  O O   . ALA A 189  ? 0.2264 0.2729 0.2401 -0.0003 -0.0021 -0.0372 187  ALA A O   
1276  C CB  . ALA A 189  ? 0.2307 0.2832 0.2406 0.0021  -0.0002 -0.0407 187  ALA A CB  
1277  N N   . MET A 190  ? 0.2015 0.2664 0.2125 0.0011  -0.0033 -0.0450 188  MET A N   
1278  C CA  . MET A 190  ? 0.2216 0.2907 0.2312 -0.0005 -0.0038 -0.0426 188  MET A CA  
1279  C C   . MET A 190  ? 0.2278 0.2904 0.2424 -0.0005 -0.0056 -0.0444 188  MET A C   
1280  O O   . MET A 190  ? 0.2534 0.3121 0.2681 -0.0020 -0.0052 -0.0396 188  MET A O   
1281  C CB  . MET A 190  ? 0.2779 0.3614 0.2848 -0.0002 -0.0045 -0.0463 188  MET A CB  
1282  C CG  . MET A 190  ? 0.2862 0.3756 0.2906 -0.0021 -0.0047 -0.0426 188  MET A CG  
1283  S SD  . MET A 190  ? 0.3987 0.5062 0.3998 -0.0016 -0.0057 -0.0471 188  MET A SD  
1284  C CE  . MET A 190  ? 0.2977 0.4117 0.2958 -0.0008 -0.0040 -0.0478 188  MET A CE  
1285  N N   . ARG A 191  ? 0.2076 0.2690 0.2270 0.0014  -0.0076 -0.0512 189  ARG A N   
1286  C CA  . ARG A 191  ? 0.2588 0.3139 0.2839 0.0013  -0.0097 -0.0530 189  ARG A CA  
1287  C C   . ARG A 191  ? 0.2629 0.3057 0.2901 0.0004  -0.0085 -0.0473 189  ARG A C   
1288  O O   . ARG A 191  ? 0.2478 0.2867 0.2767 -0.0010 -0.0087 -0.0439 189  ARG A O   
1289  C CB  . ARG A 191  ? 0.2631 0.3188 0.2935 0.0036  -0.0124 -0.0616 189  ARG A CB  
1290  C CG  . ARG A 191  ? 0.3591 0.4088 0.3964 0.0035  -0.0150 -0.0639 189  ARG A CG  
1291  C CD  . ARG A 191  ? 0.4165 0.4603 0.4605 0.0055  -0.0172 -0.0696 189  ARG A CD  
1292  N NE  . ARG A 191  ? 0.5408 0.5924 0.5843 0.0079  -0.0182 -0.0768 189  ARG A NE  
1293  C CZ  . ARG A 191  ? 0.6220 0.6700 0.6709 0.0101  -0.0201 -0.0823 189  ARG A CZ  
1294  N NH1 . ARG A 191  ? 0.6281 0.6647 0.6835 0.0099  -0.0214 -0.0812 189  ARG A NH1 
1295  N NH2 . ARG A 191  ? 0.5749 0.6312 0.6228 0.0125  -0.0208 -0.0890 189  ARG A NH2 
1296  N N   . MET A 192  ? 0.2156 0.2528 0.2428 0.0011  -0.0073 -0.0460 190  MET A N   
1297  C CA  . MET A 192  ? 0.2123 0.2386 0.2416 0.0005  -0.0063 -0.0410 190  MET A CA  
1298  C C   . MET A 192  ? 0.2479 0.2728 0.2732 -0.0014 -0.0042 -0.0338 190  MET A C   
1299  O O   . MET A 192  ? 0.2269 0.2459 0.2546 -0.0023 -0.0040 -0.0303 190  MET A O   
1300  C CB  . MET A 192  ? 0.2377 0.2593 0.2671 0.0017  -0.0054 -0.0410 190  MET A CB  
1301  C CG  . MET A 192  ? 0.2497 0.2711 0.2841 0.0037  -0.0078 -0.0480 190  MET A CG  
1302  S SD  . MET A 192  ? 0.3449 0.3603 0.3801 0.0052  -0.0070 -0.0475 190  MET A SD  
1303  C CE  . MET A 192  ? 0.3436 0.3471 0.3823 0.0040  -0.0065 -0.0414 190  MET A CE  
1304  N N   . MET A 193  ? 0.2351 0.2658 0.2549 -0.0019 -0.0026 -0.0314 191  MET A N   
1305  C CA  . MET A 193  ? 0.2332 0.2619 0.2497 -0.0035 -0.0009 -0.0247 191  MET A CA  
1306  C C   . MET A 193  ? 0.2108 0.2441 0.2270 -0.0047 -0.0016 -0.0233 191  MET A C   
1307  O O   . MET A 193  ? 0.2618 0.2923 0.2767 -0.0059 -0.0005 -0.0179 191  MET A O   
1308  C CB  . MET A 193  ? 0.2363 0.2685 0.2477 -0.0038 0.0008  -0.0221 191  MET A CB  
1309  C CG  . MET A 193  ? 0.2751 0.3012 0.2865 -0.0028 0.0018  -0.0217 191  MET A CG  
1310  S SD  . MET A 193  ? 0.4132 0.4414 0.4192 -0.0037 0.0038  -0.0172 191  MET A SD  
1311  C CE  . MET A 193  ? 0.2997 0.3400 0.3040 -0.0032 0.0031  -0.0219 191  MET A CE  
1312  N N   . GLY A 194  ? 0.2342 0.2744 0.2517 -0.0044 -0.0035 -0.0282 192  GLY A N   
1313  C CA  . GLY A 194  ? 0.2144 0.2594 0.2317 -0.0056 -0.0044 -0.0269 192  GLY A CA  
1314  C C   . GLY A 194  ? 0.2614 0.3029 0.2842 -0.0056 -0.0063 -0.0293 192  GLY A C   
1315  O O   . GLY A 194  ? 0.2645 0.3074 0.2877 -0.0067 -0.0068 -0.0270 192  GLY A O   
1316  N N   . GLU A 195  ? 0.2316 0.2685 0.2590 -0.0044 -0.0075 -0.0338 193  GLU A N   
1317  C CA  . GLU A 195  ? 0.2192 0.2537 0.2529 -0.0044 -0.0099 -0.0370 193  GLU A CA  
1318  C C   . GLU A 195  ? 0.2270 0.2511 0.2661 -0.0042 -0.0101 -0.0361 193  GLU A C   
1319  O O   . GLU A 195  ? 0.2199 0.2410 0.2644 -0.0048 -0.0118 -0.0369 193  GLU A O   
1320  C CB  . GLU A 195  ? 0.2837 0.3252 0.3192 -0.0031 -0.0126 -0.0451 193  GLU A CB  
1321  C CG  . GLU A 195  ? 0.3221 0.3755 0.3527 -0.0032 -0.0127 -0.0467 193  GLU A CG  
1322  C CD  . GLU A 195  ? 0.3595 0.4202 0.3914 -0.0014 -0.0150 -0.0554 193  GLU A CD  
1323  O OE1 . GLU A 195  ? 0.4162 0.4740 0.4543 -0.0006 -0.0177 -0.0605 193  GLU A OE1 
1324  O OE2 . GLU A 195  ? 0.4634 0.5328 0.4906 -0.0007 -0.0143 -0.0571 193  GLU A OE2 
1325  N N   . GLN A 196  ? 0.2196 0.2385 0.2577 -0.0035 -0.0086 -0.0346 194  GLN A N   
1326  C CA  . GLN A 196  ? 0.2477 0.2575 0.2910 -0.0032 -0.0089 -0.0335 194  GLN A CA  
1327  C C   . GLN A 196  ? 0.2643 0.2681 0.3055 -0.0041 -0.0062 -0.0263 194  GLN A C   
1328  O O   . GLN A 196  ? 0.2569 0.2556 0.3020 -0.0049 -0.0063 -0.0232 194  GLN A O   
1329  C CB  . GLN A 196  ? 0.2774 0.2858 0.3221 -0.0015 -0.0097 -0.0379 194  GLN A CB  
1330  C CG  . GLN A 196  ? 0.3720 0.3711 0.4221 -0.0013 -0.0101 -0.0362 194  GLN A CG  
1331  C CD  . GLN A 196  ? 0.3646 0.3620 0.4163 0.0005  -0.0109 -0.0400 194  GLN A CD  
1332  O OE1 . GLN A 196  ? 0.3769 0.3801 0.4281 0.0019  -0.0122 -0.0460 194  GLN A OE1 
1333  N NE2 . GLN A 196  ? 0.4226 0.4126 0.4763 0.0007  -0.0102 -0.0366 194  GLN A NE2 
1334  N N   . PHE A 197  ? 0.2382 0.2428 0.2737 -0.0038 -0.0040 -0.0236 195  PHE A N   
1335  C CA  . PHE A 197  ? 0.2289 0.2283 0.2623 -0.0043 -0.0016 -0.0174 195  PHE A CA  
1336  C C   . PHE A 197  ? 0.2462 0.2473 0.2782 -0.0056 -0.0009 -0.0135 195  PHE A C   
1337  O O   . PHE A 197  ? 0.2400 0.2367 0.2719 -0.0060 0.0007  -0.0088 195  PHE A O   
1338  C CB  . PHE A 197  ? 0.2617 0.2616 0.2897 -0.0038 0.0002  -0.0160 195  PHE A CB  
1339  C CG  . PHE A 197  ? 0.2919 0.2893 0.3212 -0.0024 -0.0002 -0.0190 195  PHE A CG  
1340  C CD1 . PHE A 197  ? 0.2828 0.2739 0.3174 -0.0020 -0.0011 -0.0192 195  PHE A CD1 
1341  C CD2 . PHE A 197  ? 0.3334 0.3352 0.3592 -0.0016 0.0001  -0.0213 195  PHE A CD2 
1342  C CE1 . PHE A 197  ? 0.3559 0.3446 0.3922 -0.0007 -0.0017 -0.0218 195  PHE A CE1 
1343  C CE2 . PHE A 197  ? 0.3164 0.3160 0.3437 -0.0002 -0.0004 -0.0242 195  PHE A CE2 
1344  C CZ  . PHE A 197  ? 0.3039 0.2969 0.3366 0.0003  -0.0013 -0.0245 195  PHE A CZ  
1345  N N   . VAL A 198  ? 0.2036 0.2117 0.2346 -0.0061 -0.0020 -0.0155 196  VAL A N   
1346  C CA  . VAL A 198  ? 0.1838 0.1940 0.2146 -0.0073 -0.0019 -0.0124 196  VAL A CA  
1347  C C   . VAL A 198  ? 0.1991 0.2140 0.2333 -0.0076 -0.0045 -0.0167 196  VAL A C   
1348  O O   . VAL A 198  ? 0.2222 0.2410 0.2571 -0.0069 -0.0062 -0.0221 196  VAL A O   
1349  C CB  . VAL A 198  ? 0.1926 0.2072 0.2175 -0.0077 -0.0006 -0.0092 196  VAL A CB  
1350  C CG1 . VAL A 198  ? 0.2125 0.2222 0.2345 -0.0074 0.0016  -0.0052 196  VAL A CG1 
1351  C CG2 . VAL A 198  ? 0.2217 0.2448 0.2437 -0.0076 -0.0016 -0.0128 196  VAL A CG2 
1352  N N   . THR A 199  ? 0.1793 0.1942 0.2158 -0.0086 -0.0049 -0.0143 197  THR A N   
1353  C CA  . THR A 199  ? 0.1885 0.2088 0.2277 -0.0091 -0.0074 -0.0179 197  THR A CA  
1354  C C   . THR A 199  ? 0.2027 0.2320 0.2369 -0.0093 -0.0076 -0.0187 197  THR A C   
1355  O O   . THR A 199  ? 0.2498 0.2856 0.2845 -0.0091 -0.0097 -0.0237 197  THR A O   
1356  C CB  . THR A 199  ? 0.1958 0.2137 0.2391 -0.0102 -0.0077 -0.0147 197  THR A CB  
1357  O OG1 . THR A 199  ? 0.2249 0.2351 0.2727 -0.0102 -0.0072 -0.0132 197  THR A OG1 
1358  C CG2 . THR A 199  ? 0.2381 0.2610 0.2851 -0.0108 -0.0106 -0.0188 197  THR A CG2 
1359  N N   . GLY A 200  ? 0.2068 0.2369 0.2361 -0.0097 -0.0057 -0.0138 198  GLY A N   
1360  C CA  . GLY A 200  ? 0.2098 0.2484 0.2344 -0.0100 -0.0058 -0.0134 198  GLY A CA  
1361  C C   . GLY A 200  ? 0.1889 0.2257 0.2091 -0.0103 -0.0035 -0.0080 198  GLY A C   
1362  O O   . GLY A 200  ? 0.1873 0.2166 0.2082 -0.0102 -0.0020 -0.0044 198  GLY A O   
1363  N N   . GLU A 201  ? 0.2118 0.2559 0.2277 -0.0106 -0.0035 -0.0075 199  GLU A N   
1364  C CA  . GLU A 201  ? 0.2126 0.2557 0.2247 -0.0111 -0.0018 -0.0024 199  GLU A CA  
1365  C C   . GLU A 201  ? 0.2253 0.2667 0.2378 -0.0120 -0.0016 0.0032  199  GLU A C   
1366  O O   . GLU A 201  ? 0.2199 0.2558 0.2315 -0.0120 -0.0002 0.0074  199  GLU A O   
1367  C CB  . GLU A 201  ? 0.2622 0.3146 0.2701 -0.0115 -0.0020 -0.0030 199  GLU A CB  
1368  C CG  . GLU A 201  ? 0.3019 0.3541 0.3065 -0.0124 -0.0008 0.0027  199  GLU A CG  
1369  C CD  . GLU A 201  ? 0.3845 0.4470 0.3854 -0.0131 -0.0011 0.0027  199  GLU A CD  
1370  O OE1 . GLU A 201  ? 0.4136 0.4847 0.4141 -0.0130 -0.0023 -0.0013 199  GLU A OE1 
1371  O OE2 . GLU A 201  ? 0.4789 0.5412 0.4776 -0.0138 -0.0001 0.0067  199  GLU A OE2 
1372  N N   . THR A 202  ? 0.1885 0.2344 0.2027 -0.0126 -0.0031 0.0029  200  THR A N   
1373  C CA  . THR A 202  ? 0.1979 0.2432 0.2129 -0.0133 -0.0032 0.0077  200  THR A CA  
1374  C C   . THR A 202  ? 0.1746 0.2178 0.1943 -0.0132 -0.0042 0.0061  200  THR A C   
1375  O O   . THR A 202  ? 0.1909 0.2353 0.2129 -0.0129 -0.0053 0.0011  200  THR A O   
1376  C CB  . THR A 202  ? 0.2008 0.2556 0.2133 -0.0144 -0.0045 0.0098  200  THR A CB  
1377  O OG1 . THR A 202  ? 0.2313 0.2935 0.2444 -0.0145 -0.0063 0.0050  200  THR A OG1 
1378  C CG2 . THR A 202  ? 0.2255 0.2836 0.2337 -0.0148 -0.0037 0.0116  200  THR A CG2 
1379  N N   . ILE A 203  ? 0.1671 0.2078 0.1887 -0.0134 -0.0040 0.0102  201  ILE A N   
1380  C CA  . ILE A 203  ? 0.1713 0.2103 0.1976 -0.0135 -0.0048 0.0092  201  ILE A CA  
1381  C C   . ILE A 203  ? 0.1832 0.2303 0.2104 -0.0142 -0.0073 0.0058  201  ILE A C   
1382  O O   . ILE A 203  ? 0.1988 0.2453 0.2299 -0.0142 -0.0085 0.0021  201  ILE A O   
1383  C CB  . ILE A 203  ? 0.1845 0.2198 0.2126 -0.0134 -0.0040 0.0143  201  ILE A CB  
1384  C CG1 . ILE A 203  ? 0.1627 0.1959 0.1963 -0.0135 -0.0045 0.0136  201  ILE A CG1 
1385  C CG2 . ILE A 203  ? 0.2203 0.2612 0.2465 -0.0141 -0.0049 0.0181  201  ILE A CG2 
1386  C CD1 . ILE A 203  ? 0.1726 0.1999 0.2089 -0.0130 -0.0038 0.0108  201  ILE A CD1 
1387  N N   . ARG A 204  ? 0.2013 0.2564 0.2250 -0.0148 -0.0082 0.0069  202  ARG A N   
1388  C CA  . ARG A 204  ? 0.2009 0.2649 0.2250 -0.0153 -0.0106 0.0034  202  ARG A CA  
1389  C C   . ARG A 204  ? 0.2067 0.2727 0.2311 -0.0147 -0.0114 -0.0036 202  ARG A C   
1390  O O   . ARG A 204  ? 0.2115 0.2800 0.2392 -0.0147 -0.0134 -0.0080 202  ARG A O   
1391  C CB  . ARG A 204  ? 0.2560 0.3288 0.2759 -0.0162 -0.0112 0.0064  202  ARG A CB  
1392  C CG  . ARG A 204  ? 0.3038 0.3773 0.3251 -0.0169 -0.0118 0.0117  202  ARG A CG  
1393  C CD  . ARG A 204  ? 0.3683 0.4485 0.3858 -0.0178 -0.0121 0.0165  202  ARG A CD  
1394  N NE  . ARG A 204  ? 0.3788 0.4586 0.3983 -0.0182 -0.0128 0.0218  202  ARG A NE  
1395  C CZ  . ARG A 204  ? 0.3913 0.4629 0.4128 -0.0177 -0.0115 0.0259  202  ARG A CZ  
1396  N NH1 . ARG A 204  ? 0.2834 0.3466 0.3048 -0.0169 -0.0095 0.0255  202  ARG A NH1 
1397  N NH2 . ARG A 204  ? 0.3395 0.4117 0.3631 -0.0180 -0.0124 0.0303  202  ARG A NH2 
1398  N N   . GLU A 205  ? 0.1884 0.2534 0.2098 -0.0141 -0.0102 -0.0049 203  GLU A N   
1399  C CA  . GLU A 205  ? 0.2131 0.2793 0.2353 -0.0131 -0.0110 -0.0116 203  GLU A CA  
1400  C C   . GLU A 205  ? 0.2106 0.2683 0.2384 -0.0126 -0.0113 -0.0142 203  GLU A C   
1401  O O   . GLU A 205  ? 0.2187 0.2780 0.2498 -0.0122 -0.0133 -0.0200 203  GLU A O   
1402  C CB  . GLU A 205  ? 0.2341 0.3002 0.2523 -0.0125 -0.0093 -0.0116 203  GLU A CB  
1403  C CG  . GLU A 205  ? 0.2939 0.3640 0.3119 -0.0114 -0.0102 -0.0185 203  GLU A CG  
1404  C CD  . GLU A 205  ? 0.3709 0.4425 0.3845 -0.0110 -0.0085 -0.0177 203  GLU A CD  
1405  O OE1 . GLU A 205  ? 0.3126 0.3759 0.3268 -0.0105 -0.0070 -0.0166 203  GLU A OE1 
1406  O OE2 . GLU A 205  ? 0.4498 0.5313 0.4594 -0.0113 -0.0087 -0.0178 203  GLU A OE2 
1407  N N   . ALA A 206  ? 0.1764 0.2252 0.2057 -0.0127 -0.0095 -0.0098 204  ALA A N   
1408  C CA  . ALA A 206  ? 0.1948 0.2358 0.2295 -0.0124 -0.0096 -0.0112 204  ALA A CA  
1409  C C   . ALA A 206  ? 0.1898 0.2324 0.2296 -0.0131 -0.0118 -0.0126 204  ALA A C   
1410  O O   . ALA A 206  ? 0.1824 0.2230 0.2271 -0.0130 -0.0135 -0.0169 204  ALA A O   
1411  C CB  . ALA A 206  ? 0.2031 0.2359 0.2380 -0.0123 -0.0071 -0.0058 204  ALA A CB  
1412  N N   . LEU A 207  ? 0.1766 0.2229 0.2157 -0.0139 -0.0119 -0.0090 205  LEU A N   
1413  C CA  . LEU A 207  ? 0.1727 0.2211 0.2166 -0.0147 -0.0141 -0.0100 205  LEU A CA  
1414  C C   . LEU A 207  ? 0.2176 0.2728 0.2625 -0.0147 -0.0170 -0.0168 205  LEU A C   
1415  O O   . LEU A 207  ? 0.2380 0.2919 0.2887 -0.0150 -0.0191 -0.0203 205  LEU A O   
1416  C CB  . LEU A 207  ? 0.1914 0.2433 0.2338 -0.0154 -0.0138 -0.0049 205  LEU A CB  
1417  C CG  . LEU A 207  ? 0.1915 0.2366 0.2348 -0.0153 -0.0114 0.0011  205  LEU A CG  
1418  C CD1 . LEU A 207  ? 0.1819 0.2309 0.2230 -0.0157 -0.0112 0.0061  205  LEU A CD1 
1419  C CD2 . LEU A 207  ? 0.1729 0.2131 0.2229 -0.0157 -0.0118 0.0011  205  LEU A CD2 
1420  N N   . LYS A 208  ? 0.2233 0.2862 0.2631 -0.0142 -0.0173 -0.0189 206  LYS A N   
1421  C CA  . LYS A 208  ? 0.2375 0.3081 0.2777 -0.0138 -0.0201 -0.0259 206  LYS A CA  
1422  C C   . LYS A 208  ? 0.2396 0.3053 0.2844 -0.0129 -0.0213 -0.0320 206  LYS A C   
1423  O O   . LYS A 208  ? 0.2839 0.3518 0.3332 -0.0128 -0.0242 -0.0376 206  LYS A O   
1424  C CB  . LYS A 208  ? 0.2641 0.3440 0.2974 -0.0134 -0.0196 -0.0265 206  LYS A CB  
1425  C CG  . LYS A 208  ? 0.3505 0.4402 0.3835 -0.0127 -0.0223 -0.0340 206  LYS A CG  
1426  C CD  . LYS A 208  ? 0.3927 0.4911 0.4188 -0.0122 -0.0213 -0.0343 206  LYS A CD  
1427  C CE  . LYS A 208  ? 0.4856 0.5947 0.5111 -0.0111 -0.0237 -0.0424 206  LYS A CE  
1428  N NZ  . LYS A 208  ? 0.5017 0.6182 0.5285 -0.0117 -0.0264 -0.0440 206  LYS A NZ  
1429  N N   . ARG A 209  ? 0.2305 0.2893 0.2747 -0.0122 -0.0193 -0.0310 207  ARG A N   
1430  C CA  . ARG A 209  ? 0.2245 0.2782 0.2730 -0.0112 -0.0204 -0.0362 207  ARG A CA  
1431  C C   . ARG A 209  ? 0.2473 0.2924 0.3033 -0.0120 -0.0211 -0.0350 207  ARG A C   
1432  O O   . ARG A 209  ? 0.2965 0.3369 0.3574 -0.0114 -0.0226 -0.0390 207  ARG A O   
1433  C CB  . ARG A 209  ? 0.2563 0.3067 0.3010 -0.0102 -0.0180 -0.0353 207  ARG A CB  
1434  C CG  . ARG A 209  ? 0.2588 0.3186 0.2970 -0.0095 -0.0176 -0.0371 207  ARG A CG  
1435  C CD  . ARG A 209  ? 0.2683 0.3248 0.3029 -0.0087 -0.0151 -0.0355 207  ARG A CD  
1436  N NE  . ARG A 209  ? 0.3199 0.3859 0.3487 -0.0082 -0.0147 -0.0371 207  ARG A NE  
1437  C CZ  . ARG A 209  ? 0.3686 0.4341 0.3934 -0.0077 -0.0126 -0.0352 207  ARG A CZ  
1438  N NH1 . ARG A 209  ? 0.3397 0.3956 0.3653 -0.0076 -0.0108 -0.0320 207  ARG A NH1 
1439  N NH2 . ARG A 209  ? 0.4039 0.4792 0.4239 -0.0074 -0.0123 -0.0367 207  ARG A NH2 
1440  N N   . SER A 210  ? 0.2109 0.2541 0.2683 -0.0132 -0.0203 -0.0295 208  SER A N   
1441  C CA  . SER A 210  ? 0.2391 0.2749 0.3035 -0.0141 -0.0207 -0.0275 208  SER A CA  
1442  C C   . SER A 210  ? 0.2565 0.2947 0.3274 -0.0150 -0.0243 -0.0314 208  SER A C   
1443  O O   . SER A 210  ? 0.2594 0.2917 0.3374 -0.0158 -0.0254 -0.0311 208  SER A O   
1444  C CB  . SER A 210  ? 0.2165 0.2493 0.2795 -0.0149 -0.0180 -0.0197 208  SER A CB  
1445  O OG  . SER A 210  ? 0.2242 0.2534 0.2823 -0.0141 -0.0149 -0.0163 208  SER A OG  
1446  N N   . LYS A 211  ? 0.2727 0.3197 0.3415 -0.0149 -0.0263 -0.0350 209  LYS A N   
1447  C CA  . LYS A 211  ? 0.2909 0.3409 0.3656 -0.0158 -0.0298 -0.0385 209  LYS A CA  
1448  C C   . LYS A 211  ? 0.2764 0.3228 0.3582 -0.0154 -0.0329 -0.0452 209  LYS A C   
1449  O O   . LYS A 211  ? 0.2879 0.3319 0.3774 -0.0166 -0.0354 -0.0461 209  LYS A O   
1450  C CB  . LYS A 211  ? 0.2666 0.3277 0.3368 -0.0156 -0.0312 -0.0412 209  LYS A CB  
1451  C CG  . LYS A 211  ? 0.3062 0.3707 0.3703 -0.0162 -0.0286 -0.0341 209  LYS A CG  
1452  C CD  . LYS A 211  ? 0.3703 0.4463 0.4300 -0.0162 -0.0302 -0.0362 209  LYS A CD  
1453  N N   . GLU A 212  ? 0.2632 0.3090 0.3432 -0.0138 -0.0329 -0.0496 210  GLU A N   
1454  C CA  . GLU A 212  ? 0.3211 0.3638 0.4081 -0.0131 -0.0363 -0.0565 210  GLU A CA  
1455  C C   . GLU A 212  ? 0.3038 0.3364 0.3992 -0.0144 -0.0367 -0.0533 210  GLU A C   
1456  O O   . GLU A 212  ? 0.3473 0.3781 0.4511 -0.0152 -0.0403 -0.0565 210  GLU A O   
1457  C CB  . GLU A 212  ? 0.3414 0.3847 0.4246 -0.0110 -0.0357 -0.0608 210  GLU A CB  
1458  C CG  . GLU A 212  ? 0.4422 0.4827 0.5327 -0.0098 -0.0394 -0.0688 210  GLU A CG  
1459  C CD  . GLU A 212  ? 0.5472 0.5907 0.6335 -0.0074 -0.0390 -0.0740 210  GLU A CD  
1460  O OE1 . GLU A 212  ? 0.5362 0.5880 0.6142 -0.0067 -0.0371 -0.0739 210  GLU A OE1 
1461  O OE2 . GLU A 212  ? 0.6491 0.6871 0.7408 -0.0063 -0.0408 -0.0780 210  GLU A OE2 
1462  N N   . LEU A 213  ? 0.2776 0.3038 0.3711 -0.0147 -0.0332 -0.0467 211  LEU A N   
1463  C CA  . LEU A 213  ? 0.2623 0.2797 0.3634 -0.0159 -0.0334 -0.0430 211  LEU A CA  
1464  C C   . LEU A 213  ? 0.2587 0.2758 0.3632 -0.0179 -0.0330 -0.0373 211  LEU A C   
1465  O O   . LEU A 213  ? 0.2697 0.2817 0.3826 -0.0194 -0.0345 -0.0357 211  LEU A O   
1466  C CB  . LEU A 213  ? 0.2506 0.2619 0.3485 -0.0152 -0.0300 -0.0384 211  LEU A CB  
1467  C CG  . LEU A 213  ? 0.2879 0.2978 0.3853 -0.0133 -0.0310 -0.0440 211  LEU A CG  
1468  C CD1 . LEU A 213  ? 0.2802 0.2844 0.3743 -0.0127 -0.0277 -0.0394 211  LEU A CD1 
1469  C CD2 . LEU A 213  ? 0.3441 0.3505 0.4515 -0.0134 -0.0355 -0.0497 211  LEU A CD2 
1470  N N   . GLU A 214  ? 0.2448 0.2675 0.3435 -0.0182 -0.0312 -0.0343 212  GLU A N   
1471  C CA  . GLU A 214  ? 0.2251 0.2485 0.3277 -0.0200 -0.0313 -0.0298 212  GLU A CA  
1472  C C   . GLU A 214  ? 0.2893 0.3148 0.3998 -0.0211 -0.0359 -0.0347 212  GLU A C   
1473  O O   . GLU A 214  ? 0.2782 0.3009 0.3961 -0.0229 -0.0369 -0.0318 212  GLU A O   
1474  C CB  . GLU A 214  ? 0.2264 0.2558 0.3216 -0.0198 -0.0290 -0.0261 212  GLU A CB  
1475  C CG  . GLU A 214  ? 0.2210 0.2470 0.3102 -0.0191 -0.0246 -0.0199 212  GLU A CG  
1476  C CD  . GLU A 214  ? 0.2795 0.3108 0.3628 -0.0190 -0.0227 -0.0159 212  GLU A CD  
1477  O OE1 . GLU A 214  ? 0.2783 0.3166 0.3598 -0.0191 -0.0246 -0.0186 212  GLU A OE1 
1478  O OE2 . GLU A 214  ? 0.2461 0.2744 0.3266 -0.0188 -0.0195 -0.0102 212  GLU A OE2 
1479  N N   . GLU A 215  ? 0.2821 0.3129 0.3915 -0.0201 -0.0388 -0.0424 213  GLU A N   
1480  C CA  . GLU A 215  ? 0.2983 0.3313 0.4155 -0.0209 -0.0435 -0.0481 213  GLU A CA  
1481  C C   . GLU A 215  ? 0.3501 0.3750 0.4773 -0.0216 -0.0462 -0.0500 213  GLU A C   
1482  O O   . GLU A 215  ? 0.4079 0.4327 0.5436 -0.0229 -0.0501 -0.0531 213  GLU A O   
1483  C CB  . GLU A 215  ? 0.3832 0.4244 0.4963 -0.0193 -0.0459 -0.0563 213  GLU A CB  
1484  C CG  . GLU A 215  ? 0.4448 0.4950 0.5493 -0.0190 -0.0442 -0.0543 213  GLU A CG  
1485  C CD  . GLU A 215  ? 0.5651 0.6243 0.6639 -0.0172 -0.0456 -0.0615 213  GLU A CD  
1486  O OE1 . GLU A 215  ? 0.6118 0.6707 0.7140 -0.0160 -0.0485 -0.0691 213  GLU A OE1 
1487  O OE2 . GLU A 215  ? 0.5324 0.5991 0.6234 -0.0169 -0.0439 -0.0593 213  GLU A OE2 
1488  N N   . LYS A 216  ? 0.3102 0.3286 0.4370 -0.0208 -0.0443 -0.0482 214  LYS A N   
1489  C CA  . LYS A 216  ? 0.3507 0.3610 0.4871 -0.0215 -0.0466 -0.0488 214  LYS A CA  
1490  C C   . LYS A 216  ? 0.3804 0.3850 0.5213 -0.0236 -0.0445 -0.0399 214  LYS A C   
1491  O O   . LYS A 216  ? 0.4052 0.4032 0.5548 -0.0247 -0.0464 -0.0389 214  LYS A O   
1492  C CB  . LYS A 216  ? 0.3021 0.3088 0.4360 -0.0195 -0.0461 -0.0519 214  LYS A CB  
1493  C CG  . LYS A 216  ? 0.4107 0.4228 0.5425 -0.0173 -0.0488 -0.0617 214  LYS A CG  
1494  C CD  . LYS A 216  ? 0.4572 0.4659 0.5863 -0.0151 -0.0478 -0.0640 214  LYS A CD  
1495  C CE  . LYS A 216  ? 0.5178 0.5303 0.6486 -0.0129 -0.0517 -0.0747 214  LYS A CE  
1496  N NZ  . LYS A 216  ? 0.5746 0.5980 0.6994 -0.0121 -0.0523 -0.0795 214  LYS A NZ  
1497  N N   . GLY A 217  ? 0.3061 0.3132 0.4416 -0.0242 -0.0408 -0.0333 215  GLY A N   
1498  C CA  . GLY A 217  ? 0.2793 0.2826 0.4185 -0.0260 -0.0385 -0.0250 215  GLY A CA  
1499  C C   . GLY A 217  ? 0.2486 0.2491 0.3811 -0.0250 -0.0336 -0.0189 215  GLY A C   
1500  O O   . GLY A 217  ? 0.2830 0.2807 0.4182 -0.0262 -0.0315 -0.0121 215  GLY A O   
1501  N N   . PHE A 218  ? 0.2290 0.2303 0.3531 -0.0229 -0.0319 -0.0213 216  PHE A N   
1502  C CA  . PHE A 218  ? 0.2012 0.2006 0.3183 -0.0220 -0.0273 -0.0158 216  PHE A CA  
1503  C C   . PHE A 218  ? 0.2082 0.2126 0.3189 -0.0219 -0.0245 -0.0119 216  PHE A C   
1504  O O   . PHE A 218  ? 0.2177 0.2278 0.3277 -0.0221 -0.0260 -0.0143 216  PHE A O   
1505  C CB  . PHE A 218  ? 0.2058 0.2044 0.3164 -0.0198 -0.0265 -0.0196 216  PHE A CB  
1506  C CG  . PHE A 218  ? 0.2682 0.2609 0.3843 -0.0195 -0.0285 -0.0222 216  PHE A CG  
1507  C CD1 . PHE A 218  ? 0.2648 0.2577 0.3867 -0.0193 -0.0329 -0.0295 216  PHE A CD1 
1508  C CD2 . PHE A 218  ? 0.2350 0.2222 0.3504 -0.0192 -0.0260 -0.0177 216  PHE A CD2 
1509  C CE1 . PHE A 218  ? 0.2590 0.2462 0.3865 -0.0189 -0.0350 -0.0320 216  PHE A CE1 
1510  C CE2 . PHE A 218  ? 0.2670 0.2488 0.3877 -0.0189 -0.0280 -0.0198 216  PHE A CE2 
1511  C CZ  . PHE A 218  ? 0.2625 0.2440 0.3895 -0.0187 -0.0325 -0.0269 216  PHE A CZ  
1512  N N   . SER A 219  ? 0.1937 0.1961 0.3002 -0.0214 -0.0206 -0.0059 217  SER A N   
1513  C CA  . SER A 219  ? 0.1666 0.1728 0.2663 -0.0208 -0.0177 -0.0024 217  SER A CA  
1514  C C   . SER A 219  ? 0.1668 0.1712 0.2585 -0.0190 -0.0147 -0.0013 217  SER A C   
1515  O O   . SER A 219  ? 0.1706 0.1710 0.2622 -0.0184 -0.0148 -0.0031 217  SER A O   
1516  C CB  . SER A 219  ? 0.1802 0.1863 0.2835 -0.0219 -0.0160 0.0040  217  SER A CB  
1517  O OG  . SER A 219  ? 0.2249 0.2260 0.3301 -0.0219 -0.0140 0.0081  217  SER A OG  
1518  N N   . TYR A 220  ? 0.1571 0.1643 0.2424 -0.0183 -0.0123 0.0017  218  TYR A N   
1519  C CA  . TYR A 220  ? 0.1500 0.1559 0.2276 -0.0167 -0.0097 0.0025  218  TYR A CA  
1520  C C   . TYR A 220  ? 0.1680 0.1731 0.2425 -0.0161 -0.0064 0.0084  218  TYR A C   
1521  O O   . TYR A 220  ? 0.1720 0.1796 0.2483 -0.0166 -0.0061 0.0112  218  TYR A O   
1522  C CB  . TYR A 220  ? 0.1516 0.1628 0.2235 -0.0160 -0.0106 -0.0012 218  TYR A CB  
1523  C CG  . TYR A 220  ? 0.1509 0.1625 0.2236 -0.0157 -0.0130 -0.0075 218  TYR A CG  
1524  C CD1 . TYR A 220  ? 0.1932 0.2073 0.2712 -0.0165 -0.0165 -0.0122 218  TYR A CD1 
1525  C CD2 . TYR A 220  ? 0.1803 0.1899 0.2486 -0.0145 -0.0119 -0.0091 218  TYR A CD2 
1526  C CE1 . TYR A 220  ? 0.2018 0.2165 0.2809 -0.0158 -0.0189 -0.0186 218  TYR A CE1 
1527  C CE2 . TYR A 220  ? 0.2082 0.2186 0.2775 -0.0139 -0.0141 -0.0151 218  TYR A CE2 
1528  C CZ  . TYR A 220  ? 0.1939 0.2068 0.2686 -0.0145 -0.0175 -0.0200 218  TYR A CZ  
1529  O OH  . TYR A 220  ? 0.2307 0.2443 0.3064 -0.0135 -0.0198 -0.0265 218  TYR A OH  
1530  N N   . SER A 221  ? 0.1487 0.1503 0.2188 -0.0150 -0.0040 0.0100  219  SER A N   
1531  C CA  . SER A 221  ? 0.1505 0.1516 0.2161 -0.0139 -0.0011 0.0143  219  SER A CA  
1532  C C   . SER A 221  ? 0.1900 0.1905 0.2487 -0.0127 -0.0001 0.0129  219  SER A C   
1533  O O   . SER A 221  ? 0.1966 0.1940 0.2544 -0.0123 0.0000  0.0112  219  SER A O   
1534  C CB  . SER A 221  ? 0.2051 0.2024 0.2732 -0.0137 0.0011  0.0183  219  SER A CB  
1535  O OG  . SER A 221  ? 0.2044 0.2017 0.2683 -0.0124 0.0037  0.0219  219  SER A OG  
1536  N N   . TYR A 222  ? 0.1316 0.1353 0.1858 -0.0123 0.0003  0.0138  220  TYR A N   
1537  C CA  . TYR A 222  ? 0.1394 0.1436 0.1875 -0.0115 0.0008  0.0124  220  TYR A CA  
1538  C C   . TYR A 222  ? 0.1605 0.1607 0.2050 -0.0103 0.0034  0.0156  220  TYR A C   
1539  O O   . TYR A 222  ? 0.1747 0.1745 0.2192 -0.0098 0.0048  0.0191  220  TYR A O   
1540  C CB  . TYR A 222  ? 0.1510 0.1610 0.1962 -0.0118 -0.0004 0.0119  220  TYR A CB  
1541  C CG  . TYR A 222  ? 0.1317 0.1461 0.1799 -0.0128 -0.0032 0.0079  220  TYR A CG  
1542  C CD1 . TYR A 222  ? 0.1548 0.1707 0.2020 -0.0128 -0.0045 0.0032  220  TYR A CD1 
1543  C CD2 . TYR A 222  ? 0.1489 0.1659 0.2013 -0.0137 -0.0045 0.0086  220  TYR A CD2 
1544  C CE1 . TYR A 222  ? 0.1712 0.1913 0.2215 -0.0135 -0.0073 -0.0012 220  TYR A CE1 
1545  C CE2 . TYR A 222  ? 0.1685 0.1895 0.2239 -0.0146 -0.0072 0.0045  220  TYR A CE2 
1546  C CZ  . TYR A 222  ? 0.1529 0.1754 0.2071 -0.0144 -0.0087 -0.0005 220  TYR A CZ  
1547  O OH  . TYR A 222  ? 0.1841 0.2108 0.2415 -0.0150 -0.0116 -0.0052 220  TYR A OH  
1548  N N   . ASP A 223  ? 0.1855 0.1832 0.2271 -0.0097 0.0040  0.0141  221  ASP A N   
1549  C CA  . ASP A 223  ? 0.2080 0.2021 0.2461 -0.0085 0.0062  0.0162  221  ASP A CA  
1550  C C   . ASP A 223  ? 0.2523 0.2484 0.2850 -0.0083 0.0061  0.0158  221  ASP A C   
1551  O O   . ASP A 223  ? 0.2026 0.2003 0.2334 -0.0085 0.0052  0.0128  221  ASP A O   
1552  C CB  . ASP A 223  ? 0.2268 0.2168 0.2660 -0.0082 0.0065  0.0149  221  ASP A CB  
1553  C CG  . ASP A 223  ? 0.2693 0.2559 0.3042 -0.0070 0.0084  0.0163  221  ASP A CG  
1554  O OD1 . ASP A 223  ? 0.2903 0.2769 0.3222 -0.0063 0.0097  0.0186  221  ASP A OD1 
1555  O OD2 . ASP A 223  ? 0.3185 0.3026 0.3535 -0.0067 0.0084  0.0148  221  ASP A OD2 
1556  N N   . MET A 224  ? 0.2491 0.2455 0.2797 -0.0078 0.0070  0.0188  222  MET A N   
1557  C CA  . MET A 224  ? 0.2531 0.2518 0.2795 -0.0079 0.0066  0.0192  222  MET A CA  
1558  C C   . MET A 224  ? 0.2596 0.2548 0.2823 -0.0071 0.0079  0.0193  222  MET A C   
1559  O O   . MET A 224  ? 0.3212 0.3179 0.3407 -0.0072 0.0077  0.0201  222  MET A O   
1560  C CB  . MET A 224  ? 0.3043 0.3047 0.3308 -0.0078 0.0065  0.0225  222  MET A CB  
1561  C CG  . MET A 224  ? 0.2817 0.2859 0.3119 -0.0086 0.0051  0.0225  222  MET A CG  
1562  S SD  . MET A 224  ? 0.3103 0.3208 0.3405 -0.0101 0.0028  0.0186  222  MET A SD  
1563  C CE  . MET A 224  ? 0.2402 0.2543 0.2652 -0.0104 0.0023  0.0198  222  MET A CE  
1564  N N   . LEU A 225  ? 0.3157 0.3067 0.3391 -0.0063 0.0090  0.0187  223  LEU A N   
1565  C CA  . LEU A 225  ? 0.2792 0.2674 0.2996 -0.0057 0.0099  0.0179  223  LEU A CA  
1566  C C   . LEU A 225  ? 0.3675 0.3532 0.3849 -0.0048 0.0110  0.0204  223  LEU A C   
1567  O O   . LEU A 225  ? 0.3704 0.3539 0.3851 -0.0043 0.0116  0.0199  223  LEU A O   
1568  C CB  . LEU A 225  ? 0.2573 0.2486 0.2756 -0.0064 0.0087  0.0149  223  LEU A CB  
1569  C CG  . LEU A 225  ? 0.2261 0.2184 0.2473 -0.0067 0.0076  0.0112  223  LEU A CG  
1570  C CD1 . LEU A 225  ? 0.2806 0.2765 0.2995 -0.0069 0.0066  0.0079  223  LEU A CD1 
1571  C CD2 . LEU A 225  ? 0.2387 0.2258 0.2620 -0.0060 0.0084  0.0113  223  LEU A CD2 
1572  N N   . GLY A 226  ? 0.3294 0.3154 0.3475 -0.0044 0.0111  0.0229  224  GLY A N   
1573  C CA  . GLY A 226  ? 0.3424 0.3257 0.3585 -0.0033 0.0119  0.0248  224  GLY A CA  
1574  C C   . GLY A 226  ? 0.2843 0.2638 0.3009 -0.0018 0.0137  0.0254  224  GLY A C   
1575  O O   . GLY A 226  ? 0.2896 0.2693 0.3091 -0.0015 0.0143  0.0257  224  GLY A O   
1576  N N   . GLU A 227  ? 0.2396 0.2162 0.2535 -0.0007 0.0143  0.0255  225  GLU A N   
1577  C CA  . GLU A 227  ? 0.2426 0.2165 0.2564 0.0010  0.0159  0.0261  225  GLU A CA  
1578  C C   . GLU A 227  ? 0.2759 0.2472 0.2868 0.0021  0.0161  0.0261  225  GLU A C   
1579  O O   . GLU A 227  ? 0.2477 0.2190 0.2567 0.0013  0.0150  0.0257  225  GLU A O   
1580  C CB  . GLU A 227  ? 0.2654 0.2384 0.2798 0.0010  0.0168  0.0252  225  GLU A CB  
1581  C CG  . GLU A 227  ? 0.2469 0.2185 0.2587 0.0005  0.0165  0.0234  225  GLU A CG  
1582  C CD  . GLU A 227  ? 0.3382 0.3089 0.3516 0.0004  0.0169  0.0228  225  GLU A CD  
1583  O OE1 . GLU A 227  ? 0.3230 0.2953 0.3390 -0.0008 0.0160  0.0217  225  GLU A OE1 
1584  O OE2 . GLU A 227  ? 0.3333 0.3019 0.3456 0.0015  0.0181  0.0233  225  GLU A OE2 
1585  N N   . ALA A 228  ? 0.2450 0.2146 0.2558 0.0040  0.0173  0.0266  226  ALA A N   
1586  C CA  . ALA A 228  ? 0.2560 0.2229 0.2641 0.0054  0.0175  0.0260  226  ALA A CA  
1587  C C   . ALA A 228  ? 0.2314 0.1976 0.2391 0.0051  0.0158  0.0264  226  ALA A C   
1588  O O   . ALA A 228  ? 0.2633 0.2281 0.2689 0.0044  0.0150  0.0259  226  ALA A O   
1589  C CB  . ALA A 228  ? 0.2789 0.2443 0.2845 0.0051  0.0179  0.0247  226  ALA A CB  
1590  N N   . ALA A 229  ? 0.1844 0.1516 0.1946 0.0054  0.0151  0.0277  227  ALA A N   
1591  C CA  . ALA A 229  ? 0.1776 0.1437 0.1882 0.0053  0.0133  0.0286  227  ALA A CA  
1592  C C   . ALA A 229  ? 0.2163 0.1789 0.2254 0.0070  0.0132  0.0275  227  ALA A C   
1593  O O   . ALA A 229  ? 0.1973 0.1589 0.2061 0.0091  0.0146  0.0263  227  ALA A O   
1594  C CB  . ALA A 229  ? 0.1948 0.1622 0.2088 0.0061  0.0128  0.0300  227  ALA A CB  
1595  N N   . THR A 230  ? 0.1901 0.1513 0.1985 0.0059  0.0115  0.0279  228  THR A N   
1596  C CA  . THR A 230  ? 0.2117 0.1692 0.2190 0.0072  0.0109  0.0267  228  THR A CA  
1597  C C   . THR A 230  ? 0.1886 0.1441 0.1989 0.0080  0.0088  0.0277  228  THR A C   
1598  O O   . THR A 230  ? 0.1852 0.1376 0.1957 0.0100  0.0083  0.0261  228  THR A O   
1599  C CB  . THR A 230  ? 0.2160 0.1730 0.2209 0.0053  0.0102  0.0266  228  THR A CB  
1600  O OG1 . THR A 230  ? 0.3144 0.2733 0.3171 0.0046  0.0118  0.0256  228  THR A OG1 
1601  C CG2 . THR A 230  ? 0.2852 0.2386 0.2890 0.0065  0.0095  0.0252  228  THR A CG2 
1602  N N   . THR A 231  ? 0.1869 0.1441 0.1997 0.0066  0.0074  0.0301  229  THR A N   
1603  C CA  . THR A 231  ? 0.1784 0.1338 0.1947 0.0071  0.0050  0.0315  229  THR A CA  
1604  C C   . THR A 231  ? 0.1745 0.1324 0.1938 0.0075  0.0050  0.0331  229  THR A C   
1605  O O   . THR A 231  ? 0.1786 0.1400 0.1971 0.0065  0.0064  0.0334  229  THR A O   
1606  C CB  . THR A 231  ? 0.1900 0.1452 0.2069 0.0045  0.0027  0.0340  229  THR A CB  
1607  O OG1 . THR A 231  ? 0.2050 0.1650 0.2216 0.0021  0.0027  0.0363  229  THR A OG1 
1608  C CG2 . THR A 231  ? 0.1973 0.1511 0.2111 0.0036  0.0029  0.0328  229  THR A CG2 
1609  N N   . ALA A 232  ? 0.1715 0.1274 0.1946 0.0088  0.0030  0.0339  230  ALA A N   
1610  C CA  . ALA A 232  ? 0.1691 0.1274 0.1955 0.0090  0.0025  0.0358  230  ALA A CA  
1611  C C   . ALA A 232  ? 0.2087 0.1710 0.2349 0.0058  0.0016  0.0389  230  ALA A C   
1612  O O   . ALA A 232  ? 0.2124 0.1785 0.2394 0.0053  0.0023  0.0397  230  ALA A O   
1613  C CB  . ALA A 232  ? 0.1894 0.1446 0.2204 0.0109  0.0000  0.0363  230  ALA A CB  
1614  N N   . ALA A 233  ? 0.1954 0.1575 0.2206 0.0034  0.0000  0.0407  231  ALA A N   
1615  C CA  . ALA A 233  ? 0.2098 0.1768 0.2346 0.0004  -0.0008 0.0436  231  ALA A CA  
1616  C C   . ALA A 233  ? 0.2006 0.1715 0.2220 -0.0005 0.0015  0.0419  231  ALA A C   
1617  O O   . ALA A 233  ? 0.2228 0.1983 0.2444 -0.0019 0.0014  0.0432  231  ALA A O   
1618  C CB  . ALA A 233  ? 0.2522 0.2190 0.2767 -0.0019 -0.0028 0.0460  231  ALA A CB  
1619  N N   . ASP A 234  ? 0.1999 0.1690 0.2182 0.0002  0.0034  0.0389  232  ASP A N   
1620  C CA  . ASP A 234  ? 0.2111 0.1831 0.2270 -0.0005 0.0054  0.0371  232  ASP A CA  
1621  C C   . ASP A 234  ? 0.2021 0.1757 0.2199 0.0006  0.0064  0.0367  232  ASP A C   
1622  O O   . ASP A 234  ? 0.2214 0.1990 0.2392 -0.0007 0.0067  0.0367  232  ASP A O   
1623  C CB  . ASP A 234  ? 0.2902 0.2594 0.3033 0.0006  0.0072  0.0342  232  ASP A CB  
1624  C CG  . ASP A 234  ? 0.3796 0.3481 0.3902 -0.0007 0.0066  0.0341  232  ASP A CG  
1625  O OD1 . ASP A 234  ? 0.3407 0.3123 0.3511 -0.0029 0.0053  0.0359  232  ASP A OD1 
1626  O OD2 . ASP A 234  ? 0.3805 0.3460 0.3893 0.0005  0.0076  0.0320  232  ASP A OD2 
1627  N N   . ALA A 235  ? 0.1809 0.1518 0.2006 0.0031  0.0069  0.0361  233  ALA A N   
1628  C CA  . ALA A 235  ? 0.1689 0.1418 0.1908 0.0042  0.0081  0.0358  233  ALA A CA  
1629  C C   . ALA A 235  ? 0.2127 0.1890 0.2373 0.0030  0.0065  0.0382  233  ALA A C   
1630  O O   . ALA A 235  ? 0.1935 0.1733 0.2192 0.0024  0.0071  0.0382  233  ALA A O   
1631  C CB  . ALA A 235  ? 0.1923 0.1625 0.2158 0.0073  0.0089  0.0347  233  ALA A CB  
1632  N N   . GLU A 236  ? 0.1981 0.1738 0.2243 0.0026  0.0042  0.0405  234  GLU A N   
1633  C CA  . GLU A 236  ? 0.1634 0.1427 0.1922 0.0014  0.0025  0.0433  234  GLU A CA  
1634  C C   . GLU A 236  ? 0.1939 0.1782 0.2203 -0.0014 0.0022  0.0438  234  GLU A C   
1635  O O   . GLU A 236  ? 0.1880 0.1766 0.2159 -0.0022 0.0017  0.0446  234  GLU A O   
1636  C CB  . GLU A 236  ? 0.2023 0.1795 0.2336 0.0015  -0.0002 0.0460  234  GLU A CB  
1637  C CG  . GLU A 236  ? 0.2654 0.2462 0.2998 0.0005  -0.0023 0.0494  234  GLU A CG  
1638  C CD  . GLU A 236  ? 0.3798 0.3620 0.4174 0.0023  -0.0016 0.0489  234  GLU A CD  
1639  O OE1 . GLU A 236  ? 0.3835 0.3632 0.4218 0.0048  0.0001  0.0464  234  GLU A OE1 
1640  O OE2 . GLU A 236  ? 0.3513 0.3379 0.3909 0.0012  -0.0029 0.0512  234  GLU A OE2 
1641  N N   . ARG A 237  ? 0.1899 0.1741 0.2130 -0.0027 0.0025  0.0429  235  ARG A N   
1642  C CA  . ARG A 237  ? 0.2046 0.1940 0.2254 -0.0050 0.0024  0.0425  235  ARG A CA  
1643  C C   . ARG A 237  ? 0.2322 0.2232 0.2529 -0.0047 0.0041  0.0398  235  ARG A C   
1644  O O   . ARG A 237  ? 0.1908 0.1867 0.2120 -0.0059 0.0034  0.0398  235  ARG A O   
1645  C CB  . ARG A 237  ? 0.2388 0.2277 0.2563 -0.0061 0.0026  0.0418  235  ARG A CB  
1646  C CG  . ARG A 237  ? 0.3169 0.3112 0.3318 -0.0079 0.0029  0.0402  235  ARG A CG  
1647  C CD  . ARG A 237  ? 0.3869 0.3818 0.3990 -0.0091 0.0028  0.0402  235  ARG A CD  
1648  N NE  . ARG A 237  ? 0.3831 0.3722 0.3940 -0.0077 0.0041  0.0382  235  ARG A NE  
1649  C CZ  . ARG A 237  ? 0.4214 0.4097 0.4305 -0.0071 0.0057  0.0349  235  ARG A CZ  
1650  N NH1 . ARG A 237  ? 0.4690 0.4612 0.4776 -0.0078 0.0061  0.0328  235  ARG A NH1 
1651  N NH2 . ARG A 237  ? 0.4851 0.4684 0.4932 -0.0059 0.0067  0.0335  235  ARG A NH2 
1652  N N   . TYR A 238  ? 0.1867 0.1739 0.2071 -0.0031 0.0060  0.0375  236  TYR A N   
1653  C CA  . TYR A 238  ? 0.1599 0.1484 0.1809 -0.0030 0.0073  0.0355  236  TYR A CA  
1654  C C   . TYR A 238  ? 0.1597 0.1505 0.1844 -0.0026 0.0069  0.0367  236  TYR A C   
1655  O O   . TYR A 238  ? 0.1871 0.1812 0.2130 -0.0036 0.0068  0.0358  236  TYR A O   
1656  C CB  . TYR A 238  ? 0.1814 0.1657 0.2016 -0.0014 0.0093  0.0336  236  TYR A CB  
1657  C CG  . TYR A 238  ? 0.2060 0.1887 0.2228 -0.0019 0.0098  0.0320  236  TYR A CG  
1658  C CD1 . TYR A 238  ? 0.2517 0.2375 0.2669 -0.0037 0.0092  0.0307  236  TYR A CD1 
1659  C CD2 . TYR A 238  ? 0.2070 0.1854 0.2222 -0.0005 0.0108  0.0314  236  TYR A CD2 
1660  C CE1 . TYR A 238  ? 0.2768 0.2613 0.2892 -0.0040 0.0097  0.0291  236  TYR A CE1 
1661  C CE2 . TYR A 238  ? 0.2446 0.2217 0.2570 -0.0009 0.0111  0.0299  236  TYR A CE2 
1662  C CZ  . TYR A 238  ? 0.2680 0.2481 0.2790 -0.0026 0.0106  0.0289  236  TYR A CZ  
1663  O OH  . TYR A 238  ? 0.3192 0.2983 0.3277 -0.0029 0.0110  0.0273  236  TYR A OH  
1664  N N   . TYR A 239  ? 0.1829 0.1720 0.2098 -0.0011 0.0065  0.0385  237  TYR A N   
1665  C CA  . TYR A 239  ? 0.1658 0.1574 0.1965 -0.0006 0.0060  0.0398  237  TYR A CA  
1666  C C   . TYR A 239  ? 0.1896 0.1863 0.2208 -0.0027 0.0040  0.0412  237  TYR A C   
1667  O O   . TYR A 239  ? 0.1597 0.1598 0.1928 -0.0033 0.0039  0.0408  237  TYR A O   
1668  C CB  . TYR A 239  ? 0.1861 0.1750 0.2192 0.0015  0.0055  0.0414  237  TYR A CB  
1669  C CG  . TYR A 239  ? 0.1909 0.1828 0.2282 0.0021  0.0049  0.0428  237  TYR A CG  
1670  C CD1 . TYR A 239  ? 0.2047 0.1999 0.2437 0.0009  0.0026  0.0453  237  TYR A CD1 
1671  C CD2 . TYR A 239  ? 0.1905 0.1828 0.2300 0.0036  0.0067  0.0418  237  TYR A CD2 
1672  C CE1 . TYR A 239  ? 0.2631 0.2613 0.3060 0.0014  0.0020  0.0465  237  TYR A CE1 
1673  C CE2 . TYR A 239  ? 0.2054 0.2009 0.2490 0.0041  0.0062  0.0431  237  TYR A CE2 
1674  C CZ  . TYR A 239  ? 0.2447 0.2430 0.2900 0.0030  0.0038  0.0453  237  TYR A CZ  
1675  O OH  . TYR A 239  ? 0.2939 0.2956 0.3434 0.0035  0.0032  0.0466  237  TYR A OH  
1676  N N   . ARG A 240  ? 0.1659 0.1636 0.1958 -0.0038 0.0023  0.0432  238  ARG A N   
1677  C CA  . ARG A 240  ? 0.1496 0.1532 0.1800 -0.0056 0.0004  0.0449  238  ARG A CA  
1678  C C   . ARG A 240  ? 0.1435 0.1512 0.1717 -0.0073 0.0007  0.0423  238  ARG A C   
1679  O O   . ARG A 240  ? 0.1844 0.1974 0.2136 -0.0084 -0.0005 0.0424  238  ARG A O   
1680  C CB  . ARG A 240  ? 0.2346 0.2391 0.2645 -0.0066 -0.0016 0.0483  238  ARG A CB  
1681  C CG  . ARG A 240  ? 0.1955 0.1997 0.2217 -0.0078 -0.0014 0.0478  238  ARG A CG  
1682  C CD  . ARG A 240  ? 0.1813 0.1880 0.2073 -0.0094 -0.0037 0.0519  238  ARG A CD  
1683  N NE  . ARG A 240  ? 0.2330 0.2382 0.2561 -0.0102 -0.0034 0.0515  238  ARG A NE  
1684  C CZ  . ARG A 240  ? 0.2736 0.2729 0.2972 -0.0092 -0.0033 0.0519  238  ARG A CZ  
1685  N NH1 . ARG A 240  ? 0.2420 0.2363 0.2689 -0.0073 -0.0038 0.0528  238  ARG A NH1 
1686  N NH2 . ARG A 240  ? 0.3158 0.3142 0.3365 -0.0101 -0.0029 0.0512  238  ARG A NH2 
1687  N N   . ASP A 241  ? 0.1651 0.1704 0.1906 -0.0073 0.0021  0.0396  239  ASP A N   
1688  C CA  . ASP A 241  ? 0.1606 0.1691 0.1848 -0.0084 0.0023  0.0365  239  ASP A CA  
1689  C C   . ASP A 241  ? 0.1938 0.2025 0.2211 -0.0080 0.0029  0.0347  239  ASP A C   
1690  O O   . ASP A 241  ? 0.1957 0.2089 0.2238 -0.0091 0.0019  0.0332  239  ASP A O   
1691  C CB  . ASP A 241  ? 0.2228 0.2283 0.2439 -0.0083 0.0036  0.0342  239  ASP A CB  
1692  C CG  . ASP A 241  ? 0.2941 0.3009 0.3122 -0.0092 0.0028  0.0357  239  ASP A CG  
1693  O OD1 . ASP A 241  ? 0.3678 0.3784 0.3862 -0.0102 0.0012  0.0386  239  ASP A OD1 
1694  O OD2 . ASP A 241  ? 0.3996 0.4037 0.4154 -0.0089 0.0038  0.0343  239  ASP A OD2 
1695  N N   . TYR A 242  ? 0.1721 0.1763 0.2014 -0.0064 0.0044  0.0350  240  TYR A N   
1696  C CA  . TYR A 242  ? 0.1649 0.1699 0.1978 -0.0062 0.0049  0.0342  240  TYR A CA  
1697  C C   . TYR A 242  ? 0.1413 0.1507 0.1771 -0.0067 0.0033  0.0359  240  TYR A C   
1698  O O   . TYR A 242  ? 0.1455 0.1581 0.1837 -0.0076 0.0026  0.0346  240  TYR A O   
1699  C CB  . TYR A 242  ? 0.1516 0.1522 0.1860 -0.0043 0.0069  0.0347  240  TYR A CB  
1700  C CG  . TYR A 242  ? 0.1383 0.1349 0.1708 -0.0037 0.0086  0.0330  240  TYR A CG  
1701  C CD1 . TYR A 242  ? 0.1772 0.1742 0.2093 -0.0049 0.0086  0.0305  240  TYR A CD1 
1702  C CD2 . TYR A 242  ? 0.1614 0.1541 0.1928 -0.0019 0.0102  0.0337  240  TYR A CD2 
1703  C CE1 . TYR A 242  ? 0.2003 0.1937 0.2310 -0.0043 0.0101  0.0293  240  TYR A CE1 
1704  C CE2 . TYR A 242  ? 0.1581 0.1477 0.1877 -0.0013 0.0117  0.0324  240  TYR A CE2 
1705  C CZ  . TYR A 242  ? 0.1406 0.1304 0.1698 -0.0026 0.0116  0.0304  240  TYR A CZ  
1706  O OH  . TYR A 242  ? 0.1660 0.1527 0.1937 -0.0020 0.0130  0.0294  240  TYR A OH  
1707  N N   . GLU A 243  ? 0.1378 0.1474 0.1740 -0.0061 0.0025  0.0388  241  GLU A N   
1708  C CA  . GLU A 243  ? 0.1252 0.1390 0.1643 -0.0064 0.0009  0.0408  241  GLU A CA  
1709  C C   . GLU A 243  ? 0.1498 0.1697 0.1877 -0.0085 -0.0010 0.0400  241  GLU A C   
1710  O O   . GLU A 243  ? 0.1504 0.1742 0.1909 -0.0092 -0.0020 0.0394  241  GLU A O   
1711  C CB  . GLU A 243  ? 0.1662 0.1787 0.2062 -0.0053 0.0000  0.0442  241  GLU A CB  
1712  C CG  . GLU A 243  ? 0.1799 0.1964 0.2233 -0.0054 -0.0018 0.0467  241  GLU A CG  
1713  C CD  . GLU A 243  ? 0.2465 0.2617 0.2907 -0.0047 -0.0033 0.0503  241  GLU A CD  
1714  O OE1 . GLU A 243  ? 0.3360 0.3487 0.3774 -0.0049 -0.0035 0.0509  241  GLU A OE1 
1715  O OE2 . GLU A 243  ? 0.2218 0.2385 0.2697 -0.0039 -0.0045 0.0525  241  GLU A OE2 
1716  N N   . SER A 244  ? 0.1543 0.1754 0.1883 -0.0095 -0.0016 0.0397  242  SER A N   
1717  C CA  . SER A 244  ? 0.1533 0.1814 0.1858 -0.0113 -0.0033 0.0386  242  SER A CA  
1718  C C   . SER A 244  ? 0.1663 0.1957 0.1995 -0.0118 -0.0031 0.0342  242  SER A C   
1719  O O   . SER A 244  ? 0.1829 0.2180 0.2172 -0.0128 -0.0047 0.0329  242  SER A O   
1720  C CB  . SER A 244  ? 0.1909 0.2208 0.2191 -0.0122 -0.0037 0.0394  242  SER A CB  
1721  O OG  . SER A 244  ? 0.2540 0.2801 0.2799 -0.0118 -0.0021 0.0368  242  SER A OG  
1722  N N   . ALA A 245  ? 0.1441 0.1683 0.1771 -0.0111 -0.0013 0.0319  243  ALA A N   
1723  C CA  . ALA A 245  ? 0.1285 0.1533 0.1631 -0.0115 -0.0014 0.0279  243  ALA A CA  
1724  C C   . ALA A 245  ? 0.1233 0.1488 0.1629 -0.0116 -0.0019 0.0281  243  ALA A C   
1725  O O   . ALA A 245  ? 0.1366 0.1656 0.1783 -0.0126 -0.0033 0.0254  243  ALA A O   
1726  C CB  . ALA A 245  ? 0.1534 0.1723 0.1870 -0.0108 0.0005  0.0261  243  ALA A CB  
1727  N N   . ILE A 246  ? 0.1303 0.1529 0.1723 -0.0105 -0.0008 0.0311  244  ILE A N   
1728  C CA  . ILE A 246  ? 0.1234 0.1475 0.1705 -0.0106 -0.0012 0.0316  244  ILE A CA  
1729  C C   . ILE A 246  ? 0.1381 0.1688 0.1862 -0.0117 -0.0036 0.0319  244  ILE A C   
1730  O O   . ILE A 246  ? 0.1308 0.1643 0.1824 -0.0126 -0.0048 0.0301  244  ILE A O   
1731  C CB  . ILE A 246  ? 0.1102 0.1310 0.1594 -0.0089 0.0005  0.0348  244  ILE A CB  
1732  C CG1 . ILE A 246  ? 0.1419 0.1573 0.1907 -0.0079 0.0029  0.0340  244  ILE A CG1 
1733  C CG2 . ILE A 246  ? 0.1421 0.1658 0.1966 -0.0090 -0.0001 0.0360  244  ILE A CG2 
1734  C CD1 . ILE A 246  ? 0.1343 0.1468 0.1840 -0.0059 0.0047  0.0365  244  ILE A CD1 
1735  N N   . HIS A 247  ? 0.1314 0.1649 0.1770 -0.0118 -0.0047 0.0342  245  HIS A N   
1736  C CA  . HIS A 247  ? 0.1307 0.1713 0.1767 -0.0129 -0.0071 0.0346  245  HIS A CA  
1737  C C   . HIS A 247  ? 0.1330 0.1780 0.1779 -0.0143 -0.0085 0.0302  245  HIS A C   
1738  O O   . HIS A 247  ? 0.1439 0.1935 0.1916 -0.0151 -0.0103 0.0286  245  HIS A O   
1739  C CB  . HIS A 247  ? 0.1484 0.1915 0.1916 -0.0130 -0.0081 0.0382  245  HIS A CB  
1740  C CG  . HIS A 247  ? 0.1510 0.1914 0.1966 -0.0117 -0.0078 0.0424  245  HIS A CG  
1741  N ND1 . HIS A 247  ? 0.1693 0.2120 0.2193 -0.0114 -0.0087 0.0441  245  HIS A ND1 
1742  C CD2 . HIS A 247  ? 0.1922 0.2280 0.2369 -0.0105 -0.0069 0.0451  245  HIS A CD2 
1743  C CE1 . HIS A 247  ? 0.2221 0.2617 0.2739 -0.0099 -0.0084 0.0474  245  HIS A CE1 
1744  N NE2 . HIS A 247  ? 0.2026 0.2378 0.2512 -0.0093 -0.0073 0.0480  245  HIS A NE2 
1745  N N   . ALA A 248  ? 0.1513 0.1954 0.1924 -0.0144 -0.0079 0.0278  246  ALA A N   
1746  C CA  . ALA A 248  ? 0.1471 0.1956 0.1871 -0.0153 -0.0093 0.0231  246  ALA A CA  
1747  C C   . ALA A 248  ? 0.1526 0.1989 0.1973 -0.0155 -0.0096 0.0195  246  ALA A C   
1748  O O   . ALA A 248  ? 0.1578 0.2090 0.2044 -0.0163 -0.0117 0.0163  246  ALA A O   
1749  C CB  . ALA A 248  ? 0.1563 0.2040 0.1917 -0.0152 -0.0084 0.0213  246  ALA A CB  
1750  N N   . ILE A 249  ? 0.1350 0.1742 0.1818 -0.0147 -0.0076 0.0202  247  ILE A N   
1751  C CA  . ILE A 249  ? 0.1293 0.1660 0.1812 -0.0151 -0.0079 0.0176  247  ILE A CA  
1752  C C   . ILE A 249  ? 0.1406 0.1801 0.1975 -0.0157 -0.0092 0.0190  247  ILE A C   
1753  O O   . ILE A 249  ? 0.1255 0.1668 0.1865 -0.0167 -0.0110 0.0160  247  ILE A O   
1754  C CB  . ILE A 249  ? 0.1289 0.1580 0.1815 -0.0142 -0.0053 0.0190  247  ILE A CB  
1755  C CG1 . ILE A 249  ? 0.1268 0.1534 0.1748 -0.0137 -0.0044 0.0171  247  ILE A CG1 
1756  C CG2 . ILE A 249  ? 0.1507 0.1775 0.2094 -0.0148 -0.0056 0.0176  247  ILE A CG2 
1757  C CD1 . ILE A 249  ? 0.1513 0.1711 0.1986 -0.0125 -0.0017 0.0193  247  ILE A CD1 
1758  N N   . GLY A 250  ? 0.1238 0.1638 0.1809 -0.0151 -0.0085 0.0233  248  GLY A N   
1759  C CA  . GLY A 250  ? 0.1286 0.1717 0.1907 -0.0156 -0.0096 0.0249  248  GLY A CA  
1760  C C   . GLY A 250  ? 0.1372 0.1877 0.1992 -0.0167 -0.0126 0.0230  248  GLY A C   
1761  O O   . GLY A 250  ? 0.1453 0.1986 0.2121 -0.0176 -0.0144 0.0216  248  GLY A O   
1762  N N   . LYS A 251  ? 0.1373 0.1918 0.1942 -0.0167 -0.0134 0.0232  249  LYS A N   
1763  C CA  . LYS A 251  ? 0.1422 0.2049 0.1983 -0.0178 -0.0162 0.0211  249  LYS A CA  
1764  C C   . LYS A 251  ? 0.1489 0.2129 0.2069 -0.0185 -0.0178 0.0150  249  LYS A C   
1765  O O   . LYS A 251  ? 0.1741 0.2433 0.2351 -0.0194 -0.0203 0.0127  249  LYS A O   
1766  C CB  . LYS A 251  ? 0.1463 0.2134 0.1963 -0.0178 -0.0165 0.0222  249  LYS A CB  
1767  C CG  . LYS A 251  ? 0.1788 0.2462 0.2275 -0.0173 -0.0161 0.0281  249  LYS A CG  
1768  C CD  . LYS A 251  ? 0.1908 0.2609 0.2336 -0.0175 -0.0159 0.0292  249  LYS A CD  
1769  C CE  . LYS A 251  ? 0.2141 0.2842 0.2559 -0.0172 -0.0159 0.0353  249  LYS A CE  
1770  N NZ  . LYS A 251  ? 0.2047 0.2786 0.2412 -0.0178 -0.0161 0.0364  249  LYS A NZ  
1771  N N   . ALA A 252  ? 0.1617 0.2211 0.2183 -0.0181 -0.0166 0.0122  250  ALA A N   
1772  C CA  . ALA A 252  ? 0.1482 0.2081 0.2071 -0.0186 -0.0183 0.0061  250  ALA A CA  
1773  C C   . ALA A 252  ? 0.1781 0.2342 0.2443 -0.0192 -0.0189 0.0055  250  ALA A C   
1774  O O   . ALA A 252  ? 0.1898 0.2486 0.2599 -0.0201 -0.0215 0.0011  250  ALA A O   
1775  C CB  . ALA A 252  ? 0.1744 0.2300 0.2300 -0.0179 -0.0168 0.0038  250  ALA A CB  
1776  N N   . SER A 253  ? 0.1411 0.1914 0.2097 -0.0189 -0.0166 0.0097  251  SER A N   
1777  C CA  . SER A 253  ? 0.1618 0.2093 0.2378 -0.0197 -0.0170 0.0099  251  SER A CA  
1778  C C   . SER A 253  ? 0.1672 0.2206 0.2473 -0.0208 -0.0197 0.0093  251  SER A C   
1779  O O   . SER A 253  ? 0.1663 0.2198 0.2523 -0.0219 -0.0218 0.0065  251  SER A O   
1780  C CB  . SER A 253  ? 0.1441 0.1865 0.2213 -0.0190 -0.0140 0.0151  251  SER A CB  
1781  O OG  . SER A 253  ? 0.1640 0.2049 0.2485 -0.0199 -0.0144 0.0158  251  SER A OG  
1782  N N   . ALA A 254  ? 0.1645 0.2228 0.2419 -0.0205 -0.0199 0.0122  252  ALA A N   
1783  C CA  . ALA A 254  ? 0.1840 0.2491 0.2643 -0.0214 -0.0227 0.0117  252  ALA A CA  
1784  C C   . ALA A 254  ? 0.1988 0.2624 0.2872 -0.0224 -0.0233 0.0125  252  ALA A C   
1785  O O   . ALA A 254  ? 0.2073 0.2744 0.3003 -0.0236 -0.0263 0.0092  252  ALA A O   
1786  C CB  . ALA A 254  ? 0.1720 0.2430 0.2505 -0.0220 -0.0257 0.0058  252  ALA A CB  
1787  N N   . GLY A 255  ? 0.1548 0.2136 0.2453 -0.0218 -0.0206 0.0169  253  GLY A N   
1788  C CA  . GLY A 255  ? 0.1891 0.2474 0.2874 -0.0227 -0.0208 0.0187  253  GLY A CA  
1789  C C   . GLY A 255  ? 0.2029 0.2570 0.3067 -0.0239 -0.0213 0.0163  253  GLY A C   
1790  O O   . GLY A 255  ? 0.2008 0.2555 0.3119 -0.0252 -0.0221 0.0176  253  GLY A O   
1791  N N   . ARG A 256  ? 0.1594 0.2095 0.2607 -0.0237 -0.0211 0.0132  254  ARG A N   
1792  C CA  . ARG A 256  ? 0.1746 0.2203 0.2817 -0.0249 -0.0218 0.0112  254  ARG A CA  
1793  C C   . ARG A 256  ? 0.1776 0.2187 0.2881 -0.0248 -0.0189 0.0162  254  ARG A C   
1794  O O   . ARG A 256  ? 0.1863 0.2245 0.3033 -0.0262 -0.0197 0.0160  254  ARG A O   
1795  C CB  . ARG A 256  ? 0.1636 0.2063 0.2671 -0.0244 -0.0224 0.0066  254  ARG A CB  
1796  C CG  . ARG A 256  ? 0.2061 0.2533 0.3098 -0.0249 -0.0263 0.0001  254  ARG A CG  
1797  C CD  . ARG A 256  ? 0.1881 0.2329 0.2880 -0.0241 -0.0265 -0.0046 254  ARG A CD  
1798  N NE  . ARG A 256  ? 0.1763 0.2227 0.2671 -0.0225 -0.0243 -0.0035 254  ARG A NE  
1799  C CZ  . ARG A 256  ? 0.2000 0.2448 0.2863 -0.0215 -0.0238 -0.0065 254  ARG A CZ  
1800  N NH1 . ARG A 256  ? 0.2249 0.2657 0.3146 -0.0216 -0.0250 -0.0105 254  ARG A NH1 
1801  N NH2 . ARG A 256  ? 0.2096 0.2570 0.2882 -0.0204 -0.0221 -0.0052 254  ARG A NH2 
1802  N N   . GLY A 257  ? 0.1715 0.2120 0.2778 -0.0233 -0.0156 0.0206  255  GLY A N   
1803  C CA  . GLY A 257  ? 0.1749 0.2122 0.2840 -0.0230 -0.0127 0.0251  255  GLY A CA  
1804  C C   . GLY A 257  ? 0.1510 0.1824 0.2568 -0.0222 -0.0106 0.0251  255  GLY A C   
1805  O O   . GLY A 257  ? 0.1672 0.1966 0.2690 -0.0219 -0.0113 0.0215  255  GLY A O   
1806  N N   . ILE A 258  ? 0.1365 0.1659 0.2445 -0.0219 -0.0079 0.0293  256  ILE A N   
1807  C CA  . ILE A 258  ? 0.1346 0.1590 0.2386 -0.0207 -0.0054 0.0301  256  ILE A CA  
1808  C C   . ILE A 258  ? 0.1515 0.1719 0.2591 -0.0221 -0.0066 0.0282  256  ILE A C   
1809  O O   . ILE A 258  ? 0.1604 0.1766 0.2640 -0.0212 -0.0052 0.0277  256  ILE A O   
1810  C CB  . ILE A 258  ? 0.1371 0.1616 0.2413 -0.0195 -0.0018 0.0351  256  ILE A CB  
1811  C CG1 . ILE A 258  ? 0.1342 0.1603 0.2469 -0.0211 -0.0019 0.0382  256  ILE A CG1 
1812  C CG2 . ILE A 258  ? 0.1471 0.1748 0.2475 -0.0176 -0.0007 0.0367  256  ILE A CG2 
1813  C CD1 . ILE A 258  ? 0.1401 0.1677 0.2530 -0.0198 0.0017  0.0431  256  ILE A CD1 
1814  N N   . TYR A 259  ? 0.1634 0.1846 0.2787 -0.0242 -0.0094 0.0270  257  TYR A N   
1815  C CA  . TYR A 259  ? 0.1360 0.1528 0.2556 -0.0255 -0.0111 0.0252  257  TYR A CA  
1816  C C   . TYR A 259  ? 0.1920 0.2082 0.3107 -0.0258 -0.0145 0.0186  257  TYR A C   
1817  O O   . TYR A 259  ? 0.2040 0.2162 0.3202 -0.0251 -0.0146 0.0162  257  TYR A O   
1818  C CB  . TYR A 259  ? 0.1618 0.1793 0.2916 -0.0279 -0.0124 0.0280  257  TYR A CB  
1819  C CG  . TYR A 259  ? 0.1483 0.1679 0.2792 -0.0275 -0.0090 0.0344  257  TYR A CG  
1820  C CD1 . TYR A 259  ? 0.1491 0.1661 0.2766 -0.0263 -0.0056 0.0377  257  TYR A CD1 
1821  C CD2 . TYR A 259  ? 0.1789 0.2037 0.3141 -0.0283 -0.0090 0.0370  257  TYR A CD2 
1822  C CE1 . TYR A 259  ? 0.1908 0.2106 0.3190 -0.0257 -0.0024 0.0430  257  TYR A CE1 
1823  C CE2 . TYR A 259  ? 0.1676 0.1951 0.3038 -0.0277 -0.0058 0.0425  257  TYR A CE2 
1824  C CZ  . TYR A 259  ? 0.1812 0.2064 0.3138 -0.0263 -0.0025 0.0454  257  TYR A CZ  
1825  O OH  . TYR A 259  ? 0.1830 0.2117 0.3163 -0.0254 0.0008  0.0504  257  TYR A OH  
1826  N N   . GLU A 260  ? 0.1459 0.1666 0.2663 -0.0265 -0.0172 0.0156  258  GLU A N   
1827  C CA  . GLU A 260  ? 0.2128 0.2342 0.3318 -0.0264 -0.0204 0.0090  258  GLU A CA  
1828  C C   . GLU A 260  ? 0.2007 0.2233 0.3097 -0.0244 -0.0189 0.0072  258  GLU A C   
1829  O O   . GLU A 260  ? 0.2400 0.2614 0.3462 -0.0237 -0.0200 0.0026  258  GLU A O   
1830  C CB  . GLU A 260  ? 0.2478 0.2742 0.3714 -0.0277 -0.0240 0.0061  258  GLU A CB  
1831  C CG  . GLU A 260  ? 0.2988 0.3267 0.4212 -0.0275 -0.0274 -0.0014 258  GLU A CG  
1832  C CD  . GLU A 260  ? 0.3581 0.3923 0.4830 -0.0284 -0.0309 -0.0048 258  GLU A CD  
1833  O OE1 . GLU A 260  ? 0.3580 0.3946 0.4881 -0.0297 -0.0314 -0.0017 258  GLU A OE1 
1834  O OE2 . GLU A 260  ? 0.3064 0.3439 0.4281 -0.0276 -0.0331 -0.0108 258  GLU A OE2 
1835  N N   . GLY A 261  ? 0.1637 0.1889 0.2677 -0.0234 -0.0164 0.0108  259  GLY A N   
1836  C CA  . GLY A 261  ? 0.1575 0.1848 0.2530 -0.0218 -0.0155 0.0097  259  GLY A CA  
1837  C C   . GLY A 261  ? 0.1710 0.1937 0.2610 -0.0203 -0.0123 0.0116  259  GLY A C   
1838  O O   . GLY A 261  ? 0.1619 0.1803 0.2541 -0.0203 -0.0104 0.0146  259  GLY A O   
1839  N N   . PRO A 262  ? 0.1432 0.1674 0.2260 -0.0192 -0.0118 0.0100  260  PRO A N   
1840  C CA  . PRO A 262  ? 0.1426 0.1626 0.2200 -0.0178 -0.0092 0.0111  260  PRO A CA  
1841  C C   . PRO A 262  ? 0.1526 0.1714 0.2277 -0.0168 -0.0061 0.0165  260  PRO A C   
1842  O O   . PRO A 262  ? 0.1659 0.1878 0.2421 -0.0168 -0.0060 0.0191  260  PRO A O   
1843  C CB  . PRO A 262  ? 0.1539 0.1773 0.2251 -0.0172 -0.0101 0.0078  260  PRO A CB  
1844  C CG  . PRO A 262  ? 0.1771 0.2071 0.2489 -0.0179 -0.0121 0.0073  260  PRO A CG  
1845  C CD  . PRO A 262  ? 0.1618 0.1920 0.2414 -0.0192 -0.0140 0.0067  260  PRO A CD  
1846  N N   . GLY A 263  ? 0.1243 0.1386 0.1963 -0.0157 -0.0038 0.0179  261  GLY A N   
1847  C CA  . GLY A 263  ? 0.1469 0.1600 0.2160 -0.0144 -0.0010 0.0221  261  GLY A CA  
1848  C C   . GLY A 263  ? 0.1318 0.1421 0.1944 -0.0131 0.0006  0.0218  261  GLY A C   
1849  O O   . GLY A 263  ? 0.1398 0.1500 0.1996 -0.0133 -0.0005 0.0184  261  GLY A O   
1850  N N   . ILE A 264  ? 0.1413 0.1495 0.2015 -0.0117 0.0030  0.0250  262  ILE A N   
1851  C CA  . ILE A 264  ? 0.1164 0.1218 0.1707 -0.0105 0.0044  0.0250  262  ILE A CA  
1852  C C   . ILE A 264  ? 0.1475 0.1488 0.2020 -0.0094 0.0069  0.0271  262  ILE A C   
1853  O O   . ILE A 264  ? 0.1431 0.1447 0.2013 -0.0093 0.0080  0.0296  262  ILE A O   
1854  C CB  . ILE A 264  ? 0.1301 0.1376 0.1808 -0.0096 0.0046  0.0267  262  ILE A CB  
1855  C CG1 . ILE A 264  ? 0.1475 0.1529 0.1923 -0.0089 0.0052  0.0259  262  ILE A CG1 
1856  C CG2 . ILE A 264  ? 0.1384 0.1456 0.1908 -0.0083 0.0062  0.0303  262  ILE A CG2 
1857  C CD1 . ILE A 264  ? 0.1760 0.1834 0.2178 -0.0084 0.0049  0.0278  262  ILE A CD1 
1858  N N   . SER A 265  ? 0.1226 0.1208 0.1730 -0.0087 0.0078  0.0260  263  SER A N   
1859  C CA  . SER A 265  ? 0.1246 0.1192 0.1737 -0.0075 0.0101  0.0279  263  SER A CA  
1860  C C   . SER A 265  ? 0.1709 0.1642 0.2145 -0.0060 0.0112  0.0284  263  SER A C   
1861  O O   . SER A 265  ? 0.1887 0.1826 0.2289 -0.0062 0.0101  0.0268  263  SER A O   
1862  C CB  . SER A 265  ? 0.1643 0.1558 0.2140 -0.0080 0.0099  0.0262  263  SER A CB  
1863  O OG  . SER A 265  ? 0.1898 0.1818 0.2456 -0.0093 0.0089  0.0263  263  SER A OG  
1864  N N   . ILE A 266  ? 0.1415 0.1335 0.1845 -0.0044 0.0132  0.0307  264  ILE A N   
1865  C CA  . ILE A 266  ? 0.1322 0.1226 0.1708 -0.0028 0.0140  0.0312  264  ILE A CA  
1866  C C   . ILE A 266  ? 0.1547 0.1421 0.1915 -0.0015 0.0160  0.0318  264  ILE A C   
1867  O O   . ILE A 266  ? 0.1454 0.1328 0.1847 -0.0015 0.0171  0.0328  264  ILE A O   
1868  C CB  . ILE A 266  ? 0.1509 0.1432 0.1905 -0.0017 0.0142  0.0331  264  ILE A CB  
1869  C CG1 . ILE A 266  ? 0.1651 0.1585 0.2079 -0.0005 0.0159  0.0351  264  ILE A CG1 
1870  C CG2 . ILE A 266  ? 0.1631 0.1589 0.2045 -0.0031 0.0121  0.0330  264  ILE A CG2 
1871  C CD1 . ILE A 266  ? 0.2010 0.1959 0.2445 0.0013  0.0163  0.0365  264  ILE A CD1 
1872  N N   . LYS A 267  ? 0.1448 0.1299 0.1772 -0.0004 0.0164  0.0312  265  LYS A N   
1873  C CA  . LYS A 267  ? 0.1341 0.1168 0.1643 0.0012  0.0182  0.0316  265  LYS A CA  
1874  C C   . LYS A 267  ? 0.1544 0.1368 0.1832 0.0033  0.0189  0.0324  265  LYS A C   
1875  O O   . LYS A 267  ? 0.1528 0.1347 0.1801 0.0033  0.0176  0.0320  265  LYS A O   
1876  C CB  . LYS A 267  ? 0.1738 0.1536 0.2003 0.0009  0.0179  0.0298  265  LYS A CB  
1877  C CG  . LYS A 267  ? 0.2230 0.2022 0.2512 -0.0004 0.0176  0.0290  265  LYS A CG  
1878  C CD  . LYS A 267  ? 0.2308 0.2075 0.2555 -0.0005 0.0173  0.0270  265  LYS A CD  
1879  C CE  . LYS A 267  ? 0.2881 0.2637 0.3149 -0.0014 0.0169  0.0262  265  LYS A CE  
1880  N NZ  . LYS A 267  ? 0.3058 0.2833 0.3366 -0.0030 0.0152  0.0250  265  LYS A NZ  
1881  N N   . LEU A 268  ? 0.1308 0.1141 0.1606 0.0050  0.0206  0.0335  266  LEU A N   
1882  C CA  . LEU A 268  ? 0.1292 0.1125 0.1582 0.0073  0.0211  0.0337  266  LEU A CA  
1883  C C   . LEU A 268  ? 0.1530 0.1327 0.1778 0.0082  0.0207  0.0322  266  LEU A C   
1884  O O   . LEU A 268  ? 0.1456 0.1243 0.1700 0.0094  0.0198  0.0319  266  LEU A O   
1885  C CB  . LEU A 268  ? 0.1482 0.1341 0.1789 0.0092  0.0233  0.0348  266  LEU A CB  
1886  C CG  . LEU A 268  ? 0.1550 0.1450 0.1906 0.0083  0.0237  0.0367  266  LEU A CG  
1887  C CD1 . LEU A 268  ? 0.1764 0.1700 0.2135 0.0101  0.0260  0.0381  266  LEU A CD1 
1888  C CD2 . LEU A 268  ? 0.1642 0.1556 0.2022 0.0080  0.0221  0.0369  266  LEU A CD2 
1889  N N   . SER A 269  ? 0.1490 0.1266 0.1710 0.0076  0.0210  0.0313  267  SER A N   
1890  C CA  . SER A 269  ? 0.1476 0.1220 0.1659 0.0084  0.0205  0.0299  267  SER A CA  
1891  C C   . SER A 269  ? 0.1734 0.1469 0.1911 0.0070  0.0184  0.0296  267  SER A C   
1892  O O   . SER A 269  ? 0.1605 0.1316 0.1760 0.0076  0.0176  0.0290  267  SER A O   
1893  C CB  . SER A 269  ? 0.1585 0.1312 0.1741 0.0079  0.0212  0.0291  267  SER A CB  
1894  O OG  . SER A 269  ? 0.1733 0.1460 0.1893 0.0057  0.0202  0.0287  267  SER A OG  
1895  N N   . ALA A 270  ? 0.1336 0.1093 0.1532 0.0051  0.0173  0.0302  268  ALA A N   
1896  C CA  . ALA A 270  ? 0.1448 0.1209 0.1639 0.0037  0.0154  0.0304  268  ALA A CA  
1897  C C   . ALA A 270  ? 0.1608 0.1371 0.1817 0.0048  0.0144  0.0317  268  ALA A C   
1898  O O   . ALA A 270  ? 0.1618 0.1378 0.1821 0.0040  0.0127  0.0324  268  ALA A O   
1899  C CB  . ALA A 270  ? 0.1580 0.1372 0.1785 0.0016  0.0145  0.0303  268  ALA A CB  
1900  N N   . LEU A 271  ? 0.1417 0.1189 0.1651 0.0065  0.0154  0.0323  269  LEU A N   
1901  C CA  . LEU A 271  ? 0.1587 0.1369 0.1850 0.0075  0.0143  0.0336  269  LEU A CA  
1902  C C   . LEU A 271  ? 0.1478 0.1233 0.1739 0.0101  0.0143  0.0329  269  LEU A C   
1903  O O   . LEU A 271  ? 0.1618 0.1376 0.1907 0.0113  0.0132  0.0338  269  LEU A O   
1904  C CB  . LEU A 271  ? 0.1591 0.1410 0.1890 0.0076  0.0151  0.0345  269  LEU A CB  
1905  C CG  . LEU A 271  ? 0.1875 0.1722 0.2185 0.0050  0.0142  0.0350  269  LEU A CG  
1906  C CD1 . LEU A 271  ? 0.1889 0.1771 0.2241 0.0052  0.0149  0.0359  269  LEU A CD1 
1907  C CD2 . LEU A 271  ? 0.1867 0.1723 0.2177 0.0038  0.0118  0.0360  269  LEU A CD2 
1908  N N   . HIS A 272  ? 0.1512 0.1243 0.1745 0.0112  0.0154  0.0313  270  HIS A N   
1909  C CA  . HIS A 272  ? 0.1780 0.1485 0.2012 0.0138  0.0151  0.0301  270  HIS A CA  
1910  C C   . HIS A 272  ? 0.1820 0.1496 0.2013 0.0138  0.0155  0.0285  270  HIS A C   
1911  O O   . HIS A 272  ? 0.1759 0.1442 0.1930 0.0133  0.0171  0.0281  270  HIS A O   
1912  C CB  . HIS A 272  ? 0.1792 0.1519 0.2043 0.0167  0.0168  0.0294  270  HIS A CB  
1913  C CG  . HIS A 272  ? 0.2087 0.1794 0.2349 0.0196  0.0158  0.0279  270  HIS A CG  
1914  N ND1 . HIS A 272  ? 0.2065 0.1742 0.2302 0.0212  0.0158  0.0257  270  HIS A ND1 
1915  C CD2 . HIS A 272  ? 0.2271 0.1982 0.2572 0.0214  0.0146  0.0281  270  HIS A CD2 
1916  C CE1 . HIS A 272  ? 0.2340 0.2002 0.2600 0.0238  0.0144  0.0243  270  HIS A CE1 
1917  N NE2 . HIS A 272  ? 0.2445 0.2126 0.2745 0.0240  0.0137  0.0257  270  HIS A NE2 
1918  N N   . PRO A 273  ? 0.1622 0.1264 0.1808 0.0144  0.0138  0.0278  271  PRO A N   
1919  C CA  . PRO A 273  ? 0.1771 0.1385 0.1921 0.0144  0.0140  0.0262  271  PRO A CA  
1920  C C   . PRO A 273  ? 0.1810 0.1424 0.1945 0.0171  0.0157  0.0240  271  PRO A C   
1921  O O   . PRO A 273  ? 0.1905 0.1504 0.2008 0.0171  0.0162  0.0228  271  PRO A O   
1922  C CB  . PRO A 273  ? 0.1780 0.1361 0.1939 0.0140  0.0113  0.0264  271  PRO A CB  
1923  C CG  . PRO A 273  ? 0.2065 0.1648 0.2266 0.0156  0.0101  0.0271  271  PRO A CG  
1924  C CD  . PRO A 273  ? 0.1665 0.1291 0.1881 0.0148  0.0113  0.0286  271  PRO A CD  
1925  N N   . ARG A 274  ? 0.1501 0.1137 0.1657 0.0196  0.0167  0.0235  272  ARG A N   
1926  C CA  . ARG A 274  ? 0.1554 0.1203 0.1693 0.0224  0.0185  0.0215  272  ARG A CA  
1927  C C   . ARG A 274  ? 0.1768 0.1467 0.1918 0.0229  0.0210  0.0226  272  ARG A C   
1928  O O   . ARG A 274  ? 0.1922 0.1650 0.2086 0.0257  0.0221  0.0217  272  ARG A O   
1929  C CB  . ARG A 274  ? 0.1680 0.1314 0.1834 0.0256  0.0173  0.0190  272  ARG A CB  
1930  C CG  . ARG A 274  ? 0.1900 0.1483 0.2050 0.0253  0.0146  0.0178  272  ARG A CG  
1931  C CD  . ARG A 274  ? 0.1808 0.1373 0.1914 0.0243  0.0151  0.0168  272  ARG A CD  
1932  N NE  . ARG A 274  ? 0.1968 0.1558 0.2047 0.0267  0.0172  0.0147  272  ARG A NE  
1933  C CZ  . ARG A 274  ? 0.2036 0.1623 0.2112 0.0299  0.0168  0.0115  272  ARG A CZ  
1934  N NH1 . ARG A 274  ? 0.2002 0.1554 0.2104 0.0312  0.0142  0.0098  272  ARG A NH1 
1935  N NH2 . ARG A 274  ? 0.2327 0.1948 0.2374 0.0319  0.0189  0.0100  272  ARG A NH2 
1936  N N   . TYR A 275  ? 0.1802 0.1513 0.1948 0.0203  0.0218  0.0246  273  TYR A N   
1937  C CA  . TYR A 275  ? 0.1559 0.1315 0.1722 0.0202  0.0239  0.0263  273  TYR A CA  
1938  C C   . TYR A 275  ? 0.1609 0.1382 0.1744 0.0213  0.0259  0.0258  273  TYR A C   
1939  O O   . TYR A 275  ? 0.1771 0.1534 0.1886 0.0196  0.0263  0.0265  273  TYR A O   
1940  C CB  . TYR A 275  ? 0.1671 0.1430 0.1847 0.0169  0.0234  0.0283  273  TYR A CB  
1941  C CG  . TYR A 275  ? 0.1466 0.1266 0.1666 0.0163  0.0252  0.0302  273  TYR A CG  
1942  C CD1 . TYR A 275  ? 0.1548 0.1389 0.1778 0.0180  0.0263  0.0309  273  TYR A CD1 
1943  C CD2 . TYR A 275  ? 0.1518 0.1318 0.1715 0.0140  0.0256  0.0312  273  TYR A CD2 
1944  C CE1 . TYR A 275  ? 0.1714 0.1597 0.1969 0.0172  0.0279  0.0331  273  TYR A CE1 
1945  C CE2 . TYR A 275  ? 0.1542 0.1377 0.1768 0.0133  0.0269  0.0333  273  TYR A CE2 
1946  C CZ  . TYR A 275  ? 0.1702 0.1580 0.1956 0.0148  0.0281  0.0344  273  TYR A CZ  
1947  O OH  . TYR A 275  ? 0.1909 0.1825 0.2196 0.0137  0.0293  0.0369  273  TYR A OH  
1948  N N   . SER A 276  ? 0.1714 0.1518 0.1850 0.0244  0.0272  0.0247  274  SER A N   
1949  C CA  . SER A 276  ? 0.1498 0.1330 0.1606 0.0259  0.0292  0.0244  274  SER A CA  
1950  C C   . SER A 276  ? 0.1533 0.1421 0.1655 0.0291  0.0308  0.0238  274  SER A C   
1951  O O   . SER A 276  ? 0.1734 0.1625 0.1881 0.0309  0.0300  0.0223  274  SER A O   
1952  C CB  . SER A 276  ? 0.2458 0.2252 0.2526 0.0268  0.0282  0.0218  274  SER A CB  
1953  O OG  . SER A 276  ? 0.2738 0.2520 0.2808 0.0295  0.0270  0.0188  274  SER A OG  
1954  N N   . ARG A 277  ? 0.1594 0.1531 0.1701 0.0300  0.0331  0.0249  275  ARG A N   
1955  C CA  . ARG A 277  ? 0.1598 0.1603 0.1713 0.0332  0.0350  0.0242  275  ARG A CA  
1956  C C   . ARG A 277  ? 0.1672 0.1667 0.1773 0.0369  0.0340  0.0196  275  ARG A C   
1957  O O   . ARG A 277  ? 0.1588 0.1623 0.1711 0.0398  0.0345  0.0181  275  ARG A O   
1958  C CB  . ARG A 277  ? 0.1791 0.1854 0.1888 0.0333  0.0375  0.0265  275  ARG A CB  
1959  C CG  . ARG A 277  ? 0.1755 0.1905 0.1851 0.0369  0.0397  0.0258  275  ARG A CG  
1960  C CD  . ARG A 277  ? 0.1892 0.2085 0.2037 0.0377  0.0404  0.0266  275  ARG A CD  
1961  N NE  . ARG A 277  ? 0.1602 0.1886 0.1747 0.0414  0.0427  0.0257  275  ARG A NE  
1962  C CZ  . ARG A 277  ? 0.1787 0.2086 0.1925 0.0455  0.0423  0.0211  275  ARG A CZ  
1963  N NH1 . ARG A 277  ? 0.1973 0.2197 0.2108 0.0464  0.0396  0.0173  275  ARG A NH1 
1964  N NH2 . ARG A 277  ? 0.1941 0.2335 0.2081 0.0488  0.0446  0.0203  275  ARG A NH2 
1965  N N   . ALA A 278  ? 0.2014 0.1958 0.2080 0.0370  0.0325  0.0173  276  ALA A N   
1966  C CA  . ALA A 278  ? 0.1972 0.1902 0.2029 0.0404  0.0311  0.0127  276  ALA A CA  
1967  C C   . ALA A 278  ? 0.2065 0.1962 0.2163 0.0411  0.0289  0.0113  276  ALA A C   
1968  O O   . ALA A 278  ? 0.2215 0.2119 0.2325 0.0447  0.0281  0.0076  276  ALA A O   
1969  C CB  . ALA A 278  ? 0.2101 0.1977 0.2119 0.0397  0.0296  0.0108  276  ALA A CB  
1970  N N   . GLN A 279  ? 0.1777 0.1641 0.1900 0.0379  0.0279  0.0141  277  GLN A N   
1971  C CA  . GLN A 279  ? 0.1737 0.1572 0.1901 0.0381  0.0257  0.0137  277  GLN A CA  
1972  C C   . GLN A 279  ? 0.1971 0.1852 0.2174 0.0377  0.0269  0.0163  277  GLN A C   
1973  O O   . GLN A 279  ? 0.1833 0.1690 0.2068 0.0361  0.0252  0.0177  277  GLN A O   
1974  C CB  . GLN A 279  ? 0.1897 0.1664 0.2059 0.0348  0.0232  0.0148  277  GLN A CB  
1975  C CG  . GLN A 279  ? 0.2014 0.1736 0.2142 0.0349  0.0218  0.0125  277  GLN A CG  
1976  C CD  . GLN A 279  ? 0.2347 0.2048 0.2488 0.0383  0.0198  0.0086  277  GLN A CD  
1977  O OE1 . GLN A 279  ? 0.3309 0.2990 0.3491 0.0390  0.0179  0.0082  277  GLN A OE1 
1978  N NE2 . GLN A 279  ? 0.2193 0.1898 0.2303 0.0404  0.0202  0.0054  277  GLN A NE2 
1979  N N   . ALA A 280  ? 0.1745 0.1696 0.1948 0.0391  0.0297  0.0170  278  ALA A N   
1980  C CA  . ALA A 280  ? 0.1811 0.1810 0.2052 0.0382  0.0310  0.0200  278  ALA A CA  
1981  C C   . ALA A 280  ? 0.1852 0.1849 0.2140 0.0400  0.0294  0.0189  278  ALA A C   
1982  O O   . ALA A 280  ? 0.1938 0.1942 0.2261 0.0380  0.0290  0.0215  278  ALA A O   
1983  C CB  . ALA A 280  ? 0.1978 0.2062 0.2215 0.0398  0.0342  0.0209  278  ALA A CB  
1984  N N   . ALA A 281  ? 0.1725 0.1717 0.2019 0.0438  0.0283  0.0150  279  ALA A N   
1985  C CA  . ALA A 281  ? 0.2009 0.1997 0.2354 0.0456  0.0265  0.0140  279  ALA A CA  
1986  C C   . ALA A 281  ? 0.1937 0.1857 0.2299 0.0425  0.0235  0.0158  279  ALA A C   
1987  O O   . ALA A 281  ? 0.2118 0.2046 0.2522 0.0419  0.0226  0.0177  279  ALA A O   
1988  C CB  . ALA A 281  ? 0.2387 0.2374 0.2739 0.0504  0.0255  0.0089  279  ALA A CB  
1989  N N   . ARG A 282  ? 0.1693 0.1551 0.2024 0.0406  0.0220  0.0156  280  ARG A N   
1990  C CA  . ARG A 282  ? 0.1733 0.1538 0.2078 0.0374  0.0193  0.0178  280  ARG A CA  
1991  C C   . ARG A 282  ? 0.1876 0.1703 0.2221 0.0337  0.0204  0.0217  280  ARG A C   
1992  O O   . ARG A 282  ? 0.1927 0.1742 0.2300 0.0318  0.0187  0.0238  280  ARG A O   
1993  C CB  . ARG A 282  ? 0.2005 0.1749 0.2317 0.0360  0.0175  0.0168  280  ARG A CB  
1994  C CG  . ARG A 282  ? 0.2226 0.1934 0.2547 0.0391  0.0154  0.0130  280  ARG A CG  
1995  C CD  . ARG A 282  ? 0.2134 0.1780 0.2433 0.0368  0.0132  0.0131  280  ARG A CD  
1996  N NE  . ARG A 282  ? 0.2004 0.1622 0.2325 0.0335  0.0110  0.0165  280  ARG A NE  
1997  C CZ  . ARG A 282  ? 0.1975 0.1554 0.2279 0.0305  0.0094  0.0180  280  ARG A CZ  
1998  N NH1 . ARG A 282  ? 0.2140 0.1697 0.2405 0.0302  0.0097  0.0163  280  ARG A NH1 
1999  N NH2 . ARG A 282  ? 0.2394 0.1962 0.2718 0.0277  0.0076  0.0213  280  ARG A NH2 
2000  N N   . VAL A 283  ? 0.1620 0.1476 0.1937 0.0325  0.0229  0.0227  281  VAL A N   
2001  C CA  . VAL A 283  ? 0.1591 0.1467 0.1915 0.0291  0.0237  0.0260  281  VAL A CA  
2002  C C   . VAL A 283  ? 0.1845 0.1766 0.2217 0.0296  0.0240  0.0275  281  VAL A C   
2003  O O   . VAL A 283  ? 0.1693 0.1609 0.2088 0.0271  0.0227  0.0296  281  VAL A O   
2004  C CB  . VAL A 283  ? 0.1697 0.1597 0.1990 0.0281  0.0262  0.0268  281  VAL A CB  
2005  C CG1 . VAL A 283  ? 0.2017 0.1944 0.2331 0.0250  0.0270  0.0299  281  VAL A CG1 
2006  C CG2 . VAL A 283  ? 0.1731 0.1583 0.1979 0.0269  0.0255  0.0257  281  VAL A CG2 
2007  N N   . MET A 284  ? 0.1716 0.1687 0.2106 0.0328  0.0257  0.0264  282  MET A N   
2008  C CA  . MET A 284  ? 0.1683 0.1704 0.2122 0.0334  0.0261  0.0279  282  MET A CA  
2009  C C   . MET A 284  ? 0.2186 0.2178 0.2660 0.0342  0.0233  0.0275  282  MET A C   
2010  O O   . MET A 284  ? 0.2183 0.2198 0.2696 0.0330  0.0227  0.0296  282  MET A O   
2011  C CB  . MET A 284  ? 0.1762 0.1851 0.2211 0.0368  0.0287  0.0268  282  MET A CB  
2012  C CG  . MET A 284  ? 0.1812 0.1939 0.2231 0.0359  0.0316  0.0281  282  MET A CG  
2013  S SD  . MET A 284  ? 0.2182 0.2320 0.2614 0.0309  0.0322  0.0326  282  MET A SD  
2014  C CE  . MET A 284  ? 0.2279 0.2487 0.2777 0.0315  0.0328  0.0346  282  MET A CE  
2015  N N   . GLY A 285  ? 0.1680 0.1624 0.2147 0.0360  0.0213  0.0250  283  GLY A N   
2016  C CA  . GLY A 285  ? 0.1821 0.1738 0.2328 0.0370  0.0183  0.0248  283  GLY A CA  
2017  C C   . GLY A 285  ? 0.2081 0.1954 0.2586 0.0333  0.0158  0.0274  283  GLY A C   
2018  O O   . GLY A 285  ? 0.2162 0.2033 0.2707 0.0329  0.0137  0.0290  283  GLY A O   
2019  N N   . GLU A 286  ? 0.1670 0.1512 0.2131 0.0305  0.0159  0.0279  284  GLU A N   
2020  C CA  . GLU A 286  ? 0.1806 0.1609 0.2258 0.0273  0.0135  0.0298  284  GLU A CA  
2021  C C   . GLU A 286  ? 0.1985 0.1806 0.2416 0.0235  0.0145  0.0320  284  GLU A C   
2022  O O   . GLU A 286  ? 0.2263 0.2084 0.2705 0.0210  0.0128  0.0342  284  GLU A O   
2023  C CB  . GLU A 286  ? 0.2014 0.1762 0.2434 0.0273  0.0123  0.0282  284  GLU A CB  
2024  C CG  . GLU A 286  ? 0.1938 0.1660 0.2382 0.0309  0.0107  0.0255  284  GLU A CG  
2025  C CD  . GLU A 286  ? 0.2079 0.1752 0.2492 0.0311  0.0097  0.0234  284  GLU A CD  
2026  O OE1 . GLU A 286  ? 0.2369 0.2018 0.2753 0.0279  0.0091  0.0250  284  GLU A OE1 
2027  O OE2 . GLU A 286  ? 0.2694 0.2355 0.3113 0.0346  0.0095  0.0200  284  GLU A OE2 
2028  N N   . LEU A 287  ? 0.1579 0.1417 0.1982 0.0230  0.0170  0.0315  285  LEU A N   
2029  C CA  . LEU A 287  ? 0.1685 0.1536 0.2074 0.0197  0.0177  0.0331  285  LEU A CA  
2030  C C   . LEU A 287  ? 0.1958 0.1859 0.2385 0.0190  0.0184  0.0349  285  LEU A C   
2031  O O   . LEU A 287  ? 0.1758 0.1668 0.2195 0.0163  0.0173  0.0365  285  LEU A O   
2032  C CB  . LEU A 287  ? 0.1796 0.1644 0.2147 0.0194  0.0199  0.0321  285  LEU A CB  
2033  C CG  . LEU A 287  ? 0.2606 0.2443 0.2933 0.0161  0.0198  0.0328  285  LEU A CG  
2034  C CD1 . LEU A 287  ? 0.2242 0.2072 0.2535 0.0165  0.0217  0.0319  285  LEU A CD1 
2035  C CD2 . LEU A 287  ? 0.2515 0.2384 0.2868 0.0138  0.0198  0.0346  285  LEU A CD2 
2036  N N   . LEU A 288  ? 0.1610 0.1549 0.2061 0.0215  0.0202  0.0346  286  LEU A N   
2037  C CA  . LEU A 288  ? 0.1818 0.1809 0.2311 0.0209  0.0209  0.0365  286  LEU A CA  
2038  C C   . LEU A 288  ? 0.1878 0.1873 0.2404 0.0198  0.0185  0.0379  286  LEU A C   
2039  O O   . LEU A 288  ? 0.1709 0.1727 0.2251 0.0172  0.0181  0.0395  286  LEU A O   
2040  C CB  . LEU A 288  ? 0.2036 0.2074 0.2551 0.0242  0.0231  0.0358  286  LEU A CB  
2041  C CG  . LEU A 288  ? 0.2505 0.2601 0.3072 0.0240  0.0236  0.0378  286  LEU A CG  
2042  C CD1 . LEU A 288  ? 0.2163 0.2281 0.2733 0.0206  0.0247  0.0399  286  LEU A CD1 
2043  C CD2 . LEU A 288  ? 0.2988 0.3134 0.3578 0.0278  0.0255  0.0368  286  LEU A CD2 
2044  N N   . PRO A 289  ? 0.1791 0.1766 0.2332 0.0215  0.0165  0.0375  287  PRO A N   
2045  C CA  . PRO A 289  ? 0.1816 0.1800 0.2388 0.0203  0.0141  0.0394  287  PRO A CA  
2046  C C   . PRO A 289  ? 0.1649 0.1620 0.2199 0.0165  0.0126  0.0407  287  PRO A C   
2047  O O   . PRO A 289  ? 0.1691 0.1690 0.2265 0.0147  0.0112  0.0424  287  PRO A O   
2048  C CB  . PRO A 289  ? 0.2145 0.2097 0.2733 0.0228  0.0120  0.0387  287  PRO A CB  
2049  C CG  . PRO A 289  ? 0.2486 0.2436 0.3068 0.0264  0.0139  0.0360  287  PRO A CG  
2050  C CD  . PRO A 289  ? 0.1960 0.1908 0.2497 0.0250  0.0162  0.0352  287  PRO A CD  
2051  N N   . ARG A 290  ? 0.1503 0.1438 0.2008 0.0153  0.0126  0.0397  288  ARG A N   
2052  C CA  . ARG A 290  ? 0.1451 0.1381 0.1933 0.0119  0.0114  0.0405  288  ARG A CA  
2053  C C   . ARG A 290  ? 0.1556 0.1519 0.2042 0.0099  0.0125  0.0406  288  ARG A C   
2054  O O   . ARG A 290  ? 0.1464 0.1450 0.1959 0.0076  0.0111  0.0415  288  ARG A O   
2055  C CB  . ARG A 290  ? 0.1886 0.1773 0.2321 0.0113  0.0113  0.0393  288  ARG A CB  
2056  C CG  . ARG A 290  ? 0.2001 0.1853 0.2437 0.0126  0.0094  0.0395  288  ARG A CG  
2057  C CD  . ARG A 290  ? 0.2324 0.2133 0.2719 0.0126  0.0096  0.0380  288  ARG A CD  
2058  N NE  . ARG A 290  ? 0.2765 0.2540 0.3173 0.0143  0.0078  0.0380  288  ARG A NE  
2059  C CZ  . ARG A 290  ? 0.2791 0.2526 0.3176 0.0154  0.0078  0.0362  288  ARG A CZ  
2060  N NH1 . ARG A 290  ? 0.2589 0.2317 0.2935 0.0151  0.0097  0.0345  288  ARG A NH1 
2061  N NH2 . ARG A 290  ? 0.2966 0.2667 0.3372 0.0170  0.0057  0.0362  288  ARG A NH2 
2062  N N   . VAL A 291  ? 0.1532 0.1501 0.2015 0.0106  0.0150  0.0398  289  VAL A N   
2063  C CA  . VAL A 291  ? 0.1445 0.1443 0.1944 0.0087  0.0158  0.0402  289  VAL A CA  
2064  C C   . VAL A 291  ? 0.1432 0.1475 0.1981 0.0085  0.0152  0.0417  289  VAL A C   
2065  O O   . VAL A 291  ? 0.1490 0.1555 0.2056 0.0061  0.0142  0.0422  289  VAL A O   
2066  C CB  . VAL A 291  ? 0.1781 0.1780 0.2273 0.0095  0.0185  0.0398  289  VAL A CB  
2067  C CG1 . VAL A 291  ? 0.1893 0.1916 0.2408 0.0071  0.0189  0.0406  289  VAL A CG1 
2068  C CG2 . VAL A 291  ? 0.1971 0.1927 0.2414 0.0098  0.0189  0.0383  289  VAL A CG2 
2069  N N   . LYS A 292  ? 0.1288 0.1346 0.1864 0.0111  0.0156  0.0423  290  LYS A N   
2070  C CA  . LYS A 292  ? 0.1242 0.1346 0.1868 0.0111  0.0150  0.0438  290  LYS A CA  
2071  C C   . LYS A 292  ? 0.1687 0.1796 0.2320 0.0092  0.0121  0.0447  290  LYS A C   
2072  O O   . LYS A 292  ? 0.1271 0.1416 0.1932 0.0074  0.0113  0.0455  290  LYS A O   
2073  C CB  . LYS A 292  ? 0.1415 0.1536 0.2070 0.0147  0.0156  0.0438  290  LYS A CB  
2074  C CG  . LYS A 292  ? 0.1576 0.1748 0.2286 0.0148  0.0150  0.0455  290  LYS A CG  
2075  C CD  . LYS A 292  ? 0.1821 0.2013 0.2565 0.0185  0.0154  0.0453  290  LYS A CD  
2076  C CE  . LYS A 292  ? 0.1559 0.1804 0.2360 0.0184  0.0145  0.0470  290  LYS A CE  
2077  N NZ  . LYS A 292  ? 0.1834 0.2107 0.2673 0.0224  0.0152  0.0466  290  LYS A NZ  
2078  N N   . ALA A 293  ? 0.1510 0.1586 0.2116 0.0093  0.0104  0.0446  291  ALA A N   
2079  C CA  . ALA A 293  ? 0.1231 0.1320 0.1840 0.0074  0.0077  0.0459  291  ALA A CA  
2080  C C   . ALA A 293  ? 0.1384 0.1487 0.1974 0.0042  0.0072  0.0452  291  ALA A C   
2081  O O   . ALA A 293  ? 0.1563 0.1704 0.2172 0.0025  0.0055  0.0460  291  ALA A O   
2082  C CB  . ALA A 293  ? 0.1470 0.1523 0.2056 0.0080  0.0059  0.0464  291  ALA A CB  
2083  N N   . LEU A 294  ? 0.1235 0.1311 0.1789 0.0035  0.0085  0.0435  292  LEU A N   
2084  C CA  . LEU A 294  ? 0.1416 0.1505 0.1958 0.0008  0.0079  0.0422  292  LEU A CA  
2085  C C   . LEU A 294  ? 0.1253 0.1376 0.1838 -0.0001 0.0084  0.0423  292  LEU A C   
2086  O O   . LEU A 294  ? 0.1380 0.1532 0.1978 -0.0022 0.0068  0.0418  292  LEU A O   
2087  C CB  . LEU A 294  ? 0.1404 0.1454 0.1905 0.0005  0.0092  0.0404  292  LEU A CB  
2088  C CG  . LEU A 294  ? 0.1282 0.1300 0.1739 0.0008  0.0086  0.0402  292  LEU A CG  
2089  C CD1 . LEU A 294  ? 0.1549 0.1532 0.1971 0.0008  0.0101  0.0384  292  LEU A CD1 
2090  C CD2 . LEU A 294  ? 0.1353 0.1395 0.1796 -0.0011 0.0062  0.0406  292  LEU A CD2 
2091  N N   . ALA A 295  ? 0.1351 0.1475 0.1961 0.0015  0.0105  0.0429  293  ALA A N   
2092  C CA  . ALA A 295  ? 0.1220 0.1380 0.1878 0.0005  0.0109  0.0435  293  ALA A CA  
2093  C C   . ALA A 295  ? 0.1399 0.1603 0.2098 0.0002  0.0092  0.0448  293  ALA A C   
2094  O O   . ALA A 295  ? 0.1264 0.1499 0.1997 -0.0018 0.0082  0.0448  293  ALA A O   
2095  C CB  . ALA A 295  ? 0.1273 0.1436 0.1947 0.0024  0.0137  0.0444  293  ALA A CB  
2096  N N   . LEU A 296  ? 0.1101 0.1309 0.1803 0.0020  0.0085  0.0460  294  LEU A N   
2097  C CA  . LEU A 296  ? 0.1105 0.1356 0.1845 0.0017  0.0066  0.0474  294  LEU A CA  
2098  C C   . LEU A 296  ? 0.1368 0.1635 0.2095 -0.0010 0.0040  0.0468  294  LEU A C   
2099  O O   . LEU A 296  ? 0.1405 0.1716 0.2168 -0.0023 0.0025  0.0472  294  LEU A O   
2100  C CB  . LEU A 296  ? 0.1254 0.1499 0.1999 0.0043  0.0060  0.0488  294  LEU A CB  
2101  C CG  . LEU A 296  ? 0.1397 0.1646 0.2170 0.0074  0.0081  0.0491  294  LEU A CG  
2102  C CD1 . LEU A 296  ? 0.1907 0.2134 0.2678 0.0100  0.0072  0.0497  294  LEU A CD1 
2103  C CD2 . LEU A 296  ? 0.2005 0.2310 0.2837 0.0074  0.0085  0.0503  294  LEU A CD2 
2104  N N   . LEU A 297  ? 0.1337 0.1577 0.2014 -0.0017 0.0034  0.0457  295  LEU A N   
2105  C CA  A LEU A 297  ? 0.1431 0.1695 0.2091 -0.0041 0.0011  0.0447  295  LEU A CA  
2106  C CA  B LEU A 297  ? 0.1437 0.1699 0.2095 -0.0041 0.0011  0.0446  295  LEU A CA  
2107  C C   . LEU A 297  ? 0.1313 0.1590 0.1988 -0.0061 0.0011  0.0424  295  LEU A C   
2108  O O   . LEU A 297  ? 0.1390 0.1708 0.2083 -0.0077 -0.0010 0.0417  295  LEU A O   
2109  C CB  A LEU A 297  ? 0.1654 0.1891 0.2258 -0.0044 0.0006  0.0442  295  LEU A CB  
2110  C CB  B LEU A 297  ? 0.1643 0.1874 0.2244 -0.0043 0.0010  0.0439  295  LEU A CB  
2111  C CG  A LEU A 297  ? 0.1559 0.1837 0.2144 -0.0063 -0.0020 0.0440  295  LEU A CG  
2112  C CG  B LEU A 297  ? 0.1893 0.2140 0.2475 -0.0045 -0.0011 0.0457  295  LEU A CG  
2113  C CD1 A LEU A 297  ? 0.1983 0.2300 0.2595 -0.0060 -0.0039 0.0470  295  LEU A CD1 
2114  C CD1 B LEU A 297  ? 0.1916 0.2124 0.2448 -0.0044 -0.0006 0.0453  295  LEU A CD1 
2115  C CD2 A LEU A 297  ? 0.2157 0.2413 0.2688 -0.0067 -0.0021 0.0437  295  LEU A CD2 
2116  C CD2 B LEU A 297  ? 0.1959 0.2262 0.2541 -0.0068 -0.0034 0.0451  295  LEU A CD2 
2117  N N   . ALA A 298  ? 0.1116 0.1357 0.1784 -0.0059 0.0031  0.0412  296  ALA A N   
2118  C CA  . ALA A 298  ? 0.1215 0.1462 0.1908 -0.0077 0.0029  0.0394  296  ALA A CA  
2119  C C   . ALA A 298  ? 0.1397 0.1685 0.2153 -0.0083 0.0023  0.0406  296  ALA A C   
2120  O O   . ALA A 298  ? 0.1422 0.1734 0.2206 -0.0103 0.0005  0.0391  296  ALA A O   
2121  C CB  . ALA A 298  ? 0.1327 0.1531 0.2009 -0.0072 0.0052  0.0388  296  ALA A CB  
2122  N N   . LYS A 299  ? 0.1248 0.1545 0.2030 -0.0065 0.0038  0.0431  297  LYS A N   
2123  C CA  A LYS A 299  ? 0.1158 0.1500 0.2003 -0.0070 0.0033  0.0446  297  LYS A CA  
2124  C CA  B LYS A 299  ? 0.1158 0.1500 0.2003 -0.0070 0.0033  0.0446  297  LYS A CA  
2125  C C   . LYS A 299  ? 0.1400 0.1785 0.2258 -0.0082 0.0003  0.0443  297  LYS A C   
2126  O O   . LYS A 299  ? 0.1357 0.1775 0.2260 -0.0100 -0.0012 0.0438  297  LYS A O   
2127  C CB  A LYS A 299  ? 0.1148 0.1500 0.2014 -0.0044 0.0053  0.0471  297  LYS A CB  
2128  C CB  B LYS A 299  ? 0.1148 0.1499 0.2013 -0.0044 0.0053  0.0471  297  LYS A CB  
2129  C CG  A LYS A 299  ? 0.1430 0.1837 0.2358 -0.0044 0.0045  0.0489  297  LYS A CG  
2130  C CG  B LYS A 299  ? 0.1431 0.1836 0.2359 -0.0044 0.0047  0.0489  297  LYS A CG  
2131  C CD  A LYS A 299  ? 0.1567 0.1988 0.2516 -0.0015 0.0066  0.0509  297  LYS A CD  
2132  C CD  B LYS A 299  ? 0.1561 0.1979 0.2511 -0.0016 0.0071  0.0508  297  LYS A CD  
2133  C CE  A LYS A 299  ? 0.1634 0.2111 0.2641 -0.0013 0.0054  0.0526  297  LYS A CE  
2134  C CE  B LYS A 299  ? 0.1670 0.2144 0.2677 -0.0011 0.0063  0.0526  297  LYS A CE  
2135  N NZ  A LYS A 299  ? 0.1665 0.2164 0.2699 0.0018  0.0075  0.0542  297  LYS A NZ  
2136  N NZ  B LYS A 299  ? 0.1752 0.2233 0.2749 -0.0006 0.0037  0.0528  297  LYS A NZ  
2137  N N   . ASN A 300  ? 0.1409 0.1796 0.2231 -0.0075 -0.0009 0.0447  298  ASN A N   
2138  C CA  . ASN A 300  ? 0.1184 0.1620 0.2019 -0.0085 -0.0038 0.0450  298  ASN A CA  
2139  C C   . ASN A 300  ? 0.1258 0.1714 0.2086 -0.0110 -0.0059 0.0420  298  ASN A C   
2140  O O   . ASN A 300  ? 0.1717 0.2220 0.2579 -0.0124 -0.0081 0.0415  298  ASN A O   
2141  C CB  . ASN A 300  ? 0.1523 0.1962 0.2324 -0.0074 -0.0049 0.0467  298  ASN A CB  
2142  C CG  . ASN A 300  ? 0.2305 0.2803 0.3128 -0.0083 -0.0078 0.0479  298  ASN A CG  
2143  O OD1 . ASN A 300  ? 0.3423 0.3948 0.4293 -0.0074 -0.0081 0.0500  298  ASN A OD1 
2144  N ND2 . ASN A 300  ? 0.2256 0.2781 0.3047 -0.0100 -0.0100 0.0466  298  ASN A ND2 
2145  N N   . TYR A 301  ? 0.1277 0.1698 0.2063 -0.0116 -0.0054 0.0396  299  TYR A N   
2146  C CA  . TYR A 301  ? 0.1371 0.1808 0.2154 -0.0136 -0.0073 0.0359  299  TYR A CA  
2147  C C   . TYR A 301  ? 0.1484 0.1908 0.2317 -0.0148 -0.0070 0.0344  299  TYR A C   
2148  O O   . TYR A 301  ? 0.1593 0.2030 0.2437 -0.0164 -0.0090 0.0310  299  TYR A O   
2149  C CB  . TYR A 301  ? 0.1265 0.1676 0.1985 -0.0136 -0.0070 0.0339  299  TYR A CB  
2150  C CG  . TYR A 301  ? 0.1175 0.1612 0.1848 -0.0133 -0.0081 0.0350  299  TYR A CG  
2151  C CD1 . TYR A 301  ? 0.1445 0.1945 0.2114 -0.0145 -0.0108 0.0339  299  TYR A CD1 
2152  C CD2 . TYR A 301  ? 0.1368 0.1769 0.2002 -0.0119 -0.0065 0.0370  299  TYR A CD2 
2153  C CE1 . TYR A 301  ? 0.1270 0.1800 0.1895 -0.0144 -0.0119 0.0355  299  TYR A CE1 
2154  C CE2 . TYR A 301  ? 0.1363 0.1789 0.1960 -0.0119 -0.0077 0.0385  299  TYR A CE2 
2155  C CZ  . TYR A 301  ? 0.1473 0.1965 0.2065 -0.0132 -0.0103 0.0380  299  TYR A CZ  
2156  O OH  . TYR A 301  ? 0.1539 0.2061 0.2093 -0.0134 -0.0116 0.0402  299  TYR A OH  
2157  N N   . ASP A 302  ? 0.1139 0.1539 0.2003 -0.0139 -0.0046 0.0367  300  ASP A N   
2158  C CA  . ASP A 302  ? 0.1308 0.1692 0.2221 -0.0150 -0.0040 0.0363  300  ASP A CA  
2159  C C   . ASP A 302  ? 0.1326 0.1670 0.2217 -0.0159 -0.0042 0.0332  300  ASP A C   
2160  O O   . ASP A 302  ? 0.1385 0.1732 0.2312 -0.0177 -0.0061 0.0307  300  ASP A O   
2161  C CB  . ASP A 302  ? 0.1170 0.1599 0.2151 -0.0169 -0.0064 0.0360  300  ASP A CB  
2162  C CG  . ASP A 302  ? 0.1882 0.2302 0.2928 -0.0178 -0.0053 0.0376  300  ASP A CG  
2163  O OD1 . ASP A 302  ? 0.1825 0.2222 0.2865 -0.0165 -0.0023 0.0402  300  ASP A OD1 
2164  O OD2 . ASP A 302  ? 0.1759 0.2198 0.2861 -0.0199 -0.0075 0.0363  300  ASP A OD2 
2165  N N   . ILE A 303  ? 0.1136 0.1440 0.1970 -0.0145 -0.0023 0.0333  301  ILE A N   
2166  C CA  . ILE A 303  ? 0.1110 0.1373 0.1922 -0.0149 -0.0020 0.0308  301  ILE A CA  
2167  C C   . ILE A 303  ? 0.1222 0.1443 0.2030 -0.0137 0.0011  0.0331  301  ILE A C   
2168  O O   . ILE A 303  ? 0.1217 0.1442 0.2024 -0.0122 0.0031  0.0362  301  ILE A O   
2169  C CB  . ILE A 303  ? 0.1299 0.1557 0.2043 -0.0144 -0.0027 0.0283  301  ILE A CB  
2170  C CG1 . ILE A 303  ? 0.1257 0.1495 0.1951 -0.0125 -0.0005 0.0308  301  ILE A CG1 
2171  C CG2 . ILE A 303  ? 0.1441 0.1753 0.2185 -0.0154 -0.0056 0.0264  301  ILE A CG2 
2172  C CD1 . ILE A 303  ? 0.1711 0.1939 0.2342 -0.0123 -0.0009 0.0289  301  ILE A CD1 
2173  N N   . GLY A 304  ? 0.1338 0.1523 0.2147 -0.0144 0.0012  0.0315  302  GLY A N   
2174  C CA  . GLY A 304  ? 0.1210 0.1358 0.2008 -0.0133 0.0040  0.0336  302  GLY A CA  
2175  C C   . GLY A 304  ? 0.1271 0.1395 0.1998 -0.0114 0.0056  0.0336  302  GLY A C   
2176  O O   . GLY A 304  ? 0.1384 0.1505 0.2068 -0.0113 0.0045  0.0313  302  GLY A O   
2177  N N   . LEU A 305  ? 0.1105 0.1216 0.1822 -0.0097 0.0083  0.0363  303  LEU A N   
2178  C CA  . LEU A 305  ? 0.1162 0.1243 0.1818 -0.0079 0.0099  0.0362  303  LEU A CA  
2179  C C   . LEU A 305  ? 0.1355 0.1410 0.2011 -0.0072 0.0122  0.0376  303  LEU A C   
2180  O O   . LEU A 305  ? 0.1294 0.1367 0.1975 -0.0063 0.0140  0.0403  303  LEU A O   
2181  C CB  . LEU A 305  ? 0.1366 0.1464 0.2007 -0.0061 0.0106  0.0379  303  LEU A CB  
2182  C CG  . LEU A 305  ? 0.1681 0.1747 0.2264 -0.0042 0.0117  0.0376  303  LEU A CG  
2183  C CD1 . LEU A 305  ? 0.2167 0.2247 0.2735 -0.0033 0.0106  0.0382  303  LEU A CD1 
2184  C CD2 . LEU A 305  ? 0.2408 0.2459 0.2986 -0.0023 0.0144  0.0392  303  LEU A CD2 
2185  N N   . ASN A 306  ? 0.1356 0.1375 0.1982 -0.0074 0.0122  0.0359  304  ASN A N   
2186  C CA  . ASN A 306  ? 0.1237 0.1232 0.1864 -0.0070 0.0140  0.0372  304  ASN A CA  
2187  C C   . ASN A 306  ? 0.1468 0.1437 0.2035 -0.0050 0.0157  0.0371  304  ASN A C   
2188  O O   . ASN A 306  ? 0.1513 0.1464 0.2036 -0.0047 0.0149  0.0349  304  ASN A O   
2189  C CB  . ASN A 306  ? 0.1492 0.1463 0.2138 -0.0088 0.0124  0.0352  304  ASN A CB  
2190  C CG  . ASN A 306  ? 0.1542 0.1485 0.2183 -0.0084 0.0139  0.0366  304  ASN A CG  
2191  O OD1 . ASN A 306  ? 0.1941 0.1853 0.2535 -0.0076 0.0143  0.0352  304  ASN A OD1 
2192  N ND2 . ASN A 306  ? 0.1367 0.1324 0.2056 -0.0090 0.0148  0.0398  304  ASN A ND2 
2193  N N   . ILE A 307  ? 0.1346 0.1318 0.1912 -0.0036 0.0181  0.0394  305  ILE A N   
2194  C CA  . ILE A 307  ? 0.1376 0.1325 0.1890 -0.0016 0.0197  0.0391  305  ILE A CA  
2195  C C   . ILE A 307  ? 0.1336 0.1256 0.1841 -0.0022 0.0200  0.0390  305  ILE A C   
2196  O O   . ILE A 307  ? 0.1375 0.1306 0.1911 -0.0026 0.0210  0.0413  305  ILE A O   
2197  C CB  . ILE A 307  ? 0.1437 0.1412 0.1951 0.0007  0.0220  0.0412  305  ILE A CB  
2198  C CG1 . ILE A 307  ? 0.1614 0.1613 0.2139 0.0015  0.0214  0.0412  305  ILE A CG1 
2199  C CG2 . ILE A 307  ? 0.1754 0.1706 0.2216 0.0028  0.0235  0.0406  305  ILE A CG2 
2200  C CD1 . ILE A 307  ? 0.1968 0.2005 0.2509 0.0037  0.0234  0.0431  305  ILE A CD1 
2201  N N   . ASP A 308  ? 0.1368 0.1254 0.1833 -0.0022 0.0191  0.0365  306  ASP A N   
2202  C CA  . ASP A 308  ? 0.1386 0.1242 0.1840 -0.0026 0.0193  0.0360  306  ASP A CA  
2203  C C   . ASP A 308  ? 0.1310 0.1164 0.1738 -0.0008 0.0216  0.0379  306  ASP A C   
2204  O O   . ASP A 308  ? 0.1448 0.1313 0.1849 0.0011  0.0229  0.0382  306  ASP A O   
2205  C CB  . ASP A 308  ? 0.1486 0.1315 0.1899 -0.0028 0.0179  0.0328  306  ASP A CB  
2206  C CG  . ASP A 308  ? 0.1961 0.1795 0.2398 -0.0046 0.0155  0.0304  306  ASP A CG  
2207  O OD1 . ASP A 308  ? 0.1937 0.1790 0.2427 -0.0059 0.0145  0.0310  306  ASP A OD1 
2208  O OD2 . ASP A 308  ? 0.2251 0.2074 0.2657 -0.0047 0.0144  0.0277  306  ASP A OD2 
2209  N N   . ALA A 309  ? 0.1310 0.1152 0.1749 -0.0013 0.0220  0.0391  307  ALA A N   
2210  C CA  . ALA A 309  ? 0.1261 0.1108 0.1676 0.0003  0.0241  0.0410  307  ALA A CA  
2211  C C   . ALA A 309  ? 0.1510 0.1319 0.1873 0.0011  0.0239  0.0388  307  ALA A C   
2212  O O   . ALA A 309  ? 0.1571 0.1351 0.1935 -0.0001 0.0223  0.0370  307  ALA A O   
2213  C CB  . ALA A 309  ? 0.1282 0.1146 0.1743 -0.0008 0.0247  0.0446  307  ALA A CB  
2214  N N   . GLU A 310  ? 0.1493 0.1306 0.1812 0.0033  0.0255  0.0389  308  GLU A N   
2215  C CA  . GLU A 310  ? 0.1584 0.1364 0.1853 0.0042  0.0253  0.0367  308  GLU A CA  
2216  C C   . GLU A 310  ? 0.1483 0.1269 0.1731 0.0054  0.0270  0.0384  308  GLU A C   
2217  O O   . GLU A 310  ? 0.1497 0.1296 0.1776 0.0046  0.0274  0.0411  308  GLU A O   
2218  C CB  . GLU A 310  ? 0.1543 0.1316 0.1777 0.0055  0.0251  0.0346  308  GLU A CB  
2219  C CG  . GLU A 310  ? 0.1740 0.1513 0.1994 0.0040  0.0233  0.0333  308  GLU A CG  
2220  C CD  . GLU A 310  ? 0.1661 0.1425 0.1886 0.0049  0.0226  0.0317  308  GLU A CD  
2221  O OE1 . GLU A 310  ? 0.2079 0.1818 0.2271 0.0048  0.0219  0.0300  308  GLU A OE1 
2222  O OE2 . GLU A 310  ? 0.1702 0.1486 0.1941 0.0056  0.0228  0.0324  308  GLU A OE2 
2223  N N   . GLU A 311  ? 0.1506 0.1285 0.1706 0.0074  0.0277  0.0370  309  GLU A N   
2224  C CA  . GLU A 311  ? 0.1761 0.1548 0.1937 0.0087  0.0290  0.0382  309  GLU A CA  
2225  C C   . GLU A 311  ? 0.1360 0.1200 0.1552 0.0097  0.0310  0.0413  309  GLU A C   
2226  O O   . GLU A 311  ? 0.1538 0.1408 0.1751 0.0103  0.0317  0.0417  309  GLU A O   
2227  C CB  . GLU A 311  ? 0.1677 0.1445 0.1799 0.0106  0.0291  0.0356  309  GLU A CB  
2228  C CG  . GLU A 311  ? 0.1933 0.1656 0.2035 0.0096  0.0272  0.0329  309  GLU A CG  
2229  C CD  . GLU A 311  ? 0.2149 0.1859 0.2251 0.0092  0.0260  0.0310  309  GLU A CD  
2230  O OE1 . GLU A 311  ? 0.1936 0.1667 0.2063 0.0092  0.0262  0.0317  309  GLU A OE1 
2231  O OE2 . GLU A 311  ? 0.2803 0.2486 0.2884 0.0087  0.0247  0.0289  309  GLU A OE2 
2232  N N   . ALA A 312  ? 0.1526 0.1385 0.1712 0.0101  0.0321  0.0437  310  ALA A N   
2233  C CA  . ALA A 312  ? 0.1224 0.1146 0.1428 0.0108  0.0341  0.0471  310  ALA A CA  
2234  C C   . ALA A 312  ? 0.1498 0.1456 0.1673 0.0137  0.0357  0.0456  310  ALA A C   
2235  O O   . ALA A 312  ? 0.1598 0.1612 0.1799 0.0144  0.0372  0.0476  310  ALA A O   
2236  C CB  . ALA A 312  ? 0.1699 0.1637 0.1894 0.0108  0.0348  0.0501  310  ALA A CB  
2237  N N   . ASP A 313  ? 0.1668 0.1600 0.1797 0.0156  0.0352  0.0419  311  ASP A N   
2238  C CA  . ASP A 313  ? 0.1610 0.1573 0.1718 0.0186  0.0363  0.0399  311  ASP A CA  
2239  C C   . ASP A 313  ? 0.1533 0.1491 0.1667 0.0188  0.0356  0.0384  311  ASP A C   
2240  O O   . ASP A 313  ? 0.1899 0.1878 0.2023 0.0214  0.0362  0.0365  311  ASP A O   
2241  C CB  . ASP A 313  ? 0.1597 0.1535 0.1651 0.0208  0.0359  0.0364  311  ASP A CB  
2242  C CG  . ASP A 313  ? 0.2301 0.2170 0.2342 0.0197  0.0336  0.0335  311  ASP A CG  
2243  O OD1 . ASP A 313  ? 0.1937 0.1780 0.2007 0.0175  0.0324  0.0339  311  ASP A OD1 
2244  O OD2 . ASP A 313  ? 0.2836 0.2682 0.2838 0.0211  0.0330  0.0309  311  ASP A OD2 
2245  N N   . ARG A 314  ? 0.1435 0.1368 0.1604 0.0161  0.0343  0.0393  312  ARG A N   
2246  C CA  . ARG A 314  ? 0.1404 0.1340 0.1603 0.0160  0.0336  0.0386  312  ARG A CA  
2247  C C   . ARG A 314  ? 0.1421 0.1402 0.1672 0.0147  0.0344  0.0419  312  ARG A C   
2248  O O   . ARG A 314  ? 0.1580 0.1574 0.1859 0.0148  0.0341  0.0416  312  ARG A O   
2249  C CB  . ARG A 314  ? 0.1652 0.1531 0.1849 0.0141  0.0312  0.0367  312  ARG A CB  
2250  C CG  . ARG A 314  ? 0.1741 0.1582 0.1895 0.0156  0.0303  0.0336  312  ARG A CG  
2251  C CD  . ARG A 314  ? 0.1947 0.1740 0.2091 0.0135  0.0283  0.0323  312  ARG A CD  
2252  N NE  . ARG A 314  ? 0.1968 0.1733 0.2087 0.0147  0.0271  0.0298  312  ARG A NE  
2253  C CZ  . ARG A 314  ? 0.1721 0.1450 0.1825 0.0133  0.0254  0.0286  312  ARG A CZ  
2254  N NH1 . ARG A 314  ? 0.1926 0.1643 0.2032 0.0110  0.0247  0.0289  312  ARG A NH1 
2255  N NH2 . ARG A 314  ? 0.2057 0.1763 0.2147 0.0142  0.0242  0.0269  312  ARG A NH2 
2256  N N   . LEU A 315  ? 0.1530 0.1537 0.1799 0.0134  0.0354  0.0452  313  LEU A N   
2257  C CA  . LEU A 315  ? 0.1438 0.1485 0.1765 0.0116  0.0359  0.0486  313  LEU A CA  
2258  C C   . LEU A 315  ? 0.1524 0.1635 0.1867 0.0137  0.0375  0.0492  313  LEU A C   
2259  O O   . LEU A 315  ? 0.1414 0.1536 0.1796 0.0130  0.0370  0.0495  313  LEU A O   
2260  C CB  . LEU A 315  ? 0.1397 0.1466 0.1740 0.0102  0.0367  0.0525  313  LEU A CB  
2261  C CG  . LEU A 315  ? 0.1612 0.1697 0.2023 0.0072  0.0360  0.0562  313  LEU A CG  
2262  C CD1 . LEU A 315  ? 0.1793 0.1889 0.2215 0.0059  0.0365  0.0600  313  LEU A CD1 
2263  C CD2 . LEU A 315  ? 0.1961 0.2111 0.2415 0.0074  0.0373  0.0584  313  LEU A CD2 
2264  N N   . GLU A 316  ? 0.1595 0.1753 0.1911 0.0164  0.0396  0.0494  314  GLU A N   
2265  C CA  . GLU A 316  ? 0.1456 0.1686 0.1793 0.0184  0.0414  0.0502  314  GLU A CA  
2266  C C   . GLU A 316  ? 0.1488 0.1700 0.1823 0.0204  0.0404  0.0464  314  GLU A C   
2267  O O   . GLU A 316  ? 0.1677 0.1929 0.2051 0.0209  0.0408  0.0471  314  GLU A O   
2268  C CB  . GLU A 316  ? 0.1555 0.1851 0.1863 0.0210  0.0439  0.0511  314  GLU A CB  
2269  C CG  . GLU A 316  ? 0.1700 0.2034 0.2030 0.0186  0.0449  0.0564  314  GLU A CG  
2270  C CD  . GLU A 316  ? 0.1768 0.2178 0.2068 0.0209  0.0474  0.0579  314  GLU A CD  
2271  O OE1 . GLU A 316  ? 0.2043 0.2519 0.2336 0.0240  0.0491  0.0566  314  GLU A OE1 
2272  O OE2 . GLU A 316  ? 0.1996 0.2403 0.2282 0.0197  0.0475  0.0604  314  GLU A OE2 
2273  N N   . LEU A 317  ? 0.1632 0.1783 0.1926 0.0215  0.0390  0.0427  315  LEU A N   
2274  C CA  . LEU A 317  ? 0.1666 0.1791 0.1964 0.0229  0.0375  0.0396  315  LEU A CA  
2275  C C   . LEU A 317  ? 0.1561 0.1670 0.1903 0.0202  0.0360  0.0409  315  LEU A C   
2276  O O   . LEU A 317  ? 0.1593 0.1725 0.1965 0.0213  0.0357  0.0405  315  LEU A O   
2277  C CB  . LEU A 317  ? 0.1929 0.1986 0.2182 0.0235  0.0358  0.0362  315  LEU A CB  
2278  C CG  . LEU A 317  ? 0.2014 0.2036 0.2273 0.0246  0.0339  0.0335  315  LEU A CG  
2279  C CD1 . LEU A 317  ? 0.2241 0.2308 0.2515 0.0283  0.0347  0.0319  315  LEU A CD1 
2280  C CD2 . LEU A 317  ? 0.2586 0.2545 0.2803 0.0247  0.0323  0.0309  315  LEU A CD2 
2281  N N   . SER A 318  ? 0.1482 0.1557 0.1832 0.0169  0.0348  0.0423  316  SER A N   
2282  C CA  . SER A 318  ? 0.1382 0.1447 0.1772 0.0144  0.0332  0.0431  316  SER A CA  
2283  C C   . SER A 318  ? 0.1682 0.1812 0.2127 0.0141  0.0343  0.0459  316  SER A C   
2284  O O   . SER A 318  ? 0.1471 0.1606 0.1950 0.0134  0.0331  0.0460  316  SER A O   
2285  C CB  . SER A 318  ? 0.1443 0.1466 0.1834 0.0112  0.0317  0.0436  316  SER A CB  
2286  O OG  . SER A 318  ? 0.1504 0.1552 0.1920 0.0097  0.0328  0.0467  316  SER A OG  
2287  N N   . LEU A 319  ? 0.1474 0.1657 0.1927 0.0148  0.0366  0.0485  317  LEU A N   
2288  C CA  . LEU A 319  ? 0.1439 0.1693 0.1946 0.0144  0.0379  0.0515  317  LEU A CA  
2289  C C   . LEU A 319  ? 0.1705 0.1995 0.2223 0.0174  0.0384  0.0499  317  LEU A C   
2290  O O   . LEU A 319  ? 0.1593 0.1922 0.2161 0.0167  0.0383  0.0515  317  LEU A O   
2291  C CB  . LEU A 319  ? 0.1574 0.1888 0.2086 0.0146  0.0403  0.0549  317  LEU A CB  
2292  C CG  . LEU A 319  ? 0.1870 0.2154 0.2386 0.0115  0.0397  0.0574  317  LEU A CG  
2293  C CD1 . LEU A 319  ? 0.1745 0.2097 0.2265 0.0119  0.0422  0.0613  317  LEU A CD1 
2294  C CD2 . LEU A 319  ? 0.1674 0.1941 0.2249 0.0079  0.0377  0.0592  317  LEU A CD2 
2295  N N   . ASP A 320  ? 0.1552 0.1828 0.2028 0.0206  0.0386  0.0466  318  ASP A N   
2296  C CA  . ASP A 320  ? 0.1795 0.2099 0.2287 0.0236  0.0386  0.0446  318  ASP A CA  
2297  C C   . ASP A 320  ? 0.1927 0.2189 0.2443 0.0223  0.0360  0.0438  318  ASP A C   
2298  O O   . ASP A 320  ? 0.1863 0.2160 0.2417 0.0234  0.0359  0.0439  318  ASP A O   
2299  C CB  . ASP A 320  ? 0.1816 0.2109 0.2262 0.0275  0.0391  0.0409  318  ASP A CB  
2300  C CG  . ASP A 320  ? 0.2208 0.2573 0.2640 0.0297  0.0419  0.0416  318  ASP A CG  
2301  O OD1 . ASP A 320  ? 0.2374 0.2819 0.2842 0.0307  0.0437  0.0435  318  ASP A OD1 
2302  O OD2 . ASP A 320  ? 0.2646 0.2991 0.3030 0.0303  0.0424  0.0405  318  ASP A OD2 
2303  N N   . LEU A 321  ? 0.1520 0.1712 0.2013 0.0200  0.0339  0.0429  319  LEU A N   
2304  C CA  . LEU A 321  ? 0.1567 0.1731 0.2082 0.0184  0.0315  0.0426  319  LEU A CA  
2305  C C   . LEU A 321  ? 0.1599 0.1797 0.2166 0.0157  0.0313  0.0454  319  LEU A C   
2306  O O   . LEU A 321  ? 0.1556 0.1774 0.2160 0.0156  0.0302  0.0458  319  LEU A O   
2307  C CB  . LEU A 321  ? 0.1734 0.1827 0.2211 0.0167  0.0294  0.0410  319  LEU A CB  
2308  C CG  . LEU A 321  ? 0.2181 0.2233 0.2619 0.0191  0.0287  0.0382  319  LEU A CG  
2309  C CD1 . LEU A 321  ? 0.2446 0.2489 0.2842 0.0204  0.0302  0.0371  319  LEU A CD1 
2310  C CD2 . LEU A 321  ? 0.2441 0.2439 0.2864 0.0171  0.0260  0.0373  319  LEU A CD2 
2311  N N   . LEU A 322  ? 0.1552 0.1757 0.2126 0.0133  0.0320  0.0475  320  LEU A N   
2312  C CA  . LEU A 322  ? 0.1477 0.1713 0.2107 0.0106  0.0316  0.0501  320  LEU A CA  
2313  C C   . LEU A 322  ? 0.1458 0.1768 0.2134 0.0120  0.0331  0.0520  320  LEU A C   
2314  O O   . LEU A 322  ? 0.1554 0.1886 0.2276 0.0108  0.0319  0.0529  320  LEU A O   
2315  C CB  . LEU A 322  ? 0.1368 0.1601 0.2005 0.0082  0.0321  0.0523  320  LEU A CB  
2316  C CG  . LEU A 322  ? 0.1586 0.1844 0.2287 0.0050  0.0313  0.0551  320  LEU A CG  
2317  C CD1 . LEU A 322  ? 0.1673 0.1890 0.2385 0.0028  0.0283  0.0531  320  LEU A CD1 
2318  C CD2 . LEU A 322  ? 0.1438 0.1699 0.2153 0.0030  0.0320  0.0579  320  LEU A CD2 
2319  N N   . GLU A 323  ? 0.1437 0.1792 0.2101 0.0148  0.0356  0.0523  321  GLU A N   
2320  C CA  . GLU A 323  ? 0.1544 0.1981 0.2251 0.0166  0.0373  0.0539  321  GLU A CA  
2321  C C   . GLU A 323  ? 0.1637 0.2073 0.2362 0.0184  0.0359  0.0519  321  GLU A C   
2322  O O   . GLU A 323  ? 0.1740 0.2220 0.2519 0.0176  0.0356  0.0536  321  GLU A O   
2323  C CB  . GLU A 323  ? 0.1711 0.2200 0.2393 0.0197  0.0402  0.0539  321  GLU A CB  
2324  C CG  . GLU A 323  ? 0.2395 0.2972 0.3112 0.0227  0.0421  0.0544  321  GLU A CG  
2325  C CD  . GLU A 323  ? 0.2544 0.3210 0.3293 0.0219  0.0448  0.0586  321  GLU A CD  
2326  O OE1 . GLU A 323  ? 0.3334 0.3993 0.4064 0.0200  0.0455  0.0608  321  GLU A OE1 
2327  O OE2 . GLU A 323  ? 0.2809 0.3555 0.3602 0.0231  0.0461  0.0600  321  GLU A OE2 
2328  N N   . VAL A 324  ? 0.1335 0.1724 0.2020 0.0208  0.0349  0.0485  322  VAL A N   
2329  C CA  . VAL A 324  ? 0.1419 0.1808 0.2126 0.0227  0.0334  0.0469  322  VAL A CA  
2330  C C   . VAL A 324  ? 0.1408 0.1775 0.2145 0.0195  0.0308  0.0481  322  VAL A C   
2331  O O   . VAL A 324  ? 0.1714 0.2118 0.2497 0.0199  0.0301  0.0488  322  VAL A O   
2332  C CB  . VAL A 324  ? 0.1966 0.2299 0.2629 0.0254  0.0323  0.0434  322  VAL A CB  
2333  C CG1 . VAL A 324  ? 0.2035 0.2362 0.2728 0.0270  0.0302  0.0423  322  VAL A CG1 
2334  C CG2 . VAL A 324  ? 0.2135 0.2497 0.2772 0.0289  0.0346  0.0417  322  VAL A CG2 
2335  N N   . LEU A 325  ? 0.1272 0.1585 0.1985 0.0164  0.0293  0.0480  323  LEU A N   
2336  C CA  . LEU A 325  ? 0.1372 0.1669 0.2108 0.0135  0.0268  0.0486  323  LEU A CA  
2337  C C   . LEU A 325  ? 0.1385 0.1740 0.2182 0.0115  0.0271  0.0513  323  LEU A C   
2338  O O   . LEU A 325  ? 0.1346 0.1721 0.2182 0.0108  0.0255  0.0518  323  LEU A O   
2339  C CB  . LEU A 325  ? 0.1368 0.1606 0.2067 0.0108  0.0253  0.0477  323  LEU A CB  
2340  C CG  . LEU A 325  ? 0.1676 0.1857 0.2320 0.0121  0.0244  0.0452  323  LEU A CG  
2341  C CD1 . LEU A 325  ? 0.1799 0.1935 0.2406 0.0098  0.0240  0.0445  323  LEU A CD1 
2342  C CD2 . LEU A 325  ? 0.1768 0.1934 0.2417 0.0121  0.0218  0.0446  323  LEU A CD2 
2343  N N   . CYS A 326  ? 0.1247 0.1630 0.2057 0.0105  0.0291  0.0533  324  CYS A N   
2344  C CA  . CYS A 326  ? 0.1131 0.1568 0.2005 0.0082  0.0291  0.0563  324  CYS A CA  
2345  C C   . CYS A 326  ? 0.1319 0.1829 0.2238 0.0105  0.0304  0.0575  324  CYS A C   
2346  O O   . CYS A 326  ? 0.1330 0.1884 0.2307 0.0087  0.0299  0.0596  324  CYS A O   
2347  C CB  . CYS A 326  ? 0.1235 0.1683 0.2118 0.0063  0.0307  0.0587  324  CYS A CB  
2348  S SG  . CYS A 326  ? 0.1742 0.2111 0.2598 0.0030  0.0285  0.0575  324  CYS A SG  
2349  N N   . LEU A 327  ? 0.1246 0.1773 0.2141 0.0144  0.0321  0.0560  325  LEU A N   
2350  C CA  . LEU A 327  ? 0.1270 0.1870 0.2207 0.0171  0.0333  0.0567  325  LEU A CA  
2351  C C   . LEU A 327  ? 0.1339 0.1921 0.2285 0.0189  0.0311  0.0546  325  LEU A C   
2352  O O   . LEU A 327  ? 0.1415 0.2055 0.2402 0.0212  0.0316  0.0549  325  LEU A O   
2353  C CB  . LEU A 327  ? 0.1404 0.2047 0.2318 0.0208  0.0364  0.0560  325  LEU A CB  
2354  C CG  . LEU A 327  ? 0.1784 0.2465 0.2694 0.0194  0.0389  0.0588  325  LEU A CG  
2355  C CD1 . LEU A 327  ? 0.2415 0.3144 0.3296 0.0235  0.0418  0.0576  325  LEU A CD1 
2356  C CD2 . LEU A 327  ? 0.2174 0.2925 0.3154 0.0168  0.0395  0.0630  325  LEU A CD2 
2357  N N   . ASP A 328  ? 0.1393 0.1901 0.2305 0.0178  0.0285  0.0529  326  ASP A N   
2358  C CA  . ASP A 328  ? 0.1389 0.1875 0.2307 0.0193  0.0262  0.0514  326  ASP A CA  
2359  C C   . ASP A 328  ? 0.1388 0.1903 0.2357 0.0169  0.0242  0.0532  326  ASP A C   
2360  O O   . ASP A 328  ? 0.1333 0.1825 0.2301 0.0133  0.0225  0.0538  326  ASP A O   
2361  C CB  . ASP A 328  ? 0.1413 0.1818 0.2274 0.0187  0.0243  0.0494  326  ASP A CB  
2362  C CG  . ASP A 328  ? 0.1849 0.2230 0.2714 0.0206  0.0219  0.0482  326  ASP A CG  
2363  O OD1 . ASP A 328  ? 0.1945 0.2355 0.2853 0.0204  0.0204  0.0494  326  ASP A OD1 
2364  O OD2 . ASP A 328  ? 0.2188 0.2519 0.3013 0.0223  0.0214  0.0463  326  ASP A OD2 
2365  N N   . GLY A 329  ? 0.1380 0.1947 0.2397 0.0191  0.0242  0.0538  327  GLY A N   
2366  C CA  . GLY A 329  ? 0.1445 0.2047 0.2515 0.0171  0.0223  0.0555  327  GLY A CA  
2367  C C   . GLY A 329  ? 0.1658 0.2212 0.2713 0.0149  0.0188  0.0550  327  GLY A C   
2368  O O   . GLY A 329  ? 0.1385 0.1959 0.2472 0.0121  0.0171  0.0562  327  GLY A O   
2369  N N   . ASP A 330  ? 0.1353 0.1847 0.2360 0.0161  0.0176  0.0532  328  ASP A N   
2370  C CA  . ASP A 330  ? 0.1341 0.1800 0.2331 0.0140  0.0144  0.0531  328  ASP A CA  
2371  C C   . ASP A 330  ? 0.1278 0.1718 0.2247 0.0099  0.0137  0.0531  328  ASP A C   
2372  O O   . ASP A 330  ? 0.1521 0.1954 0.2487 0.0078  0.0111  0.0531  328  ASP A O   
2373  C CB  . ASP A 330  ? 0.1517 0.1915 0.2460 0.0157  0.0133  0.0517  328  ASP A CB  
2374  C CG  . ASP A 330  ? 0.2231 0.2637 0.3201 0.0195  0.0127  0.0515  328  ASP A CG  
2375  O OD1 . ASP A 330  ? 0.2246 0.2702 0.3270 0.0203  0.0121  0.0527  328  ASP A OD1 
2376  O OD2 . ASP A 330  ? 0.2024 0.2385 0.2964 0.0217  0.0126  0.0500  328  ASP A OD2 
2377  N N   . LEU A 331  ? 0.1163 0.1597 0.2119 0.0090  0.0159  0.0529  329  LEU A N   
2378  C CA  . LEU A 331  ? 0.1119 0.1532 0.2061 0.0055  0.0151  0.0525  329  LEU A CA  
2379  C C   . LEU A 331  ? 0.1305 0.1766 0.2305 0.0032  0.0153  0.0542  329  LEU A C   
2380  O O   . LEU A 331  ? 0.1353 0.1798 0.2353 0.0003  0.0146  0.0539  329  LEU A O   
2381  C CB  . LEU A 331  ? 0.1374 0.1742 0.2266 0.0057  0.0169  0.0514  329  LEU A CB  
2382  C CG  . LEU A 331  ? 0.1205 0.1517 0.2037 0.0069  0.0161  0.0496  329  LEU A CG  
2383  C CD1 . LEU A 331  ? 0.1329 0.1606 0.2118 0.0077  0.0182  0.0486  329  LEU A CD1 
2384  C CD2 . LEU A 331  ? 0.1450 0.1738 0.2262 0.0042  0.0134  0.0486  329  LEU A CD2 
2385  N N   . SER A 332  ? 0.1391 0.1911 0.2446 0.0044  0.0160  0.0560  330  SER A N   
2386  C CA  . SER A 332  ? 0.1489 0.2057 0.2604 0.0021  0.0163  0.0579  330  SER A CA  
2387  C C   . SER A 332  ? 0.1377 0.1946 0.2516 -0.0012 0.0130  0.0575  330  SER A C   
2388  O O   . SER A 332  ? 0.1562 0.2120 0.2684 -0.0011 0.0106  0.0563  330  SER A O   
2389  C CB  . SER A 332  ? 0.1648 0.2287 0.2817 0.0042  0.0178  0.0599  330  SER A CB  
2390  O OG  . SER A 332  ? 0.2078 0.2738 0.3271 0.0050  0.0157  0.0598  330  SER A OG  
2391  N N   . GLY A 333  ? 0.1166 0.1751 0.2347 -0.0042 0.0127  0.0584  331  GLY A N   
2392  C CA  . GLY A 333  ? 0.1361 0.1950 0.2571 -0.0073 0.0095  0.0575  331  GLY A CA  
2393  C C   . GLY A 333  ? 0.1644 0.2176 0.2814 -0.0094 0.0079  0.0549  331  GLY A C   
2394  O O   . GLY A 333  ? 0.2112 0.2648 0.3307 -0.0120 0.0051  0.0535  331  GLY A O   
2395  N N   . TRP A 334  ? 0.1401 0.1885 0.2513 -0.0081 0.0096  0.0540  332  TRP A N   
2396  C CA  . TRP A 334  ? 0.1257 0.1688 0.2326 -0.0095 0.0084  0.0513  332  TRP A CA  
2397  C C   . TRP A 334  ? 0.1159 0.1564 0.2227 -0.0100 0.0105  0.0522  332  TRP A C   
2398  O O   . TRP A 334  ? 0.1312 0.1720 0.2362 -0.0079 0.0134  0.0538  332  TRP A O   
2399  C CB  . TRP A 334  ? 0.1263 0.1659 0.2260 -0.0076 0.0083  0.0496  332  TRP A CB  
2400  C CG  . TRP A 334  ? 0.1276 0.1620 0.2219 -0.0083 0.0078  0.0470  332  TRP A CG  
2401  C CD1 . TRP A 334  ? 0.1101 0.1433 0.2038 -0.0105 0.0053  0.0444  332  TRP A CD1 
2402  C CD2 . TRP A 334  ? 0.1095 0.1395 0.1982 -0.0066 0.0097  0.0466  332  TRP A CD2 
2403  N NE1 . TRP A 334  ? 0.1212 0.1497 0.2093 -0.0103 0.0057  0.0425  332  TRP A NE1 
2404  C CE2 . TRP A 334  ? 0.1179 0.1442 0.2028 -0.0080 0.0084  0.0439  332  TRP A CE2 
2405  C CE3 . TRP A 334  ? 0.1400 0.1692 0.2265 -0.0040 0.0124  0.0479  332  TRP A CE3 
2406  C CZ2 . TRP A 334  ? 0.1289 0.1508 0.2083 -0.0070 0.0096  0.0429  332  TRP A CZ2 
2407  C CZ3 . TRP A 334  ? 0.1198 0.1444 0.2007 -0.0029 0.0135  0.0467  332  TRP A CZ3 
2408  C CH2 . TRP A 334  ? 0.1417 0.1626 0.2191 -0.0045 0.0121  0.0443  332  TRP A CH2 
2409  N N   . ASN A 335  ? 0.1164 0.1548 0.2253 -0.0127 0.0089  0.0511  333  ASN A N   
2410  C CA  . ASN A 335  ? 0.1205 0.1564 0.2302 -0.0135 0.0103  0.0523  333  ASN A CA  
2411  C C   . ASN A 335  ? 0.1101 0.1399 0.2140 -0.0135 0.0098  0.0493  333  ASN A C   
2412  O O   . ASN A 335  ? 0.1327 0.1597 0.2378 -0.0148 0.0099  0.0496  333  ASN A O   
2413  C CB  . ASN A 335  ? 0.1127 0.1505 0.2306 -0.0166 0.0087  0.0537  333  ASN A CB  
2414  C CG  . ASN A 335  ? 0.1438 0.1878 0.2678 -0.0166 0.0104  0.0579  333  ASN A CG  
2415  O OD1 . ASN A 335  ? 0.1373 0.1839 0.2594 -0.0142 0.0134  0.0600  333  ASN A OD1 
2416  N ND2 . ASN A 335  ? 0.1702 0.2170 0.3020 -0.0193 0.0082  0.0589  333  ASN A ND2 
2417  N N   . GLY A 336  ? 0.1298 0.1578 0.2278 -0.0123 0.0090  0.0467  334  GLY A N   
2418  C CA  . GLY A 336  ? 0.1256 0.1486 0.2183 -0.0124 0.0083  0.0437  334  GLY A CA  
2419  C C   . GLY A 336  ? 0.1188 0.1383 0.2060 -0.0105 0.0109  0.0442  334  GLY A C   
2420  O O   . GLY A 336  ? 0.1268 0.1423 0.2102 -0.0107 0.0103  0.0419  334  GLY A O   
2421  N N   . MET A 337  ? 0.1243 0.1455 0.2111 -0.0084 0.0135  0.0468  335  MET A N   
2422  C CA  A MET A 337  ? 0.1196 0.1378 0.2013 -0.0065 0.0158  0.0469  335  MET A CA  
2423  C CA  B MET A 337  ? 0.1197 0.1379 0.2014 -0.0065 0.0158  0.0469  335  MET A CA  
2424  C C   . MET A 337  ? 0.1206 0.1366 0.2035 -0.0079 0.0164  0.0477  335  MET A C   
2425  O O   . MET A 337  ? 0.1318 0.1503 0.2204 -0.0092 0.0167  0.0502  335  MET A O   
2426  C CB  A MET A 337  ? 0.1514 0.1729 0.2330 -0.0039 0.0184  0.0492  335  MET A CB  
2427  C CB  B MET A 337  ? 0.1514 0.1727 0.2328 -0.0039 0.0184  0.0491  335  MET A CB  
2428  C CG  A MET A 337  ? 0.1794 0.1982 0.2554 -0.0015 0.0205  0.0487  335  MET A CG  
2429  C CG  B MET A 337  ? 0.1818 0.2007 0.2584 -0.0018 0.0208  0.0492  335  MET A CG  
2430  S SD  A MET A 337  ? 0.1986 0.2133 0.2681 0.0000  0.0193  0.0458  335  MET A SD  
2431  S SD  B MET A 337  ? 0.1878 0.2074 0.2605 0.0020  0.0221  0.0485  335  MET A SD  
2432  C CE  A MET A 337  ? 0.2188 0.2374 0.2904 0.0022  0.0193  0.0467  335  MET A CE  
2433  C CE  B MET A 337  ? 0.1493 0.1654 0.2189 0.0013  0.0191  0.0459  335  MET A CE  
2434  N N   . GLY A 338  ? 0.1259 0.1371 0.2037 -0.0075 0.0164  0.0457  336  GLY A N   
2435  C CA  . GLY A 338  ? 0.1376 0.1461 0.2162 -0.0086 0.0166  0.0462  336  GLY A CA  
2436  C C   . GLY A 338  ? 0.1205 0.1267 0.1935 -0.0066 0.0189  0.0464  336  GLY A C   
2437  O O   . GLY A 338  ? 0.1331 0.1385 0.2010 -0.0045 0.0197  0.0452  336  GLY A O   
2438  N N   . PHE A 339  ? 0.1118 0.1169 0.1862 -0.0072 0.0197  0.0482  337  PHE A N   
2439  C CA  . PHE A 339  ? 0.1202 0.1240 0.1899 -0.0054 0.0220  0.0490  337  PHE A CA  
2440  C C   . PHE A 339  ? 0.1432 0.1440 0.2141 -0.0068 0.0215  0.0498  337  PHE A C   
2441  O O   . PHE A 339  ? 0.1308 0.1329 0.2079 -0.0088 0.0208  0.0523  337  PHE A O   
2442  C CB  . PHE A 339  ? 0.1196 0.1287 0.1902 -0.0037 0.0247  0.0523  337  PHE A CB  
2443  C CG  . PHE A 339  ? 0.1257 0.1345 0.1907 -0.0011 0.0270  0.0524  337  PHE A CG  
2444  C CD1 . PHE A 339  ? 0.1398 0.1479 0.1998 0.0015  0.0276  0.0501  337  PHE A CD1 
2445  C CD2 . PHE A 339  ? 0.1257 0.1352 0.1909 -0.0013 0.0284  0.0551  337  PHE A CD2 
2446  C CE1 . PHE A 339  ? 0.1578 0.1658 0.2130 0.0040  0.0296  0.0498  337  PHE A CE1 
2447  C CE2 . PHE A 339  ? 0.1544 0.1644 0.2144 0.0012  0.0305  0.0550  337  PHE A CE2 
2448  C CZ  . PHE A 339  ? 0.1676 0.1767 0.2225 0.0038  0.0311  0.0521  337  PHE A CZ  
2449  N N   . VAL A 340  ? 0.1318 0.1286 0.1972 -0.0058 0.0217  0.0479  338  VAL A N   
2450  C CA  . VAL A 340  ? 0.1146 0.1083 0.1809 -0.0068 0.0211  0.0484  338  VAL A CA  
2451  C C   . VAL A 340  ? 0.1230 0.1188 0.1883 -0.0057 0.0236  0.0522  338  VAL A C   
2452  O O   . VAL A 340  ? 0.1381 0.1359 0.1988 -0.0034 0.0258  0.0523  338  VAL A O   
2453  C CB  . VAL A 340  ? 0.1187 0.1076 0.1796 -0.0062 0.0200  0.0444  338  VAL A CB  
2454  C CG1 . VAL A 340  ? 0.1447 0.1303 0.2066 -0.0069 0.0194  0.0449  338  VAL A CG1 
2455  C CG2 . VAL A 340  ? 0.1481 0.1361 0.2097 -0.0071 0.0176  0.0408  338  VAL A CG2 
2456  N N   . VAL A 341  ? 0.1340 0.1297 0.2039 -0.0074 0.0232  0.0552  339  VAL A N   
2457  C CA  A VAL A 341  ? 0.1252 0.1229 0.1940 -0.0066 0.0253  0.0589  339  VAL A CA  
2458  C CA  B VAL A 341  ? 0.1255 0.1231 0.1941 -0.0066 0.0253  0.0588  339  VAL A CA  
2459  C C   . VAL A 341  ? 0.1287 0.1215 0.1980 -0.0077 0.0237  0.0587  339  VAL A C   
2460  O O   . VAL A 341  ? 0.1470 0.1368 0.2215 -0.0098 0.0211  0.0580  339  VAL A O   
2461  C CB  A VAL A 341  ? 0.1385 0.1422 0.2131 -0.0077 0.0266  0.0643  339  VAL A CB  
2462  C CB  B VAL A 341  ? 0.1389 0.1427 0.2131 -0.0075 0.0267  0.0643  339  VAL A CB  
2463  C CG1 A VAL A 341  ? 0.1628 0.1704 0.2342 -0.0061 0.0294  0.0677  339  VAL A CG1 
2464  C CG1 B VAL A 341  ? 0.1574 0.1664 0.2308 -0.0060 0.0285  0.0641  339  VAL A CG1 
2465  C CG2 A VAL A 341  ? 0.1614 0.1695 0.2377 -0.0073 0.0272  0.0640  339  VAL A CG2 
2466  C CG2 B VAL A 341  ? 0.1397 0.1427 0.2225 -0.0108 0.0243  0.0664  339  VAL A CG2 
2467  N N   . GLN A 342  ? 0.1277 0.1198 0.1917 -0.0060 0.0252  0.0591  340  GLN A N   
2468  C CA  . GLN A 342  ? 0.1545 0.1420 0.2180 -0.0065 0.0238  0.0586  340  GLN A CA  
2469  C C   . GLN A 342  ? 0.1461 0.1358 0.2137 -0.0076 0.0243  0.0643  340  GLN A C   
2470  O O   . GLN A 342  ? 0.1691 0.1632 0.2337 -0.0062 0.0269  0.0673  340  GLN A O   
2471  C CB  . GLN A 342  ? 0.1337 0.1190 0.1891 -0.0041 0.0248  0.0554  340  GLN A CB  
2472  C CG  . GLN A 342  ? 0.1299 0.1129 0.1814 -0.0032 0.0241  0.0502  340  GLN A CG  
2473  C CD  . GLN A 342  ? 0.1456 0.1290 0.1896 -0.0006 0.0259  0.0485  340  GLN A CD  
2474  O OE1 . GLN A 342  ? 0.1554 0.1427 0.1976 0.0009  0.0281  0.0505  340  GLN A OE1 
2475  N NE2 . GLN A 342  ? 0.1423 0.1218 0.1822 -0.0001 0.0248  0.0444  340  GLN A NE2 
2476  N N   . ALA A 343  ? 0.1385 0.1251 0.2128 -0.0100 0.0218  0.0655  341  ALA A N   
2477  C CA  . ALA A 343  ? 0.1624 0.1509 0.2419 -0.0115 0.0217  0.0716  341  ALA A CA  
2478  C C   . ALA A 343  ? 0.1725 0.1598 0.2477 -0.0102 0.0225  0.0729  341  ALA A C   
2479  O O   . ALA A 343  ? 0.1705 0.1609 0.2484 -0.0110 0.0232  0.0786  341  ALA A O   
2480  C CB  . ALA A 343  ? 0.1878 0.1726 0.2766 -0.0144 0.0182  0.0721  341  ALA A CB  
2481  N N   . TYR A 344  ? 0.1626 0.1457 0.2315 -0.0084 0.0222  0.0679  342  TYR A N   
2482  C CA  . TYR A 344  ? 0.1642 0.1469 0.2286 -0.0071 0.0231  0.0693  342  TYR A CA  
2483  C C   . TYR A 344  ? 0.1791 0.1681 0.2376 -0.0049 0.0266  0.0714  342  TYR A C   
2484  O O   . TYR A 344  ? 0.1852 0.1751 0.2399 -0.0037 0.0275  0.0730  342  TYR A O   
2485  C CB  . TYR A 344  ? 0.1624 0.1392 0.2223 -0.0059 0.0217  0.0637  342  TYR A CB  
2486  C CG  . TYR A 344  ? 0.1535 0.1296 0.2059 -0.0038 0.0228  0.0583  342  TYR A CG  
2487  C CD1 . TYR A 344  ? 0.1635 0.1434 0.2131 -0.0028 0.0247  0.0577  342  TYR A CD1 
2488  C CD2 . TYR A 344  ? 0.1573 0.1289 0.2060 -0.0029 0.0216  0.0540  342  TYR A CD2 
2489  C CE1 . TYR A 344  ? 0.1639 0.1425 0.2073 -0.0010 0.0252  0.0531  342  TYR A CE1 
2490  C CE2 . TYR A 344  ? 0.1579 0.1288 0.2004 -0.0014 0.0223  0.0496  342  TYR A CE2 
2491  C CZ  . TYR A 344  ? 0.1420 0.1161 0.1820 -0.0005 0.0240  0.0493  342  TYR A CZ  
2492  O OH  . TYR A 344  ? 0.1451 0.1182 0.1796 0.0009  0.0244  0.0453  342  TYR A OH  
2493  N N   . GLY A 345  ? 0.1451 0.1386 0.2030 -0.0043 0.0283  0.0713  343  GLY A N   
2494  C CA  . GLY A 345  ? 0.1504 0.1500 0.2028 -0.0019 0.0314  0.0723  343  GLY A CA  
2495  C C   . GLY A 345  ? 0.1505 0.1577 0.2068 -0.0027 0.0332  0.0789  343  GLY A C   
2496  O O   . GLY A 345  ? 0.1621 0.1709 0.2255 -0.0051 0.0324  0.0820  343  GLY A O   
2497  N N   . LYS A 346  ? 0.1503 0.1628 0.2019 -0.0008 0.0355  0.0810  344  LYS A N   
2498  C CA  . LYS A 346  ? 0.1558 0.1768 0.2105 -0.0015 0.0373  0.0878  344  LYS A CA  
2499  C C   . LYS A 346  ? 0.1642 0.1920 0.2210 -0.0011 0.0392  0.0888  344  LYS A C   
2500  O O   . LYS A 346  ? 0.1757 0.2104 0.2376 -0.0026 0.0402  0.0948  344  LYS A O   
2501  C CB  . LYS A 346  ? 0.1562 0.1819 0.2044 0.0009  0.0393  0.0892  344  LYS A CB  
2502  C CG  . LYS A 346  ? 0.1750 0.1954 0.2220 0.0004  0.0375  0.0896  344  LYS A CG  
2503  C CD  . LYS A 346  ? 0.1974 0.2222 0.2371 0.0030  0.0394  0.0898  344  LYS A CD  
2504  C CE  . LYS A 346  ? 0.2223 0.2426 0.2618 0.0022  0.0375  0.0913  344  LYS A CE  
2505  N NZ  . LYS A 346  ? 0.2303 0.2546 0.2622 0.0049  0.0391  0.0909  344  LYS A NZ  
2506  N N   . ARG A 347  ? 0.1644 0.1907 0.2180 0.0007  0.0395  0.0833  345  ARG A N   
2507  C CA  . ARG A 347  ? 0.1459 0.1783 0.2016 0.0013  0.0412  0.0837  345  ARG A CA  
2508  C C   . ARG A 347  ? 0.1633 0.1933 0.2266 -0.0016 0.0392  0.0844  345  ARG A C   
2509  O O   . ARG A 347  ? 0.1709 0.2064 0.2372 -0.0016 0.0404  0.0856  345  ARG A O   
2510  C CB  . ARG A 347  ? 0.1505 0.1825 0.1996 0.0048  0.0423  0.0777  345  ARG A CB  
2511  C CG  . ARG A 347  ? 0.1771 0.2136 0.2193 0.0080  0.0445  0.0770  345  ARG A CG  
2512  C CD  . ARG A 347  ? 0.1306 0.1641 0.1667 0.0112  0.0446  0.0704  345  ARG A CD  
2513  N NE  . ARG A 347  ? 0.1563 0.1802 0.1898 0.0106  0.0422  0.0665  345  ARG A NE  
2514  C CZ  . ARG A 347  ? 0.1577 0.1769 0.1871 0.0124  0.0415  0.0610  345  ARG A CZ  
2515  N NH1 . ARG A 347  ? 0.1622 0.1848 0.1896 0.0151  0.0427  0.0584  345  ARG A NH1 
2516  N NH2 . ARG A 347  ? 0.1622 0.1734 0.1899 0.0114  0.0393  0.0582  345  ARG A NH2 
2517  N N   . CYS A 348  ? 0.1599 0.1822 0.2266 -0.0040 0.0362  0.0834  346  CYS A N   
2518  C CA  . CYS A 348  ? 0.1610 0.1800 0.2339 -0.0064 0.0339  0.0823  346  CYS A CA  
2519  C C   . CYS A 348  ? 0.1780 0.2037 0.2585 -0.0084 0.0344  0.0875  346  CYS A C   
2520  O O   . CYS A 348  ? 0.1549 0.1820 0.2373 -0.0084 0.0344  0.0857  346  CYS A O   
2521  C CB  . CYS A 348  ? 0.1848 0.1956 0.2609 -0.0086 0.0305  0.0812  346  CYS A CB  
2522  S SG  . CYS A 348  ? 0.2228 0.2287 0.3046 -0.0108 0.0273  0.0774  346  CYS A SG  
2523  N N   . PRO A 349  ? 0.1741 0.2043 0.2594 -0.0102 0.0349  0.0942  347  PRO A N   
2524  C CA  . PRO A 349  ? 0.1456 0.1826 0.2387 -0.0123 0.0354  0.0992  347  PRO A CA  
2525  C C   . PRO A 349  ? 0.1441 0.1897 0.2343 -0.0098 0.0386  0.0989  347  PRO A C   
2526  O O   . PRO A 349  ? 0.1724 0.2217 0.2678 -0.0109 0.0386  0.1000  347  PRO A O   
2527  C CB  . PRO A 349  ? 0.1998 0.2401 0.2958 -0.0138 0.0345  0.1044  347  PRO A CB  
2528  C CG  . PRO A 349  ? 0.1997 0.2385 0.2887 -0.0118 0.0355  0.1038  347  PRO A CG  
2529  C CD  . PRO A 349  ? 0.1715 0.2016 0.2557 -0.0105 0.0350  0.0979  347  PRO A CD  
2530  N N   . PHE A 350  ? 0.1687 0.2175 0.2508 -0.0063 0.0412  0.0972  348  PHE A N   
2531  C CA  . PHE A 350  ? 0.1734 0.2306 0.2528 -0.0034 0.0443  0.0964  348  PHE A CA  
2532  C C   . PHE A 350  ? 0.1555 0.2085 0.2326 -0.0018 0.0435  0.0900  348  PHE A C   
2533  O O   . PHE A 350  ? 0.1629 0.2216 0.2419 -0.0007 0.0448  0.0898  348  PHE A O   
2534  C CB  . PHE A 350  ? 0.1893 0.2513 0.2612 -0.0002 0.0469  0.0963  348  PHE A CB  
2535  C CG  . PHE A 350  ? 0.1744 0.2401 0.2479 -0.0019 0.0474  0.1027  348  PHE A CG  
2536  C CD1 . PHE A 350  ? 0.1905 0.2656 0.2685 -0.0030 0.0481  0.1082  348  PHE A CD1 
2537  C CD2 . PHE A 350  ? 0.1927 0.2518 0.2630 -0.0022 0.0459  0.1021  348  PHE A CD2 
2538  C CE1 . PHE A 350  ? 0.2212 0.2986 0.3000 -0.0042 0.0470  0.1122  348  PHE A CE1 
2539  C CE2 . PHE A 350  ? 0.1926 0.2543 0.2642 -0.0035 0.0452  0.1069  348  PHE A CE2 
2540  C CZ  . PHE A 350  ? 0.2073 0.2781 0.2829 -0.0044 0.0455  0.1116  348  PHE A CZ  
2541  N N   . VAL A 351  ? 0.1470 0.1905 0.2203 -0.0015 0.0414  0.0849  349  VAL A N   
2542  C CA  . VAL A 351  ? 0.1277 0.1668 0.1998 -0.0006 0.0401  0.0794  349  VAL A CA  
2543  C C   . VAL A 351  ? 0.1475 0.1868 0.2275 -0.0035 0.0383  0.0809  349  VAL A C   
2544  O O   . VAL A 351  ? 0.1377 0.1792 0.2187 -0.0026 0.0386  0.0791  349  VAL A O   
2545  C CB  . VAL A 351  ? 0.1523 0.1817 0.2195 -0.0003 0.0380  0.0745  349  VAL A CB  
2546  C CG1 . VAL A 351  ? 0.1491 0.1743 0.2155 0.0002  0.0365  0.0696  349  VAL A CG1 
2547  C CG2 . VAL A 351  ? 0.1652 0.1947 0.2246 0.0027  0.0397  0.0728  349  VAL A CG2 
2548  N N   . LEU A 352  ? 0.1622 0.1990 0.2482 -0.0069 0.0364  0.0842  350  LEU A N   
2549  C CA  . LEU A 352  ? 0.1579 0.1950 0.2520 -0.0099 0.0344  0.0856  350  LEU A CA  
2550  C C   . LEU A 352  ? 0.1367 0.1838 0.2352 -0.0099 0.0366  0.0899  350  LEU A C   
2551  O O   . LEU A 352  ? 0.1698 0.2186 0.2721 -0.0104 0.0359  0.0889  350  LEU A O   
2552  C CB  . LEU A 352  ? 0.1576 0.1903 0.2580 -0.0135 0.0316  0.0883  350  LEU A CB  
2553  C CG  . LEU A 352  ? 0.1515 0.1744 0.2492 -0.0138 0.0288  0.0833  350  LEU A CG  
2554  C CD1 . LEU A 352  ? 0.1897 0.2085 0.2938 -0.0169 0.0261  0.0861  350  LEU A CD1 
2555  C CD2 . LEU A 352  ? 0.1886 0.2081 0.2865 -0.0139 0.0268  0.0780  350  LEU A CD2 
2556  N N   . ASP A 353  ? 0.1592 0.2137 0.2574 -0.0092 0.0393  0.0948  351  ASP A N   
2557  C CA  . ASP A 353  ? 0.1520 0.2173 0.2537 -0.0088 0.0418  0.0987  351  ASP A CA  
2558  C C   . ASP A 353  ? 0.1323 0.1999 0.2301 -0.0053 0.0431  0.0939  351  ASP A C   
2559  O O   . ASP A 353  ? 0.1752 0.2479 0.2777 -0.0056 0.0435  0.0948  351  ASP A O   
2560  C CB  . ASP A 353  ? 0.1594 0.2332 0.2595 -0.0078 0.0448  0.1037  351  ASP A CB  
2561  C CG  . ASP A 353  ? 0.1950 0.2681 0.2999 -0.0111 0.0427  0.1088  351  ASP A CG  
2562  O OD1 . ASP A 353  ? 0.2086 0.2769 0.3202 -0.0144 0.0394  0.1094  351  ASP A OD1 
2563  O OD2 . ASP A 353  ? 0.2495 0.3265 0.3508 -0.0100 0.0439  0.1111  351  ASP A OD2 
2564  N N   . PHE A 354  ? 0.1495 0.2135 0.2390 -0.0020 0.0438  0.0889  352  PHE A N   
2565  C CA  . PHE A 354  ? 0.1488 0.2140 0.2348 0.0014  0.0447  0.0842  352  PHE A CA  
2566  C C   . PHE A 354  ? 0.1547 0.2146 0.2439 0.0000  0.0420  0.0813  352  PHE A C   
2567  O O   . PHE A 354  ? 0.1579 0.2221 0.2494 0.0012  0.0424  0.0805  352  PHE A O   
2568  C CB  . PHE A 354  ? 0.1446 0.2059 0.2217 0.0049  0.0454  0.0796  352  PHE A CB  
2569  C CG  . PHE A 354  ? 0.1378 0.1976 0.2117 0.0080  0.0453  0.0743  352  PHE A CG  
2570  C CD1 . PHE A 354  ? 0.1854 0.2531 0.2582 0.0115  0.0478  0.0736  352  PHE A CD1 
2571  C CD2 . PHE A 354  ? 0.1647 0.2156 0.2369 0.0075  0.0426  0.0700  352  PHE A CD2 
2572  C CE1 . PHE A 354  ? 0.2050 0.2708 0.2757 0.0144  0.0473  0.0688  352  PHE A CE1 
2573  C CE2 . PHE A 354  ? 0.1865 0.2360 0.2562 0.0102  0.0423  0.0658  352  PHE A CE2 
2574  C CZ  . PHE A 354  ? 0.1778 0.2344 0.2470 0.0136  0.0445  0.0651  352  PHE A CZ  
2575  N N   . ILE A 355  ? 0.1434 0.1943 0.2325 -0.0023 0.0390  0.0793  353  ILE A N   
2576  C CA  . ILE A 355  ? 0.1438 0.1900 0.2353 -0.0035 0.0363  0.0761  353  ILE A CA  
2577  C C   . ILE A 355  ? 0.1372 0.1879 0.2374 -0.0063 0.0354  0.0796  353  ILE A C   
2578  O O   . ILE A 355  ? 0.1542 0.2064 0.2566 -0.0059 0.0346  0.0779  353  ILE A O   
2579  C CB  . ILE A 355  ? 0.1376 0.1743 0.2272 -0.0053 0.0334  0.0733  353  ILE A CB  
2580  C CG1 . ILE A 355  ? 0.1595 0.1917 0.2404 -0.0025 0.0341  0.0693  353  ILE A CG1 
2581  C CG2 . ILE A 355  ? 0.1457 0.1788 0.2385 -0.0070 0.0304  0.0705  353  ILE A CG2 
2582  C CD1 . ILE A 355  ? 0.1700 0.1939 0.2488 -0.0040 0.0317  0.0668  353  ILE A CD1 
2583  N N   . ILE A 356  ? 0.1453 0.1986 0.2512 -0.0091 0.0353  0.0846  354  ILE A N   
2584  C CA  . ILE A 356  ? 0.1361 0.1939 0.2512 -0.0120 0.0343  0.0883  354  ILE A CA  
2585  C C   . ILE A 356  ? 0.1390 0.2065 0.2555 -0.0100 0.0370  0.0900  354  ILE A C   
2586  O O   . ILE A 356  ? 0.1501 0.2200 0.2715 -0.0109 0.0359  0.0898  354  ILE A O   
2587  C CB  . ILE A 356  ? 0.1638 0.2224 0.2848 -0.0154 0.0337  0.0940  354  ILE A CB  
2588  C CG1 . ILE A 356  ? 0.1735 0.2222 0.2951 -0.0177 0.0302  0.0916  354  ILE A CG1 
2589  C CG2 . ILE A 356  ? 0.1604 0.2255 0.2913 -0.0183 0.0332  0.0988  354  ILE A CG2 
2590  C CD1 . ILE A 356  ? 0.2030 0.2511 0.3287 -0.0202 0.0296  0.0967  354  ILE A CD1 
2591  N N   . ASP A 357  ? 0.1325 0.2059 0.2446 -0.0070 0.0404  0.0912  355  ASP A N   
2592  C CA  . ASP A 357  ? 0.1441 0.2271 0.2571 -0.0045 0.0430  0.0921  355  ASP A CA  
2593  C C   . ASP A 357  ? 0.1475 0.2278 0.2573 -0.0017 0.0423  0.0864  355  ASP A C   
2594  O O   . ASP A 357  ? 0.1393 0.2253 0.2532 -0.0010 0.0427  0.0867  355  ASP A O   
2595  C CB  . ASP A 357  ? 0.1611 0.2511 0.2695 -0.0015 0.0467  0.0938  355  ASP A CB  
2596  C CG  . ASP A 357  ? 0.1466 0.2466 0.2552 0.0019  0.0494  0.0934  355  ASP A CG  
2597  O OD1 . ASP A 357  ? 0.2253 0.3342 0.3406 0.0005  0.0505  0.0981  355  ASP A OD1 
2598  O OD2 . ASP A 357  ? 0.1633 0.2622 0.2658 0.0060  0.0503  0.0885  355  ASP A OD2 
2599  N N   . LEU A 358  ? 0.1232 0.1952 0.2261 0.0000  0.0412  0.0814  356  LEU A N   
2600  C CA  . LEU A 358  ? 0.1271 0.1960 0.2274 0.0022  0.0401  0.0765  356  LEU A CA  
2601  C C   . LEU A 358  ? 0.1156 0.1823 0.2216 -0.0006 0.0372  0.0762  356  LEU A C   
2602  O O   . LEU A 358  ? 0.1507 0.2200 0.2584 0.0008  0.0369  0.0748  356  LEU A O   
2603  C CB  . LEU A 358  ? 0.1166 0.1768 0.2090 0.0038  0.0392  0.0720  356  LEU A CB  
2604  C CG  . LEU A 358  ? 0.1303 0.1861 0.2200 0.0057  0.0375  0.0673  356  LEU A CG  
2605  C CD1 . LEU A 358  ? 0.1595 0.2214 0.2489 0.0096  0.0394  0.0662  356  LEU A CD1 
2606  C CD2 . LEU A 358  ? 0.1493 0.1966 0.2319 0.0065  0.0365  0.0636  356  LEU A CD2 
2607  N N   . ALA A 359  ? 0.1427 0.2048 0.2518 -0.0044 0.0349  0.0774  357  ALA A N   
2608  C CA  . ALA A 359  ? 0.1388 0.1994 0.2537 -0.0072 0.0319  0.0771  357  ALA A CA  
2609  C C   . ALA A 359  ? 0.1368 0.2064 0.2594 -0.0081 0.0327  0.0809  357  ALA A C   
2610  O O   . ALA A 359  ? 0.1454 0.2163 0.2712 -0.0083 0.0312  0.0797  357  ALA A O   
2611  C CB  . ALA A 359  ? 0.1693 0.2238 0.2868 -0.0109 0.0292  0.0775  357  ALA A CB  
2612  N N   . ARG A 360  ? 0.1338 0.2101 0.2594 -0.0085 0.0351  0.0858  358  ARG A N   
2613  C CA  . ARG A 360  ? 0.1425 0.2287 0.2755 -0.0092 0.0364  0.0899  358  ARG A CA  
2614  C C   . ARG A 360  ? 0.1682 0.2598 0.2990 -0.0051 0.0382  0.0877  358  ARG A C   
2615  O O   . ARG A 360  ? 0.1772 0.2725 0.3130 -0.0055 0.0373  0.0878  358  ARG A O   
2616  C CB  . ARG A 360  ? 0.1675 0.2605 0.3035 -0.0104 0.0388  0.0959  358  ARG A CB  
2617  C CG  . ARG A 360  ? 0.2420 0.3313 0.3836 -0.0151 0.0365  0.0994  358  ARG A CG  
2618  C CD  . ARG A 360  ? 0.2300 0.3282 0.3768 -0.0168 0.0387  0.1068  358  ARG A CD  
2619  N NE  . ARG A 360  ? 0.2820 0.3741 0.4294 -0.0196 0.0368  0.1089  358  ARG A NE  
2620  C CZ  . ARG A 360  ? 0.3527 0.4401 0.5064 -0.0233 0.0328  0.1098  358  ARG A CZ  
2621  N NH1 . ARG A 360  ? 0.3683 0.4569 0.5287 -0.0252 0.0307  0.1096  358  ARG A NH1 
2622  N NH2 . ARG A 360  ? 0.3567 0.4382 0.5102 -0.0250 0.0308  0.1108  358  ARG A NH2 
2623  N N   . ARG A 361  ? 0.1449 0.2368 0.2685 -0.0012 0.0406  0.0854  359  ARG A N   
2624  C CA  . ARG A 361  ? 0.1685 0.2654 0.2905 0.0031  0.0422  0.0829  359  ARG A CA  
2625  C C   . ARG A 361  ? 0.1284 0.2198 0.2500 0.0037  0.0394  0.0788  359  ARG A C   
2626  O O   . ARG A 361  ? 0.1803 0.2768 0.3054 0.0051  0.0394  0.0785  359  ARG A O   
2627  C CB  . ARG A 361  ? 0.1930 0.2895 0.3071 0.0072  0.0446  0.0804  359  ARG A CB  
2628  C CG  . ARG A 361  ? 0.1997 0.3047 0.3139 0.0078  0.0479  0.0843  359  ARG A CG  
2629  C CD  . ARG A 361  ? 0.2297 0.3349 0.3361 0.0123  0.0500  0.0809  359  ARG A CD  
2630  N NE  . ARG A 361  ? 0.1975 0.2930 0.2974 0.0118  0.0488  0.0786  359  ARG A NE  
2631  C CZ  . ARG A 361  ? 0.1911 0.2799 0.2848 0.0146  0.0480  0.0734  359  ARG A CZ  
2632  N NH1 . ARG A 361  ? 0.2113 0.3005 0.3044 0.0179  0.0478  0.0697  359  ARG A NH1 
2633  N NH2 . ARG A 361  ? 0.2086 0.2900 0.2967 0.0141  0.0473  0.0720  359  ARG A NH2 
2634  N N   . SER A 362  ? 0.1265 0.2080 0.2436 0.0027  0.0370  0.0756  360  SER A N   
2635  C CA  . SER A 362  ? 0.1410 0.2173 0.2567 0.0033  0.0343  0.0718  360  SER A CA  
2636  C C   . SER A 362  ? 0.1398 0.2159 0.2617 -0.0002 0.0314  0.0728  360  SER A C   
2637  O O   . SER A 362  ? 0.1663 0.2412 0.2887 0.0004  0.0295  0.0706  360  SER A O   
2638  C CB  . SER A 362  ? 0.1443 0.2110 0.2527 0.0036  0.0330  0.0682  360  SER A CB  
2639  O OG  . SER A 362  ? 0.1459 0.2080 0.2552 -0.0001 0.0314  0.0692  360  SER A OG  
2640  N N   . GLY A 363  ? 0.1451 0.2223 0.2720 -0.0039 0.0309  0.0760  361  GLY A N   
2641  C CA  . GLY A 363  ? 0.1484 0.2245 0.2812 -0.0074 0.0277  0.0763  361  GLY A CA  
2642  C C   . GLY A 363  ? 0.1589 0.2261 0.2882 -0.0089 0.0245  0.0724  361  GLY A C   
2643  O O   . GLY A 363  ? 0.1808 0.2471 0.3140 -0.0113 0.0215  0.0716  361  GLY A O   
2644  N N   . ARG A 364  ? 0.1682 0.2294 0.2901 -0.0075 0.0250  0.0700  362  ARG A N   
2645  C CA  . ARG A 364  ? 0.1579 0.2111 0.2759 -0.0087 0.0223  0.0664  362  ARG A CA  
2646  C C   . ARG A 364  ? 0.1696 0.2192 0.2891 -0.0115 0.0215  0.0674  362  ARG A C   
2647  O O   . ARG A 364  ? 0.1857 0.2358 0.3038 -0.0110 0.0238  0.0697  362  ARG A O   
2648  C CB  . ARG A 364  ? 0.1670 0.2156 0.2764 -0.0057 0.0231  0.0632  362  ARG A CB  
2649  C CG  . ARG A 364  ? 0.2394 0.2914 0.3471 -0.0021 0.0244  0.0626  362  ARG A CG  
2650  C CD  . ARG A 364  ? 0.1888 0.2378 0.2943 -0.0017 0.0219  0.0596  362  ARG A CD  
2651  N NE  . ARG A 364  ? 0.1563 0.2093 0.2624 0.0014  0.0227  0.0597  362  ARG A NE  
2652  C CZ  . ARG A 364  ? 0.1298 0.1803 0.2311 0.0045  0.0231  0.0577  362  ARG A CZ  
2653  N NH1 . ARG A 364  ? 0.1342 0.1783 0.2292 0.0048  0.0228  0.0555  362  ARG A NH1 
2654  N NH2 . ARG A 364  ? 0.1245 0.1791 0.2277 0.0073  0.0237  0.0578  362  ARG A NH2 
2655  N N   . ARG A 365  ? 0.1562 0.2021 0.2783 -0.0143 0.0182  0.0656  363  ARG A N   
2656  C CA  . ARG A 365  ? 0.1359 0.1778 0.2603 -0.0170 0.0169  0.0661  363  ARG A CA  
2657  C C   . ARG A 365  ? 0.1390 0.1739 0.2556 -0.0157 0.0167  0.0627  363  ARG A C   
2658  O O   . ARG A 365  ? 0.1724 0.2029 0.2871 -0.0165 0.0141  0.0588  363  ARG A O   
2659  C CB  . ARG A 365  ? 0.1387 0.1800 0.2701 -0.0203 0.0131  0.0652  363  ARG A CB  
2660  C CG  . ARG A 365  ? 0.1688 0.2063 0.3044 -0.0231 0.0115  0.0661  363  ARG A CG  
2661  C CD  . ARG A 365  ? 0.2316 0.2707 0.3770 -0.0265 0.0084  0.0672  363  ARG A CD  
2662  N NE  . ARG A 365  ? 0.1915 0.2265 0.3414 -0.0290 0.0067  0.0683  363  ARG A NE  
2663  C CZ  . ARG A 365  ? 0.1764 0.2057 0.3274 -0.0304 0.0032  0.0642  363  ARG A CZ  
2664  N NH1 . ARG A 365  ? 0.2074 0.2352 0.3557 -0.0299 0.0009  0.0588  363  ARG A NH1 
2665  N NH2 . ARG A 365  ? 0.1941 0.2194 0.3490 -0.0322 0.0019  0.0654  363  ARG A NH2 
2666  N N   . ILE A 366  ? 0.1178 0.1525 0.2299 -0.0138 0.0196  0.0641  364  ILE A N   
2667  C CA  . ILE A 366  ? 0.1243 0.1532 0.2286 -0.0122 0.0199  0.0610  364  ILE A CA  
2668  C C   . ILE A 366  ? 0.1443 0.1676 0.2499 -0.0146 0.0174  0.0594  364  ILE A C   
2669  O O   . ILE A 366  ? 0.1324 0.1559 0.2434 -0.0167 0.0169  0.0622  364  ILE A O   
2670  C CB  . ILE A 366  ? 0.1210 0.1514 0.2209 -0.0097 0.0233  0.0629  364  ILE A CB  
2671  C CG1 . ILE A 366  ? 0.1478 0.1836 0.2466 -0.0069 0.0255  0.0636  364  ILE A CG1 
2672  C CG2 . ILE A 366  ? 0.1549 0.1791 0.2472 -0.0083 0.0234  0.0597  364  ILE A CG2 
2673  C CD1 . ILE A 366  ? 0.1670 0.2061 0.2624 -0.0042 0.0290  0.0655  364  ILE A CD1 
2674  N N   . MET A 367  ? 0.1347 0.1533 0.2355 -0.0141 0.0157  0.0549  365  MET A N   
2675  C CA  . MET A 367  ? 0.1336 0.1469 0.2348 -0.0158 0.0134  0.0525  365  MET A CA  
2676  C C   . MET A 367  ? 0.1586 0.1688 0.2551 -0.0145 0.0153  0.0532  365  MET A C   
2677  O O   . MET A 367  ? 0.1801 0.1891 0.2695 -0.0122 0.0168  0.0518  365  MET A O   
2678  C CB  . MET A 367  ? 0.1321 0.1430 0.2298 -0.0157 0.0110  0.0475  365  MET A CB  
2679  C CG  . MET A 367  ? 0.1649 0.1797 0.2662 -0.0165 0.0093  0.0468  365  MET A CG  
2680  S SD  . MET A 367  ? 0.1721 0.1858 0.2695 -0.0165 0.0063  0.0413  365  MET A SD  
2681  C CE  . MET A 367  ? 0.1739 0.1853 0.2773 -0.0193 0.0025  0.0383  365  MET A CE  
2682  N N   . VAL A 368  ? 0.1305 0.1395 0.2312 -0.0161 0.0150  0.0558  366  VAL A N   
2683  C CA  . VAL A 368  ? 0.1168 0.1236 0.2135 -0.0150 0.0169  0.0573  366  VAL A CA  
2684  C C   . VAL A 368  ? 0.1249 0.1258 0.2217 -0.0161 0.0145  0.0546  366  VAL A C   
2685  O O   . VAL A 368  ? 0.1482 0.1477 0.2520 -0.0185 0.0123  0.0556  366  VAL A O   
2686  C CB  . VAL A 368  ? 0.1266 0.1377 0.2276 -0.0157 0.0189  0.0632  366  VAL A CB  
2687  C CG1 . VAL A 368  ? 0.1526 0.1620 0.2487 -0.0143 0.0209  0.0646  366  VAL A CG1 
2688  C CG2 . VAL A 368  ? 0.1691 0.1870 0.2708 -0.0145 0.0212  0.0656  366  VAL A CG2 
2689  N N   . ARG A 369  ? 0.1221 0.1194 0.2117 -0.0143 0.0148  0.0511  367  ARG A N   
2690  C CA  . ARG A 369  ? 0.1232 0.1152 0.2124 -0.0150 0.0127  0.0482  367  ARG A CA  
2691  C C   . ARG A 369  ? 0.1500 0.1406 0.2380 -0.0144 0.0144  0.0513  367  ARG A C   
2692  O O   . ARG A 369  ? 0.1635 0.1546 0.2450 -0.0123 0.0169  0.0518  367  ARG A O   
2693  C CB  . ARG A 369  ? 0.1577 0.1473 0.2402 -0.0136 0.0121  0.0431  367  ARG A CB  
2694  C CG  . ARG A 369  ? 0.1522 0.1370 0.2347 -0.0140 0.0100  0.0399  367  ARG A CG  
2695  C CD  . ARG A 369  ? 0.1578 0.1408 0.2326 -0.0123 0.0102  0.0358  367  ARG A CD  
2696  N NE  . ARG A 369  ? 0.1528 0.1380 0.2260 -0.0123 0.0091  0.0328  367  ARG A NE  
2697  C CZ  . ARG A 369  ? 0.1745 0.1600 0.2411 -0.0109 0.0098  0.0307  367  ARG A CZ  
2698  N NH1 . ARG A 369  ? 0.1822 0.1659 0.2432 -0.0093 0.0116  0.0311  367  ARG A NH1 
2699  N NH2 . ARG A 369  ? 0.1752 0.1633 0.2411 -0.0111 0.0085  0.0285  367  ARG A NH2 
2700  N N   . LEU A 370  ? 0.1392 0.1281 0.2336 -0.0164 0.0128  0.0535  368  LEU A N   
2701  C CA  . LEU A 370  ? 0.1280 0.1153 0.2218 -0.0161 0.0138  0.0566  368  LEU A CA  
2702  C C   . LEU A 370  ? 0.1514 0.1329 0.2425 -0.0156 0.0119  0.0524  368  LEU A C   
2703  O O   . LEU A 370  ? 0.1372 0.1156 0.2330 -0.0170 0.0087  0.0494  368  LEU A O   
2704  C CB  . LEU A 370  ? 0.1503 0.1390 0.2532 -0.0187 0.0128  0.0619  368  LEU A CB  
2705  C CG  . LEU A 370  ? 0.1654 0.1536 0.2688 -0.0188 0.0138  0.0665  368  LEU A CG  
2706  C CD1 . LEU A 370  ? 0.1868 0.1802 0.2842 -0.0167 0.0179  0.0698  368  LEU A CD1 
2707  C CD2 . LEU A 370  ? 0.1828 0.1715 0.2967 -0.0218 0.0118  0.0716  368  LEU A CD2 
2708  N N   . VAL A 371  ? 0.1351 0.1155 0.2190 -0.0135 0.0139  0.0519  369  VAL A N   
2709  C CA  . VAL A 371  ? 0.1375 0.1130 0.2182 -0.0128 0.0126  0.0482  369  VAL A CA  
2710  C C   . VAL A 371  ? 0.1462 0.1210 0.2260 -0.0123 0.0139  0.0521  369  VAL A C   
2711  O O   . VAL A 371  ? 0.1598 0.1384 0.2394 -0.0121 0.0162  0.0569  369  VAL A O   
2712  C CB  . VAL A 371  ? 0.1500 0.1251 0.2225 -0.0107 0.0135  0.0437  369  VAL A CB  
2713  C CG1 . VAL A 371  ? 0.1474 0.1242 0.2201 -0.0111 0.0124  0.0406  369  VAL A CG1 
2714  C CG2 . VAL A 371  ? 0.1453 0.1226 0.2111 -0.0087 0.0168  0.0458  369  VAL A CG2 
2715  N N   . LYS A 372  ? 0.1495 0.1199 0.2283 -0.0119 0.0124  0.0498  370  LYS A N   
2716  C CA  . LYS A 372  ? 0.1427 0.1127 0.2196 -0.0111 0.0138  0.0534  370  LYS A CA  
2717  C C   . LYS A 372  ? 0.1599 0.1312 0.2273 -0.0086 0.0165  0.0522  370  LYS A C   
2718  O O   . LYS A 372  ? 0.2045 0.1794 0.2693 -0.0077 0.0191  0.0560  370  LYS A O   
2719  C CB  . LYS A 372  ? 0.1830 0.1480 0.2638 -0.0118 0.0110  0.0523  370  LYS A CB  
2720  C CG  . LYS A 372  ? 0.1746 0.1388 0.2659 -0.0144 0.0084  0.0553  370  LYS A CG  
2721  C CD  . LYS A 372  ? 0.1649 0.1239 0.2619 -0.0151 0.0050  0.0544  370  LYS A CD  
2722  C CE  . LYS A 372  ? 0.1765 0.1346 0.2846 -0.0178 0.0020  0.0566  370  LYS A CE  
2723  N NZ  . LYS A 372  ? 0.1942 0.1465 0.3090 -0.0185 -0.0020 0.0545  370  LYS A NZ  
2724  N N   . GLY A 373  ? 0.1601 0.1291 0.2224 -0.0074 0.0161  0.0469  371  GLY A N   
2725  C CA  . GLY A 373  ? 0.1505 0.1206 0.2046 -0.0052 0.0183  0.0455  371  GLY A CA  
2726  C C   . GLY A 373  ? 0.1523 0.1189 0.2019 -0.0042 0.0174  0.0412  371  GLY A C   
2727  O O   . GLY A 373  ? 0.1703 0.1339 0.2221 -0.0046 0.0158  0.0407  371  GLY A O   
2728  N N   . ALA A 374  ? 0.1371 0.1041 0.1809 -0.0030 0.0182  0.0382  372  ALA A N   
2729  C CA  . ALA A 374  ? 0.1516 0.1159 0.1919 -0.0024 0.0171  0.0338  372  ALA A CA  
2730  C C   . ALA A 374  ? 0.1734 0.1369 0.2075 -0.0007 0.0185  0.0336  372  ALA A C   
2731  O O   . ALA A 374  ? 0.1904 0.1521 0.2217 -0.0003 0.0176  0.0304  372  ALA A O   
2732  C CB  . ALA A 374  ? 0.1746 0.1401 0.2134 -0.0026 0.0164  0.0305  372  ALA A CB  
2733  N N   . TYR A 375  ? 0.1571 0.1225 0.1890 0.0004  0.0205  0.0368  373  TYR A N   
2734  C CA  . TYR A 375  ? 0.1482 0.1133 0.1738 0.0022  0.0218  0.0362  373  TYR A CA  
2735  C C   . TYR A 375  ? 0.1440 0.1092 0.1693 0.0028  0.0225  0.0391  373  TYR A C   
2736  O O   . TYR A 375  ? 0.1588 0.1254 0.1795 0.0044  0.0241  0.0397  373  TYR A O   
2737  C CB  . TYR A 375  ? 0.1671 0.1349 0.1894 0.0035  0.0236  0.0365  373  TYR A CB  
2738  C CG  . TYR A 375  ? 0.1477 0.1160 0.1706 0.0029  0.0230  0.0344  373  TYR A CG  
2739  C CD1 . TYR A 375  ? 0.1602 0.1303 0.1879 0.0017  0.0226  0.0356  373  TYR A CD1 
2740  C CD2 . TYR A 375  ? 0.1845 0.1515 0.2032 0.0035  0.0226  0.0314  373  TYR A CD2 
2741  C CE1 . TYR A 375  ? 0.1794 0.1502 0.2075 0.0012  0.0219  0.0338  373  TYR A CE1 
2742  C CE2 . TYR A 375  ? 0.1960 0.1638 0.2153 0.0029  0.0218  0.0300  373  TYR A CE2 
2743  C CZ  . TYR A 375  ? 0.2264 0.1961 0.2502 0.0018  0.0215  0.0311  373  TYR A CZ  
2744  O OH  . TYR A 375  ? 0.2295 0.2004 0.2538 0.0013  0.0207  0.0298  373  TYR A OH  
2745  N N   . TRP A 376  ? 0.1376 0.1013 0.1678 0.0015  0.0211  0.0407  374  TRP A N   
2746  C CA  . TRP A 376  ? 0.1594 0.1241 0.1903 0.0018  0.0218  0.0448  374  TRP A CA  
2747  C C   . TRP A 376  ? 0.1595 0.1233 0.1846 0.0035  0.0223  0.0436  374  TRP A C   
2748  O O   . TRP A 376  ? 0.1638 0.1305 0.1855 0.0048  0.0241  0.0460  374  TRP A O   
2749  C CB  . TRP A 376  ? 0.1488 0.1112 0.1867 0.0001  0.0196  0.0466  374  TRP A CB  
2750  C CG  . TRP A 376  ? 0.1562 0.1199 0.1953 0.0002  0.0201  0.0515  374  TRP A CG  
2751  C CD1 . TRP A 376  ? 0.1809 0.1489 0.2219 -0.0003 0.0216  0.0568  374  TRP A CD1 
2752  C CD2 . TRP A 376  ? 0.1891 0.1504 0.2276 0.0007  0.0190  0.0518  374  TRP A CD2 
2753  N NE1 . TRP A 376  ? 0.1900 0.1586 0.2315 -0.0001 0.0215  0.0607  374  TRP A NE1 
2754  C CE2 . TRP A 376  ? 0.1962 0.1605 0.2363 0.0005  0.0199  0.0577  374  TRP A CE2 
2755  C CE3 . TRP A 376  ? 0.2128 0.1703 0.2498 0.0013  0.0175  0.0479  374  TRP A CE3 
2756  C CZ2 . TRP A 376  ? 0.2379 0.2011 0.2780 0.0009  0.0190  0.0599  374  TRP A CZ2 
2757  C CZ3 . TRP A 376  ? 0.2133 0.1695 0.2505 0.0018  0.0167  0.0497  374  TRP A CZ3 
2758  C CH2 . TRP A 376  ? 0.2157 0.1746 0.2545 0.0016  0.0174  0.0557  374  TRP A CH2 
2759  N N   . ASP A 377  ? 0.1736 0.1339 0.1973 0.0036  0.0208  0.0399  375  ASP A N   
2760  C CA  . ASP A 377  ? 0.1692 0.1289 0.1882 0.0050  0.0211  0.0393  375  ASP A CA  
2761  C C   . ASP A 377  ? 0.1675 0.1290 0.1802 0.0066  0.0229  0.0379  375  ASP A C   
2762  O O   . ASP A 377  ? 0.1827 0.1452 0.1915 0.0080  0.0237  0.0387  375  ASP A O   
2763  C CB  . ASP A 377  ? 0.2391 0.1952 0.2585 0.0049  0.0191  0.0357  375  ASP A CB  
2764  C CG  . ASP A 377  ? 0.2973 0.2526 0.3158 0.0045  0.0184  0.0313  375  ASP A CG  
2765  O OD1 . ASP A 377  ? 0.3240 0.2808 0.3395 0.0048  0.0195  0.0305  375  ASP A OD1 
2766  O OD2 . ASP A 377  ? 0.2723 0.2257 0.2930 0.0040  0.0166  0.0285  375  ASP A OD2 
2767  N N   . ALA A 378  ? 0.1570 0.1191 0.1689 0.0066  0.0233  0.0360  376  ALA A N   
2768  C CA  . ALA A 378  ? 0.1398 0.1034 0.1467 0.0081  0.0246  0.0348  376  ALA A CA  
2769  C C   . ALA A 378  ? 0.1650 0.1326 0.1711 0.0093  0.0266  0.0379  376  ALA A C   
2770  O O   . ALA A 378  ? 0.1672 0.1364 0.1689 0.0111  0.0276  0.0372  376  ALA A O   
2771  C CB  . ALA A 378  ? 0.1832 0.1465 0.1902 0.0077  0.0243  0.0323  376  ALA A CB  
2772  N N   . GLU A 379  ? 0.1726 0.1425 0.1833 0.0083  0.0270  0.0413  377  GLU A N   
2773  C CA  . GLU A 379  ? 0.1476 0.1225 0.1578 0.0093  0.0290  0.0446  377  GLU A CA  
2774  C C   . GLU A 379  ? 0.1616 0.1381 0.1697 0.0102  0.0295  0.0469  377  GLU A C   
2775  O O   . GLU A 379  ? 0.1835 0.1642 0.1882 0.0120  0.0312  0.0478  377  GLU A O   
2776  C CB  . GLU A 379  ? 0.1702 0.1477 0.1865 0.0077  0.0293  0.0482  377  GLU A CB  
2777  C CG  . GLU A 379  ? 0.1681 0.1450 0.1868 0.0069  0.0289  0.0464  377  GLU A CG  
2778  C CD  . GLU A 379  ? 0.1776 0.1571 0.1929 0.0088  0.0303  0.0446  377  GLU A CD  
2779  O OE1 . GLU A 379  ? 0.1823 0.1645 0.1936 0.0109  0.0318  0.0446  377  GLU A OE1 
2780  O OE2 . GLU A 379  ? 0.1879 0.1667 0.2050 0.0082  0.0298  0.0430  377  GLU A OE2 
2781  N N   . ILE A 380  ? 0.1581 0.1315 0.1682 0.0090  0.0279  0.0477  378  ILE A N   
2782  C CA  . ILE A 380  ? 0.1722 0.1470 0.1802 0.0099  0.0281  0.0500  378  ILE A CA  
2783  C C   . ILE A 380  ? 0.1746 0.1491 0.1759 0.0120  0.0285  0.0466  378  ILE A C   
2784  O O   . ILE A 380  ? 0.1731 0.1516 0.1708 0.0136  0.0298  0.0478  378  ILE A O   
2785  C CB  . ILE A 380  ? 0.1675 0.1385 0.1797 0.0083  0.0260  0.0512  378  ILE A CB  
2786  C CG1 . ILE A 380  ? 0.1764 0.1472 0.1960 0.0062  0.0251  0.0545  378  ILE A CG1 
2787  C CG2 . ILE A 380  ? 0.1725 0.1448 0.1825 0.0092  0.0260  0.0538  378  ILE A CG2 
2788  C CD1 . ILE A 380  ? 0.1783 0.1549 0.2001 0.0058  0.0268  0.0603  378  ILE A CD1 
2789  N N   . LYS A 381  ? 0.1673 0.1375 0.1671 0.0119  0.0273  0.0422  379  LYS A N   
2790  C CA  . LYS A 381  ? 0.1615 0.1310 0.1557 0.0136  0.0273  0.0388  379  LYS A CA  
2791  C C   . LYS A 381  ? 0.1720 0.1450 0.1628 0.0155  0.0290  0.0380  379  LYS A C   
2792  O O   . LYS A 381  ? 0.1654 0.1406 0.1521 0.0173  0.0295  0.0373  379  LYS A O   
2793  C CB  . LYS A 381  ? 0.1765 0.1414 0.1704 0.0128  0.0258  0.0348  379  LYS A CB  
2794  C CG  . LYS A 381  ? 0.1704 0.1343 0.1592 0.0142  0.0255  0.0316  379  LYS A CG  
2795  C CD  . LYS A 381  ? 0.1652 0.1254 0.1542 0.0132  0.0239  0.0283  379  LYS A CD  
2796  C CE  . LYS A 381  ? 0.1758 0.1351 0.1604 0.0143  0.0234  0.0256  379  LYS A CE  
2797  N NZ  . LYS A 381  ? 0.1702 0.1268 0.1551 0.0131  0.0220  0.0229  379  LYS A NZ  
2798  N N   . ARG A 382  ? 0.1610 0.1350 0.1538 0.0152  0.0296  0.0377  380  ARG A N   
2799  C CA  A ARG A 382  ? 0.1787 0.1559 0.1690 0.0173  0.0309  0.0363  380  ARG A CA  
2800  C CA  B ARG A 382  ? 0.1786 0.1557 0.1688 0.0173  0.0309  0.0363  380  ARG A CA  
2801  C C   . ARG A 382  ? 0.1699 0.1533 0.1586 0.0189  0.0327  0.0391  380  ARG A C   
2802  O O   . ARG A 382  ? 0.1875 0.1734 0.1721 0.0213  0.0334  0.0370  380  ARG A O   
2803  C CB  A ARG A 382  ? 0.2134 0.1906 0.2068 0.0166  0.0311  0.0360  380  ARG A CB  
2804  C CB  B ARG A 382  ? 0.2135 0.1904 0.2067 0.0166  0.0310  0.0358  380  ARG A CB  
2805  C CG  A ARG A 382  ? 0.2485 0.2291 0.2401 0.0189  0.0323  0.0346  380  ARG A CG  
2806  C CG  B ARG A 382  ? 0.2564 0.2358 0.2477 0.0188  0.0320  0.0337  380  ARG A CG  
2807  C CD  A ARG A 382  ? 0.2581 0.2378 0.2528 0.0181  0.0321  0.0339  380  ARG A CD  
2808  C CD  B ARG A 382  ? 0.2719 0.2500 0.2585 0.0209  0.0314  0.0302  380  ARG A CD  
2809  N NE  A ARG A 382  ? 0.3206 0.2952 0.3167 0.0161  0.0302  0.0324  380  ARG A NE  
2810  N NE  B ARG A 382  ? 0.3283 0.3010 0.3142 0.0198  0.0295  0.0274  380  ARG A NE  
2811  C CZ  A ARG A 382  ? 0.3008 0.2741 0.2995 0.0149  0.0295  0.0318  380  ARG A CZ  
2812  C CZ  B ARG A 382  ? 0.3234 0.2941 0.3059 0.0210  0.0285  0.0244  380  ARG A CZ  
2813  N NH1 A ARG A 382  ? 0.2371 0.2134 0.2378 0.0157  0.0305  0.0324  380  ARG A NH1 
2814  N NH1 B ARG A 382  ? 0.2725 0.2461 0.2518 0.0235  0.0292  0.0233  380  ARG A NH1 
2815  N NH2 A ARG A 382  ? 0.3670 0.3366 0.3666 0.0131  0.0279  0.0305  380  ARG A NH2 
2816  N NH2 B ARG A 382  ? 0.3442 0.3104 0.3265 0.0197  0.0268  0.0226  380  ARG A NH2 
2817  N N   . ALA A 383  ? 0.1573 0.1436 0.1495 0.0177  0.0334  0.0437  381  ALA A N   
2818  C CA  . ALA A 383  ? 0.1596 0.1531 0.1504 0.0190  0.0352  0.0470  381  ALA A CA  
2819  C C   . ALA A 383  ? 0.1625 0.1568 0.1489 0.0203  0.0350  0.0467  381  ALA A C   
2820  O O   . ALA A 383  ? 0.1931 0.1931 0.1757 0.0226  0.0363  0.0465  381  ALA A O   
2821  C CB  . ALA A 383  ? 0.1995 0.1956 0.1957 0.0169  0.0357  0.0527  381  ALA A CB  
2822  N N   . GLN A 384  ? 0.1718 0.1609 0.1585 0.0191  0.0332  0.0462  382  GLN A N   
2823  C CA  . GLN A 384  ? 0.1751 0.1649 0.1576 0.0203  0.0327  0.0459  382  GLN A CA  
2824  C C   . GLN A 384  ? 0.1756 0.1648 0.1529 0.0226  0.0326  0.0406  382  GLN A C   
2825  O O   . GLN A 384  ? 0.1998 0.1934 0.1729 0.0247  0.0333  0.0402  382  GLN A O   
2826  C CB  . GLN A 384  ? 0.1715 0.1558 0.1561 0.0185  0.0307  0.0464  382  GLN A CB  
2827  C CG  . GLN A 384  ? 0.1748 0.1600 0.1646 0.0166  0.0305  0.0520  382  GLN A CG  
2828  C CD  . GLN A 384  ? 0.1864 0.1664 0.1787 0.0152  0.0283  0.0521  382  GLN A CD  
2829  O OE1 . GLN A 384  ? 0.2080 0.1833 0.1990 0.0153  0.0270  0.0478  382  GLN A OE1 
2830  N NE2 . GLN A 384  ? 0.1981 0.1792 0.1943 0.0140  0.0277  0.0571  382  GLN A NE2 
2831  N N   . LEU A 385  ? 0.1713 0.1553 0.1490 0.0222  0.0315  0.0367  383  LEU A N   
2832  C CA  . LEU A 385  ? 0.1891 0.1720 0.1628 0.0241  0.0310  0.0318  383  LEU A CA  
2833  C C   . LEU A 385  ? 0.1916 0.1802 0.1631 0.0267  0.0326  0.0309  383  LEU A C   
2834  O O   . LEU A 385  ? 0.2126 0.2029 0.1801 0.0290  0.0323  0.0279  383  LEU A O   
2835  C CB  . LEU A 385  ? 0.1978 0.1749 0.1732 0.0229  0.0297  0.0288  383  LEU A CB  
2836  C CG  . LEU A 385  ? 0.2285 0.2002 0.2050 0.0209  0.0279  0.0281  383  LEU A CG  
2837  C CD1 . LEU A 385  ? 0.2315 0.1994 0.2098 0.0198  0.0270  0.0258  383  LEU A CD1 
2838  C CD2 . LEU A 385  ? 0.2517 0.2224 0.2245 0.0219  0.0269  0.0259  383  LEU A CD2 
2839  N N   . ASP A 386  ? 0.1999 0.1920 0.1743 0.0266  0.0340  0.0331  384  ASP A N   
2840  C CA  . ASP A 386  ? 0.1897 0.1875 0.1626 0.0292  0.0356  0.0317  384  ASP A CA  
2841  C C   . ASP A 386  ? 0.2061 0.2124 0.1769 0.0307  0.0374  0.0347  384  ASP A C   
2842  O O   . ASP A 386  ? 0.2133 0.2257 0.1825 0.0333  0.0388  0.0335  384  ASP A O   
2843  C CB  . ASP A 386  ? 0.2271 0.2252 0.2041 0.0285  0.0363  0.0324  384  ASP A CB  
2844  C CG  . ASP A 386  ? 0.2701 0.2614 0.2484 0.0279  0.0346  0.0287  384  ASP A CG  
2845  O OD1 . ASP A 386  ? 0.3067 0.2936 0.2827 0.0282  0.0329  0.0254  384  ASP A OD1 
2846  O OD2 . ASP A 386  ? 0.2580 0.2489 0.2399 0.0270  0.0349  0.0295  384  ASP A OD2 
2847  N N   . GLY A 387  ? 0.1922 0.1992 0.1630 0.0293  0.0372  0.0387  385  GLY A N   
2848  C CA  . GLY A 387  ? 0.1885 0.2040 0.1571 0.0305  0.0388  0.0422  385  GLY A CA  
2849  C C   . GLY A 387  ? 0.2331 0.2563 0.2044 0.0307  0.0411  0.0461  385  GLY A C   
2850  O O   . GLY A 387  ? 0.2319 0.2639 0.2003 0.0330  0.0428  0.0466  385  GLY A O   
2851  N N   . LEU A 388  ? 0.2140 0.2345 0.1907 0.0282  0.0411  0.0487  386  LEU A N   
2852  C CA  . LEU A 388  ? 0.2105 0.2379 0.1903 0.0281  0.0432  0.0522  386  LEU A CA  
2853  C C   . LEU A 388  ? 0.2208 0.2535 0.2032 0.0262  0.0440  0.0596  386  LEU A C   
2854  O O   . LEU A 388  ? 0.2273 0.2570 0.2099 0.0247  0.0427  0.0621  386  LEU A O   
2855  C CB  . LEU A 388  ? 0.2130 0.2354 0.1975 0.0265  0.0427  0.0512  386  LEU A CB  
2856  C CG  . LEU A 388  ? 0.2165 0.2345 0.1988 0.0284  0.0418  0.0446  386  LEU A CG  
2857  C CD1 . LEU A 388  ? 0.2374 0.2511 0.2243 0.0268  0.0413  0.0439  386  LEU A CD1 
2858  C CD2 . LEU A 388  ? 0.2464 0.2714 0.2250 0.0322  0.0433  0.0415  386  LEU A CD2 
2859  N N   . ALA A 389  ? 0.2389 0.2801 0.2236 0.0264  0.0461  0.0634  387  ALA A N   
2860  C CA  . ALA A 389  ? 0.2443 0.2927 0.2309 0.0250  0.0471  0.0708  387  ALA A CA  
2861  C C   . ALA A 389  ? 0.2675 0.3097 0.2603 0.0211  0.0453  0.0755  387  ALA A C   
2862  O O   . ALA A 389  ? 0.2993 0.3433 0.2933 0.0197  0.0449  0.0808  387  ALA A O   
2863  C CB  . ALA A 389  ? 0.3110 0.3703 0.2992 0.0259  0.0498  0.0738  387  ALA A CB  
2864  N N   . ASP A 390  ? 0.2072 0.2420 0.2043 0.0193  0.0441  0.0736  388  ASP A N   
2865  C CA  . ASP A 390  ? 0.1993 0.2284 0.2030 0.0157  0.0423  0.0774  388  ASP A CA  
2866  C C   . ASP A 390  ? 0.1996 0.2200 0.2054 0.0149  0.0408  0.0724  388  ASP A C   
2867  O O   . ASP A 390  ? 0.2009 0.2202 0.2031 0.0169  0.0412  0.0669  388  ASP A O   
2868  C CB  . ASP A 390  ? 0.2245 0.2606 0.2342 0.0138  0.0434  0.0846  388  ASP A CB  
2869  C CG  . ASP A 390  ? 0.2552 0.2877 0.2712 0.0104  0.0414  0.0903  388  ASP A CG  
2870  O OD1 . ASP A 390  ? 0.2425 0.2655 0.2614 0.0088  0.0389  0.0880  388  ASP A OD1 
2871  O OD2 . ASP A 390  ? 0.2652 0.3049 0.2835 0.0094  0.0422  0.0973  388  ASP A OD2 
2872  N N   . PHE A 391  ? 0.1989 0.2137 0.2106 0.0120  0.0389  0.0742  389  PHE A N   
2873  C CA  . PHE A 391  ? 0.1873 0.1947 0.2012 0.0110  0.0373  0.0699  389  PHE A CA  
2874  C C   . PHE A 391  ? 0.1759 0.1862 0.1943 0.0101  0.0382  0.0712  389  PHE A C   
2875  O O   . PHE A 391  ? 0.1735 0.1903 0.1954 0.0092  0.0394  0.0765  389  PHE A O   
2876  C CB  . PHE A 391  ? 0.1934 0.1935 0.2116 0.0086  0.0346  0.0706  389  PHE A CB  
2877  C CG  . PHE A 391  ? 0.1704 0.1677 0.1847 0.0094  0.0336  0.0695  389  PHE A CG  
2878  C CD1 . PHE A 391  ? 0.1718 0.1647 0.1810 0.0110  0.0330  0.0635  389  PHE A CD1 
2879  C CD2 . PHE A 391  ? 0.1859 0.1855 0.2017 0.0088  0.0332  0.0746  389  PHE A CD2 
2880  C CE1 . PHE A 391  ? 0.1936 0.1843 0.1992 0.0118  0.0321  0.0624  389  PHE A CE1 
2881  C CE2 . PHE A 391  ? 0.1891 0.1864 0.2013 0.0097  0.0322  0.0735  389  PHE A CE2 
2882  C CZ  . PHE A 391  ? 0.1704 0.1633 0.1774 0.0113  0.0317  0.0672  389  PHE A CZ  
2883  N N   . PRO A 392  ? 0.1677 0.1739 0.1860 0.0102  0.0376  0.0665  390  PRO A N   
2884  C CA  . PRO A 392  ? 0.1810 0.1892 0.2042 0.0091  0.0380  0.0676  390  PRO A CA  
2885  C C   . PRO A 392  ? 0.1567 0.1602 0.1869 0.0058  0.0358  0.0692  390  PRO A C   
2886  O O   . PRO A 392  ? 0.1752 0.1795 0.2099 0.0046  0.0356  0.0697  390  PRO A O   
2887  C CB  . PRO A 392  ? 0.1638 0.1697 0.1834 0.0110  0.0381  0.0617  390  PRO A CB  
2888  C CG  . PRO A 392  ? 0.1449 0.1435 0.1609 0.0112  0.0363  0.0576  390  PRO A CG  
2889  C CD  . PRO A 392  ? 0.1533 0.1536 0.1671 0.0115  0.0365  0.0603  390  PRO A CD  
2890  N N   . VAL A 393  ? 0.1541 0.1525 0.1855 0.0046  0.0338  0.0697  391  VAL A N   
2891  C CA  . VAL A 393  ? 0.1585 0.1520 0.1967 0.0018  0.0313  0.0706  391  VAL A CA  
2892  C C   . VAL A 393  ? 0.1735 0.1673 0.2151 0.0005  0.0303  0.0757  391  VAL A C   
2893  O O   . VAL A 393  ? 0.1850 0.1814 0.2224 0.0018  0.0314  0.0774  391  VAL A O   
2894  C CB  . VAL A 393  ? 0.1642 0.1501 0.2010 0.0017  0.0291  0.0647  391  VAL A CB  
2895  C CG1 . VAL A 393  ? 0.1919 0.1776 0.2265 0.0026  0.0296  0.0604  391  VAL A CG1 
2896  C CG2 . VAL A 393  ? 0.1799 0.1634 0.2108 0.0034  0.0290  0.0624  391  VAL A CG2 
2897  N N   . PHE A 394  ? 0.1652 0.1563 0.2147 -0.0022 0.0282  0.0782  392  PHE A N   
2898  C CA  . PHE A 394  ? 0.1692 0.1591 0.2230 -0.0037 0.0266  0.0829  392  PHE A CA  
2899  C C   . PHE A 394  ? 0.1674 0.1511 0.2180 -0.0027 0.0248  0.0790  392  PHE A C   
2900  O O   . PHE A 394  ? 0.1966 0.1763 0.2432 -0.0015 0.0244  0.0728  392  PHE A O   
2901  C CB  . PHE A 394  ? 0.1774 0.1652 0.2413 -0.0068 0.0242  0.0859  392  PHE A CB  
2902  C CG  . PHE A 394  ? 0.1628 0.1574 0.2305 -0.0080 0.0258  0.0903  392  PHE A CG  
2903  C CD1 . PHE A 394  ? 0.2133 0.2161 0.2800 -0.0077 0.0276  0.0954  392  PHE A CD1 
2904  C CD2 . PHE A 394  ? 0.1990 0.1928 0.2700 -0.0090 0.0253  0.0878  392  PHE A CD2 
2905  C CE1 . PHE A 394  ? 0.2060 0.2162 0.2756 -0.0084 0.0291  0.0985  392  PHE A CE1 
2906  C CE2 . PHE A 394  ? 0.1771 0.1776 0.2515 -0.0099 0.0269  0.0918  392  PHE A CE2 
2907  C CZ  . PHE A 394  ? 0.2058 0.2146 0.2793 -0.0095 0.0287  0.0968  392  PHE A CZ  
2908  N N   . THR A 395  ? 0.1899 0.1735 0.2422 -0.0031 0.0239  0.0831  393  THR A N   
2909  C CA  . THR A 395  ? 0.1869 0.1651 0.2369 -0.0022 0.0222  0.0800  393  THR A CA  
2910  C C   . THR A 395  ? 0.2156 0.1881 0.2738 -0.0041 0.0186  0.0814  393  THR A C   
2911  O O   . THR A 395  ? 0.2004 0.1680 0.2577 -0.0034 0.0169  0.0781  393  THR A O   
2912  C CB  . THR A 395  ? 0.1960 0.1782 0.2400 -0.0004 0.0237  0.0826  393  THR A CB  
2913  O OG1 . THR A 395  ? 0.2187 0.2057 0.2671 -0.0018 0.0239  0.0905  393  THR A OG1 
2914  C CG2 . THR A 395  ? 0.2355 0.2225 0.2711 0.0020  0.0268  0.0799  393  THR A CG2 
2915  N N   . ARG A 396  ? 0.2037 0.1772 0.2700 -0.0065 0.0173  0.0852  394  ARG A N   
2916  C CA  . ARG A 396  ? 0.2145 0.1829 0.2889 -0.0082 0.0132  0.0842  394  ARG A CA  
2917  C C   . ARG A 396  ? 0.1987 0.1644 0.2781 -0.0096 0.0120  0.0811  394  ARG A C   
2918  O O   . ARG A 396  ? 0.2033 0.1733 0.2837 -0.0105 0.0135  0.0830  394  ARG A O   
2919  C CB  . ARG A 396  ? 0.2208 0.1928 0.3007 -0.0098 0.0116  0.0898  394  ARG A CB  
2920  C CG  . ARG A 396  ? 0.2388 0.2137 0.3146 -0.0086 0.0124  0.0932  394  ARG A CG  
2921  C CD  . ARG A 396  ? 0.2659 0.2443 0.3483 -0.0104 0.0104  0.0988  394  ARG A CD  
2922  N NE  . ARG A 396  ? 0.2968 0.2797 0.3747 -0.0093 0.0116  0.1027  394  ARG A NE  
2923  C CZ  . ARG A 396  ? 0.3388 0.3202 0.4199 -0.0096 0.0092  0.1049  394  ARG A CZ  
2924  N NH1 . ARG A 396  ? 0.3628 0.3383 0.4518 -0.0109 0.0053  0.1036  394  ARG A NH1 
2925  N NH2 . ARG A 396  ? 0.3224 0.3085 0.3985 -0.0085 0.0105  0.1083  394  ARG A NH2 
2926  N N   . LYS A 397  ? 0.2059 0.1648 0.2886 -0.0097 0.0091  0.0761  395  LYS A N   
2927  C CA  . LYS A 397  ? 0.2120 0.1682 0.2993 -0.0108 0.0077  0.0724  395  LYS A CA  
2928  C C   . LYS A 397  ? 0.2275 0.1865 0.3226 -0.0132 0.0062  0.0759  395  LYS A C   
2929  O O   . LYS A 397  ? 0.2161 0.1765 0.3131 -0.0142 0.0067  0.0752  395  LYS A O   
2930  C CB  . LYS A 397  ? 0.2372 0.1865 0.3269 -0.0103 0.0046  0.0663  395  LYS A CB  
2931  C CG  . LYS A 397  ? 0.2849 0.2329 0.3748 -0.0104 0.0037  0.0598  395  LYS A CG  
2932  C CD  . LYS A 397  ? 0.2569 0.2022 0.3576 -0.0127 0.0002  0.0601  395  LYS A CD  
2933  C CE  . LYS A 397  ? 0.2719 0.2167 0.3728 -0.0128 -0.0007 0.0537  395  LYS A CE  
2934  N NZ  . LYS A 397  ? 0.2725 0.2148 0.3844 -0.0149 -0.0044 0.0538  395  LYS A NZ  
2935  N N   . ILE A 398  ? 0.2095 0.1696 0.3094 -0.0142 0.0043  0.0798  396  ILE A N   
2936  C CA  . ILE A 398  ? 0.2109 0.1737 0.3189 -0.0166 0.0026  0.0833  396  ILE A CA  
2937  C C   . ILE A 398  ? 0.1906 0.1610 0.2962 -0.0170 0.0059  0.0878  396  ILE A C   
2938  O O   . ILE A 398  ? 0.2159 0.1886 0.3272 -0.0188 0.0052  0.0894  396  ILE A O   
2939  C CB  . ILE A 398  ? 0.2396 0.2020 0.3534 -0.0174 -0.0003 0.0869  396  ILE A CB  
2940  C CG1 . ILE A 398  ? 0.3031 0.2662 0.4272 -0.0199 -0.0033 0.0890  396  ILE A CG1 
2941  C CG2 . ILE A 398  ? 0.2738 0.2422 0.3828 -0.0168 0.0023  0.0927  396  ILE A CG2 
2942  C CD1 . ILE A 398  ? 0.3344 0.2966 0.4654 -0.0208 -0.0065 0.0923  396  ILE A CD1 
2943  N N   . HIS A 399  ? 0.2163 0.1910 0.3137 -0.0153 0.0096  0.0897  397  HIS A N   
2944  C CA  . HIS A 399  ? 0.2033 0.1856 0.2979 -0.0153 0.0129  0.0931  397  HIS A CA  
2945  C C   . HIS A 399  ? 0.1910 0.1725 0.2852 -0.0153 0.0139  0.0895  397  HIS A C   
2946  O O   . HIS A 399  ? 0.1938 0.1799 0.2910 -0.0165 0.0148  0.0918  397  HIS A O   
2947  C CB  . HIS A 399  ? 0.2044 0.1914 0.2902 -0.0130 0.0165  0.0950  397  HIS A CB  
2948  C CG  . HIS A 399  ? 0.1961 0.1858 0.2823 -0.0131 0.0158  0.0994  397  HIS A CG  
2949  N ND1 . HIS A 399  ? 0.2042 0.1973 0.2829 -0.0110 0.0181  0.1007  397  HIS A ND1 
2950  C CD2 . HIS A 399  ? 0.2490 0.2388 0.3426 -0.0149 0.0129  0.1030  397  HIS A CD2 
2951  C CE1 . HIS A 399  ? 0.2212 0.2164 0.3024 -0.0117 0.0168  0.1050  397  HIS A CE1 
2952  N NE2 . HIS A 399  ? 0.2412 0.2344 0.3315 -0.0140 0.0136  0.1065  397  HIS A NE2 
2953  N N   . THR A 400  ? 0.1729 0.1486 0.2635 -0.0141 0.0138  0.0840  398  THR A N   
2954  C CA  . THR A 400  ? 0.1701 0.1446 0.2606 -0.0143 0.0145  0.0805  398  THR A CA  
2955  C C   . THR A 400  ? 0.1842 0.1570 0.2840 -0.0167 0.0112  0.0797  398  THR A C   
2956  O O   . THR A 400  ? 0.1771 0.1525 0.2789 -0.0176 0.0119  0.0799  398  THR A O   
2957  C CB  . THR A 400  ? 0.1513 0.1212 0.2352 -0.0122 0.0142  0.0731  398  THR A CB  
2958  O OG1 . THR A 400  ? 0.1831 0.1559 0.2578 -0.0098 0.0173  0.0729  398  THR A OG1 
2959  C CG2 . THR A 400  ? 0.1639 0.1333 0.2473 -0.0122 0.0139  0.0678  398  THR A CG2 
2960  N N   . ASP A 401  ? 0.1848 0.1532 0.2905 -0.0178 0.0075  0.0789  399  ASP A N   
2961  C CA  . ASP A 401  ? 0.1858 0.1525 0.3007 -0.0200 0.0040  0.0780  399  ASP A CA  
2962  C C   . ASP A 401  ? 0.1985 0.1717 0.3180 -0.0217 0.0046  0.0838  399  ASP A C   
2963  O O   . ASP A 401  ? 0.1945 0.1689 0.3185 -0.0231 0.0038  0.0833  399  ASP A O   
2964  C CB  . ASP A 401  ? 0.1931 0.1542 0.3136 -0.0204 -0.0001 0.0760  399  ASP A CB  
2965  C CG  . ASP A 401  ? 0.2272 0.1819 0.3448 -0.0188 -0.0013 0.0692  399  ASP A CG  
2966  O OD1 . ASP A 401  ? 0.2583 0.2121 0.3718 -0.0181 0.0002  0.0656  399  ASP A OD1 
2967  O OD2 . ASP A 401  ? 0.2825 0.2333 0.4020 -0.0182 -0.0037 0.0677  399  ASP A OD2 
2968  N N   . VAL A 402  ? 0.1886 0.1665 0.3072 -0.0216 0.0058  0.0893  400  VAL A N   
2969  C CA  . VAL A 402  ? 0.2096 0.1947 0.3324 -0.0231 0.0065  0.0952  400  VAL A CA  
2970  C C   . VAL A 402  ? 0.1857 0.1762 0.3042 -0.0225 0.0102  0.0956  400  VAL A C   
2971  O O   . VAL A 402  ? 0.1845 0.1787 0.3080 -0.0240 0.0100  0.0975  400  VAL A O   
2972  C CB  . VAL A 402  ? 0.2218 0.2114 0.3437 -0.0229 0.0073  0.1009  400  VAL A CB  
2973  C CG1 . VAL A 402  ? 0.1800 0.1782 0.3058 -0.0243 0.0084  0.1071  400  VAL A CG1 
2974  C CG2 . VAL A 402  ? 0.2625 0.2469 0.3900 -0.0237 0.0033  0.1009  400  VAL A CG2 
2975  N N   . SER A 403  ? 0.1896 0.1810 0.2990 -0.0201 0.0135  0.0939  401  SER A N   
2976  C CA  . SER A 403  ? 0.1874 0.1836 0.2927 -0.0192 0.0170  0.0937  401  SER A CA  
2977  C C   . SER A 403  ? 0.2110 0.2043 0.3205 -0.0204 0.0155  0.0901  401  SER A C   
2978  O O   . SER A 403  ? 0.1776 0.1759 0.2895 -0.0212 0.0166  0.0919  401  SER A O   
2979  C CB  . SER A 403  ? 0.1755 0.1711 0.2708 -0.0163 0.0201  0.0914  401  SER A CB  
2980  O OG  . SER A 403  ? 0.1822 0.1820 0.2738 -0.0151 0.0232  0.0907  401  SER A OG  
2981  N N   . TYR A 404  ? 0.1729 0.1583 0.2833 -0.0206 0.0129  0.0849  402  TYR A N   
2982  C CA  . TYR A 404  ? 0.1724 0.1550 0.2868 -0.0218 0.0112  0.0811  402  TYR A CA  
2983  C C   . TYR A 404  ? 0.1871 0.1723 0.3109 -0.0243 0.0088  0.0836  402  TYR A C   
2984  O O   . TYR A 404  ? 0.1705 0.1587 0.2964 -0.0252 0.0094  0.0837  402  TYR A O   
2985  C CB  . TYR A 404  ? 0.1825 0.1572 0.2968 -0.0214 0.0083  0.0748  402  TYR A CB  
2986  C CG  . TYR A 404  ? 0.1734 0.1465 0.2876 -0.0213 0.0068  0.0684  402  TYR A CG  
2987  C CD1 . TYR A 404  ? 0.1772 0.1492 0.3005 -0.0237 0.0037  0.0679  402  TYR A CD1 
2988  C CD2 . TYR A 404  ? 0.1552 0.1282 0.2604 -0.0189 0.0083  0.0629  402  TYR A CD2 
2989  C CE1 . TYR A 404  ? 0.1723 0.1436 0.2954 -0.0236 0.0022  0.0620  402  TYR A CE1 
2990  C CE2 . TYR A 404  ? 0.1719 0.1442 0.2771 -0.0190 0.0069  0.0574  402  TYR A CE2 
2991  C CZ  . TYR A 404  ? 0.1699 0.1415 0.2837 -0.0212 0.0038  0.0569  402  TYR A CZ  
2992  O OH  . TYR A 404  ? 0.1858 0.1575 0.2995 -0.0213 0.0023  0.0515  402  TYR A OH  
2993  N N   . ILE A 405  ? 0.1817 0.1656 0.3112 -0.0256 0.0060  0.0859  403  ILE A N   
2994  C CA  . ILE A 405  ? 0.1987 0.1845 0.3377 -0.0280 0.0032  0.0883  403  ILE A CA  
2995  C C   . ILE A 405  ? 0.1847 0.1794 0.3239 -0.0285 0.0060  0.0942  403  ILE A C   
2996  O O   . ILE A 405  ? 0.2065 0.2039 0.3510 -0.0300 0.0053  0.0951  403  ILE A O   
2997  C CB  . ILE A 405  ? 0.1890 0.1710 0.3343 -0.0290 -0.0006 0.0893  403  ILE A CB  
2998  C CG1 . ILE A 405  ? 0.2329 0.2065 0.3788 -0.0285 -0.0036 0.0824  403  ILE A CG1 
2999  C CG2 . ILE A 405  ? 0.2563 0.2408 0.4114 -0.0315 -0.0033 0.0928  403  ILE A CG2 
3000  C CD1 . ILE A 405  ? 0.2813 0.2506 0.4308 -0.0285 -0.0068 0.0825  403  ILE A CD1 
3001  N N   . ALA A 406  ? 0.1930 0.1926 0.3262 -0.0269 0.0094  0.0979  404  ALA A N   
3002  C CA  . ALA A 406  ? 0.1916 0.2006 0.3245 -0.0269 0.0123  0.1031  404  ALA A CA  
3003  C C   . ALA A 406  ? 0.1917 0.2036 0.3219 -0.0262 0.0148  0.1010  404  ALA A C   
3004  O O   . ALA A 406  ? 0.2239 0.2417 0.3580 -0.0272 0.0154  0.1038  404  ALA A O   
3005  C CB  . ALA A 406  ? 0.2105 0.2244 0.3366 -0.0250 0.0154  0.1065  404  ALA A CB  
3006  N N   . CYS A 407  ? 0.1845 0.1924 0.3082 -0.0244 0.0162  0.0962  405  CYS A N   
3007  C CA  . CYS A 407  ? 0.1728 0.1831 0.2941 -0.0237 0.0184  0.0942  405  CYS A CA  
3008  C C   . CYS A 407  ? 0.1714 0.1789 0.2999 -0.0259 0.0154  0.0916  405  CYS A C   
3009  O O   . CYS A 407  ? 0.1759 0.1879 0.3059 -0.0261 0.0166  0.0921  405  CYS A O   
3010  C CB  . CYS A 407  ? 0.1961 0.2027 0.3087 -0.0212 0.0205  0.0901  405  CYS A CB  
3011  S SG  . CYS A 407  ? 0.2537 0.2658 0.3576 -0.0182 0.0247  0.0931  405  CYS A SG  
3012  N N   . ALA A 408  ? 0.1821 0.1826 0.3154 -0.0274 0.0113  0.0889  406  ALA A N   
3013  C CA  . ALA A 408  ? 0.1806 0.1789 0.3214 -0.0296 0.0080  0.0864  406  ALA A CA  
3014  C C   . ALA A 408  ? 0.1989 0.2031 0.3470 -0.0315 0.0072  0.0912  406  ALA A C   
3015  O O   . ALA A 408  ? 0.1956 0.2020 0.3478 -0.0327 0.0065  0.0905  406  ALA A O   
3016  C CB  . ALA A 408  ? 0.2047 0.1949 0.3495 -0.0305 0.0036  0.0823  406  ALA A CB  
3017  N N   . ALA A 409  ? 0.2069 0.2141 0.3568 -0.0318 0.0072  0.0963  407  ALA A N   
3018  C CA  . ALA A 409  ? 0.1928 0.2065 0.3494 -0.0336 0.0068  0.1016  407  ALA A CA  
3019  C C   . ALA A 409  ? 0.2185 0.2403 0.3720 -0.0326 0.0107  0.1036  407  ALA A C   
3020  O O   . ALA A 409  ? 0.2168 0.2425 0.3760 -0.0341 0.0100  0.1051  407  ALA A O   
3021  C CB  . ALA A 409  ? 0.2148 0.2310 0.3730 -0.0339 0.0065  0.1070  407  ALA A CB  
3022  N N   . LYS A 410  ? 0.1794 0.2041 0.3242 -0.0300 0.0148  0.1035  408  LYS A N   
3023  C CA  . LYS A 410  ? 0.1756 0.2079 0.3173 -0.0286 0.0185  0.1047  408  LYS A CA  
3024  C C   . LYS A 410  ? 0.2005 0.2309 0.3439 -0.0291 0.0178  0.1006  408  LYS A C   
3025  O O   . LYS A 410  ? 0.2017 0.2379 0.3486 -0.0297 0.0185  0.1022  408  LYS A O   
3026  C CB  . LYS A 410  ? 0.1983 0.2331 0.3304 -0.0255 0.0226  0.1046  408  LYS A CB  
3027  C CG  . LYS A 410  ? 0.2021 0.2451 0.3305 -0.0234 0.0267  0.1055  408  LYS A CG  
3028  C CD  . LYS A 410  ? 0.2298 0.2745 0.3488 -0.0201 0.0303  0.1046  408  LYS A CD  
3029  C CE  . LYS A 410  ? 0.2320 0.2801 0.3489 -0.0196 0.0310  0.1085  408  LYS A CE  
3030  N NZ  . LYS A 410  ? 0.2417 0.3006 0.3608 -0.0194 0.0329  0.1136  408  LYS A NZ  
3031  N N   . LEU A 411  ? 0.1472 0.1698 0.2884 -0.0289 0.0163  0.0953  409  LEU A N   
3032  C CA  . LEU A 411  ? 0.1499 0.1710 0.2924 -0.0294 0.0155  0.0912  409  LEU A CA  
3033  C C   . LEU A 411  ? 0.1672 0.1879 0.3194 -0.0324 0.0117  0.0913  409  LEU A C   
3034  O O   . LEU A 411  ? 0.1747 0.1989 0.3298 -0.0330 0.0118  0.0907  409  LEU A O   
3035  C CB  . LEU A 411  ? 0.1535 0.1668 0.2890 -0.0275 0.0141  0.0838  409  LEU A CB  
3036  C CG  . LEU A 411  ? 0.1595 0.1733 0.2837 -0.0237 0.0174  0.0812  409  LEU A CG  
3037  C CD1 . LEU A 411  ? 0.1813 0.1874 0.3001 -0.0225 0.0157  0.0754  409  LEU A CD1 
3038  C CD2 . LEU A 411  ? 0.1673 0.1855 0.2880 -0.0219 0.0191  0.0790  409  LEU A CD2 
3039  N N   . LEU A 412  ? 0.2015 0.2181 0.3591 -0.0341 0.0081  0.0918  410  LEU A N   
3040  C CA  . LEU A 412  ? 0.1985 0.2144 0.3656 -0.0368 0.0041  0.0915  410  LEU A CA  
3041  C C   . LEU A 412  ? 0.1802 0.2043 0.3519 -0.0378 0.0051  0.0969  410  LEU A C   
3042  O O   . LEU A 412  ? 0.2438 0.2687 0.4225 -0.0398 0.0025  0.0964  410  LEU A O   
3043  C CB  . LEU A 412  ? 0.2181 0.2276 0.3901 -0.0382 0.0000  0.0908  410  LEU A CB  
3044  C CG  . LEU A 412  ? 0.2214 0.2224 0.3914 -0.0377 -0.0023 0.0842  410  LEU A CG  
3045  C CD1 . LEU A 412  ? 0.2923 0.2877 0.4669 -0.0384 -0.0061 0.0837  410  LEU A CD1 
3046  C CD2 . LEU A 412  ? 0.2112 0.2106 0.3845 -0.0388 -0.0046 0.0791  410  LEU A CD2 
3047  N N   . ALA A 413  ? 0.1695 0.2001 0.3374 -0.0364 0.0088  0.1018  411  ALA A N   
3048  C CA  . ALA A 413  ? 0.1893 0.2288 0.3608 -0.0370 0.0102  0.1068  411  ALA A CA  
3049  C C   . ALA A 413  ? 0.1928 0.2378 0.3618 -0.0357 0.0131  0.1056  411  ALA A C   
3050  O O   . ALA A 413  ? 0.2443 0.2971 0.4162 -0.0360 0.0144  0.1093  411  ALA A O   
3051  C CB  . ALA A 413  ? 0.2362 0.2816 0.4048 -0.0359 0.0129  0.1124  411  ALA A CB  
3052  N N   . ALA A 414  ? 0.1834 0.2248 0.3472 -0.0343 0.0141  0.1007  412  ALA A N   
3053  C CA  . ALA A 414  ? 0.2020 0.2487 0.3630 -0.0327 0.0170  0.0997  412  ALA A CA  
3054  C C   . ALA A 414  ? 0.1854 0.2274 0.3472 -0.0332 0.0147  0.0939  412  ALA A C   
3055  O O   . ALA A 414  ? 0.1764 0.2196 0.3313 -0.0303 0.0163  0.0901  412  ALA A O   
3056  C CB  . ALA A 414  ? 0.1985 0.2473 0.3502 -0.0293 0.0215  0.0997  412  ALA A CB  
3057  N N   . THR A 415  ? 0.1795 0.2161 0.3481 -0.0361 0.0103  0.0920  413  THR A N   
3058  C CA  . THR A 415  ? 0.1857 0.2181 0.3528 -0.0357 0.0074  0.0850  413  THR A CA  
3059  C C   . THR A 415  ? 0.1757 0.2142 0.3447 -0.0355 0.0078  0.0846  413  THR A C   
3060  O O   . THR A 415  ? 0.1948 0.2311 0.3609 -0.0346 0.0060  0.0790  413  THR A O   
3061  C CB  . THR A 415  ? 0.1807 0.2066 0.3552 -0.0387 0.0024  0.0826  413  THR A CB  
3062  O OG1 . THR A 415  ? 0.2304 0.2596 0.4150 -0.0416 0.0004  0.0870  413  THR A OG1 
3063  C CG2 . THR A 415  ? 0.2060 0.2253 0.3783 -0.0385 0.0018  0.0823  413  THR A CG2 
3064  N N   . ASP A 416  ? 0.2168 0.2633 0.3907 -0.0363 0.0099  0.0905  414  ASP A N   
3065  C CA  . ASP A 416  ? 0.1904 0.2429 0.3652 -0.0356 0.0106  0.0899  414  ASP A CA  
3066  C C   . ASP A 416  ? 0.2165 0.2710 0.3811 -0.0312 0.0140  0.0872  414  ASP A C   
3067  O O   . ASP A 416  ? 0.2811 0.3377 0.4446 -0.0301 0.0135  0.0844  414  ASP A O   
3068  C CB  . ASP A 416  ? 0.2502 0.3114 0.4338 -0.0376 0.0117  0.0967  414  ASP A CB  
3069  C CG  . ASP A 416  ? 0.3423 0.4080 0.5218 -0.0358 0.0154  0.1015  414  ASP A CG  
3070  O OD1 . ASP A 416  ? 0.3023 0.3637 0.4766 -0.0348 0.0163  0.1013  414  ASP A OD1 
3071  O OD2 . ASP A 416  ? 0.4641 0.5380 0.6456 -0.0353 0.0173  0.1053  414  ASP A OD2 
3072  N N   . VAL A 417  ? 0.1817 0.2353 0.3390 -0.0288 0.0170  0.0878  415  VAL A N   
3073  C CA  . VAL A 417  ? 0.2146 0.2701 0.3631 -0.0246 0.0200  0.0854  415  VAL A CA  
3074  C C   . VAL A 417  ? 0.2103 0.2580 0.3496 -0.0225 0.0196  0.0802  415  VAL A C   
3075  O O   . VAL A 417  ? 0.2048 0.2528 0.3373 -0.0193 0.0211  0.0772  415  VAL A O   
3076  C CB  . VAL A 417  ? 0.2368 0.2999 0.3838 -0.0227 0.0243  0.0902  415  VAL A CB  
3077  C CG1 . VAL A 417  ? 0.3096 0.3816 0.4657 -0.0247 0.0249  0.0955  415  VAL A CG1 
3078  C CG2 . VAL A 417  ? 0.2180 0.2787 0.3625 -0.0229 0.0255  0.0925  415  VAL A CG2 
3079  N N   . VAL A 418  ? 0.1609 0.2020 0.3001 -0.0241 0.0176  0.0790  416  VAL A N   
3080  C CA  . VAL A 418  ? 0.1747 0.2087 0.3060 -0.0224 0.0169  0.0738  416  VAL A CA  
3081  C C   . VAL A 418  ? 0.1716 0.1995 0.3066 -0.0249 0.0127  0.0706  416  VAL A C   
3082  O O   . VAL A 418  ? 0.1614 0.1894 0.3050 -0.0279 0.0104  0.0728  416  VAL A O   
3083  C CB  . VAL A 418  ? 0.1301 0.1622 0.2554 -0.0206 0.0194  0.0751  416  VAL A CB  
3084  C CG1 . VAL A 418  ? 0.1683 0.2068 0.2894 -0.0176 0.0235  0.0773  416  VAL A CG1 
3085  C CG2 . VAL A 418  ? 0.1742 0.2053 0.3052 -0.0232 0.0187  0.0793  416  VAL A CG2 
3086  N N   . PHE A 419  ? 0.1298 0.1524 0.2584 -0.0235 0.0115  0.0651  417  PHE A N   
3087  C CA  . PHE A 419  ? 0.1591 0.1761 0.2898 -0.0252 0.0076  0.0609  417  PHE A CA  
3088  C C   . PHE A 419  ? 0.1286 0.1399 0.2550 -0.0245 0.0078  0.0597  417  PHE A C   
3089  O O   . PHE A 419  ? 0.1505 0.1594 0.2685 -0.0221 0.0089  0.0565  417  PHE A O   
3090  C CB  . PHE A 419  ? 0.1506 0.1671 0.2773 -0.0242 0.0060  0.0555  417  PHE A CB  
3091  C CG  . PHE A 419  ? 0.1533 0.1651 0.2811 -0.0254 0.0022  0.0503  417  PHE A CG  
3092  C CD1 . PHE A 419  ? 0.1851 0.1960 0.3218 -0.0283 -0.0012 0.0501  417  PHE A CD1 
3093  C CD2 . PHE A 419  ? 0.1563 0.1650 0.2765 -0.0237 0.0019  0.0455  417  PHE A CD2 
3094  C CE1 . PHE A 419  ? 0.1689 0.1759 0.3069 -0.0291 -0.0049 0.0447  417  PHE A CE1 
3095  C CE2 . PHE A 419  ? 0.1389 0.1443 0.2600 -0.0246 -0.0015 0.0404  417  PHE A CE2 
3096  C CZ  . PHE A 419  ? 0.1567 0.1613 0.2866 -0.0271 -0.0049 0.0397  417  PHE A CZ  
3097  N N   . PRO A 420  ? 0.1356 0.1446 0.2677 -0.0265 0.0067  0.0624  418  PRO A N   
3098  C CA  . PRO A 420  ? 0.1321 0.1358 0.2604 -0.0257 0.0068  0.0615  418  PRO A CA  
3099  C C   . PRO A 420  ? 0.1348 0.1330 0.2612 -0.0255 0.0037  0.0549  418  PRO A C   
3100  O O   . PRO A 420  ? 0.1697 0.1668 0.3016 -0.0273 0.0002  0.0520  418  PRO A O   
3101  C CB  . PRO A 420  ? 0.1333 0.1368 0.2701 -0.0282 0.0059  0.0668  418  PRO A CB  
3102  C CG  . PRO A 420  ? 0.1619 0.1720 0.3050 -0.0298 0.0067  0.0716  418  PRO A CG  
3103  C CD  . PRO A 420  ? 0.1454 0.1571 0.2879 -0.0295 0.0054  0.0672  418  PRO A CD  
3104  N N   . GLN A 421  ? 0.1411 0.1361 0.2595 -0.0234 0.0050  0.0524  419  GLN A N   
3105  C CA  . GLN A 421  ? 0.1476 0.1381 0.2629 -0.0228 0.0026  0.0462  419  GLN A CA  
3106  C C   . GLN A 421  ? 0.1362 0.1222 0.2497 -0.0222 0.0029  0.0467  419  GLN A C   
3107  O O   . GLN A 421  ? 0.1525 0.1385 0.2592 -0.0203 0.0058  0.0480  419  GLN A O   
3108  C CB  . GLN A 421  ? 0.1289 0.1208 0.2357 -0.0206 0.0039  0.0426  419  GLN A CB  
3109  C CG  . GLN A 421  ? 0.1466 0.1434 0.2550 -0.0210 0.0038  0.0428  419  GLN A CG  
3110  C CD  . GLN A 421  ? 0.1293 0.1278 0.2294 -0.0187 0.0056  0.0410  419  GLN A CD  
3111  O OE1 . GLN A 421  ? 0.1652 0.1642 0.2602 -0.0168 0.0086  0.0432  419  GLN A OE1 
3112  N NE2 . GLN A 421  ? 0.1489 0.1486 0.2479 -0.0188 0.0036  0.0371  419  GLN A NE2 
3113  N N   . PHE A 422  ? 0.1475 0.1296 0.2675 -0.0238 -0.0003 0.0454  420  PHE A N   
3114  C CA  . PHE A 422  ? 0.1507 0.1286 0.2710 -0.0236 -0.0005 0.0468  420  PHE A CA  
3115  C C   . PHE A 422  ? 0.1614 0.1354 0.2766 -0.0219 -0.0018 0.0404  420  PHE A C   
3116  O O   . PHE A 422  ? 0.1649 0.1360 0.2845 -0.0227 -0.0053 0.0360  420  PHE A O   
3117  C CB  . PHE A 422  ? 0.1652 0.1412 0.2965 -0.0263 -0.0033 0.0500  420  PHE A CB  
3118  C CG  . PHE A 422  ? 0.1762 0.1570 0.3126 -0.0280 -0.0018 0.0569  420  PHE A CG  
3119  C CD1 . PHE A 422  ? 0.2079 0.1919 0.3406 -0.0271 0.0020  0.0626  420  PHE A CD1 
3120  C CD2 . PHE A 422  ? 0.1942 0.1769 0.3390 -0.0304 -0.0041 0.0576  420  PHE A CD2 
3121  C CE1 . PHE A 422  ? 0.1630 0.1525 0.3003 -0.0286 0.0036  0.0691  420  PHE A CE1 
3122  C CE2 . PHE A 422  ? 0.1774 0.1652 0.3271 -0.0320 -0.0026 0.0642  420  PHE A CE2 
3123  C CZ  . PHE A 422  ? 0.2063 0.1978 0.3521 -0.0311 0.0014  0.0700  420  PHE A CZ  
3124  N N   . ALA A 423  ? 0.1565 0.1306 0.2625 -0.0197 0.0011  0.0399  421  ALA A N   
3125  C CA  . ALA A 423  ? 0.1360 0.1074 0.2362 -0.0180 0.0004  0.0344  421  ALA A CA  
3126  C C   . ALA A 423  ? 0.1582 0.1252 0.2599 -0.0178 -0.0004 0.0350  421  ALA A C   
3127  O O   . ALA A 423  ? 0.1922 0.1591 0.2906 -0.0169 0.0021  0.0391  421  ALA A O   
3128  C CB  . ALA A 423  ? 0.1468 0.1204 0.2372 -0.0159 0.0035  0.0339  421  ALA A CB  
3129  N N   . THR A 424  ? 0.1531 0.1166 0.2597 -0.0183 -0.0039 0.0309  422  THR A N   
3130  C CA  . THR A 424  ? 0.1682 0.1272 0.2766 -0.0179 -0.0050 0.0311  422  THR A CA  
3131  C C   . THR A 424  ? 0.1755 0.1315 0.2876 -0.0176 -0.0089 0.0243  422  THR A C   
3132  O O   . THR A 424  ? 0.1840 0.1408 0.3009 -0.0187 -0.0116 0.0209  422  THR A O   
3133  C CB  . THR A 424  ? 0.1842 0.1420 0.3002 -0.0197 -0.0055 0.0378  422  THR A CB  
3134  O OG1 . THR A 424  ? 0.1833 0.1368 0.3003 -0.0190 -0.0064 0.0382  422  THR A OG1 
3135  C CG2 . THR A 424  ? 0.2230 0.1801 0.3495 -0.0221 -0.0090 0.0377  422  THR A CG2 
3136  N N   . HIS A 425  ? 0.1876 0.1405 0.2971 -0.0161 -0.0093 0.0221  423  HIS A N   
3137  C CA  . HIS A 425  ? 0.1839 0.1338 0.2978 -0.0156 -0.0131 0.0159  423  HIS A CA  
3138  C C   . HIS A 425  ? 0.2031 0.1480 0.3260 -0.0165 -0.0158 0.0183  423  HIS A C   
3139  O O   . HIS A 425  ? 0.2314 0.1731 0.3588 -0.0159 -0.0192 0.0132  423  HIS A O   
3140  C CB  . HIS A 425  ? 0.1773 0.1275 0.2829 -0.0132 -0.0120 0.0112  423  HIS A CB  
3141  C CG  . HIS A 425  ? 0.1841 0.1391 0.2817 -0.0124 -0.0099 0.0087  423  HIS A CG  
3142  N ND1 . HIS A 425  ? 0.2066 0.1632 0.2949 -0.0109 -0.0067 0.0095  423  HIS A ND1 
3143  C CD2 . HIS A 425  ? 0.2129 0.1715 0.3107 -0.0130 -0.0107 0.0059  423  HIS A CD2 
3144  C CE1 . HIS A 425  ? 0.1998 0.1606 0.2832 -0.0108 -0.0057 0.0074  423  HIS A CE1 
3145  N NE2 . HIS A 425  ? 0.1908 0.1531 0.2796 -0.0120 -0.0080 0.0053  423  HIS A NE2 
3146  N N   . ASN A 426  ? 0.1806 0.1250 0.3063 -0.0179 -0.0144 0.0259  424  ASN A N   
3147  C CA  . ASN A 426  ? 0.2196 0.1597 0.3536 -0.0189 -0.0167 0.0297  424  ASN A CA  
3148  C C   . ASN A 426  ? 0.2464 0.1851 0.3923 -0.0215 -0.0205 0.0307  424  ASN A C   
3149  O O   . ASN A 426  ? 0.2137 0.1554 0.3618 -0.0234 -0.0193 0.0355  424  ASN A O   
3150  C CB  . ASN A 426  ? 0.2183 0.1599 0.3489 -0.0192 -0.0132 0.0379  424  ASN A CB  
3151  C CG  . ASN A 426  ? 0.2348 0.1725 0.3726 -0.0201 -0.0152 0.0427  424  ASN A CG  
3152  O OD1 . ASN A 426  ? 0.2603 0.1974 0.4065 -0.0213 -0.0187 0.0427  424  ASN A OD1 
3153  N ND2 . ASN A 426  ? 0.2321 0.1702 0.3642 -0.0188 -0.0128 0.0460  424  ASN A ND2 
3154  N N   . ALA A 427  ? 0.2115 0.1455 0.3654 -0.0216 -0.0251 0.0262  425  ALA A N   
3155  C CA  . ALA A 427  ? 0.2117 0.1455 0.3757 -0.0234 -0.0291 0.0257  425  ALA A CA  
3156  C C   . ALA A 427  ? 0.2252 0.1610 0.3936 -0.0251 -0.0288 0.0341  425  ALA A C   
3157  O O   . ALA A 427  ? 0.2383 0.1760 0.4131 -0.0271 -0.0305 0.0360  425  ALA A O   
3158  C CB  . ALA A 427  ? 0.2454 0.1755 0.4150 -0.0221 -0.0339 0.0181  425  ALA A CB  
3159  N N   . GLN A 428  ? 0.2304 0.1663 0.3956 -0.0244 -0.0269 0.0392  426  GLN A N   
3160  C CA  . GLN A 428  ? 0.2393 0.1782 0.4082 -0.0260 -0.0264 0.0475  426  GLN A CA  
3161  C C   . GLN A 428  ? 0.2321 0.1764 0.3975 -0.0273 -0.0225 0.0528  426  GLN A C   
3162  O O   . GLN A 428  ? 0.2317 0.1791 0.4028 -0.0293 -0.0233 0.0569  426  GLN A O   
3163  C CB  . GLN A 428  ? 0.2668 0.2052 0.4325 -0.0248 -0.0252 0.0513  426  GLN A CB  
3164  C CG  . GLN A 428  ? 0.2987 0.2395 0.4705 -0.0264 -0.0262 0.0587  426  GLN A CG  
3165  C CD  . GLN A 428  ? 0.3367 0.2838 0.5055 -0.0277 -0.0224 0.0661  426  GLN A CD  
3166  O OE1 . GLN A 428  ? 0.3044 0.2539 0.4643 -0.0268 -0.0181 0.0672  426  GLN A OE1 
3167  N NE2 . GLN A 428  ? 0.3143 0.2642 0.4907 -0.0298 -0.0240 0.0711  426  GLN A NE2 
3168  N N   . THR A 429  ? 0.2197 0.1654 0.3758 -0.0262 -0.0184 0.0526  427  THR A N   
3169  C CA  . THR A 429  ? 0.2201 0.1711 0.3726 -0.0270 -0.0147 0.0567  427  THR A CA  
3170  C C   . THR A 429  ? 0.2329 0.1850 0.3910 -0.0287 -0.0165 0.0544  427  THR A C   
3171  O O   . THR A 429  ? 0.2078 0.1645 0.3690 -0.0304 -0.0158 0.0592  427  THR A O   
3172  C CB  . THR A 429  ? 0.2194 0.1708 0.3617 -0.0252 -0.0106 0.0554  427  THR A CB  
3173  O OG1 . THR A 429  ? 0.2289 0.1789 0.3662 -0.0235 -0.0093 0.0568  427  THR A OG1 
3174  C CG2 . THR A 429  ? 0.2470 0.2044 0.3854 -0.0256 -0.0066 0.0601  427  THR A CG2 
3175  N N   . LEU A 430  ? 0.2079 0.1563 0.3674 -0.0284 -0.0191 0.0468  428  LEU A N   
3176  C CA  . LEU A 430  ? 0.2106 0.1600 0.3755 -0.0300 -0.0214 0.0436  428  LEU A CA  
3177  C C   . LEU A 430  ? 0.2313 0.1815 0.4059 -0.0318 -0.0247 0.0463  428  LEU A C   
3178  O O   . LEU A 430  ? 0.2394 0.1936 0.4173 -0.0336 -0.0244 0.0493  428  LEU A O   
3179  C CB  . LEU A 430  ? 0.2079 0.1543 0.3716 -0.0285 -0.0241 0.0339  428  LEU A CB  
3180  C CG  . LEU A 430  ? 0.2707 0.2197 0.4352 -0.0288 -0.0260 0.0279  428  LEU A CG  
3181  C CD1 . LEU A 430  ? 0.3001 0.2482 0.4590 -0.0262 -0.0271 0.0188  428  LEU A CD1 
3182  C CD2 . LEU A 430  ? 0.2617 0.2088 0.4394 -0.0315 -0.0307 0.0279  428  LEU A CD2 
3183  N N   . ALA A 431  ? 0.2259 0.1726 0.4057 -0.0314 -0.0281 0.0454  429  ALA A N   
3184  C CA  . ALA A 431  ? 0.2408 0.1878 0.4307 -0.0331 -0.0318 0.0479  429  ALA A CA  
3185  C C   . ALA A 431  ? 0.2530 0.2053 0.4438 -0.0347 -0.0293 0.0571  429  ALA A C   
3186  O O   . ALA A 431  ? 0.2457 0.2006 0.4432 -0.0366 -0.0308 0.0596  429  ALA A O   
3187  C CB  . ALA A 431  ? 0.2326 0.1751 0.4275 -0.0322 -0.0356 0.0459  429  ALA A CB  
3188  N N   . ALA A 432  ? 0.2533 0.2078 0.4375 -0.0338 -0.0254 0.0621  430  ALA A N   
3189  C CA  . ALA A 432  ? 0.2622 0.2227 0.4468 -0.0350 -0.0229 0.0706  430  ALA A CA  
3190  C C   . ALA A 432  ? 0.2807 0.2463 0.4643 -0.0361 -0.0206 0.0722  430  ALA A C   
3191  O O   . ALA A 432  ? 0.2594 0.2294 0.4485 -0.0379 -0.0209 0.0772  430  ALA A O   
3192  C CB  . ALA A 432  ? 0.2682 0.2304 0.4446 -0.0335 -0.0190 0.0745  430  ALA A CB  
3193  N N   . ILE A 433  ? 0.2532 0.2185 0.4304 -0.0352 -0.0184 0.0680  431  ILE A N   
3194  C CA  . ILE A 433  ? 0.2540 0.2243 0.4297 -0.0360 -0.0160 0.0693  431  ILE A CA  
3195  C C   . ILE A 433  ? 0.2450 0.2146 0.4290 -0.0378 -0.0198 0.0660  431  ILE A C   
3196  O O   . ILE A 433  ? 0.2521 0.2267 0.4395 -0.0393 -0.0192 0.0695  431  ILE A O   
3197  C CB  . ILE A 433  ? 0.2624 0.2325 0.4288 -0.0342 -0.0125 0.0660  431  ILE A CB  
3198  C CG1 . ILE A 433  ? 0.2398 0.2117 0.3982 -0.0324 -0.0085 0.0701  431  ILE A CG1 
3199  C CG2 . ILE A 433  ? 0.2530 0.2275 0.4187 -0.0350 -0.0107 0.0660  431  ILE A CG2 
3200  C CD1 . ILE A 433  ? 0.2439 0.2147 0.3932 -0.0305 -0.0054 0.0669  431  ILE A CD1 
3201  N N   . TYR A 434  ? 0.2476 0.2116 0.4351 -0.0376 -0.0239 0.0591  432  TYR A N   
3202  C CA  . TYR A 434  ? 0.2452 0.2084 0.4409 -0.0392 -0.0281 0.0554  432  TYR A CA  
3203  C C   . TYR A 434  ? 0.2511 0.2166 0.4555 -0.0411 -0.0302 0.0610  432  TYR A C   
3204  O O   . TYR A 434  ? 0.2825 0.2513 0.4916 -0.0428 -0.0311 0.0622  432  TYR A O   
3205  C CB  . TYR A 434  ? 0.2730 0.2301 0.4710 -0.0382 -0.0323 0.0470  432  TYR A CB  
3206  C CG  . TYR A 434  ? 0.2670 0.2228 0.4742 -0.0394 -0.0375 0.0427  432  TYR A CG  
3207  C CD1 . TYR A 434  ? 0.2604 0.2186 0.4686 -0.0404 -0.0382 0.0391  432  TYR A CD1 
3208  C CD2 . TYR A 434  ? 0.2837 0.2360 0.4989 -0.0395 -0.0418 0.0421  432  TYR A CD2 
3209  C CE1 . TYR A 434  ? 0.3043 0.2616 0.5208 -0.0414 -0.0430 0.0348  432  TYR A CE1 
3210  C CE2 . TYR A 434  ? 0.3194 0.2705 0.5431 -0.0403 -0.0467 0.0379  432  TYR A CE2 
3211  C CZ  . TYR A 434  ? 0.3799 0.3334 0.6040 -0.0413 -0.0472 0.0342  432  TYR A CZ  
3212  O OH  . TYR A 434  ? 0.4193 0.3718 0.6518 -0.0420 -0.0522 0.0297  432  TYR A OH  
3213  N N   . HIS A 435  ? 0.2596 0.2238 0.4664 -0.0409 -0.0310 0.0650  433  HIS A N   
3214  C CA  . HIS A 435  ? 0.2646 0.2312 0.4801 -0.0428 -0.0331 0.0708  433  HIS A CA  
3215  C C   . HIS A 435  ? 0.2869 0.2611 0.4998 -0.0436 -0.0288 0.0789  433  HIS A C   
3216  O O   . HIS A 435  ? 0.2840 0.2619 0.5035 -0.0455 -0.0300 0.0830  433  HIS A O   
3217  C CB  . HIS A 435  ? 0.2882 0.2511 0.5084 -0.0424 -0.0360 0.0723  433  HIS A CB  
3218  C CG  . HIS A 435  ? 0.3233 0.2796 0.5491 -0.0418 -0.0412 0.0646  433  HIS A CG  
3219  N ND1 . HIS A 435  ? 0.2973 0.2522 0.5332 -0.0432 -0.0460 0.0628  433  HIS A ND1 
3220  C CD2 . HIS A 435  ? 0.2988 0.2499 0.5213 -0.0397 -0.0423 0.0579  433  HIS A CD2 
3221  C CE1 . HIS A 435  ? 0.3254 0.2747 0.5642 -0.0418 -0.0499 0.0552  433  HIS A CE1 
3222  N NE2 . HIS A 435  ? 0.3177 0.2648 0.5484 -0.0397 -0.0477 0.0521  433  HIS A NE2 
3223  N N   . MET A 436  ? 0.2708 0.2476 0.4741 -0.0421 -0.0240 0.0809  434  MET A N   
3224  C CA  . MET A 436  ? 0.2747 0.2594 0.4748 -0.0424 -0.0197 0.0877  434  MET A CA  
3225  C C   . MET A 436  ? 0.3054 0.2941 0.5068 -0.0435 -0.0189 0.0870  434  MET A C   
3226  O O   . MET A 436  ? 0.2867 0.2818 0.4910 -0.0447 -0.0176 0.0926  434  MET A O   
3227  C CB  . MET A 436  ? 0.2740 0.2602 0.4633 -0.0402 -0.0149 0.0886  434  MET A CB  
3228  C CG  . MET A 436  ? 0.3000 0.2948 0.4852 -0.0400 -0.0103 0.0948  434  MET A CG  
3229  S SD  . MET A 436  ? 0.3251 0.3213 0.4974 -0.0371 -0.0049 0.0944  434  MET A SD  
3230  C CE  . MET A 436  ? 0.3162 0.3096 0.4881 -0.0364 -0.0060 0.0969  434  MET A CE  
3231  N N   . ALA A 437  ? 0.2538 0.2393 0.4534 -0.0431 -0.0197 0.0802  435  ALA A N   
3232  C CA  . ALA A 437  ? 0.2967 0.2861 0.4972 -0.0440 -0.0190 0.0792  435  ALA A CA  
3233  C C   . ALA A 437  ? 0.3403 0.3301 0.5512 -0.0464 -0.0232 0.0796  435  ALA A C   
3234  O O   . ALA A 437  ? 0.3133 0.3080 0.5261 -0.0474 -0.0225 0.0808  435  ALA A O   
3235  C CB  . ALA A 437  ? 0.3022 0.2884 0.4981 -0.0431 -0.0190 0.0718  435  ALA A CB  
3236  N N   . GLY A 438  ? 0.3446 0.3297 0.5625 -0.0471 -0.0276 0.0786  436  GLY A N   
3237  C CA  . GLY A 438  ? 0.3662 0.3516 0.5944 -0.0492 -0.0317 0.0796  436  GLY A CA  
3238  C C   . GLY A 438  ? 0.3994 0.3818 0.6312 -0.0498 -0.0354 0.0720  436  GLY A C   
3239  O O   . GLY A 438  ? 0.3738 0.3533 0.6007 -0.0485 -0.0353 0.0653  436  GLY A O   
3240  N N   . LYS A 439  ? 0.4160 0.3998 0.6566 -0.0517 -0.0386 0.0732  437  LYS A N   
3241  C CA  . LYS A 439  ? 0.4532 0.4339 0.6994 -0.0524 -0.0432 0.0661  437  LYS A CA  
3242  C C   . LYS A 439  ? 0.4110 0.3957 0.6542 -0.0528 -0.0418 0.0631  437  LYS A C   
3243  O O   . LYS A 439  ? 0.4097 0.3919 0.6536 -0.0526 -0.0447 0.0553  437  LYS A O   
3244  C CB  . LYS A 439  ? 0.4480 0.4282 0.7055 -0.0544 -0.0476 0.0688  437  LYS A CB  
3245  N N   . ASP A 440  ? 0.3929 0.3845 0.6330 -0.0533 -0.0375 0.0688  438  ASP A N   
3246  C CA  . ASP A 440  ? 0.4212 0.4174 0.6594 -0.0538 -0.0363 0.0665  438  ASP A CA  
3247  C C   . ASP A 440  ? 0.3995 0.3952 0.6283 -0.0519 -0.0334 0.0624  438  ASP A C   
3248  O O   . ASP A 440  ? 0.3904 0.3873 0.6123 -0.0505 -0.0290 0.0660  438  ASP A O   
3249  C CB  . ASP A 440  ? 0.4248 0.4288 0.6637 -0.0548 -0.0330 0.0741  438  ASP A CB  
3250  C CG  . ASP A 440  ? 0.5109 0.5160 0.7596 -0.0568 -0.0361 0.0784  438  ASP A CG  
3251  O OD1 . ASP A 440  ? 0.5216 0.5222 0.7773 -0.0578 -0.0412 0.0741  438  ASP A OD1 
3252  O OD2 . ASP A 440  ? 0.5038 0.5145 0.7532 -0.0574 -0.0334 0.0860  438  ASP A OD2 
3253  N N   . PHE A 441  ? 0.3393 0.3337 0.5679 -0.0519 -0.0358 0.0549  439  PHE A N   
3254  C CA  . PHE A 441  ? 0.3110 0.3056 0.5314 -0.0504 -0.0333 0.0510  439  PHE A CA  
3255  C C   . PHE A 441  ? 0.3570 0.3554 0.5781 -0.0511 -0.0347 0.0461  439  PHE A C   
3256  O O   . PHE A 441  ? 0.3345 0.3326 0.5620 -0.0523 -0.0391 0.0422  439  PHE A O   
3257  C CB  . PHE A 441  ? 0.3242 0.3118 0.5417 -0.0489 -0.0350 0.0452  439  PHE A CB  
3258  C CG  . PHE A 441  ? 0.2543 0.2427 0.4606 -0.0463 -0.0319 0.0415  439  PHE A CG  
3259  C CD1 . PHE A 441  ? 0.3040 0.2935 0.5017 -0.0445 -0.0267 0.0460  439  PHE A CD1 
3260  C CD2 . PHE A 441  ? 0.2694 0.2583 0.4710 -0.0447 -0.0338 0.0332  439  PHE A CD2 
3261  C CE1 . PHE A 441  ? 0.2711 0.2615 0.4565 -0.0412 -0.0238 0.0424  439  PHE A CE1 
3262  C CE2 . PHE A 441  ? 0.2952 0.2856 0.4842 -0.0415 -0.0306 0.0300  439  PHE A CE2 
3263  C CZ  . PHE A 441  ? 0.2348 0.2256 0.4160 -0.0399 -0.0257 0.0348  439  PHE A CZ  
3264  N N   . HIS A 442  ? 0.2760 0.2782 0.4862 -0.0486 -0.0306 0.0455  440  HIS A N   
3265  C CA  . HIS A 442  ? 0.2958 0.3017 0.5011 -0.0473 -0.0313 0.0399  440  HIS A CA  
3266  C C   . HIS A 442  ? 0.2919 0.2980 0.4835 -0.0436 -0.0275 0.0375  440  HIS A C   
3267  O O   . HIS A 442  ? 0.2496 0.2553 0.4359 -0.0423 -0.0235 0.0419  440  HIS A O   
3268  C CB  . HIS A 442  ? 0.3318 0.3449 0.5407 -0.0486 -0.0303 0.0440  440  HIS A CB  
3269  C CG  . HIS A 442  ? 0.2858 0.3031 0.4907 -0.0477 -0.0248 0.0514  440  HIS A CG  
3270  N ND1 . HIS A 442  ? 0.3235 0.3444 0.5179 -0.0448 -0.0209 0.0512  440  HIS A ND1 
3271  C CD2 . HIS A 442  ? 0.2666 0.2854 0.4765 -0.0493 -0.0227 0.0592  440  HIS A CD2 
3272  C CE1 . HIS A 442  ? 0.2811 0.3055 0.4745 -0.0444 -0.0167 0.0579  440  HIS A CE1 
3273  N NE2 . HIS A 442  ? 0.3187 0.3424 0.5211 -0.0471 -0.0176 0.0630  440  HIS A NE2 
3274  N N   . VAL A 443  ? 0.2892 0.2962 0.4753 -0.0420 -0.0291 0.0305  441  VAL A N   
3275  C CA  . VAL A 443  ? 0.3246 0.3323 0.4983 -0.0388 -0.0258 0.0285  441  VAL A CA  
3276  C C   . VAL A 443  ? 0.2960 0.3086 0.4651 -0.0379 -0.0213 0.0342  441  VAL A C   
3277  O O   . VAL A 443  ? 0.3025 0.3201 0.4753 -0.0389 -0.0215 0.0361  441  VAL A O   
3278  C CB  . VAL A 443  ? 0.3260 0.3352 0.4952 -0.0376 -0.0284 0.0207  441  VAL A CB  
3279  C CG1 . VAL A 443  ? 0.3285 0.3401 0.4855 -0.0348 -0.0248 0.0202  441  VAL A CG1 
3280  C CG2 . VAL A 443  ? 0.3365 0.3405 0.5076 -0.0375 -0.0319 0.0145  441  VAL A CG2 
3281  N N   . GLY A 444  ? 0.2528 0.2640 0.4144 -0.0358 -0.0172 0.0369  442  GLY A N   
3282  C CA  . GLY A 444  ? 0.1882 0.2037 0.3462 -0.0347 -0.0129 0.0424  442  GLY A CA  
3283  C C   . GLY A 444  ? 0.1756 0.1907 0.3372 -0.0355 -0.0104 0.0490  442  GLY A C   
3284  O O   . GLY A 444  ? 0.1961 0.2144 0.3534 -0.0340 -0.0064 0.0531  442  GLY A O   
3285  N N   . LYS A 445  ? 0.1949 0.2064 0.3643 -0.0378 -0.0128 0.0502  443  LYS A N   
3286  C CA  . LYS A 445  ? 0.1891 0.2009 0.3621 -0.0388 -0.0105 0.0572  443  LYS A CA  
3287  C C   . LYS A 445  ? 0.1779 0.1863 0.3428 -0.0365 -0.0077 0.0576  443  LYS A C   
3288  O O   . LYS A 445  ? 0.2007 0.2121 0.3615 -0.0351 -0.0037 0.0622  443  LYS A O   
3289  C CB  . LYS A 445  ? 0.2362 0.2455 0.4212 -0.0422 -0.0144 0.0591  443  LYS A CB  
3290  C CG  . LYS A 445  ? 0.2318 0.2431 0.4218 -0.0438 -0.0121 0.0675  443  LYS A CG  
3291  C CD  . LYS A 445  ? 0.2821 0.2925 0.4843 -0.0472 -0.0161 0.0701  443  LYS A CD  
3292  C CE  . LYS A 445  ? 0.3366 0.3515 0.5399 -0.0472 -0.0136 0.0779  443  LYS A CE  
3293  N NZ  . LYS A 445  ? 0.3936 0.4070 0.6059 -0.0492 -0.0176 0.0797  443  LYS A NZ  
3294  N N   . TYR A 446  ? 0.1840 0.1864 0.3467 -0.0359 -0.0100 0.0525  444  TYR A N   
3295  C CA  . TYR A 446  ? 0.1638 0.1627 0.3179 -0.0335 -0.0077 0.0515  444  TYR A CA  
3296  C C   . TYR A 446  ? 0.1866 0.1809 0.3382 -0.0327 -0.0108 0.0439  444  TYR A C   
3297  O O   . TYR A 446  ? 0.1816 0.1755 0.3384 -0.0340 -0.0146 0.0398  444  TYR A O   
3298  C CB  . TYR A 446  ? 0.1897 0.1864 0.3472 -0.0344 -0.0067 0.0570  444  TYR A CB  
3299  C CG  . TYR A 446  ? 0.2188 0.2106 0.3859 -0.0369 -0.0111 0.0563  444  TYR A CG  
3300  C CD1 . TYR A 446  ? 0.2966 0.2900 0.4749 -0.0401 -0.0134 0.0601  444  TYR A CD1 
3301  C CD2 . TYR A 446  ? 0.2666 0.2522 0.4320 -0.0360 -0.0131 0.0518  444  TYR A CD2 
3302  C CE1 . TYR A 446  ? 0.2994 0.2879 0.4874 -0.0424 -0.0178 0.0595  444  TYR A CE1 
3303  C CE2 . TYR A 446  ? 0.3339 0.3146 0.5088 -0.0380 -0.0175 0.0509  444  TYR A CE2 
3304  C CZ  . TYR A 446  ? 0.3480 0.3300 0.5343 -0.0412 -0.0199 0.0547  444  TYR A CZ  
3305  O OH  . TYR A 446  ? 0.4772 0.4546 0.6720 -0.0426 -0.0245 0.0534  444  TYR A OH  
3306  N N   . GLU A 447  ? 0.1594 0.1507 0.3029 -0.0305 -0.0092 0.0418  445  GLU A N   
3307  C CA  . GLU A 447  ? 0.1601 0.1476 0.3012 -0.0295 -0.0118 0.0348  445  GLU A CA  
3308  C C   . GLU A 447  ? 0.1698 0.1528 0.3067 -0.0282 -0.0105 0.0352  445  GLU A C   
3309  O O   . GLU A 447  ? 0.1729 0.1564 0.3069 -0.0275 -0.0072 0.0404  445  GLU A O   
3310  C CB  . GLU A 447  ? 0.1476 0.1379 0.2809 -0.0278 -0.0114 0.0300  445  GLU A CB  
3311  C CG  . GLU A 447  ? 0.1645 0.1563 0.2877 -0.0254 -0.0071 0.0319  445  GLU A CG  
3312  C CD  . GLU A 447  ? 0.1643 0.1591 0.2805 -0.0239 -0.0067 0.0282  445  GLU A CD  
3313  O OE1 . GLU A 447  ? 0.1918 0.1892 0.3107 -0.0247 -0.0093 0.0249  445  GLU A OE1 
3314  O OE2 . GLU A 447  ? 0.1634 0.1584 0.2716 -0.0219 -0.0038 0.0288  445  GLU A OE2 
3315  N N   . PHE A 448  ? 0.1854 0.1645 0.3221 -0.0276 -0.0132 0.0295  446  PHE A N   
3316  C CA  . PHE A 448  ? 0.1820 0.1575 0.3131 -0.0258 -0.0119 0.0284  446  PHE A CA  
3317  C C   . PHE A 448  ? 0.1495 0.1268 0.2704 -0.0234 -0.0104 0.0240  446  PHE A C   
3318  O O   . PHE A 448  ? 0.1737 0.1546 0.2927 -0.0233 -0.0109 0.0212  446  PHE A O   
3319  C CB  . PHE A 448  ? 0.1874 0.1576 0.3249 -0.0263 -0.0158 0.0250  446  PHE A CB  
3320  C CG  . PHE A 448  ? 0.1944 0.1622 0.3426 -0.0288 -0.0177 0.0299  446  PHE A CG  
3321  C CD1 . PHE A 448  ? 0.1980 0.1638 0.3466 -0.0289 -0.0158 0.0359  446  PHE A CD1 
3322  C CD2 . PHE A 448  ? 0.2204 0.1882 0.3785 -0.0311 -0.0215 0.0288  446  PHE A CD2 
3323  C CE1 . PHE A 448  ? 0.2441 0.2083 0.4029 -0.0314 -0.0176 0.0412  446  PHE A CE1 
3324  C CE2 . PHE A 448  ? 0.2706 0.2362 0.4392 -0.0336 -0.0235 0.0338  446  PHE A CE2 
3325  C CZ  . PHE A 448  ? 0.2361 0.2000 0.4051 -0.0339 -0.0215 0.0403  446  PHE A CZ  
3326  N N   . GLN A 449  ? 0.1586 0.1335 0.2729 -0.0216 -0.0084 0.0238  447  GLN A N   
3327  C CA  . GLN A 449  ? 0.1613 0.1376 0.2665 -0.0195 -0.0072 0.0197  447  GLN A CA  
3328  C C   . GLN A 449  ? 0.1819 0.1543 0.2846 -0.0182 -0.0077 0.0168  447  GLN A C   
3329  O O   . GLN A 449  ? 0.1680 0.1368 0.2739 -0.0185 -0.0078 0.0194  447  GLN A O   
3330  C CB  . GLN A 449  ? 0.1490 0.1280 0.2466 -0.0183 -0.0031 0.0234  447  GLN A CB  
3331  C CG  . GLN A 449  ? 0.1660 0.1492 0.2658 -0.0192 -0.0023 0.0265  447  GLN A CG  
3332  C CD  . GLN A 449  ? 0.1596 0.1456 0.2517 -0.0175 0.0009  0.0282  447  GLN A CD  
3333  O OE1 . GLN A 449  ? 0.1859 0.1704 0.2716 -0.0159 0.0030  0.0284  447  GLN A OE1 
3334  N NE2 . GLN A 449  ? 0.1588 0.1489 0.2520 -0.0179 0.0012  0.0294  447  GLN A NE2 
3335  N N   . CYS A 450  ? 0.1536 0.1273 0.2504 -0.0168 -0.0080 0.0116  448  CYS A N   
3336  C CA  . CYS A 450  ? 0.1582 0.1291 0.2521 -0.0154 -0.0085 0.0082  448  CYS A CA  
3337  C C   . CYS A 450  ? 0.1725 0.1465 0.2573 -0.0138 -0.0069 0.0054  448  CYS A C   
3338  O O   . CYS A 450  ? 0.1769 0.1550 0.2585 -0.0139 -0.0061 0.0054  448  CYS A O   
3339  C CB  . CYS A 450  ? 0.1736 0.1424 0.2744 -0.0158 -0.0127 0.0029  448  CYS A CB  
3340  S SG  . CYS A 450  ? 0.2070 0.1808 0.3071 -0.0155 -0.0154 -0.0049 448  CYS A SG  
3341  N N   . LEU A 451  ? 0.1620 0.1342 0.2432 -0.0124 -0.0066 0.0031  449  LEU A N   
3342  C CA  . LEU A 451  ? 0.1634 0.1384 0.2363 -0.0110 -0.0052 0.0007  449  LEU A CA  
3343  C C   . LEU A 451  ? 0.1607 0.1388 0.2339 -0.0106 -0.0079 -0.0061 449  LEU A C   
3344  O O   . LEU A 451  ? 0.1875 0.1637 0.2661 -0.0104 -0.0106 -0.0100 449  LEU A O   
3345  C CB  . LEU A 451  ? 0.1812 0.1532 0.2499 -0.0097 -0.0033 0.0021  449  LEU A CB  
3346  C CG  . LEU A 451  ? 0.1928 0.1674 0.2537 -0.0083 -0.0021 -0.0004 449  LEU A CG  
3347  C CD1 . LEU A 451  ? 0.2096 0.1872 0.2648 -0.0084 0.0002  0.0026  449  LEU A CD1 
3348  C CD2 . LEU A 451  ? 0.2201 0.1911 0.2787 -0.0072 -0.0010 0.0003  449  LEU A CD2 
3349  N N   . HIS A 452  ? 0.1584 0.1418 0.2263 -0.0103 -0.0073 -0.0076 450  HIS A N   
3350  C CA  . HIS A 452  ? 0.1798 0.1676 0.2464 -0.0097 -0.0094 -0.0139 450  HIS A CA  
3351  C C   . HIS A 452  ? 0.2111 0.1974 0.2766 -0.0082 -0.0098 -0.0175 450  HIS A C   
3352  O O   . HIS A 452  ? 0.2096 0.1936 0.2710 -0.0075 -0.0076 -0.0150 450  HIS A O   
3353  C CB  . HIS A 452  ? 0.1925 0.1864 0.2522 -0.0096 -0.0080 -0.0135 450  HIS A CB  
3354  C CG  . HIS A 452  ? 0.1596 0.1594 0.2168 -0.0088 -0.0096 -0.0193 450  HIS A CG  
3355  N ND1 . HIS A 452  ? 0.1999 0.2045 0.2597 -0.0092 -0.0123 -0.0238 450  HIS A ND1 
3356  C CD2 . HIS A 452  ? 0.2065 0.2085 0.2587 -0.0076 -0.0089 -0.0217 450  HIS A CD2 
3357  C CE1 . HIS A 452  ? 0.2401 0.2502 0.2965 -0.0081 -0.0130 -0.0286 450  HIS A CE1 
3358  N NE2 . HIS A 452  ? 0.2134 0.2220 0.2653 -0.0072 -0.0110 -0.0273 450  HIS A NE2 
3359  N N   . GLY A 453  ? 0.2502 0.2383 0.3193 -0.0077 -0.0128 -0.0239 451  GLY A N   
3360  C CA  . GLY A 453  ? 0.2598 0.2473 0.3281 -0.0060 -0.0135 -0.0281 451  GLY A CA  
3361  C C   . GLY A 453  ? 0.3046 0.2847 0.3768 -0.0057 -0.0134 -0.0257 451  GLY A C   
3362  O O   . GLY A 453  ? 0.3560 0.3350 0.4256 -0.0044 -0.0126 -0.0267 451  GLY A O   
3363  N N   . MET A 454  ? 0.2375 0.2130 0.3161 -0.0070 -0.0142 -0.0223 452  MET A N   
3364  C CA  . MET A 454  ? 0.2445 0.2134 0.3272 -0.0070 -0.0142 -0.0191 452  MET A CA  
3365  C C   . MET A 454  ? 0.2431 0.2083 0.3354 -0.0086 -0.0167 -0.0177 452  MET A C   
3366  O O   . MET A 454  ? 0.2603 0.2213 0.3594 -0.0084 -0.0193 -0.0194 452  MET A O   
3367  C CB  . MET A 454  ? 0.2361 0.2034 0.3132 -0.0072 -0.0103 -0.0123 452  MET A CB  
3368  C CG  . MET A 454  ? 0.2622 0.2236 0.3433 -0.0074 -0.0101 -0.0080 452  MET A CG  
3369  S SD  . MET A 454  ? 0.3267 0.2848 0.4095 -0.0056 -0.0118 -0.0119 452  MET A SD  
3370  C CE  . MET A 454  ? 0.3189 0.2810 0.3907 -0.0040 -0.0087 -0.0129 452  MET A CE  
3371  N N   . GLY A 455  ? 0.2277 0.1946 0.3210 -0.0102 -0.0162 -0.0145 453  GLY A N   
3372  C CA  . GLY A 455  ? 0.2153 0.1792 0.3179 -0.0121 -0.0184 -0.0122 453  GLY A CA  
3373  C C   . GLY A 455  ? 0.2426 0.2081 0.3519 -0.0127 -0.0224 -0.0179 453  GLY A C   
3374  O O   . GLY A 455  ? 0.2383 0.2007 0.3565 -0.0143 -0.0249 -0.0164 453  GLY A O   
3375  N N   . GLU A 456  ? 0.2382 0.2089 0.3436 -0.0115 -0.0233 -0.0242 454  GLU A N   
3376  C CA  . GLU A 456  ? 0.2694 0.2424 0.3807 -0.0120 -0.0273 -0.0300 454  GLU A CA  
3377  C C   . GLU A 456  ? 0.2939 0.2620 0.4152 -0.0118 -0.0316 -0.0341 454  GLU A C   
3378  O O   . GLU A 456  ? 0.2953 0.2625 0.4247 -0.0132 -0.0349 -0.0356 454  GLU A O   
3379  C CB  . GLU A 456  ? 0.2932 0.2736 0.3980 -0.0106 -0.0274 -0.0362 454  GLU A CB  
3380  C CG  . GLU A 456  ? 0.3099 0.2956 0.4066 -0.0111 -0.0241 -0.0325 454  GLU A CG  
3381  C CD  . GLU A 456  ? 0.3325 0.3190 0.4202 -0.0098 -0.0205 -0.0300 454  GLU A CD  
3382  O OE1 . GLU A 456  ? 0.2922 0.2739 0.3802 -0.0090 -0.0197 -0.0289 454  GLU A OE1 
3383  O OE2 . GLU A 456  ? 0.3236 0.3154 0.4041 -0.0097 -0.0185 -0.0292 454  GLU A OE2 
3384  N N   . PRO A 457  ? 0.2822 0.2470 0.4038 -0.0101 -0.0321 -0.0363 455  PRO A N   
3385  C CA  . PRO A 457  ? 0.3211 0.2807 0.4534 -0.0099 -0.0366 -0.0400 455  PRO A CA  
3386  C C   . PRO A 457  ? 0.3155 0.2693 0.4570 -0.0125 -0.0380 -0.0338 455  PRO A C   
3387  O O   . PRO A 457  ? 0.3219 0.2732 0.4734 -0.0134 -0.0424 -0.0368 455  PRO A O   
3388  C CB  . PRO A 457  ? 0.2675 0.2245 0.3971 -0.0077 -0.0359 -0.0414 455  PRO A CB  
3389  C CG  . PRO A 457  ? 0.2873 0.2507 0.4051 -0.0063 -0.0323 -0.0426 455  PRO A CG  
3390  C CD  . PRO A 457  ? 0.2533 0.2194 0.3662 -0.0081 -0.0291 -0.0365 455  PRO A CD  
3391  N N   . LEU A 458  ? 0.2629 0.2150 0.4013 -0.0137 -0.0343 -0.0251 456  LEU A N   
3392  C CA  . LEU A 458  ? 0.2380 0.1859 0.3847 -0.0163 -0.0351 -0.0183 456  LEU A CA  
3393  C C   . LEU A 458  ? 0.2543 0.2056 0.4041 -0.0183 -0.0360 -0.0176 456  LEU A C   
3394  O O   . LEU A 458  ? 0.2616 0.2102 0.4220 -0.0202 -0.0396 -0.0175 456  LEU A O   
3395  C CB  . LEU A 458  ? 0.2547 0.2014 0.3964 -0.0167 -0.0307 -0.0096 456  LEU A CB  
3396  C CG  . LEU A 458  ? 0.2287 0.1731 0.3773 -0.0194 -0.0305 -0.0014 456  LEU A CG  
3397  C CD1 . LEU A 458  ? 0.2431 0.1817 0.4042 -0.0205 -0.0352 -0.0015 456  LEU A CD1 
3398  C CD2 . LEU A 458  ? 0.2622 0.2068 0.4042 -0.0192 -0.0259 0.0062  456  LEU A CD2 
3399  N N   . TYR A 459  ? 0.2346 0.1917 0.3758 -0.0181 -0.0329 -0.0172 457  TYR A N   
3400  C CA  . TYR A 459  ? 0.2254 0.1856 0.3697 -0.0202 -0.0333 -0.0151 457  TYR A CA  
3401  C C   . TYR A 459  ? 0.2475 0.2103 0.3964 -0.0203 -0.0376 -0.0228 457  TYR A C   
3402  O O   . TYR A 459  ? 0.2656 0.2301 0.4198 -0.0223 -0.0391 -0.0215 457  TYR A O   
3403  C CB  . TYR A 459  ? 0.2470 0.2121 0.3814 -0.0200 -0.0286 -0.0108 457  TYR A CB  
3404  C CG  . TYR A 459  ? 0.1946 0.1572 0.3284 -0.0209 -0.0252 -0.0021 457  TYR A CG  
3405  C CD1 . TYR A 459  ? 0.2059 0.1679 0.3467 -0.0233 -0.0255 0.0038  457  TYR A CD1 
3406  C CD2 . TYR A 459  ? 0.2086 0.1697 0.3353 -0.0193 -0.0220 0.0002  457  TYR A CD2 
3407  C CE1 . TYR A 459  ? 0.2156 0.1764 0.3560 -0.0240 -0.0225 0.0116  457  TYR A CE1 
3408  C CE2 . TYR A 459  ? 0.1959 0.1554 0.3220 -0.0199 -0.0191 0.0078  457  TYR A CE2 
3409  C CZ  . TYR A 459  ? 0.2158 0.1754 0.3486 -0.0222 -0.0193 0.0135  457  TYR A CZ  
3410  O OH  . TYR A 459  ? 0.2295 0.1886 0.3616 -0.0227 -0.0163 0.0210  457  TYR A OH  
3411  N N   . GLU A 460  ? 0.2661 0.2297 0.4138 -0.0181 -0.0398 -0.0310 458  GLU A N   
3412  C CA  . GLU A 460  ? 0.2813 0.2467 0.4354 -0.0181 -0.0447 -0.0389 458  GLU A CA  
3413  C C   . GLU A 460  ? 0.3057 0.2645 0.4734 -0.0196 -0.0494 -0.0391 458  GLU A C   
3414  O O   . GLU A 460  ? 0.3219 0.2816 0.4968 -0.0201 -0.0539 -0.0449 458  GLU A O   
3415  C CB  . GLU A 460  ? 0.3139 0.2827 0.4631 -0.0151 -0.0457 -0.0478 458  GLU A CB  
3416  C CG  . GLU A 460  ? 0.3838 0.3607 0.5212 -0.0141 -0.0424 -0.0486 458  GLU A CG  
3417  C CD  . GLU A 460  ? 0.5056 0.4875 0.6383 -0.0113 -0.0434 -0.0572 458  GLU A CD  
3418  O OE1 . GLU A 460  ? 0.5084 0.4868 0.6448 -0.0097 -0.0455 -0.0616 458  GLU A OE1 
3419  O OE2 . GLU A 460  ? 0.5635 0.5532 0.6889 -0.0108 -0.0422 -0.0594 458  GLU A OE2 
3420  N N   . GLU A 461  ? 0.2729 0.2256 0.4447 -0.0204 -0.0487 -0.0329 459  GLU A N   
3421  C CA  . GLU A 461  ? 0.3188 0.2653 0.5040 -0.0226 -0.0527 -0.0305 459  GLU A CA  
3422  C C   . GLU A 461  ? 0.3058 0.2527 0.4946 -0.0259 -0.0511 -0.0216 459  GLU A C   
3423  O O   . GLU A 461  ? 0.3111 0.2537 0.5101 -0.0279 -0.0537 -0.0176 459  GLU A O   
3424  C CB  . GLU A 461  ? 0.2923 0.2322 0.4807 -0.0218 -0.0532 -0.0285 459  GLU A CB  
3425  C CG  . GLU A 461  ? 0.3398 0.2797 0.5245 -0.0183 -0.0543 -0.0368 459  GLU A CG  
3426  C CD  . GLU A 461  ? 0.3716 0.3125 0.5626 -0.0169 -0.0596 -0.0465 459  GLU A CD  
3427  O OE1 . GLU A 461  ? 0.3956 0.3356 0.5950 -0.0180 -0.0627 -0.0453 459  GLU A OE1 
3428  O OE2 . GLU A 461  ? 0.3991 0.3430 0.5858 -0.0143 -0.0603 -0.0551 459  GLU A OE2 
3429  N N   . VAL A 462  ? 0.2962 0.2487 0.4761 -0.0261 -0.0468 -0.0182 460  VAL A N   
3430  C CA  . VAL A 462  ? 0.2645 0.2185 0.4463 -0.0287 -0.0446 -0.0096 460  VAL A CA  
3431  C C   . VAL A 462  ? 0.2884 0.2483 0.4697 -0.0297 -0.0452 -0.0118 460  VAL A C   
3432  O O   . VAL A 462  ? 0.2967 0.2566 0.4868 -0.0323 -0.0474 -0.0092 460  VAL A O   
3433  C CB  . VAL A 462  ? 0.2586 0.2139 0.4308 -0.0281 -0.0386 -0.0024 460  VAL A CB  
3434  C CG1 . VAL A 462  ? 0.2620 0.2201 0.4356 -0.0304 -0.0362 0.0057  460  VAL A CG1 
3435  C CG2 . VAL A 462  ? 0.2737 0.2234 0.4472 -0.0274 -0.0382 0.0006  460  VAL A CG2 
3436  N N   . VAL A 463  ? 0.2865 0.2517 0.4578 -0.0277 -0.0434 -0.0164 461  VAL A N   
3437  C CA  . VAL A 463  ? 0.2626 0.2340 0.4319 -0.0283 -0.0435 -0.0180 461  VAL A CA  
3438  C C   . VAL A 463  ? 0.3155 0.2873 0.4936 -0.0290 -0.0493 -0.0254 461  VAL A C   
3439  O O   . VAL A 463  ? 0.3644 0.3342 0.5445 -0.0274 -0.0525 -0.0327 461  VAL A O   
3440  C CB  . VAL A 463  ? 0.2739 0.2510 0.4303 -0.0260 -0.0401 -0.0204 461  VAL A CB  
3441  C CG1 . VAL A 463  ? 0.3250 0.3089 0.4795 -0.0266 -0.0407 -0.0223 461  VAL A CG1 
3442  C CG2 . VAL A 463  ? 0.2386 0.2151 0.3871 -0.0254 -0.0347 -0.0131 461  VAL A CG2 
3443  N N   . GLY A 464  ? 0.3335 0.3081 0.5167 -0.0312 -0.0508 -0.0239 462  GLY A N   
3444  C CA  . GLY A 464  ? 0.3467 0.3229 0.5371 -0.0317 -0.0563 -0.0314 462  GLY A CA  
3445  C C   . GLY A 464  ? 0.3860 0.3569 0.5910 -0.0345 -0.0606 -0.0295 462  GLY A C   
3446  O O   . GLY A 464  ? 0.3147 0.2797 0.5251 -0.0355 -0.0603 -0.0242 462  GLY A O   
3447  N N   . ARG A 465  ? 0.3541 0.3276 0.5659 -0.0359 -0.0648 -0.0337 463  ARG A N   
3448  C CA  . ARG A 465  ? 0.3716 0.3412 0.5956 -0.0380 -0.0685 -0.0312 463  ARG A CA  
3449  C C   . ARG A 465  ? 0.3891 0.3524 0.6174 -0.0359 -0.0713 -0.0342 463  ARG A C   
3450  O O   . ARG A 465  ? 0.4419 0.4010 0.6775 -0.0368 -0.0724 -0.0287 463  ARG A O   
3451  C CB  . ARG A 465  ? 0.3515 0.3259 0.5794 -0.0389 -0.0720 -0.0358 463  ARG A CB  
3452  N N   . GLY A 466  ? 0.3807 0.3439 0.6050 -0.0330 -0.0726 -0.0426 464  GLY A N   
3453  C CA  . GLY A 466  ? 0.3628 0.3206 0.5910 -0.0305 -0.0752 -0.0458 464  GLY A CA  
3454  C C   . GLY A 466  ? 0.4057 0.3586 0.6321 -0.0301 -0.0722 -0.0397 464  GLY A C   
3455  O O   . GLY A 466  ? 0.4055 0.3542 0.6351 -0.0280 -0.0743 -0.0418 464  GLY A O   
3456  N N   . LYS A 467  ? 0.3685 0.3220 0.5897 -0.0319 -0.0675 -0.0319 465  LYS A N   
3457  C CA  . LYS A 467  ? 0.3386 0.2882 0.5571 -0.0315 -0.0642 -0.0257 465  LYS A CA  
3458  C C   . LYS A 467  ? 0.3687 0.3180 0.5901 -0.0343 -0.0617 -0.0145 465  LYS A C   
3459  O O   . LYS A 467  ? 0.3835 0.3321 0.6131 -0.0355 -0.0643 -0.0118 465  LYS A O   
3460  C CB  . LYS A 467  ? 0.3054 0.2564 0.5137 -0.0303 -0.0607 -0.0280 465  LYS A CB  
3461  C CG  . LYS A 467  ? 0.3312 0.2837 0.5363 -0.0273 -0.0631 -0.0392 465  LYS A CG  
3462  C CD  . LYS A 467  ? 0.3311 0.2788 0.5403 -0.0247 -0.0657 -0.0419 465  LYS A CD  
3463  C CE  . LYS A 467  ? 0.3878 0.3377 0.5926 -0.0214 -0.0672 -0.0526 465  LYS A CE  
3464  N NZ  . LYS A 467  ? 0.3962 0.3420 0.6054 -0.0187 -0.0698 -0.0553 465  LYS A NZ  
3465  N N   . LEU A 468  ? 0.2922 0.2426 0.5071 -0.0351 -0.0567 -0.0080 466  LEU A N   
3466  C CA  . LEU A 468  ? 0.3014 0.2532 0.5180 -0.0373 -0.0537 0.0024  466  LEU A CA  
3467  C C   . LEU A 468  ? 0.2903 0.2476 0.5059 -0.0394 -0.0521 0.0044  466  LEU A C   
3468  O O   . LEU A 468  ? 0.2911 0.2506 0.5087 -0.0413 -0.0500 0.0125  466  LEU A O   
3469  C CB  . LEU A 468  ? 0.3091 0.2596 0.5191 -0.0367 -0.0490 0.0088  466  LEU A CB  
3470  C CG  . LEU A 468  ? 0.2937 0.2391 0.5045 -0.0347 -0.0502 0.0083  466  LEU A CG  
3471  C CD1 . LEU A 468  ? 0.3139 0.2589 0.5182 -0.0343 -0.0454 0.0155  466  LEU A CD1 
3472  C CD2 . LEU A 468  ? 0.3614 0.3046 0.5824 -0.0353 -0.0544 0.0100  466  LEU A CD2 
3473  N N   . ASP A 469  ? 0.2929 0.2537 0.5046 -0.0388 -0.0529 -0.0029 467  ASP A N   
3474  C CA  . ASP A 469  ? 0.3033 0.2709 0.5119 -0.0396 -0.0513 -0.0017 467  ASP A CA  
3475  C C   . ASP A 469  ? 0.2889 0.2599 0.4897 -0.0396 -0.0452 0.0067  467  ASP A C   
3476  O O   . ASP A 469  ? 0.2760 0.2506 0.4796 -0.0415 -0.0439 0.0122  467  ASP A O   
3477  C CB  . ASP A 469  ? 0.2986 0.2665 0.5195 -0.0427 -0.0556 -0.0010 467  ASP A CB  
3478  C CG  . ASP A 469  ? 0.3678 0.3427 0.5863 -0.0432 -0.0554 -0.0030 467  ASP A CG  
3479  O OD1 . ASP A 469  ? 0.3964 0.3753 0.6044 -0.0407 -0.0538 -0.0080 467  ASP A OD1 
3480  O OD2 . ASP A 469  ? 0.3775 0.3542 0.6039 -0.0459 -0.0568 0.0008  467  ASP A OD2 
3481  N N   . ARG A 470  ? 0.2704 0.2403 0.4616 -0.0372 -0.0414 0.0076  468  ARG A N   
3482  C CA  . ARG A 470  ? 0.2626 0.2358 0.4447 -0.0364 -0.0356 0.0139  468  ARG A CA  
3483  C C   . ARG A 470  ? 0.2266 0.2026 0.3962 -0.0333 -0.0331 0.0091  468  ARG A C   
3484  O O   . ARG A 470  ? 0.2569 0.2305 0.4235 -0.0315 -0.0345 0.0032  468  ARG A O   
3485  C CB  . ARG A 470  ? 0.2429 0.2125 0.4255 -0.0366 -0.0332 0.0207  468  ARG A CB  
3486  C CG  . ARG A 470  ? 0.2595 0.2267 0.4547 -0.0398 -0.0354 0.0266  468  ARG A CG  
3487  C CD  . ARG A 470  ? 0.2842 0.2570 0.4825 -0.0419 -0.0339 0.0324  468  ARG A CD  
3488  N NE  . ARG A 470  ? 0.3182 0.2900 0.5268 -0.0443 -0.0360 0.0378  468  ARG A NE  
3489  C CZ  . ARG A 470  ? 0.3326 0.3042 0.5494 -0.0456 -0.0405 0.0354  468  ARG A CZ  
3490  N NH1 . ARG A 470  ? 0.2921 0.2640 0.5107 -0.0457 -0.0437 0.0277  468  ARG A NH1 
3491  N NH2 . ARG A 470  ? 0.3266 0.2981 0.5501 -0.0467 -0.0418 0.0408  468  ARG A NH2 
3492  N N   . PRO A 471  ? 0.2137 0.1949 0.3761 -0.0327 -0.0296 0.0117  469  PRO A N   
3493  C CA  . PRO A 471  ? 0.1982 0.1824 0.3492 -0.0301 -0.0275 0.0077  469  PRO A CA  
3494  C C   . PRO A 471  ? 0.2295 0.2114 0.3725 -0.0282 -0.0238 0.0099  469  PRO A C   
3495  O O   . PRO A 471  ? 0.2057 0.1850 0.3499 -0.0286 -0.0217 0.0158  469  PRO A O   
3496  C CB  . PRO A 471  ? 0.2398 0.2300 0.3880 -0.0305 -0.0254 0.0107  469  PRO A CB  
3497  C CG  . PRO A 471  ? 0.2372 0.2270 0.3915 -0.0324 -0.0239 0.0184  469  PRO A CG  
3498  C CD  . PRO A 471  ? 0.2397 0.2249 0.4051 -0.0345 -0.0279 0.0179  469  PRO A CD  
3499  N N   . CYS A 472  ? 0.1953 0.1786 0.3298 -0.0260 -0.0230 0.0051  470  CYS A N   
3500  C CA  . CYS A 472  ? 0.1833 0.1647 0.3095 -0.0240 -0.0198 0.0064  470  CYS A CA  
3501  C C   . CYS A 472  ? 0.1907 0.1768 0.3072 -0.0224 -0.0175 0.0048  470  CYS A C   
3502  O O   . CYS A 472  ? 0.2027 0.1921 0.3176 -0.0220 -0.0195 -0.0006 470  CYS A O   
3503  C CB  . CYS A 472  ? 0.1995 0.1767 0.3268 -0.0230 -0.0219 0.0016  470  CYS A CB  
3504  S SG  . CYS A 472  ? 0.2203 0.1953 0.3380 -0.0207 -0.0181 0.0031  470  CYS A SG  
3505  N N   . ARG A 473  ? 0.1795 0.1660 0.2896 -0.0215 -0.0135 0.0095  471  ARG A N   
3506  C CA  . ARG A 473  ? 0.1725 0.1626 0.2735 -0.0199 -0.0113 0.0088  471  ARG A CA  
3507  C C   . ARG A 473  ? 0.1716 0.1593 0.2661 -0.0181 -0.0101 0.0067  471  ARG A C   
3508  O O   . ARG A 473  ? 0.1827 0.1665 0.2769 -0.0177 -0.0084 0.0096  471  ARG A O   
3509  C CB  . ARG A 473  ? 0.1661 0.1582 0.2645 -0.0197 -0.0079 0.0147  471  ARG A CB  
3510  C CG  . ARG A 473  ? 0.1648 0.1605 0.2551 -0.0183 -0.0063 0.0141  471  ARG A CG  
3511  C CD  . ARG A 473  ? 0.1609 0.1587 0.2497 -0.0180 -0.0036 0.0193  471  ARG A CD  
3512  N NE  . ARG A 473  ? 0.1556 0.1555 0.2519 -0.0197 -0.0047 0.0215  471  ARG A NE  
3513  C CZ  . ARG A 473  ? 0.1747 0.1787 0.2732 -0.0205 -0.0065 0.0202  471  ARG A CZ  
3514  N NH1 . ARG A 473  ? 0.1741 0.1813 0.2675 -0.0197 -0.0071 0.0174  471  ARG A NH1 
3515  N NH2 . ARG A 473  ? 0.1657 0.1711 0.2720 -0.0222 -0.0078 0.0219  471  ARG A NH2 
3516  N N   . ILE A 474  ? 0.1828 0.1734 0.2723 -0.0171 -0.0109 0.0019  472  ILE A N   
3517  C CA  . ILE A 474  ? 0.1705 0.1599 0.2539 -0.0155 -0.0100 -0.0005 472  ILE A CA  
3518  C C   . ILE A 474  ? 0.1731 0.1640 0.2485 -0.0145 -0.0066 0.0030  472  ILE A C   
3519  O O   . ILE A 474  ? 0.1657 0.1610 0.2379 -0.0145 -0.0062 0.0032  472  ILE A O   
3520  C CB  . ILE A 474  ? 0.1855 0.1783 0.2679 -0.0150 -0.0127 -0.0075 472  ILE A CB  
3521  C CG1 . ILE A 474  ? 0.2237 0.2143 0.3147 -0.0157 -0.0164 -0.0115 472  ILE A CG1 
3522  C CG2 . ILE A 474  ? 0.1770 0.1695 0.2529 -0.0133 -0.0114 -0.0096 472  ILE A CG2 
3523  C CD1 . ILE A 474  ? 0.2404 0.2356 0.3313 -0.0151 -0.0195 -0.0190 472  ILE A CD1 
3524  N N   . TYR A 475  ? 0.1594 0.1466 0.2319 -0.0135 -0.0043 0.0055  473  TYR A N   
3525  C CA  . TYR A 475  ? 0.1621 0.1498 0.2272 -0.0124 -0.0014 0.0081  473  TYR A CA  
3526  C C   . TYR A 475  ? 0.1717 0.1614 0.2313 -0.0114 -0.0018 0.0040  473  TYR A C   
3527  O O   . TYR A 475  ? 0.1811 0.1686 0.2405 -0.0108 -0.0024 0.0013  473  TYR A O   
3528  C CB  . TYR A 475  ? 0.1803 0.1636 0.2451 -0.0118 0.0009  0.0120  473  TYR A CB  
3529  C CG  . TYR A 475  ? 0.1948 0.1776 0.2532 -0.0105 0.0039  0.0152  473  TYR A CG  
3530  C CD1 . TYR A 475  ? 0.1977 0.1827 0.2549 -0.0103 0.0055  0.0186  473  TYR A CD1 
3531  C CD2 . TYR A 475  ? 0.2989 0.2790 0.3534 -0.0094 0.0050  0.0149  473  TYR A CD2 
3532  C CE1 . TYR A 475  ? 0.1922 0.1765 0.2442 -0.0090 0.0081  0.0211  473  TYR A CE1 
3533  C CE2 . TYR A 475  ? 0.3372 0.3166 0.3865 -0.0082 0.0076  0.0175  473  TYR A CE2 
3534  C CZ  . TYR A 475  ? 0.2784 0.2598 0.3265 -0.0080 0.0090  0.0205  473  TYR A CZ  
3535  O OH  . TYR A 475  ? 0.3263 0.3069 0.3696 -0.0066 0.0112  0.0225  473  TYR A OH  
3536  N N   . ALA A 476  ? 0.1483 0.1426 0.2038 -0.0114 -0.0017 0.0037  474  ALA A N   
3537  C CA  . ALA A 476  ? 0.1537 0.1521 0.2052 -0.0109 -0.0027 -0.0004 474  ALA A CA  
3538  C C   . ALA A 476  ? 0.1561 0.1553 0.2006 -0.0102 -0.0006 0.0020  474  ALA A C   
3539  O O   . ALA A 476  ? 0.1582 0.1599 0.2005 -0.0104 0.0002  0.0048  474  ALA A O   
3540  C CB  . ALA A 476  ? 0.1884 0.1926 0.2413 -0.0118 -0.0049 -0.0028 474  ALA A CB  
3541  N N   . PRO A 477  ? 0.1697 0.1667 0.2111 -0.0093 0.0004  0.0010  475  PRO A N   
3542  C CA  . PRO A 477  ? 0.1505 0.1483 0.1857 -0.0087 0.0021  0.0031  475  PRO A CA  
3543  C C   . PRO A 477  ? 0.1693 0.1739 0.2014 -0.0091 0.0010  0.0015  475  PRO A C   
3544  O O   . PRO A 477  ? 0.1773 0.1860 0.2105 -0.0093 -0.0009 -0.0028 475  PRO A O   
3545  C CB  . PRO A 477  ? 0.1719 0.1664 0.2055 -0.0078 0.0028  0.0017  475  PRO A CB  
3546  C CG  . PRO A 477  ? 0.1991 0.1897 0.2385 -0.0078 0.0018  0.0003  475  PRO A CG  
3547  C CD  . PRO A 477  ? 0.1787 0.1725 0.2225 -0.0087 -0.0004 -0.0020 475  PRO A CD  
3548  N N   . VAL A 478  ? 0.1525 0.1585 0.1808 -0.0092 0.0022  0.0049  476  VAL A N   
3549  C CA  . VAL A 478  ? 0.1615 0.1743 0.1868 -0.0098 0.0013  0.0047  476  VAL A CA  
3550  C C   . VAL A 478  ? 0.1615 0.1738 0.1820 -0.0095 0.0027  0.0075  476  VAL A C   
3551  O O   . VAL A 478  ? 0.1956 0.2035 0.2156 -0.0092 0.0041  0.0111  476  VAL A O   
3552  C CB  . VAL A 478  ? 0.1777 0.1932 0.2047 -0.0105 0.0005  0.0071  476  VAL A CB  
3553  C CG1 . VAL A 478  ? 0.1897 0.2128 0.2135 -0.0113 -0.0005 0.0074  476  VAL A CG1 
3554  C CG2 . VAL A 478  ? 0.1849 0.2004 0.2173 -0.0109 -0.0009 0.0047  476  VAL A CG2 
3555  N N   . GLY A 479  ? 0.1917 0.2087 0.2091 -0.0097 0.0022  0.0056  477  GLY A N   
3556  C CA  . GLY A 479  ? 0.1988 0.2155 0.2122 -0.0098 0.0033  0.0085  477  GLY A CA  
3557  C C   . GLY A 479  ? 0.2096 0.2313 0.2201 -0.0099 0.0030  0.0059  477  GLY A C   
3558  O O   . GLY A 479  ? 0.2062 0.2308 0.2177 -0.0095 0.0022  0.0012  477  GLY A O   
3559  N N   . THR A 480  ? 0.2254 0.2483 0.2327 -0.0104 0.0037  0.0090  478  THR A N   
3560  C CA  . THR A 480  ? 0.2023 0.2304 0.2066 -0.0106 0.0036  0.0076  478  THR A CA  
3561  C C   . THR A 480  ? 0.2457 0.2691 0.2499 -0.0095 0.0046  0.0050  478  THR A C   
3562  O O   . THR A 480  ? 0.2341 0.2499 0.2401 -0.0086 0.0054  0.0053  478  THR A O   
3563  C CB  . THR A 480  ? 0.2460 0.2760 0.2477 -0.0117 0.0039  0.0124  478  THR A CB  
3564  O OG1 . THR A 480  ? 0.2710 0.2927 0.2730 -0.0112 0.0050  0.0153  478  THR A OG1 
3565  C CG2 . THR A 480  ? 0.2990 0.3340 0.3009 -0.0129 0.0027  0.0155  478  THR A CG2 
3566  N N   . HIS A 481  ? 0.2627 0.2911 0.2648 -0.0094 0.0045  0.0029  479  HIS A N   
3567  C CA  . HIS A 481  ? 0.2561 0.2807 0.2580 -0.0083 0.0053  0.0006  479  HIS A CA  
3568  C C   . HIS A 481  ? 0.3195 0.3363 0.3207 -0.0082 0.0066  0.0044  479  HIS A C   
3569  O O   . HIS A 481  ? 0.2857 0.2960 0.2882 -0.0071 0.0073  0.0033  479  HIS A O   
3570  C CB  . HIS A 481  ? 0.2638 0.2960 0.2632 -0.0085 0.0052  -0.0013 479  HIS A CB  
3571  C CG  . HIS A 481  ? 0.2944 0.3346 0.2945 -0.0081 0.0040  -0.0063 479  HIS A CG  
3572  N ND1 . HIS A 481  ? 0.2877 0.3360 0.2860 -0.0078 0.0038  -0.0092 479  HIS A ND1 
3573  C CD2 . HIS A 481  ? 0.2844 0.3263 0.2869 -0.0079 0.0027  -0.0091 479  HIS A CD2 
3574  C CE1 . HIS A 481  ? 0.3257 0.3804 0.3251 -0.0072 0.0025  -0.0139 479  HIS A CE1 
3575  N NE2 . HIS A 481  ? 0.2963 0.3470 0.2983 -0.0073 0.0017  -0.0140 479  HIS A NE2 
3576  N N   . GLU A 482  ? 0.3290 0.3464 0.3284 -0.0092 0.0069  0.0088  480  GLU A N   
3577  C CA  . GLU A 482  ? 0.3313 0.3418 0.3300 -0.0089 0.0078  0.0118  480  GLU A CA  
3578  C C   . GLU A 482  ? 0.3398 0.3432 0.3408 -0.0079 0.0084  0.0124  480  GLU A C   
3579  O O   . GLU A 482  ? 0.3379 0.3353 0.3390 -0.0069 0.0093  0.0124  480  GLU A O   
3580  C CB  . GLU A 482  ? 0.3536 0.3659 0.3510 -0.0103 0.0074  0.0164  480  GLU A CB  
3581  C CG  . GLU A 482  ? 0.3554 0.3606 0.3525 -0.0098 0.0081  0.0191  480  GLU A CG  
3582  C CD  . GLU A 482  ? 0.6089 0.6146 0.6060 -0.0110 0.0073  0.0236  480  GLU A CD  
3583  O OE1 . GLU A 482  ? 0.6579 0.6702 0.6547 -0.0125 0.0063  0.0254  480  GLU A OE1 
3584  O OE2 . GLU A 482  ? 0.6460 0.6455 0.6436 -0.0104 0.0075  0.0255  480  GLU A OE2 
3585  N N   . THR A 483  ? 0.2873 0.2918 0.2902 -0.0082 0.0078  0.0131  481  THR A N   
3586  C CA  . THR A 483  ? 0.2898 0.2886 0.2950 -0.0074 0.0084  0.0140  481  THR A CA  
3587  C C   . THR A 483  ? 0.3040 0.2998 0.3113 -0.0065 0.0087  0.0109  481  THR A C   
3588  O O   . THR A 483  ? 0.2932 0.2835 0.3016 -0.0056 0.0097  0.0119  481  THR A O   
3589  C CB  . THR A 483  ? 0.3123 0.3139 0.3193 -0.0081 0.0076  0.0154  481  THR A CB  
3590  O OG1 . THR A 483  ? 0.3357 0.3399 0.3412 -0.0090 0.0071  0.0188  481  THR A OG1 
3591  C CG2 . THR A 483  ? 0.3559 0.3525 0.3656 -0.0072 0.0083  0.0167  481  THR A CG2 
3592  N N   . LEU A 484  ? 0.2526 0.2523 0.2609 -0.0066 0.0077  0.0072  482  LEU A N   
3593  C CA  . LEU A 484  ? 0.2766 0.2731 0.2879 -0.0058 0.0076  0.0044  482  LEU A CA  
3594  C C   . LEU A 484  ? 0.2796 0.2723 0.2897 -0.0049 0.0084  0.0037  482  LEU A C   
3595  O O   . LEU A 484  ? 0.3090 0.2970 0.3215 -0.0041 0.0087  0.0034  482  LEU A O   
3596  C CB  . LEU A 484  ? 0.2784 0.2798 0.2918 -0.0060 0.0059  0.0001  482  LEU A CB  
3597  C CG  . LEU A 484  ? 0.2784 0.2853 0.2900 -0.0058 0.0052  -0.0036 482  LEU A CG  
3598  C CD1 . LEU A 484  ? 0.2861 0.2896 0.2997 -0.0046 0.0050  -0.0069 482  LEU A CD1 
3599  C CD2 . LEU A 484  ? 0.3110 0.3255 0.3232 -0.0063 0.0036  -0.0065 482  LEU A CD2 
3600  N N   . LEU A 485  ? 0.2736 0.2686 0.2803 -0.0050 0.0087  0.0037  483  LEU A N   
3601  C CA  . LEU A 485  ? 0.2543 0.2462 0.2601 -0.0040 0.0093  0.0029  483  LEU A CA  
3602  C C   . LEU A 485  ? 0.2643 0.2500 0.2691 -0.0035 0.0106  0.0062  483  LEU A C   
3603  O O   . LEU A 485  ? 0.2912 0.2734 0.2960 -0.0026 0.0111  0.0057  483  LEU A O   
3604  C CB  . LEU A 485  ? 0.2764 0.2732 0.2792 -0.0044 0.0092  0.0019  483  LEU A CB  
3605  C CG  . LEU A 485  ? 0.2811 0.2845 0.2847 -0.0044 0.0080  -0.0024 483  LEU A CG  
3606  C CD1 . LEU A 485  ? 0.3343 0.3442 0.3346 -0.0051 0.0081  -0.0022 483  LEU A CD1 
3607  C CD2 . LEU A 485  ? 0.2950 0.2959 0.3013 -0.0030 0.0075  -0.0063 483  LEU A CD2 
3608  N N   . ALA A 486  ? 0.2665 0.2512 0.2707 -0.0039 0.0111  0.0094  484  ALA A N   
3609  C CA  . ALA A 486  ? 0.3054 0.2853 0.3083 -0.0031 0.0122  0.0121  484  ALA A CA  
3610  C C   . ALA A 486  ? 0.3141 0.2895 0.3188 -0.0020 0.0130  0.0120  484  ALA A C   
3611  O O   . ALA A 486  ? 0.3396 0.3119 0.3427 -0.0011 0.0137  0.0124  484  ALA A O   
3612  C CB  . ALA A 486  ? 0.3060 0.2858 0.3090 -0.0035 0.0123  0.0150  484  ALA A CB  
3613  N N   . TYR A 487  ? 0.3121 0.2874 0.3202 -0.0021 0.0127  0.0116  485  TYR A N   
3614  C CA  . TYR A 487  ? 0.2895 0.2611 0.2999 -0.0013 0.0134  0.0123  485  TYR A CA  
3615  C C   . TYR A 487  ? 0.2984 0.2703 0.3127 -0.0016 0.0122  0.0099  485  TYR A C   
3616  O O   . TYR A 487  ? 0.3111 0.2809 0.3288 -0.0016 0.0122  0.0109  485  TYR A O   
3617  C CB  . TYR A 487  ? 0.3056 0.2759 0.3171 -0.0011 0.0143  0.0153  485  TYR A CB  
3618  C CG  . TYR A 487  ? 0.3393 0.3089 0.3476 -0.0005 0.0152  0.0172  485  TYR A CG  
3619  C CD1 . TYR A 487  ? 0.3278 0.2945 0.3338 0.0007  0.0163  0.0181  485  TYR A CD1 
3620  C CD2 . TYR A 487  ? 0.3144 0.2862 0.3220 -0.0011 0.0147  0.0180  485  TYR A CD2 
3621  C CE1 . TYR A 487  ? 0.3748 0.3407 0.3784 0.0014  0.0167  0.0193  485  TYR A CE1 
3622  C CE2 . TYR A 487  ? 0.3938 0.3646 0.3993 -0.0005 0.0151  0.0196  485  TYR A CE2 
3623  C CZ  . TYR A 487  ? 0.4208 0.3885 0.4244 0.0008  0.0161  0.0200  485  TYR A CZ  
3624  O OH  . TYR A 487  ? 0.4625 0.4288 0.4644 0.0015  0.0161  0.0211  485  TYR A OH  
3625  N N   . LEU A 488  ? 0.2722 0.2469 0.2862 -0.0018 0.0110  0.0065  486  LEU A N   
3626  C CA  . LEU A 488  ? 0.2693 0.2444 0.2875 -0.0018 0.0095  0.0034  486  LEU A CA  
3627  C C   . LEU A 488  ? 0.2428 0.2135 0.2630 -0.0010 0.0095  0.0035  486  LEU A C   
3628  O O   . LEU A 488  ? 0.2614 0.2305 0.2864 -0.0010 0.0083  0.0025  486  LEU A O   
3629  C CB  . LEU A 488  ? 0.2704 0.2503 0.2876 -0.0020 0.0082  -0.0006 486  LEU A CB  
3630  C CG  . LEU A 488  ? 0.3052 0.2862 0.3269 -0.0017 0.0062  -0.0049 486  LEU A CG  
3631  C CD1 . LEU A 488  ? 0.3372 0.3179 0.3632 -0.0025 0.0053  -0.0044 486  LEU A CD1 
3632  C CD2 . LEU A 488  ? 0.2547 0.2420 0.2749 -0.0016 0.0052  -0.0091 486  LEU A CD2 
3633  N N   . VAL A 489  ? 0.2752 0.2440 0.2921 -0.0002 0.0106  0.0049  487  VAL A N   
3634  C CA  . VAL A 489  ? 0.2496 0.2146 0.2682 0.0006  0.0106  0.0055  487  VAL A CA  
3635  C C   . VAL A 489  ? 0.2423 0.2046 0.2642 0.0004  0.0110  0.0087  487  VAL A C   
3636  O O   . VAL A 489  ? 0.2541 0.2142 0.2806 0.0004  0.0100  0.0087  487  VAL A O   
3637  C CB  . VAL A 489  ? 0.2262 0.1901 0.2403 0.0015  0.0117  0.0065  487  VAL A CB  
3638  C CG1 . VAL A 489  ? 0.2423 0.2025 0.2578 0.0023  0.0120  0.0084  487  VAL A CG1 
3639  C CG2 . VAL A 489  ? 0.2487 0.2154 0.2610 0.0017  0.0110  0.0031  487  VAL A CG2 
3640  N N   . ARG A 490  ? 0.2639 0.2264 0.2840 0.0002  0.0125  0.0118  488  ARG A N   
3641  C CA  . ARG A 490  ? 0.2488 0.2099 0.2720 0.0000  0.0131  0.0151  488  ARG A CA  
3642  C C   . ARG A 490  ? 0.2473 0.2088 0.2764 -0.0011 0.0115  0.0141  488  ARG A C   
3643  O O   . ARG A 490  ? 0.2674 0.2270 0.3011 -0.0014 0.0110  0.0160  488  ARG A O   
3644  C CB  . ARG A 490  ? 0.2786 0.2408 0.2990 0.0002  0.0148  0.0177  488  ARG A CB  
3645  C CG  . ARG A 490  ? 0.2876 0.2495 0.3110 0.0001  0.0158  0.0213  488  ARG A CG  
3646  C CD  . ARG A 490  ? 0.3373 0.3007 0.3583 0.0006  0.0174  0.0233  488  ARG A CD  
3647  N NE  . ARG A 490  ? 0.3311 0.2967 0.3532 -0.0003 0.0167  0.0222  488  ARG A NE  
3648  C CZ  . ARG A 490  ? 0.3149 0.2818 0.3339 0.0000  0.0170  0.0220  488  ARG A CZ  
3649  N NH1 . ARG A 490  ? 0.3216 0.2877 0.3365 0.0011  0.0180  0.0224  488  ARG A NH1 
3650  N NH2 . ARG A 490  ? 0.3245 0.2938 0.3451 -0.0009 0.0161  0.0213  488  ARG A NH2 
3651  N N   . ARG A 491  ? 0.2616 0.2258 0.2910 -0.0017 0.0104  0.0112  489  ARG A N   
3652  C CA  . ARG A 491  ? 0.2750 0.2399 0.3101 -0.0027 0.0085  0.0097  489  ARG A CA  
3653  C C   . ARG A 491  ? 0.3152 0.2781 0.3546 -0.0025 0.0064  0.0069  489  ARG A C   
3654  O O   . ARG A 491  ? 0.3069 0.2682 0.3525 -0.0032 0.0050  0.0072  489  ARG A O   
3655  C CB  . ARG A 491  ? 0.3301 0.2991 0.3639 -0.0033 0.0077  0.0070  489  ARG A CB  
3656  C CG  . ARG A 491  ? 0.3805 0.3507 0.4202 -0.0042 0.0055  0.0047  489  ARG A CG  
3657  C CD  . ARG A 491  ? 0.3775 0.3489 0.4188 -0.0052 0.0060  0.0076  489  ARG A CD  
3658  N NE  . ARG A 491  ? 0.4591 0.4346 0.4964 -0.0053 0.0065  0.0071  489  ARG A NE  
3659  C CZ  . ARG A 491  ? 0.4035 0.3806 0.4407 -0.0059 0.0072  0.0096  489  ARG A CZ  
3660  N NH1 . ARG A 491  ? 0.4394 0.4150 0.4801 -0.0062 0.0078  0.0128  489  ARG A NH1 
3661  N NH2 . ARG A 491  ? 0.3172 0.2980 0.3510 -0.0060 0.0072  0.0091  489  ARG A NH2 
3662  N N   . LEU A 492  ? 0.2711 0.2342 0.3079 -0.0015 0.0062  0.0041  490  LEU A N   
3663  C CA  . LEU A 492  ? 0.2760 0.2371 0.3171 -0.0010 0.0041  0.0011  490  LEU A CA  
3664  C C   . LEU A 492  ? 0.3189 0.2756 0.3635 -0.0009 0.0041  0.0048  490  LEU A C   
3665  O O   . LEU A 492  ? 0.3007 0.2551 0.3519 -0.0011 0.0019  0.0039  490  LEU A O   
3666  C CB  . LEU A 492  ? 0.2835 0.2464 0.3209 0.0002  0.0040  -0.0025 490  LEU A CB  
3667  C CG  . LEU A 492  ? 0.2786 0.2470 0.3136 0.0000  0.0034  -0.0064 490  LEU A CG  
3668  C CD1 . LEU A 492  ? 0.3247 0.2958 0.3551 0.0010  0.0040  -0.0087 490  LEU A CD1 
3669  C CD2 . LEU A 492  ? 0.3196 0.2894 0.3603 -0.0001 0.0008  -0.0107 490  LEU A CD2 
3670  N N   . LEU A 493  ? 0.2725 0.2282 0.3132 -0.0006 0.0064  0.0089  491  LEU A N   
3671  C CA  . LEU A 493  ? 0.2942 0.2468 0.3375 -0.0005 0.0066  0.0129  491  LEU A CA  
3672  C C   . LEU A 493  ? 0.2853 0.2371 0.3344 -0.0018 0.0061  0.0163  491  LEU A C   
3673  O O   . LEU A 493  ? 0.2998 0.2491 0.3532 -0.0021 0.0054  0.0193  491  LEU A O   
3674  C CB  . LEU A 493  ? 0.2670 0.2197 0.3042 0.0004  0.0091  0.0161  491  LEU A CB  
3675  C CG  . LEU A 493  ? 0.3357 0.2872 0.3699 0.0017  0.0091  0.0149  491  LEU A CG  
3676  C CD1 . LEU A 493  ? 0.3563 0.3092 0.3895 0.0021  0.0078  0.0095  491  LEU A CD1 
3677  C CD2 . LEU A 493  ? 0.3347 0.2869 0.3624 0.0024  0.0115  0.0173  491  LEU A CD2 
3678  N N   . GLU A 494  ? 0.2767 0.2309 0.3261 -0.0027 0.0064  0.0161  492  GLU A N   
3679  C CA  . GLU A 494  ? 0.2891 0.2431 0.3444 -0.0042 0.0059  0.0193  492  GLU A CA  
3680  C C   . GLU A 494  ? 0.2980 0.2492 0.3615 -0.0049 0.0028  0.0180  492  GLU A C   
3681  O O   . GLU A 494  ? 0.3116 0.2610 0.3804 -0.0058 0.0022  0.0221  492  GLU A O   
3682  C CB  . GLU A 494  ? 0.2785 0.2357 0.3334 -0.0050 0.0062  0.0184  492  GLU A CB  
3683  C CG  . GLU A 494  ? 0.2773 0.2369 0.3257 -0.0044 0.0090  0.0205  492  GLU A CG  
3684  C CD  . GLU A 494  ? 0.3117 0.2745 0.3598 -0.0051 0.0088  0.0189  492  GLU A CD  
3685  O OE1 . GLU A 494  ? 0.3547 0.3180 0.4079 -0.0062 0.0067  0.0170  492  GLU A OE1 
3686  O OE2 . GLU A 494  ? 0.3937 0.3585 0.4367 -0.0045 0.0105  0.0196  492  GLU A OE2 
3687  N N   . ASN A 495  ? 0.2742 0.2252 0.3389 -0.0044 0.0006  0.0122  493  ASN A N   
3688  C CA  . ASN A 495  ? 0.2478 0.1962 0.3208 -0.0048 -0.0029 0.0098  493  ASN A CA  
3689  C C   . ASN A 495  ? 0.2939 0.2399 0.3673 -0.0033 -0.0043 0.0067  493  ASN A C   
3690  O O   . ASN A 495  ? 0.3121 0.2558 0.3925 -0.0033 -0.0075 0.0037  493  ASN A O   
3691  C CB  . ASN A 495  ? 0.2862 0.2370 0.3617 -0.0054 -0.0048 0.0049  493  ASN A CB  
3692  C CG  . ASN A 495  ? 0.2632 0.2163 0.3392 -0.0069 -0.0038 0.0079  493  ASN A CG  
3693  O OD1 . ASN A 495  ? 0.2708 0.2224 0.3528 -0.0084 -0.0044 0.0118  493  ASN A OD1 
3694  N ND2 . ASN A 495  ? 0.2438 0.2010 0.3138 -0.0067 -0.0022 0.0065  493  ASN A ND2 
3695  N N   . GLY A 496  ? 0.3113 0.2578 0.3780 -0.0020 -0.0022 0.0075  494  GLY A N   
3696  C CA  . GLY A 496  ? 0.3371 0.2821 0.4035 -0.0005 -0.0033 0.0042  494  GLY A CA  
3697  C C   . GLY A 496  ? 0.3588 0.3010 0.4247 0.0002  -0.0026 0.0084  494  GLY A C   
3698  O O   . GLY A 496  ? 0.3619 0.3031 0.4272 0.0016  -0.0034 0.0059  494  GLY A O   
3699  N N   . ALA A 497  ? 0.3336 0.2751 0.3997 -0.0008 -0.0010 0.0147  495  ALA A N   
3700  C CA  . ALA A 497  ? 0.3398 0.2792 0.4055 -0.0003 -0.0005 0.0190  495  ALA A CA  
3701  C C   . ALA A 497  ? 0.3445 0.2801 0.4197 -0.0008 -0.0037 0.0204  495  ALA A C   
3702  O O   . ALA A 497  ? 0.3061 0.2404 0.3883 -0.0019 -0.0061 0.0189  495  ALA A O   
3703  C CB  . ALA A 497  ? 0.3228 0.2641 0.3845 -0.0009 0.0025  0.0251  495  ALA A CB  
3704  N N   . ASN A 498  ? 0.3721 0.3057 0.4477 -0.0001 -0.0038 0.0236  496  ASN A N   
3705  C CA  . ASN A 498  ? 0.3621 0.2917 0.4469 -0.0005 -0.0071 0.0252  496  ASN A CA  
3706  C C   . ASN A 498  ? 0.3735 0.3024 0.4655 -0.0028 -0.0081 0.0301  496  ASN A C   
3707  O O   . ASN A 498  ? 0.3430 0.2685 0.4444 -0.0036 -0.0116 0.0295  496  ASN A O   
3708  C CB  . ASN A 498  ? 0.3805 0.3089 0.4639 0.0004  -0.0068 0.0292  496  ASN A CB  
3709  C CG  . ASN A 498  ? 0.5102 0.4378 0.5910 0.0026  -0.0076 0.0239  496  ASN A CG  
3710  O OD1 . ASN A 498  ? 0.5347 0.4624 0.6163 0.0034  -0.0090 0.0172  496  ASN A OD1 
3711  N ND2 . ASN A 498  ? 0.4841 0.4115 0.5620 0.0036  -0.0069 0.0268  496  ASN A ND2 
3712  N N   . SER A 499  ? 0.3102 0.2424 0.3983 -0.0038 -0.0051 0.0350  497  SER A N   
3713  C CA  . SER A 499  ? 0.3348 0.2672 0.4293 -0.0061 -0.0056 0.0402  497  SER A CA  
3714  C C   . SER A 499  ? 0.2755 0.2090 0.3723 -0.0072 -0.0063 0.0368  497  SER A C   
3715  O O   . SER A 499  ? 0.3239 0.2577 0.4271 -0.0092 -0.0071 0.0406  497  SER A O   
3716  C CB  . SER A 499  ? 0.3507 0.2871 0.4402 -0.0065 -0.0021 0.0472  497  SER A CB  
3717  O OG  . SER A 499  ? 0.4243 0.3640 0.5037 -0.0052 0.0012  0.0448  497  SER A OG  
3718  N N   . SER A 500  ? 0.2745 0.2092 0.3664 -0.0060 -0.0059 0.0301  498  SER A N   
3719  C CA  . SER A 500  ? 0.2879 0.2244 0.3813 -0.0070 -0.0064 0.0269  498  SER A CA  
3720  C C   . SER A 500  ? 0.2877 0.2208 0.3914 -0.0079 -0.0108 0.0239  498  SER A C   
3721  O O   . SER A 500  ? 0.3053 0.2353 0.4128 -0.0068 -0.0135 0.0203  498  SER A O   
3722  C CB  . SER A 500  ? 0.2719 0.2109 0.3574 -0.0055 -0.0051 0.0207  498  SER A CB  
3723  O OG  . SER A 500  ? 0.3051 0.2469 0.3816 -0.0047 -0.0014 0.0231  498  SER A OG  
3724  N N   . PHE A 501  ? 0.2411 0.1753 0.3499 -0.0098 -0.0116 0.0253  499  PHE A N   
3725  C CA  . PHE A 501  ? 0.2436 0.1748 0.3627 -0.0109 -0.0160 0.0222  499  PHE A CA  
3726  C C   . PHE A 501  ? 0.2862 0.2170 0.4046 -0.0091 -0.0182 0.0130  499  PHE A C   
3727  O O   . PHE A 501  ? 0.2906 0.2177 0.4164 -0.0086 -0.0220 0.0095  499  PHE A O   
3728  C CB  . PHE A 501  ? 0.2360 0.1693 0.3589 -0.0131 -0.0162 0.0243  499  PHE A CB  
3729  C CG  . PHE A 501  ? 0.2613 0.1919 0.3948 -0.0143 -0.0209 0.0205  499  PHE A CG  
3730  C CD1 . PHE A 501  ? 0.2711 0.1981 0.4152 -0.0160 -0.0239 0.0247  499  PHE A CD1 
3731  C CD2 . PHE A 501  ? 0.2688 0.2010 0.4017 -0.0136 -0.0224 0.0128  499  PHE A CD2 
3732  C CE1 . PHE A 501  ? 0.3018 0.2276 0.4544 -0.0166 -0.0283 0.0207  499  PHE A CE1 
3733  C CE2 . PHE A 501  ? 0.2810 0.2109 0.4238 -0.0144 -0.0270 0.0088  499  PHE A CE2 
3734  C CZ  . PHE A 501  ? 0.3021 0.2275 0.4559 -0.0162 -0.0302 0.0127  499  PHE A CZ  
3735  N N   . VAL A 502  ? 0.2536 0.1886 0.3637 -0.0081 -0.0160 0.0091  500  VAL A N   
3736  C CA  . VAL A 502  ? 0.3147 0.2510 0.4240 -0.0065 -0.0179 0.0005  500  VAL A CA  
3737  C C   . VAL A 502  ? 0.3225 0.2564 0.4313 -0.0044 -0.0189 -0.0025 500  VAL A C   
3738  O O   . VAL A 502  ? 0.3424 0.2751 0.4561 -0.0033 -0.0223 -0.0088 500  VAL A O   
3739  C CB  . VAL A 502  ? 0.2686 0.2104 0.3686 -0.0061 -0.0151 -0.0019 500  VAL A CB  
3740  C CG1 . VAL A 502  ? 0.3291 0.2735 0.4271 -0.0043 -0.0166 -0.0102 500  VAL A CG1 
3741  C CG2 . VAL A 502  ? 0.2774 0.2215 0.3794 -0.0080 -0.0150 -0.0002 500  VAL A CG2 
3742  N N   . HIS A 503  ? 0.2910 0.2245 0.3942 -0.0037 -0.0162 0.0018  501  HIS A N   
3743  C CA  . HIS A 503  ? 0.3273 0.2587 0.4302 -0.0018 -0.0171 -0.0004 501  HIS A CA  
3744  C C   . HIS A 503  ? 0.3365 0.2624 0.4503 -0.0020 -0.0211 0.0006  501  HIS A C   
3745  O O   . HIS A 503  ? 0.3315 0.2556 0.4492 -0.0003 -0.0239 -0.0049 501  HIS A O   
3746  C CB  . HIS A 503  ? 0.3011 0.2334 0.3958 -0.0012 -0.0134 0.0045  501  HIS A CB  
3747  C CG  . HIS A 503  ? 0.3947 0.3256 0.4882 0.0008  -0.0140 0.0023  501  HIS A CG  
3748  N ND1 . HIS A 503  ? 0.4112 0.3379 0.5095 0.0010  -0.0154 0.0061  501  HIS A ND1 
3749  C CD2 . HIS A 503  ? 0.4248 0.3581 0.5128 0.0028  -0.0134 -0.0030 501  HIS A CD2 
3750  C CE1 . HIS A 503  ? 0.4412 0.3678 0.5372 0.0031  -0.0157 0.0029  501  HIS A CE1 
3751  N NE2 . HIS A 503  ? 0.4583 0.3889 0.5480 0.0041  -0.0144 -0.0026 501  HIS A NE2 
3752  N N   . ARG A 504  ? 0.3007 0.2243 0.4200 -0.0042 -0.0214 0.0074  502  ARG A N   
3753  C CA  . ARG A 504  ? 0.3065 0.2247 0.4367 -0.0047 -0.0253 0.0096  502  ARG A CA  
3754  C C   . ARG A 504  ? 0.3543 0.2712 0.4931 -0.0048 -0.0298 0.0032  502  ARG A C   
3755  O O   . ARG A 504  ? 0.3259 0.2413 0.4703 -0.0037 -0.0331 0.0007  502  ARG A O   
3756  C CB  . ARG A 504  ? 0.3059 0.2247 0.4380 -0.0071 -0.0241 0.0190  502  ARG A CB  
3757  C CG  . ARG A 504  ? 0.3654 0.2854 0.4900 -0.0068 -0.0203 0.0251  502  ARG A CG  
3758  C CD  . ARG A 504  ? 0.3566 0.2797 0.4808 -0.0090 -0.0180 0.0335  502  ARG A CD  
3759  N NE  . ARG A 504  ? 0.4098 0.3330 0.5427 -0.0107 -0.0210 0.0366  502  ARG A NE  
3760  C CZ  . ARG A 504  ? 0.3879 0.3103 0.5245 -0.0106 -0.0228 0.0396  502  ARG A CZ  
3761  N NH1 . ARG A 504  ? 0.4370 0.3583 0.5695 -0.0088 -0.0221 0.0396  502  ARG A NH1 
3762  N NH2 . ARG A 504  ? 0.4631 0.3859 0.6080 -0.0124 -0.0255 0.0429  502  ARG A NH2 
3763  N N   . ILE A 505  ? 0.3187 0.2376 0.4579 -0.0058 -0.0299 0.0004  503  ILE A N   
3764  C CA  . ILE A 505  ? 0.3731 0.2913 0.5206 -0.0057 -0.0344 -0.0060 503  ILE A CA  
3765  C C   . ILE A 505  ? 0.4053 0.3237 0.5518 -0.0027 -0.0362 -0.0155 503  ILE A C   
3766  O O   . ILE A 505  ? 0.3710 0.2893 0.5243 -0.0018 -0.0403 -0.0207 503  ILE A O   
3767  C CB  . ILE A 505  ? 0.3756 0.2960 0.5242 -0.0077 -0.0343 -0.0069 503  ILE A CB  
3768  C CG1 . ILE A 505  ? 0.4465 0.3661 0.6052 -0.0083 -0.0392 -0.0102 503  ILE A CG1 
3769  C CG2 . ILE A 505  ? 0.4238 0.3503 0.5626 -0.0061 -0.0320 -0.0131 503  ILE A CG2 
3770  C CD1 . ILE A 505  ? 0.3768 0.2982 0.5382 -0.0106 -0.0396 -0.0098 503  ILE A CD1 
3771  N N   . ASN A 506  ? 0.3578 0.2798 0.4940 -0.0010 -0.0328 -0.0174 504  ASN A N   
3772  C CA  . ASN A 506  ? 0.3889 0.3127 0.5231 0.0020  -0.0339 -0.0255 504  ASN A CA  
3773  C C   . ASN A 506  ? 0.4287 0.3485 0.5654 0.0036  -0.0350 -0.0244 504  ASN A C   
3774  O O   . ASN A 506  ? 0.4902 0.4115 0.6260 0.0063  -0.0360 -0.0310 504  ASN A O   
3775  C CB  . ASN A 506  ? 0.4407 0.3714 0.5626 0.0029  -0.0298 -0.0278 504  ASN A CB  
3776  C CG  . ASN A 506  ? 0.5073 0.4428 0.6272 0.0020  -0.0296 -0.0311 504  ASN A CG  
3777  O OD1 . ASN A 506  ? 0.5661 0.5005 0.6938 0.0014  -0.0332 -0.0345 504  ASN A OD1 
3778  N ND2 . ASN A 506  ? 0.5264 0.4673 0.6361 0.0018  -0.0258 -0.0302 504  ASN A ND2 
3779  N N   . ASP A 507  ? 0.4142 0.3306 0.5532 0.0022  -0.0345 -0.0161 505  ASP A N   
3780  C CA  . ASP A 507  ? 0.4420 0.3568 0.5824 0.0034  -0.0354 -0.0140 505  ASP A CA  
3781  C C   . ASP A 507  ? 0.4417 0.3551 0.5923 0.0033  -0.0401 -0.0153 505  ASP A C   
3782  O O   . ASP A 507  ? 0.4200 0.3323 0.5758 0.0009  -0.0411 -0.0095 505  ASP A O   
3783  C CB  . ASP A 507  ? 0.4186 0.3324 0.5552 0.0020  -0.0324 -0.0043 505  ASP A CB  
3784  C CG  . ASP A 507  ? 0.4860 0.3984 0.6227 0.0034  -0.0329 -0.0022 505  ASP A CG  
3785  O OD1 . ASP A 507  ? 0.5100 0.4214 0.6526 0.0048  -0.0364 -0.0063 505  ASP A OD1 
3786  O OD2 . ASP A 507  ? 0.4562 0.3686 0.5869 0.0032  -0.0298 0.0035  505  ASP A OD2 
3787  N N   . PRO A 508  ? 0.4758 0.3896 0.6298 0.0058  -0.0430 -0.0224 506  PRO A N   
3788  C CA  . PRO A 508  ? 0.5005 0.4128 0.6650 0.0058  -0.0478 -0.0236 506  PRO A CA  
3789  C C   . PRO A 508  ? 0.4552 0.3648 0.6238 0.0044  -0.0485 -0.0153 506  PRO A C   
3790  O O   . PRO A 508  ? 0.5352 0.4434 0.7132 0.0034  -0.0522 -0.0140 506  PRO A O   
3791  C CB  . PRO A 508  ? 0.5332 0.4473 0.6988 0.0092  -0.0500 -0.0329 506  PRO A CB  
3792  C CG  . PRO A 508  ? 0.5956 0.5131 0.7517 0.0106  -0.0467 -0.0376 506  PRO A CG  
3793  C CD  . PRO A 508  ? 0.5237 0.4399 0.6725 0.0088  -0.0422 -0.0297 506  PRO A CD  
3794  N N   . LYS A 509  ? 0.4510 0.3601 0.6132 0.0043  -0.0453 -0.0096 507  LYS A N   
3795  C CA  . LYS A 509  ? 0.4790 0.3864 0.6442 0.0030  -0.0456 -0.0013 507  LYS A CA  
3796  C C   . LYS A 509  ? 0.4955 0.4034 0.6612 -0.0003 -0.0440 0.0071  507  LYS A C   
3797  O O   . LYS A 509  ? 0.5186 0.4260 0.6866 -0.0016 -0.0441 0.0145  507  LYS A O   
3798  C CB  . LYS A 509  ? 0.5325 0.4398 0.6906 0.0044  -0.0429 0.0011  507  LYS A CB  
3799  N N   . VAL A 510  ? 0.4647 0.3740 0.6282 -0.0015 -0.0425 0.0062  508  VAL A N   
3800  C CA  . VAL A 510  ? 0.4474 0.3579 0.6120 -0.0045 -0.0412 0.0135  508  VAL A CA  
3801  C C   . VAL A 510  ? 0.3911 0.3010 0.5657 -0.0057 -0.0453 0.0113  508  VAL A C   
3802  O O   . VAL A 510  ? 0.4025 0.3127 0.5785 -0.0049 -0.0468 0.0040  508  VAL A O   
3803  C CB  . VAL A 510  ? 0.3871 0.2996 0.5428 -0.0051 -0.0367 0.0145  508  VAL A CB  
3804  C CG1 . VAL A 510  ? 0.3799 0.2943 0.5376 -0.0081 -0.0356 0.0215  508  VAL A CG1 
3805  C CG2 . VAL A 510  ? 0.4023 0.3153 0.5486 -0.0039 -0.0329 0.0170  508  VAL A CG2 
3806  N N   . SER A 511  ? 0.4135 0.3231 0.5954 -0.0076 -0.0473 0.0176  509  SER A N   
3807  C CA  . SER A 511  ? 0.3924 0.3014 0.5848 -0.0088 -0.0515 0.0162  509  SER A CA  
3808  C C   . SER A 511  ? 0.3918 0.3030 0.5835 -0.0112 -0.0498 0.0189  509  SER A C   
3809  O O   . SER A 511  ? 0.3608 0.2742 0.5452 -0.0123 -0.0455 0.0239  509  SER A O   
3810  C CB  . SER A 511  ? 0.4246 0.3326 0.6259 -0.0101 -0.0546 0.0221  509  SER A CB  
3811  O OG  . SER A 511  ? 0.4181 0.3284 0.6176 -0.0125 -0.0519 0.0318  509  SER A OG  
3812  N N   . ILE A 512  ? 0.3644 0.2752 0.5642 -0.0118 -0.0535 0.0153  510  ILE A N   
3813  C CA  . ILE A 512  ? 0.3522 0.2651 0.5527 -0.0142 -0.0525 0.0177  510  ILE A CA  
3814  C C   . ILE A 512  ? 0.4233 0.3381 0.6259 -0.0169 -0.0511 0.0282  510  ILE A C   
3815  O O   . ILE A 512  ? 0.3645 0.2821 0.5627 -0.0185 -0.0478 0.0326  510  ILE A O   
3816  C CB  . ILE A 512  ? 0.3506 0.2627 0.5600 -0.0141 -0.0572 0.0114  510  ILE A CB  
3817  C CG1 . ILE A 512  ? 0.3585 0.2701 0.5646 -0.0112 -0.0580 0.0006  510  ILE A CG1 
3818  C CG2 . ILE A 512  ? 0.3654 0.2796 0.5764 -0.0167 -0.0565 0.0143  510  ILE A CG2 
3819  C CD1 . ILE A 512  ? 0.3990 0.3109 0.6117 -0.0110 -0.0619 -0.0063 510  ILE A CD1 
3820  N N   . ASP A 513  ? 0.3900 0.3037 0.5992 -0.0173 -0.0537 0.0324  511  ASP A N   
3821  C CA  . ASP A 513  ? 0.3947 0.3112 0.6058 -0.0197 -0.0523 0.0426  511  ASP A CA  
3822  C C   . ASP A 513  ? 0.4003 0.3196 0.6000 -0.0198 -0.0466 0.0476  511  ASP A C   
3823  O O   . ASP A 513  ? 0.3806 0.3038 0.5784 -0.0217 -0.0439 0.0541  511  ASP A O   
3824  C CB  . ASP A 513  ? 0.4512 0.3660 0.6708 -0.0199 -0.0560 0.0460  511  ASP A CB  
3825  C CG  . ASP A 513  ? 0.4935 0.4068 0.7262 -0.0209 -0.0616 0.0446  511  ASP A CG  
3826  O OD1 . ASP A 513  ? 0.4931 0.4074 0.7284 -0.0222 -0.0622 0.0433  511  ASP A OD1 
3827  O OD2 . ASP A 513  ? 0.5246 0.4356 0.7653 -0.0205 -0.0656 0.0448  511  ASP A OD2 
3828  N N   . GLU A 514  ? 0.3719 0.2898 0.5642 -0.0175 -0.0448 0.0444  512  GLU A N   
3829  C CA  . GLU A 514  ? 0.4007 0.3211 0.5820 -0.0172 -0.0395 0.0483  512  GLU A CA  
3830  C C   . GLU A 514  ? 0.3455 0.2680 0.5204 -0.0176 -0.0361 0.0469  512  GLU A C   
3831  O O   . GLU A 514  ? 0.4155 0.3416 0.5839 -0.0184 -0.0320 0.0523  512  GLU A O   
3832  C CB  . GLU A 514  ? 0.4296 0.3477 0.6049 -0.0145 -0.0387 0.0445  512  GLU A CB  
3833  C CG  . GLU A 514  ? 0.4686 0.3851 0.6490 -0.0141 -0.0413 0.0472  512  GLU A CG  
3834  C CD  . GLU A 514  ? 0.5305 0.4444 0.7064 -0.0112 -0.0413 0.0421  512  GLU A CD  
3835  O OE1 . GLU A 514  ? 0.5527 0.4655 0.7238 -0.0094 -0.0404 0.0350  512  GLU A OE1 
3836  O OE2 . GLU A 514  ? 0.6684 0.5817 0.8460 -0.0107 -0.0423 0.0452  512  GLU A OE2 
3837  N N   . LEU A 515  ? 0.3623 0.2830 0.5392 -0.0171 -0.0379 0.0396  513  LEU A N   
3838  C CA  . LEU A 515  ? 0.3466 0.2692 0.5176 -0.0175 -0.0350 0.0378  513  LEU A CA  
3839  C C   . LEU A 515  ? 0.3475 0.2734 0.5225 -0.0202 -0.0346 0.0430  513  LEU A C   
3840  O O   . LEU A 515  ? 0.3099 0.2387 0.4791 -0.0209 -0.0310 0.0450  513  LEU A O   
3841  C CB  . LEU A 515  ? 0.3490 0.2693 0.5207 -0.0160 -0.0371 0.0280  513  LEU A CB  
3842  C CG  . LEU A 515  ? 0.3186 0.2368 0.4841 -0.0132 -0.0363 0.0221  513  LEU A CG  
3843  C CD1 . LEU A 515  ? 0.3736 0.2905 0.5420 -0.0117 -0.0395 0.0122  513  LEU A CD1 
3844  C CD2 . LEU A 515  ? 0.3403 0.2603 0.4949 -0.0127 -0.0312 0.0240  513  LEU A CD2 
3845  N N   . ILE A 516  ? 0.3288 0.2545 0.5139 -0.0216 -0.0383 0.0453  514  ILE A N   
3846  C CA  . ILE A 516  ? 0.3231 0.2521 0.5127 -0.0242 -0.0383 0.0503  514  ILE A CA  
3847  C C   . ILE A 516  ? 0.3547 0.2877 0.5443 -0.0257 -0.0362 0.0600  514  ILE A C   
3848  O O   . ILE A 516  ? 0.3598 0.2962 0.5537 -0.0278 -0.0363 0.0651  514  ILE A O   
3849  C CB  . ILE A 516  ? 0.3409 0.2678 0.5420 -0.0251 -0.0436 0.0471  514  ILE A CB  
3850  C CG1 . ILE A 516  ? 0.3638 0.2887 0.5731 -0.0250 -0.0475 0.0493  514  ILE A CG1 
3851  C CG2 . ILE A 516  ? 0.3440 0.2681 0.5448 -0.0235 -0.0456 0.0370  514  ILE A CG2 
3852  C CD1 . ILE A 516  ? 0.3548 0.2777 0.5762 -0.0258 -0.0530 0.0466  514  ILE A CD1 
3853  N N   . ALA A 517  ? 0.3239 0.2569 0.5085 -0.0245 -0.0345 0.0626  515  ALA A N   
3854  C CA  . ALA A 517  ? 0.3341 0.2717 0.5169 -0.0256 -0.0320 0.0715  515  ALA A CA  
3855  C C   . ALA A 517  ? 0.3707 0.3137 0.5480 -0.0266 -0.0278 0.0752  515  ALA A C   
3856  O O   . ALA A 517  ? 0.3655 0.3085 0.5356 -0.0256 -0.0250 0.0715  515  ALA A O   
3857  C CB  . ALA A 517  ? 0.3709 0.3078 0.5466 -0.0237 -0.0300 0.0723  515  ALA A CB  
3858  N N   . ASP A 518  ? 0.3739 0.3221 0.5549 -0.0285 -0.0273 0.0828  516  ASP A N   
3859  C CA  . ASP A 518  ? 0.3249 0.2791 0.5022 -0.0295 -0.0236 0.0868  516  ASP A CA  
3860  C C   . ASP A 518  ? 0.3330 0.2915 0.5002 -0.0283 -0.0188 0.0907  516  ASP A C   
3861  O O   . ASP A 518  ? 0.3182 0.2798 0.4861 -0.0287 -0.0185 0.0965  516  ASP A O   
3862  C CB  . ASP A 518  ? 0.3378 0.2960 0.5242 -0.0320 -0.0255 0.0929  516  ASP A CB  
3863  C CG  . ASP A 518  ? 0.3394 0.3042 0.5230 -0.0331 -0.0219 0.0968  516  ASP A CG  
3864  O OD1 . ASP A 518  ? 0.3298 0.2961 0.5046 -0.0318 -0.0181 0.0946  516  ASP A OD1 
3865  O OD2 . ASP A 518  ? 0.3999 0.3688 0.5906 -0.0351 -0.0232 0.1022  516  ASP A OD2 
3866  N N   . PRO A 519  ? 0.2813 0.2405 0.4394 -0.0269 -0.0150 0.0878  517  PRO A N   
3867  C CA  . PRO A 519  ? 0.3131 0.2765 0.4617 -0.0256 -0.0106 0.0912  517  PRO A CA  
3868  C C   . PRO A 519  ? 0.2837 0.2552 0.4329 -0.0268 -0.0085 0.0990  517  PRO A C   
3869  O O   . PRO A 519  ? 0.3105 0.2859 0.4549 -0.0260 -0.0063 0.1031  517  PRO A O   
3870  C CB  . PRO A 519  ? 0.2988 0.2616 0.4394 -0.0242 -0.0076 0.0865  517  PRO A CB  
3871  C CG  . PRO A 519  ? 0.3729 0.3300 0.5181 -0.0245 -0.0107 0.0799  517  PRO A CG  
3872  C CD  . PRO A 519  ? 0.3053 0.2620 0.4616 -0.0266 -0.0148 0.0817  517  PRO A CD  
3873  N N   . VAL A 520  ? 0.3195 0.2942 0.4745 -0.0287 -0.0091 0.1011  518  VAL A N   
3874  C CA  . VAL A 520  ? 0.2821 0.2654 0.4378 -0.0297 -0.0070 0.1085  518  VAL A CA  
3875  C C   . VAL A 520  ? 0.3129 0.2982 0.4740 -0.0307 -0.0090 0.1143  518  VAL A C   
3876  O O   . VAL A 520  ? 0.3069 0.2984 0.4640 -0.0303 -0.0065 0.1196  518  VAL A O   
3877  C CB  . VAL A 520  ? 0.3343 0.3202 0.4961 -0.0316 -0.0077 0.1092  518  VAL A CB  
3878  C CG1 . VAL A 520  ? 0.3674 0.3628 0.5296 -0.0325 -0.0053 0.1166  518  VAL A CG1 
3879  C CG2 . VAL A 520  ? 0.3239 0.3077 0.4807 -0.0307 -0.0059 0.1033  518  VAL A CG2 
3880  N N   . GLU A 521  ? 0.3351 0.3152 0.5054 -0.0319 -0.0138 0.1133  519  GLU A N   
3881  C CA  . GLU A 521  ? 0.3678 0.3496 0.5443 -0.0330 -0.0162 0.1190  519  GLU A CA  
3882  C C   . GLU A 521  ? 0.3699 0.3500 0.5406 -0.0312 -0.0154 0.1189  519  GLU A C   
3883  O O   . GLU A 521  ? 0.3766 0.3614 0.5480 -0.0316 -0.0151 0.1251  519  GLU A O   
3884  C CB  . GLU A 521  ? 0.3683 0.3449 0.5568 -0.0346 -0.0218 0.1178  519  GLU A CB  
3885  C CG  . GLU A 521  ? 0.3739 0.3537 0.5700 -0.0368 -0.0231 0.1203  519  GLU A CG  
3886  C CD  . GLU A 521  ? 0.4924 0.4821 0.6879 -0.0380 -0.0203 0.1286  519  GLU A CD  
3887  O OE1 . GLU A 521  ? 0.5281 0.5215 0.7236 -0.0381 -0.0199 0.1342  519  GLU A OE1 
3888  O OE2 . GLU A 521  ? 0.4909 0.4848 0.6859 -0.0387 -0.0184 0.1295  519  GLU A OE2 
3889  N N   . VAL A 522  ? 0.3621 0.3360 0.5271 -0.0292 -0.0151 0.1120  520  VAL A N   
3890  C CA  . VAL A 522  ? 0.3173 0.2894 0.4765 -0.0274 -0.0143 0.1116  520  VAL A CA  
3891  C C   . VAL A 522  ? 0.3960 0.3752 0.5457 -0.0264 -0.0095 0.1156  520  VAL A C   
3892  O O   . VAL A 522  ? 0.3935 0.3756 0.5414 -0.0259 -0.0090 0.1197  520  VAL A O   
3893  C CB  . VAL A 522  ? 0.3729 0.3371 0.5284 -0.0255 -0.0150 0.1032  520  VAL A CB  
3894  C CG1 . VAL A 522  ? 0.3380 0.3007 0.4868 -0.0235 -0.0139 0.1027  520  VAL A CG1 
3895  C CG2 . VAL A 522  ? 0.4111 0.3689 0.5763 -0.0263 -0.0201 0.0991  520  VAL A CG2 
3896  N N   . VAL A 523  ? 0.3341 0.3167 0.4779 -0.0258 -0.0059 0.1144  521  VAL A N   
3897  C CA  . VAL A 523  ? 0.3485 0.3385 0.4836 -0.0246 -0.0014 0.1178  521  VAL A CA  
3898  C C   . VAL A 523  ? 0.3672 0.3658 0.5063 -0.0261 -0.0011 0.1260  521  VAL A C   
3899  O O   . VAL A 523  ? 0.3641 0.3682 0.4984 -0.0252 0.0010  0.1299  521  VAL A O   
3900  C CB  . VAL A 523  ? 0.2894 0.2810 0.4181 -0.0236 0.0020  0.1145  521  VAL A CB  
3901  C CG1 . VAL A 523  ? 0.3242 0.3249 0.4456 -0.0225 0.0065  0.1186  521  VAL A CG1 
3902  C CG2 . VAL A 523  ? 0.3056 0.2899 0.4285 -0.0217 0.0023  0.1072  521  VAL A CG2 
3903  N N   . ARG A 524  ? 0.3412 0.3414 0.4894 -0.0284 -0.0033 0.1287  522  ARG A N   
3904  C CA  . ARG A 524  ? 0.3893 0.3982 0.5420 -0.0299 -0.0031 0.1367  522  ARG A CA  
3905  C C   . ARG A 524  ? 0.4136 0.4231 0.5691 -0.0303 -0.0050 0.1411  522  ARG A C   
3906  O O   . ARG A 524  ? 0.4487 0.4666 0.6025 -0.0303 -0.0033 0.1473  522  ARG A O   
3907  C CB  . ARG A 524  ? 0.3794 0.3887 0.5424 -0.0324 -0.0058 0.1385  522  ARG A CB  
3908  C CG  . ARG A 524  ? 0.3829 0.4023 0.5503 -0.0341 -0.0052 0.1469  522  ARG A CG  
3909  C CD  . ARG A 524  ? 0.4634 0.4816 0.6430 -0.0368 -0.0092 0.1494  522  ARG A CD  
3910  N NE  . ARG A 524  ? 0.4566 0.4696 0.6381 -0.0371 -0.0101 0.1436  522  ARG A NE  
3911  C CZ  . ARG A 524  ? 0.4379 0.4554 0.6176 -0.0373 -0.0076 0.1435  522  ARG A CZ  
3912  N NH1 . ARG A 524  ? 0.4110 0.4383 0.5865 -0.0369 -0.0040 0.1484  522  ARG A NH1 
3913  N NH2 . ARG A 524  ? 0.4425 0.4547 0.6244 -0.0377 -0.0090 0.1381  522  ARG A NH2 
3914  N N   . ALA A 525  ? 0.4123 0.4134 0.5720 -0.0303 -0.0087 0.1379  523  ALA A N   
3915  C CA  . ALA A 525  ? 0.4007 0.4017 0.5648 -0.0308 -0.0113 0.1420  523  ALA A CA  
3916  C C   . ALA A 525  ? 0.4197 0.4210 0.5747 -0.0286 -0.0091 0.1414  523  ALA A C   
3917  O O   . ALA A 525  ? 0.4642 0.4664 0.6219 -0.0289 -0.0108 0.1453  523  ALA A O   
3918  C CB  . ALA A 525  ? 0.3569 0.3490 0.5306 -0.0318 -0.0166 0.1388  523  ALA A CB  
3919  N N   . MET A 526  ? 0.4031 0.4035 0.5476 -0.0264 -0.0056 0.1366  524  MET A N   
3920  C CA  A MET A 526  ? 0.4290 0.4301 0.5646 -0.0242 -0.0035 0.1361  524  MET A CA  
3921  C CA  B MET A 526  ? 0.4291 0.4302 0.5647 -0.0242 -0.0035 0.1361  524  MET A CA  
3922  C C   . MET A 526  ? 0.4480 0.4595 0.5816 -0.0244 -0.0014 0.1436  524  MET A C   
3923  O O   . MET A 526  ? 0.4443 0.4635 0.5798 -0.0255 0.0000  0.1479  524  MET A O   
3924  C CB  A MET A 526  ? 0.4482 0.4475 0.5735 -0.0219 0.0001  0.1301  524  MET A CB  
3925  C CB  B MET A 526  ? 0.4481 0.4473 0.5734 -0.0219 0.0000  0.1300  524  MET A CB  
3926  C CG  A MET A 526  ? 0.4320 0.4213 0.5582 -0.0214 -0.0018 0.1225  524  MET A CG  
3927  C CG  B MET A 526  ? 0.4348 0.4236 0.5596 -0.0209 -0.0018 0.1224  524  MET A CG  
3928  S SD  A MET A 526  ? 0.4795 0.4607 0.6091 -0.0208 -0.0058 0.1200  524  MET A SD  
3929  S SD  B MET A 526  ? 0.4485 0.4350 0.5637 -0.0189 0.0017  0.1155  524  MET A SD  
3930  C CE  A MET A 526  ? 0.4588 0.4435 0.5774 -0.0184 -0.0026 0.1214  524  MET A CE  
3931  C CE  B MET A 526  ? 0.4063 0.3992 0.5098 -0.0165 0.0060  0.1176  524  MET A CE  
3932  N N   . PRO A 527  ? 0.4949 0.5072 0.6249 -0.0233 -0.0014 0.1453  525  PRO A N   
3933  C CA  . PRO A 527  ? 0.4911 0.5141 0.6189 -0.0233 0.0005  0.1524  525  PRO A CA  
3934  C C   . PRO A 527  ? 0.5042 0.5352 0.6230 -0.0218 0.0053  0.1523  525  PRO A C   
3935  O O   . PRO A 527  ? 0.4532 0.4937 0.5736 -0.0227 0.0067  0.1577  525  PRO A O   
3936  C CB  . PRO A 527  ? 0.4641 0.4848 0.5885 -0.0220 -0.0003 0.1525  525  PRO A CB  
3937  C CG  . PRO A 527  ? 0.4836 0.4929 0.6133 -0.0223 -0.0041 0.1476  525  PRO A CG  
3938  C CD  . PRO A 527  ? 0.4717 0.4759 0.6006 -0.0221 -0.0034 0.1414  525  PRO A CD  
3939  N N   . VAL A 528  ? 0.4897 0.5173 0.5993 -0.0194 0.0078  0.1463  526  VAL A N   
3940  C CA  . VAL A 528  ? 0.4173 0.4512 0.5186 -0.0177 0.0122  0.1449  526  VAL A CA  
3941  C C   . VAL A 528  ? 0.3700 0.3979 0.4717 -0.0177 0.0125  0.1392  526  VAL A C   
3942  O O   . VAL A 528  ? 0.4105 0.4300 0.5091 -0.0166 0.0120  0.1332  526  VAL A O   
3943  C CB  . VAL A 528  ? 0.4512 0.4865 0.5417 -0.0148 0.0147  0.1425  526  VAL A CB  
3944  C CG1 . VAL A 528  ? 0.4358 0.4788 0.5183 -0.0129 0.0191  0.1415  526  VAL A CG1 
3945  C CG2 . VAL A 528  ? 0.4956 0.5357 0.5862 -0.0148 0.0138  0.1477  526  VAL A CG2 
3946  N N   . VAL A 529  ? 0.3511 0.3836 0.4568 -0.0191 0.0132  0.1412  527  VAL A N   
3947  C CA  . VAL A 529  ? 0.3507 0.3783 0.4572 -0.0193 0.0134  0.1363  527  VAL A CA  
3948  C C   . VAL A 529  ? 0.3383 0.3661 0.4344 -0.0165 0.0171  0.1314  527  VAL A C   
3949  O O   . VAL A 529  ? 0.3152 0.3513 0.4049 -0.0149 0.0204  0.1332  527  VAL A O   
3950  C CB  . VAL A 529  ? 0.3233 0.3567 0.4363 -0.0212 0.0134  0.1400  527  VAL A CB  
3951  C CG1 . VAL A 529  ? 0.3569 0.3859 0.4704 -0.0213 0.0138  0.1349  527  VAL A CG1 
3952  C CG2 . VAL A 529  ? 0.3965 0.4289 0.5206 -0.0240 0.0093  0.1447  527  VAL A CG2 
3953  N N   . GLY A 530  ? 0.2971 0.3158 0.3915 -0.0159 0.0163  0.1251  528  GLY A N   
3954  C CA  . GLY A 530  ? 0.2953 0.3136 0.3809 -0.0135 0.0195  0.1204  528  GLY A CA  
3955  C C   . GLY A 530  ? 0.2786 0.2964 0.3555 -0.0110 0.0210  0.1187  528  GLY A C   
3956  O O   . GLY A 530  ? 0.2665 0.2863 0.3357 -0.0088 0.0241  0.1159  528  GLY A O   
3957  N N   . ALA A 531  ? 0.2483 0.2637 0.3264 -0.0112 0.0189  0.1203  529  ALA A N   
3958  C CA  . ALA A 531  ? 0.2733 0.2884 0.3434 -0.0089 0.0201  0.1188  529  ALA A CA  
3959  C C   . ALA A 531  ? 0.2189 0.2261 0.2840 -0.0073 0.0205  0.1120  529  ALA A C   
3960  O O   . ALA A 531  ? 0.2901 0.2894 0.3596 -0.0083 0.0182  0.1085  529  ALA A O   
3961  C CB  . ALA A 531  ? 0.3022 0.3152 0.3757 -0.0096 0.0172  0.1216  529  ALA A CB  
3962  N N   . LYS A 532  ? 0.2391 0.2489 0.2951 -0.0047 0.0233  0.1102  530  LYS A N   
3963  C CA  . LYS A 532  ? 0.2094 0.2123 0.2601 -0.0029 0.0238  0.1044  530  LYS A CA  
3964  C C   . LYS A 532  ? 0.2564 0.2508 0.3102 -0.0034 0.0204  0.1024  530  LYS A C   
3965  O O   . LYS A 532  ? 0.2464 0.2414 0.3033 -0.0041 0.0184  0.1057  530  LYS A O   
3966  C CB  . LYS A 532  ? 0.2749 0.2828 0.3157 0.0001  0.0269  0.1038  530  LYS A CB  
3967  C CG  . LYS A 532  ? 0.3194 0.3210 0.3541 0.0022  0.0275  0.0983  530  LYS A CG  
3968  C CD  . LYS A 532  ? 0.2718 0.2789 0.2973 0.0051  0.0299  0.0974  530  LYS A CD  
3969  C CE  . LYS A 532  ? 0.2635 0.2734 0.2885 0.0051  0.0288  0.1016  530  LYS A CE  
3970  N NZ  . LYS A 532  ? 0.2881 0.2893 0.3146 0.0049  0.0259  0.0995  530  LYS A NZ  
3971  N N   . HIS A 533  ? 0.2300 0.2168 0.2833 -0.0029 0.0196  0.0969  531  HIS A N   
3972  C CA  . HIS A 533  ? 0.2420 0.2211 0.2973 -0.0028 0.0167  0.0942  531  HIS A CA  
3973  C C   . HIS A 533  ? 0.2423 0.2229 0.2922 -0.0010 0.0171  0.0955  531  HIS A C   
3974  O O   . HIS A 533  ? 0.2651 0.2492 0.3070 0.0011  0.0199  0.0950  531  HIS A O   
3975  C CB  . HIS A 533  ? 0.2353 0.2075 0.2892 -0.0020 0.0166  0.0878  531  HIS A CB  
3976  C CG  . HIS A 533  ? 0.2659 0.2304 0.3243 -0.0023 0.0131  0.0843  531  HIS A CG  
3977  N ND1 . HIS A 533  ? 0.2772 0.2394 0.3337 -0.0010 0.0120  0.0839  531  HIS A ND1 
3978  C CD2 . HIS A 533  ? 0.3259 0.2850 0.3910 -0.0035 0.0105  0.0810  531  HIS A CD2 
3979  C CE1 . HIS A 533  ? 0.3580 0.3136 0.4198 -0.0014 0.0088  0.0803  531  HIS A CE1 
3980  N NE2 . HIS A 533  ? 0.3702 0.3240 0.4372 -0.0029 0.0078  0.0784  531  HIS A NE2 
3981  N N   . ASP A 534  ? 0.2589 0.2369 0.3134 -0.0018 0.0141  0.0971  532  ASP A N   
3982  C CA  . ASP A 534  ? 0.3080 0.2875 0.3581 -0.0003 0.0140  0.0988  532  ASP A CA  
3983  C C   . ASP A 534  ? 0.3307 0.3064 0.3738 0.0022  0.0150  0.0940  532  ASP A C   
3984  O O   . ASP A 534  ? 0.3354 0.3143 0.3722 0.0039  0.0162  0.0952  532  ASP A O   
3985  C CB  . ASP A 534  ? 0.3438 0.3200 0.4010 -0.0015 0.0102  0.1007  532  ASP A CB  
3986  C CG  . ASP A 534  ? 0.4961 0.4777 0.5595 -0.0036 0.0093  0.1067  532  ASP A CG  
3987  O OD1 . ASP A 534  ? 0.5433 0.5328 0.6036 -0.0037 0.0120  0.1102  532  ASP A OD1 
3988  O OD2 . ASP A 534  ? 0.5976 0.5757 0.6690 -0.0051 0.0060  0.1079  532  ASP A OD2 
3989  N N   . ARG A 535  ? 0.2593 0.2286 0.3033 0.0024  0.0144  0.0884  533  ARG A N   
3990  C CA  . ARG A 535  ? 0.2837 0.2498 0.3214 0.0044  0.0144  0.0814  533  ARG A CA  
3991  C C   . ARG A 535  ? 0.2710 0.2394 0.3011 0.0057  0.0171  0.0764  533  ARG A C   
3992  O O   . ARG A 535  ? 0.2980 0.2636 0.3236 0.0071  0.0171  0.0704  533  ARG A O   
3993  C CB  . ARG A 535  ? 0.3243 0.2827 0.3675 0.0040  0.0113  0.0768  533  ARG A CB  
3994  C CG  . ARG A 535  ? 0.4281 0.3835 0.4770 0.0037  0.0083  0.0798  533  ARG A CG  
3995  C CD  . ARG A 535  ? 0.4938 0.4425 0.5518 0.0026  0.0049  0.0774  533  ARG A CD  
3996  N NE  . ARG A 535  ? 0.5969 0.5422 0.6526 0.0035  0.0048  0.0691  533  ARG A NE  
3997  C CZ  . ARG A 535  ? 0.6632 0.6057 0.7167 0.0050  0.0037  0.0640  533  ARG A CZ  
3998  N NH1 . ARG A 535  ? 0.7013 0.6435 0.7545 0.0061  0.0026  0.0660  533  ARG A NH1 
3999  N NH2 . ARG A 535  ? 0.6290 0.5696 0.6805 0.0056  0.0038  0.0569  533  ARG A NH2 
4000  N N   . ILE A 536  ? 0.2601 0.2338 0.2889 0.0054  0.0195  0.0789  534  ILE A N   
4001  C CA  . ILE A 536  ? 0.2594 0.2356 0.2816 0.0068  0.0220  0.0746  534  ILE A CA  
4002  C C   . ILE A 536  ? 0.2651 0.2493 0.2817 0.0083  0.0245  0.0780  534  ILE A C   
4003  O O   . ILE A 536  ? 0.2718 0.2614 0.2912 0.0073  0.0254  0.0841  534  ILE A O   
4004  C CB  . ILE A 536  ? 0.2460 0.2217 0.2718 0.0055  0.0225  0.0736  534  ILE A CB  
4005  C CG1 . ILE A 536  ? 0.3177 0.2862 0.3488 0.0043  0.0199  0.0698  534  ILE A CG1 
4006  C CG2 . ILE A 536  ? 0.2590 0.2376 0.2783 0.0071  0.0250  0.0696  534  ILE A CG2 
4007  C CD1 . ILE A 536  ? 0.3038 0.2718 0.3389 0.0029  0.0200  0.0689  534  ILE A CD1 
4008  N N   . ALA A 537  ? 0.2292 0.2144 0.2382 0.0105  0.0255  0.0739  535  ALA A N   
4009  C CA  . ALA A 537  ? 0.2404 0.2334 0.2436 0.0123  0.0276  0.0761  535  ALA A CA  
4010  C C   . ALA A 537  ? 0.2200 0.2178 0.2209 0.0131  0.0301  0.0749  535  ALA A C   
4011  O O   . ALA A 537  ? 0.2152 0.2096 0.2149 0.0135  0.0303  0.0696  535  ALA A O   
4012  C CB  . ALA A 537  ? 0.2450 0.2372 0.2414 0.0144  0.0273  0.0719  535  ALA A CB  
4013  N N   . LEU A 538  ? 0.2273 0.2335 0.2279 0.0133  0.0320  0.0800  536  LEU A N   
4014  C CA  . LEU A 538  ? 0.2050 0.2170 0.2020 0.0150  0.0346  0.0782  536  LEU A CA  
4015  C C   . LEU A 538  ? 0.2034 0.2151 0.1927 0.0178  0.0350  0.0717  536  LEU A C   
4016  O O   . LEU A 538  ? 0.2266 0.2373 0.2126 0.0187  0.0340  0.0709  536  LEU A O   
4017  C CB  . LEU A 538  ? 0.2183 0.2409 0.2154 0.0152  0.0366  0.0846  536  LEU A CB  
4018  C CG  . LEU A 538  ? 0.2484 0.2729 0.2534 0.0123  0.0366  0.0914  536  LEU A CG  
4019  C CD1 . LEU A 538  ? 0.2654 0.3012 0.2700 0.0125  0.0385  0.0985  536  LEU A CD1 
4020  C CD2 . LEU A 538  ? 0.2632 0.2862 0.2712 0.0117  0.0374  0.0889  536  LEU A CD2 
4021  N N   . PRO A 539  ? 0.2005 0.2127 0.1874 0.0193  0.0362  0.0671  537  PRO A N   
4022  C CA  . PRO A 539  ? 0.1973 0.2086 0.1776 0.0219  0.0362  0.0609  537  PRO A CA  
4023  C C   . PRO A 539  ? 0.2386 0.2568 0.2135 0.0241  0.0370  0.0619  537  PRO A C   
4024  O O   . PRO A 539  ? 0.2405 0.2560 0.2114 0.0253  0.0358  0.0583  537  PRO A O   
4025  C CB  . PRO A 539  ? 0.2000 0.2127 0.1798 0.0231  0.0376  0.0574  537  PRO A CB  
4026  C CG  . PRO A 539  ? 0.2108 0.2203 0.1973 0.0204  0.0373  0.0598  537  PRO A CG  
4027  C CD  . PRO A 539  ? 0.2098 0.2219 0.2004 0.0184  0.0371  0.0669  537  PRO A CD  
4028  N N   . ALA A 540  ? 0.2114 0.2389 0.1863 0.0245  0.0388  0.0670  538  ALA A N   
4029  C CA  . ALA A 540  ? 0.2434 0.2785 0.2128 0.0267  0.0395  0.0680  538  ALA A CA  
4030  C C   . ALA A 540  ? 0.2737 0.3061 0.2430 0.0257  0.0376  0.0706  538  ALA A C   
4031  O O   . ALA A 540  ? 0.2891 0.3255 0.2530 0.0277  0.0375  0.0694  538  ALA A O   
4032  C CB  . ALA A 540  ? 0.2787 0.3254 0.2487 0.0270  0.0419  0.0738  538  ALA A CB  
4033  N N   . GLU A 541  ? 0.2410 0.2669 0.2162 0.0229  0.0359  0.0737  539  GLU A N   
4034  C CA  . GLU A 541  ? 0.2792 0.3026 0.2555 0.0219  0.0339  0.0769  539  GLU A CA  
4035  C C   . GLU A 541  ? 0.2446 0.2580 0.2210 0.0215  0.0316  0.0718  539  GLU A C   
4036  O O   . GLU A 541  ? 0.2582 0.2678 0.2374 0.0203  0.0296  0.0741  539  GLU A O   
4037  C CB  . GLU A 541  ? 0.2873 0.3116 0.2709 0.0191  0.0335  0.0848  539  GLU A CB  
4038  C CG  . GLU A 541  ? 0.3024 0.3380 0.2858 0.0193  0.0359  0.0908  539  GLU A CG  
4039  C CD  . GLU A 541  ? 0.4210 0.4577 0.4126 0.0162  0.0353  0.0989  539  GLU A CD  
4040  O OE1 . GLU A 541  ? 0.4758 0.5050 0.4728 0.0141  0.0328  0.1007  539  GLU A OE1 
4041  O OE2 . GLU A 541  ? 0.4709 0.5160 0.4638 0.0158  0.0373  0.1033  539  GLU A OE2 
4042  N N   . LEU A 542  ? 0.2423 0.2517 0.2160 0.0226  0.0317  0.0649  540  LEU A N   
4043  C CA  . LEU A 542  ? 0.2700 0.2707 0.2438 0.0221  0.0297  0.0600  540  LEU A CA  
4044  C C   . LEU A 542  ? 0.2575 0.2576 0.2286 0.0229  0.0281  0.0598  540  LEU A C   
4045  O O   . LEU A 542  ? 0.2759 0.2695 0.2493 0.0218  0.0261  0.0584  540  LEU A O   
4046  C CB  . LEU A 542  ? 0.2789 0.2774 0.2493 0.0235  0.0301  0.0533  540  LEU A CB  
4047  C CG  . LEU A 542  ? 0.3230 0.3164 0.2969 0.0222  0.0301  0.0508  540  LEU A CG  
4048  C CD1 . LEU A 542  ? 0.2449 0.2348 0.2152 0.0235  0.0295  0.0442  540  LEU A CD1 
4049  C CD2 . LEU A 542  ? 0.2926 0.2800 0.2724 0.0197  0.0285  0.0524  540  LEU A CD2 
4050  N N   . PHE A 543  ? 0.2349 0.2420 0.2010 0.0248  0.0289  0.0608  541  PHE A N   
4051  C CA  . PHE A 543  ? 0.2595 0.2667 0.2224 0.0258  0.0274  0.0602  541  PHE A CA  
4052  C C   . PHE A 543  ? 0.2673 0.2793 0.2318 0.0252  0.0270  0.0674  541  PHE A C   
4053  O O   . PHE A 543  ? 0.2850 0.2989 0.2464 0.0262  0.0259  0.0678  541  PHE A O   
4054  C CB  . PHE A 543  ? 0.2575 0.2687 0.2133 0.0285  0.0280  0.0552  541  PHE A CB  
4055  C CG  . PHE A 543  ? 0.2198 0.2267 0.1747 0.0291  0.0282  0.0488  541  PHE A CG  
4056  C CD1 . PHE A 543  ? 0.2537 0.2519 0.2109 0.0277  0.0267  0.0453  541  PHE A CD1 
4057  C CD2 . PHE A 543  ? 0.2400 0.2517 0.1919 0.0310  0.0299  0.0463  541  PHE A CD2 
4058  C CE1 . PHE A 543  ? 0.2663 0.2609 0.2231 0.0280  0.0267  0.0402  541  PHE A CE1 
4059  C CE2 . PHE A 543  ? 0.2562 0.2635 0.2079 0.0314  0.0299  0.0408  541  PHE A CE2 
4060  C CZ  . PHE A 543  ? 0.2509 0.2496 0.2050 0.0298  0.0282  0.0380  541  PHE A CZ  
4061  N N   . GLY A 544  ? 0.2385 0.2524 0.2082 0.0234  0.0277  0.0733  542  GLY A N   
4062  C CA  . GLY A 544  ? 0.2642 0.2819 0.2369 0.0224  0.0270  0.0810  542  GLY A CA  
4063  C C   . GLY A 544  ? 0.2784 0.3061 0.2451 0.0243  0.0280  0.0835  542  GLY A C   
4064  O O   . GLY A 544  ? 0.2832 0.3181 0.2453 0.0261  0.0302  0.0819  542  GLY A O   
4065  N N   . ASP A 545  ? 0.3150 0.3436 0.2818 0.0243  0.0263  0.0870  543  ASP A N   
4066  C CA  . ASP A 545  ? 0.3577 0.3963 0.3192 0.0259  0.0269  0.0904  543  ASP A CA  
4067  C C   . ASP A 545  ? 0.3257 0.3667 0.2791 0.0289  0.0272  0.0832  543  ASP A C   
4068  O O   . ASP A 545  ? 0.3606 0.4113 0.3086 0.0307  0.0281  0.0847  543  ASP A O   
4069  C CB  . ASP A 545  ? 0.3569 0.3951 0.3216 0.0248  0.0246  0.0966  543  ASP A CB  
4070  C CG  . ASP A 545  ? 0.4824 0.5210 0.4553 0.0221  0.0242  0.1051  543  ASP A CG  
4071  O OD1 . ASP A 545  ? 0.5361 0.5797 0.5105 0.0213  0.0262  0.1072  543  ASP A OD1 
4072  O OD2 . ASP A 545  ? 0.6604 0.6941 0.6390 0.0205  0.0216  0.1085  543  ASP A OD2 
4073  N N   . ALA A 546  ? 0.3045 0.3373 0.2569 0.0293  0.0263  0.0757  544  ALA A N   
4074  C CA  . ALA A 546  ? 0.3066 0.3405 0.2522 0.0318  0.0259  0.0690  544  ALA A CA  
4075  C C   . ALA A 546  ? 0.3153 0.3567 0.2559 0.0341  0.0282  0.0659  544  ALA A C   
4076  O O   . ALA A 546  ? 0.3040 0.3528 0.2386 0.0365  0.0285  0.0642  544  ALA A O   
4077  C CB  . ALA A 546  ? 0.3051 0.3285 0.2518 0.0313  0.0243  0.0624  544  ALA A CB  
4078  N N   . ARG A 547  ? 0.2607 0.3007 0.2037 0.0335  0.0299  0.0649  545  ARG A N   
4079  C CA  A ARG A 547  ? 0.2814 0.3285 0.2204 0.0359  0.0320  0.0617  545  ARG A CA  
4080  C CA  B ARG A 547  ? 0.2816 0.3280 0.2205 0.0359  0.0319  0.0612  545  ARG A CA  
4081  C C   . ARG A 547  ? 0.2473 0.2929 0.1908 0.0345  0.0337  0.0630  545  ARG A C   
4082  O O   . ARG A 547  ? 0.2427 0.2806 0.1920 0.0320  0.0329  0.0646  545  ARG A O   
4083  C CB  A ARG A 547  ? 0.3062 0.3503 0.2405 0.0382  0.0312  0.0528  545  ARG A CB  
4084  C CB  B ARG A 547  ? 0.2958 0.3379 0.2308 0.0379  0.0309  0.0521  545  ARG A CB  
4085  C CG  A ARG A 547  ? 0.2982 0.3306 0.2356 0.0367  0.0296  0.0483  545  ARG A CG  
4086  C CG  B ARG A 547  ? 0.3033 0.3340 0.2421 0.0363  0.0299  0.0482  545  ARG A CG  
4087  C CD  A ARG A 547  ? 0.3197 0.3499 0.2529 0.0389  0.0285  0.0403  545  ARG A CD  
4088  C CD  B ARG A 547  ? 0.2916 0.3190 0.2270 0.0382  0.0289  0.0398  545  ARG A CD  
4089  N NE  A ARG A 547  ? 0.2747 0.2943 0.2107 0.0373  0.0268  0.0367  545  ARG A NE  
4090  N NE  B ARG A 547  ? 0.3125 0.3300 0.2516 0.0364  0.0279  0.0366  545  ARG A NE  
4091  C CZ  A ARG A 547  ? 0.2676 0.2818 0.2058 0.0368  0.0269  0.0331  545  ARG A CZ  
4092  C CZ  B ARG A 547  ? 0.2222 0.2323 0.1635 0.0347  0.0260  0.0362  545  ARG A CZ  
4093  N NH1 A ARG A 547  ? 0.2493 0.2671 0.1873 0.0380  0.0287  0.0319  545  ARG A NH1 
4094  N NH1 B ARG A 547  ? 0.2564 0.2672 0.1968 0.0344  0.0247  0.0386  545  ARG A NH1 
4095  N NH2 A ARG A 547  ? 0.2956 0.3012 0.2363 0.0351  0.0253  0.0306  545  ARG A NH2 
4096  N NH2 B ARG A 547  ? 0.2444 0.2467 0.1888 0.0332  0.0253  0.0335  545  ARG A NH2 
4097  N N   . THR A 548  ? 0.2401 0.2940 0.1811 0.0365  0.0359  0.0621  546  THR A N   
4098  C CA  . THR A 548  ? 0.2345 0.2887 0.1793 0.0356  0.0377  0.0632  546  THR A CA  
4099  C C   . THR A 548  ? 0.2219 0.2693 0.1662 0.0367  0.0374  0.0552  546  THR A C   
4100  O O   . THR A 548  ? 0.2069 0.2562 0.1462 0.0395  0.0372  0.0491  546  THR A O   
4101  C CB  . THR A 548  ? 0.2144 0.2817 0.1570 0.0373  0.0404  0.0664  546  THR A CB  
4102  O OG1 . THR A 548  ? 0.2886 0.3629 0.2320 0.0361  0.0406  0.0746  546  THR A OG1 
4103  C CG2 . THR A 548  ? 0.2506 0.3185 0.1977 0.0364  0.0422  0.0675  546  THR A CG2 
4104  N N   . ASN A 549  ? 0.1968 0.2363 0.1464 0.0344  0.0371  0.0553  547  ASN A N   
4105  C CA  . ASN A 549  ? 0.1861 0.2194 0.1359 0.0350  0.0367  0.0487  547  ASN A CA  
4106  C C   . ASN A 549  ? 0.1898 0.2305 0.1374 0.0376  0.0388  0.0463  547  ASN A C   
4107  O O   . ASN A 549  ? 0.2231 0.2722 0.1716 0.0378  0.0409  0.0509  547  ASN A O   
4108  C CB  . ASN A 549  ? 0.2057 0.2307 0.1617 0.0319  0.0361  0.0501  547  ASN A CB  
4109  C CG  . ASN A 549  ? 0.2057 0.2228 0.1620 0.0321  0.0350  0.0437  547  ASN A CG  
4110  O OD1 . ASN A 549  ? 0.1965 0.2129 0.1488 0.0342  0.0343  0.0382  547  ASN A OD1 
4111  N ND2 . ASN A 549  ? 0.2115 0.2225 0.1728 0.0297  0.0346  0.0445  547  ASN A ND2 
4112  N N   . SER A 550  ? 0.1943 0.2322 0.1394 0.0398  0.0381  0.0391  548  SER A N   
4113  C CA  . SER A 550  ? 0.1955 0.2389 0.1399 0.0423  0.0398  0.0361  548  SER A CA  
4114  C C   . SER A 550  ? 0.2246 0.2655 0.1745 0.0403  0.0408  0.0385  548  SER A C   
4115  O O   . SER A 550  ? 0.2073 0.2399 0.1612 0.0374  0.0397  0.0400  548  SER A O   
4116  C CB  . SER A 550  ? 0.1961 0.2354 0.1378 0.0447  0.0382  0.0278  548  SER A CB  
4117  O OG  . SER A 550  ? 0.2067 0.2347 0.1515 0.0425  0.0363  0.0258  548  SER A OG  
4118  N N   . ALA A 551  ? 0.2025 0.2512 0.1527 0.0421  0.0430  0.0387  549  ALA A N   
4119  C CA  . ALA A 551  ? 0.2217 0.2691 0.1771 0.0405  0.0440  0.0408  549  ALA A CA  
4120  C C   . ALA A 551  ? 0.2112 0.2558 0.1668 0.0426  0.0437  0.0342  549  ALA A C   
4121  O O   . ALA A 551  ? 0.2098 0.2586 0.1616 0.0461  0.0438  0.0292  549  ALA A O   
4122  C CB  . ALA A 551  ? 0.2348 0.2934 0.1915 0.0406  0.0467  0.0466  549  ALA A CB  
4123  N N   . GLY A 552  ? 0.1972 0.2347 0.1574 0.0405  0.0431  0.0343  550  GLY A N   
4124  C CA  . GLY A 552  ? 0.2264 0.2610 0.1878 0.0421  0.0427  0.0292  550  GLY A CA  
4125  C C   . GLY A 552  ? 0.2178 0.2587 0.1825 0.0425  0.0449  0.0314  550  GLY A C   
4126  O O   . GLY A 552  ? 0.2485 0.2984 0.2134 0.0425  0.0470  0.0361  550  GLY A O   
4127  N N   . LEU A 553  ? 0.2330 0.2695 0.2006 0.0428  0.0443  0.0283  551  LEU A N   
4128  C CA  . LEU A 553  ? 0.2114 0.2531 0.1826 0.0433  0.0460  0.0297  551  LEU A CA  
4129  C C   . LEU A 553  ? 0.2293 0.2625 0.2052 0.0407  0.0447  0.0299  551  LEU A C   
4130  O O   . LEU A 553  ? 0.2535 0.2780 0.2291 0.0402  0.0425  0.0263  551  LEU A O   
4131  C CB  . LEU A 553  ? 0.2375 0.2850 0.2068 0.0479  0.0467  0.0242  551  LEU A CB  
4132  C CG  . LEU A 553  ? 0.2392 0.2974 0.2038 0.0510  0.0483  0.0236  551  LEU A CG  
4133  C CD1 . LEU A 553  ? 0.2919 0.3544 0.2550 0.0558  0.0483  0.0168  551  LEU A CD1 
4134  C CD2 . LEU A 553  ? 0.2635 0.3319 0.2295 0.0499  0.0511  0.0305  551  LEU A CD2 
4135  N N   . ASP A 554  ? 0.2072 0.2434 0.1876 0.0390  0.0461  0.0341  552  ASP A N   
4136  C CA  . ASP A 554  ? 0.1978 0.2270 0.1828 0.0363  0.0449  0.0347  552  ASP A CA  
4137  C C   . ASP A 554  ? 0.1963 0.2264 0.1832 0.0386  0.0450  0.0312  552  ASP A C   
4138  O O   . ASP A 554  ? 0.2074 0.2450 0.1966 0.0396  0.0469  0.0329  552  ASP A O   
4139  C CB  . ASP A 554  ? 0.2219 0.2530 0.2113 0.0330  0.0459  0.0412  552  ASP A CB  
4140  C CG  . ASP A 554  ? 0.2381 0.2622 0.2321 0.0302  0.0444  0.0416  552  ASP A CG  
4141  O OD1 . ASP A 554  ? 0.2316 0.2496 0.2253 0.0307  0.0428  0.0373  552  ASP A OD1 
4142  O OD2 . ASP A 554  ? 0.2365 0.2615 0.2348 0.0274  0.0448  0.0463  552  ASP A OD2 
4143  N N   . LEU A 555  ? 0.1975 0.2203 0.1840 0.0393  0.0428  0.0265  553  LEU A N   
4144  C CA  . LEU A 555  ? 0.1863 0.2094 0.1750 0.0415  0.0425  0.0230  553  LEU A CA  
4145  C C   . LEU A 555  ? 0.1999 0.2204 0.1939 0.0391  0.0422  0.0255  553  LEU A C   
4146  O O   . LEU A 555  ? 0.2179 0.2373 0.2142 0.0405  0.0415  0.0228  553  LEU A O   
4147  C CB  . LEU A 555  ? 0.1766 0.1930 0.1634 0.0432  0.0400  0.0173  553  LEU A CB  
4148  C CG  . LEU A 555  ? 0.2095 0.2286 0.1913 0.0461  0.0399  0.0139  553  LEU A CG  
4149  C CD1 . LEU A 555  ? 0.2854 0.2975 0.2663 0.0476  0.0371  0.0083  553  LEU A CD1 
4150  C CD2 . LEU A 555  ? 0.2443 0.2744 0.2250 0.0497  0.0423  0.0131  553  LEU A CD2 
4151  N N   . SER A 556  ? 0.1997 0.2194 0.1958 0.0355  0.0426  0.0303  554  SER A N   
4152  C CA  . SER A 556  ? 0.1805 0.1999 0.1817 0.0333  0.0427  0.0330  554  SER A CA  
4153  C C   . SER A 556  ? 0.1980 0.2266 0.2019 0.0332  0.0452  0.0374  554  SER A C   
4154  O O   . SER A 556  ? 0.2045 0.2340 0.2132 0.0314  0.0454  0.0399  554  SER A O   
4155  C CB  . SER A 556  ? 0.2030 0.2152 0.2059 0.0293  0.0410  0.0351  554  SER A CB  
4156  O OG  . SER A 556  ? 0.2159 0.2300 0.2189 0.0272  0.0418  0.0393  554  SER A OG  
4157  N N   . ASN A 557  ? 0.1958 0.2318 0.1970 0.0350  0.0471  0.0384  555  ASN A N   
4158  C CA  . ASN A 557  ? 0.1770 0.2228 0.1806 0.0348  0.0496  0.0433  555  ASN A CA  
4159  C C   . ASN A 557  ? 0.1813 0.2352 0.1850 0.0387  0.0513  0.0407  555  ASN A C   
4160  O O   . ASN A 557  ? 0.1755 0.2321 0.1751 0.0423  0.0516  0.0365  555  ASN A O   
4161  C CB  . ASN A 557  ? 0.2008 0.2508 0.2011 0.0344  0.0507  0.0464  555  ASN A CB  
4162  C CG  . ASN A 557  ? 0.1893 0.2499 0.1923 0.0337  0.0532  0.0524  555  ASN A CG  
4163  O OD1 . ASN A 557  ? 0.2158 0.2852 0.2197 0.0361  0.0552  0.0521  555  ASN A OD1 
4164  N ND2 . ASN A 557  ? 0.2232 0.2833 0.2279 0.0304  0.0531  0.0580  555  ASN A ND2 
4165  N N   . GLU A 558  ? 0.1940 0.2520 0.2028 0.0381  0.0523  0.0430  556  GLU A N   
4166  C CA  . GLU A 558  ? 0.1911 0.2569 0.2008 0.0420  0.0538  0.0402  556  GLU A CA  
4167  C C   . GLU A 558  ? 0.1988 0.2765 0.2055 0.0448  0.0565  0.0410  556  GLU A C   
4168  O O   . GLU A 558  ? 0.2133 0.2962 0.2183 0.0492  0.0572  0.0363  556  GLU A O   
4169  C CB  . GLU A 558  ? 0.2193 0.2881 0.2354 0.0406  0.0544  0.0430  556  GLU A CB  
4170  C CG  . GLU A 558  ? 0.2050 0.2640 0.2242 0.0387  0.0518  0.0415  556  GLU A CG  
4171  C CD  . GLU A 558  ? 0.2104 0.2641 0.2281 0.0418  0.0500  0.0351  556  GLU A CD  
4172  O OE1 . GLU A 558  ? 0.2154 0.2735 0.2307 0.0460  0.0506  0.0310  556  GLU A OE1 
4173  O OE2 . GLU A 558  ? 0.2009 0.2461 0.2204 0.0399  0.0476  0.0342  556  GLU A OE2 
4174  N N   . GLU A 559  ? 0.1706 0.2532 0.1770 0.0425  0.0579  0.0468  557  GLU A N   
4175  C CA  . GLU A 559  ? 0.1886 0.2832 0.1916 0.0451  0.0604  0.0479  557  GLU A CA  
4176  C C   . GLU A 559  ? 0.2005 0.2929 0.1969 0.0484  0.0595  0.0420  557  GLU A C   
4177  O O   . GLU A 559  ? 0.2396 0.3403 0.2331 0.0527  0.0608  0.0382  557  GLU A O   
4178  C CB  . GLU A 559  ? 0.2594 0.3586 0.2635 0.0416  0.0616  0.0558  557  GLU A CB  
4179  C CG  . GLU A 559  ? 0.2687 0.3718 0.2797 0.0383  0.0626  0.0623  557  GLU A CG  
4180  C CD  . GLU A 559  ? 0.3559 0.4613 0.3685 0.0345  0.0630  0.0701  557  GLU A CD  
4181  O OE1 . GLU A 559  ? 0.4732 0.5785 0.4812 0.0347  0.0628  0.0707  557  GLU A OE1 
4182  O OE2 . GLU A 559  ? 0.3366 0.4438 0.3554 0.0311  0.0633  0.0759  557  GLU A OE2 
4183  N N   . THR A 560  ? 0.1896 0.2710 0.1838 0.0464  0.0571  0.0409  558  THR A N   
4184  C CA  . THR A 560  ? 0.2081 0.2864 0.1966 0.0491  0.0558  0.0354  558  THR A CA  
4185  C C   . THR A 560  ? 0.2147 0.2907 0.2029 0.0530  0.0547  0.0279  558  THR A C   
4186  O O   . THR A 560  ? 0.2094 0.2899 0.1937 0.0570  0.0548  0.0230  558  THR A O   
4187  C CB  . THR A 560  ? 0.2035 0.2701 0.1906 0.0459  0.0533  0.0359  558  THR A CB  
4188  O OG1 . THR A 560  ? 0.2337 0.3023 0.2216 0.0425  0.0541  0.0427  558  THR A OG1 
4189  C CG2 . THR A 560  ? 0.2306 0.2939 0.2122 0.0484  0.0519  0.0303  558  THR A CG2 
4190  N N   . LEU A 561  ? 0.1930 0.2621 0.1855 0.0519  0.0532  0.0268  559  LEU A N   
4191  C CA  . LEU A 561  ? 0.1777 0.2441 0.1709 0.0554  0.0518  0.0201  559  LEU A CA  
4192  C C   . LEU A 561  ? 0.2261 0.3044 0.2197 0.0599  0.0540  0.0178  559  LEU A C   
4193  O O   . LEU A 561  ? 0.2216 0.3008 0.2135 0.0642  0.0531  0.0112  559  LEU A O   
4194  C CB  . LEU A 561  ? 0.1841 0.2419 0.1822 0.0532  0.0499  0.0203  559  LEU A CB  
4195  C CG  . LEU A 561  ? 0.1980 0.2438 0.1953 0.0495  0.0473  0.0210  559  LEU A CG  
4196  C CD1 . LEU A 561  ? 0.1903 0.2295 0.1924 0.0471  0.0458  0.0220  559  LEU A CD1 
4197  C CD2 . LEU A 561  ? 0.1921 0.2320 0.1854 0.0516  0.0451  0.0153  559  LEU A CD2 
4198  N N   . ALA A 562  ? 0.1966 0.2845 0.1928 0.0591  0.0567  0.0229  560  ALA A N   
4199  C CA  . ALA A 562  ? 0.2144 0.3148 0.2113 0.0633  0.0590  0.0209  560  ALA A CA  
4200  C C   . ALA A 562  ? 0.2248 0.3344 0.2160 0.0667  0.0605  0.0186  560  ALA A C   
4201  O O   . ALA A 562  ? 0.2384 0.3543 0.2284 0.0718  0.0608  0.0126  560  ALA A O   
4202  C CB  . ALA A 562  ? 0.2277 0.3364 0.2294 0.0612  0.0616  0.0275  560  ALA A CB  
4203  N N   . SER A 563  ? 0.2260 0.3369 0.2138 0.0642  0.0611  0.0232  561  SER A N   
4204  C CA  . SER A 563  ? 0.2591 0.3793 0.2411 0.0673  0.0624  0.0213  561  SER A CA  
4205  C C   . SER A 563  ? 0.2238 0.3367 0.2016 0.0702  0.0597  0.0134  561  SER A C   
4206  O O   . SER A 563  ? 0.2637 0.3843 0.2381 0.0749  0.0602  0.0080  561  SER A O   
4207  C CB  . SER A 563  ? 0.2614 0.3850 0.2414 0.0636  0.0637  0.0290  561  SER A CB  
4208  O OG  . SER A 563  ? 0.3422 0.4530 0.3209 0.0602  0.0612  0.0299  561  SER A OG  
4209  N N   . LEU A 564  ? 0.2486 0.3470 0.2271 0.0675  0.0567  0.0124  562  LEU A N   
4210  C CA  A LEU A 564  ? 0.2353 0.3261 0.2109 0.0698  0.0538  0.0051  562  LEU A CA  
4211  C CA  B LEU A 564  ? 0.2354 0.3260 0.2111 0.0698  0.0538  0.0051  562  LEU A CA  
4212  C C   . LEU A 564  ? 0.2334 0.3251 0.2113 0.0745  0.0528  -0.0022 562  LEU A C   
4213  O O   . LEU A 564  ? 0.2419 0.3355 0.2169 0.0787  0.0517  -0.0090 562  LEU A O   
4214  C CB  A LEU A 564  ? 0.2511 0.3270 0.2278 0.0657  0.0509  0.0062  562  LEU A CB  
4215  C CB  B LEU A 564  ? 0.2512 0.3268 0.2281 0.0657  0.0509  0.0060  562  LEU A CB  
4216  C CG  A LEU A 564  ? 0.2388 0.3060 0.2124 0.0668  0.0478  0.0003  562  LEU A CG  
4217  C CG  B LEU A 564  ? 0.2404 0.3116 0.2131 0.0631  0.0501  0.0084  562  LEU A CG  
4218  C CD1 A LEU A 564  ? 0.2576 0.3314 0.2252 0.0687  0.0485  -0.0008 562  LEU A CD1 
4219  C CD1 B LEU A 564  ? 0.2310 0.2882 0.2056 0.0594  0.0473  0.0087  562  LEU A CD1 
4220  C CD2 A LEU A 564  ? 0.2147 0.2689 0.1896 0.0622  0.0455  0.0028  562  LEU A CD2 
4221  C CD2 B LEU A 564  ? 0.2647 0.3393 0.2321 0.0668  0.0493  0.0028  562  LEU A CD2 
4222  N N   . THR A 565  ? 0.2219 0.3124 0.2054 0.0740  0.0530  -0.0011 563  THR A N   
4223  C CA  . THR A 565  ? 0.2387 0.3304 0.2252 0.0786  0.0520  -0.0077 563  THR A CA  
4224  C C   . THR A 565  ? 0.2378 0.3434 0.2214 0.0840  0.0540  -0.0120 563  THR A C   
4225  O O   . THR A 565  ? 0.2654 0.3704 0.2482 0.0886  0.0521  -0.0199 563  THR A O   
4226  C CB  . THR A 565  ? 0.2073 0.2990 0.2001 0.0773  0.0527  -0.0047 563  THR A CB  
4227  O OG1 . THR A 565  ? 0.2353 0.3138 0.2308 0.0729  0.0503  -0.0022 563  THR A OG1 
4228  C CG2 . THR A 565  ? 0.2481 0.3430 0.2443 0.0825  0.0520  -0.0113 563  THR A CG2 
4229  N N   . GLU A 566  ? 0.2515 0.3698 0.2334 0.0836  0.0576  -0.0069 564  GLU A N   
4230  C CA  . GLU A 566  ? 0.2531 0.3865 0.2322 0.0888  0.0599  -0.0106 564  GLU A CA  
4231  C C   . GLU A 566  ? 0.2553 0.3896 0.2279 0.0909  0.0587  -0.0150 564  GLU A C   
4232  O O   . GLU A 566  ? 0.2568 0.3944 0.2281 0.0946  0.0569  -0.0221 564  GLU A O   
4233  C CB  . GLU A 566  ? 0.2944 0.4411 0.2739 0.0869  0.0637  -0.0029 564  GLU A CB  
4234  C CG  . GLU A 566  ? 0.2977 0.4461 0.2839 0.0857  0.0652  0.0009  564  GLU A CG  
4235  C CD  . GLU A 566  ? 0.4495 0.5979 0.4395 0.0901  0.0638  -0.0064 564  GLU A CD  
4236  O OE1 . GLU A 566  ? 0.4759 0.6307 0.4638 0.0935  0.0629  -0.0122 564  GLU A OE1 
4237  O OE2 . GLU A 566  ? 0.4421 0.5820 0.4374 0.0890  0.0625  -0.0064 564  GLU A OE2 
4238  N N   . ALA A 567  ? 0.2440 0.3723 0.2132 0.0869  0.0581  -0.0106 565  ALA A N   
4239  C CA  . ALA A 567  ? 0.2436 0.3729 0.2067 0.0887  0.0570  -0.0145 565  ALA A CA  
4240  C C   . ALA A 567  ? 0.2442 0.3626 0.2076 0.0913  0.0529  -0.0233 565  ALA A C   
4241  O O   . ALA A 567  ? 0.2681 0.3896 0.2281 0.0947  0.0514  -0.0297 565  ALA A O   
4242  C CB  . ALA A 567  ? 0.2627 0.3877 0.2229 0.0836  0.0571  -0.0074 565  ALA A CB  
4243  N N   . LEU A 568  ? 0.2348 0.3395 0.2028 0.0888  0.0504  -0.0234 566  LEU A N   
4244  C CA  . LEU A 568  ? 0.2338 0.3280 0.2032 0.0909  0.0463  -0.0311 566  LEU A CA  
4245  C C   . LEU A 568  ? 0.2497 0.3504 0.2214 0.0971  0.0459  -0.0391 566  LEU A C   
4246  O O   . LEU A 568  ? 0.2549 0.3544 0.2249 0.1007  0.0433  -0.0468 566  LEU A O   
4247  C CB  . LEU A 568  ? 0.2351 0.3146 0.2093 0.0866  0.0440  -0.0285 566  LEU A CB  
4248  C CG  . LEU A 568  ? 0.2582 0.3299 0.2303 0.0808  0.0437  -0.0220 566  LEU A CG  
4249  C CD1 . LEU A 568  ? 0.2516 0.3110 0.2287 0.0769  0.0418  -0.0193 566  LEU A CD1 
4250  C CD2 . LEU A 568  ? 0.2732 0.3411 0.2406 0.0812  0.0416  -0.0254 566  LEU A CD2 
4251  N N   . ARG A 569  ? 0.2435 0.3507 0.2193 0.0982  0.0481  -0.0374 567  ARG A N   
4252  C CA  . ARG A 569  ? 0.2525 0.3651 0.2311 0.1026  0.0470  -0.0440 567  ARG A CA  
4253  C C   . ARG A 569  ? 0.2940 0.4166 0.2678 0.1045  0.0469  -0.0475 567  ARG A C   
4254  O O   . ARG A 569  ? 0.2928 0.4146 0.2672 0.1078  0.0439  -0.0553 567  ARG A O   
4255  C CB  . ARG A 569  ? 0.3240 0.4437 0.3072 0.1025  0.0497  -0.0401 567  ARG A CB  
4256  C CG  . ARG A 569  ? 0.3469 0.4569 0.3363 0.1015  0.0488  -0.0387 567  ARG A CG  
4257  C CD  . ARG A 569  ? 0.4541 0.5725 0.4481 0.1017  0.0516  -0.0350 567  ARG A CD  
4258  N NE  . ARG A 569  ? 0.4383 0.5459 0.4378 0.0979  0.0502  -0.0309 567  ARG A NE  
4259  C CZ  . ARG A 569  ? 0.4840 0.5961 0.4880 0.0966  0.0522  -0.0264 567  ARG A CZ  
4260  N NH1 . ARG A 569  ? 0.5474 0.6746 0.5513 0.0988  0.0559  -0.0248 567  ARG A NH1 
4261  N NH2 . ARG A 569  ? 0.4813 0.5830 0.4899 0.0931  0.0504  -0.0232 567  ARG A NH2 
4262  N N   . GLU A 570  ? 0.2608 0.3928 0.2300 0.1024  0.0499  -0.0415 568  GLU A N   
4263  C CA  . GLU A 570  ? 0.2870 0.4294 0.2514 0.1042  0.0498  -0.0440 568  GLU A CA  
4264  C C   . GLU A 570  ? 0.3179 0.4537 0.2785 0.1052  0.0464  -0.0495 568  GLU A C   
4265  O O   . GLU A 570  ? 0.3335 0.4744 0.2922 0.1082  0.0446  -0.0557 568  GLU A O   
4266  C CB  . GLU A 570  ? 0.3157 0.4688 0.2767 0.1013  0.0534  -0.0352 568  GLU A CB  
4267  C CG  . GLU A 570  ? 0.4045 0.5668 0.3692 0.1008  0.0564  -0.0306 568  GLU A CG  
4268  C CD  . GLU A 570  ? 0.4888 0.6578 0.4521 0.0966  0.0596  -0.0202 568  GLU A CD  
4269  O OE1 . GLU A 570  ? 0.5042 0.6686 0.4644 0.0937  0.0597  -0.0162 568  GLU A OE1 
4270  O OE2 . GLU A 570  ? 0.5604 0.7390 0.5261 0.0960  0.0619  -0.0160 568  GLU A OE2 
4271  N N   . SER A 571  ? 0.2945 0.4194 0.2542 0.1027  0.0455  -0.0477 569  SER A N   
4272  C CA  . SER A 571  ? 0.3075 0.4255 0.2640 0.1034  0.0421  -0.0529 569  SER A CA  
4273  C C   . SER A 571  ? 0.2904 0.4015 0.2509 0.1066  0.0379  -0.0621 569  SER A C   
4274  O O   . SER A 571  ? 0.3246 0.4349 0.2830 0.1083  0.0350  -0.0680 569  SER A O   
4275  C CB  . SER A 571  ? 0.2935 0.4008 0.2487 0.1000  0.0420  -0.0489 569  SER A CB  
4276  O OG  . SER A 571  ? 0.3260 0.4210 0.2864 0.1000  0.0400  -0.0508 569  SER A OG  
4277  N N   . ALA A 572  ? 0.3104 0.4166 0.2771 0.1074  0.0374  -0.0633 570  ALA A N   
4278  C CA  . ALA A 572  ? 0.2986 0.3972 0.2700 0.1101  0.0331  -0.0713 570  ALA A CA  
4279  C C   . ALA A 572  ? 0.3446 0.4531 0.3166 0.1140  0.0324  -0.0770 570  ALA A C   
4280  O O   . ALA A 572  ? 0.3621 0.4657 0.3371 0.1165  0.0284  -0.0844 570  ALA A O   
4281  C CB  . ALA A 572  ? 0.3393 0.4288 0.3175 0.1095  0.0324  -0.0700 570  ALA A CB  
4282  N N   . ALA A 573  ? 0.3224 0.4448 0.2918 0.1144  0.0361  -0.0736 571  ALA A N   
4283  C CA  . ALA A 573  ? 0.3491 0.4827 0.3182 0.1182  0.0358  -0.0785 571  ALA A CA  
4284  C C   . ALA A 573  ? 0.3915 0.5318 0.3546 0.1194  0.0347  -0.0815 571  ALA A C   
4285  O O   . ALA A 573  ? 0.4556 0.6061 0.4179 0.1227  0.0344  -0.0859 571  ALA A O   
4286  C CB  . ALA A 573  ? 0.3553 0.5012 0.3247 0.1180  0.0402  -0.0729 571  ALA A CB  
4287  N N   . MET A 574  ? 0.3405 0.4757 0.2996 0.1170  0.0342  -0.0795 572  MET A N   
4288  C CA  . MET A 574  ? 0.3647 0.5064 0.3181 0.1178  0.0333  -0.0816 572  MET A CA  
4289  C C   . MET A 574  ? 0.3832 0.5171 0.3378 0.1201  0.0281  -0.0905 572  MET A C   
4290  O O   . MET A 574  ? 0.3445 0.4650 0.3035 0.1194  0.0253  -0.0930 572  MET A O   
4291  C CB  . MET A 574  ? 0.3706 0.5113 0.3189 0.1140  0.0352  -0.0744 572  MET A CB  
4292  C CG  . MET A 574  ? 0.3833 0.5337 0.3297 0.1117  0.0400  -0.0653 572  MET A CG  
4293  S SD  . MET A 574  ? 0.4630 0.6090 0.4053 0.1068  0.0418  -0.0566 572  MET A SD  
4294  C CE  . MET A 574  ? 0.5352 0.6950 0.4767 0.1046  0.0468  -0.0466 572  MET A CE  
4295  N N   . LYS A 575  ? 0.3738 0.5166 0.3250 0.1227  0.0268  -0.0950 573  LYS A N   
4296  C CA  . LYS A 575  ? 0.3809 0.5181 0.3332 0.1249  0.0218  -0.1036 573  LYS A CA  
4297  C C   . LYS A 575  ? 0.3632 0.4962 0.3109 0.1225  0.0207  -0.1021 573  LYS A C   
4298  O O   . LYS A 575  ? 0.4139 0.5559 0.3566 0.1235  0.0207  -0.1029 573  LYS A O   
4299  C CB  . LYS A 575  ? 0.4181 0.5676 0.3698 0.1294  0.0207  -0.1099 573  LYS A CB  
4300  C CG  . LYS A 575  ? 0.4739 0.6278 0.4304 0.1320  0.0215  -0.1121 573  LYS A CG  
4301  C CD  . LYS A 575  ? 0.4922 0.6316 0.4560 0.1321  0.0183  -0.1157 573  LYS A CD  
4302  N N   . TRP A 576  ? 0.3488 0.4681 0.2983 0.1195  0.0197  -0.0998 574  TRP A N   
4303  C CA  . TRP A 576  ? 0.3205 0.4343 0.2661 0.1170  0.0186  -0.0982 574  TRP A CA  
4304  C C   . TRP A 576  ? 0.2686 0.3788 0.2148 0.1190  0.0136  -0.1064 574  TRP A C   
4305  O O   . TRP A 576  ? 0.3275 0.4308 0.2794 0.1207  0.0099  -0.1126 574  TRP A O   
4306  C CB  . TRP A 576  ? 0.3229 0.4230 0.2708 0.1134  0.0187  -0.0939 574  TRP A CB  
4307  C CG  . TRP A 576  ? 0.2709 0.3735 0.2183 0.1111  0.0234  -0.0856 574  TRP A CG  
4308  C CD1 . TRP A 576  ? 0.3249 0.4239 0.2773 0.1108  0.0247  -0.0838 574  TRP A CD1 
4309  C CD2 . TRP A 576  ? 0.2573 0.3664 0.1993 0.1085  0.0273  -0.0778 574  TRP A CD2 
4310  N NE1 . TRP A 576  ? 0.3091 0.4120 0.2596 0.1083  0.0291  -0.0754 574  TRP A NE1 
4311  C CE2 . TRP A 576  ? 0.2917 0.4008 0.2360 0.1068  0.0307  -0.0715 574  TRP A CE2 
4312  C CE3 . TRP A 576  ? 0.2696 0.3845 0.2055 0.1075  0.0280  -0.0753 574  TRP A CE3 
4313  C CZ2 . TRP A 576  ? 0.3239 0.4383 0.2648 0.1039  0.0347  -0.0627 574  TRP A CZ2 
4314  C CZ3 . TRP A 576  ? 0.3061 0.4262 0.2386 0.1046  0.0319  -0.0664 574  TRP A CZ3 
4315  C CH2 . TRP A 576  ? 0.3321 0.4518 0.2673 0.1028  0.0352  -0.0602 574  TRP A CH2 
4316  N N   . THR A 577  ? 0.2776 0.3926 0.2184 0.1187  0.0132  -0.1064 575  THR A N   
4317  C CA  . THR A 577  ? 0.2944 0.4062 0.2358 0.1203  0.0084  -0.1138 575  THR A CA  
4318  C C   . THR A 577  ? 0.3140 0.4218 0.2510 0.1175  0.0078  -0.1110 575  THR A C   
4319  O O   . THR A 577  ? 0.2972 0.4085 0.2296 0.1151  0.0114  -0.1037 575  THR A O   
4320  C CB  . THR A 577  ? 0.2835 0.4089 0.2232 0.1246  0.0075  -0.1194 575  THR A CB  
4321  O OG1 . THR A 577  ? 0.3478 0.4855 0.2806 0.1241  0.0105  -0.1147 575  THR A OG1 
4322  C CG2 . THR A 577  ? 0.3484 0.4798 0.2918 0.1276  0.0085  -0.1218 575  THR A CG2 
4323  N N   . ALA A 578  ? 0.3030 0.4034 0.2420 0.1179  0.0031  -0.1169 576  ALA A N   
4324  C CA  . ALA A 578  ? 0.2835 0.3805 0.2187 0.1158  0.0018  -0.1158 576  ALA A CA  
4325  C C   . ALA A 578  ? 0.3211 0.4213 0.2568 0.1186  -0.0026 -0.1238 576  ALA A C   
4326  O O   . ALA A 578  ? 0.3222 0.4170 0.2637 0.1205  -0.0065 -0.1305 576  ALA A O   
4327  C CB  . ALA A 578  ? 0.3025 0.3837 0.2408 0.1122  0.0001  -0.1138 576  ALA A CB  
4328  N N   . LEU A 579  ? 0.3105 0.4195 0.2404 0.1190  -0.0020 -0.1231 577  LEU A N   
4329  C CA  . LEU A 579  ? 0.3330 0.4476 0.2625 0.1220  -0.0057 -0.1303 577  LEU A CA  
4330  C C   . LEU A 579  ? 0.3274 0.4386 0.2534 0.1198  -0.0073 -0.1294 577  LEU A C   
4331  O O   . LEU A 579  ? 0.3119 0.4213 0.2340 0.1166  -0.0046 -0.1222 577  LEU A O   
4332  C CB  . LEU A 579  ? 0.3544 0.4865 0.2799 0.1253  -0.0033 -0.1308 577  LEU A CB  
4333  C CG  . LEU A 579  ? 0.3748 0.5129 0.3027 0.1275  -0.0010 -0.1308 577  LEU A CG  
4334  C CD1 . LEU A 579  ? 0.4622 0.6185 0.3857 0.1304  0.0013  -0.1308 577  LEU A CD1 
4335  C CD2 . LEU A 579  ? 0.4283 0.5590 0.3635 0.1298  -0.0051 -0.1388 577  LEU A CD2 
4336  N N   . PRO A 580  ? 0.3358 0.4464 0.2634 0.1216  -0.0119 -0.1365 578  PRO A N   
4337  C CA  . PRO A 580  ? 0.3184 0.4291 0.2420 0.1201  -0.0132 -0.1356 578  PRO A CA  
4338  C C   . PRO A 580  ? 0.3799 0.5062 0.2964 0.1212  -0.0097 -0.1318 578  PRO A C   
4339  O O   . PRO A 580  ? 0.3752 0.5131 0.2907 0.1249  -0.0103 -0.1363 578  PRO A O   
4340  C CB  . PRO A 580  ? 0.3493 0.4570 0.2772 0.1224  -0.0190 -0.1448 578  PRO A CB  
4341  C CG  . PRO A 580  ? 0.3457 0.4486 0.2808 0.1244  -0.0211 -0.1498 578  PRO A CG  
4342  C CD  . PRO A 580  ? 0.3165 0.4268 0.2497 0.1252  -0.0163 -0.1455 578  PRO A CD  
4343  N N   . GLN A 581  ? 0.3006 0.4275 0.2124 0.1180  -0.0060 -0.1233 579  GLN A N   
4344  C CA  . GLN A 581  ? 0.3331 0.4743 0.2386 0.1183  -0.0023 -0.1179 579  GLN A CA  
4345  C C   . GLN A 581  ? 0.3340 0.4765 0.2356 0.1173  -0.0040 -0.1176 579  GLN A C   
4346  O O   . GLN A 581  ? 0.3271 0.4640 0.2262 0.1139  -0.0029 -0.1117 579  GLN A O   
4347  C CB  . GLN A 581  ? 0.3167 0.4582 0.2201 0.1154  0.0027  -0.1083 579  GLN A CB  
4348  C CG  . GLN A 581  ? 0.2932 0.4342 0.2005 0.1163  0.0047  -0.1081 579  GLN A CG  
4349  C CD  . GLN A 581  ? 0.3688 0.5249 0.2753 0.1200  0.0061  -0.1102 579  GLN A CD  
4350  O OE1 . GLN A 581  ? 0.3908 0.5585 0.2938 0.1220  0.0057  -0.1115 579  GLN A OE1 
4351  N NE2 . GLN A 581  ? 0.3668 0.5232 0.2768 0.1211  0.0076  -0.1104 579  GLN A NE2 
4352  N N   . LEU A 582  ? 0.3271 0.4773 0.2283 0.1206  -0.0069 -0.1241 580  LEU A N   
4353  C CA  . LEU A 582  ? 0.3349 0.4875 0.2326 0.1201  -0.0087 -0.1244 580  LEU A CA  
4354  C C   . LEU A 582  ? 0.3674 0.5343 0.2587 0.1199  -0.0050 -0.1175 580  LEU A C   
4355  O O   . LEU A 582  ? 0.3430 0.5189 0.2330 0.1205  -0.0012 -0.1132 580  LEU A O   
4356  C CB  . LEU A 582  ? 0.3337 0.4882 0.2341 0.1236  -0.0136 -0.1345 580  LEU A CB  
4357  C CG  . LEU A 582  ? 0.4650 0.6040 0.3710 0.1225  -0.0185 -0.1403 580  LEU A CG  
4358  C CD1 . LEU A 582  ? 0.4218 0.5495 0.3336 0.1216  -0.0187 -0.1409 580  LEU A CD1 
4359  C CD2 . LEU A 582  ? 0.4499 0.5926 0.3585 0.1261  -0.0233 -0.1498 580  LEU A CD2 
4360  N N   . ALA A 583  ? 0.3329 0.5019 0.2206 0.1189  -0.0060 -0.1161 581  ALA A N   
4361  C CA  . ALA A 583  ? 0.3612 0.5438 0.2433 0.1186  -0.0029 -0.1095 581  ALA A CA  
4362  C C   . ALA A 583  ? 0.3816 0.5804 0.2628 0.1228  -0.0023 -0.1126 581  ALA A C   
4363  O O   . ALA A 583  ? 0.4639 0.6744 0.3421 0.1227  0.0014  -0.1060 581  ALA A O   
4364  C CB  . ALA A 583  ? 0.3560 0.5383 0.2349 0.1174  -0.0050 -0.1088 581  ALA A CB  
4365  N N   . THR A 584  ? 0.3424 0.5422 0.2268 0.1265  -0.0059 -0.1224 582  THR A N   
4366  C CA  . THR A 584  ? 0.3907 0.6058 0.2747 0.1310  -0.0061 -0.1271 582  THR A CA  
4367  C C   . THR A 584  ? 0.3631 0.5814 0.2496 0.1326  -0.0038 -0.1273 582  THR A C   
4368  O O   . THR A 584  ? 0.4019 0.6344 0.2877 0.1362  -0.0032 -0.1299 582  THR A O   
4369  C CB  . THR A 584  ? 0.4335 0.6473 0.3203 0.1343  -0.0114 -0.1382 582  THR A CB  
4370  O OG1 . THR A 584  ? 0.4242 0.6219 0.3168 0.1335  -0.0143 -0.1431 582  THR A OG1 
4371  C CG2 . THR A 584  ? 0.4412 0.6562 0.3248 0.1335  -0.0135 -0.1384 582  THR A CG2 
4372  N N   . GLY A 585  ? 0.3914 0.5974 0.2810 0.1301  -0.0027 -0.1247 583  GLY A N   
4373  C CA  . GLY A 585  ? 0.3837 0.5910 0.2763 0.1314  -0.0008 -0.1252 583  GLY A CA  
4374  C C   . GLY A 585  ? 0.3995 0.5910 0.2981 0.1311  -0.0036 -0.1305 583  GLY A C   
4375  O O   . GLY A 585  ? 0.4090 0.5885 0.3096 0.1297  -0.0070 -0.1336 583  GLY A O   
4376  N N   . PRO A 586  ? 0.3353 0.5266 0.2373 0.1323  -0.0022 -0.1313 584  PRO A N   
4377  C CA  . PRO A 586  ? 0.3488 0.5258 0.2572 0.1322  -0.0050 -0.1364 584  PRO A CA  
4378  C C   . PRO A 586  ? 0.4275 0.6026 0.3396 0.1355  -0.0105 -0.1470 584  PRO A C   
4379  O O   . PRO A 586  ? 0.4128 0.6004 0.3235 0.1392  -0.0117 -0.1517 584  PRO A O   
4380  C CB  . PRO A 586  ? 0.4428 0.6241 0.3533 0.1336  -0.0022 -0.1351 584  PRO A CB  
4381  C CG  . PRO A 586  ? 0.4513 0.6480 0.3564 0.1335  0.0025  -0.1279 584  PRO A CG  
4382  C CD  . PRO A 586  ? 0.4171 0.6225 0.3177 0.1342  0.0014  -0.1285 584  PRO A CD  
4383  N N   . ALA A 587  ? 0.3819 0.5415 0.2994 0.1342  -0.0141 -0.1506 585  ALA A N   
4384  C CA  . ALA A 587  ? 0.4240 0.5795 0.3463 0.1367  -0.0198 -0.1602 585  ALA A CA  
4385  C C   . ALA A 587  ? 0.4409 0.5889 0.3707 0.1382  -0.0220 -0.1652 585  ALA A C   
4386  O O   . ALA A 587  ? 0.4229 0.5638 0.3545 0.1361  -0.0196 -0.1607 585  ALA A O   
4387  C CB  . ALA A 587  ? 0.4198 0.5634 0.3429 0.1337  -0.0230 -0.1605 585  ALA A CB  
4388  N N   . ALA A 588  ? 0.4201 0.5699 0.3542 0.1420  -0.0265 -0.1745 586  ALA A N   
4389  C CA  . ALA A 588  ? 0.4331 0.5754 0.3750 0.1436  -0.0294 -0.1798 586  ALA A CA  
4390  C C   . ALA A 588  ? 0.4173 0.5413 0.3651 0.1404  -0.0333 -0.1805 586  ALA A C   
4391  O O   . ALA A 588  ? 0.4582 0.5768 0.4048 0.1380  -0.0350 -0.1797 586  ALA A O   
4392  C CB  . ALA A 588  ? 0.4291 0.5807 0.3739 0.1490  -0.0330 -0.1896 586  ALA A CB  
4393  N N   . GLY A 589  ? 0.4206 0.5356 0.3752 0.1403  -0.0347 -0.1820 587  GLY A N   
4394  C CA  . GLY A 589  ? 0.4026 0.5006 0.3637 0.1372  -0.0386 -0.1824 587  GLY A CA  
4395  C C   . GLY A 589  ? 0.4243 0.5147 0.3929 0.1377  -0.0398 -0.1839 587  GLY A C   
4396  O O   . GLY A 589  ? 0.4776 0.5760 0.4467 0.1409  -0.0382 -0.1859 587  GLY A O   
4397  N N   . GLU A 590  ? 0.4247 0.4997 0.3994 0.1344  -0.0429 -0.1828 588  GLU A N   
4398  C CA  . GLU A 590  ? 0.4456 0.5117 0.4279 0.1341  -0.0442 -0.1832 588  GLU A CA  
4399  C C   . GLU A 590  ? 0.4017 0.4673 0.3808 0.1319  -0.0385 -0.1751 588  GLU A C   
4400  O O   . GLU A 590  ? 0.4302 0.4918 0.4051 0.1281  -0.0356 -0.1682 588  GLU A O   
4401  C CB  . GLU A 590  ? 0.4717 0.5220 0.4616 0.1310  -0.0494 -0.1838 588  GLU A CB  
4402  N N   . THR A 591  ? 0.4043 0.4739 0.3857 0.1344  -0.0371 -0.1762 589  THR A N   
4403  C CA  . THR A 591  ? 0.4170 0.4884 0.3957 0.1330  -0.0315 -0.1693 589  THR A CA  
4404  C C   . THR A 591  ? 0.3689 0.4281 0.3555 0.1315  -0.0331 -0.1680 589  THR A C   
4405  O O   . THR A 591  ? 0.4412 0.4975 0.4349 0.1339  -0.0372 -0.1740 589  THR A O   
4406  C CB  . THR A 591  ? 0.3928 0.4801 0.3675 0.1371  -0.0281 -0.1708 589  THR A CB  
4407  O OG1 . THR A 591  ? 0.3832 0.4823 0.3504 0.1382  -0.0264 -0.1708 589  THR A OG1 
4408  C CG2 . THR A 591  ? 0.4223 0.5112 0.3950 0.1357  -0.0227 -0.1637 589  THR A CG2 
4409  N N   . ARG A 592  ? 0.3787 0.4310 0.3642 0.1276  -0.0299 -0.1603 590  ARG A N   
4410  C CA  . ARG A 592  ? 0.3981 0.4398 0.3906 0.1260  -0.0307 -0.1580 590  ARG A CA  
4411  C C   . ARG A 592  ? 0.3760 0.4193 0.3647 0.1239  -0.0248 -0.1500 590  ARG A C   
4412  O O   . ARG A 592  ? 0.3728 0.4229 0.3538 0.1230  -0.0206 -0.1457 590  ARG A O   
4413  C CB  . ARG A 592  ? 0.4425 0.4691 0.4408 0.1224  -0.0353 -0.1573 590  ARG A CB  
4414  C CG  . ARG A 592  ? 0.4434 0.4656 0.4367 0.1182  -0.0336 -0.1515 590  ARG A CG  
4415  C CD  . ARG A 592  ? 0.5479 0.5549 0.5475 0.1139  -0.0365 -0.1481 590  ARG A CD  
4416  N NE  . ARG A 592  ? 0.5726 0.5755 0.5674 0.1099  -0.0347 -0.1424 590  ARG A NE  
4417  C CZ  . ARG A 592  ? 0.5334 0.5352 0.5247 0.1074  -0.0303 -0.1354 590  ARG A CZ  
4418  N NH1 . ARG A 592  ? 0.4766 0.4807 0.4687 0.1083  -0.0270 -0.1327 590  ARG A NH1 
4419  N NH2 . ARG A 592  ? 0.5095 0.5079 0.4967 0.1041  -0.0291 -0.1310 590  ARG A NH2 
4420  N N   . THR A 593  ? 0.3633 0.4005 0.3576 0.1234  -0.0247 -0.1480 591  THR A N   
4421  C CA  . THR A 593  ? 0.3349 0.3737 0.3265 0.1218  -0.0193 -0.1409 591  THR A CA  
4422  C C   . THR A 593  ? 0.3833 0.4113 0.3747 0.1169  -0.0186 -0.1342 591  THR A C   
4423  O O   . THR A 593  ? 0.3837 0.4010 0.3788 0.1145  -0.0227 -0.1349 591  THR A O   
4424  C CB  . THR A 593  ? 0.4337 0.4716 0.4314 0.1235  -0.0192 -0.1415 591  THR A CB  
4425  O OG1 . THR A 593  ? 0.4282 0.4526 0.4343 0.1219  -0.0240 -0.1426 591  THR A OG1 
4426  C CG2 . THR A 593  ? 0.4307 0.4801 0.4286 0.1285  -0.0197 -0.1481 591  THR A CG2 
4427  N N   . VAL A 594  ? 0.3028 0.3342 0.2899 0.1153  -0.0134 -0.1275 592  VAL A N   
4428  C CA  . VAL A 594  ? 0.3392 0.3618 0.3255 0.1110  -0.0120 -0.1208 592  VAL A CA  
4429  C C   . VAL A 594  ? 0.3380 0.3570 0.3286 0.1103  -0.0102 -0.1167 592  VAL A C   
4430  O O   . VAL A 594  ? 0.3425 0.3706 0.3314 0.1122  -0.0062 -0.1152 592  VAL A O   
4431  C CB  . VAL A 594  ? 0.3088 0.3385 0.2864 0.1097  -0.0076 -0.1161 592  VAL A CB  
4432  C CG1 . VAL A 594  ? 0.2858 0.3064 0.2628 0.1055  -0.0064 -0.1095 592  VAL A CG1 
4433  C CG2 . VAL A 594  ? 0.3314 0.3656 0.3046 0.1106  -0.0096 -0.1202 592  VAL A CG2 
4434  N N   . LEU A 595  ? 0.3280 0.3343 0.3246 0.1075  -0.0130 -0.1148 593  LEU A N   
4435  C CA  . LEU A 595  ? 0.3394 0.3411 0.3414 0.1069  -0.0123 -0.1113 593  LEU A CA  
4436  C C   . LEU A 595  ? 0.3062 0.3036 0.3061 0.1033  -0.0092 -0.1037 593  LEU A C   
4437  O O   . LEU A 595  ? 0.3394 0.3321 0.3364 0.1005  -0.0096 -0.1013 593  LEU A O   
4438  C CB  . LEU A 595  ? 0.3274 0.3183 0.3384 0.1062  -0.0179 -0.1140 593  LEU A CB  
4439  C CG  . LEU A 595  ? 0.3751 0.3694 0.3891 0.1099  -0.0216 -0.1220 593  LEU A CG  
4440  C CD1 . LEU A 595  ? 0.3509 0.3342 0.3743 0.1089  -0.0273 -0.1240 593  LEU A CD1 
4441  C CD2 . LEU A 595  ? 0.3464 0.3525 0.3589 0.1140  -0.0185 -0.1245 593  LEU A CD2 
4442  N N   . ASN A 596  ? 0.3198 0.3190 0.3214 0.1035  -0.0063 -0.0999 594  ASN A N   
4443  C CA  . ASN A 596  ? 0.3111 0.3060 0.3120 0.1004  -0.0037 -0.0927 594  ASN A CA  
4444  C C   . ASN A 596  ? 0.2609 0.2418 0.2679 0.0970  -0.0080 -0.0909 594  ASN A C   
4445  O O   . ASN A 596  ? 0.2897 0.2654 0.3039 0.0974  -0.0112 -0.0924 594  ASN A O   
4446  C CB  . ASN A 596  ? 0.2992 0.3001 0.3016 0.1019  0.0000  -0.0899 594  ASN A CB  
4447  C CG  . ASN A 596  ? 0.3112 0.3098 0.3123 0.0992  0.0031  -0.0824 594  ASN A CG  
4448  O OD1 . ASN A 596  ? 0.2814 0.2705 0.2831 0.0954  0.0015  -0.0788 594  ASN A OD1 
4449  N ND2 . ASN A 596  ? 0.3313 0.3388 0.3307 0.1006  0.0076  -0.0795 594  ASN A ND2 
4450  N N   . PRO A 597  ? 0.2739 0.2487 0.2784 0.0936  -0.0083 -0.0873 595  PRO A N   
4451  C CA  . PRO A 597  ? 0.2658 0.2279 0.2764 0.0900  -0.0125 -0.0850 595  PRO A CA  
4452  C C   . PRO A 597  ? 0.2882 0.2460 0.3043 0.0889  -0.0123 -0.0805 595  PRO A C   
4453  O O   . PRO A 597  ? 0.2745 0.2231 0.2973 0.0865  -0.0163 -0.0793 595  PRO A O   
4454  C CB  . PRO A 597  ? 0.2848 0.2436 0.2903 0.0867  -0.0118 -0.0814 595  PRO A CB  
4455  C CG  . PRO A 597  ? 0.3343 0.3039 0.3315 0.0873  -0.0065 -0.0794 595  PRO A CG  
4456  C CD  . PRO A 597  ? 0.2439 0.2232 0.2402 0.0929  -0.0053 -0.0854 595  PRO A CD  
4457  N N   . GLY A 598  ? 0.2642 0.2290 0.2780 0.0899  -0.0077 -0.0774 596  GLY A N   
4458  C CA  . GLY A 598  ? 0.2566 0.2183 0.2754 0.0881  -0.0074 -0.0724 596  GLY A CA  
4459  C C   . GLY A 598  ? 0.3028 0.2663 0.3278 0.0923  -0.0088 -0.0768 596  GLY A C   
4460  O O   . GLY A 598  ? 0.3030 0.2632 0.3333 0.0915  -0.0093 -0.0735 596  GLY A O   
4461  N N   . ASP A 599  ? 0.2807 0.2500 0.3048 0.0955  -0.0095 -0.0830 597  ASP A N   
4462  C CA  . ASP A 599  ? 0.2979 0.2703 0.3271 0.0987  -0.0106 -0.0869 597  ASP A CA  
4463  C C   . ASP A 599  ? 0.3053 0.2829 0.3325 0.1018  -0.0121 -0.0942 597  ASP A C   
4464  O O   . ASP A 599  ? 0.3004 0.2889 0.3218 0.1043  -0.0086 -0.0962 597  ASP A O   
4465  C CB  . ASP A 599  ? 0.2892 0.2706 0.3173 0.1009  -0.0059 -0.0846 597  ASP A CB  
4466  C CG  . ASP A 599  ? 0.3416 0.3251 0.3758 0.1038  -0.0073 -0.0878 597  ASP A CG  
4467  O OD1 . ASP A 599  ? 0.3415 0.3227 0.3792 0.1054  -0.0112 -0.0933 597  ASP A OD1 
4468  O OD2 . ASP A 599  ? 0.3800 0.3677 0.4159 0.1046  -0.0045 -0.0848 597  ASP A OD2 
4469  N N   . HIS A 600  ? 0.3113 0.2817 0.3435 0.1013  -0.0174 -0.0978 598  HIS A N   
4470  C CA  . HIS A 600  ? 0.2879 0.2622 0.3186 0.1039  -0.0196 -0.1049 598  HIS A CA  
4471  C C   . HIS A 600  ? 0.3455 0.3299 0.3764 0.1087  -0.0184 -0.1100 598  HIS A C   
4472  O O   . HIS A 600  ? 0.3702 0.3600 0.3989 0.1113  -0.0196 -0.1161 598  HIS A O   
4473  C CB  . HIS A 600  ? 0.3183 0.2823 0.3554 0.1022  -0.0259 -0.1073 598  HIS A CB  
4474  C CG  . HIS A 600  ? 0.3528 0.3091 0.3884 0.0979  -0.0274 -0.1039 598  HIS A CG  
4475  N ND1 . HIS A 600  ? 0.3609 0.3081 0.4022 0.0956  -0.0328 -0.1048 598  HIS A ND1 
4476  C CD2 . HIS A 600  ? 0.3273 0.2841 0.3566 0.0955  -0.0242 -0.0995 598  HIS A CD2 
4477  C CE1 . HIS A 600  ? 0.3838 0.3262 0.4222 0.0919  -0.0328 -0.1010 598  HIS A CE1 
4478  N NE2 . HIS A 600  ? 0.3501 0.2981 0.3813 0.0918  -0.0277 -0.0980 598  HIS A NE2 
4479  N N   . ARG A 601  ? 0.3289 0.3162 0.3624 0.1099  -0.0161 -0.1078 599  ARG A N   
4480  C CA  . ARG A 601  ? 0.3479 0.3458 0.3813 0.1144  -0.0143 -0.1121 599  ARG A CA  
4481  C C   . ARG A 601  ? 0.3809 0.3916 0.4057 0.1159  -0.0089 -0.1114 599  ARG A C   
4482  O O   . ARG A 601  ? 0.3785 0.3996 0.4017 0.1196  -0.0076 -0.1156 599  ARG A O   
4483  C CB  . ARG A 601  ? 0.3260 0.3227 0.3653 0.1150  -0.0137 -0.1094 599  ARG A CB  
4484  C CG  . ARG A 601  ? 0.3736 0.3579 0.4216 0.1131  -0.0189 -0.1087 599  ARG A CG  
4485  C CD  . ARG A 601  ? 0.3435 0.3271 0.3967 0.1133  -0.0178 -0.1049 599  ARG A CD  
4486  N NE  . ARG A 601  ? 0.3429 0.3268 0.3927 0.1106  -0.0136 -0.0976 599  ARG A NE  
4487  C CZ  . ARG A 601  ? 0.3763 0.3595 0.4299 0.1100  -0.0122 -0.0930 599  ARG A CZ  
4488  N NH1 . ARG A 601  ? 0.3963 0.3782 0.4568 0.1118  -0.0144 -0.0945 599  ARG A NH1 
4489  N NH2 . ARG A 601  ? 0.3453 0.3292 0.3957 0.1076  -0.0087 -0.0867 599  ARG A NH2 
4490  N N   . ASP A 602  ? 0.3291 0.3396 0.3485 0.1129  -0.0058 -0.1059 600  ASP A N   
4491  C CA  . ASP A 602  ? 0.3595 0.3820 0.3709 0.1136  -0.0005 -0.1038 600  ASP A CA  
4492  C C   . ASP A 602  ? 0.3845 0.4099 0.3903 0.1140  -0.0016 -0.1075 600  ASP A C   
4493  O O   . ASP A 602  ? 0.3663 0.3854 0.3697 0.1111  -0.0026 -0.1055 600  ASP A O   
4494  C CB  . ASP A 602  ? 0.3459 0.3666 0.3549 0.1104  0.0031  -0.0959 600  ASP A CB  
4495  C CG  . ASP A 602  ? 0.3790 0.4118 0.3802 0.1107  0.0085  -0.0928 600  ASP A CG  
4496  O OD1 . ASP A 602  ? 0.4066 0.4507 0.4052 0.1136  0.0101  -0.0959 600  ASP A OD1 
4497  O OD2 . ASP A 602  ? 0.3813 0.4127 0.3791 0.1079  0.0111  -0.0869 600  ASP A OD2 
4498  N N   . VAL A 603  ? 0.3644 0.3997 0.3683 0.1176  -0.0016 -0.1129 601  VAL A N   
4499  C CA  . VAL A 603  ? 0.3002 0.3405 0.2984 0.1184  -0.0023 -0.1164 601  VAL A CA  
4500  C C   . VAL A 603  ? 0.3497 0.3996 0.3397 0.1173  0.0030  -0.1111 601  VAL A C   
4501  O O   . VAL A 603  ? 0.3962 0.4569 0.3840 0.1188  0.0070  -0.1091 601  VAL A O   
4502  C CB  . VAL A 603  ? 0.3410 0.3890 0.3403 0.1228  -0.0045 -0.1242 601  VAL A CB  
4503  C CG1 . VAL A 603  ? 0.3254 0.3786 0.3191 0.1237  -0.0057 -0.1279 601  VAL A CG1 
4504  C CG2 . VAL A 603  ? 0.3877 0.4262 0.3958 0.1239  -0.0098 -0.1289 601  VAL A CG2 
4505  N N   . VAL A 604  ? 0.3054 0.3513 0.2912 0.1145  0.0030  -0.1085 602  VAL A N   
4506  C CA  . VAL A 604  ? 0.2834 0.3374 0.2616 0.1131  0.0079  -0.1029 602  VAL A CA  
4507  C C   . VAL A 604  ? 0.3195 0.3853 0.2917 0.1153  0.0085  -0.1060 602  VAL A C   
4508  O O   . VAL A 604  ? 0.2932 0.3706 0.2604 0.1156  0.0128  -0.1022 602  VAL A O   
4509  C CB  . VAL A 604  ? 0.2944 0.3389 0.2709 0.1091  0.0078  -0.0981 602  VAL A CB  
4510  C CG1 . VAL A 604  ? 0.2708 0.3234 0.2400 0.1075  0.0128  -0.0917 602  VAL A CG1 
4511  C CG2 . VAL A 604  ? 0.3430 0.3759 0.3257 0.1070  0.0067  -0.0952 602  VAL A CG2 
4512  N N   . GLY A 605  ? 0.3026 0.3661 0.2757 0.1168  0.0041  -0.1126 603  GLY A N   
4513  C CA  . GLY A 605  ? 0.2890 0.3639 0.2567 0.1191  0.0044  -0.1158 603  GLY A CA  
4514  C C   . GLY A 605  ? 0.3146 0.3852 0.2848 0.1206  -0.0011 -0.1235 603  GLY A C   
4515  O O   . GLY A 605  ? 0.3310 0.3908 0.3078 0.1205  -0.0052 -0.1269 603  GLY A O   
4516  N N   . SER A 606  ? 0.3081 0.3872 0.2730 0.1220  -0.0014 -0.1259 604  SER A N   
4517  C CA  A SER A 606  ? 0.3279 0.4051 0.2945 0.1239  -0.0065 -0.1336 604  SER A CA  
4518  C CA  B SER A 606  ? 0.3279 0.4052 0.2945 0.1239  -0.0065 -0.1335 604  SER A CA  
4519  C C   . SER A 606  ? 0.3281 0.4055 0.2891 0.1221  -0.0069 -0.1323 604  SER A C   
4520  O O   . SER A 606  ? 0.3622 0.4482 0.3166 0.1212  -0.0029 -0.1274 604  SER A O   
4521  C CB  A SER A 606  ? 0.3436 0.4333 0.3102 0.1287  -0.0071 -0.1398 604  SER A CB  
4522  C CB  B SER A 606  ? 0.3436 0.4334 0.3101 0.1287  -0.0070 -0.1396 604  SER A CB  
4523  O OG  A SER A 606  ? 0.3519 0.4419 0.3236 0.1306  -0.0067 -0.1411 604  SER A OG  
4524  O OG  B SER A 606  ? 0.3586 0.4460 0.3280 0.1307  -0.0123 -0.1475 604  SER A OG  
4525  N N   . VAL A 607  ? 0.2890 0.3570 0.2532 0.1213  -0.0118 -0.1364 605  VAL A N   
4526  C CA  . VAL A 607  ? 0.3075 0.3749 0.2672 0.1196  -0.0129 -0.1360 605  VAL A CA  
4527  C C   . VAL A 607  ? 0.3374 0.4076 0.2989 0.1226  -0.0176 -0.1443 605  VAL A C   
4528  O O   . VAL A 607  ? 0.3296 0.3933 0.2981 0.1239  -0.0220 -0.1498 605  VAL A O   
4529  C CB  . VAL A 607  ? 0.3415 0.3945 0.3032 0.1152  -0.0142 -0.1321 605  VAL A CB  
4530  C CG1 . VAL A 607  ? 0.3007 0.3410 0.2714 0.1147  -0.0190 -0.1357 605  VAL A CG1 
4531  C CG2 . VAL A 607  ? 0.3057 0.3586 0.2629 0.1137  -0.0155 -0.1321 605  VAL A CG2 
4532  N N   . THR A 608  ? 0.3200 0.4001 0.2753 0.1237  -0.0169 -0.1451 606  THR A N   
4533  C CA  . THR A 608  ? 0.3431 0.4256 0.2992 0.1261  -0.0214 -0.1525 606  THR A CA  
4534  C C   . THR A 608  ? 0.3740 0.4491 0.3283 0.1228  -0.0232 -0.1507 606  THR A C   
4535  O O   . THR A 608  ? 0.3369 0.4159 0.2846 0.1208  -0.0199 -0.1451 606  THR A O   
4536  C CB  . THR A 608  ? 0.3606 0.4603 0.3112 0.1297  -0.0195 -0.1547 606  THR A CB  
4537  O OG1 . THR A 608  ? 0.3745 0.4812 0.3271 0.1328  -0.0178 -0.1564 606  THR A OG1 
4538  C CG2 . THR A 608  ? 0.4007 0.5033 0.3522 0.1323  -0.0242 -0.1625 606  THR A CG2 
4539  N N   . GLU A 609  ? 0.3662 0.4308 0.3265 0.1221  -0.0286 -0.1552 607  GLU A N   
4540  C CA  . GLU A 609  ? 0.3929 0.4488 0.3527 0.1186  -0.0305 -0.1533 607  GLU A CA  
4541  C C   . GLU A 609  ? 0.3854 0.4476 0.3425 0.1203  -0.0332 -0.1581 607  GLU A C   
4542  O O   . GLU A 609  ? 0.3780 0.4488 0.3359 0.1243  -0.0351 -0.1645 607  GLU A O   
4543  C CB  . GLU A 609  ? 0.4387 0.4790 0.4071 0.1161  -0.0347 -0.1541 607  GLU A CB  
4544  C CG  . GLU A 609  ? 0.4727 0.5063 0.4426 0.1135  -0.0315 -0.1476 607  GLU A CG  
4545  C CD  . GLU A 609  ? 0.5211 0.5402 0.4999 0.1111  -0.0355 -0.1477 607  GLU A CD  
4546  O OE1 . GLU A 609  ? 0.5428 0.5585 0.5281 0.1126  -0.0405 -0.1538 607  GLU A OE1 
4547  O OE2 . GLU A 609  ? 0.5082 0.5195 0.4875 0.1075  -0.0336 -0.1415 607  GLU A OE2 
4548  N N   . THR A 610  ? 0.3820 0.4404 0.3358 0.1172  -0.0334 -0.1549 608  THR A N   
4549  C CA  . THR A 610  ? 0.3660 0.4310 0.3157 0.1183  -0.0350 -0.1577 608  THR A CA  
4550  C C   . THR A 610  ? 0.3748 0.4323 0.3312 0.1185  -0.0414 -0.1644 608  THR A C   
4551  O O   . THR A 610  ? 0.4043 0.4486 0.3664 0.1155  -0.0441 -0.1634 608  THR A O   
4552  C CB  . THR A 610  ? 0.3913 0.4556 0.3346 0.1148  -0.0321 -0.1508 608  THR A CB  
4553  O OG1 . THR A 610  ? 0.3539 0.4227 0.2924 0.1138  -0.0263 -0.1437 608  THR A OG1 
4554  C CG2 . THR A 610  ? 0.3601 0.4341 0.2981 0.1162  -0.0328 -0.1529 608  THR A CG2 
4555  N N   . SER A 611  ? 0.3888 0.4550 0.3447 0.1221  -0.0440 -0.1709 609  SER A N   
4556  C CA  . SER A 611  ? 0.4252 0.4854 0.3866 0.1222  -0.0501 -0.1770 609  SER A CA  
4557  C C   . SER A 611  ? 0.4188 0.4752 0.3768 0.1188  -0.0505 -0.1737 609  SER A C   
4558  O O   . SER A 611  ? 0.4220 0.4844 0.3721 0.1176  -0.0463 -0.1683 609  SER A O   
4559  C CB  . SER A 611  ? 0.4060 0.4774 0.3678 0.1273  -0.0526 -0.1852 609  SER A CB  
4560  O OG  . SER A 611  ? 0.4494 0.5329 0.4029 0.1284  -0.0501 -0.1841 609  SER A OG  
4561  N N   . GLU A 612  ? 0.4399 0.4863 0.4041 0.1171  -0.0557 -0.1767 610  GLU A N   
4562  C CA  . GLU A 612  ? 0.4563 0.4992 0.4178 0.1140  -0.0566 -0.1741 610  GLU A CA  
4563  C C   . GLU A 612  ? 0.4447 0.5006 0.3994 0.1165  -0.0559 -0.1764 610  GLU A C   
4564  O O   . GLU A 612  ? 0.4567 0.5143 0.4055 0.1143  -0.0539 -0.1720 610  GLU A O   
4565  C CB  . GLU A 612  ? 0.4980 0.5290 0.4683 0.1119  -0.0628 -0.1774 610  GLU A CB  
4566  C CG  . GLU A 612  ? 0.5232 0.5404 0.4995 0.1080  -0.0633 -0.1730 610  GLU A CG  
4567  C CD  . GLU A 612  ? 0.6163 0.6226 0.6021 0.1061  -0.0697 -0.1761 610  GLU A CD  
4568  O OE1 . GLU A 612  ? 0.7094 0.7187 0.6974 0.1082  -0.0738 -0.1823 610  GLU A OE1 
4569  O OE2 . GLU A 612  ? 0.6894 0.6844 0.6806 0.1024  -0.0707 -0.1721 610  GLU A OE2 
4570  N N   . GLU A 613  ? 0.4490 0.5145 0.4045 0.1212  -0.0574 -0.1833 611  GLU A N   
4571  C CA  . GLU A 613  ? 0.4343 0.5132 0.3836 0.1240  -0.0568 -0.1856 611  GLU A CA  
4572  C C   . GLU A 613  ? 0.3976 0.4868 0.3376 0.1239  -0.0504 -0.1788 611  GLU A C   
4573  O O   . GLU A 613  ? 0.4015 0.4968 0.3352 0.1231  -0.0488 -0.1760 611  GLU A O   
4574  C CB  . GLU A 613  ? 0.4543 0.5415 0.4071 0.1292  -0.0599 -0.1946 611  GLU A CB  
4575  C CG  . GLU A 613  ? 0.4963 0.5984 0.4430 0.1326  -0.0595 -0.1977 611  GLU A CG  
4576  C CD  . GLU A 613  ? 0.6483 0.7583 0.5992 0.1380  -0.0629 -0.2072 611  GLU A CD  
4577  O OE1 . GLU A 613  ? 0.6662 0.7709 0.6236 0.1388  -0.0686 -0.2138 611  GLU A OE1 
4578  O OE2 . GLU A 613  ? 0.6016 0.7232 0.5495 0.1413  -0.0601 -0.2081 611  GLU A OE2 
4579  N N   . ASP A 614  ? 0.4066 0.4978 0.3460 0.1244  -0.0466 -0.1758 612  ASP A N   
4580  C CA  . ASP A 614  ? 0.3860 0.4870 0.3173 0.1241  -0.0406 -0.1689 612  ASP A CA  
4581  C C   . ASP A 614  ? 0.3949 0.4885 0.3227 0.1193  -0.0379 -0.1604 612  ASP A C   
4582  O O   . ASP A 614  ? 0.3462 0.4477 0.2669 0.1185  -0.0339 -0.1547 612  ASP A O   
4583  C CB  . ASP A 614  ? 0.3772 0.4825 0.3093 0.1261  -0.0375 -0.1680 612  ASP A CB  
4584  C CG  . ASP A 614  ? 0.4275 0.5459 0.3599 0.1314  -0.0385 -0.1749 612  ASP A CG  
4585  O OD1 . ASP A 614  ? 0.4298 0.5559 0.3603 0.1335  -0.0407 -0.1792 612  ASP A OD1 
4586  O OD2 . ASP A 614  ? 0.4734 0.5946 0.4080 0.1334  -0.0372 -0.1759 612  ASP A OD2 
4587  N N   . ALA A 615  ? 0.3256 0.4044 0.2586 0.1160  -0.0401 -0.1595 613  ALA A N   
4588  C CA  . ALA A 615  ? 0.3733 0.4451 0.3033 0.1115  -0.0381 -0.1522 613  ALA A CA  
4589  C C   . ALA A 615  ? 0.3462 0.4212 0.2721 0.1107  -0.0395 -0.1522 613  ALA A C   
4590  O O   . ALA A 615  ? 0.3575 0.4361 0.2770 0.1089  -0.0361 -0.1459 613  ALA A O   
4591  C CB  . ALA A 615  ? 0.3751 0.4308 0.3120 0.1082  -0.0406 -0.1516 613  ALA A CB  
4592  N N   . ARG A 616  ? 0.3816 0.4557 0.3113 0.1122  -0.0445 -0.1592 614  ARG A N   
4593  C CA  . ARG A 616  ? 0.4063 0.4845 0.3322 0.1118  -0.0460 -0.1598 614  ARG A CA  
4594  C C   . ARG A 616  ? 0.3540 0.4485 0.2723 0.1145  -0.0427 -0.1584 614  ARG A C   
4595  O O   . ARG A 616  ? 0.3631 0.4616 0.2755 0.1130  -0.0410 -0.1539 614  ARG A O   
4596  C CB  . ARG A 616  ? 0.4038 0.4779 0.3361 0.1130  -0.0523 -0.1679 614  ARG A CB  
4597  C CG  . ARG A 616  ? 0.5168 0.5749 0.4560 0.1091  -0.0558 -0.1675 614  ARG A CG  
4598  C CD  . ARG A 616  ? 0.5775 0.6318 0.5229 0.1098  -0.0620 -0.1745 614  ARG A CD  
4599  N NE  . ARG A 616  ? 0.6009 0.6550 0.5532 0.1131  -0.0652 -0.1815 614  ARG A NE  
4600  C CZ  . ARG A 616  ? 0.6468 0.6898 0.6072 0.1117  -0.0677 -0.1824 614  ARG A CZ  
4601  N NH1 . ARG A 616  ? 0.6304 0.6617 0.5933 0.1072  -0.0674 -0.1769 614  ARG A NH1 
4602  N NH2 . ARG A 616  ? 0.6130 0.6570 0.5795 0.1151  -0.0706 -0.1890 614  ARG A NH2 
4603  N N   . ARG A 617  ? 0.3480 0.4521 0.2663 0.1185  -0.0416 -0.1617 615  ARG A N   
4604  C CA  . ARG A 617  ? 0.3973 0.5176 0.3086 0.1209  -0.0381 -0.1597 615  ARG A CA  
4605  C C   . ARG A 617  ? 0.3272 0.4497 0.2324 0.1181  -0.0326 -0.1496 615  ARG A C   
4606  O O   . ARG A 617  ? 0.3338 0.4655 0.2329 0.1179  -0.0304 -0.1455 615  ARG A O   
4607  C CB  . ARG A 617  ? 0.4040 0.5337 0.3169 0.1254  -0.0376 -0.1644 615  ARG A CB  
4608  C CG  . ARG A 617  ? 0.4944 0.6266 0.4122 0.1292  -0.0428 -0.1746 615  ARG A CG  
4609  C CD  . ARG A 617  ? 0.5543 0.7026 0.4698 0.1341  -0.0415 -0.1783 615  ARG A CD  
4610  N NE  . ARG A 617  ? 0.5925 0.7417 0.5102 0.1354  -0.0391 -0.1777 615  ARG A NE  
4611  C CZ  . ARG A 617  ? 0.5630 0.7220 0.4758 0.1358  -0.0340 -0.1721 615  ARG A CZ  
4612  N NH1 . ARG A 617  ? 0.5816 0.7502 0.4873 0.1349  -0.0305 -0.1659 615  ARG A NH1 
4613  N NH2 . ARG A 617  ? 0.4992 0.6588 0.4148 0.1373  -0.0325 -0.1727 615  ARG A NH2 
4614  N N   . ALA A 618  ? 0.3467 0.4610 0.2540 0.1160  -0.0303 -0.1455 616  ALA A N   
4615  C CA  . ALA A 618  ? 0.3370 0.4533 0.2391 0.1134  -0.0251 -0.1361 616  ALA A CA  
4616  C C   . ALA A 618  ? 0.3047 0.4172 0.2031 0.1100  -0.0250 -0.1310 616  ALA A C   
4617  O O   . ALA A 618  ? 0.3197 0.4398 0.2122 0.1090  -0.0214 -0.1242 616  ALA A O   
4618  C CB  . ALA A 618  ? 0.3127 0.4196 0.2184 0.1118  -0.0233 -0.1334 616  ALA A CB  
4619  N N   . VAL A 619  ? 0.2996 0.4005 0.2017 0.1080  -0.0289 -0.1339 617  VAL A N   
4620  C CA  . VAL A 619  ? 0.3473 0.4449 0.2460 0.1049  -0.0292 -0.1296 617  VAL A CA  
4621  C C   . VAL A 619  ? 0.3054 0.4155 0.1990 0.1067  -0.0294 -0.1300 617  VAL A C   
4622  O O   . VAL A 619  ? 0.3305 0.4451 0.2188 0.1050  -0.0269 -0.1234 617  VAL A O   
4623  C CB  . VAL A 619  ? 0.3527 0.4361 0.2571 0.1025  -0.0338 -0.1330 617  VAL A CB  
4624  C CG1 . VAL A 619  ? 0.3549 0.4354 0.2557 0.0993  -0.0340 -0.1285 617  VAL A CG1 
4625  C CG2 . VAL A 619  ? 0.3187 0.3902 0.2282 0.1006  -0.0334 -0.1318 617  VAL A CG2 
4626  N N   . ARG A 620  ? 0.3507 0.4670 0.2461 0.1102  -0.0324 -0.1376 618  ARG A N   
4627  C CA  . ARG A 620  ? 0.3496 0.4786 0.2403 0.1121  -0.0326 -0.1383 618  ARG A CA  
4628  C C   . ARG A 620  ? 0.3360 0.4783 0.2207 0.1130  -0.0274 -0.1317 618  ARG A C   
4629  O O   . ARG A 620  ? 0.3580 0.5075 0.2376 0.1122  -0.0260 -0.1267 618  ARG A O   
4630  C CB  . ARG A 620  ? 0.4044 0.5383 0.2985 0.1161  -0.0366 -0.1480 618  ARG A CB  
4631  C CG  . ARG A 620  ? 0.4552 0.5778 0.3550 0.1152  -0.0422 -0.1542 618  ARG A CG  
4632  C CD  . ARG A 620  ? 0.5440 0.6735 0.4463 0.1193  -0.0463 -0.1634 618  ARG A CD  
4633  N NE  . ARG A 620  ? 0.6351 0.7674 0.5413 0.1228  -0.0467 -0.1688 618  ARG A NE  
4634  C CZ  . ARG A 620  ? 0.5775 0.6993 0.4913 0.1228  -0.0499 -0.1737 618  ARG A CZ  
4635  N NH1 . ARG A 620  ? 0.6036 0.7112 0.5221 0.1195  -0.0531 -0.1740 618  ARG A NH1 
4636  N NH2 . ARG A 620  ? 0.5985 0.7242 0.5154 0.1263  -0.0501 -0.1783 618  ARG A NH2 
4637  N N   . LEU A 621  ? 0.3139 0.4597 0.1997 0.1146  -0.0248 -0.1311 619  LEU A N   
4638  C CA  . LEU A 621  ? 0.3417 0.4998 0.2226 0.1151  -0.0199 -0.1243 619  LEU A CA  
4639  C C   . LEU A 621  ? 0.3173 0.4717 0.1947 0.1109  -0.0165 -0.1142 619  LEU A C   
4640  O O   . LEU A 621  ? 0.3624 0.5270 0.2351 0.1105  -0.0137 -0.1077 619  LEU A O   
4641  C CB  . LEU A 621  ? 0.3165 0.4777 0.1999 0.1172  -0.0179 -0.1257 619  LEU A CB  
4642  C CG  . LEU A 621  ? 0.3355 0.5031 0.2219 0.1218  -0.0207 -0.1351 619  LEU A CG  
4643  C CD1 . LEU A 621  ? 0.3267 0.4940 0.2166 0.1233  -0.0191 -0.1365 619  LEU A CD1 
4644  C CD2 . LEU A 621  ? 0.3546 0.5396 0.2364 0.1246  -0.0199 -0.1352 619  LEU A CD2 
4645  N N   . ALA A 622  ? 0.3229 0.4631 0.2032 0.1079  -0.0168 -0.1125 620  ALA A N   
4646  C CA  . ALA A 622  ? 0.3029 0.4388 0.1802 0.1041  -0.0139 -0.1034 620  ALA A CA  
4647  C C   . ALA A 622  ? 0.2905 0.4279 0.1643 0.1026  -0.0153 -0.1010 620  ALA A C   
4648  O O   . ALA A 622  ? 0.3119 0.4538 0.1816 0.1007  -0.0125 -0.0928 620  ALA A O   
4649  C CB  . ALA A 622  ? 0.3001 0.4204 0.1814 0.1014  -0.0145 -0.1031 620  ALA A CB  
4650  N N   . ALA A 623  ? 0.3135 0.4469 0.1892 0.1032  -0.0199 -0.1078 621  ALA A N   
4651  C CA  . ALA A 623  ? 0.3521 0.4877 0.2246 0.1020  -0.0214 -0.1061 621  ALA A CA  
4652  C C   . ALA A 623  ? 0.3563 0.5081 0.2240 0.1041  -0.0196 -0.1034 621  ALA A C   
4653  O O   . ALA A 623  ? 0.3158 0.4716 0.1795 0.1023  -0.0182 -0.0967 621  ALA A O   
4654  C CB  . ALA A 623  ? 0.3575 0.4861 0.2336 0.1025  -0.0268 -0.1144 621  ALA A CB  
4655  N N   . ASP A 624  ? 0.3412 0.5027 0.2095 0.1078  -0.0196 -0.1084 622  ASP A N   
4656  C CA  . ASP A 624  ? 0.4221 0.6000 0.2860 0.1100  -0.0178 -0.1060 622  ASP A CA  
4657  C C   . ASP A 624  ? 0.4050 0.5887 0.2657 0.1080  -0.0129 -0.0952 622  ASP A C   
4658  O O   . ASP A 624  ? 0.4374 0.6310 0.2942 0.1076  -0.0115 -0.0897 622  ASP A O   
4659  C CB  . ASP A 624  ? 0.3947 0.5817 0.2604 0.1144  -0.0184 -0.1131 622  ASP A CB  
4660  C CG  . ASP A 624  ? 0.5339 0.7191 0.4025 0.1169  -0.0235 -0.1235 622  ASP A CG  
4661  O OD1 . ASP A 624  ? 0.5651 0.7437 0.4337 0.1152  -0.0264 -0.1248 622  ASP A OD1 
4662  O OD2 . ASP A 624  ? 0.6522 0.8427 0.5232 0.1206  -0.0247 -0.1304 622  ASP A OD2 
4663  N N   . ALA A 625  ? 0.4224 0.6003 0.2850 0.1067  -0.0103 -0.0920 623  ALA A N   
4664  C CA  . ALA A 625  ? 0.4683 0.6513 0.3288 0.1049  -0.0057 -0.0822 623  ALA A CA  
4665  C C   . ALA A 625  ? 0.3858 0.5600 0.2453 0.1007  -0.0045 -0.0742 623  ALA A C   
4666  O O   . ALA A 625  ? 0.4233 0.6007 0.2817 0.0988  -0.0009 -0.0654 623  ALA A O   
4667  C CB  . ALA A 625  ? 0.5161 0.6980 0.3795 0.1058  -0.0034 -0.0829 623  ALA A CB  
4668  N N   . ALA A 626  ? 0.3511 0.5143 0.2113 0.0991  -0.0076 -0.0770 624  ALA A N   
4669  C CA  . ALA A 626  ? 0.3602 0.5146 0.2198 0.0952  -0.0067 -0.0699 624  ALA A CA  
4670  C C   . ALA A 626  ? 0.3936 0.5565 0.2495 0.0937  -0.0048 -0.0608 624  ALA A C   
4671  O O   . ALA A 626  ? 0.3470 0.5075 0.2027 0.0910  -0.0019 -0.0524 624  ALA A O   
4672  C CB  . ALA A 626  ? 0.3323 0.4744 0.1937 0.0940  -0.0108 -0.0752 624  ALA A CB  
4673  N N   . PRO A 627  ? 0.3803 0.5529 0.2335 0.0950  -0.0062 -0.0616 625  PRO A N   
4674  C CA  . PRO A 627  ? 0.3609 0.5413 0.2113 0.0933  -0.0043 -0.0521 625  PRO A CA  
4675  C C   . PRO A 627  ? 0.3239 0.5126 0.1741 0.0929  0.0000  -0.0442 625  PRO A C   
4676  O O   . PRO A 627  ? 0.3884 0.5772 0.2381 0.0901  0.0020  -0.0347 625  PRO A O   
4677  C CB  . PRO A 627  ? 0.3810 0.5716 0.2289 0.0957  -0.0067 -0.0561 625  PRO A CB  
4678  C CG  . PRO A 627  ? 0.3888 0.5722 0.2387 0.0974  -0.0107 -0.0670 625  PRO A CG  
4679  C CD  . PRO A 627  ? 0.4042 0.5805 0.2574 0.0980  -0.0098 -0.0708 625  PRO A CD  
4680  N N   . ASP A 628  ? 0.3330 0.5284 0.1842 0.0955  0.0013  -0.0479 626  ASP A N   
4681  C CA  . ASP A 628  ? 0.3051 0.5095 0.1565 0.0951  0.0053  -0.0405 626  ASP A CA  
4682  C C   . ASP A 628  ? 0.3560 0.5507 0.2098 0.0921  0.0078  -0.0346 626  ASP A C   
4683  O O   . ASP A 628  ? 0.3568 0.5561 0.2109 0.0901  0.0107  -0.0254 626  ASP A O   
4684  C CB  . ASP A 628  ? 0.3323 0.5466 0.1842 0.0988  0.0059  -0.0462 626  ASP A CB  
4685  C CG  . ASP A 628  ? 0.4542 0.6811 0.3037 0.1019  0.0040  -0.0507 626  ASP A CG  
4686  O OD1 . ASP A 628  ? 0.4898 0.7207 0.3369 0.1009  0.0032  -0.0469 626  ASP A OD1 
4687  O OD2 . ASP A 628  ? 0.4896 0.7227 0.3398 0.1055  0.0034  -0.0580 626  ASP A OD2 
4688  N N   . TRP A 629  ? 0.3239 0.5054 0.1797 0.0917  0.0065  -0.0398 627  TRP A N   
4689  C CA  . TRP A 629  ? 0.3282 0.5003 0.1862 0.0890  0.0087  -0.0345 627  TRP A CA  
4690  C C   . TRP A 629  ? 0.3374 0.5024 0.1947 0.0855  0.0084  -0.0277 627  TRP A C   
4691  O O   . TRP A 629  ? 0.3136 0.4769 0.1720 0.0829  0.0109  -0.0192 627  TRP A O   
4692  C CB  . TRP A 629  ? 0.2948 0.4558 0.1554 0.0899  0.0075  -0.0424 627  TRP A CB  
4693  C CG  . TRP A 629  ? 0.2680 0.4195 0.1308 0.0873  0.0097  -0.0375 627  TRP A CG  
4694  C CD1 . TRP A 629  ? 0.2618 0.3996 0.1260 0.0855  0.0084  -0.0390 627  TRP A CD1 
4695  C CD2 . TRP A 629  ? 0.2911 0.4464 0.1552 0.0860  0.0136  -0.0301 627  TRP A CD2 
4696  N NE1 . TRP A 629  ? 0.2637 0.3966 0.1297 0.0834  0.0113  -0.0332 627  TRP A NE1 
4697  C CE2 . TRP A 629  ? 0.2788 0.4221 0.1449 0.0836  0.0145  -0.0277 627  TRP A CE2 
4698  C CE3 . TRP A 629  ? 0.3099 0.4780 0.1740 0.0867  0.0163  -0.0253 627  TRP A CE3 
4699  C CZ2 . TRP A 629  ? 0.2751 0.4184 0.1433 0.0819  0.0180  -0.0207 627  TRP A CZ2 
4700  C CZ3 . TRP A 629  ? 0.3024 0.4703 0.1687 0.0847  0.0197  -0.0182 627  TRP A CZ3 
4701  C CH2 . TRP A 629  ? 0.3302 0.4857 0.1986 0.0824  0.0205  -0.0161 627  TRP A CH2 
4702  N N   . ALA A 630  ? 0.3109 0.4719 0.1667 0.0855  0.0051  -0.0313 628  ALA A N   
4703  C CA  . ALA A 630  ? 0.3183 0.4736 0.1734 0.0825  0.0044  -0.0249 628  ALA A CA  
4704  C C   . ALA A 630  ? 0.3474 0.5123 0.2016 0.0810  0.0065  -0.0148 628  ALA A C   
4705  O O   . ALA A 630  ? 0.3701 0.5305 0.2252 0.0781  0.0073  -0.0068 628  ALA A O   
4706  C CB  . ALA A 630  ? 0.3663 0.5177 0.2200 0.0830  0.0003  -0.0308 628  ALA A CB  
4707  N N   . ALA A 631  ? 0.3156 0.4940 0.1684 0.0830  0.0072  -0.0148 629  ALA A N   
4708  C CA  . ALA A 631  ? 0.3675 0.5562 0.2199 0.0818  0.0090  -0.0054 629  ALA A CA  
4709  C C   . ALA A 631  ? 0.3498 0.5401 0.2050 0.0799  0.0126  0.0027  629  ALA A C   
4710  O O   . ALA A 631  ? 0.3538 0.5501 0.2099 0.0780  0.0140  0.0118  629  ALA A O   
4711  C CB  . ALA A 631  ? 0.3335 0.5367 0.1835 0.0847  0.0085  -0.0086 629  ALA A CB  
4712  N N   . VAL A 632  ? 0.3053 0.4905 0.1624 0.0803  0.0141  -0.0003 630  VAL A N   
4713  C CA  . VAL A 632  ? 0.3233 0.5085 0.1835 0.0781  0.0174  0.0077  630  VAL A CA  
4714  C C   . VAL A 632  ? 0.3047 0.4790 0.1668 0.0745  0.0173  0.0144  630  VAL A C   
4715  O O   . VAL A 632  ? 0.3219 0.4846 0.1837 0.0741  0.0156  0.0101  630  VAL A O   
4716  C CB  . VAL A 632  ? 0.3439 0.5264 0.2058 0.0796  0.0189  0.0024  630  VAL A CB  
4717  C CG1 . VAL A 632  ? 0.3091 0.4917 0.1745 0.0772  0.0222  0.0107  630  VAL A CG1 
4718  C CG2 . VAL A 632  ? 0.2935 0.4872 0.1538 0.0835  0.0187  -0.0045 630  VAL A CG2 
4719  N N   . PRO A 633  ? 0.2885 0.4660 0.1529 0.0717  0.0187  0.0248  631  PRO A N   
4720  C CA  . PRO A 633  ? 0.2935 0.4607 0.1601 0.0685  0.0181  0.0311  631  PRO A CA  
4721  C C   . PRO A 633  ? 0.3091 0.4644 0.1779 0.0674  0.0190  0.0296  631  PRO A C   
4722  O O   . PRO A 633  ? 0.3027 0.4590 0.1730 0.0680  0.0212  0.0283  631  PRO A O   
4723  C CB  . PRO A 633  ? 0.3262 0.5004 0.1961 0.0660  0.0197  0.0421  631  PRO A CB  
4724  C CG  . PRO A 633  ? 0.3496 0.5388 0.2175 0.0682  0.0202  0.0412  631  PRO A CG  
4725  C CD  . PRO A 633  ? 0.3078 0.4990 0.1731 0.0717  0.0204  0.0311  631  PRO A CD  
4726  N N   . PRO A 634  ? 0.2410 0.3848 0.1102 0.0659  0.0174  0.0299  632  PRO A N   
4727  C CA  . PRO A 634  ? 0.2489 0.3814 0.1201 0.0649  0.0183  0.0288  632  PRO A CA  
4728  C C   . PRO A 634  ? 0.2487 0.3819 0.1242 0.0629  0.0214  0.0355  632  PRO A C   
4729  O O   . PRO A 634  ? 0.2571 0.3861 0.1336 0.0635  0.0229  0.0322  632  PRO A O   
4730  C CB  . PRO A 634  ? 0.2720 0.3946 0.1437 0.0630  0.0161  0.0312  632  PRO A CB  
4731  C CG  . PRO A 634  ? 0.3251 0.4524 0.1935 0.0643  0.0134  0.0286  632  PRO A CG  
4732  C CD  . PRO A 634  ? 0.3069 0.4481 0.1745 0.0654  0.0145  0.0305  632  PRO A CD  
4733  N N   . SER A 635  ? 0.2920 0.4302 0.1707 0.0607  0.0222  0.0449  633  SER A N   
4734  C CA  . SER A 635  ? 0.3037 0.4426 0.1874 0.0585  0.0249  0.0515  633  SER A CA  
4735  C C   . SER A 635  ? 0.2625 0.4098 0.1455 0.0606  0.0271  0.0478  633  SER A C   
4736  O O   . SER A 635  ? 0.2674 0.4119 0.1534 0.0598  0.0291  0.0489  633  SER A O   
4737  C CB  . SER A 635  ? 0.3572 0.5009 0.2448 0.0558  0.0248  0.0617  633  SER A CB  
4738  O OG  . SER A 635  ? 0.4452 0.6015 0.3302 0.0573  0.0245  0.0618  633  SER A OG  
4739  N N   . GLU A 636  ? 0.2408 0.3985 0.1201 0.0634  0.0266  0.0434  634  GLU A N   
4740  C CA  . GLU A 636  ? 0.2635 0.4298 0.1423 0.0658  0.0284  0.0394  634  GLU A CA  
4741  C C   . GLU A 636  ? 0.2541 0.4136 0.1311 0.0682  0.0281  0.0295  634  GLU A C   
4742  O O   . GLU A 636  ? 0.2797 0.4407 0.1584 0.0690  0.0300  0.0276  634  GLU A O   
4743  C CB  . GLU A 636  ? 0.2882 0.4684 0.1641 0.0680  0.0278  0.0382  634  GLU A CB  
4744  C CG  . GLU A 636  ? 0.3443 0.5346 0.2197 0.0708  0.0295  0.0339  634  GLU A CG  
4745  C CD  . GLU A 636  ? 0.4086 0.6009 0.2886 0.0691  0.0324  0.0399  634  GLU A CD  
4746  O OE1 . GLU A 636  ? 0.3680 0.5596 0.2517 0.0656  0.0331  0.0495  634  GLU A OE1 
4747  O OE2 . GLU A 636  ? 0.4400 0.6344 0.3203 0.0711  0.0337  0.0350  634  GLU A OE2 
4748  N N   . ARG A 637  ? 0.2453 0.3974 0.1194 0.0693  0.0256  0.0231  635  ARG A N   
4749  C CA  . ARG A 637  ? 0.2487 0.3925 0.1222 0.0710  0.0250  0.0143  635  ARG A CA  
4750  C C   . ARG A 637  ? 0.2423 0.3768 0.1193 0.0688  0.0269  0.0178  635  ARG A C   
4751  O O   . ARG A 637  ? 0.2497 0.3822 0.1279 0.0701  0.0281  0.0134  635  ARG A O   
4752  C CB  . ARG A 637  ? 0.2355 0.3720 0.1061 0.0720  0.0217  0.0077  635  ARG A CB  
4753  C CG  . ARG A 637  ? 0.2720 0.4175 0.1393 0.0741  0.0196  0.0042  635  ARG A CG  
4754  C CD  . ARG A 637  ? 0.2769 0.4156 0.1419 0.0756  0.0161  -0.0046 635  ARG A CD  
4755  N NE  . ARG A 637  ? 0.2618 0.3900 0.1268 0.0733  0.0146  -0.0021 635  ARG A NE  
4756  C CZ  . ARG A 637  ? 0.2931 0.4215 0.1563 0.0726  0.0123  -0.0006 635  ARG A CZ  
4757  N NH1 . ARG A 637  ? 0.3144 0.4532 0.1756 0.0738  0.0114  -0.0004 635  ARG A NH1 
4758  N NH2 . ARG A 637  ? 0.2773 0.3955 0.1407 0.0708  0.0108  0.0007  635  ARG A NH2 
4759  N N   . ALA A 638  ? 0.2275 0.3564 0.1066 0.0656  0.0271  0.0256  636  ALA A N   
4760  C CA  . ALA A 638  ? 0.2175 0.3379 0.1003 0.0633  0.0288  0.0295  636  ALA A CA  
4761  C C   . ALA A 638  ? 0.2432 0.3704 0.1295 0.0628  0.0317  0.0335  636  ALA A C   
4762  O O   . ALA A 638  ? 0.2421 0.3644 0.1307 0.0625  0.0334  0.0325  636  ALA A O   
4763  C CB  . ALA A 638  ? 0.2437 0.3567 0.1301 0.0596  0.0278  0.0370  636  ALA A CB  
4764  N N   . ALA A 639  ? 0.2263 0.3651 0.1131 0.0627  0.0324  0.0381  637  ALA A N   
4765  C CA  . ALA A 639  ? 0.2416 0.3881 0.1317 0.0623  0.0350  0.0419  637  ALA A CA  
4766  C C   . ALA A 639  ? 0.2587 0.4081 0.1475 0.0656  0.0359  0.0336  637  ALA A C   
4767  O O   . ALA A 639  ? 0.2406 0.3908 0.1326 0.0651  0.0380  0.0350  637  ALA A O   
4768  C CB  . ALA A 639  ? 0.2366 0.3959 0.1271 0.0619  0.0352  0.0477  637  ALA A CB  
4769  N N   . CYS A 640  ? 0.2370 0.3879 0.1215 0.0689  0.0341  0.0248  638  CYS A N   
4770  C CA  . CYS A 640  ? 0.2618 0.4135 0.1457 0.0721  0.0343  0.0160  638  CYS A CA  
4771  C C   . CYS A 640  ? 0.2493 0.3889 0.1354 0.0714  0.0349  0.0137  638  CYS A C   
4772  O O   . CYS A 640  ? 0.2460 0.3866 0.1345 0.0724  0.0366  0.0119  638  CYS A O   
4773  C CB  . CYS A 640  ? 0.2465 0.3996 0.1264 0.0754  0.0315  0.0067  638  CYS A CB  
4774  S SG  . CYS A 640  ? 0.2771 0.4464 0.1543 0.0773  0.0309  0.0073  638  CYS A SG  
4775  N N   . LEU A 641  ? 0.2273 0.3556 0.1127 0.0700  0.0335  0.0135  639  LEU A N   
4776  C CA  . LEU A 641  ? 0.2153 0.3315 0.1036 0.0690  0.0337  0.0115  639  LEU A CA  
4777  C C   . LEU A 641  ? 0.2096 0.3255 0.1028 0.0662  0.0365  0.0191  639  LEU A C   
4778  O O   . LEU A 641  ? 0.2409 0.3524 0.1376 0.0663  0.0374  0.0166  639  LEU A O   
4779  C CB  . LEU A 641  ? 0.2293 0.3322 0.1198 0.0662  0.0307  0.0110  639  LEU A CB  
4780  C CG  . LEU A 641  ? 0.2228 0.3197 0.1114 0.0681  0.0274  0.0015  639  LEU A CG  
4781  C CD1 . LEU A 641  ? 0.2645 0.3727 0.1464 0.0717  0.0265  -0.0023 639  LEU A CD1 
4782  C CD2 . LEU A 641  ? 0.2076 0.2917 0.0993 0.0647  0.0249  0.0025  639  LEU A CD2 
4783  N N   . ASP A 642  ? 0.2355 0.3557 0.1294 0.0637  0.0377  0.0285  640  ASP A N   
4784  C CA  . ASP A 642  ? 0.2164 0.3361 0.1156 0.0608  0.0399  0.0361  640  ASP A CA  
4785  C C   . ASP A 642  ? 0.2259 0.3553 0.1267 0.0624  0.0420  0.0352  640  ASP A C   
4786  O O   . ASP A 642  ? 0.2354 0.3622 0.1399 0.0615  0.0439  0.0368  640  ASP A O   
4787  C CB  . ASP A 642  ? 0.2553 0.3768 0.1570 0.0574  0.0398  0.0460  640  ASP A CB  
4788  C CG  . ASP A 642  ? 0.2458 0.3543 0.1503 0.0544  0.0376  0.0479  640  ASP A CG  
4789  O OD1 . ASP A 642  ? 0.2529 0.3494 0.1602 0.0536  0.0363  0.0428  640  ASP A OD1 
4790  O OD2 . ASP A 642  ? 0.2634 0.3733 0.1682 0.0526  0.0368  0.0544  640  ASP A OD2 
4791  N N   . ARG A 643  ? 0.2401 0.3807 0.1383 0.0648  0.0417  0.0326  641  ARG A N   
4792  C CA  . ARG A 643  ? 0.2340 0.3841 0.1335 0.0668  0.0434  0.0308  641  ARG A CA  
4793  C C   . ARG A 643  ? 0.2334 0.3781 0.1328 0.0695  0.0434  0.0221  641  ARG A C   
4794  O O   . ARG A 643  ? 0.2518 0.3985 0.1544 0.0697  0.0453  0.0225  641  ARG A O   
4795  C CB  . ARG A 643  ? 0.2368 0.4000 0.1333 0.0692  0.0427  0.0291  641  ARG A CB  
4796  C CG  . ARG A 643  ? 0.2451 0.4170 0.1433 0.0667  0.0434  0.0388  641  ARG A CG  
4797  C CD  . ARG A 643  ? 0.2548 0.4414 0.1503 0.0693  0.0432  0.0372  641  ARG A CD  
4798  N NE  . ARG A 643  ? 0.2556 0.4423 0.1461 0.0717  0.0407  0.0309  641  ARG A NE  
4799  C CZ  . ARG A 643  ? 0.2566 0.4445 0.1454 0.0705  0.0393  0.0345  641  ARG A CZ  
4800  N NH1 . ARG A 643  ? 0.2856 0.4740 0.1775 0.0669  0.0399  0.0444  641  ARG A NH1 
4801  N NH2 . ARG A 643  ? 0.2884 0.4767 0.1728 0.0729  0.0370  0.0280  641  ARG A NH2 
4802  N N   . ALA A 644  ? 0.2268 0.3647 0.1230 0.0716  0.0412  0.0141  642  ALA A N   
4803  C CA  . ALA A 644  ? 0.2465 0.3782 0.1434 0.0741  0.0407  0.0057  642  ALA A CA  
4804  C C   . ALA A 644  ? 0.2474 0.3697 0.1480 0.0719  0.0424  0.0088  642  ALA A C   
4805  O O   . ALA A 644  ? 0.2412 0.3617 0.1446 0.0732  0.0431  0.0051  642  ALA A O   
4806  C CB  . ALA A 644  ? 0.2416 0.3666 0.1353 0.0761  0.0375  -0.0027 642  ALA A CB  
4807  N N   . ALA A 645  ? 0.2038 0.3175 0.1072 0.0675  0.0416  0.0151  643  ALA A N   
4808  C CA  . ALA A 645  ? 0.2190 0.3217 0.1288 0.0639  0.0418  0.0182  643  ALA A CA  
4809  C C   . ALA A 645  ? 0.2180 0.3282 0.1308 0.0634  0.0450  0.0237  643  ALA A C   
4810  O O   . ALA A 645  ? 0.2192 0.3240 0.1363 0.0627  0.0456  0.0225  643  ALA A O   
4811  C CB  . ALA A 645  ? 0.2226 0.3163 0.1347 0.0597  0.0403  0.0238  643  ALA A CB  
4812  N N   . GLU A 646  ? 0.2436 0.3665 0.1543 0.0635  0.0472  0.0302  644  GLU A N   
4813  C CA  . GLU A 646  ? 0.2435 0.3739 0.1582 0.0625  0.0497  0.0353  644  GLU A CA  
4814  C C   . GLU A 646  ? 0.2384 0.3737 0.1530 0.0661  0.0504  0.0284  644  GLU A C   
4815  O O   . GLU A 646  ? 0.2409 0.3760 0.1596 0.0656  0.0522  0.0297  644  GLU A O   
4816  C CB  . GLU A 646  ? 0.2943 0.4354 0.2095 0.0609  0.0498  0.0423  644  GLU A CB  
4817  C CG  . GLU A 646  ? 0.3094 0.4460 0.2264 0.0570  0.0490  0.0504  644  GLU A CG  
4818  C CD  . GLU A 646  ? 0.4088 0.5373 0.3317 0.0533  0.0499  0.0563  644  GLU A CD  
4819  O OE1 . GLU A 646  ? 0.4859 0.6171 0.4126 0.0530  0.0517  0.0575  644  GLU A OE1 
4820  O OE2 . GLU A 646  ? 0.3809 0.5002 0.3048 0.0508  0.0487  0.0594  644  GLU A OE2 
4821  N N   . LEU A 647  ? 0.2176 0.3573 0.1283 0.0698  0.0489  0.0207  645  LEU A N   
4822  C CA  . LEU A 647  ? 0.2301 0.3745 0.1411 0.0735  0.0491  0.0135  645  LEU A CA  
4823  C C   . LEU A 647  ? 0.2437 0.3772 0.1568 0.0745  0.0489  0.0081  645  LEU A C   
4824  O O   . LEU A 647  ? 0.2663 0.4018 0.1826 0.0757  0.0501  0.0062  645  LEU A O   
4825  C CB  . LEU A 647  ? 0.2401 0.3907 0.1468 0.0770  0.0470  0.0064  645  LEU A CB  
4826  C CG  . LEU A 647  ? 0.2573 0.4209 0.1621 0.0769  0.0473  0.0108  645  LEU A CG  
4827  C CD1 . LEU A 647  ? 0.2373 0.4052 0.1377 0.0804  0.0448  0.0031  645  LEU A CD1 
4828  C CD2 . LEU A 647  ? 0.3087 0.4837 0.2164 0.0771  0.0496  0.0146  645  LEU A CD2 
4829  N N   . MET A 648  ? 0.2142 0.3357 0.1264 0.0736  0.0470  0.0055  646  MET A N   
4830  C CA  . MET A 648  ? 0.2181 0.3268 0.1349 0.0730  0.0452  0.0008  646  MET A CA  
4831  C C   . MET A 648  ? 0.2446 0.3486 0.1673 0.0693  0.0467  0.0073  646  MET A C   
4832  O O   . MET A 648  ? 0.2360 0.3360 0.1626 0.0699  0.0468  0.0044  646  MET A O   
4833  C CB  . MET A 648  ? 0.2461 0.3416 0.1627 0.0715  0.0416  -0.0027 646  MET A CB  
4834  C CG  . MET A 648  ? 0.2628 0.3605 0.1751 0.0754  0.0393  -0.0111 646  MET A CG  
4835  S SD  . MET A 648  ? 0.2762 0.3569 0.1905 0.0733  0.0350  -0.0157 646  MET A SD  
4836  C CE  . MET A 648  ? 0.2880 0.3742 0.1967 0.0781  0.0325  -0.0247 646  MET A CE  
4837  N N   . GLN A 649  ? 0.2286 0.3330 0.1524 0.0655  0.0478  0.0160  647  GLN A N   
4838  C CA  . GLN A 649  ? 0.2186 0.3190 0.1482 0.0619  0.0491  0.0221  647  GLN A CA  
4839  C C   . GLN A 649  ? 0.2552 0.3666 0.1864 0.0638  0.0521  0.0234  647  GLN A C   
4840  O O   . GLN A 649  ? 0.2370 0.3442 0.1730 0.0629  0.0526  0.0234  647  GLN A O   
4841  C CB  . GLN A 649  ? 0.2471 0.3466 0.1780 0.0577  0.0494  0.0311  647  GLN A CB  
4842  C CG  . GLN A 649  ? 0.2524 0.3470 0.1898 0.0539  0.0503  0.0372  647  GLN A CG  
4843  C CD  . GLN A 649  ? 0.2578 0.3371 0.1987 0.0514  0.0478  0.0346  647  GLN A CD  
4844  O OE1 . GLN A 649  ? 0.2266 0.2983 0.1675 0.0492  0.0460  0.0358  647  GLN A OE1 
4845  N NE2 . GLN A 649  ? 0.2663 0.3416 0.2104 0.0520  0.0479  0.0310  647  GLN A NE2 
4846  N N   . ALA A 650  ? 0.2432 0.3695 0.1704 0.0665  0.0541  0.0244  648  ALA A N   
4847  C CA  . ALA A 650  ? 0.2590 0.3962 0.1883 0.0681  0.0564  0.0253  648  ALA A CA  
4848  C C   . ALA A 650  ? 0.3000 0.4361 0.2298 0.0722  0.0561  0.0162  648  ALA A C   
4849  O O   . ALA A 650  ? 0.3072 0.4462 0.2409 0.0725  0.0576  0.0167  648  ALA A O   
4850  C CB  . ALA A 650  ? 0.2728 0.4230 0.1999 0.0687  0.0564  0.0275  648  ALA A CB  
4851  N N   . ARG A 651  ? 0.2405 0.3722 0.1668 0.0752  0.0538  0.0079  649  ARG A N   
4852  C CA  . ARG A 651  ? 0.2500 0.3803 0.1772 0.0792  0.0525  -0.0013 649  ARG A CA  
4853  C C   . ARG A 651  ? 0.2589 0.3738 0.1906 0.0777  0.0504  -0.0042 649  ARG A C   
4854  O O   . ARG A 651  ? 0.2611 0.3728 0.1942 0.0809  0.0488  -0.0120 649  ARG A O   
4855  C CB  . ARG A 651  ? 0.3031 0.4358 0.2260 0.0824  0.0498  -0.0089 649  ARG A CB  
4856  C CG  . ARG A 651  ? 0.3517 0.4868 0.2760 0.0867  0.0484  -0.0179 649  ARG A CG  
4857  C CD  . ARG A 651  ? 0.3249 0.4712 0.2458 0.0893  0.0473  -0.0212 649  ARG A CD  
4858  N NE  . ARG A 651  ? 0.3468 0.4941 0.2691 0.0935  0.0454  -0.0305 649  ARG A NE  
4859  C CZ  . ARG A 651  ? 0.3084 0.4625 0.2337 0.0953  0.0466  -0.0317 649  ARG A CZ  
4860  N NH1 . ARG A 651  ? 0.3517 0.5119 0.2791 0.0933  0.0498  -0.0242 649  ARG A NH1 
4861  N NH2 . ARG A 651  ? 0.3323 0.4869 0.2590 0.0992  0.0444  -0.0405 649  ARG A NH2 
4862  N N   . MET A 652  ? 0.2405 0.3453 0.1751 0.0727  0.0498  0.0018  650  MET A N   
4863  C CA  . MET A 652  ? 0.2602 0.3500 0.1990 0.0706  0.0472  -0.0008 650  MET A CA  
4864  C C   . MET A 652  ? 0.2725 0.3609 0.2155 0.0727  0.0472  -0.0049 650  MET A C   
4865  O O   . MET A 652  ? 0.2743 0.3542 0.2187 0.0740  0.0444  -0.0113 650  MET A O   
4866  C CB  . MET A 652  ? 0.2307 0.3124 0.1726 0.0651  0.0472  0.0068  650  MET A CB  
4867  C CG  . MET A 652  ? 0.2440 0.3115 0.1900 0.0629  0.0447  0.0047  650  MET A CG  
4868  S SD  . MET A 652  ? 0.2776 0.3364 0.2273 0.0567  0.0446  0.0126  650  MET A SD  
4869  C CE  . MET A 652  ? 0.2595 0.3136 0.2049 0.0556  0.0424  0.0124  650  MET A CE  
4870  N N   . PRO A 653  ? 0.2518 0.3484 0.1975 0.0731  0.0500  -0.0016 651  PRO A N   
4871  C CA  . PRO A 653  ? 0.2621 0.3565 0.2124 0.0750  0.0497  -0.0056 651  PRO A CA  
4872  C C   . PRO A 653  ? 0.2619 0.3590 0.2107 0.0805  0.0482  -0.0152 651  PRO A C   
4873  O O   . PRO A 653  ? 0.2568 0.3453 0.2092 0.0815  0.0458  -0.0202 651  PRO A O   
4874  C CB  . PRO A 653  ? 0.2676 0.3730 0.2202 0.0747  0.0534  0.0001  651  PRO A CB  
4875  C CG  . PRO A 653  ? 0.2947 0.4021 0.2461 0.0705  0.0548  0.0088  651  PRO A CG  
4876  C CD  . PRO A 653  ? 0.2842 0.3912 0.2299 0.0713  0.0534  0.0066  651  PRO A CD  
4877  N N   . THR A 654  ? 0.2490 0.3579 0.1929 0.0842  0.0494  -0.0179 652  THR A N   
4878  C CA  . THR A 654  ? 0.2294 0.3407 0.1717 0.0897  0.0475  -0.0278 652  THR A CA  
4879  C C   . THR A 654  ? 0.2859 0.3844 0.2276 0.0892  0.0433  -0.0328 652  THR A C   
4880  O O   . THR A 654  ? 0.2706 0.3631 0.2149 0.0918  0.0405  -0.0402 652  THR A O   
4881  C CB  . THR A 654  ? 0.2727 0.3976 0.2109 0.0915  0.0482  -0.0284 652  THR A CB  
4882  O OG1 . THR A 654  ? 0.2830 0.4187 0.2230 0.0907  0.0514  -0.0227 652  THR A OG1 
4883  C CG2 . THR A 654  ? 0.2637 0.3896 0.2021 0.0958  0.0451  -0.0382 652  THR A CG2 
4884  N N   . LEU A 655  ? 0.2579 0.3521 0.1965 0.0858  0.0427  -0.0289 653  LEU A N   
4885  C CA  . LEU A 655  ? 0.2415 0.3236 0.1797 0.0848  0.0388  -0.0330 653  LEU A CA  
4886  C C   . LEU A 655  ? 0.2972 0.3655 0.2414 0.0824  0.0365  -0.0334 653  LEU A C   
4887  O O   . LEU A 655  ? 0.2563 0.3164 0.2022 0.0836  0.0330  -0.0396 653  LEU A O   
4888  C CB  . LEU A 655  ? 0.2582 0.3385 0.1926 0.0812  0.0387  -0.0277 653  LEU A CB  
4889  C CG  . LEU A 655  ? 0.2475 0.3408 0.1756 0.0833  0.0405  -0.0269 653  LEU A CG  
4890  C CD1 . LEU A 655  ? 0.2580 0.3473 0.1832 0.0797  0.0397  -0.0221 653  LEU A CD1 
4891  C CD2 . LEU A 655  ? 0.3087 0.4080 0.2338 0.0889  0.0389  -0.0364 653  LEU A CD2 
4892  N N   . LEU A 656  ? 0.2758 0.3418 0.2236 0.0789  0.0383  -0.0268 654  LEU A N   
4893  C CA  . LEU A 656  ? 0.2756 0.3298 0.2289 0.0766  0.0363  -0.0269 654  LEU A CA  
4894  C C   . LEU A 656  ? 0.2622 0.3156 0.2190 0.0808  0.0345  -0.0342 654  LEU A C   
4895  O O   . LEU A 656  ? 0.2903 0.3331 0.2503 0.0804  0.0311  -0.0377 654  LEU A O   
4896  C CB  . LEU A 656  ? 0.2759 0.3304 0.2326 0.0731  0.0388  -0.0193 654  LEU A CB  
4897  C CG  . LEU A 656  ? 0.2571 0.3114 0.2121 0.0686  0.0404  -0.0115 654  LEU A CG  
4898  C CD1 . LEU A 656  ? 0.2804 0.3338 0.2399 0.0656  0.0422  -0.0055 654  LEU A CD1 
4899  C CD2 . LEU A 656  ? 0.2767 0.3203 0.2306 0.0658  0.0377  -0.0117 654  LEU A CD2 
4900  N N   . GLY A 657  ? 0.2648 0.3295 0.2215 0.0848  0.0368  -0.0362 655  GLY A N   
4901  C CA  . GLY A 657  ? 0.3165 0.3811 0.2771 0.0891  0.0352  -0.0433 655  GLY A CA  
4902  C C   . GLY A 657  ? 0.2681 0.3282 0.2277 0.0922  0.0313  -0.0517 655  GLY A C   
4903  O O   . GLY A 657  ? 0.2830 0.3353 0.2474 0.0936  0.0281  -0.0567 655  GLY A O   
4904  N N   . LEU A 658  ? 0.2601 0.3253 0.2140 0.0933  0.0314  -0.0534 656  LEU A N   
4905  C CA  . LEU A 658  ? 0.2798 0.3412 0.2328 0.0963  0.0275  -0.0618 656  LEU A CA  
4906  C C   . LEU A 658  ? 0.2665 0.3127 0.2221 0.0923  0.0238  -0.0612 656  LEU A C   
4907  O O   . LEU A 658  ? 0.2819 0.3207 0.2411 0.0940  0.0198  -0.0675 656  LEU A O   
4908  C CB  . LEU A 658  ? 0.2416 0.3132 0.1878 0.0981  0.0285  -0.0633 656  LEU A CB  
4909  C CG  . LEU A 658  ? 0.2882 0.3568 0.2339 0.0997  0.0240  -0.0709 656  LEU A CG  
4910  C CD1 . LEU A 658  ? 0.2931 0.3607 0.2444 0.1027  0.0211  -0.0779 656  LEU A CD1 
4911  C CD2 . LEU A 658  ? 0.2472 0.3273 0.1867 0.1004  0.0251  -0.0706 656  LEU A CD2 
4912  N N   . ILE A 659  ? 0.2313 0.2728 0.1856 0.0870  0.0249  -0.0535 657  ILE A N   
4913  C CA  . ILE A 659  ? 0.2229 0.2510 0.1795 0.0831  0.0216  -0.0526 657  ILE A CA  
4914  C C   . ILE A 659  ? 0.2683 0.2877 0.2318 0.0821  0.0198  -0.0527 657  ILE A C   
4915  O O   . ILE A 659  ? 0.2500 0.2598 0.2171 0.0816  0.0159  -0.0560 657  ILE A O   
4916  C CB  . ILE A 659  ? 0.2325 0.2587 0.1863 0.0780  0.0233  -0.0446 657  ILE A CB  
4917  C CG1 . ILE A 659  ? 0.2589 0.2926 0.2062 0.0791  0.0243  -0.0450 657  ILE A CG1 
4918  C CG2 . ILE A 659  ? 0.2461 0.2592 0.2030 0.0738  0.0204  -0.0431 657  ILE A CG2 
4919  C CD1 . ILE A 659  ? 0.2689 0.3027 0.2135 0.0747  0.0264  -0.0369 657  ILE A CD1 
4920  N N   . ILE A 660  ? 0.2607 0.2836 0.2267 0.0817  0.0225  -0.0488 658  ILE A N   
4921  C CA  . ILE A 660  ? 0.2420 0.2576 0.2145 0.0809  0.0209  -0.0487 658  ILE A CA  
4922  C C   . ILE A 660  ? 0.2382 0.2515 0.2146 0.0854  0.0173  -0.0571 658  ILE A C   
4923  O O   . ILE A 660  ? 0.2703 0.2733 0.2516 0.0843  0.0137  -0.0586 658  ILE A O   
4924  C CB  . ILE A 660  ? 0.2699 0.2918 0.2441 0.0806  0.0245  -0.0440 658  ILE A CB  
4925  C CG1 . ILE A 660  ? 0.2491 0.2698 0.2217 0.0753  0.0269  -0.0354 658  ILE A CG1 
4926  C CG2 . ILE A 660  ? 0.2423 0.2595 0.2234 0.0817  0.0228  -0.0457 658  ILE A CG2 
4927  C CD1 . ILE A 660  ? 0.2700 0.2985 0.2436 0.0749  0.0307  -0.0305 658  ILE A CD1 
4928  N N   . ARG A 661  ? 0.2266 0.2497 0.2011 0.0907  0.0183  -0.0628 659  ARG A N   
4929  C CA  . ARG A 661  ? 0.2623 0.2840 0.2412 0.0956  0.0150  -0.0712 659  ARG A CA  
4930  C C   . ARG A 661  ? 0.2923 0.3088 0.2706 0.0970  0.0108  -0.0777 659  ARG A C   
4931  O O   . ARG A 661  ? 0.2924 0.3008 0.2765 0.0980  0.0065  -0.0823 659  ARG A O   
4932  C CB  . ARG A 661  ? 0.3212 0.3563 0.2990 0.1010  0.0177  -0.0750 659  ARG A CB  
4933  C CG  . ARG A 661  ? 0.2932 0.3312 0.2746 0.1004  0.0205  -0.0703 659  ARG A CG  
4934  C CD  . ARG A 661  ? 0.2962 0.3478 0.2771 0.1043  0.0232  -0.0726 659  ARG A CD  
4935  N NE  . ARG A 661  ? 0.3546 0.4066 0.3384 0.1073  0.0197  -0.0803 659  ARG A NE  
4936  C CZ  . ARG A 661  ? 0.3277 0.3888 0.3078 0.1096  0.0197  -0.0843 659  ARG A CZ  
4937  N NH1 . ARG A 661  ? 0.3456 0.4161 0.3189 0.1090  0.0229  -0.0812 659  ARG A NH1 
4938  N NH2 . ARG A 661  ? 0.3450 0.4060 0.3285 0.1125  0.0163  -0.0913 659  ARG A NH2 
4939  N N   . GLU A 662  ? 0.2474 0.2681 0.2192 0.0967  0.0116  -0.0779 660  GLU A N   
4940  C CA  . GLU A 662  ? 0.2815 0.2973 0.2531 0.0975  0.0073  -0.0838 660  GLU A CA  
4941  C C   . GLU A 662  ? 0.2637 0.2663 0.2379 0.0929  0.0043  -0.0809 660  GLU A C   
4942  O O   . GLU A 662  ? 0.2799 0.2744 0.2583 0.0935  -0.0005 -0.0859 660  GLU A O   
4943  C CB  . GLU A 662  ? 0.3144 0.3398 0.2787 0.0983  0.0088  -0.0848 660  GLU A CB  
4944  C CG  . GLU A 662  ? 0.3044 0.3251 0.2686 0.0982  0.0042  -0.0900 660  GLU A CG  
4945  C CD  . GLU A 662  ? 0.2858 0.3163 0.2427 0.0991  0.0055  -0.0909 660  GLU A CD  
4946  O OE1 . GLU A 662  ? 0.3112 0.3477 0.2624 0.0980  0.0095  -0.0854 660  GLU A OE1 
4947  O OE2 . GLU A 662  ? 0.3210 0.3535 0.2784 0.1010  0.0024  -0.0970 660  GLU A OE2 
4948  N N   . ALA A 663  ? 0.2507 0.2512 0.2228 0.0877  0.0067  -0.0725 661  ALA A N   
4949  C CA  . ALA A 663  ? 0.2407 0.2306 0.2141 0.0827  0.0043  -0.0690 661  ALA A CA  
4950  C C   . ALA A 663  ? 0.2446 0.2260 0.2239 0.0791  0.0036  -0.0642 661  ALA A C   
4951  O O   . ALA A 663  ? 0.2769 0.2496 0.2581 0.0751  0.0013  -0.0614 661  ALA A O   
4952  C CB  . ALA A 663  ? 0.2568 0.2499 0.2238 0.0794  0.0071  -0.0633 661  ALA A CB  
4953  N N   . GLY A 664  ? 0.2405 0.2248 0.2228 0.0806  0.0053  -0.0631 662  GLY A N   
4954  C CA  . GLY A 664  ? 0.2596 0.2366 0.2475 0.0775  0.0044  -0.0588 662  GLY A CA  
4955  C C   . GLY A 664  ? 0.2675 0.2434 0.2535 0.0723  0.0073  -0.0503 662  GLY A C   
4956  O O   . GLY A 664  ? 0.2610 0.2297 0.2511 0.0688  0.0059  -0.0466 662  GLY A O   
4957  N N   . LYS A 665  ? 0.2457 0.2289 0.2259 0.0716  0.0111  -0.0471 663  LYS A N   
4958  C CA  . LYS A 665  ? 0.2489 0.2309 0.2273 0.0667  0.0134  -0.0395 663  LYS A CA  
4959  C C   . LYS A 665  ? 0.2294 0.2159 0.2094 0.0663  0.0166  -0.0351 663  LYS A C   
4960  O O   . LYS A 665  ? 0.2415 0.2353 0.2217 0.0699  0.0183  -0.0373 663  LYS A O   
4961  C CB  . LYS A 665  ? 0.2499 0.2368 0.2220 0.0659  0.0154  -0.0378 663  LYS A CB  
4962  C CG  . LYS A 665  ? 0.2446 0.2269 0.2150 0.0656  0.0123  -0.0411 663  LYS A CG  
4963  C CD  . LYS A 665  ? 0.3073 0.2916 0.2726 0.0629  0.0141  -0.0369 663  LYS A CD  
4964  C CE  . LYS A 665  ? 0.3212 0.3001 0.2856 0.0619  0.0109  -0.0396 663  LYS A CE  
4965  N NZ  . LYS A 665  ? 0.2931 0.2729 0.2532 0.0590  0.0124  -0.0351 663  LYS A NZ  
4966  N N   . SER A 666  ? 0.2280 0.2106 0.2089 0.0617  0.0175  -0.0290 664  SER A N   
4967  C CA  . SER A 666  ? 0.2337 0.2207 0.2157 0.0605  0.0207  -0.0241 664  SER A CA  
4968  C C   . SER A 666  ? 0.2696 0.2655 0.2466 0.0608  0.0243  -0.0215 664  SER A C   
4969  O O   . SER A 666  ? 0.2517 0.2490 0.2244 0.0607  0.0244  -0.0219 664  SER A O   
4970  C CB  . SER A 666  ? 0.2495 0.2300 0.2336 0.0556  0.0203  -0.0187 664  SER A CB  
4971  O OG  . SER A 666  ? 0.2366 0.2160 0.2169 0.0526  0.0209  -0.0158 664  SER A OG  
4972  N N   . ALA A 667  ? 0.2444 0.2467 0.2226 0.0612  0.0272  -0.0184 665  ALA A N   
4973  C CA  . ALA A 667  ? 0.2529 0.2639 0.2273 0.0611  0.0306  -0.0149 665  ALA A CA  
4974  C C   . ALA A 667  ? 0.2479 0.2553 0.2202 0.0566  0.0310  -0.0098 665  ALA A C   
4975  O O   . ALA A 667  ? 0.2191 0.2310 0.1872 0.0567  0.0323  -0.0085 665  ALA A O   
4976  C CB  . ALA A 667  ? 0.2696 0.2875 0.2467 0.0616  0.0334  -0.0118 665  ALA A CB  
4977  N N   . LEU A 668  ? 0.2369 0.2367 0.2121 0.0529  0.0299  -0.0069 666  LEU A N   
4978  C CA  . LEU A 668  ? 0.2103 0.2064 0.1840 0.0489  0.0299  -0.0027 666  LEU A CA  
4979  C C   . LEU A 668  ? 0.2310 0.2248 0.2009 0.0492  0.0283  -0.0052 666  LEU A C   
4980  O O   . LEU A 668  ? 0.2340 0.2302 0.2006 0.0481  0.0295  -0.0026 666  LEU A O   
4981  C CB  . LEU A 668  ? 0.2980 0.2864 0.2755 0.0455  0.0284  -0.0007 666  LEU A CB  
4982  C CG  . LEU A 668  ? 0.3150 0.2998 0.2922 0.0413  0.0286  0.0037  666  LEU A CG  
4983  C CD1 . LEU A 668  ? 0.4190 0.4098 0.3960 0.0403  0.0314  0.0084  666  LEU A CD1 
4984  C CD2 . LEU A 668  ? 0.3788 0.3575 0.3600 0.0388  0.0270  0.0048  666  LEU A CD2 
4985  N N   . ASN A 669  ? 0.2065 0.1954 0.1770 0.0506  0.0255  -0.0101 667  ASN A N   
4986  C CA  . ASN A 669  ? 0.2200 0.2064 0.1873 0.0508  0.0237  -0.0127 667  ASN A CA  
4987  C C   . ASN A 669  ? 0.2195 0.2140 0.1825 0.0543  0.0249  -0.0153 667  ASN A C   
4988  O O   . ASN A 669  ? 0.2114 0.2065 0.1707 0.0540  0.0245  -0.0154 667  ASN A O   
4989  C CB  . ASN A 669  ? 0.2102 0.1892 0.1801 0.0511  0.0200  -0.0170 667  ASN A CB  
4990  C CG  . ASN A 669  ? 0.2217 0.1931 0.1952 0.0472  0.0186  -0.0140 667  ASN A CG  
4991  O OD1 . ASN A 669  ? 0.2754 0.2455 0.2481 0.0438  0.0196  -0.0096 667  ASN A OD1 
4992  N ND2 . ASN A 669  ? 0.2087 0.1752 0.1862 0.0477  0.0161  -0.0163 667  ASN A ND2 
4993  N N   . ALA A 670  ? 0.2033 0.2046 0.1666 0.0579  0.0262  -0.0176 668  ALA A N   
4994  C CA  . ALA A 670  ? 0.2001 0.2106 0.1591 0.0614  0.0276  -0.0199 668  ALA A CA  
4995  C C   . ALA A 670  ? 0.2321 0.2488 0.1879 0.0596  0.0306  -0.0139 668  ALA A C   
4996  O O   . ALA A 670  ? 0.2185 0.2402 0.1699 0.0607  0.0310  -0.0143 668  ALA A O   
4997  C CB  . ALA A 670  ? 0.2140 0.2311 0.1744 0.0657  0.0285  -0.0238 668  ALA A CB  
4998  N N   . ILE A 671  ? 0.2051 0.2220 0.1635 0.0568  0.0325  -0.0081 669  ILE A N   
4999  C CA  . ILE A 671  ? 0.1992 0.2211 0.1558 0.0547  0.0349  -0.0019 669  ILE A CA  
5000  C C   . ILE A 671  ? 0.2337 0.2505 0.1879 0.0522  0.0335  -0.0006 669  ILE A C   
5001  O O   . ILE A 671  ? 0.2352 0.2572 0.1857 0.0525  0.0344  0.0013  669  ILE A O   
5002  C CB  . ILE A 671  ? 0.2139 0.2351 0.1747 0.0518  0.0366  0.0036  669  ILE A CB  
5003  C CG1 . ILE A 671  ? 0.2326 0.2608 0.1955 0.0544  0.0384  0.0028  669  ILE A CG1 
5004  C CG2 . ILE A 671  ? 0.2359 0.2600 0.1956 0.0490  0.0383  0.0101  669  ILE A CG2 
5005  C CD1 . ILE A 671  ? 0.2400 0.2658 0.2080 0.0517  0.0393  0.0069  669  ILE A CD1 
5006  N N   . ALA A 672  ? 0.1985 0.2054 0.1549 0.0498  0.0312  -0.0013 670  ALA A N   
5007  C CA  . ALA A 672  ? 0.2029 0.2048 0.1575 0.0474  0.0297  -0.0003 670  ALA A CA  
5008  C C   . ALA A 672  ? 0.2218 0.2258 0.1721 0.0500  0.0283  -0.0046 670  ALA A C   
5009  O O   . ALA A 672  ? 0.2286 0.2332 0.1761 0.0489  0.0281  -0.0029 670  ALA A O   
5010  C CB  . ALA A 672  ? 0.2150 0.2071 0.1730 0.0446  0.0275  -0.0007 670  ALA A CB  
5011  N N   . GLU A 673  ? 0.1948 0.2002 0.1449 0.0534  0.0272  -0.0105 671  GLU A N   
5012  C CA  . GLU A 673  ? 0.2145 0.2220 0.1608 0.0560  0.0256  -0.0152 671  GLU A CA  
5013  C C   . GLU A 673  ? 0.2240 0.2425 0.1657 0.0581  0.0279  -0.0138 671  GLU A C   
5014  O O   . GLU A 673  ? 0.2230 0.2434 0.1609 0.0584  0.0272  -0.0142 671  GLU A O   
5015  C CB  . GLU A 673  ? 0.2250 0.2306 0.1728 0.0592  0.0233  -0.0223 671  GLU A CB  
5016  C CG  . GLU A 673  ? 0.2743 0.2841 0.2180 0.0625  0.0219  -0.0277 671  GLU A CG  
5017  C CD  . GLU A 673  ? 0.2767 0.2810 0.2225 0.0645  0.0183  -0.0348 671  GLU A CD  
5018  O OE1 . GLU A 673  ? 0.2924 0.2917 0.2430 0.0644  0.0172  -0.0362 671  GLU A OE1 
5019  O OE2 . GLU A 673  ? 0.2572 0.2624 0.2003 0.0661  0.0163  -0.0391 671  GLU A OE2 
5020  N N   . VAL A 674  ? 0.2099 0.2363 0.1520 0.0597  0.0307  -0.0120 672  VAL A N   
5021  C CA  . VAL A 674  ? 0.2203 0.2581 0.1582 0.0614  0.0331  -0.0096 672  VAL A CA  
5022  C C   . VAL A 674  ? 0.2188 0.2562 0.1559 0.0578  0.0340  -0.0025 672  VAL A C   
5023  O O   . VAL A 674  ? 0.1929 0.2359 0.1258 0.0585  0.0343  -0.0013 672  VAL A O   
5024  C CB  . VAL A 674  ? 0.2111 0.2579 0.1502 0.0635  0.0360  -0.0084 672  VAL A CB  
5025  C CG1 . VAL A 674  ? 0.2037 0.2631 0.1386 0.0648  0.0386  -0.0049 672  VAL A CG1 
5026  C CG2 . VAL A 674  ? 0.2237 0.2714 0.1638 0.0676  0.0348  -0.0161 672  VAL A CG2 
5027  N N   . ARG A 675  ? 0.2107 0.2415 0.1517 0.0540  0.0342  0.0020  673  ARG A N   
5028  C CA  . ARG A 675  ? 0.1943 0.2232 0.1353 0.0506  0.0345  0.0081  673  ARG A CA  
5029  C C   . ARG A 675  ? 0.2120 0.2370 0.1501 0.0504  0.0322  0.0059  673  ARG A C   
5030  O O   . ARG A 675  ? 0.2023 0.2310 0.1378 0.0498  0.0325  0.0093  673  ARG A O   
5031  C CB  . ARG A 675  ? 0.1705 0.1916 0.1166 0.0469  0.0344  0.0116  673  ARG A CB  
5032  C CG  . ARG A 675  ? 0.2174 0.2429 0.1667 0.0463  0.0369  0.0156  673  ARG A CG  
5033  C CD  . ARG A 675  ? 0.2090 0.2271 0.1628 0.0423  0.0365  0.0195  673  ARG A CD  
5034  N NE  . ARG A 675  ? 0.2018 0.2195 0.1554 0.0399  0.0364  0.0244  673  ARG A NE  
5035  C CZ  . ARG A 675  ? 0.2033 0.2143 0.1602 0.0366  0.0356  0.0271  673  ARG A CZ  
5036  N NH1 . ARG A 675  ? 0.2043 0.2088 0.1646 0.0352  0.0347  0.0255  673  ARG A NH1 
5037  N NH2 . ARG A 675  ? 0.2082 0.2194 0.1654 0.0348  0.0354  0.0315  673  ARG A NH2 
5038  N N   . GLU A 676  ? 0.1886 0.2060 0.1273 0.0506  0.0296  0.0005  674  GLU A N   
5039  C CA  . GLU A 676  ? 0.2152 0.2286 0.1517 0.0501  0.0272  -0.0016 674  GLU A CA  
5040  C C   . GLU A 676  ? 0.2211 0.2425 0.1524 0.0533  0.0271  -0.0042 674  GLU A C   
5041  O O   . GLU A 676  ? 0.1990 0.2213 0.1277 0.0526  0.0264  -0.0026 674  GLU A O   
5042  C CB  . GLU A 676  ? 0.2095 0.2139 0.1483 0.0497  0.0244  -0.0067 674  GLU A CB  
5043  C CG  . GLU A 676  ? 0.2459 0.2456 0.1834 0.0486  0.0218  -0.0083 674  GLU A CG  
5044  C CD  . GLU A 676  ? 0.3531 0.3435 0.2940 0.0471  0.0191  -0.0115 674  GLU A CD  
5045  O OE1 . GLU A 676  ? 0.3963 0.3832 0.3409 0.0463  0.0193  -0.0113 674  GLU A OE1 
5046  O OE2 . GLU A 676  ? 0.4039 0.3908 0.3440 0.0466  0.0167  -0.0138 674  GLU A OE2 
5047  N N   . ALA A 677  ? 0.2046 0.2326 0.1344 0.0570  0.0278  -0.0082 675  ALA A N   
5048  C CA  . ALA A 677  ? 0.2022 0.2393 0.1267 0.0603  0.0278  -0.0108 675  ALA A CA  
5049  C C   . ALA A 677  ? 0.1920 0.2375 0.1140 0.0594  0.0302  -0.0040 675  ALA A C   
5050  O O   . ALA A 677  ? 0.1992 0.2484 0.1173 0.0600  0.0295  -0.0036 675  ALA A O   
5051  C CB  . ALA A 677  ? 0.2056 0.2492 0.1294 0.0646  0.0284  -0.0164 675  ALA A CB  
5052  N N   . ILE A 678  ? 0.1901 0.2386 0.1145 0.0580  0.0329  0.0017  676  ILE A N   
5053  C CA  . ILE A 678  ? 0.1957 0.2515 0.1190 0.0567  0.0349  0.0092  676  ILE A CA  
5054  C C   . ILE A 678  ? 0.1918 0.2411 0.1154 0.0535  0.0334  0.0129  676  ILE A C   
5055  O O   . ILE A 678  ? 0.1901 0.2451 0.1108 0.0535  0.0336  0.0163  676  ILE A O   
5056  C CB  . ILE A 678  ? 0.1999 0.2581 0.1271 0.0552  0.0376  0.0146  676  ILE A CB  
5057  C CG1 . ILE A 678  ? 0.2153 0.2824 0.1417 0.0588  0.0394  0.0113  676  ILE A CG1 
5058  C CG2 . ILE A 678  ? 0.2146 0.2780 0.1422 0.0528  0.0392  0.0233  676  ILE A CG2 
5059  C CD1 . ILE A 678  ? 0.2087 0.2755 0.1400 0.0573  0.0414  0.0148  676  ILE A CD1 
5060  N N   . ASP A 679  ? 0.1809 0.2189 0.1084 0.0508  0.0319  0.0123  677  ASP A N   
5061  C CA  . ASP A 679  ? 0.1819 0.2135 0.1105 0.0478  0.0304  0.0155  677  ASP A CA  
5062  C C   . ASP A 679  ? 0.2136 0.2454 0.1381 0.0491  0.0282  0.0120  677  ASP A C   
5063  O O   . ASP A 679  ? 0.1849 0.2180 0.1083 0.0480  0.0278  0.0159  677  ASP A O   
5064  C CB  . ASP A 679  ? 0.1970 0.2175 0.1303 0.0450  0.0292  0.0147  677  ASP A CB  
5065  C CG  . ASP A 679  ? 0.2378 0.2574 0.1756 0.0431  0.0310  0.0189  677  ASP A CG  
5066  O OD1 . ASP A 679  ? 0.2453 0.2716 0.1836 0.0429  0.0331  0.0242  677  ASP A OD1 
5067  O OD2 . ASP A 679  ? 0.2392 0.2514 0.1805 0.0417  0.0303  0.0172  677  ASP A OD2 
5068  N N   . PHE A 680  ? 0.1918 0.2224 0.1145 0.0515  0.0266  0.0048  678  PHE A N   
5069  C CA  . PHE A 680  ? 0.1974 0.2289 0.1162 0.0530  0.0243  0.0010  678  PHE A CA  
5070  C C   . PHE A 680  ? 0.1866 0.2295 0.1006 0.0549  0.0256  0.0037  678  PHE A C   
5071  O O   . PHE A 680  ? 0.2102 0.2542 0.1220 0.0544  0.0244  0.0054  678  PHE A O   
5072  C CB  . PHE A 680  ? 0.1967 0.2263 0.1147 0.0557  0.0224  -0.0073 678  PHE A CB  
5073  C CG  . PHE A 680  ? 0.2046 0.2229 0.1264 0.0537  0.0199  -0.0104 678  PHE A CG  
5074  C CD1 . PHE A 680  ? 0.2169 0.2289 0.1396 0.0510  0.0182  -0.0090 678  PHE A CD1 
5075  C CD2 . PHE A 680  ? 0.1990 0.2133 0.1237 0.0545  0.0193  -0.0147 678  PHE A CD2 
5076  C CE1 . PHE A 680  ? 0.2334 0.2360 0.1596 0.0491  0.0160  -0.0116 678  PHE A CE1 
5077  C CE2 . PHE A 680  ? 0.2316 0.2362 0.1600 0.0526  0.0170  -0.0171 678  PHE A CE2 
5078  C CZ  . PHE A 680  ? 0.2201 0.2191 0.1492 0.0498  0.0154  -0.0154 678  PHE A CZ  
5079  N N   . LEU A 681  ? 0.1892 0.2413 0.1016 0.0573  0.0279  0.0040  679  LEU A N   
5080  C CA  . LEU A 681  ? 0.1937 0.2583 0.1014 0.0593  0.0292  0.0066  679  LEU A CA  
5081  C C   . LEU A 681  ? 0.2043 0.2701 0.1129 0.0563  0.0300  0.0154  679  LEU A C   
5082  O O   . LEU A 681  ? 0.2007 0.2711 0.1059 0.0567  0.0292  0.0172  679  LEU A O   
5083  C CB  . LEU A 681  ? 0.1962 0.2706 0.1029 0.0619  0.0319  0.0061  679  LEU A CB  
5084  C CG  . LEU A 681  ? 0.2084 0.2844 0.1135 0.0659  0.0309  -0.0032 679  LEU A CG  
5085  C CD1 . LEU A 681  ? 0.2151 0.2981 0.1213 0.0679  0.0336  -0.0034 679  LEU A CD1 
5086  C CD2 . LEU A 681  ? 0.2255 0.3096 0.1245 0.0693  0.0296  -0.0077 679  LEU A CD2 
5087  N N   . ARG A 682  ? 0.2083 0.2698 0.1218 0.0533  0.0313  0.0209  680  ARG A N   
5088  C CA  . ARG A 682  ? 0.2039 0.2664 0.1193 0.0506  0.0319  0.0293  680  ARG A CA  
5089  C C   . ARG A 682  ? 0.1989 0.2526 0.1155 0.0484  0.0293  0.0296  680  ARG A C   
5090  O O   . ARG A 682  ? 0.2034 0.2598 0.1196 0.0474  0.0289  0.0348  680  ARG A O   
5091  C CB  . ARG A 682  ? 0.1914 0.2518 0.1123 0.0481  0.0338  0.0346  680  ARG A CB  
5092  C CG  . ARG A 682  ? 0.2187 0.2901 0.1386 0.0500  0.0367  0.0362  680  ARG A CG  
5093  C CD  . ARG A 682  ? 0.1935 0.2624 0.1192 0.0474  0.0383  0.0411  680  ARG A CD  
5094  N NE  . ARG A 682  ? 0.2088 0.2891 0.1339 0.0490  0.0411  0.0434  680  ARG A NE  
5095  C CZ  . ARG A 682  ? 0.2303 0.3104 0.1598 0.0479  0.0428  0.0457  680  ARG A CZ  
5096  N NH1 . ARG A 682  ? 0.2326 0.3018 0.1673 0.0451  0.0420  0.0459  680  ARG A NH1 
5097  N NH2 . ARG A 682  ? 0.2660 0.3578 0.1946 0.0496  0.0455  0.0477  680  ARG A NH2 
5098  N N   . TYR A 683  ? 0.1951 0.2387 0.1135 0.0478  0.0275  0.0243  681  TYR A N   
5099  C CA  . TYR A 683  ? 0.1797 0.2154 0.0995 0.0458  0.0251  0.0242  681  TYR A CA  
5100  C C   . TYR A 683  ? 0.2078 0.2474 0.1227 0.0477  0.0233  0.0215  681  TYR A C   
5101  O O   . TYR A 683  ? 0.2046 0.2441 0.1194 0.0465  0.0223  0.0251  681  TYR A O   
5102  C CB  . TYR A 683  ? 0.1803 0.2055 0.1034 0.0445  0.0238  0.0194  681  TYR A CB  
5103  C CG  . TYR A 683  ? 0.2026 0.2204 0.1270 0.0427  0.0214  0.0187  681  TYR A CG  
5104  C CD1 . TYR A 683  ? 0.2052 0.2185 0.1337 0.0399  0.0213  0.0236  681  TYR A CD1 
5105  C CD2 . TYR A 683  ? 0.1874 0.2033 0.1093 0.0439  0.0191  0.0131  681  TYR A CD2 
5106  C CE1 . TYR A 683  ? 0.1946 0.2019 0.1244 0.0384  0.0192  0.0229  681  TYR A CE1 
5107  C CE2 . TYR A 683  ? 0.1901 0.2001 0.1134 0.0422  0.0170  0.0127  681  TYR A CE2 
5108  C CZ  . TYR A 683  ? 0.2093 0.2152 0.1364 0.0395  0.0171  0.0176  681  TYR A CZ  
5109  O OH  . TYR A 683  ? 0.2196 0.2203 0.1484 0.0380  0.0151  0.0170  681  TYR A OH  
5110  N N   . TYR A 684  ? 0.2010 0.2442 0.1121 0.0507  0.0227  0.0150  682  TYR A N   
5111  C CA  . TYR A 684  ? 0.2034 0.2508 0.1098 0.0525  0.0208  0.0123  682  TYR A CA  
5112  C C   . TYR A 684  ? 0.2116 0.2704 0.1145 0.0535  0.0222  0.0179  682  TYR A C   
5113  O O   . TYR A 684  ? 0.2073 0.2686 0.1075 0.0538  0.0206  0.0188  682  TYR A O   
5114  C CB  . TYR A 684  ? 0.2138 0.2624 0.1172 0.0556  0.0195  0.0035  682  TYR A CB  
5115  C CG  . TYR A 684  ? 0.1911 0.2284 0.0982 0.0544  0.0176  -0.0017 682  TYR A CG  
5116  C CD1 . TYR A 684  ? 0.1874 0.2158 0.0976 0.0515  0.0159  -0.0004 682  TYR A CD1 
5117  C CD2 . TYR A 684  ? 0.1919 0.2278 0.0998 0.0563  0.0174  -0.0076 682  TYR A CD2 
5118  C CE1 . TYR A 684  ? 0.2234 0.2424 0.1371 0.0502  0.0141  -0.0046 682  TYR A CE1 
5119  C CE2 . TYR A 684  ? 0.1893 0.2151 0.1009 0.0550  0.0155  -0.0117 682  TYR A CE2 
5120  C CZ  . TYR A 684  ? 0.1920 0.2096 0.1064 0.0518  0.0139  -0.0100 682  TYR A CZ  
5121  O OH  . TYR A 684  ? 0.2287 0.2373 0.1469 0.0504  0.0121  -0.0135 682  TYR A OH  
5122  N N   . ALA A 685  ? 0.1997 0.2658 0.1025 0.0540  0.0250  0.0219  683  ALA A N   
5123  C CA  . ALA A 685  ? 0.2127 0.2899 0.1130 0.0544  0.0263  0.0287  683  ALA A CA  
5124  C C   . ALA A 685  ? 0.2151 0.2879 0.1188 0.0512  0.0255  0.0361  683  ALA A C   
5125  O O   . ALA A 685  ? 0.2211 0.2992 0.1223 0.0515  0.0245  0.0394  683  ALA A O   
5126  C CB  . ALA A 685  ? 0.2316 0.3170 0.1324 0.0550  0.0295  0.0323  683  ALA A CB  
5127  N N   . GLU A 686  ? 0.2260 0.2894 0.1358 0.0482  0.0256  0.0386  684  GLU A N   
5128  C CA  . GLU A 686  ? 0.2561 0.3150 0.1699 0.0454  0.0246  0.0450  684  GLU A CA  
5129  C C   . GLU A 686  ? 0.2387 0.2922 0.1515 0.0452  0.0217  0.0420  684  GLU A C   
5130  O O   . GLU A 686  ? 0.2374 0.2931 0.1502 0.0446  0.0206  0.0468  684  GLU A O   
5131  C CB  . GLU A 686  ? 0.2511 0.3013 0.1717 0.0425  0.0253  0.0474  684  GLU A CB  
5132  C CG  . GLU A 686  ? 0.3181 0.3624 0.2436 0.0397  0.0238  0.0530  684  GLU A CG  
5133  C CD  . GLU A 686  ? 0.3352 0.3874 0.2612 0.0392  0.0242  0.0616  684  GLU A CD  
5134  O OE1 . GLU A 686  ? 0.3223 0.3851 0.2452 0.0405  0.0260  0.0644  684  GLU A OE1 
5135  O OE2 . GLU A 686  ? 0.3559 0.4039 0.2857 0.0373  0.0225  0.0659  684  GLU A OE2 
5136  N N   . GLN A 687  ? 0.2218 0.2687 0.1340 0.0458  0.0203  0.0344  685  GLN A N   
5137  C CA  . GLN A 687  ? 0.2006 0.2428 0.1120 0.0456  0.0175  0.0314  685  GLN A CA  
5138  C C   . GLN A 687  ? 0.2319 0.2833 0.1376 0.0479  0.0166  0.0313  685  GLN A C   
5139  O O   . GLN A 687  ? 0.2334 0.2839 0.1390 0.0474  0.0146  0.0329  685  GLN A O   
5140  C CB  . GLN A 687  ? 0.2234 0.2583 0.1351 0.0459  0.0162  0.0234  685  GLN A CB  
5141  C CG  . GLN A 687  ? 0.2076 0.2328 0.1251 0.0434  0.0167  0.0235  685  GLN A CG  
5142  C CD  . GLN A 687  ? 0.2701 0.2900 0.1919 0.0408  0.0157  0.0280  685  GLN A CD  
5143  O OE1 . GLN A 687  ? 0.2394 0.2570 0.1608 0.0405  0.0136  0.0267  685  GLN A OE1 
5144  N NE2 . GLN A 687  ? 0.2925 0.3107 0.2185 0.0390  0.0172  0.0331  685  GLN A NE2 
5145  N N   . THR A 688  ? 0.2121 0.2728 0.1131 0.0506  0.0179  0.0293  686  THR A N   
5146  C CA  . THR A 688  ? 0.2032 0.2744 0.0984 0.0530  0.0172  0.0295  686  THR A CA  
5147  C C   . THR A 688  ? 0.2186 0.2954 0.1145 0.0517  0.0176  0.0389  686  THR A C   
5148  O O   . THR A 688  ? 0.2418 0.3208 0.1358 0.0519  0.0157  0.0404  686  THR A O   
5149  C CB  . THR A 688  ? 0.2169 0.2979 0.1073 0.0563  0.0188  0.0256  686  THR A CB  
5150  O OG1 . THR A 688  ? 0.2350 0.3108 0.1247 0.0578  0.0174  0.0162  686  THR A OG1 
5151  C CG2 . THR A 688  ? 0.2135 0.3070 0.0978 0.0587  0.0184  0.0268  686  THR A CG2 
5152  N N   . ARG A 689  ? 0.2244 0.3034 0.1234 0.0503  0.0200  0.0454  687  ARG A N   
5153  C CA  . ARG A 689  ? 0.2338 0.3177 0.1346 0.0488  0.0203  0.0550  687  ARG A CA  
5154  C C   . ARG A 689  ? 0.2508 0.3257 0.1562 0.0465  0.0178  0.0577  687  ARG A C   
5155  O O   . ARG A 689  ? 0.2748 0.3540 0.1804 0.0459  0.0169  0.0641  687  ARG A O   
5156  C CB  . ARG A 689  ? 0.2377 0.3237 0.1425 0.0473  0.0230  0.0611  687  ARG A CB  
5157  C CG  . ARG A 689  ? 0.2684 0.3672 0.1685 0.0497  0.0256  0.0610  687  ARG A CG  
5158  C CD  . ARG A 689  ? 0.2834 0.3853 0.1880 0.0478  0.0280  0.0686  687  ARG A CD  
5159  N NE  . ARG A 689  ? 0.2654 0.3565 0.1755 0.0460  0.0286  0.0663  687  ARG A NE  
5160  C CZ  . ARG A 689  ? 0.2525 0.3442 0.1620 0.0472  0.0305  0.0618  687  ARG A CZ  
5161  N NH1 . ARG A 689  ? 0.3033 0.4060 0.2074 0.0503  0.0320  0.0587  687  ARG A NH1 
5162  N NH2 . ARG A 689  ? 0.2813 0.3629 0.1960 0.0453  0.0307  0.0602  687  ARG A NH2 
5163  N N   . ARG A 690  ? 0.2218 0.2848 0.1309 0.0451  0.0168  0.0531  688  ARG A N   
5164  C CA  A ARG A 690  ? 0.2426 0.2972 0.1561 0.0432  0.0145  0.0546  688  ARG A CA  
5165  C CA  B ARG A 690  ? 0.2426 0.2973 0.1560 0.0432  0.0145  0.0547  688  ARG A CA  
5166  C C   . ARG A 690  ? 0.2447 0.2997 0.1546 0.0445  0.0119  0.0506  688  ARG A C   
5167  O O   . ARG A 690  ? 0.2415 0.2924 0.1543 0.0433  0.0099  0.0531  688  ARG A O   
5168  C CB  A ARG A 690  ? 0.2242 0.2669 0.1428 0.0413  0.0143  0.0511  688  ARG A CB  
5169  C CB  B ARG A 690  ? 0.2251 0.2681 0.1438 0.0413  0.0144  0.0515  688  ARG A CB  
5170  C CG  A ARG A 690  ? 0.2581 0.2982 0.1818 0.0394  0.0164  0.0550  688  ARG A CG  
5171  C CG  B ARG A 690  ? 0.2584 0.2996 0.1820 0.0395  0.0165  0.0559  688  ARG A CG  
5172  C CD  A ARG A 690  ? 0.2593 0.2978 0.1888 0.0373  0.0158  0.0631  688  ARG A CD  
5173  C CD  B ARG A 690  ? 0.2600 0.3026 0.1879 0.0378  0.0161  0.0648  688  ARG A CD  
5174  N NE  A ARG A 690  ? 0.2436 0.2738 0.1770 0.0361  0.0134  0.0623  688  ARG A NE  
5175  N NE  B ARG A 690  ? 0.2754 0.3126 0.2062 0.0370  0.0134  0.0655  688  ARG A NE  
5176  C CZ  A ARG A 690  ? 0.2683 0.3001 0.2017 0.0363  0.0113  0.0651  688  ARG A CZ  
5177  C CZ  B ARG A 690  ? 0.2556 0.2829 0.1914 0.0354  0.0122  0.0633  688  ARG A CZ  
5178  N NH1 A ARG A 690  ? 0.2409 0.2820 0.1705 0.0375  0.0113  0.0694  688  ARG A NH1 
5179  N NH1 B ARG A 690  ? 0.2329 0.2543 0.1715 0.0343  0.0134  0.0605  688  ARG A NH1 
5180  N NH2 A ARG A 690  ? 0.2472 0.2715 0.1846 0.0353  0.0092  0.0637  688  ARG A NH2 
5181  N NH2 B ARG A 690  ? 0.2504 0.2740 0.1885 0.0350  0.0098  0.0638  688  ARG A NH2 
5182  N N   . THR A 691  ? 0.2202 0.2796 0.1241 0.0470  0.0116  0.0442  689  THR A N   
5183  C CA  . THR A 691  ? 0.2412 0.2986 0.1430 0.0478  0.0088  0.0393  689  THR A CA  
5184  C C   . THR A 691  ? 0.3004 0.3682 0.1953 0.0506  0.0078  0.0372  689  THR A C   
5185  O O   . THR A 691  ? 0.2948 0.3639 0.1887 0.0507  0.0056  0.0383  689  THR A O   
5186  C CB  . THR A 691  ? 0.2463 0.2949 0.1493 0.0475  0.0080  0.0312  689  THR A CB  
5187  O OG1 . THR A 691  ? 0.2482 0.2998 0.1482 0.0493  0.0095  0.0264  689  THR A OG1 
5188  C CG2 . THR A 691  ? 0.2322 0.2703 0.1419 0.0447  0.0083  0.0327  689  THR A CG2 
5189  N N   . LEU A 692  ? 0.2475 0.3228 0.1376 0.0529  0.0093  0.0339  690  LEU A N   
5190  C CA  . LEU A 692  ? 0.2499 0.3329 0.1336 0.0559  0.0078  0.0285  690  LEU A CA  
5191  C C   . LEU A 692  ? 0.2663 0.3611 0.1460 0.0570  0.0076  0.0345  690  LEU A C   
5192  O O   . LEU A 692  ? 0.2972 0.3997 0.1763 0.0570  0.0098  0.0411  690  LEU A O   
5193  C CB  . LEU A 692  ? 0.2365 0.3236 0.1169 0.0584  0.0092  0.0220  690  LEU A CB  
5194  C CG  . LEU A 692  ? 0.2700 0.3456 0.1538 0.0576  0.0086  0.0151  690  LEU A CG  
5195  C CD1 . LEU A 692  ? 0.2910 0.3711 0.1717 0.0606  0.0094  0.0081  690  LEU A CD1 
5196  C CD2 . LEU A 692  ? 0.2811 0.3488 0.1664 0.0568  0.0053  0.0105  690  LEU A CD2 
5197  N N   . GLY A 693  ? 0.2456 0.3420 0.1227 0.0579  0.0048  0.0323  691  GLY A N   
5198  C CA  . GLY A 693  ? 0.2850 0.3927 0.1580 0.0590  0.0041  0.0374  691  GLY A CA  
5199  C C   . GLY A 693  ? 0.2799 0.3947 0.1462 0.0621  0.0021  0.0301  691  GLY A C   
5200  O O   . GLY A 693  ? 0.3056 0.4168 0.1708 0.0634  0.0014  0.0211  691  GLY A O   
5201  N N   . PRO A 694  ? 0.3115 0.4354 0.1759 0.0626  0.0010  0.0334  692  PRO A N   
5202  C CA  . PRO A 694  ? 0.2803 0.4113 0.1405 0.0651  -0.0007 0.0261  692  PRO A CA  
5203  C C   . PRO A 694  ? 0.2965 0.4206 0.1548 0.0660  -0.0041 0.0184  692  PRO A C   
5204  O O   . PRO A 694  ? 0.3546 0.4815 0.2101 0.0681  -0.0055 0.0099  692  PRO A O   
5205  C CB  . PRO A 694  ? 0.3183 0.4588 0.1786 0.0645  -0.0011 0.0328  692  PRO A CB  
5206  C CG  . PRO A 694  ? 0.3626 0.4984 0.2275 0.0616  -0.0006 0.0428  692  PRO A CG  
5207  C CD  . PRO A 694  ? 0.3038 0.4315 0.1715 0.0605  0.0015  0.0438  692  PRO A CD  
5208  N N   . GLY A 695  ? 0.2960 0.4099 0.1581 0.0638  -0.0056 0.0207  693  GLY A N   
5209  C CA  . GLY A 695  ? 0.3318 0.4375 0.1955 0.0634  -0.0087 0.0136  693  GLY A CA  
5210  C C   . GLY A 695  ? 0.3319 0.4278 0.1986 0.0629  -0.0086 0.0060  693  GLY A C   
5211  O O   . GLY A 695  ? 0.3593 0.4486 0.2276 0.0625  -0.0113 0.0001  693  GLY A O   
5212  N N   . HIS A 696  ? 0.2942 0.3889 0.1620 0.0629  -0.0056 0.0064  694  HIS A N   
5213  C CA  . HIS A 696  ? 0.2697 0.3551 0.1407 0.0623  -0.0055 -0.0001 694  HIS A CA  
5214  C C   . HIS A 696  ? 0.3192 0.4117 0.1854 0.0658  -0.0052 -0.0072 694  HIS A C   
5215  O O   . HIS A 696  ? 0.3514 0.4467 0.2170 0.0667  -0.0024 -0.0067 694  HIS A O   
5216  C CB  . HIS A 696  ? 0.3041 0.3823 0.1804 0.0598  -0.0026 0.0050  694  HIS A CB  
5217  C CG  . HIS A 696  ? 0.2612 0.3347 0.1419 0.0570  -0.0027 0.0126  694  HIS A CG  
5218  N ND1 . HIS A 696  ? 0.3026 0.3797 0.1845 0.0561  -0.0005 0.0213  694  HIS A ND1 
5219  C CD2 . HIS A 696  ? 0.2834 0.3492 0.1679 0.0550  -0.0049 0.0126  694  HIS A CD2 
5220  C CE1 . HIS A 696  ? 0.2599 0.3312 0.1464 0.0538  -0.0015 0.0261  694  HIS A CE1 
5221  N NE2 . HIS A 696  ? 0.3043 0.3690 0.1922 0.0532  -0.0040 0.0209  694  HIS A NE2 
5222  N N   . GLY A 697  ? 0.3204 0.4162 0.1831 0.0679  -0.0082 -0.0140 695  GLY A N   
5223  C CA  . GLY A 697  ? 0.3026 0.4068 0.1604 0.0716  -0.0085 -0.0211 695  GLY A CA  
5224  C C   . GLY A 697  ? 0.3230 0.4191 0.1841 0.0719  -0.0087 -0.0284 695  GLY A C   
5225  O O   . GLY A 697  ? 0.2967 0.3808 0.1631 0.0695  -0.0101 -0.0303 695  GLY A O   
5226  N N   . PRO A 698  ? 0.3173 0.4201 0.1754 0.0750  -0.0072 -0.0325 696  PRO A N   
5227  C CA  . PRO A 698  ? 0.3032 0.3986 0.1646 0.0756  -0.0076 -0.0396 696  PRO A CA  
5228  C C   . PRO A 698  ? 0.3154 0.4052 0.1782 0.0763  -0.0120 -0.0488 696  PRO A C   
5229  O O   . PRO A 698  ? 0.3335 0.4279 0.1938 0.0773  -0.0147 -0.0513 696  PRO A O   
5230  C CB  . PRO A 698  ? 0.3546 0.4600 0.2147 0.0784  -0.0052 -0.0413 696  PRO A CB  
5231  C CG  . PRO A 698  ? 0.4165 0.5339 0.2738 0.0790  -0.0048 -0.0373 696  PRO A CG  
5232  C CD  . PRO A 698  ? 0.3786 0.4942 0.2348 0.0764  -0.0047 -0.0291 696  PRO A CD  
5233  N N   . LEU A 699  ? 0.3135 0.3924 0.1817 0.0752  -0.0129 -0.0531 697  LEU A N   
5234  C CA  . LEU A 699  ? 0.3064 0.3798 0.1768 0.0759  -0.0173 -0.0622 697  LEU A CA  
5235  C C   . LEU A 699  ? 0.2898 0.3716 0.1582 0.0799  -0.0186 -0.0697 697  LEU A C   
5236  O O   . LEU A 699  ? 0.3216 0.4046 0.1905 0.0806  -0.0222 -0.0750 697  LEU A O   
5237  C CB  . LEU A 699  ? 0.2954 0.3558 0.1728 0.0737  -0.0178 -0.0641 697  LEU A CB  
5238  C CG  . LEU A 699  ? 0.3202 0.3704 0.2028 0.0689  -0.0171 -0.0574 697  LEU A CG  
5239  C CD1 . LEU A 699  ? 0.2839 0.3233 0.1728 0.0673  -0.0173 -0.0597 697  LEU A CD1 
5240  C CD2 . LEU A 699  ? 0.3403 0.3876 0.2239 0.0669  -0.0203 -0.0573 697  LEU A CD2 
5241  N N   . GLY A 700  ? 0.2783 0.3653 0.1467 0.0817  -0.0157 -0.0696 698  GLY A N   
5242  C CA  . GLY A 700  ? 0.2943 0.3874 0.1639 0.0847  -0.0168 -0.0764 698  GLY A CA  
5243  C C   . GLY A 700  ? 0.2941 0.3826 0.1676 0.0857  -0.0157 -0.0796 698  GLY A C   
5244  O O   . GLY A 700  ? 0.2860 0.3691 0.1601 0.0841  -0.0131 -0.0752 698  GLY A O   
5245  N N   . PRO A 701  ? 0.2964 0.3867 0.1726 0.0883  -0.0178 -0.0873 699  PRO A N   
5246  C CA  . PRO A 701  ? 0.2892 0.3755 0.1695 0.0894  -0.0169 -0.0904 699  PRO A CA  
5247  C C   . PRO A 701  ? 0.2759 0.3477 0.1602 0.0868  -0.0180 -0.0906 699  PRO A C   
5248  O O   . PRO A 701  ? 0.2779 0.3415 0.1649 0.0853  -0.0217 -0.0939 699  PRO A O   
5249  C CB  . PRO A 701  ? 0.3062 0.3957 0.1894 0.0924  -0.0203 -0.0994 699  PRO A CB  
5250  C CG  . PRO A 701  ? 0.3177 0.4186 0.1965 0.0938  -0.0208 -0.0991 699  PRO A CG  
5251  C CD  . PRO A 701  ? 0.2720 0.3694 0.1478 0.0907  -0.0208 -0.0932 699  PRO A CD  
5252  N N   . ILE A 702  ? 0.2534 0.3225 0.1384 0.0861  -0.0146 -0.0867 700  ILE A N   
5253  C CA  A ILE A 702  ? 0.2726 0.3287 0.1614 0.0838  -0.0152 -0.0863 700  ILE A CA  
5254  C CA  B ILE A 702  ? 0.2725 0.3287 0.1613 0.0838  -0.0150 -0.0861 700  ILE A CA  
5255  C C   . ILE A 702  ? 0.2899 0.3426 0.1838 0.0853  -0.0153 -0.0907 700  ILE A C   
5256  O O   . ILE A 702  ? 0.2706 0.3309 0.1636 0.0873  -0.0123 -0.0896 700  ILE A O   
5257  C CB  A ILE A 702  ? 0.2603 0.3144 0.1475 0.0807  -0.0113 -0.0767 700  ILE A CB  
5258  C CB  B ILE A 702  ? 0.2600 0.3147 0.1471 0.0809  -0.0110 -0.0765 700  ILE A CB  
5259  C CG1 A ILE A 702  ? 0.2606 0.3152 0.1455 0.0782  -0.0122 -0.0722 700  ILE A CG1 
5260  C CG1 B ILE A 702  ? 0.2599 0.3180 0.1434 0.0789  -0.0108 -0.0709 700  ILE A CG1 
5261  C CG2 A ILE A 702  ? 0.2675 0.3087 0.1619 0.0772  -0.0112 -0.0744 700  ILE A CG2 
5262  C CG2 B ILE A 702  ? 0.2671 0.3080 0.1614 0.0769  -0.0114 -0.0741 700  ILE A CG2 
5263  C CD1 A ILE A 702  ? 0.2464 0.2984 0.1321 0.0743  -0.0091 -0.0620 700  ILE A CD1 
5264  C CD1 B ILE A 702  ? 0.2789 0.3288 0.1652 0.0765  -0.0149 -0.0729 700  ILE A CD1 
5265  N N   . VAL A 703  ? 0.2646 0.3060 0.1643 0.0843  -0.0189 -0.0953 701  VAL A N   
5266  C CA  . VAL A 703  ? 0.2498 0.2860 0.1555 0.0852  -0.0196 -0.0992 701  VAL A CA  
5267  C C   . VAL A 703  ? 0.2428 0.2709 0.1499 0.0830  -0.0172 -0.0942 701  VAL A C   
5268  O O   . VAL A 703  ? 0.2441 0.2634 0.1546 0.0786  -0.0183 -0.0902 701  VAL A O   
5269  C CB  . VAL A 703  ? 0.2655 0.2940 0.1778 0.0851  -0.0252 -0.1063 701  VAL A CB  
5270  C CG1 . VAL A 703  ? 0.3022 0.3238 0.2213 0.0855  -0.0262 -0.1091 701  VAL A CG1 
5271  C CG2 . VAL A 703  ? 0.2687 0.3061 0.1799 0.0879  -0.0276 -0.1118 701  VAL A CG2 
5272  N N   . CYS A 704  ? 0.2487 0.2802 0.1559 0.0843  -0.0137 -0.0921 702  CYS A N   
5273  C CA  . CYS A 704  ? 0.2536 0.2781 0.1648 0.0809  -0.0111 -0.0855 702  CYS A CA  
5274  C C   . CYS A 704  ? 0.2555 0.2737 0.1728 0.0822  -0.0128 -0.0905 702  CYS A C   
5275  O O   . CYS A 704  ? 0.2633 0.2877 0.1803 0.0859  -0.0120 -0.0944 702  CYS A O   
5276  C CB  . CYS A 704  ? 0.2646 0.2977 0.1716 0.0809  -0.0057 -0.0784 702  CYS A CB  
5277  S SG  . CYS A 704  ? 0.2599 0.3006 0.1603 0.0793  -0.0037 -0.0715 702  CYS A SG  
5278  N N   . ILE A 705  ? 0.2573 0.2635 0.1810 0.0786  -0.0152 -0.0892 703  ILE A N   
5279  C CA  . ILE A 705  ? 0.2407 0.2393 0.1712 0.0792  -0.0173 -0.0930 703  ILE A CA  
5280  C C   . ILE A 705  ? 0.2490 0.2423 0.1825 0.0754  -0.0143 -0.0851 703  ILE A C   
5281  O O   . ILE A 705  ? 0.2401 0.2277 0.1750 0.0709  -0.0141 -0.0792 703  ILE A O   
5282  C CB  . ILE A 705  ? 0.2713 0.2607 0.2073 0.0781  -0.0230 -0.0981 703  ILE A CB  
5283  C CG1 . ILE A 705  ? 0.2809 0.2765 0.2148 0.0812  -0.0259 -0.1051 703  ILE A CG1 
5284  C CG2 . ILE A 705  ? 0.2928 0.2736 0.2367 0.0780  -0.0253 -0.1007 703  ILE A CG2 
5285  C CD1 . ILE A 705  ? 0.3195 0.3073 0.2588 0.0792  -0.0315 -0.1088 703  ILE A CD1 
5286  N N   . SER A 706  ? 0.2503 0.2462 0.1850 0.0775  -0.0120 -0.0851 704  SER A N   
5287  C CA  . SER A 706  ? 0.2426 0.2358 0.1791 0.0745  -0.0085 -0.0777 704  SER A CA  
5288  C C   . SER A 706  ? 0.2295 0.2148 0.1732 0.0744  -0.0104 -0.0796 704  SER A C   
5289  O O   . SER A 706  ? 0.2588 0.2428 0.2056 0.0776  -0.0136 -0.0870 704  SER A O   
5290  C CB  . SER A 706  ? 0.2683 0.2725 0.1998 0.0766  -0.0037 -0.0745 704  SER A CB  
5291  O OG  . SER A 706  ? 0.2829 0.2940 0.2135 0.0818  -0.0038 -0.0812 704  SER A OG  
5292  N N   . PRO A 707  ? 0.2359 0.2159 0.1827 0.0706  -0.0086 -0.0730 705  PRO A N   
5293  C CA  . PRO A 707  ? 0.2340 0.2056 0.1880 0.0696  -0.0107 -0.0737 705  PRO A CA  
5294  C C   . PRO A 707  ? 0.2440 0.2194 0.1990 0.0722  -0.0081 -0.0737 705  PRO A C   
5295  O O   . PRO A 707  ? 0.2465 0.2311 0.1967 0.0741  -0.0043 -0.0721 705  PRO A O   
5296  C CB  . PRO A 707  ? 0.2498 0.2147 0.2058 0.0640  -0.0101 -0.0662 705  PRO A CB  
5297  C CG  . PRO A 707  ? 0.2407 0.2125 0.1907 0.0630  -0.0056 -0.0604 705  PRO A CG  
5298  C CD  . PRO A 707  ? 0.2445 0.2245 0.1888 0.0665  -0.0056 -0.0647 705  PRO A CD  
5299  N N   . TRP A 708  ? 0.2504 0.2193 0.2121 0.0722  -0.0103 -0.0753 706  TRP A N   
5300  C CA  . TRP A 708  ? 0.2166 0.1887 0.1800 0.0747  -0.0082 -0.0755 706  TRP A CA  
5301  C C   . TRP A 708  ? 0.2471 0.2177 0.2115 0.0710  -0.0048 -0.0672 706  TRP A C   
5302  O O   . TRP A 708  ? 0.2659 0.2407 0.2306 0.0726  -0.0021 -0.0661 706  TRP A O   
5303  C CB  . TRP A 708  ? 0.2597 0.2259 0.2304 0.0771  -0.0124 -0.0817 706  TRP A CB  
5304  C CG  . TRP A 708  ? 0.2687 0.2234 0.2455 0.0731  -0.0163 -0.0799 706  TRP A CG  
5305  C CD1 . TRP A 708  ? 0.2840 0.2331 0.2635 0.0726  -0.0210 -0.0840 706  TRP A CD1 
5306  C CD2 . TRP A 708  ? 0.2528 0.2010 0.2338 0.0687  -0.0159 -0.0732 706  TRP A CD2 
5307  N NE1 . TRP A 708  ? 0.2940 0.2337 0.2793 0.0682  -0.0235 -0.0799 706  TRP A NE1 
5308  C CE2 . TRP A 708  ? 0.2820 0.2212 0.2680 0.0657  -0.0203 -0.0733 706  TRP A CE2 
5309  C CE3 . TRP A 708  ? 0.2211 0.1707 0.2021 0.0670  -0.0122 -0.0671 706  TRP A CE3 
5310  C CZ2 . TRP A 708  ? 0.2692 0.2014 0.2599 0.0612  -0.0211 -0.0673 706  TRP A CZ2 
5311  C CZ3 . TRP A 708  ? 0.2563 0.1986 0.2418 0.0626  -0.0131 -0.0617 706  TRP A CZ3 
5312  C CH2 . TRP A 708  ? 0.2847 0.2187 0.2749 0.0598  -0.0174 -0.0617 706  TRP A CH2 
5313  N N   . ASN A 709  ? 0.2308 0.1959 0.1954 0.0661  -0.0049 -0.0616 707  ASN A N   
5314  C CA  . ASN A 709  ? 0.2263 0.1892 0.1924 0.0625  -0.0022 -0.0544 707  ASN A CA  
5315  C C   . ASN A 709  ? 0.2430 0.2133 0.2035 0.0617  0.0024  -0.0493 707  ASN A C   
5316  O O   . ASN A 709  ? 0.2711 0.2419 0.2327 0.0601  0.0051  -0.0443 707  ASN A O   
5317  C CB  . ASN A 709  ? 0.2421 0.1962 0.2116 0.0577  -0.0046 -0.0509 707  ASN A CB  
5318  C CG  . ASN A 709  ? 0.2422 0.1967 0.2077 0.0552  -0.0042 -0.0485 707  ASN A CG  
5319  O OD1 . ASN A 709  ? 0.2778 0.2376 0.2387 0.0573  -0.0039 -0.0512 707  ASN A OD1 
5320  N ND2 . ASN A 709  ? 0.2518 0.2011 0.2191 0.0506  -0.0045 -0.0435 707  ASN A ND2 
5321  N N   . PHE A 710  ? 0.2588 0.2349 0.2139 0.0630  0.0033  -0.0502 708  PHE A N   
5322  C CA  . PHE A 710  ? 0.2151 0.1995 0.1651 0.0630  0.0075  -0.0459 708  PHE A CA  
5323  C C   . PHE A 710  ? 0.2186 0.2121 0.1640 0.0676  0.0078  -0.0509 708  PHE A C   
5324  O O   . PHE A 710  ? 0.2460 0.2432 0.1869 0.0677  0.0079  -0.0509 708  PHE A O   
5325  C CB  . PHE A 710  ? 0.2189 0.2013 0.1669 0.0589  0.0083  -0.0402 708  PHE A CB  
5326  C CG  . PHE A 710  ? 0.2519 0.2279 0.2036 0.0548  0.0089  -0.0348 708  PHE A CG  
5327  C CD1 . PHE A 710  ? 0.2816 0.2608 0.2333 0.0537  0.0123  -0.0297 708  PHE A CD1 
5328  C CD2 . PHE A 710  ? 0.2567 0.2241 0.2122 0.0520  0.0060  -0.0349 708  PHE A CD2 
5329  C CE1 . PHE A 710  ? 0.2718 0.2456 0.2269 0.0501  0.0128  -0.0252 708  PHE A CE1 
5330  C CE2 . PHE A 710  ? 0.2698 0.2324 0.2286 0.0484  0.0066  -0.0301 708  PHE A CE2 
5331  C CZ  . PHE A 710  ? 0.2846 0.2504 0.2431 0.0475  0.0100  -0.0255 708  PHE A CZ  
5332  N N   . PRO A 711  ? 0.2236 0.2213 0.1702 0.0716  0.0080  -0.0554 709  PRO A N   
5333  C CA  . PRO A 711  ? 0.2486 0.2546 0.1917 0.0765  0.0075  -0.0619 709  PRO A CA  
5334  C C   . PRO A 711  ? 0.2228 0.2408 0.1597 0.0779  0.0114  -0.0589 709  PRO A C   
5335  O O   . PRO A 711  ? 0.2559 0.2820 0.1888 0.0817  0.0111  -0.0637 709  PRO A O   
5336  C CB  . PRO A 711  ? 0.2604 0.2666 0.2078 0.0802  0.0066  -0.0672 709  PRO A CB  
5337  C CG  . PRO A 711  ? 0.2292 0.2330 0.1798 0.0775  0.0092  -0.0608 709  PRO A CG  
5338  C CD  . PRO A 711  ? 0.2377 0.2334 0.1892 0.0719  0.0088  -0.0546 709  PRO A CD  
5339  N N   . LEU A 712  ? 0.2213 0.2412 0.1575 0.0750  0.0149  -0.0510 710  LEU A N   
5340  C CA  . LEU A 712  ? 0.2160 0.2464 0.1468 0.0753  0.0183  -0.0467 710  LEU A CA  
5341  C C   . LEU A 712  ? 0.2304 0.2574 0.1591 0.0712  0.0184  -0.0409 710  LEU A C   
5342  O O   . LEU A 712  ? 0.2288 0.2621 0.1527 0.0720  0.0187  -0.0406 710  LEU A O   
5343  C CB  . LEU A 712  ? 0.2222 0.2587 0.1538 0.0753  0.0222  -0.0418 710  LEU A CB  
5344  C CG  . LEU A 712  ? 0.2558 0.3040 0.1824 0.0756  0.0256  -0.0368 710  LEU A CG  
5345  C CD1 . LEU A 712  ? 0.2270 0.2865 0.1486 0.0805  0.0256  -0.0424 710  LEU A CD1 
5346  C CD2 . LEU A 712  ? 0.2428 0.2954 0.1713 0.0743  0.0293  -0.0305 710  LEU A CD2 
5347  N N   . ALA A 713  ? 0.2071 0.2248 0.1395 0.0669  0.0180  -0.0366 711  ALA A N   
5348  C CA  . ALA A 713  ? 0.1925 0.2081 0.1234 0.0632  0.0186  -0.0307 711  ALA A CA  
5349  C C   . ALA A 713  ? 0.2158 0.2282 0.1446 0.0630  0.0156  -0.0337 711  ALA A C   
5350  O O   . ALA A 713  ? 0.2237 0.2409 0.1486 0.0627  0.0162  -0.0314 711  ALA A O   
5351  C CB  . ALA A 713  ? 0.2239 0.2311 0.1594 0.0590  0.0190  -0.0257 711  ALA A CB  
5352  N N   . ILE A 714  ? 0.2040 0.2085 0.1359 0.0628  0.0121  -0.0387 712  ILE A N   
5353  C CA  . ILE A 714  ? 0.2282 0.2297 0.1587 0.0623  0.0091  -0.0413 712  ILE A CA  
5354  C C   . ILE A 714  ? 0.2467 0.2563 0.1727 0.0666  0.0082  -0.0470 712  ILE A C   
5355  O O   . ILE A 714  ? 0.2383 0.2504 0.1607 0.0665  0.0073  -0.0472 712  ILE A O   
5356  C CB  . ILE A 714  ? 0.2152 0.2060 0.1509 0.0604  0.0055  -0.0442 712  ILE A CB  
5357  C CG1 . ILE A 714  ? 0.2395 0.2236 0.1786 0.0558  0.0065  -0.0379 712  ILE A CG1 
5358  C CG2 . ILE A 714  ? 0.2325 0.2211 0.1672 0.0605  0.0020  -0.0483 712  ILE A CG2 
5359  C CD1 . ILE A 714  ? 0.2793 0.2536 0.2236 0.0534  0.0032  -0.0393 712  ILE A CD1 
5360  N N   . PHE A 715  ? 0.2412 0.2556 0.1673 0.0705  0.0085  -0.0518 713  PHE A N   
5361  C CA  . PHE A 715  ? 0.2280 0.2524 0.1494 0.0750  0.0084  -0.0570 713  PHE A CA  
5362  C C   . PHE A 715  ? 0.2295 0.2636 0.1450 0.0748  0.0113  -0.0517 713  PHE A C   
5363  O O   . PHE A 715  ? 0.2174 0.2558 0.1288 0.0759  0.0101  -0.0535 713  PHE A O   
5364  C CB  . PHE A 715  ? 0.2462 0.2756 0.1690 0.0790  0.0093  -0.0614 713  PHE A CB  
5365  C CG  . PHE A 715  ? 0.2357 0.2770 0.1536 0.0841  0.0096  -0.0669 713  PHE A CG  
5366  C CD1 . PHE A 715  ? 0.2505 0.2909 0.1685 0.0873  0.0057  -0.0759 713  PHE A CD1 
5367  C CD2 . PHE A 715  ? 0.2747 0.3284 0.1881 0.0857  0.0136  -0.0633 713  PHE A CD2 
5368  C CE1 . PHE A 715  ? 0.2839 0.3355 0.1985 0.0912  0.0056  -0.0806 713  PHE A CE1 
5369  C CE2 . PHE A 715  ? 0.2650 0.3308 0.1739 0.0903  0.0139  -0.0683 713  PHE A CE2 
5370  C CZ  . PHE A 715  ? 0.2566 0.3208 0.1672 0.0922  0.0096  -0.0762 713  PHE A CZ  
5371  N N   . THR A 716  ? 0.2339 0.2715 0.1495 0.0733  0.0151  -0.0448 714  THR A N   
5372  C CA  . THR A 716  ? 0.2415 0.2884 0.1525 0.0729  0.0179  -0.0387 714  THR A CA  
5373  C C   . THR A 716  ? 0.2194 0.2617 0.1294 0.0694  0.0168  -0.0345 714  THR A C   
5374  O O   . THR A 716  ? 0.2222 0.2716 0.1276 0.0702  0.0171  -0.0330 714  THR A O   
5375  C CB  . THR A 716  ? 0.2408 0.2910 0.1534 0.0716  0.0218  -0.0321 714  THR A CB  
5376  O OG1 . THR A 716  ? 0.2359 0.2920 0.1492 0.0752  0.0229  -0.0361 714  THR A OG1 
5377  C CG2 . THR A 716  ? 0.2626 0.3217 0.1715 0.0706  0.0245  -0.0248 714  THR A CG2 
5378  N N   . GLY A 717  ? 0.2097 0.2407 0.1242 0.0657  0.0156  -0.0325 715  GLY A N   
5379  C CA  . GLY A 717  ? 0.2187 0.2455 0.1327 0.0624  0.0147  -0.0282 715  GLY A CA  
5380  C C   . GLY A 717  ? 0.2315 0.2594 0.1424 0.0637  0.0118  -0.0327 715  GLY A C   
5381  O O   . GLY A 717  ? 0.2412 0.2736 0.1487 0.0632  0.0121  -0.0295 715  GLY A O   
5382  N N   . GLN A 718  ? 0.2073 0.2311 0.1196 0.0654  0.0087  -0.0402 716  GLN A N   
5383  C CA  . GLN A 718  ? 0.2267 0.2510 0.1366 0.0665  0.0055  -0.0449 716  GLN A CA  
5384  C C   . GLN A 718  ? 0.2215 0.2584 0.1251 0.0702  0.0065  -0.0463 716  GLN A C   
5385  O O   . GLN A 718  ? 0.2319 0.2723 0.1320 0.0699  0.0057  -0.0450 716  GLN A O   
5386  C CB  . GLN A 718  ? 0.2294 0.2472 0.1427 0.0678  0.0017  -0.0529 716  GLN A CB  
5387  C CG  . GLN A 718  ? 0.2307 0.2365 0.1504 0.0641  0.0003  -0.0514 716  GLN A CG  
5388  C CD  . GLN A 718  ? 0.2383 0.2372 0.1621 0.0649  -0.0039 -0.0585 716  GLN A CD  
5389  O OE1 . GLN A 718  ? 0.2512 0.2418 0.1788 0.0619  -0.0064 -0.0582 716  GLN A OE1 
5390  N NE2 . GLN A 718  ? 0.2391 0.2417 0.1628 0.0690  -0.0047 -0.0649 716  GLN A NE2 
5391  N N   . ILE A 719  ? 0.2232 0.2677 0.1254 0.0737  0.0082  -0.0489 717  ILE A N   
5392  C CA  . ILE A 719  ? 0.2209 0.2788 0.1169 0.0775  0.0092  -0.0508 717  ILE A CA  
5393  C C   . ILE A 719  ? 0.2380 0.3032 0.1305 0.0759  0.0122  -0.0421 717  ILE A C   
5394  O O   . ILE A 719  ? 0.2382 0.3114 0.1256 0.0772  0.0118  -0.0420 717  ILE A O   
5395  C CB  . ILE A 719  ? 0.2637 0.3281 0.1597 0.0815  0.0107  -0.0553 717  ILE A CB  
5396  C CG1 . ILE A 719  ? 0.2659 0.3244 0.1650 0.0839  0.0069  -0.0651 717  ILE A CG1 
5397  C CG2 . ILE A 719  ? 0.3086 0.3889 0.1982 0.0850  0.0129  -0.0552 717  ILE A CG2 
5398  C CD1 . ILE A 719  ? 0.3094 0.3696 0.2112 0.0867  0.0080  -0.0687 717  ILE A CD1 
5399  N N   . ALA A 720  ? 0.2284 0.2913 0.1236 0.0730  0.0151  -0.0347 718  ALA A N   
5400  C CA  . ALA A 720  ? 0.2311 0.3005 0.1239 0.0713  0.0177  -0.0260 718  ALA A CA  
5401  C C   . ALA A 720  ? 0.2151 0.2808 0.1070 0.0689  0.0157  -0.0233 718  ALA A C   
5402  O O   . ALA A 720  ? 0.2344 0.3085 0.1222 0.0694  0.0163  -0.0196 718  ALA A O   
5403  C CB  . ALA A 720  ? 0.2225 0.2883 0.1196 0.0683  0.0205  -0.0191 718  ALA A CB  
5404  N N   . ALA A 721  ? 0.2202 0.2738 0.1160 0.0663  0.0134  -0.0248 719  ALA A N   
5405  C CA  . ALA A 721  ? 0.2116 0.2614 0.1071 0.0641  0.0113  -0.0228 719  ALA A CA  
5406  C C   . ALA A 721  ? 0.2169 0.2733 0.1074 0.0670  0.0090  -0.0278 719  ALA A C   
5407  O O   . ALA A 721  ? 0.2313 0.2932 0.1186 0.0667  0.0089  -0.0240 719  ALA A O   
5408  C CB  . ALA A 721  ? 0.2144 0.2510 0.1151 0.0612  0.0091  -0.0245 719  ALA A CB  
5409  N N   . ALA A 722  ? 0.2168 0.2728 0.1069 0.0698  0.0068  -0.0364 720  ALA A N   
5410  C CA  . ALA A 722  ? 0.2229 0.2852 0.1085 0.0727  0.0043  -0.0420 720  ALA A CA  
5411  C C   . ALA A 722  ? 0.2565 0.3336 0.1358 0.0754  0.0065  -0.0395 720  ALA A C   
5412  O O   . ALA A 722  ? 0.2502 0.3331 0.1255 0.0758  0.0055  -0.0382 720  ALA A O   
5413  C CB  . ALA A 722  ? 0.2424 0.3019 0.1294 0.0754  0.0015  -0.0520 720  ALA A CB  
5414  N N   . LEU A 723  ? 0.2334 0.3174 0.1120 0.0772  0.0097  -0.0383 721  LEU A N   
5415  C CA  . LEU A 723  ? 0.2323 0.3315 0.1051 0.0798  0.0121  -0.0355 721  LEU A CA  
5416  C C   . LEU A 723  ? 0.2333 0.3357 0.1048 0.0769  0.0136  -0.0255 721  LEU A C   
5417  O O   . LEU A 723  ? 0.2341 0.3458 0.1025 0.0776  0.0132  -0.0234 721  LEU A O   
5418  C CB  . LEU A 723  ? 0.2368 0.3411 0.1118 0.0809  0.0151  -0.0348 721  LEU A CB  
5419  C CG  . LEU A 723  ? 0.2482 0.3531 0.1256 0.0840  0.0137  -0.0437 721  LEU A CG  
5420  C CD1 . LEU A 723  ? 0.2580 0.3666 0.1377 0.0844  0.0172  -0.0411 721  LEU A CD1 
5421  C CD2 . LEU A 723  ? 0.2638 0.3787 0.1392 0.0866  0.0118  -0.0484 721  LEU A CD2 
5422  N N   . VAL A 724  ? 0.2331 0.3270 0.1095 0.0729  0.0149  -0.0186 722  VAL A N   
5423  C CA  . VAL A 724  ? 0.2384 0.3360 0.1144 0.0705  0.0165  -0.0088 722  VAL A CA  
5424  C C   . VAL A 724  ? 0.2449 0.3393 0.1198 0.0692  0.0136  -0.0082 722  VAL A C   
5425  O O   . VAL A 724  ? 0.2417 0.3428 0.1142 0.0686  0.0141  -0.0019 722  VAL A O   
5426  C CB  . VAL A 724  ? 0.2182 0.3082 0.1000 0.0669  0.0187  -0.0021 722  VAL A CB  
5427  C CG1 . VAL A 724  ? 0.2457 0.3212 0.1324 0.0636  0.0166  -0.0025 722  VAL A CG1 
5428  C CG2 . VAL A 724  ? 0.2160 0.3136 0.0973 0.0654  0.0210  0.0080  722  VAL A CG2 
5429  N N   . ALA A 725  ? 0.2306 0.3155 0.1074 0.0688  0.0105  -0.0146 723  ALA A N   
5430  C CA  . ALA A 725  ? 0.2536 0.3367 0.1290 0.0681  0.0075  -0.0154 723  ALA A CA  
5431  C C   . ALA A 725  ? 0.2726 0.3671 0.1415 0.0718  0.0060  -0.0199 723  ALA A C   
5432  O O   . ALA A 725  ? 0.2884 0.3824 0.1559 0.0716  0.0033  -0.0210 723  ALA A O   
5433  C CB  . ALA A 725  ? 0.2607 0.3308 0.1405 0.0665  0.0045  -0.0209 723  ALA A CB  
5434  N N   . GLY A 726  ? 0.2444 0.3496 0.1095 0.0753  0.0077  -0.0226 724  GLY A N   
5435  C CA  . GLY A 726  ? 0.2457 0.3616 0.1082 0.0776  0.0063  -0.0258 724  GLY A CA  
5436  C C   . GLY A 726  ? 0.2658 0.3805 0.1287 0.0803  0.0033  -0.0368 724  GLY A C   
5437  O O   . GLY A 726  ? 0.2920 0.4146 0.1532 0.0820  0.0016  -0.0400 724  GLY A O   
5438  N N   . ASN A 727  ? 0.2748 0.3800 0.1404 0.0806  0.0025  -0.0426 725  ASN A N   
5439  C CA  . ASN A 727  ? 0.2523 0.3547 0.1198 0.0828  -0.0008 -0.0529 725  ASN A CA  
5440  C C   . ASN A 727  ? 0.2855 0.3929 0.1549 0.0854  0.0006  -0.0567 725  ASN A C   
5441  O O   . ASN A 727  ? 0.2844 0.3903 0.1553 0.0848  0.0035  -0.0534 725  ASN A O   
5442  C CB  . ASN A 727  ? 0.2651 0.3530 0.1355 0.0814  -0.0032 -0.0569 725  ASN A CB  
5443  C CG  . ASN A 727  ? 0.2718 0.3531 0.1428 0.0780  -0.0045 -0.0521 725  ASN A CG  
5444  O OD1 . ASN A 727  ? 0.3023 0.3847 0.1714 0.0783  -0.0075 -0.0548 725  ASN A OD1 
5445  N ND2 . ASN A 727  ? 0.2573 0.3314 0.1322 0.0742  -0.0023 -0.0447 725  ASN A ND2 
5446  N N   . PRO A 728  ? 0.2561 0.3693 0.1259 0.0882  -0.0016 -0.0637 726  PRO A N   
5447  C CA  . PRO A 728  ? 0.2667 0.3824 0.1392 0.0908  -0.0010 -0.0688 726  PRO A CA  
5448  C C   . PRO A 728  ? 0.2719 0.3742 0.1490 0.0904  -0.0032 -0.0746 726  PRO A C   
5449  O O   . PRO A 728  ? 0.2812 0.3742 0.1597 0.0890  -0.0064 -0.0774 726  PRO A O   
5450  C CB  . PRO A 728  ? 0.2786 0.4041 0.1501 0.0939  -0.0033 -0.0748 726  PRO A CB  
5451  C CG  . PRO A 728  ? 0.2849 0.4070 0.1550 0.0929  -0.0066 -0.0764 726  PRO A CG  
5452  C CD  . PRO A 728  ? 0.2646 0.3813 0.1327 0.0893  -0.0051 -0.0681 726  PRO A CD  
5453  N N   . VAL A 729  ? 0.2649 0.3665 0.1450 0.0916  -0.0016 -0.0761 727  VAL A N   
5454  C CA  . VAL A 729  ? 0.2527 0.3416 0.1377 0.0909  -0.0030 -0.0798 727  VAL A CA  
5455  C C   . VAL A 729  ? 0.2576 0.3470 0.1469 0.0939  -0.0052 -0.0881 727  VAL A C   
5456  O O   . VAL A 729  ? 0.2823 0.3817 0.1710 0.0964  -0.0035 -0.0888 727  VAL A O   
5457  C CB  . VAL A 729  ? 0.2549 0.3403 0.1404 0.0890  0.0010  -0.0731 727  VAL A CB  
5458  C CG1 . VAL A 729  ? 0.2685 0.3420 0.1595 0.0887  -0.0003 -0.0771 727  VAL A CG1 
5459  C CG2 . VAL A 729  ? 0.2742 0.3569 0.1565 0.0859  0.0025  -0.0655 727  VAL A CG2 
5460  N N   . LEU A 730  ? 0.2582 0.3365 0.1521 0.0935  -0.0092 -0.0941 728  LEU A N   
5461  C CA  . LEU A 730  ? 0.2852 0.3602 0.1848 0.0956  -0.0114 -0.1011 728  LEU A CA  
5462  C C   . LEU A 730  ? 0.2644 0.3284 0.1680 0.0937  -0.0104 -0.0990 728  LEU A C   
5463  O O   . LEU A 730  ? 0.2641 0.3170 0.1699 0.0911  -0.0123 -0.0984 728  LEU A O   
5464  C CB  . LEU A 730  ? 0.2978 0.3679 0.2010 0.0964  -0.0169 -0.1088 728  LEU A CB  
5465  C CG  . LEU A 730  ? 0.2793 0.3588 0.1792 0.0982  -0.0189 -0.1119 728  LEU A CG  
5466  C CD1 . LEU A 730  ? 0.2920 0.3864 0.1885 0.1015  -0.0161 -0.1116 728  LEU A CD1 
5467  C CD2 . LEU A 730  ? 0.2806 0.3598 0.1761 0.0957  -0.0187 -0.1073 728  LEU A CD2 
5468  N N   . ALA A 731  ? 0.2595 0.3270 0.1643 0.0950  -0.0075 -0.0976 729  ALA A N   
5469  C CA  . ALA A 731  ? 0.2651 0.3235 0.1735 0.0934  -0.0060 -0.0951 729  ALA A CA  
5470  C C   . ALA A 731  ? 0.2522 0.3039 0.1679 0.0948  -0.0094 -0.1019 729  ALA A C   
5471  O O   . ALA A 731  ? 0.2743 0.3327 0.1914 0.0978  -0.0093 -0.1056 729  ALA A O   
5472  C CB  . ALA A 731  ? 0.2757 0.3419 0.1815 0.0936  -0.0007 -0.0888 729  ALA A CB  
5473  N N   . LYS A 732  ? 0.2593 0.2979 0.1797 0.0925  -0.0124 -0.1033 730  LYS A N   
5474  C CA  . LYS A 732  ? 0.2941 0.3248 0.2223 0.0932  -0.0160 -0.1087 730  LYS A CA  
5475  C C   . LYS A 732  ? 0.2815 0.3041 0.2131 0.0913  -0.0141 -0.1047 730  LYS A C   
5476  O O   . LYS A 732  ? 0.2732 0.2858 0.2064 0.0882  -0.0150 -0.1019 730  LYS A O   
5477  C CB  . LYS A 732  ? 0.2936 0.3156 0.2258 0.0917  -0.0214 -0.1130 730  LYS A CB  
5478  C CG  . LYS A 732  ? 0.3352 0.3552 0.2741 0.0938  -0.0260 -0.1205 730  LYS A CG  
5479  C CD  . LYS A 732  ? 0.3641 0.3777 0.3095 0.0940  -0.0262 -0.1209 730  LYS A CD  
5480  C CE  . LYS A 732  ? 0.4099 0.4097 0.3605 0.0900  -0.0281 -0.1181 730  LYS A CE  
5481  N NZ  . LYS A 732  ? 0.4036 0.3977 0.3609 0.0902  -0.0285 -0.1182 730  LYS A NZ  
5482  N N   . PRO A 733  ? 0.2493 0.2760 0.1822 0.0932  -0.0116 -0.1041 731  PRO A N   
5483  C CA  . PRO A 733  ? 0.2709 0.2903 0.2072 0.0915  -0.0098 -0.1002 731  PRO A CA  
5484  C C   . PRO A 733  ? 0.2498 0.2578 0.1947 0.0908  -0.0142 -0.1041 731  PRO A C   
5485  O O   . PRO A 733  ? 0.2928 0.3004 0.2414 0.0924  -0.0181 -0.1102 731  PRO A O   
5486  C CB  . PRO A 733  ? 0.2869 0.3163 0.2216 0.0940  -0.0057 -0.0988 731  PRO A CB  
5487  C CG  . PRO A 733  ? 0.2909 0.3286 0.2257 0.0974  -0.0077 -0.1051 731  PRO A CG  
5488  C CD  . PRO A 733  ? 0.2752 0.3141 0.2064 0.0968  -0.0101 -0.1068 731  PRO A CD  
5489  N N   . ALA A 734  ? 0.2802 0.2792 0.2284 0.0883  -0.0135 -0.1000 732  ALA A N   
5490  C CA  . ALA A 734  ? 0.2945 0.2829 0.2513 0.0872  -0.0175 -0.1022 732  ALA A CA  
5491  C C   . ALA A 734  ? 0.2712 0.2634 0.2322 0.0905  -0.0186 -0.1072 732  ALA A C   
5492  O O   . ALA A 734  ? 0.2866 0.2881 0.2448 0.0931  -0.0151 -0.1068 732  ALA A O   
5493  C CB  . ALA A 734  ? 0.2635 0.2440 0.2227 0.0845  -0.0158 -0.0965 732  ALA A CB  
5494  N N   . GLU A 735  ? 0.3029 0.2882 0.2711 0.0903  -0.0238 -0.1116 733  GLU A N   
5495  C CA  . GLU A 735  ? 0.3180 0.3061 0.2909 0.0935  -0.0256 -0.1168 733  GLU A CA  
5496  C C   . GLU A 735  ? 0.2776 0.2668 0.2523 0.0944  -0.0224 -0.1141 733  GLU A C   
5497  O O   . GLU A 735  ? 0.3021 0.2990 0.2770 0.0979  -0.0215 -0.1174 733  GLU A O   
5498  C CB  . GLU A 735  ? 0.3657 0.3441 0.3471 0.0923  -0.0317 -0.1206 733  GLU A CB  
5499  C CG  . GLU A 735  ? 0.4562 0.4373 0.4427 0.0958  -0.0346 -0.1270 733  GLU A CG  
5500  C CD  . GLU A 735  ? 0.5317 0.5033 0.5267 0.0944  -0.0410 -0.1303 733  GLU A CD  
5501  O OE1 . GLU A 735  ? 0.5575 0.5210 0.5542 0.0906  -0.0429 -0.1274 733  GLU A OE1 
5502  O OE2 . GLU A 735  ? 0.6246 0.5972 0.6249 0.0971  -0.0440 -0.1357 733  GLU A OE2 
5503  N N   . GLU A 736  ? 0.2749 0.2572 0.2509 0.0914  -0.0208 -0.1082 734  GLU A N   
5504  C CA  . GLU A 736  ? 0.2815 0.2632 0.2604 0.0918  -0.0184 -0.1054 734  GLU A CA  
5505  C C   . GLU A 736  ? 0.2954 0.2881 0.2677 0.0937  -0.0125 -0.1023 734  GLU A C   
5506  O O   . GLU A 736  ? 0.2961 0.2916 0.2706 0.0953  -0.0106 -0.1016 734  GLU A O   
5507  C CB  . GLU A 736  ? 0.3137 0.2840 0.2965 0.0878  -0.0191 -0.1000 734  GLU A CB  
5508  C CG  . GLU A 736  ? 0.3495 0.3088 0.3401 0.0854  -0.0249 -0.1016 734  GLU A CG  
5509  C CD  . GLU A 736  ? 0.4243 0.3793 0.4132 0.0827  -0.0273 -0.1015 734  GLU A CD  
5510  O OE1 . GLU A 736  ? 0.3241 0.2853 0.3056 0.0833  -0.0252 -0.1017 734  GLU A OE1 
5511  O OE2 . GLU A 736  ? 0.4554 0.4010 0.4507 0.0797  -0.0316 -0.1008 734  GLU A OE2 
5512  N N   . THR A 737  ? 0.2588 0.2577 0.2234 0.0934  -0.0097 -0.1001 735  THR A N   
5513  C CA  . THR A 737  ? 0.2789 0.2875 0.2376 0.0942  -0.0040 -0.0955 735  THR A CA  
5514  C C   . THR A 737  ? 0.2734 0.2943 0.2252 0.0962  -0.0023 -0.0968 735  THR A C   
5515  O O   . THR A 737  ? 0.2907 0.3160 0.2362 0.0950  0.0008  -0.0922 735  THR A O   
5516  C CB  . THR A 737  ? 0.2557 0.2590 0.2123 0.0908  -0.0016 -0.0883 735  THR A CB  
5517  O OG1 . THR A 737  ? 0.2546 0.2533 0.2090 0.0879  -0.0037 -0.0875 735  THR A OG1 
5518  C CG2 . THR A 737  ? 0.2619 0.2547 0.2258 0.0878  -0.0029 -0.0851 735  THR A CG2 
5519  N N   . PRO A 738  ? 0.2529 0.2799 0.2056 0.0993  -0.0042 -0.1029 736  PRO A N   
5520  C CA  . PRO A 738  ? 0.2686 0.3082 0.2149 0.1013  -0.0027 -0.1040 736  PRO A CA  
5521  C C   . PRO A 738  ? 0.2597 0.3116 0.2016 0.1026  0.0026  -0.0998 736  PRO A C   
5522  O O   . PRO A 738  ? 0.2853 0.3471 0.2211 0.1030  0.0046  -0.0980 736  PRO A O   
5523  C CB  . PRO A 738  ? 0.2592 0.3006 0.2090 0.1043  -0.0069 -0.1122 736  PRO A CB  
5524  C CG  . PRO A 738  ? 0.2609 0.2964 0.2179 0.1051  -0.0082 -0.1140 736  PRO A CG  
5525  C CD  . PRO A 738  ? 0.2552 0.2786 0.2151 0.1013  -0.0081 -0.1089 736  PRO A CD  
5526  N N   . LEU A 739  ? 0.2564 0.3088 0.2017 0.1032  0.0047  -0.0980 737  LEU A N   
5527  C CA  . LEU A 739  ? 0.2536 0.3189 0.1957 0.1047  0.0092  -0.0947 737  LEU A CA  
5528  C C   . LEU A 739  ? 0.2505 0.3196 0.1871 0.1021  0.0136  -0.0864 737  LEU A C   
5529  O O   . LEU A 739  ? 0.2660 0.3470 0.1975 0.1027  0.0163  -0.0836 737  LEU A O   
5530  C CB  . LEU A 739  ? 0.2691 0.3337 0.2165 0.1059  0.0102  -0.0950 737  LEU A CB  
5531  C CG  . LEU A 739  ? 0.2879 0.3493 0.2412 0.1087  0.0059  -0.1029 737  LEU A CG  
5532  C CD1 . LEU A 739  ? 0.2799 0.3397 0.2387 0.1095  0.0070  -0.1022 737  LEU A CD1 
5533  C CD2 . LEU A 739  ? 0.2750 0.3480 0.2257 0.1122  0.0050  -0.1082 737  LEU A CD2 
5534  N N   . ILE A 740  ? 0.2375 0.2966 0.1752 0.0991  0.0142  -0.0821 738  ILE A N   
5535  C CA  . ILE A 740  ? 0.2637 0.3258 0.1966 0.0966  0.0182  -0.0740 738  ILE A CA  
5536  C C   . ILE A 740  ? 0.2460 0.3111 0.1733 0.0958  0.0174  -0.0736 738  ILE A C   
5537  O O   . ILE A 740  ? 0.2668 0.3396 0.1891 0.0946  0.0206  -0.0677 738  ILE A O   
5538  C CB  . ILE A 740  ? 0.2555 0.3057 0.1920 0.0928  0.0183  -0.0690 738  ILE A CB  
5539  C CG1 . ILE A 740  ? 0.2613 0.3137 0.1949 0.0883  0.0219  -0.0590 738  ILE A CG1 
5540  C CG2 . ILE A 740  ? 0.2751 0.3124 0.2142 0.0907  0.0137  -0.0719 738  ILE A CG2 
5541  C CD1 . ILE A 740  ? 0.2810 0.3445 0.2136 0.0892  0.0265  -0.0543 738  ILE A CD1 
5542  N N   . ALA A 741  ? 0.2626 0.3220 0.1909 0.0963  0.0129  -0.0798 739  ALA A N   
5543  C CA  . ALA A 741  ? 0.2617 0.3247 0.1848 0.0959  0.0119  -0.0801 739  ALA A CA  
5544  C C   . ALA A 741  ? 0.2458 0.3236 0.1651 0.0983  0.0133  -0.0807 739  ALA A C   
5545  O O   . ALA A 741  ? 0.2591 0.3441 0.1730 0.0974  0.0153  -0.0762 739  ALA A O   
5546  C CB  . ALA A 741  ? 0.2739 0.3276 0.1997 0.0960  0.0065  -0.0867 739  ALA A CB  
5547  N N   . ALA A 742  ? 0.2546 0.3371 0.1769 0.1015  0.0122  -0.0861 740  ALA A N   
5548  C CA  . ALA A 742  ? 0.2487 0.3460 0.1676 0.1040  0.0135  -0.0869 740  ALA A CA  
5549  C C   . ALA A 742  ? 0.2443 0.3510 0.1600 0.1028  0.0187  -0.0784 740  ALA A C   
5550  O O   . ALA A 742  ? 0.2795 0.3974 0.1907 0.1031  0.0203  -0.0754 740  ALA A O   
5551  C CB  . ALA A 742  ? 0.2611 0.3613 0.1843 0.1077  0.0115  -0.0941 740  ALA A CB  
5552  N N   . GLU A 743  ? 0.2513 0.3536 0.1698 0.1012  0.0212  -0.0740 741  GLU A N   
5553  C CA  . GLU A 743  ? 0.2687 0.3795 0.1850 0.0996  0.0260  -0.0654 741  GLU A CA  
5554  C C   . GLU A 743  ? 0.2563 0.3665 0.1682 0.0964  0.0274  -0.0585 741  GLU A C   
5555  O O   . GLU A 743  ? 0.2685 0.3892 0.1771 0.0956  0.0301  -0.0524 741  GLU A O   
5556  C CB  . GLU A 743  ? 0.2604 0.3663 0.1814 0.0988  0.0280  -0.0628 741  GLU A CB  
5557  C CG  . GLU A 743  ? 0.2785 0.3914 0.1983 0.0966  0.0327  -0.0534 741  GLU A CG  
5558  C CD  . GLU A 743  ? 0.2880 0.4163 0.2063 0.0982  0.0349  -0.0517 741  GLU A CD  
5559  O OE1 . GLU A 743  ? 0.3102 0.4442 0.2285 0.1015  0.0329  -0.0583 741  GLU A OE1 
5560  O OE2 . GLU A 743  ? 0.3230 0.4580 0.2403 0.0960  0.0384  -0.0434 741  GLU A OE2 
5561  N N   . GLY A 744  ? 0.2636 0.3619 0.1756 0.0946  0.0254  -0.0593 742  GLY A N   
5562  C CA  . GLY A 744  ? 0.2397 0.3372 0.1475 0.0919  0.0262  -0.0535 742  GLY A CA  
5563  C C   . GLY A 744  ? 0.2327 0.3395 0.1360 0.0928  0.0252  -0.0543 742  GLY A C   
5564  O O   . GLY A 744  ? 0.2585 0.3716 0.1582 0.0910  0.0273  -0.0473 742  GLY A O   
5565  N N   . VAL A 745  ? 0.2511 0.3590 0.1549 0.0956  0.0217  -0.0626 743  VAL A N   
5566  C CA  . VAL A 745  ? 0.2580 0.3753 0.1577 0.0969  0.0206  -0.0639 743  VAL A CA  
5567  C C   . VAL A 745  ? 0.2553 0.3879 0.1533 0.0981  0.0236  -0.0599 743  VAL A C   
5568  O O   . VAL A 745  ? 0.2925 0.4338 0.1865 0.0974  0.0246  -0.0555 743  VAL A O   
5569  C CB  . VAL A 745  ? 0.2587 0.3732 0.1601 0.0998  0.0160  -0.0741 743  VAL A CB  
5570  C CG1 . VAL A 745  ? 0.3132 0.4400 0.2107 0.1019  0.0150  -0.0761 743  VAL A CG1 
5571  C CG2 . VAL A 745  ? 0.3078 0.4082 0.2104 0.0979  0.0127  -0.0767 743  VAL A CG2 
5572  N N   . ARG A 746  ? 0.2708 0.4069 0.1718 0.0998  0.0251  -0.0612 744  ARG A N   
5573  C CA  . ARG A 746  ? 0.2484 0.3992 0.1483 0.1006  0.0281  -0.0569 744  ARG A CA  
5574  C C   . ARG A 746  ? 0.2775 0.4313 0.1754 0.0970  0.0316  -0.0459 744  ARG A C   
5575  O O   . ARG A 746  ? 0.2923 0.4577 0.1875 0.0968  0.0329  -0.0412 744  ARG A O   
5576  C CB  . ARG A 746  ? 0.2562 0.4088 0.1602 0.1026  0.0292  -0.0596 744  ARG A CB  
5577  C CG  . ARG A 746  ? 0.3047 0.4729 0.2078 0.1040  0.0318  -0.0564 744  ARG A CG  
5578  C CD  . ARG A 746  ? 0.2899 0.4591 0.1974 0.1050  0.0336  -0.0566 744  ARG A CD  
5579  N NE  . ARG A 746  ? 0.3200 0.4825 0.2295 0.1014  0.0364  -0.0492 744  ARG A NE  
5580  C CZ  . ARG A 746  ? 0.3632 0.5312 0.2714 0.0984  0.0395  -0.0396 744  ARG A CZ  
5581  N NH1 . ARG A 746  ? 0.3692 0.5497 0.2743 0.0984  0.0405  -0.0357 744  ARG A NH1 
5582  N NH2 . ARG A 746  ? 0.2849 0.4460 0.1956 0.0953  0.0416  -0.0336 744  ARG A NH2 
5583  N N   . ILE A 747  ? 0.2510 0.3945 0.1508 0.0940  0.0328  -0.0416 745  ILE A N   
5584  C CA  . ILE A 747  ? 0.2629 0.4081 0.1619 0.0903  0.0358  -0.0311 745  ILE A CA  
5585  C C   . ILE A 747  ? 0.2327 0.3792 0.1276 0.0887  0.0348  -0.0277 745  ILE A C   
5586  O O   . ILE A 747  ? 0.2550 0.4101 0.1484 0.0870  0.0367  -0.0201 745  ILE A O   
5587  C CB  . ILE A 747  ? 0.2465 0.3799 0.1486 0.0878  0.0370  -0.0281 745  ILE A CB  
5588  C CG1 . ILE A 747  ? 0.2383 0.3735 0.1447 0.0889  0.0389  -0.0289 745  ILE A CG1 
5589  C CG2 . ILE A 747  ? 0.2623 0.3946 0.1635 0.0837  0.0392  -0.0180 745  ILE A CG2 
5590  C CD1 . ILE A 747  ? 0.2687 0.3918 0.1787 0.0874  0.0395  -0.0281 745  ILE A CD1 
5591  N N   . LEU A 748  ? 0.2338 0.3717 0.1271 0.0890  0.0317  -0.0330 746  LEU A N   
5592  C CA  . LEU A 748  ? 0.2544 0.3933 0.1439 0.0876  0.0306  -0.0302 746  LEU A CA  
5593  C C   . LEU A 748  ? 0.2702 0.4228 0.1569 0.0897  0.0301  -0.0309 746  LEU A C   
5594  O O   . LEU A 748  ? 0.2522 0.4108 0.1365 0.0880  0.0308  -0.0246 746  LEU A O   
5595  C CB  . LEU A 748  ? 0.2476 0.3748 0.1364 0.0878  0.0270  -0.0365 746  LEU A CB  
5596  C CG  . LEU A 748  ? 0.2979 0.4121 0.1881 0.0850  0.0275  -0.0334 746  LEU A CG  
5597  C CD1 . LEU A 748  ? 0.3144 0.4167 0.2058 0.0859  0.0238  -0.0417 746  LEU A CD1 
5598  C CD2 . LEU A 748  ? 0.2935 0.4081 0.1811 0.0818  0.0285  -0.0250 746  LEU A CD2 
5599  N N   . ARG A 749  ? 0.2537 0.4117 0.1411 0.0933  0.0289  -0.0385 747  ARG A N   
5600  C CA  . ARG A 749  ? 0.2680 0.4402 0.1529 0.0956  0.0286  -0.0393 747  ARG A CA  
5601  C C   . ARG A 749  ? 0.2566 0.4407 0.1418 0.0945  0.0322  -0.0308 747  ARG A C   
5602  O O   . ARG A 749  ? 0.2791 0.4735 0.1619 0.0941  0.0327  -0.0262 747  ARG A O   
5603  C CB  . ARG A 749  ? 0.2799 0.4546 0.1658 0.0999  0.0262  -0.0498 747  ARG A CB  
5604  C CG  . ARG A 749  ? 0.3039 0.4709 0.1891 0.1011  0.0219  -0.0579 747  ARG A CG  
5605  C CD  . ARG A 749  ? 0.3559 0.5242 0.2434 0.1052  0.0193  -0.0682 747  ARG A CD  
5606  N NE  . ARG A 749  ? 0.3155 0.4779 0.2027 0.1063  0.0149  -0.0757 747  ARG A NE  
5607  C CZ  . ARG A 749  ? 0.3106 0.4764 0.1991 0.1100  0.0119  -0.0845 747  ARG A CZ  
5608  N NH1 . ARG A 749  ? 0.3295 0.5047 0.2194 0.1131  0.0127  -0.0874 747  ARG A NH1 
5609  N NH2 . ARG A 749  ? 0.3444 0.5044 0.2329 0.1106  0.0079  -0.0905 747  ARG A NH2 
5610  N N   . GLU A 750  ? 0.2500 0.4327 0.1385 0.0938  0.0346  -0.0282 748  GLU A N   
5611  C CA  . GLU A 750  ? 0.2592 0.4524 0.1488 0.0922  0.0379  -0.0195 748  GLU A CA  
5612  C C   . GLU A 750  ? 0.2597 0.4518 0.1485 0.0881  0.0390  -0.0095 748  GLU A C   
5613  O O   . GLU A 750  ? 0.2968 0.4999 0.1852 0.0871  0.0404  -0.0027 748  GLU A O   
5614  C CB  . GLU A 750  ? 0.2510 0.4413 0.1448 0.0918  0.0400  -0.0185 748  GLU A CB  
5615  C CG  . GLU A 750  ? 0.3070 0.5087 0.2026 0.0903  0.0432  -0.0099 748  GLU A CG  
5616  C CD  . GLU A 750  ? 0.3402 0.5381 0.2402 0.0893  0.0454  -0.0078 748  GLU A CD  
5617  O OE1 . GLU A 750  ? 0.4176 0.6072 0.3192 0.0910  0.0445  -0.0147 748  GLU A OE1 
5618  O OE2 . GLU A 750  ? 0.3316 0.5345 0.2338 0.0867  0.0479  0.0008  748  GLU A OE2 
5619  N N   . ALA A 751  ? 0.2409 0.4198 0.1297 0.0857  0.0381  -0.0086 749  ALA A N   
5620  C CA  . ALA A 751  ? 0.2738 0.4498 0.1624 0.0818  0.0387  0.0004  749  ALA A CA  
5621  C C   . ALA A 751  ? 0.2800 0.4617 0.1649 0.0820  0.0370  0.0013  749  ALA A C   
5622  O O   . ALA A 751  ? 0.2735 0.4545 0.1584 0.0789  0.0374  0.0092  749  ALA A O   
5623  C CB  . ALA A 751  ? 0.2579 0.4182 0.1475 0.0797  0.0381  0.0000  749  ALA A CB  
5624  N N   . GLY A 752  ? 0.2630 0.4500 0.1451 0.0855  0.0350  -0.0066 750  GLY A N   
5625  C CA  . GLY A 752  ? 0.2871 0.4812 0.1658 0.0861  0.0334  -0.0061 750  GLY A CA  
5626  C C   . GLY A 752  ? 0.2894 0.4766 0.1654 0.0877  0.0299  -0.0141 750  GLY A C   
5627  O O   . GLY A 752  ? 0.2925 0.4856 0.1656 0.0883  0.0284  -0.0142 750  GLY A O   
5628  N N   . ILE A 753  ? 0.2696 0.4445 0.1467 0.0882  0.0284  -0.0206 751  ILE A N   
5629  C CA  . ILE A 753  ? 0.2815 0.4500 0.1568 0.0897  0.0248  -0.0286 751  ILE A CA  
5630  C C   . ILE A 753  ? 0.2748 0.4527 0.1490 0.0938  0.0231  -0.0365 751  ILE A C   
5631  O O   . ILE A 753  ? 0.3105 0.4907 0.1869 0.0962  0.0235  -0.0413 751  ILE A O   
5632  C CB  . ILE A 753  ? 0.2617 0.4151 0.1393 0.0893  0.0235  -0.0336 751  ILE A CB  
5633  C CG1 . ILE A 753  ? 0.2729 0.4173 0.1515 0.0854  0.0253  -0.0259 751  ILE A CG1 
5634  C CG2 . ILE A 753  ? 0.2984 0.4453 0.1748 0.0906  0.0194  -0.0418 751  ILE A CG2 
5635  C CD1 . ILE A 753  ? 0.3012 0.4442 0.1772 0.0830  0.0245  -0.0206 751  ILE A CD1 
5636  N N   . PRO A 754  ? 0.2839 0.4678 0.1551 0.0949  0.0210  -0.0383 752  PRO A N   
5637  C CA  . PRO A 754  ? 0.3096 0.5032 0.1800 0.0990  0.0193  -0.0460 752  PRO A CA  
5638  C C   . PRO A 754  ? 0.2742 0.4588 0.1469 0.1014  0.0163  -0.0568 752  PRO A C   
5639  O O   . PRO A 754  ? 0.2863 0.4573 0.1603 0.0999  0.0146  -0.0591 752  PRO A O   
5640  C CB  . PRO A 754  ? 0.3269 0.5261 0.1937 0.0991  0.0175  -0.0452 752  PRO A CB  
5641  C CG  . PRO A 754  ? 0.3107 0.5073 0.1767 0.0950  0.0193  -0.0348 752  PRO A CG  
5642  C CD  . PRO A 754  ? 0.2795 0.4624 0.1481 0.0925  0.0203  -0.0331 752  PRO A CD  
5643  N N   . ALA A 755  ? 0.3052 0.4979 0.1789 0.1052  0.0156  -0.0632 753  ALA A N   
5644  C CA  . ALA A 755  ? 0.2823 0.4675 0.1591 0.1076  0.0125  -0.0735 753  ALA A CA  
5645  C C   . ALA A 755  ? 0.3122 0.4896 0.1885 0.1077  0.0083  -0.0793 753  ALA A C   
5646  O O   . ALA A 755  ? 0.3363 0.5015 0.2158 0.1077  0.0057  -0.0851 753  ALA A O   
5647  C CB  . ALA A 755  ? 0.3302 0.5273 0.2079 0.1119  0.0122  -0.0793 753  ALA A CB  
5648  N N   . SER A 756  ? 0.3094 0.4938 0.1821 0.1076  0.0076  -0.0775 754  SER A N   
5649  C CA  . SER A 756  ? 0.3296 0.5071 0.2017 0.1075  0.0036  -0.0826 754  SER A CA  
5650  C C   . SER A 756  ? 0.3194 0.4830 0.1918 0.1036  0.0033  -0.0786 754  SER A C   
5651  O O   . SER A 756  ? 0.3186 0.4733 0.1919 0.1032  -0.0002 -0.0835 754  SER A O   
5652  C CB  . SER A 756  ? 0.3066 0.4961 0.1747 0.1086  0.0029  -0.0815 754  SER A CB  
5653  O OG  . SER A 756  ? 0.3775 0.5710 0.2426 0.1056  0.0059  -0.0711 754  SER A OG  
5654  N N   . ALA A 757  ? 0.2805 0.4423 0.1524 0.1007  0.0069  -0.0698 755  ALA A N   
5655  C CA  . ALA A 757  ? 0.2748 0.4240 0.1468 0.0971  0.0068  -0.0657 755  ALA A CA  
5656  C C   . ALA A 757  ? 0.2996 0.4361 0.1758 0.0963  0.0066  -0.0685 755  ALA A C   
5657  O O   . ALA A 757  ? 0.2795 0.4043 0.1564 0.0939  0.0055  -0.0676 755  ALA A O   
5658  C CB  . ALA A 757  ? 0.3131 0.4663 0.1829 0.0941  0.0104  -0.0545 755  ALA A CB  
5659  N N   . LEU A 758  ? 0.2818 0.4203 0.1607 0.0985  0.0074  -0.0720 756  LEU A N   
5660  C CA  . LEU A 758  ? 0.2770 0.4040 0.1603 0.0978  0.0073  -0.0742 756  LEU A CA  
5661  C C   . LEU A 758  ? 0.2834 0.4121 0.1703 0.1013  0.0054  -0.0827 756  LEU A C   
5662  O O   . LEU A 758  ? 0.2958 0.4340 0.1829 0.1033  0.0076  -0.0821 756  LEU A O   
5663  C CB  . LEU A 758  ? 0.2793 0.4065 0.1628 0.0957  0.0117  -0.0659 756  LEU A CB  
5664  C CG  . LEU A 758  ? 0.2782 0.3950 0.1662 0.0953  0.0121  -0.0677 756  LEU A CG  
5665  C CD1 . LEU A 758  ? 0.2832 0.3852 0.1735 0.0938  0.0089  -0.0715 756  LEU A CD1 
5666  C CD2 . LEU A 758  ? 0.2935 0.4113 0.1814 0.0929  0.0165  -0.0587 756  LEU A CD2 
5667  N N   . GLN A 759  ? 0.2704 0.3897 0.1605 0.1020  0.0012  -0.0903 757  GLN A N   
5668  C CA  . GLN A 759  ? 0.2878 0.4069 0.1823 0.1052  -0.0015 -0.0989 757  GLN A CA  
5669  C C   . GLN A 759  ? 0.3002 0.4053 0.2002 0.1040  -0.0026 -0.1010 757  GLN A C   
5670  O O   . GLN A 759  ? 0.3134 0.4072 0.2146 0.1012  -0.0039 -0.0996 757  GLN A O   
5671  C CB  . GLN A 759  ? 0.2925 0.4128 0.1871 0.1071  -0.0060 -0.1063 757  GLN A CB  
5672  C CG  . GLN A 759  ? 0.2867 0.4217 0.1763 0.1088  -0.0051 -0.1050 757  GLN A CG  
5673  C CD  . GLN A 759  ? 0.3013 0.4371 0.1910 0.1104  -0.0097 -0.1120 757  GLN A CD  
5674  O OE1 . GLN A 759  ? 0.3262 0.4665 0.2182 0.1139  -0.0121 -0.1194 757  GLN A OE1 
5675  N NE2 . GLN A 759  ? 0.2997 0.4310 0.1872 0.1080  -0.0109 -0.1097 757  GLN A NE2 
5676  N N   . LEU A 760  ? 0.3043 0.4107 0.2079 0.1061  -0.0022 -0.1039 758  LEU A N   
5677  C CA  . LEU A 760  ? 0.2847 0.3789 0.1942 0.1052  -0.0032 -0.1058 758  LEU A CA  
5678  C C   . LEU A 760  ? 0.3093 0.3988 0.2243 0.1075  -0.0083 -0.1151 758  LEU A C   
5679  O O   . LEU A 760  ? 0.3064 0.4049 0.2218 0.1110  -0.0093 -0.1201 758  LEU A O   
5680  C CB  . LEU A 760  ? 0.2770 0.3753 0.1877 0.1059  0.0006  -0.1025 758  LEU A CB  
5681  C CG  . LEU A 760  ? 0.2915 0.3777 0.2084 0.1051  -0.0003 -0.1039 758  LEU A CG  
5682  C CD1 . LEU A 760  ? 0.3105 0.3867 0.2270 0.1011  0.0012  -0.0976 758  LEU A CD1 
5683  C CD2 . LEU A 760  ? 0.3201 0.4124 0.2390 0.1071  0.0024  -0.1035 758  LEU A CD2 
5684  N N   . LEU A 761  ? 0.2746 0.3502 0.1941 0.1055  -0.0117 -0.1172 759  LEU A N   
5685  C CA  . LEU A 761  ? 0.3057 0.3752 0.2314 0.1069  -0.0170 -0.1254 759  LEU A CA  
5686  C C   . LEU A 761  ? 0.3105 0.3676 0.2432 0.1056  -0.0184 -0.1259 759  LEU A C   
5687  O O   . LEU A 761  ? 0.3144 0.3594 0.2502 0.1026  -0.0208 -0.1251 759  LEU A O   
5688  C CB  . LEU A 761  ? 0.2877 0.3525 0.2130 0.1056  -0.0209 -0.1277 759  LEU A CB  
5689  C CG  . LEU A 761  ? 0.3260 0.4017 0.2456 0.1069  -0.0210 -0.1287 759  LEU A CG  
5690  C CD1 . LEU A 761  ? 0.3254 0.4150 0.2434 0.1113  -0.0201 -0.1324 759  LEU A CD1 
5691  C CD2 . LEU A 761  ? 0.3666 0.4452 0.2795 0.1043  -0.0173 -0.1207 759  LEU A CD2 
5692  N N   . PRO A 762  ? 0.3007 0.3603 0.2361 0.1076  -0.0170 -0.1268 760  PRO A N   
5693  C CA  . PRO A 762  ? 0.3101 0.3582 0.2527 0.1063  -0.0184 -0.1271 760  PRO A CA  
5694  C C   . PRO A 762  ? 0.3786 0.4179 0.3283 0.1066  -0.0245 -0.1338 760  PRO A C   
5695  O O   . PRO A 762  ? 0.3327 0.3770 0.2827 0.1091  -0.0275 -0.1398 760  PRO A O   
5696  C CB  . PRO A 762  ? 0.3044 0.3599 0.2479 0.1092  -0.0157 -0.1276 760  PRO A CB  
5697  C CG  . PRO A 762  ? 0.2758 0.3465 0.2119 0.1110  -0.0118 -0.1252 760  PRO A CG  
5698  C CD  . PRO A 762  ? 0.2853 0.3589 0.2178 0.1110  -0.0141 -0.1275 760  PRO A CD  
5699  N N   . GLY A 763  ? 0.3336 0.3600 0.2893 0.1039  -0.0265 -0.1324 761  GLY A N   
5700  C CA  . GLY A 763  ? 0.4032 0.4208 0.3669 0.1038  -0.0323 -0.1378 761  GLY A CA  
5701  C C   . GLY A 763  ? 0.4524 0.4563 0.4203 0.0993  -0.0343 -0.1341 761  GLY A C   
5702  O O   . GLY A 763  ? 0.4305 0.4312 0.3956 0.0966  -0.0310 -0.1277 761  GLY A O   
5703  N N   . ASP A 764  ? 0.4922 0.4883 0.4671 0.0986  -0.0398 -0.1382 762  ASP A N   
5704  C CA  . ASP A 764  ? 0.4836 0.4665 0.4642 0.0942  -0.0426 -0.1350 762  ASP A CA  
5705  C C   . ASP A 764  ? 0.5396 0.5205 0.5169 0.0916  -0.0436 -0.1336 762  ASP A C   
5706  O O   . ASP A 764  ? 0.4967 0.4860 0.4663 0.0927  -0.0411 -0.1333 762  ASP A O   
5707  C CB  . ASP A 764  ? 0.5593 0.5352 0.5500 0.0946  -0.0481 -0.1395 762  ASP A CB  
5708  C CG  . ASP A 764  ? 0.6178 0.5982 0.6101 0.0975  -0.0523 -0.1471 762  ASP A CG  
5709  O OD1 . ASP A 764  ? 0.6100 0.5920 0.5989 0.0968  -0.0534 -0.1480 762  ASP A OD1 
5710  O OD2 . ASP A 764  ? 0.6713 0.6535 0.6683 0.1006  -0.0546 -0.1522 762  ASP A OD2 
5711  N N   . GLY A 765  ? 0.5202 0.4902 0.5034 0.0880  -0.0475 -0.1324 763  GLY A N   
5712  C CA  . GLY A 765  ? 0.5626 0.5297 0.5432 0.0850  -0.0484 -0.1302 763  GLY A CA  
5713  C C   . GLY A 765  ? 0.5018 0.4737 0.4811 0.0866  -0.0515 -0.1357 763  GLY A C   
5714  O O   . GLY A 765  ? 0.5240 0.4971 0.4987 0.0850  -0.0511 -0.1340 763  GLY A O   
5715  N N   . ARG A 766  ? 0.4821 0.4569 0.4655 0.0898  -0.0548 -0.1422 764  ARG A N   
5716  C CA  . ARG A 766  ? 0.5325 0.5126 0.5147 0.0917  -0.0577 -0.1477 764  ARG A CA  
5717  C C   . ARG A 766  ? 0.4751 0.4683 0.4475 0.0947  -0.0537 -0.1483 764  ARG A C   
5718  O O   . ARG A 766  ? 0.4443 0.4422 0.4135 0.0953  -0.0550 -0.1507 764  ARG A O   
5719  C CB  . ARG A 766  ? 0.5984 0.5777 0.5885 0.0943  -0.0628 -0.1548 764  ARG A CB  
5720  C CG  . ARG A 766  ? 0.6323 0.6211 0.6208 0.0992  -0.0611 -0.1591 764  ARG A CG  
5721  C CD  . ARG A 766  ? 0.6688 0.6524 0.6670 0.1006  -0.0653 -0.1632 764  ARG A CD  
5722  N NE  . ARG A 766  ? 0.7044 0.6934 0.7014 0.1036  -0.0620 -0.1635 764  ARG A NE  
5723  C CZ  . ARG A 766  ? 0.7552 0.7530 0.7523 0.1083  -0.0626 -0.1697 764  ARG A CZ  
5724  N NH1 . ARG A 766  ? 0.7370 0.7390 0.7355 0.1109  -0.0665 -0.1765 764  ARG A NH1 
5725  N NH2 . ARG A 766  ? 0.7715 0.7741 0.7673 0.1106  -0.0593 -0.1692 764  ARG A NH2 
5726  N N   . VAL A 767  ? 0.4904 0.4900 0.4583 0.0965  -0.0488 -0.1459 765  VAL A N   
5727  C CA  . VAL A 767  ? 0.4441 0.4557 0.4024 0.0983  -0.0444 -0.1443 765  VAL A CA  
5728  C C   . VAL A 767  ? 0.3573 0.3667 0.3103 0.0948  -0.0424 -0.1384 765  VAL A C   
5729  O O   . VAL A 767  ? 0.3956 0.4116 0.3431 0.0953  -0.0421 -0.1387 765  VAL A O   
5730  C CB  . VAL A 767  ? 0.3785 0.3971 0.3339 0.1005  -0.0396 -0.1421 765  VAL A CB  
5731  C CG1 . VAL A 767  ? 0.3723 0.4035 0.3181 0.1019  -0.0349 -0.1391 765  VAL A CG1 
5732  C CG2 . VAL A 767  ? 0.4523 0.4739 0.4127 0.1043  -0.0418 -0.1484 765  VAL A CG2 
5733  N N   . GLY A 768  ? 0.4041 0.4043 0.3589 0.0913  -0.0411 -0.1330 766  GLY A N   
5734  C CA  . GLY A 768  ? 0.3576 0.3550 0.3081 0.0880  -0.0397 -0.1277 766  GLY A CA  
5735  C C   . GLY A 768  ? 0.3883 0.3819 0.3408 0.0863  -0.0442 -0.1303 766  GLY A C   
5736  O O   . GLY A 768  ? 0.3533 0.3506 0.3000 0.0855  -0.0432 -0.1284 766  GLY A O   
5737  N N   . ALA A 769  ? 0.4075 0.3939 0.3683 0.0858  -0.0493 -0.1345 767  ALA A N   
5738  C CA  . ALA A 769  ? 0.3987 0.3812 0.3624 0.0840  -0.0539 -0.1370 767  ALA A CA  
5739  C C   . ALA A 769  ? 0.4131 0.4062 0.3721 0.0872  -0.0546 -0.1416 767  ALA A C   
5740  O O   . ALA A 769  ? 0.3839 0.3780 0.3398 0.0858  -0.0555 -0.1410 767  ALA A O   
5741  C CB  . ALA A 769  ? 0.4282 0.4014 0.4026 0.0829  -0.0593 -0.1402 767  ALA A CB  
5742  N N   . ALA A 770  ? 0.4046 0.4059 0.3630 0.0915  -0.0542 -0.1462 768  ALA A N   
5743  C CA  . ALA A 770  ? 0.4121 0.4245 0.3658 0.0948  -0.0546 -0.1506 768  ALA A CA  
5744  C C   . ALA A 770  ? 0.3505 0.3712 0.2944 0.0946  -0.0501 -0.1456 768  ALA A C   
5745  O O   . ALA A 770  ? 0.3659 0.3920 0.3061 0.0950  -0.0511 -0.1470 768  ALA A O   
5746  C CB  . ALA A 770  ? 0.4120 0.4323 0.3668 0.0995  -0.0545 -0.1557 768  ALA A CB  
5747  N N   . LEU A 771  ? 0.3361 0.3582 0.2758 0.0939  -0.0451 -0.1398 769  LEU A N   
5748  C CA  . LEU A 771  ? 0.3288 0.3582 0.2598 0.0933  -0.0407 -0.1342 769  LEU A CA  
5749  C C   . LEU A 771  ? 0.3422 0.3653 0.2720 0.0895  -0.0421 -0.1310 769  LEU A C   
5750  O O   . LEU A 771  ? 0.3396 0.3693 0.2637 0.0896  -0.0414 -0.1297 769  LEU A O   
5751  C CB  . LEU A 771  ? 0.3327 0.3634 0.2608 0.0930  -0.0355 -0.1284 769  LEU A CB  
5752  C CG  . LEU A 771  ? 0.3150 0.3538 0.2430 0.0966  -0.0333 -0.1304 769  LEU A CG  
5753  C CD1 . LEU A 771  ? 0.3188 0.3566 0.2452 0.0956  -0.0285 -0.1243 769  LEU A CD1 
5754  C CD2 . LEU A 771  ? 0.3456 0.3989 0.2675 0.0997  -0.0318 -0.1318 769  LEU A CD2 
5755  N N   . VAL A 772  ? 0.3353 0.3460 0.2708 0.0862  -0.0440 -0.1295 770  VAL A N   
5756  C CA  . VAL A 772  ? 0.3251 0.3297 0.2598 0.0824  -0.0451 -0.1262 770  VAL A CA  
5757  C C   . VAL A 772  ? 0.3499 0.3559 0.2859 0.0825  -0.0496 -0.1307 770  VAL A C   
5758  O O   . VAL A 772  ? 0.3596 0.3674 0.2912 0.0811  -0.0495 -0.1284 770  VAL A O   
5759  C CB  . VAL A 772  ? 0.3017 0.2931 0.2431 0.0788  -0.0465 -0.1237 770  VAL A CB  
5760  C CG1 . VAL A 772  ? 0.3497 0.3345 0.2920 0.0749  -0.0490 -0.1215 770  VAL A CG1 
5761  C CG2 . VAL A 772  ? 0.3313 0.3217 0.2701 0.0783  -0.0417 -0.1181 770  VAL A CG2 
5762  N N   . ALA A 773  ? 0.3643 0.3694 0.3062 0.0844  -0.0536 -0.1372 771  ALA A N   
5763  C CA  . ALA A 773  ? 0.3465 0.3523 0.2907 0.0846  -0.0582 -0.1419 771  ALA A CA  
5764  C C   . ALA A 773  ? 0.4227 0.4415 0.3599 0.0878  -0.0571 -0.1441 771  ALA A C   
5765  O O   . ALA A 773  ? 0.4121 0.4323 0.3497 0.0878  -0.0604 -0.1471 771  ALA A O   
5766  C CB  . ALA A 773  ? 0.4053 0.4057 0.3588 0.0856  -0.0631 -0.1481 771  ALA A CB  
5767  N N   . ALA A 774  ? 0.3820 0.4106 0.3130 0.0906  -0.0526 -0.1424 772  ALA A N   
5768  C CA  . ALA A 774  ? 0.3723 0.4141 0.2975 0.0939  -0.0518 -0.1447 772  ALA A CA  
5769  C C   . ALA A 774  ? 0.3360 0.3811 0.2554 0.0920  -0.0511 -0.1407 772  ALA A C   
5770  O O   . ALA A 774  ? 0.3374 0.3794 0.2535 0.0892  -0.0483 -0.1341 772  ALA A O   
5771  C CB  . ALA A 774  ? 0.3667 0.4185 0.2872 0.0968  -0.0470 -0.1428 772  ALA A CB  
5772  N N   . ALA A 775  ? 0.3963 0.4478 0.3145 0.0938  -0.0537 -0.1448 773  ALA A N   
5773  C CA  . ALA A 775  ? 0.3926 0.4461 0.3064 0.0918  -0.0540 -0.1418 773  ALA A CA  
5774  C C   . ALA A 775  ? 0.3530 0.4143 0.2584 0.0915  -0.0487 -0.1343 773  ALA A C   
5775  O O   . ALA A 775  ? 0.4050 0.4647 0.3073 0.0889  -0.0482 -0.1295 773  ALA A O   
5776  C CB  . ALA A 775  ? 0.4568 0.5173 0.3707 0.0943  -0.0575 -0.1479 773  ALA A CB  
5777  N N   . GLU A 776  ? 0.3611 0.4311 0.2631 0.0942  -0.0449 -0.1329 774  GLU A N   
5778  C CA  . GLU A 776  ? 0.3352 0.4135 0.2298 0.0939  -0.0400 -0.1254 774  GLU A CA  
5779  C C   . GLU A 776  ? 0.2824 0.3538 0.1765 0.0912  -0.0366 -0.1187 774  GLU A C   
5780  O O   . GLU A 776  ? 0.3499 0.4267 0.2384 0.0905  -0.0327 -0.1117 774  GLU A O   
5781  C CB  . GLU A 776  ? 0.3500 0.4419 0.2411 0.0978  -0.0374 -0.1262 774  GLU A CB  
5782  C CG  . GLU A 776  ? 0.4760 0.5762 0.3671 0.1008  -0.0406 -0.1328 774  GLU A CG  
5783  C CD  . GLU A 776  ? 0.4875 0.5863 0.3845 0.1037  -0.0434 -0.1412 774  GLU A CD  
5784  O OE1 . GLU A 776  ? 0.4136 0.5013 0.3164 0.1025  -0.0447 -0.1429 774  GLU A OE1 
5785  O OE2 . GLU A 776  ? 0.5804 0.6895 0.4765 0.1074  -0.0444 -0.1461 774  GLU A OE2 
5786  N N   . THR A 777  ? 0.2986 0.3583 0.1986 0.0897  -0.0381 -0.1206 775  THR A N   
5787  C CA  . THR A 777  ? 0.2945 0.3473 0.1944 0.0872  -0.0350 -0.1146 775  THR A CA  
5788  C C   . THR A 777  ? 0.2939 0.3423 0.1912 0.0838  -0.0351 -0.1095 775  THR A C   
5789  O O   . THR A 777  ? 0.3410 0.3829 0.2414 0.0820  -0.0391 -0.1121 775  THR A O   
5790  C CB  . THR A 777  ? 0.2988 0.3403 0.2062 0.0864  -0.0371 -0.1181 775  THR A CB  
5791  O OG1 . THR A 777  ? 0.3163 0.3628 0.2254 0.0897  -0.0364 -0.1219 775  THR A OG1 
5792  C CG2 . THR A 777  ? 0.2825 0.3158 0.1902 0.0835  -0.0344 -0.1121 775  THR A CG2 
5793  N N   . ALA A 778  ? 0.2670 0.3193 0.1588 0.0830  -0.0308 -0.1021 776  ALA A N   
5794  C CA  . ALA A 778  ? 0.2716 0.3221 0.1601 0.0803  -0.0305 -0.0967 776  ALA A CA  
5795  C C   . ALA A 778  ? 0.3037 0.3442 0.1944 0.0771  -0.0290 -0.0918 776  ALA A C   
5796  O O   . ALA A 778  ? 0.2867 0.3238 0.1782 0.0736  -0.0288 -0.0858 776  ALA A O   
5797  C CB  . ALA A 778  ? 0.2803 0.3431 0.1619 0.0813  -0.0271 -0.0907 776  ALA A CB  
5798  N N   . GLY A 779  ? 0.2809 0.3163 0.1754 0.0771  -0.0276 -0.0922 777  GLY A N   
5799  C CA  . GLY A 779  ? 0.2717 0.2974 0.1714 0.0728  -0.0258 -0.0856 777  GLY A CA  
5800  C C   . GLY A 779  ? 0.2554 0.2770 0.1589 0.0739  -0.0249 -0.0882 777  GLY A C   
5801  O O   . GLY A 779  ? 0.2679 0.2961 0.1689 0.0781  -0.0244 -0.0930 777  GLY A O   
5802  N N   . VAL A 780  ? 0.2482 0.2593 0.1580 0.0702  -0.0250 -0.0850 778  VAL A N   
5803  C CA  . VAL A 780  ? 0.2579 0.2638 0.1723 0.0708  -0.0247 -0.0869 778  VAL A CA  
5804  C C   . VAL A 780  ? 0.2541 0.2550 0.1709 0.0670  -0.0211 -0.0784 778  VAL A C   
5805  O O   . VAL A 780  ? 0.2473 0.2428 0.1663 0.0630  -0.0214 -0.0736 778  VAL A O   
5806  C CB  . VAL A 780  ? 0.2591 0.2561 0.1803 0.0703  -0.0298 -0.0935 778  VAL A CB  
5807  C CG1 . VAL A 780  ? 0.2619 0.2532 0.1883 0.0707  -0.0295 -0.0946 778  VAL A CG1 
5808  C CG2 . VAL A 780  ? 0.2822 0.2840 0.2013 0.0743  -0.0337 -0.1027 778  VAL A CG2 
5809  N N   . MET A 781  ? 0.2422 0.2454 0.1587 0.0683  -0.0179 -0.0768 779  MET A N   
5810  C CA  . MET A 781  ? 0.2334 0.2316 0.1529 0.0652  -0.0149 -0.0700 779  MET A CA  
5811  C C   . MET A 781  ? 0.2353 0.2274 0.1603 0.0658  -0.0161 -0.0736 779  MET A C   
5812  O O   . MET A 781  ? 0.2457 0.2424 0.1697 0.0697  -0.0157 -0.0781 779  MET A O   
5813  C CB  . MET A 781  ? 0.2583 0.2646 0.1731 0.0660  -0.0100 -0.0643 779  MET A CB  
5814  C CG  . MET A 781  ? 0.2520 0.2650 0.1614 0.0657  -0.0090 -0.0606 779  MET A CG  
5815  S SD  . MET A 781  ? 0.2548 0.2790 0.1589 0.0671  -0.0039 -0.0543 779  MET A SD  
5816  C CE  . MET A 781  ? 0.2321 0.2489 0.1403 0.0622  -0.0012 -0.0453 779  MET A CE  
5817  N N   . PHE A 782  ? 0.2512 0.2336 0.1823 0.0621  -0.0177 -0.0716 780  PHE A N   
5818  C CA  . PHE A 782  ? 0.2533 0.2288 0.1905 0.0622  -0.0196 -0.0745 780  PHE A CA  
5819  C C   . PHE A 782  ? 0.2594 0.2294 0.2002 0.0585  -0.0173 -0.0676 780  PHE A C   
5820  O O   . PHE A 782  ? 0.2276 0.1942 0.1693 0.0546  -0.0169 -0.0625 780  PHE A O   
5821  C CB  . PHE A 782  ? 0.2605 0.2290 0.2029 0.0613  -0.0251 -0.0796 780  PHE A CB  
5822  C CG  . PHE A 782  ? 0.2632 0.2237 0.2130 0.0607  -0.0274 -0.0815 780  PHE A CG  
5823  C CD1 . PHE A 782  ? 0.2856 0.2473 0.2370 0.0650  -0.0289 -0.0882 780  PHE A CD1 
5824  C CD2 . PHE A 782  ? 0.2783 0.2307 0.2336 0.0561  -0.0281 -0.0766 780  PHE A CD2 
5825  C CE1 . PHE A 782  ? 0.3207 0.2749 0.2794 0.0646  -0.0313 -0.0899 780  PHE A CE1 
5826  C CE2 . PHE A 782  ? 0.2581 0.2035 0.2204 0.0555  -0.0304 -0.0779 780  PHE A CE2 
5827  C CZ  . PHE A 782  ? 0.2953 0.2412 0.2594 0.0597  -0.0321 -0.0845 780  PHE A CZ  
5828  N N   . THR A 783  ? 0.2416 0.2108 0.1846 0.0598  -0.0159 -0.0679 781  THR A N   
5829  C CA  . THR A 783  ? 0.2522 0.2155 0.1996 0.0564  -0.0145 -0.0626 781  THR A CA  
5830  C C   . THR A 783  ? 0.2792 0.2368 0.2327 0.0575  -0.0174 -0.0668 781  THR A C   
5831  O O   . THR A 783  ? 0.2689 0.2301 0.2220 0.0616  -0.0173 -0.0715 781  THR A O   
5832  C CB  . THR A 783  ? 0.2438 0.2121 0.1880 0.0564  -0.0095 -0.0571 781  THR A CB  
5833  O OG1 . THR A 783  ? 0.2635 0.2370 0.2025 0.0556  -0.0073 -0.0532 781  THR A OG1 
5834  C CG2 . THR A 783  ? 0.2869 0.2491 0.2355 0.0528  -0.0084 -0.0517 781  THR A CG2 
5835  N N   . GLY A 784  ? 0.2861 0.2354 0.2456 0.0540  -0.0200 -0.0651 782  GLY A N   
5836  C CA  . GLY A 784  ? 0.2835 0.2264 0.2497 0.0546  -0.0236 -0.0689 782  GLY A CA  
5837  C C   . GLY A 784  ? 0.2901 0.2249 0.2622 0.0501  -0.0269 -0.0665 782  GLY A C   
5838  O O   . GLY A 784  ? 0.3228 0.2569 0.2940 0.0463  -0.0253 -0.0607 782  GLY A O   
5839  N N   . SER A 785  ? 0.3230 0.2521 0.3014 0.0507  -0.0315 -0.0709 783  SER A N   
5840  C CA  . SER A 785  ? 0.3521 0.2735 0.3373 0.0463  -0.0348 -0.0680 783  SER A CA  
5841  C C   . SER A 785  ? 0.3357 0.2567 0.3200 0.0440  -0.0369 -0.0681 783  SER A C   
5842  O O   . SER A 785  ? 0.3399 0.2651 0.3202 0.0466  -0.0376 -0.0727 783  SER A O   
5843  C CB  . SER A 785  ? 0.3283 0.2434 0.3214 0.0475  -0.0396 -0.0725 783  SER A CB  
5844  O OG  . SER A 785  ? 0.4076 0.3225 0.4017 0.0504  -0.0437 -0.0802 783  SER A OG  
5845  N N   . THR A 786  ? 0.3622 0.2788 0.3506 0.0391  -0.0380 -0.0629 784  THR A N   
5846  C CA  A THR A 786  ? 0.3370 0.2530 0.3257 0.0366  -0.0403 -0.0625 784  THR A CA  
5847  C CA  B THR A 786  ? 0.3375 0.2537 0.3262 0.0367  -0.0402 -0.0626 784  THR A CA  
5848  C C   . THR A 786  ? 0.3641 0.2768 0.3572 0.0382  -0.0459 -0.0695 784  THR A C   
5849  O O   . THR A 786  ? 0.3385 0.2535 0.3294 0.0385  -0.0475 -0.0722 784  THR A O   
5850  C CB  A THR A 786  ? 0.3737 0.2860 0.3669 0.0311  -0.0406 -0.0557 784  THR A CB  
5851  C CB  B THR A 786  ? 0.3726 0.2853 0.3651 0.0312  -0.0402 -0.0556 784  THR A CB  
5852  O OG1 A THR A 786  ? 0.4403 0.3461 0.4418 0.0297  -0.0442 -0.0557 784  THR A OG1 
5853  O OG1 B THR A 786  ? 0.3688 0.2815 0.3621 0.0288  -0.0425 -0.0554 784  THR A OG1 
5854  C CG2 A THR A 786  ? 0.3002 0.2156 0.2895 0.0296  -0.0354 -0.0494 784  THR A CG2 
5855  C CG2 B THR A 786  ? 0.4279 0.3341 0.4288 0.0294  -0.0432 -0.0544 784  THR A CG2 
5856  N N   . GLU A 787  ? 0.3691 0.2765 0.3688 0.0392  -0.0492 -0.0725 785  GLU A N   
5857  C CA  . GLU A 787  ? 0.3986 0.3021 0.4037 0.0407  -0.0552 -0.0793 785  GLU A CA  
5858  C C   . GLU A 787  ? 0.2812 0.1904 0.2805 0.0459  -0.0552 -0.0871 785  GLU A C   
5859  O O   . GLU A 787  ? 0.3499 0.2592 0.3497 0.0464  -0.0587 -0.0917 785  GLU A O   
5860  C CB  . GLU A 787  ? 0.4546 0.3514 0.4683 0.0411  -0.0585 -0.0808 785  GLU A CB  
5861  N N   . VAL A 788  ? 0.3679 0.2825 0.3617 0.0498  -0.0513 -0.0885 786  VAL A N   
5862  C CA  . VAL A 788  ? 0.3269 0.2483 0.3148 0.0549  -0.0510 -0.0957 786  VAL A CA  
5863  C C   . VAL A 788  ? 0.2899 0.2177 0.2702 0.0542  -0.0486 -0.0936 786  VAL A C   
5864  O O   . VAL A 788  ? 0.3114 0.2427 0.2891 0.0566  -0.0507 -0.0993 786  VAL A O   
5865  C CB  . VAL A 788  ? 0.3462 0.2724 0.3308 0.0592  -0.0475 -0.0973 786  VAL A CB  
5866  C CG1 . VAL A 788  ? 0.3273 0.2628 0.3048 0.0640  -0.0462 -0.1032 786  VAL A CG1 
5867  C CG2 . VAL A 788  ? 0.4201 0.3415 0.4131 0.0600  -0.0504 -0.0995 786  VAL A CG2 
5868  N N   . ALA A 789  ? 0.3146 0.2441 0.2917 0.0509  -0.0442 -0.0856 787  ALA A N   
5869  C CA  . ALA A 789  ? 0.2905 0.2252 0.2615 0.0498  -0.0423 -0.0832 787  ALA A CA  
5870  C C   . ALA A 789  ? 0.2907 0.2221 0.2651 0.0477  -0.0470 -0.0853 787  ALA A C   
5871  O O   . ALA A 789  ? 0.2540 0.1903 0.2238 0.0490  -0.0476 -0.0879 787  ALA A O   
5872  C CB  . ALA A 789  ? 0.2682 0.2036 0.2369 0.0462  -0.0378 -0.0743 787  ALA A CB  
5873  N N   . ARG A 790  ? 0.2949 0.2185 0.2775 0.0443  -0.0506 -0.0840 788  ARG A N   
5874  C CA  . ARG A 790  ? 0.2925 0.2128 0.2794 0.0418  -0.0553 -0.0857 788  ARG A CA  
5875  C C   . ARG A 790  ? 0.2784 0.1992 0.2661 0.0458  -0.0599 -0.0952 788  ARG A C   
5876  O O   . ARG A 790  ? 0.2939 0.2167 0.2804 0.0456  -0.0623 -0.0978 788  ARG A O   
5877  C CB  . ARG A 790  ? 0.3611 0.2733 0.3572 0.0373  -0.0580 -0.0816 788  ARG A CB  
5878  C CG  . ARG A 790  ? 0.3671 0.2762 0.3682 0.0333  -0.0621 -0.0805 788  ARG A CG  
5879  C CD  . ARG A 790  ? 0.3999 0.3025 0.4095 0.0282  -0.0638 -0.0745 788  ARG A CD  
5880  N NE  . ARG A 790  ? 0.3952 0.3000 0.4022 0.0248  -0.0591 -0.0661 788  ARG A NE  
5881  C CZ  . ARG A 790  ? 0.4272 0.3303 0.4357 0.0235  -0.0566 -0.0613 788  ARG A CZ  
5882  N NH1 . ARG A 790  ? 0.4519 0.3511 0.4642 0.0253  -0.0580 -0.0634 788  ARG A NH1 
5883  N NH2 . ARG A 790  ? 0.4118 0.3175 0.4182 0.0203  -0.0528 -0.0542 788  ARG A NH2 
5884  N N   . LEU A 791  ? 0.2890 0.2087 0.2788 0.0496  -0.0612 -0.1007 789  LEU A N   
5885  C CA  . LEU A 791  ? 0.3160 0.2392 0.3066 0.0532  -0.0643 -0.1083 789  LEU A CA  
5886  C C   . LEU A 791  ? 0.2876 0.2206 0.2683 0.0569  -0.0617 -0.1114 789  LEU A C   
5887  O O   . LEU A 791  ? 0.3077 0.2444 0.2880 0.0581  -0.0643 -0.1157 789  LEU A O   
5888  C CB  . LEU A 791  ? 0.3318 0.2545 0.3271 0.0557  -0.0649 -0.1108 789  LEU A CB  
5889  C CG  . LEU A 791  ? 0.3592 0.2733 0.3656 0.0527  -0.0688 -0.1091 789  LEU A CG  
5890  C CD1 . LEU A 791  ? 0.3536 0.2682 0.3628 0.0556  -0.0681 -0.1109 789  LEU A CD1 
5891  C CD2 . LEU A 791  ? 0.3895 0.3014 0.4026 0.0515  -0.0745 -0.1125 789  LEU A CD2 
5892  N N   . ILE A 792  ? 0.2897 0.2272 0.2625 0.0586  -0.0565 -0.1087 790  ILE A N   
5893  C CA  . ILE A 792  ? 0.3242 0.2719 0.2876 0.0615  -0.0535 -0.1099 790  ILE A CA  
5894  C C   . ILE A 792  ? 0.2914 0.2403 0.2528 0.0584  -0.0543 -0.1070 790  ILE A C   
5895  O O   . ILE A 792  ? 0.2779 0.2324 0.2352 0.0608  -0.0559 -0.1117 790  ILE A O   
5896  C CB  . ILE A 792  ? 0.2848 0.2382 0.2422 0.0625  -0.0471 -0.1045 790  ILE A CB  
5897  C CG1 . ILE A 792  ? 0.2900 0.2448 0.2482 0.0668  -0.0467 -0.1094 790  ILE A CG1 
5898  C CG2 . ILE A 792  ? 0.2938 0.2572 0.2421 0.0640  -0.0438 -0.1030 790  ILE A CG2 
5899  C CD1 . ILE A 792  ? 0.3298 0.2877 0.2850 0.0668  -0.0410 -0.1034 790  ILE A CD1 
5900  N N   . GLN A 793  ? 0.2465 0.1906 0.2109 0.0533  -0.0533 -0.0995 791  GLN A N   
5901  C CA  . GLN A 793  ? 0.2720 0.2171 0.2353 0.0503  -0.0540 -0.0965 791  GLN A CA  
5902  C C   . GLN A 793  ? 0.2769 0.2198 0.2441 0.0506  -0.0602 -0.1032 791  GLN A C   
5903  O O   . GLN A 793  ? 0.2934 0.2410 0.2569 0.0509  -0.0611 -0.1046 791  GLN A O   
5904  C CB  . GLN A 793  ? 0.2885 0.2284 0.2559 0.0449  -0.0525 -0.0882 791  GLN A CB  
5905  C CG  . GLN A 793  ? 0.3202 0.2603 0.2880 0.0413  -0.0536 -0.0849 791  GLN A CG  
5906  C CD  . GLN A 793  ? 0.4051 0.3398 0.3783 0.0361  -0.0529 -0.0778 791  GLN A CD  
5907  O OE1 . GLN A 793  ? 0.4504 0.3876 0.4209 0.0338  -0.0496 -0.0718 791  GLN A OE1 
5908  N NE2 . GLN A 793  ? 0.4013 0.3291 0.3825 0.0342  -0.0561 -0.0784 791  GLN A NE2 
5909  N N   . ALA A 794  ? 0.2963 0.2321 0.2715 0.0504  -0.0647 -0.1075 792  ALA A N   
5910  C CA  . ALA A 794  ? 0.3282 0.2621 0.3085 0.0504  -0.0706 -0.1133 792  ALA A CA  
5911  C C   . ALA A 794  ? 0.3009 0.2438 0.2765 0.0552  -0.0706 -0.1193 792  ALA A C   
5912  O O   . ALA A 794  ? 0.3391 0.2850 0.3142 0.0553  -0.0733 -0.1221 792  ALA A O   
5913  C CB  . ALA A 794  ? 0.3129 0.2390 0.3042 0.0485  -0.0743 -0.1136 792  ALA A CB  
5914  N N   . GLN A 795  ? 0.3118 0.2593 0.2842 0.0591  -0.0678 -0.1213 793  GLN A N   
5915  C CA  . GLN A 795  ? 0.3203 0.2778 0.2874 0.0638  -0.0671 -0.1263 793  GLN A CA  
5916  C C   . GLN A 795  ? 0.3236 0.2883 0.2819 0.0641  -0.0651 -0.1249 793  GLN A C   
5917  O O   . GLN A 795  ? 0.3058 0.2759 0.2626 0.0656  -0.0673 -0.1287 793  GLN A O   
5918  C CB  . GLN A 795  ? 0.3737 0.3360 0.3376 0.0674  -0.0632 -0.1269 793  GLN A CB  
5919  C CG  . GLN A 795  ? 0.3425 0.3004 0.3143 0.0685  -0.0653 -0.1298 793  GLN A CG  
5920  C CD  . GLN A 795  ? 0.3580 0.3230 0.3258 0.0727  -0.0616 -0.1313 793  GLN A CD  
5921  O OE1 . GLN A 795  ? 0.4118 0.3758 0.3775 0.0724  -0.0578 -0.1272 793  GLN A OE1 
5922  N NE2 . GLN A 795  ? 0.3631 0.3357 0.3298 0.0767  -0.0628 -0.1371 793  GLN A NE2 
5923  N N   . LEU A 796  ? 0.3164 0.2816 0.2688 0.0629  -0.0610 -0.1193 794  LEU A N   
5924  C CA  . LEU A 796  ? 0.3184 0.2913 0.2620 0.0636  -0.0587 -0.1174 794  LEU A CA  
5925  C C   . LEU A 796  ? 0.3244 0.2950 0.2696 0.0607  -0.0623 -0.1172 794  LEU A C   
5926  O O   . LEU A 796  ? 0.3554 0.3334 0.2950 0.0619  -0.0621 -0.1177 794  LEU A O   
5927  C CB  . LEU A 796  ? 0.2769 0.2516 0.2162 0.0621  -0.0528 -0.1089 794  LEU A CB  
5928  C CG  . LEU A 796  ? 0.2629 0.2419 0.1984 0.0655  -0.0487 -0.1088 794  LEU A CG  
5929  C CD1 . LEU A 796  ? 0.2947 0.2747 0.2275 0.0630  -0.0430 -0.0992 794  LEU A CD1 
5930  C CD2 . LEU A 796  ? 0.2584 0.2487 0.1874 0.0704  -0.0483 -0.1139 794  LEU A CD2 
5931  N N   . ALA A 797  ? 0.3015 0.2629 0.2550 0.0564  -0.0652 -0.1153 795  ALA A N   
5932  C CA  . ALA A 797  ? 0.3374 0.2973 0.2934 0.0532  -0.0684 -0.1143 795  ALA A CA  
5933  C C   . ALA A 797  ? 0.3555 0.3186 0.3130 0.0553  -0.0729 -0.1216 795  ALA A C   
5934  O O   . ALA A 797  ? 0.3577 0.3223 0.3149 0.0538  -0.0753 -0.1218 795  ALA A O   
5935  C CB  . ALA A 797  ? 0.3372 0.2874 0.3024 0.0479  -0.0702 -0.1099 795  ALA A CB  
5936  N N   . ASP A 798  ? 0.3531 0.3182 0.3127 0.0586  -0.0736 -0.1264 796  ASP A N   
5937  C CA  . ASP A 798  ? 0.3464 0.3166 0.3070 0.0611  -0.0769 -0.1324 796  ASP A CA  
5938  C C   . ASP A 798  ? 0.3856 0.3671 0.3365 0.0641  -0.0744 -0.1330 796  ASP A C   
5939  O O   . ASP A 798  ? 0.3705 0.3567 0.3215 0.0654  -0.0772 -0.1370 796  ASP A O   
5940  C CB  . ASP A 798  ? 0.3465 0.3166 0.3120 0.0642  -0.0783 -0.1376 796  ASP A CB  
5941  C CG  . ASP A 798  ? 0.4822 0.4418 0.4589 0.0614  -0.0827 -0.1383 796  ASP A CG  
5942  O OD1 . ASP A 798  ? 0.4586 0.4122 0.4401 0.0571  -0.0853 -0.1357 796  ASP A OD1 
5943  O OD2 . ASP A 798  ? 0.4567 0.4147 0.4380 0.0634  -0.0835 -0.1412 796  ASP A OD2 
5944  N N   . ARG A 799  ? 0.3547 0.3412 0.2977 0.0652  -0.0693 -0.1287 797  ARG A N   
5945  C CA  . ARG A 799  ? 0.3565 0.3548 0.2906 0.0685  -0.0665 -0.1288 797  ARG A CA  
5946  C C   . ARG A 799  ? 0.3478 0.3490 0.2752 0.0668  -0.0642 -0.1230 797  ARG A C   
5947  O O   . ARG A 799  ? 0.3555 0.3502 0.2838 0.0636  -0.0635 -0.1185 797  ARG A O   
5948  C CB  . ARG A 799  ? 0.4380 0.4420 0.3682 0.0721  -0.0623 -0.1288 797  ARG A CB  
5949  C CG  . ARG A 799  ? 0.4070 0.4093 0.3433 0.0744  -0.0644 -0.1347 797  ARG A CG  
5950  C CD  . ARG A 799  ? 0.4171 0.4296 0.3486 0.0789  -0.0610 -0.1363 797  ARG A CD  
5951  N NE  . ARG A 799  ? 0.4515 0.4637 0.3800 0.0789  -0.0562 -0.1315 797  ARG A NE  
5952  C CZ  . ARG A 799  ? 0.4308 0.4497 0.3514 0.0793  -0.0516 -0.1261 797  ARG A CZ  
5953  N NH1 . ARG A 799  ? 0.4339 0.4607 0.3485 0.0798  -0.0510 -0.1246 797  ARG A NH1 
5954  N NH2 . ARG A 799  ? 0.3606 0.3785 0.2795 0.0792  -0.0475 -0.1220 797  ARG A NH2 
5955  N N   . LEU A 800  ? 0.3407 0.3522 0.2617 0.0690  -0.0632 -0.1232 798  LEU A N   
5956  C CA  . LEU A 800  ? 0.3519 0.3686 0.2656 0.0683  -0.0605 -0.1174 798  LEU A CA  
5957  C C   . LEU A 800  ? 0.3286 0.3572 0.2347 0.0720  -0.0565 -0.1160 798  LEU A C   
5958  O O   . LEU A 800  ? 0.3836 0.4178 0.2900 0.0752  -0.0569 -0.1207 798  LEU A O   
5959  C CB  . LEU A 800  ? 0.3916 0.4094 0.3056 0.0666  -0.0640 -0.1178 798  LEU A CB  
5960  C CG  . LEU A 800  ? 0.3915 0.3989 0.3129 0.0624  -0.0681 -0.1181 798  LEU A CG  
5961  C CD1 . LEU A 800  ? 0.3557 0.3661 0.2776 0.0614  -0.0717 -0.1195 798  LEU A CD1 
5962  C CD2 . LEU A 800  ? 0.3664 0.3680 0.2892 0.0586  -0.0648 -0.1099 798  LEU A CD2 
5963  N N   . SER A 801  ? 0.3672 0.4000 0.2669 0.0716  -0.0528 -0.1093 799  SER A N   
5964  C CA  . SER A 801  ? 0.4280 0.4728 0.3207 0.0745  -0.0491 -0.1066 799  SER A CA  
5965  C C   . SER A 801  ? 0.4419 0.4948 0.3325 0.0759  -0.0515 -0.1093 799  SER A C   
5966  O O   . SER A 801  ? 0.4338 0.4828 0.3279 0.0743  -0.0557 -0.1122 799  SER A O   
5967  C CB  . SER A 801  ? 0.4250 0.4715 0.3123 0.0732  -0.0451 -0.0981 799  SER A CB  
5968  O OG  . SER A 801  ? 0.4243 0.4703 0.3109 0.0709  -0.0468 -0.0948 799  SER A OG  
5969  N N   . PRO A 802  ? 0.4190 0.4838 0.3043 0.0788  -0.0491 -0.1082 800  PRO A N   
5970  C CA  . PRO A 802  ? 0.4370 0.5101 0.3199 0.0800  -0.0511 -0.1099 800  PRO A CA  
5971  C C   . PRO A 802  ? 0.4615 0.5333 0.3427 0.0773  -0.0524 -0.1054 800  PRO A C   
5972  O O   . PRO A 802  ? 0.5108 0.5852 0.3926 0.0773  -0.0557 -0.1083 800  PRO A O   
5973  C CB  . PRO A 802  ? 0.4618 0.5479 0.3389 0.0830  -0.0472 -0.1072 800  PRO A CB  
5974  C CG  . PRO A 802  ? 0.5385 0.6227 0.4142 0.0825  -0.0428 -0.1018 800  PRO A CG  
5975  C CD  . PRO A 802  ? 0.4299 0.5015 0.3118 0.0811  -0.0445 -0.1056 800  PRO A CD  
5976  N N   . ALA A 803  ? 0.4596 0.5277 0.3391 0.0751  -0.0499 -0.0985 801  ALA A N   
5977  C CA  . ALA A 803  ? 0.4985 0.5648 0.3770 0.0726  -0.0512 -0.0941 801  ALA A CA  
5978  C C   . ALA A 803  ? 0.5024 0.5575 0.3873 0.0696  -0.0554 -0.0974 801  ALA A C   
5979  O O   . ALA A 803  ? 0.4682 0.5214 0.3535 0.0673  -0.0569 -0.0941 801  ALA A O   
5980  C CB  . ALA A 803  ? 0.4545 0.5215 0.3291 0.0715  -0.0471 -0.0852 801  ALA A CB  
5981  N N   . GLY A 804  ? 0.4616 0.5094 0.3521 0.0694  -0.0572 -0.1031 802  GLY A N   
5982  C CA  . GLY A 804  ? 0.4081 0.4454 0.3056 0.0663  -0.0613 -0.1059 802  GLY A CA  
5983  C C   . GLY A 804  ? 0.4295 0.4577 0.3318 0.0623  -0.0588 -0.0992 802  GLY A C   
5984  O O   . GLY A 804  ? 0.3847 0.4066 0.2924 0.0586  -0.0608 -0.0971 802  GLY A O   
5985  N N   . ARG A 805  ? 0.4135 0.4409 0.3145 0.0626  -0.0543 -0.0951 803  ARG A N   
5986  C CA  . ARG A 805  ? 0.3713 0.3909 0.2769 0.0589  -0.0513 -0.0881 803  ARG A CA  
5987  C C   . ARG A 805  ? 0.2937 0.3076 0.2026 0.0593  -0.0503 -0.0905 803  ARG A C   
5988  O O   . ARG A 805  ? 0.3304 0.3480 0.2365 0.0630  -0.0507 -0.0963 803  ARG A O   
5989  C CB  . ARG A 805  ? 0.4108 0.4353 0.3119 0.0586  -0.0464 -0.0795 803  ARG A CB  
5990  C CG  . ARG A 805  ? 0.4056 0.4360 0.3035 0.0583  -0.0474 -0.0765 803  ARG A CG  
5991  C CD  . ARG A 805  ? 0.3935 0.4172 0.2977 0.0544  -0.0501 -0.0753 803  ARG A CD  
5992  N NE  . ARG A 805  ? 0.3995 0.4287 0.3013 0.0542  -0.0511 -0.0724 803  ARG A NE  
5993  C CZ  . ARG A 805  ? 0.4107 0.4433 0.3119 0.0550  -0.0553 -0.0772 803  ARG A CZ  
5994  N NH1 . ARG A 805  ? 0.4196 0.4507 0.3224 0.0562  -0.0592 -0.0855 803  ARG A NH1 
5995  N NH2 . ARG A 805  ? 0.4723 0.5099 0.3713 0.0547  -0.0559 -0.0737 803  ARG A NH2 
5996  N N   . PRO A 806  ? 0.3108 0.3159 0.2257 0.0557  -0.0492 -0.0864 804  PRO A N   
5997  C CA  . PRO A 806  ? 0.3160 0.3153 0.2345 0.0559  -0.0485 -0.0885 804  PRO A CA  
5998  C C   . PRO A 806  ? 0.3141 0.3188 0.2273 0.0589  -0.0441 -0.0869 804  PRO A C   
5999  O O   . PRO A 806  ? 0.2835 0.2936 0.1920 0.0591  -0.0403 -0.0809 804  PRO A O   
6000  C CB  . PRO A 806  ? 0.3124 0.3031 0.2372 0.0511  -0.0474 -0.0825 804  PRO A CB  
6001  C CG  . PRO A 806  ? 0.3579 0.3484 0.2844 0.0485  -0.0497 -0.0807 804  PRO A CG  
6002  C CD  . PRO A 806  ? 0.3335 0.3335 0.2527 0.0512  -0.0492 -0.0807 804  PRO A CD  
6003  N N   . ILE A 807  ? 0.2980 0.3012 0.2126 0.0612  -0.0447 -0.0922 805  ILE A N   
6004  C CA  . ILE A 807  ? 0.2803 0.2877 0.1913 0.0639  -0.0407 -0.0912 805  ILE A CA  
6005  C C   . ILE A 807  ? 0.2787 0.2798 0.1930 0.0607  -0.0371 -0.0840 805  ILE A C   
6006  O O   . ILE A 807  ? 0.2948 0.2870 0.2158 0.0582  -0.0387 -0.0845 805  ILE A O   
6007  C CB  . ILE A 807  ? 0.2767 0.2841 0.1890 0.0676  -0.0430 -0.1000 805  ILE A CB  
6008  C CG1 . ILE A 807  ? 0.3303 0.3437 0.2397 0.0709  -0.0471 -0.1081 805  ILE A CG1 
6009  C CG2 . ILE A 807  ? 0.3230 0.3355 0.2316 0.0704  -0.0387 -0.0987 805  ILE A CG2 
6010  C CD1 . ILE A 807  ? 0.3304 0.3565 0.2319 0.0735  -0.0445 -0.1062 805  ILE A CD1 
6011  N N   . PRO A 808  ? 0.2638 0.2695 0.1742 0.0605  -0.0325 -0.0772 806  PRO A N   
6012  C CA  . PRO A 808  ? 0.2678 0.2674 0.1816 0.0573  -0.0293 -0.0706 806  PRO A CA  
6013  C C   . PRO A 808  ? 0.2737 0.2692 0.1908 0.0582  -0.0286 -0.0729 806  PRO A C   
6014  O O   . PRO A 808  ? 0.2719 0.2723 0.1863 0.0620  -0.0282 -0.0772 806  PRO A O   
6015  C CB  . PRO A 808  ? 0.3114 0.3181 0.2199 0.0578  -0.0249 -0.0638 806  PRO A CB  
6016  C CG  . PRO A 808  ? 0.3085 0.3232 0.2118 0.0597  -0.0264 -0.0653 806  PRO A CG  
6017  C CD  . PRO A 808  ? 0.3028 0.3189 0.2059 0.0627  -0.0303 -0.0746 806  PRO A CD  
6018  N N   . LEU A 809  ? 0.2927 0.2796 0.2157 0.0547  -0.0286 -0.0700 807  LEU A N   
6019  C CA  . LEU A 809  ? 0.2733 0.2552 0.2002 0.0548  -0.0280 -0.0710 807  LEU A CA  
6020  C C   . LEU A 809  ? 0.2639 0.2429 0.1922 0.0517  -0.0241 -0.0632 807  LEU A C   
6021  O O   . LEU A 809  ? 0.2630 0.2376 0.1942 0.0480  -0.0244 -0.0591 807  LEU A O   
6022  C CB  . LEU A 809  ? 0.2498 0.2234 0.1837 0.0533  -0.0325 -0.0755 807  LEU A CB  
6023  C CG  . LEU A 809  ? 0.2716 0.2389 0.2107 0.0527  -0.0322 -0.0755 807  LEU A CG  
6024  C CD1 . LEU A 809  ? 0.2844 0.2562 0.2211 0.0572  -0.0310 -0.0798 807  LEU A CD1 
6025  C CD2 . LEU A 809  ? 0.3426 0.3015 0.2893 0.0505  -0.0370 -0.0786 807  LEU A CD2 
6026  N N   . ILE A 810  ? 0.2292 0.2111 0.1556 0.0533  -0.0206 -0.0613 808  ILE A N   
6027  C CA  . ILE A 810  ? 0.2201 0.1985 0.1488 0.0507  -0.0174 -0.0550 808  ILE A CA  
6028  C C   . ILE A 810  ? 0.2388 0.2117 0.1723 0.0509  -0.0183 -0.0578 808  ILE A C   
6029  O O   . ILE A 810  ? 0.2655 0.2416 0.1976 0.0543  -0.0178 -0.0615 808  ILE A O   
6030  C CB  . ILE A 810  ? 0.2259 0.2112 0.1498 0.0520  -0.0130 -0.0504 808  ILE A CB  
6031  C CG1 . ILE A 810  ? 0.2790 0.2701 0.1983 0.0521  -0.0124 -0.0477 808  ILE A CG1 
6032  C CG2 . ILE A 810  ? 0.2430 0.2242 0.1698 0.0492  -0.0101 -0.0443 808  ILE A CG2 
6033  C CD1 . ILE A 810  ? 0.3190 0.3166 0.2345 0.0528  -0.0083 -0.0420 808  ILE A CD1 
6034  N N   . ALA A 811  ? 0.2353 0.2003 0.1744 0.0474  -0.0197 -0.0559 809  ALA A N   
6035  C CA  . ALA A 811  ? 0.2402 0.1994 0.1848 0.0471  -0.0211 -0.0579 809  ALA A CA  
6036  C C   . ALA A 811  ? 0.2624 0.2175 0.2099 0.0437  -0.0186 -0.0516 809  ALA A C   
6037  O O   . ALA A 811  ? 0.2739 0.2260 0.2236 0.0401  -0.0190 -0.0479 809  ALA A O   
6038  C CB  . ALA A 811  ? 0.3101 0.2635 0.2599 0.0461  -0.0262 -0.0625 809  ALA A CB  
6039  N N   . GLU A 812  ? 0.2411 0.1969 0.1887 0.0450  -0.0162 -0.0506 810  GLU A N   
6040  C CA  . GLU A 812  ? 0.2423 0.1946 0.1929 0.0421  -0.0140 -0.0453 810  GLU A CA  
6041  C C   . GLU A 812  ? 0.2693 0.2157 0.2257 0.0420  -0.0164 -0.0478 810  GLU A C   
6042  O O   . GLU A 812  ? 0.2648 0.2124 0.2213 0.0453  -0.0171 -0.0523 810  GLU A O   
6043  C CB  . GLU A 812  ? 0.2879 0.2452 0.2348 0.0434  -0.0096 -0.0419 810  GLU A CB  
6044  N N   A THR A 813  ? 0.2513 0.1918 0.2128 0.0382  -0.0178 -0.0449 811  THR A N   
6045  N N   B THR A 813  ? 0.2514 0.1921 0.2128 0.0382  -0.0179 -0.0450 811  THR A N   
6046  C CA  A THR A 813  ? 0.2752 0.2097 0.2431 0.0377  -0.0215 -0.0476 811  THR A CA  
6047  C CA  B THR A 813  ? 0.2753 0.2101 0.2428 0.0376  -0.0206 -0.0466 811  THR A CA  
6048  C C   A THR A 813  ? 0.2823 0.2124 0.2549 0.0343  -0.0209 -0.0426 811  THR A C   
6049  C C   B THR A 813  ? 0.2703 0.2027 0.2405 0.0348  -0.0185 -0.0410 811  THR A C   
6050  O O   A THR A 813  ? 0.2885 0.2132 0.2669 0.0320  -0.0242 -0.0425 811  THR A O   
6051  O O   B THR A 813  ? 0.2659 0.2016 0.2327 0.0343  -0.0146 -0.0370 811  THR A O   
6052  C CB  A THR A 813  ? 0.2814 0.2128 0.2521 0.0366  -0.0260 -0.0507 811  THR A CB  
6053  C CB  B THR A 813  ? 0.2708 0.2011 0.2427 0.0357  -0.0253 -0.0489 811  THR A CB  
6054  O OG1 A THR A 813  ? 0.2679 0.1995 0.2380 0.0331  -0.0255 -0.0465 811  THR A OG1 
6055  O OG1 B THR A 813  ? 0.2833 0.2143 0.2542 0.0325  -0.0247 -0.0449 811  THR A OG1 
6056  C CG2 A THR A 813  ? 0.2610 0.1964 0.2280 0.0406  -0.0274 -0.0571 811  THR A CG2 
6057  C CG2 B THR A 813  ? 0.2875 0.2197 0.2579 0.0393  -0.0280 -0.0559 811  THR A CG2 
6058  N N   A GLY A 814  ? 0.2727 0.2050 0.2432 0.0338  -0.0169 -0.0383 812  GLY A N   
6059  N N   B GLY A 814  ? 0.2872 0.2139 0.2636 0.0328  -0.0211 -0.0405 812  GLY A N   
6060  C CA  A GLY A 814  ? 0.2632 0.1919 0.2381 0.0314  -0.0166 -0.0346 812  GLY A CA  
6061  C CA  B GLY A 814  ? 0.2683 0.1931 0.2473 0.0306  -0.0194 -0.0358 812  GLY A CA  
6062  C C   A GLY A 814  ? 0.2535 0.1803 0.2305 0.0269  -0.0165 -0.0295 812  GLY A C   
6063  C C   B GLY A 814  ? 0.2704 0.1949 0.2501 0.0263  -0.0183 -0.0301 812  GLY A C   
6064  O O   A GLY A 814  ? 0.2293 0.1582 0.2038 0.0255  -0.0158 -0.0280 812  GLY A O   
6065  O O   B GLY A 814  ? 0.2597 0.1853 0.2381 0.0248  -0.0188 -0.0295 812  GLY A O   
6066  N N   A GLY A 815  ? 0.2514 0.1748 0.2333 0.0246  -0.0173 -0.0267 813  GLY A N   
6067  N N   B GLY A 815  ? 0.2492 0.1725 0.2312 0.0243  -0.0169 -0.0261 813  GLY A N   
6068  C CA  A GLY A 815  ? 0.2526 0.1752 0.2366 0.0203  -0.0171 -0.0218 813  GLY A CA  
6069  C CA  B GLY A 815  ? 0.2444 0.1680 0.2272 0.0204  -0.0158 -0.0209 813  GLY A CA  
6070  C C   A GLY A 815  ? 0.2535 0.1727 0.2430 0.0181  -0.0184 -0.0190 813  GLY A C   
6071  C C   B GLY A 815  ? 0.2365 0.1572 0.2245 0.0181  -0.0166 -0.0177 813  GLY A C   
6072  O O   A GLY A 815  ? 0.2736 0.1902 0.2659 0.0198  -0.0197 -0.0210 813  GLY A O   
6073  O O   B GLY A 815  ? 0.2347 0.1545 0.2238 0.0197  -0.0160 -0.0181 813  GLY A O   
6074  N N   . GLN A 816  ? 0.2617 0.1813 0.2529 0.0143  -0.0181 -0.0144 814  GLN A N   
6075  C CA  . GLN A 816  ? 0.2247 0.1424 0.2206 0.0116  -0.0188 -0.0106 814  GLN A CA  
6076  C C   . GLN A 816  ? 0.1929 0.1145 0.1862 0.0099  -0.0151 -0.0063 814  GLN A C   
6077  O O   . GLN A 816  ? 0.2456 0.1690 0.2399 0.0067  -0.0150 -0.0030 814  GLN A O   
6078  C CB  . GLN A 816  ? 0.2537 0.1688 0.2551 0.0083  -0.0226 -0.0090 814  GLN A CB  
6079  C CG  . GLN A 816  ? 0.2848 0.1976 0.2920 0.0059  -0.0244 -0.0054 814  GLN A CG  
6080  C CD  . GLN A 816  ? 0.3624 0.2707 0.3732 0.0084  -0.0267 -0.0084 814  GLN A CD  
6081  O OE1 . GLN A 816  ? 0.3876 0.2964 0.3963 0.0111  -0.0246 -0.0095 814  GLN A OE1 
6082  N NE2 . GLN A 816  ? 0.3764 0.2802 0.3931 0.0077  -0.0313 -0.0096 814  GLN A NE2 
6083  N N   . ASN A 817  ? 0.1827 0.1061 0.1726 0.0122  -0.0121 -0.0068 815  ASN A N   
6084  C CA  . ASN A 817  ? 0.1698 0.0971 0.1562 0.0115  -0.0086 -0.0041 815  ASN A CA  
6085  C C   . ASN A 817  ? 0.1763 0.1043 0.1652 0.0088  -0.0079 0.0000  815  ASN A C   
6086  O O   . ASN A 817  ? 0.1960 0.1222 0.1879 0.0089  -0.0086 0.0008  815  ASN A O   
6087  C CB  . ASN A 817  ? 0.1956 0.1249 0.1780 0.0148  -0.0058 -0.0058 815  ASN A CB  
6088  C CG  . ASN A 817  ? 0.1884 0.1176 0.1683 0.0178  -0.0066 -0.0101 815  ASN A CG  
6089  O OD1 . ASN A 817  ? 0.1847 0.1149 0.1627 0.0176  -0.0072 -0.0111 815  ASN A OD1 
6090  N ND2 . ASN A 817  ? 0.1754 0.1039 0.1553 0.0208  -0.0067 -0.0128 815  ASN A ND2 
6091  N N   . ALA A 818  ? 0.1669 0.0981 0.1548 0.0065  -0.0065 0.0026  816  ALA A N   
6092  C CA  . ALA A 818  ? 0.1701 0.1033 0.1598 0.0037  -0.0058 0.0064  816  ALA A CA  
6093  C C   . ALA A 818  ? 0.1747 0.1111 0.1614 0.0043  -0.0025 0.0074  816  ALA A C   
6094  O O   . ALA A 818  ? 0.1878 0.1255 0.1710 0.0060  -0.0007 0.0059  816  ALA A O   
6095  C CB  . ALA A 818  ? 0.1885 0.1237 0.1801 0.0005  -0.0072 0.0085  816  ALA A CB  
6096  N N   . MET A 819  ? 0.1622 0.1001 0.1505 0.0028  -0.0018 0.0101  817  MET A N   
6097  C CA  . MET A 819  ? 0.1750 0.1163 0.1614 0.0025  0.0009  0.0113  817  MET A CA  
6098  C C   . MET A 819  ? 0.1642 0.1088 0.1527 -0.0006 0.0005  0.0142  817  MET A C   
6099  O O   . MET A 819  ? 0.1823 0.1262 0.1738 -0.0022 -0.0012 0.0163  817  MET A O   
6100  C CB  . MET A 819  ? 0.1851 0.1257 0.1712 0.0042  0.0023  0.0112  817  MET A CB  
6101  C CG  . MET A 819  ? 0.1851 0.1291 0.1701 0.0037  0.0047  0.0125  817  MET A CG  
6102  S SD  . MET A 819  ? 0.2085 0.1521 0.1940 0.0052  0.0062  0.0130  817  MET A SD  
6103  C CE  . MET A 819  ? 0.2286 0.1708 0.2114 0.0087  0.0074  0.0103  817  MET A CE  
6104  N N   . ILE A 820  ? 0.1484 0.0968 0.1353 -0.0015 0.0019  0.0144  818  ILE A N   
6105  C CA  . ILE A 820  ? 0.1677 0.1207 0.1560 -0.0042 0.0018  0.0169  818  ILE A CA  
6106  C C   . ILE A 820  ? 0.1432 0.0990 0.1305 -0.0039 0.0039  0.0172  818  ILE A C   
6107  O O   . ILE A 820  ? 0.1734 0.1289 0.1585 -0.0021 0.0056  0.0154  818  ILE A O   
6108  C CB  . ILE A 820  ? 0.1591 0.1153 0.1468 -0.0053 0.0017  0.0165  818  ILE A CB  
6109  C CG1 . ILE A 820  ? 0.1811 0.1346 0.1704 -0.0059 -0.0007 0.0163  818  ILE A CG1 
6110  C CG2 . ILE A 820  ? 0.1821 0.1445 0.1711 -0.0078 0.0020  0.0187  818  ILE A CG2 
6111  C CD1 . ILE A 820  ? 0.2036 0.1603 0.1928 -0.0071 -0.0012 0.0161  818  ILE A CD1 
6112  N N   . VAL A 821  ? 0.1569 0.1153 0.1460 -0.0057 0.0036  0.0196  819  VAL A N   
6113  C CA  . VAL A 821  ? 0.1650 0.1261 0.1536 -0.0056 0.0052  0.0199  819  VAL A CA  
6114  C C   . VAL A 821  ? 0.1688 0.1364 0.1582 -0.0080 0.0051  0.0216  819  VAL A C   
6115  O O   . VAL A 821  ? 0.1904 0.1597 0.1818 -0.0101 0.0035  0.0244  819  VAL A O   
6116  C CB  . VAL A 821  ? 0.1679 0.1265 0.1580 -0.0051 0.0048  0.0212  819  VAL A CB  
6117  C CG1 . VAL A 821  ? 0.2081 0.1699 0.1979 -0.0052 0.0062  0.0216  819  VAL A CG1 
6118  C CG2 . VAL A 821  ? 0.1808 0.1340 0.1702 -0.0025 0.0049  0.0193  819  VAL A CG2 
6119  N N   . ASP A 822  ? 0.1599 0.1313 0.1479 -0.0076 0.0066  0.0201  820  ASP A N   
6120  C CA  . ASP A 822  ? 0.1618 0.1404 0.1503 -0.0096 0.0066  0.0212  820  ASP A CA  
6121  C C   . ASP A 822  ? 0.1780 0.1595 0.1668 -0.0098 0.0073  0.0216  820  ASP A C   
6122  O O   . ASP A 822  ? 0.1905 0.1681 0.1794 -0.0085 0.0077  0.0213  820  ASP A O   
6123  C CB  . ASP A 822  ? 0.1967 0.1790 0.1842 -0.0094 0.0073  0.0189  820  ASP A CB  
6124  C CG  . ASP A 822  ? 0.1891 0.1711 0.1755 -0.0073 0.0088  0.0158  820  ASP A CG  
6125  O OD1 . ASP A 822  ? 0.1929 0.1729 0.1793 -0.0063 0.0095  0.0154  820  ASP A OD1 
6126  O OD2 . ASP A 822  ? 0.2114 0.1952 0.1974 -0.0066 0.0092  0.0137  820  ASP A OD2 
6127  N N   . SER A 823  ? 0.1895 0.1784 0.1785 -0.0113 0.0073  0.0222  821  SER A N   
6128  C CA  . SER A 823  ? 0.2027 0.1951 0.1920 -0.0117 0.0077  0.0228  821  SER A CA  
6129  C C   . SER A 823  ? 0.2055 0.1975 0.1940 -0.0098 0.0090  0.0193  821  SER A C   
6130  O O   . SER A 823  ? 0.2552 0.2499 0.2442 -0.0100 0.0092  0.0193  821  SER A O   
6131  C CB  . SER A 823  ? 0.2154 0.2169 0.2049 -0.0140 0.0072  0.0246  821  SER A CB  
6132  O OG  . SER A 823  ? 0.2408 0.2473 0.2294 -0.0137 0.0079  0.0219  821  SER A OG  
6133  N N   . SER A 824  ? 0.2017 0.1905 0.1895 -0.0081 0.0097  0.0165  822  SER A N   
6134  C CA  . SER A 824  ? 0.1978 0.1854 0.1857 -0.0063 0.0107  0.0136  822  SER A CA  
6135  C C   . SER A 824  ? 0.2121 0.1929 0.2002 -0.0049 0.0111  0.0139  822  SER A C   
6136  O O   . SER A 824  ? 0.2236 0.2033 0.2124 -0.0038 0.0118  0.0123  822  SER A O   
6137  C CB  . SER A 824  ? 0.1907 0.1790 0.1783 -0.0052 0.0111  0.0107  822  SER A CB  
6138  O OG  . SER A 824  ? 0.1957 0.1782 0.1826 -0.0041 0.0112  0.0108  822  SER A OG  
6139  N N   . ALA A 825  ? 0.2008 0.1773 0.1886 -0.0049 0.0107  0.0158  823  ALA A N   
6140  C CA  . ALA A 825  ? 0.2132 0.1842 0.2011 -0.0033 0.0112  0.0160  823  ALA A CA  
6141  C C   . ALA A 825  ? 0.2085 0.1801 0.1976 -0.0036 0.0113  0.0172  823  ALA A C   
6142  O O   . ALA A 825  ? 0.2466 0.2219 0.2365 -0.0052 0.0106  0.0187  823  ALA A O   
6143  C CB  . ALA A 825  ? 0.2247 0.1916 0.2121 -0.0030 0.0105  0.0171  823  ALA A CB  
6144  N N   . LEU A 826  ? 0.2291 0.1974 0.2186 -0.0021 0.0122  0.0168  824  LEU A N   
6145  C CA  . LEU A 826  ? 0.2633 0.2320 0.2543 -0.0021 0.0123  0.0179  824  LEU A CA  
6146  C C   . LEU A 826  ? 0.2550 0.2206 0.2464 -0.0018 0.0117  0.0198  824  LEU A C   
6147  O O   . LEU A 826  ? 0.2597 0.2214 0.2505 -0.0002 0.0121  0.0193  824  LEU A O   
6148  C CB  . LEU A 826  ? 0.2942 0.2614 0.2861 -0.0008 0.0134  0.0167  824  LEU A CB  
6149  C CG  . LEU A 826  ? 0.3617 0.3300 0.3555 -0.0011 0.0135  0.0176  824  LEU A CG  
6150  C CD1 . LEU A 826  ? 0.3746 0.3482 0.3692 -0.0027 0.0128  0.0171  824  LEU A CD1 
6151  C CD2 . LEU A 826  ? 0.4007 0.3673 0.3959 0.0001  0.0146  0.0170  824  LEU A CD2 
6152  N N   . ALA A 827  ? 0.2559 0.2235 0.2486 -0.0031 0.0107  0.0218  825  ALA A N   
6153  C CA  . ALA A 827  ? 0.2312 0.1960 0.2250 -0.0029 0.0096  0.0236  825  ALA A CA  
6154  C C   . ALA A 827  ? 0.2332 0.1940 0.2275 -0.0007 0.0104  0.0230  825  ALA A C   
6155  O O   . ALA A 827  ? 0.2060 0.1633 0.2003 0.0005  0.0099  0.0227  825  ALA A O   
6156  C CB  . ALA A 827  ? 0.2580 0.2259 0.2535 -0.0047 0.0082  0.0262  825  ALA A CB  
6157  N N   . GLU A 828  ? 0.2308 0.1927 0.2258 -0.0001 0.0115  0.0227  826  GLU A N   
6158  C CA  . GLU A 828  ? 0.2431 0.2025 0.2388 0.0020  0.0124  0.0224  826  GLU A CA  
6159  C C   . GLU A 828  ? 0.2309 0.1877 0.2248 0.0038  0.0134  0.0208  826  GLU A C   
6160  O O   . GLU A 828  ? 0.2425 0.1970 0.2364 0.0057  0.0136  0.0204  826  GLU A O   
6161  C CB  . GLU A 828  ? 0.2942 0.2558 0.2914 0.0019  0.0134  0.0226  826  GLU A CB  
6162  C CG  . GLU A 828  ? 0.3677 0.3317 0.3670 0.0008  0.0124  0.0243  826  GLU A CG  
6163  C CD  . GLU A 828  ? 0.4003 0.3685 0.3994 -0.0015 0.0116  0.0246  826  GLU A CD  
6164  O OE1 . GLU A 828  ? 0.3758 0.3449 0.3731 -0.0021 0.0116  0.0234  826  GLU A OE1 
6165  O OE2 . GLU A 828  ? 0.4710 0.4421 0.4717 -0.0024 0.0108  0.0260  826  GLU A OE2 
6166  N N   . GLN A 829  ? 0.2362 0.1935 0.2285 0.0034  0.0140  0.0197  827  GLN A N   
6167  C CA  . GLN A 829  ? 0.2117 0.1670 0.2021 0.0050  0.0148  0.0184  827  GLN A CA  
6168  C C   . GLN A 829  ? 0.1972 0.1503 0.1866 0.0054  0.0136  0.0179  827  GLN A C   
6169  O O   . GLN A 829  ? 0.2087 0.1597 0.1970 0.0073  0.0139  0.0170  827  GLN A O   
6170  C CB  . GLN A 829  ? 0.2641 0.2205 0.2535 0.0043  0.0152  0.0174  827  GLN A CB  
6171  C CG  . GLN A 829  ? 0.3594 0.3170 0.3501 0.0044  0.0163  0.0174  827  GLN A CG  
6172  C CD  . GLN A 829  ? 0.3759 0.3338 0.3660 0.0043  0.0164  0.0162  827  GLN A CD  
6173  O OE1 . GLN A 829  ? 0.3184 0.2769 0.3074 0.0036  0.0156  0.0153  827  GLN A OE1 
6174  N NE2 . GLN A 829  ? 0.3924 0.3501 0.3837 0.0049  0.0172  0.0164  827  GLN A NE2 
6175  N N   . VAL A 830  ? 0.2111 0.1649 0.2006 0.0035  0.0122  0.0184  828  VAL A N   
6176  C CA  . VAL A 830  ? 0.1708 0.1224 0.1601 0.0035  0.0106  0.0183  828  VAL A CA  
6177  C C   . VAL A 830  ? 0.1887 0.1377 0.1796 0.0049  0.0098  0.0184  828  VAL A C   
6178  O O   . VAL A 830  ? 0.1915 0.1378 0.1817 0.0066  0.0094  0.0168  828  VAL A O   
6179  C CB  . VAL A 830  ? 0.1905 0.1444 0.1808 0.0009  0.0091  0.0197  828  VAL A CB  
6180  C CG1 . VAL A 830  ? 0.2115 0.1628 0.2027 0.0005  0.0071  0.0202  828  VAL A CG1 
6181  C CG2 . VAL A 830  ? 0.2101 0.1669 0.1988 -0.0001 0.0098  0.0189  828  VAL A CG2 
6182  N N   . VAL A 831  ? 0.1980 0.1478 0.1911 0.0045  0.0095  0.0199  829  VAL A N   
6183  C CA  . VAL A 831  ? 0.1846 0.1320 0.1798 0.0058  0.0084  0.0201  829  VAL A CA  
6184  C C   . VAL A 831  ? 0.1745 0.1207 0.1688 0.0088  0.0098  0.0180  829  VAL A C   
6185  O O   . VAL A 831  ? 0.1802 0.1237 0.1749 0.0106  0.0088  0.0165  829  VAL A O   
6186  C CB  . VAL A 831  ? 0.1832 0.1323 0.1812 0.0047  0.0078  0.0224  829  VAL A CB  
6187  C CG1 . VAL A 831  ? 0.2009 0.1476 0.2015 0.0067  0.0069  0.0222  829  VAL A CG1 
6188  C CG2 . VAL A 831  ? 0.2028 0.1534 0.2020 0.0019  0.0060  0.0247  829  VAL A CG2 
6189  N N   . GLY A 832  ? 0.1862 0.1345 0.1792 0.0094  0.0120  0.0179  830  GLY A N   
6190  C CA  . GLY A 832  ? 0.1770 0.1252 0.1689 0.0121  0.0135  0.0164  830  GLY A CA  
6191  C C   . GLY A 832  ? 0.1998 0.1465 0.1891 0.0134  0.0133  0.0143  830  GLY A C   
6192  O O   . GLY A 832  ? 0.1984 0.1442 0.1873 0.0159  0.0132  0.0125  830  GLY A O   
6193  N N   . ASP A 833  ? 0.1819 0.1285 0.1695 0.0120  0.0131  0.0143  831  ASP A N   
6194  C CA  . ASP A 833  ? 0.1617 0.1071 0.1469 0.0131  0.0128  0.0124  831  ASP A CA  
6195  C C   . ASP A 833  ? 0.1843 0.1270 0.1706 0.0134  0.0104  0.0111  831  ASP A C   
6196  O O   . ASP A 833  ? 0.1915 0.1330 0.1763 0.0152  0.0099  0.0088  831  ASP A O   
6197  C CB  . ASP A 833  ? 0.1676 0.1140 0.1512 0.0115  0.0131  0.0128  831  ASP A CB  
6198  C CG  . ASP A 833  ? 0.2066 0.1552 0.1895 0.0116  0.0151  0.0137  831  ASP A CG  
6199  O OD1 . ASP A 833  ? 0.2234 0.1731 0.2064 0.0132  0.0165  0.0139  831  ASP A OD1 
6200  O OD2 . ASP A 833  ? 0.2078 0.1574 0.1905 0.0101  0.0153  0.0141  831  ASP A OD2 
6201  N N   . VAL A 834  ? 0.1732 0.1148 0.1622 0.0115  0.0086  0.0126  832  VAL A N   
6202  C CA  . VAL A 834  ? 0.1588 0.0973 0.1498 0.0115  0.0059  0.0118  832  VAL A CA  
6203  C C   . VAL A 834  ? 0.1732 0.1100 0.1659 0.0143  0.0054  0.0100  832  VAL A C   
6204  O O   . VAL A 834  ? 0.1882 0.1227 0.1811 0.0160  0.0039  0.0074  832  VAL A O   
6205  C CB  . VAL A 834  ? 0.1541 0.0926 0.1479 0.0084  0.0042  0.0146  832  VAL A CB  
6206  C CG1 . VAL A 834  ? 0.1784 0.1134 0.1757 0.0084  0.0011  0.0144  832  VAL A CG1 
6207  C CG2 . VAL A 834  ? 0.1894 0.1299 0.1816 0.0061  0.0044  0.0155  832  VAL A CG2 
6208  N N   . ILE A 835  ? 0.1866 0.1248 0.1809 0.0148  0.0064  0.0112  833  ILE A N   
6209  C CA  . ILE A 835  ? 0.1825 0.1198 0.1787 0.0176  0.0060  0.0095  833  ILE A CA  
6210  C C   . ILE A 835  ? 0.2061 0.1444 0.1994 0.0207  0.0073  0.0062  833  ILE A C   
6211  O O   . ILE A 835  ? 0.2010 0.1377 0.1952 0.0232  0.0059  0.0032  833  ILE A O   
6212  C CB  . ILE A 835  ? 0.1996 0.1392 0.1976 0.0175  0.0073  0.0115  833  ILE A CB  
6213  C CG1 . ILE A 835  ? 0.2051 0.1438 0.2064 0.0148  0.0054  0.0145  833  ILE A CG1 
6214  C CG2 . ILE A 835  ? 0.2352 0.1751 0.2346 0.0210  0.0076  0.0093  833  ILE A CG2 
6215  C CD1 . ILE A 835  ? 0.2324 0.1676 0.2380 0.0154  0.0023  0.0143  833  ILE A CD1 
6216  N N   . THR A 836  ? 0.1725 0.1138 0.1623 0.0207  0.0099  0.0067  834  THR A N   
6217  C CA  . THR A 836  ? 0.1971 0.1404 0.1839 0.0234  0.0112  0.0043  834  THR A CA  
6218  C C   . THR A 836  ? 0.1848 0.1258 0.1701 0.0239  0.0093  0.0017  834  THR A C   
6219  O O   . THR A 836  ? 0.1972 0.1381 0.1820 0.0267  0.0086  -0.0016 834  THR A O   
6220  C CB  . THR A 836  ? 0.2402 0.1868 0.2243 0.0227  0.0139  0.0062  834  THR A CB  
6221  O OG1 . THR A 836  ? 0.2826 0.2315 0.2684 0.0226  0.0155  0.0082  834  THR A OG1 
6222  C CG2 . THR A 836  ? 0.2573 0.2065 0.2380 0.0252  0.0152  0.0044  834  THR A CG2 
6223  N N   . SER A 837  ? 0.1730 0.1124 0.1579 0.0212  0.0084  0.0030  835  SER A N   
6224  C CA  . SER A 837  ? 0.1608 0.0987 0.1441 0.0215  0.0068  0.0008  835  SER A CA  
6225  C C   . SER A 837  ? 0.1807 0.1149 0.1669 0.0223  0.0036  -0.0016 835  SER A C   
6226  O O   . SER A 837  ? 0.2057 0.1391 0.1908 0.0241  0.0024  -0.0049 835  SER A O   
6227  C CB  . SER A 837  ? 0.1719 0.1095 0.1545 0.0184  0.0065  0.0028  835  SER A CB  
6228  O OG  . SER A 837  ? 0.1893 0.1299 0.1694 0.0178  0.0091  0.0045  835  SER A OG  
6229  N N   . ALA A 838  ? 0.1749 0.1069 0.1653 0.0211  0.0020  -0.0001 836  ALA A N   
6230  C CA  . ALA A 838  ? 0.1779 0.1058 0.1723 0.0215  -0.0015 -0.0019 836  ALA A CA  
6231  C C   . ALA A 838  ? 0.1937 0.1211 0.1896 0.0253  -0.0020 -0.0053 836  ALA A C   
6232  O O   . ALA A 838  ? 0.1856 0.1102 0.1836 0.0269  -0.0047 -0.0087 836  ALA A O   
6233  C CB  . ALA A 838  ? 0.1839 0.1098 0.1826 0.0183  -0.0033 0.0018  836  ALA A CB  
6234  N N   . PHE A 839  ? 0.2096 0.1400 0.2051 0.0267  0.0004  -0.0046 837  PHE A N   
6235  C CA  . PHE A 839  ? 0.1753 0.1055 0.1735 0.0300  -0.0003 -0.0073 837  PHE A CA  
6236  C C   . PHE A 839  ? 0.2082 0.1432 0.2029 0.0336  0.0025  -0.0099 837  PHE A C   
6237  O O   . PHE A 839  ? 0.2090 0.1445 0.2055 0.0370  0.0018  -0.0133 837  PHE A O   
6238  C CB  . PHE A 839  ? 0.1833 0.1128 0.1856 0.0288  -0.0006 -0.0042 837  PHE A CB  
6239  C CG  . PHE A 839  ? 0.1879 0.1135 0.1938 0.0253  -0.0034 -0.0011 837  PHE A CG  
6240  C CD1 . PHE A 839  ? 0.2019 0.1230 0.2111 0.0251  -0.0071 -0.0027 837  PHE A CD1 
6241  C CD2 . PHE A 839  ? 0.2084 0.1355 0.2146 0.0221  -0.0023 0.0036  837  PHE A CD2 
6242  C CE1 . PHE A 839  ? 0.1928 0.1111 0.2056 0.0215  -0.0097 0.0008  837  PHE A CE1 
6243  C CE2 . PHE A 839  ? 0.2013 0.1261 0.2106 0.0187  -0.0047 0.0068  837  PHE A CE2 
6244  C CZ  . PHE A 839  ? 0.1955 0.1160 0.2082 0.0184  -0.0084 0.0057  837  PHE A CZ  
6245  N N   . ASP A 840  ? 0.2112 0.1501 0.2013 0.0330  0.0055  -0.0083 838  ASP A N   
6246  C CA  . ASP A 840  ? 0.2026 0.1468 0.1893 0.0362  0.0080  -0.0104 838  ASP A CA  
6247  C C   . ASP A 840  ? 0.2169 0.1607 0.2028 0.0394  0.0061  -0.0158 838  ASP A C   
6248  O O   . ASP A 840  ? 0.2057 0.1458 0.1917 0.0384  0.0035  -0.0172 838  ASP A O   
6249  C CB  . ASP A 840  ? 0.2129 0.1602 0.1952 0.0345  0.0106  -0.0077 838  ASP A CB  
6250  C CG  . ASP A 840  ? 0.2368 0.1900 0.2154 0.0374  0.0131  -0.0090 838  ASP A CG  
6251  O OD1 . ASP A 840  ? 0.2249 0.1792 0.2011 0.0396  0.0123  -0.0125 838  ASP A OD1 
6252  O OD2 . ASP A 840  ? 0.2677 0.2249 0.2459 0.0372  0.0158  -0.0062 838  ASP A OD2 
6253  N N   . SER A 841  ? 0.2059 0.1538 0.1913 0.0433  0.0071  -0.0189 839  SER A N   
6254  C CA  . SER A 841  ? 0.2000 0.1486 0.1845 0.0469  0.0053  -0.0248 839  SER A CA  
6255  C C   . SER A 841  ? 0.1984 0.1402 0.1878 0.0470  0.0009  -0.0277 839  SER A C   
6256  O O   . SER A 841  ? 0.2161 0.1564 0.2052 0.0485  -0.0016 -0.0321 839  SER A O   
6257  C CB  . SER A 841  ? 0.2099 0.1613 0.1890 0.0469  0.0062  -0.0254 839  SER A CB  
6258  O OG  . SER A 841  ? 0.2353 0.1932 0.2105 0.0471  0.0101  -0.0226 839  SER A OG  
6259  N N   . ALA A 842  ? 0.1961 0.1339 0.1906 0.0452  -0.0005 -0.0253 840  ALA A N   
6260  C CA  . ALA A 842  ? 0.1881 0.1192 0.1884 0.0447  -0.0049 -0.0269 840  ALA A CA  
6261  C C   . ALA A 842  ? 0.1829 0.1099 0.1826 0.0419  -0.0073 -0.0264 840  ALA A C   
6262  O O   . ALA A 842  ? 0.2260 0.1485 0.2295 0.0423  -0.0112 -0.0295 840  ALA A O   
6263  C CB  . ALA A 842  ? 0.2293 0.1603 0.2324 0.0495  -0.0072 -0.0333 840  ALA A CB  
6264  N N   . GLY A 843  ? 0.2141 0.1428 0.2098 0.0388  -0.0050 -0.0225 841  GLY A N   
6265  C CA  . GLY A 843  ? 0.2086 0.1345 0.2038 0.0360  -0.0068 -0.0218 841  GLY A CA  
6266  C C   . GLY A 843  ? 0.2213 0.1478 0.2140 0.0384  -0.0081 -0.0268 841  GLY A C   
6267  O O   . GLY A 843  ? 0.2289 0.1523 0.2223 0.0365  -0.0105 -0.0271 841  GLY A O   
6268  N N   . GLN A 844  ? 0.1955 0.1264 0.1853 0.0425  -0.0066 -0.0308 842  GLN A N   
6269  C CA  . GLN A 844  ? 0.2035 0.1360 0.1907 0.0453  -0.0079 -0.0361 842  GLN A CA  
6270  C C   . GLN A 844  ? 0.2450 0.1825 0.2257 0.0448  -0.0051 -0.0346 842  GLN A C   
6271  O O   . GLN A 844  ? 0.3064 0.2488 0.2831 0.0480  -0.0041 -0.0382 842  GLN A O   
6272  C CB  . GLN A 844  ? 0.2284 0.1639 0.2163 0.0504  -0.0082 -0.0417 842  GLN A CB  
6273  C CG  . GLN A 844  ? 0.2226 0.1524 0.2177 0.0513  -0.0120 -0.0442 842  GLN A CG  
6274  C CD  . GLN A 844  ? 0.2206 0.1538 0.2168 0.0567  -0.0122 -0.0501 842  GLN A CD  
6275  O OE1 . GLN A 844  ? 0.2304 0.1597 0.2314 0.0590  -0.0162 -0.0552 842  GLN A OE1 
6276  N NE2 . GLN A 844  ? 0.2584 0.1989 0.2507 0.0588  -0.0081 -0.0495 842  GLN A NE2 
6277  N N   . ARG A 845  ? 0.2169 0.1537 0.1964 0.0409  -0.0036 -0.0294 843  ARG A N   
6278  C CA  . ARG A 845  ? 0.2112 0.1514 0.1855 0.0400  -0.0017 -0.0278 843  ARG A CA  
6279  C C   . ARG A 845  ? 0.2332 0.1692 0.2086 0.0373  -0.0045 -0.0277 843  ARG A C   
6280  O O   . ARG A 845  ? 0.2267 0.1579 0.2063 0.0343  -0.0064 -0.0255 843  ARG A O   
6281  C CB  . ARG A 845  ? 0.1946 0.1372 0.1672 0.0377  0.0019  -0.0222 843  ARG A CB  
6282  C CG  . ARG A 845  ? 0.2214 0.1687 0.1929 0.0398  0.0049  -0.0214 843  ARG A CG  
6283  C CD  . ARG A 845  ? 0.2423 0.1913 0.2128 0.0371  0.0078  -0.0159 843  ARG A CD  
6284  N NE  . ARG A 845  ? 0.2290 0.1825 0.1991 0.0386  0.0106  -0.0145 843  ARG A NE  
6285  C CZ  . ARG A 845  ? 0.2345 0.1937 0.2010 0.0396  0.0135  -0.0129 843  ARG A CZ  
6286  N NH1 . ARG A 845  ? 0.2273 0.1885 0.1901 0.0394  0.0138  -0.0125 843  ARG A NH1 
6287  N NH2 . ARG A 845  ? 0.2309 0.1942 0.1980 0.0408  0.0158  -0.0113 843  ARG A NH2 
6288  N N   . CYS A 846  ? 0.2240 0.1622 0.1957 0.0381  -0.0048 -0.0298 844  CYS A N   
6289  C CA  . CYS A 846  ? 0.2658 0.2007 0.2384 0.0353  -0.0071 -0.0291 844  CYS A CA  
6290  C C   . CYS A 846  ? 0.2160 0.1506 0.1887 0.0314  -0.0053 -0.0234 844  CYS A C   
6291  O O   . CYS A 846  ? 0.2354 0.1667 0.2106 0.0284  -0.0073 -0.0219 844  CYS A O   
6292  C CB  . CYS A 846  ? 0.2635 0.2015 0.2319 0.0370  -0.0076 -0.0323 844  CYS A CB  
6293  S SG  . CYS A 846  ? 0.3650 0.3028 0.3345 0.0414  -0.0109 -0.0401 844  CYS A SG  
6294  N N   . SER A 847  ? 0.2079 0.1459 0.1782 0.0313  -0.0018 -0.0202 845  SER A N   
6295  C CA  . SER A 847  ? 0.1891 0.1272 0.1594 0.0281  0.0001  -0.0152 845  SER A CA  
6296  C C   . SER A 847  ? 0.1946 0.1298 0.1692 0.0260  -0.0002 -0.0126 845  SER A C   
6297  O O   . SER A 847  ? 0.1997 0.1352 0.1746 0.0233  0.0011  -0.0089 845  SER A O   
6298  C CB  . SER A 847  ? 0.2180 0.1610 0.1846 0.0292  0.0037  -0.0131 845  SER A CB  
6299  O OG  . SER A 847  ? 0.2130 0.1577 0.1799 0.0317  0.0050  -0.0142 845  SER A OG  
6300  N N   . ALA A 848  ? 0.1879 0.1208 0.1658 0.0272  -0.0019 -0.0146 846  ALA A N   
6301  C CA  . ALA A 848  ? 0.1740 0.1050 0.1556 0.0256  -0.0018 -0.0118 846  ALA A CA  
6302  C C   . ALA A 848  ? 0.1732 0.1017 0.1577 0.0216  -0.0034 -0.0085 846  ALA A C   
6303  O O   . ALA A 848  ? 0.1937 0.1203 0.1792 0.0203  -0.0057 -0.0093 846  ALA A O   
6304  C CB  . ALA A 848  ? 0.2195 0.1482 0.2048 0.0279  -0.0039 -0.0147 846  ALA A CB  
6305  N N   . LEU A 849  ? 0.1709 0.0998 0.1569 0.0197  -0.0021 -0.0049 847  LEU A N   
6306  C CA  . LEU A 849  ? 0.1833 0.1112 0.1720 0.0159  -0.0033 -0.0015 847  LEU A CA  
6307  C C   . LEU A 849  ? 0.1848 0.1085 0.1787 0.0151  -0.0070 -0.0017 847  LEU A C   
6308  O O   . LEU A 849  ? 0.1866 0.1088 0.1834 0.0164  -0.0077 -0.0021 847  LEU A O   
6309  C CB  . LEU A 849  ? 0.1680 0.0982 0.1568 0.0144  -0.0010 0.0021  847  LEU A CB  
6310  C CG  . LEU A 849  ? 0.1752 0.1053 0.1666 0.0106  -0.0022 0.0057  847  LEU A CG  
6311  C CD1 . LEU A 849  ? 0.1914 0.1229 0.1812 0.0087  -0.0023 0.0061  847  LEU A CD1 
6312  C CD2 . LEU A 849  ? 0.1783 0.1112 0.1697 0.0096  0.0000  0.0086  847  LEU A CD2 
6313  N N   . ARG A 850  ? 0.1736 0.0957 0.1693 0.0130  -0.0095 -0.0014 848  ARG A N   
6314  C CA  . ARG A 850  ? 0.1882 0.1061 0.1895 0.0118  -0.0134 -0.0012 848  ARG A CA  
6315  C C   . ARG A 850  ? 0.1965 0.1149 0.2013 0.0076  -0.0144 0.0039  848  ARG A C   
6316  O O   . ARG A 850  ? 0.1938 0.1094 0.2038 0.0065  -0.0171 0.0055  848  ARG A O   
6317  C CB  . ARG A 850  ? 0.2083 0.1239 0.2104 0.0124  -0.0162 -0.0046 848  ARG A CB  
6318  C CG  . ARG A 850  ? 0.2184 0.1345 0.2168 0.0165  -0.0155 -0.0099 848  ARG A CG  
6319  C CD  . ARG A 850  ? 0.2184 0.1334 0.2180 0.0198  -0.0154 -0.0123 848  ARG A CD  
6320  N NE  . ARG A 850  ? 0.2159 0.1322 0.2123 0.0238  -0.0151 -0.0177 848  ARG A NE  
6321  C CZ  . ARG A 850  ? 0.2376 0.1543 0.2341 0.0274  -0.0147 -0.0208 848  ARG A CZ  
6322  N NH1 . ARG A 850  ? 0.2278 0.1434 0.2278 0.0276  -0.0146 -0.0192 848  ARG A NH1 
6323  N NH2 . ARG A 850  ? 0.2341 0.1531 0.2274 0.0311  -0.0143 -0.0257 848  ARG A NH2 
6324  N N   . VAL A 851  ? 0.1952 0.1173 0.1973 0.0052  -0.0125 0.0064  849  VAL A N   
6325  C CA  A VAL A 851  ? 0.1867 0.1108 0.1915 0.0013  -0.0133 0.0111  849  VAL A CA  
6326  C CA  B VAL A 851  ? 0.1871 0.1111 0.1920 0.0013  -0.0133 0.0112  849  VAL A CA  
6327  C C   . VAL A 851  ? 0.1876 0.1167 0.1889 0.0005  -0.0097 0.0133  849  VAL A C   
6328  O O   . VAL A 851  ? 0.1923 0.1239 0.1897 0.0008  -0.0077 0.0121  849  VAL A O   
6329  C CB  A VAL A 851  ? 0.2179 0.1422 0.2243 -0.0012 -0.0154 0.0118  849  VAL A CB  
6330  C CB  B VAL A 851  ? 0.2169 0.1409 0.2238 -0.0013 -0.0156 0.0120  849  VAL A CB  
6331  C CG1 A VAL A 851  ? 0.1987 0.1254 0.2086 -0.0052 -0.0165 0.0171  849  VAL A CG1 
6332  C CG1 B VAL A 851  ? 0.2308 0.1498 0.2436 -0.0017 -0.0200 0.0117  849  VAL A CG1 
6333  C CG2 A VAL A 851  ? 0.2559 0.1752 0.2652 0.0001  -0.0189 0.0086  849  VAL A CG2 
6334  C CG2 B VAL A 851  ? 0.2206 0.1456 0.2233 0.0001  -0.0146 0.0088  849  VAL A CG2 
6335  N N   . LEU A 852  ? 0.1772 0.1076 0.1801 -0.0006 -0.0092 0.0162  850  LEU A N   
6336  C CA  . LEU A 852  ? 0.1945 0.1297 0.1948 -0.0017 -0.0064 0.0183  850  LEU A CA  
6337  C C   . LEU A 852  ? 0.1610 0.0999 0.1632 -0.0055 -0.0073 0.0221  850  LEU A C   
6338  O O   . LEU A 852  ? 0.1749 0.1129 0.1815 -0.0074 -0.0099 0.0250  850  LEU A O   
6339  C CB  . LEU A 852  ? 0.1833 0.1186 0.1843 -0.0007 -0.0054 0.0192  850  LEU A CB  
6340  C CG  . LEU A 852  ? 0.1949 0.1350 0.1941 -0.0019 -0.0030 0.0212  850  LEU A CG  
6341  C CD1 . LEU A 852  ? 0.1940 0.1360 0.1888 -0.0004 -0.0001 0.0189  850  LEU A CD1 
6342  C CD2 . LEU A 852  ? 0.1946 0.1343 0.1957 -0.0011 -0.0028 0.0224  850  LEU A CD2 
6343  N N   . CYS A 853  ? 0.1698 0.1132 0.1691 -0.0065 -0.0054 0.0223  851  CYS A N   
6344  C CA  . CYS A 853  ? 0.1777 0.1261 0.1784 -0.0098 -0.0060 0.0255  851  CYS A CA  
6345  C C   . CYS A 853  ? 0.1656 0.1194 0.1644 -0.0105 -0.0036 0.0268  851  CYS A C   
6346  O O   . CYS A 853  ? 0.1684 0.1238 0.1638 -0.0090 -0.0013 0.0245  851  CYS A O   
6347  C CB  . CYS A 853  ? 0.1837 0.1334 0.1830 -0.0102 -0.0060 0.0240  851  CYS A CB  
6348  S SG  . CYS A 853  ? 0.2179 0.1613 0.2184 -0.0087 -0.0085 0.0211  851  CYS A SG  
6349  N N   . LEU A 854  ? 0.1737 0.1304 0.1749 -0.0127 -0.0045 0.0305  852  LEU A N   
6350  C CA  . LEU A 854  ? 0.1699 0.1318 0.1698 -0.0132 -0.0027 0.0317  852  LEU A CA  
6351  C C   . LEU A 854  ? 0.1644 0.1338 0.1647 -0.0161 -0.0027 0.0344  852  LEU A C   
6352  O O   . LEU A 854  ? 0.1714 0.1423 0.1748 -0.0187 -0.0048 0.0380  852  LEU A O   
6353  C CB  . LEU A 854  ? 0.1738 0.1343 0.1762 -0.0133 -0.0036 0.0340  852  LEU A CB  
6354  C CG  . LEU A 854  ? 0.1657 0.1198 0.1680 -0.0102 -0.0034 0.0314  852  LEU A CG  
6355  C CD1 . LEU A 854  ? 0.1956 0.1489 0.2008 -0.0104 -0.0045 0.0339  852  LEU A CD1 
6356  C CD2 . LEU A 854  ? 0.2014 0.1556 0.1998 -0.0078 -0.0005 0.0279  852  LEU A CD2 
6357  N N   . GLN A 855  ? 0.1831 0.1575 0.1805 -0.0158 -0.0005 0.0327  853  GLN A N   
6358  C CA  . GLN A 855  ? 0.1655 0.1484 0.1630 -0.0182 -0.0003 0.0349  853  GLN A CA  
6359  C C   . GLN A 855  ? 0.1810 0.1676 0.1808 -0.0204 -0.0014 0.0392  853  GLN A C   
6360  O O   . GLN A 855  ? 0.1876 0.1724 0.1872 -0.0194 -0.0010 0.0392  853  GLN A O   
6361  C CB  . GLN A 855  ? 0.1850 0.1725 0.1794 -0.0170 0.0021  0.0317  853  GLN A CB  
6362  C CG  . GLN A 855  ? 0.1691 0.1659 0.1635 -0.0191 0.0024  0.0330  853  GLN A CG  
6363  C CD  . GLN A 855  ? 0.2105 0.2123 0.2025 -0.0178 0.0044  0.0295  853  GLN A CD  
6364  O OE1 . GLN A 855  ? 0.2309 0.2289 0.2213 -0.0154 0.0055  0.0258  853  GLN A OE1 
6365  N NE2 . GLN A 855  ? 0.2317 0.2426 0.2236 -0.0193 0.0047  0.0308  853  GLN A NE2 
6366  N N   . GLU A 856  ? 0.1838 0.1758 0.1856 -0.0234 -0.0028 0.0432  854  GLU A N   
6367  C CA  . GLU A 856  ? 0.2062 0.2012 0.2110 -0.0258 -0.0045 0.0484  854  GLU A CA  
6368  C C   . GLU A 856  ? 0.1915 0.1910 0.1946 -0.0253 -0.0031 0.0484  854  GLU A C   
6369  O O   . GLU A 856  ? 0.2352 0.2325 0.2402 -0.0255 -0.0042 0.0507  854  GLU A O   
6370  C CB  . GLU A 856  ? 0.2086 0.2110 0.2156 -0.0293 -0.0057 0.0528  854  GLU A CB  
6371  C CG  . GLU A 856  ? 0.2381 0.2454 0.2481 -0.0322 -0.0074 0.0590  854  GLU A CG  
6372  C CD  . GLU A 856  ? 0.3383 0.3373 0.3526 -0.0324 -0.0102 0.0616  854  GLU A CD  
6373  O OE1 . GLU A 856  ? 0.3126 0.3036 0.3287 -0.0314 -0.0115 0.0599  854  GLU A OE1 
6374  O OE2 . GLU A 856  ? 0.3133 0.3140 0.3294 -0.0333 -0.0112 0.0653  854  GLU A OE2 
6375  N N   . ASP A 857  ? 0.2022 0.2076 0.2020 -0.0245 -0.0009 0.0454  855  ASP A N   
6376  C CA  . ASP A 857  ? 0.2523 0.2633 0.2507 -0.0244 0.0001  0.0453  855  ASP A CA  
6377  C C   . ASP A 857  ? 0.2514 0.2556 0.2496 -0.0221 0.0005  0.0435  855  ASP A C   
6378  O O   . ASP A 857  ? 0.3012 0.3086 0.2996 -0.0225 0.0005  0.0449  855  ASP A O   
6379  C CB  . ASP A 857  ? 0.2881 0.3062 0.2835 -0.0236 0.0022  0.0416  855  ASP A CB  
6380  C CG  . ASP A 857  ? 0.4099 0.4367 0.4043 -0.0243 0.0027  0.0422  855  ASP A CG  
6381  O OD1 . ASP A 857  ? 0.4928 0.5261 0.4885 -0.0268 0.0016  0.0469  855  ASP A OD1 
6382  O OD2 . ASP A 857  ? 0.5325 0.5597 0.5250 -0.0223 0.0041  0.0380  855  ASP A OD2 
6383  N N   . VAL A 858  ? 0.2100 0.2056 0.2079 -0.0198 0.0009  0.0405  856  VAL A N   
6384  C CA  . VAL A 858  ? 0.2125 0.2024 0.2103 -0.0176 0.0014  0.0387  856  VAL A CA  
6385  C C   . VAL A 858  ? 0.1916 0.1739 0.1921 -0.0171 -0.0003 0.0403  856  VAL A C   
6386  O O   . VAL A 858  ? 0.2049 0.1824 0.2056 -0.0151 0.0001  0.0389  856  VAL A O   
6387  C CB  . VAL A 858  ? 0.2100 0.1970 0.2052 -0.0149 0.0035  0.0337  856  VAL A CB  
6388  C CG1 . VAL A 858  ? 0.2709 0.2649 0.2641 -0.0151 0.0049  0.0317  856  VAL A CG1 
6389  C CG2 . VAL A 858  ? 0.2076 0.1903 0.2022 -0.0141 0.0035  0.0319  856  VAL A CG2 
6390  N N   . ALA A 859  ? 0.1846 0.1657 0.1875 -0.0188 -0.0023 0.0430  857  ALA A N   
6391  C CA  . ALA A 859  ? 0.1833 0.1566 0.1891 -0.0179 -0.0043 0.0435  857  ALA A CA  
6392  C C   . ALA A 859  ? 0.2228 0.1942 0.2313 -0.0177 -0.0055 0.0458  857  ALA A C   
6393  O O   . ALA A 859  ? 0.2113 0.1764 0.2208 -0.0153 -0.0058 0.0439  857  ALA A O   
6394  C CB  . ALA A 859  ? 0.2184 0.1913 0.2271 -0.0202 -0.0066 0.0462  857  ALA A CB  
6395  N N   . ASP A 860  ? 0.2174 0.1950 0.2272 -0.0200 -0.0062 0.0499  858  ASP A N   
6396  C CA  . ASP A 860  ? 0.2417 0.2175 0.2545 -0.0199 -0.0077 0.0526  858  ASP A CA  
6397  C C   . ASP A 860  ? 0.2112 0.1853 0.2220 -0.0172 -0.0057 0.0493  858  ASP A C   
6398  O O   . ASP A 860  ? 0.2210 0.1900 0.2341 -0.0155 -0.0065 0.0491  858  ASP A O   
6399  C CB  . ASP A 860  ? 0.2280 0.2117 0.2423 -0.0230 -0.0089 0.0580  858  ASP A CB  
6400  C CG  . ASP A 860  ? 0.3144 0.2988 0.3323 -0.0259 -0.0116 0.0627  858  ASP A CG  
6401  O OD1 . ASP A 860  ? 0.3613 0.3383 0.3826 -0.0254 -0.0136 0.0626  858  ASP A OD1 
6402  O OD2 . ASP A 860  ? 0.4958 0.4887 0.5136 -0.0288 -0.0118 0.0665  858  ASP A OD2 
6403  N N   . ARG A 861  ? 0.1933 0.1719 0.2003 -0.0167 -0.0032 0.0467  859  ARG A N   
6404  C CA  . ARG A 861  ? 0.2031 0.1804 0.2087 -0.0145 -0.0015 0.0439  859  ARG A CA  
6405  C C   . ARG A 861  ? 0.1930 0.1629 0.1983 -0.0115 -0.0007 0.0403  859  ARG A C   
6406  O O   . ARG A 861  ? 0.2132 0.1798 0.2196 -0.0097 -0.0005 0.0395  859  ARG A O   
6407  C CB  . ARG A 861  ? 0.2660 0.2494 0.2683 -0.0147 0.0006  0.0416  859  ARG A CB  
6408  C CG  . ARG A 861  ? 0.3605 0.3425 0.3621 -0.0126 0.0022  0.0389  859  ARG A CG  
6409  C CD  . ARG A 861  ? 0.4789 0.4674 0.4785 -0.0131 0.0034  0.0373  859  ARG A CD  
6410  N NE  . ARG A 861  ? 0.5718 0.5579 0.5713 -0.0111 0.0048  0.0347  859  ARG A NE  
6411  C CZ  . ARG A 861  ? 0.5294 0.5127 0.5275 -0.0094 0.0064  0.0312  859  ARG A CZ  
6412  N NH1 . ARG A 861  ? 0.5539 0.5363 0.5502 -0.0093 0.0069  0.0295  859  ARG A NH1 
6413  N NH2 . ARG A 861  ? 0.4519 0.4333 0.4505 -0.0079 0.0074  0.0295  859  ARG A NH2 
6414  N N   . ILE A 862  ? 0.1913 0.1590 0.1950 -0.0111 -0.0002 0.0381  860  ILE A N   
6415  C CA  . ILE A 862  ? 0.1800 0.1416 0.1829 -0.0083 0.0006  0.0347  860  ILE A CA  
6416  C C   . ILE A 862  ? 0.1989 0.1550 0.2053 -0.0073 -0.0016 0.0355  860  ILE A C   
6417  O O   . ILE A 862  ? 0.2015 0.1538 0.2082 -0.0047 -0.0010 0.0334  860  ILE A O   
6418  C CB  . ILE A 862  ? 0.1853 0.1464 0.1856 -0.0081 0.0014  0.0323  860  ILE A CB  
6419  C CG1 . ILE A 862  ? 0.2390 0.2047 0.2364 -0.0082 0.0036  0.0305  860  ILE A CG1 
6420  C CG2 . ILE A 862  ? 0.2114 0.1665 0.2112 -0.0054 0.0017  0.0293  860  ILE A CG2 
6421  C CD1 . ILE A 862  ? 0.2819 0.2480 0.2771 -0.0081 0.0044  0.0284  860  ILE A CD1 
6422  N N   . LEU A 863  ? 0.1846 0.1404 0.1939 -0.0093 -0.0041 0.0386  861  LEU A N   
6423  C CA  . LEU A 863  ? 0.1998 0.1500 0.2132 -0.0085 -0.0067 0.0393  861  LEU A CA  
6424  C C   . LEU A 863  ? 0.2079 0.1575 0.2236 -0.0073 -0.0070 0.0404  861  LEU A C   
6425  O O   . LEU A 863  ? 0.1953 0.1401 0.2128 -0.0047 -0.0076 0.0383  861  LEU A O   
6426  C CB  . LEU A 863  ? 0.2412 0.1918 0.2581 -0.0114 -0.0097 0.0432  861  LEU A CB  
6427  C CG  . LEU A 863  ? 0.3245 0.2685 0.3462 -0.0106 -0.0129 0.0433  861  LEU A CG  
6428  C CD1 . LEU A 863  ? 0.2746 0.2136 0.2944 -0.0076 -0.0122 0.0380  861  LEU A CD1 
6429  C CD2 . LEU A 863  ? 0.3462 0.2914 0.3711 -0.0141 -0.0156 0.0475  861  LEU A CD2 
6430  N N   . THR A 864  ? 0.1776 0.1327 0.1933 -0.0091 -0.0066 0.0433  862  THR A N   
6431  C CA  . THR A 864  ? 0.1976 0.1526 0.2153 -0.0080 -0.0068 0.0444  862  THR A CA  
6432  C C   . THR A 864  ? 0.1677 0.1207 0.1834 -0.0048 -0.0044 0.0402  862  THR A C   
6433  O O   . THR A 864  ? 0.1843 0.1341 0.2024 -0.0025 -0.0049 0.0394  862  THR A O   
6434  C CB  . THR A 864  ? 0.1982 0.1603 0.2154 -0.0104 -0.0065 0.0477  862  THR A CB  
6435  O OG1 . THR A 864  ? 0.2431 0.2077 0.2627 -0.0134 -0.0090 0.0523  862  THR A OG1 
6436  C CG2 . THR A 864  ? 0.2164 0.1791 0.2354 -0.0092 -0.0065 0.0484  862  THR A CG2 
6437  N N   . MET A 865  ? 0.1758 0.1311 0.1873 -0.0045 -0.0018 0.0376  863  MET A N   
6438  C CA  . MET A 865  ? 0.1579 0.1119 0.1676 -0.0018 0.0006  0.0343  863  MET A CA  
6439  C C   . MET A 865  ? 0.1743 0.1228 0.1843 0.0009  0.0003  0.0315  863  MET A C   
6440  O O   . MET A 865  ? 0.1656 0.1125 0.1764 0.0035  0.0011  0.0298  863  MET A O   
6441  C CB  . MET A 865  ? 0.1811 0.1383 0.1869 -0.0023 0.0030  0.0325  863  MET A CB  
6442  C CG  . MET A 865  ? 0.2292 0.1859 0.2336 -0.0001 0.0053  0.0300  863  MET A CG  
6443  S SD  . MET A 865  ? 0.2601 0.2203 0.2610 -0.0008 0.0075  0.0282  863  MET A SD  
6444  C CE  . MET A 865  ? 0.2632 0.2291 0.2647 -0.0040 0.0062  0.0309  863  MET A CE  
6445  N N   . LEU A 866  ? 0.1617 0.1080 0.1713 0.0004  -0.0008 0.0308  864  LEU A N   
6446  C CA  . LEU A 866  ? 0.1563 0.0979 0.1662 0.0030  -0.0013 0.0278  864  LEU A CA  
6447  C C   . LEU A 866  ? 0.1472 0.0852 0.1616 0.0046  -0.0035 0.0279  864  LEU A C   
6448  O O   . LEU A 866  ? 0.1815 0.1175 0.1961 0.0078  -0.0029 0.0249  864  LEU A O   
6449  C CB  . LEU A 866  ? 0.1955 0.1356 0.2046 0.0017  -0.0025 0.0274  864  LEU A CB  
6450  C CG  . LEU A 866  ? 0.2384 0.1740 0.2475 0.0041  -0.0033 0.0238  864  LEU A CG  
6451  C CD1 . LEU A 866  ? 0.2383 0.1746 0.2436 0.0068  -0.0004 0.0205  864  LEU A CD1 
6452  C CD2 . LEU A 866  ? 0.2630 0.1978 0.2716 0.0023  -0.0047 0.0240  864  LEU A CD2 
6453  N N   . LYS A 867  ? 0.1666 0.1044 0.1850 0.0026  -0.0062 0.0315  865  LYS A N   
6454  C CA  . LYS A 867  ? 0.1825 0.1167 0.2059 0.0042  -0.0087 0.0318  865  LYS A CA  
6455  C C   . LYS A 867  ? 0.1896 0.1254 0.2133 0.0063  -0.0070 0.0312  865  LYS A C   
6456  O O   . LYS A 867  ? 0.1881 0.1213 0.2142 0.0094  -0.0076 0.0288  865  LYS A O   
6457  C CB  . LYS A 867  ? 0.2129 0.1470 0.2409 0.0012  -0.0120 0.0366  865  LYS A CB  
6458  C CG  . LYS A 867  ? 0.1878 0.1199 0.2165 -0.0008 -0.0140 0.0373  865  LYS A CG  
6459  C CD  . LYS A 867  ? 0.2469 0.1801 0.2801 -0.0042 -0.0171 0.0430  865  LYS A CD  
6460  C CE  . LYS A 867  ? 0.2794 0.2112 0.3135 -0.0065 -0.0190 0.0441  865  LYS A CE  
6461  N NZ  . LYS A 867  ? 0.3177 0.2518 0.3560 -0.0104 -0.0218 0.0504  865  LYS A NZ  
6462  N N   . GLY A 868  ? 0.1824 0.1231 0.2040 0.0048  -0.0050 0.0330  866  GLY A N   
6463  C CA  . GLY A 868  ? 0.1869 0.1295 0.2089 0.0066  -0.0034 0.0325  866  GLY A CA  
6464  C C   . GLY A 868  ? 0.1907 0.1326 0.2102 0.0098  -0.0009 0.0283  866  GLY A C   
6465  O O   . GLY A 868  ? 0.1872 0.1288 0.2086 0.0124  -0.0006 0.0270  866  GLY A O   
6466  N N   . ALA A 869  ? 0.1756 0.1178 0.1910 0.0096  0.0008  0.0264  867  ALA A N   
6467  C CA  . ALA A 869  ? 0.1521 0.0942 0.1650 0.0125  0.0031  0.0229  867  ALA A CA  
6468  C C   . ALA A 869  ? 0.1796 0.1180 0.1943 0.0155  0.0016  0.0199  867  ALA A C   
6469  O O   . ALA A 869  ? 0.1797 0.1188 0.1942 0.0186  0.0030  0.0174  867  ALA A O   
6470  C CB  . ALA A 869  ? 0.1690 0.1122 0.1774 0.0115  0.0049  0.0219  867  ALA A CB  
6471  N N   . LEU A 870  ? 0.1630 0.0978 0.1798 0.0146  -0.0013 0.0201  868  LEU A N   
6472  C CA  . LEU A 870  ? 0.1763 0.1072 0.1955 0.0174  -0.0034 0.0169  868  LEU A CA  
6473  C C   . LEU A 870  ? 0.1990 0.1296 0.2221 0.0201  -0.0040 0.0162  868  LEU A C   
6474  O O   . LEU A 870  ? 0.2016 0.1317 0.2250 0.0238  -0.0036 0.0122  868  LEU A O   
6475  C CB  . LEU A 870  ? 0.1930 0.1199 0.2153 0.0154  -0.0070 0.0183  868  LEU A CB  
6476  C CG  . LEU A 870  ? 0.1961 0.1182 0.2213 0.0180  -0.0098 0.0147  868  LEU A CG  
6477  C CD1 . LEU A 870  ? 0.2414 0.1633 0.2624 0.0187  -0.0087 0.0113  868  LEU A CD1 
6478  C CD2 . LEU A 870  ? 0.2232 0.1412 0.2545 0.0160  -0.0142 0.0172  868  LEU A CD2 
6479  N N   . HIS A 871  ? 0.1835 0.1150 0.2098 0.0185  -0.0049 0.0198  869  HIS A N   
6480  C CA  . HIS A 871  ? 0.1946 0.1257 0.2254 0.0210  -0.0060 0.0194  869  HIS A CA  
6481  C C   . HIS A 871  ? 0.2040 0.1394 0.2331 0.0234  -0.0026 0.0178  869  HIS A C   
6482  O O   . HIS A 871  ? 0.2461 0.1819 0.2788 0.0259  -0.0032 0.0170  869  HIS A O   
6483  C CB  . HIS A 871  ? 0.2306 0.1615 0.2656 0.0184  -0.0083 0.0241  869  HIS A CB  
6484  C CG  . HIS A 871  ? 0.2384 0.1648 0.2772 0.0168  -0.0123 0.0257  869  HIS A CG  
6485  N ND1 . HIS A 871  ? 0.2854 0.2070 0.3293 0.0192  -0.0155 0.0234  869  HIS A ND1 
6486  C CD2 . HIS A 871  ? 0.2324 0.1587 0.2709 0.0129  -0.0137 0.0292  869  HIS A CD2 
6487  C CE1 . HIS A 871  ? 0.2945 0.2127 0.3415 0.0168  -0.0188 0.0258  869  HIS A CE1 
6488  N NE2 . HIS A 871  ? 0.2616 0.1828 0.3052 0.0129  -0.0177 0.0295  869  HIS A NE2 
6489  N N   . GLU A 872  ? 0.1854 0.1241 0.2094 0.0227  0.0006  0.0175  870  GLU A N   
6490  C CA  . GLU A 872  ? 0.1926 0.1355 0.2150 0.0248  0.0038  0.0163  870  GLU A CA  
6491  C C   . GLU A 872  ? 0.2040 0.1474 0.2242 0.0283  0.0051  0.0119  870  GLU A C   
6492  O O   . GLU A 872  ? 0.2092 0.1568 0.2280 0.0301  0.0079  0.0110  870  GLU A O   
6493  C CB  . GLU A 872  ? 0.2098 0.1563 0.2287 0.0220  0.0063  0.0187  870  GLU A CB  
6494  C CG  . GLU A 872  ? 0.2236 0.1711 0.2443 0.0189  0.0053  0.0226  870  GLU A CG  
6495  C CD  . GLU A 872  ? 0.2276 0.1767 0.2525 0.0200  0.0048  0.0238  870  GLU A CD  
6496  O OE1 . GLU A 872  ? 0.2310 0.1820 0.2566 0.0230  0.0064  0.0218  870  GLU A OE1 
6497  O OE2 . GLU A 872  ? 0.2536 0.2026 0.2813 0.0181  0.0028  0.0268  870  GLU A OE2 
6498  N N   . LEU A 873  ? 0.1900 0.1297 0.2099 0.0292  0.0032  0.0093  871  LEU A N   
6499  C CA  . LEU A 873  ? 0.1911 0.1318 0.2087 0.0326  0.0043  0.0048  871  LEU A CA  
6500  C C   . LEU A 873  ? 0.1951 0.1360 0.2166 0.0368  0.0032  0.0015  871  LEU A C   
6501  O O   . LEU A 873  ? 0.2276 0.1649 0.2541 0.0371  0.0001  0.0017  871  LEU A O   
6502  C CB  . LEU A 873  ? 0.1989 0.1358 0.2147 0.0320  0.0025  0.0030  871  LEU A CB  
6503  C CG  . LEU A 873  ? 0.2001 0.1370 0.2120 0.0283  0.0034  0.0056  871  LEU A CG  
6504  C CD1 . LEU A 873  ? 0.2184 0.1512 0.2300 0.0277  0.0009  0.0039  871  LEU A CD1 
6505  C CD2 . LEU A 873  ? 0.2187 0.1603 0.2258 0.0288  0.0072  0.0054  871  LEU A CD2 
6506  N N   . HIS A 874  ? 0.2051 0.1505 0.2243 0.0401  0.0057  -0.0014 872  HIS A N   
6507  C CA  . HIS A 874  ? 0.1997 0.1467 0.2220 0.0446  0.0051  -0.0054 872  HIS A CA  
6508  C C   . HIS A 874  ? 0.2201 0.1659 0.2407 0.0475  0.0040  -0.0107 872  HIS A C   
6509  O O   . HIS A 874  ? 0.2120 0.1609 0.2273 0.0478  0.0062  -0.0118 872  HIS A O   
6510  C CB  . HIS A 874  ? 0.2246 0.1789 0.2457 0.0464  0.0088  -0.0050 872  HIS A CB  
6511  C CG  . HIS A 874  ? 0.2546 0.2119 0.2789 0.0513  0.0086  -0.0091 872  HIS A CG  
6512  N ND1 . HIS A 874  ? 0.3731 0.3260 0.4024 0.0536  0.0050  -0.0123 872  HIS A ND1 
6513  C CD2 . HIS A 874  ? 0.3072 0.2719 0.3305 0.0544  0.0116  -0.0107 872  HIS A CD2 
6514  C CE1 . HIS A 874  ? 0.3157 0.2731 0.3470 0.0582  0.0057  -0.0162 872  HIS A CE1 
6515  N NE2 . HIS A 874  ? 0.3130 0.2779 0.3405 0.0588  0.0098  -0.0152 872  HIS A NE2 
6516  N N   . ILE A 875  ? 0.2211 0.1625 0.2464 0.0496  0.0003  -0.0140 873  ILE A N   
6517  C CA  . ILE A 875  ? 0.2289 0.1685 0.2535 0.0526  -0.0015 -0.0197 873  ILE A CA  
6518  C C   . ILE A 875  ? 0.2444 0.1876 0.2718 0.0581  -0.0016 -0.0249 873  ILE A C   
6519  O O   . ILE A 875  ? 0.2584 0.2004 0.2914 0.0593  -0.0032 -0.0247 873  ILE A O   
6520  C CB  . ILE A 875  ? 0.2513 0.1828 0.2799 0.0508  -0.0063 -0.0199 873  ILE A CB  
6521  C CG1 . ILE A 875  ? 0.3119 0.2411 0.3369 0.0460  -0.0061 -0.0160 873  ILE A CG1 
6522  C CG2 . ILE A 875  ? 0.2717 0.2014 0.3011 0.0545  -0.0087 -0.0266 873  ILE A CG2 
6523  C CD1 . ILE A 875  ? 0.3182 0.2487 0.3420 0.0418  -0.0041 -0.0097 873  ILE A CD1 
6524  N N   . GLY A 876  ? 0.2181 0.1660 0.2416 0.0615  -0.0001 -0.0296 874  GLY A N   
6525  C CA  . GLY A 876  ? 0.1982 0.1502 0.2241 0.0671  -0.0003 -0.0354 874  GLY A CA  
6526  C C   . GLY A 876  ? 0.2328 0.1918 0.2530 0.0703  0.0022  -0.0397 874  GLY A C   
6527  O O   . GLY A 876  ? 0.2304 0.1903 0.2450 0.0682  0.0037  -0.0383 874  GLY A O   
6528  N N   . ARG A 877  ? 0.2330 0.1974 0.2547 0.0756  0.0026  -0.0451 875  ARG A N   
6529  C CA  . ARG A 877  ? 0.2255 0.1985 0.2419 0.0791  0.0051  -0.0493 875  ARG A CA  
6530  C C   . ARG A 877  ? 0.2450 0.2248 0.2553 0.0765  0.0100  -0.0437 875  ARG A C   
6531  O O   . ARG A 877  ? 0.2370 0.2189 0.2485 0.0745  0.0123  -0.0387 875  ARG A O   
6532  C CB  . ARG A 877  ? 0.2428 0.2220 0.2622 0.0852  0.0052  -0.0553 875  ARG A CB  
6533  C CG  . ARG A 877  ? 0.2547 0.2414 0.2695 0.0897  0.0062  -0.0617 875  ARG A CG  
6534  C CD  . ARG A 877  ? 0.3142 0.3071 0.3327 0.0961  0.0058  -0.0685 875  ARG A CD  
6535  N NE  . ARG A 877  ? 0.3217 0.3253 0.3387 0.0974  0.0104  -0.0659 875  ARG A NE  
6536  C CZ  . ARG A 877  ? 0.3877 0.3992 0.4072 0.1028  0.0112  -0.0709 875  ARG A CZ  
6537  N NH1 . ARG A 877  ? 0.3908 0.3999 0.4143 0.1056  0.0074  -0.0775 875  ARG A NH1 
6538  N NH2 . ARG A 877  ? 0.3970 0.4189 0.4150 0.1034  0.0157  -0.0677 875  ARG A NH2 
6539  N N   . THR A 878  ? 0.2532 0.2364 0.2573 0.0764  0.0115  -0.0445 876  THR A N   
6540  C CA  . THR A 878  ? 0.2391 0.2262 0.2381 0.0728  0.0152  -0.0384 876  THR A CA  
6541  C C   . THR A 878  ? 0.2624 0.2610 0.2586 0.0750  0.0196  -0.0374 876  THR A C   
6542  O O   . THR A 878  ? 0.2721 0.2751 0.2638 0.0727  0.0225  -0.0331 876  THR A O   
6543  C CB  . THR A 878  ? 0.2397 0.2244 0.2337 0.0710  0.0146  -0.0386 876  THR A CB  
6544  O OG1 . THR A 878  ? 0.2973 0.2854 0.2892 0.0753  0.0135  -0.0454 876  THR A OG1 
6545  C CG2 . THR A 878  ? 0.2651 0.2389 0.2616 0.0671  0.0112  -0.0369 876  THR A CG2 
6546  N N   . ASP A 879  ? 0.2618 0.2660 0.2612 0.0793  0.0201  -0.0409 877  ASP A N   
6547  C CA  . ASP A 879  ? 0.2926 0.3084 0.2899 0.0809  0.0244  -0.0389 877  ASP A CA  
6548  C C   . ASP A 879  ? 0.2725 0.2886 0.2734 0.0781  0.0261  -0.0329 877  ASP A C   
6549  O O   . ASP A 879  ? 0.2572 0.2822 0.2591 0.0801  0.0289  -0.0321 877  ASP A O   
6550  C CB  . ASP A 879  ? 0.2785 0.3026 0.2765 0.0873  0.0246  -0.0460 877  ASP A CB  
6551  C CG  . ASP A 879  ? 0.3178 0.3377 0.3229 0.0901  0.0216  -0.0501 877  ASP A CG  
6552  O OD1 . ASP A 879  ? 0.3126 0.3216 0.3218 0.0876  0.0183  -0.0491 877  ASP A OD1 
6553  O OD2 . ASP A 879  ? 0.3398 0.3680 0.3466 0.0951  0.0226  -0.0545 877  ASP A OD2 
6554  N N   . ARG A 880  ? 0.2341 0.2411 0.2369 0.0734  0.0245  -0.0286 878  ARG A N   
6555  C CA  . ARG A 880  ? 0.2151 0.2219 0.2206 0.0700  0.0261  -0.0225 878  ARG A CA  
6556  C C   . ARG A 880  ? 0.1942 0.1966 0.1967 0.0647  0.0266  -0.0170 878  ARG A C   
6557  O O   . ARG A 880  ? 0.2273 0.2218 0.2289 0.0627  0.0241  -0.0176 878  ARG A O   
6558  C CB  . ARG A 880  ? 0.2417 0.2420 0.2536 0.0700  0.0232  -0.0230 878  ARG A CB  
6559  C CG  . ARG A 880  ? 0.3096 0.3148 0.3258 0.0752  0.0228  -0.0278 878  ARG A CG  
6560  C CD  . ARG A 880  ? 0.3519 0.3493 0.3747 0.0750  0.0192  -0.0281 878  ARG A CD  
6561  N NE  . ARG A 880  ? 0.4947 0.4960 0.5222 0.0804  0.0183  -0.0334 878  ARG A NE  
6562  C CZ  . ARG A 880  ? 0.5398 0.5450 0.5716 0.0815  0.0193  -0.0319 878  ARG A CZ  
6563  N NH1 . ARG A 880  ? 0.5691 0.5751 0.6015 0.0775  0.0212  -0.0254 878  ARG A NH1 
6564  N NH2 . ARG A 880  ? 0.5381 0.5469 0.5742 0.0868  0.0183  -0.0373 878  ARG A NH2 
6565  N N   . LEU A 881  ? 0.1943 0.2017 0.1957 0.0623  0.0298  -0.0117 879  LEU A N   
6566  C CA  . LEU A 881  ? 0.2162 0.2199 0.2155 0.0573  0.0303  -0.0065 879  LEU A CA  
6567  C C   . LEU A 881  ? 0.1903 0.1844 0.1925 0.0540  0.0274  -0.0050 879  LEU A C   
6568  O O   . LEU A 881  ? 0.2158 0.2048 0.2158 0.0506  0.0267  -0.0029 879  LEU A O   
6569  C CB  . LEU A 881  ? 0.2161 0.2266 0.2156 0.0555  0.0336  -0.0012 879  LEU A CB  
6570  C CG  . LEU A 881  ? 0.2280 0.2357 0.2258 0.0507  0.0344  0.0041  879  LEU A CG  
6571  C CD1 . LEU A 881  ? 0.2250 0.2335 0.2175 0.0505  0.0349  0.0038  879  LEU A CD1 
6572  C CD2 . LEU A 881  ? 0.2505 0.2643 0.2506 0.0490  0.0370  0.0091  879  LEU A CD2 
6573  N N   . SER A 882  ? 0.1969 0.1887 0.2040 0.0549  0.0258  -0.0059 880  SER A N   
6574  C CA  . SER A 882  ? 0.1891 0.1730 0.1991 0.0517  0.0232  -0.0038 880  SER A CA  
6575  C C   . SER A 882  ? 0.2227 0.1989 0.2323 0.0514  0.0198  -0.0066 880  SER A C   
6576  O O   . SER A 882  ? 0.2337 0.2038 0.2450 0.0483  0.0177  -0.0043 880  SER A O   
6577  C CB  . SER A 882  ? 0.2015 0.1857 0.2172 0.0528  0.0223  -0.0036 880  SER A CB  
6578  O OG  . SER A 882  ? 0.2590 0.2439 0.2770 0.0575  0.0208  -0.0089 880  SER A OG  
6579  N N   . VAL A 883  ? 0.2097 0.1865 0.2171 0.0545  0.0191  -0.0113 881  VAL A N   
6580  C CA  . VAL A 883  ? 0.2175 0.1869 0.2253 0.0542  0.0155  -0.0140 881  VAL A CA  
6581  C C   . VAL A 883  ? 0.2085 0.1753 0.2120 0.0506  0.0158  -0.0116 881  VAL A C   
6582  O O   . VAL A 883  ? 0.2395 0.2107 0.2383 0.0508  0.0183  -0.0112 881  VAL A O   
6583  C CB  . VAL A 883  ? 0.2208 0.1918 0.2286 0.0591  0.0142  -0.0206 881  VAL A CB  
6584  C CG1 . VAL A 883  ? 0.2434 0.2072 0.2508 0.0583  0.0108  -0.0231 881  VAL A CG1 
6585  C CG2 . VAL A 883  ? 0.2147 0.1863 0.2281 0.0625  0.0129  -0.0233 881  VAL A CG2 
6586  N N   . ASP A 884  ? 0.1945 0.1543 0.1996 0.0475  0.0133  -0.0099 882  ASP A N   
6587  C CA  . ASP A 884  ? 0.2158 0.1727 0.2174 0.0441  0.0131  -0.0079 882  ASP A CA  
6588  C C   . ASP A 884  ? 0.2293 0.1826 0.2297 0.0451  0.0106  -0.0118 882  ASP A C   
6589  O O   . ASP A 884  ? 0.2470 0.2006 0.2432 0.0440  0.0114  -0.0116 882  ASP A O   
6590  C CB  . ASP A 884  ? 0.2000 0.1524 0.2040 0.0399  0.0118  -0.0036 882  ASP A CB  
6591  C CG  . ASP A 884  ? 0.1990 0.1549 0.2044 0.0386  0.0140  0.0001  882  ASP A CG  
6592  O OD1 . ASP A 884  ? 0.2096 0.1701 0.2120 0.0381  0.0169  0.0017  882  ASP A OD1 
6593  O OD2 . ASP A 884  ? 0.2220 0.1760 0.2316 0.0381  0.0125  0.0013  882  ASP A OD2 
6594  N N   . VAL A 885  ? 0.1964 0.1458 0.2008 0.0471  0.0074  -0.0151 883  VAL A N   
6595  C CA  . VAL A 885  ? 0.2019 0.1471 0.2065 0.0480  0.0044  -0.0190 883  VAL A CA  
6596  C C   . VAL A 885  ? 0.2101 0.1564 0.2171 0.0530  0.0029  -0.0249 883  VAL A C   
6597  O O   . VAL A 885  ? 0.2220 0.1673 0.2340 0.0545  0.0016  -0.0256 883  VAL A O   
6598  C CB  . VAL A 885  ? 0.2440 0.1817 0.2523 0.0445  0.0008  -0.0167 883  VAL A CB  
6599  C CG1 . VAL A 885  ? 0.2563 0.1896 0.2654 0.0453  -0.0026 -0.0206 883  VAL A CG1 
6600  C CG2 . VAL A 885  ? 0.2309 0.1684 0.2368 0.0398  0.0024  -0.0112 883  VAL A CG2 
6601  N N   . GLY A 886  ? 0.2063 0.1550 0.2099 0.0556  0.0029  -0.0295 884  GLY A N   
6602  C CA  . GLY A 886  ? 0.2010 0.1515 0.2063 0.0608  0.0014  -0.0361 884  GLY A CA  
6603  C C   . GLY A 886  ? 0.2063 0.1495 0.2157 0.0614  -0.0036 -0.0402 884  GLY A C   
6604  O O   . GLY A 886  ? 0.2290 0.1654 0.2410 0.0576  -0.0061 -0.0372 884  GLY A O   
6605  N N   . PRO A 887  ? 0.2130 0.1579 0.2231 0.0661  -0.0052 -0.0472 885  PRO A N   
6606  C CA  . PRO A 887  ? 0.2002 0.1381 0.2149 0.0670  -0.0104 -0.0518 885  PRO A CA  
6607  C C   . PRO A 887  ? 0.2168 0.1526 0.2278 0.0650  -0.0114 -0.0523 885  PRO A C   
6608  O O   . PRO A 887  ? 0.2210 0.1617 0.2253 0.0639  -0.0082 -0.0505 885  PRO A O   
6609  C CB  . PRO A 887  ? 0.2294 0.1716 0.2455 0.0733  -0.0111 -0.0596 885  PRO A CB  
6610  C CG  . PRO A 887  ? 0.2689 0.2216 0.2777 0.0751  -0.0060 -0.0595 885  PRO A CG  
6611  C CD  . PRO A 887  ? 0.2220 0.1761 0.2289 0.0709  -0.0024 -0.0513 885  PRO A CD  
6612  N N   . VAL A 888  ? 0.2386 0.1669 0.2543 0.0643  -0.0163 -0.0548 886  VAL A N   
6613  C CA  . VAL A 888  ? 0.2273 0.1541 0.2401 0.0636  -0.0180 -0.0573 886  VAL A CA  
6614  C C   . VAL A 888  ? 0.2534 0.1843 0.2651 0.0694  -0.0191 -0.0659 886  VAL A C   
6615  O O   . VAL A 888  ? 0.2410 0.1743 0.2556 0.0736  -0.0193 -0.0701 886  VAL A O   
6616  C CB  . VAL A 888  ? 0.2309 0.1484 0.2493 0.0599  -0.0228 -0.0556 886  VAL A CB  
6617  C CG1 . VAL A 888  ? 0.2567 0.1722 0.2751 0.0543  -0.0211 -0.0470 886  VAL A CG1 
6618  C CG2 . VAL A 888  ? 0.2627 0.1743 0.2900 0.0622  -0.0276 -0.0594 886  VAL A CG2 
6619  N N   . ILE A 889  ? 0.2538 0.1859 0.2613 0.0696  -0.0197 -0.0690 887  ILE A N   
6620  C CA  . ILE A 889  ? 0.2413 0.1806 0.2451 0.0750  -0.0192 -0.0763 887  ILE A CA  
6621  C C   . ILE A 889  ? 0.2767 0.2138 0.2867 0.0784  -0.0236 -0.0835 887  ILE A C   
6622  O O   . ILE A 889  ? 0.2793 0.2240 0.2877 0.0824  -0.0224 -0.0880 887  ILE A O   
6623  C CB  . ILE A 889  ? 0.2504 0.1923 0.2477 0.0738  -0.0185 -0.0767 887  ILE A CB  
6624  C CG1 . ILE A 889  ? 0.2825 0.2338 0.2746 0.0792  -0.0171 -0.0834 887  ILE A CG1 
6625  C CG2 . ILE A 889  ? 0.2600 0.1933 0.2613 0.0712  -0.0235 -0.0779 887  ILE A CG2 
6626  C CD1 . ILE A 889  ? 0.2698 0.2311 0.2566 0.0808  -0.0115 -0.0807 887  ILE A CD1 
6627  N N   . THR A 890  ? 0.2611 0.1894 0.2781 0.0756  -0.0284 -0.0830 888  THR A N   
6628  C CA  . THR A 890  ? 0.2697 0.1968 0.2927 0.0772  -0.0327 -0.0882 888  THR A CA  
6629  C C   . THR A 890  ? 0.2696 0.1877 0.3017 0.0740  -0.0367 -0.0849 888  THR A C   
6630  O O   . THR A 890  ? 0.2712 0.1837 0.3046 0.0699  -0.0367 -0.0786 888  THR A O   
6631  C CB  . THR A 890  ? 0.3019 0.2291 0.3237 0.0773  -0.0358 -0.0930 888  THR A CB  
6632  O OG1 . THR A 890  ? 0.3028 0.2228 0.3257 0.0727  -0.0377 -0.0889 888  THR A OG1 
6633  C CG2 . THR A 890  ? 0.3357 0.2727 0.3488 0.0806  -0.0324 -0.0967 888  THR A CG2 
6634  N N   . SER A 891  ? 0.2984 0.2154 0.3367 0.0758  -0.0404 -0.0891 889  SER A N   
6635  C CA  A SER A 891  ? 0.2970 0.2059 0.3444 0.0727  -0.0448 -0.0860 889  SER A CA  
6636  C CA  B SER A 891  ? 0.2969 0.2058 0.3443 0.0727  -0.0449 -0.0862 889  SER A CA  
6637  C C   . SER A 891  ? 0.3099 0.2124 0.3594 0.0683  -0.0482 -0.0837 889  SER A C   
6638  O O   . SER A 891  ? 0.3143 0.2105 0.3690 0.0641  -0.0502 -0.0779 889  SER A O   
6639  C CB  A SER A 891  ? 0.3266 0.2360 0.3803 0.0758  -0.0483 -0.0915 889  SER A CB  
6640  C CB  B SER A 891  ? 0.3265 0.2360 0.3802 0.0759  -0.0485 -0.0919 889  SER A CB  
6641  O OG  A SER A 891  ? 0.3342 0.2457 0.3872 0.0778  -0.0509 -0.0981 889  SER A OG  
6642  O OG  B SER A 891  ? 0.3254 0.2406 0.3781 0.0798  -0.0456 -0.0938 889  SER A OG  
6643  N N   . GLU A 892  ? 0.3019 0.2066 0.3476 0.0691  -0.0490 -0.0879 890  GLU A N   
6644  C CA  . GLU A 892  ? 0.3081 0.2073 0.3558 0.0650  -0.0521 -0.0858 890  GLU A CA  
6645  C C   . GLU A 892  ? 0.3062 0.2030 0.3503 0.0609  -0.0494 -0.0785 890  GLU A C   
6646  O O   . GLU A 892  ? 0.3180 0.2088 0.3666 0.0563  -0.0519 -0.0736 890  GLU A O   
6647  C CB  . GLU A 892  ? 0.3343 0.2370 0.3782 0.0669  -0.0533 -0.0920 890  GLU A CB  
6648  C CG  . GLU A 892  ? 0.4241 0.3309 0.4703 0.0715  -0.0557 -0.0999 890  GLU A CG  
6649  C CD  . GLU A 892  ? 0.4422 0.3582 0.4814 0.0764  -0.0511 -0.1036 890  GLU A CD  
6650  O OE1 . GLU A 892  ? 0.4211 0.3387 0.4616 0.0780  -0.0491 -0.1025 890  GLU A OE1 
6651  O OE2 . GLU A 892  ? 0.6031 0.5254 0.6357 0.0785  -0.0494 -0.1074 890  GLU A OE2 
6652  N N   . ALA A 893  ? 0.2862 0.1880 0.3224 0.0625  -0.0443 -0.0778 891  ALA A N   
6653  C CA  . ALA A 893  ? 0.2738 0.1735 0.3068 0.0591  -0.0416 -0.0711 891  ALA A CA  
6654  C C   . ALA A 893  ? 0.2829 0.1780 0.3218 0.0561  -0.0422 -0.0648 891  ALA A C   
6655  O O   . ALA A 893  ? 0.2959 0.1864 0.3368 0.0515  -0.0432 -0.0589 891  ALA A O   
6656  C CB  . ALA A 893  ? 0.2618 0.1683 0.2859 0.0619  -0.0361 -0.0717 891  ALA A CB  
6657  N N   . LYS A 894  ? 0.2636 0.1606 0.3051 0.0588  -0.0415 -0.0659 892  LYS A N   
6658  C CA  . LYS A 894  ? 0.3026 0.1959 0.3499 0.0563  -0.0422 -0.0601 892  LYS A CA  
6659  C C   . LYS A 894  ? 0.3174 0.2043 0.3725 0.0522  -0.0473 -0.0572 892  LYS A C   
6660  O O   . LYS A 894  ? 0.2990 0.1825 0.3566 0.0478  -0.0478 -0.0503 892  LYS A O   
6661  C CB  . LYS A 894  ? 0.3050 0.2015 0.3544 0.0604  -0.0414 -0.0630 892  LYS A CB  
6662  C CG  . LYS A 894  ? 0.2981 0.1911 0.3539 0.0582  -0.0425 -0.0576 892  LYS A CG  
6663  C CD  . LYS A 894  ? 0.3147 0.2114 0.3725 0.0626  -0.0416 -0.0608 892  LYS A CD  
6664  C CE  . LYS A 894  ? 0.3648 0.2578 0.4295 0.0604  -0.0433 -0.0555 892  LYS A CE  
6665  N NZ  . LYS A 894  ? 0.4493 0.3452 0.5172 0.0646  -0.0434 -0.0592 892  LYS A NZ  
6666  N N   . ASP A 895  ? 0.2984 0.1843 0.3575 0.0535  -0.0513 -0.0624 893  ASP A N   
6667  C CA  . ASP A 895  ? 0.3161 0.1963 0.3833 0.0499  -0.0564 -0.0598 893  ASP A CA  
6668  C C   . ASP A 895  ? 0.3172 0.1948 0.3833 0.0450  -0.0570 -0.0551 893  ASP A C   
6669  O O   . ASP A 895  ? 0.3029 0.1768 0.3742 0.0405  -0.0592 -0.0489 893  ASP A O   
6670  C CB  . ASP A 895  ? 0.3093 0.1893 0.3809 0.0526  -0.0607 -0.0670 893  ASP A CB  
6671  C CG  . ASP A 895  ? 0.4464 0.3290 0.5205 0.0572  -0.0608 -0.0716 893  ASP A CG  
6672  O OD1 . ASP A 895  ? 0.4917 0.3755 0.5653 0.0579  -0.0581 -0.0687 893  ASP A OD1 
6673  O OD2 . ASP A 895  ? 0.4975 0.3810 0.5742 0.0602  -0.0638 -0.0784 893  ASP A OD2 
6674  N N   . ASN A 896  ? 0.2864 0.1664 0.3456 0.0458  -0.0550 -0.0577 894  ASN A N   
6675  C CA  . ASN A 896  ? 0.3030 0.1807 0.3608 0.0414  -0.0554 -0.0537 894  ASN A CA  
6676  C C   . ASN A 896  ? 0.3293 0.2063 0.3858 0.0377  -0.0527 -0.0456 894  ASN A C   
6677  O O   . ASN A 896  ? 0.3211 0.1953 0.3812 0.0328  -0.0545 -0.0397 894  ASN A O   
6678  C CB  . ASN A 896  ? 0.3660 0.2471 0.4163 0.0436  -0.0535 -0.0586 894  ASN A CB  
6679  C CG  . ASN A 896  ? 0.4711 0.3502 0.5198 0.0394  -0.0540 -0.0550 894  ASN A CG  
6680  O OD1 . ASN A 896  ? 0.5239 0.4035 0.5678 0.0376  -0.0508 -0.0506 894  ASN A OD1 
6681  N ND2 . ASN A 896  ? 0.5150 0.3920 0.5677 0.0379  -0.0582 -0.0568 894  ASN A ND2 
6682  N N   . ILE A 897  ? 0.2926 0.1726 0.3441 0.0399  -0.0484 -0.0451 895  ILE A N   
6683  C CA  . ILE A 897  ? 0.3032 0.1829 0.3530 0.0367  -0.0458 -0.0377 895  ILE A CA  
6684  C C   . ILE A 897  ? 0.2890 0.1662 0.3462 0.0336  -0.0480 -0.0321 895  ILE A C   
6685  O O   . ILE A 897  ? 0.3079 0.1839 0.3667 0.0288  -0.0483 -0.0252 895  ILE A O   
6686  C CB  . ILE A 897  ? 0.2511 0.1372 0.2936 0.0394  -0.0401 -0.0381 895  ILE A CB  
6687  C CG1 . ILE A 897  ? 0.2882 0.1796 0.3223 0.0413  -0.0370 -0.0420 895  ILE A CG1 
6688  C CG2 . ILE A 897  ? 0.2944 0.1828 0.3351 0.0354  -0.0368 -0.0300 895  ILE A CG2 
6689  C CD1 . ILE A 897  ? 0.2852 0.1834 0.3133 0.0452  -0.0323 -0.0443 895  ILE A CD1 
6690  N N   . GLU A 898  ? 0.2850 0.1620 0.3469 0.0363  -0.0497 -0.0348 896  GLU A N   
6691  C CA  . GLU A 898  ? 0.2930 0.1680 0.3620 0.0337  -0.0519 -0.0295 896  GLU A CA  
6692  C C   . GLU A 898  ? 0.3193 0.1911 0.3945 0.0292  -0.0564 -0.0262 896  GLU A C   
6693  O O   . GLU A 898  ? 0.3085 0.1795 0.3876 0.0252  -0.0574 -0.0192 896  GLU A O   
6694  C CB  . GLU A 898  ? 0.3146 0.1900 0.3873 0.0378  -0.0530 -0.0337 896  GLU A CB  
6695  C CG  . GLU A 898  ? 0.3369 0.2160 0.4051 0.0412  -0.0486 -0.0346 896  GLU A CG  
6696  C CD  . GLU A 898  ? 0.3764 0.2566 0.4481 0.0456  -0.0495 -0.0393 896  GLU A CD  
6697  O OE1 . GLU A 898  ? 0.5192 0.3977 0.5959 0.0468  -0.0534 -0.0435 896  GLU A OE1 
6698  O OE2 . GLU A 898  ? 0.5399 0.4230 0.6099 0.0479  -0.0465 -0.0389 896  GLU A OE2 
6699  N N   . LYS A 899  ? 0.3178 0.1882 0.3942 0.0299  -0.0592 -0.0309 897  LYS A N   
6700  C CA  . LYS A 899  ? 0.3133 0.1810 0.3959 0.0256  -0.0634 -0.0275 897  LYS A CA  
6701  C C   . LYS A 899  ? 0.2973 0.1657 0.3771 0.0206  -0.0617 -0.0204 897  LYS A C   
6702  O O   . LYS A 899  ? 0.3106 0.1783 0.3958 0.0162  -0.0640 -0.0141 897  LYS A O   
6703  C CB  . LYS A 899  ? 0.3386 0.2051 0.4222 0.0274  -0.0664 -0.0342 897  LYS A CB  
6704  C CG  . LYS A 899  ? 0.4572 0.3225 0.5465 0.0311  -0.0699 -0.0401 897  LYS A CG  
6705  C CD  . LYS A 899  ? 0.5159 0.3805 0.6065 0.0327  -0.0731 -0.0467 897  LYS A CD  
6706  C CE  . LYS A 899  ? 0.5638 0.4280 0.6595 0.0369  -0.0763 -0.0532 897  LYS A CE  
6707  N NZ  . LYS A 899  ? 0.5900 0.4516 0.6941 0.0353  -0.0791 -0.0490 897  LYS A NZ  
6708  N N   . HIS A 900  ? 0.2579 0.1283 0.3298 0.0213  -0.0577 -0.0212 898  HIS A N   
6709  C CA  . HIS A 900  ? 0.2831 0.1547 0.3522 0.0167  -0.0559 -0.0147 898  HIS A CA  
6710  C C   . HIS A 900  ? 0.2668 0.1399 0.3373 0.0141  -0.0544 -0.0074 898  HIS A C   
6711  O O   . HIS A 900  ? 0.3012 0.1752 0.3746 0.0093  -0.0555 -0.0007 898  HIS A O   
6712  C CB  . HIS A 900  ? 0.2758 0.1491 0.3361 0.0185  -0.0520 -0.0174 898  HIS A CB  
6713  C CG  . HIS A 900  ? 0.2857 0.1619 0.3421 0.0143  -0.0492 -0.0108 898  HIS A CG  
6714  N ND1 . HIS A 900  ? 0.3195 0.1958 0.3767 0.0102  -0.0506 -0.0079 898  HIS A ND1 
6715  C CD2 . HIS A 900  ? 0.2803 0.1617 0.3314 0.0133  -0.0444 -0.0067 898  HIS A CD2 
6716  C CE1 . HIS A 900  ? 0.3321 0.2138 0.3846 0.0072  -0.0468 -0.0025 898  HIS A CE1 
6717  N NE2 . HIS A 900  ? 0.2817 0.1663 0.3305 0.0089  -0.0431 -0.0018 898  HIS A NE2 
6718  N N   . ILE A 901  ? 0.2586 0.1329 0.3270 0.0172  -0.0519 -0.0085 899  ILE A N   
6719  C CA  . ILE A 901  ? 0.2787 0.1549 0.3481 0.0149  -0.0504 -0.0019 899  ILE A CA  
6720  C C   . ILE A 901  ? 0.2987 0.1739 0.3762 0.0118  -0.0544 0.0026  899  ILE A C   
6721  O O   . ILE A 901  ? 0.3094 0.1868 0.3883 0.0075  -0.0543 0.0098  899  ILE A O   
6722  C CB  . ILE A 901  ? 0.2652 0.1425 0.3320 0.0192  -0.0476 -0.0046 899  ILE A CB  
6723  C CG1 . ILE A 901  ? 0.2672 0.1470 0.3256 0.0218  -0.0433 -0.0080 899  ILE A CG1 
6724  C CG2 . ILE A 901  ? 0.2595 0.1388 0.3280 0.0169  -0.0466 0.0021  899  ILE A CG2 
6725  C CD1 . ILE A 901  ? 0.2554 0.1380 0.3106 0.0264  -0.0403 -0.0119 899  ILE A CD1 
6726  N N   . GLU A 902  ? 0.3069 0.1794 0.3902 0.0140  -0.0580 -0.0017 900  GLU A N   
6727  C CA  . GLU A 902  ? 0.3104 0.1818 0.4021 0.0113  -0.0621 0.0025  900  GLU A CA  
6728  C C   . GLU A 902  ? 0.3087 0.1804 0.4036 0.0064  -0.0647 0.0070  900  GLU A C   
6729  O O   . GLU A 902  ? 0.3279 0.2009 0.4277 0.0026  -0.0665 0.0137  900  GLU A O   
6730  C CB  . GLU A 902  ? 0.3162 0.1846 0.4136 0.0151  -0.0657 -0.0035 900  GLU A CB  
6731  C CG  . GLU A 902  ? 0.4135 0.2826 0.5094 0.0195  -0.0636 -0.0069 900  GLU A CG  
6732  C CD  . GLU A 902  ? 0.4168 0.2884 0.5119 0.0176  -0.0612 -0.0002 900  GLU A CD  
6733  O OE1 . GLU A 902  ? 0.4542 0.3261 0.5549 0.0139  -0.0637 0.0060  900  GLU A OE1 
6734  O OE2 . GLU A 902  ? 0.4174 0.2911 0.5065 0.0198  -0.0570 -0.0011 900  GLU A OE2 
6735  N N   . ARG A 903  ? 0.3023 0.1731 0.3946 0.0064  -0.0648 0.0038  901  ARG A N   
6736  C CA  . ARG A 903  ? 0.3113 0.1828 0.4061 0.0016  -0.0668 0.0083  901  ARG A CA  
6737  C C   . ARG A 903  ? 0.3426 0.2186 0.4340 -0.0025 -0.0638 0.0161  901  ARG A C   
6738  O O   . ARG A 903  ? 0.3375 0.2157 0.4335 -0.0068 -0.0657 0.0226  901  ARG A O   
6739  C CB  . ARG A 903  ? 0.3579 0.2280 0.4496 0.0026  -0.0671 0.0031  901  ARG A CB  
6740  N N   . MET A 904  ? 0.3090 0.1868 0.3925 -0.0012 -0.0591 0.0155  902  MET A N   
6741  C CA  . MET A 904  ? 0.2913 0.1738 0.3713 -0.0047 -0.0561 0.0224  902  MET A CA  
6742  C C   . MET A 904  ? 0.3022 0.1871 0.3864 -0.0064 -0.0568 0.0280  902  MET A C   
6743  O O   . MET A 904  ? 0.3119 0.2011 0.3974 -0.0107 -0.0568 0.0349  902  MET A O   
6744  C CB  . MET A 904  ? 0.2631 0.1467 0.3347 -0.0024 -0.0513 0.0201  902  MET A CB  
6745  C CG  . MET A 904  ? 0.2805 0.1625 0.3472 -0.0009 -0.0502 0.0152  902  MET A CG  
6746  S SD  . MET A 904  ? 0.3837 0.2681 0.4506 -0.0063 -0.0511 0.0199  902  MET A SD  
6747  C CE  . MET A 904  ? 0.3840 0.2642 0.4572 -0.0057 -0.0563 0.0153  902  MET A CE  
6748  N N   . ARG A 905  ? 0.2857 0.1684 0.3718 -0.0030 -0.0572 0.0251  903  ARG A N   
6749  C CA  . ARG A 905  ? 0.2911 0.1759 0.3813 -0.0043 -0.0581 0.0302  903  ARG A CA  
6750  C C   . ARG A 905  ? 0.3147 0.1998 0.4131 -0.0079 -0.0627 0.0346  903  ARG A C   
6751  O O   . ARG A 905  ? 0.3339 0.2234 0.4345 -0.0115 -0.0630 0.0416  903  ARG A O   
6752  C CB  . ARG A 905  ? 0.3428 0.2249 0.4343 0.0003  -0.0582 0.0257  903  ARG A CB  
6753  C CG  . ARG A 905  ? 0.3619 0.2467 0.4552 -0.0005 -0.0576 0.0305  903  ARG A CG  
6754  C CD  . ARG A 905  ? 0.3480 0.2300 0.4443 0.0039  -0.0586 0.0260  903  ARG A CD  
6755  N NE  . ARG A 905  ? 0.3453 0.2255 0.4364 0.0087  -0.0560 0.0188  903  ARG A NE  
6756  C CZ  . ARG A 905  ? 0.3247 0.2068 0.4101 0.0107  -0.0519 0.0183  903  ARG A CZ  
6757  N NH1 . ARG A 905  ? 0.3156 0.2016 0.3994 0.0083  -0.0499 0.0243  903  ARG A NH1 
6758  N NH2 . ARG A 905  ? 0.3939 0.2748 0.4756 0.0154  -0.0499 0.0116  903  ARG A NH2 
6759  N N   . GLY A 906  ? 0.3289 0.2099 0.4322 -0.0069 -0.0664 0.0305  904  GLY A N   
6760  C CA  . GLY A 906  ? 0.3344 0.2153 0.4462 -0.0101 -0.0712 0.0344  904  GLY A CA  
6761  C C   . GLY A 906  ? 0.3563 0.2418 0.4677 -0.0151 -0.0710 0.0408  904  GLY A C   
6762  O O   . GLY A 906  ? 0.3834 0.2712 0.5015 -0.0186 -0.0741 0.0466  904  GLY A O   
6763  N N   . LEU A 907  ? 0.3558 0.2432 0.4599 -0.0157 -0.0674 0.0401  905  LEU A N   
6764  C CA  . LEU A 907  ? 0.3323 0.2250 0.4353 -0.0204 -0.0667 0.0461  905  LEU A CA  
6765  C C   . LEU A 907  ? 0.3403 0.2397 0.4401 -0.0228 -0.0636 0.0527  905  LEU A C   
6766  O O   . LEU A 907  ? 0.4165 0.3216 0.5150 -0.0267 -0.0626 0.0579  905  LEU A O   
6767  C CB  . LEU A 907  ? 0.3321 0.2242 0.4289 -0.0200 -0.0643 0.0425  905  LEU A CB  
6768  C CG  . LEU A 907  ? 0.3757 0.2624 0.4753 -0.0181 -0.0674 0.0364  905  LEU A CG  
6769  C CD1 . LEU A 907  ? 0.4019 0.2880 0.4943 -0.0172 -0.0646 0.0325  905  LEU A CD1 
6770  C CD2 . LEU A 907  ? 0.4435 0.3309 0.5514 -0.0217 -0.0721 0.0402  905  LEU A CD2 
6771  N N   . GLY A 908  ? 0.3347 0.2340 0.4333 -0.0207 -0.0622 0.0524  906  GLY A N   
6772  C CA  . GLY A 908  ? 0.3339 0.2396 0.4300 -0.0228 -0.0597 0.0583  906  GLY A CA  
6773  C C   . GLY A 908  ? 0.3206 0.2289 0.4076 -0.0219 -0.0545 0.0573  906  GLY A C   
6774  O O   . GLY A 908  ? 0.3330 0.2476 0.4173 -0.0240 -0.0523 0.0622  906  GLY A O   
6775  N N   . ARG A 909  ? 0.2870 0.1910 0.3693 -0.0189 -0.0527 0.0511  907  ARG A N   
6776  C CA  . ARG A 909  ? 0.2672 0.1734 0.3413 -0.0179 -0.0480 0.0501  907  ARG A CA  
6777  C C   . ARG A 909  ? 0.3176 0.2231 0.3898 -0.0149 -0.0461 0.0488  907  ARG A C   
6778  O O   . ARG A 909  ? 0.3226 0.2236 0.3983 -0.0118 -0.0479 0.0454  907  ARG A O   
6779  C CB  . ARG A 909  ? 0.2891 0.1911 0.3593 -0.0158 -0.0470 0.0442  907  ARG A CB  
6780  C CG  . ARG A 909  ? 0.3482 0.2498 0.4215 -0.0183 -0.0497 0.0447  907  ARG A CG  
6781  C CD  . ARG A 909  ? 0.4286 0.3344 0.4967 -0.0209 -0.0470 0.0467  907  ARG A CD  
6782  N NE  . ARG A 909  ? 0.4712 0.3785 0.5429 -0.0243 -0.0495 0.0490  907  ARG A NE  
6783  C CZ  . ARG A 909  ? 0.5503 0.4529 0.6247 -0.0234 -0.0522 0.0449  907  ARG A CZ  
6784  N NH1 . ARG A 909  ? 0.5789 0.4750 0.6527 -0.0191 -0.0529 0.0379  907  ARG A NH1 
6785  N NH2 . ARG A 909  ? 0.5743 0.4793 0.6521 -0.0269 -0.0543 0.0478  907  ARG A NH2 
6786  N N   . LYS A 910  ? 0.2460 0.1563 0.3128 -0.0157 -0.0424 0.0514  908  LYS A N   
6787  C CA  . LYS A 910  ? 0.2575 0.1680 0.3225 -0.0132 -0.0405 0.0507  908  LYS A CA  
6788  C C   . LYS A 910  ? 0.2528 0.1578 0.3147 -0.0084 -0.0390 0.0437  908  LYS A C   
6789  O O   . LYS A 910  ? 0.2520 0.1584 0.3079 -0.0076 -0.0361 0.0404  908  LYS A O   
6790  C CB  . LYS A 910  ? 0.2631 0.1806 0.3232 -0.0154 -0.0372 0.0551  908  LYS A CB  
6791  C CG  . LYS A 910  ? 0.3602 0.2845 0.4232 -0.0196 -0.0384 0.0620  908  LYS A CG  
6792  C CD  . LYS A 910  ? 0.3353 0.2669 0.3931 -0.0211 -0.0351 0.0654  908  LYS A CD  
6793  C CE  . LYS A 910  ? 0.3875 0.3174 0.4436 -0.0179 -0.0334 0.0635  908  LYS A CE  
6794  N NZ  . LYS A 910  ? 0.4865 0.4242 0.5395 -0.0198 -0.0311 0.0675  908  LYS A NZ  
6795  N N   . VAL A 911  ? 0.2421 0.1435 0.3071 -0.0050 -0.0402 0.0406  909  VAL A N   
6796  C CA  . VAL A 911  ? 0.2433 0.1404 0.3061 0.0000  -0.0390 0.0338  909  VAL A CA  
6797  C C   . VAL A 911  ? 0.2569 0.1566 0.3178 0.0023  -0.0364 0.0335  909  VAL A C   
6798  O O   . VAL A 911  ? 0.2803 0.1797 0.3461 0.0021  -0.0384 0.0364  909  VAL A O   
6799  C CB  . VAL A 911  ? 0.2319 0.1239 0.2999 0.0025  -0.0426 0.0288  909  VAL A CB  
6800  C CG1 . VAL A 911  ? 0.2655 0.1544 0.3310 0.0080  -0.0412 0.0215  909  VAL A CG1 
6801  C CG2 . VAL A 911  ? 0.2579 0.1486 0.3274 0.0001  -0.0449 0.0287  909  VAL A CG2 
6802  N N   . GLU A 912  ? 0.2408 0.1442 0.2943 0.0043  -0.0318 0.0301  910  GLU A N   
6803  C CA  . GLU A 912  ? 0.2300 0.1361 0.2813 0.0068  -0.0290 0.0292  910  GLU A CA  
6804  C C   . GLU A 912  ? 0.2344 0.1384 0.2842 0.0118  -0.0279 0.0221  910  GLU A C   
6805  O O   . GLU A 912  ? 0.2311 0.1353 0.2763 0.0129  -0.0262 0.0182  910  GLU A O   
6806  C CB  . GLU A 912  ? 0.2261 0.1390 0.2706 0.0049  -0.0245 0.0313  910  GLU A CB  
6807  C CG  . GLU A 912  ? 0.2497 0.1658 0.2928 0.0065  -0.0220 0.0316  910  GLU A CG  
6808  C CD  . GLU A 912  ? 0.2844 0.2017 0.3322 0.0043  -0.0241 0.0373  910  GLU A CD  
6809  O OE1 . GLU A 912  ? 0.2967 0.2138 0.3479 0.0009  -0.0269 0.0418  910  GLU A OE1 
6810  O OE2 . GLU A 912  ? 0.3121 0.2311 0.3605 0.0060  -0.0230 0.0374  910  GLU A OE2 
6811  N N   . GLN A 913  ? 0.2308 0.1332 0.2843 0.0149  -0.0288 0.0205  911  GLN A N   
6812  C CA  . GLN A 913  ? 0.2409 0.1423 0.2931 0.0199  -0.0277 0.0138  911  GLN A CA  
6813  C C   . GLN A 913  ? 0.2584 0.1630 0.3105 0.0223  -0.0255 0.0137  911  GLN A C   
6814  O O   . GLN A 913  ? 0.2831 0.1877 0.3395 0.0210  -0.0269 0.0179  911  GLN A O   
6815  C CB  . GLN A 913  ? 0.2627 0.1578 0.3217 0.0224  -0.0323 0.0100  911  GLN A CB  
6816  C CG  . GLN A 913  ? 0.2890 0.1806 0.3488 0.0205  -0.0349 0.0092  911  GLN A CG  
6817  C CD  . GLN A 913  ? 0.3092 0.1947 0.3750 0.0238  -0.0393 0.0039  911  GLN A CD  
6818  O OE1 . GLN A 913  ? 0.3080 0.1922 0.3800 0.0234  -0.0423 0.0050  911  GLN A OE1 
6819  N NE2 . GLN A 913  ? 0.2767 0.1620 0.3389 0.0263  -0.0386 -0.0022 911  GLN A NE2 
6820  N N   . ILE A 914  ? 0.2923 0.1999 0.3399 0.0257  -0.0221 0.0092  912  ILE A N   
6821  C CA  . ILE A 914  ? 0.2811 0.1916 0.3293 0.0284  -0.0202 0.0085  912  ILE A CA  
6822  C C   . ILE A 914  ? 0.3263 0.2330 0.3810 0.0325  -0.0235 0.0044  912  ILE A C   
6823  O O   . ILE A 914  ? 0.3244 0.2272 0.3810 0.0343  -0.0260 0.0002  912  ILE A O   
6824  C CB  . ILE A 914  ? 0.3364 0.2526 0.3777 0.0301  -0.0152 0.0061  912  ILE A CB  
6825  C CG1 . ILE A 914  ? 0.3537 0.2694 0.3926 0.0338  -0.0148 -0.0002 912  ILE A CG1 
6826  C CG2 . ILE A 914  ? 0.3456 0.2647 0.3813 0.0262  -0.0126 0.0096  912  ILE A CG2 
6827  C CD1 . ILE A 914  ? 0.4358 0.3541 0.4758 0.0387  -0.0136 -0.0045 912  ILE A CD1 
6828  N N   . GLY A 915  ? 0.3365 0.2443 0.3951 0.0340  -0.0238 0.0056  913  GLY A N   
6829  C CA  . GLY A 915  ? 0.3453 0.2501 0.4103 0.0384  -0.0267 0.0014  913  GLY A CA  
6830  C C   . GLY A 915  ? 0.3663 0.2750 0.4276 0.0432  -0.0236 -0.0051 913  GLY A C   
6831  O O   . GLY A 915  ? 0.4379 0.3526 0.4935 0.0434  -0.0191 -0.0046 913  GLY A O   
6832  N N   . LEU A 916  ? 0.3384 0.2440 0.4030 0.0472  -0.0263 -0.0112 914  LEU A N   
6833  C CA  . LEU A 916  ? 0.3522 0.2621 0.4137 0.0523  -0.0238 -0.0179 914  LEU A CA  
6834  C C   . LEU A 916  ? 0.3815 0.2933 0.4482 0.0565  -0.0242 -0.0201 914  LEU A C   
6835  O O   . LEU A 916  ? 0.3877 0.2947 0.4622 0.0569  -0.0284 -0.0193 914  LEU A O   
6836  C CB  . LEU A 916  ? 0.3850 0.2915 0.4469 0.0547  -0.0264 -0.0241 914  LEU A CB  
6837  C CG  . LEU A 916  ? 0.3827 0.2885 0.4388 0.0513  -0.0255 -0.0230 914  LEU A CG  
6838  C CD1 . LEU A 916  ? 0.3791 0.2833 0.4346 0.0545  -0.0273 -0.0301 914  LEU A CD1 
6839  C CD2 . LEU A 916  ? 0.4073 0.3198 0.4552 0.0495  -0.0199 -0.0202 914  LEU A CD2 
6840  N N   . ALA A 917  ? 0.3593 0.2784 0.4218 0.0595  -0.0200 -0.0227 915  ALA A N   
6841  C CA  . ALA A 917  ? 0.3804 0.3024 0.4474 0.0640  -0.0200 -0.0256 915  ALA A CA  
6842  C C   . ALA A 917  ? 0.4008 0.3201 0.4726 0.0692  -0.0235 -0.0334 915  ALA A C   
6843  O O   . ALA A 917  ? 0.3643 0.2817 0.4338 0.0700  -0.0246 -0.0376 915  ALA A O   
6844  C CB  . ALA A 917  ? 0.3997 0.3310 0.4610 0.0656  -0.0144 -0.0259 915  ALA A CB  
6845  N N   . SER A 918  ? 0.3992 0.3187 0.4777 0.0728  -0.0254 -0.0356 916  SER A N   
6846  C CA  . SER A 918  ? 0.3941 0.3131 0.4754 0.0759  -0.0280 -0.0419 916  SER A CA  
6847  C C   . SER A 918  ? 0.3787 0.3042 0.4546 0.0803  -0.0251 -0.0491 916  SER A C   
6848  O O   . SER A 918  ? 0.3566 0.2811 0.4329 0.0819  -0.0274 -0.0545 916  SER A O   
6849  C CB  . SER A 918  ? 0.4277 0.3478 0.5156 0.0781  -0.0294 -0.0421 916  SER A CB  
6850  O OG  . SER A 918  ? 0.5277 0.4547 0.6142 0.0805  -0.0254 -0.0412 916  SER A OG  
6851  N N   . GLU A 919  ? 0.4191 0.3517 0.4899 0.0822  -0.0204 -0.0490 917  GLU A N   
6852  C CA  . GLU A 919  ? 0.3863 0.3266 0.4512 0.0861  -0.0172 -0.0549 917  GLU A CA  
6853  C C   . GLU A 919  ? 0.3644 0.3019 0.4245 0.0848  -0.0181 -0.0572 917  GLU A C   
6854  O O   . GLU A 919  ? 0.3802 0.3231 0.4366 0.0879  -0.0169 -0.0630 917  GLU A O   
6855  C CB  . GLU A 919  ? 0.4007 0.3503 0.4592 0.0854  -0.0112 -0.0512 917  GLU A CB  
6856  C CG  . GLU A 919  ? 0.4741 0.4297 0.5363 0.0881  -0.0094 -0.0508 917  GLU A CG  
6857  C CD  . GLU A 919  ? 0.5235 0.4745 0.5904 0.0843  -0.0106 -0.0439 917  GLU A CD  
6858  O OE1 . GLU A 919  ? 0.5199 0.4641 0.5865 0.0792  -0.0124 -0.0389 917  GLU A OE1 
6859  O OE2 . GLU A 919  ? 0.5656 0.5206 0.6364 0.0864  -0.0098 -0.0434 917  GLU A OE2 
6860  N N   . THR A 920  ? 0.3634 0.2935 0.4235 0.0799  -0.0201 -0.0527 918  THR A N   
6861  C CA  . THR A 920  ? 0.3258 0.2534 0.3817 0.0787  -0.0210 -0.0548 918  THR A CA  
6862  C C   . THR A 920  ? 0.3050 0.2296 0.3644 0.0797  -0.0252 -0.0601 918  THR A C   
6863  O O   . THR A 920  ? 0.3080 0.2325 0.3638 0.0797  -0.0258 -0.0636 918  THR A O   
6864  C CB  . THR A 920  ? 0.3133 0.2354 0.3677 0.0720  -0.0215 -0.0474 918  THR A CB  
6865  O OG1 . THR A 920  ? 0.3349 0.2493 0.3973 0.0698  -0.0259 -0.0441 918  THR A OG1 
6866  C CG2 . THR A 920  ? 0.3198 0.2477 0.3681 0.0687  -0.0162 -0.0410 918  THR A CG2 
6867  N N   . GLY A 921  ? 0.3537 0.2762 0.4200 0.0807  -0.0282 -0.0612 919  GLY A N   
6868  C CA  . GLY A 921  ? 0.3778 0.2966 0.4485 0.0812  -0.0328 -0.0658 919  GLY A CA  
6869  C C   . GLY A 921  ? 0.3334 0.2581 0.4004 0.0854  -0.0321 -0.0738 919  GLY A C   
6870  O O   . GLY A 921  ? 0.3653 0.2869 0.4339 0.0853  -0.0357 -0.0776 919  GLY A O   
6871  N N   . VAL A 922  ? 0.3194 0.2533 0.3815 0.0892  -0.0276 -0.0763 920  VAL A N   
6872  C CA  . VAL A 922  ? 0.3299 0.2710 0.3880 0.0932  -0.0266 -0.0836 920  VAL A CA  
6873  C C   . VAL A 922  ? 0.2996 0.2423 0.3502 0.0921  -0.0250 -0.0844 920  VAL A C   
6874  O O   . VAL A 922  ? 0.3180 0.2665 0.3650 0.0950  -0.0247 -0.0902 920  VAL A O   
6875  C CB  . VAL A 922  ? 0.3081 0.2599 0.3638 0.0975  -0.0223 -0.0858 920  VAL A CB  
6876  C CG1 . VAL A 922  ? 0.3489 0.3001 0.4120 0.0997  -0.0244 -0.0873 920  VAL A CG1 
6877  C CG2 . VAL A 922  ? 0.3355 0.2909 0.3868 0.0963  -0.0173 -0.0800 920  VAL A CG2 
6878  N N   . GLY A 923  ? 0.3226 0.2607 0.3709 0.0881  -0.0242 -0.0787 921  GLY A N   
6879  C CA  . GLY A 923  ? 0.3248 0.2634 0.3666 0.0867  -0.0231 -0.0790 921  GLY A CA  
6880  C C   . GLY A 923  ? 0.2992 0.2279 0.3437 0.0820  -0.0269 -0.0757 921  GLY A C   
6881  O O   . GLY A 923  ? 0.2847 0.2067 0.3364 0.0801  -0.0310 -0.0742 921  GLY A O   
6882  N N   . THR A 924  ? 0.2744 0.2025 0.3133 0.0799  -0.0257 -0.0742 922  THR A N   
6883  C CA  . THR A 924  ? 0.2645 0.1842 0.3055 0.0753  -0.0291 -0.0711 922  THR A CA  
6884  C C   . THR A 924  ? 0.2629 0.1803 0.3010 0.0718  -0.0267 -0.0641 922  THR A C   
6885  O O   . THR A 924  ? 0.2548 0.1761 0.2856 0.0706  -0.0235 -0.0628 922  THR A O   
6886  C CB  . THR A 924  ? 0.2609 0.1813 0.2986 0.0757  -0.0307 -0.0760 922  THR A CB  
6887  O OG1 . THR A 924  ? 0.2626 0.1908 0.2917 0.0781  -0.0263 -0.0778 922  THR A OG1 
6888  C CG2 . THR A 924  ? 0.2997 0.2211 0.3418 0.0786  -0.0342 -0.0826 922  THR A CG2 
6889  N N   . PHE A 925  ? 0.2519 0.1644 0.2952 0.0689  -0.0279 -0.0585 923  PHE A N   
6890  C CA  . PHE A 925  ? 0.2435 0.1564 0.2835 0.0637  -0.0248 -0.0502 923  PHE A CA  
6891  C C   . PHE A 925  ? 0.2373 0.1422 0.2816 0.0586  -0.0285 -0.0453 923  PHE A C   
6892  O O   . PHE A 925  ? 0.2761 0.1749 0.3282 0.0586  -0.0332 -0.0461 923  PHE A O   
6893  C CB  . PHE A 925  ? 0.2456 0.1619 0.2869 0.0641  -0.0222 -0.0465 923  PHE A CB  
6894  C CG  . PHE A 925  ? 0.2258 0.1514 0.2622 0.0680  -0.0176 -0.0493 923  PHE A CG  
6895  C CD1 . PHE A 925  ? 0.2378 0.1663 0.2770 0.0738  -0.0186 -0.0562 923  PHE A CD1 
6896  C CD2 . PHE A 925  ? 0.2305 0.1622 0.2599 0.0659  -0.0125 -0.0449 923  PHE A CD2 
6897  C CE1 . PHE A 925  ? 0.2482 0.1862 0.2829 0.0774  -0.0143 -0.0584 923  PHE A CE1 
6898  C CE2 . PHE A 925  ? 0.2119 0.1525 0.2373 0.0692  -0.0085 -0.0468 923  PHE A CE2 
6899  C CZ  . PHE A 925  ? 0.2222 0.1663 0.2501 0.0749  -0.0092 -0.0534 923  PHE A CZ  
6900  N N   . VAL A 926  ? 0.2403 0.1461 0.2796 0.0541  -0.0261 -0.0399 924  VAL A N   
6901  C CA  . VAL A 926  ? 0.2415 0.1420 0.2839 0.0487  -0.0283 -0.0337 924  VAL A CA  
6902  C C   . VAL A 926  ? 0.2416 0.1457 0.2809 0.0454  -0.0244 -0.0268 924  VAL A C   
6903  O O   . VAL A 926  ? 0.2390 0.1488 0.2713 0.0453  -0.0200 -0.0260 924  VAL A O   
6904  C CB  . VAL A 926  ? 0.2401 0.1387 0.2796 0.0460  -0.0294 -0.0338 924  VAL A CB  
6905  C CG1 . VAL A 926  ? 0.2712 0.1659 0.3135 0.0403  -0.0311 -0.0270 924  VAL A CG1 
6906  C CG2 . VAL A 926  ? 0.2659 0.1607 0.3088 0.0492  -0.0337 -0.0411 924  VAL A CG2 
6907  N N   . PRO A 927  ? 0.2448 0.1461 0.2892 0.0427  -0.0261 -0.0216 925  PRO A N   
6908  C CA  . PRO A 927  ? 0.2485 0.1536 0.2898 0.0396  -0.0225 -0.0154 925  PRO A CA  
6909  C C   . PRO A 927  ? 0.2389 0.1450 0.2752 0.0353  -0.0209 -0.0117 925  PRO A C   
6910  O O   . PRO A 927  ? 0.2345 0.1366 0.2726 0.0331  -0.0238 -0.0112 925  PRO A O   
6911  C CB  . PRO A 927  ? 0.2937 0.1950 0.3424 0.0378  -0.0257 -0.0111 925  PRO A CB  
6912  C CG  . PRO A 927  ? 0.3150 0.2095 0.3703 0.0379  -0.0311 -0.0131 925  PRO A CG  
6913  C CD  . PRO A 927  ? 0.3040 0.1985 0.3574 0.0421  -0.0315 -0.0210 925  PRO A CD  
6914  N N   . PRO A 928  ? 0.2320 0.1433 0.2623 0.0341  -0.0164 -0.0091 926  PRO A N   
6915  C CA  . PRO A 928  ? 0.2225 0.1349 0.2491 0.0297  -0.0150 -0.0049 926  PRO A CA  
6916  C C   . PRO A 928  ? 0.2170 0.1259 0.2485 0.0257  -0.0182 0.0000  926  PRO A C   
6917  O O   . PRO A 928  ? 0.2098 0.1178 0.2459 0.0252  -0.0195 0.0027  926  PRO A O   
6918  C CB  . PRO A 928  ? 0.2154 0.1335 0.2374 0.0293  -0.0105 -0.0026 926  PRO A CB  
6919  C CG  . PRO A 928  ? 0.2464 0.1674 0.2670 0.0341  -0.0087 -0.0071 926  PRO A CG  
6920  C CD  . PRO A 928  ? 0.2200 0.1370 0.2469 0.0369  -0.0125 -0.0105 926  PRO A CD  
6921  N N   . THR A 929  ? 0.2069 0.1144 0.2374 0.0227  -0.0193 0.0014  927  THR A N   
6922  C CA  . THR A 929  ? 0.1981 0.1023 0.2336 0.0189  -0.0229 0.0057  927  THR A CA  
6923  C C   . THR A 929  ? 0.2194 0.1265 0.2510 0.0148  -0.0212 0.0095  927  THR A C   
6924  O O   . THR A 929  ? 0.2281 0.1370 0.2545 0.0152  -0.0192 0.0072  927  THR A O   
6925  C CB  . THR A 929  ? 0.2307 0.1291 0.2713 0.0200  -0.0275 0.0023  927  THR A CB  
6926  O OG1 . THR A 929  ? 0.2386 0.1346 0.2832 0.0242  -0.0291 -0.0017 927  THR A OG1 
6927  C CG2 . THR A 929  ? 0.2314 0.1265 0.2780 0.0158  -0.0314 0.0073  927  THR A CG2 
6928  N N   . ILE A 930  ? 0.2049 0.1129 0.2390 0.0110  -0.0222 0.0153  928  ILE A N   
6929  C CA  . ILE A 930  ? 0.1856 0.0968 0.2171 0.0070  -0.0212 0.0190  928  ILE A CA  
6930  C C   . ILE A 930  ? 0.2156 0.1238 0.2532 0.0038  -0.0255 0.0226  928  ILE A C   
6931  O O   . ILE A 930  ? 0.2337 0.1402 0.2769 0.0030  -0.0281 0.0257  928  ILE A O   
6932  C CB  . ILE A 930  ? 0.1975 0.1141 0.2261 0.0052  -0.0182 0.0229  928  ILE A CB  
6933  C CG1 . ILE A 930  ? 0.2105 0.1299 0.2336 0.0080  -0.0141 0.0198  928  ILE A CG1 
6934  C CG2 . ILE A 930  ? 0.1944 0.1147 0.2208 0.0011  -0.0175 0.0265  928  ILE A CG2 
6935  C CD1 . ILE A 930  ? 0.2453 0.1695 0.2668 0.0067  -0.0115 0.0231  928  ILE A CD1 
6936  N N   . ILE A 931  ? 0.1958 0.1037 0.2325 0.0019  -0.0264 0.0225  929  ILE A N   
6937  C CA  . ILE A 931  ? 0.1854 0.0910 0.2280 -0.0014 -0.0305 0.0261  929  ILE A CA  
6938  C C   . ILE A 931  ? 0.2265 0.1376 0.2662 -0.0054 -0.0289 0.0302  929  ILE A C   
6939  O O   . ILE A 931  ? 0.2171 0.1306 0.2515 -0.0051 -0.0264 0.0278  929  ILE A O   
6940  C CB  . ILE A 931  ? 0.2131 0.1131 0.2587 0.0001  -0.0338 0.0216  929  ILE A CB  
6941  C CG1 . ILE A 931  ? 0.2401 0.1354 0.2883 0.0047  -0.0352 0.0166  929  ILE A CG1 
6942  C CG2 . ILE A 931  ? 0.2502 0.1477 0.3027 -0.0037 -0.0383 0.0259  929  ILE A CG2 
6943  C CD1 . ILE A 931  ? 0.2781 0.1681 0.3292 0.0068  -0.0385 0.0112  929  ILE A CD1 
6944  N N   . GLU A 932  ? 0.2168 0.1302 0.2602 -0.0091 -0.0304 0.0365  930  GLU A N   
6945  C CA  . GLU A 932  ? 0.2152 0.1351 0.2562 -0.0129 -0.0289 0.0407  930  GLU A CA  
6946  C C   . GLU A 932  ? 0.2046 0.1229 0.2497 -0.0158 -0.0322 0.0425  930  GLU A C   
6947  O O   . GLU A 932  ? 0.2290 0.1437 0.2813 -0.0173 -0.0364 0.0455  930  GLU A O   
6948  C CB  . GLU A 932  ? 0.2281 0.1529 0.2701 -0.0154 -0.0285 0.0466  930  GLU A CB  
6949  C CG  . GLU A 932  ? 0.2175 0.1452 0.2546 -0.0131 -0.0248 0.0448  930  GLU A CG  
6950  C CD  . GLU A 932  ? 0.2803 0.2120 0.3192 -0.0150 -0.0249 0.0500  930  GLU A CD  
6951  O OE1 . GLU A 932  ? 0.2795 0.2170 0.3188 -0.0187 -0.0252 0.0550  930  GLU A OE1 
6952  O OE2 . GLU A 932  ? 0.2674 0.1971 0.3075 -0.0128 -0.0249 0.0492  930  GLU A OE2 
6953  N N   . LEU A 933  ? 0.2145 0.1355 0.2556 -0.0164 -0.0305 0.0408  931  LEU A N   
6954  C CA  . LEU A 933  ? 0.2147 0.1350 0.2594 -0.0191 -0.0334 0.0422  931  LEU A CA  
6955  C C   . LEU A 933  ? 0.2484 0.1767 0.2917 -0.0232 -0.0321 0.0475  931  LEU A C   
6956  O O   . LEU A 933  ? 0.2780 0.2124 0.3159 -0.0232 -0.0283 0.0479  931  LEU A O   
6957  C CB  . LEU A 933  ? 0.2573 0.1746 0.2988 -0.0166 -0.0329 0.0360  931  LEU A CB  
6958  C CG  . LEU A 933  ? 0.2870 0.1973 0.3293 -0.0123 -0.0342 0.0300  931  LEU A CG  
6959  C CD1 . LEU A 933  ? 0.3057 0.2149 0.3439 -0.0101 -0.0334 0.0244  931  LEU A CD1 
6960  C CD2 . LEU A 933  ? 0.3059 0.2100 0.3569 -0.0129 -0.0395 0.0312  931  LEU A CD2 
6961  N N   . GLU A 934  ? 0.2769 0.2055 0.3256 -0.0267 -0.0353 0.0513  932  GLU A N   
6962  C CA  . GLU A 934  ? 0.3244 0.2615 0.3723 -0.0307 -0.0342 0.0562  932  GLU A CA  
6963  C C   . GLU A 934  ? 0.3647 0.3050 0.4070 -0.0299 -0.0314 0.0524  932  GLU A C   
6964  O O   . GLU A 934  ? 0.3719 0.3199 0.4096 -0.0308 -0.0281 0.0536  932  GLU A O   
6965  C CB  . GLU A 934  ? 0.3924 0.3293 0.4485 -0.0349 -0.0387 0.0622  932  GLU A CB  
6966  C CG  . GLU A 934  ? 0.4852 0.4202 0.5472 -0.0357 -0.0415 0.0664  932  GLU A CG  
6967  C CD  . GLU A 934  ? 0.5867 0.5295 0.6459 -0.0369 -0.0389 0.0707  932  GLU A CD  
6968  O OE1 . GLU A 934  ? 0.6545 0.6063 0.7122 -0.0401 -0.0374 0.0750  932  GLU A OE1 
6969  O OE2 . GLU A 934  ? 0.5986 0.5390 0.6572 -0.0345 -0.0383 0.0696  932  GLU A OE2 
6970  N N   . LYS A 935  ? 0.3234 0.2581 0.3660 -0.0282 -0.0328 0.0478  933  LYS A N   
6971  C CA  . LYS A 935  ? 0.3451 0.2826 0.3827 -0.0273 -0.0305 0.0442  933  LYS A CA  
6972  C C   . LYS A 935  ? 0.3493 0.2799 0.3849 -0.0233 -0.0308 0.0373  933  LYS A C   
6973  O O   . LYS A 935  ? 0.3089 0.2326 0.3481 -0.0216 -0.0335 0.0354  933  LYS A O   
6974  C CB  . LYS A 935  ? 0.4105 0.3518 0.4515 -0.0312 -0.0323 0.0476  933  LYS A CB  
6975  C CG  . LYS A 935  ? 0.4646 0.4006 0.5140 -0.0334 -0.0376 0.0501  933  LYS A CG  
6976  C CD  . LYS A 935  ? 0.4973 0.4392 0.5510 -0.0382 -0.0392 0.0557  933  LYS A CD  
6977  C CE  . LYS A 935  ? 0.5273 0.4638 0.5905 -0.0409 -0.0448 0.0592  933  LYS A CE  
6978  N NZ  . LYS A 935  ? 0.5841 0.5106 0.6491 -0.0376 -0.0475 0.0529  933  LYS A NZ  
6979  N N   . LEU A 936  ? 0.3626 0.2955 0.3924 -0.0216 -0.0280 0.0335  934  LEU A N   
6980  C CA  . LEU A 936  ? 0.3718 0.2996 0.3986 -0.0176 -0.0277 0.0271  934  LEU A CA  
6981  C C   . LEU A 936  ? 0.3635 0.2854 0.3953 -0.0177 -0.0322 0.0251  934  LEU A C   
6982  O O   . LEU A 936  ? 0.3973 0.3137 0.4290 -0.0143 -0.0332 0.0203  934  LEU A O   
6983  C CB  . LEU A 936  ? 0.4050 0.3368 0.4254 -0.0163 -0.0244 0.0243  934  LEU A CB  
6984  C CG  . LEU A 936  ? 0.4365 0.3669 0.4511 -0.0120 -0.0214 0.0197  934  LEU A CG  
6985  C CD1 . LEU A 936  ? 0.4786 0.4130 0.4879 -0.0111 -0.0185 0.0177  934  LEU A CD1 
6986  C CD2 . LEU A 936  ? 0.4157 0.3395 0.4313 -0.0089 -0.0234 0.0152  934  LEU A CD2 
6987  N N   . SER A 937  ? 0.4038 0.3272 0.4404 -0.0214 -0.0348 0.0286  935  SER A N   
6988  C CA  . SER A 937  ? 0.4217 0.3395 0.4640 -0.0218 -0.0394 0.0268  935  SER A CA  
6989  C C   . SER A 937  ? 0.4244 0.3354 0.4730 -0.0213 -0.0432 0.0271  935  SER A C   
6990  O O   . SER A 937  ? 0.4282 0.3334 0.4818 -0.0208 -0.0473 0.0244  935  SER A O   
6991  C CB  . SER A 937  ? 0.4356 0.3571 0.4822 -0.0264 -0.0415 0.0312  935  SER A CB  
6992  O OG  . SER A 937  ? 0.4710 0.3966 0.5213 -0.0302 -0.0418 0.0383  935  SER A OG  
6993  N N   . ASP A 938  ? 0.4140 0.3256 0.4630 -0.0212 -0.0421 0.0300  936  ASP A N   
6994  C CA  . ASP A 938  ? 0.3522 0.2572 0.4071 -0.0201 -0.0455 0.0297  936  ASP A CA  
6995  C C   . ASP A 938  ? 0.3725 0.2721 0.4249 -0.0148 -0.0454 0.0221  936  ASP A C   
6996  O O   . ASP A 938  ? 0.3946 0.2880 0.4525 -0.0133 -0.0490 0.0202  936  ASP A O   
6997  C CB  . ASP A 938  ? 0.3619 0.2695 0.4175 -0.0212 -0.0442 0.0347  936  ASP A CB  
6998  C CG  . ASP A 938  ? 0.4538 0.3666 0.5133 -0.0265 -0.0451 0.0428  936  ASP A CG  
6999  O OD1 . ASP A 938  ? 0.4589 0.3715 0.5233 -0.0295 -0.0482 0.0451  936  ASP A OD1 
7000  O OD2 . ASP A 938  ? 0.4411 0.3587 0.4989 -0.0276 -0.0429 0.0470  936  ASP A OD2 
7001  N N   . LEU A 939  ? 0.3558 0.2579 0.4003 -0.0119 -0.0416 0.0177  937  LEU A N   
7002  C CA  . LEU A 939  ? 0.4330 0.3316 0.4745 -0.0069 -0.0410 0.0107  937  LEU A CA  
7003  C C   . LEU A 939  ? 0.5280 0.4250 0.5686 -0.0058 -0.0427 0.0058  937  LEU A C   
7004  O O   . LEU A 939  ? 0.5209 0.4222 0.5567 -0.0065 -0.0403 0.0057  937  LEU A O   
7005  C CB  . LEU A 939  ? 0.4322 0.3351 0.4658 -0.0044 -0.0357 0.0095  937  LEU A CB  
7006  C CG  . LEU A 939  ? 0.4320 0.3331 0.4614 0.0007  -0.0343 0.0029  937  LEU A CG  
7007  C CD1 . LEU A 939  ? 0.3895 0.2851 0.4240 0.0031  -0.0374 0.0003  937  LEU A CD1 
7008  C CD2 . LEU A 939  ? 0.3668 0.2726 0.3891 0.0023  -0.0291 0.0030  937  LEU A CD2 
7009  N N   . GLN A 940  ? 0.5290 0.4200 0.5744 -0.0039 -0.0469 0.0016  938  GLN A N   
7010  C CA  . GLN A 940  ? 0.6163 0.5054 0.6627 -0.0036 -0.0497 -0.0025 938  GLN A CA  
7011  C C   . GLN A 940  ? 0.6357 0.5234 0.6779 0.0016  -0.0493 -0.0106 938  GLN A C   
7012  O O   . GLN A 940  ? 0.6675 0.5560 0.7073 0.0022  -0.0499 -0.0140 938  GLN A O   
7013  C CB  . GLN A 940  ? 0.6856 0.5692 0.7423 -0.0062 -0.0558 -0.0010 938  GLN A CB  
7014  C CG  . GLN A 940  ? 0.7474 0.6340 0.8074 -0.0118 -0.0569 0.0055  938  GLN A CG  
7015  C CD  . GLN A 940  ? 0.8263 0.7087 0.8968 -0.0154 -0.0620 0.0103  938  GLN A CD  
7016  O OE1 . GLN A 940  ? 0.8132 0.6920 0.8880 -0.0137 -0.0640 0.0095  938  GLN A OE1 
7017  N NE2 . GLN A 940  ? 0.8686 0.7535 0.9430 -0.0202 -0.0636 0.0156  938  GLN A NE2 
7018  N N   . ARG A 941  ? 0.6000 0.4862 0.6410 0.0055  -0.0483 -0.0137 939  ARG A N   
7019  C CA  . ARG A 941  ? 0.5600 0.4464 0.5963 0.0106  -0.0474 -0.0212 939  ARG A CA  
7020  C C   . ARG A 941  ? 0.4601 0.3509 0.4894 0.0132  -0.0421 -0.0211 939  ARG A C   
7021  O O   . ARG A 941  ? 0.5081 0.4001 0.5377 0.0116  -0.0400 -0.0163 939  ARG A O   
7022  C CB  . ARG A 941  ? 0.5946 0.4750 0.6372 0.0135  -0.0522 -0.0267 939  ARG A CB  
7023  C CG  . ARG A 941  ? 0.6496 0.5253 0.6990 0.0118  -0.0579 -0.0285 939  ARG A CG  
7024  C CD  . ARG A 941  ? 0.7172 0.5885 0.7699 0.0163  -0.0620 -0.0369 939  ARG A CD  
7025  N NE  . ARG A 941  ? 0.7231 0.5985 0.7681 0.0204  -0.0597 -0.0434 939  ARG A NE  
7026  C CZ  . ARG A 941  ? 0.7128 0.5897 0.7542 0.0256  -0.0583 -0.0492 939  ARG A CZ  
7027  N NH1 . ARG A 941  ? 0.6848 0.5597 0.7297 0.0276  -0.0587 -0.0498 939  ARG A NH1 
7028  N NH2 . ARG A 941  ? 0.6604 0.5419 0.6945 0.0288  -0.0562 -0.0543 939  ARG A NH2 
7029  N N   . GLU A 942  ? 0.4870 0.3805 0.5100 0.0170  -0.0399 -0.0263 940  GLU A N   
7030  C CA  . GLU A 942  ? 0.4603 0.3580 0.4772 0.0198  -0.0352 -0.0267 940  GLU A CA  
7031  C C   . GLU A 942  ? 0.4285 0.3235 0.4490 0.0230  -0.0364 -0.0294 940  GLU A C   
7032  O O   . GLU A 942  ? 0.4446 0.3364 0.4685 0.0257  -0.0399 -0.0349 940  GLU A O   
7033  C CB  . GLU A 942  ? 0.4973 0.3994 0.5069 0.0228  -0.0327 -0.0309 940  GLU A CB  
7034  C CG  . GLU A 942  ? 0.4565 0.3639 0.4593 0.0247  -0.0274 -0.0298 940  GLU A CG  
7035  C CD  . GLU A 942  ? 0.4855 0.3972 0.4819 0.0284  -0.0256 -0.0344 940  GLU A CD  
7036  O OE1 . GLU A 942  ? 0.4604 0.3709 0.4577 0.0310  -0.0285 -0.0401 940  GLU A OE1 
7037  O OE2 . GLU A 942  ? 0.3967 0.3133 0.3873 0.0287  -0.0214 -0.0324 940  GLU A OE2 
7038  N N   . VAL A 943  ? 0.3545 0.2509 0.3745 0.0226  -0.0337 -0.0257 941  VAL A N   
7039  C CA  . VAL A 943  ? 0.3289 0.2232 0.3524 0.0254  -0.0345 -0.0275 941  VAL A CA  
7040  C C   . VAL A 943  ? 0.2930 0.1928 0.3098 0.0288  -0.0297 -0.0291 941  VAL A C   
7041  O O   . VAL A 943  ? 0.2842 0.1875 0.2977 0.0272  -0.0259 -0.0246 941  VAL A O   
7042  C CB  . VAL A 943  ? 0.3424 0.2342 0.3715 0.0222  -0.0355 -0.0214 941  VAL A CB  
7043  C CG1 . VAL A 943  ? 0.3680 0.2577 0.4012 0.0253  -0.0366 -0.0235 941  VAL A CG1 
7044  C CG2 . VAL A 943  ? 0.3779 0.2653 0.4136 0.0183  -0.0401 -0.0188 941  VAL A CG2 
7045  N N   . PHE A 944  ? 0.2999 0.2009 0.3150 0.0335  -0.0300 -0.0356 942  PHE A N   
7046  C CA  . PHE A 944  ? 0.2848 0.1922 0.2929 0.0366  -0.0254 -0.0374 942  PHE A CA  
7047  C C   . PHE A 944  ? 0.2818 0.1902 0.2914 0.0390  -0.0239 -0.0373 942  PHE A C   
7048  O O   . PHE A 944  ? 0.2964 0.2066 0.3057 0.0435  -0.0239 -0.0425 942  PHE A O   
7049  C CB  . PHE A 944  ? 0.2755 0.1851 0.2803 0.0404  -0.0263 -0.0442 942  PHE A CB  
7050  C CG  . PHE A 944  ? 0.3015 0.2182 0.2981 0.0419  -0.0217 -0.0441 942  PHE A CG  
7051  C CD1 . PHE A 944  ? 0.2772 0.1957 0.2698 0.0388  -0.0198 -0.0402 942  PHE A CD1 
7052  C CD2 . PHE A 944  ? 0.3286 0.2505 0.3218 0.0464  -0.0195 -0.0479 942  PHE A CD2 
7053  C CE1 . PHE A 944  ? 0.3034 0.2281 0.2890 0.0400  -0.0160 -0.0398 942  PHE A CE1 
7054  C CE2 . PHE A 944  ? 0.2856 0.2144 0.2716 0.0474  -0.0155 -0.0472 942  PHE A CE2 
7055  C CZ  . PHE A 944  ? 0.3139 0.2438 0.2963 0.0442  -0.0138 -0.0430 942  PHE A CZ  
7056  N N   . GLY A 945  ? 0.2478 0.1555 0.2592 0.0359  -0.0226 -0.0313 943  GLY A N   
7057  C CA  . GLY A 945  ? 0.2355 0.1439 0.2492 0.0375  -0.0215 -0.0304 943  GLY A CA  
7058  C C   . GLY A 945  ? 0.2230 0.1332 0.2355 0.0339  -0.0186 -0.0236 943  GLY A C   
7059  O O   . GLY A 945  ? 0.2091 0.1207 0.2183 0.0307  -0.0170 -0.0201 943  GLY A O   
7060  N N   . PRO A 946  ? 0.2180 0.1285 0.2332 0.0347  -0.0178 -0.0220 944  PRO A N   
7061  C CA  . PRO A 946  ? 0.2336 0.1465 0.2475 0.0317  -0.0149 -0.0160 944  PRO A CA  
7062  C C   . PRO A 946  ? 0.2136 0.1227 0.2321 0.0274  -0.0175 -0.0110 944  PRO A C   
7063  O O   . PRO A 946  ? 0.2038 0.1116 0.2266 0.0267  -0.0184 -0.0083 944  PRO A O   
7064  C CB  . PRO A 946  ? 0.2025 0.1177 0.2175 0.0349  -0.0134 -0.0171 944  PRO A CB  
7065  C CG  . PRO A 946  ? 0.2135 0.1247 0.2339 0.0380  -0.0173 -0.0219 944  PRO A CG  
7066  C CD  . PRO A 946  ? 0.2029 0.1122 0.2221 0.0387  -0.0195 -0.0261 944  PRO A CD  
7067  N N   . VAL A 947  ? 0.2192 0.1270 0.2371 0.0245  -0.0188 -0.0097 945  VAL A N   
7068  C CA  . VAL A 947  ? 0.2048 0.1094 0.2276 0.0205  -0.0217 -0.0053 945  VAL A CA  
7069  C C   . VAL A 947  ? 0.2045 0.1123 0.2232 0.0168  -0.0196 -0.0016 945  VAL A C   
7070  O O   . VAL A 947  ? 0.2139 0.1221 0.2299 0.0165  -0.0196 -0.0034 945  VAL A O   
7071  C CB  . VAL A 947  ? 0.2468 0.1459 0.2753 0.0206  -0.0267 -0.0079 945  VAL A CB  
7072  C CG1 . VAL A 947  ? 0.2425 0.1389 0.2766 0.0162  -0.0298 -0.0024 945  VAL A CG1 
7073  C CG2 . VAL A 947  ? 0.2614 0.1576 0.2940 0.0248  -0.0289 -0.0125 945  VAL A CG2 
7074  N N   . LEU A 948  ? 0.1980 0.1084 0.2165 0.0142  -0.0179 0.0034  946  LEU A N   
7075  C CA  . LEU A 948  ? 0.1737 0.0877 0.1887 0.0109  -0.0158 0.0069  946  LEU A CA  
7076  C C   . LEU A 948  ? 0.2134 0.1263 0.2330 0.0068  -0.0187 0.0113  946  LEU A C   
7077  O O   . LEU A 948  ? 0.2307 0.1422 0.2550 0.0057  -0.0205 0.0143  946  LEU A O   
7078  C CB  . LEU A 948  ? 0.1799 0.0983 0.1917 0.0106  -0.0121 0.0092  946  LEU A CB  
7079  C CG  . LEU A 948  ? 0.1826 0.1050 0.1917 0.0073  -0.0102 0.0127  946  LEU A CG  
7080  C CD1 . LEU A 948  ? 0.2020 0.1258 0.2062 0.0080  -0.0085 0.0101  946  LEU A CD1 
7081  C CD2 . LEU A 948  ? 0.2373 0.1633 0.2449 0.0069  -0.0075 0.0151  946  LEU A CD2 
7082  N N   . HIS A 949  ? 0.2028 0.1167 0.2212 0.0045  -0.0191 0.0121  947  HIS A N   
7083  C CA  . HIS A 949  ? 0.1995 0.1139 0.2218 0.0003  -0.0214 0.0169  947  HIS A CA  
7084  C C   . HIS A 949  ? 0.2062 0.1266 0.2247 -0.0023 -0.0183 0.0204  947  HIS A C   
7085  O O   . HIS A 949  ? 0.2196 0.1428 0.2326 -0.0012 -0.0151 0.0184  947  HIS A O   
7086  C CB  . HIS A 949  ? 0.2205 0.1322 0.2448 -0.0007 -0.0243 0.0154  947  HIS A CB  
7087  C CG  . HIS A 949  ? 0.2235 0.1293 0.2513 0.0022  -0.0274 0.0109  947  HIS A CG  
7088  N ND1 . HIS A 949  ? 0.2294 0.1344 0.2535 0.0062  -0.0262 0.0050  947  HIS A ND1 
7089  C CD2 . HIS A 949  ? 0.2605 0.1613 0.2955 0.0018  -0.0319 0.0113  947  HIS A CD2 
7090  C CE1 . HIS A 949  ? 0.2651 0.1651 0.2936 0.0083  -0.0298 0.0015  947  HIS A CE1 
7091  N NE2 . HIS A 949  ? 0.2666 0.1636 0.3022 0.0058  -0.0333 0.0051  947  HIS A NE2 
7092  N N   . VAL A 950  ? 0.1902 0.1130 0.2117 -0.0055 -0.0192 0.0256  948  VAL A N   
7093  C CA  . VAL A 950  ? 0.1820 0.1112 0.2003 -0.0078 -0.0164 0.0287  948  VAL A CA  
7094  C C   . VAL A 950  ? 0.2183 0.1505 0.2393 -0.0118 -0.0183 0.0330  948  VAL A C   
7095  O O   . VAL A 950  ? 0.2313 0.1617 0.2579 -0.0139 -0.0215 0.0365  948  VAL A O   
7096  C CB  . VAL A 950  ? 0.2028 0.1342 0.2213 -0.0077 -0.0152 0.0311  948  VAL A CB  
7097  C CG1 . VAL A 950  ? 0.2440 0.1824 0.2591 -0.0098 -0.0125 0.0336  948  VAL A CG1 
7098  C CG2 . VAL A 950  ? 0.2309 0.1599 0.2472 -0.0037 -0.0134 0.0271  948  VAL A CG2 
7099  N N   . ILE A 951  ? 0.1837 0.1207 0.2010 -0.0131 -0.0162 0.0330  949  ILE A N   
7100  C CA  . ILE A 951  ? 0.2149 0.1567 0.2341 -0.0170 -0.0173 0.0372  949  ILE A CA  
7101  C C   . ILE A 951  ? 0.2372 0.1867 0.2524 -0.0180 -0.0140 0.0387  949  ILE A C   
7102  O O   . ILE A 951  ? 0.1951 0.1455 0.2059 -0.0157 -0.0111 0.0357  949  ILE A O   
7103  C CB  . ILE A 951  ? 0.2180 0.1588 0.2377 -0.0177 -0.0186 0.0357  949  ILE A CB  
7104  C CG1 . ILE A 951  ? 0.2421 0.1840 0.2559 -0.0153 -0.0155 0.0311  949  ILE A CG1 
7105  C CG2 . ILE A 951  ? 0.2449 0.1781 0.2692 -0.0168 -0.0223 0.0340  949  ILE A CG2 
7106  C CD1 . ILE A 951  ? 0.2995 0.2411 0.3136 -0.0160 -0.0168 0.0297  949  ILE A CD1 
7107  N N   . ARG A 952  ? 0.2272 0.1826 0.2443 -0.0216 -0.0147 0.0433  950  ARG A N   
7108  C CA  . ARG A 952  ? 0.2012 0.1650 0.2151 -0.0227 -0.0121 0.0447  950  ARG A CA  
7109  C C   . ARG A 952  ? 0.2126 0.1816 0.2258 -0.0246 -0.0117 0.0450  950  ARG A C   
7110  O O   . ARG A 952  ? 0.2334 0.2009 0.2501 -0.0264 -0.0142 0.0467  950  ARG A O   
7111  C CB  . ARG A 952  ? 0.2318 0.2002 0.2484 -0.0253 -0.0131 0.0501  950  ARG A CB  
7112  C CG  . ARG A 952  ? 0.2823 0.2455 0.3011 -0.0238 -0.0141 0.0505  950  ARG A CG  
7113  C CD  . ARG A 952  ? 0.3166 0.2826 0.3401 -0.0269 -0.0166 0.0568  950  ARG A CD  
7114  N NE  . ARG A 952  ? 0.3091 0.2837 0.3302 -0.0282 -0.0147 0.0593  950  ARG A NE  
7115  C CZ  . ARG A 952  ? 0.2914 0.2665 0.3121 -0.0273 -0.0142 0.0600  950  ARG A CZ  
7116  N NH1 . ARG A 952  ? 0.3084 0.2762 0.3312 -0.0251 -0.0152 0.0586  950  ARG A NH1 
7117  N NH2 . ARG A 952  ? 0.3014 0.2851 0.3199 -0.0286 -0.0126 0.0619  950  ARG A NH2 
7118  N N   . TYR A 953  ? 0.2140 0.1890 0.2230 -0.0241 -0.0089 0.0433  951  TYR A N   
7119  C CA  . TYR A 953  ? 0.2047 0.1855 0.2131 -0.0256 -0.0084 0.0434  951  TYR A CA  
7120  C C   . TYR A 953  ? 0.1929 0.1834 0.1989 -0.0265 -0.0061 0.0443  951  TYR A C   
7121  O O   . TYR A 953  ? 0.1990 0.1902 0.2023 -0.0248 -0.0042 0.0424  951  TYR A O   
7122  C CB  . TYR A 953  ? 0.1957 0.1726 0.2013 -0.0231 -0.0074 0.0384  951  TYR A CB  
7123  C CG  . TYR A 953  ? 0.1764 0.1537 0.1775 -0.0202 -0.0044 0.0343  951  TYR A CG  
7124  C CD1 . TYR A 953  ? 0.1793 0.1506 0.1789 -0.0175 -0.0036 0.0319  951  TYR A CD1 
7125  C CD2 . TYR A 953  ? 0.2013 0.1851 0.2000 -0.0201 -0.0024 0.0328  951  TYR A CD2 
7126  C CE1 . TYR A 953  ? 0.1849 0.1565 0.1809 -0.0151 -0.0011 0.0286  951  TYR A CE1 
7127  C CE2 . TYR A 953  ? 0.1883 0.1720 0.1836 -0.0175 0.0000  0.0292  951  TYR A CE2 
7128  C CZ  . TYR A 953  ? 0.1950 0.1725 0.1891 -0.0152 0.0006  0.0273  951  TYR A CZ  
7129  O OH  . TYR A 953  ? 0.2162 0.1937 0.2076 -0.0129 0.0027  0.0243  951  TYR A OH  
7130  N N   . ARG A 954  ? 0.2156 0.2138 0.2228 -0.0292 -0.0064 0.0470  952  ARG A N   
7131  C CA  . ARG A 954  ? 0.2300 0.2384 0.2348 -0.0297 -0.0042 0.0468  952  ARG A CA  
7132  C C   . ARG A 954  ? 0.1967 0.2053 0.1980 -0.0271 -0.0021 0.0413  952  ARG A C   
7133  O O   . ARG A 954  ? 0.2056 0.2098 0.2071 -0.0263 -0.0026 0.0393  952  ARG A O   
7134  C CB  . ARG A 954  ? 0.2773 0.2949 0.2848 -0.0334 -0.0053 0.0517  952  ARG A CB  
7135  C CG  . ARG A 954  ? 0.3714 0.3890 0.3832 -0.0365 -0.0078 0.0581  952  ARG A CG  
7136  C CD  . ARG A 954  ? 0.4017 0.4207 0.4123 -0.0360 -0.0072 0.0592  952  ARG A CD  
7137  N NE  . ARG A 954  ? 0.4391 0.4690 0.4465 -0.0360 -0.0048 0.0584  952  ARG A NE  
7138  C CZ  . ARG A 954  ? 0.5688 0.6092 0.5772 -0.0387 -0.0051 0.0632  952  ARG A CZ  
7139  N NH1 . ARG A 954  ? 0.6088 0.6500 0.6216 -0.0419 -0.0076 0.0697  952  ARG A NH1 
7140  N NH2 . ARG A 954  ? 0.5463 0.5968 0.5515 -0.0382 -0.0029 0.0613  952  ARG A NH2 
7141  N N   . ARG A 955  ? 0.2395 0.2530 0.2378 -0.0256 0.0002  0.0387  953  ARG A N   
7142  C CA  . ARG A 955  ? 0.2505 0.2627 0.2461 -0.0228 0.0020  0.0334  953  ARG A CA  
7143  C C   . ARG A 955  ? 0.2187 0.2346 0.2147 -0.0234 0.0019  0.0327  953  ARG A C   
7144  O O   . ARG A 955  ? 0.2340 0.2452 0.2289 -0.0214 0.0022  0.0293  953  ARG A O   
7145  C CB  . ARG A 955  ? 0.2901 0.3075 0.2833 -0.0214 0.0039  0.0307  953  ARG A CB  
7146  C CG  . ARG A 955  ? 0.3635 0.3793 0.3547 -0.0184 0.0055  0.0254  953  ARG A CG  
7147  C CD  . ARG A 955  ? 0.3904 0.3956 0.3810 -0.0164 0.0052  0.0234  953  ARG A CD  
7148  N NE  . ARG A 955  ? 0.4000 0.4038 0.3891 -0.0138 0.0064  0.0191  953  ARG A NE  
7149  C CZ  . ARG A 955  ? 0.4100 0.4156 0.3991 -0.0134 0.0064  0.0176  953  ARG A CZ  
7150  N NH1 . ARG A 955  ? 0.3839 0.3934 0.3744 -0.0156 0.0054  0.0199  953  ARG A NH1 
7151  N NH2 . ARG A 955  ? 0.3849 0.3885 0.3729 -0.0109 0.0073  0.0139  953  ARG A NH2 
7152  N N   . ASP A 956  ? 0.2310 0.2559 0.2288 -0.0262 0.0014  0.0360  954  ASP A N   
7153  C CA  . ASP A 956  ? 0.2231 0.2522 0.2218 -0.0268 0.0013  0.0355  954  ASP A CA  
7154  C C   . ASP A 956  ? 0.2348 0.2560 0.2355 -0.0273 -0.0007 0.0363  954  ASP A C   
7155  O O   . ASP A 956  ? 0.2432 0.2657 0.2442 -0.0271 -0.0008 0.0347  954  ASP A O   
7156  C CB  . ASP A 956  ? 0.2463 0.2875 0.2468 -0.0300 0.0012  0.0396  954  ASP A CB  
7157  C CG  . ASP A 956  ? 0.2995 0.3505 0.2977 -0.0291 0.0032  0.0377  954  ASP A CG  
7158  O OD1 . ASP A 956  ? 0.3594 0.4079 0.3550 -0.0260 0.0047  0.0326  954  ASP A OD1 
7159  O OD2 . ASP A 956  ? 0.3951 0.4566 0.3944 -0.0316 0.0032  0.0413  954  ASP A OD2 
7160  N N   . ASP A 957  ? 0.2134 0.2267 0.2156 -0.0278 -0.0024 0.0382  955  ASP A N   
7161  C CA  . ASP A 957  ? 0.2198 0.2255 0.2243 -0.0281 -0.0047 0.0385  955  ASP A CA  
7162  C C   . ASP A 957  ? 0.2277 0.2241 0.2296 -0.0246 -0.0042 0.0337  955  ASP A C   
7163  O O   . ASP A 957  ? 0.2236 0.2128 0.2269 -0.0243 -0.0061 0.0333  955  ASP A O   
7164  C CB  . ASP A 957  ? 0.2449 0.2477 0.2534 -0.0307 -0.0073 0.0433  955  ASP A CB  
7165  C CG  . ASP A 957  ? 0.3507 0.3626 0.3626 -0.0347 -0.0083 0.0488  955  ASP A CG  
7166  O OD1 . ASP A 957  ? 0.3191 0.3381 0.3311 -0.0357 -0.0077 0.0489  955  ASP A OD1 
7167  O OD2 . ASP A 957  ? 0.3489 0.3614 0.3635 -0.0368 -0.0097 0.0533  955  ASP A OD2 
7168  N N   . LEU A 958  ? 0.1998 0.1966 0.1981 -0.0219 -0.0018 0.0302  956  LEU A N   
7169  C CA  . LEU A 958  ? 0.1849 0.1738 0.1808 -0.0186 -0.0012 0.0262  956  LEU A CA  
7170  C C   . LEU A 958  ? 0.2058 0.1917 0.2017 -0.0179 -0.0022 0.0243  956  LEU A C   
7171  O O   . LEU A 958  ? 0.1957 0.1743 0.1913 -0.0165 -0.0033 0.0228  956  LEU A O   
7172  C CB  . LEU A 958  ? 0.2091 0.1999 0.2019 -0.0163 0.0013  0.0232  956  LEU A CB  
7173  C CG  . LEU A 958  ? 0.2141 0.1980 0.2045 -0.0131 0.0021  0.0197  956  LEU A CG  
7174  C CD1 . LEU A 958  ? 0.2152 0.1919 0.2057 -0.0123 0.0013  0.0202  956  LEU A CD1 
7175  C CD2 . LEU A 958  ? 0.1986 0.1850 0.1870 -0.0112 0.0042  0.0172  956  LEU A CD2 
7176  N N   . ASP A 959  ? 0.1916 0.1836 0.1879 -0.0187 -0.0019 0.0240  957  ASP A N   
7177  C CA  . ASP A 959  ? 0.1895 0.1790 0.1858 -0.0179 -0.0028 0.0220  957  ASP A CA  
7178  C C   . ASP A 959  ? 0.2167 0.2019 0.2160 -0.0197 -0.0057 0.0240  957  ASP A C   
7179  O O   . ASP A 959  ? 0.1997 0.1790 0.1985 -0.0182 -0.0069 0.0217  957  ASP A O   
7180  C CB  . ASP A 959  ? 0.1858 0.1834 0.1825 -0.0186 -0.0020 0.0216  957  ASP A CB  
7181  C CG  . ASP A 959  ? 0.2415 0.2368 0.2375 -0.0171 -0.0026 0.0190  957  ASP A CG  
7182  O OD1 . ASP A 959  ? 0.2266 0.2168 0.2199 -0.0141 -0.0018 0.0159  957  ASP A OD1 
7183  O OD2 . ASP A 959  ? 0.2784 0.2774 0.2768 -0.0189 -0.0038 0.0202  957  ASP A OD2 
7184  N N   . ARG A 960  ? 0.2065 0.1947 0.2093 -0.0229 -0.0071 0.0282  958  ARG A N   
7185  C CA  . ARG A 960  ? 0.2160 0.1998 0.2227 -0.0248 -0.0103 0.0303  958  ARG A CA  
7186  C C   . ARG A 960  ? 0.2299 0.2044 0.2361 -0.0228 -0.0113 0.0286  958  ARG A C   
7187  O O   . ARG A 960  ? 0.2419 0.2105 0.2496 -0.0223 -0.0136 0.0272  958  ARG A O   
7188  C CB  . ARG A 960  ? 0.2339 0.2232 0.2448 -0.0288 -0.0116 0.0359  958  ARG A CB  
7189  C CG  . ARG A 960  ? 0.2570 0.2413 0.2731 -0.0311 -0.0154 0.0386  958  ARG A CG  
7190  C CD  . ARG A 960  ? 0.4289 0.4197 0.4496 -0.0354 -0.0168 0.0449  958  ARG A CD  
7191  N NE  . ARG A 960  ? 0.5133 0.5045 0.5342 -0.0358 -0.0164 0.0477  958  ARG A NE  
7192  C CZ  . ARG A 960  ? 0.5146 0.5125 0.5385 -0.0392 -0.0169 0.0534  958  ARG A CZ  
7193  N NH1 . ARG A 960  ? 0.5586 0.5641 0.5857 -0.0426 -0.0178 0.0572  958  ARG A NH1 
7194  N NH2 . ARG A 960  ? 0.5027 0.5003 0.5265 -0.0393 -0.0167 0.0555  958  ARG A NH2 
7195  N N   . LEU A 961  ? 0.2057 0.1794 0.2098 -0.0214 -0.0096 0.0284  959  LEU A N   
7196  C CA  . LEU A 961  ? 0.2134 0.1792 0.2168 -0.0192 -0.0101 0.0267  959  LEU A CA  
7197  C C   . LEU A 961  ? 0.2449 0.2060 0.2452 -0.0160 -0.0096 0.0220  959  LEU A C   
7198  O O   . LEU A 961  ? 0.2230 0.1779 0.2242 -0.0147 -0.0115 0.0203  959  LEU A O   
7199  C CB  . LEU A 961  ? 0.2031 0.1700 0.2047 -0.0183 -0.0080 0.0272  959  LEU A CB  
7200  C CG  . LEU A 961  ? 0.2301 0.1898 0.2305 -0.0155 -0.0080 0.0249  959  LEU A CG  
7201  C CD1 . LEU A 961  ? 0.2526 0.2073 0.2574 -0.0166 -0.0113 0.0265  959  LEU A CD1 
7202  C CD2 . LEU A 961  ? 0.2529 0.2144 0.2515 -0.0146 -0.0058 0.0253  959  LEU A CD2 
7203  N N   . VAL A 962  ? 0.1986 0.1628 0.1955 -0.0144 -0.0073 0.0198  960  VAL A N   
7204  C CA  . VAL A 962  ? 0.1931 0.1536 0.1870 -0.0115 -0.0069 0.0160  960  VAL A CA  
7205  C C   . VAL A 962  ? 0.2462 0.2047 0.2421 -0.0122 -0.0096 0.0152  960  VAL A C   
7206  O O   . VAL A 962  ? 0.2227 0.1762 0.2176 -0.0102 -0.0107 0.0125  960  VAL A O   
7207  C CB  . VAL A 962  ? 0.2064 0.1710 0.1972 -0.0101 -0.0043 0.0144  960  VAL A CB  
7208  C CG1 . VAL A 962  ? 0.2437 0.2054 0.2319 -0.0074 -0.0043 0.0111  960  VAL A CG1 
7209  C CG2 . VAL A 962  ? 0.1999 0.1654 0.1890 -0.0091 -0.0020 0.0145  960  VAL A CG2 
7210  N N   . ASP A 963  ? 0.2221 0.1850 0.2210 -0.0152 -0.0108 0.0176  961  ASP A N   
7211  C CA  . ASP A 963  ? 0.2578 0.2188 0.2597 -0.0164 -0.0139 0.0174  961  ASP A CA  
7212  C C   . ASP A 963  ? 0.2657 0.2201 0.2705 -0.0165 -0.0166 0.0174  961  ASP A C   
7213  O O   . ASP A 963  ? 0.3078 0.2577 0.3130 -0.0152 -0.0187 0.0145  961  ASP A O   
7214  C CB  . ASP A 963  ? 0.2900 0.2574 0.2956 -0.0201 -0.0148 0.0209  961  ASP A CB  
7215  C CG  . ASP A 963  ? 0.3100 0.2836 0.3136 -0.0197 -0.0129 0.0199  961  ASP A CG  
7216  O OD1 . ASP A 963  ? 0.4347 0.4071 0.4343 -0.0167 -0.0113 0.0166  961  ASP A OD1 
7217  O OD2 . ASP A 963  ? 0.5028 0.4830 0.5091 -0.0225 -0.0132 0.0228  961  ASP A OD2 
7218  N N   . ASP A 964  ? 0.2781 0.2321 0.2851 -0.0179 -0.0169 0.0203  962  ASP A N   
7219  C CA  . ASP A 964  ? 0.3233 0.2710 0.3339 -0.0179 -0.0198 0.0205  962  ASP A CA  
7220  C C   . ASP A 964  ? 0.3423 0.2843 0.3497 -0.0139 -0.0193 0.0158  962  ASP A C   
7221  O O   . ASP A 964  ? 0.3695 0.3062 0.3789 -0.0129 -0.0221 0.0134  962  ASP A O   
7222  C CB  . ASP A 964  ? 0.3349 0.2838 0.3482 -0.0199 -0.0198 0.0247  962  ASP A CB  
7223  C CG  . ASP A 964  ? 0.3725 0.3271 0.3903 -0.0243 -0.0212 0.0300  962  ASP A CG  
7224  O OD1 . ASP A 964  ? 0.3900 0.3465 0.4096 -0.0260 -0.0226 0.0303  962  ASP A OD1 
7225  O OD2 . ASP A 964  ? 0.4821 0.4395 0.5014 -0.0261 -0.0208 0.0340  962  ASP A OD2 
7226  N N   . VAL A 965  ? 0.2698 0.2130 0.2723 -0.0115 -0.0160 0.0143  963  VAL A N   
7227  C CA  . VAL A 965  ? 0.2443 0.1833 0.2434 -0.0076 -0.0152 0.0103  963  VAL A CA  
7228  C C   . VAL A 965  ? 0.2937 0.2315 0.2912 -0.0060 -0.0163 0.0067  963  VAL A C   
7229  O O   . VAL A 965  ? 0.3120 0.2455 0.3095 -0.0039 -0.0179 0.0035  963  VAL A O   
7230  C CB  . VAL A 965  ? 0.2423 0.1836 0.2370 -0.0058 -0.0114 0.0100  963  VAL A CB  
7231  C CG1 . VAL A 965  ? 0.2472 0.1852 0.2384 -0.0019 -0.0105 0.0063  963  VAL A CG1 
7232  C CG2 . VAL A 965  ? 0.2423 0.1848 0.2386 -0.0071 -0.0105 0.0132  963  VAL A CG2 
7233  N N   . ASN A 966  ? 0.2402 0.1821 0.2363 -0.0069 -0.0154 0.0070  964  ASN A N   
7234  C CA  . ASN A 966  ? 0.2413 0.1826 0.2358 -0.0055 -0.0165 0.0039  964  ASN A CA  
7235  C C   . ASN A 966  ? 0.3082 0.2463 0.3072 -0.0069 -0.0206 0.0032  964  ASN A C   
7236  O O   . ASN A 966  ? 0.3189 0.2543 0.3169 -0.0049 -0.0222 -0.0005 964  ASN A O   
7237  C CB  . ASN A 966  ? 0.2442 0.1908 0.2372 -0.0064 -0.0150 0.0048  964  ASN A CB  
7238  C CG  . ASN A 966  ? 0.2358 0.1849 0.2244 -0.0044 -0.0114 0.0043  964  ASN A CG  
7239  O OD1 . ASN A 966  ? 0.2462 0.1927 0.2319 -0.0018 -0.0101 0.0028  964  ASN A OD1 
7240  N ND2 . ASN A 966  ? 0.2403 0.1944 0.2286 -0.0054 -0.0100 0.0056  964  ASN A ND2 
7241  N N   . ALA A 967  ? 0.3161 0.2547 0.3203 -0.0104 -0.0225 0.0068  965  ALA A N   
7242  C CA  . ALA A 967  ? 0.3574 0.2934 0.3670 -0.0124 -0.0267 0.0068  965  ALA A CA  
7243  C C   . ALA A 967  ? 0.3278 0.2571 0.3391 -0.0102 -0.0294 0.0033  965  ALA A C   
7244  O O   . ALA A 967  ? 0.3930 0.3194 0.4078 -0.0108 -0.0331 0.0015  965  ALA A O   
7245  C CB  . ALA A 967  ? 0.3714 0.3098 0.3866 -0.0167 -0.0280 0.0122  965  ALA A CB  
7246  N N   . THR A 968  ? 0.3138 0.2406 0.3228 -0.0077 -0.0279 0.0021  966  THR A N   
7247  C CA  . THR A 968  ? 0.3132 0.2343 0.3236 -0.0051 -0.0303 -0.0019 966  THR A CA  
7248  C C   . THR A 968  ? 0.2793 0.1996 0.2865 -0.0021 -0.0311 -0.0073 966  THR A C   
7249  O O   . THR A 968  ? 0.3373 0.2532 0.3468 -0.0005 -0.0342 -0.0111 966  THR A O   
7250  C CB  . THR A 968  ? 0.3435 0.2634 0.3516 -0.0026 -0.0280 -0.0024 966  THR A CB  
7251  O OG1 . THR A 968  ? 0.3132 0.2358 0.3144 0.0003  -0.0243 -0.0045 966  THR A OG1 
7252  C CG2 . THR A 968  ? 0.3601 0.2818 0.3704 -0.0053 -0.0267 0.0030  966  THR A CG2 
7253  N N   . GLY A 969  ? 0.2948 0.2193 0.2968 -0.0012 -0.0284 -0.0078 967  GLY A N   
7254  C CA  . GLY A 969  ? 0.2694 0.1941 0.2676 0.0017  -0.0288 -0.0125 967  GLY A CA  
7255  C C   . GLY A 969  ? 0.2600 0.1851 0.2525 0.0058  -0.0261 -0.0153 967  GLY A C   
7256  O O   . GLY A 969  ? 0.2454 0.1722 0.2338 0.0082  -0.0257 -0.0185 967  GLY A O   
7257  N N   . TYR A 970  ? 0.2392 0.1633 0.2314 0.0066  -0.0243 -0.0142 968  TYR A N   
7258  C CA  . TYR A 970  ? 0.2481 0.1735 0.2351 0.0102  -0.0212 -0.0160 968  TYR A CA  
7259  C C   . TYR A 970  ? 0.2397 0.1695 0.2225 0.0098  -0.0174 -0.0131 968  TYR A C   
7260  O O   . TYR A 970  ? 0.2648 0.1967 0.2490 0.0070  -0.0168 -0.0099 968  TYR A O   
7261  C CB  . TYR A 970  ? 0.2629 0.1857 0.2518 0.0111  -0.0210 -0.0157 968  TYR A CB  
7262  C CG  . TYR A 970  ? 0.3003 0.2186 0.2933 0.0124  -0.0248 -0.0195 968  TYR A CG  
7263  C CD1 . TYR A 970  ? 0.3342 0.2524 0.3245 0.0163  -0.0254 -0.0248 968  TYR A CD1 
7264  C CD2 . TYR A 970  ? 0.3954 0.3099 0.3951 0.0097  -0.0281 -0.0176 968  TYR A CD2 
7265  C CE1 . TYR A 970  ? 0.3703 0.2844 0.3647 0.0179  -0.0292 -0.0290 968  TYR A CE1 
7266  C CE2 . TYR A 970  ? 0.3606 0.2705 0.3649 0.0110  -0.0320 -0.0213 968  TYR A CE2 
7267  C CZ  . TYR A 970  ? 0.3905 0.3000 0.3921 0.0152  -0.0326 -0.0272 968  TYR A CZ  
7268  O OH  . TYR A 970  ? 0.5041 0.4090 0.5106 0.0167  -0.0368 -0.0314 968  TYR A OH  
7269  N N   . GLY A 971  ? 0.1983 0.1300 0.1765 0.0128  -0.0147 -0.0143 969  GLY A N   
7270  C CA  . GLY A 971  ? 0.1965 0.1319 0.1712 0.0127  -0.0114 -0.0118 969  GLY A CA  
7271  C C   . GLY A 971  ? 0.2086 0.1457 0.1791 0.0159  -0.0088 -0.0128 969  GLY A C   
7272  O O   . GLY A 971  ? 0.2053 0.1451 0.1720 0.0174  -0.0075 -0.0132 969  GLY A O   
7273  N N   . LEU A 972  ? 0.1914 0.1270 0.1627 0.0169  -0.0081 -0.0129 970  LEU A N   
7274  C CA  . LEU A 972  ? 0.1874 0.1251 0.1551 0.0199  -0.0057 -0.0138 970  LEU A CA  
7275  C C   . LEU A 972  ? 0.1883 0.1276 0.1555 0.0190  -0.0025 -0.0100 970  LEU A C   
7276  O O   . LEU A 972  ? 0.2040 0.1459 0.1691 0.0187  -0.0008 -0.0082 970  LEU A O   
7277  C CB  . LEU A 972  ? 0.2004 0.1362 0.1691 0.0223  -0.0069 -0.0170 970  LEU A CB  
7278  C CG  . LEU A 972  ? 0.2202 0.1593 0.1850 0.0258  -0.0046 -0.0185 970  LEU A CG  
7279  C CD1 . LEU A 972  ? 0.2543 0.1974 0.2145 0.0274  -0.0039 -0.0195 970  LEU A CD1 
7280  C CD2 . LEU A 972  ? 0.2191 0.1566 0.1854 0.0284  -0.0064 -0.0227 970  LEU A CD2 
7281  N N   . THR A 973  ? 0.1815 0.1192 0.1510 0.0185  -0.0020 -0.0089 971  THR A N   
7282  C CA  . THR A 973  ? 0.1669 0.1062 0.1363 0.0176  0.0008  -0.0056 971  THR A CA  
7283  C C   . THR A 973  ? 0.1599 0.0981 0.1328 0.0142  0.0001  -0.0030 971  THR A C   
7284  O O   . THR A 973  ? 0.1658 0.1017 0.1418 0.0128  -0.0023 -0.0033 971  THR A O   
7285  C CB  . THR A 973  ? 0.1760 0.1155 0.1452 0.0195  0.0023  -0.0058 971  THR A CB  
7286  O OG1 . THR A 973  ? 0.1747 0.1111 0.1473 0.0194  0.0003  -0.0069 971  THR A OG1 
7287  C CG2 . THR A 973  ? 0.1821 0.1242 0.1475 0.0229  0.0034  -0.0079 971  THR A CG2 
7288  N N   . PHE A 974  ? 0.1567 0.0969 0.1291 0.0131  0.0023  -0.0004 972  PHE A N   
7289  C CA  . PHE A 974  ? 0.1569 0.0976 0.1320 0.0101  0.0020  0.0020  972  PHE A CA  
7290  C C   . PHE A 974  ? 0.1538 0.0964 0.1285 0.0099  0.0045  0.0040  972  PHE A C   
7291  O O   . PHE A 974  ? 0.1750 0.1192 0.1475 0.0111  0.0062  0.0040  972  PHE A O   
7292  C CB  . PHE A 974  ? 0.1670 0.1092 0.1422 0.0084  0.0012  0.0023  972  PHE A CB  
7293  C CG  . PHE A 974  ? 0.1613 0.1056 0.1389 0.0056  0.0013  0.0048  972  PHE A CG  
7294  C CD1 . PHE A 974  ? 0.1779 0.1214 0.1587 0.0034  -0.0006 0.0060  972  PHE A CD1 
7295  C CD2 . PHE A 974  ? 0.1771 0.1243 0.1538 0.0052  0.0033  0.0058  972  PHE A CD2 
7296  C CE1 . PHE A 974  ? 0.1856 0.1320 0.1683 0.0008  -0.0004 0.0085  972  PHE A CE1 
7297  C CE2 . PHE A 974  ? 0.1702 0.1201 0.1489 0.0028  0.0034  0.0076  972  PHE A CE2 
7298  C CZ  . PHE A 974  ? 0.1877 0.1377 0.1691 0.0006  0.0018  0.0090  972  PHE A CZ  
7299  N N   . GLY A 975  ? 0.1552 0.0978 0.1324 0.0082  0.0045  0.0058  973  GLY A N   
7300  C CA  . GLY A 975  ? 0.1506 0.0952 0.1279 0.0078  0.0066  0.0074  973  GLY A CA  
7301  C C   . GLY A 975  ? 0.1579 0.1049 0.1369 0.0051  0.0064  0.0092  973  GLY A C   
7302  O O   . GLY A 975  ? 0.1496 0.0966 0.1304 0.0033  0.0047  0.0099  973  GLY A O   
7303  N N   . LEU A 976  ? 0.1542 0.1035 0.1327 0.0050  0.0081  0.0097  974  LEU A N   
7304  C CA  . LEU A 976  ? 0.1531 0.1056 0.1331 0.0028  0.0081  0.0109  974  LEU A CA  
7305  C C   . LEU A 976  ? 0.1477 0.1014 0.1281 0.0030  0.0097  0.0115  974  LEU A C   
7306  O O   . LEU A 976  ? 0.1544 0.1077 0.1340 0.0045  0.0110  0.0109  974  LEU A O   
7307  C CB  . LEU A 976  ? 0.1722 0.1271 0.1516 0.0025  0.0081  0.0100  974  LEU A CB  
7308  C CG  . LEU A 976  ? 0.1691 0.1284 0.1498 0.0008  0.0085  0.0105  974  LEU A CG  
7309  C CD1 . LEU A 976  ? 0.1919 0.1535 0.1743 -0.0016 0.0072  0.0121  974  LEU A CD1 
7310  C CD2 . LEU A 976  ? 0.1960 0.1574 0.1762 0.0013  0.0087  0.0091  974  LEU A CD2 
7311  N N   . HIS A 977  ? 0.1374 0.0929 0.1195 0.0014  0.0094  0.0129  975  HIS A N   
7312  C CA  . HIS A 977  ? 0.1685 0.1258 0.1515 0.0012  0.0105  0.0134  975  HIS A CA  
7313  C C   . HIS A 977  ? 0.1577 0.1197 0.1415 -0.0005 0.0104  0.0134  975  HIS A C   
7314  O O   . HIS A 977  ? 0.1610 0.1255 0.1458 -0.0024 0.0094  0.0148  975  HIS A O   
7315  C CB  . HIS A 977  ? 0.1525 0.1087 0.1367 0.0011  0.0103  0.0148  975  HIS A CB  
7316  C CG  . HIS A 977  ? 0.2113 0.1646 0.1949 0.0032  0.0113  0.0144  975  HIS A CG  
7317  N ND1 . HIS A 977  ? 0.2691 0.2233 0.2535 0.0036  0.0126  0.0147  975  HIS A ND1 
7318  C CD2 . HIS A 977  ? 0.2682 0.2186 0.2509 0.0050  0.0112  0.0136  975  HIS A CD2 
7319  C CE1 . HIS A 977  ? 0.2388 0.1909 0.2226 0.0055  0.0133  0.0145  975  HIS A CE1 
7320  N NE2 . HIS A 977  ? 0.2347 0.1847 0.2174 0.0065  0.0126  0.0137  975  HIS A NE2 
7321  N N   . THR A 978  ? 0.1533 0.1169 0.1369 0.0001  0.0113  0.0120  976  THR A N   
7322  C CA  . THR A 978  ? 0.1551 0.1237 0.1395 -0.0010 0.0113  0.0112  976  THR A CA  
7323  C C   . THR A 978  ? 0.1444 0.1130 0.1294 0.0003  0.0122  0.0094  976  THR A C   
7324  O O   . THR A 978  ? 0.1780 0.1432 0.1626 0.0019  0.0126  0.0091  976  THR A O   
7325  C CB  . THR A 978  ? 0.1603 0.1315 0.1444 -0.0017 0.0106  0.0107  976  THR A CB  
7326  O OG1 . THR A 978  ? 0.1777 0.1548 0.1627 -0.0025 0.0107  0.0096  976  THR A OG1 
7327  C CG2 . THR A 978  ? 0.1970 0.1655 0.1801 -0.0001 0.0107  0.0093  976  THR A CG2 
7328  N N   . ARG A 979  ? 0.1632 0.1362 0.1496 -0.0003 0.0122  0.0083  977  ARG A N   
7329  C CA  . ARG A 979  ? 0.1523 0.1254 0.1401 0.0008  0.0125  0.0062  977  ARG A CA  
7330  C C   . ARG A 979  ? 0.1664 0.1425 0.1546 0.0012  0.0121  0.0040  977  ARG A C   
7331  O O   . ARG A 979  ? 0.1933 0.1694 0.1832 0.0024  0.0121  0.0019  977  ARG A O   
7332  C CB  . ARG A 979  ? 0.2039 0.1798 0.1933 0.0003  0.0126  0.0055  977  ARG A CB  
7333  C CG  . ARG A 979  ? 0.2251 0.1978 0.2146 0.0003  0.0130  0.0075  977  ARG A CG  
7334  C CD  . ARG A 979  ? 0.2808 0.2568 0.2719 -0.0005 0.0128  0.0070  977  ARG A CD  
7335  N NE  . ARG A 979  ? 0.3044 0.2776 0.2961 -0.0004 0.0132  0.0088  977  ARG A NE  
7336  C CZ  . ARG A 979  ? 0.3583 0.3333 0.3516 -0.0009 0.0131  0.0086  977  ARG A CZ  
7337  N NH1 . ARG A 979  ? 0.3086 0.2884 0.3029 -0.0015 0.0125  0.0065  977  ARG A NH1 
7338  N NH2 . ARG A 979  ? 0.3689 0.3414 0.3630 -0.0007 0.0135  0.0104  977  ARG A NH2 
7339  N N   . LEU A 980  ? 0.1483 0.1271 0.1354 0.0003  0.0117  0.0044  978  LEU A N   
7340  C CA  . LEU A 980  ? 0.1396 0.1233 0.1274 0.0004  0.0114  0.0022  978  LEU A CA  
7341  C C   . LEU A 980  ? 0.1741 0.1552 0.1614 0.0015  0.0112  0.0018  978  LEU A C   
7342  O O   . LEU A 980  ? 0.1790 0.1580 0.1648 0.0010  0.0109  0.0035  978  LEU A O   
7343  C CB  . LEU A 980  ? 0.1474 0.1373 0.1347 -0.0016 0.0111  0.0032  978  LEU A CB  
7344  C CG  . LEU A 980  ? 0.1602 0.1532 0.1478 -0.0029 0.0112  0.0042  978  LEU A CG  
7345  C CD1 . LEU A 980  ? 0.1997 0.1988 0.1869 -0.0051 0.0108  0.0062  978  LEU A CD1 
7346  C CD2 . LEU A 980  ? 0.1848 0.1808 0.1739 -0.0019 0.0113  0.0010  978  LEU A CD2 
7347  N N   . ASP A 981  ? 0.1532 0.1347 0.1421 0.0030  0.0110  -0.0007 979  ASP A N   
7348  C CA  . ASP A 981  ? 0.1714 0.1508 0.1601 0.0042  0.0107  -0.0011 979  ASP A CA  
7349  C C   . ASP A 981  ? 0.1660 0.1489 0.1537 0.0032  0.0102  -0.0008 979  ASP A C   
7350  O O   . ASP A 981  ? 0.1696 0.1499 0.1563 0.0036  0.0099  0.0000  979  ASP A O   
7351  C CB  . ASP A 981  ? 0.1692 0.1491 0.1606 0.0060  0.0103  -0.0039 979  ASP A CB  
7352  C CG  . ASP A 981  ? 0.2125 0.1877 0.2054 0.0070  0.0103  -0.0036 979  ASP A CG  
7353  O OD1 . ASP A 981  ? 0.2416 0.2128 0.2331 0.0067  0.0109  -0.0011 979  ASP A OD1 
7354  O OD2 . ASP A 981  ? 0.2362 0.2118 0.2322 0.0082  0.0097  -0.0059 979  ASP A OD2 
7355  N N   . GLU A 982  ? 0.1641 0.1537 0.1524 0.0019  0.0102  -0.0015 980  GLU A N   
7356  C CA  . GLU A 982  ? 0.1580 0.1516 0.1459 0.0007  0.0098  -0.0009 980  GLU A CA  
7357  C C   . GLU A 982  ? 0.1764 0.1665 0.1627 -0.0008 0.0094  0.0023  980  GLU A C   
7358  O O   . GLU A 982  ? 0.1846 0.1739 0.1705 -0.0011 0.0087  0.0030  980  GLU A O   
7359  C CB  . GLU A 982  ? 0.1818 0.1843 0.1706 -0.0005 0.0099  -0.0017 980  GLU A CB  
7360  C CG  . GLU A 982  ? 0.2006 0.2078 0.1894 -0.0023 0.0095  -0.0001 980  GLU A CG  
7361  C CD  . GLU A 982  ? 0.2499 0.2666 0.2392 -0.0040 0.0097  0.0004  980  GLU A CD  
7362  O OE1 . GLU A 982  ? 0.3125 0.3304 0.3014 -0.0054 0.0099  0.0021  980  GLU A OE1 
7363  O OE2 . GLU A 982  ? 0.2586 0.2823 0.2490 -0.0041 0.0097  -0.0008 980  GLU A OE2 
7364  N N   . THR A 983  ? 0.1684 0.1563 0.1541 -0.0016 0.0096  0.0041  981  THR A N   
7365  C CA  . THR A 983  ? 0.1793 0.1637 0.1642 -0.0028 0.0090  0.0067  981  THR A CA  
7366  C C   . THR A 983  ? 0.1643 0.1419 0.1478 -0.0011 0.0088  0.0065  981  THR A C   
7367  O O   . THR A 983  ? 0.1792 0.1547 0.1621 -0.0016 0.0079  0.0074  981  THR A O   
7368  C CB  . THR A 983  ? 0.1870 0.1713 0.1720 -0.0040 0.0091  0.0085  981  THR A CB  
7369  O OG1 . THR A 983  ? 0.2050 0.1967 0.1909 -0.0057 0.0091  0.0090  981  THR A OG1 
7370  C CG2 . THR A 983  ? 0.1951 0.1752 0.1797 -0.0050 0.0082  0.0110  981  THR A CG2 
7371  N N   . ILE A 984  ? 0.1654 0.1399 0.1486 0.0008  0.0096  0.0054  982  ILE A N   
7372  C CA  . ILE A 984  ? 0.1547 0.1240 0.1365 0.0024  0.0096  0.0054  982  ILE A CA  
7373  C C   . ILE A 984  ? 0.1549 0.1251 0.1365 0.0029  0.0088  0.0045  982  ILE A C   
7374  O O   . ILE A 984  ? 0.1698 0.1372 0.1500 0.0032  0.0081  0.0049  982  ILE A O   
7375  C CB  . ILE A 984  ? 0.1671 0.1342 0.1494 0.0041  0.0105  0.0048  982  ILE A CB  
7376  C CG1 . ILE A 984  ? 0.1970 0.1631 0.1796 0.0036  0.0111  0.0058  982  ILE A CG1 
7377  C CG2 . ILE A 984  ? 0.1998 0.1629 0.1806 0.0059  0.0105  0.0052  982  ILE A CG2 
7378  C CD1 . ILE A 984  ? 0.2139 0.1788 0.1979 0.0048  0.0119  0.0054  982  ILE A CD1 
7379  N N   . ALA A 985  ? 0.1635 0.1376 0.1465 0.0032  0.0088  0.0029  983  ALA A N   
7380  C CA  . ALA A 985  ? 0.1663 0.1415 0.1494 0.0038  0.0080  0.0020  983  ALA A CA  
7381  C C   . ALA A 985  ? 0.1567 0.1336 0.1395 0.0020  0.0071  0.0031  983  ALA A C   
7382  O O   . ALA A 985  ? 0.1863 0.1611 0.1682 0.0024  0.0062  0.0031  983  ALA A O   
7383  C CB  . ALA A 985  ? 0.1793 0.1591 0.1646 0.0044  0.0082  -0.0001 983  ALA A CB  
7384  N N   . HIS A 986  ? 0.1632 0.1440 0.1470 -0.0001 0.0070  0.0040  984  HIS A N   
7385  C CA  . HIS A 986  ? 0.1648 0.1475 0.1492 -0.0022 0.0059  0.0056  984  HIS A CA  
7386  C C   . HIS A 986  ? 0.1772 0.1539 0.1604 -0.0023 0.0049  0.0067  984  HIS A C   
7387  O O   . HIS A 986  ? 0.1775 0.1529 0.1606 -0.0024 0.0036  0.0067  984  HIS A O   
7388  C CB  . HIS A 986  ? 0.1908 0.1789 0.1765 -0.0045 0.0061  0.0071  984  HIS A CB  
7389  C CG  . HIS A 986  ? 0.1794 0.1694 0.1664 -0.0071 0.0047  0.0096  984  HIS A CG  
7390  N ND1 . HIS A 986  ? 0.2625 0.2570 0.2507 -0.0094 0.0046  0.0119  984  HIS A ND1 
7391  C CD2 . HIS A 986  ? 0.2138 0.2021 0.2014 -0.0078 0.0032  0.0102  984  HIS A CD2 
7392  C CE1 . HIS A 986  ? 0.2507 0.2459 0.2406 -0.0117 0.0031  0.0143  984  HIS A CE1 
7393  N NE2 . HIS A 986  ? 0.2235 0.2146 0.2130 -0.0107 0.0021  0.0131  984  HIS A NE2 
7394  N N   . VAL A 987  ? 0.1852 0.1585 0.1677 -0.0021 0.0054  0.0076  985  VAL A N   
7395  C CA  . VAL A 987  ? 0.1730 0.1414 0.1550 -0.0022 0.0043  0.0084  985  VAL A CA  
7396  C C   . VAL A 987  ? 0.1843 0.1488 0.1643 0.0001  0.0041  0.0068  985  VAL A C   
7397  O O   . VAL A 987  ? 0.1958 0.1580 0.1755 0.0000  0.0027  0.0065  985  VAL A O   
7398  C CB  . VAL A 987  ? 0.1547 0.1209 0.1367 -0.0023 0.0049  0.0095  985  VAL A CB  
7399  C CG1 . VAL A 987  ? 0.1727 0.1336 0.1541 -0.0015 0.0039  0.0095  985  VAL A CG1 
7400  C CG2 . VAL A 987  ? 0.1767 0.1471 0.1607 -0.0048 0.0047  0.0115  985  VAL A CG2 
7401  N N   . THR A 988  ? 0.1720 0.1358 0.1507 0.0021  0.0055  0.0058  986  THR A N   
7402  C CA  . THR A 988  ? 0.1711 0.1317 0.1477 0.0042  0.0053  0.0049  986  THR A CA  
7403  C C   . THR A 988  ? 0.2037 0.1659 0.1803 0.0044  0.0042  0.0039  986  THR A C   
7404  O O   . THR A 988  ? 0.2562 0.2163 0.2311 0.0056  0.0034  0.0032  986  THR A O   
7405  C CB  . THR A 988  ? 0.2220 0.1816 0.1978 0.0061  0.0069  0.0048  986  THR A CB  
7406  O OG1 . THR A 988  ? 0.2308 0.1933 0.2081 0.0062  0.0073  0.0042  986  THR A OG1 
7407  C CG2 . THR A 988  ? 0.2421 0.2001 0.2179 0.0061  0.0079  0.0057  986  THR A CG2 
7408  N N   . SER A 989  ? 0.1926 0.1591 0.1711 0.0032  0.0041  0.0038  987  SER A N   
7409  C CA  . SER A 989  ? 0.2280 0.1963 0.2068 0.0033  0.0029  0.0030  987  SER A CA  
7410  C C   . SER A 989  ? 0.2497 0.2175 0.2291 0.0015  0.0011  0.0035  987  SER A C   
7411  O O   . SER A 989  ? 0.3076 0.2750 0.2866 0.0020  -0.0002 0.0026  987  SER A O   
7412  C CB  . SER A 989  ? 0.2638 0.2374 0.2446 0.0029  0.0034  0.0024  987  SER A CB  
7413  O OG  . SER A 989  ? 0.3466 0.3243 0.3293 0.0005  0.0032  0.0034  987  SER A OG  
7414  N N   . ARG A 990  ? 0.2040 0.1717 0.1847 -0.0004 0.0007  0.0048  988  ARG A N   
7415  C CA  . ARG A 990  ? 0.2131 0.1807 0.1957 -0.0025 -0.0013 0.0057  988  ARG A CA  
7416  C C   . ARG A 990  ? 0.2188 0.1809 0.2007 -0.0020 -0.0026 0.0053  988  ARG A C   
7417  O O   . ARG A 990  ? 0.2476 0.2085 0.2309 -0.0029 -0.0048 0.0051  988  ARG A O   
7418  C CB  . ARG A 990  ? 0.2445 0.2163 0.2298 -0.0053 -0.0013 0.0080  988  ARG A CB  
7419  C CG  . ARG A 990  ? 0.2997 0.2782 0.2860 -0.0059 -0.0002 0.0080  988  ARG A CG  
7420  C CD  . ARG A 990  ? 0.3419 0.3238 0.3299 -0.0070 -0.0016 0.0080  988  ARG A CD  
7421  N NE  . ARG A 990  ? 0.3203 0.3067 0.3113 -0.0103 -0.0025 0.0106  988  ARG A NE  
7422  C CZ  . ARG A 990  ? 0.2891 0.2795 0.2824 -0.0120 -0.0038 0.0114  988  ARG A CZ  
7423  N NH1 . ARG A 990  ? 0.3178 0.3079 0.3107 -0.0108 -0.0045 0.0096  988  ARG A NH1 
7424  N NH2 . ARG A 990  ? 0.2754 0.2708 0.2716 -0.0151 -0.0044 0.0144  988  ARG A NH2 
7425  N N   . ILE A 991  ? 0.1959 0.1549 0.1762 -0.0005 -0.0015 0.0051  989  ILE A N   
7426  C CA  . ILE A 991  ? 0.1986 0.1529 0.1783 0.0005  -0.0026 0.0042  989  ILE A CA  
7427  C C   . ILE A 991  ? 0.1922 0.1448 0.1695 0.0027  -0.0034 0.0019  989  ILE A C   
7428  O O   . ILE A 991  ? 0.2152 0.1695 0.1905 0.0041  -0.0023 0.0013  989  ILE A O   
7429  C CB  . ILE A 991  ? 0.1832 0.1356 0.1617 0.0018  -0.0009 0.0046  989  ILE A CB  
7430  C CG1 . ILE A 991  ? 0.2005 0.1487 0.1793 0.0026  -0.0022 0.0038  989  ILE A CG1 
7431  C CG2 . ILE A 991  ? 0.2106 0.1634 0.1862 0.0041  0.0012  0.0038  989  ILE A CG2 
7432  C CD1 . ILE A 991  ? 0.2272 0.1745 0.2097 0.0001  -0.0041 0.0054  989  ILE A CD1 
7433  N N   . LYS A 992  ? 0.1873 0.1369 0.1651 0.0030  -0.0055 0.0005  990  LYS A N   
7434  C CA  . LYS A 992  ? 0.2144 0.1628 0.1897 0.0052  -0.0064 -0.0021 990  LYS A CA  
7435  C C   . LYS A 992  ? 0.1904 0.1355 0.1641 0.0075  -0.0065 -0.0038 990  LYS A C   
7436  O O   . LYS A 992  ? 0.2457 0.1880 0.2211 0.0073  -0.0088 -0.0053 990  LYS A O   
7437  C CB  . LYS A 992  ? 0.2326 0.1810 0.2101 0.0038  -0.0094 -0.0030 990  LYS A CB  
7438  C CG  . LYS A 992  ? 0.3002 0.2527 0.2791 0.0019  -0.0092 -0.0016 990  LYS A CG  
7439  C CD  . LYS A 992  ? 0.3873 0.3400 0.3692 0.0002  -0.0123 -0.0022 990  LYS A CD  
7440  C CE  . LYS A 992  ? 0.4821 0.4398 0.4658 -0.0018 -0.0121 -0.0006 990  LYS A CE  
7441  N NZ  . LYS A 992  ? 0.5399 0.5002 0.5206 0.0002  -0.0102 -0.0012 990  LYS A NZ  
7442  N N   . ALA A 993  ? 0.2131 0.1587 0.1839 0.0095  -0.0041 -0.0036 991  ALA A N   
7443  C CA  . ALA A 993  ? 0.1963 0.1400 0.1654 0.0119  -0.0037 -0.0052 991  ALA A CA  
7444  C C   . ALA A 993  ? 0.1999 0.1456 0.1651 0.0144  -0.0016 -0.0053 991  ALA A C   
7445  O O   . ALA A 993  ? 0.2095 0.1574 0.1740 0.0141  -0.0002 -0.0035 991  ALA A O   
7446  C CB  . ALA A 993  ? 0.1979 0.1400 0.1689 0.0111  -0.0028 -0.0037 991  ALA A CB  
7447  N N   . GLY A 994  ? 0.1757 0.1212 0.1386 0.0170  -0.0017 -0.0073 992  GLY A N   
7448  C CA  . GLY A 994  ? 0.2018 0.1500 0.1609 0.0193  0.0000  -0.0072 992  GLY A CA  
7449  C C   . GLY A 994  ? 0.1844 0.1337 0.1429 0.0198  0.0028  -0.0047 992  GLY A C   
7450  O O   . GLY A 994  ? 0.1687 0.1204 0.1253 0.0208  0.0043  -0.0031 992  GLY A O   
7451  N N   . ASN A 995  ? 0.1634 0.1109 0.1240 0.0192  0.0034  -0.0042 993  ASN A N   
7452  C CA  . ASN A 995  ? 0.1843 0.1327 0.1447 0.0197  0.0059  -0.0020 993  ASN A CA  
7453  C C   . ASN A 995  ? 0.1699 0.1169 0.1336 0.0172  0.0062  -0.0002 993  ASN A C   
7454  O O   . ASN A 995  ? 0.1814 0.1264 0.1472 0.0165  0.0053  -0.0008 993  ASN A O   
7455  C CB  . ASN A 995  ? 0.1629 0.1118 0.1220 0.0220  0.0065  -0.0035 993  ASN A CB  
7456  C CG  . ASN A 995  ? 0.1818 0.1342 0.1371 0.0247  0.0071  -0.0043 993  ASN A CG  
7457  O OD1 . ASN A 995  ? 0.1856 0.1384 0.1392 0.0259  0.0054  -0.0071 993  ASN A OD1 
7458  N ND2 . ASN A 995  ? 0.1937 0.1488 0.1479 0.0253  0.0094  -0.0017 993  ASN A ND2 
7459  N N   . LEU A 996  ? 0.1641 0.1124 0.1285 0.0161  0.0074  0.0019  994  LEU A N   
7460  C CA  . LEU A 996  ? 0.1546 0.1025 0.1217 0.0138  0.0078  0.0034  994  LEU A CA  
7461  C C   . LEU A 996  ? 0.1449 0.0934 0.1124 0.0143  0.0099  0.0051  994  LEU A C   
7462  O O   . LEU A 996  ? 0.1604 0.1101 0.1264 0.0157  0.0112  0.0060  994  LEU A O   
7463  C CB  . LEU A 996  ? 0.1705 0.1198 0.1386 0.0124  0.0076  0.0040  994  LEU A CB  
7464  C CG  . LEU A 996  ? 0.1819 0.1314 0.1495 0.0121  0.0057  0.0026  994  LEU A CG  
7465  C CD1 . LEU A 996  ? 0.2154 0.1670 0.1843 0.0108  0.0057  0.0033  994  LEU A CD1 
7466  C CD2 . LEU A 996  ? 0.2114 0.1592 0.1805 0.0109  0.0038  0.0016  994  LEU A CD2 
7467  N N   . TYR A 997  ? 0.1543 0.1021 0.1240 0.0129  0.0101  0.0059  995  TYR A N   
7468  C CA  . TYR A 997  ? 0.1442 0.0925 0.1147 0.0131  0.0118  0.0074  995  TYR A CA  
7469  C C   . TYR A 997  ? 0.1519 0.1007 0.1250 0.0109  0.0118  0.0084  995  TYR A C   
7470  O O   . TYR A 997  ? 0.1684 0.1168 0.1428 0.0094  0.0106  0.0083  995  TYR A O   
7471  C CB  . TYR A 997  ? 0.1639 0.1112 0.1344 0.0144  0.0119  0.0069  995  TYR A CB  
7472  C CG  . TYR A 997  ? 0.1635 0.1113 0.1314 0.0169  0.0120  0.0054  995  TYR A CG  
7473  C CD1 . TYR A 997  ? 0.1748 0.1248 0.1411 0.0185  0.0138  0.0065  995  TYR A CD1 
7474  C CD2 . TYR A 997  ? 0.1790 0.1255 0.1462 0.0177  0.0102  0.0030  995  TYR A CD2 
7475  C CE1 . TYR A 997  ? 0.1812 0.1328 0.1447 0.0209  0.0140  0.0053  995  TYR A CE1 
7476  C CE2 . TYR A 997  ? 0.1873 0.1349 0.1518 0.0203  0.0102  0.0012  995  TYR A CE2 
7477  C CZ  . TYR A 997  ? 0.2121 0.1627 0.1746 0.0219  0.0122  0.0023  995  TYR A CZ  
7478  O OH  . TYR A 997  ? 0.2062 0.1590 0.1657 0.0245  0.0122  0.0006  995  TYR A OH  
7479  N N   . ILE A 998  ? 0.1512 0.1014 0.1252 0.0106  0.0130  0.0094  996  ILE A N   
7480  C CA  A ILE A 998  ? 0.1635 0.1150 0.1397 0.0088  0.0130  0.0099  996  ILE A CA  
7481  C CA  B ILE A 998  ? 0.1636 0.1151 0.1398 0.0088  0.0130  0.0099  996  ILE A CA  
7482  C C   . ILE A 998  ? 0.1522 0.1039 0.1298 0.0088  0.0141  0.0110  996  ILE A C   
7483  O O   . ILE A 998  ? 0.1576 0.1093 0.1353 0.0098  0.0152  0.0118  996  ILE A O   
7484  C CB  A ILE A 998  ? 0.1529 0.1059 0.1297 0.0085  0.0129  0.0094  996  ILE A CB  
7485  C CB  B ILE A 998  ? 0.1529 0.1059 0.1297 0.0085  0.0129  0.0095  996  ILE A CB  
7486  C CG1 A ILE A 998  ? 0.1957 0.1490 0.1714 0.0083  0.0117  0.0084  996  ILE A CG1 
7487  C CG1 B ILE A 998  ? 0.2085 0.1615 0.1838 0.0089  0.0119  0.0085  996  ILE A CG1 
7488  C CG2 A ILE A 998  ? 0.1704 0.1255 0.1495 0.0070  0.0130  0.0094  996  ILE A CG2 
7489  C CG2 B ILE A 998  ? 0.1689 0.1242 0.1478 0.0068  0.0127  0.0092  996  ILE A CG2 
7490  C CD1 A ILE A 998  ? 0.2225 0.1776 0.1990 0.0082  0.0115  0.0078  996  ILE A CD1 
7491  C CD1 B ILE A 998  ? 0.2142 0.1678 0.1899 0.0073  0.0106  0.0079  996  ILE A CD1 
7492  N N   . ASN A 999  ? 0.1457 0.0977 0.1246 0.0075  0.0138  0.0114  997  ASN A N   
7493  C CA  . ASN A 999  ? 0.1500 0.1026 0.1306 0.0072  0.0146  0.0124  997  ASN A CA  
7494  C C   . ASN A 999  ? 0.1514 0.1028 0.1315 0.0089  0.0156  0.0131  997  ASN A C   
7495  O O   . ASN A 999  ? 0.1682 0.1202 0.1496 0.0091  0.0167  0.0140  997  ASN A O   
7496  C CB  . ASN A 999  ? 0.1449 0.0992 0.1272 0.0066  0.0150  0.0123  997  ASN A CB  
7497  C CG  . ASN A 999  ? 0.1449 0.1016 0.1279 0.0049  0.0142  0.0114  997  ASN A CG  
7498  O OD1 . ASN A 999  ? 0.1626 0.1202 0.1456 0.0038  0.0134  0.0118  997  ASN A OD1 
7499  N ND2 . ASN A 999  ? 0.1720 0.1301 0.1559 0.0049  0.0141  0.0104  997  ASN A ND2 
7500  N N   . ARG A 1000 ? 0.1534 0.1035 0.1319 0.0101  0.0152  0.0124  998  ARG A N   
7501  C CA  . ARG A 1000 ? 0.1452 0.0949 0.1230 0.0121  0.0161  0.0126  998  ARG A CA  
7502  C C   . ARG A 1000 ? 0.1662 0.1143 0.1433 0.0129  0.0148  0.0111  998  ARG A C   
7503  O O   . ARG A 1000 ? 0.1838 0.1308 0.1612 0.0117  0.0132  0.0104  998  ARG A O   
7504  C CB  . ARG A 1000 ? 0.1526 0.1034 0.1288 0.0136  0.0173  0.0130  998  ARG A CB  
7505  C CG  . ARG A 1000 ? 0.1513 0.1018 0.1254 0.0139  0.0165  0.0120  998  ARG A CG  
7506  C CD  . ARG A 1000 ? 0.1770 0.1288 0.1488 0.0160  0.0174  0.0122  998  ARG A CD  
7507  N NE  . ARG A 1000 ? 0.1615 0.1135 0.1321 0.0178  0.0174  0.0109  998  ARG A NE  
7508  C CZ  . ARG A 1000 ? 0.1723 0.1262 0.1404 0.0200  0.0181  0.0107  998  ARG A CZ  
7509  N NH1 . ARG A 1000 ? 0.2025 0.1585 0.1694 0.0204  0.0189  0.0122  998  ARG A NH1 
7510  N NH2 . ARG A 1000 ? 0.1783 0.1325 0.1455 0.0218  0.0178  0.0087  998  ARG A NH2 
7511  N N   . ASN A 1001 ? 0.1568 0.1050 0.1334 0.0150  0.0154  0.0106  999  ASN A N   
7512  C CA  . ASN A 1001 ? 0.1471 0.0935 0.1233 0.0162  0.0139  0.0085  999  ASN A CA  
7513  C C   . ASN A 1001 ? 0.1660 0.1122 0.1396 0.0172  0.0132  0.0068  999  ASN A C   
7514  O O   . ASN A 1001 ? 0.1793 0.1268 0.1513 0.0171  0.0140  0.0074  999  ASN A O   
7515  C CB  . ASN A 1001 ? 0.1655 0.1127 0.1423 0.0184  0.0147  0.0079  999  ASN A CB  
7516  C CG  . ASN A 1001 ? 0.2150 0.1651 0.1893 0.0207  0.0165  0.0077  999  ASN A CG  
7517  O OD1 . ASN A 1001 ? 0.2020 0.1527 0.1738 0.0216  0.0163  0.0067  999  ASN A OD1 
7518  N ND2 . ASN A 1001 ? 0.2434 0.1958 0.2187 0.0216  0.0181  0.0089  999  ASN A ND2 
7519  N N   . ILE A 1002 ? 0.1525 0.0968 0.1262 0.0180  0.0113  0.0045  1000 ILE A N   
7520  C CA  . ILE A 1002 ? 0.1607 0.1047 0.1323 0.0187  0.0102  0.0026  1000 ILE A CA  
7521  C C   . ILE A 1002 ? 0.1858 0.1308 0.1553 0.0219  0.0102  0.0000  1000 ILE A C   
7522  O O   . ILE A 1002 ? 0.1899 0.1344 0.1580 0.0228  0.0087  -0.0024 1000 ILE A O   
7523  C CB  . ILE A 1002 ? 0.1594 0.1006 0.1329 0.0169  0.0076  0.0019  1000 ILE A CB  
7524  C CG1 . ILE A 1002 ? 0.1744 0.1129 0.1505 0.0174  0.0056  0.0005  1000 ILE A CG1 
7525  C CG2 . ILE A 1002 ? 0.1638 0.1054 0.1390 0.0138  0.0077  0.0044  1000 ILE A CG2 
7526  C CD1 . ILE A 1002 ? 0.1955 0.1313 0.1738 0.0156  0.0026  -0.0001 1000 ILE A CD1 
7527  N N   . ILE A 1003 ? 0.1688 0.1158 0.1381 0.0237  0.0119  0.0002  1001 ILE A N   
7528  C CA  . ILE A 1003 ? 0.1786 0.1277 0.1459 0.0270  0.0121  -0.0026 1001 ILE A CA  
7529  C C   . ILE A 1003 ? 0.1986 0.1526 0.1632 0.0284  0.0147  -0.0009 1001 ILE A C   
7530  O O   . ILE A 1003 ? 0.2000 0.1552 0.1650 0.0269  0.0164  0.0024  1001 ILE A O   
7531  C CB  . ILE A 1003 ? 0.1858 0.1339 0.1558 0.0285  0.0114  -0.0043 1001 ILE A CB  
7532  C CG1 . ILE A 1003 ? 0.2021 0.1514 0.1739 0.0278  0.0133  -0.0014 1001 ILE A CG1 
7533  C CG2 . ILE A 1003 ? 0.2130 0.1562 0.1861 0.0271  0.0083  -0.0056 1001 ILE A CG2 
7534  C CD1 . ILE A 1003 ? 0.2527 0.2026 0.2266 0.0302  0.0132  -0.0033 1001 ILE A CD1 
7535  N N   . GLY A 1004 ? 0.2048 0.1621 0.1670 0.0315  0.0150  -0.0033 1002 GLY A N   
7536  C CA  . GLY A 1004 ? 0.2153 0.1782 0.1751 0.0329  0.0176  -0.0015 1002 GLY A CA  
7537  C C   . GLY A 1004 ? 0.2129 0.1774 0.1703 0.0320  0.0182  0.0009  1002 GLY A C   
7538  O O   . GLY A 1004 ? 0.2141 0.1814 0.1715 0.0313  0.0202  0.0045  1002 GLY A O   
7539  N N   . ALA A 1005 ? 0.2089 0.1718 0.1646 0.0319  0.0163  -0.0011 1003 ALA A N   
7540  C CA  . ALA A 1005 ? 0.2076 0.1723 0.1611 0.0313  0.0167  0.0009  1003 ALA A CA  
7541  C C   . ALA A 1005 ? 0.2198 0.1910 0.1706 0.0334  0.0187  0.0026  1003 ALA A C   
7542  O O   . ALA A 1005 ? 0.2323 0.2072 0.1813 0.0361  0.0191  0.0003  1003 ALA A O   
7543  C CB  . ALA A 1005 ? 0.2123 0.1753 0.1642 0.0316  0.0143  -0.0022 1003 ALA A CB  
7544  N N   . VAL A 1006 ? 0.1809 0.1538 0.1317 0.0321  0.0199  0.0068  1004 VAL A N   
7545  C CA  . VAL A 1006 ? 0.1831 0.1623 0.1321 0.0334  0.0219  0.0098  1004 VAL A CA  
7546  C C   . VAL A 1006 ? 0.1939 0.1760 0.1395 0.0343  0.0212  0.0101  1004 VAL A C   
7547  O O   . VAL A 1006 ? 0.1926 0.1715 0.1387 0.0327  0.0200  0.0109  1004 VAL A O   
7548  C CB  . VAL A 1006 ? 0.2086 0.1876 0.1609 0.0313  0.0235  0.0148  1004 VAL A CB  
7549  C CG1 . VAL A 1006 ? 0.2349 0.2204 0.1859 0.0322  0.0252  0.0189  1004 VAL A CG1 
7550  C CG2 . VAL A 1006 ? 0.2231 0.2004 0.1785 0.0308  0.0242  0.0145  1004 VAL A CG2 
7551  N N   . VAL A 1007 ? 0.1946 0.1832 0.1367 0.0370  0.0220  0.0093  1005 VAL A N   
7552  C CA  . VAL A 1007 ? 0.1745 0.1669 0.1128 0.0382  0.0213  0.0095  1005 VAL A CA  
7553  C C   . VAL A 1007 ? 0.1919 0.1843 0.1315 0.0362  0.0217  0.0149  1005 VAL A C   
7554  O O   . VAL A 1007 ? 0.1934 0.1875 0.1352 0.0351  0.0234  0.0195  1005 VAL A O   
7555  C CB  . VAL A 1007 ? 0.1822 0.1832 0.1167 0.0414  0.0226  0.0086  1005 VAL A CB  
7556  C CG1 . VAL A 1007 ? 0.1927 0.1992 0.1233 0.0424  0.0222  0.0100  1005 VAL A CG1 
7557  C CG2 . VAL A 1007 ? 0.2149 0.2151 0.1483 0.0436  0.0215  0.0021  1005 VAL A CG2 
7558  N N   . GLY A 1008 ? 0.1882 0.1787 0.1268 0.0356  0.0199  0.0145  1006 GLY A N   
7559  C CA  . GLY A 1008 ? 0.1852 0.1756 0.1254 0.0340  0.0199  0.0193  1006 GLY A CA  
7560  C C   . GLY A 1008 ? 0.1990 0.1834 0.1441 0.0313  0.0198  0.0213  1006 GLY A C   
7561  O O   . GLY A 1008 ? 0.2106 0.1943 0.1578 0.0300  0.0195  0.0249  1006 GLY A O   
7562  N N   . VAL A 1009 ? 0.1820 0.1624 0.1293 0.0304  0.0200  0.0190  1007 VAL A N   
7563  C CA  . VAL A 1009 ? 0.1957 0.1711 0.1476 0.0279  0.0199  0.0203  1007 VAL A CA  
7564  C C   . VAL A 1009 ? 0.1808 0.1510 0.1334 0.0270  0.0182  0.0163  1007 VAL A C   
7565  O O   . VAL A 1009 ? 0.1848 0.1518 0.1396 0.0253  0.0172  0.0165  1007 VAL A O   
7566  C CB  . VAL A 1009 ? 0.1868 0.1627 0.1412 0.0274  0.0217  0.0221  1007 VAL A CB  
7567  C CG1 . VAL A 1009 ? 0.1866 0.1578 0.1457 0.0249  0.0214  0.0232  1007 VAL A CG1 
7568  C CG2 . VAL A 1009 ? 0.1879 0.1697 0.1418 0.0282  0.0233  0.0266  1007 VAL A CG2 
7569  N N   . GLN A 1010 ? 0.1885 0.1582 0.1397 0.0280  0.0178  0.0126  1008 GLN A N   
7570  C CA  . GLN A 1010 ? 0.1746 0.1403 0.1259 0.0273  0.0158  0.0088  1008 GLN A CA  
7571  C C   . GLN A 1010 ? 0.1989 0.1670 0.1466 0.0296  0.0147  0.0055  1008 GLN A C   
7572  O O   . GLN A 1010 ? 0.2265 0.1945 0.1736 0.0309  0.0145  0.0026  1008 GLN A O   
7573  C CB  . GLN A 1010 ? 0.1968 0.1591 0.1508 0.0262  0.0157  0.0074  1008 GLN A CB  
7574  C CG  . GLN A 1010 ? 0.1936 0.1543 0.1511 0.0242  0.0168  0.0102  1008 GLN A CG  
7575  C CD  . GLN A 1010 ? 0.1889 0.1517 0.1473 0.0248  0.0187  0.0121  1008 GLN A CD  
7576  O OE1 . GLN A 1010 ? 0.2039 0.1687 0.1607 0.0266  0.0192  0.0106  1008 GLN A OE1 
7577  N NE2 . GLN A 1010 ? 0.1949 0.1577 0.1559 0.0234  0.0197  0.0153  1008 GLN A NE2 
7578  N N   . PRO A 1011 ? 0.1986 0.1688 0.1439 0.0302  0.0139  0.0058  1009 PRO A N   
7579  C CA  . PRO A 1011 ? 0.2187 0.1907 0.1608 0.0322  0.0123  0.0020  1009 PRO A CA  
7580  C C   . PRO A 1011 ? 0.1893 0.1566 0.1330 0.0315  0.0104  -0.0021 1009 PRO A C   
7581  O O   . PRO A 1011 ? 0.1961 0.1593 0.1428 0.0292  0.0096  -0.0017 1009 PRO A O   
7582  C CB  . PRO A 1011 ? 0.2094 0.1825 0.1502 0.0319  0.0113  0.0032  1009 PRO A CB  
7583  C CG  . PRO A 1011 ? 0.2031 0.1776 0.1453 0.0310  0.0130  0.0083  1009 PRO A CG  
7584  C CD  . PRO A 1011 ? 0.2138 0.1846 0.1598 0.0292  0.0140  0.0093  1009 PRO A CD  
7585  N N   . PHE A 1012 ? 0.1967 0.1651 0.1388 0.0336  0.0095  -0.0060 1010 PHE A N   
7586  C CA  . PHE A 1012 ? 0.1797 0.1436 0.1245 0.0331  0.0078  -0.0093 1010 PHE A CA  
7587  C C   . PHE A 1012 ? 0.1914 0.1540 0.1355 0.0337  0.0048  -0.0135 1010 PHE A C   
7588  O O   . PHE A 1012 ? 0.2071 0.1734 0.1479 0.0362  0.0042  -0.0162 1010 PHE A O   
7589  C CB  . PHE A 1012 ? 0.1927 0.1579 0.1376 0.0351  0.0088  -0.0110 1010 PHE A CB  
7590  C CG  . PHE A 1012 ? 0.1781 0.1383 0.1265 0.0345  0.0070  -0.0137 1010 PHE A CG  
7591  C CD1 . PHE A 1012 ? 0.2199 0.1761 0.1721 0.0318  0.0072  -0.0113 1010 PHE A CD1 
7592  C CD2 . PHE A 1012 ? 0.2002 0.1599 0.1485 0.0365  0.0047  -0.0188 1010 PHE A CD2 
7593  C CE1 . PHE A 1012 ? 0.2101 0.1619 0.1658 0.0310  0.0054  -0.0132 1010 PHE A CE1 
7594  C CE2 . PHE A 1012 ? 0.2122 0.1668 0.1645 0.0358  0.0026  -0.0209 1010 PHE A CE2 
7595  C CZ  . PHE A 1012 ? 0.2239 0.1747 0.1799 0.0329  0.0030  -0.0178 1010 PHE A CZ  
7596  N N   . GLY A 1013 ? 0.1927 0.1504 0.1402 0.0314  0.0029  -0.0142 1011 GLY A N   
7597  C CA  . GLY A 1013 ? 0.2066 0.1625 0.1546 0.0316  -0.0003 -0.0182 1011 GLY A CA  
7598  C C   . GLY A 1013 ? 0.1946 0.1466 0.1458 0.0283  -0.0018 -0.0168 1011 GLY A C   
7599  O O   . GLY A 1013 ? 0.2214 0.1737 0.1731 0.0264  -0.0004 -0.0133 1011 GLY A O   
7600  N N   . GLY A 1014 ? 0.2204 0.1691 0.1742 0.0275  -0.0048 -0.0198 1012 GLY A N   
7601  C CA  . GLY A 1014 ? 0.2629 0.2088 0.2203 0.0243  -0.0063 -0.0183 1012 GLY A CA  
7602  C C   . GLY A 1014 ? 0.2497 0.1954 0.2074 0.0238  -0.0092 -0.0205 1012 GLY A C   
7603  O O   . GLY A 1014 ? 0.2934 0.2419 0.2478 0.0259  -0.0098 -0.0227 1012 GLY A O   
7604  N N   . ARG A 1015 ? 0.2277 0.1705 0.1896 0.0208  -0.0112 -0.0197 1013 ARG A N   
7605  C CA  . ARG A 1015 ? 0.2469 0.1896 0.2100 0.0195  -0.0138 -0.0209 1013 ARG A CA  
7606  C C   . ARG A 1015 ? 0.2410 0.1796 0.2092 0.0179  -0.0172 -0.0226 1013 ARG A C   
7607  O O   . ARG A 1015 ? 0.2068 0.1426 0.1775 0.0177  -0.0174 -0.0225 1013 ARG A O   
7608  C CB  . ARG A 1015 ? 0.2518 0.1963 0.2157 0.0170  -0.0127 -0.0173 1013 ARG A CB  
7609  C CG  . ARG A 1015 ? 0.2320 0.1749 0.1997 0.0141  -0.0118 -0.0141 1013 ARG A CG  
7610  C CD  . ARG A 1015 ? 0.2959 0.2410 0.2651 0.0116  -0.0113 -0.0113 1013 ARG A CD  
7611  N NE  . ARG A 1015 ? 0.3470 0.2934 0.3163 0.0113  -0.0135 -0.0127 1013 ARG A NE  
7612  C CZ  . ARG A 1015 ? 0.3699 0.3148 0.3426 0.0096  -0.0166 -0.0139 1013 ARG A CZ  
7613  N NH1 . ARG A 1015 ? 0.3085 0.2504 0.2852 0.0078  -0.0181 -0.0134 1013 ARG A NH1 
7614  N NH2 . ARG A 1015 ? 0.3727 0.3191 0.3452 0.0096  -0.0185 -0.0154 1013 ARG A NH2 
7615  N N   . GLY A 1016 ? 0.2262 0.1645 0.1964 0.0165  -0.0201 -0.0238 1014 GLY A N   
7616  C CA  . GLY A 1016 ? 0.2252 0.1595 0.2009 0.0145  -0.0237 -0.0249 1014 GLY A CA  
7617  C C   . GLY A 1016 ? 0.2310 0.1624 0.2074 0.0171  -0.0257 -0.0293 1014 GLY A C   
7618  O O   . GLY A 1016 ? 0.2453 0.1785 0.2180 0.0205  -0.0259 -0.0333 1014 GLY A O   
7619  N N   . LEU A 1017 ? 0.2287 0.1560 0.2102 0.0157  -0.0272 -0.0286 1015 LEU A N   
7620  C CA  . LEU A 1017 ? 0.2536 0.1776 0.2370 0.0181  -0.0293 -0.0328 1015 LEU A CA  
7621  C C   . LEU A 1017 ? 0.2295 0.1556 0.2082 0.0217  -0.0261 -0.0340 1015 LEU A C   
7622  O O   . LEU A 1017 ? 0.2396 0.1642 0.2191 0.0245  -0.0276 -0.0381 1015 LEU A O   
7623  C CB  . LEU A 1017 ? 0.2464 0.1656 0.2367 0.0154  -0.0316 -0.0307 1015 LEU A CB  
7624  C CG  . LEU A 1017 ? 0.2493 0.1661 0.2456 0.0118  -0.0354 -0.0294 1015 LEU A CG  
7625  C CD1 . LEU A 1017 ? 0.2760 0.1888 0.2789 0.0091  -0.0371 -0.0262 1015 LEU A CD1 
7626  C CD2 . LEU A 1017 ? 0.2802 0.1952 0.2780 0.0135  -0.0396 -0.0352 1015 LEU A CD2 
7627  N N   . SER A 1018 ? 0.2141 0.1440 0.1886 0.0217  -0.0220 -0.0306 1016 SER A N   
7628  C CA  . SER A 1018 ? 0.2272 0.1596 0.1977 0.0247  -0.0189 -0.0309 1016 SER A CA  
7629  C C   . SER A 1018 ? 0.2206 0.1576 0.1854 0.0280  -0.0179 -0.0338 1016 SER A C   
7630  O O   . SER A 1018 ? 0.2370 0.1767 0.1987 0.0309  -0.0157 -0.0347 1016 SER A O   
7631  C CB  . SER A 1018 ? 0.2224 0.1563 0.1919 0.0229  -0.0151 -0.0255 1016 SER A CB  
7632  O OG  . SER A 1018 ? 0.2388 0.1692 0.2131 0.0201  -0.0159 -0.0229 1016 SER A OG  
7633  N N   . GLY A 1019 ? 0.2343 0.1728 0.1976 0.0278  -0.0194 -0.0351 1017 GLY A N   
7634  C CA  . GLY A 1019 ? 0.3166 0.2601 0.2744 0.0312  -0.0187 -0.0380 1017 GLY A CA  
7635  C C   . GLY A 1019 ? 0.2458 0.1921 0.2012 0.0304  -0.0191 -0.0372 1017 GLY A C   
7636  O O   . GLY A 1019 ? 0.2595 0.2043 0.2174 0.0273  -0.0196 -0.0342 1017 GLY A O   
7637  N N   . THR A 1020 ? 0.2480 0.1990 0.1986 0.0335  -0.0190 -0.0399 1018 THR A N   
7638  C CA  . THR A 1020 ? 0.2340 0.1886 0.1817 0.0335  -0.0195 -0.0396 1018 THR A CA  
7639  C C   . THR A 1020 ? 0.2488 0.2075 0.1927 0.0335  -0.0158 -0.0348 1018 THR A C   
7640  O O   . THR A 1020 ? 0.2425 0.2031 0.1853 0.0325  -0.0160 -0.0329 1018 THR A O   
7641  C CB  . THR A 1020 ? 0.2070 0.1653 0.1513 0.0370  -0.0216 -0.0452 1018 THR A CB  
7642  O OG1 . THR A 1020 ? 0.2296 0.1921 0.1698 0.0403  -0.0191 -0.0461 1018 THR A OG1 
7643  C CG2 . THR A 1020 ? 0.2916 0.2456 0.2402 0.0371  -0.0259 -0.0507 1018 THR A CG2 
7644  N N   . GLY A 1021 ? 0.2101 0.1703 0.1523 0.0347  -0.0127 -0.0327 1019 GLY A N   
7645  C CA  . GLY A 1021 ? 0.2388 0.2040 0.1771 0.0356  -0.0096 -0.0290 1019 GLY A CA  
7646  C C   . GLY A 1021 ? 0.2519 0.2232 0.1850 0.0388  -0.0101 -0.0314 1019 GLY A C   
7647  O O   . GLY A 1021 ? 0.2406 0.2124 0.1732 0.0404  -0.0129 -0.0367 1019 GLY A O   
7648  N N   . PRO A 1022 ? 0.2245 0.2010 0.1541 0.0397  -0.0076 -0.0277 1020 PRO A N   
7649  C CA  . PRO A 1022 ? 0.2384 0.2146 0.1687 0.0381  -0.0045 -0.0218 1020 PRO A CA  
7650  C C   . PRO A 1022 ? 0.2247 0.2000 0.1560 0.0385  -0.0022 -0.0209 1020 PRO A C   
7651  O O   . PRO A 1022 ? 0.2500 0.2261 0.1807 0.0406  -0.0025 -0.0246 1020 PRO A O   
7652  C CB  . PRO A 1022 ? 0.2467 0.2294 0.1728 0.0396  -0.0033 -0.0189 1020 PRO A CB  
7653  C CG  . PRO A 1022 ? 0.2581 0.2461 0.1801 0.0429  -0.0045 -0.0234 1020 PRO A CG  
7654  C CD  . PRO A 1022 ? 0.2510 0.2344 0.1754 0.0425  -0.0079 -0.0291 1020 PRO A CD  
7655  N N   . LYS A 1023 ? 0.2007 0.1747 0.1339 0.0367  0.0002  -0.0161 1021 LYS A N   
7656  C CA  . LYS A 1023 ? 0.1998 0.1730 0.1343 0.0368  0.0024  -0.0148 1021 LYS A CA  
7657  C C   . LYS A 1023 ? 0.1952 0.1748 0.1259 0.0397  0.0044  -0.0145 1021 LYS A C   
7658  O O   . LYS A 1023 ? 0.2005 0.1854 0.1282 0.0406  0.0054  -0.0118 1021 LYS A O   
7659  C CB  . LYS A 1023 ? 0.2105 0.1813 0.1478 0.0342  0.0043  -0.0098 1021 LYS A CB  
7660  C CG  . LYS A 1023 ? 0.1887 0.1537 0.1302 0.0313  0.0030  -0.0099 1021 LYS A CG  
7661  C CD  . LYS A 1023 ? 0.1806 0.1447 0.1241 0.0293  0.0048  -0.0052 1021 LYS A CD  
7662  C CE  . LYS A 1023 ? 0.2092 0.1687 0.1570 0.0265  0.0042  -0.0050 1021 LYS A CE  
7663  N NZ  . LYS A 1023 ? 0.1848 0.1419 0.1344 0.0262  0.0046  -0.0059 1021 LYS A NZ  
7664  N N   . ALA A 1024 ? 0.2126 0.1923 0.1439 0.0412  0.0049  -0.0169 1022 ALA A N   
7665  C CA  . ALA A 1024 ? 0.1922 0.1782 0.1207 0.0436  0.0073  -0.0160 1022 ALA A CA  
7666  C C   . ALA A 1024 ? 0.2027 0.1895 0.1325 0.0419  0.0102  -0.0098 1022 ALA A C   
7667  O O   . ALA A 1024 ? 0.2271 0.2083 0.1607 0.0392  0.0104  -0.0075 1022 ALA A O   
7668  C CB  . ALA A 1024 ? 0.2229 0.2082 0.1525 0.0455  0.0071  -0.0203 1022 ALA A CB  
7669  N N   . GLY A 1025 ? 0.1947 0.1885 0.1215 0.0435  0.0123  -0.0069 1023 GLY A N   
7670  C CA  . GLY A 1025 ? 0.2101 0.2048 0.1387 0.0418  0.0147  -0.0007 1023 GLY A CA  
7671  C C   . GLY A 1025 ? 0.2046 0.1960 0.1349 0.0393  0.0141  0.0030  1023 GLY A C   
7672  O O   . GLY A 1025 ? 0.1992 0.1884 0.1326 0.0373  0.0154  0.0071  1023 GLY A O   
7673  N N   . GLY A 1026 ? 0.1829 0.1743 0.1115 0.0395  0.0120  0.0013  1024 GLY A N   
7674  C CA  . GLY A 1026 ? 0.1860 0.1749 0.1162 0.0374  0.0113  0.0044  1024 GLY A CA  
7675  C C   . GLY A 1026 ? 0.1950 0.1894 0.1216 0.0389  0.0104  0.0055  1024 GLY A C   
7676  O O   . GLY A 1026 ? 0.2172 0.2173 0.1397 0.0414  0.0103  0.0032  1024 GLY A O   
7677  N N   . PRO A 1027 ? 0.1765 0.1695 0.1047 0.0374  0.0098  0.0088  1025 PRO A N   
7678  C CA  . PRO A 1027 ? 0.2021 0.2007 0.1274 0.0385  0.0093  0.0114  1025 PRO A CA  
7679  C C   . PRO A 1027 ? 0.1740 0.1740 0.0964 0.0396  0.0067  0.0073  1025 PRO A C   
7680  O O   . PRO A 1027 ? 0.2141 0.2197 0.1334 0.0409  0.0062  0.0091  1025 PRO A O   
7681  C CB  . PRO A 1027 ? 0.2083 0.2039 0.1376 0.0363  0.0093  0.0164  1025 PRO A CB  
7682  C CG  . PRO A 1027 ? 0.2212 0.2092 0.1545 0.0343  0.0087  0.0138  1025 PRO A CG  
7683  C CD  . PRO A 1027 ? 0.1856 0.1724 0.1186 0.0347  0.0097  0.0107  1025 PRO A CD  
7684  N N   . LEU A 1028 ? 0.1906 0.1858 0.1139 0.0392  0.0050  0.0022  1026 LEU A N   
7685  C CA  . LEU A 1028 ? 0.2040 0.2002 0.1251 0.0402  0.0023  -0.0021 1026 LEU A CA  
7686  C C   . LEU A 1028 ? 0.1978 0.1977 0.1153 0.0428  0.0018  -0.0072 1026 LEU A C   
7687  O O   . LEU A 1028 ? 0.2225 0.2241 0.1377 0.0440  -0.0006 -0.0111 1026 LEU A O   
7688  C CB  . LEU A 1028 ? 0.2032 0.1925 0.1280 0.0379  0.0004  -0.0046 1026 LEU A CB  
7689  C CG  . LEU A 1028 ? 0.2035 0.1906 0.1313 0.0359  0.0000  -0.0009 1026 LEU A CG  
7690  C CD1 . LEU A 1028 ? 0.2571 0.2379 0.1892 0.0335  -0.0011 -0.0028 1026 LEU A CD1 
7691  C CD2 . LEU A 1028 ? 0.2545 0.2459 0.1795 0.0371  -0.0018 -0.0009 1026 LEU A CD2 
7692  N N   . TYR A 1029 ? 0.1944 0.1957 0.1114 0.0439  0.0038  -0.0075 1027 TYR A N   
7693  C CA  . TYR A 1029 ? 0.2061 0.2101 0.1208 0.0465  0.0031  -0.0132 1027 TYR A CA  
7694  C C   . TYR A 1029 ? 0.2182 0.2310 0.1273 0.0494  0.0025  -0.0146 1027 TYR A C   
7695  O O   . TYR A 1029 ? 0.2200 0.2338 0.1274 0.0511  0.0001  -0.0205 1027 TYR A O   
7696  C CB  . TYR A 1029 ? 0.2263 0.2309 0.1419 0.0471  0.0057  -0.0124 1027 TYR A CB  
7697  C CG  . TYR A 1029 ? 0.1914 0.1952 0.1070 0.0490  0.0048  -0.0186 1027 TYR A CG  
7698  C CD1 . TYR A 1029 ? 0.2137 0.2097 0.1330 0.0477  0.0026  -0.0224 1027 TYR A CD1 
7699  C CD2 . TYR A 1029 ? 0.2126 0.2237 0.1250 0.0522  0.0063  -0.0202 1027 TYR A CD2 
7700  C CE1 . TYR A 1029 ? 0.2254 0.2201 0.1457 0.0495  0.0016  -0.0279 1027 TYR A CE1 
7701  C CE2 . TYR A 1029 ? 0.2318 0.2419 0.1449 0.0543  0.0054  -0.0262 1027 TYR A CE2 
7702  C CZ  . TYR A 1029 ? 0.2066 0.2081 0.1239 0.0529  0.0030  -0.0299 1027 TYR A CZ  
7703  O OH  . TYR A 1029 ? 0.2384 0.2384 0.1572 0.0549  0.0018  -0.0357 1027 TYR A OH  
7704  N N   . LEU A 1030 ? 0.1941 0.2139 0.1006 0.0501  0.0047  -0.0094 1028 LEU A N   
7705  C CA  . LEU A 1030 ? 0.2143 0.2440 0.1152 0.0531  0.0044  -0.0103 1028 LEU A CA  
7706  C C   . LEU A 1030 ? 0.2236 0.2537 0.1229 0.0532  0.0015  -0.0123 1028 LEU A C   
7707  O O   . LEU A 1030 ? 0.2362 0.2724 0.1312 0.0558  0.0000  -0.0165 1028 LEU A O   
7708  C CB  . LEU A 1030 ? 0.2603 0.2974 0.1595 0.0532  0.0072  -0.0031 1028 LEU A CB  
7709  C CG  . LEU A 1030 ? 0.2572 0.2964 0.1574 0.0535  0.0103  -0.0007 1028 LEU A CG  
7710  C CD1 . LEU A 1030 ? 0.2556 0.3030 0.1542 0.0536  0.0126  0.0069  1028 LEU A CD1 
7711  C CD2 . LEU A 1030 ? 0.2820 0.3250 0.1797 0.0567  0.0105  -0.0074 1028 LEU A CD2 
7712  N N   . GLY A 1031 ? 0.2150 0.2389 0.1177 0.0504  0.0004  -0.0095 1029 GLY A N   
7713  C CA  . GLY A 1031 ? 0.2673 0.2918 0.1689 0.0503  -0.0024 -0.0108 1029 GLY A CA  
7714  C C   . GLY A 1031 ? 0.2537 0.2758 0.1549 0.0513  -0.0055 -0.0186 1029 GLY A C   
7715  O O   . GLY A 1031 ? 0.2513 0.2765 0.1503 0.0521  -0.0079 -0.0208 1029 GLY A O   
7716  N N   . ARG A 1032 ? 0.2437 0.2605 0.1475 0.0511  -0.0057 -0.0228 1030 ARG A N   
7717  C CA  . ARG A 1032 ? 0.2100 0.2242 0.1144 0.0520  -0.0089 -0.0303 1030 ARG A CA  
7718  C C   . ARG A 1032 ? 0.2323 0.2544 0.1317 0.0559  -0.0095 -0.0355 1030 ARG A C   
7719  O O   . ARG A 1032 ? 0.2611 0.2825 0.1604 0.0572  -0.0128 -0.0421 1030 ARG A O   
7720  C CB  . ARG A 1032 ? 0.2469 0.2526 0.1564 0.0503  -0.0089 -0.0324 1030 ARG A CB  
7721  C CG  . ARG A 1032 ? 0.2480 0.2488 0.1601 0.0502  -0.0126 -0.0390 1030 ARG A CG  
7722  C CD  . ARG A 1032 ? 0.2680 0.2645 0.1829 0.0474  -0.0150 -0.0381 1030 ARG A CD  
7723  N NE  . ARG A 1032 ? 0.2675 0.2587 0.1860 0.0468  -0.0187 -0.0438 1030 ARG A NE  
7724  C CZ  . ARG A 1032 ? 0.3046 0.2968 0.2228 0.0471  -0.0221 -0.0477 1030 ARG A CZ  
7725  N NH1 . ARG A 1032 ? 0.3074 0.3059 0.2214 0.0483  -0.0225 -0.0468 1030 ARG A NH1 
7726  N NH2 . ARG A 1032 ? 0.3358 0.3225 0.2582 0.0462  -0.0255 -0.0524 1030 ARG A NH2 
7727  N N   . LEU A 1033 ? 0.2195 0.2495 0.1151 0.0580  -0.0067 -0.0327 1031 LEU A N   
7728  C CA  . LEU A 1033 ? 0.2256 0.2642 0.1165 0.0620  -0.0067 -0.0375 1031 LEU A CA  
7729  C C   . LEU A 1033 ? 0.2659 0.3152 0.1509 0.0639  -0.0069 -0.0360 1031 LEU A C   
7730  O O   . LEU A 1033 ? 0.2569 0.3158 0.1372 0.0674  -0.0062 -0.0386 1031 LEU A O   
7731  C CB  . LEU A 1033 ? 0.2300 0.2713 0.1209 0.0630  -0.0031 -0.0354 1031 LEU A CB  
7732  C CG  . LEU A 1033 ? 0.2496 0.2809 0.1463 0.0611  -0.0029 -0.0366 1031 LEU A CG  
7733  C CD1 . LEU A 1033 ? 0.2498 0.2842 0.1466 0.0621  0.0006  -0.0344 1031 LEU A CD1 
7734  C CD2 . LEU A 1033 ? 0.3224 0.3486 0.2212 0.0621  -0.0064 -0.0450 1031 LEU A CD2 
7735  N N   . VAL A 1034 ? 0.2534 0.3016 0.1386 0.0619  -0.0079 -0.0318 1032 VAL A N   
7736  C CA  . VAL A 1034 ? 0.2516 0.3092 0.1318 0.0635  -0.0087 -0.0302 1032 VAL A CA  
7737  C C   . VAL A 1034 ? 0.2766 0.3298 0.1582 0.0623  -0.0126 -0.0331 1032 VAL A C   
7738  O O   . VAL A 1034 ? 0.2740 0.3172 0.1608 0.0597  -0.0139 -0.0343 1032 VAL A O   
7739  C CB  . VAL A 1034 ? 0.2675 0.3293 0.1470 0.0621  -0.0060 -0.0205 1032 VAL A CB  
7740  C CG1 . VAL A 1034 ? 0.2718 0.3402 0.1493 0.0636  -0.0023 -0.0175 1032 VAL A CG1 
7741  C CG2 . VAL A 1034 ? 0.2577 0.3091 0.1431 0.0582  -0.0056 -0.0156 1032 VAL A CG2 
7742  N N   . THR A 1035 ? 0.2859 0.3472 0.1629 0.0641  -0.0143 -0.0338 1033 THR A N   
7743  C CA  . THR A 1035 ? 0.3119 0.3701 0.1902 0.0632  -0.0182 -0.0371 1033 THR A CA  
7744  C C   . THR A 1035 ? 0.3467 0.3995 0.2287 0.0598  -0.0181 -0.0305 1033 THR A C   
7745  O O   . THR A 1035 ? 0.3759 0.4216 0.2619 0.0577  -0.0205 -0.0326 1033 THR A O   
7746  C CB  . THR A 1035 ? 0.3414 0.4103 0.2135 0.0663  -0.0203 -0.0405 1033 THR A CB  
7747  O OG1 . THR A 1035 ? 0.4627 0.5410 0.3306 0.0671  -0.0180 -0.0332 1033 THR A OG1 
7748  C CG2 . THR A 1035 ? 0.3068 0.3805 0.1759 0.0699  -0.0209 -0.0484 1033 THR A CG2 
7749  N N   . THR A 1036 ? 0.2849 0.3412 0.1660 0.0592  -0.0154 -0.0224 1034 THR A N   
7750  C CA  . THR A 1036 ? 0.3131 0.3647 0.1981 0.0563  -0.0151 -0.0160 1034 THR A CA  
7751  C C   . THR A 1036 ? 0.2828 0.3306 0.1710 0.0546  -0.0116 -0.0104 1034 THR A C   
7752  O O   . THR A 1036 ? 0.2916 0.3458 0.1771 0.0558  -0.0091 -0.0064 1034 THR A O   
7753  C CB  . THR A 1036 ? 0.3564 0.4162 0.2380 0.0571  -0.0159 -0.0113 1034 THR A CB  
7754  O OG1 . THR A 1036 ? 0.3601 0.4251 0.2379 0.0592  -0.0191 -0.0170 1034 THR A OG1 
7755  C CG2 . THR A 1036 ? 0.3974 0.4517 0.2838 0.0544  -0.0164 -0.0058 1034 THR A CG2 
7756  N N   . ALA A 1037 ? 0.2693 0.3071 0.1632 0.0519  -0.0115 -0.0100 1035 ALA A N   
7757  C CA  . ALA A 1037 ? 0.2597 0.2932 0.1570 0.0503  -0.0085 -0.0060 1035 ALA A CA  
7758  C C   . ALA A 1037 ? 0.2752 0.3107 0.1736 0.0493  -0.0070 0.0024  1035 ALA A C   
7759  O O   . ALA A 1037 ? 0.2818 0.3170 0.1815 0.0485  -0.0086 0.0048  1035 ALA A O   
7760  C CB  . ALA A 1037 ? 0.2870 0.3102 0.1900 0.0477  -0.0091 -0.0083 1035 ALA A CB  
7761  N N   . PRO A 1038 ? 0.2473 0.2850 0.1457 0.0493  -0.0041 0.0069  1036 PRO A N   
7762  C CA  . PRO A 1038 ? 0.2381 0.2765 0.1391 0.0480  -0.0029 0.0150  1036 PRO A CA  
7763  C C   . PRO A 1038 ? 0.2487 0.2772 0.1561 0.0452  -0.0027 0.0164  1036 PRO A C   
7764  O O   . PRO A 1038 ? 0.2412 0.2632 0.1510 0.0442  -0.0030 0.0118  1036 PRO A O   
7765  C CB  . PRO A 1038 ? 0.2500 0.2940 0.1491 0.0489  0.0001  0.0185  1036 PRO A CB  
7766  C CG  . PRO A 1038 ? 0.2701 0.3105 0.1690 0.0494  0.0010  0.0125  1036 PRO A CG  
7767  C CD  . PRO A 1038 ? 0.2805 0.3202 0.1773 0.0506  -0.0019 0.0048  1036 PRO A CD  
7768  N N   . VAL A 1039 ? 0.2302 0.2581 0.1409 0.0440  -0.0023 0.0229  1037 VAL A N   
7769  C CA  . VAL A 1039 ? 0.2250 0.2446 0.1420 0.0416  -0.0018 0.0246  1037 VAL A CA  
7770  C C   . VAL A 1039 ? 0.1966 0.2148 0.1152 0.0410  0.0010  0.0267  1037 VAL A C   
7771  O O   . VAL A 1039 ? 0.2277 0.2508 0.1458 0.0413  0.0024  0.0321  1037 VAL A O   
7772  C CB  . VAL A 1039 ? 0.2167 0.2360 0.1372 0.0408  -0.0029 0.0304  1037 VAL A CB  
7773  C CG1 . VAL A 1039 ? 0.2540 0.2652 0.1812 0.0387  -0.0026 0.0313  1037 VAL A CG1 
7774  C CG2 . VAL A 1039 ? 0.2730 0.2946 0.1919 0.0416  -0.0057 0.0286  1037 VAL A CG2 
7775  N N   . PRO A 1040 ? 0.2042 0.2164 0.1249 0.0399  0.0018  0.0228  1038 PRO A N   
7776  C CA  . PRO A 1040 ? 0.2367 0.2479 0.1589 0.0394  0.0043  0.0246  1038 PRO A CA  
7777  C C   . PRO A 1040 ? 0.2322 0.2409 0.1594 0.0377  0.0051  0.0308  1038 PRO A C   
7778  O O   . PRO A 1040 ? 0.2098 0.2153 0.1404 0.0367  0.0036  0.0324  1038 PRO A O   
7779  C CB  . PRO A 1040 ? 0.2184 0.2230 0.1423 0.0384  0.0043  0.0190  1038 PRO A CB  
7780  C CG  . PRO A 1040 ? 0.2561 0.2600 0.1781 0.0390  0.0018  0.0138  1038 PRO A CG  
7781  C CD  . PRO A 1040 ? 0.2262 0.2329 0.1480 0.0392  0.0002  0.0167  1038 PRO A CD  
7782  N N   . PRO A 1041 ? 0.2103 0.2206 0.1385 0.0374  0.0073  0.0343  1039 PRO A N   
7783  C CA  . PRO A 1041 ? 0.2034 0.2103 0.1375 0.0356  0.0079  0.0396  1039 PRO A CA  
7784  C C   . PRO A 1041 ? 0.2127 0.2111 0.1515 0.0338  0.0071  0.0368  1039 PRO A C   
7785  O O   . PRO A 1041 ? 0.2089 0.2038 0.1472 0.0335  0.0073  0.0316  1039 PRO A O   
7786  C CB  . PRO A 1041 ? 0.2413 0.2508 0.1752 0.0355  0.0104  0.0420  1039 PRO A CB  
7787  C CG  . PRO A 1041 ? 0.2817 0.2985 0.2091 0.0378  0.0112  0.0395  1039 PRO A CG  
7788  C CD  . PRO A 1041 ? 0.2571 0.2717 0.1819 0.0386  0.0093  0.0329  1039 PRO A CD  
7789  N N   . GLN A 1042 ? 0.2098 0.2052 0.1536 0.0327  0.0060  0.0402  1040 GLN A N   
7790  C CA  . GLN A 1042 ? 0.2101 0.1985 0.1591 0.0312  0.0053  0.0381  1040 GLN A CA  
7791  C C   . GLN A 1042 ? 0.2124 0.1984 0.1602 0.0312  0.0038  0.0325  1040 GLN A C   
7792  O O   . GLN A 1042 ? 0.2224 0.2035 0.1738 0.0300  0.0035  0.0301  1040 GLN A O   
7793  C CB  . GLN A 1042 ? 0.2538 0.2386 0.2052 0.0299  0.0072  0.0373  1040 GLN A CB  
7794  C CG  . GLN A 1042 ? 0.2765 0.2638 0.2293 0.0297  0.0087  0.0426  1040 GLN A CG  
7795  C CD  . GLN A 1042 ? 0.3271 0.3109 0.2826 0.0284  0.0103  0.0414  1040 GLN A CD  
7796  O OE1 . GLN A 1042 ? 0.4658 0.4460 0.4268 0.0271  0.0102  0.0434  1040 GLN A OE1 
7797  N NE2 . GLN A 1042 ? 0.4077 0.3924 0.3595 0.0289  0.0116  0.0378  1040 GLN A NE2 
7798  N N   . HIS A 1043 ? 0.2039 0.1937 0.1470 0.0326  0.0028  0.0305  1041 HIS A N   
7799  C CA  . HIS A 1043 ? 0.1875 0.1753 0.1294 0.0325  0.0014  0.0250  1041 HIS A CA  
7800  C C   . HIS A 1043 ? 0.1998 0.1872 0.1441 0.0324  -0.0008 0.0257  1041 HIS A C   
7801  O O   . HIS A 1043 ? 0.2097 0.2014 0.1513 0.0337  -0.0021 0.0267  1041 HIS A O   
7802  C CB  . HIS A 1043 ? 0.2090 0.2009 0.1451 0.0340  0.0012  0.0218  1041 HIS A CB  
7803  C CG  . HIS A 1043 ? 0.2022 0.1922 0.1373 0.0339  -0.0005 0.0163  1041 HIS A CG  
7804  N ND1 . HIS A 1043 ? 0.1999 0.1863 0.1355 0.0330  -0.0003 0.0121  1041 HIS A ND1 
7805  C CD2 . HIS A 1043 ? 0.2043 0.1959 0.1382 0.0344  -0.0028 0.0146  1041 HIS A CD2 
7806  C CE1 . HIS A 1043 ? 0.2058 0.1914 0.1409 0.0328  -0.0023 0.0082  1041 HIS A CE1 
7807  N NE2 . HIS A 1043 ? 0.2106 0.1994 0.1446 0.0337  -0.0038 0.0095  1041 HIS A NE2 
7808  N N   . SER A 1044 ? 0.1728 0.1556 0.1220 0.0311  -0.0012 0.0249  1042 SER A N   
7809  C CA  . SER A 1044 ? 0.1940 0.1762 0.1462 0.0311  -0.0032 0.0248  1042 SER A CA  
7810  C C   . SER A 1044 ? 0.1920 0.1696 0.1490 0.0296  -0.0031 0.0224  1042 SER A C   
7811  O O   . SER A 1044 ? 0.2024 0.1773 0.1606 0.0286  -0.0015 0.0218  1042 SER A O   
7812  C CB  . SER A 1044 ? 0.2152 0.1991 0.1697 0.0319  -0.0040 0.0302  1042 SER A CB  
7813  O OG  . SER A 1044 ? 0.1987 0.1795 0.1580 0.0310  -0.0030 0.0330  1042 SER A OG  
7814  N N   . SER A 1045 ? 0.1864 0.1636 0.1461 0.0296  -0.0048 0.0211  1043 SER A N   
7815  C CA  . SER A 1045 ? 0.1719 0.1461 0.1363 0.0284  -0.0048 0.0189  1043 SER A CA  
7816  C C   . SER A 1045 ? 0.1715 0.1463 0.1399 0.0291  -0.0067 0.0196  1043 SER A C   
7817  O O   . SER A 1045 ? 0.1871 0.1646 0.1539 0.0299  -0.0083 0.0194  1043 SER A O   
7818  C CB  . SER A 1045 ? 0.1755 0.1490 0.1385 0.0272  -0.0047 0.0144  1043 SER A CB  
7819  O OG  . SER A 1045 ? 0.1846 0.1565 0.1521 0.0261  -0.0047 0.0126  1043 SER A OG  
7820  N N   . VAL A 1046 ? 0.1818 0.1543 0.1557 0.0288  -0.0067 0.0199  1044 VAL A N   
7821  C CA  . VAL A 1046 ? 0.1949 0.1679 0.1734 0.0297  -0.0085 0.0199  1044 VAL A CA  
7822  C C   . VAL A 1046 ? 0.1819 0.1558 0.1617 0.0290  -0.0091 0.0155  1044 VAL A C   
7823  O O   . VAL A 1046 ? 0.2074 0.1825 0.1908 0.0298  -0.0106 0.0149  1044 VAL A O   
7824  C CB  . VAL A 1046 ? 0.1969 0.1673 0.1817 0.0301  -0.0088 0.0217  1044 VAL A CB  
7825  C CG1 . VAL A 1046 ? 0.2299 0.1999 0.2144 0.0305  -0.0086 0.0269  1044 VAL A CG1 
7826  C CG2 . VAL A 1046 ? 0.1978 0.1659 0.1849 0.0289  -0.0074 0.0188  1044 VAL A CG2 
7827  N N   . HIS A 1047 ? 0.1795 0.1533 0.1566 0.0276  -0.0079 0.0127  1045 HIS A N   
7828  C CA  . HIS A 1047 ? 0.1800 0.1552 0.1587 0.0266  -0.0082 0.0091  1045 HIS A CA  
7829  C C   . HIS A 1047 ? 0.2104 0.1881 0.1860 0.0265  -0.0097 0.0079  1045 HIS A C   
7830  O O   . HIS A 1047 ? 0.2136 0.1917 0.1848 0.0268  -0.0098 0.0086  1045 HIS A O   
7831  C CB  . HIS A 1047 ? 0.2047 0.1783 0.1828 0.0248  -0.0065 0.0072  1045 HIS A CB  
7832  C CG  . HIS A 1047 ? 0.2470 0.2182 0.2281 0.0249  -0.0052 0.0082  1045 HIS A CG  
7833  N ND1 . HIS A 1047 ? 0.2762 0.2475 0.2625 0.0254  -0.0057 0.0073  1045 HIS A ND1 
7834  C CD2 . HIS A 1047 ? 0.2905 0.2592 0.2702 0.0246  -0.0038 0.0100  1045 HIS A CD2 
7835  C CE1 . HIS A 1047 ? 0.2958 0.2646 0.2840 0.0253  -0.0047 0.0084  1045 HIS A CE1 
7836  N NE2 . HIS A 1047 ? 0.3111 0.2783 0.2954 0.0248  -0.0035 0.0102  1045 HIS A NE2 
7837  N N   . THR A 1048 ? 0.1933 0.1735 0.1719 0.0264  -0.0109 0.0060  1046 THR A N   
7838  C CA  . THR A 1048 ? 0.1911 0.1740 0.1678 0.0262  -0.0125 0.0046  1046 THR A CA  
7839  C C   . THR A 1048 ? 0.1842 0.1683 0.1621 0.0241  -0.0123 0.0017  1046 THR A C   
7840  O O   . THR A 1048 ? 0.2141 0.1993 0.1960 0.0236  -0.0117 0.0005  1046 THR A O   
7841  C CB  . THR A 1048 ? 0.1972 0.1827 0.1767 0.0278  -0.0145 0.0054  1046 THR A CB  
7842  O OG1 . THR A 1048 ? 0.2275 0.2119 0.2067 0.0295  -0.0147 0.0089  1046 THR A OG1 
7843  C CG2 . THR A 1048 ? 0.2397 0.2281 0.2168 0.0276  -0.0163 0.0042  1046 THR A CG2 
7844  N N   . ASP A 1049 ? 0.1892 0.1734 0.1639 0.0229  -0.0128 0.0004  1047 ASP A N   
7845  C CA  . ASP A 1049 ? 0.1636 0.1490 0.1399 0.0207  -0.0128 -0.0017 1047 ASP A CA  
7846  C C   . ASP A 1049 ? 0.1801 0.1697 0.1602 0.0205  -0.0141 -0.0028 1047 ASP A C   
7847  O O   . ASP A 1049 ? 0.1802 0.1717 0.1601 0.0216  -0.0159 -0.0026 1047 ASP A O   
7848  C CB  . ASP A 1049 ? 0.1683 0.1526 0.1410 0.0196  -0.0137 -0.0029 1047 ASP A CB  
7849  C CG  . ASP A 1049 ? 0.1895 0.1747 0.1643 0.0170  -0.0141 -0.0045 1047 ASP A CG  
7850  O OD1 . ASP A 1049 ? 0.1981 0.1866 0.1753 0.0162  -0.0156 -0.0053 1047 ASP A OD1 
7851  O OD2 . ASP A 1049 ? 0.2134 0.1963 0.1879 0.0156  -0.0128 -0.0045 1047 ASP A OD2 
7852  N N   . PRO A 1050 ? 0.1770 0.1686 0.1607 0.0191  -0.0133 -0.0038 1048 PRO A N   
7853  C CA  . PRO A 1050 ? 0.1752 0.1718 0.1631 0.0193  -0.0143 -0.0048 1048 PRO A CA  
7854  C C   . PRO A 1050 ? 0.1837 0.1832 0.1717 0.0176  -0.0161 -0.0057 1048 PRO A C   
7855  O O   . PRO A 1050 ? 0.1940 0.1974 0.1845 0.0182  -0.0175 -0.0062 1048 PRO A O   
7856  C CB  . PRO A 1050 ? 0.1988 0.1974 0.1899 0.0184  -0.0126 -0.0057 1048 PRO A CB  
7857  C CG  . PRO A 1050 ? 0.2027 0.1981 0.1914 0.0166  -0.0113 -0.0053 1048 PRO A CG  
7858  C CD  . PRO A 1050 ? 0.1893 0.1797 0.1737 0.0178  -0.0113 -0.0040 1048 PRO A CD  
7859  N N   . VAL A 1051 ? 0.1661 0.1636 0.1518 0.0156  -0.0163 -0.0060 1049 VAL A N   
7860  C CA  . VAL A 1051 ? 0.1736 0.1733 0.1599 0.0139  -0.0185 -0.0069 1049 VAL A CA  
7861  C C   . VAL A 1051 ? 0.1853 0.1843 0.1687 0.0157  -0.0205 -0.0071 1049 VAL A C   
7862  O O   . VAL A 1051 ? 0.1867 0.1890 0.1717 0.0155  -0.0225 -0.0077 1049 VAL A O   
7863  C CB  . VAL A 1051 ? 0.1813 0.1787 0.1668 0.0113  -0.0184 -0.0072 1049 VAL A CB  
7864  C CG1 . VAL A 1051 ? 0.2096 0.2090 0.1966 0.0094  -0.0210 -0.0081 1049 VAL A CG1 
7865  C CG2 . VAL A 1051 ? 0.2062 0.2052 0.1944 0.0096  -0.0164 -0.0066 1049 VAL A CG2 
7866  N N   . LEU A 1052 ? 0.1647 0.1600 0.1441 0.0174  -0.0199 -0.0063 1050 LEU A N   
7867  C CA  . LEU A 1052 ? 0.1703 0.1660 0.1469 0.0195  -0.0216 -0.0060 1050 LEU A CA  
7868  C C   . LEU A 1052 ? 0.1830 0.1824 0.1625 0.0210  -0.0225 -0.0053 1050 LEU A C   
7869  O O   . LEU A 1052 ? 0.1693 0.1714 0.1487 0.0215  -0.0247 -0.0058 1050 LEU A O   
7870  C CB  . LEU A 1052 ? 0.1905 0.1828 0.1627 0.0213  -0.0203 -0.0046 1050 LEU A CB  
7871  C CG  . LEU A 1052 ? 0.1587 0.1519 0.1273 0.0236  -0.0216 -0.0036 1050 LEU A CG  
7872  C CD1 . LEU A 1052 ? 0.1752 0.1706 0.1461 0.0255  -0.0220 -0.0014 1050 LEU A CD1 
7873  C CD2 . LEU A 1052 ? 0.1905 0.1857 0.1572 0.0232  -0.0243 -0.0058 1050 LEU A CD2 
7874  N N   . LEU A 1053 ? 0.1805 0.1801 0.1629 0.0219  -0.0209 -0.0043 1051 LEU A N   
7875  C CA  . LEU A 1053 ? 0.1879 0.1907 0.1738 0.0237  -0.0219 -0.0038 1051 LEU A CA  
7876  C C   . LEU A 1053 ? 0.1709 0.1787 0.1605 0.0224  -0.0233 -0.0054 1051 LEU A C   
7877  O O   . LEU A 1053 ? 0.1803 0.1910 0.1711 0.0236  -0.0253 -0.0053 1051 LEU A O   
7878  C CB  . LEU A 1053 ? 0.1801 0.1819 0.1691 0.0248  -0.0202 -0.0031 1051 LEU A CB  
7879  C CG  . LEU A 1053 ? 0.2115 0.2091 0.1981 0.0265  -0.0193 -0.0007 1051 LEU A CG  
7880  C CD1 . LEU A 1053 ? 0.1877 0.1840 0.1781 0.0271  -0.0177 -0.0006 1051 LEU A CD1 
7881  C CD2 . LEU A 1053 ? 0.2396 0.2379 0.2252 0.0287  -0.0211 0.0014  1051 LEU A CD2 
7882  N N   . ASP A 1054 ? 0.1627 0.1717 0.1540 0.0199  -0.0225 -0.0066 1052 ASP A N   
7883  C CA  . ASP A 1054 ? 0.1808 0.1951 0.1758 0.0183  -0.0237 -0.0078 1052 ASP A CA  
7884  C C   . ASP A 1054 ? 0.1849 0.1997 0.1781 0.0175  -0.0264 -0.0083 1052 ASP A C   
7885  O O   . ASP A 1054 ? 0.1978 0.2170 0.1937 0.0175  -0.0282 -0.0088 1052 ASP A O   
7886  C CB  . ASP A 1054 ? 0.1874 0.2031 0.1845 0.0155  -0.0223 -0.0083 1052 ASP A CB  
7887  C CG  . ASP A 1054 ? 0.2146 0.2322 0.2145 0.0163  -0.0200 -0.0085 1052 ASP A CG  
7888  O OD1 . ASP A 1054 ? 0.2185 0.2361 0.2197 0.0190  -0.0199 -0.0084 1052 ASP A OD1 
7889  O OD2 . ASP A 1054 ? 0.2479 0.2669 0.2491 0.0141  -0.0186 -0.0086 1052 ASP A OD2 
7890  N N   . PHE A 1055 ? 0.1674 0.1778 0.1561 0.0171  -0.0267 -0.0084 1053 PHE A N   
7891  C CA  . PHE A 1055 ? 0.1805 0.1912 0.1672 0.0166  -0.0294 -0.0095 1053 PHE A CA  
7892  C C   . PHE A 1055 ? 0.1858 0.1983 0.1711 0.0194  -0.0310 -0.0089 1053 PHE A C   
7893  O O   . PHE A 1055 ? 0.1874 0.2031 0.1737 0.0192  -0.0336 -0.0098 1053 PHE A O   
7894  C CB  . PHE A 1055 ? 0.1894 0.1953 0.1719 0.0160  -0.0294 -0.0102 1053 PHE A CB  
7895  C CG  . PHE A 1055 ? 0.1870 0.1929 0.1672 0.0158  -0.0323 -0.0120 1053 PHE A CG  
7896  C CD1 . PHE A 1055 ? 0.2220 0.2306 0.2057 0.0136  -0.0347 -0.0133 1053 PHE A CD1 
7897  C CD2 . PHE A 1055 ? 0.1992 0.2027 0.1741 0.0178  -0.0328 -0.0125 1053 PHE A CD2 
7898  C CE1 . PHE A 1055 ? 0.2408 0.2492 0.2228 0.0134  -0.0377 -0.0154 1053 PHE A CE1 
7899  C CE2 . PHE A 1055 ? 0.2183 0.2223 0.1910 0.0178  -0.0357 -0.0148 1053 PHE A CE2 
7900  C CZ  . PHE A 1055 ? 0.2094 0.2156 0.1858 0.0157  -0.0382 -0.0164 1053 PHE A CZ  
7901  N N   . ALA A 1056 ? 0.1854 0.1958 0.1685 0.0218  -0.0298 -0.0072 1054 ALA A N   
7902  C CA  . ALA A 1056 ? 0.1854 0.1978 0.1675 0.0244  -0.0314 -0.0059 1054 ALA A CA  
7903  C C   . ALA A 1056 ? 0.2106 0.2278 0.1980 0.0248  -0.0325 -0.0060 1054 ALA A C   
7904  O O   . ALA A 1056 ? 0.2152 0.2354 0.2025 0.0258  -0.0349 -0.0060 1054 ALA A O   
7905  C CB  . ALA A 1056 ? 0.2227 0.2322 0.2027 0.0266  -0.0297 -0.0034 1054 ALA A CB  
7906  N N   . LYS A 1057 ? 0.1929 0.2113 0.1847 0.0242  -0.0309 -0.0063 1055 LYS A N   
7907  C CA  . LYS A 1057 ? 0.2102 0.2340 0.2075 0.0247  -0.0319 -0.0068 1055 LYS A CA  
7908  C C   . LYS A 1057 ? 0.2047 0.2325 0.2036 0.0225  -0.0339 -0.0083 1055 LYS A C   
7909  O O   . LYS A 1057 ? 0.2288 0.2609 0.2302 0.0234  -0.0360 -0.0085 1055 LYS A O   
7910  C CB  . LYS A 1057 ? 0.2317 0.2565 0.2332 0.0246  -0.0297 -0.0072 1055 LYS A CB  
7911  C CG  . LYS A 1057 ? 0.2744 0.2968 0.2768 0.0275  -0.0288 -0.0059 1055 LYS A CG  
7912  C CD  . LYS A 1057 ? 0.2858 0.3105 0.2933 0.0279  -0.0271 -0.0071 1055 LYS A CD  
7913  C CE  . LYS A 1057 ? 0.3210 0.3449 0.3276 0.0252  -0.0249 -0.0081 1055 LYS A CE  
7914  N NZ  . LYS A 1057 ? 0.3472 0.3731 0.3580 0.0260  -0.0230 -0.0094 1055 LYS A NZ  
7915  N N   . TRP A 1058 ? 0.2134 0.2398 0.2113 0.0196  -0.0336 -0.0093 1056 TRP A N   
7916  C CA  . TRP A 1058 ? 0.2090 0.2385 0.2086 0.0172  -0.0358 -0.0105 1056 TRP A CA  
7917  C C   . TRP A 1058 ? 0.2308 0.2603 0.2274 0.0183  -0.0388 -0.0110 1056 TRP A C   
7918  O O   . TRP A 1058 ? 0.2587 0.2926 0.2579 0.0179  -0.0412 -0.0117 1056 TRP A O   
7919  C CB  . TRP A 1058 ? 0.2247 0.2516 0.2238 0.0140  -0.0352 -0.0111 1056 TRP A CB  
7920  C CG  . TRP A 1058 ? 0.2304 0.2597 0.2318 0.0112  -0.0378 -0.0122 1056 TRP A CG  
7921  C CD1 . TRP A 1058 ? 0.2943 0.3291 0.3013 0.0087  -0.0383 -0.0121 1056 TRP A CD1 
7922  C CD2 . TRP A 1058 ? 0.2636 0.2901 0.2622 0.0105  -0.0404 -0.0137 1056 TRP A CD2 
7923  N NE1 . TRP A 1058 ? 0.2948 0.3299 0.3030 0.0063  -0.0412 -0.0130 1056 TRP A NE1 
7924  C CE2 . TRP A 1058 ? 0.2534 0.2833 0.2566 0.0074  -0.0427 -0.0143 1056 TRP A CE2 
7925  C CE3 . TRP A 1058 ? 0.2704 0.2925 0.2634 0.0122  -0.0412 -0.0146 1056 TRP A CE3 
7926  C CZ2 . TRP A 1058 ? 0.2860 0.3141 0.2884 0.0060  -0.0459 -0.0161 1056 TRP A CZ2 
7927  C CZ3 . TRP A 1058 ? 0.2836 0.3044 0.2754 0.0110  -0.0442 -0.0168 1056 TRP A CZ3 
7928  C CH2 . TRP A 1058 ? 0.2970 0.3206 0.2937 0.0080  -0.0467 -0.0176 1056 TRP A CH2 
7929  N N   . LEU A 1059 ? 0.2109 0.2359 0.2018 0.0198  -0.0387 -0.0107 1057 LEU A N   
7930  C CA  . LEU A 1059 ? 0.2466 0.2724 0.2340 0.0212  -0.0414 -0.0112 1057 LEU A CA  
7931  C C   . LEU A 1059 ? 0.2641 0.2943 0.2536 0.0235  -0.0427 -0.0100 1057 LEU A C   
7932  O O   . LEU A 1059 ? 0.2570 0.2908 0.2472 0.0235  -0.0456 -0.0109 1057 LEU A O   
7933  C CB  . LEU A 1059 ? 0.2238 0.2454 0.2049 0.0228  -0.0406 -0.0107 1057 LEU A CB  
7934  C CG  . LEU A 1059 ? 0.2084 0.2259 0.1869 0.0209  -0.0402 -0.0127 1057 LEU A CG  
7935  C CD1 . LEU A 1059 ? 0.2012 0.2150 0.1741 0.0227  -0.0386 -0.0118 1057 LEU A CD1 
7936  C CD2 . LEU A 1059 ? 0.2356 0.2546 0.2138 0.0197  -0.0437 -0.0154 1057 LEU A CD2 
7937  N N   . ASP A 1060 ? 0.2252 0.2550 0.2161 0.0255  -0.0409 -0.0079 1058 ASP A N   
7938  C CA  . ASP A 1060 ? 0.2472 0.2809 0.2411 0.0278  -0.0424 -0.0066 1058 ASP A CA  
7939  C C   . ASP A 1060 ? 0.2324 0.2716 0.2319 0.0265  -0.0438 -0.0080 1058 ASP A C   
7940  O O   . ASP A 1060 ? 0.2905 0.3336 0.2912 0.0276  -0.0464 -0.0079 1058 ASP A O   
7941  C CB  . ASP A 1060 ? 0.2960 0.3279 0.2919 0.0299  -0.0403 -0.0046 1058 ASP A CB  
7942  C CG  . ASP A 1060 ? 0.2919 0.3204 0.2832 0.0321  -0.0401 -0.0019 1058 ASP A CG  
7943  O OD1 . ASP A 1060 ? 0.4030 0.4330 0.3909 0.0331  -0.0422 -0.0011 1058 ASP A OD1 
7944  O OD2 . ASP A 1060 ? 0.3987 0.4236 0.3901 0.0327  -0.0378 -0.0006 1058 ASP A OD2 
7945  N N   . GLY A 1061 ? 0.2520 0.2921 0.2550 0.0242  -0.0422 -0.0092 1059 GLY A N   
7946  C CA  . GLY A 1061 ? 0.2683 0.3145 0.2769 0.0227  -0.0434 -0.0103 1059 GLY A CA  
7947  C C   . GLY A 1061 ? 0.3152 0.3636 0.3234 0.0208  -0.0464 -0.0116 1059 GLY A C   
7948  O O   . GLY A 1061 ? 0.3681 0.4221 0.3805 0.0205  -0.0484 -0.0120 1059 GLY A O   
7949  N N   . LYS A 1062 ? 0.3019 0.3459 0.3054 0.0195  -0.0470 -0.0124 1060 LYS A N   
7950  C CA  . LYS A 1062 ? 0.3158 0.3611 0.3187 0.0179  -0.0503 -0.0141 1060 LYS A CA  
7951  C C   . LYS A 1062 ? 0.3093 0.3556 0.3086 0.0205  -0.0529 -0.0141 1060 LYS A C   
7952  O O   . LYS A 1062 ? 0.3669 0.4150 0.3657 0.0196  -0.0560 -0.0158 1060 LYS A O   
7953  C CB  . LYS A 1062 ? 0.3313 0.3714 0.3310 0.0156  -0.0503 -0.0155 1060 LYS A CB  
7954  C CG  . LYS A 1062 ? 0.3281 0.3676 0.3316 0.0124  -0.0485 -0.0154 1060 LYS A CG  
7955  C CD  . LYS A 1062 ? 0.3878 0.4328 0.3976 0.0095  -0.0505 -0.0158 1060 LYS A CD  
7956  C CE  . LYS A 1062 ? 0.4369 0.4819 0.4504 0.0059  -0.0490 -0.0151 1060 LYS A CE  
7957  N NZ  . LYS A 1062 ? 0.4692 0.5206 0.4893 0.0030  -0.0507 -0.0148 1060 LYS A NZ  
7958  N N   . GLY A 1063 ? 0.2859 0.3316 0.2831 0.0236  -0.0518 -0.0120 1061 GLY A N   
7959  C CA  . GLY A 1063 ? 0.2888 0.3360 0.2825 0.0262  -0.0540 -0.0113 1061 GLY A CA  
7960  C C   . GLY A 1063 ? 0.3056 0.3490 0.2920 0.0271  -0.0541 -0.0115 1061 GLY A C   
7961  O O   . GLY A 1063 ? 0.2958 0.3414 0.2787 0.0291  -0.0562 -0.0110 1061 GLY A O   
7962  N N   . ALA A 1064 ? 0.2836 0.3222 0.2676 0.0259  -0.0519 -0.0122 1062 ALA A N   
7963  C CA  . ALA A 1064 ? 0.2549 0.2904 0.2321 0.0268  -0.0519 -0.0128 1062 ALA A CA  
7964  C C   . ALA A 1064 ? 0.2623 0.2957 0.2366 0.0293  -0.0494 -0.0095 1062 ALA A C   
7965  O O   . ALA A 1064 ? 0.2279 0.2571 0.2007 0.0290  -0.0467 -0.0090 1062 ALA A O   
7966  C CB  . ALA A 1064 ? 0.2887 0.3201 0.2652 0.0243  -0.0511 -0.0154 1062 ALA A CB  
7967  N N   . ARG A 1065 ? 0.2454 0.2822 0.2196 0.0317  -0.0506 -0.0070 1063 ARG A N   
7968  C CA  . ARG A 1065 ? 0.2841 0.3193 0.2573 0.0339  -0.0486 -0.0031 1063 ARG A CA  
7969  C C   . ARG A 1065 ? 0.2863 0.3192 0.2528 0.0348  -0.0474 -0.0023 1063 ARG A C   
7970  O O   . ARG A 1065 ? 0.2550 0.2844 0.2211 0.0352  -0.0447 -0.0002 1063 ARG A O   
7971  C CB  . ARG A 1065 ? 0.2951 0.3346 0.2703 0.0362  -0.0507 -0.0004 1063 ARG A CB  
7972  C CG  . ARG A 1065 ? 0.3515 0.3908 0.3234 0.0387  -0.0502 0.0040  1063 ARG A CG  
7973  C CD  . ARG A 1065 ? 0.4649 0.4999 0.4393 0.0392  -0.0473 0.0067  1063 ARG A CD  
7974  N NE  . ARG A 1065 ? 0.5186 0.5520 0.4877 0.0403  -0.0461 0.0097  1063 ARG A NE  
7975  C CZ  . ARG A 1065 ? 0.4297 0.4644 0.3985 0.0424  -0.0467 0.0144  1063 ARG A CZ  
7976  N NH1 . ARG A 1065 ? 0.5640 0.6010 0.5377 0.0438  -0.0486 0.0166  1063 ARG A NH1 
7977  N NH2 . ARG A 1065 ? 0.5538 0.5879 0.5177 0.0431  -0.0455 0.0171  1063 ARG A NH2 
7978  N N   . ALA A 1066 ? 0.2366 0.2718 0.1981 0.0352  -0.0494 -0.0042 1064 ALA A N   
7979  C CA  . ALA A 1066 ? 0.2467 0.2806 0.2017 0.0361  -0.0482 -0.0038 1064 ALA A CA  
7980  C C   . ALA A 1066 ? 0.2386 0.2670 0.1934 0.0344  -0.0455 -0.0056 1064 ALA A C   
7981  O O   . ALA A 1066 ? 0.2314 0.2574 0.1838 0.0352  -0.0430 -0.0035 1064 ALA A O   
7982  C CB  . ALA A 1066 ? 0.2839 0.3217 0.2338 0.0369  -0.0510 -0.0066 1064 ALA A CB  
7983  N N   . GLU A 1067 ? 0.2487 0.2754 0.2064 0.0320  -0.0461 -0.0092 1065 GLU A N   
7984  C CA  . GLU A 1067 ? 0.2284 0.2501 0.1862 0.0303  -0.0438 -0.0107 1065 GLU A CA  
7985  C C   . GLU A 1067 ? 0.2264 0.2452 0.1879 0.0299  -0.0407 -0.0079 1065 GLU A C   
7986  O O   . GLU A 1067 ? 0.2307 0.2457 0.1909 0.0295  -0.0382 -0.0076 1065 GLU A O   
7987  C CB  . GLU A 1067 ? 0.2462 0.2670 0.2068 0.0277  -0.0455 -0.0147 1065 GLU A CB  
7988  C CG  . GLU A 1067 ? 0.2367 0.2588 0.1933 0.0280  -0.0484 -0.0185 1065 GLU A CG  
7989  C CD  . GLU A 1067 ? 0.2649 0.2924 0.2215 0.0289  -0.0518 -0.0192 1065 GLU A CD  
7990  O OE1 . GLU A 1067 ? 0.2530 0.2831 0.2133 0.0291  -0.0521 -0.0168 1065 GLU A OE1 
7991  O OE2 . GLU A 1067 ? 0.2669 0.2961 0.2199 0.0297  -0.0543 -0.0224 1065 GLU A OE2 
7992  N N   . ALA A 1068 ? 0.2347 0.2556 0.2011 0.0301  -0.0410 -0.0063 1066 ALA A N   
7993  C CA  . ALA A 1068 ? 0.2253 0.2439 0.1955 0.0301  -0.0384 -0.0041 1066 ALA A CA  
7994  C C   . ALA A 1068 ? 0.2142 0.2310 0.1814 0.0321  -0.0367 -0.0007 1066 ALA A C   
7995  O O   . ALA A 1068 ? 0.2076 0.2207 0.1754 0.0317  -0.0341 0.0003  1066 ALA A O   
7996  C CB  . ALA A 1068 ? 0.2289 0.2507 0.2050 0.0304  -0.0394 -0.0033 1066 ALA A CB  
7997  N N   . GLU A 1069 ? 0.2530 0.2727 0.2172 0.0342  -0.0382 0.0015  1067 GLU A N   
7998  C CA  . GLU A 1069 ? 0.2376 0.2563 0.1989 0.0359  -0.0368 0.0053  1067 GLU A CA  
7999  C C   . GLU A 1069 ? 0.2485 0.2646 0.2048 0.0354  -0.0350 0.0042  1067 GLU A C   
8000  O O   . GLU A 1069 ? 0.2444 0.2576 0.2006 0.0356  -0.0325 0.0065  1067 GLU A O   
8001  C CB  . GLU A 1069 ? 0.3018 0.3253 0.2605 0.0380  -0.0391 0.0080  1067 GLU A CB  
8002  C CG  . GLU A 1069 ? 0.3278 0.3512 0.2837 0.0397  -0.0378 0.0126  1067 GLU A CG  
8003  C CD  . GLU A 1069 ? 0.5250 0.5536 0.4789 0.0417  -0.0401 0.0162  1067 GLU A CD  
8004  O OE1 . GLU A 1069 ? 0.5333 0.5661 0.4855 0.0420  -0.0427 0.0141  1067 GLU A OE1 
8005  O OE2 . GLU A 1069 ? 0.6169 0.6456 0.5710 0.0429  -0.0395 0.0212  1067 GLU A OE2 
8006  N N   . ALA A 1070 ? 0.2503 0.2676 0.2029 0.0348  -0.0362 0.0007  1068 ALA A N   
8007  C CA  . ALA A 1070 ? 0.2358 0.2507 0.1841 0.0345  -0.0346 -0.0010 1068 ALA A CA  
8008  C C   . ALA A 1070 ? 0.2328 0.2426 0.1843 0.0326  -0.0322 -0.0018 1068 ALA A C   
8009  O O   . ALA A 1070 ? 0.2242 0.2313 0.1734 0.0326  -0.0299 -0.0011 1068 ALA A O   
8010  C CB  . ALA A 1070 ? 0.2870 0.3039 0.2320 0.0343  -0.0369 -0.0054 1068 ALA A CB  
8011  N N   . ALA A 1071 ? 0.2060 0.2148 0.1625 0.0308  -0.0326 -0.0033 1069 ALA A N   
8012  C CA  . ALA A 1071 ? 0.1834 0.1883 0.1431 0.0289  -0.0304 -0.0039 1069 ALA A CA  
8013  C C   . ALA A 1071 ? 0.1873 0.1903 0.1486 0.0298  -0.0279 -0.0005 1069 ALA A C   
8014  O O   . ALA A 1071 ? 0.1839 0.1835 0.1445 0.0292  -0.0256 -0.0002 1069 ALA A O   
8015  C CB  . ALA A 1071 ? 0.1870 0.1929 0.1519 0.0269  -0.0314 -0.0058 1069 ALA A CB  
8016  N N   . ARG A 1072 ? 0.2020 0.2070 0.1659 0.0312  -0.0286 0.0021  1070 ARG A N   
8017  C CA  A ARG A 1072 ? 0.2027 0.2056 0.1688 0.0321  -0.0268 0.0053  1070 ARG A CA  
8018  C CA  B ARG A 1072 ? 0.2028 0.2057 0.1689 0.0321  -0.0268 0.0053  1070 ARG A CA  
8019  C C   . ARG A 1072 ? 0.1846 0.1863 0.1462 0.0331  -0.0255 0.0078  1070 ARG A C   
8020  O O   . ARG A 1072 ? 0.2174 0.2160 0.1799 0.0329  -0.0233 0.0093  1070 ARG A O   
8021  C CB  A ARG A 1072 ? 0.2307 0.2359 0.2008 0.0337  -0.0283 0.0076  1070 ARG A CB  
8022  C CB  B ARG A 1072 ? 0.2308 0.2360 0.2010 0.0336  -0.0283 0.0075  1070 ARG A CB  
8023  C CG  A ARG A 1072 ? 0.2459 0.2522 0.2219 0.0329  -0.0288 0.0055  1070 ARG A CG  
8024  C CG  B ARG A 1072 ? 0.2454 0.2524 0.2206 0.0327  -0.0292 0.0050  1070 ARG A CG  
8025  C CD  A ARG A 1072 ? 0.2622 0.2706 0.2426 0.0348  -0.0303 0.0077  1070 ARG A CD  
8026  C CD  B ARG A 1072 ? 0.2689 0.2781 0.2488 0.0345  -0.0307 0.0069  1070 ARG A CD  
8027  N NE  A ARG A 1072 ? 0.2822 0.2944 0.2605 0.0360  -0.0329 0.0088  1070 ARG A NE  
8028  N NE  B ARG A 1072 ? 0.3068 0.3192 0.2910 0.0338  -0.0319 0.0042  1070 ARG A NE  
8029  C CZ  A ARG A 1072 ? 0.2862 0.3020 0.2660 0.0357  -0.0350 0.0067  1070 ARG A CZ  
8030  C CZ  B ARG A 1072 ? 0.2565 0.2685 0.2448 0.0326  -0.0305 0.0022  1070 ARG A CZ  
8031  N NH1 A ARG A 1072 ? 0.2388 0.2554 0.2223 0.0342  -0.0347 0.0037  1070 ARG A NH1 
8032  N NH1 B ARG A 1072 ? 0.2895 0.2980 0.2784 0.0321  -0.0282 0.0023  1070 ARG A NH1 
8033  N NH2 A ARG A 1072 ? 0.3076 0.3270 0.2852 0.0370  -0.0374 0.0078  1070 ARG A NH2 
8034  N NH2 B ARG A 1072 ? 0.2113 0.2273 0.2032 0.0318  -0.0316 0.0000  1070 ARG A NH2 
8035  N N   . ASN A 1073 ? 0.2012 0.2059 0.1578 0.0343  -0.0268 0.0083  1071 ASN A N   
8036  C CA  . ASN A 1073 ? 0.2102 0.2152 0.1622 0.0353  -0.0254 0.0106  1071 ASN A CA  
8037  C C   . ASN A 1073 ? 0.2173 0.2189 0.1672 0.0341  -0.0234 0.0082  1071 ASN A C   
8038  O O   . ASN A 1073 ? 0.2369 0.2369 0.1858 0.0343  -0.0213 0.0105  1071 ASN A O   
8039  C CB  . ASN A 1073 ? 0.2280 0.2380 0.1748 0.0368  -0.0273 0.0109  1071 ASN A CB  
8040  C CG  . ASN A 1073 ? 0.2870 0.3004 0.2354 0.0383  -0.0292 0.0147  1071 ASN A CG  
8041  O OD1 . ASN A 1073 ? 0.3167 0.3285 0.2699 0.0386  -0.0288 0.0179  1071 ASN A OD1 
8042  N ND2 . ASN A 1073 ? 0.3116 0.3301 0.2563 0.0395  -0.0314 0.0144  1071 ASN A ND2 
8043  N N   . ALA A 1074 ? 0.1996 0.2005 0.1492 0.0327  -0.0241 0.0038  1072 ALA A N   
8044  C CA  . ALA A 1074 ? 0.1939 0.1913 0.1424 0.0314  -0.0224 0.0015  1072 ALA A CA  
8045  C C   . ALA A 1074 ? 0.1898 0.1834 0.1424 0.0302  -0.0201 0.0028  1072 ALA A C   
8046  O O   . ALA A 1074 ? 0.2021 0.1932 0.1535 0.0300  -0.0181 0.0034  1072 ALA A O   
8047  C CB  . ALA A 1074 ? 0.2299 0.2269 0.1786 0.0300  -0.0241 -0.0030 1072 ALA A CB  
8048  N N   . GLY A 1075 ? 0.1937 0.1872 0.1514 0.0296  -0.0206 0.0032  1073 GLY A N   
8049  C CA  . GLY A 1075 ? 0.1940 0.1846 0.1557 0.0287  -0.0186 0.0040  1073 GLY A CA  
8050  C C   . GLY A 1075 ? 0.2303 0.2194 0.1916 0.0299  -0.0170 0.0076  1073 GLY A C   
8051  O O   . GLY A 1075 ? 0.2202 0.2064 0.1825 0.0291  -0.0149 0.0079  1073 GLY A O   
8052  N N   . SER A 1076 ? 0.2077 0.1991 0.1680 0.0316  -0.0179 0.0107  1074 SER A N   
8053  C CA  . SER A 1076 ? 0.1968 0.1873 0.1572 0.0326  -0.0167 0.0149  1074 SER A CA  
8054  C C   . SER A 1076 ? 0.2366 0.2272 0.1919 0.0328  -0.0152 0.0155  1074 SER A C   
8055  O O   . SER A 1076 ? 0.2562 0.2445 0.2121 0.0326  -0.0133 0.0176  1074 SER A O   
8056  C CB  . SER A 1076 ? 0.2488 0.2423 0.2100 0.0344  -0.0185 0.0186  1074 SER A CB  
8057  O OG  . SER A 1076 ? 0.3370 0.3302 0.3038 0.0346  -0.0198 0.0184  1074 SER A OG  
8058  N N   . SER A 1077 ? 0.2233 0.2167 0.1736 0.0333  -0.0161 0.0136  1075 SER A N   
8059  C CA  A SER A 1077 ? 0.2382 0.2327 0.1834 0.0339  -0.0148 0.0137  1075 SER A CA  
8060  C CA  B SER A 1077 ? 0.2382 0.2326 0.1834 0.0339  -0.0147 0.0139  1075 SER A CA  
8061  C CA  C SER A 1077 ? 0.2382 0.2326 0.1835 0.0339  -0.0147 0.0139  1075 SER A CA  
8062  C C   . SER A 1077 ? 0.2310 0.2217 0.1762 0.0325  -0.0130 0.0110  1075 SER A C   
8063  O O   . SER A 1077 ? 0.2357 0.2264 0.1785 0.0329  -0.0112 0.0119  1075 SER A O   
8064  C CB  A SER A 1077 ? 0.2382 0.2371 0.1784 0.0350  -0.0166 0.0115  1075 SER A CB  
8065  C CB  B SER A 1077 ? 0.2386 0.2377 0.1788 0.0351  -0.0165 0.0119  1075 SER A CB  
8066  C CB  C SER A 1077 ? 0.2388 0.2380 0.1789 0.0352  -0.0164 0.0122  1075 SER A CB  
8067  O OG  A SER A 1077 ? 0.2580 0.2585 0.1933 0.0358  -0.0155 0.0105  1075 SER A OG  
8068  O OG  B SER A 1077 ? 0.2410 0.2443 0.1804 0.0366  -0.0179 0.0155  1075 SER A OG  
8069  O OG  C SER A 1077 ? 0.2382 0.2366 0.1786 0.0343  -0.0181 0.0074  1075 SER A OG  
8070  N N   . SER A 1078 ? 0.2001 0.1882 0.1483 0.0309  -0.0134 0.0078  1076 SER A N   
8071  C CA  . SER A 1078 ? 0.1862 0.1708 0.1348 0.0294  -0.0120 0.0054  1076 SER A CA  
8072  C C   . SER A 1078 ? 0.2054 0.1876 0.1557 0.0292  -0.0096 0.0082  1076 SER A C   
8073  O O   . SER A 1078 ? 0.2045 0.1861 0.1582 0.0293  -0.0093 0.0109  1076 SER A O   
8074  C CB  . SER A 1078 ? 0.1943 0.1772 0.1467 0.0275  -0.0128 0.0027  1076 SER A CB  
8075  O OG  . SER A 1078 ? 0.1894 0.1691 0.1429 0.0260  -0.0114 0.0013  1076 SER A OG  
8076  N N   . ALA A 1079 ? 0.1785 0.1592 0.1267 0.0290  -0.0080 0.0074  1077 ALA A N   
8077  C CA  . ALA A 1079 ? 0.1797 0.1579 0.1297 0.0285  -0.0057 0.0096  1077 ALA A CA  
8078  C C   . ALA A 1079 ? 0.1787 0.1534 0.1318 0.0265  -0.0050 0.0074  1077 ALA A C   
8079  O O   . ALA A 1079 ? 0.1810 0.1536 0.1352 0.0260  -0.0032 0.0084  1077 ALA A O   
8080  C CB  . ALA A 1079 ? 0.1666 0.1463 0.1127 0.0296  -0.0043 0.0108  1077 ALA A CB  
8081  N N   . LEU A 1080 ? 0.1851 0.1595 0.1396 0.0254  -0.0064 0.0045  1078 LEU A N   
8082  C CA  . LEU A 1080 ? 0.1782 0.1503 0.1360 0.0234  -0.0058 0.0030  1078 LEU A CA  
8083  C C   . LEU A 1080 ? 0.1735 0.1446 0.1350 0.0231  -0.0046 0.0051  1078 LEU A C   
8084  O O   . LEU A 1080 ? 0.1737 0.1460 0.1372 0.0239  -0.0052 0.0065  1078 LEU A O   
8085  C CB  . LEU A 1080 ? 0.1622 0.1354 0.1217 0.0222  -0.0078 0.0007  1078 LEU A CB  
8086  C CG  . LEU A 1080 ? 0.1627 0.1350 0.1260 0.0201  -0.0073 -0.0003 1078 LEU A CG  
8087  C CD1 . LEU A 1080 ? 0.1864 0.1564 0.1488 0.0188  -0.0068 -0.0016 1078 LEU A CD1 
8088  C CD2 . LEU A 1080 ? 0.1741 0.1489 0.1398 0.0191  -0.0092 -0.0017 1078 LEU A CD2 
8089  N N   . GLY A 1081 ? 0.1569 0.1258 0.1196 0.0221  -0.0029 0.0051  1079 GLY A N   
8090  C CA  . GLY A 1081 ? 0.1887 0.1565 0.1550 0.0219  -0.0019 0.0065  1079 GLY A CA  
8091  C C   . GLY A 1081 ? 0.1803 0.1470 0.1461 0.0228  -0.0006 0.0094  1079 GLY A C   
8092  O O   . GLY A 1081 ? 0.2063 0.1719 0.1756 0.0226  0.0002  0.0104  1079 GLY A O   
8093  N N   . LEU A 1082 ? 0.1716 0.1393 0.1336 0.0240  -0.0004 0.0107  1080 LEU A N   
8094  C CA  . LEU A 1082 ? 0.1541 0.1214 0.1155 0.0246  0.0011  0.0137  1080 LEU A CA  
8095  C C   . LEU A 1082 ? 0.1717 0.1365 0.1348 0.0233  0.0027  0.0130  1080 LEU A C   
8096  O O   . LEU A 1082 ? 0.1742 0.1380 0.1363 0.0223  0.0029  0.0104  1080 LEU A O   
8097  C CB  . LEU A 1082 ? 0.1636 0.1331 0.1199 0.0258  0.0014  0.0141  1080 LEU A CB  
8098  C CG  . LEU A 1082 ? 0.1717 0.1422 0.1269 0.0265  0.0030  0.0173  1080 LEU A CG  
8099  C CD1 . LEU A 1082 ? 0.2753 0.2459 0.2340 0.0267  0.0029  0.0214  1080 LEU A CD1 
8100  C CD2 . LEU A 1082 ? 0.2349 0.2092 0.1849 0.0281  0.0029  0.0175  1080 LEU A CD2 
8101  N N   . ASP A 1083 ? 0.1739 0.1375 0.1398 0.0232  0.0036  0.0155  1081 ASP A N   
8102  C CA  . ASP A 1083 ? 0.1954 0.1568 0.1636 0.0220  0.0049  0.0149  1081 ASP A CA  
8103  C C   . ASP A 1083 ? 0.2382 0.1992 0.2076 0.0223  0.0060  0.0185  1081 ASP A C   
8104  O O   . ASP A 1083 ? 0.2599 0.2203 0.2332 0.0225  0.0055  0.0205  1081 ASP A O   
8105  C CB  . ASP A 1083 ? 0.2294 0.1900 0.2019 0.0211  0.0042  0.0132  1081 ASP A CB  
8106  C CG  . ASP A 1083 ? 0.3173 0.2763 0.2920 0.0198  0.0054  0.0122  1081 ASP A CG  
8107  O OD1 . ASP A 1083 ? 0.3616 0.3200 0.3343 0.0194  0.0066  0.0124  1081 ASP A OD1 
8108  O OD2 . ASP A 1083 ? 0.4061 0.3649 0.3846 0.0194  0.0050  0.0111  1081 ASP A OD2 
8109  N N   . LEU A 1084 ? 0.1887 0.1504 0.1552 0.0225  0.0074  0.0193  1082 LEU A N   
8110  C CA  . LEU A 1084 ? 0.2045 0.1669 0.1717 0.0229  0.0085  0.0231  1082 LEU A CA  
8111  C C   . LEU A 1084 ? 0.1968 0.1577 0.1649 0.0219  0.0100  0.0227  1082 LEU A C   
8112  O O   . LEU A 1084 ? 0.2309 0.1910 0.1976 0.0213  0.0104  0.0198  1082 LEU A O   
8113  C CB  . LEU A 1084 ? 0.2252 0.1913 0.1878 0.0243  0.0089  0.0249  1082 LEU A CB  
8114  C CG  . LEU A 1084 ? 0.2553 0.2239 0.2162 0.0255  0.0074  0.0258  1082 LEU A CG  
8115  C CD1 . LEU A 1084 ? 0.2728 0.2457 0.2283 0.0270  0.0080  0.0265  1082 LEU A CD1 
8116  C CD2 . LEU A 1084 ? 0.3025 0.2708 0.2676 0.0255  0.0066  0.0299  1082 LEU A CD2 
8117  N N   . GLU A 1085 ? 0.1985 0.1592 0.1695 0.0216  0.0108  0.0261  1083 GLU A N   
8118  C CA  . GLU A 1085 ? 0.1976 0.1578 0.1693 0.0209  0.0123  0.0265  1083 GLU A CA  
8119  C C   . GLU A 1085 ? 0.2053 0.1690 0.1745 0.0219  0.0136  0.0299  1083 GLU A C   
8120  O O   . GLU A 1085 ? 0.2364 0.2019 0.2069 0.0223  0.0132  0.0338  1083 GLU A O   
8121  C CB  . GLU A 1085 ? 0.2044 0.1622 0.1818 0.0197  0.0122  0.0275  1083 GLU A CB  
8122  C CG  . GLU A 1085 ? 0.2448 0.2023 0.2228 0.0190  0.0137  0.0282  1083 GLU A CG  
8123  C CD  . GLU A 1085 ? 0.3075 0.2627 0.2911 0.0176  0.0135  0.0283  1083 GLU A CD  
8124  O OE1 . GLU A 1085 ? 0.3201 0.2734 0.3070 0.0173  0.0121  0.0267  1083 GLU A OE1 
8125  O OE2 . GLU A 1085 ? 0.3110 0.2664 0.2957 0.0170  0.0146  0.0297  1083 GLU A OE2 
8126  N N   . LEU A 1086 ? 0.1858 0.1509 0.1518 0.0223  0.0149  0.0285  1084 LEU A N   
8127  C CA  . LEU A 1086 ? 0.1966 0.1661 0.1597 0.0235  0.0162  0.0310  1084 LEU A CA  
8128  C C   . LEU A 1086 ? 0.2234 0.1933 0.1897 0.0226  0.0177  0.0340  1084 LEU A C   
8129  O O   . LEU A 1086 ? 0.2358 0.2026 0.2045 0.0215  0.0180  0.0323  1084 LEU A O   
8130  C CB  . LEU A 1086 ? 0.2308 0.2019 0.1891 0.0248  0.0167  0.0274  1084 LEU A CB  
8131  C CG  . LEU A 1086 ? 0.2169 0.1876 0.1724 0.0255  0.0150  0.0241  1084 LEU A CG  
8132  C CD1 . LEU A 1086 ? 0.2378 0.2098 0.1892 0.0268  0.0151  0.0203  1084 LEU A CD1 
8133  C CD2 . LEU A 1086 ? 0.2952 0.2689 0.2496 0.0264  0.0142  0.0268  1084 LEU A CD2 
8134  N N   . PRO A 1087 ? 0.2209 0.1948 0.1874 0.0231  0.0186  0.0386  1085 PRO A N   
8135  C CA  . PRO A 1087 ? 0.2181 0.1929 0.1878 0.0221  0.0199  0.0418  1085 PRO A CA  
8136  C C   . PRO A 1087 ? 0.2276 0.2034 0.1952 0.0226  0.0215  0.0391  1085 PRO A C   
8137  O O   . PRO A 1087 ? 0.2454 0.2240 0.2083 0.0243  0.0221  0.0367  1085 PRO A O   
8138  C CB  . PRO A 1087 ? 0.2474 0.2278 0.2166 0.0228  0.0206  0.0473  1085 PRO A CB  
8139  C CG  . PRO A 1087 ? 0.2956 0.2766 0.2630 0.0236  0.0190  0.0476  1085 PRO A CG  
8140  C CD  . PRO A 1087 ? 0.2250 0.2032 0.1891 0.0242  0.0182  0.0416  1085 PRO A CD  
8141  N N   . GLY A 1088 ? 0.2258 0.1993 0.1972 0.0212  0.0221  0.0394  1086 GLY A N   
8142  C CA  . GLY A 1088 ? 0.2574 0.2314 0.2276 0.0215  0.0234  0.0371  1086 GLY A CA  
8143  C C   . GLY A 1088 ? 0.2152 0.1881 0.1904 0.0199  0.0240  0.0392  1086 GLY A C   
8144  O O   . GLY A 1088 ? 0.2056 0.1784 0.1849 0.0187  0.0237  0.0432  1086 GLY A O   
8145  N N   . PRO A 1089 ? 0.2245 0.1964 0.1997 0.0198  0.0247  0.0367  1087 PRO A N   
8146  C CA  . PRO A 1089 ? 0.2060 0.1771 0.1858 0.0183  0.0252  0.0384  1087 PRO A CA  
8147  C C   . PRO A 1089 ? 0.1799 0.1461 0.1641 0.0164  0.0236  0.0376  1087 PRO A C   
8148  O O   . PRO A 1089 ? 0.2002 0.1634 0.1835 0.0163  0.0223  0.0349  1087 PRO A O   
8149  C CB  . PRO A 1089 ? 0.2541 0.2254 0.2322 0.0189  0.0261  0.0353  1087 PRO A CB  
8150  C CG  . PRO A 1089 ? 0.2608 0.2298 0.2351 0.0198  0.0250  0.0310  1087 PRO A CG  
8151  C CD  . PRO A 1089 ? 0.2494 0.2205 0.2209 0.0209  0.0247  0.0321  1087 PRO A CD  
8152  N N   . VAL A 1090 ? 0.2046 0.1704 0.1938 0.0149  0.0237  0.0400  1088 VAL A N   
8153  C CA  . VAL A 1090 ? 0.1831 0.1446 0.1766 0.0133  0.0221  0.0385  1088 VAL A CA  
8154  C C   . VAL A 1090 ? 0.1823 0.1417 0.1741 0.0131  0.0220  0.0340  1088 VAL A C   
8155  O O   . VAL A 1090 ? 0.1984 0.1593 0.1872 0.0139  0.0231  0.0327  1088 VAL A O   
8156  C CB  . VAL A 1090 ? 0.2104 0.1720 0.2100 0.0118  0.0220  0.0417  1088 VAL A CB  
8157  C CG1 . VAL A 1090 ? 0.2193 0.1828 0.2214 0.0116  0.0218  0.0469  1088 VAL A CG1 
8158  C CG2 . VAL A 1090 ? 0.2066 0.1705 0.2060 0.0116  0.0236  0.0421  1088 VAL A CG2 
8159  N N   . GLY A 1091 ? 0.1993 0.1557 0.1935 0.0121  0.0204  0.0316  1089 GLY A N   
8160  C CA  . GLY A 1091 ? 0.1863 0.1413 0.1794 0.0116  0.0201  0.0278  1089 GLY A CA  
8161  C C   . GLY A 1091 ? 0.1682 0.1231 0.1565 0.0125  0.0200  0.0253  1089 GLY A C   
8162  O O   . GLY A 1091 ? 0.1712 0.1256 0.1583 0.0122  0.0200  0.0229  1089 GLY A O   
8163  N N   . GLU A 1092 ? 0.1830 0.1385 0.1690 0.0136  0.0199  0.0259  1090 GLU A N   
8164  C CA  . GLU A 1092 ? 0.1978 0.1530 0.1796 0.0145  0.0195  0.0234  1090 GLU A CA  
8165  C C   . GLU A 1092 ? 0.1607 0.1157 0.1421 0.0150  0.0185  0.0237  1090 GLU A C   
8166  O O   . GLU A 1092 ? 0.2072 0.1631 0.1901 0.0153  0.0186  0.0267  1090 GLU A O   
8167  C CB  . GLU A 1092 ? 0.2273 0.1846 0.2054 0.0159  0.0206  0.0236  1090 GLU A CB  
8168  C CG  . GLU A 1092 ? 0.2829 0.2394 0.2578 0.0165  0.0200  0.0204  1090 GLU A CG  
8169  C CD  . GLU A 1092 ? 0.2750 0.2334 0.2473 0.0181  0.0210  0.0201  1090 GLU A CD  
8170  O OE1 . GLU A 1092 ? 0.2526 0.2135 0.2224 0.0196  0.0215  0.0211  1090 GLU A OE1 
8171  O OE2 . GLU A 1092 ? 0.2978 0.2556 0.2705 0.0179  0.0212  0.0189  1090 GLU A OE2 
8172  N N   . ARG A 1093 ? 0.1597 0.1137 0.1396 0.0149  0.0174  0.0210  1091 ARG A N   
8173  C CA  . ARG A 1093 ? 0.1808 0.1349 0.1598 0.0156  0.0164  0.0210  1091 ARG A CA  
8174  C C   . ARG A 1093 ? 0.1734 0.1283 0.1478 0.0166  0.0163  0.0194  1091 ARG A C   
8175  O O   . ARG A 1093 ? 0.1699 0.1240 0.1431 0.0161  0.0160  0.0169  1091 ARG A O   
8176  C CB  . ARG A 1093 ? 0.2204 0.1731 0.2021 0.0148  0.0151  0.0190  1091 ARG A CB  
8177  C CG  . ARG A 1093 ? 0.2908 0.2436 0.2725 0.0155  0.0139  0.0193  1091 ARG A CG  
8178  C CD  . ARG A 1093 ? 0.3897 0.3417 0.3747 0.0149  0.0126  0.0170  1091 ARG A CD  
8179  N NE  . ARG A 1093 ? 0.4241 0.3752 0.4136 0.0141  0.0126  0.0173  1091 ARG A NE  
8180  C CZ  . ARG A 1093 ? 0.4124 0.3636 0.4034 0.0131  0.0125  0.0149  1091 ARG A CZ  
8181  N NH1 . ARG A 1093 ? 0.4979 0.4502 0.4866 0.0126  0.0125  0.0124  1091 ARG A NH1 
8182  N NH2 . ARG A 1093 ? 0.4131 0.3636 0.4082 0.0125  0.0123  0.0151  1091 ARG A NH2 
8183  N N   . ASN A 1094 ? 0.1802 0.1369 0.1523 0.0180  0.0164  0.0209  1092 ASN A N   
8184  C CA  . ASN A 1094 ? 0.1589 0.1167 0.1266 0.0192  0.0162  0.0192  1092 ASN A CA  
8185  C C   . ASN A 1094 ? 0.1775 0.1358 0.1441 0.0198  0.0149  0.0189  1092 ASN A C   
8186  O O   . ASN A 1094 ? 0.2101 0.1699 0.1771 0.0204  0.0149  0.0216  1092 ASN A O   
8187  C CB  . ASN A 1094 ? 0.1698 0.1306 0.1352 0.0207  0.0176  0.0207  1092 ASN A CB  
8188  C CG  . ASN A 1094 ? 0.1768 0.1371 0.1429 0.0203  0.0187  0.0202  1092 ASN A CG  
8189  O OD1 . ASN A 1094 ? 0.1848 0.1438 0.1500 0.0202  0.0182  0.0173  1092 ASN A OD1 
8190  N ND2 . ASN A 1094 ? 0.1810 0.1426 0.1493 0.0200  0.0199  0.0230  1092 ASN A ND2 
8191  N N   . LEU A 1095 ? 0.1813 0.1384 0.1471 0.0193  0.0137  0.0160  1093 LEU A N   
8192  C CA  . LEU A 1095 ? 0.1747 0.1320 0.1403 0.0195  0.0123  0.0153  1093 LEU A CA  
8193  C C   . LEU A 1095 ? 0.1716 0.1302 0.1333 0.0206  0.0115  0.0135  1093 LEU A C   
8194  O O   . LEU A 1095 ? 0.1884 0.1464 0.1484 0.0207  0.0115  0.0114  1093 LEU A O   
8195  C CB  . LEU A 1095 ? 0.2002 0.1559 0.1686 0.0180  0.0114  0.0134  1093 LEU A CB  
8196  C CG  . LEU A 1095 ? 0.2038 0.1586 0.1762 0.0170  0.0120  0.0144  1093 LEU A CG  
8197  C CD1 . LEU A 1095 ? 0.3046 0.2590 0.2793 0.0157  0.0112  0.0121  1093 LEU A CD1 
8198  C CD2 . LEU A 1095 ? 0.2526 0.2076 0.2273 0.0177  0.0120  0.0173  1093 LEU A CD2 
8199  N N   . TYR A 1096 ? 0.1770 0.1370 0.1374 0.0215  0.0105  0.0141  1094 TYR A N   
8200  C CA  . TYR A 1096 ? 0.1786 0.1402 0.1354 0.0227  0.0095  0.0122  1094 TYR A CA  
8201  C C   . TYR A 1096 ? 0.1843 0.1460 0.1420 0.0224  0.0078  0.0115  1094 TYR A C   
8202  O O   . TYR A 1096 ? 0.1924 0.1547 0.1518 0.0226  0.0076  0.0137  1094 TYR A O   
8203  C CB  . TYR A 1096 ? 0.1926 0.1577 0.1462 0.0246  0.0103  0.0141  1094 TYR A CB  
8204  C CG  . TYR A 1096 ? 0.2044 0.1720 0.1540 0.0261  0.0090  0.0122  1094 TYR A CG  
8205  C CD1 . TYR A 1096 ? 0.2308 0.2004 0.1797 0.0267  0.0079  0.0134  1094 TYR A CD1 
8206  C CD2 . TYR A 1096 ? 0.1857 0.1539 0.1327 0.0271  0.0088  0.0091  1094 TYR A CD2 
8207  C CE1 . TYR A 1096 ? 0.2045 0.1768 0.1496 0.0282  0.0066  0.0115  1094 TYR A CE1 
8208  C CE2 . TYR A 1096 ? 0.2118 0.1825 0.1552 0.0286  0.0075  0.0068  1094 TYR A CE2 
8209  C CZ  . TYR A 1096 ? 0.2241 0.1970 0.1665 0.0291  0.0064  0.0081  1094 TYR A CZ  
8210  O OH  . TYR A 1096 ? 0.2196 0.1954 0.1584 0.0307  0.0049  0.0056  1094 TYR A OH  
8211  N N   . THR A 1097 ? 0.1668 0.1278 0.1238 0.0218  0.0065  0.0085  1095 THR A N   
8212  C CA  . THR A 1097 ? 0.1883 0.1496 0.1467 0.0213  0.0049  0.0076  1095 THR A CA  
8213  C C   . THR A 1097 ? 0.1996 0.1618 0.1554 0.0218  0.0032  0.0052  1095 THR A C   
8214  O O   . THR A 1097 ? 0.1911 0.1528 0.1451 0.0220  0.0030  0.0033  1095 THR A O   
8215  C CB  . THR A 1097 ? 0.2261 0.1858 0.1881 0.0193  0.0048  0.0066  1095 THR A CB  
8216  O OG1 . THR A 1097 ? 0.2545 0.2129 0.2162 0.0182  0.0049  0.0048  1095 THR A OG1 
8217  C CG2 . THR A 1097 ? 0.2146 0.1736 0.1795 0.0189  0.0062  0.0085  1095 THR A CG2 
8218  N N   . LEU A 1098 ? 0.1871 0.1508 0.1432 0.0220  0.0018  0.0050  1096 LEU A N   
8219  C CA  . LEU A 1098 ? 0.1460 0.1107 0.1002 0.0223  -0.0002 0.0025  1096 LEU A CA  
8220  C C   . LEU A 1098 ? 0.1681 0.1324 0.1253 0.0205  -0.0015 0.0011  1096 LEU A C   
8221  O O   . LEU A 1098 ? 0.1793 0.1445 0.1391 0.0201  -0.0015 0.0021  1096 LEU A O   
8222  C CB  . LEU A 1098 ? 0.1537 0.1214 0.1053 0.0241  -0.0010 0.0036  1096 LEU A CB  
8223  C CG  . LEU A 1098 ? 0.1632 0.1329 0.1114 0.0260  0.0003  0.0052  1096 LEU A CG  
8224  C CD1 . LEU A 1098 ? 0.1892 0.1627 0.1348 0.0277  -0.0007 0.0064  1096 LEU A CD1 
8225  C CD2 . LEU A 1098 ? 0.1795 0.1487 0.1253 0.0265  0.0004  0.0023  1096 LEU A CD2 
8226  N N   . HIS A 1099 ? 0.1730 0.1363 0.1303 0.0194  -0.0027 -0.0013 1097 HIS A N   
8227  C CA  . HIS A 1099 ? 0.1531 0.1164 0.1134 0.0173  -0.0039 -0.0024 1097 HIS A CA  
8228  C C   . HIS A 1099 ? 0.1945 0.1586 0.1539 0.0174  -0.0064 -0.0046 1097 HIS A C   
8229  O O   . HIS A 1099 ? 0.2016 0.1660 0.1579 0.0190  -0.0071 -0.0058 1097 HIS A O   
8230  C CB  . HIS A 1099 ? 0.1902 0.1515 0.1527 0.0154  -0.0034 -0.0027 1097 HIS A CB  
8231  C CG  . HIS A 1099 ? 0.2035 0.1641 0.1670 0.0152  -0.0011 -0.0009 1097 HIS A CG  
8232  N ND1 . HIS A 1099 ? 0.2572 0.2187 0.2238 0.0137  -0.0005 -0.0001 1097 HIS A ND1 
8233  C CD2 . HIS A 1099 ? 0.2267 0.1861 0.1887 0.0164  0.0005  0.0003  1097 HIS A CD2 
8234  C CE1 . HIS A 1099 ? 0.2640 0.2246 0.2310 0.0139  0.0013  0.0011  1097 HIS A CE1 
8235  N NE2 . HIS A 1099 ? 0.2328 0.1919 0.1971 0.0154  0.0020  0.0016  1097 HIS A NE2 
8236  N N   . ALA A 1100 ? 0.1963 0.1613 0.1587 0.0155  -0.0077 -0.0053 1098 ALA A N   
8237  C CA  . ALA A 1100 ? 0.1885 0.1537 0.1509 0.0150  -0.0104 -0.0075 1098 ALA A CA  
8238  C C   . ALA A 1100 ? 0.1948 0.1570 0.1570 0.0145  -0.0111 -0.0091 1098 ALA A C   
8239  O O   . ALA A 1100 ? 0.2175 0.1777 0.1808 0.0136  -0.0098 -0.0083 1098 ALA A O   
8240  C CB  . ALA A 1100 ? 0.1927 0.1599 0.1590 0.0127  -0.0116 -0.0073 1098 ALA A CB  
8241  N N   . ARG A 1101 ? 0.2223 0.1842 0.1833 0.0152  -0.0135 -0.0118 1099 ARG A N   
8242  C CA  . ARG A 1101 ? 0.2071 0.1658 0.1686 0.0149  -0.0148 -0.0139 1099 ARG A CA  
8243  C C   . ARG A 1101 ? 0.2105 0.1678 0.1769 0.0118  -0.0165 -0.0138 1099 ARG A C   
8244  O O   . ARG A 1101 ? 0.2467 0.2012 0.2151 0.0107  -0.0166 -0.0137 1099 ARG A O   
8245  C CB  . ARG A 1101 ? 0.2266 0.1857 0.1853 0.0171  -0.0170 -0.0173 1099 ARG A CB  
8246  C CG  . ARG A 1101 ? 0.2534 0.2145 0.2070 0.0203  -0.0152 -0.0174 1099 ARG A CG  
8247  C CD  . ARG A 1101 ? 0.2218 0.1843 0.1725 0.0225  -0.0175 -0.0212 1099 ARG A CD  
8248  N NE  . ARG A 1101 ? 0.2462 0.2062 0.1969 0.0234  -0.0186 -0.0245 1099 ARG A NE  
8249  C CZ  . ARG A 1101 ? 0.2917 0.2523 0.2394 0.0257  -0.0169 -0.0251 1099 ARG A CZ  
8250  N NH1 . ARG A 1101 ? 0.3045 0.2677 0.2493 0.0269  -0.0139 -0.0220 1099 ARG A NH1 
8251  N NH2 . ARG A 1101 ? 0.2964 0.2550 0.2444 0.0268  -0.0184 -0.0288 1099 ARG A NH2 
8252  N N   . GLY A 1102 ? 0.1921 0.1517 0.1609 0.0102  -0.0181 -0.0135 1100 GLY A N   
8253  C CA  . GLY A 1102 ? 0.2012 0.1602 0.1749 0.0070  -0.0200 -0.0130 1100 GLY A CA  
8254  C C   . GLY A 1102 ? 0.1799 0.1410 0.1554 0.0061  -0.0228 -0.0142 1100 GLY A C   
8255  O O   . GLY A 1102 ? 0.2199 0.1845 0.1944 0.0068  -0.0223 -0.0137 1100 GLY A O   
8256  N N   . ARG A 1103 ? 0.1957 0.1546 0.1743 0.0045  -0.0259 -0.0158 1101 ARG A N   
8257  C CA  . ARG A 1103 ? 0.2020 0.1626 0.1827 0.0036  -0.0291 -0.0173 1101 ARG A CA  
8258  C C   . ARG A 1103 ? 0.2063 0.1651 0.1839 0.0063  -0.0312 -0.0215 1101 ARG A C   
8259  O O   . ARG A 1103 ? 0.2239 0.1789 0.2017 0.0069  -0.0325 -0.0237 1101 ARG A O   
8260  C CB  . ARG A 1103 ? 0.2338 0.1936 0.2209 -0.0002 -0.0316 -0.0161 1101 ARG A CB  
8261  C CG  . ARG A 1103 ? 0.2463 0.2090 0.2362 -0.0017 -0.0344 -0.0167 1101 ARG A CG  
8262  C CD  . ARG A 1103 ? 0.3166 0.2799 0.3135 -0.0060 -0.0365 -0.0144 1101 ARG A CD  
8263  N NE  . ARG A 1103 ? 0.3070 0.2741 0.3056 -0.0080 -0.0338 -0.0103 1101 ARG A NE  
8264  C CZ  . ARG A 1103 ? 0.3524 0.3254 0.3524 -0.0091 -0.0328 -0.0084 1101 ARG A CZ  
8265  N NH1 . ARG A 1103 ? 0.3208 0.2965 0.3207 -0.0085 -0.0344 -0.0100 1101 ARG A NH1 
8266  N NH2 . ARG A 1103 ? 0.4259 0.4025 0.4273 -0.0107 -0.0303 -0.0051 1101 ARG A NH2 
8267  N N   . ILE A 1104 ? 0.1913 0.1534 0.1662 0.0080  -0.0317 -0.0227 1102 ILE A N   
8268  C CA  . ILE A 1104 ? 0.1894 0.1514 0.1607 0.0108  -0.0337 -0.0267 1102 ILE A CA  
8269  C C   . ILE A 1104 ? 0.2200 0.1820 0.1951 0.0092  -0.0380 -0.0292 1102 ILE A C   
8270  O O   . ILE A 1104 ? 0.2065 0.1712 0.1844 0.0072  -0.0388 -0.0275 1102 ILE A O   
8271  C CB  . ILE A 1104 ? 0.1839 0.1498 0.1499 0.0136  -0.0318 -0.0261 1102 ILE A CB  
8272  C CG1 . ILE A 1104 ? 0.2014 0.1673 0.1648 0.0147  -0.0276 -0.0231 1102 ILE A CG1 
8273  C CG2 . ILE A 1104 ? 0.2020 0.1689 0.1637 0.0167  -0.0336 -0.0301 1102 ILE A CG2 
8274  C CD1 . ILE A 1104 ? 0.2318 0.1946 0.1931 0.0161  -0.0266 -0.0243 1102 ILE A CD1 
8275  N N   . LEU A 1105 ? 0.2088 0.1679 0.1841 0.0102  -0.0409 -0.0334 1103 LEU A N   
8276  C CA  . LEU A 1105 ? 0.2144 0.1732 0.1932 0.0091  -0.0455 -0.0364 1103 LEU A CA  
8277  C C   . LEU A 1105 ? 0.2053 0.1685 0.1795 0.0116  -0.0463 -0.0387 1103 LEU A C   
8278  O O   . LEU A 1105 ? 0.2236 0.1879 0.1921 0.0151  -0.0453 -0.0409 1103 LEU A O   
8279  C CB  . LEU A 1105 ? 0.2359 0.1898 0.2168 0.0095  -0.0486 -0.0406 1103 LEU A CB  
8280  C CG  . LEU A 1105 ? 0.2461 0.1993 0.2307 0.0089  -0.0539 -0.0449 1103 LEU A CG  
8281  C CD1 . LEU A 1105 ? 0.2631 0.2161 0.2550 0.0043  -0.0560 -0.0418 1103 LEU A CD1 
8282  C CD2 . LEU A 1105 ? 0.2714 0.2196 0.2575 0.0104  -0.0568 -0.0498 1103 LEU A CD2 
8283  N N   . LEU A 1106 ? 0.1982 0.1643 0.1750 0.0099  -0.0480 -0.0379 1104 LEU A N   
8284  C CA  . LEU A 1106 ? 0.2081 0.1787 0.1813 0.0120  -0.0492 -0.0397 1104 LEU A CA  
8285  C C   . LEU A 1106 ? 0.2487 0.2185 0.2250 0.0114  -0.0544 -0.0442 1104 LEU A C   
8286  O O   . LEU A 1106 ? 0.2305 0.1990 0.2133 0.0079  -0.0568 -0.0434 1104 LEU A O   
8287  C CB  . LEU A 1106 ? 0.2227 0.1977 0.1967 0.0109  -0.0476 -0.0357 1104 LEU A CB  
8288  C CG  . LEU A 1106 ? 0.2859 0.2634 0.2551 0.0130  -0.0433 -0.0325 1104 LEU A CG  
8289  C CD1 . LEU A 1106 ? 0.2778 0.2521 0.2455 0.0134  -0.0400 -0.0308 1104 LEU A CD1 
8290  C CD2 . LEU A 1106 ? 0.2391 0.2202 0.2108 0.0115  -0.0422 -0.0289 1104 LEU A CD2 
8291  N N   . VAL A 1107 ? 0.2136 0.1847 0.1854 0.0146  -0.0561 -0.0488 1105 VAL A N   
8292  C CA  . VAL A 1107 ? 0.2297 0.2005 0.2041 0.0145  -0.0613 -0.0539 1105 VAL A CA  
8293  C C   . VAL A 1107 ? 0.2119 0.1888 0.1816 0.0167  -0.0620 -0.0551 1105 VAL A C   
8294  O O   . VAL A 1107 ? 0.2508 0.2301 0.2147 0.0204  -0.0622 -0.0586 1105 VAL A O   
8295  C CB  . VAL A 1107 ? 0.2094 0.1764 0.1833 0.0165  -0.0635 -0.0594 1105 VAL A CB  
8296  C CG1 . VAL A 1107 ? 0.2279 0.1936 0.2066 0.0155  -0.0694 -0.0646 1105 VAL A CG1 
8297  C CG2 . VAL A 1107 ? 0.2510 0.2124 0.2284 0.0148  -0.0619 -0.0574 1105 VAL A CG2 
8298  N N   . PRO A 1108 ? 0.2032 0.1833 0.1754 0.0148  -0.0623 -0.0522 1106 PRO A N   
8299  C CA  . PRO A 1108 ? 0.2051 0.1913 0.1731 0.0169  -0.0630 -0.0527 1106 PRO A CA  
8300  C C   . PRO A 1108 ? 0.2550 0.2423 0.2251 0.0168  -0.0684 -0.0580 1106 PRO A C   
8301  O O   . PRO A 1108 ? 0.2633 0.2465 0.2393 0.0145  -0.0718 -0.0605 1106 PRO A O   
8302  C CB  . PRO A 1108 ? 0.2395 0.2282 0.2105 0.0146  -0.0610 -0.0473 1106 PRO A CB  
8303  C CG  . PRO A 1108 ? 0.2541 0.2389 0.2329 0.0104  -0.0623 -0.0461 1106 PRO A CG  
8304  C CD  . PRO A 1108 ? 0.2398 0.2190 0.2184 0.0107  -0.0616 -0.0477 1106 PRO A CD  
8305  N N   . ALA A 1109 ? 0.2257 0.2185 0.1910 0.0193  -0.0693 -0.0593 1107 ALA A N   
8306  C CA  . ALA A 1109 ? 0.2287 0.2238 0.1957 0.0193  -0.0744 -0.0639 1107 ALA A CA  
8307  C C   . ALA A 1109 ? 0.2555 0.2561 0.2233 0.0185  -0.0751 -0.0612 1107 ALA A C   
8308  O O   . ALA A 1109 ? 0.2811 0.2826 0.2535 0.0167  -0.0793 -0.0634 1107 ALA A O   
8309  C CB  . ALA A 1109 ? 0.2697 0.2675 0.2302 0.0235  -0.0761 -0.0697 1107 ALA A CB  
8310  N N   . THR A 1110 ? 0.2246 0.2288 0.1884 0.0199  -0.0713 -0.0565 1108 THR A N   
8311  C CA  . THR A 1110 ? 0.2426 0.2523 0.2070 0.0196  -0.0717 -0.0538 1108 THR A CA  
8312  C C   . THR A 1110 ? 0.2200 0.2295 0.1869 0.0180  -0.0677 -0.0476 1108 THR A C   
8313  O O   . THR A 1110 ? 0.2105 0.2165 0.1764 0.0180  -0.0640 -0.0452 1108 THR A O   
8314  C CB  . THR A 1110 ? 0.2442 0.2598 0.2010 0.0236  -0.0716 -0.0544 1108 THR A CB  
8315  O OG1 . THR A 1110 ? 0.2449 0.2604 0.1965 0.0258  -0.0671 -0.0510 1108 THR A OG1 
8316  C CG2 . THR A 1110 ? 0.2592 0.2760 0.2129 0.0256  -0.0754 -0.0610 1108 THR A CG2 
8317  N N   . GLU A 1111 ? 0.2603 0.2738 0.2301 0.0170  -0.0684 -0.0452 1109 GLU A N   
8318  C CA  . GLU A 1111 ? 0.2393 0.2536 0.2116 0.0159  -0.0649 -0.0399 1109 GLU A CA  
8319  C C   . GLU A 1111 ? 0.2447 0.2595 0.2113 0.0188  -0.0609 -0.0369 1109 GLU A C   
8320  O O   . GLU A 1111 ? 0.2173 0.2294 0.1848 0.0182  -0.0573 -0.0339 1109 GLU A O   
8321  C CB  . GLU A 1111 ? 0.2743 0.2939 0.2503 0.0150  -0.0668 -0.0386 1109 GLU A CB  
8322  C CG  . GLU A 1111 ? 0.2982 0.3199 0.2764 0.0147  -0.0634 -0.0336 1109 GLU A CG  
8323  C CD  . GLU A 1111 ? 0.3523 0.3786 0.3364 0.0129  -0.0653 -0.0326 1109 GLU A CD  
8324  O OE1 . GLU A 1111 ? 0.3632 0.3889 0.3531 0.0095  -0.0671 -0.0334 1109 GLU A OE1 
8325  O OE2 . GLU A 1111 ? 0.3336 0.3643 0.3167 0.0148  -0.0650 -0.0307 1109 GLU A OE2 
8326  N N   . SER A 1112 ? 0.2355 0.2539 0.1963 0.0220  -0.0614 -0.0375 1110 SER A N   
8327  C CA  . SER A 1112 ? 0.2251 0.2443 0.1808 0.0247  -0.0579 -0.0342 1110 SER A CA  
8328  C C   . SER A 1112 ? 0.2158 0.2304 0.1687 0.0252  -0.0554 -0.0349 1110 SER A C   
8329  O O   . SER A 1112 ? 0.2235 0.2363 0.1754 0.0256  -0.0517 -0.0314 1110 SER A O   
8330  C CB  . SER A 1112 ? 0.2582 0.2829 0.2083 0.0279  -0.0593 -0.0343 1110 SER A CB  
8331  O OG  . SER A 1112 ? 0.2402 0.2660 0.1864 0.0301  -0.0559 -0.0302 1110 SER A OG  
8332  N N   . GLY A 1113 ? 0.2064 0.2190 0.1582 0.0252  -0.0576 -0.0397 1111 GLY A N   
8333  C CA  . GLY A 1113 ? 0.2001 0.2083 0.1498 0.0257  -0.0555 -0.0407 1111 GLY A CA  
8334  C C   . GLY A 1113 ? 0.1946 0.1978 0.1493 0.0229  -0.0530 -0.0380 1111 GLY A C   
8335  O O   . GLY A 1113 ? 0.1970 0.1979 0.1499 0.0235  -0.0495 -0.0358 1111 GLY A O   
8336  N N   . LEU A 1114 ? 0.1928 0.1950 0.1540 0.0197  -0.0548 -0.0381 1112 LEU A N   
8337  C CA  . LEU A 1114 ? 0.2042 0.2029 0.1702 0.0168  -0.0526 -0.0353 1112 LEU A CA  
8338  C C   . LEU A 1114 ? 0.1852 0.1854 0.1505 0.0175  -0.0487 -0.0305 1112 LEU A C   
8339  O O   . LEU A 1114 ? 0.2002 0.1974 0.1656 0.0170  -0.0456 -0.0285 1112 LEU A O   
8340  C CB  . LEU A 1114 ? 0.2040 0.2028 0.1770 0.0133  -0.0553 -0.0356 1112 LEU A CB  
8341  C CG  . LEU A 1114 ? 0.2089 0.2062 0.1872 0.0102  -0.0530 -0.0321 1112 LEU A CG  
8342  C CD1 . LEU A 1114 ? 0.2416 0.2335 0.2197 0.0095  -0.0512 -0.0321 1112 LEU A CD1 
8343  C CD2 . LEU A 1114 ? 0.2663 0.2653 0.2516 0.0067  -0.0558 -0.0320 1112 LEU A CD2 
8344  N N   . TYR A 1115 ? 0.2071 0.2119 0.1719 0.0187  -0.0489 -0.0288 1113 TYR A N   
8345  C CA  . TYR A 1115 ? 0.1944 0.2005 0.1592 0.0195  -0.0457 -0.0245 1113 TYR A CA  
8346  C C   . TYR A 1115 ? 0.1987 0.2030 0.1581 0.0220  -0.0428 -0.0232 1113 TYR A C   
8347  O O   . TYR A 1115 ? 0.1983 0.2008 0.1585 0.0218  -0.0396 -0.0204 1113 TYR A O   
8348  C CB  . TYR A 1115 ? 0.1920 0.2032 0.1573 0.0207  -0.0469 -0.0231 1113 TYR A CB  
8349  C CG  . TYR A 1115 ? 0.2058 0.2197 0.1770 0.0183  -0.0493 -0.0237 1113 TYR A CG  
8350  C CD1 . TYR A 1115 ? 0.2274 0.2393 0.2038 0.0150  -0.0494 -0.0242 1113 TYR A CD1 
8351  C CD2 . TYR A 1115 ? 0.2358 0.2547 0.2076 0.0193  -0.0515 -0.0235 1113 TYR A CD2 
8352  C CE1 . TYR A 1115 ? 0.2347 0.2498 0.2167 0.0126  -0.0516 -0.0243 1113 TYR A CE1 
8353  C CE2 . TYR A 1115 ? 0.2365 0.2583 0.2139 0.0172  -0.0536 -0.0240 1113 TYR A CE2 
8354  C CZ  . TYR A 1115 ? 0.2559 0.2760 0.2383 0.0138  -0.0536 -0.0244 1113 TYR A CZ  
8355  O OH  . TYR A 1115 ? 0.3020 0.3258 0.2903 0.0115  -0.0558 -0.0244 1113 TYR A OH  
8356  N N   . HIS A 1116 ? 0.1955 0.2009 0.1494 0.0243  -0.0439 -0.0252 1114 HIS A N   
8357  C CA  . HIS A 1116 ? 0.2035 0.2081 0.1525 0.0265  -0.0412 -0.0238 1114 HIS A CA  
8358  C C   . HIS A 1116 ? 0.1960 0.1954 0.1457 0.0253  -0.0393 -0.0246 1114 HIS A C   
8359  O O   . HIS A 1116 ? 0.2087 0.2064 0.1572 0.0259  -0.0361 -0.0218 1114 HIS A O   
8360  C CB  . HIS A 1116 ? 0.2083 0.2165 0.1513 0.0293  -0.0429 -0.0260 1114 HIS A CB  
8361  C CG  . HIS A 1116 ? 0.2276 0.2411 0.1684 0.0312  -0.0435 -0.0234 1114 HIS A CG  
8362  N ND1 . HIS A 1116 ? 0.2613 0.2784 0.2037 0.0310  -0.0467 -0.0245 1114 HIS A ND1 
8363  C CD2 . HIS A 1116 ? 0.2576 0.2738 0.1951 0.0334  -0.0416 -0.0194 1114 HIS A CD2 
8364  C CE1 . HIS A 1116 ? 0.2449 0.2666 0.1849 0.0330  -0.0466 -0.0213 1114 HIS A CE1 
8365  N NE2 . HIS A 1116 ? 0.2956 0.3167 0.2326 0.0345  -0.0436 -0.0181 1114 HIS A NE2 
8366  N N   . GLN A 1117 ? 0.1833 0.1801 0.1352 0.0236  -0.0414 -0.0282 1115 GLN A N   
8367  C CA  . GLN A 1117 ? 0.1818 0.1735 0.1349 0.0224  -0.0399 -0.0289 1115 GLN A CA  
8368  C C   . GLN A 1117 ? 0.1759 0.1657 0.1333 0.0201  -0.0373 -0.0253 1115 GLN A C   
8369  O O   . GLN A 1117 ? 0.1842 0.1712 0.1408 0.0202  -0.0345 -0.0237 1115 GLN A O   
8370  C CB  . GLN A 1117 ? 0.1979 0.1872 0.1539 0.0208  -0.0434 -0.0332 1115 GLN A CB  
8371  C CG  . GLN A 1117 ? 0.2185 0.2090 0.1705 0.0232  -0.0460 -0.0379 1115 GLN A CG  
8372  C CD  . GLN A 1117 ? 0.2332 0.2205 0.1892 0.0214  -0.0497 -0.0424 1115 GLN A CD  
8373  O OE1 . GLN A 1117 ? 0.2240 0.2087 0.1860 0.0181  -0.0506 -0.0413 1115 GLN A OE1 
8374  N NE2 . GLN A 1117 ? 0.2097 0.1973 0.1626 0.0237  -0.0519 -0.0473 1115 GLN A NE2 
8375  N N   . LEU A 1118 ? 0.1737 0.1653 0.1356 0.0182  -0.0383 -0.0241 1116 LEU A N   
8376  C CA  A LEU A 1118 ? 0.1884 0.1794 0.1544 0.0162  -0.0360 -0.0211 1116 LEU A CA  
8377  C CA  B LEU A 1118 ? 0.1884 0.1794 0.1544 0.0162  -0.0360 -0.0210 1116 LEU A CA  
8378  C C   . LEU A 1118 ? 0.1754 0.1672 0.1392 0.0181  -0.0328 -0.0178 1116 LEU A C   
8379  O O   . LEU A 1118 ? 0.1740 0.1636 0.1389 0.0174  -0.0301 -0.0160 1116 LEU A O   
8380  C CB  A LEU A 1118 ? 0.1989 0.1929 0.1701 0.0140  -0.0378 -0.0207 1116 LEU A CB  
8381  C CB  B LEU A 1118 ? 0.1990 0.1934 0.1700 0.0142  -0.0378 -0.0206 1116 LEU A CB  
8382  C CG  A LEU A 1118 ? 0.1789 0.1730 0.1551 0.0114  -0.0359 -0.0183 1116 LEU A CG  
8383  C CG  B LEU A 1118 ? 0.1880 0.1813 0.1635 0.0112  -0.0405 -0.0225 1116 LEU A CG  
8384  C CD1 A LEU A 1118 ? 0.1816 0.1714 0.1586 0.0097  -0.0349 -0.0185 1116 LEU A CD1 
8385  C CD1 B LEU A 1118 ? 0.2021 0.2000 0.1817 0.0098  -0.0426 -0.0222 1116 LEU A CD1 
8386  C CD2 A LEU A 1118 ? 0.2181 0.2159 0.1996 0.0090  -0.0381 -0.0184 1116 LEU A CD2 
8387  C CD2 B LEU A 1118 ? 0.1927 0.1833 0.1714 0.0087  -0.0386 -0.0208 1116 LEU A CD2 
8388  N N   . ALA A 1119 ? 0.2042 0.1992 0.1652 0.0205  -0.0332 -0.0170 1117 ALA A N   
8389  C CA  . ALA A 1119 ? 0.2058 0.2012 0.1652 0.0223  -0.0305 -0.0137 1117 ALA A CA  
8390  C C   . ALA A 1119 ? 0.1992 0.1915 0.1553 0.0233  -0.0281 -0.0131 1117 ALA A C   
8391  O O   . ALA A 1119 ? 0.2000 0.1906 0.1572 0.0231  -0.0255 -0.0108 1117 ALA A O   
8392  C CB  . ALA A 1119 ? 0.2285 0.2280 0.1855 0.0247  -0.0318 -0.0126 1117 ALA A CB  
8393  N N   . ALA A 1120 ? 0.1906 0.1824 0.1427 0.0243  -0.0291 -0.0156 1118 ALA A N   
8394  C CA  . ALA A 1120 ? 0.1923 0.1818 0.1412 0.0253  -0.0269 -0.0152 1118 ALA A CA  
8395  C C   . ALA A 1120 ? 0.1889 0.1740 0.1409 0.0232  -0.0253 -0.0152 1118 ALA A C   
8396  O O   . ALA A 1120 ? 0.1885 0.1719 0.1401 0.0235  -0.0225 -0.0130 1118 ALA A O   
8397  C CB  . ALA A 1120 ? 0.1753 0.1656 0.1198 0.0269  -0.0286 -0.0187 1118 ALA A CB  
8398  N N   . ALA A 1121 ? 0.1663 0.1498 0.1218 0.0209  -0.0271 -0.0174 1119 ALA A N   
8399  C CA  . ALA A 1121 ? 0.1916 0.1716 0.1502 0.0186  -0.0258 -0.0171 1119 ALA A CA  
8400  C C   . ALA A 1121 ? 0.1682 0.1486 0.1300 0.0174  -0.0236 -0.0140 1119 ALA A C   
8401  O O   . ALA A 1121 ? 0.1668 0.1449 0.1292 0.0168  -0.0213 -0.0127 1119 ALA A O   
8402  C CB  . ALA A 1121 ? 0.2142 0.1927 0.1762 0.0163  -0.0287 -0.0197 1119 ALA A CB  
8403  N N   . LEU A 1122 ? 0.1741 0.1578 0.1383 0.0171  -0.0243 -0.0131 1120 LEU A N   
8404  C CA  . LEU A 1122 ? 0.1578 0.1425 0.1254 0.0162  -0.0224 -0.0108 1120 LEU A CA  
8405  C C   . LEU A 1122 ? 0.1611 0.1454 0.1268 0.0183  -0.0200 -0.0085 1120 LEU A C   
8406  O O   . LEU A 1122 ? 0.1698 0.1531 0.1375 0.0176  -0.0179 -0.0071 1120 LEU A O   
8407  C CB  . LEU A 1122 ? 0.1943 0.1832 0.1653 0.0155  -0.0240 -0.0107 1120 LEU A CB  
8408  C CG  . LEU A 1122 ? 0.1906 0.1807 0.1649 0.0130  -0.0264 -0.0123 1120 LEU A CG  
8409  C CD1 . LEU A 1122 ? 0.2155 0.2104 0.1928 0.0129  -0.0278 -0.0121 1120 LEU A CD1 
8410  C CD2 . LEU A 1122 ? 0.1965 0.1853 0.1742 0.0102  -0.0252 -0.0117 1120 LEU A CD2 
8411  N N   . ALA A 1123 ? 0.1664 0.1517 0.1284 0.0207  -0.0204 -0.0080 1121 ALA A N   
8412  C CA  . ALA A 1123 ? 0.1634 0.1483 0.1240 0.0225  -0.0184 -0.0052 1121 ALA A CA  
8413  C C   . ALA A 1123 ? 0.1833 0.1649 0.1425 0.0223  -0.0161 -0.0047 1121 ALA A C   
8414  O O   . ALA A 1123 ? 0.1846 0.1654 0.1444 0.0230  -0.0142 -0.0023 1121 ALA A O   
8415  C CB  . ALA A 1123 ? 0.1753 0.1626 0.1320 0.0249  -0.0195 -0.0044 1121 ALA A CB  
8416  N N   . THR A 1124 ? 0.1547 0.1344 0.1126 0.0214  -0.0165 -0.0068 1122 THR A N   
8417  C CA  . THR A 1124 ? 0.1732 0.1497 0.1299 0.0212  -0.0145 -0.0066 1122 THR A CA  
8418  C C   . THR A 1124 ? 0.1720 0.1465 0.1324 0.0187  -0.0139 -0.0070 1122 THR A C   
8419  O O   . THR A 1124 ? 0.1828 0.1546 0.1427 0.0181  -0.0127 -0.0073 1122 THR A O   
8420  C CB  . THR A 1124 ? 0.1795 0.1556 0.1320 0.0225  -0.0153 -0.0087 1122 THR A CB  
8421  O OG1 . THR A 1124 ? 0.1790 0.1556 0.1321 0.0217  -0.0182 -0.0117 1122 THR A OG1 
8422  C CG2 . THR A 1124 ? 0.1897 0.1687 0.1382 0.0252  -0.0151 -0.0072 1122 THR A CG2 
8423  N N   . GLY A 1125 ? 0.1594 0.1357 0.1236 0.0171  -0.0146 -0.0070 1123 GLY A N   
8424  C CA  . GLY A 1125 ? 0.1858 0.1616 0.1536 0.0148  -0.0137 -0.0066 1123 GLY A CA  
8425  C C   . GLY A 1125 ? 0.1788 0.1536 0.1483 0.0124  -0.0153 -0.0081 1123 GLY A C   
8426  O O   . GLY A 1125 ? 0.1953 0.1700 0.1678 0.0103  -0.0145 -0.0074 1123 GLY A O   
8427  N N   . ASN A 1126 ? 0.1772 0.1514 0.1452 0.0128  -0.0176 -0.0101 1124 ASN A N   
8428  C CA  . ASN A 1126 ? 0.1805 0.1529 0.1505 0.0107  -0.0196 -0.0117 1124 ASN A CA  
8429  C C   . ASN A 1126 ? 0.1688 0.1439 0.1431 0.0083  -0.0216 -0.0117 1124 ASN A C   
8430  O O   . ASN A 1126 ? 0.1855 0.1642 0.1605 0.0088  -0.0220 -0.0114 1124 ASN A O   
8431  C CB  . ASN A 1126 ? 0.1785 0.1490 0.1453 0.0124  -0.0215 -0.0145 1124 ASN A CB  
8432  C CG  . ASN A 1126 ? 0.1957 0.1643 0.1584 0.0147  -0.0195 -0.0145 1124 ASN A CG  
8433  O OD1 . ASN A 1126 ? 0.1987 0.1645 0.1619 0.0141  -0.0184 -0.0142 1124 ASN A OD1 
8434  N ND2 . ASN A 1126 ? 0.1729 0.1434 0.1316 0.0173  -0.0192 -0.0145 1124 ASN A ND2 
8435  N N   . SER A 1127 ? 0.1946 0.1682 0.1721 0.0057  -0.0229 -0.0119 1125 SER A N   
8436  C CA  . SER A 1127 ? 0.1746 0.1503 0.1562 0.0033  -0.0256 -0.0123 1125 SER A CA  
8437  C C   . SER A 1127 ? 0.1966 0.1699 0.1772 0.0040  -0.0288 -0.0154 1125 SER A C   
8438  O O   . SER A 1127 ? 0.2017 0.1720 0.1786 0.0062  -0.0287 -0.0172 1125 SER A O   
8439  C CB  . SER A 1127 ? 0.2220 0.1978 0.2083 -0.0002 -0.0256 -0.0103 1125 SER A CB  
8440  O OG  . SER A 1127 ? 0.2699 0.2409 0.2562 -0.0006 -0.0261 -0.0108 1125 SER A OG  
8441  N N   . VAL A 1128 ? 0.2154 0.1904 0.1996 0.0021  -0.0318 -0.0161 1126 VAL A N   
8442  C CA  . VAL A 1128 ? 0.2050 0.1780 0.1887 0.0028  -0.0353 -0.0196 1126 VAL A CA  
8443  C C   . VAL A 1128 ? 0.2344 0.2066 0.2243 -0.0008 -0.0386 -0.0196 1126 VAL A C   
8444  O O   . VAL A 1128 ? 0.2361 0.2114 0.2305 -0.0037 -0.0384 -0.0168 1126 VAL A O   
8445  C CB  . VAL A 1128 ? 0.2278 0.2043 0.2089 0.0049  -0.0365 -0.0211 1126 VAL A CB  
8446  C CG1 . VAL A 1128 ? 0.2137 0.1911 0.1892 0.0082  -0.0335 -0.0205 1126 VAL A CG1 
8447  C CG2 . VAL A 1128 ? 0.2206 0.2019 0.2058 0.0028  -0.0373 -0.0194 1126 VAL A CG2 
8448  N N   . ALA A 1129 ? 0.2255 0.1939 0.2159 -0.0005 -0.0417 -0.0229 1127 ALA A N   
8449  C CA  . ALA A 1129 ? 0.2139 0.1811 0.2102 -0.0034 -0.0459 -0.0239 1127 ALA A CA  
8450  C C   . ALA A 1129 ? 0.2258 0.1936 0.2202 -0.0014 -0.0491 -0.0282 1127 ALA A C   
8451  O O   . ALA A 1129 ? 0.2441 0.2094 0.2341 0.0017  -0.0495 -0.0318 1127 ALA A O   
8452  C CB  . ALA A 1129 ? 0.2511 0.2128 0.2508 -0.0048 -0.0475 -0.0243 1127 ALA A CB  
8453  N N   . ILE A 1130 ? 0.2094 0.1809 0.2069 -0.0030 -0.0512 -0.0279 1128 ILE A N   
8454  C CA  . ILE A 1130 ? 0.2226 0.1955 0.2182 -0.0012 -0.0543 -0.0319 1128 ILE A CA  
8455  C C   . ILE A 1130 ? 0.2636 0.2334 0.2649 -0.0033 -0.0594 -0.0347 1128 ILE A C   
8456  O O   . ILE A 1130 ? 0.2759 0.2458 0.2842 -0.0073 -0.0610 -0.0322 1128 ILE A O   
8457  C CB  . ILE A 1130 ? 0.2092 0.1883 0.2048 -0.0012 -0.0538 -0.0302 1128 ILE A CB  
8458  C CG1 . ILE A 1130 ? 0.2473 0.2292 0.2390 0.0004  -0.0490 -0.0270 1128 ILE A CG1 
8459  C CG2 . ILE A 1130 ? 0.2293 0.2101 0.2217 0.0013  -0.0567 -0.0343 1128 ILE A CG2 
8460  C CD1 . ILE A 1130 ? 0.2204 0.2083 0.2134 0.0000  -0.0485 -0.0249 1128 ILE A CD1 
8461  N N   . ASP A 1131 ? 0.2348 0.2023 0.2335 -0.0007 -0.0621 -0.0399 1129 ASP A N   
8462  C CA  . ASP A 1131 ? 0.2612 0.2256 0.2654 -0.0023 -0.0675 -0.0436 1129 ASP A CA  
8463  C C   . ASP A 1131 ? 0.2453 0.2132 0.2549 -0.0053 -0.0705 -0.0426 1129 ASP A C   
8464  O O   . ASP A 1131 ? 0.2619 0.2344 0.2686 -0.0038 -0.0709 -0.0438 1129 ASP A O   
8465  C CB  . ASP A 1131 ? 0.2280 0.1910 0.2272 0.0018  -0.0697 -0.0500 1129 ASP A CB  
8466  C CG  . ASP A 1131 ? 0.3090 0.2684 0.3139 0.0006  -0.0756 -0.0548 1129 ASP A CG  
8467  O OD1 . ASP A 1131 ? 0.2885 0.2439 0.3011 -0.0030 -0.0778 -0.0531 1129 ASP A OD1 
8468  O OD2 . ASP A 1131 ? 0.2896 0.2504 0.2915 0.0033  -0.0783 -0.0601 1129 ASP A OD2 
8469  N N   . ALA A 1132 ? 0.2980 0.2643 0.3158 -0.0097 -0.0727 -0.0400 1130 ALA A N   
8470  C CA  . ALA A 1132 ? 0.2697 0.2398 0.2935 -0.0130 -0.0757 -0.0387 1130 ALA A CA  
8471  C C   . ALA A 1132 ? 0.2950 0.2639 0.3203 -0.0121 -0.0811 -0.0445 1130 ALA A C   
8472  O O   . ALA A 1132 ? 0.3627 0.3360 0.3904 -0.0133 -0.0833 -0.0445 1130 ALA A O   
8473  C CB  . ALA A 1132 ? 0.3477 0.3169 0.3803 -0.0181 -0.0766 -0.0340 1130 ALA A CB  
8474  N N   . ALA A 1133 ? 0.3075 0.2710 0.3315 -0.0099 -0.0835 -0.0497 1131 ALA A N   
8475  C CA  . ALA A 1133 ? 0.3207 0.2834 0.3455 -0.0085 -0.0888 -0.0561 1131 ALA A CA  
8476  C C   . ALA A 1133 ? 0.3550 0.3232 0.3719 -0.0047 -0.0878 -0.0588 1131 ALA A C   
8477  O O   . ALA A 1133 ? 0.3846 0.3537 0.4018 -0.0035 -0.0921 -0.0640 1131 ALA A O   
8478  C CB  . ALA A 1133 ? 0.3665 0.3225 0.3917 -0.0066 -0.0914 -0.0614 1131 ALA A CB  
8479  N N   . SER A 1134 ? 0.3206 0.2927 0.3309 -0.0027 -0.0825 -0.0555 1132 SER A N   
8480  C CA  . SER A 1134 ? 0.3027 0.2806 0.3063 0.0006  -0.0816 -0.0569 1132 SER A CA  
8481  C C   . SER A 1134 ? 0.2838 0.2668 0.2914 -0.0016 -0.0839 -0.0556 1132 SER A C   
8482  O O   . SER A 1134 ? 0.2996 0.2869 0.3031 0.0008  -0.0850 -0.0581 1132 SER A O   
8483  C CB  . SER A 1134 ? 0.2889 0.2694 0.2858 0.0028  -0.0755 -0.0529 1132 SER A CB  
8484  O OG  . SER A 1134 ? 0.3048 0.2871 0.3056 -0.0003 -0.0728 -0.0469 1132 SER A OG  
8485  N N   . GLY A 1135 ? 0.3297 0.3129 0.3449 -0.0061 -0.0843 -0.0514 1133 GLY A N   
8486  C CA  . GLY A 1135 ? 0.3112 0.2999 0.3307 -0.0084 -0.0860 -0.0495 1133 GLY A CA  
8487  C C   . GLY A 1135 ? 0.3429 0.3379 0.3579 -0.0069 -0.0819 -0.0460 1133 GLY A C   
8488  O O   . GLY A 1135 ? 0.3542 0.3545 0.3714 -0.0076 -0.0834 -0.0454 1133 GLY A O   
8489  N N   . LEU A 1136 ? 0.2924 0.2870 0.3019 -0.0046 -0.0768 -0.0436 1134 LEU A N   
8490  C CA  . LEU A 1136 ? 0.3036 0.3036 0.3087 -0.0025 -0.0732 -0.0408 1134 LEU A CA  
8491  C C   . LEU A 1136 ? 0.3415 0.3442 0.3505 -0.0051 -0.0698 -0.0353 1134 LEU A C   
8492  O O   . LEU A 1136 ? 0.3266 0.3324 0.3321 -0.0031 -0.0662 -0.0328 1134 LEU A O   
8493  C CB  . LEU A 1136 ? 0.2943 0.2929 0.2907 0.0018  -0.0701 -0.0418 1134 LEU A CB  
8494  C CG  . LEU A 1136 ? 0.2636 0.2620 0.2547 0.0052  -0.0728 -0.0471 1134 LEU A CG  
8495  C CD1 . LEU A 1136 ? 0.2544 0.2515 0.2377 0.0090  -0.0693 -0.0473 1134 LEU A CD1 
8496  C CD2 . LEU A 1136 ? 0.2943 0.2988 0.2844 0.0063  -0.0749 -0.0479 1134 LEU A CD2 
8497  N N   . GLN A 1137 ? 0.2983 0.3002 0.3147 -0.0094 -0.0711 -0.0332 1135 GLN A N   
8498  C CA  . GLN A 1137 ? 0.3184 0.3237 0.3383 -0.0117 -0.0678 -0.0281 1135 GLN A CA  
8499  C C   . GLN A 1137 ? 0.2966 0.3093 0.3168 -0.0110 -0.0666 -0.0263 1135 GLN A C   
8500  O O   . GLN A 1137 ? 0.2973 0.3131 0.3164 -0.0103 -0.0626 -0.0232 1135 GLN A O   
8501  C CB  . GLN A 1137 ? 0.3067 0.3111 0.3350 -0.0167 -0.0700 -0.0260 1135 GLN A CB  
8502  C CG  . GLN A 1137 ? 0.3198 0.3171 0.3488 -0.0177 -0.0704 -0.0265 1135 GLN A CG  
8503  C CD  . GLN A 1137 ? 0.3237 0.3156 0.3534 -0.0172 -0.0753 -0.0316 1135 GLN A CD  
8504  O OE1 . GLN A 1137 ? 0.3614 0.3548 0.3896 -0.0155 -0.0781 -0.0352 1135 GLN A OE1 
8505  N NE2 . GLN A 1137 ? 0.3746 0.3602 0.4067 -0.0185 -0.0765 -0.0320 1135 GLN A NE2 
8506  N N   . ALA A 1138 ? 0.2969 0.3128 0.3186 -0.0109 -0.0701 -0.0284 1136 ALA A N   
8507  C CA  . ALA A 1138 ? 0.3199 0.3430 0.3424 -0.0102 -0.0694 -0.0269 1136 ALA A CA  
8508  C C   . ALA A 1138 ? 0.3454 0.3695 0.3606 -0.0056 -0.0664 -0.0270 1136 ALA A C   
8509  O O   . ALA A 1138 ? 0.3676 0.3974 0.3835 -0.0045 -0.0654 -0.0254 1136 ALA A O   
8510  C CB  . ALA A 1138 ? 0.3001 0.3261 0.3261 -0.0113 -0.0744 -0.0292 1136 ALA A CB  
8511  N N   . SER A 1139 ? 0.3372 0.3563 0.3459 -0.0028 -0.0652 -0.0287 1137 SER A N   
8512  C CA  . SER A 1139 ? 0.3092 0.3292 0.3115 0.0013  -0.0623 -0.0281 1137 SER A CA  
8513  C C   . SER A 1139 ? 0.3062 0.3261 0.3082 0.0015  -0.0576 -0.0246 1137 SER A C   
8514  O O   . SER A 1139 ? 0.3309 0.3519 0.3289 0.0046  -0.0552 -0.0235 1137 SER A O   
8515  C CB  . SER A 1139 ? 0.2993 0.3149 0.2948 0.0042  -0.0629 -0.0313 1137 SER A CB  
8516  O OG  . SER A 1139 ? 0.3246 0.3413 0.3193 0.0048  -0.0672 -0.0350 1137 SER A OG  
8517  N N   . LEU A 1140 ? 0.2905 0.3092 0.2967 -0.0016 -0.0563 -0.0228 1138 LEU A N   
8518  C CA  . LEU A 1140 ? 0.3067 0.3251 0.3124 -0.0014 -0.0520 -0.0200 1138 LEU A CA  
8519  C C   . LEU A 1140 ? 0.3080 0.3317 0.3203 -0.0045 -0.0511 -0.0172 1138 LEU A C   
8520  O O   . LEU A 1140 ? 0.3486 0.3713 0.3628 -0.0065 -0.0491 -0.0153 1138 LEU A O   
8521  C CB  . LEU A 1140 ? 0.3627 0.3746 0.3663 -0.0019 -0.0507 -0.0203 1138 LEU A CB  
8522  C CG  . LEU A 1140 ? 0.3730 0.3801 0.3695 0.0015  -0.0493 -0.0217 1138 LEU A CG  
8523  C CD1 . LEU A 1140 ? 0.3340 0.3368 0.3304 0.0003  -0.0469 -0.0205 1138 LEU A CD1 
8524  C CD2 . LEU A 1140 ? 0.2877 0.2972 0.2801 0.0050  -0.0470 -0.0207 1138 LEU A CD2 
8525  N N   . LYS A 1141 ? 0.3135 0.3434 0.3292 -0.0048 -0.0525 -0.0169 1139 LYS A N   
8526  C CA  . LYS A 1141 ? 0.3579 0.3943 0.3799 -0.0075 -0.0516 -0.0144 1139 LYS A CA  
8527  C C   . LYS A 1141 ? 0.3349 0.3749 0.3560 -0.0053 -0.0477 -0.0128 1139 LYS A C   
8528  O O   . LYS A 1141 ? 0.3360 0.3755 0.3532 -0.0016 -0.0467 -0.0136 1139 LYS A O   
8529  C CB  . LYS A 1141 ? 0.3846 0.4267 0.4114 -0.0089 -0.0550 -0.0148 1139 LYS A CB  
8530  C CG  . LYS A 1141 ? 0.4156 0.4552 0.4455 -0.0120 -0.0592 -0.0161 1139 LYS A CG  
8531  C CD  . LYS A 1141 ? 0.4181 0.4643 0.4535 -0.0137 -0.0623 -0.0161 1139 LYS A CD  
8532  N N   . ASN A 1142 ? 0.3368 0.3810 0.3621 -0.0076 -0.0456 -0.0105 1140 ASN A N   
8533  C CA  . ASN A 1142 ? 0.3518 0.4009 0.3777 -0.0058 -0.0423 -0.0094 1140 ASN A CA  
8534  C C   . ASN A 1142 ? 0.2899 0.3338 0.3102 -0.0025 -0.0395 -0.0099 1140 ASN A C   
8535  O O   . ASN A 1142 ? 0.3075 0.3531 0.3266 0.0007  -0.0380 -0.0103 1140 ASN A O   
8536  C CB  . ASN A 1142 ? 0.3573 0.4130 0.3856 -0.0040 -0.0433 -0.0100 1140 ASN A CB  
8537  C CG  . ASN A 1142 ? 0.4795 0.5399 0.5130 -0.0070 -0.0466 -0.0098 1140 ASN A CG  
8538  O OD1 . ASN A 1142 ? 0.4850 0.5445 0.5177 -0.0061 -0.0496 -0.0114 1140 ASN A OD1 
8539  N ND2 . ASN A 1142 ? 0.5067 0.5724 0.5456 -0.0107 -0.0462 -0.0077 1140 ASN A ND2 
8540  N N   . LEU A 1143 ? 0.3040 0.3412 0.3211 -0.0032 -0.0389 -0.0099 1141 LEU A N   
8541  C CA  . LEU A 1143 ? 0.2898 0.3223 0.3021 -0.0005 -0.0361 -0.0100 1141 LEU A CA  
8542  C C   . LEU A 1143 ? 0.2919 0.3285 0.3061 -0.0003 -0.0328 -0.0087 1141 LEU A C   
8543  O O   . LEU A 1143 ? 0.3058 0.3474 0.3243 -0.0031 -0.0322 -0.0074 1141 LEU A O   
8544  C CB  . LEU A 1143 ? 0.2780 0.3032 0.2871 -0.0015 -0.0361 -0.0103 1141 LEU A CB  
8545  C CG  . LEU A 1143 ? 0.3066 0.3264 0.3117 -0.0003 -0.0386 -0.0124 1141 LEU A CG  
8546  C CD1 . LEU A 1143 ? 0.2755 0.2892 0.2791 -0.0018 -0.0385 -0.0125 1141 LEU A CD1 
8547  C CD2 . LEU A 1143 ? 0.2631 0.2812 0.2631 0.0038  -0.0377 -0.0131 1141 LEU A CD2 
8548  N N   . PRO A 1144 ? 0.2732 0.3081 0.2846 0.0030  -0.0307 -0.0091 1142 PRO A N   
8549  C CA  . PRO A 1144 ? 0.2992 0.3367 0.3120 0.0033  -0.0276 -0.0085 1142 PRO A CA  
8550  C C   . PRO A 1144 ? 0.2782 0.3133 0.2906 0.0005  -0.0264 -0.0073 1142 PRO A C   
8551  O O   . PRO A 1144 ? 0.2481 0.2769 0.2576 -0.0003 -0.0272 -0.0073 1142 PRO A O   
8552  C CB  . PRO A 1144 ? 0.3089 0.3423 0.3181 0.0072  -0.0262 -0.0091 1142 PRO A CB  
8553  C CG  . PRO A 1144 ? 0.3085 0.3397 0.3154 0.0091  -0.0286 -0.0097 1142 PRO A CG  
8554  C CD  . PRO A 1144 ? 0.2972 0.3273 0.3040 0.0064  -0.0311 -0.0100 1142 PRO A CD  
8555  N N   . GLN A 1145 ? 0.2788 0.3194 0.2943 -0.0009 -0.0244 -0.0063 1143 GLN A N   
8556  C CA  . GLN A 1145 ? 0.2492 0.2882 0.2647 -0.0038 -0.0234 -0.0047 1143 GLN A CA  
8557  C C   . GLN A 1145 ? 0.2521 0.2830 0.2627 -0.0023 -0.0221 -0.0051 1143 GLN A C   
8558  O O   . GLN A 1145 ? 0.2796 0.3062 0.2892 -0.0043 -0.0225 -0.0041 1143 GLN A O   
8559  C CB  . GLN A 1145 ? 0.3456 0.3929 0.3647 -0.0051 -0.0213 -0.0036 1143 GLN A CB  
8560  C CG  . GLN A 1145 ? 0.4477 0.4958 0.4684 -0.0092 -0.0211 -0.0010 1143 GLN A CG  
8561  C CD  . GLN A 1145 ? 0.4986 0.5439 0.5210 -0.0122 -0.0244 0.0001  1143 GLN A CD  
8562  O OE1 . GLN A 1145 ? 0.4848 0.5222 0.5047 -0.0127 -0.0255 0.0001  1143 GLN A OE1 
8563  N NE2 . GLN A 1145 ? 0.5670 0.6190 0.5939 -0.0141 -0.0260 0.0009  1143 GLN A NE2 
8564  N N   . THR A 1146 ? 0.2545 0.2833 0.2625 0.0012  -0.0207 -0.0063 1144 THR A N   
8565  C CA  . THR A 1146 ? 0.2685 0.2901 0.2721 0.0026  -0.0193 -0.0064 1144 THR A CA  
8566  C C   . THR A 1146 ? 0.2807 0.2958 0.2810 0.0024  -0.0213 -0.0066 1144 THR A C   
8567  O O   . THR A 1146 ? 0.2701 0.2801 0.2679 0.0019  -0.0206 -0.0063 1144 THR A O   
8568  C CB  . THR A 1146 ? 0.2850 0.3056 0.2872 0.0064  -0.0181 -0.0073 1144 THR A CB  
8569  O OG1 . THR A 1146 ? 0.2817 0.3030 0.2838 0.0082  -0.0199 -0.0080 1144 THR A OG1 
8570  C CG2 . THR A 1146 ? 0.2967 0.3232 0.3021 0.0069  -0.0161 -0.0077 1144 THR A CG2 
8571  N N   . VAL A 1147 ? 0.2746 0.2902 0.2749 0.0031  -0.0237 -0.0075 1145 VAL A N   
8572  C CA  . VAL A 1147 ? 0.2262 0.2366 0.2234 0.0031  -0.0258 -0.0084 1145 VAL A CA  
8573  C C   . VAL A 1147 ? 0.2059 0.2159 0.2058 -0.0005 -0.0277 -0.0081 1145 VAL A C   
8574  O O   . VAL A 1147 ? 0.2449 0.2495 0.2428 -0.0011 -0.0284 -0.0086 1145 VAL A O   
8575  C CB  . VAL A 1147 ? 0.2113 0.2227 0.2074 0.0052  -0.0278 -0.0096 1145 VAL A CB  
8576  C CG1 . VAL A 1147 ? 0.2200 0.2266 0.2124 0.0057  -0.0300 -0.0111 1145 VAL A CG1 
8577  C CG2 . VAL A 1147 ? 0.2365 0.2485 0.2310 0.0087  -0.0263 -0.0093 1145 VAL A CG2 
8578  N N   . GLY A 1148 ? 0.2238 0.2398 0.2287 -0.0030 -0.0285 -0.0071 1146 GLY A N   
8579  C CA  . GLY A 1148 ? 0.2457 0.2615 0.2540 -0.0068 -0.0305 -0.0062 1146 GLY A CA  
8580  C C   . GLY A 1148 ? 0.2607 0.2731 0.2688 -0.0084 -0.0291 -0.0048 1146 GLY A C   
8581  O O   . GLY A 1148 ? 0.2640 0.2725 0.2732 -0.0105 -0.0311 -0.0046 1146 GLY A O   
8582  N N   . LEU A 1149 ? 0.2477 0.2614 0.2546 -0.0075 -0.0259 -0.0038 1147 LEU A N   
8583  C CA  . LEU A 1149 ? 0.2618 0.2724 0.2681 -0.0088 -0.0244 -0.0024 1147 LEU A CA  
8584  C C   . LEU A 1149 ? 0.2304 0.2326 0.2327 -0.0075 -0.0251 -0.0038 1147 LEU A C   
8585  O O   . LEU A 1149 ? 0.2814 0.2803 0.2842 -0.0092 -0.0252 -0.0028 1147 LEU A O   
8586  C CB  . LEU A 1149 ? 0.3019 0.3153 0.3071 -0.0074 -0.0209 -0.0018 1147 LEU A CB  
8587  C CG  . LEU A 1149 ? 0.3884 0.4109 0.3975 -0.0086 -0.0196 -0.0006 1147 LEU A CG  
8588  C CD1 . LEU A 1149 ? 0.3556 0.3794 0.3629 -0.0064 -0.0165 -0.0011 1147 LEU A CD1 
8589  C CD2 . LEU A 1149 ? 0.4083 0.4345 0.4214 -0.0129 -0.0203 0.0022  1147 LEU A CD2 
8590  N N   . ARG A 1150 ? 0.2351 0.2346 0.2337 -0.0045 -0.0257 -0.0060 1148 ARG A N   
8591  C CA  . ARG A 1150 ? 0.2221 0.2148 0.2166 -0.0028 -0.0262 -0.0076 1148 ARG A CA  
8592  C C   . ARG A 1150 ? 0.2268 0.2169 0.2219 -0.0035 -0.0299 -0.0096 1148 ARG A C   
8593  O O   . ARG A 1150 ? 0.2562 0.2412 0.2482 -0.0021 -0.0306 -0.0113 1148 ARG A O   
8594  C CB  . ARG A 1150 ? 0.2159 0.2074 0.2056 0.0010  -0.0246 -0.0086 1148 ARG A CB  
8595  C CG  . ARG A 1150 ? 0.2538 0.2456 0.2424 0.0021  -0.0213 -0.0073 1148 ARG A CG  
8596  C CD  . ARG A 1150 ? 0.2346 0.2221 0.2183 0.0050  -0.0201 -0.0080 1148 ARG A CD  
8597  N NE  . ARG A 1150 ? 0.2237 0.2116 0.2067 0.0065  -0.0173 -0.0069 1148 ARG A NE  
8598  C CZ  . ARG A 1150 ? 0.2417 0.2278 0.2215 0.0093  -0.0163 -0.0069 1148 ARG A CZ  
8599  N NH1 . ARG A 1150 ? 0.2083 0.1929 0.1849 0.0110  -0.0177 -0.0078 1148 ARG A NH1 
8600  N NH2 . ARG A 1150 ? 0.2225 0.2090 0.2026 0.0103  -0.0141 -0.0059 1148 ARG A NH2 
8601  N N   . VAL A 1151 ? 0.2257 0.2195 0.2247 -0.0054 -0.0323 -0.0094 1149 VAL A N   
8602  C CA  . VAL A 1151 ? 0.2384 0.2303 0.2383 -0.0059 -0.0361 -0.0117 1149 VAL A CA  
8603  C C   . VAL A 1151 ? 0.2830 0.2743 0.2887 -0.0099 -0.0385 -0.0105 1149 VAL A C   
8604  O O   . VAL A 1151 ? 0.2828 0.2790 0.2931 -0.0128 -0.0381 -0.0077 1149 VAL A O   
8605  C CB  . VAL A 1151 ? 0.2566 0.2531 0.2567 -0.0048 -0.0374 -0.0127 1149 VAL A CB  
8606  C CG1 . VAL A 1151 ? 0.2704 0.2656 0.2725 -0.0058 -0.0418 -0.0151 1149 VAL A CG1 
8607  C CG2 . VAL A 1151 ? 0.2318 0.2280 0.2263 -0.0007 -0.0357 -0.0138 1149 VAL A CG2 
8608  N N   . SER A 1152 ? 0.2695 0.2553 0.2753 -0.0101 -0.0412 -0.0126 1150 SER A N   
8609  C CA  . SER A 1152 ? 0.2648 0.2495 0.2769 -0.0139 -0.0446 -0.0119 1150 SER A CA  
8610  C C   . SER A 1152 ? 0.2800 0.2611 0.2918 -0.0129 -0.0487 -0.0161 1150 SER A C   
8611  O O   . SER A 1152 ? 0.2849 0.2637 0.2911 -0.0092 -0.0485 -0.0194 1150 SER A O   
8612  C CB  . SER A 1152 ? 0.3109 0.2915 0.3248 -0.0157 -0.0441 -0.0100 1150 SER A CB  
8613  O OG  . SER A 1152 ? 0.3486 0.3230 0.3582 -0.0129 -0.0439 -0.0128 1150 SER A OG  
8614  N N   . TRP A 1153 ? 0.2828 0.2640 0.3010 -0.0161 -0.0526 -0.0158 1151 TRP A N   
8615  C CA  . TRP A 1153 ? 0.2874 0.2652 0.3066 -0.0157 -0.0571 -0.0200 1151 TRP A CA  
8616  C C   . TRP A 1153 ? 0.3301 0.3018 0.3540 -0.0178 -0.0600 -0.0204 1151 TRP A C   
8617  O O   . TRP A 1153 ? 0.3757 0.3478 0.4052 -0.0215 -0.0601 -0.0163 1151 TRP A O   
8618  C CB  . TRP A 1153 ? 0.2689 0.2516 0.2926 -0.0177 -0.0600 -0.0198 1151 TRP A CB  
8619  C CG  . TRP A 1153 ? 0.3006 0.2887 0.3200 -0.0151 -0.0582 -0.0205 1151 TRP A CG  
8620  C CD1 . TRP A 1153 ? 0.3061 0.3002 0.3250 -0.0151 -0.0547 -0.0172 1151 TRP A CD1 
8621  C CD2 . TRP A 1153 ? 0.2789 0.2671 0.2940 -0.0119 -0.0599 -0.0246 1151 TRP A CD2 
8622  N NE1 . TRP A 1153 ? 0.3095 0.3069 0.3246 -0.0122 -0.0543 -0.0190 1151 TRP A NE1 
8623  C CE2 . TRP A 1153 ? 0.2761 0.2702 0.2887 -0.0103 -0.0574 -0.0232 1151 TRP A CE2 
8624  C CE3 . TRP A 1153 ? 0.2756 0.2599 0.2889 -0.0101 -0.0634 -0.0295 1151 TRP A CE3 
8625  C CZ2 . TRP A 1153 ? 0.2945 0.2905 0.3027 -0.0071 -0.0584 -0.0260 1151 TRP A CZ2 
8626  C CZ3 . TRP A 1153 ? 0.2728 0.2597 0.2814 -0.0069 -0.0642 -0.0325 1151 TRP A CZ3 
8627  C CH2 . TRP A 1153 ? 0.3159 0.3086 0.3221 -0.0056 -0.0617 -0.0304 1151 TRP A CH2 
8628  N N   . SER A 1154 ? 0.2890 0.2552 0.3105 -0.0153 -0.0623 -0.0252 1152 SER A N   
8629  C CA  . SER A 1154 ? 0.2856 0.2452 0.3110 -0.0164 -0.0649 -0.0263 1152 SER A CA  
8630  C C   . SER A 1154 ? 0.3493 0.3058 0.3787 -0.0167 -0.0707 -0.0309 1152 SER A C   
8631  O O   . SER A 1154 ? 0.3127 0.2694 0.3375 -0.0133 -0.0718 -0.0359 1152 SER A O   
8632  C CB  . SER A 1154 ? 0.2995 0.2551 0.3188 -0.0127 -0.0622 -0.0283 1152 SER A CB  
8633  O OG  . SER A 1154 ? 0.3319 0.2811 0.3553 -0.0136 -0.0648 -0.0294 1152 SER A OG  
8634  N N   . LYS A 1155 ? 0.3071 0.2610 0.3452 -0.0207 -0.0745 -0.0292 1153 LYS A N   
8635  C CA  . LYS A 1155 ? 0.3739 0.3233 0.4169 -0.0211 -0.0805 -0.0339 1153 LYS A CA  
8636  C C   . LYS A 1155 ? 0.3852 0.3270 0.4289 -0.0194 -0.0822 -0.0371 1153 LYS A C   
8637  O O   . LYS A 1155 ? 0.4838 0.4221 0.5264 -0.0166 -0.0855 -0.0437 1153 LYS A O   
8638  C CB  . LYS A 1155 ? 0.3396 0.2903 0.3928 -0.0266 -0.0844 -0.0303 1153 LYS A CB  
8639  N N   . ASP A 1156 ? 0.3751 0.3146 0.4204 -0.0209 -0.0800 -0.0330 1154 ASP A N   
8640  C CA  . ASP A 1156 ? 0.3796 0.3119 0.4261 -0.0195 -0.0813 -0.0352 1154 ASP A CA  
8641  C C   . ASP A 1156 ? 0.3564 0.2896 0.3943 -0.0159 -0.0755 -0.0348 1154 ASP A C   
8642  O O   . ASP A 1156 ? 0.3528 0.2873 0.3907 -0.0176 -0.0720 -0.0294 1154 ASP A O   
8643  C CB  . ASP A 1156 ? 0.4107 0.3398 0.4671 -0.0244 -0.0838 -0.0301 1154 ASP A CB  
8644  C CG  . ASP A 1156 ? 0.4994 0.4208 0.5582 -0.0230 -0.0856 -0.0324 1154 ASP A CG  
8645  O OD1 . ASP A 1156 ? 0.5519 0.4710 0.6043 -0.0182 -0.0845 -0.0378 1154 ASP A OD1 
8646  O OD2 . ASP A 1156 ? 0.5405 0.4585 0.6078 -0.0267 -0.0884 -0.0286 1154 ASP A OD2 
8647  N N   . TRP A 1157 ? 0.3469 0.2797 0.3776 -0.0110 -0.0747 -0.0405 1155 TRP A N   
8648  C CA  . TRP A 1157 ? 0.3258 0.2601 0.3482 -0.0077 -0.0692 -0.0400 1155 TRP A CA  
8649  C C   . TRP A 1157 ? 0.3380 0.2679 0.3624 -0.0082 -0.0679 -0.0377 1155 TRP A C   
8650  O O   . TRP A 1157 ? 0.3119 0.2437 0.3323 -0.0078 -0.0632 -0.0340 1155 TRP A O   
8651  C CB  . TRP A 1157 ? 0.3219 0.2566 0.3370 -0.0025 -0.0691 -0.0465 1155 TRP A CB  
8652  C CG  . TRP A 1157 ? 0.2998 0.2391 0.3122 -0.0014 -0.0705 -0.0491 1155 TRP A CG  
8653  C CD1 . TRP A 1157 ? 0.2951 0.2386 0.3099 -0.0042 -0.0709 -0.0462 1155 TRP A CD1 
8654  C CD2 . TRP A 1157 ? 0.2970 0.2375 0.3037 0.0030  -0.0716 -0.0554 1155 TRP A CD2 
8655  N NE1 . TRP A 1157 ? 0.3121 0.2590 0.3232 -0.0019 -0.0724 -0.0501 1155 TRP A NE1 
8656  C CE2 . TRP A 1157 ? 0.3191 0.2644 0.3251 0.0025  -0.0729 -0.0558 1155 TRP A CE2 
8657  C CE3 . TRP A 1157 ? 0.3070 0.2458 0.3093 0.0073  -0.0717 -0.0608 1155 TRP A CE3 
8658  C CZ2 . TRP A 1157 ? 0.3169 0.2653 0.3177 0.0061  -0.0743 -0.0612 1155 TRP A CZ2 
8659  C CZ3 . TRP A 1157 ? 0.2847 0.2269 0.2817 0.0109  -0.0730 -0.0662 1155 TRP A CZ3 
8660  C CH2 . TRP A 1157 ? 0.3038 0.2507 0.3000 0.0103  -0.0743 -0.0663 1155 TRP A CH2 
8661  N N   . ALA A 1158 ? 0.3311 0.2549 0.3619 -0.0089 -0.0723 -0.0399 1156 ALA A N   
8662  C CA  . ALA A 1158 ? 0.3520 0.2714 0.3850 -0.0092 -0.0714 -0.0380 1156 ALA A CA  
8663  C C   . ALA A 1158 ? 0.3875 0.3088 0.4243 -0.0137 -0.0693 -0.0300 1156 ALA A C   
8664  O O   . ALA A 1158 ? 0.4550 0.3755 0.4904 -0.0135 -0.0663 -0.0271 1156 ALA A O   
8665  C CB  . ALA A 1158 ? 0.3996 0.3119 0.4397 -0.0091 -0.0772 -0.0421 1156 ALA A CB  
8666  N N   . ALA A 1159 ? 0.3662 0.2908 0.4079 -0.0178 -0.0709 -0.0263 1157 ALA A N   
8667  C CA  . ALA A 1159 ? 0.4072 0.3350 0.4526 -0.0221 -0.0690 -0.0187 1157 ALA A CA  
8668  C C   . ALA A 1159 ? 0.3824 0.3168 0.4208 -0.0212 -0.0629 -0.0157 1157 ALA A C   
8669  O O   . ALA A 1159 ? 0.3936 0.3305 0.4332 -0.0237 -0.0604 -0.0101 1157 ALA A O   
8670  C CB  . ALA A 1159 ? 0.3664 0.2963 0.4199 -0.0268 -0.0728 -0.0157 1157 ALA A CB  
8671  N N   . ASP A 1160 ? 0.3484 0.2855 0.3795 -0.0178 -0.0607 -0.0192 1158 ASP A N   
8672  C CA  . ASP A 1160 ? 0.3709 0.3144 0.3965 -0.0171 -0.0557 -0.0165 1158 ASP A CA  
8673  C C   . ASP A 1160 ? 0.3246 0.2674 0.3425 -0.0131 -0.0515 -0.0179 1158 ASP A C   
8674  O O   . ASP A 1160 ? 0.3487 0.2961 0.3617 -0.0120 -0.0475 -0.0163 1158 ASP A O   
8675  C CB  . ASP A 1160 ? 0.3928 0.3409 0.4166 -0.0166 -0.0564 -0.0182 1158 ASP A CB  
8676  C CG  . ASP A 1160 ? 0.4305 0.3809 0.4621 -0.0210 -0.0599 -0.0157 1158 ASP A CG  
8677  O OD1 . ASP A 1160 ? 0.4788 0.4291 0.5163 -0.0248 -0.0604 -0.0110 1158 ASP A OD1 
8678  O OD2 . ASP A 1160 ? 0.4059 0.3585 0.4379 -0.0208 -0.0620 -0.0181 1158 ASP A OD2 
8679  N N   . GLY A 1161 ? 0.3411 0.2784 0.3582 -0.0110 -0.0524 -0.0208 1159 GLY A N   
8680  C CA  . GLY A 1161 ? 0.3151 0.2518 0.3257 -0.0074 -0.0485 -0.0218 1159 GLY A CA  
8681  C C   . GLY A 1161 ? 0.3519 0.2887 0.3636 -0.0092 -0.0457 -0.0170 1159 GLY A C   
8682  O O   . GLY A 1161 ? 0.3949 0.3330 0.4120 -0.0131 -0.0464 -0.0125 1159 GLY A O   
8683  N N   . PRO A 1162 ? 0.3413 0.2770 0.3481 -0.0063 -0.0425 -0.0176 1160 PRO A N   
8684  C CA  . PRO A 1162 ? 0.3543 0.2890 0.3550 -0.0017 -0.0414 -0.0223 1160 PRO A CA  
8685  C C   . PRO A 1162 ? 0.3166 0.2562 0.3114 0.0002  -0.0389 -0.0228 1160 PRO A C   
8686  O O   . PRO A 1162 ? 0.2925 0.2361 0.2862 -0.0011 -0.0361 -0.0193 1160 PRO A O   
8687  C CB  . PRO A 1162 ? 0.3342 0.2670 0.3330 -0.0005 -0.0385 -0.0210 1160 PRO A CB  
8688  C CG  . PRO A 1162 ? 0.3893 0.3249 0.3901 -0.0038 -0.0362 -0.0153 1160 PRO A CG  
8689  C CD  . PRO A 1162 ? 0.3578 0.2939 0.3651 -0.0077 -0.0396 -0.0132 1160 PRO A CD  
8690  N N   . PHE A 1163 ? 0.2433 0.1829 0.2345 0.0033  -0.0401 -0.0274 1161 PHE A N   
8691  C CA  . PHE A 1163 ? 0.2238 0.1678 0.2089 0.0057  -0.0377 -0.0279 1161 PHE A CA  
8692  C C   . PHE A 1163 ? 0.2591 0.2033 0.2386 0.0090  -0.0342 -0.0283 1161 PHE A C   
8693  O O   . PHE A 1163 ? 0.2839 0.2248 0.2637 0.0099  -0.0339 -0.0292 1161 PHE A O   
8694  C CB  . PHE A 1163 ? 0.2082 0.1532 0.1924 0.0071  -0.0409 -0.0322 1161 PHE A CB  
8695  C CG  . PHE A 1163 ? 0.2501 0.1949 0.2405 0.0037  -0.0447 -0.0318 1161 PHE A CG  
8696  C CD1 . PHE A 1163 ? 0.2936 0.2422 0.2861 0.0009  -0.0436 -0.0277 1161 PHE A CD1 
8697  C CD2 . PHE A 1163 ? 0.2768 0.2180 0.2715 0.0033  -0.0494 -0.0356 1161 PHE A CD2 
8698  C CE1 . PHE A 1163 ? 0.2736 0.2227 0.2721 -0.0025 -0.0469 -0.0269 1161 PHE A CE1 
8699  C CE2 . PHE A 1163 ? 0.2931 0.2341 0.2941 -0.0002 -0.0530 -0.0348 1161 PHE A CE2 
8700  C CZ  . PHE A 1163 ? 0.2862 0.2315 0.2891 -0.0032 -0.0516 -0.0302 1161 PHE A CZ  
8701  N N   . ALA A 1164 ? 0.2366 0.1848 0.2111 0.0106  -0.0314 -0.0272 1162 ALA A N   
8702  C CA  . ALA A 1164 ? 0.2441 0.1932 0.2135 0.0135  -0.0280 -0.0268 1162 ALA A CA  
8703  C C   . ALA A 1164 ? 0.2299 0.1820 0.1939 0.0170  -0.0281 -0.0298 1162 ALA A C   
8704  O O   . ALA A 1164 ? 0.2793 0.2333 0.2388 0.0194  -0.0253 -0.0291 1162 ALA A O   
8705  C CB  . ALA A 1164 ? 0.2490 0.2003 0.2179 0.0124  -0.0244 -0.0222 1162 ALA A CB  
8706  N N   . GLY A 1165 ? 0.2126 0.1656 0.1772 0.0172  -0.0314 -0.0329 1163 GLY A N   
8707  C CA  . GLY A 1165 ? 0.2239 0.1804 0.1834 0.0205  -0.0321 -0.0360 1163 GLY A CA  
8708  C C   . GLY A 1165 ? 0.2376 0.1952 0.1992 0.0194  -0.0358 -0.0382 1163 GLY A C   
8709  O O   . GLY A 1165 ? 0.2364 0.1923 0.2033 0.0162  -0.0375 -0.0369 1163 GLY A O   
8710  N N   . ALA A 1166 ? 0.2107 0.1718 0.1681 0.0222  -0.0371 -0.0414 1164 ALA A N   
8711  C CA  . ALA A 1166 ? 0.2128 0.1754 0.1717 0.0215  -0.0407 -0.0437 1164 ALA A CA  
8712  C C   . ALA A 1166 ? 0.2231 0.1916 0.1762 0.0243  -0.0403 -0.0444 1164 ALA A C   
8713  O O   . ALA A 1166 ? 0.2421 0.2132 0.1897 0.0273  -0.0382 -0.0447 1164 ALA A O   
8714  C CB  . ALA A 1166 ? 0.2398 0.1991 0.2020 0.0216  -0.0452 -0.0493 1164 ALA A CB  
8715  N N   . LEU A 1167 ? 0.1925 0.1633 0.1470 0.0231  -0.0424 -0.0442 1165 LEU A N   
8716  C CA  . LEU A 1167 ? 0.1949 0.1713 0.1449 0.0253  -0.0431 -0.0450 1165 LEU A CA  
8717  C C   . LEU A 1167 ? 0.2260 0.2029 0.1784 0.0249  -0.0480 -0.0497 1165 LEU A C   
8718  O O   . LEU A 1167 ? 0.2248 0.1993 0.1831 0.0217  -0.0501 -0.0492 1165 LEU A O   
8719  C CB  . LEU A 1167 ? 0.2125 0.1918 0.1625 0.0243  -0.0409 -0.0398 1165 LEU A CB  
8720  C CG  . LEU A 1167 ? 0.1947 0.1736 0.1432 0.0245  -0.0363 -0.0351 1165 LEU A CG  
8721  C CD1 . LEU A 1167 ? 0.2467 0.2279 0.1966 0.0233  -0.0349 -0.0307 1165 LEU A CD1 
8722  C CD2 . LEU A 1167 ? 0.2221 0.2039 0.1642 0.0280  -0.0345 -0.0354 1165 LEU A CD2 
8723  N N   . VAL A 1168 ? 0.2214 0.2015 0.1693 0.0281  -0.0498 -0.0542 1166 VAL A N   
8724  C CA  . VAL A 1168 ? 0.2184 0.1988 0.1683 0.0281  -0.0548 -0.0597 1166 VAL A CA  
8725  C C   . VAL A 1168 ? 0.2378 0.2252 0.1827 0.0304  -0.0558 -0.0606 1166 VAL A C   
8726  O O   . VAL A 1168 ? 0.2257 0.2177 0.1642 0.0334  -0.0533 -0.0596 1166 VAL A O   
8727  C CB  . VAL A 1168 ? 0.2452 0.2230 0.1951 0.0301  -0.0570 -0.0659 1166 VAL A CB  
8728  C CG1 . VAL A 1168 ? 0.2539 0.2314 0.2068 0.0300  -0.0626 -0.0719 1166 VAL A CG1 
8729  C CG2 . VAL A 1168 ? 0.2604 0.2314 0.2150 0.0281  -0.0559 -0.0645 1166 VAL A CG2 
8730  N N   . GLU A 1169 ? 0.2155 0.2039 0.1636 0.0289  -0.0595 -0.0622 1167 GLU A N   
8731  C CA  . GLU A 1169 ? 0.2347 0.2296 0.1787 0.0309  -0.0614 -0.0639 1167 GLU A CA  
8732  C C   . GLU A 1169 ? 0.2572 0.2519 0.2031 0.0314  -0.0668 -0.0711 1167 GLU A C   
8733  O O   . GLU A 1169 ? 0.2718 0.2616 0.2247 0.0284  -0.0698 -0.0727 1167 GLU A O   
8734  C CB  . GLU A 1169 ? 0.2220 0.2193 0.1682 0.0288  -0.0610 -0.0591 1167 GLU A CB  
8735  C CG  . GLU A 1169 ? 0.2361 0.2403 0.1787 0.0306  -0.0632 -0.0603 1167 GLU A CG  
8736  C CD  . GLU A 1169 ? 0.2479 0.2537 0.1946 0.0281  -0.0639 -0.0566 1167 GLU A CD  
8737  O OE1 . GLU A 1169 ? 0.2467 0.2485 0.1994 0.0248  -0.0632 -0.0539 1167 GLU A OE1 
8738  O OE2 . GLU A 1169 ? 0.2497 0.2612 0.1938 0.0295  -0.0653 -0.0564 1167 GLU A OE2 
8739  N N   . GLY A 1170 ? 0.2351 0.2353 0.1751 0.0351  -0.0681 -0.0754 1168 GLY A N   
8740  C CA  . GLY A 1170 ? 0.2604 0.2611 0.2021 0.0358  -0.0736 -0.0827 1168 GLY A CA  
8741  C C   . GLY A 1170 ? 0.2603 0.2677 0.1943 0.0406  -0.0741 -0.0876 1168 GLY A C   
8742  O O   . GLY A 1170 ? 0.2728 0.2842 0.2003 0.0431  -0.0701 -0.0850 1168 GLY A O   
8743  N N   . ASP A 1171 ? 0.2768 0.2856 0.2116 0.0417  -0.0792 -0.0949 1169 ASP A N   
8744  C CA  . ASP A 1171 ? 0.2781 0.2934 0.2060 0.0465  -0.0801 -0.1008 1169 ASP A CA  
8745  C C   . ASP A 1171 ? 0.3046 0.3158 0.2329 0.0482  -0.0794 -0.1048 1169 ASP A C   
8746  O O   . ASP A 1171 ? 0.2798 0.2831 0.2138 0.0457  -0.0783 -0.1026 1169 ASP A O   
8747  C CB  . ASP A 1171 ? 0.2943 0.3134 0.2226 0.0475  -0.0860 -0.1076 1169 ASP A CB  
8748  C CG  . ASP A 1171 ? 0.3712 0.3826 0.3085 0.0450  -0.0913 -0.1131 1169 ASP A CG  
8749  O OD1 . ASP A 1171 ? 0.3311 0.3352 0.2730 0.0441  -0.0912 -0.1144 1169 ASP A OD1 
8750  O OD2 . ASP A 1171 ? 0.4444 0.4572 0.3846 0.0440  -0.0958 -0.1161 1169 ASP A OD2 
8751  N N   . ALA A 1172 ? 0.3031 0.3205 0.2254 0.0528  -0.0799 -0.1106 1170 ALA A N   
8752  C CA  . ALA A 1172 ? 0.2990 0.3141 0.2205 0.0551  -0.0782 -0.1136 1170 ALA A CA  
8753  C C   . ALA A 1172 ? 0.2787 0.2840 0.2093 0.0531  -0.0818 -0.1181 1170 ALA A C   
8754  O O   . ALA A 1172 ? 0.3172 0.3166 0.2506 0.0524  -0.0798 -0.1168 1170 ALA A O   
8755  C CB  . ALA A 1172 ? 0.3053 0.3296 0.2213 0.0597  -0.0770 -0.1173 1170 ALA A CB  
8756  N N   . GLU A 1173 ? 0.3389 0.3427 0.2755 0.0518  -0.0864 -0.1221 1171 GLU A N   
8757  C CA  . GLU A 1173 ? 0.3299 0.3246 0.2762 0.0499  -0.0897 -0.1254 1171 GLU A CA  
8758  C C   . GLU A 1173 ? 0.2822 0.2683 0.2344 0.0449  -0.0907 -0.1210 1171 GLU A C   
8759  O O   . GLU A 1173 ? 0.3270 0.3052 0.2857 0.0433  -0.0915 -0.1214 1171 GLU A O   
8760  C CB  . GLU A 1173 ? 0.3883 0.3838 0.3397 0.0501  -0.0945 -0.1310 1171 GLU A CB  
8761  C CG  . GLU A 1173 ? 0.4170 0.4195 0.3648 0.0551  -0.0941 -0.1366 1171 GLU A CG  
8762  C CD  . GLU A 1173 ? 0.4377 0.4385 0.3852 0.0576  -0.0914 -0.1380 1171 GLU A CD  
8763  O OE1 . GLU A 1173 ? 0.4147 0.4065 0.3689 0.0555  -0.0924 -0.1377 1171 GLU A OE1 
8764  O OE2 . GLU A 1173 ? 0.4392 0.4481 0.3797 0.0617  -0.0884 -0.1392 1171 GLU A OE2 
8765  N N   . ARG A 1174 ? 0.2731 0.2613 0.2244 0.0422  -0.0891 -0.1146 1172 ARG A N   
8766  C CA  . ARG A 1174 ? 0.2833 0.2652 0.2408 0.0373  -0.0873 -0.1072 1172 ARG A CA  
8767  C C   . ARG A 1174 ? 0.2654 0.2450 0.2210 0.0375  -0.0818 -0.1024 1172 ARG A C   
8768  O O   . ARG A 1174 ? 0.2739 0.2463 0.2358 0.0346  -0.0815 -0.0998 1172 ARG A O   
8769  C CB  . ARG A 1174 ? 0.2654 0.2513 0.2220 0.0349  -0.0861 -0.1013 1172 ARG A CB  
8770  C CG  . ARG A 1174 ? 0.2626 0.2438 0.2248 0.0302  -0.0835 -0.0933 1172 ARG A CG  
8771  C CD  . ARG A 1174 ? 0.2811 0.2549 0.2536 0.0262  -0.0877 -0.0946 1172 ARG A CD  
8772  N NE  . ARG A 1174 ? 0.2871 0.2579 0.2644 0.0218  -0.0851 -0.0869 1172 ARG A NE  
8773  C CZ  . ARG A 1174 ? 0.3285 0.2927 0.3142 0.0181  -0.0867 -0.0854 1172 ARG A CZ  
8774  N NH1 . ARG A 1174 ? 0.3458 0.3049 0.3366 0.0182  -0.0912 -0.0909 1172 ARG A NH1 
8775  N NH2 . ARG A 1174 ? 0.2924 0.2555 0.2815 0.0144  -0.0840 -0.0782 1172 ARG A NH2 
8776  N N   . ILE A 1175 ? 0.2655 0.2512 0.2125 0.0410  -0.0776 -0.1011 1173 ILE A N   
8777  C CA  . ILE A 1175 ? 0.2463 0.2305 0.1910 0.0414  -0.0723 -0.0965 1173 ILE A CA  
8778  C C   . ILE A 1175 ? 0.2495 0.2282 0.1976 0.0426  -0.0737 -0.1014 1173 ILE A C   
8779  O O   . ILE A 1175 ? 0.2837 0.2566 0.2356 0.0406  -0.0715 -0.0977 1173 ILE A O   
8780  C CB  . ILE A 1175 ? 0.2741 0.2669 0.2093 0.0450  -0.0682 -0.0943 1173 ILE A CB  
8781  C CG1 . ILE A 1175 ? 0.2859 0.2826 0.2190 0.0432  -0.0663 -0.0878 1173 ILE A CG1 
8782  C CG2 . ILE A 1175 ? 0.2640 0.2557 0.1967 0.0462  -0.0634 -0.0915 1173 ILE A CG2 
8783  C CD1 . ILE A 1175 ? 0.2937 0.2991 0.2180 0.0464  -0.0627 -0.0851 1173 ILE A CD1 
8784  N N   . ARG A 1176 ? 0.2880 0.2687 0.2351 0.0461  -0.0774 -0.1099 1174 ARG A N   
8785  C CA  . ARG A 1176 ? 0.2635 0.2390 0.2142 0.0477  -0.0791 -0.1153 1174 ARG A CA  
8786  C C   . ARG A 1176 ? 0.2670 0.2326 0.2284 0.0434  -0.0825 -0.1146 1174 ARG A C   
8787  O O   . ARG A 1176 ? 0.2835 0.2432 0.2488 0.0426  -0.0815 -0.1134 1174 ARG A O   
8788  C CB  . ARG A 1176 ? 0.2979 0.2784 0.2472 0.0519  -0.0820 -0.1235 1174 ARG A CB  
8789  C CG  . ARG A 1176 ? 0.3329 0.3106 0.2858 0.0541  -0.0817 -0.1270 1174 ARG A CG  
8790  C CD  . ARG A 1176 ? 0.3373 0.3187 0.2928 0.0571  -0.0849 -0.1339 1174 ARG A CD  
8791  N NE  . ARG A 1176 ? 0.3215 0.3135 0.2695 0.0600  -0.0840 -0.1355 1174 ARG A NE  
8792  C CZ  . ARG A 1176 ? 0.3921 0.3929 0.3328 0.0641  -0.0806 -0.1365 1174 ARG A CZ  
8793  N NH1 . ARG A 1176 ? 0.3606 0.3613 0.3003 0.0661  -0.0776 -0.1363 1174 ARG A NH1 
8794  N NH2 . ARG A 1176 ? 0.3764 0.3869 0.3111 0.0663  -0.0803 -0.1374 1174 ARG A NH2 
8795  N N   . ALA A 1177 ? 0.2751 0.2390 0.2414 0.0403  -0.0866 -0.1149 1175 ALA A N   
8796  C CA  . ALA A 1177 ? 0.3201 0.2753 0.2971 0.0358  -0.0901 -0.1135 1175 ALA A CA  
8797  C C   . ALA A 1177 ? 0.2728 0.2246 0.2520 0.0319  -0.0856 -0.1043 1175 ALA A C   
8798  O O   . ALA A 1177 ? 0.2897 0.2345 0.2755 0.0298  -0.0863 -0.1028 1175 ALA A O   
8799  C CB  . ALA A 1177 ? 0.3064 0.2620 0.2878 0.0332  -0.0949 -0.1148 1175 ALA A CB  
8800  N N   . VAL A 1178 ? 0.2856 0.2423 0.2597 0.0310  -0.0813 -0.0980 1176 VAL A N   
8801  C CA  . VAL A 1178 ? 0.2491 0.2034 0.2249 0.0276  -0.0770 -0.0896 1176 VAL A CA  
8802  C C   . VAL A 1178 ? 0.2735 0.2259 0.2469 0.0295  -0.0732 -0.0885 1176 VAL A C   
8803  O O   . VAL A 1178 ? 0.2657 0.2129 0.2437 0.0267  -0.0718 -0.0842 1176 VAL A O   
8804  C CB  . VAL A 1178 ? 0.2503 0.2107 0.2210 0.0269  -0.0734 -0.0839 1176 VAL A CB  
8805  C CG1 . VAL A 1178 ? 0.2447 0.2036 0.2159 0.0244  -0.0685 -0.0761 1176 VAL A CG1 
8806  C CG2 . VAL A 1178 ? 0.2542 0.2157 0.2290 0.0242  -0.0772 -0.0840 1176 VAL A CG2 
8807  N N   . ASN A 1179 ? 0.2746 0.2315 0.2408 0.0343  -0.0715 -0.0923 1177 ASN A N   
8808  C CA  . ASN A 1179 ? 0.2654 0.2213 0.2292 0.0363  -0.0678 -0.0915 1177 ASN A CA  
8809  C C   . ASN A 1179 ? 0.2675 0.2157 0.2387 0.0357  -0.0709 -0.0948 1177 ASN A C   
8810  O O   . ASN A 1179 ? 0.2714 0.2159 0.2445 0.0347  -0.0683 -0.0912 1177 ASN A O   
8811  C CB  . ASN A 1179 ? 0.3106 0.2740 0.2656 0.0416  -0.0660 -0.0954 1177 ASN A CB  
8812  C CG  . ASN A 1179 ? 0.3605 0.3259 0.3106 0.0431  -0.0603 -0.0913 1177 ASN A CG  
8813  O OD1 . ASN A 1179 ? 0.3804 0.3428 0.3324 0.0403  -0.0571 -0.0847 1177 ASN A OD1 
8814  N ND2 . ASN A 1179 ? 0.3734 0.3447 0.3174 0.0478  -0.0591 -0.0953 1177 ASN A ND2 
8815  N N   . LYS A 1180 ? 0.2925 0.2381 0.2685 0.0362  -0.0768 -0.1015 1178 LYS A N   
8816  C CA  . LYS A 1180 ? 0.2739 0.2116 0.2583 0.0353  -0.0806 -0.1046 1178 LYS A CA  
8817  C C   . LYS A 1180 ? 0.3111 0.2425 0.3035 0.0296  -0.0811 -0.0978 1178 LYS A C   
8818  O O   . LYS A 1180 ? 0.3356 0.2616 0.3325 0.0283  -0.0806 -0.0956 1178 LYS A O   
8819  C CB  . LYS A 1180 ? 0.2843 0.2210 0.2721 0.0373  -0.0871 -0.1138 1178 LYS A CB  
8820  C CG  . LYS A 1180 ? 0.3323 0.2764 0.3133 0.0431  -0.0857 -0.1196 1178 LYS A CG  
8821  C CD  . LYS A 1180 ? 0.3591 0.3055 0.3437 0.0446  -0.0901 -0.1253 1178 LYS A CD  
8822  C CE  . LYS A 1180 ? 0.3658 0.3206 0.3440 0.0503  -0.0883 -0.1305 1178 LYS A CE  
8823  N NZ  . LYS A 1180 ? 0.3891 0.3475 0.3694 0.0518  -0.0923 -0.1360 1178 LYS A NZ  
8824  N N   . ALA A 1181 ? 0.2834 0.2162 0.2777 0.0260  -0.0821 -0.0943 1179 ALA A N   
8825  C CA  . ALA A 1181 ? 0.2831 0.2115 0.2846 0.0205  -0.0822 -0.0873 1179 ALA A CA  
8826  C C   . ALA A 1181 ? 0.3136 0.2425 0.3122 0.0194  -0.0762 -0.0801 1179 ALA A C   
8827  O O   . ALA A 1181 ? 0.3134 0.2376 0.3180 0.0161  -0.0761 -0.0758 1179 ALA A O   
8828  C CB  . ALA A 1181 ? 0.2824 0.2138 0.2853 0.0173  -0.0836 -0.0848 1179 ALA A CB  
8829  N N   . ILE A 1182 ? 0.2844 0.2192 0.2741 0.0221  -0.0712 -0.0787 1180 ILE A N   
8830  C CA  . ILE A 1182 ? 0.2475 0.1827 0.2345 0.0213  -0.0657 -0.0722 1180 ILE A CA  
8831  C C   . ILE A 1182 ? 0.2841 0.2154 0.2722 0.0231  -0.0649 -0.0737 1180 ILE A C   
8832  O O   . ILE A 1182 ? 0.2750 0.2030 0.2662 0.0206  -0.0630 -0.0688 1180 ILE A O   
8833  C CB  . ILE A 1182 ? 0.2787 0.2211 0.2568 0.0235  -0.0611 -0.0701 1180 ILE A CB  
8834  C CG1 . ILE A 1182 ? 0.2649 0.2106 0.2432 0.0210  -0.0614 -0.0670 1180 ILE A CG1 
8835  C CG2 . ILE A 1182 ? 0.2931 0.2358 0.2679 0.0237  -0.0556 -0.0650 1180 ILE A CG2 
8836  C CD1 . ILE A 1182 ? 0.2902 0.2428 0.2602 0.0233  -0.0577 -0.0652 1180 ILE A CD1 
8837  N N   . ALA A 1183 ? 0.2976 0.2293 0.2832 0.0274  -0.0665 -0.0806 1181 ALA A N   
8838  C CA  . ALA A 1183 ? 0.2834 0.2116 0.2705 0.0294  -0.0661 -0.0826 1181 ALA A CA  
8839  C C   . ALA A 1183 ? 0.3044 0.2245 0.3017 0.0261  -0.0700 -0.0818 1181 ALA A C   
8840  O O   . ALA A 1183 ? 0.3339 0.2505 0.3336 0.0260  -0.0687 -0.0799 1181 ALA A O   
8841  C CB  . ALA A 1183 ? 0.3066 0.2376 0.2899 0.0349  -0.0676 -0.0910 1181 ALA A CB  
8842  N N   . ALA A 1184 ? 0.2986 0.2161 0.3022 0.0232  -0.0748 -0.0827 1182 ALA A N   
8843  C CA  . ALA A 1184 ? 0.3034 0.2135 0.3174 0.0196  -0.0790 -0.0814 1182 ALA A CA  
8844  C C   . ALA A 1184 ? 0.3439 0.2529 0.3611 0.0146  -0.0763 -0.0722 1182 ALA A C   
8845  O O   . ALA A 1184 ? 0.3424 0.2458 0.3680 0.0114  -0.0792 -0.0698 1182 ALA A O   
8846  C CB  . ALA A 1184 ? 0.3040 0.2119 0.3242 0.0181  -0.0854 -0.0856 1182 ALA A CB  
8847  N N   . LEU A 1185 ? 0.2734 0.1878 0.2844 0.0139  -0.0713 -0.0672 1183 LEU A N   
8848  C CA  . LEU A 1185 ? 0.2953 0.2096 0.3089 0.0095  -0.0686 -0.0590 1183 LEU A CA  
8849  C C   . LEU A 1185 ? 0.2910 0.2022 0.3055 0.0099  -0.0663 -0.0566 1183 LEU A C   
8850  O O   . LEU A 1185 ? 0.3159 0.2283 0.3246 0.0138  -0.0635 -0.0590 1183 LEU A O   
8851  C CB  . LEU A 1185 ? 0.2621 0.1829 0.2688 0.0092  -0.0639 -0.0550 1183 LEU A CB  
8852  C CG  . LEU A 1185 ? 0.3170 0.2417 0.3227 0.0087  -0.0658 -0.0567 1183 LEU A CG  
8853  C CD1 . LEU A 1185 ? 0.2984 0.2293 0.2976 0.0089  -0.0609 -0.0526 1183 LEU A CD1 
8854  C CD2 . LEU A 1185 ? 0.2944 0.2165 0.3090 0.0041  -0.0702 -0.0548 1183 LEU A CD2 
8855  N N   . PRO A 1186 ? 0.3362 0.2438 0.3577 0.0058  -0.0674 -0.0515 1184 PRO A N   
8856  C CA  . PRO A 1186 ? 0.3025 0.2075 0.3249 0.0059  -0.0652 -0.0487 1184 PRO A CA  
8857  C C   . PRO A 1186 ? 0.2732 0.1832 0.2882 0.0065  -0.0588 -0.0444 1184 PRO A C   
8858  O O   . PRO A 1186 ? 0.3125 0.2273 0.3241 0.0051  -0.0564 -0.0415 1184 PRO A O   
8859  C CB  . PRO A 1186 ? 0.3748 0.2762 0.4066 0.0007  -0.0681 -0.0433 1184 PRO A CB  
8860  C CG  . PRO A 1186 ? 0.4025 0.3077 0.4352 -0.0027 -0.0685 -0.0404 1184 PRO A CG  
8861  C CD  . PRO A 1186 ? 0.3483 0.2557 0.3767 0.0006  -0.0699 -0.0470 1184 PRO A CD  
8862  N N   . GLY A 1187 ? 0.2799 0.1887 0.2928 0.0087  -0.0563 -0.0443 1185 GLY A N   
8863  C CA  . GLY A 1187 ? 0.3275 0.2403 0.3347 0.0089  -0.0506 -0.0400 1185 GLY A CA  
8864  C C   . GLY A 1187 ? 0.3142 0.2307 0.3129 0.0135  -0.0473 -0.0434 1185 GLY A C   
8865  O O   . GLY A 1187 ? 0.3068 0.2222 0.3041 0.0172  -0.0484 -0.0488 1185 GLY A O   
8866  N N   . PRO A 1188 ? 0.2518 0.1733 0.2450 0.0133  -0.0431 -0.0402 1186 PRO A N   
8867  C CA  . PRO A 1188 ? 0.2592 0.1846 0.2447 0.0172  -0.0394 -0.0419 1186 PRO A CA  
8868  C C   . PRO A 1188 ? 0.2476 0.1755 0.2293 0.0205  -0.0411 -0.0475 1186 PRO A C   
8869  O O   . PRO A 1188 ? 0.2855 0.2135 0.2693 0.0193  -0.0443 -0.0492 1186 PRO A O   
8870  C CB  . PRO A 1188 ? 0.2971 0.2266 0.2793 0.0155  -0.0353 -0.0364 1186 PRO A CB  
8871  C CG  . PRO A 1188 ? 0.3043 0.2336 0.2910 0.0116  -0.0374 -0.0338 1186 PRO A CG  
8872  C CD  . PRO A 1188 ? 0.2756 0.1996 0.2697 0.0095  -0.0416 -0.0346 1186 PRO A CD  
8873  N N   . LEU A 1189 ? 0.2541 0.1848 0.2303 0.0245  -0.0390 -0.0502 1187 LEU A N   
8874  C CA  . LEU A 1189 ? 0.2308 0.1658 0.2020 0.0279  -0.0397 -0.0550 1187 LEU A CA  
8875  C C   . LEU A 1189 ? 0.3064 0.2464 0.2728 0.0272  -0.0370 -0.0514 1187 LEU A C   
8876  O O   . LEU A 1189 ? 0.4308 0.3729 0.3943 0.0269  -0.0329 -0.0469 1187 LEU A O   
8877  C CB  . LEU A 1189 ? 0.2526 0.1899 0.2195 0.0324  -0.0380 -0.0585 1187 LEU A CB  
8878  C CG  . LEU A 1189 ? 0.3378 0.2716 0.3085 0.0347  -0.0414 -0.0645 1187 LEU A CG  
8879  C CD1 . LEU A 1189 ? 0.3355 0.2634 0.3120 0.0326  -0.0415 -0.0618 1187 LEU A CD1 
8880  C CD2 . LEU A 1189 ? 0.3712 0.3100 0.3361 0.0397  -0.0398 -0.0691 1187 LEU A CD2 
8881  N N   . LEU A 1190 ? 0.2612 0.2031 0.2273 0.0269  -0.0396 -0.0534 1188 LEU A N   
8882  C CA  . LEU A 1190 ? 0.2554 0.2017 0.2180 0.0261  -0.0376 -0.0499 1188 LEU A CA  
8883  C C   . LEU A 1190 ? 0.2391 0.1914 0.1944 0.0299  -0.0359 -0.0519 1188 LEU A C   
8884  O O   . LEU A 1190 ? 0.3028 0.2567 0.2562 0.0329  -0.0382 -0.0575 1188 LEU A O   
8885  C CB  . LEU A 1190 ? 0.2919 0.2376 0.2582 0.0234  -0.0411 -0.0503 1188 LEU A CB  
8886  C CG  . LEU A 1190 ? 0.3143 0.2552 0.2883 0.0191  -0.0430 -0.0477 1188 LEU A CG  
8887  C CD1 . LEU A 1190 ? 0.3281 0.2702 0.3051 0.0165  -0.0457 -0.0471 1188 LEU A CD1 
8888  C CD2 . LEU A 1190 ? 0.3406 0.2811 0.3151 0.0171  -0.0390 -0.0417 1188 LEU A CD2 
8889  N N   . LEU A 1191 ? 0.2461 0.2021 0.1975 0.0300  -0.0321 -0.0472 1189 LEU A N   
8890  C CA  . LEU A 1191 ? 0.2754 0.2378 0.2203 0.0330  -0.0306 -0.0477 1189 LEU A CA  
8891  C C   . LEU A 1191 ? 0.2800 0.2448 0.2246 0.0322  -0.0330 -0.0483 1189 LEU A C   
8892  O O   . LEU A 1191 ? 0.2723 0.2369 0.2187 0.0296  -0.0324 -0.0442 1189 LEU A O   
8893  C CB  . LEU A 1191 ? 0.2634 0.2283 0.2052 0.0331  -0.0259 -0.0422 1189 LEU A CB  
8894  C CG  . LEU A 1191 ? 0.2443 0.2158 0.1795 0.0364  -0.0237 -0.0416 1189 LEU A CG  
8895  C CD1 . LEU A 1191 ? 0.2814 0.2537 0.2156 0.0360  -0.0194 -0.0360 1189 LEU A CD1 
8896  C CD2 . LEU A 1191 ? 0.2398 0.2160 0.1722 0.0369  -0.0250 -0.0414 1189 LEU A CD2 
8897  N N   . VAL A 1192 ? 0.2520 0.2194 0.1945 0.0346  -0.0360 -0.0537 1190 VAL A N   
8898  C CA  . VAL A 1192 ? 0.2659 0.2353 0.2088 0.0341  -0.0392 -0.0556 1190 VAL A CA  
8899  C C   . VAL A 1192 ? 0.2514 0.2284 0.1875 0.0368  -0.0378 -0.0550 1190 VAL A C   
8900  O O   . VAL A 1192 ? 0.2914 0.2724 0.2226 0.0402  -0.0367 -0.0571 1190 VAL A O   
8901  C CB  . VAL A 1192 ? 0.2747 0.2416 0.2207 0.0347  -0.0441 -0.0624 1190 VAL A CB  
8902  C CG1 . VAL A 1192 ? 0.3057 0.2752 0.2519 0.0342  -0.0475 -0.0645 1190 VAL A CG1 
8903  C CG2 . VAL A 1192 ? 0.3220 0.2814 0.2754 0.0317  -0.0457 -0.0623 1190 VAL A CG2 
8904  N N   . GLN A 1193 ? 0.2501 0.2294 0.1861 0.0355  -0.0381 -0.0520 1191 GLN A N   
8905  C CA  . GLN A 1193 ? 0.2079 0.1944 0.1381 0.0379  -0.0378 -0.0516 1191 GLN A CA  
8906  C C   . GLN A 1193 ? 0.2151 0.2030 0.1466 0.0374  -0.0420 -0.0549 1191 GLN A C   
8907  O O   . GLN A 1193 ? 0.2468 0.2314 0.1835 0.0342  -0.0436 -0.0535 1191 GLN A O   
8908  C CB  . GLN A 1193 ? 0.2259 0.2145 0.1546 0.0371  -0.0342 -0.0447 1191 GLN A CB  
8909  C CG  . GLN A 1193 ? 0.2229 0.2104 0.1506 0.0374  -0.0301 -0.0410 1191 GLN A CG  
8910  C CD  . GLN A 1193 ? 0.2209 0.2113 0.1469 0.0371  -0.0272 -0.0348 1191 GLN A CD  
8911  O OE1 . GLN A 1193 ? 0.2593 0.2557 0.1805 0.0394  -0.0265 -0.0336 1191 GLN A OE1 
8912  N NE2 . GLN A 1193 ? 0.2371 0.2236 0.1672 0.0344  -0.0257 -0.0309 1191 GLN A NE2 
8913  N N   . ALA A 1194 ? 0.2191 0.2126 0.1458 0.0405  -0.0438 -0.0590 1192 ALA A N   
8914  C CA  . ALA A 1194 ? 0.2187 0.2142 0.1463 0.0404  -0.0481 -0.0627 1192 ALA A CA  
8915  C C   . ALA A 1194 ? 0.2391 0.2428 0.1607 0.0425  -0.0476 -0.0610 1192 ALA A C   
8916  O O   . ALA A 1194 ? 0.2497 0.2585 0.1657 0.0450  -0.0447 -0.0590 1192 ALA A O   
8917  C CB  . ALA A 1194 ? 0.2481 0.2426 0.1764 0.0422  -0.0520 -0.0708 1192 ALA A CB  
8918  N N   . ALA A 1195 ? 0.2218 0.2272 0.1449 0.0414  -0.0507 -0.0617 1193 ALA A N   
8919  C CA  . ALA A 1195 ? 0.2504 0.2637 0.1684 0.0434  -0.0510 -0.0604 1193 ALA A CA  
8920  C C   . ALA A 1195 ? 0.2358 0.2501 0.1562 0.0426  -0.0559 -0.0644 1193 ALA A C   
8921  O O   . ALA A 1195 ? 0.2660 0.2746 0.1928 0.0396  -0.0580 -0.0654 1193 ALA A O   
8922  C CB  . ALA A 1195 ? 0.2563 0.2708 0.1740 0.0422  -0.0476 -0.0524 1193 ALA A CB  
8923  N N   . SER A 1196 ? 0.2440 0.2659 0.1592 0.0453  -0.0576 -0.0666 1194 SER A N   
8924  C CA  . SER A 1196 ? 0.2526 0.2767 0.1694 0.0447  -0.0621 -0.0696 1194 SER A CA  
8925  C C   . SER A 1196 ? 0.2463 0.2715 0.1650 0.0426  -0.0613 -0.0633 1194 SER A C   
8926  O O   . SER A 1196 ? 0.2359 0.2618 0.1533 0.0425  -0.0574 -0.0569 1194 SER A O   
8927  C CB  . SER A 1196 ? 0.2940 0.3267 0.2042 0.0485  -0.0642 -0.0743 1194 SER A CB  
8928  O OG  . SER A 1196 ? 0.2668 0.3067 0.1709 0.0505  -0.0611 -0.0688 1194 SER A OG  
8929  N N   . SER A 1197 ? 0.2384 0.2640 0.1607 0.0410  -0.0651 -0.0653 1195 SER A N   
8930  C CA  . SER A 1197 ? 0.2713 0.2989 0.1955 0.0395  -0.0647 -0.0598 1195 SER A CA  
8931  C C   . SER A 1197 ? 0.2720 0.3074 0.1895 0.0423  -0.0630 -0.0561 1195 SER A C   
8932  O O   . SER A 1197 ? 0.2463 0.2823 0.1644 0.0417  -0.0604 -0.0496 1195 SER A O   
8933  C CB  . SER A 1197 ? 0.2696 0.2975 0.1985 0.0377  -0.0694 -0.0631 1195 SER A CB  
8934  O OG  . SER A 1197 ? 0.2911 0.3118 0.2266 0.0348  -0.0711 -0.0659 1195 SER A OG  
8935  N N   . GLY A 1198 ? 0.2818 0.3237 0.1932 0.0456  -0.0646 -0.0600 1196 GLY A N   
8936  C CA  . GLY A 1198 ? 0.2571 0.3072 0.1620 0.0483  -0.0631 -0.0561 1196 GLY A CA  
8937  C C   . GLY A 1198 ? 0.2681 0.3177 0.1704 0.0490  -0.0581 -0.0504 1196 GLY A C   
8938  O O   . GLY A 1198 ? 0.2708 0.3239 0.1714 0.0494  -0.0561 -0.0439 1196 GLY A O   
8939  N N   . GLU A 1199 ? 0.2488 0.2940 0.1513 0.0491  -0.0562 -0.0526 1197 GLU A N   
8940  C CA  . GLU A 1199 ? 0.2645 0.3089 0.1652 0.0495  -0.0515 -0.0473 1197 GLU A CA  
8941  C C   . GLU A 1199 ? 0.2864 0.3253 0.1924 0.0466  -0.0492 -0.0410 1197 GLU A C   
8942  O O   . GLU A 1199 ? 0.2595 0.3002 0.1640 0.0470  -0.0462 -0.0347 1197 GLU A O   
8943  C CB  . GLU A 1199 ? 0.3000 0.3404 0.2007 0.0500  -0.0503 -0.0515 1197 GLU A CB  
8944  C CG  . GLU A 1199 ? 0.2992 0.3397 0.1974 0.0508  -0.0456 -0.0468 1197 GLU A CG  
8945  C CD  . GLU A 1199 ? 0.3906 0.4275 0.2890 0.0515  -0.0448 -0.0514 1197 GLU A CD  
8946  O OE1 . GLU A 1199 ? 0.4144 0.4485 0.3148 0.0515  -0.0480 -0.0583 1197 GLU A OE1 
8947  O OE2 . GLU A 1199 ? 0.4609 0.4976 0.3577 0.0521  -0.0410 -0.0482 1197 GLU A OE2 
8948  N N   . ILE A 1200 ? 0.2372 0.2699 0.1496 0.0437  -0.0508 -0.0424 1198 ILE A N   
8949  C CA  . ILE A 1200 ? 0.2475 0.2761 0.1650 0.0411  -0.0488 -0.0369 1198 ILE A CA  
8950  C C   . ILE A 1200 ? 0.2462 0.2800 0.1629 0.0418  -0.0492 -0.0323 1198 ILE A C   
8951  O O   . ILE A 1200 ? 0.2382 0.2711 0.1564 0.0414  -0.0466 -0.0265 1198 ILE A O   
8952  C CB  . ILE A 1200 ? 0.2366 0.2590 0.1612 0.0379  -0.0507 -0.0395 1198 ILE A CB  
8953  C CG1 . ILE A 1200 ? 0.2354 0.2518 0.1615 0.0370  -0.0498 -0.0426 1198 ILE A CG1 
8954  C CG2 . ILE A 1200 ? 0.2315 0.2515 0.1613 0.0355  -0.0491 -0.0343 1198 ILE A CG2 
8955  C CD1 . ILE A 1200 ? 0.2270 0.2380 0.1599 0.0338  -0.0523 -0.0455 1198 ILE A CD1 
8956  N N   . ALA A 1201 ? 0.2391 0.2784 0.1537 0.0430  -0.0527 -0.0349 1199 ALA A N   
8957  C CA  . ALA A 1201 ? 0.2696 0.3142 0.1835 0.0438  -0.0534 -0.0304 1199 ALA A CA  
8958  C C   . ALA A 1201 ? 0.2752 0.3252 0.1835 0.0463  -0.0510 -0.0255 1199 ALA A C   
8959  O O   . ALA A 1201 ? 0.2606 0.3121 0.1701 0.0464  -0.0499 -0.0195 1199 ALA A O   
8960  C CB  . ALA A 1201 ? 0.2772 0.3268 0.1902 0.0444  -0.0579 -0.0345 1199 ALA A CB  
8961  N N   . ARG A 1202 ? 0.2587 0.3120 0.1614 0.0484  -0.0503 -0.0280 1200 ARG A N   
8962  C CA  . ARG A 1202 ? 0.2761 0.3362 0.1730 0.0508  -0.0483 -0.0234 1200 ARG A CA  
8963  C C   . ARG A 1202 ? 0.2844 0.3408 0.1822 0.0503  -0.0440 -0.0184 1200 ARG A C   
8964  O O   . ARG A 1202 ? 0.3167 0.3769 0.2128 0.0512  -0.0423 -0.0120 1200 ARG A O   
8965  C CB  . ARG A 1202 ? 0.2821 0.3490 0.1722 0.0536  -0.0494 -0.0285 1200 ARG A CB  
8966  C CG  . ARG A 1202 ? 0.2440 0.3172 0.1316 0.0549  -0.0538 -0.0328 1200 ARG A CG  
8967  C CD  . ARG A 1202 ? 0.2883 0.3694 0.1686 0.0581  -0.0546 -0.0376 1200 ARG A CD  
8968  N NE  . ARG A 1202 ? 0.3358 0.4119 0.2168 0.0581  -0.0540 -0.0438 1200 ARG A NE  
8969  C CZ  . ARG A 1202 ? 0.3180 0.3913 0.2007 0.0580  -0.0573 -0.0518 1200 ARG A CZ  
8970  N NH1 . ARG A 1202 ? 0.3064 0.3825 0.1898 0.0579  -0.0616 -0.0553 1200 ARG A NH1 
8971  N NH2 . ARG A 1202 ? 0.3354 0.4031 0.2198 0.0578  -0.0566 -0.0564 1200 ARG A NH2 
8972  N N   . ASN A 1203 ? 0.2599 0.3092 0.1605 0.0488  -0.0423 -0.0209 1201 ASN A N   
8973  C CA  . ASN A 1203 ? 0.2837 0.3301 0.1845 0.0486  -0.0384 -0.0171 1201 ASN A CA  
8974  C C   . ASN A 1203 ? 0.2874 0.3251 0.1950 0.0457  -0.0369 -0.0152 1201 ASN A C   
8975  O O   . ASN A 1203 ? 0.2596 0.2916 0.1703 0.0441  -0.0374 -0.0196 1201 ASN A O   
8976  C CB  . ASN A 1203 ? 0.3013 0.3482 0.1983 0.0500  -0.0374 -0.0218 1201 ASN A CB  
8977  C CG  . ASN A 1203 ? 0.2978 0.3423 0.1949 0.0498  -0.0333 -0.0180 1201 ASN A CG  
8978  O OD1 . ASN A 1203 ? 0.3139 0.3566 0.2136 0.0487  -0.0313 -0.0117 1201 ASN A OD1 
8979  N ND2 . ASN A 1203 ? 0.3153 0.3601 0.2097 0.0510  -0.0323 -0.0219 1201 ASN A ND2 
8980  N N   . PRO A 1204 ? 0.2746 0.3112 0.1849 0.0451  -0.0351 -0.0089 1202 PRO A N   
8981  C CA  . PRO A 1204 ? 0.3107 0.3398 0.2273 0.0426  -0.0336 -0.0074 1202 PRO A CA  
8982  C C   . PRO A 1204 ? 0.2858 0.3098 0.2030 0.0417  -0.0311 -0.0091 1202 PRO A C   
8983  O O   . PRO A 1204 ? 0.2976 0.3154 0.2196 0.0395  -0.0305 -0.0100 1202 PRO A O   
8984  C CB  . PRO A 1204 ? 0.3196 0.3497 0.2380 0.0428  -0.0322 -0.0004 1202 PRO A CB  
8985  C CG  . PRO A 1204 ? 0.3564 0.3944 0.2707 0.0449  -0.0341 0.0017  1202 PRO A CG  
8986  C CD  . PRO A 1204 ? 0.3001 0.3427 0.2081 0.0466  -0.0348 -0.0028 1202 PRO A CD  
8987  N N   . ASP A 1205 ? 0.2922 0.3190 0.2046 0.0434  -0.0296 -0.0096 1203 ASP A N   
8988  C CA  . ASP A 1205 ? 0.2871 0.3096 0.1998 0.0429  -0.0273 -0.0112 1203 ASP A CA  
8989  C C   . ASP A 1205 ? 0.3216 0.3434 0.2326 0.0434  -0.0290 -0.0183 1203 ASP A C   
8990  O O   . ASP A 1205 ? 0.3100 0.3303 0.2197 0.0439  -0.0274 -0.0201 1203 ASP A O   
8991  C CB  . ASP A 1205 ? 0.3140 0.3400 0.2231 0.0444  -0.0244 -0.0069 1203 ASP A CB  
8992  C CG  . ASP A 1205 ? 0.3952 0.4210 0.3070 0.0438  -0.0228 0.0002  1203 ASP A CG  
8993  O OD1 . ASP A 1205 ? 0.3800 0.4009 0.2970 0.0419  -0.0232 0.0014  1203 ASP A OD1 
8994  O OD2 . ASP A 1205 ? 0.4998 0.5305 0.4086 0.0452  -0.0214 0.0047  1203 ASP A OD2 
8995  N N   . ALA A 1206 ? 0.2526 0.2753 0.1640 0.0433  -0.0325 -0.0224 1204 ALA A N   
8996  C CA  . ALA A 1206 ? 0.2300 0.2517 0.1408 0.0437  -0.0348 -0.0294 1204 ALA A CA  
8997  C C   . ALA A 1206 ? 0.2475 0.2618 0.1621 0.0419  -0.0335 -0.0312 1204 ALA A C   
8998  O O   . ALA A 1206 ? 0.3018 0.3154 0.2147 0.0431  -0.0337 -0.0355 1204 ALA A O   
8999  C CB  . ALA A 1206 ? 0.2795 0.3017 0.1924 0.0428  -0.0388 -0.0329 1204 ALA A CB  
9000  N N   . TYR A 1207 ? 0.2495 0.2585 0.1694 0.0392  -0.0324 -0.0282 1205 TYR A N   
9001  C CA  . TYR A 1207 ? 0.2226 0.2251 0.1461 0.0373  -0.0308 -0.0285 1205 TYR A CA  
9002  C C   . TYR A 1207 ? 0.2560 0.2579 0.1791 0.0373  -0.0269 -0.0231 1205 TYR A C   
9003  O O   . TYR A 1207 ? 0.3174 0.3196 0.2424 0.0365  -0.0259 -0.0186 1205 TYR A O   
9004  C CB  . TYR A 1207 ? 0.2229 0.2205 0.1526 0.0341  -0.0323 -0.0290 1205 TYR A CB  
9005  C CG  . TYR A 1207 ? 0.2271 0.2248 0.1582 0.0337  -0.0365 -0.0342 1205 TYR A CG  
9006  C CD1 . TYR A 1207 ? 0.2266 0.2227 0.1570 0.0345  -0.0383 -0.0396 1205 TYR A CD1 
9007  C CD2 . TYR A 1207 ? 0.2087 0.2080 0.1424 0.0324  -0.0387 -0.0338 1205 TYR A CD2 
9008  C CE1 . TYR A 1207 ? 0.2366 0.2325 0.1691 0.0340  -0.0425 -0.0445 1205 TYR A CE1 
9009  C CE2 . TYR A 1207 ? 0.2180 0.2174 0.1535 0.0318  -0.0427 -0.0384 1205 TYR A CE2 
9010  C CZ  . TYR A 1207 ? 0.2253 0.2228 0.1603 0.0325  -0.0447 -0.0438 1205 TYR A CZ  
9011  O OH  . TYR A 1207 ? 0.2427 0.2399 0.1801 0.0318  -0.0490 -0.0485 1205 TYR A OH  
9012  N N   . CYS A 1208 ? 0.2361 0.2376 0.1571 0.0384  -0.0248 -0.0236 1206 CYS A N   
9013  C CA  . CYS A 1208 ? 0.2519 0.2536 0.1723 0.0387  -0.0213 -0.0184 1206 CYS A CA  
9014  C C   . CYS A 1208 ? 0.2402 0.2354 0.1658 0.0360  -0.0197 -0.0166 1206 CYS A C   
9015  O O   . CYS A 1208 ? 0.2181 0.2089 0.1460 0.0348  -0.0201 -0.0196 1206 CYS A O   
9016  C CB  . CYS A 1208 ? 0.2499 0.2547 0.1658 0.0410  -0.0197 -0.0195 1206 CYS A CB  
9017  S SG  . CYS A 1208 ? 0.3038 0.3095 0.2192 0.0412  -0.0155 -0.0130 1206 CYS A SG  
9018  N N   . LEU A 1209 ? 0.1973 0.1921 0.1250 0.0351  -0.0181 -0.0117 1207 LEU A N   
9019  C CA  . LEU A 1209 ? 0.2059 0.1954 0.1385 0.0327  -0.0167 -0.0101 1207 LEU A CA  
9020  C C   . LEU A 1209 ? 0.2104 0.1974 0.1428 0.0327  -0.0140 -0.0095 1207 LEU A C   
9021  O O   . LEU A 1209 ? 0.2026 0.1853 0.1387 0.0307  -0.0131 -0.0092 1207 LEU A O   
9022  C CB  . LEU A 1209 ? 0.2007 0.1907 0.1358 0.0322  -0.0160 -0.0057 1207 LEU A CB  
9023  C CG  . LEU A 1209 ? 0.2146 0.2072 0.1505 0.0322  -0.0185 -0.0060 1207 LEU A CG  
9024  C CD1 . LEU A 1209 ? 0.2583 0.2507 0.1978 0.0317  -0.0178 -0.0019 1207 LEU A CD1 
9025  C CD2 . LEU A 1209 ? 0.2313 0.2219 0.1699 0.0304  -0.0208 -0.0100 1207 LEU A CD2 
9026  N N   . ASN A 1210 ? 0.2346 0.2249 0.1627 0.0348  -0.0128 -0.0091 1208 ASN A N   
9027  C CA  . ASN A 1210 ? 0.2461 0.2344 0.1742 0.0349  -0.0104 -0.0087 1208 ASN A CA  
9028  C C   . ASN A 1210 ? 0.2213 0.2049 0.1516 0.0337  -0.0113 -0.0130 1208 ASN A C   
9029  O O   . ASN A 1210 ? 0.2411 0.2212 0.1737 0.0326  -0.0096 -0.0122 1208 ASN A O   
9030  C CB  . ASN A 1210 ? 0.2435 0.2371 0.1665 0.0376  -0.0093 -0.0086 1208 ASN A CB  
9031  C CG  . ASN A 1210 ? 0.2604 0.2590 0.1816 0.0386  -0.0080 -0.0032 1208 ASN A CG  
9032  O OD1 . ASN A 1210 ? 0.3239 0.3220 0.2472 0.0376  -0.0085 -0.0001 1208 ASN A OD1 
9033  N ND2 . ASN A 1210 ? 0.3358 0.3397 0.2529 0.0407  -0.0066 -0.0021 1208 ASN A ND2 
9034  N N   . TRP A 1211 ? 0.2085 0.1922 0.1385 0.0339  -0.0142 -0.0174 1209 TRP A N   
9035  C CA  . TRP A 1211 ? 0.1962 0.1757 0.1284 0.0331  -0.0155 -0.0215 1209 TRP A CA  
9036  C C   . TRP A 1211 ? 0.2120 0.1872 0.1494 0.0300  -0.0170 -0.0217 1209 TRP A C   
9037  O O   . TRP A 1211 ? 0.2371 0.2088 0.1772 0.0290  -0.0187 -0.0248 1209 TRP A O   
9038  C CB  . TRP A 1211 ? 0.2102 0.1922 0.1394 0.0354  -0.0180 -0.0269 1209 TRP A CB  
9039  C CG  . TRP A 1211 ? 0.2314 0.2199 0.1550 0.0385  -0.0167 -0.0264 1209 TRP A CG  
9040  C CD1 . TRP A 1211 ? 0.2235 0.2177 0.1431 0.0406  -0.0184 -0.0280 1209 TRP A CD1 
9041  C CD2 . TRP A 1211 ? 0.2330 0.2236 0.1542 0.0399  -0.0135 -0.0238 1209 TRP A CD2 
9042  N NE1 . TRP A 1211 ? 0.2454 0.2457 0.1603 0.0431  -0.0163 -0.0264 1209 TRP A NE1 
9043  C CE2 . TRP A 1211 ? 0.2342 0.2324 0.1502 0.0427  -0.0133 -0.0237 1209 TRP A CE2 
9044  C CE3 . TRP A 1211 ? 0.2262 0.2137 0.1495 0.0390  -0.0109 -0.0214 1209 TRP A CE3 
9045  C CZ2 . TRP A 1211 ? 0.2614 0.2642 0.1742 0.0445  -0.0105 -0.0211 1209 TRP A CZ2 
9046  C CZ3 . TRP A 1211 ? 0.2631 0.2547 0.1834 0.0407  -0.0081 -0.0191 1209 TRP A CZ3 
9047  C CH2 . TRP A 1211 ? 0.2400 0.2392 0.1552 0.0434  -0.0079 -0.0188 1209 TRP A CH2 
9048  N N   . LEU A 1212 ? 0.1936 0.1693 0.1329 0.0286  -0.0165 -0.0184 1210 LEU A N   
9049  C CA  . LEU A 1212 ? 0.1969 0.1698 0.1411 0.0258  -0.0175 -0.0180 1210 LEU A CA  
9050  C C   . LEU A 1212 ? 0.2010 0.1716 0.1480 0.0241  -0.0149 -0.0145 1210 LEU A C   
9051  O O   . LEU A 1212 ? 0.1947 0.1641 0.1458 0.0217  -0.0154 -0.0138 1210 LEU A O   
9052  C CB  . LEU A 1212 ? 0.1962 0.1721 0.1409 0.0256  -0.0193 -0.0176 1210 LEU A CB  
9053  C CG  . LEU A 1212 ? 0.1809 0.1581 0.1243 0.0263  -0.0227 -0.0218 1210 LEU A CG  
9054  C CD1 . LEU A 1212 ? 0.2086 0.1901 0.1509 0.0270  -0.0241 -0.0209 1210 LEU A CD1 
9055  C CD2 . LEU A 1212 ? 0.2205 0.1942 0.1686 0.0237  -0.0250 -0.0242 1210 LEU A CD2 
9056  N N   . VAL A 1213 ? 0.2004 0.1711 0.1457 0.0252  -0.0123 -0.0124 1211 VAL A N   
9057  C CA  . VAL A 1213 ? 0.2055 0.1739 0.1534 0.0237  -0.0100 -0.0097 1211 VAL A CA  
9058  C C   . VAL A 1213 ? 0.1831 0.1489 0.1306 0.0239  -0.0090 -0.0109 1211 VAL A C   
9059  O O   . VAL A 1213 ? 0.2199 0.1863 0.1647 0.0256  -0.0096 -0.0133 1211 VAL A O   
9060  C CB  . VAL A 1213 ? 0.1903 0.1605 0.1376 0.0247  -0.0078 -0.0059 1211 VAL A CB  
9061  C CG1 . VAL A 1213 ? 0.2197 0.1919 0.1684 0.0244  -0.0089 -0.0046 1211 VAL A CG1 
9062  C CG2 . VAL A 1213 ? 0.1982 0.1710 0.1411 0.0272  -0.0068 -0.0051 1211 VAL A CG2 
9063  N N   . GLU A 1214 ? 0.1928 0.1562 0.1433 0.0222  -0.0074 -0.0092 1212 GLU A N   
9064  C CA  . GLU A 1214 ? 0.2140 0.1748 0.1649 0.0219  -0.0065 -0.0098 1212 GLU A CA  
9065  C C   . GLU A 1214 ? 0.1963 0.1573 0.1468 0.0224  -0.0036 -0.0067 1212 GLU A C   
9066  O O   . GLU A 1214 ? 0.1962 0.1574 0.1487 0.0213  -0.0026 -0.0043 1212 GLU A O   
9067  C CB  . GLU A 1214 ? 0.2580 0.2158 0.2131 0.0192  -0.0076 -0.0103 1212 GLU A CB  
9068  C CG  . GLU A 1214 ? 0.2990 0.2540 0.2555 0.0186  -0.0069 -0.0105 1212 GLU A CG  
9069  C CD  . GLU A 1214 ? 0.3637 0.3165 0.3245 0.0158  -0.0085 -0.0107 1212 GLU A CD  
9070  O OE1 . GLU A 1214 ? 0.4120 0.3642 0.3739 0.0152  -0.0112 -0.0128 1212 GLU A OE1 
9071  O OE2 . GLU A 1214 ? 0.4724 0.4244 0.4354 0.0141  -0.0072 -0.0086 1212 GLU A OE2 
9072  N N   . GLU A 1215 ? 0.1973 0.1587 0.1456 0.0240  -0.0024 -0.0070 1213 GLU A N   
9073  C CA  . GLU A 1215 ? 0.1826 0.1442 0.1308 0.0243  0.0003  -0.0040 1213 GLU A CA  
9074  C C   . GLU A 1215 ? 0.1793 0.1378 0.1307 0.0225  0.0011  -0.0037 1213 GLU A C   
9075  O O   . GLU A 1215 ? 0.1822 0.1386 0.1343 0.0222  0.0001  -0.0059 1213 GLU A O   
9076  C CB  . GLU A 1215 ? 0.1862 0.1505 0.1309 0.0269  0.0014  -0.0042 1213 GLU A CB  
9077  C CG  . GLU A 1215 ? 0.1930 0.1616 0.1339 0.0289  0.0007  -0.0042 1213 GLU A CG  
9078  C CD  . GLU A 1215 ? 0.1929 0.1649 0.1301 0.0315  0.0016  -0.0054 1213 GLU A CD  
9079  O OE1 . GLU A 1215 ? 0.2231 0.1949 0.1592 0.0326  0.0000  -0.0096 1213 GLU A OE1 
9080  O OE2 . GLU A 1215 ? 0.2187 0.1936 0.1546 0.0324  0.0036  -0.0022 1213 GLU A OE2 
9081  N N   . VAL A 1216 ? 0.1645 0.1226 0.1178 0.0215  0.0028  -0.0009 1214 VAL A N   
9082  C CA  . VAL A 1216 ? 0.1685 0.1243 0.1245 0.0200  0.0038  -0.0003 1214 VAL A CA  
9083  C C   . VAL A 1216 ? 0.1848 0.1413 0.1406 0.0206  0.0061  0.0023  1214 VAL A C   
9084  O O   . VAL A 1216 ? 0.1809 0.1388 0.1370 0.0209  0.0068  0.0045  1214 VAL A O   
9085  C CB  . VAL A 1216 ? 0.1899 0.1448 0.1491 0.0175  0.0032  0.0001  1214 VAL A CB  
9086  C CG1 . VAL A 1216 ? 0.1926 0.1460 0.1543 0.0160  0.0042  0.0010  1214 VAL A CG1 
9087  C CG2 . VAL A 1216 ? 0.1894 0.1440 0.1494 0.0166  0.0008  -0.0020 1214 VAL A CG2 
9088  N N   . SER A 1217 ? 0.1683 0.1238 0.1242 0.0209  0.0070  0.0021  1215 SER A N   
9089  C CA  . SER A 1217 ? 0.1655 0.1215 0.1220 0.0211  0.0092  0.0045  1215 SER A CA  
9090  C C   . SER A 1217 ? 0.1527 0.1066 0.1125 0.0191  0.0096  0.0051  1215 SER A C   
9091  O O   . SER A 1217 ? 0.1775 0.1296 0.1383 0.0181  0.0087  0.0035  1215 SER A O   
9092  C CB  . SER A 1217 ? 0.1977 0.1550 0.1520 0.0230  0.0100  0.0039  1215 SER A CB  
9093  O OG  . SER A 1217 ? 0.2185 0.1761 0.1740 0.0229  0.0119  0.0060  1215 SER A OG  
9094  N N   . ALA A 1218 ? 0.1534 0.1076 0.1151 0.0184  0.0108  0.0073  1216 ALA A N   
9095  C CA  . ALA A 1218 ? 0.1649 0.1178 0.1295 0.0166  0.0113  0.0078  1216 ALA A CA  
9096  C C   . ALA A 1218 ? 0.1857 0.1390 0.1513 0.0170  0.0131  0.0099  1216 ALA A C   
9097  O O   . ALA A 1218 ? 0.2031 0.1575 0.1691 0.0176  0.0136  0.0118  1216 ALA A O   
9098  C CB  . ALA A 1218 ? 0.1845 0.1375 0.1515 0.0151  0.0106  0.0076  1216 ALA A CB  
9099  N N   . SER A 1219 ? 0.1599 0.1125 0.1265 0.0165  0.0137  0.0099  1217 SER A N   
9100  C CA  . SER A 1219 ? 0.1754 0.1285 0.1432 0.0167  0.0153  0.0119  1217 SER A CA  
9101  C C   . SER A 1219 ? 0.1629 0.1150 0.1338 0.0148  0.0153  0.0120  1217 SER A C   
9102  O O   . SER A 1219 ? 0.1854 0.1366 0.1567 0.0140  0.0148  0.0109  1217 SER A O   
9103  C CB  . SER A 1219 ? 0.1944 0.1482 0.1606 0.0182  0.0161  0.0117  1217 SER A CB  
9104  O OG  . SER A 1219 ? 0.1863 0.1413 0.1541 0.0182  0.0177  0.0139  1217 SER A OG  
9105  N N   . ILE A 1220 ? 0.1566 0.1091 0.1299 0.0142  0.0157  0.0133  1218 ILE A N   
9106  C CA  . ILE A 1220 ? 0.1695 0.1216 0.1457 0.0126  0.0156  0.0130  1218 ILE A CA  
9107  C C   . ILE A 1220 ? 0.1698 0.1222 0.1480 0.0125  0.0168  0.0148  1218 ILE A C   
9108  O O   . ILE A 1220 ? 0.1727 0.1254 0.1519 0.0131  0.0173  0.0166  1218 ILE A O   
9109  C CB  . ILE A 1220 ? 0.2088 0.1613 0.1868 0.0120  0.0148  0.0124  1218 ILE A CB  
9110  C CG1 . ILE A 1220 ? 0.2565 0.2094 0.2328 0.0120  0.0137  0.0108  1218 ILE A CG1 
9111  C CG2 . ILE A 1220 ? 0.2211 0.1743 0.2021 0.0106  0.0147  0.0116  1218 ILE A CG2 
9112  C CD1 . ILE A 1220 ? 0.3479 0.3015 0.3257 0.0122  0.0129  0.0104  1218 ILE A CD1 
9113  N N   . ASN A 1221 ? 0.1587 0.1110 0.1378 0.0117  0.0170  0.0145  1219 ASN A N   
9114  C CA  . ASN A 1221 ? 0.1577 0.1104 0.1392 0.0114  0.0180  0.0160  1219 ASN A CA  
9115  C C   . ASN A 1221 ? 0.1780 0.1308 0.1628 0.0102  0.0174  0.0157  1219 ASN A C   
9116  O O   . ASN A 1221 ? 0.1974 0.1508 0.1832 0.0090  0.0168  0.0143  1219 ASN A O   
9117  C CB  . ASN A 1221 ? 0.1669 0.1195 0.1482 0.0110  0.0182  0.0157  1219 ASN A CB  
9118  C CG  . ASN A 1221 ? 0.1631 0.1165 0.1472 0.0105  0.0190  0.0171  1219 ASN A CG  
9119  O OD1 . ASN A 1221 ? 0.1659 0.1197 0.1519 0.0105  0.0195  0.0185  1219 ASN A OD1 
9120  N ND2 . ASN A 1221 ? 0.1990 0.1525 0.1835 0.0100  0.0190  0.0168  1219 ASN A ND2 
9121  N N   . THR A 1222 ? 0.1633 0.1159 0.1501 0.0105  0.0175  0.0170  1220 THR A N   
9122  C CA  . THR A 1222 ? 0.1653 0.1177 0.1558 0.0097  0.0166  0.0162  1220 THR A CA  
9123  C C   . THR A 1222 ? 0.2111 0.1638 0.2048 0.0088  0.0169  0.0169  1220 THR A C   
9124  O O   . THR A 1222 ? 0.2586 0.2112 0.2558 0.0082  0.0159  0.0158  1220 THR A O   
9125  C CB  . THR A 1222 ? 0.2141 0.1658 0.2063 0.0105  0.0161  0.0174  1220 THR A CB  
9126  O OG1 . THR A 1222 ? 0.2028 0.1545 0.1955 0.0110  0.0170  0.0207  1220 THR A OG1 
9127  C CG2 . THR A 1222 ? 0.2124 0.1641 0.2015 0.0113  0.0156  0.0166  1220 THR A CG2 
9128  N N   . ALA A 1223 ? 0.1640 0.1171 0.1568 0.0089  0.0180  0.0184  1221 ALA A N   
9129  C CA  . ALA A 1223 ? 0.2030 0.1567 0.1988 0.0080  0.0182  0.0190  1221 ALA A CA  
9130  C C   . ALA A 1223 ? 0.2346 0.1892 0.2296 0.0071  0.0179  0.0172  1221 ALA A C   
9131  O O   . ALA A 1223 ? 0.2371 0.1925 0.2342 0.0064  0.0181  0.0176  1221 ALA A O   
9132  C CB  . ALA A 1223 ? 0.2218 0.1762 0.2179 0.0086  0.0195  0.0219  1221 ALA A CB  
9133  N N   . ALA A 1224 ? 0.2361 0.1909 0.2282 0.0071  0.0175  0.0156  1222 ALA A N   
9134  C CA  . ALA A 1224 ? 0.2430 0.1989 0.2342 0.0063  0.0173  0.0148  1222 ALA A CA  
9135  C C   . ALA A 1224 ? 0.2772 0.2350 0.2709 0.0049  0.0165  0.0136  1222 ALA A C   
9136  O O   . ALA A 1224 ? 0.2776 0.2367 0.2714 0.0041  0.0164  0.0138  1222 ALA A O   
9137  C CB  . ALA A 1224 ? 0.2563 0.2121 0.2447 0.0063  0.0167  0.0138  1222 ALA A CB  
9138  N N   . ALA A 1225 ? 0.2461 0.2044 0.2422 0.0048  0.0158  0.0122  1223 ALA A N   
9139  C CA  . ALA A 1225 ? 0.2720 0.2327 0.2705 0.0037  0.0150  0.0104  1223 ALA A CA  
9140  C C   . ALA A 1225 ? 0.2916 0.2521 0.2931 0.0033  0.0151  0.0114  1223 ALA A C   
9141  O O   . ALA A 1225 ? 0.3125 0.2752 0.3161 0.0025  0.0143  0.0099  1223 ALA A O   
9142  C CB  . ALA A 1225 ? 0.2637 0.2249 0.2640 0.0040  0.0140  0.0079  1223 ALA A CB  
9143  N N   . GLY A 1226 ? 0.2587 0.2173 0.2606 0.0039  0.0161  0.0140  1224 GLY A N   
9144  C CA  . GLY A 1226 ? 0.2713 0.2302 0.2762 0.0034  0.0163  0.0154  1224 GLY A CA  
9145  C C   . GLY A 1226 ? 0.2503 0.2076 0.2585 0.0037  0.0164  0.0171  1224 GLY A C   
9146  O O   . GLY A 1226 ? 0.2946 0.2523 0.3056 0.0033  0.0168  0.0188  1224 GLY A O   
9147  N N   . GLY A 1227 ? 0.2440 0.1998 0.2524 0.0043  0.0161  0.0170  1225 GLY A N   
9148  C CA  . GLY A 1227 ? 0.3023 0.2566 0.3142 0.0045  0.0159  0.0192  1225 GLY A CA  
9149  C C   . GLY A 1227 ? 0.2624 0.2153 0.2730 0.0055  0.0158  0.0196  1225 GLY A C   
9150  O O   . GLY A 1227 ? 0.2347 0.1878 0.2418 0.0060  0.0157  0.0177  1225 GLY A O   
9151  N N   . ASN A 1228 ? 0.2247 0.1765 0.2383 0.0056  0.0156  0.0224  1226 ASN A N   
9152  C CA  . ASN A 1228 ? 0.2401 0.1908 0.2529 0.0065  0.0154  0.0237  1226 ASN A CA  
9153  C C   . ASN A 1228 ? 0.2454 0.1942 0.2638 0.0063  0.0133  0.0229  1226 ASN A C   
9154  O O   . ASN A 1228 ? 0.2633 0.2112 0.2869 0.0055  0.0126  0.0251  1226 ASN A O   
9155  C CB  . ASN A 1228 ? 0.2414 0.1932 0.2533 0.0070  0.0169  0.0282  1226 ASN A CB  
9156  C CG  . ASN A 1228 ? 0.2778 0.2293 0.2883 0.0080  0.0169  0.0301  1226 ASN A CG  
9157  O OD1 . ASN A 1228 ? 0.2874 0.2370 0.3005 0.0081  0.0153  0.0295  1226 ASN A OD1 
9158  N ND2 . ASN A 1228 ? 0.2924 0.2459 0.2988 0.0090  0.0185  0.0323  1226 ASN A ND2 
9159  N N   . ALA A 1229 ? 0.2537 0.2018 0.2713 0.0069  0.0122  0.0198  1227 ALA A N   
9160  C CA  . ALA A 1229 ? 0.2643 0.2106 0.2875 0.0070  0.0100  0.0182  1227 ALA A CA  
9161  C C   . ALA A 1229 ? 0.2533 0.1977 0.2800 0.0072  0.0093  0.0224  1227 ALA A C   
9162  O O   . ALA A 1229 ? 0.2892 0.2317 0.3224 0.0067  0.0075  0.0230  1227 ALA A O   
9163  C CB  . ALA A 1229 ? 0.2872 0.2340 0.3085 0.0079  0.0091  0.0141  1227 ALA A CB  
9164  N N   . SER A 1230 ? 0.2900 0.2350 0.3125 0.0080  0.0106  0.0253  1228 SER A N   
9165  C CA  . SER A 1230 ? 0.3127 0.2567 0.3381 0.0082  0.0100  0.0298  1228 SER A CA  
9166  C C   . SER A 1230 ? 0.2985 0.2428 0.3283 0.0069  0.0102  0.0339  1228 SER A C   
9167  O O   . SER A 1230 ? 0.3000 0.2426 0.3359 0.0063  0.0085  0.0367  1228 SER A O   
9168  C CB  . SER A 1230 ? 0.3931 0.3389 0.4125 0.0092  0.0115  0.0320  1228 SER A CB  
9169  O OG  . SER A 1230 ? 0.4589 0.4041 0.4760 0.0103  0.0107  0.0289  1228 SER A OG  
9170  N N   . LEU A 1231 ? 0.2841 0.2306 0.3113 0.0063  0.0121  0.0345  1229 LEU A N   
9171  C CA  . LEU A 1231 ? 0.2813 0.2288 0.3125 0.0051  0.0125  0.0386  1229 LEU A CA  
9172  C C   . LEU A 1231 ? 0.3033 0.2488 0.3415 0.0037  0.0105  0.0369  1229 LEU A C   
9173  O O   . LEU A 1231 ? 0.3164 0.2622 0.3595 0.0024  0.0102  0.0405  1229 LEU A O   
9174  C CB  . LEU A 1231 ? 0.2966 0.2475 0.3229 0.0052  0.0151  0.0396  1229 LEU A CB  
9175  C CG  . LEU A 1231 ? 0.3171 0.2711 0.3400 0.0060  0.0170  0.0442  1229 LEU A CG  
9176  C CD1 . LEU A 1231 ? 0.3466 0.3004 0.3650 0.0075  0.0169  0.0434  1229 LEU A CD1 
9177  C CD2 . LEU A 1231 ? 0.2979 0.2554 0.3166 0.0065  0.0194  0.0443  1229 LEU A CD2 
9178  N N   . MET A 1232 ? 0.2926 0.2364 0.3316 0.0040  0.0089  0.0315  1230 MET A N   
9179  C CA  . MET A 1232 ? 0.2992 0.2412 0.3454 0.0030  0.0066  0.0294  1230 MET A CA  
9180  C C   . MET A 1232 ? 0.3343 0.2732 0.3880 0.0025  0.0041  0.0320  1230 MET A C   
9181  O O   . MET A 1232 ? 0.3346 0.2719 0.3956 0.0014  0.0020  0.0317  1230 MET A O   
9182  C CB  . MET A 1232 ? 0.2988 0.2406 0.3439 0.0036  0.0054  0.0227  1230 MET A CB  
9183  C CG  . MET A 1232 ? 0.2789 0.2236 0.3184 0.0035  0.0072  0.0202  1230 MET A CG  
9184  S SD  . MET A 1232 ? 0.3174 0.2633 0.3549 0.0043  0.0061  0.0132  1230 MET A SD  
9185  C CE  . MET A 1232 ? 0.3090 0.2540 0.3547 0.0036  0.0031  0.0096  1230 MET A CE  
9186  N N   . ALA A 1233 ? 0.3305 0.2688 0.3832 0.0034  0.0041  0.0347  1231 ALA A N   
9187  C CA  . ALA A 1233 ? 0.3314 0.2669 0.3915 0.0030  0.0016  0.0381  1231 ALA A CA  
9188  C C   . ALA A 1233 ? 0.3833 0.3204 0.4453 0.0018  0.0026  0.0458  1231 ALA A C   
9189  O O   . ALA A 1233 ? 0.3956 0.3307 0.4642 0.0012  0.0005  0.0497  1231 ALA A O   
9190  C CB  . ALA A 1233 ? 0.3543 0.2885 0.4129 0.0047  0.0007  0.0369  1231 ALA A CB  
9191  N N   . ILE A 1234 ? 0.3515 0.2925 0.4084 0.0015  0.0056  0.0481  1232 ILE A N   
9192  C CA  . ILE A 1234 ? 0.3696 0.3138 0.4271 0.0006  0.0070  0.0553  1232 ILE A CA  
9193  C C   . ILE A 1234 ? 0.3821 0.3274 0.4445 -0.0013 0.0071  0.0573  1232 ILE A C   
9194  O O   . ILE A 1234 ? 0.3407 0.2881 0.3994 -0.0013 0.0089  0.0550  1232 ILE A O   
9195  C CB  . ILE A 1234 ? 0.3335 0.2821 0.3817 0.0020  0.0103  0.0566  1232 ILE A CB  
9196  C CG1 . ILE A 1234 ? 0.3683 0.3157 0.4124 0.0037  0.0099  0.0549  1232 ILE A CG1 
9197  C CG2 . ILE A 1234 ? 0.3221 0.2751 0.3709 0.0012  0.0119  0.0638  1232 ILE A CG2 
9198  C CD1 . ILE A 1234 ? 0.3813 0.3329 0.4171 0.0051  0.0126  0.0564  1232 ILE A CD1 
9199  N N   . GLY A 1235 ? 0.3670 0.3110 0.4380 -0.0030 0.0050  0.0618  1233 GLY A N   
9200  C CA  . GLY A 1235 ? 0.3130 0.2580 0.3900 -0.0051 0.0046  0.0643  1233 GLY A CA  
9201  C C   . GLY A 1235 ? 0.3744 0.3222 0.4566 -0.0067 0.0039  0.0714  1233 GLY A C   
9202  O O   . GLY A 1235 ? 0.3092 0.2613 0.3928 -0.0081 0.0051  0.0749  1233 GLY A O   
9203  O OXT . GLY A 1235 ? 0.3986 0.3454 0.4830 -0.0065 0.0020  0.0731  1233 GLY A OXT 
9204  N N   . PRO B 17   ? 0.6277 0.5285 0.5826 0.1069  -0.0532 -0.0521 15   PRO B N   
9205  C CA  . PRO B 17   ? 0.5306 0.4190 0.4767 0.1019  -0.0545 -0.0509 15   PRO B CA  
9206  C C   . PRO B 17   ? 0.5605 0.4499 0.5062 0.0989  -0.0514 -0.0523 15   PRO B C   
9207  O O   . PRO B 17   ? 0.5545 0.4561 0.5085 0.0983  -0.0482 -0.0531 15   PRO B O   
9208  C CB  . PRO B 17   ? 0.5465 0.4373 0.4955 0.0986  -0.0560 -0.0486 15   PRO B CB  
9209  C CG  . PRO B 17   ? 0.5838 0.4829 0.5392 0.1026  -0.0572 -0.0483 15   PRO B CG  
9210  C CD  . PRO B 17   ? 0.5802 0.4896 0.5423 0.1068  -0.0543 -0.0506 15   PRO B CD  
9211  N N   . ALA B 18   ? 0.4914 0.3681 0.4274 0.0967  -0.0522 -0.0524 16   ALA B N   
9212  C CA  . ALA B 18   ? 0.5455 0.4222 0.4802 0.0936  -0.0496 -0.0538 16   ALA B CA  
9213  C C   . ALA B 18   ? 0.5014 0.3825 0.4398 0.0883  -0.0486 -0.0526 16   ALA B C   
9214  O O   . ALA B 18   ? 0.4776 0.3548 0.4145 0.0856  -0.0509 -0.0505 16   ALA B O   
9215  C CB  . ALA B 18   ? 0.5264 0.3878 0.4494 0.0916  -0.0513 -0.0539 16   ALA B CB  
9216  N N   . PRO B 19   ? 0.4377 0.3270 0.3807 0.0869  -0.0453 -0.0540 17   PRO B N   
9217  C CA  . PRO B 19   ? 0.3995 0.2962 0.3471 0.0802  -0.0436 -0.0518 17   PRO B CA  
9218  C C   . PRO B 19   ? 0.4115 0.2979 0.3514 0.0734  -0.0454 -0.0495 17   PRO B C   
9219  O O   . PRO B 19   ? 0.4010 0.2769 0.3326 0.0721  -0.0463 -0.0503 17   PRO B O   
9220  C CB  . PRO B 19   ? 0.4341 0.3396 0.3860 0.0797  -0.0396 -0.0536 17   PRO B CB  
9221  C CG  . PRO B 19   ? 0.4778 0.3855 0.4315 0.0876  -0.0388 -0.0567 17   PRO B CG  
9222  C CD  . PRO B 19   ? 0.4590 0.3547 0.4047 0.0899  -0.0421 -0.0564 17   PRO B CD  
9223  N N   . PHE B 20   ? 0.4154 0.3052 0.3580 0.0692  -0.0460 -0.0465 18   PHE B N   
9224  C CA  . PHE B 20   ? 0.3885 0.2721 0.3260 0.0620  -0.0470 -0.0438 18   PHE B CA  
9225  C C   . PHE B 20   ? 0.4283 0.2956 0.3548 0.0618  -0.0506 -0.0432 18   PHE B C   
9226  O O   . PHE B 20   ? 0.4314 0.2924 0.3526 0.0557  -0.0515 -0.0412 18   PHE B O   
9227  C CB  . PHE B 20   ? 0.3332 0.2203 0.2712 0.0570  -0.0444 -0.0439 18   PHE B CB  
9228  C CG  . PHE B 20   ? 0.3402 0.2423 0.2881 0.0567  -0.0409 -0.0443 18   PHE B CG  
9229  C CD1 . PHE B 20   ? 0.3476 0.2584 0.3017 0.0534  -0.0399 -0.0420 18   PHE B CD1 
9230  C CD2 . PHE B 20   ? 0.3047 0.2120 0.2554 0.0599  -0.0385 -0.0469 18   PHE B CD2 
9231  C CE1 . PHE B 20   ? 0.3346 0.2585 0.2975 0.0530  -0.0368 -0.0422 18   PHE B CE1 
9232  C CE2 . PHE B 20   ? 0.3233 0.2439 0.2827 0.0594  -0.0352 -0.0470 18   PHE B CE2 
9233  C CZ  . PHE B 20   ? 0.3310 0.2597 0.2965 0.0559  -0.0345 -0.0446 18   PHE B CZ  
9234  N N   . ALA B 21   ? 0.4504 0.3110 0.3736 0.0683  -0.0529 -0.0448 19   ALA B N   
9235  C CA  . ALA B 21   ? 0.4596 0.3038 0.3720 0.0686  -0.0566 -0.0442 19   ALA B CA  
9236  C C   . ALA B 21   ? 0.5163 0.3570 0.4265 0.0647  -0.0588 -0.0406 19   ALA B C   
9237  O O   . ALA B 21   ? 0.5353 0.3626 0.4361 0.0620  -0.0614 -0.0392 19   ALA B O   
9238  C CB  . ALA B 21   ? 0.4758 0.3154 0.3863 0.0769  -0.0583 -0.0465 19   ALA B CB  
9239  N N   . ASP B 22   ? 0.4466 0.2986 0.3647 0.0641  -0.0577 -0.0392 20   ASP B N   
9240  C CA  . ASP B 22   ? 0.3897 0.2394 0.3059 0.0605  -0.0594 -0.0359 20   ASP B CA  
9241  C C   . ASP B 22   ? 0.3736 0.2354 0.2970 0.0549  -0.0565 -0.0341 20   ASP B C   
9242  O O   . ASP B 22   ? 0.3884 0.2556 0.3153 0.0543  -0.0567 -0.0323 20   ASP B O   
9243  C CB  . ASP B 22   ? 0.5041 0.3535 0.4214 0.0664  -0.0618 -0.0358 20   ASP B CB  
9244  N N   . PHE B 23   ? 0.3046 0.1704 0.2296 0.0507  -0.0539 -0.0344 21   PHE B N   
9245  C CA  . PHE B 23   ? 0.2948 0.1732 0.2275 0.0465  -0.0509 -0.0332 21   PHE B CA  
9246  C C   . PHE B 23   ? 0.2894 0.1661 0.2198 0.0410  -0.0516 -0.0298 21   PHE B C   
9247  O O   . PHE B 23   ? 0.2920 0.1765 0.2276 0.0406  -0.0508 -0.0286 21   PHE B O   
9248  C CB  . PHE B 23   ? 0.2931 0.1753 0.2274 0.0432  -0.0483 -0.0342 21   PHE B CB  
9249  C CG  . PHE B 23   ? 0.2904 0.1843 0.2318 0.0388  -0.0454 -0.0327 21   PHE B CG  
9250  C CD1 . PHE B 23   ? 0.2873 0.1932 0.2375 0.0411  -0.0435 -0.0333 21   PHE B CD1 
9251  C CD2 . PHE B 23   ? 0.3103 0.2032 0.2494 0.0322  -0.0447 -0.0308 21   PHE B CD2 
9252  C CE1 . PHE B 23   ? 0.2545 0.1703 0.2107 0.0372  -0.0410 -0.0319 21   PHE B CE1 
9253  C CE2 . PHE B 23   ? 0.3311 0.2346 0.2766 0.0285  -0.0421 -0.0295 21   PHE B CE2 
9254  C CZ  . PHE B 23   ? 0.3009 0.2154 0.2547 0.0311  -0.0403 -0.0301 21   PHE B CZ  
9255  N N   . ALA B 24   ? 0.3042 0.1706 0.2265 0.0364  -0.0529 -0.0282 22   ALA B N   
9256  C CA  . ALA B 24   ? 0.3103 0.1756 0.2303 0.0307  -0.0531 -0.0248 22   ALA B CA  
9257  C C   . ALA B 24   ? 0.3112 0.1618 0.2205 0.0275  -0.0558 -0.0232 22   ALA B C   
9258  O O   . ALA B 24   ? 0.3268 0.1759 0.2336 0.0211  -0.0551 -0.0215 22   ALA B O   
9259  C CB  . ALA B 24   ? 0.3251 0.2006 0.2507 0.0253  -0.0499 -0.0239 22   ALA B CB  
9260  N N   . PRO B 25   ? 0.3373 0.1768 0.2400 0.0316  -0.0590 -0.0237 23   PRO B N   
9261  C CA  . PRO B 25   ? 0.3734 0.1978 0.2653 0.0284  -0.0617 -0.0221 23   PRO B CA  
9262  C C   . PRO B 25   ? 0.3579 0.1813 0.2472 0.0223  -0.0618 -0.0182 23   PRO B C   
9263  O O   . PRO B 25   ? 0.3495 0.1786 0.2420 0.0234  -0.0615 -0.0169 23   PRO B O   
9264  C CB  . PRO B 25   ? 0.4101 0.2246 0.2969 0.0353  -0.0650 -0.0233 23   PRO B CB  
9265  C CG  . PRO B 25   ? 0.4019 0.2273 0.2968 0.0403  -0.0643 -0.0240 23   PRO B CG  
9266  C CD  . PRO B 25   ? 0.3680 0.2086 0.2731 0.0391  -0.0604 -0.0252 23   PRO B CD  
9267  N N   . PRO B 26   ? 0.3469 0.1637 0.2303 0.0157  -0.0621 -0.0163 24   PRO B N   
9268  C CA  . PRO B 26   ? 0.3528 0.1691 0.2336 0.0096  -0.0618 -0.0125 24   PRO B CA  
9269  C C   . PRO B 26   ? 0.3760 0.1811 0.2490 0.0115  -0.0650 -0.0107 24   PRO B C   
9270  O O   . PRO B 26   ? 0.4037 0.1981 0.2710 0.0162  -0.0679 -0.0120 24   PRO B O   
9271  C CB  . PRO B 26   ? 0.3725 0.1836 0.2488 0.0025  -0.0617 -0.0113 24   PRO B CB  
9272  C CG  . PRO B 26   ? 0.4095 0.2109 0.2811 0.0056  -0.0637 -0.0141 24   PRO B CG  
9273  C CD  . PRO B 26   ? 0.3798 0.1893 0.2586 0.0133  -0.0627 -0.0175 24   PRO B CD  
9274  N N   . VAL B 27   ? 0.3567 0.1644 0.2291 0.0078  -0.0643 -0.0075 25   VAL B N   
9275  C CA  . VAL B 27   ? 0.3438 0.1413 0.2084 0.0089  -0.0672 -0.0053 25   VAL B CA  
9276  C C   . VAL B 27   ? 0.3837 0.1639 0.2368 0.0067  -0.0703 -0.0042 25   VAL B C   
9277  O O   . VAL B 27   ? 0.4078 0.1765 0.2540 0.0110  -0.0737 -0.0042 25   VAL B O   
9278  C CB  . VAL B 27   ? 0.3606 0.1640 0.2260 0.0044  -0.0655 -0.0020 25   VAL B CB  
9279  C CG1 . VAL B 27   ? 0.4019 0.1932 0.2575 0.0045  -0.0685 0.0007  25   VAL B CG1 
9280  C CG2 . VAL B 27   ? 0.3739 0.1922 0.2494 0.0076  -0.0631 -0.0033 25   VAL B CG2 
9281  N N   . ARG B 28   ? 0.3869 0.1647 0.2377 0.0001  -0.0694 -0.0034 26   ARG B N   
9282  C CA  . ARG B 28   ? 0.3857 0.1470 0.2257 -0.0028 -0.0723 -0.0024 26   ARG B CA  
9283  C C   . ARG B 28   ? 0.4170 0.1798 0.2587 -0.0065 -0.0711 -0.0041 26   ARG B C   
9284  O O   . ARG B 28   ? 0.3933 0.1700 0.2438 -0.0088 -0.0679 -0.0046 26   ARG B O   
9285  C CB  . ARG B 28   ? 0.4611 0.2155 0.2936 -0.0096 -0.0729 0.0021  26   ARG B CB  
9286  C CG  . ARG B 28   ? 0.4279 0.1930 0.2652 -0.0176 -0.0694 0.0043  26   ARG B CG  
9287  C CD  . ARG B 28   ? 0.4677 0.2285 0.2988 -0.0233 -0.0695 0.0088  26   ARG B CD  
9288  N NE  . ARG B 28   ? 0.4993 0.2656 0.3327 -0.0194 -0.0690 0.0096  26   ARG B NE  
9289  C CZ  . ARG B 28   ? 0.4993 0.2555 0.3256 -0.0158 -0.0719 0.0107  26   ARG B CZ  
9290  N NH1 . ARG B 28   ? 0.5482 0.2875 0.3640 -0.0155 -0.0756 0.0113  26   ARG B NH1 
9291  N NH2 . ARG B 28   ? 0.4721 0.2348 0.3012 -0.0123 -0.0714 0.0112  26   ARG B NH2 
9292  N N   . PRO B 29   ? 0.4340 0.1826 0.2673 -0.0071 -0.0739 -0.0049 27   PRO B N   
9293  C CA  . PRO B 29   ? 0.4578 0.2068 0.2915 -0.0119 -0.0731 -0.0060 27   PRO B CA  
9294  C C   . PRO B 29   ? 0.4157 0.1709 0.2510 -0.0213 -0.0710 -0.0026 27   PRO B C   
9295  O O   . PRO B 29   ? 0.4584 0.2083 0.2884 -0.0256 -0.0717 0.0010  27   PRO B O   
9296  C CB  . PRO B 29   ? 0.4556 0.1854 0.2775 -0.0114 -0.0770 -0.0068 27   PRO B CB  
9297  C CG  . PRO B 29   ? 0.4749 0.1968 0.2928 -0.0034 -0.0795 -0.0076 27   PRO B CG  
9298  C CD  . PRO B 29   ? 0.4831 0.2141 0.3056 -0.0034 -0.0780 -0.0049 27   PRO B CD  
9299  N N   . GLN B 30   ? 0.4287 0.1956 0.2716 -0.0242 -0.0684 -0.0036 28   GLN B N   
9300  C CA  . GLN B 30   ? 0.4279 0.2040 0.2747 -0.0322 -0.0660 -0.0007 28   GLN B CA  
9301  C C   . GLN B 30   ? 0.3998 0.1652 0.2386 -0.0401 -0.0679 0.0012  28   GLN B C   
9302  O O   . GLN B 30   ? 0.4679 0.2283 0.3044 -0.0409 -0.0692 -0.0010 28   GLN B O   
9303  C CB  . GLN B 30   ? 0.4069 0.1995 0.2648 -0.0318 -0.0627 -0.0026 28   GLN B CB  
9304  C CG  . GLN B 30   ? 0.3800 0.1831 0.2460 -0.0244 -0.0608 -0.0046 28   GLN B CG  
9305  C CD  . GLN B 30   ? 0.3935 0.2032 0.2622 -0.0248 -0.0592 -0.0020 28   GLN B CD  
9306  O OE1 . GLN B 30   ? 0.3496 0.1704 0.2240 -0.0292 -0.0564 -0.0002 28   GLN B OE1 
9307  N NE2 . GLN B 30   ? 0.3789 0.1818 0.2435 -0.0200 -0.0610 -0.0018 28   GLN B NE2 
9308  N N   . SER B 31   ? 0.4336 0.1956 0.2680 -0.0461 -0.0680 0.0052  29   SER B N   
9309  C CA  . SER B 31   ? 0.4031 0.1559 0.2304 -0.0546 -0.0697 0.0076  29   SER B CA  
9310  C C   . SER B 31   ? 0.4208 0.1855 0.2551 -0.0608 -0.0674 0.0078  29   SER B C   
9311  O O   . SER B 31   ? 0.3910 0.1714 0.2357 -0.0588 -0.0644 0.0065  29   SER B O   
9312  C CB  . SER B 31   ? 0.4377 0.1858 0.2594 -0.0595 -0.0697 0.0122  29   SER B CB  
9313  O OG  . SER B 31   ? 0.4147 0.1792 0.2451 -0.0617 -0.0658 0.0141  29   SER B OG  
9314  N N   . THR B 32   ? 0.4608 0.2176 0.2892 -0.0685 -0.0692 0.0094  30   THR B N   
9315  C CA  . THR B 32   ? 0.4109 0.1789 0.2456 -0.0754 -0.0675 0.0102  30   THR B CA  
9316  C C   . THR B 32   ? 0.3783 0.1631 0.2219 -0.0780 -0.0634 0.0129  30   THR B C   
9317  O O   . THR B 32   ? 0.3849 0.1848 0.2383 -0.0781 -0.0608 0.0119  30   THR B O   
9318  C CB  . THR B 32   ? 0.4511 0.2073 0.2773 -0.0842 -0.0702 0.0122  30   THR B CB  
9319  O OG1 . THR B 32   ? 0.5622 0.3073 0.3821 -0.0802 -0.0731 0.0093  30   THR B OG1 
9320  C CG2 . THR B 32   ? 0.4466 0.2152 0.2797 -0.0918 -0.0686 0.0134  30   THR B CG2 
9321  N N   . LEU B 33   ? 0.4018 0.1838 0.2417 -0.0798 -0.0629 0.0162  31   LEU B N   
9322  C CA  . LEU B 33   ? 0.3624 0.1597 0.2100 -0.0822 -0.0589 0.0188  31   LEU B CA  
9323  C C   . LEU B 33   ? 0.3671 0.1767 0.2236 -0.0742 -0.0563 0.0164  31   LEU B C   
9324  O O   . LEU B 33   ? 0.3510 0.1764 0.2169 -0.0753 -0.0529 0.0167  31   LEU B O   
9325  C CB  . LEU B 33   ? 0.3847 0.1751 0.2252 -0.0856 -0.0590 0.0229  31   LEU B CB  
9326  C CG  . LEU B 33   ? 0.4336 0.2152 0.2669 -0.0953 -0.0606 0.0261  31   LEU B CG  
9327  C CD1 . LEU B 33   ? 0.4258 0.1958 0.2493 -0.0973 -0.0617 0.0296  31   LEU B CD1 
9328  C CD2 . LEU B 33   ? 0.4482 0.2453 0.2896 -0.1026 -0.0575 0.0282  31   LEU B CD2 
9329  N N   . ARG B 34   ? 0.3633 0.1661 0.2172 -0.0663 -0.0579 0.0139  32   ARG B N   
9330  C CA  . ARG B 34   ? 0.3410 0.1556 0.2035 -0.0591 -0.0556 0.0116  32   ARG B CA  
9331  C C   . ARG B 34   ? 0.3510 0.1756 0.2217 -0.0578 -0.0543 0.0086  32   ARG B C   
9332  O O   . ARG B 34   ? 0.3228 0.1619 0.2029 -0.0559 -0.0513 0.0080  32   ARG B O   
9333  C CB  . ARG B 34   ? 0.3313 0.1369 0.1896 -0.0511 -0.0577 0.0096  32   ARG B CB  
9334  C CG  . ARG B 34   ? 0.3597 0.1584 0.2116 -0.0509 -0.0585 0.0125  32   ARG B CG  
9335  C CD  . ARG B 34   ? 0.3583 0.1708 0.2172 -0.0501 -0.0550 0.0138  32   ARG B CD  
9336  N NE  . ARG B 34   ? 0.3481 0.1690 0.2144 -0.0423 -0.0540 0.0106  32   ARG B NE  
9337  C CZ  . ARG B 34   ? 0.3692 0.1861 0.2336 -0.0358 -0.0554 0.0095  32   ARG B CZ  
9338  N NH1 . ARG B 34   ? 0.3728 0.1771 0.2279 -0.0356 -0.0580 0.0114  32   ARG B NH1 
9339  N NH2 . ARG B 34   ? 0.3483 0.1740 0.2203 -0.0295 -0.0544 0.0066  32   ARG B NH2 
9340  N N   . ARG B 35   ? 0.3516 0.1684 0.2186 -0.0590 -0.0567 0.0068  33   ARG B N   
9341  C CA  . ARG B 35   ? 0.3368 0.1625 0.2108 -0.0578 -0.0557 0.0041  33   ARG B CA  
9342  C C   . ARG B 35   ? 0.2934 0.1327 0.1746 -0.0641 -0.0531 0.0060  33   ARG B C   
9343  O O   . ARG B 35   ? 0.3153 0.1669 0.2050 -0.0621 -0.0510 0.0043  33   ARG B O   
9344  C CB  . ARG B 35   ? 0.3617 0.1751 0.2289 -0.0580 -0.0590 0.0017  33   ARG B CB  
9345  C CG  . ARG B 35   ? 0.4167 0.2196 0.2790 -0.0502 -0.0611 -0.0012 33   ARG B CG  
9346  C CD  . ARG B 35   ? 0.4722 0.2617 0.3267 -0.0505 -0.0644 -0.0034 33   ARG B CD  
9347  N NE  . ARG B 35   ? 0.6020 0.3811 0.4515 -0.0426 -0.0663 -0.0061 33   ARG B NE  
9348  C CZ  . ARG B 35   ? 0.6434 0.4283 0.4981 -0.0349 -0.0652 -0.0094 33   ARG B CZ  
9349  N NH1 . ARG B 35   ? 0.6753 0.4752 0.5397 -0.0341 -0.0622 -0.0105 33   ARG B NH1 
9350  N NH2 . ARG B 35   ? 0.6911 0.4665 0.5411 -0.0279 -0.0670 -0.0114 33   ARG B NH2 
9351  N N   . ALA B 36   ? 0.3199 0.1572 0.1978 -0.0717 -0.0533 0.0095  34   ALA B N   
9352  C CA  . ALA B 36   ? 0.3149 0.1660 0.2001 -0.0776 -0.0507 0.0115  34   ALA B CA  
9353  C C   . ALA B 36   ? 0.2781 0.1437 0.1718 -0.0747 -0.0468 0.0123  34   ALA B C   
9354  O O   . ALA B 36   ? 0.3358 0.2152 0.2381 -0.0757 -0.0444 0.0122  34   ALA B O   
9355  C CB  . ALA B 36   ? 0.3545 0.2005 0.2344 -0.0866 -0.0517 0.0153  34   ALA B CB  
9356  N N   . ILE B 37   ? 0.2973 0.1596 0.1883 -0.0711 -0.0463 0.0130  35   ILE B N   
9357  C CA  . ILE B 37   ? 0.2911 0.1659 0.1895 -0.0673 -0.0429 0.0131  35   ILE B CA  
9358  C C   . ILE B 37   ? 0.2959 0.1786 0.2017 -0.0611 -0.0420 0.0095  35   ILE B C   
9359  O O   . ILE B 37   ? 0.2651 0.1616 0.1796 -0.0610 -0.0391 0.0094  35   ILE B O   
9360  C CB  . ILE B 37   ? 0.2740 0.1418 0.1670 -0.0639 -0.0433 0.0140  35   ILE B CB  
9361  C CG1 . ILE B 37   ? 0.2858 0.1471 0.1718 -0.0704 -0.0437 0.0180  35   ILE B CG1 
9362  C CG2 . ILE B 37   ? 0.2890 0.1686 0.1893 -0.0589 -0.0402 0.0134  35   ILE B CG2 
9363  C CD1 . ILE B 37   ? 0.2907 0.1410 0.1688 -0.0673 -0.0453 0.0189  35   ILE B CD1 
9364  N N   . THR B 38   ? 0.2789 0.1531 0.1815 -0.0557 -0.0443 0.0066  36   THR B N   
9365  C CA  . THR B 38   ? 0.2575 0.1388 0.1667 -0.0497 -0.0433 0.0033  36   THR B CA  
9366  C C   . THR B 38   ? 0.2655 0.1554 0.1805 -0.0524 -0.0423 0.0025  36   THR B C   
9367  O O   . THR B 38   ? 0.2443 0.1459 0.1674 -0.0497 -0.0400 0.0013  36   THR B O   
9368  C CB  . THR B 38   ? 0.3021 0.1724 0.2064 -0.0439 -0.0460 0.0004  36   THR B CB  
9369  O OG1 . THR B 38   ? 0.2984 0.1601 0.1968 -0.0415 -0.0472 0.0014  36   THR B OG1 
9370  C CG2 . THR B 38   ? 0.2855 0.1638 0.1969 -0.0374 -0.0445 -0.0028 36   THR B CG2 
9371  N N   . ALA B 39   ? 0.2702 0.1544 0.1809 -0.0581 -0.0443 0.0032  37   ALA B N   
9372  C CA  . ALA B 39   ? 0.2768 0.1686 0.1924 -0.0611 -0.0439 0.0026  37   ALA B CA  
9373  C C   . ALA B 39   ? 0.2942 0.2017 0.2185 -0.0638 -0.0406 0.0046  37   ALA B C   
9374  O O   . ALA B 39   ? 0.2796 0.1963 0.2102 -0.0638 -0.0397 0.0035  37   ALA B O   
9375  C CB  . ALA B 39   ? 0.2988 0.1809 0.2075 -0.0675 -0.0469 0.0034  37   ALA B CB  
9376  N N   . ALA B 40   ? 0.2643 0.1748 0.1889 -0.0659 -0.0389 0.0074  38   ALA B N   
9377  C CA  . ALA B 40   ? 0.2374 0.1625 0.1699 -0.0684 -0.0356 0.0093  38   ALA B CA  
9378  C C   . ALA B 40   ? 0.2388 0.1732 0.1779 -0.0623 -0.0327 0.0082  38   ALA B C   
9379  O O   . ALA B 40   ? 0.2495 0.1962 0.1953 -0.0635 -0.0299 0.0095  38   ALA B O   
9380  C CB  . ALA B 40   ? 0.2615 0.1857 0.1909 -0.0744 -0.0349 0.0131  38   ALA B CB  
9381  N N   . TYR B 41   ? 0.2451 0.1740 0.1822 -0.0560 -0.0334 0.0059  39   TYR B N   
9382  C CA  . TYR B 41   ? 0.2139 0.1499 0.1561 -0.0506 -0.0311 0.0050  39   TYR B CA  
9383  C C   . TYR B 41   ? 0.2108 0.1613 0.1623 -0.0501 -0.0282 0.0048  39   TYR B C   
9384  O O   . TYR B 41   ? 0.2052 0.1638 0.1605 -0.0500 -0.0256 0.0061  39   TYR B O   
9385  C CB  . TYR B 41   ? 0.2279 0.1571 0.1680 -0.0441 -0.0327 0.0020  39   TYR B CB  
9386  C CG  . TYR B 41   ? 0.2106 0.1415 0.1522 -0.0388 -0.0315 0.0014  39   TYR B CG  
9387  C CD1 . TYR B 41   ? 0.2094 0.1507 0.1566 -0.0382 -0.0285 0.0023  39   TYR B CD1 
9388  C CD2 . TYR B 41   ? 0.2249 0.1470 0.1623 -0.0340 -0.0336 -0.0004 39   TYR B CD2 
9389  C CE1 . TYR B 41   ? 0.2160 0.1585 0.1643 -0.0334 -0.0278 0.0015  39   TYR B CE1 
9390  C CE2 . TYR B 41   ? 0.2184 0.1423 0.1574 -0.0292 -0.0329 -0.0011 39   TYR B CE2 
9391  C CZ  . TYR B 41   ? 0.2357 0.1696 0.1800 -0.0291 -0.0300 -0.0002 39   TYR B CZ  
9392  O OH  . TYR B 41   ? 0.2195 0.1549 0.1651 -0.0246 -0.0296 -0.0010 39   TYR B OH  
9393  N N   . ARG B 42   ? 0.2370 0.1904 0.1916 -0.0497 -0.0288 0.0031  40   ARG B N   
9394  C CA  . ARG B 42   ? 0.2584 0.2249 0.2215 -0.0489 -0.0264 0.0028  40   ARG B CA  
9395  C C   . ARG B 42   ? 0.2474 0.2180 0.2124 -0.0539 -0.0271 0.0037  40   ARG B C   
9396  O O   . ARG B 42   ? 0.2400 0.2176 0.2102 -0.0526 -0.0266 0.0025  40   ARG B O   
9397  C CB  . ARG B 42   ? 0.2296 0.1980 0.1961 -0.0426 -0.0260 -0.0001 40   ARG B CB  
9398  C CG  . ARG B 42   ? 0.2271 0.1942 0.1933 -0.0380 -0.0250 -0.0006 40   ARG B CG  
9399  C CD  . ARG B 42   ? 0.2397 0.2070 0.2083 -0.0320 -0.0250 -0.0035 40   ARG B CD  
9400  N NE  . ARG B 42   ? 0.2226 0.1851 0.1885 -0.0284 -0.0252 -0.0040 40   ARG B NE  
9401  C CZ  . ARG B 42   ? 0.1979 0.1656 0.1667 -0.0266 -0.0233 -0.0034 40   ARG B CZ  
9402  N NH1 . ARG B 42   ? 0.2031 0.1810 0.1777 -0.0273 -0.0207 -0.0026 40   ARG B NH1 
9403  N NH2 . ARG B 42   ? 0.2111 0.1735 0.1767 -0.0238 -0.0241 -0.0038 40   ARG B NH2 
9404  N N   . ARG B 43   ? 0.2325 0.1992 0.1935 -0.0600 -0.0283 0.0059  41   ARG B N   
9405  C CA  . ARG B 43   ? 0.2360 0.2062 0.1984 -0.0656 -0.0293 0.0069  41   ARG B CA  
9406  C C   . ARG B 43   ? 0.2475 0.2331 0.2190 -0.0661 -0.0266 0.0080  41   ARG B C   
9407  O O   . ARG B 43   ? 0.2432 0.2355 0.2180 -0.0651 -0.0238 0.0094  41   ARG B O   
9408  C CB  . ARG B 43   ? 0.2460 0.2097 0.2026 -0.0722 -0.0307 0.0096  41   ARG B CB  
9409  C CG  . ARG B 43   ? 0.2387 0.2056 0.1963 -0.0790 -0.0321 0.0110  41   ARG B CG  
9410  C CD  . ARG B 43   ? 0.2623 0.2188 0.2122 -0.0853 -0.0343 0.0130  41   ARG B CD  
9411  N NE  . ARG B 43   ? 0.2736 0.2145 0.2148 -0.0835 -0.0375 0.0109  41   ARG B NE  
9412  C CZ  . ARG B 43   ? 0.2969 0.2253 0.2297 -0.0858 -0.0393 0.0120  41   ARG B CZ  
9413  N NH1 . ARG B 43   ? 0.3079 0.2370 0.2393 -0.0904 -0.0382 0.0153  41   ARG B NH1 
9414  N NH2 . ARG B 43   ? 0.3378 0.2525 0.2632 -0.0832 -0.0422 0.0098  41   ARG B NH2 
9415  N N   . PRO B 44   ? 0.2237 0.2149 0.1990 -0.0673 -0.0274 0.0074  42   PRO B N   
9416  C CA  . PRO B 44   ? 0.2274 0.2332 0.2114 -0.0677 -0.0250 0.0085  42   PRO B CA  
9417  C C   . PRO B 44   ? 0.2080 0.2201 0.1938 -0.0725 -0.0233 0.0118  42   PRO B C   
9418  O O   . PRO B 44   ? 0.2181 0.2250 0.1995 -0.0783 -0.0247 0.0136  42   PRO B O   
9419  C CB  . PRO B 44   ? 0.2199 0.2279 0.2054 -0.0699 -0.0272 0.0077  42   PRO B CB  
9420  C CG  . PRO B 44   ? 0.2902 0.2864 0.2695 -0.0669 -0.0296 0.0049  42   PRO B CG  
9421  C CD  . PRO B 44   ? 0.2661 0.2507 0.2381 -0.0675 -0.0304 0.0053  42   PRO B CD  
9422  N N   . GLU B 45   ? 0.2193 0.2427 0.2117 -0.0702 -0.0200 0.0126  43   GLU B N   
9423  C CA  . GLU B 45   ? 0.2337 0.2646 0.2287 -0.0740 -0.0176 0.0156  43   GLU B CA  
9424  C C   . GLU B 45   ? 0.2198 0.2559 0.2169 -0.0811 -0.0189 0.0177  43   GLU B C   
9425  O O   . GLU B 45   ? 0.2491 0.2852 0.2442 -0.0865 -0.0185 0.0203  43   GLU B O   
9426  C CB  . GLU B 45   ? 0.2731 0.3156 0.2751 -0.0695 -0.0140 0.0156  43   GLU B CB  
9427  C CG  . GLU B 45   ? 0.2810 0.3268 0.2828 -0.0702 -0.0110 0.0176  43   GLU B CG  
9428  C CD  . GLU B 45   ? 0.1813 0.2323 0.1866 -0.0639 -0.0080 0.0165  43   GLU B CD  
9429  O OE1 . GLU B 45   ? 0.1984 0.2490 0.2055 -0.0585 -0.0082 0.0141  43   GLU B OE1 
9430  O OE2 . GLU B 45   ? 0.2016 0.2567 0.2071 -0.0645 -0.0052 0.0182  43   GLU B OE2 
9431  N N   . THR B 46   ? 0.2347 0.2750 0.2354 -0.0814 -0.0206 0.0166  44   THR B N   
9432  C CA  . THR B 46   ? 0.2248 0.2702 0.2276 -0.0882 -0.0223 0.0185  44   THR B CA  
9433  C C   . THR B 46   ? 0.2435 0.2767 0.2382 -0.0940 -0.0255 0.0191  44   THR B C   
9434  O O   . THR B 46   ? 0.2827 0.3192 0.2781 -0.1009 -0.0265 0.0213  44   THR B O   
9435  C CB  . THR B 46   ? 0.2599 0.3116 0.2676 -0.0868 -0.0238 0.0170  44   THR B CB  
9436  O OG1 . THR B 46   ? 0.2564 0.2978 0.2593 -0.0826 -0.0258 0.0140  44   THR B OG1 
9437  C CG2 . THR B 46   ? 0.2522 0.3179 0.2687 -0.0824 -0.0207 0.0173  44   THR B CG2 
9438  N N   . GLU B 47   ? 0.2214 0.2404 0.2082 -0.0915 -0.0272 0.0171  45   GLU B N   
9439  C CA  . GLU B 47   ? 0.2267 0.2323 0.2048 -0.0965 -0.0302 0.0176  45   GLU B CA  
9440  C C   . GLU B 47   ? 0.2510 0.2524 0.2249 -0.0988 -0.0287 0.0200  45   GLU B C   
9441  O O   . GLU B 47   ? 0.2941 0.2889 0.2628 -0.1053 -0.0305 0.0219  45   GLU B O   
9442  C CB  . GLU B 47   ? 0.2593 0.2514 0.2306 -0.0923 -0.0329 0.0144  45   GLU B CB  
9443  C CG  . GLU B 47   ? 0.3297 0.3233 0.3028 -0.0911 -0.0350 0.0121  45   GLU B CG  
9444  C CD  . GLU B 47   ? 0.3795 0.3601 0.3459 -0.0866 -0.0371 0.0088  45   GLU B CD  
9445  O OE1 . GLU B 47   ? 0.4127 0.3807 0.3712 -0.0872 -0.0385 0.0087  45   GLU B OE1 
9446  O OE2 . GLU B 47   ? 0.4279 0.4111 0.3967 -0.0823 -0.0373 0.0065  45   GLU B OE2 
9447  N N   . CYS B 48   ? 0.2531 0.2578 0.2289 -0.0939 -0.0255 0.0201  46   CYS B N   
9448  C CA  . CYS B 48   ? 0.2555 0.2553 0.2264 -0.0956 -0.0241 0.0222  46   CYS B CA  
9449  C C   . CYS B 48   ? 0.2442 0.2541 0.2189 -0.1019 -0.0220 0.0258  46   CYS B C   
9450  O O   . CYS B 48   ? 0.2559 0.2598 0.2251 -0.1070 -0.0223 0.0282  46   CYS B O   
9451  C CB  . CYS B 48   ? 0.2397 0.2405 0.2115 -0.0885 -0.0215 0.0210  46   CYS B CB  
9452  S SG  . CYS B 48   ? 0.2571 0.2459 0.2241 -0.0811 -0.0235 0.0173  46   CYS B SG  
9453  N N   . LEU B 49   ? 0.2350 0.2602 0.2190 -0.1015 -0.0198 0.0263  47   LEU B N   
9454  C CA  . LEU B 49   ? 0.2423 0.2787 0.2307 -0.1059 -0.0167 0.0295  47   LEU B CA  
9455  C C   . LEU B 49   ? 0.2400 0.2774 0.2278 -0.1151 -0.0185 0.0322  47   LEU B C   
9456  O O   . LEU B 49   ? 0.2487 0.2887 0.2355 -0.1198 -0.0165 0.0353  47   LEU B O   
9457  C CB  . LEU B 49   ? 0.2313 0.2842 0.2300 -0.1020 -0.0136 0.0292  47   LEU B CB  
9458  C CG  . LEU B 49   ? 0.2096 0.2660 0.2094 -0.0964 -0.0097 0.0291  47   LEU B CG  
9459  C CD1 . LEU B 49   ? 0.2422 0.2987 0.2387 -0.1006 -0.0073 0.0322  47   LEU B CD1 
9460  C CD2 . LEU B 49   ? 0.2292 0.2745 0.2239 -0.0898 -0.0107 0.0261  47   LEU B CD2 
9461  N N   . PRO B 50   ? 0.2644 0.3001 0.2525 -0.1183 -0.0220 0.0314  48   PRO B N   
9462  C CA  . PRO B 50   ? 0.2820 0.3197 0.2700 -0.1277 -0.0236 0.0341  48   PRO B CA  
9463  C C   . PRO B 50   ? 0.3000 0.3250 0.2786 -0.1331 -0.0245 0.0363  48   PRO B C   
9464  O O   . PRO B 50   ? 0.2980 0.3288 0.2779 -0.1398 -0.0231 0.0397  48   PRO B O   
9465  C CB  . PRO B 50   ? 0.2906 0.3249 0.2784 -0.1288 -0.0279 0.0320  48   PRO B CB  
9466  C CG  . PRO B 50   ? 0.2669 0.3079 0.2605 -0.1206 -0.0267 0.0292  48   PRO B CG  
9467  C CD  . PRO B 50   ? 0.2597 0.2950 0.2500 -0.1139 -0.0243 0.0281  48   PRO B CD  
9468  N N   . PRO B 51   ? 0.2902 0.2982 0.2591 -0.1307 -0.0268 0.0346  49   PRO B N   
9469  C CA  . PRO B 51   ? 0.3008 0.2966 0.2605 -0.1359 -0.0277 0.0370  49   PRO B CA  
9470  C C   . PRO B 51   ? 0.3056 0.3052 0.2650 -0.1351 -0.0235 0.0394  49   PRO B C   
9471  O O   . PRO B 51   ? 0.3150 0.3106 0.2696 -0.1415 -0.0232 0.0426  49   PRO B O   
9472  C CB  . PRO B 51   ? 0.3407 0.3181 0.2909 -0.1319 -0.0312 0.0341  49   PRO B CB  
9473  C CG  . PRO B 51   ? 0.3553 0.3367 0.3101 -0.1232 -0.0306 0.0306  49   PRO B CG  
9474  C CD  . PRO B 51   ? 0.2720 0.2703 0.2375 -0.1240 -0.0293 0.0307  49   PRO B CD  
9475  N N   . LEU B 52   ? 0.2928 0.2998 0.2569 -0.1276 -0.0203 0.0380  50   LEU B N   
9476  C CA  . LEU B 52   ? 0.2759 0.2881 0.2403 -0.1268 -0.0162 0.0402  50   LEU B CA  
9477  C C   . LEU B 52   ? 0.3034 0.3317 0.2753 -0.1325 -0.0131 0.0434  50   LEU B C   
9478  O O   . LEU B 52   ? 0.3040 0.3333 0.2733 -0.1369 -0.0108 0.0465  50   LEU B O   
9479  C CB  . LEU B 52   ? 0.2584 0.2742 0.2258 -0.1174 -0.0138 0.0376  50   LEU B CB  
9480  C CG  . LEU B 52   ? 0.2799 0.2814 0.2407 -0.1111 -0.0163 0.0345  50   LEU B CG  
9481  C CD1 . LEU B 52   ? 0.2476 0.2555 0.2134 -0.1025 -0.0140 0.0319  50   LEU B CD1 
9482  C CD2 . LEU B 52   ? 0.2799 0.2670 0.2300 -0.1127 -0.0173 0.0359  50   LEU B CD2 
9483  N N   . VAL B 53   ? 0.2699 0.3113 0.2513 -0.1325 -0.0129 0.0426  51   VAL B N   
9484  C CA  . VAL B 53   ? 0.2883 0.3459 0.2777 -0.1380 -0.0103 0.0456  51   VAL B CA  
9485  C C   . VAL B 53   ? 0.3141 0.3660 0.2984 -0.1456 -0.0120 0.0481  51   VAL B C   
9486  O O   . VAL B 53   ? 0.3332 0.3914 0.3184 -0.1482 -0.0091 0.0507  51   VAL B O   
9487  C CB  . VAL B 53   ? 0.2925 0.3631 0.2921 -0.1365 -0.0109 0.0441  51   VAL B CB  
9488  C CG1 . VAL B 53   ? 0.2918 0.3763 0.2982 -0.1392 -0.0091 0.0461  51   VAL B CG1 
9489  C CG2 . VAL B 53   ? 0.3174 0.3947 0.3223 -0.1268 -0.0086 0.0414  51   VAL B CG2 
9490  N N   . GLU B 54   ? 0.3268 0.3659 0.3049 -0.1483 -0.0168 0.0470  52   GLU B N   
9491  C CA  . GLU B 54   ? 0.3313 0.3635 0.3038 -0.1546 -0.0188 0.0489  52   GLU B CA  
9492  C C   . GLU B 54   ? 0.3607 0.3839 0.3248 -0.1567 -0.0172 0.0514  52   GLU B C   
9493  O O   . GLU B 54   ? 0.3424 0.3697 0.3064 -0.1611 -0.0156 0.0541  52   GLU B O   
9494  C CB  . GLU B 54   ? 0.3611 0.3793 0.3273 -0.1561 -0.0242 0.0469  52   GLU B CB  
9495  N N   . ALA B 55   ? 0.3228 0.3340 0.2799 -0.1536 -0.0176 0.0505  53   ALA B N   
9496  C CA  . ALA B 55   ? 0.3774 0.3780 0.3253 -0.1552 -0.0166 0.0527  53   ALA B CA  
9497  C C   . ALA B 55   ? 0.3303 0.3435 0.2824 -0.1544 -0.0112 0.0550  53   ALA B C   
9498  O O   . ALA B 55   ? 0.3901 0.3990 0.3363 -0.1574 -0.0098 0.0575  53   ALA B O   
9499  C CB  . ALA B 55   ? 0.4096 0.3941 0.3491 -0.1511 -0.0188 0.0509  53   ALA B CB  
9500  N N   . ALA B 56   ? 0.3119 0.3405 0.2738 -0.1503 -0.0079 0.0540  54   ALA B N   
9501  C CA  . ALA B 56   ? 0.3089 0.3500 0.2751 -0.1487 -0.0025 0.0557  54   ALA B CA  
9502  C C   . ALA B 56   ? 0.3555 0.4116 0.3294 -0.1518 -0.0003 0.0574  54   ALA B C   
9503  O O   . ALA B 56   ? 0.3920 0.4592 0.3699 -0.1504 0.0043  0.0587  54   ALA B O   
9504  C CB  . ALA B 56   ? 0.3091 0.3588 0.2816 -0.1411 0.0000  0.0534  54   ALA B CB  
9505  N N   . THR B 57   ? 0.3342 0.3907 0.3102 -0.1558 -0.0035 0.0573  55   THR B N   
9506  C CA  . THR B 57   ? 0.3769 0.4476 0.3605 -0.1589 -0.0018 0.0589  55   THR B CA  
9507  C C   . THR B 57   ? 0.3721 0.4410 0.3507 -0.1637 0.0003  0.0621  55   THR B C   
9508  O O   . THR B 57   ? 0.4145 0.4683 0.3830 -0.1674 -0.0021 0.0632  55   THR B O   
9509  C CB  . THR B 57   ? 0.3346 0.4045 0.3203 -0.1624 -0.0062 0.0580  55   THR B CB  
9510  O OG1 . THR B 57   ? 0.3891 0.4622 0.3800 -0.1577 -0.0077 0.0551  55   THR B OG1 
9511  C CG2 . THR B 57   ? 0.3856 0.4697 0.3787 -0.1661 -0.0046 0.0599  55   THR B CG2 
9512  N N   . GLN B 58   ? 0.3506 0.4347 0.3362 -0.1633 0.0048  0.0636  56   GLN B N   
9513  C CA  . GLN B 58   ? 0.3744 0.4596 0.3569 -0.1679 0.0073  0.0667  56   GLN B CA  
9514  C C   . GLN B 58   ? 0.4118 0.5128 0.4037 -0.1708 0.0087  0.0680  56   GLN B C   
9515  O O   . GLN B 58   ? 0.3930 0.5069 0.3948 -0.1675 0.0094  0.0665  56   GLN B O   
9516  C CB  . GLN B 58   ? 0.4135 0.5006 0.3937 -0.1642 0.0121  0.0675  56   GLN B CB  
9517  C CG  . GLN B 58   ? 0.3615 0.4334 0.3323 -0.1611 0.0108  0.0665  56   GLN B CG  
9518  C CD  . GLN B 58   ? 0.4152 0.4855 0.3805 -0.1593 0.0148  0.0680  56   GLN B CD  
9519  O OE1 . GLN B 58   ? 0.4283 0.4902 0.3856 -0.1635 0.0148  0.0704  56   GLN B OE1 
9520  N NE2 . GLN B 58   ? 0.3934 0.4717 0.3628 -0.1530 0.0183  0.0666  56   GLN B NE2 
9521  N N   . SER B 59   ? 0.4487 0.5486 0.4374 -0.1770 0.0093  0.0708  57   SER B N   
9522  C CA  . SER B 59   ? 0.4726 0.5867 0.4696 -0.1806 0.0106  0.0723  57   SER B CA  
9523  C C   . SER B 59   ? 0.4604 0.5926 0.4673 -0.1756 0.0159  0.0722  57   SER B C   
9524  O O   . SER B 59   ? 0.3941 0.5270 0.3997 -0.1704 0.0193  0.0716  57   SER B O   
9525  C CB  . SER B 59   ? 0.4472 0.5563 0.4381 -0.1880 0.0108  0.0756  57   SER B CB  
9526  O OG  . SER B 59   ? 0.4251 0.5330 0.4115 -0.1869 0.0150  0.0772  57   SER B OG  
9527  N N   . LYS B 60   ? 0.4294 0.5760 0.4459 -0.1770 0.0166  0.0727  58   LYS B N   
9528  C CA  . LYS B 60   ? 0.4209 0.5851 0.4472 -0.1722 0.0215  0.0725  58   LYS B CA  
9529  C C   . LYS B 60   ? 0.4354 0.6020 0.4588 -0.1725 0.0266  0.0747  58   LYS B C   
9530  O O   . LYS B 60   ? 0.3656 0.5396 0.3921 -0.1665 0.0308  0.0739  58   LYS B O   
9531  C CB  . LYS B 60   ? 0.4953 0.6735 0.5317 -0.1745 0.0208  0.0730  58   LYS B CB  
9532  C CG  . LYS B 60   ? 0.4567 0.6533 0.5033 -0.1702 0.0258  0.0732  58   LYS B CG  
9533  C CD  . LYS B 60   ? 0.5122 0.7149 0.5647 -0.1615 0.0267  0.0702  58   LYS B CD  
9534  C CE  . LYS B 60   ? 0.5300 0.7504 0.5923 -0.1571 0.0315  0.0703  58   LYS B CE  
9535  N NZ  . LYS B 60   ? 0.5638 0.7896 0.6316 -0.1484 0.0322  0.0674  58   LYS B NZ  
9536  N N   . GLU B 61   ? 0.4055 0.5656 0.4225 -0.1795 0.0263  0.0775  59   GLU B N   
9537  C CA  . GLU B 61   ? 0.4339 0.5961 0.4477 -0.1802 0.0311  0.0797  59   GLU B CA  
9538  C C   . GLU B 61   ? 0.4024 0.5538 0.4077 -0.1757 0.0325  0.0788  59   GLU B C   
9539  O O   . GLU B 61   ? 0.3834 0.5405 0.3890 -0.1720 0.0374  0.0792  59   GLU B O   
9540  C CB  . GLU B 61   ? 0.4843 0.6409 0.4926 -0.1889 0.0302  0.0829  59   GLU B CB  
9541  C CG  . GLU B 61   ? 0.5797 0.7249 0.5837 -0.1946 0.0240  0.0829  59   GLU B CG  
9542  C CD  . GLU B 61   ? 0.6161 0.7727 0.6300 -0.1967 0.0219  0.0824  59   GLU B CD  
9543  O OE1 . GLU B 61   ? 0.7126 0.8845 0.7347 -0.1978 0.0251  0.0839  59   GLU B OE1 
9544  O OE2 . GLU B 61   ? 0.6180 0.7682 0.6312 -0.1970 0.0170  0.0806  59   GLU B OE2 
9545  N N   . ILE B 62   ? 0.4076 0.5431 0.4050 -0.1758 0.0282  0.0777  60   ILE B N   
9546  C CA  . ILE B 62   ? 0.3958 0.5209 0.3852 -0.1714 0.0292  0.0767  60   ILE B CA  
9547  C C   . ILE B 62   ? 0.4024 0.5368 0.3986 -0.1631 0.0316  0.0740  60   ILE B C   
9548  O O   . ILE B 62   ? 0.4060 0.5419 0.4001 -0.1586 0.0355  0.0738  60   ILE B O   
9549  C CB  . ILE B 62   ? 0.4297 0.5355 0.4092 -0.1735 0.0237  0.0761  60   ILE B CB  
9550  C CG1 . ILE B 62   ? 0.4790 0.5732 0.4489 -0.1806 0.0223  0.0790  60   ILE B CG1 
9551  C CG2 . ILE B 62   ? 0.4512 0.5485 0.4252 -0.1674 0.0240  0.0742  60   ILE B CG2 
9552  C CD1 . ILE B 62   ? 0.4849 0.5601 0.4453 -0.1831 0.0166  0.0784  60   ILE B CD1 
9553  N N   . ARG B 63   ? 0.3896 0.5305 0.3939 -0.1608 0.0293  0.0719  61   ARG B N   
9554  C CA  . ARG B 63   ? 0.3994 0.5495 0.4107 -0.1529 0.0315  0.0693  61   ARG B CA  
9555  C C   . ARG B 63   ? 0.3549 0.5205 0.3729 -0.1497 0.0372  0.0699  61   ARG B C   
9556  O O   . ARG B 63   ? 0.3902 0.5591 0.4088 -0.1432 0.0405  0.0685  61   ARG B O   
9557  C CB  . ARG B 63   ? 0.3812 0.5356 0.3999 -0.1516 0.0278  0.0671  61   ARG B CB  
9558  C CG  . ARG B 63   ? 0.3940 0.5327 0.4058 -0.1534 0.0224  0.0660  61   ARG B CG  
9559  C CD  . ARG B 63   ? 0.4165 0.5589 0.4350 -0.1510 0.0191  0.0635  61   ARG B CD  
9560  N NE  . ARG B 63   ? 0.4102 0.5573 0.4331 -0.1561 0.0164  0.0643  61   ARG B NE  
9561  C CZ  . ARG B 63   ? 0.4611 0.6235 0.4944 -0.1547 0.0175  0.0641  61   ARG B CZ  
9562  N NH1 . ARG B 63   ? 0.4675 0.6419 0.5079 -0.1481 0.0213  0.0630  61   ARG B NH1 
9563  N NH2 . ARG B 63   ? 0.4596 0.6248 0.4959 -0.1598 0.0147  0.0650  61   ARG B NH2 
9564  N N   . ASP B 64   ? 0.3571 0.5320 0.3799 -0.1541 0.0385  0.0720  62   ASP B N   
9565  C CA  . ASP B 64   ? 0.3207 0.5099 0.3495 -0.1513 0.0441  0.0727  62   ASP B CA  
9566  C C   . ASP B 64   ? 0.3502 0.5339 0.3706 -0.1505 0.0481  0.0740  62   ASP B C   
9567  O O   . ASP B 64   ? 0.3726 0.5633 0.3952 -0.1444 0.0525  0.0729  62   ASP B O   
9568  C CB  . ASP B 64   ? 0.3598 0.5594 0.3949 -0.1570 0.0445  0.0749  62   ASP B CB  
9569  C CG  . ASP B 64   ? 0.4183 0.6272 0.4633 -0.1562 0.0417  0.0735  62   ASP B CG  
9570  O OD1 . ASP B 64   ? 0.4325 0.6429 0.4812 -0.1500 0.0406  0.0707  62   ASP B OD1 
9571  O OD2 . ASP B 64   ? 0.4677 0.6825 0.5169 -0.1617 0.0405  0.0752  62   ASP B OD2 
9572  N N   . ALA B 65   ? 0.3330 0.5038 0.3435 -0.1564 0.0465  0.0761  63   ALA B N   
9573  C CA  . ALA B 65   ? 0.3422 0.5074 0.3441 -0.1560 0.0501  0.0776  63   ALA B CA  
9574  C C   . ALA B 65   ? 0.3571 0.5147 0.3537 -0.1494 0.0505  0.0753  63   ALA B C   
9575  O O   . ALA B 65   ? 0.3625 0.5219 0.3562 -0.1455 0.0548  0.0753  63   ALA B O   
9576  C CB  . ALA B 65   ? 0.3794 0.5315 0.3715 -0.1638 0.0478  0.0804  63   ALA B CB  
9577  N N   . ALA B 66   ? 0.3769 0.5261 0.3721 -0.1480 0.0460  0.0733  64   ALA B N   
9578  C CA  . ALA B 66   ? 0.3662 0.5084 0.3566 -0.1420 0.0462  0.0712  64   ALA B CA  
9579  C C   . ALA B 66   ? 0.3636 0.5191 0.3625 -0.1342 0.0498  0.0688  64   ALA B C   
9580  O O   . ALA B 66   ? 0.3363 0.4901 0.3313 -0.1289 0.0525  0.0676  64   ALA B O   
9581  C CB  . ALA B 66   ? 0.2961 0.4260 0.2830 -0.1428 0.0405  0.0697  64   ALA B CB  
9582  N N   . ALA B 67   ? 0.3326 0.5011 0.3426 -0.1332 0.0497  0.0679  65   ALA B N   
9583  C CA  . ALA B 67   ? 0.3397 0.5208 0.3578 -0.1256 0.0532  0.0657  65   ALA B CA  
9584  C C   . ALA B 67   ? 0.3253 0.5134 0.3427 -0.1236 0.0590  0.0667  65   ALA B C   
9585  O O   . ALA B 67   ? 0.3903 0.5828 0.4089 -0.1166 0.0623  0.0648  65   ALA B O   
9586  C CB  . ALA B 67   ? 0.3429 0.5362 0.3728 -0.1254 0.0517  0.0649  65   ALA B CB  
9587  N N   . SER B 68   ? 0.3586 0.5477 0.3738 -0.1296 0.0605  0.0697  66   SER B N   
9588  C CA  . SER B 68   ? 0.3283 0.5233 0.3420 -0.1280 0.0662  0.0708  66   SER B CA  
9589  C C   . SER B 68   ? 0.3772 0.5601 0.3790 -0.1263 0.0675  0.0710  66   SER B C   
9590  O O   . SER B 68   ? 0.3398 0.5266 0.3401 -0.1212 0.0721  0.0702  66   SER B O   
9591  C CB  . SER B 68   ? 0.4437 0.6435 0.4587 -0.1351 0.0674  0.0741  66   SER B CB  
9592  O OG  . SER B 68   ? 0.4790 0.6931 0.5058 -0.1353 0.0676  0.0739  66   SER B OG  
9593  N N   . THR B 69   ? 0.3571 0.5249 0.3497 -0.1305 0.0636  0.0719  67   THR B N   
9594  C CA  . THR B 69   ? 0.3593 0.5147 0.3401 -0.1287 0.0643  0.0720  67   THR B CA  
9595  C C   . THR B 69   ? 0.3158 0.4712 0.2973 -0.1206 0.0647  0.0686  67   THR B C   
9596  O O   . THR B 69   ? 0.3241 0.4778 0.3000 -0.1162 0.0680  0.0679  67   THR B O   
9597  C CB  . THR B 69   ? 0.3799 0.5186 0.3512 -0.1344 0.0594  0.0735  67   THR B CB  
9598  O OG1 . THR B 69   ? 0.3379 0.4754 0.3068 -0.1418 0.0594  0.0768  67   THR B OG1 
9599  C CG2 . THR B 69   ? 0.3621 0.4874 0.3212 -0.1318 0.0593  0.0733  67   THR B CG2 
9600  N N   . ALA B 70   ? 0.3215 0.4788 0.3095 -0.1186 0.0615  0.0664  68   ALA B N   
9601  C CA  . ALA B 70   ? 0.3523 0.5100 0.3415 -0.1111 0.0617  0.0632  68   ALA B CA  
9602  C C   . ALA B 70   ? 0.3722 0.5430 0.3676 -0.1046 0.0668  0.0616  68   ALA B C   
9603  O O   . ALA B 70   ? 0.3582 0.5271 0.3498 -0.0987 0.0689  0.0597  68   ALA B O   
9604  C CB  . ALA B 70   ? 0.3561 0.5138 0.3516 -0.1107 0.0572  0.0614  68   ALA B CB  
9605  N N   . ARG B 71   ? 0.3616 0.5454 0.3663 -0.1055 0.0687  0.0623  69   ARG B N   
9606  C CA  . ARG B 71   ? 0.3316 0.5276 0.3423 -0.0992 0.0735  0.0608  69   ARG B CA  
9607  C C   . ARG B 71   ? 0.3478 0.5412 0.3502 -0.0978 0.0781  0.0616  69   ARG B C   
9608  O O   . ARG B 71   ? 0.3259 0.5216 0.3275 -0.0909 0.0812  0.0593  69   ARG B O   
9609  C CB  . ARG B 71   ? 0.3774 0.5873 0.3990 -0.1012 0.0745  0.0618  69   ARG B CB  
9610  C CG  . ARG B 71   ? 0.4307 0.6529 0.4578 -0.0953 0.0798  0.0606  69   ARG B CG  
9611  C CD  . ARG B 71   ? 0.4882 0.7244 0.5262 -0.0972 0.0806  0.0616  69   ARG B CD  
9612  N NE  . ARG B 71   ? 0.4517 0.6928 0.4987 -0.0949 0.0771  0.0598  69   ARG B NE  
9613  C CZ  . ARG B 71   ? 0.5079 0.7543 0.5601 -0.0871 0.0778  0.0569  69   ARG B CZ  
9614  N NH1 . ARG B 71   ? 0.4719 0.7189 0.5213 -0.0807 0.0818  0.0552  69   ARG B NH1 
9615  N NH2 . ARG B 71   ? 0.5204 0.7709 0.5804 -0.0858 0.0744  0.0556  69   ARG B NH2 
9616  N N   . LYS B 72   ? 0.3160 0.5040 0.3117 -0.1043 0.0785  0.0648  70   LYS B N   
9617  C CA  . LYS B 72   ? 0.3358 0.5202 0.3225 -0.1034 0.0826  0.0658  70   LYS B CA  
9618  C C   . LYS B 72   ? 0.3587 0.5314 0.3356 -0.0991 0.0818  0.0640  70   LYS B C   
9619  O O   . LYS B 72   ? 0.3716 0.5449 0.3442 -0.0940 0.0856  0.0627  70   LYS B O   
9620  C CB  . LYS B 72   ? 0.3438 0.5231 0.3247 -0.1116 0.0824  0.0697  70   LYS B CB  
9621  C CG  . LYS B 72   ? 0.4012 0.5764 0.3723 -0.1114 0.0866  0.0712  70   LYS B CG  
9622  C CD  . LYS B 72   ? 0.3845 0.5564 0.3515 -0.1198 0.0865  0.0752  70   LYS B CD  
9623  C CE  . LYS B 72   ? 0.4443 0.6104 0.4003 -0.1199 0.0902  0.0770  70   LYS B CE  
9624  N NZ  . LYS B 72   ? 0.3624 0.5402 0.3217 -0.1150 0.0966  0.0761  70   LYS B NZ  
9625  N N   . LEU B 73   ? 0.3531 0.5149 0.3261 -0.1011 0.0768  0.0637  71   LEU B N   
9626  C CA  . LEU B 73   ? 0.3669 0.5178 0.3308 -0.0971 0.0757  0.0619  71   LEU B CA  
9627  C C   . LEU B 73   ? 0.3666 0.5243 0.3357 -0.0886 0.0774  0.0581  71   LEU B C   
9628  O O   . LEU B 73   ? 0.3191 0.4731 0.2815 -0.0836 0.0795  0.0565  71   LEU B O   
9629  C CB  . LEU B 73   ? 0.3228 0.4613 0.2825 -0.1007 0.0698  0.0622  71   LEU B CB  
9630  C CG  . LEU B 73   ? 0.3125 0.4411 0.2652 -0.1088 0.0673  0.0657  71   LEU B CG  
9631  C CD1 . LEU B 73   ? 0.3027 0.4203 0.2532 -0.1115 0.0614  0.0654  71   LEU B CD1 
9632  C CD2 . LEU B 73   ? 0.3949 0.5142 0.3349 -0.1092 0.0693  0.0673  71   LEU B CD2 
9633  N N   . ILE B 74   ? 0.3420 0.5092 0.3227 -0.0867 0.0764  0.0566  72   ILE B N   
9634  C CA  . ILE B 74   ? 0.3362 0.5089 0.3221 -0.0787 0.0774  0.0530  72   ILE B CA  
9635  C C   . ILE B 74   ? 0.3656 0.5470 0.3532 -0.0735 0.0829  0.0519  72   ILE B C   
9636  O O   . ILE B 74   ? 0.3695 0.5498 0.3542 -0.0668 0.0847  0.0492  72   ILE B O   
9637  C CB  . ILE B 74   ? 0.3444 0.5240 0.3417 -0.0783 0.0744  0.0518  72   ILE B CB  
9638  C CG1 . ILE B 74   ? 0.3492 0.5183 0.3433 -0.0820 0.0690  0.0521  72   ILE B CG1 
9639  C CG2 . ILE B 74   ? 0.3391 0.5258 0.3427 -0.0698 0.0759  0.0483  72   ILE B CG2 
9640  C CD1 . ILE B 74   ? 0.3159 0.4903 0.3198 -0.0837 0.0656  0.0518  72   ILE B CD1 
9641  N N   . GLU B 75   ? 0.3735 0.5635 0.3655 -0.0765 0.0857  0.0540  73   GLU B N   
9642  C CA  . GLU B 75   ? 0.3322 0.5300 0.3248 -0.0722 0.0912  0.0534  73   GLU B CA  
9643  C C   . GLU B 75   ? 0.3587 0.5472 0.3385 -0.0706 0.0936  0.0533  73   GLU B C   
9644  O O   . GLU B 75   ? 0.4317 0.6218 0.4095 -0.0640 0.0968  0.0509  73   GLU B O   
9645  C CB  . GLU B 75   ? 0.3407 0.5483 0.3392 -0.0769 0.0935  0.0561  73   GLU B CB  
9646  N N   . ALA B 76   ? 0.3624 0.5404 0.3329 -0.0766 0.0918  0.0560  74   ALA B N   
9647  C CA  . ALA B 76   ? 0.3344 0.5026 0.2919 -0.0753 0.0934  0.0561  74   ALA B CA  
9648  C C   . ALA B 76   ? 0.4232 0.5843 0.3759 -0.0691 0.0918  0.0527  74   ALA B C   
9649  O O   . ALA B 76   ? 0.4358 0.5942 0.3815 -0.0643 0.0945  0.0510  74   ALA B O   
9650  C CB  . ALA B 76   ? 0.3730 0.5303 0.3216 -0.0830 0.0910  0.0597  74   ALA B CB  
9651  N N   . LEU B 77   ? 0.3568 0.5147 0.3128 -0.0692 0.0872  0.0515  75   LEU B N   
9652  C CA  . LEU B 77   ? 0.3721 0.5237 0.3242 -0.0636 0.0854  0.0483  75   LEU B CA  
9653  C C   . LEU B 77   ? 0.3905 0.5506 0.3482 -0.0554 0.0885  0.0447  75   LEU B C   
9654  O O   . LEU B 77   ? 0.4241 0.5796 0.3749 -0.0501 0.0898  0.0423  75   LEU B O   
9655  C CB  . LEU B 77   ? 0.3245 0.4721 0.2801 -0.0657 0.0801  0.0479  75   LEU B CB  
9656  C CG  . LEU B 77   ? 0.3887 0.5229 0.3352 -0.0719 0.0758  0.0502  75   LEU B CG  
9657  C CD1 . LEU B 77   ? 0.3606 0.4914 0.3134 -0.0734 0.0704  0.0494  75   LEU B CD1 
9658  C CD2 . LEU B 77   ? 0.4133 0.5333 0.3480 -0.0679 0.0741  0.0483  75   LEU B CD2 
9659  N N   . ARG B 78   ? 0.3498 0.5217 0.3198 -0.0541 0.0895  0.0442  76   ARG B N   
9660  C CA  . ARG B 78   ? 0.3500 0.5293 0.3258 -0.0462 0.0921  0.0409  76   ARG B CA  
9661  C C   . ARG B 78   ? 0.4221 0.6052 0.3945 -0.0434 0.0975  0.0407  76   ARG B C   
9662  O O   . ARG B 78   ? 0.3893 0.5745 0.3622 -0.0363 0.0997  0.0375  76   ARG B O   
9663  C CB  . ARG B 78   ? 0.3561 0.5462 0.3455 -0.0458 0.0910  0.0406  76   ARG B CB  
9664  C CG  . ARG B 78   ? 0.3397 0.5263 0.3327 -0.0474 0.0858  0.0402  76   ARG B CG  
9665  C CD  . ARG B 78   ? 0.3295 0.5264 0.3355 -0.0464 0.0846  0.0396  76   ARG B CD  
9666  N NE  . ARG B 78   ? 0.3217 0.5158 0.3308 -0.0431 0.0810  0.0373  76   ARG B NE  
9667  C CZ  . ARG B 78   ? 0.3286 0.5296 0.3480 -0.0414 0.0791  0.0364  76   ARG B CZ  
9668  N NH1 . ARG B 78   ? 0.3809 0.5922 0.4086 -0.0429 0.0802  0.0377  76   ARG B NH1 
9669  N NH2 . ARG B 78   ? 0.4130 0.6105 0.4341 -0.0382 0.0760  0.0342  76   ARG B NH2 
9670  N N   . GLY B 79   ? 0.3948 0.5784 0.3637 -0.0489 0.0996  0.0439  77   GLY B N   
9671  C CA  . GLY B 79   ? 0.4190 0.6066 0.3847 -0.0467 0.1051  0.0440  77   GLY B CA  
9672  C C   . GLY B 79   ? 0.5382 0.7155 0.4905 -0.0437 0.1065  0.0427  77   GLY B C   
9673  O O   . GLY B 79   ? 0.5074 0.6869 0.4574 -0.0382 0.1104  0.0405  77   GLY B O   
9674  N N   . LYS B 80   ? 0.4933 0.6589 0.4363 -0.0472 0.1031  0.0439  78   LYS B N   
9675  C CA  . LYS B 80   ? 0.5632 0.7180 0.4926 -0.0447 0.1036  0.0428  78   LYS B CA  
9676  C C   . LYS B 80   ? 0.5701 0.7190 0.4973 -0.0391 0.1006  0.0390  78   LYS B C   
9677  O O   . LYS B 80   ? 0.6145 0.7536 0.5302 -0.0370 0.1000  0.0378  78   LYS B O   
9678  C CB  . LYS B 80   ? 0.5438 0.6885 0.4631 -0.0516 0.1015  0.0464  78   LYS B CB  
9679  C CG  . LYS B 80   ? 0.4928 0.6304 0.4122 -0.0559 0.0957  0.0474  78   LYS B CG  
9680  C CD  . LYS B 80   ? 0.5352 0.6644 0.4468 -0.0635 0.0939  0.0516  78   LYS B CD  
9681  C CE  . LYS B 80   ? 0.3989 0.5201 0.3102 -0.0677 0.0880  0.0525  78   LYS B CE  
9682  N NZ  . LYS B 80   ? 0.3929 0.5045 0.2961 -0.0749 0.0859  0.0564  78   LYS B NZ  
9683  N N   . HIS B 81   ? 0.5666 0.7211 0.5042 -0.0365 0.0987  0.0371  79   HIS B N   
9684  C CA  . HIS B 81   ? 0.6313 0.7811 0.5677 -0.0308 0.0961  0.0334  79   HIS B CA  
9685  C C   . HIS B 81   ? 0.6925 0.8427 0.6256 -0.0232 0.0995  0.0299  79   HIS B C   
9686  O O   . HIS B 81   ? 0.6578 0.8166 0.5966 -0.0206 0.1034  0.0293  79   HIS B O   
9687  C CB  . HIS B 81   ? 0.6407 0.7969 0.5895 -0.0299 0.0934  0.0324  79   HIS B CB  
9688  C CG  . HIS B 81   ? 0.7297 0.8824 0.6786 -0.0234 0.0914  0.0284  79   HIS B CG  
9689  N ND1 . HIS B 81   ? 0.7609 0.9011 0.7064 -0.0236 0.0856  0.0272  79   HIS B ND1 
9690  C CD2 . HIS B 81   ? 0.7494 0.9055 0.7021 -0.0159 0.0930  0.0248  79   HIS B CD2 
9691  C CE1 . HIS B 81   ? 0.7740 0.9112 0.7213 -0.0169 0.0840  0.0232  79   HIS B CE1 
9692  N NE2 . HIS B 81   ? 0.7786 0.9263 0.7296 -0.0123 0.0889  0.0219  79   HIS B NE2 
9693  N N   . SER B 82   ? 0.7335 0.8739 0.6569 -0.0197 0.0978  0.0274  80   SER B N   
9694  C CA  . SER B 82   ? 0.7359 0.8747 0.6559 -0.0120 0.1000  0.0233  80   SER B CA  
9695  C C   . SER B 82   ? 0.7575 0.8886 0.6753 -0.0080 0.0956  0.0201  80   SER B C   
9696  O O   . SER B 82   ? 0.7660 0.8898 0.6855 -0.0110 0.0901  0.0207  80   SER B O   
9697  C CB  . SER B 82   ? 0.6816 0.8149 0.5893 -0.0118 0.1031  0.0236  80   SER B CB  
9698  O OG  . SER B 82   ? 0.7227 0.8467 0.6201 -0.0169 0.1005  0.0261  80   SER B OG  
9699  N N   . GLY B 83   ? 0.7459 0.8748 0.6607 -0.0009 0.0968  0.0161  81   GLY B N   
9700  C CA  . GLY B 83   ? 0.7171 0.8357 0.6317 0.0033  0.0916  0.0124  81   GLY B CA  
9701  C C   . GLY B 83   ? 0.7175 0.8208 0.6217 0.0011  0.0867  0.0123  81   GLY B C   
9702  O O   . GLY B 83   ? 0.6895 0.7880 0.5831 -0.0005 0.0881  0.0133  81   GLY B O   
9703  N N   . SER B 84   ? 0.6958 0.7915 0.6033 0.0010  0.0808  0.0110  82   SER B N   
9704  C CA  . SER B 84   ? 0.6390 0.7205 0.5379 -0.0004 0.0756  0.0104  82   SER B CA  
9705  C C   . SER B 84   ? 0.5881 0.6618 0.4781 0.0051  0.0754  0.0067  82   SER B C   
9706  O O   . SER B 84   ? 0.5106 0.5890 0.4013 0.0102  0.0789  0.0042  82   SER B O   
9707  C CB  . SER B 84   ? 0.5998 0.6764 0.5052 -0.0015 0.0697  0.0099  82   SER B CB  
9708  O OG  . SER B 84   ? 0.5485 0.6258 0.4597 0.0039  0.0686  0.0063  82   SER B OG  
9709  N N   . GLY B 85   ? 0.5820 0.6433 0.4631 0.0041  0.0710  0.0062  83   GLY B N   
9710  C CA  . GLY B 85   ? 0.4991 0.5521 0.3712 0.0087  0.0701  0.0027  83   GLY B CA  
9711  C C   . GLY B 85   ? 0.5039 0.5559 0.3817 0.0140  0.0682  -0.0014 83   GLY B C   
9712  O O   . GLY B 85   ? 0.4675 0.5191 0.3417 0.0189  0.0705  -0.0045 83   GLY B O   
9713  N N   . VAL B 86   ? 0.4951 0.5463 0.3816 0.0130  0.0641  -0.0015 84   VAL B N   
9714  C CA  . VAL B 86   ? 0.4633 0.5129 0.3552 0.0175  0.0619  -0.0051 84   VAL B CA  
9715  C C   . VAL B 86   ? 0.4572 0.5171 0.3556 0.0214  0.0668  -0.0062 84   VAL B C   
9716  O O   . VAL B 86   ? 0.4017 0.4596 0.2993 0.0266  0.0671  -0.0097 84   VAL B O   
9717  C CB  . VAL B 86   ? 0.4651 0.5122 0.3646 0.0152  0.0567  -0.0046 84   VAL B CB  
9718  C CG1 . VAL B 86   ? 0.4598 0.5079 0.3668 0.0194  0.0555  -0.0076 84   VAL B CG1 
9719  C CG2 . VAL B 86   ? 0.5211 0.5567 0.4136 0.0133  0.0515  -0.0048 84   VAL B CG2 
9720  N N   . GLU B 87   ? 0.4792 0.5503 0.3839 0.0190  0.0706  -0.0032 85   GLU B N   
9721  C CA  . GLU B 87   ? 0.4661 0.5482 0.3774 0.0228  0.0754  -0.0040 85   GLU B CA  
9722  C C   . GLU B 87   ? 0.4631 0.5452 0.3663 0.0274  0.0798  -0.0061 85   GLU B C   
9723  O O   . GLU B 87   ? 0.4265 0.5101 0.3316 0.0331  0.0813  -0.0091 85   GLU B O   
9724  C CB  . GLU B 87   ? 0.5228 0.6173 0.4418 0.0187  0.0785  -0.0001 85   GLU B CB  
9725  C CG  . GLU B 87   ? 0.5075 0.6028 0.4352 0.0147  0.0745  0.0018  85   GLU B CG  
9726  C CD  . GLU B 87   ? 0.6986 0.8064 0.6342 0.0106  0.0775  0.0054  85   GLU B CD  
9727  O OE1 . GLU B 87   ? 0.6855 0.7989 0.6176 0.0085  0.0818  0.0076  85   GLU B OE1 
9728  O OE2 . GLU B 87   ? 0.6624 0.7747 0.6077 0.0095  0.0755  0.0061  85   GLU B OE2 
9729  N N   . GLY B 88   ? 0.4237 0.5038 0.3173 0.0251  0.0819  -0.0046 86   GLY B N   
9730  C CA  . GLY B 88   ? 0.4500 0.5293 0.3347 0.0295  0.0861  -0.0068 86   GLY B CA  
9731  C C   . GLY B 88   ? 0.4012 0.4687 0.2789 0.0340  0.0828  -0.0112 86   GLY B C   
9732  O O   . GLY B 88   ? 0.4381 0.5056 0.3118 0.0394  0.0859  -0.0141 86   GLY B O   
9733  N N   . LEU B 89   ? 0.4093 0.4666 0.2855 0.0319  0.0766  -0.0118 87   LEU B N   
9734  C CA  . LEU B 89   ? 0.4400 0.4862 0.3106 0.0357  0.0729  -0.0159 87   LEU B CA  
9735  C C   . LEU B 89   ? 0.3940 0.4427 0.2728 0.0404  0.0727  -0.0186 87   LEU B C   
9736  O O   . LEU B 89   ? 0.3694 0.4141 0.2436 0.0455  0.0736  -0.0222 87   LEU B O   
9737  C CB  . LEU B 89   ? 0.4511 0.4874 0.3195 0.0320  0.0662  -0.0154 87   LEU B CB  
9738  C CG  . LEU B 89   ? 0.4892 0.5144 0.3534 0.0348  0.0614  -0.0193 87   LEU B CG  
9739  C CD1 . LEU B 89   ? 0.4988 0.5178 0.3503 0.0377  0.0629  -0.0217 87   LEU B CD1 
9740  C CD2 . LEU B 89   ? 0.4994 0.5174 0.3639 0.0309  0.0551  -0.0182 87   LEU B CD2 
9741  N N   . VAL B 90   ? 0.3831 0.4382 0.2737 0.0387  0.0716  -0.0170 88   VAL B N   
9742  C CA  . VAL B 90   ? 0.3813 0.4394 0.2802 0.0428  0.0716  -0.0190 88   VAL B CA  
9743  C C   . VAL B 90   ? 0.4210 0.4870 0.3201 0.0479  0.0776  -0.0202 88   VAL B C   
9744  O O   . VAL B 90   ? 0.3867 0.4501 0.2855 0.0533  0.0780  -0.0235 88   VAL B O   
9745  C CB  . VAL B 90   ? 0.3514 0.4158 0.2623 0.0396  0.0696  -0.0165 88   VAL B CB  
9746  C CG1 . VAL B 90   ? 0.3743 0.4442 0.2942 0.0439  0.0706  -0.0180 88   VAL B CG1 
9747  C CG2 . VAL B 90   ? 0.3400 0.3954 0.2507 0.0360  0.0633  -0.0163 88   VAL B CG2 
9748  N N   . GLN B 91   ? 0.3893 0.4649 0.2887 0.0462  0.0826  -0.0175 89   GLN B N   
9749  C CA  . GLN B 91   ? 0.4280 0.5111 0.3296 0.0502  0.0877  -0.0184 89   GLN B CA  
9750  C C   . GLN B 91   ? 0.4145 0.4890 0.3052 0.0536  0.0886  -0.0216 89   GLN B C   
9751  O O   . GLN B 91   ? 0.4184 0.4923 0.3107 0.0582  0.0897  -0.0244 89   GLN B O   
9752  C CB  . GLN B 91   ? 0.4419 0.5367 0.3483 0.0461  0.0918  -0.0144 89   GLN B CB  
9753  N N   . GLU B 92   ? 0.4046 0.4720 0.2839 0.0513  0.0879  -0.0214 90   GLU B N   
9754  C CA  . GLU B 92   ? 0.4247 0.4843 0.2933 0.0540  0.0888  -0.0244 90   GLU B CA  
9755  C C   . GLU B 92   ? 0.4475 0.4971 0.3137 0.0587  0.0854  -0.0288 90   GLU B C   
9756  O O   . GLU B 92   ? 0.4312 0.4779 0.2940 0.0624  0.0868  -0.0317 90   GLU B O   
9757  C CB  . GLU B 92   ? 0.4141 0.4672 0.2707 0.0504  0.0880  -0.0231 90   GLU B CB  
9758  C CG  . GLU B 92   ? 0.5020 0.5474 0.3472 0.0527  0.0889  -0.0260 90   GLU B CG  
9759  C CD  . GLU B 92   ? 0.4878 0.5260 0.3206 0.0492  0.0875  -0.0247 90   GLU B CD  
9760  O OE1 . GLU B 92   ? 0.5682 0.6076 0.4010 0.0448  0.0862  -0.0213 90   GLU B OE1 
9761  O OE2 . GLU B 92   ? 0.5232 0.5541 0.3460 0.0508  0.0874  -0.0272 90   GLU B OE2 
9762  N N   . TYR B 93   ? 0.3851 0.4294 0.2529 0.0584  0.0808  -0.0294 91   TYR B N   
9763  C CA  . TYR B 93   ? 0.4269 0.4610 0.2920 0.0621  0.0771  -0.0335 91   TYR B CA  
9764  C C   . TYR B 93   ? 0.3815 0.4193 0.2578 0.0646  0.0763  -0.0342 91   TYR B C   
9765  O O   . TYR B 93   ? 0.3859 0.4153 0.2611 0.0671  0.0729  -0.0372 91   TYR B O   
9766  C CB  . TYR B 93   ? 0.3949 0.4179 0.2527 0.0596  0.0716  -0.0343 91   TYR B CB  
9767  C CG  . TYR B 93   ? 0.4006 0.4172 0.2449 0.0585  0.0720  -0.0347 91   TYR B CG  
9768  C CD1 . TYR B 93   ? 0.3816 0.3891 0.2176 0.0612  0.0709  -0.0383 91   TYR B CD1 
9769  C CD2 . TYR B 93   ? 0.4221 0.4416 0.2642 0.0536  0.0725  -0.0310 91   TYR B CD2 
9770  C CE1 . TYR B 93   ? 0.4302 0.4320 0.2545 0.0598  0.0709  -0.0385 91   TYR B CE1 
9771  C CE2 . TYR B 93   ? 0.4568 0.4702 0.2860 0.0526  0.0729  -0.0312 91   TYR B CE2 
9772  C CZ  . TYR B 93   ? 0.4156 0.4204 0.2364 0.0557  0.0719  -0.0350 91   TYR B CZ  
9773  O OH  . TYR B 93   ? 0.4410 0.4400 0.2500 0.0541  0.0717  -0.0350 91   TYR B OH  
9774  N N   . SER B 94   ? 0.3342 0.3842 0.2212 0.0639  0.0792  -0.0314 92   SER B N   
9775  C CA  . SER B 94   ? 0.3743 0.4288 0.2722 0.0663  0.0786  -0.0317 92   SER B CA  
9776  C C   . SER B 94   ? 0.3400 0.3884 0.2397 0.0658  0.0737  -0.0325 92   SER B C   
9777  O O   . SER B 94   ? 0.3512 0.3950 0.2536 0.0689  0.0716  -0.0349 92   SER B O   
9778  C CB  . SER B 94   ? 0.3462 0.3984 0.2441 0.0715  0.0800  -0.0347 92   SER B CB  
9779  O OG  . SER B 94   ? 0.4018 0.4607 0.2989 0.0720  0.0848  -0.0338 92   SER B OG  
9780  N N   . LEU B 95   ? 0.2827 0.3295 0.1828 0.0600  0.0705  -0.0302 93   LEU B N   
9781  C CA  . LEU B 95   ? 0.2878 0.3279 0.1916 0.0574  0.0646  -0.0305 93   LEU B CA  
9782  C C   . LEU B 95   ? 0.2961 0.3440 0.2125 0.0567  0.0641  -0.0286 93   LEU B C   
9783  O O   . LEU B 95   ? 0.3217 0.3803 0.2443 0.0549  0.0670  -0.0256 93   LEU B O   
9784  C CB  . LEU B 95   ? 0.3253 0.3608 0.2252 0.0517  0.0612  -0.0286 93   LEU B CB  
9785  C CG  . LEU B 95   ? 0.2927 0.3203 0.1798 0.0516  0.0610  -0.0300 93   LEU B CG  
9786  C CD1 . LEU B 95   ? 0.3140 0.3373 0.1987 0.0461  0.0570  -0.0279 93   LEU B CD1 
9787  C CD2 . LEU B 95   ? 0.3163 0.3338 0.1966 0.0558  0.0591  -0.0343 93   LEU B CD2 
9788  N N   . SER B 96   ? 0.2590 0.3014 0.1791 0.0576  0.0602  -0.0302 94   SER B N   
9789  C CA  . SER B 96   ? 0.2719 0.3198 0.2030 0.0557  0.0585  -0.0282 94   SER B CA  
9790  C C   . SER B 96   ? 0.2493 0.2964 0.1820 0.0495  0.0551  -0.0257 94   SER B C   
9791  O O   . SER B 96   ? 0.2568 0.2978 0.1821 0.0471  0.0535  -0.0257 94   SER B O   
9792  C CB  . SER B 96   ? 0.2898 0.3313 0.2234 0.0583  0.0553  -0.0306 94   SER B CB  
9793  O OG  . SER B 96   ? 0.2653 0.2960 0.1933 0.0562  0.0508  -0.0322 94   SER B OG  
9794  N N   . SER B 97   ? 0.2367 0.2894 0.1788 0.0471  0.0539  -0.0235 95   SER B N   
9795  C CA  . SER B 97   ? 0.2169 0.2683 0.1607 0.0415  0.0505  -0.0212 95   SER B CA  
9796  C C   . SER B 97   ? 0.2385 0.2787 0.1778 0.0406  0.0456  -0.0232 95   SER B C   
9797  O O   . SER B 97   ? 0.2304 0.2661 0.1646 0.0373  0.0435  -0.0224 95   SER B O   
9798  C CB  . SER B 97   ? 0.3187 0.3773 0.2732 0.0396  0.0498  -0.0190 95   SER B CB  
9799  O OG  . SER B 97   ? 0.3825 0.4521 0.3412 0.0392  0.0539  -0.0167 95   SER B OG  
9800  N N   . GLN B 98   ? 0.2452 0.2807 0.1861 0.0433  0.0436  -0.0256 96   GLN B N   
9801  C CA  . GLN B 98   ? 0.2208 0.2463 0.1581 0.0422  0.0389  -0.0274 96   GLN B CA  
9802  C C   . GLN B 98   ? 0.2215 0.2398 0.1479 0.0430  0.0387  -0.0293 96   GLN B C   
9803  O O   . GLN B 98   ? 0.2172 0.2292 0.1397 0.0404  0.0350  -0.0295 96   GLN B O   
9804  C CB  . GLN B 98   ? 0.2043 0.2263 0.1452 0.0449  0.0371  -0.0296 96   GLN B CB  
9805  C CG  . GLN B 98   ? 0.2223 0.2490 0.1732 0.0435  0.0357  -0.0280 96   GLN B CG  
9806  C CD  . GLN B 98   ? 0.2295 0.2543 0.1824 0.0390  0.0319  -0.0266 96   GLN B CD  
9807  O OE1 . GLN B 98   ? 0.2548 0.2836 0.2085 0.0359  0.0324  -0.0242 96   GLN B OE1 
9808  N NE2 . GLN B 98   ? 0.2396 0.2583 0.1934 0.0385  0.0282  -0.0280 96   GLN B NE2 
9809  N N   . GLU B 99   ? 0.2064 0.2258 0.1276 0.0465  0.0426  -0.0305 97   GLU B N   
9810  C CA  . GLU B 99   ? 0.2254 0.2381 0.1354 0.0471  0.0427  -0.0322 97   GLU B CA  
9811  C C   . GLU B 99   ? 0.2754 0.2898 0.1819 0.0431  0.0429  -0.0295 97   GLU B C   
9812  O O   . GLU B 99   ? 0.2629 0.2701 0.1622 0.0415  0.0400  -0.0301 97   GLU B O   
9813  C CB  . GLU B 99   ? 0.2512 0.2653 0.1565 0.0520  0.0473  -0.0341 97   GLU B CB  
9814  C CG  . GLU B 99   ? 0.2665 0.2746 0.1714 0.0562  0.0462  -0.0375 97   GLU B CG  
9815  C CD  . GLU B 99   ? 0.2767 0.2873 0.1789 0.0617  0.0510  -0.0392 97   GLU B CD  
9816  O OE1 . GLU B 99   ? 0.2989 0.3166 0.1996 0.0623  0.0555  -0.0378 97   GLU B OE1 
9817  O OE2 . GLU B 99   ? 0.2915 0.2966 0.1925 0.0654  0.0504  -0.0420 97   GLU B OE2 
9818  N N   . GLY B 100  ? 0.2337 0.2575 0.1454 0.0413  0.0460  -0.0264 98   GLY B N   
9819  C CA  . GLY B 100  ? 0.2568 0.2817 0.1654 0.0370  0.0459  -0.0235 98   GLY B CA  
9820  C C   . GLY B 100  ? 0.2365 0.2558 0.1461 0.0333  0.0405  -0.0227 98   GLY B C   
9821  O O   . GLY B 100  ? 0.2395 0.2533 0.1420 0.0311  0.0385  -0.0223 98   GLY B O   
9822  N N   . VAL B 101  ? 0.2123 0.2329 0.1307 0.0327  0.0380  -0.0227 99   VAL B N   
9823  C CA  . VAL B 101  ? 0.2309 0.2467 0.1509 0.0295  0.0329  -0.0220 99   VAL B CA  
9824  C C   . VAL B 101  ? 0.2448 0.2508 0.1580 0.0305  0.0292  -0.0248 99   VAL B C   
9825  O O   . VAL B 101  ? 0.2398 0.2410 0.1486 0.0281  0.0260  -0.0241 99   VAL B O   
9826  C CB  . VAL B 101  ? 0.2263 0.2457 0.1569 0.0291  0.0314  -0.0216 99   VAL B CB  
9827  C CG1 . VAL B 101  ? 0.2246 0.2388 0.1565 0.0265  0.0263  -0.0215 99   VAL B CG1 
9828  C CG2 . VAL B 101  ? 0.2224 0.2513 0.1594 0.0274  0.0345  -0.0187 99   VAL B CG2 
9829  N N   . ALA B 102  ? 0.2103 0.2133 0.1223 0.0340  0.0293  -0.0278 100  ALA B N   
9830  C CA  . ALA B 102  ? 0.2496 0.2433 0.1552 0.0348  0.0256  -0.0306 100  ALA B CA  
9831  C C   . ALA B 102  ? 0.2629 0.2522 0.1576 0.0343  0.0257  -0.0307 100  ALA B C   
9832  O O   . ALA B 102  ? 0.2444 0.2272 0.1345 0.0329  0.0215  -0.0314 100  ALA B O   
9833  C CB  . ALA B 102  ? 0.2321 0.2231 0.1373 0.0387  0.0263  -0.0338 100  ALA B CB  
9834  N N   . LEU B 103  ? 0.2213 0.2143 0.1117 0.0356  0.0305  -0.0300 101  LEU B N   
9835  C CA  . LEU B 103  ? 0.2320 0.2209 0.1112 0.0353  0.0312  -0.0299 101  LEU B CA  
9836  C C   . LEU B 103  ? 0.2743 0.2624 0.1521 0.0310  0.0288  -0.0270 101  LEU B C   
9837  O O   . LEU B 103  ? 0.2959 0.2772 0.1652 0.0302  0.0260  -0.0275 101  LEU B O   
9838  C CB  . LEU B 103  ? 0.2582 0.2529 0.1344 0.0374  0.0374  -0.0294 101  LEU B CB  
9839  C CG  . LEU B 103  ? 0.2660 0.2580 0.1309 0.0368  0.0391  -0.0288 101  LEU B CG  
9840  C CD1 . LEU B 103  ? 0.3109 0.2930 0.1663 0.0389  0.0363  -0.0324 101  LEU B CD1 
9841  C CD2 . LEU B 103  ? 0.2788 0.2786 0.1428 0.0386  0.0457  -0.0279 101  LEU B CD2 
9842  N N   . MET B 104  ? 0.2454 0.2398 0.1308 0.0285  0.0296  -0.0240 102  MET B N   
9843  C CA  . MET B 104  ? 0.2666 0.2596 0.1506 0.0245  0.0272  -0.0212 102  MET B CA  
9844  C C   . MET B 104  ? 0.2768 0.2634 0.1620 0.0235  0.0211  -0.0221 102  MET B C   
9845  O O   . MET B 104  ? 0.2755 0.2570 0.1549 0.0216  0.0181  -0.0211 102  MET B O   
9846  C CB  . MET B 104  ? 0.2769 0.2781 0.1686 0.0219  0.0296  -0.0178 102  MET B CB  
9847  C CG  . MET B 104  ? 0.2904 0.2989 0.1810 0.0226  0.0358  -0.0165 102  MET B CG  
9848  S SD  . MET B 104  ? 0.3856 0.3907 0.2627 0.0217  0.0381  -0.0154 102  MET B SD  
9849  C CE  . MET B 104  ? 0.4040 0.4073 0.2806 0.0162  0.0353  -0.0114 102  MET B CE  
9850  N N   . CYS B 105  ? 0.2424 0.2291 0.1347 0.0249  0.0191  -0.0241 103  CYS B N   
9851  C CA  . CYS B 105  ? 0.2343 0.2153 0.1277 0.0242  0.0135  -0.0254 103  CYS B CA  
9852  C C   . CYS B 105  ? 0.2780 0.2512 0.1617 0.0253  0.0110  -0.0276 103  CYS B C   
9853  O O   . CYS B 105  ? 0.2856 0.2540 0.1661 0.0239  0.0066  -0.0274 103  CYS B O   
9854  C CB  . CYS B 105  ? 0.2704 0.2533 0.1728 0.0255  0.0125  -0.0271 103  CYS B CB  
9855  S SG  . CYS B 105  ? 0.2523 0.2432 0.1663 0.0238  0.0139  -0.0245 103  CYS B SG  
9856  N N   . LEU B 106  ? 0.2612 0.2330 0.1399 0.0281  0.0134  -0.0300 104  LEU B N   
9857  C CA  . LEU B 106  ? 0.2695 0.2336 0.1378 0.0292  0.0112  -0.0323 104  LEU B CA  
9858  C C   . LEU B 106  ? 0.3103 0.2721 0.1698 0.0274  0.0111  -0.0302 104  LEU B C   
9859  O O   . LEU B 106  ? 0.3100 0.2655 0.1637 0.0266  0.0068  -0.0307 104  LEU B O   
9860  C CB  . LEU B 106  ? 0.2873 0.2504 0.1511 0.0327  0.0147  -0.0350 104  LEU B CB  
9861  C CG  . LEU B 106  ? 0.3132 0.2683 0.1647 0.0339  0.0131  -0.0374 104  LEU B CG  
9862  C CD1 . LEU B 106  ? 0.3394 0.2881 0.1909 0.0333  0.0069  -0.0397 104  LEU B CD1 
9863  C CD2 . LEU B 106  ? 0.3379 0.2925 0.1842 0.0376  0.0175  -0.0398 104  LEU B CD2 
9864  N N   . ALA B 107  ? 0.2637 0.2307 0.1224 0.0267  0.0158  -0.0276 105  ALA B N   
9865  C CA  . ALA B 107  ? 0.2965 0.2613 0.1466 0.0247  0.0161  -0.0252 105  ALA B CA  
9866  C C   . ALA B 107  ? 0.3131 0.2751 0.1650 0.0217  0.0112  -0.0232 105  ALA B C   
9867  O O   . ALA B 107  ? 0.3295 0.2853 0.1729 0.0209  0.0081  -0.0228 105  ALA B O   
9868  C CB  . ALA B 107  ? 0.3302 0.3022 0.1809 0.0239  0.0221  -0.0225 105  ALA B CB  
9869  N N   . GLU B 108  ? 0.2846 0.2508 0.1470 0.0204  0.0103  -0.0219 106  GLU B N   
9870  C CA  . GLU B 108  ? 0.2941 0.2577 0.1589 0.0181  0.0056  -0.0203 106  GLU B CA  
9871  C C   . GLU B 108  ? 0.3441 0.3009 0.2056 0.0191  0.0000  -0.0226 106  GLU B C   
9872  O O   . GLU B 108  ? 0.3515 0.3035 0.2078 0.0179  -0.0037 -0.0215 106  GLU B O   
9873  C CB  . GLU B 108  ? 0.2959 0.2651 0.1728 0.0172  0.0056  -0.0193 106  GLU B CB  
9874  C CG  . GLU B 108  ? 0.3269 0.2933 0.2072 0.0156  0.0004  -0.0185 106  GLU B CG  
9875  C CD  . GLU B 108  ? 0.3506 0.3215 0.2425 0.0154  -0.0001 -0.0186 106  GLU B CD  
9876  O OE1 . GLU B 108  ? 0.3192 0.2960 0.2168 0.0159  0.0037  -0.0186 106  GLU B OE1 
9877  O OE2 . GLU B 108  ? 0.3569 0.3257 0.2523 0.0149  -0.0044 -0.0186 106  GLU B OE2 
9878  N N   . ALA B 109  ? 0.3079 0.2642 0.1723 0.0212  -0.0010 -0.0259 107  ALA B N   
9879  C CA  . ALA B 109  ? 0.3678 0.3183 0.2299 0.0218  -0.0064 -0.0282 107  ALA B CA  
9880  C C   . ALA B 109  ? 0.3604 0.3044 0.2097 0.0222  -0.0077 -0.0289 107  ALA B C   
9881  O O   . ALA B 109  ? 0.3849 0.3241 0.2305 0.0216  -0.0127 -0.0290 107  ALA B O   
9882  C CB  . ALA B 109  ? 0.3399 0.2909 0.2073 0.0235  -0.0068 -0.0315 107  ALA B CB  
9883  N N   . LEU B 110  ? 0.3096 0.2537 0.1519 0.0234  -0.0032 -0.0293 108  LEU B N   
9884  C CA  . LEU B 110  ? 0.3641 0.3020 0.1934 0.0239  -0.0040 -0.0300 108  LEU B CA  
9885  C C   . LEU B 110  ? 0.3901 0.3259 0.2139 0.0217  -0.0052 -0.0266 108  LEU B C   
9886  O O   . LEU B 110  ? 0.4381 0.3676 0.2525 0.0216  -0.0086 -0.0269 108  LEU B O   
9887  C CB  . LEU B 110  ? 0.3534 0.2923 0.1767 0.0259  0.0017  -0.0311 108  LEU B CB  
9888  C CG  . LEU B 110  ? 0.3682 0.3061 0.1930 0.0287  0.0022  -0.0351 108  LEU B CG  
9889  C CD1 . LEU B 110  ? 0.3932 0.3343 0.2151 0.0311  0.0087  -0.0358 108  LEU B CD1 
9890  C CD2 . LEU B 110  ? 0.4181 0.3476 0.2347 0.0294  -0.0028 -0.0381 108  LEU B CD2 
9891  N N   . LEU B 111  ? 0.3974 0.3381 0.2266 0.0197  -0.0029 -0.0233 109  LEU B N   
9892  C CA  . LEU B 111  ? 0.4144 0.3525 0.2382 0.0174  -0.0042 -0.0198 109  LEU B CA  
9893  C C   . LEU B 111  ? 0.4158 0.3500 0.2421 0.0166  -0.0107 -0.0194 109  LEU B C   
9894  O O   . LEU B 111  ? 0.4776 0.4078 0.2980 0.0151  -0.0129 -0.0169 109  LEU B O   
9895  C CB  . LEU B 111  ? 0.4333 0.3774 0.2616 0.0153  0.0005  -0.0165 109  LEU B CB  
9896  C CG  . LEU B 111  ? 0.3648 0.3126 0.1884 0.0158  0.0070  -0.0161 109  LEU B CG  
9897  C CD1 . LEU B 111  ? 0.3763 0.3315 0.2063 0.0135  0.0114  -0.0130 109  LEU B CD1 
9898  C CD2 . LEU B 111  ? 0.4331 0.3752 0.2426 0.0156  0.0073  -0.0154 109  LEU B CD2 
9899  N N   . ARG B 112  ? 0.3923 0.3276 0.2270 0.0177  -0.0139 -0.0218 110  ARG B N   
9900  C CA  . ARG B 112  ? 0.4338 0.3659 0.2708 0.0174  -0.0202 -0.0219 110  ARG B CA  
9901  C C   . ARG B 112  ? 0.4852 0.4105 0.3127 0.0184  -0.0246 -0.0237 110  ARG B C   
9902  O O   . ARG B 112  ? 0.5185 0.4408 0.3461 0.0183  -0.0301 -0.0235 110  ARG B O   
9903  C CB  . ARG B 112  ? 0.4123 0.3486 0.2617 0.0180  -0.0217 -0.0238 110  ARG B CB  
9904  C CG  . ARG B 112  ? 0.4093 0.3519 0.2684 0.0170  -0.0183 -0.0219 110  ARG B CG  
9905  C CD  . ARG B 112  ? 0.4553 0.4024 0.3254 0.0178  -0.0184 -0.0240 110  ARG B CD  
9906  N NE  . ARG B 112  ? 0.5887 0.5346 0.4638 0.0180  -0.0239 -0.0251 110  ARG B NE  
9907  C CZ  . ARG B 112  ? 0.5625 0.5108 0.4451 0.0173  -0.0255 -0.0237 110  ARG B CZ  
9908  N NH1 . ARG B 112  ? 0.5732 0.5245 0.4588 0.0160  -0.0225 -0.0211 110  ARG B NH1 
9909  N NH2 . ARG B 112  ? 0.6037 0.5513 0.4906 0.0178  -0.0303 -0.0249 110  ARG B NH2 
9910  N N   . ILE B 113  ? 0.4265 0.3496 0.2458 0.0195  -0.0224 -0.0255 111  ILE B N   
9911  C CA  . ILE B 113  ? 0.4733 0.3894 0.2814 0.0202  -0.0260 -0.0269 111  ILE B CA  
9912  C C   . ILE B 113  ? 0.5387 0.4514 0.3363 0.0190  -0.0249 -0.0236 111  ILE B C   
9913  O O   . ILE B 113  ? 0.5411 0.4553 0.3340 0.0188  -0.0192 -0.0226 111  ILE B O   
9914  C CB  . ILE B 113  ? 0.5024 0.4169 0.3057 0.0220  -0.0242 -0.0305 111  ILE B CB  
9915  C CG1 . ILE B 113  ? 0.4555 0.3730 0.2692 0.0229  -0.0253 -0.0334 111  ILE B CG1 
9916  C CG2 . ILE B 113  ? 0.5313 0.4382 0.3221 0.0226  -0.0281 -0.0319 111  ILE B CG2 
9917  C CD1 . ILE B 113  ? 0.5314 0.4475 0.3415 0.0248  -0.0226 -0.0368 111  ILE B CD1 
9918  N N   . PRO B 114  ? 0.5343 0.4424 0.3280 0.0183  -0.0298 -0.0219 112  PRO B N   
9919  C CA  . PRO B 114  ? 0.5711 0.4757 0.3549 0.0169  -0.0286 -0.0183 112  PRO B CA  
9920  C C   . PRO B 114  ? 0.5547 0.4543 0.3244 0.0175  -0.0273 -0.0190 112  PRO B C   
9921  O O   . PRO B 114  ? 0.6221 0.5209 0.3843 0.0162  -0.0233 -0.0163 112  PRO B O   
9922  C CB  . PRO B 114  ? 0.5385 0.4391 0.3226 0.0165  -0.0352 -0.0167 112  PRO B CB  
9923  C CG  . PRO B 114  ? 0.5747 0.4753 0.3642 0.0182  -0.0403 -0.0202 112  PRO B CG  
9924  C CD  . PRO B 114  ? 0.5574 0.4643 0.3565 0.0187  -0.0366 -0.0227 112  PRO B CD  
9925  N N   . ASP B 115  ? 0.5450 0.4411 0.3105 0.0192  -0.0304 -0.0225 113  ASP B N   
9926  C CA  . ASP B 115  ? 0.6411 0.5316 0.3922 0.0199  -0.0299 -0.0235 113  ASP B CA  
9927  C C   . ASP B 115  ? 0.6101 0.5038 0.3593 0.0209  -0.0229 -0.0250 113  ASP B C   
9928  O O   . ASP B 115  ? 0.5757 0.4719 0.3309 0.0224  -0.0220 -0.0284 113  ASP B O   
9929  C CB  . ASP B 115  ? 0.6053 0.4906 0.3525 0.0212  -0.0364 -0.0267 113  ASP B CB  
9930  C CG  . ASP B 115  ? 0.6548 0.5339 0.3868 0.0221  -0.0360 -0.0282 113  ASP B CG  
9931  O OD1 . ASP B 115  ? 0.7232 0.5994 0.4453 0.0212  -0.0342 -0.0254 113  ASP B OD1 
9932  O OD2 . ASP B 115  ? 0.6813 0.5588 0.4123 0.0234  -0.0374 -0.0321 113  ASP B OD2 
9933  N N   . THR B 116  ? 0.5990 0.4926 0.3398 0.0200  -0.0178 -0.0226 114  THR B N   
9934  C CA  . THR B 116  ? 0.6201 0.5174 0.3590 0.0212  -0.0108 -0.0238 114  THR B CA  
9935  C C   . THR B 116  ? 0.6386 0.5321 0.3715 0.0239  -0.0116 -0.0285 114  THR B C   
9936  O O   . THR B 116  ? 0.6111 0.5083 0.3488 0.0257  -0.0079 -0.0311 114  THR B O   
9937  C CB  . THR B 116  ? 0.6933 0.5904 0.4222 0.0198  -0.0059 -0.0205 114  THR B CB  
9938  O OG1 . THR B 116  ? 0.7243 0.6241 0.4584 0.0170  -0.0054 -0.0161 114  THR B OG1 
9939  C CG2 . THR B 116  ? 0.6591 0.5615 0.3874 0.0212  0.0018  -0.0216 114  THR B CG2 
9940  N N   . ALA B 117  ? 0.6525 0.5381 0.3746 0.0242  -0.0166 -0.0297 115  ALA B N   
9941  C CA  . ALA B 117  ? 0.6224 0.5052 0.3408 0.0261  -0.0173 -0.0337 115  ALA B CA  
9942  C C   . ALA B 117  ? 0.5877 0.4710 0.3150 0.0273  -0.0207 -0.0375 115  ALA B C   
9943  O O   . ALA B 117  ? 0.6458 0.5292 0.3737 0.0291  -0.0184 -0.0408 115  ALA B O   
9944  C CB  . ALA B 117  ? 0.6169 0.4937 0.3269 0.0254  -0.0221 -0.0334 115  ALA B CB  
9945  N N   . THR B 118  ? 0.5965 0.4804 0.3318 0.0262  -0.0259 -0.0368 116  THR B N   
9946  C CA  . THR B 118  ? 0.5699 0.4559 0.3162 0.0268  -0.0286 -0.0397 116  THR B CA  
9947  C C   . THR B 118  ? 0.5614 0.4545 0.3178 0.0275  -0.0225 -0.0400 116  THR B C   
9948  O O   . THR B 118  ? 0.5731 0.4664 0.3330 0.0290  -0.0219 -0.0433 116  THR B O   
9949  C CB  . THR B 118  ? 0.5697 0.4569 0.3248 0.0253  -0.0348 -0.0383 116  THR B CB  
9950  O OG1 . THR B 118  ? 0.6684 0.5493 0.4139 0.0248  -0.0405 -0.0378 116  THR B OG1 
9951  C CG2 . THR B 118  ? 0.5566 0.4456 0.3220 0.0256  -0.0379 -0.0415 116  THR B CG2 
9952  N N   . ARG B 119  ? 0.5578 0.4565 0.3188 0.0265  -0.0182 -0.0364 117  ARG B N   
9953  C CA  . ARG B 119  ? 0.5229 0.4289 0.2937 0.0271  -0.0125 -0.0362 117  ARG B CA  
9954  C C   . ARG B 119  ? 0.5487 0.4543 0.3131 0.0296  -0.0072 -0.0387 117  ARG B C   
9955  O O   . ARG B 119  ? 0.4996 0.4073 0.2700 0.0314  -0.0055 -0.0413 117  ARG B O   
9956  C CB  . ARG B 119  ? 0.4919 0.4034 0.2668 0.0251  -0.0091 -0.0317 117  ARG B CB  
9957  C CG  . ARG B 119  ? 0.4357 0.3554 0.2216 0.0254  -0.0037 -0.0311 117  ARG B CG  
9958  C CD  . ARG B 119  ? 0.4825 0.4068 0.2689 0.0234  0.0004  -0.0268 117  ARG B CD  
9959  N NE  . ARG B 119  ? 0.4961 0.4186 0.2842 0.0208  -0.0040 -0.0239 117  ARG B NE  
9960  C CZ  . ARG B 119  ? 0.5569 0.4781 0.3389 0.0187  -0.0031 -0.0203 117  ARG B CZ  
9961  N NH1 . ARG B 119  ? 0.5362 0.4582 0.3101 0.0185  0.0021  -0.0189 117  ARG B NH1 
9962  N NH2 . ARG B 119  ? 0.5336 0.4525 0.3175 0.0168  -0.0075 -0.0179 117  ARG B NH2 
9963  N N   . ASP B 120  ? 0.5520 0.4549 0.3040 0.0300  -0.0043 -0.0378 118  ASP B N   
9964  C CA  . ASP B 120  ? 0.5960 0.4987 0.3413 0.0327  0.0011  -0.0401 118  ASP B CA  
9965  C C   . ASP B 120  ? 0.5533 0.4496 0.2943 0.0349  -0.0019 -0.0451 118  ASP B C   
9966  O O   . ASP B 120  ? 0.5336 0.4314 0.2761 0.0374  0.0019  -0.0476 118  ASP B O   
9967  C CB  . ASP B 120  ? 0.5713 0.4717 0.3031 0.0324  0.0043  -0.0382 118  ASP B CB  
9968  C CG  . ASP B 120  ? 0.6522 0.5593 0.3879 0.0300  0.0084  -0.0333 118  ASP B CG  
9969  O OD1 . ASP B 120  ? 0.6160 0.5301 0.3648 0.0291  0.0098  -0.0319 118  ASP B OD1 
9970  O OD2 . ASP B 120  ? 0.7126 0.6177 0.4381 0.0288  0.0101  -0.0309 118  ASP B OD2 
9971  N N   . ALA B 121  ? 0.5710 0.4614 0.3094 0.0337  -0.0089 -0.0461 119  ALA B N   
9972  C CA  . ALA B 121  ? 0.6135 0.4994 0.3518 0.0347  -0.0121 -0.0502 119  ALA B CA  
9973  C C   . ALA B 121  ? 0.6021 0.4900 0.3507 0.0356  -0.0128 -0.0524 119  ALA B C   
9974  O O   . ALA B 121  ? 0.5668 0.4532 0.3163 0.0374  -0.0115 -0.0555 119  ALA B O   
9975  C CB  . ALA B 121  ? 0.6082 0.4885 0.3429 0.0328  -0.0196 -0.0504 119  ALA B CB  
9976  N N   . LEU B 122  ? 0.5334 0.4262 0.2929 0.0339  -0.0145 -0.0502 120  LEU B N   
9977  C CA  . LEU B 122  ? 0.5617 0.4582 0.3340 0.0341  -0.0148 -0.0515 120  LEU B CA  
9978  C C   . LEU B 122  ? 0.5548 0.4560 0.3306 0.0365  -0.0078 -0.0519 120  LEU B C   
9979  O O   . LEU B 122  ? 0.5381 0.4388 0.3182 0.0380  -0.0073 -0.0546 120  LEU B O   
9980  C CB  . LEU B 122  ? 0.5256 0.4275 0.3098 0.0316  -0.0175 -0.0485 120  LEU B CB  
9981  C CG  . LEU B 122  ? 0.5095 0.4155 0.3072 0.0315  -0.0180 -0.0494 120  LEU B CG  
9982  C CD1 . LEU B 122  ? 0.5845 0.4851 0.3819 0.0312  -0.0237 -0.0529 120  LEU B CD1 
9983  C CD2 . LEU B 122  ? 0.5014 0.4138 0.3104 0.0295  -0.0188 -0.0461 120  LEU B CD2 
9984  N N   . ILE B 123  ? 0.4859 0.3918 0.2598 0.0367  -0.0023 -0.0491 121  ILE B N   
9985  C CA  . ILE B 123  ? 0.5303 0.4417 0.3074 0.0391  0.0046  -0.0492 121  ILE B CA  
9986  C C   . ILE B 123  ? 0.5468 0.4526 0.3144 0.0426  0.0066  -0.0532 121  ILE B C   
9987  O O   . ILE B 123  ? 0.5659 0.4726 0.3381 0.0450  0.0087  -0.0555 121  ILE B O   
9988  C CB  . ILE B 123  ? 0.4719 0.3895 0.2480 0.0382  0.0098  -0.0452 121  ILE B CB  
9989  C CG1 . ILE B 123  ? 0.4561 0.3794 0.2430 0.0351  0.0082  -0.0414 121  ILE B CG1 
9990  C CG2 . ILE B 123  ? 0.4644 0.3875 0.2415 0.0411  0.0171  -0.0457 121  ILE B CG2 
9991  C CD1 . ILE B 123  ? 0.4519 0.3798 0.2367 0.0333  0.0120  -0.0373 121  ILE B CD1 
9992  N N   . ARG B 124  ? 0.5594 0.4595 0.3146 0.0426  0.0058  -0.0540 122  ARG B N   
9993  C CA  . ARG B 124  ? 0.5942 0.4915 0.3442 0.0450  0.0083  -0.0567 122  ARG B CA  
9994  C C   . ARG B 124  ? 0.6372 0.5283 0.3890 0.0455  0.0037  -0.0605 122  ARG B C   
9995  O O   . ARG B 124  ? 0.6824 0.5727 0.4350 0.0480  0.0064  -0.0629 122  ARG B O   
9996  C CB  . ARG B 124  ? 0.6274 0.5215 0.3663 0.0442  0.0084  -0.0558 122  ARG B CB  
9997  N N   . ASP B 125  ? 0.6311 0.5182 0.3840 0.0430  -0.0031 -0.0608 123  ASP B N   
9998  C CA  . ASP B 125  ? 0.6824 0.5632 0.4357 0.0427  -0.0079 -0.0642 123  ASP B CA  
9999  C C   . ASP B 125  ? 0.6314 0.5133 0.3951 0.0422  -0.0104 -0.0652 123  ASP B C   
10000 O O   . ASP B 125  ? 0.6847 0.5619 0.4496 0.0420  -0.0135 -0.0680 123  ASP B O   
10001 C CB  . ASP B 125  ? 0.7459 0.6215 0.4931 0.0401  -0.0141 -0.0642 123  ASP B CB  
10002 C CG  . ASP B 125  ? 0.7534 0.6278 0.4899 0.0404  -0.0118 -0.0628 123  ASP B CG  
10003 O OD1 . ASP B 125  ? 0.7290 0.6041 0.4612 0.0428  -0.0063 -0.0636 123  ASP B OD1 
10004 O OD2 . ASP B 125  ? 0.8142 0.6873 0.5470 0.0382  -0.0155 -0.0609 123  ASP B OD2 
10005 N N   . LYS B 126  ? 0.6080 0.4958 0.3791 0.0418  -0.0092 -0.0631 124  LYS B N   
10006 C CA  . LYS B 126  ? 0.6111 0.5006 0.3931 0.0411  -0.0114 -0.0638 124  LYS B CA  
10007 C C   . LYS B 126  ? 0.6433 0.5409 0.4353 0.0425  -0.0057 -0.0620 124  LYS B C   
10008 O O   . LYS B 126  ? 0.7213 0.6185 0.5181 0.0441  -0.0046 -0.0638 124  LYS B O   
10009 C CB  . LYS B 126  ? 0.6613 0.5529 0.4501 0.0374  -0.0171 -0.0617 124  LYS B CB  
10010 N N   . ILE B 127  ? 0.5572 0.4620 0.3523 0.0419  -0.0023 -0.0582 125  ILE B N   
10011 C CA  . ILE B 127  ? 0.5634 0.4769 0.3695 0.0426  0.0023  -0.0561 125  ILE B CA  
10012 C C   . ILE B 127  ? 0.5804 0.4946 0.3832 0.0466  0.0083  -0.0577 125  ILE B C   
10013 O O   . ILE B 127  ? 0.5377 0.4556 0.3488 0.0482  0.0106  -0.0581 125  ILE B O   
10014 C CB  . ILE B 127  ? 0.4998 0.4203 0.3097 0.0404  0.0039  -0.0517 125  ILE B CB  
10015 C CG1 . ILE B 127  ? 0.4993 0.4177 0.3099 0.0370  -0.0021 -0.0503 125  ILE B CG1 
10016 C CG2 . ILE B 127  ? 0.4604 0.3897 0.2831 0.0404  0.0073  -0.0495 125  ILE B CG2 
10017 C CD1 . ILE B 127  ? 0.5543 0.4738 0.3757 0.0354  -0.0064 -0.0506 125  ILE B CD1 
10018 N N   . ALA B 128  ? 0.5710 0.4822 0.3619 0.0485  0.0111  -0.0587 126  ALA B N   
10019 C CA  . ALA B 128  ? 0.5436 0.4568 0.3315 0.0527  0.0175  -0.0599 126  ALA B CA  
10020 C C   . ALA B 128  ? 0.6411 0.5495 0.4306 0.0551  0.0169  -0.0635 126  ALA B C   
10021 O O   . ALA B 128  ? 0.5902 0.5024 0.3830 0.0582  0.0217  -0.0638 126  ALA B O   
10022 C CB  . ALA B 128  ? 0.5987 0.5106 0.3760 0.0532  0.0201  -0.0596 126  ALA B CB  
10023 N N   . ASP B 129  ? 0.7429 0.6437 0.5311 0.0535  0.0109  -0.0657 127  ASP B N   
10024 C CA  . ASP B 129  ? 0.8288 0.7245 0.6188 0.0550  0.0098  -0.0687 127  ASP B CA  
10025 C C   . ASP B 129  ? 0.8195 0.7176 0.6199 0.0549  0.0088  -0.0686 127  ASP B C   
10026 O O   . ASP B 129  ? 0.8946 0.7903 0.6983 0.0520  0.0035  -0.0689 127  ASP B O   
10027 C CB  . ASP B 129  ? 0.8943 0.7808 0.6779 0.0530  0.0040  -0.0711 127  ASP B CB  
10028 C CG  . ASP B 129  ? 0.9399 0.8231 0.7126 0.0536  0.0052  -0.0717 127  ASP B CG  
10029 O OD1 . ASP B 129  ? 0.9614 0.8454 0.7313 0.0568  0.0101  -0.0725 127  ASP B OD1 
10030 O OD2 . ASP B 129  ? 0.9617 0.8418 0.7290 0.0510  0.0012  -0.0714 127  ASP B OD2 
10031 N N   . ASN B 131  ? 0.7909 0.6959 0.6156 0.0476  0.0004  -0.0651 129  ASN B N   
10032 C CA  . ASN B 131  ? 0.7917 0.6935 0.6198 0.0440  -0.0060 -0.0655 129  ASN B CA  
10033 C C   . ASN B 131  ? 0.7429 0.6510 0.5767 0.0407  -0.0080 -0.0620 129  ASN B C   
10034 O O   . ASN B 131  ? 0.7646 0.6701 0.5974 0.0380  -0.0132 -0.0622 129  ASN B O   
10035 C CB  . ASN B 131  ? 0.7268 0.6185 0.5435 0.0436  -0.0102 -0.0690 129  ASN B CB  
10036 N N   . TRP B 132  ? 0.6651 0.5816 0.5048 0.0411  -0.0038 -0.0589 130  TRP B N   
10037 C CA  . TRP B 132  ? 0.6232 0.5452 0.4675 0.0383  -0.0051 -0.0555 130  TRP B CA  
10038 C C   . TRP B 132  ? 0.6454 0.5691 0.4996 0.0355  -0.0096 -0.0548 130  TRP B C   
10039 O O   . TRP B 132  ? 0.6725 0.5979 0.5285 0.0331  -0.0127 -0.0529 130  TRP B O   
10040 C CB  . TRP B 132  ? 0.5384 0.4687 0.3874 0.0392  0.0004  -0.0524 130  TRP B CB  
10041 C CG  . TRP B 132  ? 0.5190 0.4543 0.3780 0.0404  0.0032  -0.0520 130  TRP B CG  
10042 C CD1 . TRP B 132  ? 0.5279 0.4631 0.3861 0.0438  0.0071  -0.0536 130  TRP B CD1 
10043 C CD2 . TRP B 132  ? 0.4544 0.3952 0.3252 0.0384  0.0020  -0.0500 130  TRP B CD2 
10044 N NE1 . TRP B 132  ? 0.4518 0.3921 0.3205 0.0440  0.0083  -0.0525 130  TRP B NE1 
10045 C CE2 . TRP B 132  ? 0.4413 0.3850 0.3178 0.0406  0.0053  -0.0503 130  TRP B CE2 
10046 C CE3 . TRP B 132  ? 0.4572 0.4005 0.3339 0.0352  -0.0016 -0.0480 130  TRP B CE3 
10047 C CZ2 . TRP B 132  ? 0.3942 0.3433 0.2818 0.0395  0.0051  -0.0486 130  TRP B CZ2 
10048 C CZ3 . TRP B 132  ? 0.3821 0.3308 0.2700 0.0342  -0.0015 -0.0465 130  TRP B CZ3 
10049 C CH2 . TRP B 132  ? 0.3996 0.3511 0.2927 0.0362  0.0018  -0.0468 130  TRP B CH2 
10050 N N   . LYS B 133  ? 0.6599 0.5832 0.5204 0.0358  -0.0100 -0.0561 131  LYS B N   
10051 C CA  . LYS B 133  ? 0.6662 0.5927 0.5373 0.0332  -0.0133 -0.0551 131  LYS B CA  
10052 C C   . LYS B 133  ? 0.7699 0.6928 0.6392 0.0305  -0.0195 -0.0559 131  LYS B C   
10053 O O   . LYS B 133  ? 0.7977 0.7247 0.6744 0.0283  -0.0222 -0.0542 131  LYS B O   
10054 C CB  . LYS B 133  ? 0.6404 0.5659 0.5169 0.0340  -0.0126 -0.0566 131  LYS B CB  
10055 C CG  . LYS B 133  ? 0.6371 0.5665 0.5163 0.0369  -0.0069 -0.0558 131  LYS B CG  
10056 C CD  . LYS B 133  ? 0.6368 0.5654 0.5223 0.0375  -0.0067 -0.0568 131  LYS B CD  
10057 C CE  . LYS B 133  ? 0.5753 0.5089 0.4646 0.0404  -0.0013 -0.0556 131  LYS B CE  
10058 N NZ  . LYS B 133  ? 0.5577 0.4957 0.4578 0.0395  -0.0013 -0.0541 131  LYS B NZ  
10059 N N   . SER B 134  ? 0.8057 0.7210 0.6651 0.0309  -0.0219 -0.0587 132  SER B N   
10060 C CA  . SER B 134  ? 0.8141 0.7258 0.6715 0.0284  -0.0282 -0.0598 132  SER B CA  
10061 C C   . SER B 134  ? 0.8556 0.7664 0.7053 0.0281  -0.0297 -0.0586 132  SER B C   
10062 O O   . SER B 134  ? 0.8286 0.7335 0.6705 0.0275  -0.0337 -0.0606 132  SER B O   
10063 C CB  . SER B 134  ? 0.8208 0.7243 0.6720 0.0285  -0.0307 -0.0636 132  SER B CB  
10064 N N   . HIS B 135  ? 0.8711 0.7873 0.7227 0.0284  -0.0268 -0.0555 133  HIS B N   
10065 C CA  . HIS B 135  ? 0.8698 0.7845 0.7134 0.0281  -0.0280 -0.0541 133  HIS B CA  
10066 C C   . HIS B 135  ? 0.8319 0.7530 0.6811 0.0271  -0.0267 -0.0502 133  HIS B C   
10067 O O   . HIS B 135  ? 0.8880 0.8079 0.7328 0.0262  -0.0293 -0.0488 133  HIS B O   
10068 C CB  . HIS B 135  ? 0.8186 0.7292 0.6504 0.0304  -0.0241 -0.0552 133  HIS B CB  
10069 C CG  . HIS B 135  ? 0.8797 0.7819 0.7018 0.0311  -0.0267 -0.0589 133  HIS B CG  
10070 N ND1 . HIS B 135  ? 0.8749 0.7734 0.6938 0.0333  -0.0240 -0.0618 133  HIS B ND1 
10071 C CD2 . HIS B 135  ? 0.9280 0.8245 0.7427 0.0300  -0.0320 -0.0604 133  HIS B CD2 
10072 C CE1 . HIS B 135  ? 0.9239 0.8144 0.7335 0.0333  -0.0275 -0.0649 133  HIS B CE1 
10073 N NE2 . HIS B 135  ? 0.9345 0.8238 0.7414 0.0312  -0.0325 -0.0641 133  HIS B NE2 
10074 N N   . LEU B 136  ? 0.8064 0.7336 0.6645 0.0274  -0.0230 -0.0486 134  LEU B N   
10075 C CA  . LEU B 136  ? 0.7483 0.6809 0.6107 0.0264  -0.0215 -0.0449 134  LEU B CA  
10076 C C   . LEU B 136  ? 0.7596 0.6981 0.6348 0.0252  -0.0221 -0.0436 134  LEU B C   
10077 O O   . LEU B 136  ? 0.7014 0.6423 0.5803 0.0239  -0.0241 -0.0414 134  LEU B O   
10078 C CB  . LEU B 136  ? 0.6288 0.5640 0.4876 0.0277  -0.0154 -0.0434 134  LEU B CB  
10079 C CG  . LEU B 136  ? 0.5984 0.5296 0.4448 0.0282  -0.0145 -0.0429 134  LEU B CG  
10080 C CD1 . LEU B 136  ? 0.5099 0.4453 0.3550 0.0292  -0.0081 -0.0411 134  LEU B CD1 
10081 C CD2 . LEU B 136  ? 0.5587 0.4884 0.4027 0.0262  -0.0186 -0.0409 134  LEU B CD2 
10082 N N   . GLY B 137  ? 0.7636 0.7040 0.6452 0.0259  -0.0202 -0.0449 135  GLY B N   
10083 C CA  . GLY B 137  ? 0.7340 0.6796 0.6272 0.0248  -0.0208 -0.0438 135  GLY B CA  
10084 C C   . GLY B 137  ? 0.7718 0.7161 0.6688 0.0232  -0.0265 -0.0449 135  GLY B C   
10085 O O   . GLY B 137  ? 0.7807 0.7234 0.6746 0.0223  -0.0302 -0.0443 135  GLY B O   
10086 N N   . GLY B 138  ? 0.7588 0.7040 0.6624 0.0227  -0.0272 -0.0463 136  GLY B N   
10087 C CA  . GLY B 138  ? 0.7704 0.7152 0.6783 0.0210  -0.0324 -0.0473 136  GLY B CA  
10088 C C   . GLY B 138  ? 0.6905 0.6414 0.6080 0.0198  -0.0335 -0.0452 136  GLY B C   
10089 O O   . GLY B 138  ? 0.6914 0.6465 0.6169 0.0197  -0.0313 -0.0444 136  GLY B O   
10090 N N   . SER B 139  ? 0.5817 0.5328 0.4981 0.0192  -0.0369 -0.0441 137  SER B N   
10091 C CA  . SER B 139  ? 0.5411 0.4976 0.4661 0.0185  -0.0381 -0.0422 137  SER B CA  
10092 C C   . SER B 139  ? 0.5274 0.4874 0.4546 0.0191  -0.0338 -0.0397 137  SER B C   
10093 O O   . SER B 139  ? 0.5043 0.4690 0.4400 0.0186  -0.0329 -0.0386 137  SER B O   
10094 C CB  . SER B 139  ? 0.5543 0.5097 0.4771 0.0182  -0.0430 -0.0418 137  SER B CB  
10095 O OG  . SER B 139  ? 0.5864 0.5400 0.5092 0.0173  -0.0474 -0.0441 137  SER B OG  
10096 N N   . ARG B 140  ? 0.4794 0.4373 0.3992 0.0198  -0.0311 -0.0387 138  ARG B N   
10097 C CA  . ARG B 140  ? 0.4914 0.4525 0.4126 0.0200  -0.0269 -0.0362 138  ARG B CA  
10098 C C   . ARG B 140  ? 0.4544 0.4157 0.3732 0.0211  -0.0221 -0.0368 138  ARG B C   
10099 O O   . ARG B 140  ? 0.4661 0.4233 0.3765 0.0220  -0.0214 -0.0380 138  ARG B O   
10100 C CB  . ARG B 140  ? 0.5000 0.4593 0.4149 0.0198  -0.0276 -0.0341 138  ARG B CB  
10101 C CG  . ARG B 140  ? 0.5397 0.5018 0.4547 0.0195  -0.0233 -0.0315 138  ARG B CG  
10102 C CD  . ARG B 140  ? 0.5937 0.5526 0.5006 0.0190  -0.0239 -0.0295 138  ARG B CD  
10103 N NE  . ARG B 140  ? 0.6036 0.5652 0.5106 0.0182  -0.0200 -0.0268 138  ARG B NE  
10104 C CZ  . ARG B 140  ? 0.6045 0.5667 0.5068 0.0184  -0.0156 -0.0263 138  ARG B CZ  
10105 N NH1 . ARG B 140  ? 0.5650 0.5249 0.4618 0.0198  -0.0144 -0.0283 138  ARG B NH1 
10106 N NH2 . ARG B 140  ? 0.5653 0.5307 0.4687 0.0173  -0.0124 -0.0236 138  ARG B NH2 
10107 N N   . SER B 141  ? 0.3897 0.3556 0.3155 0.0212  -0.0189 -0.0360 139  SER B N   
10108 C CA  . SER B 141  ? 0.3535 0.3204 0.2777 0.0226  -0.0142 -0.0362 139  SER B CA  
10109 C C   . SER B 141  ? 0.3542 0.3206 0.2710 0.0230  -0.0116 -0.0347 139  SER B C   
10110 O O   . SER B 141  ? 0.3519 0.3194 0.2681 0.0218  -0.0120 -0.0324 139  SER B O   
10111 C CB  . SER B 141  ? 0.3436 0.3162 0.2769 0.0225  -0.0115 -0.0350 139  SER B CB  
10112 O OG  . SER B 141  ? 0.3277 0.3021 0.2597 0.0241  -0.0069 -0.0348 139  SER B OG  
10113 N N   . LEU B 142  ? 0.3123 0.2765 0.2229 0.0246  -0.0088 -0.0360 140  LEU B N   
10114 C CA  A LEU B 142  ? 0.3136 0.2785 0.2177 0.0250  -0.0053 -0.0345 140  LEU B CA  
10115 C CA  B LEU B 142  ? 0.3127 0.2777 0.2169 0.0250  -0.0053 -0.0345 140  LEU B CA  
10116 C C   . LEU B 142  ? 0.2930 0.2645 0.2031 0.0243  -0.0019 -0.0317 140  LEU B C   
10117 O O   . LEU B 142  ? 0.2750 0.2479 0.1814 0.0234  0.0001  -0.0295 140  LEU B O   
10118 C CB  A LEU B 142  ? 0.3361 0.2987 0.2339 0.0274  -0.0023 -0.0365 140  LEU B CB  
10119 C CB  B LEU B 142  ? 0.3364 0.2990 0.2345 0.0275  -0.0024 -0.0366 140  LEU B CB  
10120 C CG  A LEU B 142  ? 0.3598 0.3151 0.2478 0.0282  -0.0047 -0.0390 140  LEU B CG  
10121 C CG  B LEU B 142  ? 0.3315 0.2914 0.2190 0.0281  -0.0006 -0.0364 140  LEU B CG  
10122 C CD1 A LEU B 142  ? 0.3559 0.3100 0.2366 0.0307  -0.0004 -0.0402 140  LEU B CD1 
10123 C CD1 B LEU B 142  ? 0.3586 0.3118 0.2390 0.0273  -0.0055 -0.0376 140  LEU B CD1 
10124 C CD2 A LEU B 142  ? 0.3992 0.3517 0.2817 0.0265  -0.0079 -0.0377 140  LEU B CD2 
10125 C CD2 B LEU B 142  ? 0.3543 0.3133 0.2379 0.0309  0.0031  -0.0384 140  LEU B CD2 
10126 N N   . PHE B 143  ? 0.2626 0.2383 0.1818 0.0244  -0.0012 -0.0316 141  PHE B N   
10127 C CA  . PHE B 143  ? 0.2565 0.2388 0.1814 0.0240  0.0025  -0.0294 141  PHE B CA  
10128 C C   . PHE B 143  ? 0.2492 0.2343 0.1806 0.0217  0.0007  -0.0273 141  PHE B C   
10129 O O   . PHE B 143  ? 0.2387 0.2291 0.1763 0.0213  0.0030  -0.0258 141  PHE B O   
10130 C CB  . PHE B 143  ? 0.2401 0.2249 0.1697 0.0261  0.0050  -0.0308 141  PHE B CB  
10131 C CG  . PHE B 143  ? 0.2532 0.2342 0.1761 0.0286  0.0065  -0.0332 141  PHE B CG  
10132 C CD1 . PHE B 143  ? 0.2434 0.2248 0.1593 0.0296  0.0098  -0.0327 141  PHE B CD1 
10133 C CD2 . PHE B 143  ? 0.2649 0.2419 0.1881 0.0300  0.0048  -0.0359 141  PHE B CD2 
10134 C CE1 . PHE B 143  ? 0.2595 0.2372 0.1687 0.0323  0.0113  -0.0351 141  PHE B CE1 
10135 C CE2 . PHE B 143  ? 0.2559 0.2286 0.1723 0.0324  0.0061  -0.0383 141  PHE B CE2 
10136 C CZ  . PHE B 143  ? 0.2625 0.2354 0.1717 0.0338  0.0094  -0.0380 141  PHE B CZ  
10137 N N   . VAL B 144  ? 0.2622 0.2437 0.1919 0.0204  -0.0034 -0.0271 142  VAL B N   
10138 C CA  . VAL B 144  ? 0.2445 0.2280 0.1799 0.0187  -0.0054 -0.0254 142  VAL B CA  
10139 C C   . VAL B 144  ? 0.2633 0.2506 0.1997 0.0172  -0.0025 -0.0225 142  VAL B C   
10140 O O   . VAL B 144  ? 0.2730 0.2640 0.2161 0.0163  -0.0023 -0.0214 142  VAL B O   
10141 C CB  . VAL B 144  ? 0.2940 0.2727 0.2258 0.0180  -0.0101 -0.0256 142  VAL B CB  
10142 C CG1 . VAL B 144  ? 0.3518 0.3319 0.2882 0.0166  -0.0119 -0.0237 142  VAL B CG1 
10143 C CG2 . VAL B 144  ? 0.3457 0.3219 0.2787 0.0190  -0.0132 -0.0283 142  VAL B CG2 
10144 N N   . ASN B 145  ? 0.2764 0.2631 0.2059 0.0169  -0.0002 -0.0214 143  ASN B N   
10145 C CA  . ASN B 145  ? 0.2546 0.2449 0.1845 0.0150  0.0025  -0.0185 143  ASN B CA  
10146 C C   . ASN B 145  ? 0.2551 0.2511 0.1867 0.0158  0.0075  -0.0181 143  ASN B C   
10147 O O   . ASN B 145  ? 0.2599 0.2590 0.1898 0.0143  0.0103  -0.0159 143  ASN B O   
10148 C CB  . ASN B 145  ? 0.2613 0.2473 0.1824 0.0136  0.0018  -0.0169 143  ASN B CB  
10149 C CG  . ASN B 145  ? 0.3355 0.3170 0.2562 0.0125  -0.0029 -0.0163 143  ASN B CG  
10150 O OD1 . ASN B 145  ? 0.3540 0.3374 0.2811 0.0115  -0.0042 -0.0155 143  ASN B OD1 
10151 N ND2 . ASN B 145  ? 0.3228 0.2986 0.2360 0.0129  -0.0057 -0.0168 143  ASN B ND2 
10152 N N   . ALA B 146  ? 0.2431 0.2409 0.1784 0.0181  0.0086  -0.0202 144  ALA B N   
10153 C CA  . ALA B 146  ? 0.2497 0.2528 0.1865 0.0196  0.0132  -0.0201 144  ALA B CA  
10154 C C   . ALA B 146  ? 0.2449 0.2551 0.1886 0.0179  0.0154  -0.0177 144  ALA B C   
10155 O O   . ALA B 146  ? 0.2594 0.2749 0.2035 0.0183  0.0193  -0.0167 144  ALA B O   
10156 C CB  . ALA B 146  ? 0.2362 0.2388 0.1753 0.0226  0.0134  -0.0229 144  ALA B CB  
10157 N N   . ALA B 147  ? 0.2476 0.2582 0.1967 0.0161  0.0129  -0.0168 145  ALA B N   
10158 C CA  . ALA B 147  ? 0.2349 0.2518 0.1898 0.0142  0.0147  -0.0145 145  ALA B CA  
10159 C C   . ALA B 147  ? 0.2742 0.2921 0.2246 0.0117  0.0164  -0.0119 145  ALA B C   
10160 O O   . ALA B 147  ? 0.2686 0.2930 0.2217 0.0106  0.0196  -0.0102 145  ALA B O   
10161 C CB  . ALA B 147  ? 0.2505 0.2666 0.2109 0.0128  0.0115  -0.0142 145  ALA B CB  
10162 N N   . THR B 148  ? 0.2499 0.2618 0.1933 0.0105  0.0143  -0.0115 146  THR B N   
10163 C CA  . THR B 148  ? 0.2991 0.3111 0.2372 0.0079  0.0159  -0.0089 146  THR B CA  
10164 C C   . THR B 148  ? 0.2652 0.2809 0.1995 0.0091  0.0204  -0.0089 146  THR B C   
10165 O O   . THR B 148  ? 0.2894 0.3109 0.2248 0.0073  0.0237  -0.0067 146  THR B O   
10166 C CB  . THR B 148  ? 0.3126 0.3166 0.2435 0.0068  0.0123  -0.0086 146  THR B CB  
10167 O OG1 . THR B 148  ? 0.3276 0.3289 0.2626 0.0060  0.0084  -0.0087 146  THR B OG1 
10168 C CG2 . THR B 148  ? 0.3487 0.3520 0.2734 0.0039  0.0139  -0.0057 146  THR B CG2 
10169 N N   . TRP B 149  ? 0.2584 0.2709 0.1883 0.0121  0.0205  -0.0114 147  TRP B N   
10170 C CA  . TRP B 149  ? 0.2576 0.2733 0.1836 0.0139  0.0249  -0.0117 147  TRP B CA  
10171 C C   . TRP B 149  ? 0.2567 0.2811 0.1903 0.0153  0.0285  -0.0117 147  TRP B C   
10172 O O   . TRP B 149  ? 0.2591 0.2890 0.1915 0.0158  0.0328  -0.0107 147  TRP B O   
10173 C CB  . TRP B 149  ? 0.2676 0.2772 0.1870 0.0170  0.0238  -0.0147 147  TRP B CB  
10174 C CG  . TRP B 149  ? 0.2545 0.2563 0.1654 0.0156  0.0206  -0.0145 147  TRP B CG  
10175 C CD1 . TRP B 149  ? 0.2667 0.2617 0.1759 0.0161  0.0159  -0.0162 147  TRP B CD1 
10176 C CD2 . TRP B 149  ? 0.2880 0.2885 0.1913 0.0135  0.0219  -0.0122 147  TRP B CD2 
10177 N NE1 . TRP B 149  ? 0.2603 0.2496 0.1610 0.0147  0.0139  -0.0152 147  TRP B NE1 
10178 C CE2 . TRP B 149  ? 0.3054 0.2975 0.2021 0.0130  0.0176  -0.0127 147  TRP B CE2 
10179 C CE3 . TRP B 149  ? 0.3175 0.3230 0.2187 0.0117  0.0263  -0.0097 147  TRP B CE3 
10180 C CZ2 . TRP B 149  ? 0.3206 0.3088 0.2083 0.0111  0.0174  -0.0108 147  TRP B CZ2 
10181 C CZ3 . TRP B 149  ? 0.3478 0.3494 0.2401 0.0095  0.0263  -0.0077 147  TRP B CZ3 
10182 C CH2 . TRP B 149  ? 0.3463 0.3390 0.2317 0.0093  0.0219  -0.0082 147  TRP B CH2 
10183 N N   . GLY B 150  ? 0.2456 0.2715 0.1869 0.0162  0.0268  -0.0126 148  GLY B N   
10184 C CA  . GLY B 150  ? 0.2448 0.2790 0.1937 0.0174  0.0299  -0.0122 148  GLY B CA  
10185 C C   . GLY B 150  ? 0.2677 0.3090 0.2197 0.0141  0.0322  -0.0090 148  GLY B C   
10186 O O   . GLY B 150  ? 0.2781 0.3271 0.2326 0.0150  0.0362  -0.0082 148  GLY B O   
10187 N N   . LEU B 151  ? 0.2680 0.3069 0.2199 0.0103  0.0296  -0.0071 149  LEU B N   
10188 C CA  . LEU B 151  ? 0.2916 0.3359 0.2451 0.0064  0.0315  -0.0039 149  LEU B CA  
10189 C C   . LEU B 151  ? 0.3131 0.3596 0.2602 0.0058  0.0353  -0.0026 149  LEU B C   
10190 O O   . LEU B 151  ? 0.3363 0.3912 0.2865 0.0048  0.0390  -0.0008 149  LEU B O   
10191 C CB  . LEU B 151  ? 0.3653 0.4044 0.3178 0.0027  0.0278  -0.0023 149  LEU B CB  
10192 C CG  . LEU B 151  ? 0.3495 0.3910 0.3100 0.0013  0.0258  -0.0018 149  LEU B CG  
10193 C CD1 . LEU B 151  ? 0.3314 0.3664 0.2893 -0.0019 0.0221  -0.0006 149  LEU B CD1 
10194 C CD2 . LEU B 151  ? 0.3328 0.3841 0.2992 -0.0004 0.0290  0.0001  149  LEU B CD2 
10195 N N   . VAL B 152  ? 0.3145 0.3536 0.2526 0.0065  0.0343  -0.0034 150  VAL B N   
10196 C CA  . VAL B 152  ? 0.3404 0.3809 0.2715 0.0058  0.0379  -0.0021 150  VAL B CA  
10197 C C   . VAL B 152  ? 0.3389 0.3870 0.2719 0.0092  0.0427  -0.0032 150  VAL B C   
10198 O O   . VAL B 152  ? 0.3746 0.4297 0.3074 0.0079  0.0469  -0.0013 150  VAL B O   
10199 C CB  . VAL B 152  ? 0.3264 0.3571 0.2471 0.0063  0.0356  -0.0032 150  VAL B CB  
10200 C CG1 . VAL B 152  ? 0.3626 0.3947 0.2754 0.0061  0.0396  -0.0021 150  VAL B CG1 
10201 C CG2 . VAL B 152  ? 0.3657 0.3896 0.2843 0.0029  0.0312  -0.0017 150  VAL B CG2 
10202 N N   . VAL B 153  ? 0.2961 0.3429 0.2312 0.0137  0.0422  -0.0064 151  VAL B N   
10203 C CA  . VAL B 153  ? 0.2968 0.3489 0.2321 0.0178  0.0464  -0.0079 151  VAL B CA  
10204 C C   . VAL B 153  ? 0.2925 0.3553 0.2378 0.0182  0.0490  -0.0068 151  VAL B C   
10205 O O   . VAL B 153  ? 0.3091 0.3799 0.2553 0.0195  0.0536  -0.0061 151  VAL B O   
10206 C CB  . VAL B 153  ? 0.2780 0.3231 0.2103 0.0223  0.0446  -0.0117 151  VAL B CB  
10207 C CG1 . VAL B 153  ? 0.3112 0.3613 0.2446 0.0270  0.0487  -0.0135 151  VAL B CG1 
10208 C CG2 . VAL B 153  ? 0.2937 0.3293 0.2156 0.0219  0.0424  -0.0127 151  VAL B CG2 
10209 N N   . THR B 154  ? 0.2886 0.3520 0.2414 0.0174  0.0461  -0.0067 152  THR B N   
10210 C CA  . THR B 154  ? 0.2809 0.3535 0.2433 0.0185  0.0478  -0.0062 152  THR B CA  
10211 C C   . THR B 154  ? 0.3395 0.4178 0.3079 0.0136  0.0472  -0.0030 152  THR B C   
10212 O O   . THR B 154  ? 0.3715 0.4591 0.3473 0.0139  0.0492  -0.0020 152  THR B O   
10213 C CB  . THR B 154  ? 0.3076 0.3768 0.2743 0.0217  0.0450  -0.0087 152  THR B CB  
10214 O OG1 . THR B 154  ? 0.3039 0.3688 0.2732 0.0186  0.0407  -0.0081 152  THR B OG1 
10215 C CG2 . THR B 154  ? 0.3717 0.4327 0.3316 0.0255  0.0443  -0.0119 152  THR B CG2 
10216 N N   . GLY B 155  ? 0.2939 0.3666 0.2591 0.0094  0.0443  -0.0016 153  GLY B N   
10217 C CA  . GLY B 155  ? 0.2854 0.3616 0.2557 0.0048  0.0430  0.0011  153  GLY B CA  
10218 C C   . GLY B 155  ? 0.3229 0.3981 0.3000 0.0051  0.0396  0.0002  153  GLY B C   
10219 O O   . GLY B 155  ? 0.3769 0.4542 0.3579 0.0014  0.0381  0.0021  153  GLY B O   
10220 N N   . LYS B 156  ? 0.3098 0.3816 0.2879 0.0093  0.0383  -0.0026 154  LYS B N   
10221 C CA  . LYS B 156  ? 0.3040 0.3745 0.2879 0.0098  0.0352  -0.0035 154  LYS B CA  
10222 C C   . LYS B 156  ? 0.2944 0.3545 0.2742 0.0099  0.0312  -0.0052 154  LYS B C   
10223 O O   . LYS B 156  ? 0.2782 0.3324 0.2514 0.0115  0.0309  -0.0067 154  LYS B O   
10224 C CB  . LYS B 156  ? 0.3813 0.4562 0.3703 0.0143  0.0367  -0.0052 154  LYS B CB  
10225 N N   . LEU B 157  ? 0.3087 0.3668 0.2922 0.0081  0.0280  -0.0049 155  LEU B N   
10226 C CA  . LEU B 157  ? 0.2986 0.3481 0.2797 0.0083  0.0241  -0.0064 155  LEU B CA  
10227 C C   . LEU B 157  ? 0.3229 0.3720 0.3085 0.0114  0.0229  -0.0086 155  LEU B C   
10228 O O   . LEU B 157  ? 0.3272 0.3815 0.3192 0.0116  0.0234  -0.0081 155  LEU B O   
10229 C CB  . LEU B 157  ? 0.3310 0.3780 0.3127 0.0044  0.0213  -0.0048 155  LEU B CB  
10230 C CG  . LEU B 157  ? 0.3391 0.3779 0.3189 0.0048  0.0172  -0.0063 155  LEU B CG  
10231 C CD1 . LEU B 157  ? 0.3317 0.3641 0.3038 0.0057  0.0164  -0.0072 155  LEU B CD1 
10232 C CD2 . LEU B 157  ? 0.3650 0.4019 0.3460 0.0015  0.0147  -0.0049 155  LEU B CD2 
10233 N N   . THR B 158  ? 0.3412 0.3841 0.3233 0.0137  0.0214  -0.0109 156  THR B N   
10234 C CA  . THR B 158  ? 0.3265 0.3672 0.3120 0.0160  0.0197  -0.0129 156  THR B CA  
10235 C C   . THR B 158  ? 0.3556 0.3893 0.3391 0.0149  0.0158  -0.0138 156  THR B C   
10236 O O   . THR B 158  ? 0.3779 0.4066 0.3553 0.0147  0.0147  -0.0143 156  THR B O   
10237 C CB  . THR B 158  ? 0.4127 0.4523 0.3960 0.0198  0.0214  -0.0150 156  THR B CB  
10238 O OG1 . THR B 158  ? 0.4138 0.4600 0.3978 0.0210  0.0253  -0.0141 156  THR B OG1 
10239 C CG2 . THR B 158  ? 0.4448 0.4832 0.4324 0.0219  0.0200  -0.0166 156  THR B CG2 
10240 N N   . SER B 159  ? 0.3114 0.3451 0.2999 0.0142  0.0137  -0.0139 157  SER B N   
10241 C CA  . SER B 159  ? 0.2991 0.3276 0.2866 0.0129  0.0101  -0.0143 157  SER B CA  
10242 C C   . SER B 159  ? 0.3305 0.3533 0.3148 0.0147  0.0081  -0.0166 157  SER B C   
10243 O O   . SER B 159  ? 0.3226 0.3407 0.3035 0.0139  0.0056  -0.0168 157  SER B O   
10244 C CB  . SER B 159  ? 0.3495 0.3798 0.3432 0.0121  0.0087  -0.0140 157  SER B CB  
10245 O OG  . SER B 159  ? 0.3550 0.3875 0.3529 0.0143  0.0095  -0.0151 157  SER B OG  
10246 N N   . THR B 160  ? 0.2973 0.3202 0.2828 0.0171  0.0090  -0.0182 158  THR B N   
10247 C CA  . THR B 160  ? 0.2640 0.2815 0.2461 0.0186  0.0072  -0.0205 158  THR B CA  
10248 C C   . THR B 160  ? 0.2484 0.2653 0.2261 0.0207  0.0096  -0.0215 158  THR B C   
10249 O O   . THR B 160  ? 0.2924 0.3138 0.2707 0.0215  0.0129  -0.0205 158  THR B O   
10250 C CB  . THR B 160  ? 0.2691 0.2857 0.2560 0.0193  0.0055  -0.0218 158  THR B CB  
10251 O OG1 . THR B 160  ? 0.3135 0.3340 0.3044 0.0208  0.0079  -0.0217 158  THR B OG1 
10252 C CG2 . THR B 160  ? 0.3622 0.3793 0.3531 0.0175  0.0031  -0.0211 158  THR B CG2 
10253 N N   . VAL B 161  ? 0.1974 0.2090 0.1708 0.0218  0.0080  -0.0235 159  VAL B N   
10254 C CA  . VAL B 161  ? 0.2329 0.2422 0.1999 0.0237  0.0098  -0.0247 159  VAL B CA  
10255 C C   . VAL B 161  ? 0.2104 0.2177 0.1783 0.0262  0.0101  -0.0269 159  VAL B C   
10256 O O   . VAL B 161  ? 0.1925 0.1963 0.1619 0.0260  0.0073  -0.0283 159  VAL B O   
10257 C CB  . VAL B 161  ? 0.2696 0.2732 0.2296 0.0229  0.0073  -0.0254 159  VAL B CB  
10258 C CG1 . VAL B 161  ? 0.2855 0.2857 0.2384 0.0250  0.0086  -0.0271 159  VAL B CG1 
10259 C CG2 . VAL B 161  ? 0.3016 0.3066 0.2599 0.0206  0.0073  -0.0230 159  VAL B CG2 
10260 N N   . ASN B 162  ? 0.2023 0.2116 0.1690 0.0287  0.0134  -0.0272 160  ASN B N   
10261 C CA  . ASN B 162  ? 0.1963 0.2021 0.1622 0.0313  0.0135  -0.0295 160  ASN B CA  
10262 C C   . ASN B 162  ? 0.1772 0.1764 0.1348 0.0322  0.0126  -0.0317 160  ASN B C   
10263 O O   . ASN B 162  ? 0.1968 0.1957 0.1492 0.0343  0.0152  -0.0323 160  ASN B O   
10264 C CB  . ASN B 162  ? 0.2033 0.2137 0.1717 0.0340  0.0172  -0.0291 160  ASN B CB  
10265 C CG  . ASN B 162  ? 0.2048 0.2108 0.1727 0.0368  0.0171  -0.0313 160  ASN B CG  
10266 O OD1 . ASN B 162  ? 0.2035 0.2027 0.1672 0.0368  0.0148  -0.0334 160  ASN B OD1 
10267 N ND2 . ASN B 162  ? 0.2512 0.2610 0.2231 0.0391  0.0194  -0.0309 160  ASN B ND2 
10268 N N   . ASP B 163  ? 0.1913 0.1855 0.1477 0.0307  0.0087  -0.0329 161  ASP B N   
10269 C CA  . ASP B 163  ? 0.2044 0.1922 0.1527 0.0310  0.0071  -0.0348 161  ASP B CA  
10270 C C   . ASP B 163  ? 0.2105 0.1936 0.1549 0.0338  0.0079  -0.0374 161  ASP B C   
10271 O O   . ASP B 163  ? 0.2167 0.1950 0.1532 0.0348  0.0078  -0.0391 161  ASP B O   
10272 C CB  . ASP B 163  ? 0.2197 0.2042 0.1683 0.0286  0.0025  -0.0352 161  ASP B CB  
10273 C CG  . ASP B 163  ? 0.2435 0.2281 0.1990 0.0276  0.0003  -0.0357 161  ASP B CG  
10274 O OD1 . ASP B 163  ? 0.2250 0.2141 0.1870 0.0277  0.0018  -0.0344 161  ASP B OD1 
10275 O OD2 . ASP B 163  ? 0.2877 0.2680 0.2420 0.0267  -0.0031 -0.0373 161  ASP B OD2 
10276 N N   . ARG B 164  ? 0.1963 0.1799 0.1453 0.0351  0.0087  -0.0379 162  ARG B N   
10277 C CA  . ARG B 164  ? 0.2007 0.1792 0.1454 0.0381  0.0097  -0.0403 162  ARG B CA  
10278 C C   . ARG B 164  ? 0.1910 0.1724 0.1324 0.0413  0.0142  -0.0401 162  ARG B C   
10279 O O   . ARG B 164  ? 0.2036 0.1802 0.1379 0.0437  0.0152  -0.0423 162  ARG B O   
10280 C CB  . ARG B 164  ? 0.1981 0.1757 0.1483 0.0385  0.0090  -0.0407 162  ARG B CB  
10281 C CG  . ARG B 164  ? 0.2038 0.1780 0.1567 0.0355  0.0047  -0.0413 162  ARG B CG  
10282 C CD  . ARG B 164  ? 0.2616 0.2295 0.2077 0.0343  0.0016  -0.0433 162  ARG B CD  
10283 N NE  . ARG B 164  ? 0.3448 0.3059 0.2831 0.0367  0.0022  -0.0459 162  ARG B NE  
10284 C CZ  . ARG B 164  ? 0.3949 0.3508 0.3253 0.0366  0.0006  -0.0477 162  ARG B CZ  
10285 N NH1 . ARG B 164  ? 0.3876 0.3445 0.3169 0.0342  -0.0017 -0.0470 162  ARG B NH1 
10286 N NH2 . ARG B 164  ? 0.3822 0.3316 0.3054 0.0390  0.0013  -0.0502 162  ARG B NH2 
10287 N N   . SER B 165  ? 0.1954 0.1849 0.1423 0.0414  0.0170  -0.0376 163  SER B N   
10288 C CA  . SER B 165  ? 0.1752 0.1690 0.1198 0.0441  0.0214  -0.0371 163  SER B CA  
10289 C C   . SER B 165  ? 0.1817 0.1743 0.1186 0.0436  0.0221  -0.0373 163  SER B C   
10290 O O   . SER B 165  ? 0.1892 0.1808 0.1203 0.0465  0.0249  -0.0385 163  SER B O   
10291 C CB  . SER B 165  ? 0.1824 0.1857 0.1349 0.0435  0.0236  -0.0342 163  SER B CB  
10292 O OG  . SER B 165  ? 0.2062 0.2150 0.1571 0.0456  0.0278  -0.0334 163  SER B OG  
10293 N N   . LEU B 166  ? 0.1944 0.1869 0.1311 0.0401  0.0197  -0.0360 164  LEU B N   
10294 C CA  . LEU B 166  ? 0.1918 0.1826 0.1206 0.0393  0.0201  -0.0358 164  LEU B CA  
10295 C C   . LEU B 166  ? 0.2031 0.1851 0.1232 0.0406  0.0182  -0.0389 164  LEU B C   
10296 O O   . LEU B 166  ? 0.2173 0.1975 0.1295 0.0421  0.0202  -0.0397 164  LEU B O   
10297 C CB  . LEU B 166  ? 0.2010 0.1932 0.1317 0.0354  0.0176  -0.0336 164  LEU B CB  
10298 C CG  . LEU B 166  ? 0.2231 0.2237 0.1605 0.0339  0.0198  -0.0305 164  LEU B CG  
10299 C CD1 . LEU B 166  ? 0.2270 0.2278 0.1668 0.0302  0.0168  -0.0286 164  LEU B CD1 
10300 C CD2 . LEU B 166  ? 0.2143 0.2197 0.1484 0.0348  0.0243  -0.0292 164  LEU B CD2 
10301 N N   . ALA B 167  ? 0.2058 0.1821 0.1269 0.0399  0.0143  -0.0407 165  ALA B N   
10302 C CA  . ALA B 167  ? 0.2276 0.1954 0.1404 0.0410  0.0123  -0.0438 165  ALA B CA  
10303 C C   . ALA B 167  ? 0.2256 0.1912 0.1339 0.0452  0.0158  -0.0458 165  ALA B C   
10304 O O   . ALA B 167  ? 0.2550 0.2157 0.1541 0.0468  0.0164  -0.0477 165  ALA B O   
10305 C CB  . ALA B 167  ? 0.2446 0.2074 0.1602 0.0392  0.0077  -0.0452 165  ALA B CB  
10306 N N   . ALA B 168  ? 0.2197 0.1888 0.1342 0.0472  0.0179  -0.0455 166  ALA B N   
10307 C CA  . ALA B 168  ? 0.2147 0.1822 0.1255 0.0518  0.0214  -0.0472 166  ALA B CA  
10308 C C   . ALA B 168  ? 0.2188 0.1910 0.1251 0.0536  0.0258  -0.0464 166  ALA B C   
10309 O O   . ALA B 168  ? 0.2359 0.2040 0.1341 0.0568  0.0278  -0.0487 166  ALA B O   
10310 C CB  . ALA B 168  ? 0.2269 0.1985 0.1460 0.0534  0.0229  -0.0464 166  ALA B CB  
10311 N N   . ALA B 169  ? 0.2117 0.1924 0.1230 0.0516  0.0275  -0.0433 167  ALA B N   
10312 C CA  . ALA B 169  ? 0.2152 0.2015 0.1232 0.0528  0.0319  -0.0420 167  ALA B CA  
10313 C C   . ALA B 169  ? 0.2258 0.2066 0.1232 0.0519  0.0311  -0.0431 167  ALA B C   
10314 O O   . ALA B 169  ? 0.2441 0.2254 0.1349 0.0545  0.0347  -0.0439 167  ALA B O   
10315 C CB  . ALA B 169  ? 0.2102 0.2061 0.1259 0.0499  0.0332  -0.0383 167  ALA B CB  
10316 N N   . LEU B 170  ? 0.2490 0.2249 0.1446 0.0484  0.0265  -0.0430 168  LEU B N   
10317 C CA  . LEU B 170  ? 0.2358 0.2063 0.1211 0.0476  0.0253  -0.0439 168  LEU B CA  
10318 C C   . LEU B 170  ? 0.2442 0.2062 0.1207 0.0508  0.0250  -0.0478 168  LEU B C   
10319 O O   . LEU B 170  ? 0.2562 0.2158 0.1233 0.0524  0.0271  -0.0488 168  LEU B O   
10320 C CB  . LEU B 170  ? 0.2546 0.2222 0.1408 0.0434  0.0201  -0.0430 168  LEU B CB  
10321 C CG  . LEU B 170  ? 0.2599 0.2222 0.1357 0.0423  0.0185  -0.0434 168  LEU B CG  
10322 C CD1 . LEU B 170  ? 0.2902 0.2578 0.1626 0.0421  0.0228  -0.0409 168  LEU B CD1 
10323 C CD2 . LEU B 170  ? 0.2910 0.2508 0.1689 0.0387  0.0131  -0.0425 168  LEU B CD2 
10324 N N   . THR B 171  ? 0.2473 0.2042 0.1260 0.0516  0.0224  -0.0500 169  THR B N   
10325 C CA  . THR B 171  ? 0.2565 0.2048 0.1269 0.0548  0.0221  -0.0538 169  THR B CA  
10326 C C   . THR B 171  ? 0.2606 0.2115 0.1276 0.0595  0.0279  -0.0546 169  THR B C   
10327 O O   . THR B 171  ? 0.2726 0.2184 0.1294 0.0620  0.0292  -0.0569 169  THR B O   
10328 C CB  . THR B 171  ? 0.2832 0.2266 0.1581 0.0546  0.0188  -0.0555 169  THR B CB  
10329 O OG1 . THR B 171  ? 0.3300 0.2711 0.2075 0.0503  0.0136  -0.0550 169  THR B OG1 
10330 C CG2 . THR B 171  ? 0.3033 0.2371 0.1694 0.0579  0.0186  -0.0594 169  THR B CG2 
10331 N N   . ARG B 172  ? 0.2528 0.2122 0.1285 0.0610  0.0313  -0.0526 170  ARG B N   
10332 C CA  . ARG B 172  ? 0.2577 0.2208 0.1315 0.0659  0.0368  -0.0533 170  ARG B CA  
10333 C C   . ARG B 172  ? 0.2636 0.2303 0.1307 0.0661  0.0403  -0.0524 170  ARG B C   
10334 O O   . ARG B 172  ? 0.2750 0.2389 0.1338 0.0700  0.0433  -0.0546 170  ARG B O   
10335 C CB  . ARG B 172  ? 0.2605 0.2333 0.1458 0.0668  0.0393  -0.0509 170  ARG B CB  
10336 C CG  . ARG B 172  ? 0.2525 0.2280 0.1370 0.0727  0.0441  -0.0522 170  ARG B CG  
10337 C CD  . ARG B 172  ? 0.2422 0.2282 0.1382 0.0735  0.0465  -0.0495 170  ARG B CD  
10338 N NE  . ARG B 172  ? 0.2333 0.2179 0.1371 0.0710  0.0426  -0.0487 170  ARG B NE  
10339 C CZ  . ARG B 172  ? 0.2226 0.2126 0.1340 0.0665  0.0407  -0.0457 170  ARG B CZ  
10340 N NH1 . ARG B 172  ? 0.2339 0.2307 0.1462 0.0637  0.0422  -0.0432 170  ARG B NH1 
10341 N NH2 . ARG B 172  ? 0.2156 0.2039 0.1334 0.0647  0.0374  -0.0453 170  ARG B NH2 
10342 N N   . LEU B 173  ? 0.2715 0.2442 0.1417 0.0620  0.0401  -0.0491 171  LEU B N   
10343 C CA  . LEU B 173  ? 0.2628 0.2397 0.1272 0.0620  0.0439  -0.0477 171  LEU B CA  
10344 C C   . LEU B 173  ? 0.2751 0.2426 0.1264 0.0620  0.0422  -0.0500 171  LEU B C   
10345 O O   . LEU B 173  ? 0.2951 0.2633 0.1385 0.0642  0.0462  -0.0506 171  LEU B O   
10346 C CB  . LEU B 173  ? 0.2619 0.2467 0.1325 0.0574  0.0440  -0.0435 171  LEU B CB  
10347 C CG  . LEU B 173  ? 0.2767 0.2577 0.1470 0.0523  0.0388  -0.0420 171  LEU B CG  
10348 C CD1 . LEU B 173  ? 0.2941 0.2719 0.1533 0.0511  0.0393  -0.0417 171  LEU B CD1 
10349 C CD2 . LEU B 173  ? 0.2966 0.2855 0.1771 0.0489  0.0386  -0.0384 171  LEU B CD2 
10350 N N   . ILE B 174  ? 0.2970 0.2562 0.1458 0.0594  0.0365  -0.0513 172  ILE B N   
10351 C CA  . ILE B 174  ? 0.2879 0.2381 0.1241 0.0594  0.0344  -0.0536 172  ILE B CA  
10352 C C   . ILE B 174  ? 0.3188 0.2619 0.1472 0.0642  0.0358  -0.0578 172  ILE B C   
10353 O O   . ILE B 174  ? 0.3371 0.2769 0.1557 0.0656  0.0375  -0.0591 172  ILE B O   
10354 C CB  . ILE B 174  ? 0.2856 0.2295 0.1218 0.0553  0.0276  -0.0538 172  ILE B CB  
10355 C CG1 . ILE B 174  ? 0.2938 0.2436 0.1354 0.0509  0.0264  -0.0498 172  ILE B CG1 
10356 C CG2 . ILE B 174  ? 0.3217 0.2557 0.1448 0.0556  0.0250  -0.0566 172  ILE B CG2 
10357 C CD1 . ILE B 174  ? 0.3155 0.2607 0.1593 0.0473  0.0199  -0.0497 172  ILE B CD1 
10358 N N   . SER B 175  ? 0.3125 0.2531 0.1460 0.0661  0.0347  -0.0596 173  SER B N   
10359 C CA  . SER B 175  ? 0.3192 0.2537 0.1483 0.0696  0.0355  -0.0627 173  SER B CA  
10360 C C   . SER B 175  ? 0.3096 0.2511 0.1393 0.0729  0.0417  -0.0618 173  SER B C   
10361 O O   . SER B 175  ? 0.3559 0.2930 0.1800 0.0752  0.0428  -0.0639 173  SER B O   
10362 C CB  . SER B 175  ? 0.3506 0.2813 0.1859 0.0705  0.0330  -0.0642 173  SER B CB  
10363 O OG  . SER B 175  ? 0.3953 0.3187 0.2292 0.0673  0.0270  -0.0654 173  SER B OG  
10364 N N   . ARG B 176  ? 0.3018 0.2546 0.1388 0.0731  0.0456  -0.0588 174  ARG B N   
10365 C CA  . ARG B 176  ? 0.3051 0.2658 0.1438 0.0759  0.0515  -0.0578 174  ARG B CA  
10366 C C   . ARG B 176  ? 0.3406 0.3035 0.1716 0.0746  0.0541  -0.0567 174  ARG B C   
10367 O O   . ARG B 176  ? 0.3552 0.3184 0.1820 0.0769  0.0573  -0.0577 174  ARG B O   
10368 C CB  . ARG B 176  ? 0.3208 0.2931 0.1713 0.0763  0.0544  -0.0548 174  ARG B CB  
10369 C CG  . ARG B 176  ? 0.3315 0.3131 0.1861 0.0793  0.0601  -0.0538 174  ARG B CG  
10370 C CD  . ARG B 176  ? 0.3004 0.2929 0.1677 0.0794  0.0619  -0.0510 174  ARG B CD  
10371 N NE  . ARG B 176  ? 0.3331 0.3339 0.2035 0.0758  0.0631  -0.0476 174  ARG B NE  
10372 C CZ  . ARG B 176  ? 0.3252 0.3281 0.2011 0.0733  0.0607  -0.0459 174  ARG B CZ  
10373 N NH1 . ARG B 176  ? 0.2853 0.2835 0.1657 0.0736  0.0569  -0.0471 174  ARG B NH1 
10374 N NH2 . ARG B 176  ? 0.3821 0.3919 0.2605 0.0691  0.0615  -0.0425 174  ARG B NH2 
10375 N N   . CYS B 177  ? 0.3282 0.2923 0.1570 0.0708  0.0527  -0.0546 175  CYS B N   
10376 C CA  . CYS B 177  ? 0.3505 0.3185 0.1735 0.0692  0.0557  -0.0526 175  CYS B CA  
10377 C C   . CYS B 177  ? 0.3954 0.3545 0.2073 0.0665  0.0519  -0.0534 175  CYS B C   
10378 O O   . CYS B 177  ? 0.3986 0.3590 0.2037 0.0655  0.0543  -0.0523 175  CYS B O   
10379 C CB  . CYS B 177  ? 0.3483 0.3274 0.1783 0.0669  0.0584  -0.0485 175  CYS B CB  
10380 S SG  . CYS B 177  ? 0.4253 0.4167 0.2696 0.0694  0.0627  -0.0470 175  CYS B SG  
10381 N N   . GLY B 178  ? 0.3770 0.3275 0.1872 0.0651  0.0460  -0.0551 176  GLY B N   
10382 C CA  . GLY B 178  ? 0.3850 0.3265 0.1846 0.0629  0.0419  -0.0563 176  GLY B CA  
10383 C C   . GLY B 178  ? 0.3713 0.3147 0.1667 0.0593  0.0414  -0.0532 176  GLY B C   
10384 O O   . GLY B 178  ? 0.3688 0.3196 0.1718 0.0570  0.0423  -0.0498 176  GLY B O   
10385 N N   . GLU B 179  ? 0.3876 0.3245 0.1727 0.0580  0.0393  -0.0539 177  GLU B N   
10386 C CA  . GLU B 179  ? 0.3968 0.3337 0.1765 0.0544  0.0380  -0.0510 177  GLU B CA  
10387 C C   . GLU B 179  ? 0.3625 0.3094 0.1444 0.0536  0.0439  -0.0471 177  GLU B C   
10388 O O   . GLU B 179  ? 0.3722 0.3220 0.1575 0.0497  0.0422  -0.0436 177  GLU B O   
10389 C CB  . GLU B 179  ? 0.4154 0.3441 0.1833 0.0536  0.0355  -0.0524 177  GLU B CB  
10390 C CG  . GLU B 179  ? 0.4939 0.4209 0.2553 0.0499  0.0331  -0.0495 177  GLU B CG  
10391 C CD  . GLU B 179  ? 0.5723 0.5051 0.3292 0.0492  0.0387  -0.0466 177  GLU B CD  
10392 O OE1 . GLU B 179  ? 0.5740 0.5117 0.3317 0.0517  0.0442  -0.0473 177  GLU B OE1 
10393 O OE2 . GLU B 179  ? 0.6137 0.5460 0.3662 0.0461  0.0375  -0.0435 177  GLU B OE2 
10394 N N   . PRO B 180  ? 0.3751 0.3285 0.1582 0.0558  0.0499  -0.0469 178  PRO B N   
10395 C CA  . PRO B 180  ? 0.3873 0.3507 0.1726 0.0542  0.0552  -0.0429 178  PRO B CA  
10396 C C   . PRO B 180  ? 0.3765 0.3473 0.1730 0.0522  0.0553  -0.0399 178  PRO B C   
10397 O O   . PRO B 180  ? 0.3954 0.3706 0.1933 0.0481  0.0558  -0.0359 178  PRO B O   
10398 C CB  . PRO B 180  ? 0.4047 0.3741 0.1920 0.0574  0.0610  -0.0440 178  PRO B CB  
10399 C CG  . PRO B 180  ? 0.4066 0.3664 0.1860 0.0598  0.0587  -0.0481 178  PRO B CG  
10400 C CD  . PRO B 180  ? 0.4156 0.3670 0.1963 0.0594  0.0521  -0.0502 178  PRO B CD  
10401 N N   . VAL B 181  ? 0.3499 0.3225 0.1567 0.0537  0.0539  -0.0411 179  VAL B N   
10402 C CA  . VAL B 181  ? 0.3653 0.3458 0.1854 0.0506  0.0532  -0.0378 179  VAL B CA  
10403 C C   . VAL B 181  ? 0.3163 0.2918 0.1378 0.0460  0.0468  -0.0363 179  VAL B C   
10404 O O   . VAL B 181  ? 0.3355 0.3164 0.1638 0.0422  0.0465  -0.0327 179  VAL B O   
10405 C CB  . VAL B 181  ? 0.3475 0.3317 0.1781 0.0536  0.0539  -0.0394 179  VAL B CB  
10406 C CG1 . VAL B 181  ? 0.3129 0.2881 0.1444 0.0541  0.0479  -0.0424 179  VAL B CG1 
10407 C CG2 . VAL B 181  ? 0.3606 0.3553 0.2041 0.0510  0.0552  -0.0358 179  VAL B CG2 
10408 N N   . ILE B 182  ? 0.3354 0.3006 0.1507 0.0462  0.0416  -0.0390 180  ILE B N   
10409 C CA  . ILE B 182  ? 0.3215 0.2822 0.1377 0.0422  0.0355  -0.0376 180  ILE B CA  
10410 C C   . ILE B 182  ? 0.3532 0.3140 0.1625 0.0390  0.0361  -0.0344 180  ILE B C   
10411 O O   . ILE B 182  ? 0.3526 0.3153 0.1665 0.0353  0.0339  -0.0312 180  ILE B O   
10412 C CB  . ILE B 182  ? 0.3363 0.2866 0.1470 0.0431  0.0299  -0.0413 180  ILE B CB  
10413 C CG1 . ILE B 182  ? 0.3519 0.3017 0.1699 0.0457  0.0291  -0.0442 180  ILE B CG1 
10414 C CG2 . ILE B 182  ? 0.3488 0.2950 0.1602 0.0393  0.0236  -0.0398 180  ILE B CG2 
10415 C CD1 . ILE B 182  ? 0.3671 0.3066 0.1780 0.0472  0.0248  -0.0483 180  ILE B CD1 
10416 N N   . ARG B 183  ? 0.3742 0.3325 0.1717 0.0406  0.0392  -0.0351 181  ARG B N   
10417 C CA  . ARG B 183  ? 0.4042 0.3626 0.1939 0.0377  0.0405  -0.0319 181  ARG B CA  
10418 C C   . ARG B 183  ? 0.4081 0.3765 0.2059 0.0349  0.0443  -0.0276 181  ARG B C   
10419 O O   . ARG B 183  ? 0.4099 0.3780 0.2082 0.0309  0.0422  -0.0242 181  ARG B O   
10420 C CB  . ARG B 183  ? 0.4183 0.3739 0.1950 0.0405  0.0445  -0.0337 181  ARG B CB  
10421 C CG  . ARG B 183  ? 0.4844 0.4392 0.2512 0.0378  0.0462  -0.0306 181  ARG B CG  
10422 C CD  . ARG B 183  ? 0.5486 0.4931 0.3070 0.0358  0.0396  -0.0308 181  ARG B CD  
10423 N NE  . ARG B 183  ? 0.4941 0.4393 0.2589 0.0316  0.0357  -0.0273 181  ARG B NE  
10424 C CZ  . ARG B 183  ? 0.5578 0.4961 0.3221 0.0301  0.0287  -0.0277 181  ARG B CZ  
10425 N NH1 . ARG B 183  ? 0.5351 0.4656 0.2936 0.0322  0.0245  -0.0314 181  ARG B NH1 
10426 N NH2 . ARG B 183  ? 0.5020 0.4413 0.2716 0.0265  0.0259  -0.0243 181  ARG B NH2 
10427 N N   . ARG B 184  ? 0.3882 0.3654 0.1925 0.0371  0.0499  -0.0276 182  ARG B N   
10428 C CA  . ARG B 184  ? 0.4021 0.3896 0.2147 0.0343  0.0536  -0.0236 182  ARG B CA  
10429 C C   . ARG B 184  ? 0.3934 0.3822 0.2169 0.0311  0.0492  -0.0217 182  ARG B C   
10430 O O   . ARG B 184  ? 0.3982 0.3906 0.2246 0.0270  0.0496  -0.0179 182  ARG B O   
10431 C CB  . ARG B 184  ? 0.3973 0.3942 0.2156 0.0378  0.0598  -0.0245 182  ARG B CB  
10432 C CG  . ARG B 184  ? 0.4601 0.4583 0.2682 0.0405  0.0655  -0.0253 182  ARG B CG  
10433 C CD  . ARG B 184  ? 0.4962 0.5030 0.3043 0.0371  0.0704  -0.0209 182  ARG B CD  
10434 N NE  . ARG B 184  ? 0.4718 0.4913 0.2915 0.0379  0.0752  -0.0196 182  ARG B NE  
10435 C CZ  . ARG B 184  ? 0.4783 0.5053 0.3079 0.0339  0.0753  -0.0159 182  ARG B CZ  
10436 N NH1 . ARG B 184  ? 0.4823 0.5052 0.3119 0.0288  0.0710  -0.0132 182  ARG B NH1 
10437 N NH2 . ARG B 184  ? 0.4589 0.4975 0.2985 0.0351  0.0796  -0.0151 182  ARG B NH2 
10438 N N   . GLY B 185  ? 0.3405 0.3261 0.1699 0.0327  0.0452  -0.0243 183  GLY B N   
10439 C CA  . GLY B 185  ? 0.3260 0.3126 0.1653 0.0299  0.0412  -0.0228 183  GLY B CA  
10440 C C   . GLY B 185  ? 0.3545 0.3344 0.1890 0.0263  0.0363  -0.0209 183  GLY B C   
10441 O O   . GLY B 185  ? 0.3420 0.3246 0.1818 0.0228  0.0351  -0.0178 183  GLY B O   
10442 N N   . VAL B 186  ? 0.3512 0.3222 0.1752 0.0272  0.0332  -0.0229 184  VAL B N   
10443 C CA  . VAL B 186  ? 0.3885 0.3528 0.2073 0.0242  0.0282  -0.0212 184  VAL B CA  
10444 C C   . VAL B 186  ? 0.3762 0.3428 0.1906 0.0209  0.0309  -0.0170 184  VAL B C   
10445 O O   . VAL B 186  ? 0.3758 0.3415 0.1926 0.0175  0.0282  -0.0142 184  VAL B O   
10446 C CB  . VAL B 186  ? 0.3902 0.3450 0.1981 0.0261  0.0247  -0.0242 184  VAL B CB  
10447 C CG1 . VAL B 186  ? 0.3894 0.3377 0.1895 0.0233  0.0204  -0.0221 184  VAL B CG1 
10448 C CG2 . VAL B 186  ? 0.3699 0.3216 0.1831 0.0281  0.0205  -0.0278 184  VAL B CG2 
10449 N N   . ASP B 187  ? 0.3863 0.3559 0.1942 0.0217  0.0365  -0.0166 185  ASP B N   
10450 C CA  . ASP B 187  ? 0.4049 0.3770 0.2082 0.0183  0.0395  -0.0124 185  ASP B CA  
10451 C C   . ASP B 187  ? 0.4080 0.3885 0.2225 0.0152  0.0414  -0.0092 185  ASP B C   
10452 O O   . ASP B 187  ? 0.4205 0.4003 0.2338 0.0111  0.0405  -0.0055 185  ASP B O   
10453 C CB  . ASP B 187  ? 0.3965 0.3712 0.1912 0.0201  0.0456  -0.0128 185  ASP B CB  
10454 C CG  . ASP B 187  ? 0.4789 0.4442 0.2603 0.0226  0.0436  -0.0157 185  ASP B CG  
10455 O OD1 . ASP B 187  ? 0.5184 0.4752 0.2961 0.0218  0.0374  -0.0163 185  ASP B OD1 
10456 O OD2 . ASP B 187  ? 0.4809 0.4474 0.2555 0.0254  0.0482  -0.0174 185  ASP B OD2 
10457 N N   . MET B 188  ? 0.3923 0.3802 0.2175 0.0171  0.0437  -0.0105 186  MET B N   
10458 C CA  . MET B 188  ? 0.3792 0.3755 0.2154 0.0144  0.0454  -0.0076 186  MET B CA  
10459 C C   . MET B 188  ? 0.3826 0.3749 0.2241 0.0116  0.0395  -0.0065 186  MET B C   
10460 O O   . MET B 188  ? 0.4144 0.4088 0.2586 0.0076  0.0395  -0.0029 186  MET B O   
10461 C CB  . MET B 188  ? 0.3742 0.3789 0.2201 0.0176  0.0487  -0.0096 186  MET B CB  
10462 C CG  . MET B 188  ? 0.4406 0.4547 0.2980 0.0150  0.0506  -0.0069 186  MET B CG  
10463 S SD  . MET B 188  ? 0.5463 0.5676 0.4008 0.0107  0.0560  -0.0023 186  MET B SD  
10464 C CE  . MET B 188  ? 0.5365 0.5600 0.3821 0.0149  0.0619  -0.0043 186  MET B CE  
10465 N N   . ALA B 189  ? 0.3850 0.3717 0.2284 0.0138  0.0347  -0.0094 187  ALA B N   
10466 C CA  . ALA B 189  ? 0.3791 0.3622 0.2275 0.0117  0.0292  -0.0085 187  ALA B CA  
10467 C C   . ALA B 189  ? 0.3825 0.3583 0.2220 0.0088  0.0262  -0.0061 187  ALA B C   
10468 O O   . ALA B 189  ? 0.3907 0.3656 0.2336 0.0057  0.0238  -0.0036 187  ALA B O   
10469 C CB  . ALA B 189  ? 0.3785 0.3574 0.2302 0.0146  0.0249  -0.0123 187  ALA B CB  
10470 N N   . MET B 190  ? 0.3639 0.3341 0.1917 0.0097  0.0262  -0.0068 188  MET B N   
10471 C CA  . MET B 190  ? 0.3988 0.3618 0.2172 0.0071  0.0234  -0.0043 188  MET B CA  
10472 C C   . MET B 190  ? 0.4240 0.3908 0.2425 0.0029  0.0266  0.0003  188  MET B C   
10473 O O   . MET B 190  ? 0.4319 0.3945 0.2495 -0.0001 0.0233  0.0029  188  MET B O   
10474 C CB  . MET B 190  ? 0.4190 0.3763 0.2244 0.0090  0.0237  -0.0057 188  MET B CB  
10475 C CG  . MET B 190  ? 0.4784 0.4267 0.2733 0.0070  0.0197  -0.0037 188  MET B CG  
10476 S SD  . MET B 190  ? 0.5651 0.5074 0.3439 0.0090  0.0208  -0.0052 188  MET B SD  
10477 C CE  . MET B 190  ? 0.4578 0.3975 0.2389 0.0136  0.0175  -0.0109 188  MET B CE  
10478 N N   . ARG B 191  ? 0.3983 0.3730 0.2178 0.0026  0.0329  0.0012  189  ARG B N   
10479 C CA  . ARG B 191  ? 0.4246 0.4040 0.2447 -0.0019 0.0363  0.0055  189  ARG B CA  
10480 C C   . ARG B 191  ? 0.4086 0.3915 0.2402 -0.0043 0.0345  0.0070  189  ARG B C   
10481 O O   . ARG B 191  ? 0.4218 0.4018 0.2521 -0.0083 0.0328  0.0103  189  ARG B O   
10482 C CB  . ARG B 191  ? 0.4460 0.4346 0.2662 -0.0013 0.0436  0.0058  189  ARG B CB  
10483 C CG  . ARG B 191  ? 0.5361 0.5297 0.3554 -0.0062 0.0476  0.0105  189  ARG B CG  
10484 C CD  . ARG B 191  ? 0.6107 0.6141 0.4297 -0.0052 0.0550  0.0106  189  ARG B CD  
10485 N NE  . ARG B 191  ? 0.6541 0.6679 0.4859 -0.0033 0.0577  0.0092  189  ARG B NE  
10486 C CZ  . ARG B 191  ? 0.6658 0.6899 0.5005 -0.0020 0.0639  0.0092  189  ARG B CZ  
10487 N NH1 . ARG B 191  ? 0.7253 0.7511 0.5511 -0.0023 0.0686  0.0104  189  ARG B NH1 
10488 N NH2 . ARG B 191  ? 0.6875 0.7204 0.5341 -0.0001 0.0656  0.0080  189  ARG B NH2 
10489 N N   . MET B 192  ? 0.3877 0.3763 0.2301 -0.0019 0.0347  0.0046  190  MET B N   
10490 C CA  . MET B 192  ? 0.3837 0.3761 0.2368 -0.0042 0.0334  0.0059  190  MET B CA  
10491 C C   . MET B 192  ? 0.3658 0.3495 0.2181 -0.0054 0.0270  0.0064  190  MET B C   
10492 O O   . MET B 192  ? 0.3788 0.3619 0.2333 -0.0091 0.0258  0.0092  190  MET B O   
10493 C CB  . MET B 192  ? 0.3866 0.3859 0.2505 -0.0010 0.0345  0.0031  190  MET B CB  
10494 C CG  . MET B 192  ? 0.4012 0.4096 0.2668 0.0007  0.0408  0.0027  190  MET B CG  
10495 S SD  . MET B 192  ? 0.5437 0.5600 0.4221 0.0043  0.0419  -0.0002 190  MET B SD  
10496 C CE  . MET B 192  ? 0.4461 0.4678 0.3347 -0.0001 0.0410  0.0029  190  MET B CE  
10497 N N   . MET B 193  ? 0.3625 0.3395 0.2117 -0.0024 0.0228  0.0035  191  MET B N   
10498 C CA  . MET B 193  ? 0.3740 0.3437 0.2235 -0.0029 0.0167  0.0036  191  MET B CA  
10499 C C   . MET B 193  ? 0.4253 0.3868 0.2641 -0.0052 0.0144  0.0063  191  MET B C   
10500 O O   . MET B 193  ? 0.4155 0.3713 0.2546 -0.0062 0.0097  0.0072  191  MET B O   
10501 C CB  . MET B 193  ? 0.3941 0.3606 0.2452 0.0011  0.0129  -0.0004 191  MET B CB  
10502 C CG  . MET B 193  ? 0.4012 0.3745 0.2634 0.0033  0.0142  -0.0029 191  MET B CG  
10503 S SD  . MET B 193  ? 0.5421 0.5108 0.4077 0.0066  0.0086  -0.0067 191  MET B SD  
10504 C CE  . MET B 193  ? 0.4242 0.3917 0.2830 0.0099  0.0106  -0.0099 191  MET B CE  
10505 N N   . GLY B 194  ? 0.3961 0.3567 0.2252 -0.0060 0.0175  0.0076  192  GLY B N   
10506 C CA  . GLY B 194  ? 0.4290 0.3813 0.2470 -0.0083 0.0154  0.0104  192  GLY B CA  
10507 C C   . GLY B 194  ? 0.4458 0.4000 0.2614 -0.0131 0.0187  0.0148  192  GLY B C   
10508 O O   . GLY B 194  ? 0.4363 0.3830 0.2445 -0.0157 0.0162  0.0177  192  GLY B O   
10509 N N   . GLU B 195  ? 0.3951 0.3591 0.2167 -0.0144 0.0243  0.0155  193  GLU B N   
10510 C CA  . GLU B 195  ? 0.4012 0.3684 0.2202 -0.0192 0.0284  0.0198  193  GLU B CA  
10511 C C   . GLU B 195  ? 0.3870 0.3633 0.2174 -0.0218 0.0310  0.0211  193  GLU B C   
10512 O O   . GLU B 195  ? 0.3873 0.3650 0.2165 -0.0267 0.0329  0.0249  193  GLU B O   
10513 C CB  . GLU B 195  ? 0.4460 0.4169 0.2574 -0.0189 0.0339  0.0201  193  GLU B CB  
10514 C CG  . GLU B 195  ? 0.5092 0.4710 0.3076 -0.0168 0.0318  0.0192  193  GLU B CG  
10515 C CD  . GLU B 195  ? 0.5809 0.5469 0.3726 -0.0155 0.0375  0.0187  193  GLU B CD  
10516 O OE1 . GLU B 195  ? 0.6188 0.5939 0.4137 -0.0176 0.0434  0.0205  193  GLU B OE1 
10517 O OE2 . GLU B 195  ? 0.6574 0.6178 0.4407 -0.0123 0.0361  0.0164  193  GLU B OE2 
10518 N N   . GLN B 196  ? 0.4049 0.3874 0.2462 -0.0190 0.0311  0.0182  194  GLN B N   
10519 C CA  . GLN B 196  ? 0.3845 0.3762 0.2369 -0.0212 0.0335  0.0192  194  GLN B CA  
10520 C C   . GLN B 196  ? 0.3865 0.3751 0.2461 -0.0216 0.0286  0.0187  194  GLN B C   
10521 O O   . GLN B 196  ? 0.3980 0.3868 0.2601 -0.0259 0.0281  0.0215  194  GLN B O   
10522 C CB  . GLN B 196  ? 0.3962 0.3981 0.2555 -0.0177 0.0378  0.0166  194  GLN B CB  
10523 C CG  . GLN B 196  ? 0.4834 0.4956 0.3546 -0.0194 0.0402  0.0174  194  GLN B CG  
10524 C CD  . GLN B 196  ? 0.4861 0.5077 0.3638 -0.0153 0.0441  0.0147  194  GLN B CD  
10525 O OE1 . GLN B 196  ? 0.5807 0.6026 0.4528 -0.0121 0.0467  0.0131  194  GLN B OE1 
10526 N NE2 . GLN B 196  ? 0.5419 0.5708 0.4308 -0.0151 0.0444  0.0142  194  GLN B NE2 
10527 N N   . PHE B 197  ? 0.3683 0.3539 0.2311 -0.0175 0.0249  0.0153  195  PHE B N   
10528 C CA  . PHE B 197  ? 0.3551 0.3378 0.2245 -0.0176 0.0204  0.0147  195  PHE B CA  
10529 C C   . PHE B 197  ? 0.3507 0.3228 0.2130 -0.0197 0.0158  0.0166  195  PHE B C   
10530 O O   . PHE B 197  ? 0.3819 0.3514 0.2486 -0.0209 0.0126  0.0171  195  PHE B O   
10531 C CB  . PHE B 197  ? 0.3866 0.3694 0.2613 -0.0128 0.0180  0.0105  195  PHE B CB  
10532 C CG  . PHE B 197  ? 0.3793 0.3718 0.2615 -0.0105 0.0221  0.0085  195  PHE B CG  
10533 C CD1 . PHE B 197  ? 0.4378 0.4391 0.3270 -0.0128 0.0257  0.0102  195  PHE B CD1 
10534 C CD2 . PHE B 197  ? 0.4254 0.4179 0.3076 -0.0060 0.0220  0.0050  195  PHE B CD2 
10535 C CE1 . PHE B 197  ? 0.4409 0.4511 0.3371 -0.0104 0.0292  0.0084  195  PHE B CE1 
10536 C CE2 . PHE B 197  ? 0.3949 0.3956 0.2836 -0.0036 0.0256  0.0032  195  PHE B CE2 
10537 C CZ  . PHE B 197  ? 0.4594 0.4690 0.3551 -0.0056 0.0292  0.0050  195  PHE B CZ  
10538 N N   . VAL B 198  ? 0.3635 0.3292 0.2146 -0.0199 0.0154  0.0177  196  VAL B N   
10539 C CA  . VAL B 198  ? 0.3635 0.3188 0.2065 -0.0221 0.0114  0.0202  196  VAL B CA  
10540 C C   . VAL B 198  ? 0.3509 0.3047 0.1837 -0.0253 0.0147  0.0235  196  VAL B C   
10541 O O   . VAL B 198  ? 0.3874 0.3458 0.2171 -0.0244 0.0189  0.0229  196  VAL B O   
10542 C CB  . VAL B 198  ? 0.3694 0.3162 0.2081 -0.0182 0.0059  0.0178  196  VAL B CB  
10543 C CG1 . VAL B 198  ? 0.3753 0.3237 0.2240 -0.0152 0.0027  0.0147  196  VAL B CG1 
10544 C CG2 . VAL B 198  ? 0.3938 0.3399 0.2251 -0.0155 0.0071  0.0161  196  VAL B CG2 
10545 N N   . THR B 199  ? 0.3615 0.3083 0.1886 -0.0292 0.0128  0.0270  197  THR B N   
10546 C CA  . THR B 199  ? 0.3599 0.3032 0.1755 -0.0324 0.0151  0.0304  197  THR B CA  
10547 C C   . THR B 199  ? 0.3786 0.3142 0.1837 -0.0292 0.0126  0.0292  197  THR B C   
10548 O O   . THR B 199  ? 0.4188 0.3543 0.2152 -0.0300 0.0158  0.0305  197  THR B O   
10549 C CB  . THR B 199  ? 0.3598 0.2968 0.1721 -0.0375 0.0134  0.0345  197  THR B CB  
10550 O OG1 . THR B 199  ? 0.4059 0.3502 0.2286 -0.0403 0.0153  0.0351  197  THR B OG1 
10551 C CG2 . THR B 199  ? 0.4246 0.3591 0.2258 -0.0416 0.0166  0.0384  197  THR B CG2 
10552 N N   . GLY B 200  ? 0.3782 0.3075 0.1840 -0.0256 0.0070  0.0268  198  GLY B N   
10553 C CA  . GLY B 200  ? 0.3866 0.3093 0.1837 -0.0222 0.0040  0.0252  198  GLY B CA  
10554 C C   . GLY B 200  ? 0.3443 0.2641 0.1470 -0.0182 -0.0017 0.0219  198  GLY B C   
10555 O O   . GLY B 200  ? 0.3599 0.2806 0.1711 -0.0183 -0.0038 0.0215  198  GLY B O   
10556 N N   . GLU B 201  ? 0.4184 0.3348 0.2160 -0.0145 -0.0042 0.0194  199  GLU B N   
10557 C CA  . GLU B 201  ? 0.4169 0.3310 0.2196 -0.0107 -0.0096 0.0162  199  GLU B CA  
10558 C C   . GLU B 201  ? 0.3912 0.2959 0.1902 -0.0109 -0.0154 0.0180  199  GLU B C   
10559 O O   . GLU B 201  ? 0.4247 0.3290 0.2312 -0.0090 -0.0192 0.0164  199  GLU B O   
10560 C CB  . GLU B 201  ? 0.4583 0.3714 0.2564 -0.0071 -0.0107 0.0131  199  GLU B CB  
10561 C CG  . GLU B 201  ? 0.4979 0.4112 0.3033 -0.0033 -0.0154 0.0094  199  GLU B CG  
10562 C CD  . GLU B 201  ? 0.5463 0.4565 0.3455 -0.0003 -0.0178 0.0067  199  GLU B CD  
10563 O OE1 . GLU B 201  ? 0.5568 0.4638 0.3450 -0.0008 -0.0163 0.0077  199  GLU B OE1 
10564 O OE2 . GLU B 201  ? 0.6011 0.5123 0.4065 0.0026  -0.0213 0.0035  199  GLU B OE2 
10565 N N   . THR B 202  ? 0.3938 0.2910 0.1812 -0.0131 -0.0161 0.0214  200  THR B N   
10566 C CA  . THR B 202  ? 0.3984 0.2856 0.1804 -0.0134 -0.0214 0.0236  200  THR B CA  
10567 C C   . THR B 202  ? 0.4461 0.3301 0.2235 -0.0185 -0.0191 0.0281  200  THR B C   
10568 O O   . THR B 202  ? 0.4293 0.3183 0.2053 -0.0218 -0.0135 0.0298  200  THR B O   
10569 C CB  . THR B 202  ? 0.4445 0.3237 0.2148 -0.0112 -0.0254 0.0236  200  THR B CB  
10570 O OG1 . THR B 202  ? 0.4472 0.3252 0.2068 -0.0138 -0.0214 0.0259  200  THR B OG1 
10571 C CG2 . THR B 202  ? 0.5127 0.3952 0.2869 -0.0068 -0.0276 0.0191  200  THR B CG2 
10572 N N   . ILE B 203  ? 0.4060 0.2813 0.1804 -0.0191 -0.0236 0.0302  201  ILE B N   
10573 C CA  . ILE B 203  ? 0.4537 0.3245 0.2229 -0.0242 -0.0218 0.0347  201  ILE B CA  
10574 C C   . ILE B 203  ? 0.4292 0.2956 0.1848 -0.0268 -0.0196 0.0378  201  ILE B C   
10575 O O   . ILE B 203  ? 0.4251 0.2928 0.1776 -0.0317 -0.0153 0.0411  201  ILE B O   
10576 C CB  . ILE B 203  ? 0.4223 0.2837 0.1907 -0.0240 -0.0274 0.0361  201  ILE B CB  
10577 C CG1 . ILE B 203  ? 0.4184 0.2764 0.1839 -0.0298 -0.0252 0.0403  201  ILE B CG1 
10578 C CG2 . ILE B 203  ? 0.4146 0.2654 0.1724 -0.0212 -0.0330 0.0367  201  ILE B CG2 
10579 C CD1 . ILE B 203  ? 0.3977 0.2660 0.1745 -0.0326 -0.0206 0.0397  201  ILE B CD1 
10580 N N   . ARG B 204  ? 0.4030 0.2646 0.1502 -0.0237 -0.0224 0.0369  202  ARG B N   
10581 C CA  . ARG B 204  ? 0.4645 0.3222 0.1983 -0.0259 -0.0201 0.0397  202  ARG B CA  
10582 C C   . ARG B 204  ? 0.4301 0.2982 0.1660 -0.0280 -0.0125 0.0394  202  ARG B C   
10583 O O   . ARG B 204  ? 0.4784 0.3463 0.2073 -0.0324 -0.0083 0.0429  202  ARG B O   
10584 C CB  . ARG B 204  ? 0.4708 0.3223 0.1960 -0.0218 -0.0246 0.0381  202  ARG B CB  
10585 C CG  . ARG B 204  ? 0.5478 0.3930 0.2573 -0.0239 -0.0231 0.0413  202  ARG B CG  
10586 C CD  . ARG B 204  ? 0.6019 0.4404 0.3028 -0.0198 -0.0284 0.0397  202  ARG B CD  
10587 N NE  . ARG B 204  ? 0.5802 0.4262 0.2876 -0.0158 -0.0281 0.0347  202  ARG B NE  
10588 C CZ  . ARG B 204  ? 0.6974 0.5490 0.4019 -0.0157 -0.0233 0.0333  202  ARG B CZ  
10589 N NH1 . ARG B 204  ? 0.7171 0.5682 0.4122 -0.0192 -0.0184 0.0363  202  ARG B NH1 
10590 N NH2 . ARG B 204  ? 0.6900 0.5478 0.4013 -0.0121 -0.0234 0.0286  202  ARG B NH2 
10591 N N   . GLU B 205  ? 0.4321 0.3096 0.1778 -0.0250 -0.0107 0.0352  203  GLU B N   
10592 C CA  . GLU B 205  ? 0.4347 0.3222 0.1827 -0.0262 -0.0037 0.0346  203  GLU B CA  
10593 C C   . GLU B 205  ? 0.4347 0.3289 0.1901 -0.0307 0.0008  0.0369  203  GLU B C   
10594 O O   . GLU B 205  ? 0.4445 0.3433 0.1966 -0.0342 0.0064  0.0393  203  GLU B O   
10595 C CB  . GLU B 205  ? 0.4449 0.3395 0.2010 -0.0214 -0.0036 0.0295  203  GLU B CB  
10596 C CG  . GLU B 205  ? 0.5120 0.4168 0.2710 -0.0214 0.0031  0.0281  203  GLU B CG  
10597 C CD  . GLU B 205  ? 0.5602 0.4692 0.3251 -0.0164 0.0022  0.0230  203  GLU B CD  
10598 O OE1 . GLU B 205  ? 0.6692 0.5742 0.4258 -0.0138 0.0008  0.0213  203  GLU B OE1 
10599 O OE2 . GLU B 205  ? 0.5545 0.4702 0.3318 -0.0152 0.0027  0.0208  203  GLU B OE2 
10600 N N   . ALA B 206  ? 0.4083 0.3032 0.1735 -0.0308 -0.0018 0.0364  204  ALA B N   
10601 C CA  . ALA B 206  ? 0.3793 0.2800 0.1517 -0.0353 0.0018  0.0385  204  ALA B CA  
10602 C C   . ALA B 206  ? 0.4239 0.3186 0.1867 -0.0410 0.0030  0.0437  204  ALA B C   
10603 O O   . ALA B 206  ? 0.4130 0.3143 0.1772 -0.0453 0.0084  0.0460  204  ALA B O   
10604 C CB  . ALA B 206  ? 0.3520 0.2524 0.1348 -0.0342 -0.0020 0.0370  204  ALA B CB  
10605 N N   . LEU B 207  ? 0.4196 0.3016 0.1724 -0.0410 -0.0020 0.0457  205  LEU B N   
10606 C CA  . LEU B 207  ? 0.4535 0.3283 0.1964 -0.0466 -0.0013 0.0509  205  LEU B CA  
10607 C C   . LEU B 207  ? 0.4806 0.3585 0.2147 -0.0490 0.0042  0.0530  205  LEU B C   
10608 O O   . LEU B 207  ? 0.5053 0.3847 0.2364 -0.0548 0.0082  0.0569  205  LEU B O   
10609 C CB  . LEU B 207  ? 0.4628 0.3229 0.1962 -0.0454 -0.0080 0.0524  205  LEU B CB  
10610 C CG  . LEU B 207  ? 0.4586 0.3135 0.1985 -0.0443 -0.0133 0.0516  205  LEU B CG  
10611 C CD1 . LEU B 207  ? 0.4938 0.3353 0.2248 -0.0412 -0.0202 0.0521  205  LEU B CD1 
10612 C CD2 . LEU B 207  ? 0.4645 0.3190 0.2068 -0.0504 -0.0113 0.0550  205  LEU B CD2 
10613 N N   . LYS B 208  ? 0.4649 0.3438 0.1945 -0.0449 0.0045  0.0505  206  LYS B N   
10614 C CA  . LYS B 208  ? 0.4939 0.3755 0.2143 -0.0466 0.0098  0.0522  206  LYS B CA  
10615 C C   . LYS B 208  ? 0.4713 0.3669 0.2002 -0.0490 0.0172  0.0520  206  LYS B C   
10616 O O   . LYS B 208  ? 0.5038 0.4023 0.2271 -0.0534 0.0224  0.0554  206  LYS B O   
10617 C CB  . LYS B 208  ? 0.5464 0.4256 0.2604 -0.0412 0.0080  0.0489  206  LYS B CB  
10618 C CG  . LYS B 208  ? 0.6488 0.5261 0.3491 -0.0429 0.0117  0.0512  206  LYS B CG  
10619 C CD  . LYS B 208  ? 0.7463 0.6193 0.4394 -0.0375 0.0087  0.0480  206  LYS B CD  
10620 C CE  . LYS B 208  ? 0.7501 0.6332 0.4512 -0.0333 0.0116  0.0430  206  LYS B CE  
10621 N NZ  . LYS B 208  ? 0.7893 0.6680 0.4815 -0.0289 0.0093  0.0402  206  LYS B NZ  
10622 N N   . ARG B 209  ? 0.4721 0.3768 0.2146 -0.0462 0.0178  0.0483  207  ARG B N   
10623 C CA  . ARG B 209  ? 0.4536 0.3722 0.2053 -0.0476 0.0245  0.0478  207  ARG B CA  
10624 C C   . ARG B 209  ? 0.4807 0.4030 0.2385 -0.0536 0.0264  0.0512  207  ARG B C   
10625 O O   . ARG B 209  ? 0.5110 0.4451 0.2759 -0.0556 0.0320  0.0516  207  ARG B O   
10626 C CB  . ARG B 209  ? 0.4450 0.3713 0.2085 -0.0423 0.0241  0.0426  207  ARG B CB  
10627 C CG  . ARG B 209  ? 0.4708 0.3947 0.2287 -0.0368 0.0229  0.0391  207  ARG B CG  
10628 C CD  . ARG B 209  ? 0.4395 0.3693 0.2090 -0.0318 0.0217  0.0341  207  ARG B CD  
10629 N NE  . ARG B 209  ? 0.5424 0.4709 0.3070 -0.0269 0.0211  0.0306  207  ARG B NE  
10630 C CZ  . ARG B 209  ? 0.5737 0.5056 0.3458 -0.0223 0.0197  0.0261  207  ARG B CZ  
10631 N NH1 . ARG B 209  ? 0.4929 0.4298 0.2779 -0.0218 0.0187  0.0246  207  ARG B NH1 
10632 N NH2 . ARG B 209  ? 0.5713 0.5012 0.3377 -0.0184 0.0191  0.0231  207  ARG B NH2 
10633 N N   . SER B 210  ? 0.4425 0.3548 0.1976 -0.0563 0.0217  0.0537  208  SER B N   
10634 C CA  . SER B 210  ? 0.4624 0.3767 0.2227 -0.0622 0.0227  0.0568  208  SER B CA  
10635 C C   . SER B 210  ? 0.4705 0.3829 0.2214 -0.0689 0.0263  0.0621  208  SER B C   
10636 O O   . SER B 210  ? 0.4699 0.3869 0.2255 -0.0744 0.0288  0.0649  208  SER B O   
10637 C CB  . SER B 210  ? 0.4363 0.3403 0.1980 -0.0619 0.0159  0.0568  208  SER B CB  
10638 O OG  . SER B 210  ? 0.4481 0.3550 0.2198 -0.0564 0.0130  0.0521  208  SER B OG  
10639 N N   . LYS B 211  ? 0.4736 0.3791 0.2110 -0.0686 0.0266  0.0638  209  LYS B N   
10640 C CA  . LYS B 211  ? 0.4747 0.3781 0.2050 -0.0742 0.0293  0.0685  209  LYS B CA  
10641 C C   . LYS B 211  ? 0.4891 0.4076 0.2267 -0.0774 0.0369  0.0696  209  LYS B C   
10642 O O   . LYS B 211  ? 0.4871 0.4075 0.2265 -0.0830 0.0390  0.0731  209  LYS B O   
10643 C CB  . LYS B 211  ? 0.5034 0.3990 0.2219 -0.0714 0.0280  0.0688  209  LYS B CB  
10644 C CG  . LYS B 211  ? 0.5793 0.4616 0.2915 -0.0671 0.0204  0.0671  209  LYS B CG  
10645 C CD  . LYS B 211  ? 0.5780 0.4494 0.2891 -0.0700 0.0152  0.0696  209  LYS B CD  
10646 C CE  . LYS B 211  ? 0.6825 0.5412 0.3878 -0.0651 0.0076  0.0679  209  LYS B CE  
10647 N NZ  . LYS B 211  ? 0.6609 0.5086 0.3653 -0.0671 0.0023  0.0700  209  LYS B NZ  
10648 N N   . GLU B 212  ? 0.4603 0.3898 0.2026 -0.0739 0.0411  0.0664  210  GLU B N   
10649 C CA  . GLU B 212  ? 0.5019 0.4464 0.2511 -0.0758 0.0485  0.0671  210  GLU B CA  
10650 C C   . GLU B 212  ? 0.4977 0.4495 0.2578 -0.0812 0.0499  0.0691  210  GLU B C   
10651 O O   . GLU B 212  ? 0.4922 0.4495 0.2546 -0.0859 0.0536  0.0723  210  GLU B O   
10652 C CB  . GLU B 212  ? 0.5512 0.5053 0.3041 -0.0703 0.0519  0.0628  210  GLU B CB  
10653 C CG  . GLU B 212  ? 0.6358 0.6068 0.3984 -0.0713 0.0593  0.0629  210  GLU B CG  
10654 C CD  . GLU B 212  ? 0.7044 0.6839 0.4708 -0.0653 0.0622  0.0583  210  GLU B CD  
10655 O OE1 . GLU B 212  ? 0.7880 0.7604 0.5471 -0.0602 0.0597  0.0554  210  GLU B OE1 
10656 O OE2 . GLU B 212  ? 0.7979 0.7910 0.5754 -0.0653 0.0666  0.0573  210  GLU B OE2 
10657 N N   . LEU B 213  ? 0.4815 0.4336 0.2486 -0.0806 0.0470  0.0672  211  LEU B N   
10658 C CA  . LEU B 213  ? 0.4786 0.4380 0.2566 -0.0855 0.0480  0.0687  211  LEU B CA  
10659 C C   . LEU B 213  ? 0.4642 0.4123 0.2385 -0.0908 0.0437  0.0723  211  LEU B C   
10660 O O   . LEU B 213  ? 0.4576 0.4110 0.2384 -0.0962 0.0454  0.0746  211  LEU B O   
10661 C CB  . LEU B 213  ? 0.4065 0.3718 0.1980 -0.0808 0.0458  0.0642  211  LEU B CB  
10662 C CG  . LEU B 213  ? 0.4693 0.4483 0.2685 -0.0756 0.0505  0.0605  211  LEU B CG  
10663 C CD1 . LEU B 213  ? 0.4852 0.4700 0.2981 -0.0715 0.0483  0.0564  211  LEU B CD1 
10664 C CD2 . LEU B 213  ? 0.5378 0.5302 0.3393 -0.0796 0.0580  0.0631  211  LEU B CD2 
10665 N N   . GLU B 214  ? 0.4210 0.3534 0.1849 -0.0893 0.0381  0.0726  212  GLU B N   
10666 C CA  . GLU B 214  ? 0.4040 0.3251 0.1636 -0.0940 0.0342  0.0759  212  GLU B CA  
10667 C C   . GLU B 214  ? 0.4704 0.3941 0.2272 -0.0988 0.0381  0.0797  212  GLU B C   
10668 O O   . GLU B 214  ? 0.4853 0.4066 0.2437 -0.1046 0.0373  0.0825  212  GLU B O   
10669 C CB  . GLU B 214  ? 0.4353 0.3396 0.1843 -0.0905 0.0276  0.0754  212  GLU B CB  
10670 C CG  . GLU B 214  ? 0.4415 0.3414 0.1948 -0.0868 0.0224  0.0724  212  GLU B CG  
10671 C CD  . GLU B 214  ? 0.4936 0.3774 0.2375 -0.0832 0.0156  0.0719  212  GLU B CD  
10672 O OE1 . GLU B 214  ? 0.5135 0.3909 0.2469 -0.0823 0.0152  0.0733  212  GLU B OE1 
10673 O OE2 . GLU B 214  ? 0.4611 0.3401 0.2103 -0.0805 0.0106  0.0697  212  GLU B OE2 
10674 N N   . GLU B 215  ? 0.4744 0.4027 0.2265 -0.0966 0.0423  0.0796  213  GLU B N   
10675 C CA  . GLU B 215  ? 0.5160 0.4476 0.2654 -0.1010 0.0465  0.0831  213  GLU B CA  
10676 C C   . GLU B 215  ? 0.5110 0.4579 0.2722 -0.1052 0.0518  0.0842  213  GLU B C   
10677 O O   . GLU B 215  ? 0.5281 0.4772 0.2887 -0.1102 0.0545  0.0876  213  GLU B O   
10678 C CB  . GLU B 215  ? 0.5367 0.4696 0.2782 -0.0969 0.0496  0.0825  213  GLU B CB  
10679 C CG  . GLU B 215  ? 0.6103 0.5273 0.3389 -0.0938 0.0441  0.0824  213  GLU B CG  
10680 C CD  . GLU B 215  ? 0.7498 0.6683 0.4710 -0.0890 0.0466  0.0809  213  GLU B CD  
10681 O OE1 . GLU B 215  ? 0.7455 0.6736 0.4673 -0.0902 0.0528  0.0822  213  GLU B OE1 
10682 O OE2 . GLU B 215  ? 0.7370 0.6472 0.4519 -0.0840 0.0423  0.0785  213  GLU B OE2 
10683 N N   . LYS B 216  ? 0.5050 0.4627 0.2771 -0.1032 0.0533  0.0814  214  LYS B N   
10684 C CA  . LYS B 216  ? 0.4958 0.4680 0.2803 -0.1069 0.0576  0.0822  214  LYS B CA  
10685 C C   . LYS B 216  ? 0.5517 0.5208 0.3422 -0.1119 0.0538  0.0833  214  LYS B C   
10686 O O   . LYS B 216  ? 0.5064 0.4863 0.3067 -0.1159 0.0566  0.0844  214  LYS B O   
10687 C CB  . LYS B 216  ? 0.4944 0.4808 0.2883 -0.1021 0.0613  0.0785  214  LYS B CB  
10688 C CG  . LYS B 216  ? 0.5379 0.5297 0.3275 -0.0972 0.0660  0.0771  214  LYS B CG  
10689 C CD  . LYS B 216  ? 0.6154 0.6201 0.4145 -0.0921 0.0692  0.0732  214  LYS B CD  
10690 C CE  . LYS B 216  ? 0.6844 0.6929 0.4783 -0.0865 0.0732  0.0711  214  LYS B CE  
10691 N NZ  . LYS B 216  ? 0.7552 0.7737 0.5571 -0.0808 0.0752  0.0668  214  LYS B NZ  
10692 N N   . GLY B 217  ? 0.4831 0.4376 0.2679 -0.1116 0.0473  0.0830  215  GLY B N   
10693 C CA  . GLY B 217  ? 0.4829 0.4328 0.2722 -0.1160 0.0434  0.0840  215  GLY B CA  
10694 C C   . GLY B 217  ? 0.4679 0.4162 0.2622 -0.1128 0.0396  0.0808  215  GLY B C   
10695 O O   . GLY B 217  ? 0.4656 0.4105 0.2641 -0.1162 0.0364  0.0813  215  GLY B O   
10696 N N   . PHE B 218  ? 0.4190 0.3696 0.2129 -0.1066 0.0400  0.0776  216  PHE B N   
10697 C CA  . PHE B 218  ? 0.4020 0.3492 0.1994 -0.1029 0.0359  0.0746  216  PHE B CA  
10698 C C   . PHE B 218  ? 0.4247 0.3536 0.2124 -0.1008 0.0291  0.0744  216  PHE B C   
10699 O O   . PHE B 218  ? 0.4416 0.3606 0.2175 -0.1014 0.0281  0.0766  216  PHE B O   
10700 C CB  . PHE B 218  ? 0.3915 0.3480 0.1952 -0.0950 0.0379  0.0698  216  PHE B CB  
10701 C CG  . PHE B 218  ? 0.3993 0.3741 0.2146 -0.0955 0.0437  0.0689  216  PHE B CG  
10702 C CD1 . PHE B 218  ? 0.4026 0.3868 0.2156 -0.0980 0.0502  0.0712  216  PHE B CD1 
10703 C CD2 . PHE B 218  ? 0.3928 0.3755 0.2214 -0.0930 0.0427  0.0658  216  PHE B CD2 
10704 C CE1 . PHE B 218  ? 0.4522 0.4535 0.2767 -0.0975 0.0554  0.0701  216  PHE B CE1 
10705 C CE2 . PHE B 218  ? 0.3814 0.3809 0.2207 -0.0930 0.0479  0.0650  216  PHE B CE2 
10706 C CZ  . PHE B 218  ? 0.3764 0.3854 0.2136 -0.0953 0.0543  0.0673  216  PHE B CZ  
10707 N N   . SER B 219  ? 0.3928 0.3178 0.1869 -0.0975 0.0242  0.0714  217  SER B N   
10708 C CA  . SER B 219  ? 0.3923 0.3019 0.1796 -0.0935 0.0177  0.0701  217  SER B CA  
10709 C C   . SER B 219  ? 0.3705 0.2842 0.1663 -0.0855 0.0156  0.0646  217  SER B C   
10710 O O   . SER B 219  ? 0.3467 0.2739 0.1528 -0.0834 0.0191  0.0621  217  SER B O   
10711 C CB  . SER B 219  ? 0.3793 0.2778 0.1643 -0.0981 0.0132  0.0724  217  SER B CB  
10712 O OG  . SER B 219  ? 0.4109 0.3168 0.2084 -0.0988 0.0130  0.0704  217  SER B OG  
10713 N N   . TYR B 220  ? 0.3909 0.2929 0.1826 -0.0809 0.0098  0.0627  218  TYR B N   
10714 C CA  . TYR B 220  ? 0.3507 0.2557 0.1490 -0.0733 0.0076  0.0577  218  TYR B CA  
10715 C C   . TYR B 220  ? 0.3458 0.2417 0.1464 -0.0707 0.0015  0.0559  218  TYR B C   
10716 O O   . TYR B 220  ? 0.3573 0.2407 0.1503 -0.0730 -0.0023 0.0583  218  TYR B O   
10717 C CB  . TYR B 220  ? 0.3553 0.2570 0.1457 -0.0684 0.0073  0.0565  218  TYR B CB  
10718 C CG  . TYR B 220  ? 0.3607 0.2746 0.1529 -0.0679 0.0134  0.0559  218  TYR B CG  
10719 C CD1 . TYR B 220  ? 0.3966 0.3127 0.1818 -0.0728 0.0180  0.0597  218  TYR B CD1 
10720 C CD2 . TYR B 220  ? 0.3372 0.2605 0.1383 -0.0625 0.0147  0.0515  218  TYR B CD2 
10721 C CE1 . TYR B 220  ? 0.3844 0.3119 0.1713 -0.0720 0.0238  0.0590  218  TYR B CE1 
10722 C CE2 . TYR B 220  ? 0.3528 0.2868 0.1553 -0.0616 0.0203  0.0508  218  TYR B CE2 
10723 C CZ  . TYR B 220  ? 0.3523 0.2885 0.1478 -0.0662 0.0249  0.0545  218  TYR B CZ  
10724 O OH  . TYR B 220  ? 0.4278 0.3749 0.2246 -0.0649 0.0307  0.0537  218  TYR B OH  
10725 N N   . SER B 221  ? 0.3319 0.2342 0.1429 -0.0657 0.0006  0.0516  219  SER B N   
10726 C CA  . SER B 221  ? 0.3335 0.2287 0.1472 -0.0615 -0.0051 0.0489  219  SER B CA  
10727 C C   . SER B 221  ? 0.3182 0.2183 0.1367 -0.0545 -0.0057 0.0446  219  SER B C   
10728 O O   . SER B 221  ? 0.3199 0.2319 0.1473 -0.0530 -0.0022 0.0423  219  SER B O   
10729 C CB  . SER B 221  ? 0.3384 0.2369 0.1614 -0.0637 -0.0056 0.0482  219  SER B CB  
10730 O OG  . SER B 221  ? 0.3517 0.2436 0.1771 -0.0592 -0.0107 0.0455  219  SER B OG  
10731 N N   . TYR B 222  ? 0.3243 0.2153 0.1367 -0.0501 -0.0101 0.0434  220  TYR B N   
10732 C CA  . TYR B 222  ? 0.3155 0.2107 0.1312 -0.0439 -0.0108 0.0396  220  TYR B CA  
10733 C C   . TYR B 222  ? 0.3454 0.2425 0.1710 -0.0396 -0.0138 0.0358  220  TYR B C   
10734 O O   . TYR B 222  ? 0.3397 0.2289 0.1648 -0.0391 -0.0180 0.0359  220  TYR B O   
10735 C CB  . TYR B 222  ? 0.3265 0.2121 0.1308 -0.0413 -0.0139 0.0402  220  TYR B CB  
10736 C CG  . TYR B 222  ? 0.3372 0.2226 0.1320 -0.0452 -0.0100 0.0436  220  TYR B CG  
10737 C CD1 . TYR B 222  ? 0.3488 0.2441 0.1453 -0.0447 -0.0051 0.0426  220  TYR B CD1 
10738 C CD2 . TYR B 222  ? 0.3513 0.2268 0.1357 -0.0497 -0.0110 0.0480  220  TYR B CD2 
10739 C CE1 . TYR B 222  ? 0.3434 0.2391 0.1313 -0.0482 -0.0012 0.0457  220  TYR B CE1 
10740 C CE2 . TYR B 222  ? 0.3686 0.2443 0.1444 -0.0536 -0.0072 0.0513  220  TYR B CE2 
10741 C CZ  . TYR B 222  ? 0.3637 0.2498 0.1414 -0.0528 -0.0022 0.0501  220  TYR B CZ  
10742 O OH  . TYR B 222  ? 0.3688 0.2556 0.1379 -0.0566 0.0020  0.0533  220  TYR B OH  
10743 N N   . ASP B 223  ? 0.3366 0.2441 0.1709 -0.0366 -0.0115 0.0326  221  ASP B N   
10744 C CA  . ASP B 223  ? 0.3693 0.2807 0.2138 -0.0326 -0.0135 0.0289  221  ASP B CA  
10745 C C   . ASP B 223  ? 0.3986 0.3091 0.2420 -0.0270 -0.0159 0.0259  221  ASP B C   
10746 O O   . ASP B 223  ? 0.3640 0.2811 0.2088 -0.0255 -0.0130 0.0244  221  ASP B O   
10747 C CB  . ASP B 223  ? 0.3632 0.2869 0.2180 -0.0338 -0.0090 0.0277  221  ASP B CB  
10748 C CG  . ASP B 223  ? 0.4358 0.3647 0.3010 -0.0295 -0.0104 0.0238  221  ASP B CG  
10749 O OD1 . ASP B 223  ? 0.4256 0.3485 0.2909 -0.0262 -0.0149 0.0221  221  ASP B OD1 
10750 O OD2 . ASP B 223  ? 0.4747 0.4139 0.3477 -0.0292 -0.0069 0.0224  221  ASP B OD2 
10751 N N   . MET B 224  ? 0.3981 0.3002 0.2390 -0.0240 -0.0211 0.0251  222  MET B N   
10752 C CA  . MET B 224  ? 0.4185 0.3191 0.2578 -0.0191 -0.0240 0.0226  222  MET B CA  
10753 C C   . MET B 224  ? 0.4739 0.3825 0.3242 -0.0152 -0.0241 0.0185  222  MET B C   
10754 O O   . MET B 224  ? 0.5697 0.4770 0.4200 -0.0111 -0.0272 0.0162  222  MET B O   
10755 C CB  . MET B 224  ? 0.4607 0.3497 0.2931 -0.0173 -0.0298 0.0235  222  MET B CB  
10756 C CG  . MET B 224  ? 0.4414 0.3212 0.2619 -0.0211 -0.0301 0.0278  222  MET B CG  
10757 S SD  . MET B 224  ? 0.4826 0.3638 0.2936 -0.0231 -0.0262 0.0297  222  MET B SD  
10758 C CE  . MET B 224  ? 0.4162 0.2965 0.2257 -0.0171 -0.0299 0.0263  222  MET B CE  
10759 N N   . LEU B 225  ? 0.5135 0.4303 0.3729 -0.0166 -0.0209 0.0177  223  LEU B N   
10760 C CA  . LEU B 225  ? 0.4910 0.4164 0.3601 -0.0135 -0.0198 0.0141  223  LEU B CA  
10761 C C   . LEU B 225  ? 0.6001 0.5230 0.4735 -0.0093 -0.0245 0.0115  223  LEU B C   
10762 O O   . LEU B 225  ? 0.6462 0.5722 0.5228 -0.0059 -0.0254 0.0087  223  LEU B O   
10763 C CB  . LEU B 225  ? 0.4513 0.3814 0.3187 -0.0122 -0.0171 0.0129  223  LEU B CB  
10764 C CG  . LEU B 225  ? 0.4553 0.3914 0.3218 -0.0157 -0.0114 0.0147  223  LEU B CG  
10765 C CD1 . LEU B 225  ? 0.4252 0.3665 0.2910 -0.0136 -0.0086 0.0129  223  LEU B CD1 
10766 C CD2 . LEU B 225  ? 0.4215 0.3645 0.2972 -0.0178 -0.0089 0.0149  223  LEU B CD2 
10767 N N   . GLY B 226  ? 0.5797 0.4969 0.4532 -0.0096 -0.0275 0.0123  224  GLY B N   
10768 C CA  . GLY B 226  ? 0.5463 0.4622 0.4250 -0.0057 -0.0314 0.0099  224  GLY B CA  
10769 C C   . GLY B 226  ? 0.4465 0.3654 0.3329 -0.0067 -0.0306 0.0093  224  GLY B C   
10770 O O   . GLY B 226  ? 0.4590 0.3754 0.3433 -0.0103 -0.0295 0.0116  224  GLY B O   
10771 N N   . GLU B 227  ? 0.4349 0.3591 0.3301 -0.0036 -0.0313 0.0063  225  GLU B N   
10772 C CA  . GLU B 227  ? 0.4070 0.3334 0.3090 -0.0040 -0.0310 0.0056  225  GLU B CA  
10773 C C   . GLU B 227  ? 0.3546 0.2851 0.2646 0.0001  -0.0328 0.0023  225  GLU B C   
10774 O O   . GLU B 227  ? 0.3584 0.2920 0.2700 0.0026  -0.0333 0.0005  225  GLU B O   
10775 C CB  . GLU B 227  ? 0.4164 0.3500 0.3228 -0.0076 -0.0264 0.0064  225  GLU B CB  
10776 C CG  . GLU B 227  ? 0.3913 0.3343 0.3040 -0.0064 -0.0234 0.0044  225  GLU B CG  
10777 C CD  . GLU B 227  ? 0.3950 0.3446 0.3110 -0.0099 -0.0190 0.0056  225  GLU B CD  
10778 O OE1 . GLU B 227  ? 0.4057 0.3558 0.3167 -0.0124 -0.0165 0.0076  225  GLU B OE1 
10779 O OE2 . GLU B 227  ? 0.3914 0.3459 0.3147 -0.0101 -0.0180 0.0046  225  GLU B OE2 
10780 N N   . ALA B 228  ? 0.2977 0.2277 0.2122 0.0006  -0.0338 0.0016  226  ALA B N   
10781 C CA  . ALA B 228  ? 0.2993 0.2343 0.2224 0.0039  -0.0346 -0.0013 226  ALA B CA  
10782 C C   . ALA B 228  ? 0.3047 0.2383 0.2275 0.0080  -0.0381 -0.0030 226  ALA B C   
10783 O O   . ALA B 228  ? 0.3363 0.2758 0.2639 0.0098  -0.0376 -0.0050 226  ALA B O   
10784 C CB  . ALA B 228  ? 0.3560 0.3007 0.2863 0.0031  -0.0308 -0.0026 226  ALA B CB  
10785 N N   . ALA B 229  ? 0.2792 0.2046 0.1962 0.0095  -0.0419 -0.0021 227  ALA B N   
10786 C CA  . ALA B 229  ? 0.2594 0.1837 0.1770 0.0137  -0.0457 -0.0038 227  ALA B CA  
10787 C C   . ALA B 229  ? 0.2471 0.1782 0.1747 0.0165  -0.0459 -0.0067 227  ALA B C   
10788 O O   . ALA B 229  ? 0.2916 0.2236 0.2232 0.0162  -0.0450 -0.0071 227  ALA B O   
10789 C CB  . ALA B 229  ? 0.2753 0.1898 0.1860 0.0153  -0.0498 -0.0024 227  ALA B CB  
10790 N N   . THR B 230  ? 0.2664 0.2022 0.1977 0.0188  -0.0469 -0.0086 228  THR B N   
10791 C CA  . THR B 230  ? 0.2888 0.2311 0.2294 0.0214  -0.0473 -0.0112 228  THR B CA  
10792 C C   . THR B 230  ? 0.2435 0.1834 0.1848 0.0254  -0.0518 -0.0122 228  THR B C   
10793 O O   . THR B 230  ? 0.2551 0.1983 0.2031 0.0276  -0.0522 -0.0139 228  THR B O   
10794 C CB  . THR B 230  ? 0.2991 0.2485 0.2440 0.0212  -0.0458 -0.0128 228  THR B CB  
10795 O OG1 . THR B 230  ? 0.3497 0.3014 0.2938 0.0179  -0.0417 -0.0119 228  THR B OG1 
10796 C CG2 . THR B 230  ? 0.2815 0.2380 0.2362 0.0231  -0.0456 -0.0153 228  THR B CG2 
10797 N N   . THR B 231  ? 0.2430 0.1774 0.1777 0.0267  -0.0551 -0.0113 229  THR B N   
10798 C CA  . THR B 231  ? 0.2369 0.1693 0.1721 0.0308  -0.0596 -0.0122 229  THR B CA  
10799 C C   . THR B 231  ? 0.2811 0.2032 0.2070 0.0314  -0.0624 -0.0099 229  THR B C   
10800 O O   . THR B 231  ? 0.2646 0.1812 0.1829 0.0282  -0.0610 -0.0076 229  THR B O   
10801 C CB  . THR B 231  ? 0.2504 0.1867 0.1870 0.0324  -0.0619 -0.0135 229  THR B CB  
10802 O OG1 . THR B 231  ? 0.2763 0.2070 0.2036 0.0308  -0.0626 -0.0117 229  THR B OG1 
10803 C CG2 . THR B 231  ? 0.2683 0.2138 0.2129 0.0312  -0.0590 -0.0155 229  THR B CG2 
10804 N N   . ALA B 232  ? 0.2525 0.1720 0.1789 0.0356  -0.0665 -0.0105 230  ALA B N   
10805 C CA  . ALA B 232  ? 0.2779 0.1869 0.1950 0.0368  -0.0699 -0.0085 230  ALA B CA  
10806 C C   . ALA B 232  ? 0.2863 0.1912 0.1950 0.0352  -0.0711 -0.0067 230  ALA B C   
10807 O O   . ALA B 232  ? 0.3147 0.2110 0.2140 0.0332  -0.0713 -0.0040 230  ALA B O   
10808 C CB  . ALA B 232  ? 0.2675 0.1758 0.1875 0.0423  -0.0743 -0.0098 230  ALA B CB  
10809 N N   . ALA B 233  ? 0.2804 0.1912 0.1918 0.0359  -0.0718 -0.0081 231  ALA B N   
10810 C CA  . ALA B 233  ? 0.2760 0.1830 0.1790 0.0347  -0.0731 -0.0066 231  ALA B CA  
10811 C C   . ALA B 233  ? 0.2827 0.1880 0.1803 0.0297  -0.0687 -0.0048 231  ALA B C   
10812 O O   . ALA B 233  ? 0.2933 0.1917 0.1809 0.0281  -0.0693 -0.0024 231  ALA B O   
10813 C CB  . ALA B 233  ? 0.2749 0.1890 0.1825 0.0361  -0.0747 -0.0088 231  ALA B CB  
10814 N N   . ASP B 234  ? 0.2782 0.1899 0.1822 0.0274  -0.0641 -0.0057 232  ASP B N   
10815 C CA  . ASP B 234  ? 0.2857 0.1969 0.1857 0.0228  -0.0597 -0.0039 232  ASP B CA  
10816 C C   . ASP B 234  ? 0.2710 0.1732 0.1633 0.0209  -0.0597 -0.0010 232  ASP B C   
10817 O O   . ASP B 234  ? 0.2840 0.1817 0.1679 0.0180  -0.0585 0.0014  232  ASP B O   
10818 C CB  . ASP B 234  ? 0.2680 0.1873 0.1767 0.0211  -0.0553 -0.0053 232  ASP B CB  
10819 C CG  . ASP B 234  ? 0.3291 0.2568 0.2445 0.0218  -0.0542 -0.0079 232  ASP B CG  
10820 O OD1 . ASP B 234  ? 0.3508 0.2784 0.2629 0.0225  -0.0557 -0.0083 232  ASP B OD1 
10821 O OD2 . ASP B 234  ? 0.3245 0.2588 0.2483 0.0215  -0.0517 -0.0094 232  ASP B OD2 
10822 N N   . ALA B 235  ? 0.2622 0.1620 0.1573 0.0223  -0.0609 -0.0012 233  ALA B N   
10823 C CA  . ALA B 235  ? 0.2761 0.1672 0.1645 0.0202  -0.0609 0.0014  233  ALA B CA  
10824 C C   . ALA B 235  ? 0.2849 0.1659 0.1626 0.0211  -0.0647 0.0036  233  ALA B C   
10825 O O   . ALA B 235  ? 0.3039 0.1780 0.1731 0.0177  -0.0638 0.0066  233  ALA B O   
10826 C CB  . ALA B 235  ? 0.2803 0.1706 0.1738 0.0221  -0.0618 0.0002  233  ALA B CB  
10827 N N   . GLU B 236  ? 0.2850 0.1654 0.1630 0.0255  -0.0690 0.0024  234  GLU B N   
10828 C CA  . GLU B 236  ? 0.3257 0.1965 0.1933 0.0268  -0.0730 0.0046  234  GLU B CA  
10829 C C   . GLU B 236  ? 0.3161 0.1858 0.1761 0.0236  -0.0714 0.0064  234  GLU B C   
10830 O O   . GLU B 236  ? 0.3344 0.1950 0.1837 0.0217  -0.0723 0.0094  234  GLU B O   
10831 C CB  . GLU B 236  ? 0.3239 0.1956 0.1945 0.0325  -0.0781 0.0027  234  GLU B CB  
10832 C CG  . GLU B 236  ? 0.3774 0.2385 0.2374 0.0345  -0.0829 0.0050  234  GLU B CG  
10833 C CD  . GLU B 236  ? 0.4927 0.3550 0.3562 0.0405  -0.0882 0.0031  234  GLU B CD  
10834 O OE1 . GLU B 236  ? 0.4920 0.3644 0.3660 0.0426  -0.0880 0.0001  234  GLU B OE1 
10835 O OE2 . GLU B 236  ? 0.4951 0.3484 0.3508 0.0430  -0.0926 0.0049  234  GLU B OE2 
10836 N N   . ARG B 237  ? 0.2859 0.1645 0.1507 0.0228  -0.0689 0.0046  235  ARG B N   
10837 C CA  . ARG B 237  ? 0.3137 0.1918 0.1714 0.0199  -0.0669 0.0060  235  ARG B CA  
10838 C C   . ARG B 237  ? 0.3073 0.1832 0.1606 0.0148  -0.0624 0.0086  235  ARG B C   
10839 O O   . ARG B 237  ? 0.3181 0.1877 0.1612 0.0124  -0.0621 0.0114  235  ARG B O   
10840 C CB  . ARG B 237  ? 0.3257 0.2136 0.1899 0.0203  -0.0651 0.0032  235  ARG B CB  
10841 C CG  . ARG B 237  ? 0.3333 0.2205 0.1898 0.0177  -0.0629 0.0045  235  ARG B CG  
10842 C CD  . ARG B 237  ? 0.3723 0.2686 0.2348 0.0172  -0.0598 0.0019  235  ARG B CD  
10843 N NE  . ARG B 237  ? 0.4337 0.3283 0.2876 0.0151  -0.0578 0.0031  235  ARG B NE  
10844 C CZ  . ARG B 237  ? 0.4304 0.3300 0.2853 0.0153  -0.0565 0.0011  235  ARG B CZ  
10845 N NH1 . ARG B 237  ? 0.4673 0.3741 0.3318 0.0172  -0.0568 -0.0021 235  ARG B NH1 
10846 N NH2 . ARG B 237  ? 0.4206 0.3177 0.2664 0.0135  -0.0547 0.0023  235  ARG B NH2 
10847 N N   . TYR B 238  ? 0.3022 0.1835 0.1630 0.0129  -0.0588 0.0079  236  TYR B N   
10848 C CA  . TYR B 238  ? 0.3104 0.1902 0.1677 0.0079  -0.0547 0.0104  236  TYR B CA  
10849 C C   . TYR B 238  ? 0.3113 0.1794 0.1590 0.0065  -0.0570 0.0137  236  TYR B C   
10850 O O   . TYR B 238  ? 0.3169 0.1809 0.1566 0.0025  -0.0549 0.0167  236  TYR B O   
10851 C CB  . TYR B 238  ? 0.2981 0.1849 0.1651 0.0065  -0.0514 0.0091  236  TYR B CB  
10852 C CG  . TYR B 238  ? 0.3187 0.2166 0.1939 0.0065  -0.0479 0.0067  236  TYR B CG  
10853 C CD1 . TYR B 238  ? 0.4027 0.3036 0.2745 0.0050  -0.0454 0.0070  236  TYR B CD1 
10854 C CD2 . TYR B 238  ? 0.3230 0.2278 0.2088 0.0080  -0.0471 0.0041  236  TYR B CD2 
10855 C CE1 . TYR B 238  ? 0.4573 0.3675 0.3361 0.0053  -0.0424 0.0047  236  TYR B CE1 
10856 C CE2 . TYR B 238  ? 0.3359 0.2501 0.2287 0.0081  -0.0441 0.0020  236  TYR B CE2 
10857 C CZ  . TYR B 238  ? 0.4362 0.3529 0.3256 0.0068  -0.0418 0.0023  236  TYR B CZ  
10858 O OH  . TYR B 238  ? 0.4796 0.4048 0.3756 0.0070  -0.0390 0.0002  236  TYR B OH  
10859 N N   . TYR B 239  ? 0.3031 0.1655 0.1512 0.0098  -0.0612 0.0132  237  TYR B N   
10860 C CA  . TYR B 239  ? 0.3085 0.1586 0.1469 0.0090  -0.0639 0.0162  237  TYR B CA  
10861 C C   . TYR B 239  ? 0.3375 0.1807 0.1645 0.0086  -0.0659 0.0186  237  TYR B C   
10862 O O   . TYR B 239  ? 0.3381 0.1740 0.1558 0.0047  -0.0649 0.0221  237  TYR B O   
10863 C CB  . TYR B 239  ? 0.3212 0.1671 0.1626 0.0138  -0.0684 0.0147  237  TYR B CB  
10864 C CG  . TYR B 239  ? 0.3389 0.1710 0.1700 0.0143  -0.0722 0.0173  237  TYR B CG  
10865 C CD1 . TYR B 239  ? 0.3925 0.2170 0.2169 0.0095  -0.0706 0.0204  237  TYR B CD1 
10866 C CD2 . TYR B 239  ? 0.4542 0.2811 0.2825 0.0196  -0.0776 0.0168  237  TYR B CD2 
10867 C CE1 . TYR B 239  ? 0.3917 0.2028 0.2063 0.0099  -0.0743 0.0229  237  TYR B CE1 
10868 C CE2 . TYR B 239  ? 0.5217 0.3354 0.3403 0.0205  -0.0813 0.0193  237  TYR B CE2 
10869 C CZ  . TYR B 239  ? 0.5174 0.3228 0.3289 0.0156  -0.0797 0.0223  237  TYR B CZ  
10870 O OH  . TYR B 239  ? 0.5690 0.3604 0.3703 0.0165  -0.0836 0.0249  237  TYR B OH  
10871 N N   . ARG B 240  ? 0.3272 0.1726 0.1545 0.0125  -0.0687 0.0170  238  ARG B N   
10872 C CA  . ARG B 240  ? 0.3450 0.1836 0.1610 0.0125  -0.0709 0.0192  238  ARG B CA  
10873 C C   . ARG B 240  ? 0.3275 0.1689 0.1387 0.0077  -0.0661 0.0209  238  ARG B C   
10874 O O   . ARG B 240  ? 0.3781 0.2117 0.1779 0.0054  -0.0664 0.0241  238  ARG B O   
10875 C CB  . ARG B 240  ? 0.3553 0.1965 0.1734 0.0177  -0.0752 0.0168  238  ARG B CB  
10876 C CG  . ARG B 240  ? 0.3941 0.2321 0.2157 0.0229  -0.0804 0.0155  238  ARG B CG  
10877 C CD  . ARG B 240  ? 0.4427 0.2669 0.2533 0.0233  -0.0840 0.0187  238  ARG B CD  
10878 N NE  . ARG B 240  ? 0.4698 0.2912 0.2847 0.0282  -0.0882 0.0174  238  ARG B NE  
10879 C CZ  . ARG B 240  ? 0.5833 0.3929 0.3907 0.0296  -0.0916 0.0195  238  ARG B CZ  
10880 N NH1 . ARG B 240  ? 0.6072 0.4063 0.4023 0.0261  -0.0916 0.0234  238  ARG B NH1 
10881 N NH2 . ARG B 240  ? 0.6039 0.4121 0.4162 0.0346  -0.0951 0.0178  238  ARG B NH2 
10882 N N   . ASP B 241  ? 0.3314 0.1836 0.1510 0.0062  -0.0616 0.0188  239  ASP B N   
10883 C CA  . ASP B 241  ? 0.3438 0.1995 0.1596 0.0020  -0.0566 0.0202  239  ASP B CA  
10884 C C   . ASP B 241  ? 0.3217 0.1730 0.1327 -0.0033 -0.0536 0.0237  239  ASP B C   
10885 O O   . ASP B 241  ? 0.3416 0.1902 0.1439 -0.0068 -0.0513 0.0265  239  ASP B O   
10886 C CB  . ASP B 241  ? 0.3512 0.2194 0.1776 0.0021  -0.0527 0.0171  239  ASP B CB  
10887 C CG  . ASP B 241  ? 0.3644 0.2369 0.1934 0.0061  -0.0550 0.0140  239  ASP B CG  
10888 O OD1 . ASP B 241  ? 0.4293 0.2959 0.2509 0.0082  -0.0589 0.0145  239  ASP B OD1 
10889 O OD2 . ASP B 241  ? 0.4210 0.3028 0.2595 0.0070  -0.0528 0.0111  239  ASP B OD2 
10890 N N   . TYR B 242  ? 0.3255 0.1761 0.1417 -0.0042 -0.0535 0.0238  240  TYR B N   
10891 C CA  . TYR B 242  ? 0.3248 0.1701 0.1360 -0.0095 -0.0513 0.0272  240  TYR B CA  
10892 C C   . TYR B 242  ? 0.3459 0.1778 0.1439 -0.0102 -0.0548 0.0307  240  TYR B C   
10893 O O   . TYR B 242  ? 0.3505 0.1784 0.1404 -0.0151 -0.0524 0.0342  240  TYR B O   
10894 C CB  . TYR B 242  ? 0.3186 0.1645 0.1373 -0.0097 -0.0515 0.0262  240  TYR B CB  
10895 C CG  . TYR B 242  ? 0.3041 0.1620 0.1343 -0.0110 -0.0471 0.0240  240  TYR B CG  
10896 C CD1 . TYR B 242  ? 0.3223 0.1882 0.1539 -0.0147 -0.0419 0.0247  240  TYR B CD1 
10897 C CD2 . TYR B 242  ? 0.3253 0.1863 0.1647 -0.0086 -0.0483 0.0214  240  TYR B CD2 
10898 C CE1 . TYR B 242  ? 0.3434 0.2201 0.1856 -0.0156 -0.0382 0.0227  240  TYR B CE1 
10899 C CE2 . TYR B 242  ? 0.3325 0.2039 0.1819 -0.0097 -0.0446 0.0195  240  TYR B CE2 
10900 C CZ  . TYR B 242  ? 0.2964 0.1754 0.1472 -0.0131 -0.0397 0.0202  240  TYR B CZ  
10901 O OH  . TYR B 242  ? 0.3140 0.2030 0.1750 -0.0138 -0.0364 0.0183  240  TYR B OH  
10902 N N   . GLU B 243  ? 0.3465 0.1714 0.1424 -0.0055 -0.0604 0.0299  241  GLU B N   
10903 C CA  . GLU B 243  ? 0.3670 0.1785 0.1502 -0.0054 -0.0643 0.0332  241  GLU B CA  
10904 C C   . GLU B 243  ? 0.3736 0.1835 0.1469 -0.0073 -0.0631 0.0354  241  GLU B C   
10905 O O   . GLU B 243  ? 0.3844 0.1858 0.1469 -0.0111 -0.0627 0.0393  241  GLU B O   
10906 C CB  . GLU B 243  ? 0.4159 0.2226 0.2000 0.0012  -0.0705 0.0313  241  GLU B CB  
10907 C CG  . GLU B 243  ? 0.4636 0.2562 0.2350 0.0024  -0.0754 0.0343  241  GLU B CG  
10908 C CD  . GLU B 243  ? 0.5235 0.3131 0.2972 0.0094  -0.0814 0.0321  241  GLU B CD  
10909 O OE1 . GLU B 243  ? 0.5284 0.3276 0.3111 0.0132  -0.0820 0.0286  241  GLU B OE1 
10910 O OE2 . GLU B 243  ? 0.6106 0.3883 0.3772 0.0111  -0.0856 0.0340  241  GLU B OE2 
10911 N N   . SER B 244  ? 0.3649 0.1828 0.1417 -0.0046 -0.0626 0.0328  242  SER B N   
10912 C CA  . SER B 244  ? 0.3729 0.1896 0.1402 -0.0059 -0.0615 0.0344  242  SER B CA  
10913 C C   . SER B 244  ? 0.3736 0.1939 0.1383 -0.0121 -0.0551 0.0368  242  SER B C   
10914 O O   . SER B 244  ? 0.3859 0.2002 0.1392 -0.0151 -0.0542 0.0402  242  SER B O   
10915 C CB  . SER B 244  ? 0.3660 0.1908 0.1385 -0.0018 -0.0624 0.0307  242  SER B CB  
10916 O OG  . SER B 244  ? 0.4232 0.2479 0.1871 -0.0031 -0.0608 0.0318  242  SER B OG  
10917 N N   . ALA B 245  ? 0.3609 0.1911 0.1361 -0.0141 -0.0507 0.0352  243  ALA B N   
10918 C CA  . ALA B 245  ? 0.3609 0.1958 0.1350 -0.0198 -0.0446 0.0374  243  ALA B CA  
10919 C C   . ALA B 245  ? 0.3725 0.1981 0.1388 -0.0248 -0.0444 0.0418  243  ALA B C   
10920 O O   . ALA B 245  ? 0.3812 0.2057 0.1399 -0.0295 -0.0410 0.0450  243  ALA B O   
10921 C CB  . ALA B 245  ? 0.3460 0.1933 0.1335 -0.0204 -0.0405 0.0346  243  ALA B CB  
10922 N N   . ILE B 246  ? 0.3743 0.1928 0.1419 -0.0241 -0.0481 0.0420  244  ILE B N   
10923 C CA  . ILE B 246  ? 0.4101 0.2185 0.1697 -0.0290 -0.0483 0.0462  244  ILE B CA  
10924 C C   . ILE B 246  ? 0.4165 0.2138 0.1612 -0.0298 -0.0505 0.0498  244  ILE B C   
10925 O O   . ILE B 246  ? 0.4206 0.2133 0.1570 -0.0355 -0.0480 0.0538  244  ILE B O   
10926 C CB  . ILE B 246  ? 0.3859 0.1879 0.1492 -0.0272 -0.0523 0.0454  244  ILE B CB  
10927 C CG1 . ILE B 246  ? 0.3709 0.1834 0.1473 -0.0283 -0.0492 0.0428  244  ILE B CG1 
10928 C CG2 . ILE B 246  ? 0.4117 0.2003 0.1643 -0.0315 -0.0538 0.0497  244  ILE B CG2 
10929 C CD1 . ILE B 246  ? 0.3755 0.1832 0.1568 -0.0253 -0.0530 0.0410  244  ILE B CD1 
10930 N N   . HIS B 247  ? 0.4073 0.2004 0.1481 -0.0243 -0.0551 0.0485  245  HIS B N   
10931 C CA  . HIS B 247  ? 0.4276 0.2105 0.1538 -0.0250 -0.0572 0.0519  245  HIS B CA  
10932 C C   . HIS B 247  ? 0.4262 0.2147 0.1475 -0.0292 -0.0516 0.0536  245  HIS B C   
10933 O O   . HIS B 247  ? 0.4431 0.2241 0.1528 -0.0335 -0.0506 0.0579  245  HIS B O   
10934 C CB  . HIS B 247  ? 0.4521 0.2314 0.1760 -0.0182 -0.0629 0.0498  245  HIS B CB  
10935 C CG  . HIS B 247  ? 0.4502 0.2200 0.1739 -0.0142 -0.0691 0.0495  245  HIS B CG  
10936 N ND1 . HIS B 247  ? 0.4627 0.2200 0.1779 -0.0159 -0.0715 0.0527  245  HIS B ND1 
10937 C CD2 . HIS B 247  ? 0.4602 0.2328 0.1932 -0.0085 -0.0728 0.0458  245  HIS B CD2 
10938 C CE1 . HIS B 247  ? 0.4938 0.2458 0.2122 -0.0111 -0.0766 0.0510  245  HIS B CE1 
10939 N NE2 . HIS B 247  ? 0.5075 0.2677 0.2351 -0.0065 -0.0778 0.0474  245  HIS B NE2 
10940 N N   . ALA B 248  ? 0.4135 0.2149 0.1431 -0.0278 -0.0481 0.0504  246  ALA B N   
10941 C CA  . ALA B 248  ? 0.4155 0.2228 0.1408 -0.0310 -0.0426 0.0516  246  ALA B CA  
10942 C C   . ALA B 248  ? 0.4165 0.2267 0.1422 -0.0380 -0.0371 0.0547  246  ALA B C   
10943 O O   . ALA B 248  ? 0.4516 0.2591 0.1675 -0.0424 -0.0342 0.0583  246  ALA B O   
10944 C CB  . ALA B 248  ? 0.4278 0.2478 0.1624 -0.0276 -0.0403 0.0471  246  ALA B CB  
10945 N N   . ILE B 249  ? 0.4101 0.2260 0.1470 -0.0392 -0.0357 0.0533  247  ILE B N   
10946 C CA  . ILE B 249  ? 0.4088 0.2286 0.1474 -0.0460 -0.0307 0.0561  247  ILE B CA  
10947 C C   . ILE B 249  ? 0.4335 0.2399 0.1610 -0.0506 -0.0326 0.0609  247  ILE B C   
10948 O O   . ILE B 249  ? 0.4292 0.2357 0.1512 -0.0568 -0.0286 0.0646  247  ILE B O   
10949 C CB  . ILE B 249  ? 0.3901 0.2187 0.1432 -0.0459 -0.0294 0.0533  247  ILE B CB  
10950 C CG1 . ILE B 249  ? 0.3749 0.2170 0.1385 -0.0420 -0.0268 0.0489  247  ILE B CG1 
10951 C CG2 . ILE B 249  ? 0.3914 0.2229 0.1460 -0.0531 -0.0251 0.0563  247  ILE B CG2 
10952 C CD1 . ILE B 249  ? 0.3599 0.2087 0.1373 -0.0398 -0.0274 0.0454  247  ILE B CD1 
10953 N N   . GLY B 250  ? 0.4293 0.2240 0.1533 -0.0477 -0.0388 0.0609  248  GLY B N   
10954 C CA  . GLY B 250  ? 0.4439 0.2244 0.1569 -0.0517 -0.0412 0.0654  248  GLY B CA  
10955 C C   . GLY B 250  ? 0.4719 0.2484 0.1751 -0.0531 -0.0403 0.0678  248  GLY B C   
10956 O O   . GLY B 250  ? 0.4799 0.2531 0.1787 -0.0587 -0.0380 0.0711  248  GLY B O   
10957 N N   . LYS B 251  ? 0.4580 0.2348 0.1579 -0.0480 -0.0422 0.0661  249  LYS B N   
10958 C CA  . LYS B 251  ? 0.5009 0.2749 0.1918 -0.0492 -0.0410 0.0681  249  LYS B CA  
10959 C C   . LYS B 251  ? 0.4919 0.2754 0.1826 -0.0547 -0.0336 0.0700  249  LYS B C   
10960 O O   . LYS B 251  ? 0.5171 0.2977 0.2015 -0.0591 -0.0313 0.0732  249  LYS B O   
10961 C CB  . LYS B 251  ? 0.5347 0.3084 0.2230 -0.0427 -0.0443 0.0655  249  LYS B CB  
10962 C CG  . LYS B 251  ? 0.6289 0.3918 0.3148 -0.0376 -0.0516 0.0646  249  LYS B CG  
10963 C CD  . LYS B 251  ? 0.6425 0.3941 0.3195 -0.0404 -0.0532 0.0681  249  LYS B CD  
10964 C CE  . LYS B 251  ? 0.7470 0.4890 0.4202 -0.0347 -0.0600 0.0671  249  LYS B CE  
10965 N NZ  . LYS B 251  ? 0.7316 0.4730 0.4126 -0.0293 -0.0647 0.0639  249  LYS B NZ  
10966 N N   . ALA B 252  ? 0.4853 0.2805 0.1832 -0.0546 -0.0297 0.0680  250  ALA B N   
10967 C CA  . ALA B 252  ? 0.4643 0.2700 0.1631 -0.0592 -0.0224 0.0693  250  ALA B CA  
10968 C C   . ALA B 252  ? 0.4691 0.2753 0.1699 -0.0664 -0.0193 0.0727  250  ALA B C   
10969 O O   . ALA B 252  ? 0.5135 0.3238 0.2116 -0.0710 -0.0144 0.0752  250  ALA B O   
10970 C CB  . ALA B 252  ? 0.4838 0.3017 0.1903 -0.0571 -0.0193 0.0661  250  ALA B CB  
10971 N N   . SER B 253  ? 0.4536 0.2561 0.1594 -0.0674 -0.0220 0.0725  251  SER B N   
10972 C CA  . SER B 253  ? 0.4573 0.2594 0.1650 -0.0743 -0.0197 0.0755  251  SER B CA  
10973 C C   . SER B 253  ? 0.4876 0.2809 0.1861 -0.0777 -0.0202 0.0789  251  SER B C   
10974 O O   . SER B 253  ? 0.4972 0.2945 0.1958 -0.0840 -0.0158 0.0818  251  SER B O   
10975 C CB  . SER B 253  ? 0.4857 0.2824 0.1985 -0.0740 -0.0238 0.0745  251  SER B CB  
10976 O OG  . SER B 253  ? 0.4773 0.2731 0.1917 -0.0808 -0.0220 0.0772  251  SER B OG  
10977 N N   . ALA B 254  ? 0.4836 0.2653 0.1745 -0.0736 -0.0255 0.0788  252  ALA B N   
10978 C CA  . ALA B 254  ? 0.5480 0.3207 0.2290 -0.0761 -0.0262 0.0819  252  ALA B CA  
10979 C C   . ALA B 254  ? 0.5080 0.2765 0.1888 -0.0830 -0.0253 0.0850  252  ALA B C   
10980 O O   . ALA B 254  ? 0.5268 0.2960 0.2031 -0.0882 -0.0219 0.0882  252  ALA B O   
10981 C CB  . ALA B 254  ? 0.5316 0.3111 0.2080 -0.0769 -0.0215 0.0830  252  ALA B CB  
10982 N N   . GLY B 255  ? 0.5339 0.2982 0.2195 -0.0832 -0.0284 0.0840  253  GLY B N   
10983 C CA  . GLY B 255  ? 0.5503 0.3086 0.2351 -0.0893 -0.0287 0.0865  253  GLY B CA  
10984 C C   . GLY B 255  ? 0.5372 0.3068 0.2289 -0.0963 -0.0229 0.0880  253  GLY B C   
10985 O O   . GLY B 255  ? 0.5714 0.3368 0.2616 -0.1022 -0.0226 0.0905  253  GLY B O   
10986 N N   . ARG B 256  ? 0.5055 0.2894 0.2048 -0.0958 -0.0183 0.0865  254  ARG B N   
10987 C CA  . ARG B 256  ? 0.5061 0.3021 0.2131 -0.1021 -0.0127 0.0878  254  ARG B CA  
10988 C C   . ARG B 256  ? 0.5070 0.3022 0.2213 -0.1045 -0.0146 0.0869  254  ARG B C   
10989 O O   . ARG B 256  ? 0.5300 0.3333 0.2503 -0.1106 -0.0109 0.0883  254  ARG B O   
10990 C CB  . ARG B 256  ? 0.4738 0.2854 0.1870 -0.1004 -0.0074 0.0861  254  ARG B CB  
10991 C CG  . ARG B 256  ? 0.4988 0.3151 0.2064 -0.1009 -0.0031 0.0878  254  ARG B CG  
10992 C CD  . ARG B 256  ? 0.5019 0.3328 0.2152 -0.0983 0.0018  0.0856  254  ARG B CD  
10993 N NE  . ARG B 256  ? 0.4795 0.3076 0.1914 -0.0908 -0.0016 0.0823  254  ARG B NE  
10994 C CZ  . ARG B 256  ? 0.5131 0.3517 0.2300 -0.0872 0.0011  0.0795  254  ARG B CZ  
10995 N NH1 . ARG B 256  ? 0.5022 0.3552 0.2266 -0.0900 0.0073  0.0794  254  ARG B NH1 
10996 N NH2 . ARG B 256  ? 0.5141 0.3489 0.2286 -0.0806 -0.0026 0.0765  254  ARG B NH2 
10997 N N   . GLY B 257  ? 0.4781 0.2641 0.1922 -0.0999 -0.0203 0.0846  255  GLY B N   
10998 C CA  . GLY B 257  ? 0.4730 0.2573 0.1933 -0.1017 -0.0223 0.0836  255  GLY B CA  
10999 C C   . GLY B 257  ? 0.4793 0.2760 0.2102 -0.1001 -0.0200 0.0811  255  GLY B C   
11000 O O   . GLY B 257  ? 0.4791 0.2862 0.2127 -0.0977 -0.0166 0.0800  255  GLY B O   
11001 N N   . ILE B 258  ? 0.4871 0.2825 0.2238 -0.1017 -0.0219 0.0801  256  ILE B N   
11002 C CA  . ILE B 258  ? 0.4651 0.2699 0.2112 -0.0994 -0.0209 0.0774  256  ILE B CA  
11003 C C   . ILE B 258  ? 0.4556 0.2772 0.2105 -0.1043 -0.0145 0.0781  256  ILE B C   
11004 O O   . ILE B 258  ? 0.4568 0.2906 0.2224 -0.1007 -0.0127 0.0746  256  ILE B O   
11005 C CB  . ILE B 258  ? 0.5002 0.2971 0.2492 -0.0987 -0.0255 0.0758  256  ILE B CB  
11006 C CG1 . ILE B 258  ? 0.4806 0.2755 0.2306 -0.1062 -0.0250 0.0778  256  ILE B CG1 
11007 C CG2 . ILE B 258  ? 0.4848 0.2664 0.2265 -0.0924 -0.0319 0.0745  256  ILE B CG2 
11008 C CD1 . ILE B 258  ? 0.5117 0.2992 0.2645 -0.1058 -0.0293 0.0760  256  ILE B CD1 
11009 N N   . TYR B 259  ? 0.4725 0.2983 0.2270 -0.1108 -0.0110 0.0809  257  TYR B N   
11010 C CA  . TYR B 259  ? 0.4228 0.2656 0.1865 -0.1151 -0.0049 0.0815  257  TYR B CA  
11011 C C   . TYR B 259  ? 0.4575 0.3103 0.2201 -0.1138 0.0003  0.0820  257  TYR B C   
11012 O O   . TYR B 259  ? 0.4265 0.2922 0.1962 -0.1118 0.0039  0.0803  257  TYR B O   
11013 C CB  . TYR B 259  ? 0.4675 0.3108 0.2330 -0.1230 -0.0039 0.0840  257  TYR B CB  
11014 C CG  . TYR B 259  ? 0.4597 0.2920 0.2252 -0.1242 -0.0091 0.0832  257  TYR B CG  
11015 C CD1 . TYR B 259  ? 0.4699 0.3067 0.2439 -0.1232 -0.0101 0.0808  257  TYR B CD1 
11016 C CD2 . TYR B 259  ? 0.5032 0.3204 0.2599 -0.1261 -0.0132 0.0848  257  TYR B CD2 
11017 C CE1 . TYR B 259  ? 0.4655 0.2920 0.2391 -0.1239 -0.0149 0.0799  257  TYR B CE1 
11018 C CE2 . TYR B 259  ? 0.4887 0.2955 0.2449 -0.1267 -0.0180 0.0837  257  TYR B CE2 
11019 C CZ  . TYR B 259  ? 0.5139 0.3255 0.2786 -0.1255 -0.0188 0.0812  257  TYR B CZ  
11020 O OH  . TYR B 259  ? 0.5420 0.3433 0.3062 -0.1258 -0.0235 0.0799  257  TYR B OH  
11021 N N   . GLU B 260  ? 0.4613 0.3082 0.2150 -0.1146 0.0006  0.0842  258  GLU B N   
11022 C CA  . GLU B 260  ? 0.4725 0.3280 0.2243 -0.1128 0.0053  0.0845  258  GLU B CA  
11023 C C   . GLU B 260  ? 0.4548 0.3072 0.2029 -0.1050 0.0032  0.0817  258  GLU B C   
11024 O O   . GLU B 260  ? 0.4900 0.3530 0.2408 -0.1023 0.0071  0.0803  258  GLU B O   
11025 C CB  . GLU B 260  ? 0.4773 0.3276 0.2205 -0.1163 0.0065  0.0879  258  GLU B CB  
11026 C CG  . GLU B 260  ? 0.5628 0.4221 0.3038 -0.1149 0.0118  0.0883  258  GLU B CG  
11027 C CD  . GLU B 260  ? 0.5765 0.4279 0.3071 -0.1172 0.0119  0.0915  258  GLU B CD  
11028 O OE1 . GLU B 260  ? 0.6396 0.4814 0.3664 -0.1216 0.0091  0.0938  258  GLU B OE1 
11029 O OE2 . GLU B 260  ? 0.5606 0.4150 0.2863 -0.1147 0.0147  0.0917  258  GLU B OE2 
11030 N N   . GLY B 261  ? 0.4795 0.3178 0.2219 -0.1012 -0.0031 0.0807  259  GLY B N   
11031 C CA  . GLY B 261  ? 0.4974 0.3315 0.2353 -0.0939 -0.0058 0.0783  259  GLY B CA  
11032 C C   . GLY B 261  ? 0.4409 0.2825 0.1894 -0.0887 -0.0067 0.0739  259  GLY B C   
11033 O O   . GLY B 261  ? 0.4201 0.2674 0.1788 -0.0902 -0.0064 0.0725  259  GLY B O   
11034 N N   . PRO B 262  ? 0.4100 0.2532 0.1586 -0.0817 -0.0079 0.0706  260  PRO B N   
11035 C CA  . PRO B 262  ? 0.3929 0.2452 0.1541 -0.0756 -0.0084 0.0654  260  PRO B CA  
11036 C C   . PRO B 262  ? 0.3903 0.2339 0.1542 -0.0720 -0.0146 0.0632  260  PRO B C   
11037 O O   . PRO B 262  ? 0.4388 0.2681 0.1937 -0.0723 -0.0192 0.0651  260  PRO B O   
11038 C CB  . PRO B 262  ? 0.4003 0.2552 0.1584 -0.0700 -0.0080 0.0632  260  PRO B CB  
11039 C CG  . PRO B 262  ? 0.4240 0.2649 0.1668 -0.0709 -0.0109 0.0665  260  PRO B CG  
11040 C CD  . PRO B 262  ? 0.4347 0.2719 0.1717 -0.0792 -0.0085 0.0717  260  PRO B CD  
11041 N N   . GLY B 263  ? 0.4014 0.2539 0.1779 -0.0684 -0.0146 0.0591  261  GLY B N   
11042 C CA  . GLY B 263  ? 0.3704 0.2169 0.1510 -0.0643 -0.0198 0.0563  261  GLY B CA  
11043 C C   . GLY B 263  ? 0.3563 0.2108 0.1460 -0.0572 -0.0205 0.0514  261  GLY B C   
11044 O O   . GLY B 263  ? 0.3618 0.2249 0.1532 -0.0554 -0.0173 0.0501  261  GLY B O   
11045 N N   . ILE B 264  ? 0.3503 0.2019 0.1455 -0.0533 -0.0245 0.0485  262  ILE B N   
11046 C CA  . ILE B 264  ? 0.3421 0.2009 0.1464 -0.0469 -0.0254 0.0439  262  ILE B CA  
11047 C C   . ILE B 264  ? 0.3510 0.2155 0.1666 -0.0469 -0.0252 0.0416  262  ILE B C   
11048 O O   . ILE B 264  ? 0.3393 0.1983 0.1541 -0.0503 -0.0265 0.0432  262  ILE B O   
11049 C CB  . ILE B 264  ? 0.3862 0.2357 0.1855 -0.0410 -0.0310 0.0424  262  ILE B CB  
11050 C CG1 . ILE B 264  ? 0.3311 0.1889 0.1383 -0.0349 -0.0313 0.0380  262  ILE B CG1 
11051 C CG2 . ILE B 264  ? 0.3752 0.2142 0.1734 -0.0400 -0.0359 0.0424  262  ILE B CG2 
11052 C CD1 . ILE B 264  ? 0.3479 0.1978 0.1506 -0.0293 -0.0367 0.0366  262  ILE B CD1 
11053 N N   . SER B 265  ? 0.3116 0.1871 0.1373 -0.0432 -0.0236 0.0380  263  SER B N   
11054 C CA  . SER B 265  ? 0.2999 0.1811 0.1365 -0.0421 -0.0237 0.0353  263  SER B CA  
11055 C C   . SER B 265  ? 0.3232 0.2043 0.1644 -0.0352 -0.0271 0.0314  263  SER B C   
11056 O O   . SER B 265  ? 0.3719 0.2552 0.2120 -0.0316 -0.0273 0.0300  263  SER B O   
11057 C CB  . SER B 265  ? 0.3366 0.2318 0.1821 -0.0442 -0.0185 0.0346  263  SER B CB  
11058 O OG  . SER B 265  ? 0.3619 0.2582 0.2052 -0.0510 -0.0156 0.0381  263  SER B OG  
11059 N N   . ILE B 266  ? 0.2892 0.1676 0.1350 -0.0335 -0.0300 0.0297  264  ILE B N   
11060 C CA  . ILE B 266  ? 0.2892 0.1679 0.1400 -0.0272 -0.0332 0.0261  264  ILE B CA  
11061 C C   . ILE B 266  ? 0.2874 0.1740 0.1494 -0.0265 -0.0320 0.0234  264  ILE B C   
11062 O O   . ILE B 266  ? 0.2809 0.1694 0.1454 -0.0306 -0.0302 0.0246  264  ILE B O   
11063 C CB  . ILE B 266  ? 0.3087 0.1746 0.1530 -0.0244 -0.0386 0.0264  264  ILE B CB  
11064 C CG1 . ILE B 266  ? 0.3187 0.1784 0.1627 -0.0271 -0.0400 0.0273  264  ILE B CG1 
11065 C CG2 . ILE B 266  ? 0.3159 0.1732 0.1483 -0.0252 -0.0401 0.0292  264  ILE B CG2 
11066 C CD1 . ILE B 266  ? 0.3558 0.2034 0.1947 -0.0236 -0.0453 0.0270  264  ILE B CD1 
11067 N N   . LYS B 267  ? 0.2723 0.1636 0.1410 -0.0213 -0.0332 0.0200  265  LYS B N   
11068 C CA  . LYS B 267  ? 0.2503 0.1474 0.1288 -0.0197 -0.0329 0.0173  265  LYS B CA  
11069 C C   . LYS B 267  ? 0.2590 0.1496 0.1378 -0.0151 -0.0375 0.0154  265  LYS B C   
11070 O O   . LYS B 267  ? 0.2793 0.1679 0.1564 -0.0109 -0.0400 0.0142  265  LYS B O   
11071 C CB  . LYS B 267  ? 0.2939 0.2031 0.1810 -0.0178 -0.0299 0.0148  265  LYS B CB  
11072 C CG  . LYS B 267  ? 0.3188 0.2361 0.2080 -0.0220 -0.0249 0.0163  265  LYS B CG  
11073 C CD  . LYS B 267  ? 0.3764 0.3046 0.2736 -0.0195 -0.0223 0.0137  265  LYS B CD  
11074 C CE  . LYS B 267  ? 0.3784 0.3152 0.2786 -0.0232 -0.0174 0.0150  265  LYS B CE  
11075 N NZ  . LYS B 267  ? 0.4235 0.3580 0.3155 -0.0265 -0.0156 0.0180  265  LYS B NZ  
11076 N N   . LEU B 268  ? 0.2748 0.1624 0.1558 -0.0158 -0.0386 0.0150  266  LEU B N   
11077 C CA  . LEU B 268  ? 0.2651 0.1468 0.1464 -0.0111 -0.0427 0.0130  266  LEU B CA  
11078 C C   . LEU B 268  ? 0.2612 0.1509 0.1510 -0.0060 -0.0430 0.0095  266  LEU B C   
11079 O O   . LEU B 268  ? 0.2619 0.1478 0.1511 -0.0013 -0.0464 0.0081  266  LEU B O   
11080 C CB  . LEU B 268  ? 0.2685 0.1458 0.1505 -0.0129 -0.0434 0.0130  266  LEU B CB  
11081 C CG  . LEU B 268  ? 0.2819 0.1496 0.1549 -0.0182 -0.0439 0.0165  266  LEU B CG  
11082 C CD1 . LEU B 268  ? 0.2938 0.1567 0.1676 -0.0192 -0.0452 0.0159  266  LEU B CD1 
11083 C CD2 . LEU B 268  ? 0.3146 0.1711 0.1774 -0.0169 -0.0472 0.0184  266  LEU B CD2 
11084 N N   . SER B 269  ? 0.2585 0.1592 0.1562 -0.0067 -0.0394 0.0081  267  SER B N   
11085 C CA  . SER B 269  ? 0.2391 0.1473 0.1446 -0.0022 -0.0396 0.0050  267  SER B CA  
11086 C C   . SER B 269  ? 0.2394 0.1470 0.1420 0.0007  -0.0413 0.0046  267  SER B C   
11087 O O   . SER B 269  ? 0.2650 0.1764 0.1728 0.0048  -0.0427 0.0020  267  SER B O   
11088 C CB  . SER B 269  ? 0.2624 0.1817 0.1759 -0.0038 -0.0354 0.0039  267  SER B CB  
11089 O OG  . SER B 269  ? 0.2636 0.1864 0.1747 -0.0061 -0.0327 0.0053  267  SER B OG  
11090 N N   . ALA B 270  ? 0.2371 0.1400 0.1313 -0.0014 -0.0412 0.0070  268  ALA B N   
11091 C CA  . ALA B 270  ? 0.2501 0.1512 0.1403 0.0013  -0.0433 0.0068  268  ALA B CA  
11092 C C   . ALA B 270  ? 0.2631 0.1557 0.1493 0.0050  -0.0484 0.0066  268  ALA B C   
11093 O O   . ALA B 270  ? 0.2636 0.1561 0.1488 0.0084  -0.0509 0.0056  268  ALA B O   
11094 C CB  . ALA B 270  ? 0.2710 0.1695 0.1528 -0.0022 -0.0416 0.0096  268  ALA B CB  
11095 N N   . LEU B 271  ? 0.2614 0.1469 0.1452 0.0046  -0.0501 0.0075  269  LEU B N   
11096 C CA  . LEU B 271  ? 0.2589 0.1346 0.1368 0.0079  -0.0549 0.0079  269  LEU B CA  
11097 C C   . LEU B 271  ? 0.2550 0.1320 0.1396 0.0128  -0.0574 0.0050  269  LEU B C   
11098 O O   . LEU B 271  ? 0.3003 0.1699 0.1810 0.0164  -0.0616 0.0051  269  LEU B O   
11099 C CB  . LEU B 271  ? 0.2837 0.1484 0.1525 0.0044  -0.0556 0.0111  269  LEU B CB  
11100 C CG  . LEU B 271  ? 0.2947 0.1566 0.1551 0.0000  -0.0539 0.0143  269  LEU B CG  
11101 C CD1 . LEU B 271  ? 0.3590 0.2109 0.2117 -0.0042 -0.0542 0.0175  269  LEU B CD1 
11102 C CD2 . LEU B 271  ? 0.3133 0.1714 0.1674 0.0028  -0.0568 0.0149  269  LEU B CD2 
11103 N N   . HIS B 272  ? 0.2787 0.1651 0.1732 0.0133  -0.0550 0.0026  270  HIS B N   
11104 C CA  . HIS B 272  ? 0.2735 0.1623 0.1746 0.0180  -0.0570 -0.0002 270  HIS B CA  
11105 C C   . HIS B 272  ? 0.2430 0.1438 0.1545 0.0183  -0.0540 -0.0027 270  HIS B C   
11106 O O   . HIS B 272  ? 0.2643 0.1697 0.1781 0.0145  -0.0502 -0.0022 270  HIS B O   
11107 C CB  . HIS B 272  ? 0.2717 0.1538 0.1713 0.0180  -0.0579 -0.0001 270  HIS B CB  
11108 C CG  . HIS B 272  ? 0.3098 0.1915 0.2135 0.0237  -0.0609 -0.0025 270  HIS B CG  
11109 N ND1 . HIS B 272  ? 0.3008 0.1914 0.2143 0.0258  -0.0594 -0.0054 270  HIS B ND1 
11110 C CD2 . HIS B 272  ? 0.3374 0.2110 0.2366 0.0278  -0.0651 -0.0025 270  HIS B CD2 
11111 C CE1 . HIS B 272  ? 0.3442 0.2328 0.2594 0.0310  -0.0625 -0.0071 270  HIS B CE1 
11112 N NE2 . HIS B 272  ? 0.3582 0.2367 0.2650 0.0325  -0.0660 -0.0054 270  HIS B NE2 
11113 N N   . PRO B 273  ? 0.2386 0.1447 0.1566 0.0226  -0.0556 -0.0052 271  PRO B N   
11114 C CA  . PRO B 273  ? 0.2313 0.1485 0.1589 0.0226  -0.0528 -0.0074 271  PRO B CA  
11115 C C   . PRO B 273  ? 0.2336 0.1538 0.1670 0.0223  -0.0508 -0.0087 271  PRO B C   
11116 O O   . PRO B 273  ? 0.2500 0.1788 0.1906 0.0215  -0.0479 -0.0100 271  PRO B O   
11117 C CB  . PRO B 273  ? 0.2629 0.1837 0.1946 0.0272  -0.0556 -0.0095 271  PRO B CB  
11118 C CG  . PRO B 273  ? 0.2939 0.2065 0.2208 0.0305  -0.0598 -0.0090 271  PRO B CG  
11119 C CD  . PRO B 273  ? 0.2602 0.1630 0.1768 0.0274  -0.0601 -0.0060 271  PRO B CD  
11120 N N   . ARG B 274  ? 0.2413 0.1545 0.1717 0.0230  -0.0522 -0.0083 272  ARG B N   
11121 C CA  . ARG B 274  ? 0.2335 0.1487 0.1685 0.0227  -0.0506 -0.0095 272  ARG B CA  
11122 C C   . ARG B 274  ? 0.2469 0.1545 0.1755 0.0189  -0.0500 -0.0075 272  ARG B C   
11123 O O   . ARG B 274  ? 0.2667 0.1681 0.1930 0.0200  -0.0515 -0.0078 272  ARG B O   
11124 C CB  . ARG B 274  ? 0.2443 0.1590 0.1827 0.0280  -0.0531 -0.0118 272  ARG B CB  
11125 C CG  . ARG B 274  ? 0.2576 0.1809 0.2034 0.0316  -0.0537 -0.0140 272  ARG B CG  
11126 C CD  . ARG B 274  ? 0.2346 0.1685 0.1885 0.0296  -0.0500 -0.0151 272  ARG B CD  
11127 N NE  . ARG B 274  ? 0.2499 0.1855 0.2069 0.0284  -0.0476 -0.0158 272  ARG B NE  
11128 C CZ  . ARG B 274  ? 0.2373 0.1756 0.1993 0.0314  -0.0477 -0.0179 272  ARG B CZ  
11129 N NH1 . ARG B 274  ? 0.2413 0.1811 0.2062 0.0360  -0.0501 -0.0195 272  ARG B NH1 
11130 N NH2 . ARG B 274  ? 0.2308 0.1705 0.1949 0.0298  -0.0454 -0.0184 272  ARG B NH2 
11131 N N   . TYR B 275  ? 0.2498 0.1578 0.1752 0.0142  -0.0478 -0.0053 273  TYR B N   
11132 C CA  . TYR B 275  ? 0.2752 0.1769 0.1948 0.0097  -0.0470 -0.0030 273  TYR B CA  
11133 C C   . TYR B 275  ? 0.2658 0.1731 0.1913 0.0076  -0.0442 -0.0040 273  TYR B C   
11134 O O   . TYR B 275  ? 0.2472 0.1621 0.1765 0.0046  -0.0410 -0.0037 273  TYR B O   
11135 C CB  . TYR B 275  ? 0.2550 0.1558 0.1692 0.0055  -0.0455 -0.0002 273  TYR B CB  
11136 C CG  . TYR B 275  ? 0.2456 0.1414 0.1546 0.0001  -0.0443 0.0023  273  TYR B CG  
11137 C CD1 . TYR B 275  ? 0.2723 0.1576 0.1753 -0.0004 -0.0468 0.0032  273  TYR B CD1 
11138 C CD2 . TYR B 275  ? 0.2566 0.1583 0.1668 -0.0045 -0.0407 0.0039  273  TYR B CD2 
11139 C CE1 . TYR B 275  ? 0.2683 0.1489 0.1666 -0.0058 -0.0459 0.0055  273  TYR B CE1 
11140 C CE2 . TYR B 275  ? 0.2514 0.1494 0.1574 -0.0098 -0.0396 0.0063  273  TYR B CE2 
11141 C CZ  . TYR B 275  ? 0.2728 0.1603 0.1729 -0.0106 -0.0422 0.0071  273  TYR B CZ  
11142 O OH  . TYR B 275  ? 0.2894 0.1731 0.1854 -0.0163 -0.0413 0.0095  273  TYR B OH  
11143 N N   . SER B 276  ? 0.2324 0.1361 0.1585 0.0094  -0.0456 -0.0054 274  SER B N   
11144 C CA  . SER B 276  ? 0.2290 0.1375 0.1603 0.0077  -0.0433 -0.0065 274  SER B CA  
11145 C C   . SER B 276  ? 0.2415 0.1416 0.1692 0.0087  -0.0454 -0.0073 274  SER B C   
11146 O O   . SER B 276  ? 0.2641 0.1567 0.1878 0.0124  -0.0486 -0.0078 274  SER B O   
11147 C CB  . SER B 276  ? 0.2913 0.2104 0.2319 0.0106  -0.0416 -0.0091 274  SER B CB  
11148 O OG  . SER B 276  ? 0.3160 0.2334 0.2582 0.0159  -0.0440 -0.0112 274  SER B OG  
11149 N N   . ARG B 277  ? 0.2540 0.1553 0.1831 0.0057  -0.0438 -0.0074 275  ARG B N   
11150 C CA  . ARG B 277  ? 0.2573 0.1505 0.1829 0.0066  -0.0457 -0.0085 275  ARG B CA  
11151 C C   . ARG B 277  ? 0.2450 0.1392 0.1743 0.0129  -0.0470 -0.0115 275  ARG B C   
11152 O O   . ARG B 277  ? 0.2631 0.1483 0.1877 0.0156  -0.0497 -0.0123 275  ARG B O   
11153 C CB  . ARG B 277  ? 0.2324 0.1283 0.1598 0.0022  -0.0437 -0.0083 275  ARG B CB  
11154 C CG  . ARG B 277  ? 0.2506 0.1391 0.1750 0.0031  -0.0454 -0.0099 275  ARG B CG  
11155 C CD  . ARG B 277  ? 0.2595 0.1336 0.1737 0.0024  -0.0487 -0.0085 275  ARG B CD  
11156 N NE  . ARG B 277  ? 0.2677 0.1344 0.1787 0.0034  -0.0502 -0.0103 275  ARG B NE  
11157 C CZ  . ARG B 277  ? 0.2977 0.1611 0.2087 0.0093  -0.0519 -0.0129 275  ARG B CZ  
11158 N NH1 . ARG B 277  ? 0.2960 0.1637 0.2110 0.0148  -0.0522 -0.0141 275  ARG B NH1 
11159 N NH2 . ARG B 277  ? 0.2960 0.1513 0.2027 0.0099  -0.0533 -0.0144 275  ARG B NH2 
11160 N N   . ALA B 278  ? 0.2442 0.1491 0.1818 0.0154  -0.0453 -0.0132 276  ALA B N   
11161 C CA  . ALA B 278  ? 0.2577 0.1647 0.1995 0.0212  -0.0462 -0.0160 276  ALA B CA  
11162 C C   . ALA B 278  ? 0.2657 0.1665 0.2037 0.0255  -0.0496 -0.0161 276  ALA B C   
11163 O O   . ALA B 278  ? 0.2783 0.1769 0.2170 0.0304  -0.0512 -0.0181 276  ALA B O   
11164 C CB  . ALA B 278  ? 0.2587 0.1783 0.2098 0.0224  -0.0437 -0.0174 276  ALA B CB  
11165 N N   . GLN B 279  ? 0.2504 0.1484 0.1843 0.0240  -0.0506 -0.0139 277  GLN B N   
11166 C CA  . GLN B 279  ? 0.2334 0.1253 0.1631 0.0279  -0.0541 -0.0136 277  GLN B CA  
11167 C C   . GLN B 279  ? 0.2583 0.1370 0.1774 0.0257  -0.0564 -0.0112 277  GLN B C   
11168 O O   . GLN B 279  ? 0.2721 0.1457 0.1861 0.0267  -0.0587 -0.0097 277  GLN B O   
11169 C CB  . GLN B 279  ? 0.2847 0.1834 0.2176 0.0285  -0.0539 -0.0132 277  GLN B CB  
11170 C CG  . GLN B 279  ? 0.2788 0.1897 0.2218 0.0306  -0.0519 -0.0154 277  GLN B CG  
11171 C CD  . GLN B 279  ? 0.3273 0.2396 0.2744 0.0363  -0.0534 -0.0181 277  GLN B CD  
11172 O OE1 . GLN B 279  ? 0.3782 0.2834 0.3211 0.0401  -0.0567 -0.0182 277  GLN B OE1 
11173 N NE2 . GLN B 279  ? 0.2665 0.1876 0.2215 0.0372  -0.0511 -0.0201 277  GLN B NE2 
11174 N N   . ALA B 280  ? 0.2782 0.1509 0.1935 0.0227  -0.0560 -0.0108 278  ALA B N   
11175 C CA  . ALA B 280  ? 0.2814 0.1416 0.1865 0.0195  -0.0579 -0.0083 278  ALA B CA  
11176 C C   . ALA B 280  ? 0.3012 0.1510 0.1997 0.0240  -0.0620 -0.0081 278  ALA B C   
11177 O O   . ALA B 280  ? 0.3075 0.1493 0.1982 0.0219  -0.0637 -0.0054 278  ALA B O   
11178 C CB  . ALA B 280  ? 0.3182 0.1734 0.2208 0.0164  -0.0574 -0.0086 278  ALA B CB  
11179 N N   . ALA B 281  ? 0.3039 0.1536 0.2052 0.0304  -0.0637 -0.0108 279  ALA B N   
11180 C CA  . ALA B 281  ? 0.3431 0.1830 0.2384 0.0354  -0.0678 -0.0107 279  ALA B CA  
11181 C C   . ALA B 281  ? 0.3496 0.1917 0.2444 0.0364  -0.0692 -0.0092 279  ALA B C   
11182 O O   . ALA B 281  ? 0.3490 0.1808 0.2352 0.0368  -0.0722 -0.0071 279  ALA B O   
11183 C CB  . ALA B 281  ? 0.3767 0.2185 0.2766 0.0423  -0.0689 -0.0141 279  ALA B CB  
11184 N N   . ARG B 282  ? 0.3168 0.1718 0.2200 0.0369  -0.0672 -0.0101 280  ARG B N   
11185 C CA  . ARG B 282  ? 0.3035 0.1609 0.2061 0.0374  -0.0684 -0.0087 280  ARG B CA  
11186 C C   . ARG B 282  ? 0.3033 0.1562 0.1988 0.0313  -0.0675 -0.0053 280  ARG B C   
11187 O O   . ARG B 282  ? 0.3167 0.1649 0.2065 0.0316  -0.0697 -0.0034 280  ARG B O   
11188 C CB  . ARG B 282  ? 0.3137 0.1856 0.2267 0.0387  -0.0663 -0.0106 280  ARG B CB  
11189 C CG  . ARG B 282  ? 0.3142 0.1918 0.2347 0.0451  -0.0674 -0.0137 280  ARG B CG  
11190 C CD  . ARG B 282  ? 0.2934 0.1840 0.2228 0.0460  -0.0661 -0.0149 280  ARG B CD  
11191 N NE  . ARG B 282  ? 0.3129 0.2023 0.2388 0.0462  -0.0684 -0.0134 280  ARG B NE  
11192 C CZ  . ARG B 282  ? 0.3359 0.2343 0.2668 0.0453  -0.0674 -0.0136 280  ARG B CZ  
11193 N NH1 . ARG B 282  ? 0.3199 0.2289 0.2593 0.0441  -0.0641 -0.0153 280  ARG B NH1 
11194 N NH2 . ARG B 282  ? 0.3431 0.2391 0.2696 0.0457  -0.0698 -0.0122 280  ARG B NH2 
11195 N N   . VAL B 283  ? 0.2896 0.1446 0.1857 0.0257  -0.0642 -0.0045 281  VAL B N   
11196 C CA  . VAL B 283  ? 0.3009 0.1526 0.1908 0.0196  -0.0629 -0.0012 281  VAL B CA  
11197 C C   . VAL B 283  ? 0.3220 0.1586 0.2004 0.0187  -0.0661 0.0012  281  VAL B C   
11198 O O   . VAL B 283  ? 0.3309 0.1626 0.2026 0.0171  -0.0672 0.0038  281  VAL B O   
11199 C CB  . VAL B 283  ? 0.2880 0.1456 0.1816 0.0140  -0.0589 -0.0009 281  VAL B CB  
11200 C CG1 . VAL B 283  ? 0.3186 0.1712 0.2049 0.0075  -0.0578 0.0027  281  VAL B CG1 
11201 C CG2 . VAL B 283  ? 0.2971 0.1691 0.2008 0.0144  -0.0557 -0.0026 281  VAL B CG2 
11202 N N   . MET B 284  ? 0.3231 0.1515 0.1986 0.0199  -0.0677 0.0003  282  MET B N   
11203 C CA  . MET B 284  ? 0.3223 0.1351 0.1863 0.0190  -0.0708 0.0026  282  MET B CA  
11204 C C   . MET B 284  ? 0.3673 0.1738 0.2270 0.0249  -0.0750 0.0028  282  MET B C   
11205 O O   . MET B 284  ? 0.3990 0.1940 0.2486 0.0236  -0.0775 0.0055  282  MET B O   
11206 C CB  . MET B 284  ? 0.3420 0.1471 0.2038 0.0191  -0.0717 0.0013  282  MET B CB  
11207 C CG  . MET B 284  ? 0.3802 0.1903 0.2454 0.0133  -0.0682 0.0012  282  MET B CG  
11208 S SD  . MET B 284  ? 0.3937 0.2023 0.2534 0.0040  -0.0660 0.0056  282  MET B SD  
11209 C CE  . MET B 284  ? 0.4380 0.2265 0.2834 0.0024  -0.0700 0.0082  282  MET B CE  
11210 N N   . GLY B 285  ? 0.3605 0.1745 0.2276 0.0311  -0.0759 0.0000  283  GLY B N   
11211 C CA  . GLY B 285  ? 0.3633 0.1720 0.2270 0.0372  -0.0802 -0.0001 283  GLY B CA  
11212 C C   . GLY B 285  ? 0.3700 0.1831 0.2332 0.0370  -0.0807 0.0014  283  GLY B C   
11213 O O   . GLY B 285  ? 0.4118 0.2172 0.2684 0.0399  -0.0845 0.0028  283  GLY B O   
11214 N N   . GLU B 286  ? 0.3497 0.1745 0.2193 0.0335  -0.0770 0.0013  284  GLU B N   
11215 C CA  . GLU B 286  ? 0.3283 0.1591 0.1988 0.0337  -0.0772 0.0020  284  GLU B CA  
11216 C C   . GLU B 286  ? 0.3538 0.1858 0.2205 0.0269  -0.0742 0.0048  284  GLU B C   
11217 O O   . GLU B 286  ? 0.3948 0.2237 0.2555 0.0263  -0.0755 0.0068  284  GLU B O   
11218 C CB  . GLU B 286  ? 0.3469 0.1919 0.2294 0.0370  -0.0759 -0.0012 284  GLU B CB  
11219 C CG  . GLU B 286  ? 0.3410 0.1869 0.2284 0.0440  -0.0786 -0.0040 284  GLU B CG  
11220 C CD  . GLU B 286  ? 0.3855 0.2459 0.2854 0.0460  -0.0764 -0.0071 284  GLU B CD  
11221 O OE1 . GLU B 286  ? 0.3961 0.2650 0.2999 0.0436  -0.0744 -0.0070 284  GLU B OE1 
11222 O OE2 . GLU B 286  ? 0.4120 0.2750 0.3174 0.0498  -0.0766 -0.0096 284  GLU B OE2 
11223 N N   . LEU B 287  ? 0.3477 0.1844 0.2179 0.0220  -0.0701 0.0048  285  LEU B N   
11224 C CA  . LEU B 287  ? 0.3414 0.1800 0.2085 0.0157  -0.0669 0.0074  285  LEU B CA  
11225 C C   . LEU B 287  ? 0.3431 0.1686 0.1985 0.0117  -0.0681 0.0109  285  LEU B C   
11226 O O   . LEU B 287  ? 0.3544 0.1769 0.2031 0.0091  -0.0680 0.0136  285  LEU B O   
11227 C CB  . LEU B 287  ? 0.3030 0.1517 0.1782 0.0121  -0.0623 0.0062  285  LEU B CB  
11228 C CG  . LEU B 287  ? 0.3362 0.1932 0.2131 0.0073  -0.0583 0.0075  285  LEU B CG  
11229 C CD1 . LEU B 287  ? 0.3030 0.1705 0.1892 0.0054  -0.0544 0.0059  285  LEU B CD1 
11230 C CD2 . LEU B 287  ? 0.3448 0.1943 0.2122 0.0017  -0.0575 0.0114  285  LEU B CD2 
11231 N N   . LEU B 288  ? 0.3612 0.1785 0.2137 0.0111  -0.0692 0.0110  286  LEU B N   
11232 C CA  . LEU B 288  ? 0.3681 0.1724 0.2095 0.0067  -0.0703 0.0144  286  LEU B CA  
11233 C C   . LEU B 288  ? 0.3925 0.1867 0.2239 0.0083  -0.0739 0.0168  286  LEU B C   
11234 O O   . LEU B 288  ? 0.3808 0.1703 0.2045 0.0031  -0.0730 0.0203  286  LEU B O   
11235 C CB  . LEU B 288  ? 0.3820 0.1778 0.2217 0.0072  -0.0719 0.0134  286  LEU B CB  
11236 C CG  . LEU B 288  ? 0.4400 0.2199 0.2675 0.0036  -0.0741 0.0166  286  LEU B CG  
11237 C CD1 . LEU B 288  ? 0.4334 0.2145 0.2576 -0.0049 -0.0708 0.0199  286  LEU B CD1 
11238 C CD2 . LEU B 288  ? 0.5053 0.2779 0.3321 0.0047  -0.0756 0.0148  286  LEU B CD2 
11239 N N   . PRO B 289  ? 0.3827 0.1737 0.2136 0.0152  -0.0779 0.0154  287  PRO B N   
11240 C CA  . PRO B 289  ? 0.3984 0.1796 0.2191 0.0165  -0.0814 0.0180  287  PRO B CA  
11241 C C   . PRO B 289  ? 0.3856 0.1728 0.2049 0.0137  -0.0795 0.0198  287  PRO B C   
11242 O O   . PRO B 289  ? 0.4313 0.2096 0.2402 0.0118  -0.0811 0.0231  287  PRO B O   
11243 C CB  . PRO B 289  ? 0.4337 0.2143 0.2574 0.0250  -0.0857 0.0154  287  PRO B CB  
11244 C CG  . PRO B 289  ? 0.4297 0.2131 0.2608 0.0272  -0.0849 0.0122  287  PRO B CG  
11245 C CD  . PRO B 289  ? 0.4160 0.2107 0.2545 0.0219  -0.0797 0.0116  287  PRO B CD  
11246 N N   . ARG B 290  ? 0.3686 0.1701 0.1976 0.0135  -0.0761 0.0178  288  ARG B N   
11247 C CA  . ARG B 290  ? 0.3614 0.1686 0.1889 0.0106  -0.0739 0.0192  288  ARG B CA  
11248 C C   . ARG B 290  ? 0.3370 0.1418 0.1589 0.0030  -0.0703 0.0225  288  ARG B C   
11249 O O   . ARG B 290  ? 0.3712 0.1715 0.1845 0.0003  -0.0703 0.0255  288  ARG B O   
11250 C CB  . ARG B 290  ? 0.3704 0.1930 0.2097 0.0123  -0.0712 0.0161  288  ARG B CB  
11251 C CG  . ARG B 290  ? 0.4001 0.2258 0.2437 0.0192  -0.0748 0.0135  288  ARG B CG  
11252 C CD  . ARG B 290  ? 0.4299 0.2701 0.2853 0.0205  -0.0721 0.0103  288  ARG B CD  
11253 N NE  . ARG B 290  ? 0.4566 0.3001 0.3153 0.0263  -0.0756 0.0082  288  ARG B NE  
11254 C CZ  . ARG B 290  ? 0.4246 0.2795 0.2936 0.0286  -0.0746 0.0052  288  ARG B CZ  
11255 N NH1 . ARG B 290  ? 0.4237 0.2877 0.3005 0.0261  -0.0703 0.0038  288  ARG B NH1 
11256 N NH2 . ARG B 290  ? 0.4322 0.2896 0.3037 0.0336  -0.0781 0.0036  288  ARG B NH2 
11257 N N   . VAL B 291  ? 0.3569 0.1647 0.1834 -0.0007 -0.0674 0.0221  289  VAL B N   
11258 C CA  . VAL B 291  ? 0.3609 0.1668 0.1825 -0.0082 -0.0642 0.0254  289  VAL B CA  
11259 C C   . VAL B 291  ? 0.3638 0.1538 0.1724 -0.0104 -0.0671 0.0290  289  VAL B C   
11260 O O   . VAL B 291  ? 0.3717 0.1586 0.1728 -0.0154 -0.0656 0.0324  289  VAL B O   
11261 C CB  . VAL B 291  ? 0.3328 0.1447 0.1618 -0.0116 -0.0611 0.0242  289  VAL B CB  
11262 C CG1 . VAL B 291  ? 0.3863 0.1985 0.2115 -0.0195 -0.0575 0.0276  289  VAL B CG1 
11263 C CG2 . VAL B 291  ? 0.3811 0.2076 0.2225 -0.0090 -0.0585 0.0207  289  VAL B CG2 
11264 N N   . LYS B 292  ? 0.3619 0.1415 0.1673 -0.0067 -0.0714 0.0282  290  LYS B N   
11265 C CA  . LYS B 292  ? 0.4062 0.1695 0.1987 -0.0084 -0.0746 0.0316  290  LYS B CA  
11266 C C   . LYS B 292  ? 0.4071 0.1662 0.1912 -0.0076 -0.0762 0.0341  290  LYS B C   
11267 O O   . LYS B 292  ? 0.4266 0.1773 0.2004 -0.0126 -0.0760 0.0381  290  LYS B O   
11268 C CB  . LYS B 292  ? 0.4099 0.1631 0.2008 -0.0030 -0.0792 0.0299  290  LYS B CB  
11269 C CG  . LYS B 292  ? 0.5507 0.2868 0.3285 -0.0017 -0.0839 0.0327  290  LYS B CG  
11270 C CD  . LYS B 292  ? 0.5757 0.3009 0.3435 -0.0093 -0.0831 0.0367  290  LYS B CD  
11271 C CE  . LYS B 292  ? 0.5789 0.2860 0.3330 -0.0076 -0.0881 0.0395  290  LYS B CE  
11272 N NZ  . LYS B 292  ? 0.5372 0.2377 0.2925 -0.0008 -0.0921 0.0364  290  LYS B NZ  
11273 N N   . ALA B 293  ? 0.3985 0.1637 0.1867 -0.0017 -0.0778 0.0319  291  ALA B N   
11274 C CA  . ALA B 293  ? 0.4292 0.1905 0.2092 -0.0006 -0.0797 0.0341  291  ALA B CA  
11275 C C   . ALA B 293  ? 0.4136 0.1807 0.1912 -0.0068 -0.0751 0.0365  291  ALA B C   
11276 O O   . ALA B 293  ? 0.4407 0.1999 0.2073 -0.0094 -0.0758 0.0401  291  ALA B O   
11277 C CB  . ALA B 293  ? 0.4240 0.1919 0.2100 0.0068  -0.0824 0.0309  291  ALA B CB  
11278 N N   . LEU B 294  ? 0.3888 0.1698 0.1765 -0.0089 -0.0704 0.0346  292  LEU B N   
11279 C CA  . LEU B 294  ? 0.3823 0.1696 0.1683 -0.0146 -0.0656 0.0367  292  LEU B CA  
11280 C C   . LEU B 294  ? 0.4058 0.1855 0.1842 -0.0219 -0.0638 0.0407  292  LEU B C   
11281 O O   . LEU B 294  ? 0.4061 0.1838 0.1767 -0.0262 -0.0619 0.0440  292  LEU B O   
11282 C CB  . LEU B 294  ? 0.3553 0.1587 0.1541 -0.0150 -0.0612 0.0337  292  LEU B CB  
11283 C CG  . LEU B 294  ? 0.3671 0.1789 0.1738 -0.0086 -0.0625 0.0298  292  LEU B CG  
11284 C CD1 . LEU B 294  ? 0.3381 0.1642 0.1570 -0.0093 -0.0582 0.0271  292  LEU B CD1 
11285 C CD2 . LEU B 294  ? 0.3890 0.2004 0.1895 -0.0071 -0.0634 0.0307  292  LEU B CD2 
11286 N N   . ALA B 295  ? 0.4094 0.1851 0.1899 -0.0236 -0.0643 0.0404  293  ALA B N   
11287 C CA  . ALA B 295  ? 0.4063 0.1742 0.1797 -0.0309 -0.0630 0.0442  293  ALA B CA  
11288 C C   . ALA B 295  ? 0.4342 0.1860 0.1932 -0.0316 -0.0666 0.0479  293  ALA B C   
11289 O O   . ALA B 295  ? 0.4534 0.2005 0.2042 -0.0380 -0.0648 0.0520  293  ALA B O   
11290 C CB  . ALA B 295  ? 0.3983 0.1642 0.1766 -0.0320 -0.0634 0.0427  293  ALA B CB  
11291 N N   . LEU B 296  ? 0.4198 0.1630 0.1752 -0.0250 -0.0719 0.0468  294  LEU B N   
11292 C CA  . LEU B 296  ? 0.4643 0.1916 0.2056 -0.0249 -0.0759 0.0503  294  LEU B CA  
11293 C C   . LEU B 296  ? 0.4655 0.1945 0.2000 -0.0269 -0.0742 0.0530  294  LEU B C   
11294 O O   . LEU B 296  ? 0.4898 0.2109 0.2149 -0.0313 -0.0740 0.0564  294  LEU B O   
11295 C CB  . LEU B 296  ? 0.5018 0.2214 0.2422 -0.0166 -0.0818 0.0481  294  LEU B CB  
11296 C CG  . LEU B 296  ? 0.5767 0.2835 0.3075 -0.0153 -0.0855 0.0494  294  LEU B CG  
11297 C CD1 . LEU B 296  ? 0.6018 0.2991 0.3275 -0.0212 -0.0849 0.0513  294  LEU B CD1 
11298 C CD2 . LEU B 296  ? 0.6112 0.3152 0.3448 -0.0064 -0.0905 0.0461  294  LEU B CD2 
11299 N N   . LEU B 297  ? 0.4310 0.1729 0.1727 -0.0238 -0.0724 0.0505  295  LEU B N   
11300 C CA  A LEU B 297  ? 0.4595 0.2039 0.1950 -0.0257 -0.0704 0.0527  295  LEU B CA  
11301 C CA  B LEU B 297  ? 0.4595 0.2040 0.1950 -0.0257 -0.0704 0.0527  295  LEU B CA  
11302 C C   . LEU B 297  ? 0.4351 0.1842 0.1692 -0.0341 -0.0646 0.0556  295  LEU B C   
11303 O O   . LEU B 297  ? 0.4564 0.1998 0.1797 -0.0381 -0.0636 0.0596  295  LEU B O   
11304 C CB  A LEU B 297  ? 0.4296 0.1867 0.1735 -0.0205 -0.0699 0.0490  295  LEU B CB  
11305 C CB  B LEU B 297  ? 0.4295 0.1867 0.1734 -0.0205 -0.0698 0.0490  295  LEU B CB  
11306 C CG  A LEU B 297  ? 0.4439 0.2010 0.1799 -0.0201 -0.0698 0.0506  295  LEU B CG  
11307 C CG  B LEU B 297  ? 0.4525 0.2069 0.1982 -0.0123 -0.0755 0.0462  295  LEU B CG  
11308 C CD1 A LEU B 297  ? 0.4670 0.2092 0.1907 -0.0178 -0.0752 0.0530  295  LEU B CD1 
11309 C CD1 B LEU B 297  ? 0.4215 0.1895 0.1762 -0.0084 -0.0743 0.0426  295  LEU B CD1 
11310 C CD2 A LEU B 297  ? 0.4528 0.2222 0.1979 -0.0150 -0.0696 0.0464  295  LEU B CD2 
11311 C CD2 B LEU B 297  ? 0.4721 0.2121 0.2041 -0.0104 -0.0805 0.0492  295  LEU B CD2 
11312 N N   . ALA B 298  ? 0.4447 0.2045 0.1896 -0.0368 -0.0607 0.0538  296  ALA B N   
11313 C CA  . ALA B 298  ? 0.4296 0.1950 0.1745 -0.0446 -0.0551 0.0564  296  ALA B CA  
11314 C C   . ALA B 298  ? 0.4641 0.2159 0.1978 -0.0508 -0.0561 0.0611  296  ALA B C   
11315 O O   . ALA B 298  ? 0.4703 0.2218 0.1974 -0.0568 -0.0528 0.0648  296  ALA B O   
11316 C CB  . ALA B 298  ? 0.4055 0.1837 0.1641 -0.0459 -0.0516 0.0535  296  ALA B CB  
11317 N N   . LYS B 299  ? 0.4451 0.1854 0.1766 -0.0493 -0.0604 0.0608  297  LYS B N   
11318 C CA  . LYS B 299  ? 0.5017 0.2300 0.2247 -0.0544 -0.0615 0.0640  297  LYS B CA  
11319 C C   . LYS B 299  ? 0.5109 0.2330 0.2246 -0.0540 -0.0626 0.0659  297  LYS B C   
11320 O O   . LYS B 299  ? 0.5438 0.2633 0.2520 -0.0603 -0.0603 0.0690  297  LYS B O   
11321 C CB  . LYS B 299  ? 0.4741 0.1922 0.1976 -0.0513 -0.0662 0.0620  297  LYS B CB  
11322 C CG  . LYS B 299  ? 0.5320 0.2375 0.2468 -0.0547 -0.0681 0.0641  297  LYS B CG  
11323 C CD  . LYS B 299  ? 0.6041 0.2990 0.3184 -0.0513 -0.0727 0.0619  297  LYS B CD  
11324 C CE  . LYS B 299  ? 0.6346 0.3171 0.3395 -0.0550 -0.0744 0.0642  297  LYS B CE  
11325 N NZ  . LYS B 299  ? 0.6986 0.3710 0.4027 -0.0528 -0.0784 0.0622  297  LYS B NZ  
11326 N N   . ASN B 300  ? 0.4938 0.2137 0.2058 -0.0468 -0.0661 0.0641  298  ASN B N   
11327 C CA  . ASN B 300  ? 0.5085 0.2215 0.2115 -0.0460 -0.0678 0.0658  298  ASN B CA  
11328 C C   . ASN B 300  ? 0.5087 0.2288 0.2085 -0.0510 -0.0628 0.0685  298  ASN B C   
11329 O O   . ASN B 300  ? 0.5451 0.2591 0.2367 -0.0539 -0.0625 0.0711  298  ASN B O   
11330 C CB  . ASN B 300  ? 0.5788 0.2899 0.2819 -0.0372 -0.0725 0.0631  298  ASN B CB  
11331 C CG  . ASN B 300  ? 0.6847 0.3877 0.3899 -0.0320 -0.0777 0.0607  298  ASN B CG  
11332 O OD1 . ASN B 300  ? 0.7600 0.4550 0.4630 -0.0350 -0.0784 0.0615  298  ASN B OD1 
11333 N ND2 . ASN B 300  ? 0.7055 0.4109 0.4152 -0.0242 -0.0811 0.0575  298  ASN B ND2 
11334 N N   . TYR B 301  ? 0.4795 0.2123 0.1854 -0.0520 -0.0586 0.0677  299  TYR B N   
11335 C CA  . TYR B 301  ? 0.4952 0.2360 0.1989 -0.0568 -0.0531 0.0700  299  TYR B CA  
11336 C C   . TYR B 301  ? 0.4748 0.2204 0.1813 -0.0651 -0.0482 0.0723  299  TYR B C   
11337 O O   . TYR B 301  ? 0.4893 0.2418 0.1943 -0.0697 -0.0432 0.0744  299  TYR B O   
11338 C CB  . TYR B 301  ? 0.4636 0.2162 0.1721 -0.0532 -0.0510 0.0678  299  TYR B CB  
11339 C CG  . TYR B 301  ? 0.4642 0.2144 0.1698 -0.0460 -0.0550 0.0658  299  TYR B CG  
11340 C CD1 . TYR B 301  ? 0.4805 0.2276 0.1779 -0.0460 -0.0549 0.0674  299  TYR B CD1 
11341 C CD2 . TYR B 301  ? 0.4625 0.2147 0.1741 -0.0392 -0.0587 0.0622  299  TYR B CD2 
11342 C CE1 . TYR B 301  ? 0.4912 0.2369 0.1864 -0.0396 -0.0586 0.0654  299  TYR B CE1 
11343 C CE2 . TYR B 301  ? 0.4552 0.2065 0.1651 -0.0328 -0.0623 0.0602  299  TYR B CE2 
11344 C CZ  . TYR B 301  ? 0.4659 0.2139 0.1677 -0.0331 -0.0624 0.0618  299  TYR B CZ  
11345 O OH  . TYR B 301  ? 0.5127 0.2600 0.2130 -0.0270 -0.0662 0.0597  299  TYR B OH  
11346 N N   . ASP B 302  ? 0.4730 0.2153 0.1835 -0.0669 -0.0495 0.0718  300  ASP B N   
11347 C CA  . ASP B 302  ? 0.4783 0.2258 0.1931 -0.0745 -0.0455 0.0735  300  ASP B CA  
11348 C C   . ASP B 302  ? 0.4805 0.2439 0.2023 -0.0767 -0.0397 0.0733  300  ASP B C   
11349 O O   . ASP B 302  ? 0.4753 0.2459 0.1971 -0.0825 -0.0347 0.0756  300  ASP B O   
11350 C CB  . ASP B 302  ? 0.5055 0.2467 0.2133 -0.0810 -0.0444 0.0770  300  ASP B CB  
11351 C CG  . ASP B 302  ? 0.5419 0.2852 0.2540 -0.0881 -0.0422 0.0782  300  ASP B CG  
11352 O OD1 . ASP B 302  ? 0.5239 0.2660 0.2415 -0.0869 -0.0444 0.0761  300  ASP B OD1 
11353 O OD2 . ASP B 302  ? 0.5983 0.3447 0.3085 -0.0949 -0.0386 0.0811  300  ASP B OD2 
11354 N N   . ILE B 303  ? 0.4436 0.2133 0.1723 -0.0715 -0.0404 0.0701  301  ILE B N   
11355 C CA  . ILE B 303  ? 0.4273 0.2152 0.1679 -0.0719 -0.0349 0.0677  301  ILE B CA  
11356 C C   . ILE B 303  ? 0.4324 0.2262 0.1854 -0.0710 -0.0353 0.0644  301  ILE B C   
11357 O O   . ILE B 303  ? 0.4170 0.2018 0.1698 -0.0684 -0.0399 0.0631  301  ILE B O   
11358 C CB  . ILE B 303  ? 0.4192 0.2149 0.1624 -0.0654 -0.0343 0.0647  301  ILE B CB  
11359 C CG1 . ILE B 303  ? 0.4246 0.2189 0.1738 -0.0574 -0.0391 0.0602  301  ILE B CG1 
11360 C CG2 . ILE B 303  ? 0.4332 0.2216 0.1630 -0.0658 -0.0347 0.0678  301  ILE B CG2 
11361 C CD1 . ILE B 303  ? 0.4147 0.2190 0.1692 -0.0516 -0.0382 0.0566  301  ILE B CD1 
11362 N N   . GLY B 304  ? 0.4012 0.2104 0.1647 -0.0729 -0.0303 0.0629  302  GLY B N   
11363 C CA  . GLY B 304  ? 0.3879 0.2043 0.1636 -0.0717 -0.0303 0.0596  302  GLY B CA  
11364 C C   . GLY B 304  ? 0.3754 0.1968 0.1588 -0.0633 -0.0323 0.0547  302  GLY B C   
11365 O O   . GLY B 304  ? 0.3994 0.2260 0.1830 -0.0594 -0.0313 0.0533  302  GLY B O   
11366 N N   . LEU B 305  ? 0.3695 0.1892 0.1591 -0.0607 -0.0351 0.0519  303  LEU B N   
11367 C CA  . LEU B 305  ? 0.3565 0.1822 0.1550 -0.0534 -0.0366 0.0472  303  LEU B CA  
11368 C C   . LEU B 305  ? 0.3560 0.1904 0.1658 -0.0547 -0.0349 0.0450  303  LEU B C   
11369 O O   . LEU B 305  ? 0.3627 0.1903 0.1721 -0.0566 -0.0371 0.0453  303  LEU B O   
11370 C CB  . LEU B 305  ? 0.3886 0.2021 0.1823 -0.0477 -0.0426 0.0459  303  LEU B CB  
11371 C CG  . LEU B 305  ? 0.4004 0.2203 0.2032 -0.0402 -0.0444 0.0411  303  LEU B CG  
11372 C CD1 . LEU B 305  ? 0.4702 0.2818 0.2669 -0.0343 -0.0490 0.0405  303  LEU B CD1 
11373 C CD2 . LEU B 305  ? 0.4103 0.2305 0.2205 -0.0392 -0.0457 0.0387  303  LEU B CD2 
11374 N N   . ASN B 306  ? 0.3307 0.1796 0.1502 -0.0535 -0.0311 0.0428  304  ASN B N   
11375 C CA  . ASN B 306  ? 0.3318 0.1906 0.1621 -0.0551 -0.0288 0.0410  304  ASN B CA  
11376 C C   . ASN B 306  ? 0.3249 0.1885 0.1641 -0.0484 -0.0305 0.0364  304  ASN B C   
11377 O O   . ASN B 306  ? 0.3089 0.1768 0.1501 -0.0436 -0.0304 0.0344  304  ASN B O   
11378 C CB  . ASN B 306  ? 0.3222 0.1944 0.1574 -0.0587 -0.0231 0.0420  304  ASN B CB  
11379 C CG  . ASN B 306  ? 0.3453 0.2288 0.1923 -0.0592 -0.0209 0.0398  304  ASN B CG  
11380 O OD1 . ASN B 306  ? 0.3398 0.2327 0.1951 -0.0547 -0.0196 0.0366  304  ASN B OD1 
11381 N ND2 . ASN B 306  ? 0.3268 0.2092 0.1747 -0.0647 -0.0207 0.0415  304  ASN B ND2 
11382 N N   . ILE B 307  ? 0.3022 0.1656 0.1469 -0.0484 -0.0318 0.0348  305  ILE B N   
11383 C CA  . ILE B 307  ? 0.3134 0.1829 0.1676 -0.0429 -0.0326 0.0305  305  ILE B CA  
11384 C C   . ILE B 307  ? 0.2922 0.1762 0.1566 -0.0446 -0.0282 0.0294  305  ILE B C   
11385 O O   . ILE B 307  ? 0.2793 0.1659 0.1466 -0.0492 -0.0269 0.0303  305  ILE B O   
11386 C CB  . ILE B 307  ? 0.2987 0.1596 0.1527 -0.0412 -0.0366 0.0291  305  ILE B CB  
11387 C CG1 . ILE B 307  ? 0.3655 0.2122 0.2095 -0.0386 -0.0411 0.0301  305  ILE B CG1 
11388 C CG2 . ILE B 307  ? 0.3027 0.1714 0.1670 -0.0361 -0.0367 0.0249  305  ILE B CG2 
11389 C CD1 . ILE B 307  ? 0.3750 0.2109 0.2163 -0.0378 -0.0449 0.0294  305  ILE B CD1 
11390 N N   . ASP B 308  ? 0.2703 0.1636 0.1400 -0.0410 -0.0262 0.0274  306  ASP B N   
11391 C CA  . ASP B 308  ? 0.2817 0.1887 0.1613 -0.0416 -0.0222 0.0261  306  ASP B CA  
11392 C C   . ASP B 308  ? 0.2738 0.1832 0.1612 -0.0400 -0.0235 0.0234  306  ASP B C   
11393 O O   . ASP B 308  ? 0.2778 0.1808 0.1647 -0.0361 -0.0271 0.0215  306  ASP B O   
11394 C CB  . ASP B 308  ? 0.2798 0.1943 0.1625 -0.0374 -0.0204 0.0241  306  ASP B CB  
11395 C CG  . ASP B 308  ? 0.3251 0.2402 0.2012 -0.0395 -0.0179 0.0266  306  ASP B CG  
11396 O OD1 . ASP B 308  ? 0.2915 0.2027 0.1614 -0.0447 -0.0169 0.0301  306  ASP B OD1 
11397 O OD2 . ASP B 308  ? 0.3452 0.2647 0.2223 -0.0360 -0.0168 0.0250  306  ASP B OD2 
11398 N N   . ALA B 309  ? 0.2408 0.1598 0.1354 -0.0427 -0.0205 0.0233  307  ALA B N   
11399 C CA  . ALA B 309  ? 0.2352 0.1576 0.1374 -0.0413 -0.0213 0.0208  307  ALA B CA  
11400 C C   . ALA B 309  ? 0.2293 0.1619 0.1401 -0.0366 -0.0196 0.0178  307  ALA B C   
11401 O O   . ALA B 309  ? 0.2375 0.1784 0.1509 -0.0367 -0.0163 0.0180  307  ALA B O   
11402 C CB  . ALA B 309  ? 0.2385 0.1650 0.1435 -0.0471 -0.0195 0.0225  307  ALA B CB  
11403 N N   . GLU B 310  ? 0.2130 0.1447 0.1279 -0.0326 -0.0218 0.0149  308  GLU B N   
11404 C CA  . GLU B 310  ? 0.2063 0.1461 0.1286 -0.0280 -0.0206 0.0120  308  GLU B CA  
11405 C C   . GLU B 310  ? 0.2055 0.1513 0.1358 -0.0279 -0.0200 0.0103  308  GLU B C   
11406 O O   . GLU B 310  ? 0.1986 0.1484 0.1308 -0.0321 -0.0182 0.0117  308  GLU B O   
11407 C CB  . GLU B 310  ? 0.2035 0.1375 0.1235 -0.0227 -0.0237 0.0101  308  GLU B CB  
11408 C CG  . GLU B 310  ? 0.2697 0.1978 0.1813 -0.0228 -0.0245 0.0119  308  GLU B CG  
11409 C CD  . GLU B 310  ? 0.2730 0.1967 0.1829 -0.0175 -0.0276 0.0101  308  GLU B CD  
11410 O OE1 . GLU B 310  ? 0.2839 0.2141 0.1986 -0.0143 -0.0267 0.0080  308  GLU B OE1 
11411 O OE2 . GLU B 310  ? 0.2679 0.1818 0.1716 -0.0166 -0.0311 0.0107  308  GLU B OE2 
11412 N N   . GLU B 311  ? 0.2075 0.1545 0.1424 -0.0233 -0.0213 0.0074  309  GLU B N   
11413 C CA  . GLU B 311  ? 0.2014 0.1547 0.1438 -0.0230 -0.0204 0.0057  309  GLU B CA  
11414 C C   . GLU B 311  ? 0.1910 0.1387 0.1314 -0.0258 -0.0223 0.0063  309  GLU B C   
11415 O O   . GLU B 311  ? 0.2163 0.1538 0.1499 -0.0265 -0.0249 0.0071  309  GLU B O   
11416 C CB  . GLU B 311  ? 0.1908 0.1463 0.1381 -0.0176 -0.0214 0.0026  309  GLU B CB  
11417 C CG  . GLU B 311  ? 0.2475 0.2088 0.1973 -0.0148 -0.0197 0.0017  309  GLU B CG  
11418 C CD  . GLU B 311  ? 0.2663 0.2214 0.2104 -0.0125 -0.0218 0.0017  309  GLU B CD  
11419 O OE1 . GLU B 311  ? 0.2315 0.1778 0.1689 -0.0134 -0.0241 0.0030  309  GLU B OE1 
11420 O OE2 . GLU B 311  ? 0.3252 0.2839 0.2713 -0.0097 -0.0212 0.0004  309  GLU B OE2 
11421 N N   . ALA B 312  ? 0.1887 0.1426 0.1348 -0.0273 -0.0210 0.0057  310  ALA B N   
11422 C CA  . ALA B 312  ? 0.2034 0.1526 0.1477 -0.0304 -0.0226 0.0061  310  ALA B CA  
11423 C C   . ALA B 312  ? 0.2171 0.1570 0.1582 -0.0272 -0.0260 0.0043  310  ALA B C   
11424 O O   . ALA B 312  ? 0.2106 0.1416 0.1460 -0.0297 -0.0282 0.0051  310  ALA B O   
11425 C CB  . ALA B 312  ? 0.2081 0.1663 0.1596 -0.0319 -0.0208 0.0055  310  ALA B CB  
11426 N N   . ASP B 313  ? 0.2050 0.1462 0.1492 -0.0217 -0.0266 0.0017  311  ASP B N   
11427 C CA  . ASP B 313  ? 0.2040 0.1373 0.1459 -0.0182 -0.0297 -0.0002 311  ASP B CA  
11428 C C   . ASP B 313  ? 0.2276 0.1508 0.1618 -0.0168 -0.0323 0.0006  311  ASP B C   
11429 O O   . ASP B 313  ? 0.2401 0.1566 0.1721 -0.0134 -0.0350 -0.0010 311  ASP B O   
11430 C CB  . ASP B 313  ? 0.2086 0.1477 0.1571 -0.0131 -0.0293 -0.0032 311  ASP B CB  
11431 C CG  . ASP B 313  ? 0.2613 0.2053 0.2125 -0.0100 -0.0283 -0.0037 311  ASP B CG  
11432 O OD1 . ASP B 313  ? 0.2396 0.1816 0.1869 -0.0109 -0.0283 -0.0021 311  ASP B OD1 
11433 O OD2 . ASP B 313  ? 0.2964 0.2461 0.2536 -0.0066 -0.0277 -0.0059 311  ASP B OD2 
11434 N N   . ARG B 314  ? 0.2063 0.1281 0.1363 -0.0195 -0.0317 0.0031  312  ARG B N   
11435 C CA  . ARG B 314  ? 0.2269 0.1383 0.1485 -0.0189 -0.0343 0.0044  312  ARG B CA  
11436 C C   . ARG B 314  ? 0.2269 0.1305 0.1412 -0.0244 -0.0350 0.0073  312  ARG B C   
11437 O O   . ARG B 314  ? 0.2493 0.1425 0.1557 -0.0242 -0.0375 0.0086  312  ARG B O   
11438 C CB  . ARG B 314  ? 0.2301 0.1447 0.1513 -0.0171 -0.0333 0.0050  312  ARG B CB  
11439 C CG  . ARG B 314  ? 0.2311 0.1495 0.1573 -0.0111 -0.0341 0.0021  312  ARG B CG  
11440 C CD  . ARG B 314  ? 0.2629 0.1878 0.1910 -0.0100 -0.0323 0.0022  312  ARG B CD  
11441 N NE  . ARG B 314  ? 0.2583 0.1840 0.1888 -0.0046 -0.0341 -0.0001 312  ARG B NE  
11442 C CZ  . ARG B 314  ? 0.2399 0.1706 0.1724 -0.0029 -0.0332 -0.0007 312  ARG B CZ  
11443 N NH1 . ARG B 314  ? 0.2417 0.1779 0.1746 -0.0055 -0.0302 0.0005  312  ARG B NH1 
11444 N NH2 . ARG B 314  ? 0.2661 0.1963 0.1999 0.0017  -0.0355 -0.0025 312  ARG B NH2 
11445 N N   . LEU B 315  ? 0.2325 0.1406 0.1492 -0.0293 -0.0330 0.0085  313  LEU B N   
11446 C CA  . LEU B 315  ? 0.2289 0.1307 0.1392 -0.0355 -0.0334 0.0115  313  LEU B CA  
11447 C C   . LEU B 315  ? 0.2769 0.1648 0.1797 -0.0352 -0.0373 0.0113  313  LEU B C   
11448 O O   . LEU B 315  ? 0.2675 0.1456 0.1619 -0.0367 -0.0391 0.0135  313  LEU B O   
11449 C CB  . LEU B 315  ? 0.2239 0.1340 0.1393 -0.0404 -0.0310 0.0122  313  LEU B CB  
11450 C CG  . LEU B 315  ? 0.2324 0.1409 0.1435 -0.0476 -0.0301 0.0158  313  LEU B CG  
11451 C CD1 . LEU B 315  ? 0.2501 0.1693 0.1682 -0.0515 -0.0276 0.0162  313  LEU B CD1 
11452 C CD2 . LEU B 315  ? 0.3064 0.2006 0.2083 -0.0506 -0.0335 0.0172  313  LEU B CD2 
11453 N N   . GLU B 316  ? 0.2609 0.1473 0.1661 -0.0331 -0.0387 0.0088  314  GLU B N   
11454 C CA  . GLU B 316  ? 0.2678 0.1408 0.1656 -0.0334 -0.0422 0.0087  314  GLU B CA  
11455 C C   . GLU B 316  ? 0.2880 0.1519 0.1806 -0.0279 -0.0450 0.0079  314  GLU B C   
11456 O O   . GLU B 316  ? 0.3052 0.1564 0.1889 -0.0289 -0.0478 0.0093  314  GLU B O   
11457 C CB  . GLU B 316  ? 0.2887 0.1626 0.1901 -0.0327 -0.0428 0.0061  314  GLU B CB  
11458 C CG  . GLU B 316  ? 0.2668 0.1467 0.1711 -0.0392 -0.0409 0.0075  314  GLU B CG  
11459 C CD  . GLU B 316  ? 0.3030 0.1836 0.2101 -0.0391 -0.0416 0.0051  314  GLU B CD  
11460 O OE1 . GLU B 316  ? 0.3011 0.1712 0.2032 -0.0368 -0.0444 0.0035  314  GLU B OE1 
11461 O OE2 . GLU B 316  ? 0.3044 0.1956 0.2183 -0.0412 -0.0393 0.0049  314  GLU B OE2 
11462 N N   . LEU B 317  ? 0.2658 0.1361 0.1636 -0.0222 -0.0445 0.0059  315  LEU B N   
11463 C CA  . LEU B 317  ? 0.3035 0.1669 0.1971 -0.0170 -0.0472 0.0054  315  LEU B CA  
11464 C C   . LEU B 317  ? 0.3084 0.1649 0.1939 -0.0198 -0.0480 0.0087  315  LEU B C   
11465 O O   . LEU B 317  ? 0.3201 0.1646 0.1976 -0.0181 -0.0513 0.0094  315  LEU B O   
11466 C CB  . LEU B 317  ? 0.2919 0.1651 0.1932 -0.0116 -0.0461 0.0030  315  LEU B CB  
11467 C CG  . LEU B 317  ? 0.3052 0.1733 0.2037 -0.0059 -0.0489 0.0022  315  LEU B CG  
11468 C CD1 . LEU B 317  ? 0.3480 0.2044 0.2411 -0.0028 -0.0525 0.0011  315  LEU B CD1 
11469 C CD2 . LEU B 317  ? 0.3383 0.2172 0.2456 -0.0012 -0.0477 -0.0003 315  LEU B CD2 
11470 N N   . SER B 318  ? 0.2825 0.1464 0.1695 -0.0239 -0.0449 0.0109  316  SER B N   
11471 C CA  . SER B 318  ? 0.2779 0.1360 0.1570 -0.0268 -0.0453 0.0142  316  SER B CA  
11472 C C   . SER B 318  ? 0.2843 0.1298 0.1543 -0.0316 -0.0473 0.0167  316  SER B C   
11473 O O   . SER B 318  ? 0.3132 0.1488 0.1744 -0.0322 -0.0493 0.0190  316  SER B O   
11474 C CB  . SER B 318  ? 0.2843 0.1532 0.1669 -0.0305 -0.0412 0.0159  316  SER B CB  
11475 O OG  . SER B 318  ? 0.2830 0.1562 0.1677 -0.0366 -0.0389 0.0174  316  SER B OG  
11476 N N   . LEU B 319  ? 0.2996 0.1445 0.1711 -0.0349 -0.0471 0.0162  317  LEU B N   
11477 C CA  . LEU B 319  ? 0.3071 0.1395 0.1699 -0.0397 -0.0493 0.0184  317  LEU B CA  
11478 C C   . LEU B 319  ? 0.3287 0.1464 0.1837 -0.0352 -0.0537 0.0175  317  LEU B C   
11479 O O   . LEU B 319  ? 0.3608 0.1658 0.2061 -0.0382 -0.0560 0.0201  317  LEU B O   
11480 C CB  . LEU B 319  ? 0.3220 0.1571 0.1883 -0.0439 -0.0485 0.0177  317  LEU B CB  
11481 C CG  . LEU B 319  ? 0.3003 0.1491 0.1738 -0.0491 -0.0444 0.0190  317  LEU B CG  
11482 C CD1 . LEU B 319  ? 0.2893 0.1398 0.1660 -0.0525 -0.0445 0.0179  317  LEU B CD1 
11483 C CD2 . LEU B 319  ? 0.3297 0.1777 0.1981 -0.0553 -0.0429 0.0232  317  LEU B CD2 
11484 N N   . ASP B 320  ? 0.3218 0.1409 0.1810 -0.0280 -0.0551 0.0141  318  ASP B N   
11485 C CA  . ASP B 320  ? 0.3616 0.1675 0.2140 -0.0230 -0.0593 0.0131  318  ASP B CA  
11486 C C   . ASP B 320  ? 0.3647 0.1646 0.2104 -0.0213 -0.0609 0.0153  318  ASP B C   
11487 O O   . ASP B 320  ? 0.3901 0.1760 0.2267 -0.0198 -0.0645 0.0162  318  ASP B O   
11488 C CB  . ASP B 320  ? 0.3509 0.1614 0.2102 -0.0156 -0.0599 0.0088  318  ASP B CB  
11489 C CG  . ASP B 320  ? 0.3765 0.1878 0.2390 -0.0167 -0.0595 0.0066  318  ASP B CG  
11490 O OD1 . ASP B 320  ? 0.3937 0.1930 0.2488 -0.0190 -0.0618 0.0072  318  ASP B OD1 
11491 O OD2 . ASP B 320  ? 0.3983 0.2218 0.2701 -0.0155 -0.0570 0.0045  318  ASP B OD2 
11492 N N   . LEU B 321  ? 0.3373 0.1472 0.1869 -0.0213 -0.0585 0.0161  319  LEU B N   
11493 C CA  . LEU B 321  ? 0.3443 0.1486 0.1869 -0.0204 -0.0599 0.0185  319  LEU B CA  
11494 C C   . LEU B 321  ? 0.3618 0.1580 0.1952 -0.0277 -0.0597 0.0228  319  LEU B C   
11495 O O   . LEU B 321  ? 0.3959 0.1795 0.2194 -0.0274 -0.0627 0.0249  319  LEU B O   
11496 C CB  . LEU B 321  ? 0.3506 0.1678 0.1998 -0.0183 -0.0574 0.0179  319  LEU B CB  
11497 C CG  . LEU B 321  ? 0.3375 0.1599 0.1932 -0.0105 -0.0588 0.0143  319  LEU B CG  
11498 C CD1 . LEU B 321  ? 0.3658 0.2000 0.2326 -0.0096 -0.0562 0.0112  319  LEU B CD1 
11499 C CD2 . LEU B 321  ? 0.4154 0.2427 0.2714 -0.0082 -0.0585 0.0148  319  LEU B CD2 
11500 N N   . LEU B 322  ? 0.3545 0.1581 0.1913 -0.0343 -0.0562 0.0242  320  LEU B N   
11501 C CA  . LEU B 322  ? 0.3711 0.1683 0.2000 -0.0419 -0.0555 0.0283  320  LEU B CA  
11502 C C   . LEU B 322  ? 0.3883 0.1687 0.2077 -0.0434 -0.0594 0.0293  320  LEU B C   
11503 O O   . LEU B 322  ? 0.3872 0.1563 0.1962 -0.0464 -0.0610 0.0327  320  LEU B O   
11504 C CB  . LEU B 322  ? 0.3444 0.1534 0.1801 -0.0482 -0.0513 0.0291  320  LEU B CB  
11505 C CG  . LEU B 322  ? 0.3635 0.1690 0.1928 -0.0567 -0.0499 0.0335  320  LEU B CG  
11506 C CD1 . LEU B 322  ? 0.3721 0.1782 0.1966 -0.0571 -0.0486 0.0362  320  LEU B CD1 
11507 C CD2 . LEU B 322  ? 0.3479 0.1657 0.1851 -0.0625 -0.0461 0.0338  320  LEU B CD2 
11508 N N   . GLU B 323  ? 0.4025 0.1806 0.2248 -0.0414 -0.0609 0.0265  321  GLU B N   
11509 C CA  . GLU B 323  ? 0.4061 0.1676 0.2194 -0.0422 -0.0648 0.0268  321  GLU B CA  
11510 C C   . GLU B 323  ? 0.4277 0.1758 0.2316 -0.0374 -0.0687 0.0276  321  GLU B C   
11511 O O   . GLU B 323  ? 0.4544 0.1884 0.2473 -0.0410 -0.0710 0.0307  321  GLU B O   
11512 C CB  . GLU B 323  ? 0.4108 0.1732 0.2294 -0.0387 -0.0657 0.0227  321  GLU B CB  
11513 C CG  . GLU B 323  ? 0.4808 0.2254 0.2900 -0.0380 -0.0700 0.0223  321  GLU B CG  
11514 C CD  . GLU B 323  ? 0.5245 0.2642 0.3304 -0.0461 -0.0699 0.0237  321  GLU B CD  
11515 O OE1 . GLU B 323  ? 0.4944 0.2459 0.3068 -0.0517 -0.0664 0.0246  321  GLU B OE1 
11516 O OE2 . GLU B 323  ? 0.5211 0.2449 0.3178 -0.0469 -0.0734 0.0239  321  GLU B OE2 
11517 N N   . VAL B 324  ? 0.3993 0.1516 0.2074 -0.0293 -0.0697 0.0251  322  VAL B N   
11518 C CA  . VAL B 324  ? 0.4038 0.1441 0.2037 -0.0239 -0.0738 0.0256  322  VAL B CA  
11519 C C   . VAL B 324  ? 0.4400 0.1760 0.2319 -0.0277 -0.0736 0.0299  322  VAL B C   
11520 O O   . VAL B 324  ? 0.4625 0.1834 0.2432 -0.0277 -0.0770 0.0323  322  VAL B O   
11521 C CB  . VAL B 324  ? 0.4443 0.1921 0.2516 -0.0149 -0.0746 0.0220  322  VAL B CB  
11522 C CG1 . VAL B 324  ? 0.4760 0.2127 0.2752 -0.0094 -0.0789 0.0228  322  VAL B CG1 
11523 C CG2 . VAL B 324  ? 0.4622 0.2123 0.2760 -0.0109 -0.0750 0.0178  322  VAL B CG2 
11524 N N   . LEU B 325  ? 0.4127 0.1617 0.2097 -0.0308 -0.0697 0.0311  323  LEU B N   
11525 C CA  . LEU B 325  ? 0.4266 0.1726 0.2161 -0.0340 -0.0692 0.0351  323  LEU B CA  
11526 C C   . LEU B 325  ? 0.4213 0.1560 0.2009 -0.0422 -0.0693 0.0392  323  LEU B C   
11527 O O   . LEU B 325  ? 0.4643 0.1874 0.2329 -0.0434 -0.0714 0.0425  323  LEU B O   
11528 C CB  . LEU B 325  ? 0.4184 0.1811 0.2158 -0.0356 -0.0645 0.0351  323  LEU B CB  
11529 C CG  . LEU B 325  ? 0.4286 0.2015 0.2345 -0.0279 -0.0645 0.0315  323  LEU B CG  
11530 C CD1 . LEU B 325  ? 0.4253 0.2148 0.2401 -0.0300 -0.0597 0.0310  323  LEU B CD1 
11531 C CD2 . LEU B 325  ? 0.4217 0.1872 0.2207 -0.0228 -0.0680 0.0323  323  LEU B CD2 
11532 N N   . CYS B 326  ? 0.4396 0.1776 0.2228 -0.0480 -0.0673 0.0392  324  CYS B N   
11533 C CA  . CYS B 326  ? 0.4287 0.1571 0.2033 -0.0565 -0.0673 0.0432  324  CYS B CA  
11534 C C   . CYS B 326  ? 0.4481 0.1563 0.2114 -0.0556 -0.0724 0.0439  324  CYS B C   
11535 O O   . CYS B 326  ? 0.4871 0.1860 0.2415 -0.0613 -0.0730 0.0473  324  CYS B O   
11536 C CB  . CYS B 326  ? 0.4631 0.2010 0.2450 -0.0629 -0.0640 0.0429  324  CYS B CB  
11537 S SG  . CYS B 326  ? 0.4565 0.2160 0.2489 -0.0662 -0.0578 0.0436  324  CYS B SG  
11538 N N   . LEU B 327  ? 0.4412 0.1447 0.2061 -0.0481 -0.0756 0.0401  325  LEU B N   
11539 C CA  . LEU B 327  ? 0.4856 0.1735 0.2421 -0.0455 -0.0800 0.0394  325  LEU B CA  
11540 C C   . LEU B 327  ? 0.5015 0.1832 0.2528 -0.0384 -0.0831 0.0391  325  LEU B C   
11541 O O   . LEU B 327  ? 0.4952 0.1663 0.2406 -0.0354 -0.0865 0.0380  325  LEU B O   
11542 C CB  . LEU B 327  ? 0.4572 0.1443 0.2187 -0.0416 -0.0814 0.0351  325  LEU B CB  
11543 C CG  . LEU B 327  ? 0.5069 0.1981 0.2723 -0.0489 -0.0791 0.0350  325  LEU B CG  
11544 C CD1 . LEU B 327  ? 0.5275 0.2208 0.2995 -0.0442 -0.0798 0.0305  325  LEU B CD1 
11545 C CD2 . LEU B 327  ? 0.6014 0.2841 0.3590 -0.0554 -0.0800 0.0370  325  LEU B CD2 
11546 N N   . ASP B 328  ? 0.5099 0.1980 0.2631 -0.0356 -0.0822 0.0401  326  ASP B N   
11547 C CA  . ASP B 328  ? 0.5158 0.1994 0.2649 -0.0288 -0.0852 0.0397  326  ASP B CA  
11548 C C   . ASP B 328  ? 0.4724 0.1483 0.2114 -0.0333 -0.0857 0.0433  326  ASP B C   
11549 O O   . ASP B 328  ? 0.5077 0.1883 0.2452 -0.0387 -0.0828 0.0466  326  ASP B O   
11550 C CB  . ASP B 328  ? 0.5152 0.2093 0.2703 -0.0243 -0.0841 0.0393  326  ASP B CB  
11551 C CG  . ASP B 328  ? 0.5671 0.2583 0.3201 -0.0160 -0.0877 0.0380  326  ASP B CG  
11552 O OD1 . ASP B 328  ? 0.5317 0.2132 0.2764 -0.0157 -0.0902 0.0390  326  ASP B OD1 
11553 O OD2 . ASP B 328  ? 0.6016 0.3019 0.3620 -0.0100 -0.0878 0.0355  326  ASP B OD2 
11554 N N   . GLY B 329  ? 0.5135 0.1775 0.2453 -0.0311 -0.0892 0.0427  327  GLY B N   
11555 C CA  . GLY B 329  ? 0.5184 0.1737 0.2401 -0.0352 -0.0900 0.0460  327  GLY B CA  
11556 C C   . GLY B 329  ? 0.5029 0.1608 0.2219 -0.0336 -0.0898 0.0481  327  GLY B C   
11557 O O   . GLY B 329  ? 0.5512 0.2047 0.2627 -0.0387 -0.0890 0.0515  327  GLY B O   
11558 N N   . ASP B 330  ? 0.5256 0.1907 0.2503 -0.0268 -0.0903 0.0462  328  ASP B N   
11559 C CA  . ASP B 330  ? 0.5361 0.2048 0.2584 -0.0256 -0.0899 0.0480  328  ASP B CA  
11560 C C   . ASP B 330  ? 0.5479 0.2245 0.2705 -0.0333 -0.0851 0.0514  328  ASP B C   
11561 O O   . ASP B 330  ? 0.5690 0.2469 0.2873 -0.0343 -0.0843 0.0536  328  ASP B O   
11562 C CB  . ASP B 330  ? 0.5345 0.2106 0.2638 -0.0169 -0.0915 0.0451  328  ASP B CB  
11563 C CG  . ASP B 330  ? 0.6187 0.2879 0.3471 -0.0087 -0.0962 0.0421  328  ASP B CG  
11564 O OD1 . ASP B 330  ? 0.6197 0.2774 0.3401 -0.0093 -0.0986 0.0429  328  ASP B OD1 
11565 O OD2 . ASP B 330  ? 0.5819 0.2575 0.3176 -0.0015 -0.0976 0.0390  328  ASP B OD2 
11566 N N   . LEU B 331  ? 0.4905 0.1732 0.2184 -0.0387 -0.0818 0.0516  329  LEU B N   
11567 C CA  . LEU B 331  ? 0.4893 0.1807 0.2184 -0.0462 -0.0768 0.0546  329  LEU B CA  
11568 C C   . LEU B 331  ? 0.4904 0.1770 0.2145 -0.0551 -0.0751 0.0574  329  LEU B C   
11569 O O   . LEU B 331  ? 0.4947 0.1896 0.2215 -0.0620 -0.0708 0.0595  329  LEU B O   
11570 C CB  . LEU B 331  ? 0.4881 0.1915 0.2274 -0.0463 -0.0740 0.0531  329  LEU B CB  
11571 C CG  . LEU B 331  ? 0.4484 0.1599 0.1947 -0.0376 -0.0751 0.0497  329  LEU B CG  
11572 C CD1 . LEU B 331  ? 0.4577 0.1862 0.2188 -0.0372 -0.0713 0.0459  329  LEU B CD1 
11573 C CD2 . LEU B 331  ? 0.4882 0.2030 0.2307 -0.0365 -0.0744 0.0515  329  LEU B CD2 
11574 N N   . SER B 332  ? 0.5266 0.2005 0.2436 -0.0549 -0.0786 0.0574  330  SER B N   
11575 C CA  . SER B 332  ? 0.5234 0.1915 0.2353 -0.0629 -0.0777 0.0598  330  SER B CA  
11576 C C   . SER B 332  ? 0.5407 0.2146 0.2503 -0.0705 -0.0735 0.0638  330  SER B C   
11577 O O   . SER B 332  ? 0.5611 0.2350 0.2663 -0.0691 -0.0731 0.0655  330  SER B O   
11578 C CB  . SER B 332  ? 0.5626 0.2154 0.2652 -0.0605 -0.0823 0.0596  330  SER B CB  
11579 O OG  . SER B 332  ? 0.6083 0.2549 0.3058 -0.0681 -0.0818 0.0617  330  SER B OG  
11580 N N   . GLY B 333  ? 0.5305 0.2095 0.2431 -0.0785 -0.0702 0.0653  331  GLY B N   
11581 C CA  . GLY B 333  ? 0.5605 0.2452 0.2712 -0.0863 -0.0660 0.0691  331  GLY B CA  
11582 C C   . GLY B 333  ? 0.5576 0.2570 0.2744 -0.0869 -0.0613 0.0699  331  GLY B C   
11583 O O   . GLY B 333  ? 0.5748 0.2811 0.2914 -0.0934 -0.0571 0.0728  331  GLY B O   
11584 N N   . TRP B 334  ? 0.5202 0.2250 0.2424 -0.0802 -0.0618 0.0673  332  TRP B N   
11585 C CA  . TRP B 334  ? 0.5300 0.2486 0.2577 -0.0801 -0.0576 0.0678  332  TRP B CA  
11586 C C   . TRP B 334  ? 0.4746 0.2046 0.2115 -0.0849 -0.0539 0.0675  332  TRP B C   
11587 O O   . TRP B 334  ? 0.5025 0.2325 0.2450 -0.0826 -0.0555 0.0649  332  TRP B O   
11588 C CB  . TRP B 334  ? 0.5299 0.2490 0.2592 -0.0709 -0.0602 0.0651  332  TRP B CB  
11589 C CG  . TRP B 334  ? 0.5019 0.2345 0.2367 -0.0697 -0.0564 0.0650  332  TRP B CG  
11590 C CD1 . TRP B 334  ? 0.4894 0.2291 0.2221 -0.0724 -0.0526 0.0672  332  TRP B CD1 
11591 C CD2 . TRP B 334  ? 0.4729 0.2175 0.2200 -0.0643 -0.0557 0.0605  332  TRP B CD2 
11592 N NE1 . TRP B 334  ? 0.4406 0.1951 0.1826 -0.0691 -0.0497 0.0646  332  TRP B NE1 
11593 C CE2 . TRP B 334  ? 0.4489 0.2076 0.2009 -0.0640 -0.0514 0.0601  332  TRP B CE2 
11594 C CE3 . TRP B 334  ? 0.4467 0.1925 0.2018 -0.0595 -0.0580 0.0563  332  TRP B CE3 
11595 C CZ2 . TRP B 334  ? 0.4297 0.2029 0.1942 -0.0593 -0.0495 0.0558  332  TRP B CZ2 
11596 C CZ3 . TRP B 334  ? 0.4833 0.2440 0.2509 -0.0549 -0.0559 0.0522  332  TRP B CZ3 
11597 C CH2 . TRP B 334  ? 0.4762 0.2502 0.2484 -0.0549 -0.0518 0.0520  332  TRP B CH2 
11598 N N   . ASN B 335  ? 0.4787 0.2191 0.2178 -0.0914 -0.0488 0.0701  333  ASN B N   
11599 C CA  . ASN B 335  ? 0.4549 0.2075 0.2033 -0.0962 -0.0450 0.0699  333  ASN B CA  
11600 C C   . ASN B 335  ? 0.4745 0.2428 0.2312 -0.0933 -0.0411 0.0685  333  ASN B C   
11601 O O   . ASN B 335  ? 0.4527 0.2350 0.2185 -0.0971 -0.0368 0.0681  333  ASN B O   
11602 C CB  . ASN B 335  ? 0.4892 0.2456 0.2372 -0.1053 -0.0417 0.0729  333  ASN B CB  
11603 C CG  . ASN B 335  ? 0.5252 0.2687 0.2678 -0.1084 -0.0454 0.0733  333  ASN B CG  
11604 O OD1 . ASN B 335  ? 0.5160 0.2511 0.2584 -0.1049 -0.0495 0.0707  333  ASN B OD1 
11605 N ND2 . ASN B 335  ? 0.5288 0.2708 0.2666 -0.1147 -0.0439 0.0763  333  ASN B ND2 
11606 N N   . GLY B 336  ? 0.4402 0.2088 0.1962 -0.0857 -0.0424 0.0664  334  GLY B N   
11607 C CA  . GLY B 336  ? 0.4293 0.2142 0.1948 -0.0819 -0.0388 0.0637  334  GLY B CA  
11608 C C   . GLY B 336  ? 0.3963 0.1898 0.1739 -0.0756 -0.0395 0.0585  334  GLY B C   
11609 O O   . GLY B 336  ? 0.3903 0.1966 0.1756 -0.0721 -0.0368 0.0561  334  GLY B O   
11610 N N   . MET B 337  ? 0.4135 0.2003 0.1930 -0.0742 -0.0430 0.0566  335  MET B N   
11611 C CA  . MET B 337  ? 0.3985 0.1941 0.1897 -0.0688 -0.0432 0.0518  335  MET B CA  
11612 C C   . MET B 337  ? 0.4054 0.2169 0.2073 -0.0729 -0.0383 0.0512  335  MET B C   
11613 O O   . MET B 337  ? 0.3932 0.2045 0.1951 -0.0797 -0.0371 0.0533  335  MET B O   
11614 C CB  . MET B 337  ? 0.4181 0.2026 0.2081 -0.0669 -0.0478 0.0501  335  MET B CB  
11615 C CG  . MET B 337  ? 0.4436 0.2362 0.2449 -0.0611 -0.0482 0.0451  335  MET B CG  
11616 S SD  . MET B 337  ? 0.5682 0.3616 0.3712 -0.0509 -0.0508 0.0418  335  MET B SD  
11617 C CE  . MET B 337  ? 0.4517 0.2654 0.2664 -0.0500 -0.0455 0.0399  335  MET B CE  
11618 N N   . GLY B 338  ? 0.4041 0.2292 0.2150 -0.0687 -0.0356 0.0484  336  GLY B N   
11619 C CA  . GLY B 338  ? 0.3560 0.1969 0.1775 -0.0714 -0.0310 0.0476  336  GLY B CA  
11620 C C   . GLY B 338  ? 0.3516 0.2000 0.1842 -0.0664 -0.0315 0.0430  336  GLY B C   
11621 O O   . GLY B 338  ? 0.3418 0.1876 0.1756 -0.0596 -0.0343 0.0401  336  GLY B O   
11622 N N   . PHE B 339  ? 0.3219 0.1801 0.1628 -0.0699 -0.0289 0.0425  337  PHE B N   
11623 C CA  . PHE B 339  ? 0.3058 0.1705 0.1566 -0.0659 -0.0295 0.0386  337  PHE B CA  
11624 C C   . PHE B 339  ? 0.2946 0.1748 0.1552 -0.0689 -0.0250 0.0383  337  PHE B C   
11625 O O   . PHE B 339  ? 0.3050 0.1874 0.1652 -0.0757 -0.0232 0.0411  337  PHE B O   
11626 C CB  . PHE B 339  ? 0.3294 0.1834 0.1778 -0.0667 -0.0334 0.0378  337  PHE B CB  
11627 C CG  . PHE B 339  ? 0.3067 0.1648 0.1634 -0.0613 -0.0347 0.0335  337  PHE B CG  
11628 C CD1 . PHE B 339  ? 0.3249 0.1781 0.1810 -0.0541 -0.0376 0.0308  337  PHE B CD1 
11629 C CD2 . PHE B 339  ? 0.3091 0.1760 0.1740 -0.0637 -0.0329 0.0323  337  PHE B CD2 
11630 C CE1 . PHE B 339  ? 0.3116 0.1688 0.1753 -0.0493 -0.0385 0.0269  337  PHE B CE1 
11631 C CE2 . PHE B 339  ? 0.3306 0.2009 0.2027 -0.0590 -0.0340 0.0285  337  PHE B CE2 
11632 C CZ  . PHE B 339  ? 0.2969 0.1625 0.1683 -0.0518 -0.0367 0.0258  337  PHE B CZ  
11633 N N   . VAL B 340  ? 0.2919 0.1828 0.1613 -0.0640 -0.0233 0.0352  338  VAL B N   
11634 C CA  . VAL B 340  ? 0.2698 0.1757 0.1489 -0.0657 -0.0192 0.0347  338  VAL B CA  
11635 C C   . VAL B 340  ? 0.2816 0.1900 0.1675 -0.0661 -0.0204 0.0327  338  VAL B C   
11636 O O   . VAL B 340  ? 0.2757 0.1789 0.1625 -0.0617 -0.0235 0.0299  338  VAL B O   
11637 C CB  . VAL B 340  ? 0.2592 0.1746 0.1437 -0.0600 -0.0170 0.0323  338  VAL B CB  
11638 C CG1 . VAL B 340  ? 0.2773 0.2079 0.1720 -0.0611 -0.0129 0.0315  338  VAL B CG1 
11639 C CG2 . VAL B 340  ? 0.2709 0.1836 0.1481 -0.0595 -0.0159 0.0341  338  VAL B CG2 
11640 N N   . VAL B 341  ? 0.2605 0.1776 0.1515 -0.0713 -0.0178 0.0340  339  VAL B N   
11641 C CA  A VAL B 341  ? 0.2535 0.1758 0.1522 -0.0716 -0.0183 0.0320  339  VAL B CA  
11642 C CA  B VAL B 341  ? 0.2536 0.1759 0.1523 -0.0716 -0.0183 0.0320  339  VAL B CA  
11643 C C   . VAL B 341  ? 0.2418 0.1805 0.1502 -0.0718 -0.0140 0.0316  339  VAL B C   
11644 O O   . VAL B 341  ? 0.2500 0.1955 0.1586 -0.0754 -0.0107 0.0342  339  VAL B O   
11645 C CB  A VAL B 341  ? 0.2650 0.1804 0.1602 -0.0780 -0.0204 0.0339  339  VAL B CB  
11646 C CB  B VAL B 341  ? 0.2651 0.1805 0.1603 -0.0781 -0.0204 0.0339  339  VAL B CB  
11647 C CG1 A VAL B 341  ? 0.2831 0.1999 0.1841 -0.0766 -0.0222 0.0310  339  VAL B CG1 
11648 C CG1 B VAL B 341  ? 0.2771 0.1755 0.1626 -0.0771 -0.0249 0.0339  339  VAL B CG1 
11649 C CG2 A VAL B 341  ? 0.2822 0.1810 0.1660 -0.0789 -0.0239 0.0353  339  VAL B CG2 
11650 C CG2 B VAL B 341  ? 0.2751 0.1949 0.1687 -0.0857 -0.0176 0.0379  339  VAL B CG2 
11651 N N   . GLN B 342  ? 0.2357 0.1808 0.1521 -0.0676 -0.0141 0.0284  340  GLN B N   
11652 C CA  . GLN B 342  ? 0.2421 0.2021 0.1680 -0.0662 -0.0105 0.0274  340  GLN B CA  
11653 C C   . GLN B 342  ? 0.2150 0.1822 0.1470 -0.0706 -0.0100 0.0280  340  GLN B C   
11654 O O   . GLN B 342  ? 0.2126 0.1773 0.1469 -0.0698 -0.0124 0.0261  340  GLN B O   
11655 C CB  . GLN B 342  ? 0.2111 0.1734 0.1416 -0.0588 -0.0110 0.0237  340  GLN B CB  
11656 C CG  . GLN B 342  ? 0.2109 0.1677 0.1363 -0.0543 -0.0116 0.0230  340  GLN B CG  
11657 C CD  . GLN B 342  ? 0.2124 0.1656 0.1397 -0.0480 -0.0141 0.0195  340  GLN B CD  
11658 O OE1 . GLN B 342  ? 0.2194 0.1668 0.1464 -0.0476 -0.0170 0.0183  340  GLN B OE1 
11659 N NE2 . GLN B 342  ? 0.2008 0.1576 0.1300 -0.0431 -0.0131 0.0178  340  GLN B NE2 
11660 N N   . ALA B 343  ? 0.2148 0.1915 0.1497 -0.0751 -0.0066 0.0305  341  ALA B N   
11661 C CA  . ALA B 343  ? 0.2136 0.1980 0.1545 -0.0798 -0.0061 0.0314  341  ALA B CA  
11662 C C   . ALA B 343  ? 0.2075 0.2019 0.1579 -0.0759 -0.0054 0.0286  341  ALA B C   
11663 O O   . ALA B 343  ? 0.2057 0.2042 0.1606 -0.0789 -0.0063 0.0287  341  ALA B O   
11664 C CB  . ALA B 343  ? 0.2155 0.2085 0.1573 -0.0854 -0.0026 0.0349  341  ALA B CB  
11665 N N   . TYR B 344  ? 0.2046 0.2025 0.1581 -0.0693 -0.0042 0.0262  342  TYR B N   
11666 C CA  . TYR B 344  ? 0.2018 0.2075 0.1636 -0.0657 -0.0040 0.0237  342  TYR B CA  
11667 C C   . TYR B 344  ? 0.1859 0.1833 0.1465 -0.0637 -0.0078 0.0213  342  TYR B C   
11668 O O   . TYR B 344  ? 0.1989 0.2017 0.1658 -0.0612 -0.0080 0.0193  342  TYR B O   
11669 C CB  . TYR B 344  ? 0.2012 0.2134 0.1668 -0.0595 -0.0014 0.0218  342  TYR B CB  
11670 C CG  . TYR B 344  ? 0.1846 0.1890 0.1464 -0.0538 -0.0028 0.0196  342  TYR B CG  
11671 C CD1 . TYR B 344  ? 0.1858 0.1775 0.1406 -0.0535 -0.0063 0.0191  342  TYR B CD1 
11672 C CD2 . TYR B 344  ? 0.1656 0.1757 0.1308 -0.0487 -0.0007 0.0179  342  TYR B CD2 
11673 C CE1 . TYR B 344  ? 0.1787 0.1644 0.1307 -0.0481 -0.0076 0.0171  342  TYR B CE1 
11674 C CE2 . TYR B 344  ? 0.1785 0.1825 0.1407 -0.0439 -0.0020 0.0159  342  TYR B CE2 
11675 C CZ  . TYR B 344  ? 0.1735 0.1658 0.1294 -0.0435 -0.0054 0.0155  342  TYR B CZ  
11676 O OH  . TYR B 344  ? 0.1872 0.1746 0.1409 -0.0386 -0.0067 0.0135  342  TYR B OH  
11677 N N   . GLY B 345  ? 0.1932 0.1776 0.1459 -0.0648 -0.0109 0.0216  343  GLY B N   
11678 C CA  . GLY B 345  ? 0.2103 0.1862 0.1613 -0.0626 -0.0144 0.0192  343  GLY B CA  
11679 C C   . GLY B 345  ? 0.2150 0.1880 0.1650 -0.0682 -0.0165 0.0201  343  GLY B C   
11680 O O   . GLY B 345  ? 0.2154 0.1859 0.1615 -0.0742 -0.0166 0.0230  343  GLY B O   
11681 N N   . LYS B 346  ? 0.2158 0.1884 0.1687 -0.0662 -0.0184 0.0177  344  LYS B N   
11682 C CA  . LYS B 346  ? 0.2029 0.1730 0.1551 -0.0711 -0.0206 0.0181  344  LYS B CA  
11683 C C   . LYS B 346  ? 0.2265 0.1816 0.1691 -0.0740 -0.0239 0.0189  344  LYS B C   
11684 O O   . LYS B 346  ? 0.2422 0.1942 0.1826 -0.0797 -0.0256 0.0201  344  LYS B O   
11685 C CB  . LYS B 346  ? 0.2174 0.1901 0.1743 -0.0677 -0.0218 0.0151  344  LYS B CB  
11686 C CG  . LYS B 346  ? 0.2089 0.1960 0.1751 -0.0654 -0.0188 0.0146  344  LYS B CG  
11687 C CD  . LYS B 346  ? 0.2189 0.2076 0.1890 -0.0615 -0.0199 0.0116  344  LYS B CD  
11688 C CE  . LYS B 346  ? 0.2115 0.2144 0.1906 -0.0600 -0.0173 0.0116  344  LYS B CE  
11689 N NZ  . LYS B 346  ? 0.2165 0.2212 0.1992 -0.0561 -0.0181 0.0089  344  LYS B NZ  
11690 N N   . ARG B 347  ? 0.2141 0.1596 0.1508 -0.0701 -0.0250 0.0182  345  ARG B N   
11691 C CA  . ARG B 347  ? 0.2472 0.1776 0.1742 -0.0722 -0.0283 0.0188  345  ARG B CA  
11692 C C   . ARG B 347  ? 0.2608 0.1874 0.1821 -0.0776 -0.0277 0.0225  345  ARG B C   
11693 O O   . ARG B 347  ? 0.2690 0.1828 0.1818 -0.0805 -0.0305 0.0236  345  ARG B O   
11694 C CB  . ARG B 347  ? 0.2431 0.1646 0.1664 -0.0653 -0.0302 0.0163  345  ARG B CB  
11695 C CG  . ARG B 347  ? 0.2401 0.1627 0.1675 -0.0607 -0.0313 0.0127  345  ARG B CG  
11696 C CD  . ARG B 347  ? 0.2239 0.1421 0.1502 -0.0533 -0.0322 0.0102  345  ARG B CD  
11697 N NE  . ARG B 347  ? 0.2109 0.1390 0.1429 -0.0497 -0.0293 0.0100  345  ARG B NE  
11698 C CZ  . ARG B 347  ? 0.2339 0.1596 0.1652 -0.0440 -0.0297 0.0084  345  ARG B CZ  
11699 N NH1 . ARG B 347  ? 0.2518 0.1666 0.1778 -0.0408 -0.0327 0.0069  345  ARG B NH1 
11700 N NH2 . ARG B 347  ? 0.2217 0.1560 0.1577 -0.0413 -0.0271 0.0083  345  ARG B NH2 
11701 N N   . CYS B 348  ? 0.2342 0.1714 0.1594 -0.0790 -0.0241 0.0245  346  CYS B N   
11702 C CA  . CYS B 348  ? 0.2515 0.1856 0.1709 -0.0830 -0.0229 0.0280  346  CYS B CA  
11703 C C   . CYS B 348  ? 0.2905 0.2157 0.2032 -0.0906 -0.0251 0.0306  346  CYS B C   
11704 O O   . CYS B 348  ? 0.2935 0.2062 0.1970 -0.0916 -0.0269 0.0321  346  CYS B O   
11705 C CB  . CYS B 348  ? 0.2354 0.1844 0.1614 -0.0841 -0.0184 0.0296  346  CYS B CB  
11706 S SG  . CYS B 348  ? 0.3236 0.2701 0.2426 -0.0872 -0.0161 0.0333  346  CYS B SG  
11707 N N   . PRO B 349  ? 0.2636 0.1936 0.1798 -0.0963 -0.0253 0.0315  347  PRO B N   
11708 C CA  . PRO B 349  ? 0.3058 0.2264 0.2148 -0.1040 -0.0275 0.0342  347  PRO B CA  
11709 C C   . PRO B 349  ? 0.3172 0.2200 0.2172 -0.1026 -0.0320 0.0327  347  PRO B C   
11710 O O   . PRO B 349  ? 0.3151 0.2059 0.2060 -0.1070 -0.0340 0.0351  347  PRO B O   
11711 C CB  . PRO B 349  ? 0.3202 0.2510 0.2363 -0.1095 -0.0270 0.0347  347  PRO B CB  
11712 C CG  . PRO B 349  ? 0.2743 0.2150 0.1992 -0.1035 -0.0261 0.0314  347  PRO B CG  
11713 C CD  . PRO B 349  ? 0.2740 0.2176 0.2004 -0.0962 -0.0239 0.0301  347  PRO B CD  
11714 N N   . PHE B 350  ? 0.2954 0.1960 0.1974 -0.0963 -0.0338 0.0289  348  PHE B N   
11715 C CA  . PHE B 350  ? 0.3040 0.1883 0.1977 -0.0940 -0.0380 0.0271  348  PHE B CA  
11716 C C   . PHE B 350  ? 0.3268 0.2014 0.2136 -0.0894 -0.0387 0.0273  348  PHE B C   
11717 O O   . PHE B 350  ? 0.3350 0.1942 0.2123 -0.0903 -0.0419 0.0279  348  PHE B O   
11718 C CB  . PHE B 350  ? 0.2915 0.1780 0.1901 -0.0889 -0.0391 0.0230  348  PHE B CB  
11719 C CG  . PHE B 350  ? 0.3029 0.2003 0.2088 -0.0929 -0.0383 0.0229  348  PHE B CG  
11720 C CD1 . PHE B 350  ? 0.3531 0.2445 0.2553 -0.0994 -0.0408 0.0237  348  PHE B CD1 
11721 C CD2 . PHE B 350  ? 0.2939 0.2074 0.2101 -0.0906 -0.0350 0.0221  348  PHE B CD2 
11722 C CE1 . PHE B 350  ? 0.3722 0.2739 0.2811 -0.1035 -0.0403 0.0237  348  PHE B CE1 
11723 C CE2 . PHE B 350  ? 0.3009 0.2247 0.2239 -0.0943 -0.0344 0.0222  348  PHE B CE2 
11724 C CZ  . PHE B 350  ? 0.3373 0.2554 0.2567 -0.1008 -0.0371 0.0230  348  PHE B CZ  
11725 N N   . VAL B 351  ? 0.2988 0.1818 0.1900 -0.0846 -0.0359 0.0269  349  VAL B N   
11726 C CA  . VAL B 351  ? 0.2832 0.1584 0.1681 -0.0809 -0.0365 0.0276  349  VAL B CA  
11727 C C   . VAL B 351  ? 0.3243 0.1928 0.2012 -0.0875 -0.0365 0.0318  349  VAL B C   
11728 O O   . VAL B 351  ? 0.3382 0.1928 0.2056 -0.0867 -0.0390 0.0328  349  VAL B O   
11729 C CB  . VAL B 351  ? 0.2706 0.1575 0.1622 -0.0754 -0.0333 0.0264  349  VAL B CB  
11730 C CG1 . VAL B 351  ? 0.3078 0.1874 0.1927 -0.0722 -0.0338 0.0274  349  VAL B CG1 
11731 C CG2 . VAL B 351  ? 0.2766 0.1685 0.1752 -0.0689 -0.0337 0.0223  349  VAL B CG2 
11732 N N   . LEU B 352  ? 0.3150 0.1931 0.1954 -0.0940 -0.0336 0.0346  350  LEU B N   
11733 C CA  . LEU B 352  ? 0.3496 0.2221 0.2227 -0.1009 -0.0332 0.0389  350  LEU B CA  
11734 C C   . LEU B 352  ? 0.3364 0.1933 0.2006 -0.1057 -0.0373 0.0399  350  LEU B C   
11735 O O   . LEU B 352  ? 0.3772 0.2219 0.2315 -0.1081 -0.0388 0.0425  350  LEU B O   
11736 C CB  . LEU B 352  ? 0.3420 0.2296 0.2219 -0.1069 -0.0291 0.0414  350  LEU B CB  
11737 C CG  . LEU B 352  ? 0.3291 0.2302 0.2153 -0.1028 -0.0248 0.0412  350  LEU B CG  
11738 C CD1 . LEU B 352  ? 0.3298 0.2460 0.2231 -0.1085 -0.0208 0.0435  350  LEU B CD1 
11739 C CD2 . LEU B 352  ? 0.3591 0.2526 0.2371 -0.1008 -0.0245 0.0429  350  LEU B CD2 
11740 N N   . ASP B 353  ? 0.3343 0.1908 0.2014 -0.1071 -0.0392 0.0379  351  ASP B N   
11741 C CA  . ASP B 353  ? 0.3709 0.2112 0.2290 -0.1109 -0.0435 0.0383  351  ASP B CA  
11742 C C   . ASP B 353  ? 0.3821 0.2062 0.2311 -0.1048 -0.0468 0.0369  351  ASP B C   
11743 O O   . ASP B 353  ? 0.4014 0.2102 0.2398 -0.1081 -0.0496 0.0389  351  ASP B O   
11744 C CB  . ASP B 353  ? 0.3705 0.2132 0.2334 -0.1116 -0.0451 0.0355  351  ASP B CB  
11745 C CG  . ASP B 353  ? 0.3937 0.2500 0.2641 -0.1190 -0.0429 0.0373  351  ASP B CG  
11746 O OD1 . ASP B 353  ? 0.4294 0.2891 0.2987 -0.1256 -0.0409 0.0412  351  ASP B OD1 
11747 O OD2 . ASP B 353  ? 0.4055 0.2691 0.2827 -0.1181 -0.0431 0.0348  351  ASP B OD2 
11748 N N   . PHE B 354  ? 0.3475 0.1747 0.2006 -0.0959 -0.0467 0.0334  352  PHE B N   
11749 C CA  . PHE B 354  ? 0.3429 0.1565 0.1886 -0.0894 -0.0497 0.0319  352  PHE B CA  
11750 C C   . PHE B 354  ? 0.3675 0.1752 0.2059 -0.0901 -0.0494 0.0352  352  PHE B C   
11751 O O   . PHE B 354  ? 0.3891 0.1807 0.2171 -0.0896 -0.0527 0.0361  352  PHE B O   
11752 C CB  . PHE B 354  ? 0.3573 0.1782 0.2103 -0.0803 -0.0491 0.0278  352  PHE B CB  
11753 C CG  . PHE B 354  ? 0.3469 0.1571 0.1939 -0.0731 -0.0516 0.0265  352  PHE B CG  
11754 C CD1 . PHE B 354  ? 0.4010 0.1973 0.2418 -0.0699 -0.0556 0.0244  352  PHE B CD1 
11755 C CD2 . PHE B 354  ? 0.3838 0.1977 0.2311 -0.0696 -0.0501 0.0274  352  PHE B CD2 
11756 C CE1 . PHE B 354  ? 0.3951 0.1819 0.2307 -0.0630 -0.0581 0.0233  352  PHE B CE1 
11757 C CE2 . PHE B 354  ? 0.3816 0.1860 0.2235 -0.0631 -0.0527 0.0264  352  PHE B CE2 
11758 C CZ  . PHE B 354  ? 0.4164 0.2075 0.2527 -0.0598 -0.0567 0.0243  352  PHE B CZ  
11759 N N   . ILE B 355  ? 0.3643 0.1845 0.2075 -0.0911 -0.0455 0.0370  353  ILE B N   
11760 C CA  . ILE B 355  ? 0.3688 0.1843 0.2052 -0.0911 -0.0449 0.0400  353  ILE B CA  
11761 C C   . ILE B 355  ? 0.3914 0.1966 0.2183 -0.0996 -0.0459 0.0443  353  ILE B C   
11762 O O   . ILE B 355  ? 0.4097 0.2012 0.2261 -0.0993 -0.0481 0.0463  353  ILE B O   
11763 C CB  . ILE B 355  ? 0.3499 0.1816 0.1937 -0.0900 -0.0402 0.0406  353  ILE B CB  
11764 C CG1 . ILE B 355  ? 0.3824 0.2219 0.2339 -0.0812 -0.0397 0.0364  353  ILE B CG1 
11765 C CG2 . ILE B 355  ? 0.3848 0.2121 0.2207 -0.0918 -0.0392 0.0442  353  ILE B CG2 
11766 C CD1 . ILE B 355  ? 0.3558 0.2117 0.2155 -0.0801 -0.0352 0.0365  353  ILE B CD1 
11767 N N   . ILE B 356  ? 0.3699 0.1815 0.2003 -0.1074 -0.0442 0.0460  354  ILE B N   
11768 C CA  . ILE B 356  ? 0.4192 0.2217 0.2411 -0.1164 -0.0451 0.0503  354  ILE B CA  
11769 C C   . ILE B 356  ? 0.4123 0.1943 0.2235 -0.1163 -0.0504 0.0498  354  ILE B C   
11770 O O   . ILE B 356  ? 0.4363 0.2059 0.2372 -0.1191 -0.0521 0.0527  354  ILE B O   
11771 C CB  . ILE B 356  ? 0.3975 0.2121 0.2266 -0.1245 -0.0426 0.0517  354  ILE B CB  
11772 C CG1 . ILE B 356  ? 0.3867 0.2198 0.2242 -0.1255 -0.0372 0.0533  354  ILE B CG1 
11773 C CG2 . ILE B 356  ? 0.4193 0.2240 0.2405 -0.1332 -0.0444 0.0551  354  ILE B CG2 
11774 C CD1 . ILE B 356  ? 0.3975 0.2461 0.2452 -0.1308 -0.0346 0.0535  354  ILE B CD1 
11775 N N   . ASP B 357  ? 0.4229 0.2021 0.2368 -0.1123 -0.0529 0.0458  355  ASP B N   
11776 C CA  . ASP B 357  ? 0.4455 0.2051 0.2493 -0.1112 -0.0579 0.0449  355  ASP B CA  
11777 C C   . ASP B 357  ? 0.4806 0.2286 0.2768 -0.1039 -0.0602 0.0445  355  ASP B C   
11778 O O   . ASP B 357  ? 0.4735 0.2083 0.2603 -0.1035 -0.0631 0.0451  355  ASP B O   
11779 C CB  . ASP B 357  ? 0.4577 0.2180 0.2663 -0.1080 -0.0598 0.0404  355  ASP B CB  
11780 C CG  . ASP B 357  ? 0.4724 0.2156 0.2722 -0.1038 -0.0644 0.0382  355  ASP B CG  
11781 O OD1 . ASP B 357  ? 0.4987 0.2353 0.2930 -0.1081 -0.0662 0.0390  355  ASP B OD1 
11782 O OD2 . ASP B 357  ? 0.4617 0.1993 0.2605 -0.0956 -0.0661 0.0354  355  ASP B OD2 
11783 N N   . LEU B 358  ? 0.4404 0.1981 0.2430 -0.0962 -0.0584 0.0423  356  LEU B N   
11784 C CA  . LEU B 358  ? 0.4385 0.1868 0.2347 -0.0892 -0.0605 0.0420  356  LEU B CA  
11785 C C   . LEU B 358  ? 0.4706 0.2114 0.2572 -0.0938 -0.0603 0.0469  356  LEU B C   
11786 O O   . LEU B 358  ? 0.4758 0.2015 0.2523 -0.0913 -0.0637 0.0477  356  LEU B O   
11787 C CB  . LEU B 358  ? 0.3987 0.1609 0.2044 -0.0813 -0.0582 0.0391  356  LEU B CB  
11788 C CG  . LEU B 358  ? 0.3924 0.1484 0.1931 -0.0742 -0.0599 0.0390  356  LEU B CG  
11789 C CD1 . LEU B 358  ? 0.4553 0.1947 0.2485 -0.0690 -0.0648 0.0371  356  LEU B CD1 
11790 C CD2 . LEU B 358  ? 0.3921 0.1635 0.2033 -0.0677 -0.0572 0.0362  356  LEU B CD2 
11791 N N   . ALA B 359  ? 0.4276 0.1798 0.2177 -0.1001 -0.0562 0.0499  357  ALA B N   
11792 C CA  . ALA B 359  ? 0.4515 0.1983 0.2330 -0.1050 -0.0554 0.0546  357  ALA B CA  
11793 C C   . ALA B 359  ? 0.4885 0.2243 0.2625 -0.1091 -0.0582 0.0554  357  ALA B C   
11794 O O   . ALA B 359  ? 0.4872 0.2124 0.2521 -0.1079 -0.0601 0.0567  357  ALA B O   
11795 C CB  . ALA B 359  ? 0.4673 0.2307 0.2556 -0.1110 -0.0500 0.0572  357  ALA B CB  
11796 N N   . ARG B 360  ? 0.5209 0.2589 0.2983 -0.1138 -0.0585 0.0544  358  ARG B N   
11797 C CA  . ARG B 360  ? 0.5410 0.2682 0.3112 -0.1177 -0.0613 0.0550  358  ARG B CA  
11798 C C   . ARG B 360  ? 0.4892 0.2000 0.2511 -0.1107 -0.0662 0.0526  358  ARG B C   
11799 O O   . ARG B 360  ? 0.5492 0.2486 0.3017 -0.1115 -0.0684 0.0540  358  ARG B O   
11800 C CB  . ARG B 360  ? 0.5338 0.2669 0.3099 -0.1228 -0.0612 0.0538  358  ARG B CB  
11801 C CG  . ARG B 360  ? 0.5482 0.2964 0.3312 -0.1309 -0.0569 0.0565  358  ARG B CG  
11802 C CD  . ARG B 360  ? 0.6522 0.4032 0.4389 -0.1358 -0.0579 0.0553  358  ARG B CD  
11803 N NE  . ARG B 360  ? 0.6731 0.4422 0.4715 -0.1396 -0.0541 0.0556  358  ARG B NE  
11804 C CZ  . ARG B 360  ? 0.6445 0.4252 0.4469 -0.1464 -0.0507 0.0587  358  ARG B CZ  
11805 N NH1 . ARG B 360  ? 0.7319 0.5079 0.5276 -0.1506 -0.0504 0.0619  358  ARG B NH1 
11806 N NH2 . ARG B 360  ? 0.6581 0.4557 0.4716 -0.1488 -0.0474 0.0586  358  ARG B NH2 
11807 N N   . ARG B 361  ? 0.5219 0.2319 0.2875 -0.1038 -0.0677 0.0488  359  ARG B N   
11808 C CA  . ARG B 361  ? 0.5632 0.2594 0.3224 -0.0961 -0.0721 0.0460  359  ARG B CA  
11809 C C   . ARG B 361  ? 0.5782 0.2670 0.3302 -0.0917 -0.0733 0.0474  359  ARG B C   
11810 O O   . ARG B 361  ? 0.5168 0.1925 0.2603 -0.0889 -0.0768 0.0470  359  ARG B O   
11811 C CB  . ARG B 361  ? 0.5797 0.2794 0.3458 -0.0890 -0.0726 0.0418  359  ARG B CB  
11812 C CG  . ARG B 361  ? 0.6562 0.3592 0.4274 -0.0909 -0.0728 0.0392  359  ARG B CG  
11813 C CD  . ARG B 361  ? 0.5601 0.2635 0.3359 -0.0822 -0.0740 0.0348  359  ARG B CD  
11814 N NE  . ARG B 361  ? 0.4714 0.1873 0.2565 -0.0807 -0.0710 0.0343  359  ARG B NE  
11815 C CZ  . ARG B 361  ? 0.4657 0.1847 0.2546 -0.0720 -0.0711 0.0317  359  ARG B CZ  
11816 N NH1 . ARG B 361  ? 0.5121 0.2184 0.2939 -0.0653 -0.0745 0.0307  359  ARG B NH1 
11817 N NH2 . ARG B 361  ? 0.4407 0.1779 0.2416 -0.0695 -0.0675 0.0299  359  ARG B NH2 
11818 N N   . SER B 362  ? 0.5323 0.2294 0.2878 -0.0905 -0.0706 0.0490  360  SER B N   
11819 C CA  . SER B 362  ? 0.5094 0.2009 0.2596 -0.0844 -0.0720 0.0495  360  SER B CA  
11820 C C   . SER B 362  ? 0.5059 0.1952 0.2493 -0.0892 -0.0709 0.0536  360  SER B C   
11821 O O   . SER B 362  ? 0.5184 0.2022 0.2564 -0.0845 -0.0724 0.0542  360  SER B O   
11822 C CB  . SER B 362  ? 0.5299 0.2313 0.2875 -0.0792 -0.0701 0.0485  360  SER B CB  
11823 O OG  . SER B 362  ? 0.4783 0.1926 0.2412 -0.0853 -0.0655 0.0511  360  SER B OG  
11824 N N   . GLY B 363  ? 0.5024 0.1963 0.2461 -0.0982 -0.0683 0.0564  361  GLY B N   
11825 C CA  . GLY B 363  ? 0.5173 0.2100 0.2548 -0.1026 -0.0669 0.0603  361  GLY B CA  
11826 C C   . GLY B 363  ? 0.5031 0.2052 0.2434 -0.1010 -0.0636 0.0619  361  GLY B C   
11827 O O   . GLY B 363  ? 0.5456 0.2438 0.2793 -0.1008 -0.0635 0.0642  361  GLY B O   
11828 N N   . ARG B 364  ? 0.4891 0.2035 0.2388 -0.0996 -0.0609 0.0607  362  ARG B N   
11829 C CA  . ARG B 364  ? 0.5323 0.2573 0.2854 -0.0982 -0.0574 0.0620  362  ARG B CA  
11830 C C   . ARG B 364  ? 0.5092 0.2495 0.2703 -0.1053 -0.0523 0.0636  362  ARG B C   
11831 O O   . ARG B 364  ? 0.5296 0.2754 0.2979 -0.1073 -0.0518 0.0620  362  ARG B O   
11832 C CB  . ARG B 364  ? 0.4882 0.2153 0.2458 -0.0897 -0.0586 0.0590  362  ARG B CB  
11833 C CG  . ARG B 364  ? 0.5250 0.2393 0.2766 -0.0815 -0.0635 0.0569  362  ARG B CG  
11834 C CD  . ARG B 364  ? 0.5104 0.2209 0.2546 -0.0793 -0.0639 0.0590  362  ARG B CD  
11835 N NE  . ARG B 364  ? 0.5249 0.2234 0.2637 -0.0717 -0.0689 0.0569  362  ARG B NE  
11836 C CZ  . ARG B 364  ? 0.4625 0.1617 0.2046 -0.0633 -0.0709 0.0541  362  ARG B CZ  
11837 N NH1 . ARG B 364  ? 0.4705 0.1821 0.2210 -0.0611 -0.0684 0.0529  362  ARG B NH1 
11838 N NH2 . ARG B 364  ? 0.5032 0.1919 0.2409 -0.0566 -0.0755 0.0520  362  ARG B NH2 
11839 N N   . ARG B 365  ? 0.4651 0.2127 0.2253 -0.1090 -0.0485 0.0667  363  ARG B N   
11840 C CA  . ARG B 365  ? 0.4572 0.2217 0.2264 -0.1139 -0.0432 0.0678  363  ARG B CA  
11841 C C   . ARG B 365  ? 0.4317 0.2063 0.2076 -0.1076 -0.0414 0.0657  363  ARG B C   
11842 O O   . ARG B 365  ? 0.4726 0.2465 0.2450 -0.1029 -0.0412 0.0658  363  ARG B O   
11843 C CB  . ARG B 365  ? 0.4583 0.2284 0.2250 -0.1200 -0.0395 0.0715  363  ARG B CB  
11844 C CG  . ARG B 365  ? 0.4855 0.2734 0.2621 -0.1258 -0.0342 0.0725  363  ARG B CG  
11845 C CD  . ARG B 365  ? 0.5118 0.3047 0.2860 -0.1322 -0.0307 0.0761  363  ARG B CD  
11846 N NE  . ARG B 365  ? 0.5101 0.3201 0.2946 -0.1377 -0.0260 0.0768  363  ARG B NE  
11847 C CZ  . ARG B 365  ? 0.5038 0.3274 0.2920 -0.1396 -0.0207 0.0786  363  ARG B CZ  
11848 N NH1 . ARG B 365  ? 0.4982 0.3201 0.2803 -0.1370 -0.0192 0.0800  363  ARG B NH1 
11849 N NH2 . ARG B 365  ? 0.4715 0.3108 0.2699 -0.1439 -0.0169 0.0789  363  ARG B NH2 
11850 N N   . ILE B 366  ? 0.4187 0.2051 0.2065 -0.1058 -0.0402 0.0622  364  ILE B N   
11851 C CA  . ILE B 366  ? 0.4043 0.2033 0.2018 -0.0981 -0.0385 0.0582  364  ILE B CA  
11852 C C   . ILE B 366  ? 0.4181 0.2351 0.2236 -0.1010 -0.0327 0.0592  364  ILE B C   
11853 O O   . ILE B 366  ? 0.4121 0.2365 0.2220 -0.1077 -0.0302 0.0607  364  ILE B O   
11854 C CB  . ILE B 366  ? 0.3852 0.1860 0.1907 -0.0938 -0.0406 0.0537  364  ILE B CB  
11855 C CG1 . ILE B 366  ? 0.4090 0.1916 0.2061 -0.0903 -0.0463 0.0527  364  ILE B CG1 
11856 C CG2 . ILE B 366  ? 0.3729 0.1875 0.1889 -0.0864 -0.0387 0.0498  364  ILE B CG2 
11857 C CD1 . ILE B 366  ? 0.4259 0.2084 0.2291 -0.0866 -0.0486 0.0484  364  ILE B CD1 
11858 N N   . MET B 367  ? 0.3961 0.2200 0.2032 -0.0961 -0.0306 0.0583  365  MET B N   
11859 C CA  . MET B 367  ? 0.3712 0.2125 0.1862 -0.0975 -0.0251 0.0585  365  MET B CA  
11860 C C   . MET B 367  ? 0.4082 0.2618 0.2362 -0.0933 -0.0241 0.0542  365  MET B C   
11861 O O   . MET B 367  ? 0.3758 0.2278 0.2064 -0.0861 -0.0265 0.0506  365  MET B O   
11862 C CB  . MET B 367  ? 0.3823 0.2253 0.1932 -0.0936 -0.0234 0.0590  365  MET B CB  
11863 C CG  . MET B 367  ? 0.4113 0.2404 0.2082 -0.0966 -0.0250 0.0631  365  MET B CG  
11864 S SD  . MET B 367  ? 0.4412 0.2705 0.2313 -0.0923 -0.0236 0.0639  365  MET B SD  
11865 C CE  . MET B 367  ? 0.5378 0.3783 0.3274 -0.1000 -0.0169 0.0680  365  MET B CE  
11866 N N   . VAL B 368  ? 0.3614 0.2270 0.1975 -0.0981 -0.0209 0.0547  366  VAL B N   
11867 C CA  . VAL B 368  ? 0.3227 0.1997 0.1709 -0.0948 -0.0201 0.0509  366  VAL B CA  
11868 C C   . VAL B 368  ? 0.3237 0.2178 0.1799 -0.0945 -0.0148 0.0508  366  VAL B C   
11869 O O   . VAL B 368  ? 0.3434 0.2452 0.2013 -0.1008 -0.0114 0.0537  366  VAL B O   
11870 C CB  . VAL B 368  ? 0.3386 0.2147 0.1900 -0.0998 -0.0216 0.0510  366  VAL B CB  
11871 C CG1 . VAL B 368  ? 0.3410 0.2290 0.2044 -0.0961 -0.0207 0.0472  366  VAL B CG1 
11872 C CG2 . VAL B 368  ? 0.3771 0.2351 0.2197 -0.0995 -0.0269 0.0508  366  VAL B CG2 
11873 N N   . ARG B 369  ? 0.3010 0.2013 0.1623 -0.0873 -0.0141 0.0475  367  ARG B N   
11874 C CA  . ARG B 369  ? 0.2903 0.2064 0.1595 -0.0861 -0.0092 0.0469  367  ARG B CA  
11875 C C   . ARG B 369  ? 0.2951 0.2218 0.1759 -0.0854 -0.0085 0.0444  367  ARG B C   
11876 O O   . ARG B 369  ? 0.2902 0.2156 0.1749 -0.0801 -0.0109 0.0409  367  ARG B O   
11877 C CB  . ARG B 369  ? 0.3080 0.2251 0.1764 -0.0790 -0.0088 0.0447  367  ARG B CB  
11878 C CG  . ARG B 369  ? 0.2987 0.2311 0.1741 -0.0778 -0.0038 0.0441  367  ARG B CG  
11879 C CD  . ARG B 369  ? 0.3077 0.2422 0.1848 -0.0703 -0.0039 0.0408  367  ARG B CD  
11880 N NE  . ARG B 369  ? 0.3151 0.2403 0.1820 -0.0687 -0.0051 0.0420  367  ARG B NE  
11881 C CZ  . ARG B 369  ? 0.3173 0.2386 0.1824 -0.0624 -0.0073 0.0394  367  ARG B CZ  
11882 N NH1 . ARG B 369  ? 0.3107 0.2360 0.1836 -0.0571 -0.0085 0.0356  367  ARG B NH1 
11883 N NH2 . ARG B 369  ? 0.3181 0.2312 0.1734 -0.0615 -0.0085 0.0409  367  ARG B NH2 
11884 N N   . LEU B 370  ? 0.2753 0.2127 0.1614 -0.0908 -0.0052 0.0462  368  LEU B N   
11885 C CA  . LEU B 370  ? 0.2771 0.2259 0.1744 -0.0902 -0.0042 0.0441  368  LEU B CA  
11886 C C   . LEU B 370  ? 0.2556 0.2180 0.1602 -0.0856 -0.0002 0.0424  368  LEU B C   
11887 O O   . LEU B 370  ? 0.2802 0.2499 0.1845 -0.0876 0.0038  0.0444  368  LEU B O   
11888 C CB  . LEU B 370  ? 0.2768 0.2306 0.1767 -0.0983 -0.0031 0.0469  368  LEU B CB  
11889 C CG  . LEU B 370  ? 0.2618 0.2265 0.1727 -0.0983 -0.0027 0.0449  368  LEU B CG  
11890 C CD1 . LEU B 370  ? 0.3081 0.2644 0.2193 -0.0953 -0.0073 0.0419  368  LEU B CD1 
11891 C CD2 . LEU B 370  ? 0.2596 0.2309 0.1731 -0.1067 -0.0011 0.0482  368  LEU B CD2 
11892 N N   . VAL B 371  ? 0.2416 0.2068 0.1522 -0.0794 -0.0013 0.0386  369  VAL B N   
11893 C CA  . VAL B 371  ? 0.2485 0.2257 0.1663 -0.0747 0.0020  0.0365  369  VAL B CA  
11894 C C   . VAL B 371  ? 0.2441 0.2302 0.1722 -0.0739 0.0021  0.0345  369  VAL B C   
11895 O O   . VAL B 371  ? 0.2529 0.2345 0.1818 -0.0758 -0.0009 0.0341  369  VAL B O   
11896 C CB  . VAL B 371  ? 0.2282 0.2004 0.1433 -0.0675 0.0007  0.0338  369  VAL B CB  
11897 C CG1 . VAL B 371  ? 0.2396 0.2016 0.1439 -0.0682 -0.0001 0.0357  369  VAL B CG1 
11898 C CG2 . VAL B 371  ? 0.2379 0.2041 0.1552 -0.0635 -0.0034 0.0307  369  VAL B CG2 
11899 N N   . LYS B 372  ? 0.2104 0.2086 0.1459 -0.0705 0.0053  0.0331  370  LYS B N   
11900 C CA  . LYS B 372  ? 0.2001 0.2060 0.1449 -0.0687 0.0051  0.0309  370  LYS B CA  
11901 C C   . LYS B 372  ? 0.1944 0.1948 0.1401 -0.0623 0.0022  0.0272  370  LYS B C   
11902 O O   . LYS B 372  ? 0.2296 0.2259 0.1768 -0.0624 -0.0008 0.0259  370  LYS B O   
11903 C CB  . LYS B 372  ? 0.2191 0.2402 0.1717 -0.0682 0.0096  0.0311  370  LYS B CB  
11904 C CG  . LYS B 372  ? 0.2206 0.2477 0.1738 -0.0754 0.0117  0.0348  370  LYS B CG  
11905 C CD  . LYS B 372  ? 0.2258 0.2689 0.1872 -0.0753 0.0162  0.0353  370  LYS B CD  
11906 C CE  . LYS B 372  ? 0.2476 0.2957 0.2080 -0.0825 0.0186  0.0392  370  LYS B CE  
11907 N NZ  . LYS B 372  ? 0.2385 0.3029 0.2070 -0.0820 0.0233  0.0398  370  LYS B NZ  
11908 N N   . GLY B 373  ? 0.1981 0.1982 0.1426 -0.0571 0.0031  0.0255  371  GLY B N   
11909 C CA  . GLY B 373  ? 0.1937 0.1875 0.1380 -0.0515 0.0001  0.0224  371  GLY B CA  
11910 C C   . GLY B 373  ? 0.1992 0.1989 0.1473 -0.0459 0.0020  0.0200  371  GLY B C   
11911 O O   . GLY B 373  ? 0.2066 0.2172 0.1608 -0.0455 0.0053  0.0199  371  GLY B O   
11912 N N   . ALA B 374  ? 0.1819 0.1749 0.1266 -0.0414 0.0000  0.0181  372  ALA B N   
11913 C CA  . ALA B 374  ? 0.1760 0.1731 0.1224 -0.0367 0.0017  0.0162  372  ALA B CA  
11914 C C   . ALA B 374  ? 0.1906 0.1899 0.1431 -0.0319 0.0006  0.0129  372  ALA B C   
11915 O O   . ALA B 374  ? 0.2027 0.2053 0.1569 -0.0281 0.0019  0.0112  372  ALA B O   
11916 C CB  . ALA B 374  ? 0.1833 0.1722 0.1213 -0.0351 0.0005  0.0164  372  ALA B CB  
11917 N N   . TYR B 375  ? 0.1696 0.1670 0.1253 -0.0322 -0.0018 0.0120  373  TYR B N   
11918 C CA  . TYR B 375  ? 0.1577 0.1554 0.1180 -0.0277 -0.0033 0.0090  373  TYR B CA  
11919 C C   . TYR B 375  ? 0.1863 0.1918 0.1545 -0.0280 -0.0023 0.0082  373  TYR B C   
11920 O O   . TYR B 375  ? 0.1707 0.1750 0.1421 -0.0256 -0.0041 0.0062  373  TYR B O   
11921 C CB  . TYR B 375  ? 0.1954 0.1830 0.1519 -0.0264 -0.0073 0.0080  373  TYR B CB  
11922 C CG  . TYR B 375  ? 0.1980 0.1774 0.1466 -0.0258 -0.0089 0.0087  373  TYR B CG  
11923 C CD1 . TYR B 375  ? 0.2001 0.1743 0.1419 -0.0299 -0.0091 0.0115  373  TYR B CD1 
11924 C CD2 . TYR B 375  ? 0.2257 0.2025 0.1733 -0.0213 -0.0103 0.0067  373  TYR B CD2 
11925 C CE1 . TYR B 375  ? 0.2313 0.1977 0.1654 -0.0293 -0.0106 0.0123  373  TYR B CE1 
11926 C CE2 . TYR B 375  ? 0.2618 0.2313 0.2021 -0.0207 -0.0120 0.0074  373  TYR B CE2 
11927 C CZ  . TYR B 375  ? 0.2442 0.2082 0.1775 -0.0245 -0.0122 0.0102  373  TYR B CZ  
11928 O OH  . TYR B 375  ? 0.2985 0.2548 0.2239 -0.0238 -0.0140 0.0111  373  TYR B OH  
11929 N N   . TRP B 376  ? 0.1655 0.1791 0.1369 -0.0307 0.0006  0.0099  374  TRP B N   
11930 C CA  . TRP B 376  ? 0.1531 0.1733 0.1312 -0.0319 0.0009  0.0097  374  TRP B CA  
11931 C C   . TRP B 376  ? 0.1645 0.1882 0.1484 -0.0273 0.0009  0.0070  374  TRP B C   
11932 O O   . TRP B 376  ? 0.1530 0.1754 0.1394 -0.0269 -0.0011 0.0059  374  TRP B O   
11933 C CB  . TRP B 376  ? 0.1772 0.2068 0.1583 -0.0351 0.0042  0.0119  374  TRP B CB  
11934 C CG  . TRP B 376  ? 0.1578 0.1942 0.1455 -0.0365 0.0043  0.0119  374  TRP B CG  
11935 C CD1 . TRP B 376  ? 0.1550 0.1894 0.1427 -0.0405 0.0022  0.0129  374  TRP B CD1 
11936 C CD2 . TRP B 376  ? 0.1763 0.2221 0.1713 -0.0337 0.0061  0.0109  374  TRP B CD2 
11937 N NE1 . TRP B 376  ? 0.1639 0.2064 0.1587 -0.0405 0.0027  0.0125  374  TRP B NE1 
11938 C CE2 . TRP B 376  ? 0.1807 0.2302 0.1800 -0.0363 0.0051  0.0113  374  TRP B CE2 
11939 C CE3 . TRP B 376  ? 0.2184 0.2694 0.2164 -0.0294 0.0085  0.0096  374  TRP B CE3 
11940 C CZ2 . TRP B 376  ? 0.1839 0.2422 0.1903 -0.0345 0.0062  0.0107  374  TRP B CZ2 
11941 C CZ3 . TRP B 376  ? 0.2254 0.2848 0.2305 -0.0275 0.0097  0.0089  374  TRP B CZ3 
11942 C CH2 . TRP B 376  ? 0.2049 0.2680 0.2142 -0.0300 0.0085  0.0095  374  TRP B CH2 
11943 N N   . ASP B 377  ? 0.1718 0.1997 0.1575 -0.0239 0.0029  0.0060  375  ASP B N   
11944 C CA  . ASP B 377  ? 0.1745 0.2061 0.1658 -0.0200 0.0030  0.0037  375  ASP B CA  
11945 C C   . ASP B 377  ? 0.1468 0.1713 0.1370 -0.0175 0.0000  0.0016  375  ASP B C   
11946 O O   . ASP B 377  ? 0.1638 0.1899 0.1583 -0.0159 -0.0007 0.0002  375  ASP B O   
11947 C CB  . ASP B 377  ? 0.2260 0.2631 0.2193 -0.0169 0.0058  0.0029  375  ASP B CB  
11948 C CG  . ASP B 377  ? 0.2942 0.3264 0.2817 -0.0154 0.0060  0.0026  375  ASP B CG  
11949 O OD1 . ASP B 377  ? 0.3558 0.3799 0.3385 -0.0153 0.0034  0.0022  375  ASP B OD1 
11950 O OD2 . ASP B 377  ? 0.3437 0.3802 0.3312 -0.0140 0.0087  0.0026  375  ASP B OD2 
11951 N N   . ALA B 378  ? 0.1625 0.1791 0.1468 -0.0172 -0.0018 0.0016  376  ALA B N   
11952 C CA  . ALA B 378  ? 0.1418 0.1520 0.1251 -0.0148 -0.0047 -0.0003 376  ALA B CA  
11953 C C   . ALA B 378  ? 0.1685 0.1757 0.1522 -0.0167 -0.0068 -0.0002 376  ALA B C   
11954 O O   . ALA B 378  ? 0.1714 0.1769 0.1572 -0.0144 -0.0084 -0.0020 376  ALA B O   
11955 C CB  . ALA B 378  ? 0.1808 0.1836 0.1576 -0.0139 -0.0063 -0.0003 376  ALA B CB  
11956 N N   . GLU B 379  ? 0.1590 0.1650 0.1401 -0.0210 -0.0068 0.0019  377  GLU B N   
11957 C CA  . GLU B 379  ? 0.1490 0.1517 0.1299 -0.0230 -0.0089 0.0020  377  GLU B CA  
11958 C C   . GLU B 379  ? 0.1504 0.1601 0.1379 -0.0226 -0.0080 0.0011  377  GLU B C   
11959 O O   . GLU B 379  ? 0.1588 0.1659 0.1472 -0.0218 -0.0098 -0.0002 377  GLU B O   
11960 C CB  . GLU B 379  ? 0.1634 0.1633 0.1401 -0.0282 -0.0092 0.0046  377  GLU B CB  
11961 C CG  . GLU B 379  ? 0.1994 0.1912 0.1685 -0.0290 -0.0103 0.0058  377  GLU B CG  
11962 C CD  . GLU B 379  ? 0.2099 0.1915 0.1745 -0.0266 -0.0137 0.0043  377  GLU B CD  
11963 O OE1 . GLU B 379  ? 0.2074 0.1879 0.1746 -0.0245 -0.0152 0.0024  377  GLU B OE1 
11964 O OE2 . GLU B 379  ? 0.2066 0.1815 0.1650 -0.0267 -0.0148 0.0053  377  GLU B OE2 
11965 N N   . ILE B 380  ? 0.1363 0.1549 0.1284 -0.0229 -0.0053 0.0018  378  ILE B N   
11966 C CA  . ILE B 380  ? 0.1298 0.1550 0.1280 -0.0221 -0.0047 0.0010  378  ILE B CA  
11967 C C   . ILE B 380  ? 0.1450 0.1690 0.1455 -0.0176 -0.0054 -0.0015 378  ILE B C   
11968 O O   . ILE B 380  ? 0.1376 0.1613 0.1401 -0.0170 -0.0066 -0.0026 378  ILE B O   
11969 C CB  . ILE B 380  ? 0.1371 0.1720 0.1397 -0.0226 -0.0016 0.0022  378  ILE B CB  
11970 C CG1 . ILE B 380  ? 0.1537 0.1906 0.1544 -0.0273 -0.0007 0.0049  378  ILE B CG1 
11971 C CG2 . ILE B 380  ? 0.1578 0.1992 0.1666 -0.0214 -0.0012 0.0015  378  ILE B CG2 
11972 C CD1 . ILE B 380  ? 0.1609 0.1964 0.1612 -0.0316 -0.0026 0.0059  378  ILE B CD1 
11973 N N   . LYS B 381  ? 0.1339 0.1574 0.1339 -0.0146 -0.0046 -0.0024 379  LYS B N   
11974 C CA  . LYS B 381  ? 0.1339 0.1566 0.1361 -0.0107 -0.0052 -0.0047 379  LYS B CA  
11975 C C   . LYS B 381  ? 0.1512 0.1672 0.1512 -0.0100 -0.0079 -0.0059 379  LYS B C   
11976 O O   . LYS B 381  ? 0.1508 0.1677 0.1539 -0.0083 -0.0084 -0.0073 379  LYS B O   
11977 C CB  . LYS B 381  ? 0.1326 0.1549 0.1338 -0.0080 -0.0044 -0.0054 379  LYS B CB  
11978 C CG  . LYS B 381  ? 0.1485 0.1702 0.1523 -0.0044 -0.0050 -0.0077 379  LYS B CG  
11979 C CD  . LYS B 381  ? 0.1287 0.1505 0.1316 -0.0022 -0.0042 -0.0084 379  LYS B CD  
11980 C CE  . LYS B 381  ? 0.1621 0.1843 0.1682 0.0009  -0.0047 -0.0105 379  LYS B CE  
11981 N NZ  . LYS B 381  ? 0.1406 0.1621 0.1454 0.0028  -0.0043 -0.0114 379  LYS B NZ  
11982 N N   . ARG B 382  ? 0.1364 0.1455 0.1310 -0.0112 -0.0096 -0.0053 380  ARG B N   
11983 C CA  . ARG B 382  ? 0.1670 0.1693 0.1592 -0.0098 -0.0122 -0.0067 380  ARG B CA  
11984 C C   . ARG B 382  ? 0.1503 0.1522 0.1435 -0.0113 -0.0131 -0.0069 380  ARG B C   
11985 O O   . ARG B 382  ? 0.1506 0.1509 0.1451 -0.0090 -0.0142 -0.0087 380  ARG B O   
11986 C CB  . ARG B 382  ? 0.1832 0.1777 0.1688 -0.0109 -0.0140 -0.0057 380  ARG B CB  
11987 C CG  . ARG B 382  ? 0.2676 0.2549 0.2506 -0.0086 -0.0168 -0.0072 380  ARG B CG  
11988 C CD  . ARG B 382  ? 0.3743 0.3626 0.3595 -0.0044 -0.0170 -0.0090 380  ARG B CD  
11989 N NE  . ARG B 382  ? 0.4297 0.4203 0.4193 -0.0019 -0.0172 -0.0111 380  ARG B NE  
11990 C CZ  . ARG B 382  ? 0.4355 0.4290 0.4287 0.0013  -0.0170 -0.0127 380  ARG B CZ  
11991 N NH1 . ARG B 382  ? 0.4429 0.4375 0.4359 0.0023  -0.0166 -0.0126 380  ARG B NH1 
11992 N NH2 . ARG B 382  ? 0.3768 0.3722 0.3737 0.0032  -0.0171 -0.0143 380  ARG B NH2 
11993 N N   . ALA B 383  ? 0.1454 0.1489 0.1380 -0.0152 -0.0127 -0.0052 381  ALA B N   
11994 C CA  . ALA B 383  ? 0.1390 0.1418 0.1321 -0.0169 -0.0138 -0.0054 381  ALA B CA  
11995 C C   . ALA B 383  ? 0.1465 0.1557 0.1453 -0.0149 -0.0127 -0.0067 381  ALA B C   
11996 O O   . ALA B 383  ? 0.1431 0.1502 0.1420 -0.0140 -0.0139 -0.0080 381  ALA B O   
11997 C CB  . ALA B 383  ? 0.1514 0.1556 0.1432 -0.0219 -0.0136 -0.0031 381  ALA B CB  
11998 N N   . GLN B 384  ? 0.1382 0.1546 0.1413 -0.0139 -0.0104 -0.0063 382  GLN B N   
11999 C CA  . GLN B 384  ? 0.1201 0.1421 0.1283 -0.0118 -0.0094 -0.0073 382  GLN B CA  
12000 C C   . GLN B 384  ? 0.1386 0.1578 0.1473 -0.0080 -0.0100 -0.0095 382  GLN B C   
12001 O O   . GLN B 384  ? 0.1556 0.1755 0.1661 -0.0070 -0.0104 -0.0106 382  GLN B O   
12002 C CB  . GLN B 384  ? 0.1348 0.1643 0.1469 -0.0113 -0.0069 -0.0064 382  GLN B CB  
12003 C CG  . GLN B 384  ? 0.1251 0.1598 0.1384 -0.0147 -0.0060 -0.0043 382  GLN B CG  
12004 C CD  . GLN B 384  ? 0.1220 0.1644 0.1396 -0.0135 -0.0035 -0.0037 382  GLN B CD  
12005 O OE1 . GLN B 384  ? 0.1630 0.2056 0.1812 -0.0105 -0.0024 -0.0046 382  GLN B OE1 
12006 N NE2 . GLN B 384  ? 0.1180 0.1668 0.1384 -0.0157 -0.0026 -0.0021 382  GLN B NE2 
12007 N N   . LEU B 385  ? 0.1279 0.1444 0.1352 -0.0061 -0.0102 -0.0101 383  LEU B N   
12008 C CA  . LEU B 385  ? 0.1176 0.1321 0.1258 -0.0027 -0.0109 -0.0121 383  LEU B CA  
12009 C C   . LEU B 385  ? 0.1406 0.1500 0.1465 -0.0023 -0.0128 -0.0132 383  LEU B C   
12010 O O   . LEU B 385  ? 0.1632 0.1733 0.1714 0.0000  -0.0129 -0.0147 383  LEU B O   
12011 C CB  . LEU B 385  ? 0.1440 0.1559 0.1504 -0.0011 -0.0112 -0.0124 383  LEU B CB  
12012 C CG  . LEU B 385  ? 0.1835 0.2000 0.1921 -0.0004 -0.0093 -0.0120 383  LEU B CG  
12013 C CD1 . LEU B 385  ? 0.1939 0.2067 0.1994 0.0008  -0.0102 -0.0123 383  LEU B CD1 
12014 C CD2 . LEU B 385  ? 0.2288 0.2497 0.2422 0.0018  -0.0082 -0.0132 383  LEU B CD2 
12015 N N   . ASP B 386  ? 0.1516 0.1555 0.1528 -0.0044 -0.0143 -0.0124 384  ASP B N   
12016 C CA  . ASP B 386  ? 0.1477 0.1453 0.1457 -0.0037 -0.0164 -0.0136 384  ASP B CA  
12017 C C   . ASP B 386  ? 0.1752 0.1733 0.1733 -0.0055 -0.0166 -0.0137 384  ASP B C   
12018 O O   . ASP B 386  ? 0.1783 0.1710 0.1734 -0.0048 -0.0182 -0.0149 384  ASP B O   
12019 C CB  . ASP B 386  ? 0.1818 0.1718 0.1739 -0.0049 -0.0183 -0.0127 384  ASP B CB  
12020 C CG  . ASP B 386  ? 0.2357 0.2237 0.2268 -0.0024 -0.0188 -0.0131 384  ASP B CG  
12021 O OD1 . ASP B 386  ? 0.2319 0.2242 0.2271 0.0004  -0.0178 -0.0142 384  ASP B OD1 
12022 O OD2 . ASP B 386  ? 0.2626 0.2446 0.2487 -0.0033 -0.0202 -0.0122 384  ASP B OD2 
12023 N N   . GLY B 387  ? 0.1480 0.1523 0.1492 -0.0075 -0.0152 -0.0126 385  GLY B N   
12024 C CA  . GLY B 387  ? 0.1609 0.1663 0.1625 -0.0091 -0.0155 -0.0128 385  GLY B CA  
12025 C C   . GLY B 387  ? 0.1718 0.1711 0.1683 -0.0123 -0.0176 -0.0122 385  GLY B C   
12026 O O   . GLY B 387  ? 0.1976 0.1939 0.1922 -0.0125 -0.0188 -0.0133 385  GLY B O   
12027 N N   . LEU B 388  ? 0.1600 0.1568 0.1536 -0.0149 -0.0180 -0.0105 386  LEU B N   
12028 C CA  . LEU B 388  ? 0.1787 0.1681 0.1667 -0.0181 -0.0202 -0.0100 386  LEU B CA  
12029 C C   . LEU B 388  ? 0.2135 0.2068 0.2024 -0.0227 -0.0202 -0.0084 386  LEU B C   
12030 O O   . LEU B 388  ? 0.1854 0.1873 0.1794 -0.0232 -0.0184 -0.0075 386  LEU B O   
12031 C CB  . LEU B 388  ? 0.1832 0.1669 0.1669 -0.0188 -0.0209 -0.0089 386  LEU B CB  
12032 C CG  . LEU B 388  ? 0.2045 0.1842 0.1871 -0.0142 -0.0214 -0.0105 386  LEU B CG  
12033 C CD1 . LEU B 388  ? 0.2525 0.2260 0.2301 -0.0149 -0.0225 -0.0092 386  LEU B CD1 
12034 C CD2 . LEU B 388  ? 0.2269 0.2012 0.2075 -0.0114 -0.0230 -0.0128 386  LEU B CD2 
12035 N N   . ALA B 389  ? 0.2037 0.1903 0.1875 -0.0259 -0.0224 -0.0081 387  ALA B N   
12036 C CA  . ALA B 389  ? 0.2356 0.2251 0.2200 -0.0302 -0.0230 -0.0071 387  ALA B CA  
12037 C C   . ALA B 389  ? 0.2276 0.2249 0.2155 -0.0337 -0.0214 -0.0045 387  ALA B C   
12038 O O   . ALA B 389  ? 0.2466 0.2514 0.2386 -0.0357 -0.0209 -0.0037 387  ALA B O   
12039 C CB  . ALA B 389  ? 0.2628 0.2422 0.2402 -0.0333 -0.0259 -0.0073 387  ALA B CB  
12040 N N   . ASP B 390  ? 0.2014 0.1974 0.1878 -0.0344 -0.0207 -0.0031 388  ASP B N   
12041 C CA  . ASP B 390  ? 0.2000 0.2029 0.1891 -0.0378 -0.0190 -0.0005 388  ASP B CA  
12042 C C   . ASP B 390  ? 0.1721 0.1727 0.1592 -0.0362 -0.0178 0.0002  388  ASP B C   
12043 O O   . ASP B 390  ? 0.1889 0.1828 0.1729 -0.0329 -0.0187 -0.0013 388  ASP B O   
12044 C CB  . ASP B 390  ? 0.2018 0.2029 0.1881 -0.0440 -0.0205 0.0013  388  ASP B CB  
12045 C CG  . ASP B 390  ? 0.2383 0.2504 0.2301 -0.0474 -0.0187 0.0036  388  ASP B CG  
12046 O OD1 . ASP B 390  ? 0.2079 0.2260 0.2026 -0.0464 -0.0162 0.0048  388  ASP B OD1 
12047 O OD2 . ASP B 390  ? 0.2551 0.2698 0.2480 -0.0511 -0.0200 0.0042  388  ASP B OD2 
12048 N N   . PHE B 391  ? 0.1728 0.1792 0.1617 -0.0386 -0.0159 0.0023  389  PHE B N   
12049 C CA  . PHE B 391  ? 0.1655 0.1698 0.1518 -0.0379 -0.0148 0.0033  389  PHE B CA  
12050 C C   . PHE B 391  ? 0.1534 0.1484 0.1324 -0.0417 -0.0167 0.0048  389  PHE B C   
12051 O O   . PHE B 391  ? 0.1833 0.1762 0.1605 -0.0462 -0.0181 0.0058  389  PHE B O   
12052 C CB  . PHE B 391  ? 0.1804 0.1949 0.1713 -0.0388 -0.0117 0.0050  389  PHE B CB  
12053 C CG  . PHE B 391  ? 0.1412 0.1641 0.1388 -0.0351 -0.0100 0.0037  389  PHE B CG  
12054 C CD1 . PHE B 391  ? 0.1473 0.1696 0.1458 -0.0301 -0.0093 0.0019  389  PHE B CD1 
12055 C CD2 . PHE B 391  ? 0.1509 0.1819 0.1537 -0.0366 -0.0094 0.0042  389  PHE B CD2 
12056 C CE1 . PHE B 391  ? 0.1345 0.1635 0.1386 -0.0268 -0.0079 0.0008  389  PHE B CE1 
12057 C CE2 . PHE B 391  ? 0.1552 0.1931 0.1636 -0.0330 -0.0081 0.0031  389  PHE B CE2 
12058 C CZ  . PHE B 391  ? 0.1311 0.1677 0.1400 -0.0282 -0.0072 0.0014  389  PHE B CZ  
12059 N N   . PRO B 392  ? 0.1682 0.1572 0.1428 -0.0401 -0.0168 0.0049  390  PRO B N   
12060 C CA  . PRO B 392  ? 0.1627 0.1428 0.1300 -0.0437 -0.0184 0.0067  390  PRO B CA  
12061 C C   . PRO B 392  ? 0.1852 0.1699 0.1521 -0.0477 -0.0162 0.0097  390  PRO B C   
12062 O O   . PRO B 392  ? 0.1933 0.1710 0.1539 -0.0510 -0.0171 0.0115  390  PRO B O   
12063 C CB  . PRO B 392  ? 0.1978 0.1699 0.1608 -0.0391 -0.0197 0.0053  390  PRO B CB  
12064 C CG  . PRO B 392  ? 0.1965 0.1767 0.1650 -0.0347 -0.0173 0.0042  390  PRO B CG  
12065 C CD  . PRO B 392  ? 0.1719 0.1614 0.1477 -0.0346 -0.0160 0.0033  390  PRO B CD  
12066 N N   . VAL B 393  ? 0.1742 0.1704 0.1476 -0.0472 -0.0133 0.0101  391  VAL B N   
12067 C CA  . VAL B 393  ? 0.1650 0.1679 0.1394 -0.0506 -0.0106 0.0127  391  VAL B CA  
12068 C C   . VAL B 393  ? 0.1585 0.1726 0.1400 -0.0529 -0.0091 0.0134  391  VAL B C   
12069 O O   . VAL B 393  ? 0.1671 0.1846 0.1532 -0.0507 -0.0097 0.0116  391  VAL B O   
12070 C CB  . VAL B 393  ? 0.1581 0.1643 0.1331 -0.0467 -0.0081 0.0125  391  VAL B CB  
12071 C CG1 . VAL B 393  ? 0.1843 0.1796 0.1520 -0.0447 -0.0098 0.0120  391  VAL B CG1 
12072 C CG2 . VAL B 393  ? 0.1619 0.1749 0.1435 -0.0416 -0.0069 0.0101  391  VAL B CG2 
12073 N N   . PHE B 394  ? 0.1642 0.1845 0.1468 -0.0573 -0.0071 0.0161  392  PHE B N   
12074 C CA  . PHE B 394  ? 0.1619 0.1945 0.1520 -0.0591 -0.0054 0.0169  392  PHE B CA  
12075 C C   . PHE B 394  ? 0.1607 0.2022 0.1569 -0.0537 -0.0027 0.0155  392  PHE B C   
12076 O O   . PHE B 394  ? 0.1839 0.2229 0.1782 -0.0496 -0.0016 0.0145  392  PHE B O   
12077 C CB  . PHE B 394  ? 0.1638 0.2011 0.1536 -0.0651 -0.0037 0.0202  392  PHE B CB  
12078 C CG  . PHE B 394  ? 0.1890 0.2173 0.1728 -0.0709 -0.0065 0.0217  392  PHE B CG  
12079 C CD1 . PHE B 394  ? 0.1851 0.2116 0.1699 -0.0734 -0.0094 0.0210  392  PHE B CD1 
12080 C CD2 . PHE B 394  ? 0.1976 0.2180 0.1739 -0.0737 -0.0066 0.0236  392  PHE B CD2 
12081 C CE1 . PHE B 394  ? 0.2052 0.2223 0.1838 -0.0786 -0.0122 0.0221  392  PHE B CE1 
12082 C CE2 . PHE B 394  ? 0.2021 0.2128 0.1723 -0.0790 -0.0095 0.0249  392  PHE B CE2 
12083 C CZ  . PHE B 394  ? 0.2065 0.2155 0.1778 -0.0814 -0.0123 0.0241  392  PHE B CZ  
12084 N N   . THR B 395  ? 0.1743 0.2257 0.1776 -0.0536 -0.0018 0.0155  393  THR B N   
12085 C CA  . THR B 395  ? 0.1576 0.2174 0.1668 -0.0486 0.0006  0.0143  393  THR B CA  
12086 C C   . THR B 395  ? 0.1684 0.2406 0.1829 -0.0499 0.0039  0.0162  393  THR B C   
12087 O O   . THR B 395  ? 0.1784 0.2570 0.1969 -0.0456 0.0062  0.0154  393  THR B O   
12088 C CB  . THR B 395  ? 0.1667 0.2284 0.1802 -0.0459 -0.0010 0.0123  393  THR B CB  
12089 O OG1 . THR B 395  ? 0.1614 0.2277 0.1779 -0.0501 -0.0023 0.0135  393  THR B OG1 
12090 C CG2 . THR B 395  ? 0.1618 0.2126 0.1709 -0.0433 -0.0037 0.0100  393  THR B CG2 
12091 N N   . ARG B 396  ? 0.1605 0.2363 0.1752 -0.0558 0.0041  0.0188  394  ARG B N   
12092 C CA  . ARG B 396  ? 0.1738 0.2613 0.1930 -0.0574 0.0075  0.0209  394  ARG B CA  
12093 C C   . ARG B 396  ? 0.1971 0.2810 0.2104 -0.0605 0.0091  0.0229  394  ARG B C   
12094 O O   . ARG B 396  ? 0.1984 0.2737 0.2059 -0.0649 0.0070  0.0240  394  ARG B O   
12095 C CB  . ARG B 396  ? 0.1689 0.2653 0.1937 -0.0620 0.0069  0.0226  394  ARG B CB  
12096 C CG  . ARG B 396  ? 0.1797 0.2802 0.2101 -0.0592 0.0053  0.0209  394  ARG B CG  
12097 C CD  . ARG B 396  ? 0.2055 0.3171 0.2423 -0.0635 0.0051  0.0228  394  ARG B CD  
12098 N NE  . ARG B 396  ? 0.2292 0.3436 0.2704 -0.0612 0.0030  0.0213  394  ARG B NE  
12099 C CZ  . ARG B 396  ? 0.2471 0.3736 0.2960 -0.0596 0.0041  0.0217  394  ARG B CZ  
12100 N NH1 . ARG B 396  ? 0.3194 0.4573 0.3732 -0.0599 0.0074  0.0235  394  ARG B NH1 
12101 N NH2 . ARG B 396  ? 0.2319 0.3593 0.2837 -0.0574 0.0019  0.0203  394  ARG B NH2 
12102 N N   . LYS B 397  ? 0.2105 0.3008 0.2251 -0.0582 0.0129  0.0235  395  LYS B N   
12103 C CA  . LYS B 397  ? 0.2019 0.2887 0.2104 -0.0606 0.0147  0.0253  395  LYS B CA  
12104 C C   . LYS B 397  ? 0.1668 0.2560 0.1746 -0.0683 0.0147  0.0285  395  LYS B C   
12105 O O   . LYS B 397  ? 0.2002 0.2808 0.2006 -0.0719 0.0140  0.0300  395  LYS B O   
12106 C CB  . LYS B 397  ? 0.2051 0.2996 0.2156 -0.0565 0.0190  0.0251  395  LYS B CB  
12107 C CG  . LYS B 397  ? 0.2312 0.3197 0.2340 -0.0570 0.0206  0.0260  395  LYS B CG  
12108 C CD  . LYS B 397  ? 0.2618 0.3574 0.2646 -0.0624 0.0235  0.0294  395  LYS B CD  
12109 C CE  . LYS B 397  ? 0.2686 0.3582 0.2632 -0.0627 0.0252  0.0304  395  LYS B CE  
12110 N NZ  . LYS B 397  ? 0.2481 0.3449 0.2426 -0.0684 0.0283  0.0339  395  LYS B NZ  
12111 N N   . ILE B 398  ? 0.1749 0.2754 0.1901 -0.0711 0.0153  0.0298  396  ILE B N   
12112 C CA  . ILE B 398  ? 0.2134 0.3166 0.2283 -0.0790 0.0151  0.0330  396  ILE B CA  
12113 C C   . ILE B 398  ? 0.1924 0.2829 0.2012 -0.0834 0.0106  0.0331  396  ILE B C   
12114 O O   . ILE B 398  ? 0.2052 0.2928 0.2103 -0.0900 0.0101  0.0357  396  ILE B O   
12115 C CB  . ILE B 398  ? 0.2783 0.3970 0.3030 -0.0813 0.0163  0.0343  396  ILE B CB  
12116 C CG1 . ILE B 398  ? 0.2387 0.3585 0.2683 -0.0789 0.0133  0.0321  396  ILE B CG1 
12117 C CG2 . ILE B 398  ? 0.3609 0.4925 0.3908 -0.0780 0.0213  0.0348  396  ILE B CG2 
12118 C CD1 . ILE B 398  ? 0.3727 0.5078 0.4120 -0.0810 0.0140  0.0334  396  ILE B CD1 
12119 N N   . HIS B 399  ? 0.2161 0.2987 0.2238 -0.0799 0.0073  0.0303  397  HIS B N   
12120 C CA  . HIS B 399  ? 0.2182 0.2878 0.2194 -0.0834 0.0032  0.0301  397  HIS B CA  
12121 C C   . HIS B 399  ? 0.2033 0.2606 0.1949 -0.0839 0.0029  0.0308  397  HIS B C   
12122 O O   . HIS B 399  ? 0.2112 0.2602 0.1968 -0.0894 0.0008  0.0325  397  HIS B O   
12123 C CB  . HIS B 399  ? 0.1750 0.2395 0.1770 -0.0789 0.0002  0.0269  397  HIS B CB  
12124 C CG  . HIS B 399  ? 0.1752 0.2500 0.1854 -0.0792 -0.0004 0.0264  397  HIS B CG  
12125 N ND1 . HIS B 399  ? 0.1945 0.2679 0.2070 -0.0747 -0.0022 0.0237  397  HIS B ND1 
12126 C CD2 . HIS B 399  ? 0.2297 0.3162 0.2462 -0.0834 0.0005  0.0285  397  HIS B CD2 
12127 C CE1 . HIS B 399  ? 0.2121 0.2956 0.2316 -0.0760 -0.0025 0.0241  397  HIS B CE1 
12128 N NE2 . HIS B 399  ? 0.2332 0.3250 0.2555 -0.0812 -0.0009 0.0269  397  HIS B NE2 
12129 N N   . THR B 400  ? 0.1933 0.2489 0.1830 -0.0783 0.0047  0.0295  398  THR B N   
12130 C CA  . THR B 400  ? 0.2064 0.2514 0.1871 -0.0785 0.0046  0.0303  398  THR B CA  
12131 C C   . THR B 400  ? 0.1853 0.2334 0.1636 -0.0847 0.0069  0.0340  398  THR B C   
12132 O O   . THR B 400  ? 0.2099 0.2477 0.1801 -0.0885 0.0054  0.0357  398  THR B O   
12133 C CB  . THR B 400  ? 0.1988 0.2435 0.1790 -0.0714 0.0063  0.0282  398  THR B CB  
12134 O OG1 . THR B 400  ? 0.1813 0.2212 0.1627 -0.0663 0.0038  0.0249  398  THR B OG1 
12135 C CG2 . THR B 400  ? 0.1926 0.2276 0.1637 -0.0716 0.0064  0.0292  398  THR B CG2 
12136 N N   . ASP B 401  ? 0.2112 0.2735 0.1962 -0.0858 0.0106  0.0354  399  ASP B N   
12137 C CA  . ASP B 401  ? 0.1989 0.2657 0.1822 -0.0918 0.0133  0.0390  399  ASP B CA  
12138 C C   . ASP B 401  ? 0.1962 0.2590 0.1775 -0.0999 0.0106  0.0413  399  ASP B C   
12139 O O   . ASP B 401  ? 0.2334 0.2901 0.2080 -0.1052 0.0106  0.0441  399  ASP B O   
12140 C CB  . ASP B 401  ? 0.2299 0.3140 0.2220 -0.0910 0.0178  0.0399  399  ASP B CB  
12141 C CG  . ASP B 401  ? 0.2890 0.3762 0.2813 -0.0839 0.0210  0.0381  399  ASP B CG  
12142 O OD1 . ASP B 401  ? 0.2475 0.3241 0.2319 -0.0814 0.0205  0.0374  399  ASP B OD1 
12143 O OD2 . ASP B 401  ? 0.2582 0.3580 0.2583 -0.0807 0.0238  0.0374  399  ASP B OD2 
12144 N N   . VAL B 402  ? 0.2370 0.3027 0.2238 -0.1011 0.0080  0.0403  400  VAL B N   
12145 C CA  . VAL B 402  ? 0.2393 0.3006 0.2239 -0.1088 0.0050  0.0422  400  VAL B CA  
12146 C C   . VAL B 402  ? 0.2319 0.2746 0.2058 -0.1096 0.0012  0.0417  400  VAL B C   
12147 O O   . VAL B 402  ? 0.2475 0.2831 0.2152 -0.1162 0.0001  0.0444  400  VAL B O   
12148 C CB  . VAL B 402  ? 0.2480 0.3164 0.2405 -0.1093 0.0029  0.0408  400  VAL B CB  
12149 C CG1 . VAL B 402  ? 0.2688 0.3305 0.2581 -0.1170 -0.0009 0.0423  400  VAL B CG1 
12150 C CG2 . VAL B 402  ? 0.2814 0.3685 0.2843 -0.1090 0.0066  0.0418  400  VAL B CG2 
12151 N N   . SER B 403  ? 0.2197 0.2542 0.1913 -0.1030 -0.0008 0.0384  401  SER B N   
12152 C CA  . SER B 403  ? 0.2471 0.2641 0.2087 -0.1024 -0.0042 0.0377  401  SER B CA  
12153 C C   . SER B 403  ? 0.2282 0.2386 0.1817 -0.1048 -0.0029 0.0403  401  SER B C   
12154 O O   . SER B 403  ? 0.2528 0.2512 0.1982 -0.1093 -0.0054 0.0419  401  SER B O   
12155 C CB  . SER B 403  ? 0.2065 0.2189 0.1683 -0.0940 -0.0055 0.0338  401  SER B CB  
12156 O OG  . SER B 403  ? 0.2536 0.2502 0.2064 -0.0927 -0.0087 0.0330  401  SER B OG  
12157 N N   . TYR B 404  ? 0.2539 0.2718 0.2091 -0.1019 0.0011  0.0408  402  TYR B N   
12158 C CA  . TYR B 404  ? 0.2523 0.2646 0.1995 -0.1038 0.0027  0.0433  402  TYR B CA  
12159 C C   . TYR B 404  ? 0.2787 0.2914 0.2233 -0.1130 0.0033  0.0474  402  TYR B C   
12160 O O   . TYR B 404  ? 0.2711 0.2716 0.2062 -0.1166 0.0016  0.0494  402  TYR B O   
12161 C CB  . TYR B 404  ? 0.2314 0.2537 0.1818 -0.0992 0.0073  0.0430  402  TYR B CB  
12162 C CG  . TYR B 404  ? 0.2420 0.2575 0.1835 -0.0990 0.0088  0.0447  402  TYR B CG  
12163 C CD1 . TYR B 404  ? 0.2633 0.2809 0.2013 -0.1053 0.0113  0.0486  402  TYR B CD1 
12164 C CD2 . TYR B 404  ? 0.2524 0.2601 0.1894 -0.0924 0.0077  0.0424  402  TYR B CD2 
12165 C CE1 . TYR B 404  ? 0.2804 0.2916 0.2097 -0.1050 0.0126  0.0502  402  TYR B CE1 
12166 C CE2 . TYR B 404  ? 0.2537 0.2552 0.1823 -0.0921 0.0088  0.0439  402  TYR B CE2 
12167 C CZ  . TYR B 404  ? 0.2769 0.2800 0.2014 -0.0983 0.0113  0.0478  402  TYR B CZ  
12168 O OH  . TYR B 404  ? 0.3000 0.2968 0.2156 -0.0982 0.0125  0.0495  402  TYR B OH  
12169 N N   . ILE B 405  ? 0.2637 0.2905 0.2167 -0.1170 0.0054  0.0488  403  ILE B N   
12170 C CA  . ILE B 405  ? 0.2794 0.3086 0.2310 -0.1261 0.0063  0.0529  403  ILE B CA  
12171 C C   . ILE B 405  ? 0.2818 0.2979 0.2277 -0.1316 0.0013  0.0534  403  ILE B C   
12172 O O   . ILE B 405  ? 0.2967 0.3044 0.2349 -0.1379 0.0006  0.0565  403  ILE B O   
12173 C CB  . ILE B 405  ? 0.2712 0.3199 0.2342 -0.1285 0.0097  0.0540  403  ILE B CB  
12174 C CG1 . ILE B 405  ? 0.3328 0.3929 0.2997 -0.1232 0.0148  0.0537  403  ILE B CG1 
12175 C CG2 . ILE B 405  ? 0.2739 0.3262 0.2365 -0.1384 0.0104  0.0582  403  ILE B CG2 
12176 C CD1 . ILE B 405  ? 0.3954 0.4752 0.3743 -0.1236 0.0183  0.0541  403  ILE B CD1 
12177 N N   . ALA B 406  ? 0.2665 0.2798 0.2153 -0.1290 -0.0022 0.0504  404  ALA B N   
12178 C CA  . ALA B 406  ? 0.2995 0.2993 0.2423 -0.1332 -0.0071 0.0503  404  ALA B CA  
12179 C C   . ALA B 406  ? 0.2849 0.2661 0.2155 -0.1319 -0.0096 0.0504  404  ALA B C   
12180 O O   . ALA B 406  ? 0.3164 0.2860 0.2392 -0.1380 -0.0122 0.0525  404  ALA B O   
12181 C CB  . ALA B 406  ? 0.2882 0.2886 0.2361 -0.1293 -0.0100 0.0466  404  ALA B CB  
12182 N N   . CYS B 407  ? 0.2767 0.2545 0.2055 -0.1239 -0.0090 0.0481  405  CYS B N   
12183 C CA  . CYS B 407  ? 0.3347 0.2955 0.2524 -0.1218 -0.0114 0.0480  405  CYS B CA  
12184 C C   . CYS B 407  ? 0.2920 0.2496 0.2025 -0.1265 -0.0094 0.0520  405  CYS B C   
12185 O O   . CYS B 407  ? 0.3335 0.2758 0.2337 -0.1288 -0.0121 0.0535  405  CYS B O   
12186 C CB  . CYS B 407  ? 0.3159 0.2757 0.2346 -0.1121 -0.0114 0.0444  405  CYS B CB  
12187 S SG  . CYS B 407  ? 0.3601 0.3182 0.2838 -0.1069 -0.0148 0.0398  405  CYS B SG  
12188 N N   . ALA B 408  ? 0.2964 0.2680 0.2121 -0.1280 -0.0046 0.0540  406  ALA B N   
12189 C CA  . ALA B 408  ? 0.2978 0.2680 0.2072 -0.1335 -0.0022 0.0582  406  ALA B CA  
12190 C C   . ALA B 408  ? 0.3171 0.2817 0.2226 -0.1434 -0.0041 0.0615  406  ALA B C   
12191 O O   . ALA B 408  ? 0.3599 0.3131 0.2553 -0.1477 -0.0049 0.0644  406  ALA B O   
12192 C CB  . ALA B 408  ? 0.3318 0.3199 0.2487 -0.1332 0.0036  0.0593  406  ALA B CB  
12193 N N   . ALA B 409  ? 0.3468 0.3188 0.2598 -0.1472 -0.0051 0.0611  407  ALA B N   
12194 C CA  . ALA B 409  ? 0.3625 0.3295 0.2724 -0.1550 -0.0075 0.0632  407  ALA B CA  
12195 C C   . ALA B 409  ? 0.3623 0.3078 0.2607 -0.1554 -0.0127 0.0626  407  ALA B C   
12196 O O   . ALA B 409  ? 0.4118 0.3481 0.3026 -0.1595 -0.0142 0.0646  407  ALA B O   
12197 C CB  . ALA B 409  ? 0.3350 0.3139 0.2554 -0.1569 -0.0082 0.0618  407  ALA B CB  
12198 N N   . LYS B 410  ? 0.3194 0.2571 0.2167 -0.1497 -0.0156 0.0593  408  LYS B N   
12199 C CA  . LYS B 410  ? 0.3874 0.3046 0.2739 -0.1486 -0.0206 0.0583  408  LYS B CA  
12200 C C   . LYS B 410  ? 0.4021 0.3079 0.2779 -0.1478 -0.0203 0.0605  408  LYS B C   
12201 O O   . LYS B 410  ? 0.3986 0.2898 0.2646 -0.1512 -0.0232 0.0621  408  LYS B O   
12202 C CB  . LYS B 410  ? 0.3826 0.2973 0.2721 -0.1398 -0.0230 0.0533  408  LYS B CB  
12203 C CG  . LYS B 410  ? 0.4026 0.2974 0.2822 -0.1376 -0.0281 0.0516  408  LYS B CG  
12204 C CD  . LYS B 410  ? 0.4186 0.3130 0.3021 -0.1287 -0.0298 0.0467  408  LYS B CD  
12205 C CE  . LYS B 410  ? 0.4279 0.3323 0.3206 -0.1296 -0.0301 0.0446  408  LYS B CE  
12206 N NZ  . LYS B 410  ? 0.4481 0.3415 0.3359 -0.1347 -0.0344 0.0444  408  LYS B NZ  
12207 N N   . LEU B 411  ? 0.3883 0.3012 0.2661 -0.1422 -0.0168 0.0602  409  LEU B N   
12208 C CA  . LEU B 411  ? 0.3861 0.2882 0.2535 -0.1407 -0.0168 0.0620  409  LEU B CA  
12209 C C   . LEU B 411  ? 0.3854 0.2860 0.2471 -0.1494 -0.0151 0.0669  409  LEU B C   
12210 O O   . LEU B 411  ? 0.4089 0.2950 0.2600 -0.1501 -0.0175 0.0682  409  LEU B O   
12211 C CB  . LEU B 411  ? 0.3607 0.2717 0.2319 -0.1331 -0.0134 0.0603  409  LEU B CB  
12212 C CG  . LEU B 411  ? 0.3728 0.2797 0.2456 -0.1235 -0.0159 0.0556  409  LEU B CG  
12213 C CD1 . LEU B 411  ? 0.3747 0.2945 0.2544 -0.1169 -0.0122 0.0537  409  LEU B CD1 
12214 C CD2 . LEU B 411  ? 0.4130 0.3010 0.2740 -0.1208 -0.0199 0.0556  409  LEU B CD2 
12215 N N   . LEU B 412  ? 0.3951 0.3126 0.2656 -0.1532 -0.0112 0.0681  410  LEU B N   
12216 C CA  . LEU B 412  ? 0.4186 0.3385 0.2866 -0.1587 -0.0093 0.0712  410  LEU B CA  
12217 C C   . LEU B 412  ? 0.4534 0.3625 0.3163 -0.1639 -0.0134 0.0719  410  LEU B C   
12218 O O   . LEU B 412  ? 0.4666 0.3722 0.3241 -0.1682 -0.0129 0.0745  410  LEU B O   
12219 C CB  . LEU B 412  ? 0.4004 0.3418 0.2800 -0.1607 -0.0042 0.0721  410  LEU B CB  
12220 C CG  . LEU B 412  ? 0.4107 0.3620 0.2928 -0.1561 0.0007  0.0722  410  LEU B CG  
12221 C CD1 . LEU B 412  ? 0.4553 0.4284 0.3505 -0.1564 0.0053  0.0720  410  LEU B CD1 
12222 C CD2 . LEU B 412  ? 0.4224 0.3672 0.2951 -0.1567 0.0024  0.0749  410  LEU B CD2 
12223 N N   . ALA B 413  ? 0.4442 0.3475 0.3082 -0.1636 -0.0175 0.0694  411  ALA B N   
12224 C CA  . ALA B 413  ? 0.4681 0.3592 0.3259 -0.1679 -0.0219 0.0697  411  ALA B CA  
12225 C C   . ALA B 413  ? 0.4908 0.3604 0.3356 -0.1650 -0.0260 0.0692  411  ALA B C   
12226 O O   . ALA B 413  ? 0.5169 0.3746 0.3553 -0.1679 -0.0298 0.0692  411  ALA B O   
12227 C CB  . ALA B 413  ? 0.4195 0.3141 0.2839 -0.1687 -0.0244 0.0671  411  ALA B CB  
12228 N N   . ALA B 414  ? 0.4466 0.3112 0.2874 -0.1592 -0.0254 0.0688  412  ALA B N   
12229 C CA  . ALA B 414  ? 0.4578 0.3027 0.2873 -0.1551 -0.0297 0.0679  412  ALA B CA  
12230 C C   . ALA B 414  ? 0.4764 0.3166 0.2986 -0.1530 -0.0280 0.0701  412  ALA B C   
12231 O O   . ALA B 414  ? 0.4734 0.3013 0.2884 -0.1473 -0.0305 0.0691  412  ALA B O   
12232 C CB  . ALA B 414  ? 0.4773 0.3176 0.3085 -0.1487 -0.0322 0.0643  412  ALA B CB  
12233 N N   . THR B 415  ? 0.4799 0.3296 0.3034 -0.1571 -0.0239 0.0731  413  THR B N   
12234 C CA  . THR B 415  ? 0.4545 0.3020 0.2718 -0.1548 -0.0218 0.0751  413  THR B CA  
12235 C C   . THR B 415  ? 0.5064 0.3349 0.3105 -0.1545 -0.0256 0.0762  413  THR B C   
12236 O O   . THR B 415  ? 0.5148 0.3390 0.3127 -0.1515 -0.0247 0.0774  413  THR B O   
12237 C CB  . THR B 415  ? 0.4749 0.3380 0.2973 -0.1593 -0.0162 0.0778  413  THR B CB  
12238 O OG1 . THR B 415  ? 0.5328 0.3964 0.3551 -0.1665 -0.0166 0.0796  413  THR B OG1 
12239 C CG2 . THR B 415  ? 0.4324 0.3145 0.2674 -0.1578 -0.0122 0.0764  413  THR B CG2 
12240 N N   . ASP B 416  ? 0.4748 0.2921 0.2744 -0.1574 -0.0297 0.0758  414  ASP B N   
12241 C CA  . ASP B 416  ? 0.4814 0.2797 0.2684 -0.1560 -0.0338 0.0764  414  ASP B CA  
12242 C C   . ASP B 416  ? 0.5474 0.3354 0.3302 -0.1474 -0.0368 0.0739  414  ASP B C   
12243 O O   . ASP B 416  ? 0.5906 0.3682 0.3645 -0.1441 -0.0382 0.0748  414  ASP B O   
12244 C CB  . ASP B 416  ? 0.5857 0.3743 0.3691 -0.1603 -0.0377 0.0761  414  ASP B CB  
12245 C CG  . ASP B 416  ? 0.6732 0.4653 0.4553 -0.1686 -0.0360 0.0794  414  ASP B CG  
12246 O OD1 . ASP B 416  ? 0.6874 0.4895 0.4715 -0.1709 -0.0316 0.0820  414  ASP B OD1 
12247 O OD2 . ASP B 416  ? 0.7278 0.5128 0.5069 -0.1729 -0.0390 0.0794  414  ASP B OD2 
12248 N N   . VAL B 417  ? 0.4992 0.2904 0.2884 -0.1435 -0.0377 0.0708  415  VAL B N   
12249 C CA  . VAL B 417  ? 0.5196 0.3006 0.3053 -0.1353 -0.0410 0.0681  415  VAL B CA  
12250 C C   . VAL B 417  ? 0.4555 0.2468 0.2475 -0.1303 -0.0382 0.0671  415  VAL B C   
12251 O O   . VAL B 417  ? 0.5431 0.3267 0.3318 -0.1232 -0.0406 0.0653  415  VAL B O   
12252 C CB  . VAL B 417  ? 0.5177 0.2902 0.3036 -0.1336 -0.0454 0.0649  415  VAL B CB  
12253 C CG1 . VAL B 417  ? 0.5502 0.3098 0.3277 -0.1375 -0.0488 0.0658  415  VAL B CG1 
12254 C CG2 . VAL B 417  ? 0.4755 0.2616 0.2727 -0.1363 -0.0435 0.0634  415  VAL B CG2 
12255 N N   . VAL B 418  ? 0.4545 0.2630 0.2554 -0.1334 -0.0332 0.0682  416  VAL B N   
12256 C CA  . VAL B 418  ? 0.4480 0.2672 0.2547 -0.1280 -0.0303 0.0669  416  VAL B CA  
12257 C C   . VAL B 418  ? 0.4361 0.2678 0.2446 -0.1318 -0.0248 0.0701  416  VAL B C   
12258 O O   . VAL B 418  ? 0.4548 0.2928 0.2652 -0.1384 -0.0225 0.0722  416  VAL B O   
12259 C CB  . VAL B 418  ? 0.3914 0.2233 0.2113 -0.1240 -0.0297 0.0624  416  VAL B CB  
12260 C CG1 . VAL B 418  ? 0.4248 0.2452 0.2430 -0.1187 -0.0347 0.0588  416  VAL B CG1 
12261 C CG2 . VAL B 418  ? 0.4258 0.2695 0.2534 -0.1317 -0.0271 0.0637  416  VAL B CG2 
12262 N N   . PHE B 419  ? 0.3912 0.2294 0.2016 -0.1252 -0.0227 0.0686  417  PHE B N   
12263 C CA  . PHE B 419  ? 0.3906 0.2412 0.2029 -0.1272 -0.0173 0.0709  417  PHE B CA  
12264 C C   . PHE B 419  ? 0.3928 0.2620 0.2187 -0.1230 -0.0138 0.0675  417  PHE B C   
12265 O O   . PHE B 419  ? 0.3660 0.2374 0.1950 -0.1148 -0.0143 0.0640  417  PHE B O   
12266 C CB  . PHE B 419  ? 0.3960 0.2387 0.1986 -0.1231 -0.0176 0.0720  417  PHE B CB  
12267 C CG  . PHE B 419  ? 0.4372 0.2921 0.2410 -0.1241 -0.0121 0.0738  417  PHE B CG  
12268 C CD1 . PHE B 419  ? 0.4255 0.2870 0.2293 -0.1317 -0.0083 0.0774  417  PHE B CD1 
12269 C CD2 . PHE B 419  ? 0.4130 0.2736 0.2189 -0.1165 -0.0107 0.0712  417  PHE B CD2 
12270 C CE1 . PHE B 419  ? 0.4407 0.3137 0.2458 -0.1319 -0.0030 0.0787  417  PHE B CE1 
12271 C CE2 . PHE B 419  ? 0.4216 0.2928 0.2279 -0.1171 -0.0056 0.0727  417  PHE B CE2 
12272 C CZ  . PHE B 419  ? 0.4005 0.2773 0.2054 -0.1253 -0.0016 0.0769  417  PHE B CZ  
12273 N N   . PRO B 420  ? 0.3577 0.2406 0.1923 -0.1282 -0.0104 0.0684  418  PRO B N   
12274 C CA  . PRO B 420  ? 0.3445 0.2442 0.1921 -0.1238 -0.0076 0.0650  418  PRO B CA  
12275 C C   . PRO B 420  ? 0.3562 0.2666 0.2057 -0.1203 -0.0030 0.0650  418  PRO B C   
12276 O O   . PRO B 420  ? 0.3428 0.2556 0.1878 -0.1247 0.0003  0.0686  418  PRO B O   
12277 C CB  . PRO B 420  ? 0.3769 0.2867 0.2320 -0.1312 -0.0058 0.0665  418  PRO B CB  
12278 C CG  . PRO B 420  ? 0.3980 0.2935 0.2440 -0.1387 -0.0091 0.0697  418  PRO B CG  
12279 C CD  . PRO B 420  ? 0.3665 0.2492 0.1998 -0.1382 -0.0098 0.0722  418  PRO B CD  
12280 N N   . GLN B 421  ? 0.3629 0.2793 0.2187 -0.1123 -0.0028 0.0610  419  GLN B N   
12281 C CA  . GLN B 421  ? 0.3476 0.2735 0.2053 -0.1080 0.0012  0.0602  419  GLN B CA  
12282 C C   . GLN B 421  ? 0.3513 0.2933 0.2223 -0.1048 0.0039  0.0572  419  GLN B C   
12283 O O   . GLN B 421  ? 0.3105 0.2522 0.1865 -0.0992 0.0014  0.0534  419  GLN B O   
12284 C CB  . GLN B 421  ? 0.3430 0.2588 0.1938 -0.1009 -0.0014 0.0583  419  GLN B CB  
12285 C CG  . GLN B 421  ? 0.3453 0.2437 0.1830 -0.1034 -0.0050 0.0610  419  GLN B CG  
12286 C CD  . GLN B 421  ? 0.3352 0.2229 0.1677 -0.0959 -0.0090 0.0585  419  GLN B CD  
12287 O OE1 . GLN B 421  ? 0.3397 0.2246 0.1764 -0.0913 -0.0123 0.0551  419  GLN B OE1 
12288 N NE2 . GLN B 421  ? 0.3453 0.2273 0.1686 -0.0947 -0.0087 0.0602  419  GLN B NE2 
12289 N N   . PHE B 422  ? 0.3238 0.2798 0.2003 -0.1083 0.0088  0.0589  420  PHE B N   
12290 C CA  . PHE B 422  ? 0.3132 0.2848 0.2025 -0.1063 0.0112  0.0566  420  PHE B CA  
12291 C C   . PHE B 422  ? 0.2741 0.2541 0.1665 -0.0995 0.0145  0.0542  420  PHE B C   
12292 O O   . PHE B 422  ? 0.3055 0.2941 0.1979 -0.1007 0.0191  0.0560  420  PHE B O   
12293 C CB  . PHE B 422  ? 0.3066 0.2891 0.2010 -0.1140 0.0144  0.0597  420  PHE B CB  
12294 C CG  . PHE B 422  ? 0.3448 0.3189 0.2364 -0.1210 0.0109  0.0618  420  PHE B CG  
12295 C CD1 . PHE B 422  ? 0.3512 0.3210 0.2465 -0.1196 0.0068  0.0592  420  PHE B CD1 
12296 C CD2 . PHE B 422  ? 0.3573 0.3271 0.2419 -0.1290 0.0118  0.0663  420  PHE B CD2 
12297 C CE1 . PHE B 422  ? 0.3452 0.3064 0.2372 -0.1259 0.0034  0.0608  420  PHE B CE1 
12298 C CE2 . PHE B 422  ? 0.3496 0.3107 0.2311 -0.1356 0.0083  0.0681  420  PHE B CE2 
12299 C CZ  . PHE B 422  ? 0.3568 0.3135 0.2420 -0.1340 0.0041  0.0653  420  PHE B CZ  
12300 N N   . ALA B 423  ? 0.2779 0.2553 0.1729 -0.0923 0.0120  0.0502  421  ALA B N   
12301 C CA  . ALA B 423  ? 0.2646 0.2483 0.1623 -0.0855 0.0143  0.0476  421  ALA B CA  
12302 C C   . ALA B 423  ? 0.2617 0.2610 0.1715 -0.0838 0.0174  0.0458  421  ALA B C   
12303 O O   . ALA B 423  ? 0.2875 0.2883 0.2041 -0.0817 0.0151  0.0433  421  ALA B O   
12304 C CB  . ALA B 423  ? 0.2807 0.2544 0.1758 -0.0789 0.0101  0.0442  421  ALA B CB  
12305 N N   . THR B 424  ? 0.2879 0.2987 0.2003 -0.0845 0.0225  0.0469  422  THR B N   
12306 C CA  . THR B 424  ? 0.2633 0.2890 0.1870 -0.0822 0.0254  0.0452  422  THR B CA  
12307 C C   . THR B 424  ? 0.2667 0.3027 0.1909 -0.0809 0.0310  0.0459  422  THR B C   
12308 O O   . THR B 424  ? 0.2944 0.3293 0.2119 -0.0848 0.0334  0.0490  422  THR B O   
12309 C CB  . THR B 424  ? 0.2907 0.3236 0.2217 -0.0879 0.0254  0.0468  422  THR B CB  
12310 O OG1 . THR B 424  ? 0.2831 0.3303 0.2251 -0.0849 0.0279  0.0450  422  THR B OG1 
12311 C CG2 . THR B 424  ? 0.2980 0.3337 0.2256 -0.0957 0.0280  0.0514  422  THR B CG2 
12312 N N   . HIS B 425  ? 0.2734 0.3192 0.2052 -0.0754 0.0331  0.0431  423  HIS B N   
12313 C CA  . HIS B 425  ? 0.2620 0.3192 0.1958 -0.0737 0.0386  0.0434  423  HIS B CA  
12314 C C   . HIS B 425  ? 0.2417 0.3145 0.1861 -0.0761 0.0419  0.0444  423  HIS B C   
12315 O O   . HIS B 425  ? 0.2794 0.3634 0.2270 -0.0742 0.0467  0.0445  423  HIS B O   
12316 C CB  . HIS B 425  ? 0.2257 0.2827 0.1599 -0.0656 0.0390  0.0395  423  HIS B CB  
12317 C CG  . HIS B 425  ? 0.2565 0.2995 0.1806 -0.0630 0.0360  0.0385  423  HIS B CG  
12318 N ND1 . HIS B 425  ? 0.2607 0.2972 0.1852 -0.0574 0.0324  0.0350  423  HIS B ND1 
12319 C CD2 . HIS B 425  ? 0.3137 0.3478 0.2270 -0.0654 0.0358  0.0407  423  HIS B CD2 
12320 C CE1 . HIS B 425  ? 0.3174 0.3423 0.2322 -0.0563 0.0301  0.0349  423  HIS B CE1 
12321 N NE2 . HIS B 425  ? 0.2968 0.3198 0.2045 -0.0610 0.0320  0.0384  423  HIS B NE2 
12322 N N   . ASN B 426  ? 0.2672 0.3409 0.2167 -0.0802 0.0393  0.0453  424  ASN B N   
12323 C CA  . ASN B 426  ? 0.2589 0.3472 0.2192 -0.0824 0.0414  0.0460  424  ASN B CA  
12324 C C   . ASN B 426  ? 0.2392 0.3329 0.1985 -0.0905 0.0440  0.0504  424  ASN B C   
12325 O O   . ASN B 426  ? 0.2806 0.3660 0.2352 -0.0966 0.0412  0.0527  424  ASN B O   
12326 C CB  . ASN B 426  ? 0.2411 0.3271 0.2071 -0.0826 0.0369  0.0444  424  ASN B CB  
12327 C CG  . ASN B 426  ? 0.2418 0.3428 0.2194 -0.0841 0.0385  0.0448  424  ASN B CG  
12328 O OD1 . ASN B 426  ? 0.2562 0.3672 0.2368 -0.0892 0.0415  0.0478  424  ASN B OD1 
12329 N ND2 . ASN B 426  ? 0.2766 0.3796 0.2607 -0.0797 0.0363  0.0419  424  ASN B ND2 
12330 N N   . ALA B 427  ? 0.2704 0.3779 0.2338 -0.0904 0.0495  0.0516  425  ALA B N   
12331 C CA  . ALA B 427  ? 0.2929 0.4069 0.2554 -0.0980 0.0527  0.0560  425  ALA B CA  
12332 C C   . ALA B 427  ? 0.2832 0.4028 0.2528 -0.1047 0.0509  0.0580  425  ALA B C   
12333 O O   . ALA B 427  ? 0.2791 0.3954 0.2458 -0.1109 0.0502  0.0607  425  ALA B O   
12334 C CB  . ALA B 427  ? 0.3224 0.4508 0.2888 -0.0953 0.0591  0.0563  425  ALA B CB  
12335 N N   . GLN B 428  ? 0.2863 0.4121 0.2654 -0.1019 0.0490  0.0557  426  GLN B N   
12336 C CA  . GLN B 428  ? 0.2723 0.4016 0.2579 -0.1073 0.0462  0.0568  426  GLN B CA  
12337 C C   . GLN B 428  ? 0.2966 0.4101 0.2745 -0.1125 0.0411  0.0578  426  GLN B C   
12338 O O   . GLN B 428  ? 0.2877 0.3988 0.2646 -0.1191 0.0394  0.0601  426  GLN B O   
12339 C CB  . GLN B 428  ? 0.2836 0.4229 0.2803 -0.1029 0.0454  0.0542  426  GLN B CB  
12340 C CG  . GLN B 428  ? 0.3115 0.4575 0.3167 -0.1068 0.0431  0.0548  426  GLN B CG  
12341 C CD  . GLN B 428  ? 0.3124 0.4471 0.3139 -0.1121 0.0377  0.0553  426  GLN B CD  
12342 O OE1 . GLN B 428  ? 0.3314 0.4546 0.3277 -0.1099 0.0348  0.0535  426  GLN B OE1 
12343 N NE2 . GLN B 428  ? 0.3468 0.4829 0.3507 -0.1180 0.0358  0.0570  426  GLN B NE2 
12344 N N   . THR B 429  ? 0.2878 0.3878 0.2601 -0.1072 0.0376  0.0548  427  THR B N   
12345 C CA  . THR B 429  ? 0.3100 0.3930 0.2739 -0.1102 0.0326  0.0552  427  THR B CA  
12346 C C   . THR B 429  ? 0.2897 0.3652 0.2437 -0.1163 0.0335  0.0589  427  THR B C   
12347 O O   . THR B 429  ? 0.3139 0.3822 0.2640 -0.1233 0.0308  0.0613  427  THR B O   
12348 C CB  . THR B 429  ? 0.2943 0.3657 0.2540 -0.1026 0.0295  0.0514  427  THR B CB  
12349 O OG1 . THR B 429  ? 0.2757 0.3539 0.2444 -0.0972 0.0287  0.0480  427  THR B OG1 
12350 C CG2 . THR B 429  ? 0.3132 0.3675 0.2648 -0.1052 0.0242  0.0515  427  THR B CG2 
12351 N N   . LEU B 430  ? 0.2962 0.3722 0.2451 -0.1136 0.0372  0.0594  428  LEU B N   
12352 C CA  . LEU B 430  ? 0.3116 0.3804 0.2503 -0.1189 0.0384  0.0631  428  LEU B CA  
12353 C C   . LEU B 430  ? 0.3174 0.3935 0.2597 -0.1265 0.0398  0.0663  428  LEU B C   
12354 O O   . LEU B 430  ? 0.3214 0.3871 0.2570 -0.1320 0.0372  0.0686  428  LEU B O   
12355 C CB  . LEU B 430  ? 0.3275 0.3992 0.2620 -0.1142 0.0428  0.0627  428  LEU B CB  
12356 C CG  . LEU B 430  ? 0.3095 0.3726 0.2318 -0.1170 0.0444  0.0657  428  LEU B CG  
12357 C CD1 . LEU B 430  ? 0.3327 0.3988 0.2526 -0.1099 0.0479  0.0637  428  LEU B CD1 
12358 C CD2 . LEU B 430  ? 0.3493 0.4179 0.2726 -0.1233 0.0468  0.0690  428  LEU B CD2 
12359 N N   . ALA B 431  ? 0.2974 0.3902 0.2508 -0.1251 0.0430  0.0657  429  ALA B N   
12360 C CA  . ALA B 431  ? 0.3421 0.4422 0.3000 -0.1304 0.0441  0.0680  429  ALA B CA  
12361 C C   . ALA B 431  ? 0.3198 0.4146 0.2792 -0.1362 0.0391  0.0686  429  ALA B C   
12362 O O   . ALA B 431  ? 0.3552 0.4453 0.3108 -0.1423 0.0380  0.0711  429  ALA B O   
12363 C CB  . ALA B 431  ? 0.3120 0.4309 0.2817 -0.1269 0.0483  0.0669  429  ALA B CB  
12364 N N   . ALA B 432  ? 0.3185 0.4133 0.2828 -0.1342 0.0360  0.0663  430  ALA B N   
12365 C CA  . ALA B 432  ? 0.2759 0.3645 0.2408 -0.1391 0.0310  0.0664  430  ALA B CA  
12366 C C   . ALA B 432  ? 0.3460 0.4160 0.2985 -0.1437 0.0275  0.0682  430  ALA B C   
12367 O O   . ALA B 432  ? 0.3446 0.4104 0.2954 -0.1497 0.0251  0.0698  430  ALA B O   
12368 C CB  . ALA B 432  ? 0.3242 0.4135 0.2944 -0.1355 0.0282  0.0635  430  ALA B CB  
12369 N N   . ILE B 433  ? 0.3863 0.4448 0.3296 -0.1407 0.0272  0.0678  431  ILE B N   
12370 C CA  . ILE B 433  ? 0.3483 0.3880 0.2792 -0.1441 0.0236  0.0693  431  ILE B CA  
12371 C C   . ILE B 433  ? 0.3653 0.4033 0.2903 -0.1480 0.0259  0.0724  431  ILE B C   
12372 O O   . ILE B 433  ? 0.3849 0.4118 0.3032 -0.1532 0.0229  0.0742  431  ILE B O   
12373 C CB  . ILE B 433  ? 0.3511 0.3791 0.2741 -0.1392 0.0222  0.0680  431  ILE B CB  
12374 C CG1 . ILE B 433  ? 0.3698 0.3976 0.2993 -0.1338 0.0188  0.0637  431  ILE B CG1 
12375 C CG2 . ILE B 433  ? 0.4045 0.4128 0.3141 -0.1418 0.0186  0.0696  431  ILE B CG2 
12376 C CD1 . ILE B 433  ? 0.3598 0.3786 0.2854 -0.1249 0.0170  0.0601  431  ILE B CD1 
12377 N N   . TYR B 434  ? 0.3742 0.4230 0.3015 -0.1455 0.0311  0.0730  432  TYR B N   
12378 C CA  . TYR B 434  ? 0.3488 0.3973 0.2711 -0.1491 0.0338  0.0760  432  TYR B CA  
12379 C C   . TYR B 434  ? 0.3731 0.4256 0.2995 -0.1560 0.0328  0.0779  432  TYR B C   
12380 O O   . TYR B 434  ? 0.3822 0.4251 0.3008 -0.1612 0.0315  0.0804  432  TYR B O   
12381 C CB  . TYR B 434  ? 0.3580 0.4199 0.2841 -0.1448 0.0399  0.0758  432  TYR B CB  
12382 C CG  . TYR B 434  ? 0.3849 0.4505 0.3084 -0.1484 0.0436  0.0788  432  TYR B CG  
12383 C CD1 . TYR B 434  ? 0.3562 0.4085 0.2672 -0.1504 0.0431  0.0810  432  TYR B CD1 
12384 C CD2 . TYR B 434  ? 0.3941 0.4762 0.3275 -0.1496 0.0474  0.0794  432  TYR B CD2 
12385 C CE1 . TYR B 434  ? 0.4059 0.4616 0.3145 -0.1539 0.0466  0.0838  432  TYR B CE1 
12386 C CE2 . TYR B 434  ? 0.4194 0.5052 0.3506 -0.1531 0.0509  0.0822  432  TYR B CE2 
12387 C CZ  . TYR B 434  ? 0.4279 0.5005 0.3467 -0.1553 0.0506  0.0844  432  TYR B CZ  
12388 O OH  . TYR B 434  ? 0.4638 0.5400 0.3803 -0.1588 0.0542  0.0873  432  TYR B OH  
12389 N N   . HIS B 435  ? 0.4007 0.4663 0.3388 -0.1563 0.0330  0.0767  433  HIS B N   
12390 C CA  . HIS B 435  ? 0.4202 0.4899 0.3622 -0.1629 0.0318  0.0784  433  HIS B CA  
12391 C C   . HIS B 435  ? 0.3933 0.4496 0.3312 -0.1669 0.0256  0.0781  433  HIS B C   
12392 O O   . HIS B 435  ? 0.4323 0.4841 0.3672 -0.1733 0.0237  0.0802  433  HIS B O   
12393 C CB  . HIS B 435  ? 0.3699 0.4592 0.3258 -0.1614 0.0345  0.0774  433  HIS B CB  
12394 C CG  . HIS B 435  ? 0.3678 0.4701 0.3275 -0.1589 0.0406  0.0783  433  HIS B CG  
12395 N ND1 . HIS B 435  ? 0.3753 0.4831 0.3353 -0.1637 0.0433  0.0812  433  HIS B ND1 
12396 C CD2 . HIS B 435  ? 0.3610 0.4714 0.3238 -0.1521 0.0447  0.0767  433  HIS B CD2 
12397 C CE1 . HIS B 435  ? 0.4053 0.5242 0.3686 -0.1598 0.0488  0.0812  433  HIS B CE1 
12398 N NE2 . HIS B 435  ? 0.3610 0.4815 0.3259 -0.1526 0.0497  0.0785  433  HIS B NE2 
12399 N N   . MET B 436  ? 0.4020 0.4513 0.3390 -0.1632 0.0224  0.0755  434  MET B N   
12400 C CA  . MET B 436  ? 0.3633 0.3983 0.2952 -0.1662 0.0165  0.0749  434  MET B CA  
12401 C C   . MET B 436  ? 0.4564 0.4736 0.3749 -0.1698 0.0142  0.0770  434  MET B C   
12402 O O   . MET B 436  ? 0.4501 0.4576 0.3644 -0.1746 0.0102  0.0777  434  MET B O   
12403 C CB  . MET B 436  ? 0.4067 0.4368 0.3391 -0.1608 0.0140  0.0718  434  MET B CB  
12404 C CG  . MET B 436  ? 0.3910 0.4047 0.3170 -0.1628 0.0080  0.0708  434  MET B CG  
12405 S SD  . MET B 436  ? 0.4436 0.4513 0.3696 -0.1561 0.0057  0.0673  434  MET B SD  
12406 C CE  . MET B 436  ? 0.3855 0.4142 0.3274 -0.1538 0.0078  0.0653  434  MET B CE  
12407 N N   . ALA B 437  ? 0.3902 0.4027 0.3016 -0.1671 0.0167  0.0780  435  ALA B N   
12408 C CA  . ALA B 437  ? 0.4419 0.4367 0.3401 -0.1696 0.0143  0.0799  435  ALA B CA  
12409 C C   . ALA B 437  ? 0.4898 0.4853 0.3859 -0.1764 0.0153  0.0831  435  ALA B C   
12410 O O   . ALA B 437  ? 0.4966 0.4768 0.3826 -0.1799 0.0120  0.0845  435  ALA B O   
12411 C CB  . ALA B 437  ? 0.4685 0.4584 0.3597 -0.1645 0.0166  0.0800  435  ALA B CB  
12412 N N   . GLY B 438  ? 0.4683 0.4810 0.3733 -0.1782 0.0196  0.0842  436  GLY B N   
12413 C CA  . GLY B 438  ? 0.5041 0.5190 0.4080 -0.1850 0.0207  0.0873  436  GLY B CA  
12414 C C   . GLY B 438  ? 0.5653 0.5819 0.4643 -0.1848 0.0253  0.0897  436  GLY B C   
12415 O O   . GLY B 438  ? 0.5413 0.5578 0.4377 -0.1792 0.0278  0.0889  436  GLY B O   
12416 N N   . LYS B 439  ? 0.5902 0.6081 0.4877 -0.1911 0.0264  0.0927  437  LYS B N   
12417 C CA  . LYS B 439  ? 0.5908 0.6114 0.4840 -0.1917 0.0311  0.0953  437  LYS B CA  
12418 C C   . LYS B 439  ? 0.6003 0.6017 0.4787 -0.1923 0.0289  0.0969  437  LYS B C   
12419 O O   . LYS B 439  ? 0.6475 0.6483 0.5206 -0.1901 0.0324  0.0981  437  LYS B O   
12420 C CB  . LYS B 439  ? 0.6252 0.6566 0.5236 -0.1983 0.0337  0.0981  437  LYS B CB  
12421 N N   . ASP B 440  ? 0.5642 0.5494 0.4355 -0.1950 0.0231  0.0967  438  ASP B N   
12422 C CA  . ASP B 440  ? 0.6678 0.6339 0.5249 -0.1954 0.0205  0.0981  438  ASP B CA  
12423 C C   . ASP B 440  ? 0.6130 0.5716 0.4653 -0.1878 0.0196  0.0959  438  ASP B C   
12424 O O   . ASP B 440  ? 0.6203 0.5752 0.4747 -0.1844 0.0164  0.0931  438  ASP B O   
12425 C CB  . ASP B 440  ? 0.7008 0.6521 0.5521 -0.2002 0.0145  0.0984  438  ASP B CB  
12426 C CG  . ASP B 440  ? 0.7829 0.7392 0.6366 -0.2084 0.0150  0.1011  438  ASP B CG  
12427 O OD1 . ASP B 440  ? 0.7573 0.7225 0.6122 -0.2110 0.0197  0.1037  438  ASP B OD1 
12428 O OD2 . ASP B 440  ? 0.8502 0.8014 0.7045 -0.2122 0.0108  0.1005  438  ASP B OD2 
12429 N N   . PHE B 441  ? 0.5570 0.5134 0.4027 -0.1851 0.0226  0.0972  439  PHE B N   
12430 C CA  . PHE B 441  ? 0.5870 0.5362 0.4275 -0.1779 0.0217  0.0952  439  PHE B CA  
12431 C C   . PHE B 441  ? 0.5837 0.5195 0.4108 -0.1773 0.0214  0.0973  439  PHE B C   
12432 O O   . PHE B 441  ? 0.5918 0.5309 0.4162 -0.1806 0.0248  0.1001  439  PHE B O   
12433 C CB  . PHE B 441  ? 0.5209 0.4861 0.3700 -0.1724 0.0265  0.0934  439  PHE B CB  
12434 C CG  . PHE B 441  ? 0.4964 0.4543 0.3402 -0.1651 0.0254  0.0912  439  PHE B CG  
12435 C CD1 . PHE B 441  ? 0.5233 0.4776 0.3700 -0.1616 0.0218  0.0882  439  PHE B CD1 
12436 C CD2 . PHE B 441  ? 0.4927 0.4466 0.3282 -0.1620 0.0276  0.0922  439  PHE B CD2 
12437 C CE1 . PHE B 441  ? 0.4625 0.4099 0.3043 -0.1551 0.0206  0.0863  439  PHE B CE1 
12438 C CE2 . PHE B 441  ? 0.5254 0.4722 0.3558 -0.1554 0.0262  0.0902  439  PHE B CE2 
12439 C CZ  . PHE B 441  ? 0.4946 0.4383 0.3282 -0.1520 0.0226  0.0873  439  PHE B CZ  
12440 N N   . HIS B 442  ? 0.5580 0.4790 0.3770 -0.1728 0.0173  0.0958  440  HIS B N   
12441 C CA  . HIS B 442  ? 0.5821 0.4903 0.3886 -0.1702 0.0165  0.0971  440  HIS B CA  
12442 C C   . HIS B 442  ? 0.5281 0.4314 0.3326 -0.1624 0.0147  0.0942  440  HIS B C   
12443 O O   . HIS B 442  ? 0.5142 0.4164 0.3234 -0.1602 0.0118  0.0916  440  HIS B O   
12444 C CB  . HIS B 442  ? 0.6737 0.5636 0.4697 -0.1741 0.0116  0.0988  440  HIS B CB  
12445 C CG  . HIS B 442  ? 0.7113 0.5905 0.5070 -0.1734 0.0057  0.0966  440  HIS B CG  
12446 N ND1 . HIS B 442  ? 0.6759 0.5430 0.4663 -0.1673 0.0016  0.0943  440  HIS B ND1 
12447 C CD2 . HIS B 442  ? 0.7322 0.6112 0.5325 -0.1780 0.0031  0.0962  440  HIS B CD2 
12448 C CE1 . HIS B 442  ? 0.7037 0.5634 0.4952 -0.1680 -0.0030 0.0926  440  HIS B CE1 
12449 N NE2 . HIS B 442  ? 0.7452 0.6117 0.5424 -0.1745 -0.0022 0.0936  440  HIS B NE2 
12450 N N   . VAL B 443  ? 0.5287 0.4289 0.3261 -0.1582 0.0163  0.0946  441  VAL B N   
12451 C CA  . VAL B 443  ? 0.4726 0.3664 0.2667 -0.1508 0.0139  0.0919  441  VAL B CA  
12452 C C   . VAL B 443  ? 0.5566 0.4324 0.3442 -0.1500 0.0070  0.0911  441  VAL B C   
12453 O O   . VAL B 443  ? 0.5531 0.4162 0.3322 -0.1532 0.0042  0.0931  441  VAL B O   
12454 C CB  . VAL B 443  ? 0.5186 0.4108 0.3049 -0.1468 0.0162  0.0927  441  VAL B CB  
12455 C CG1 . VAL B 443  ? 0.4894 0.3711 0.2699 -0.1396 0.0123  0.0902  441  VAL B CG1 
12456 C CG2 . VAL B 443  ? 0.5177 0.4286 0.3116 -0.1459 0.0230  0.0925  441  VAL B CG2 
12457 N N   . GLY B 444  ? 0.4910 0.3655 0.2824 -0.1456 0.0044  0.0881  442  GLY B N   
12458 C CA  . GLY B 444  ? 0.4864 0.3454 0.2733 -0.1444 -0.0019 0.0868  442  GLY B CA  
12459 C C   . GLY B 444  ? 0.5015 0.3640 0.2967 -0.1476 -0.0035 0.0855  442  GLY B C   
12460 O O   . GLY B 444  ? 0.4676 0.3191 0.2608 -0.1455 -0.0084 0.0836  442  GLY B O   
12461 N N   . LYS B 445  ? 0.4856 0.3633 0.2902 -0.1525 0.0005  0.0863  443  LYS B N   
12462 C CA  . LYS B 445  ? 0.4721 0.3547 0.2855 -0.1552 -0.0010 0.0848  443  LYS B CA  
12463 C C   . LYS B 445  ? 0.4327 0.3227 0.2539 -0.1500 -0.0007 0.0817  443  LYS B C   
12464 O O   . LYS B 445  ? 0.4583 0.3409 0.2800 -0.1482 -0.0048 0.0795  443  LYS B O   
12465 C CB  . LYS B 445  ? 0.5115 0.4086 0.3328 -0.1618 0.0029  0.0866  443  LYS B CB  
12466 C CG  . LYS B 445  ? 0.5439 0.4416 0.3710 -0.1661 0.0000  0.0857  443  LYS B CG  
12467 C CD  . LYS B 445  ? 0.6130 0.5304 0.4541 -0.1670 0.0036  0.0846  443  LYS B CD  
12468 C CE  . LYS B 445  ? 0.6231 0.5528 0.4689 -0.1730 0.0075  0.0873  443  LYS B CE  
12469 N NZ  . LYS B 445  ? 0.6521 0.5987 0.5114 -0.1747 0.0093  0.0861  443  LYS B NZ  
12470 N N   . TYR B 446  ? 0.4284 0.3328 0.2554 -0.1473 0.0043  0.0813  444  TYR B N   
12471 C CA  . TYR B 446  ? 0.3981 0.3099 0.2318 -0.1420 0.0050  0.0785  444  TYR B CA  
12472 C C   . TYR B 446  ? 0.4024 0.3241 0.2365 -0.1384 0.0100  0.0786  444  TYR B C   
12473 O O   . TYR B 446  ? 0.4130 0.3376 0.2439 -0.1405 0.0131  0.0809  444  TYR B O   
12474 C CB  . TYR B 446  ? 0.4203 0.3450 0.2667 -0.1445 0.0059  0.0771  444  TYR B CB  
12475 C CG  . TYR B 446  ? 0.4311 0.3753 0.2871 -0.1472 0.0116  0.0781  444  TYR B CG  
12476 C CD1 . TYR B 446  ? 0.4152 0.3739 0.2785 -0.1430 0.0160  0.0767  444  TYR B CD1 
12477 C CD2 . TYR B 446  ? 0.4393 0.3874 0.2972 -0.1537 0.0126  0.0803  444  TYR B CD2 
12478 C CE1 . TYR B 446  ? 0.4481 0.4244 0.3202 -0.1447 0.0211  0.0774  444  TYR B CE1 
12479 C CE2 . TYR B 446  ? 0.4433 0.4094 0.3103 -0.1557 0.0177  0.0812  444  TYR B CE2 
12480 C CZ  . TYR B 446  ? 0.4380 0.4181 0.3122 -0.1510 0.0219  0.0797  444  TYR B CZ  
12481 O OH  . TYR B 446  ? 0.5104 0.5082 0.3938 -0.1523 0.0269  0.0803  444  TYR B OH  
12482 N N   . GLU B 447  ? 0.3707 0.2980 0.2097 -0.1319 0.0106  0.0755  445  GLU B N   
12483 C CA  . GLU B 447  ? 0.3758 0.3140 0.2168 -0.1276 0.0153  0.0747  445  GLU B CA  
12484 C C   . GLU B 447  ? 0.3493 0.3013 0.2035 -0.1219 0.0167  0.0704  445  GLU B C   
12485 O O   . GLU B 447  ? 0.3421 0.2932 0.2025 -0.1202 0.0135  0.0678  445  GLU B O   
12486 C CB  . GLU B 447  ? 0.3522 0.2789 0.1827 -0.1221 0.0135  0.0741  445  GLU B CB  
12487 C CG  . GLU B 447  ? 0.3455 0.2642 0.1773 -0.1143 0.0085  0.0696  445  GLU B CG  
12488 C CD  . GLU B 447  ? 0.3520 0.2594 0.1736 -0.1090 0.0062  0.0690  445  GLU B CD  
12489 O OE1 . GLU B 447  ? 0.4106 0.3122 0.2219 -0.1119 0.0074  0.0725  445  GLU B OE1 
12490 O OE2 . GLU B 447  ? 0.3568 0.2614 0.1810 -0.1017 0.0031  0.0651  445  GLU B OE2 
12491 N N   . PHE B 448  ? 0.3383 0.3030 0.1965 -0.1189 0.0217  0.0697  446  PHE B N   
12492 C CA  . PHE B 448  ? 0.3134 0.2893 0.1820 -0.1119 0.0230  0.0654  446  PHE B CA  
12493 C C   . PHE B 448  ? 0.3056 0.2745 0.1691 -0.1039 0.0213  0.0624  446  PHE B C   
12494 O O   . PHE B 448  ? 0.3307 0.2886 0.1830 -0.1039 0.0202  0.0640  446  PHE B O   
12495 C CB  . PHE B 448  ? 0.3700 0.3640 0.2461 -0.1130 0.0294  0.0661  446  PHE B CB  
12496 C CG  . PHE B 448  ? 0.3385 0.3421 0.2218 -0.1203 0.0311  0.0686  446  PHE B CG  
12497 C CD1 . PHE B 448  ? 0.3501 0.3607 0.2444 -0.1195 0.0296  0.0663  446  PHE B CD1 
12498 C CD2 . PHE B 448  ? 0.3616 0.3675 0.2408 -0.1282 0.0341  0.0733  446  PHE B CD2 
12499 C CE1 . PHE B 448  ? 0.3478 0.3675 0.2489 -0.1263 0.0308  0.0685  446  PHE B CE1 
12500 C CE2 . PHE B 448  ? 0.3670 0.3821 0.2552 -0.1330 0.0348  0.0743  446  PHE B CE2 
12501 C CZ  . PHE B 448  ? 0.3766 0.3988 0.2749 -0.1329 0.0333  0.0724  446  PHE B CZ  
12502 N N   . GLN B 449  ? 0.3143 0.2893 0.1861 -0.0971 0.0210  0.0581  447  GLN B N   
12503 C CA  . GLN B 449  ? 0.3150 0.2856 0.1836 -0.0895 0.0197  0.0550  447  GLN B CA  
12504 C C   . GLN B 449  ? 0.2767 0.2611 0.1550 -0.0842 0.0230  0.0517  447  GLN B C   
12505 O O   . GLN B 449  ? 0.2749 0.2700 0.1634 -0.0850 0.0246  0.0509  447  GLN B O   
12506 C CB  . GLN B 449  ? 0.2966 0.2545 0.1632 -0.0857 0.0135  0.0525  447  GLN B CB  
12507 C CG  . GLN B 449  ? 0.3465 0.2895 0.2036 -0.0901 0.0096  0.0553  447  GLN B CG  
12508 C CD  . GLN B 449  ? 0.3028 0.2329 0.1556 -0.0848 0.0041  0.0529  447  GLN B CD  
12509 O OE1 . GLN B 449  ? 0.3460 0.2792 0.2048 -0.0786 0.0029  0.0490  447  GLN B OE1 
12510 N NE2 . GLN B 449  ? 0.3221 0.2377 0.1642 -0.0870 0.0007  0.0552  447  GLN B NE2 
12511 N N   . CYS B 450  ? 0.2774 0.2607 0.1520 -0.0786 0.0238  0.0498  448  CYS B N   
12512 C CA  . CYS B 450  ? 0.2672 0.2617 0.1495 -0.0731 0.0267  0.0465  448  CYS B CA  
12513 C C   . CYS B 450  ? 0.2647 0.2521 0.1424 -0.0663 0.0243  0.0435  448  CYS B C   
12514 O O   . CYS B 450  ? 0.2915 0.2668 0.1596 -0.0661 0.0212  0.0442  448  CYS B O   
12515 C CB  . CYS B 450  ? 0.2735 0.2801 0.1569 -0.0750 0.0330  0.0483  448  CYS B CB  
12516 S SG  . CYS B 450  ? 0.3264 0.3275 0.1965 -0.0746 0.0355  0.0501  448  CYS B SG  
12517 N N   . LEU B 451  ? 0.2618 0.2573 0.1462 -0.0609 0.0260  0.0401  449  LEU B N   
12518 C CA  . LEU B 451  ? 0.2891 0.2798 0.1705 -0.0545 0.0241  0.0368  449  LEU B CA  
12519 C C   . LEU B 451  ? 0.3193 0.3124 0.1941 -0.0532 0.0280  0.0373  449  LEU B C   
12520 O O   . LEU B 451  ? 0.3392 0.3430 0.2172 -0.0544 0.0331  0.0382  449  LEU B O   
12521 C CB  . LEU B 451  ? 0.2677 0.2650 0.1594 -0.0495 0.0237  0.0329  449  LEU B CB  
12522 C CG  . LEU B 451  ? 0.3003 0.2935 0.1904 -0.0430 0.0216  0.0292  449  LEU B CG  
12523 C CD1 . LEU B 451  ? 0.3531 0.3333 0.2376 -0.0421 0.0159  0.0288  449  LEU B CD1 
12524 C CD2 . LEU B 451  ? 0.3253 0.3267 0.2261 -0.0390 0.0221  0.0259  449  LEU B CD2 
12525 N N   . HIS B 452  ? 0.2911 0.2742 0.1566 -0.0506 0.0255  0.0367  450  HIS B N   
12526 C CA  . HIS B 452  ? 0.3417 0.3260 0.2004 -0.0484 0.0285  0.0364  450  HIS B CA  
12527 C C   . HIS B 452  ? 0.3307 0.3258 0.1968 -0.0438 0.0319  0.0331  450  HIS B C   
12528 O O   . HIS B 452  ? 0.3450 0.3416 0.2185 -0.0399 0.0298  0.0298  450  HIS B O   
12529 C CB  . HIS B 452  ? 0.3268 0.2988 0.1762 -0.0452 0.0241  0.0352  450  HIS B CB  
12530 C CG  . HIS B 452  ? 0.3577 0.3303 0.2004 -0.0420 0.0265  0.0340  450  HIS B CG  
12531 N ND1 . HIS B 452  ? 0.3555 0.3260 0.1880 -0.0448 0.0293  0.0369  450  HIS B ND1 
12532 C CD2 . HIS B 452  ? 0.3385 0.3136 0.1830 -0.0364 0.0267  0.0302  450  HIS B CD2 
12533 C CE1 . HIS B 452  ? 0.3777 0.3493 0.2058 -0.0408 0.0310  0.0348  450  HIS B CE1 
12534 N NE2 . HIS B 452  ? 0.3399 0.3141 0.1751 -0.0357 0.0295  0.0307  450  HIS B NE2 
12535 N N   . GLY B 453  ? 0.4082 0.4103 0.2719 -0.0440 0.0372  0.0339  451  GLY B N   
12536 C CA  . GLY B 453  ? 0.3691 0.3802 0.2383 -0.0392 0.0405  0.0307  451  GLY B CA  
12537 C C   . GLY B 453  ? 0.4594 0.4815 0.3416 -0.0391 0.0422  0.0298  451  GLY B C   
12538 O O   . GLY B 453  ? 0.4739 0.5011 0.3621 -0.0342 0.0429  0.0265  451  GLY B O   
12539 N N   . MET B 454  ? 0.3803 0.4059 0.2667 -0.0444 0.0425  0.0328  452  MET B N   
12540 C CA  . MET B 454  ? 0.3493 0.3852 0.2479 -0.0449 0.0437  0.0323  452  MET B CA  
12541 C C   . MET B 454  ? 0.3390 0.3809 0.2394 -0.0517 0.0463  0.0364  452  MET B C   
12542 O O   . MET B 454  ? 0.3323 0.3869 0.2399 -0.0525 0.0506  0.0370  452  MET B O   
12543 C CB  . MET B 454  ? 0.3072 0.3377 0.2110 -0.0434 0.0383  0.0302  452  MET B CB  
12544 C CG  . MET B 454  ? 0.3340 0.3733 0.2492 -0.0450 0.0387  0.0303  452  MET B CG  
12545 S SD  . MET B 454  ? 0.4026 0.4562 0.3270 -0.0402 0.0434  0.0279  452  MET B SD  
12546 C CE  . MET B 454  ? 0.4467 0.4930 0.3691 -0.0328 0.0404  0.0232  452  MET B CE  
12547 N N   . GLY B 455  ? 0.2963 0.3290 0.1901 -0.0567 0.0436  0.0393  453  GLY B N   
12548 C CA  . GLY B 455  ? 0.3138 0.3505 0.2090 -0.0639 0.0452  0.0433  453  GLY B CA  
12549 C C   . GLY B 455  ? 0.3727 0.4125 0.2611 -0.0679 0.0498  0.0468  453  GLY B C   
12550 O O   . GLY B 455  ? 0.3616 0.4072 0.2524 -0.0740 0.0520  0.0501  453  GLY B O   
12551 N N   . GLU B 456  ? 0.3723 0.4082 0.2519 -0.0648 0.0514  0.0461  454  GLU B N   
12552 C CA  . GLU B 456  ? 0.3619 0.3997 0.2338 -0.0689 0.0558  0.0497  454  GLU B CA  
12553 C C   . GLU B 456  ? 0.3654 0.4198 0.2447 -0.0707 0.0622  0.0510  454  GLU B C   
12554 O O   . GLU B 456  ? 0.3826 0.4403 0.2596 -0.0771 0.0650  0.0551  454  GLU B O   
12555 C CB  . GLU B 456  ? 0.4262 0.4564 0.2868 -0.0647 0.0561  0.0484  454  GLU B CB  
12556 C CG  . GLU B 456  ? 0.4484 0.4621 0.3002 -0.0640 0.0498  0.0481  454  GLU B CG  
12557 C CD  . GLU B 456  ? 0.4914 0.5012 0.3464 -0.0570 0.0460  0.0433  454  GLU B CD  
12558 O OE1 . GLU B 456  ? 0.4684 0.4869 0.3341 -0.0539 0.0468  0.0406  454  GLU B OE1 
12559 O OE2 . GLU B 456  ? 0.4629 0.4609 0.3094 -0.0546 0.0420  0.0424  454  GLU B OE2 
12560 N N   . PRO B 457  ? 0.3769 0.4423 0.2651 -0.0655 0.0648  0.0479  455  PRO B N   
12561 C CA  . PRO B 457  ? 0.3925 0.4744 0.2884 -0.0673 0.0708  0.0494  455  PRO B CA  
12562 C C   . PRO B 457  ? 0.3965 0.4840 0.2989 -0.0747 0.0707  0.0529  455  PRO B C   
12563 O O   . PRO B 457  ? 0.4080 0.5050 0.3114 -0.0794 0.0753  0.0561  455  PRO B O   
12564 C CB  . PRO B 457  ? 0.3781 0.4679 0.2832 -0.0600 0.0717  0.0450  455  PRO B CB  
12565 C CG  . PRO B 457  ? 0.4240 0.5021 0.3220 -0.0541 0.0685  0.0416  455  PRO B CG  
12566 C CD  . PRO B 457  ? 0.3754 0.4387 0.2660 -0.0576 0.0629  0.0430  455  PRO B CD  
12567 N N   . LEU B 458  ? 0.3459 0.4279 0.2528 -0.0760 0.0654  0.0522  456  LEU B N   
12568 C CA  . LEU B 458  ? 0.3745 0.4607 0.2869 -0.0833 0.0646  0.0554  456  LEU B CA  
12569 C C   . LEU B 458  ? 0.3464 0.4234 0.2487 -0.0907 0.0639  0.0597  456  LEU B C   
12570 O O   . LEU B 458  ? 0.3708 0.4544 0.2755 -0.0965 0.0664  0.0630  456  LEU B O   
12571 C CB  . LEU B 458  ? 0.3024 0.3845 0.2216 -0.0823 0.0591  0.0533  456  LEU B CB  
12572 C CG  . LEU B 458  ? 0.3069 0.3898 0.2303 -0.0900 0.0570  0.0562  456  LEU B CG  
12573 C CD1 . LEU B 458  ? 0.3603 0.4604 0.2923 -0.0942 0.0619  0.0587  456  LEU B CD1 
12574 C CD2 . LEU B 458  ? 0.3152 0.3936 0.2445 -0.0880 0.0516  0.0536  456  LEU B CD2 
12575 N N   . TYR B 459  ? 0.3307 0.3915 0.2225 -0.0896 0.0597  0.0594  457  TYR B N   
12576 C CA  . TYR B 459  ? 0.3461 0.3966 0.2284 -0.0966 0.0581  0.0635  457  TYR B CA  
12577 C C   . TYR B 459  ? 0.3641 0.4155 0.2374 -0.0986 0.0627  0.0663  457  TYR B C   
12578 O O   . TYR B 459  ? 0.3660 0.4106 0.2339 -0.1039 0.0618  0.0695  457  TYR B O   
12579 C CB  . TYR B 459  ? 0.3687 0.4015 0.2439 -0.0947 0.0514  0.0621  457  TYR B CB  
12580 C CG  . TYR B 459  ? 0.3180 0.3498 0.2016 -0.0956 0.0470  0.0608  457  TYR B CG  
12581 C CD1 . TYR B 459  ? 0.3226 0.3514 0.2061 -0.1032 0.0452  0.0641  457  TYR B CD1 
12582 C CD2 . TYR B 459  ? 0.3257 0.3599 0.2172 -0.0891 0.0449  0.0564  457  TYR B CD2 
12583 C CE1 . TYR B 459  ? 0.3050 0.3328 0.1956 -0.1042 0.0414  0.0629  457  TYR B CE1 
12584 C CE2 . TYR B 459  ? 0.3152 0.3488 0.2141 -0.0901 0.0412  0.0553  457  TYR B CE2 
12585 C CZ  . TYR B 459  ? 0.2871 0.3173 0.1852 -0.0976 0.0394  0.0585  457  TYR B CZ  
12586 O OH  . TYR B 459  ? 0.3291 0.3583 0.2338 -0.0986 0.0356  0.0573  457  TYR B OH  
12587 N N   . GLU B 460  ? 0.3575 0.4163 0.2309 -0.0931 0.0671  0.0642  458  GLU B N   
12588 C CA  . GLU B 460  ? 0.3861 0.4491 0.2561 -0.0934 0.0719  0.0659  458  GLU B CA  
12589 C C   . GLU B 460  ? 0.4217 0.4953 0.3007 -0.0985 0.0745  0.0684  458  GLU B C   
12590 O O   . GLU B 460  ? 0.4152 0.4891 0.2901 -0.1014 0.0773  0.0711  458  GLU B O   
12591 C CB  . GLU B 460  ? 0.4228 0.4942 0.2940 -0.0863 0.0763  0.0628  458  GLU B CB  
12592 C CG  . GLU B 460  ? 0.4666 0.5274 0.3253 -0.0818 0.0752  0.0610  458  GLU B CG  
12593 C CD  . GLU B 460  ? 0.6275 0.6969 0.4887 -0.0745 0.0791  0.0573  458  GLU B CD  
12594 O OE1 . GLU B 460  ? 0.5760 0.6594 0.4488 -0.0727 0.0827  0.0562  458  GLU B OE1 
12595 O OE2 . GLU B 460  ? 0.6763 0.7378 0.5281 -0.0701 0.0783  0.0552  458  GLU B OE2 
12596 N N   . GLU B 461  ? 0.4022 0.4848 0.2934 -0.0993 0.0737  0.0676  459  GLU B N   
12597 C CA  . GLU B 461  ? 0.4006 0.4939 0.3016 -0.1040 0.0756  0.0696  459  GLU B CA  
12598 C C   . GLU B 461  ? 0.4479 0.5332 0.3479 -0.1114 0.0710  0.0723  459  GLU B C   
12599 O O   . GLU B 461  ? 0.4044 0.4979 0.3130 -0.1156 0.0715  0.0736  459  GLU B O   
12600 C CB  . GLU B 461  ? 0.3625 0.4705 0.2776 -0.1004 0.0770  0.0669  459  GLU B CB  
12601 C CG  . GLU B 461  ? 0.3264 0.4417 0.2430 -0.0924 0.0810  0.0638  459  GLU B CG  
12602 C CD  . GLU B 461  ? 0.3986 0.5196 0.3126 -0.0917 0.0867  0.0650  459  GLU B CD  
12603 O OE1 . GLU B 461  ? 0.4323 0.5573 0.3487 -0.0972 0.0881  0.0680  459  GLU B OE1 
12604 O OE2 . GLU B 461  ? 0.4682 0.5895 0.3776 -0.0859 0.0896  0.0629  459  GLU B OE2 
12605 N N   . VAL B 462  ? 0.3787 0.4477 0.2681 -0.1130 0.0665  0.0730  460  VAL B N   
12606 C CA  . VAL B 462  ? 0.3831 0.4425 0.2707 -0.1193 0.0616  0.0751  460  VAL B CA  
12607 C C   . VAL B 462  ? 0.4500 0.4950 0.3242 -0.1227 0.0601  0.0780  460  VAL B C   
12608 O O   . VAL B 462  ? 0.4013 0.4437 0.2745 -0.1289 0.0594  0.0809  460  VAL B O   
12609 C CB  . VAL B 462  ? 0.3687 0.4213 0.2574 -0.1175 0.0565  0.0728  460  VAL B CB  
12610 C CG1 . VAL B 462  ? 0.3884 0.4287 0.2735 -0.1236 0.0512  0.0748  460  VAL B CG1 
12611 C CG2 . VAL B 462  ? 0.3651 0.4322 0.2675 -0.1146 0.0579  0.0702  460  VAL B CG2 
12612 N N   . VAL B 463  ? 0.4126 0.4480 0.2764 -0.1185 0.0595  0.0771  461  VAL B N   
12613 C CA  . VAL B 463  ? 0.3931 0.4135 0.2434 -0.1208 0.0574  0.0796  461  VAL B CA  
12614 C C   . VAL B 463  ? 0.4299 0.4562 0.2779 -0.1228 0.0625  0.0820  461  VAL B C   
12615 O O   . VAL B 463  ? 0.4526 0.4901 0.3038 -0.1188 0.0676  0.0808  461  VAL B O   
12616 C CB  . VAL B 463  ? 0.4116 0.4205 0.2517 -0.1153 0.0549  0.0776  461  VAL B CB  
12617 C CG1 . VAL B 463  ? 0.4353 0.4292 0.2614 -0.1171 0.0529  0.0802  461  VAL B CG1 
12618 C CG2 . VAL B 463  ? 0.3837 0.3862 0.2257 -0.1135 0.0498  0.0754  461  VAL B CG2 
12619 N N   . GLY B 464  ? 0.4209 0.4394 0.2631 -0.1287 0.0611  0.0855  462  GLY B N   
12620 C CA  . GLY B 464  ? 0.4379 0.4591 0.2756 -0.1309 0.0654  0.0882  462  GLY B CA  
12621 C C   . GLY B 464  ? 0.4940 0.5241 0.3393 -0.1374 0.0675  0.0908  462  GLY B C   
12622 O O   . GLY B 464  ? 0.4753 0.5155 0.3323 -0.1387 0.0675  0.0898  462  GLY B O   
12623 N N   . ARG B 465  ? 0.5360 0.5624 0.3744 -0.1417 0.0692  0.0942  463  ARG B N   
12624 C CA  . ARG B 465  ? 0.5342 0.5686 0.3789 -0.1484 0.0712  0.0970  463  ARG B CA  
12625 C C   . ARG B 465  ? 0.5500 0.6045 0.4073 -0.1466 0.0769  0.0959  463  ARG B C   
12626 O O   . ARG B 465  ? 0.5840 0.6478 0.4507 -0.1511 0.0776  0.0969  463  ARG B O   
12627 C CB  . ARG B 465  ? 0.5969 0.6238 0.4312 -0.1528 0.0724  0.1008  463  ARG B CB  
12628 N N   . GLY B 466  ? 0.5199 0.5811 0.3775 -0.1398 0.0809  0.0937  464  GLY B N   
12629 C CA  . GLY B 466  ? 0.4901 0.5698 0.3595 -0.1370 0.0862  0.0922  464  GLY B CA  
12630 C C   . GLY B 466  ? 0.5314 0.6192 0.4127 -0.1341 0.0845  0.0889  464  GLY B C   
12631 O O   . GLY B 466  ? 0.5165 0.6198 0.4085 -0.1317 0.0885  0.0876  464  GLY B O   
12632 N N   . LYS B 467  ? 0.4963 0.5740 0.3760 -0.1342 0.0787  0.0876  465  LYS B N   
12633 C CA  . LYS B 467  ? 0.4350 0.5196 0.3254 -0.1314 0.0768  0.0846  465  LYS B CA  
12634 C C   . LYS B 467  ? 0.3863 0.4666 0.2801 -0.1379 0.0719  0.0859  465  LYS B C   
12635 O O   . LYS B 467  ? 0.4636 0.5490 0.3612 -0.1436 0.0729  0.0884  465  LYS B O   
12636 C CB  . LYS B 467  ? 0.4337 0.5116 0.3197 -0.1248 0.0748  0.0813  465  LYS B CB  
12637 C CG  . LYS B 467  ? 0.4883 0.5698 0.3701 -0.1184 0.0795  0.0798  465  LYS B CG  
12638 C CD  . LYS B 467  ? 0.4671 0.5667 0.3609 -0.1145 0.0845  0.0779  465  LYS B CD  
12639 C CE  . LYS B 467  ? 0.5113 0.6136 0.4003 -0.1080 0.0892  0.0762  465  LYS B CE  
12640 N NZ  . LYS B 467  ? 0.4902 0.6089 0.3908 -0.1033 0.0936  0.0738  465  LYS B NZ  
12641 N N   . LEU B 468  ? 0.3911 0.4623 0.2838 -0.1370 0.0666  0.0842  466  LEU B N   
12642 C CA  . LEU B 468  ? 0.3833 0.4483 0.2778 -0.1428 0.0615  0.0852  466  LEU B CA  
12643 C C   . LEU B 468  ? 0.4221 0.4684 0.3035 -0.1468 0.0575  0.0875  466  LEU B C   
12644 O O   . LEU B 468  ? 0.4198 0.4591 0.3010 -0.1519 0.0532  0.0885  466  LEU B O   
12645 C CB  . LEU B 468  ? 0.4091 0.4747 0.3100 -0.1396 0.0581  0.0820  466  LEU B CB  
12646 C CG  . LEU B 468  ? 0.3881 0.4714 0.3020 -0.1349 0.0615  0.0794  466  LEU B CG  
12647 C CD1 . LEU B 468  ? 0.4104 0.4933 0.3302 -0.1326 0.0576  0.0767  466  LEU B CD1 
12648 C CD2 . LEU B 468  ? 0.4232 0.5206 0.3465 -0.1388 0.0645  0.0811  466  LEU B CD2 
12649 N N   . ASP B 469  ? 0.4277 0.4654 0.2980 -0.1443 0.0586  0.0882  467  ASP B N   
12650 C CA  . ASP B 469  ? 0.4535 0.4731 0.3107 -0.1473 0.0548  0.0903  467  ASP B CA  
12651 C C   . ASP B 469  ? 0.4313 0.4377 0.2858 -0.1472 0.0482  0.0889  467  ASP B C   
12652 O O   . ASP B 469  ? 0.4447 0.4395 0.2942 -0.1521 0.0440  0.0906  467  ASP B O   
12653 C CB  . ASP B 469  ? 0.4867 0.5056 0.3420 -0.1547 0.0556  0.0941  467  ASP B CB  
12654 C CG  . ASP B 469  ? 0.5342 0.5369 0.3749 -0.1565 0.0538  0.0966  467  ASP B CG  
12655 O OD1 . ASP B 469  ? 0.5349 0.5289 0.3672 -0.1515 0.0528  0.0955  467  ASP B OD1 
12656 O OD2 . ASP B 469  ? 0.5821 0.5806 0.4197 -0.1629 0.0532  0.0996  467  ASP B OD2 
12657 N N   . ARG B 470  ? 0.4452 0.4533 0.3028 -0.1414 0.0473  0.0857  468  ARG B N   
12658 C CA  . ARG B 470  ? 0.4192 0.4155 0.2743 -0.1402 0.0415  0.0840  468  ARG B CA  
12659 C C   . ARG B 470  ? 0.4028 0.3913 0.2502 -0.1336 0.0406  0.0821  468  ARG B C   
12660 O O   . ARG B 470  ? 0.4262 0.4240 0.2759 -0.1288 0.0446  0.0805  468  ARG B O   
12661 C CB  . ARG B 470  ? 0.4190 0.4255 0.2868 -0.1398 0.0408  0.0818  468  ARG B CB  
12662 C CG  . ARG B 470  ? 0.3983 0.4119 0.2739 -0.1463 0.0408  0.0833  468  ARG B CG  
12663 C CD  . ARG B 470  ? 0.4087 0.4067 0.2765 -0.1520 0.0358  0.0854  468  ARG B CD  
12664 N NE  . ARG B 470  ? 0.4427 0.4472 0.3176 -0.1583 0.0355  0.0867  468  ARG B NE  
12665 C CZ  . ARG B 470  ? 0.4702 0.4784 0.3445 -0.1635 0.0379  0.0896  468  ARG B CZ  
12666 N NH1 . ARG B 470  ? 0.4781 0.4842 0.3450 -0.1632 0.0410  0.0916  468  ARG B NH1 
12667 N NH2 . ARG B 470  ? 0.5042 0.5182 0.3852 -0.1691 0.0371  0.0906  468  ARG B NH2 
12668 N N   . PRO B 471  ? 0.4142 0.3855 0.2522 -0.1329 0.0352  0.0821  469  PRO B N   
12669 C CA  . PRO B 471  ? 0.3711 0.3339 0.2008 -0.1268 0.0338  0.0805  469  PRO B CA  
12670 C C   . PRO B 471  ? 0.3744 0.3413 0.2101 -0.1218 0.0328  0.0770  469  PRO B C   
12671 O O   . PRO B 471  ? 0.3725 0.3448 0.2175 -0.1231 0.0317  0.0758  469  PRO B O   
12672 C CB  . PRO B 471  ? 0.4142 0.3570 0.2324 -0.1283 0.0280  0.0819  469  PRO B CB  
12673 C CG  . PRO B 471  ? 0.4632 0.4042 0.2864 -0.1337 0.0252  0.0827  469  PRO B CG  
12674 C CD  . PRO B 471  ? 0.4448 0.4030 0.2788 -0.1378 0.0301  0.0836  469  PRO B CD  
12675 N N   . CYS B 472  ? 0.3614 0.3261 0.1933 -0.1148 0.0328  0.0744  470  CYS B N   
12676 C CA  . CYS B 472  ? 0.3543 0.3223 0.1945 -0.1069 0.0308  0.0692  470  CYS B CA  
12677 C C   . CYS B 472  ? 0.3685 0.3236 0.2001 -0.1006 0.0268  0.0671  470  CYS B C   
12678 O O   . CYS B 472  ? 0.3697 0.3219 0.1925 -0.0994 0.0286  0.0681  470  CYS B O   
12679 C CB  . CYS B 472  ? 0.3374 0.3227 0.1868 -0.1034 0.0362  0.0671  470  CYS B CB  
12680 S SG  . CYS B 472  ? 0.3746 0.3635 0.2339 -0.0942 0.0338  0.0610  470  CYS B SG  
12681 N N   . ARG B 473  ? 0.3598 0.3074 0.1939 -0.0968 0.0215  0.0642  471  ARG B N   
12682 C CA  . ARG B 473  ? 0.3441 0.2814 0.1724 -0.0902 0.0175  0.0616  471  ARG B CA  
12683 C C   . ARG B 473  ? 0.3355 0.2821 0.1724 -0.0829 0.0186  0.0568  471  ARG B C   
12684 O O   . ARG B 473  ? 0.3398 0.2941 0.1877 -0.0815 0.0185  0.0545  471  ARG B O   
12685 C CB  . ARG B 473  ? 0.3325 0.2562 0.1583 -0.0898 0.0111  0.0610  471  ARG B CB  
12686 C CG  . ARG B 473  ? 0.3362 0.2480 0.1545 -0.0836 0.0066  0.0591  471  ARG B CG  
12687 C CD  . ARG B 473  ? 0.3457 0.2437 0.1608 -0.0838 0.0005  0.0591  471  ARG B CD  
12688 N NE  . ARG B 473  ? 0.3920 0.2828 0.2004 -0.0915 0.0003  0.0637  471  ARG B NE  
12689 C CZ  . ARG B 473  ? 0.4039 0.2839 0.1997 -0.0943 -0.0006 0.0672  471  ARG B CZ  
12690 N NH1 . ARG B 473  ? 0.4011 0.2750 0.1890 -0.0897 -0.0020 0.0667  471  ARG B NH1 
12691 N NH2 . ARG B 473  ? 0.3798 0.2547 0.1704 -0.1020 -0.0002 0.0715  471  ARG B NH2 
12692 N N   . ILE B 474  ? 0.3339 0.2793 0.1654 -0.0783 0.0194  0.0556  472  ILE B N   
12693 C CA  . ILE B 474  ? 0.3065 0.2596 0.1446 -0.0715 0.0204  0.0512  472  ILE B CA  
12694 C C   . ILE B 474  ? 0.3264 0.2704 0.1644 -0.0660 0.0146  0.0480  472  ILE B C   
12695 O O   . ILE B 474  ? 0.3263 0.2583 0.1547 -0.0649 0.0110  0.0487  472  ILE B O   
12696 C CB  . ILE B 474  ? 0.3383 0.2946 0.1701 -0.0695 0.0243  0.0513  472  ILE B CB  
12697 C CG1 . ILE B 474  ? 0.3246 0.2916 0.1576 -0.0747 0.0306  0.0544  472  ILE B CG1 
12698 C CG2 . ILE B 474  ? 0.3662 0.3282 0.2035 -0.0622 0.0246  0.0466  472  ILE B CG2 
12699 C CD1 . ILE B 474  ? 0.3860 0.3543 0.2103 -0.0738 0.0345  0.0554  472  ILE B CD1 
12700 N N   . TYR B 475  ? 0.3090 0.2588 0.1577 -0.0625 0.0136  0.0445  473  TYR B N   
12701 C CA  . TYR B 475  ? 0.2903 0.2341 0.1408 -0.0569 0.0088  0.0410  473  TYR B CA  
12702 C C   . TYR B 475  ? 0.3065 0.2527 0.1555 -0.0513 0.0097  0.0383  473  TYR B C   
12703 O O   . TYR B 475  ? 0.3345 0.2915 0.1901 -0.0492 0.0134  0.0364  473  TYR B O   
12704 C CB  . TYR B 475  ? 0.3092 0.2592 0.1716 -0.0560 0.0081  0.0387  473  TYR B CB  
12705 C CG  . TYR B 475  ? 0.3491 0.2938 0.2149 -0.0510 0.0032  0.0353  473  TYR B CG  
12706 C CD1 . TYR B 475  ? 0.3373 0.2702 0.1985 -0.0515 -0.0017 0.0360  473  TYR B CD1 
12707 C CD2 . TYR B 475  ? 0.4696 0.4214 0.3434 -0.0459 0.0037  0.0315  473  TYR B CD2 
12708 C CE1 . TYR B 475  ? 0.3329 0.2619 0.1977 -0.0468 -0.0058 0.0328  473  TYR B CE1 
12709 C CE2 . TYR B 475  ? 0.5220 0.4698 0.3993 -0.0417 -0.0005 0.0286  473  TYR B CE2 
12710 C CZ  . TYR B 475  ? 0.3955 0.3324 0.2685 -0.0421 -0.0051 0.0292  473  TYR B CZ  
12711 O OH  . TYR B 475  ? 0.4988 0.4325 0.3756 -0.0376 -0.0089 0.0262  473  TYR B OH  
12712 N N   . ALA B 476  ? 0.3021 0.2381 0.1420 -0.0488 0.0064  0.0382  474  ALA B N   
12713 C CA  . ALA B 476  ? 0.3498 0.2867 0.1855 -0.0447 0.0074  0.0363  474  ALA B CA  
12714 C C   . ALA B 476  ? 0.3105 0.2432 0.1481 -0.0386 0.0028  0.0325  474  ALA B C   
12715 O O   . ALA B 476  ? 0.3343 0.2563 0.1655 -0.0375 -0.0020 0.0329  474  ALA B O   
12716 C CB  . ALA B 476  ? 0.3527 0.2819 0.1750 -0.0471 0.0077  0.0396  474  ALA B CB  
12717 N N   . PRO B 477  ? 0.3234 0.2641 0.1694 -0.0347 0.0039  0.0289  475  PRO B N   
12718 C CA  . PRO B 477  ? 0.3460 0.2833 0.1939 -0.0293 -0.0003 0.0254  475  PRO B CA  
12719 C C   . PRO B 477  ? 0.3299 0.2611 0.1678 -0.0269 -0.0018 0.0251  475  PRO B C   
12720 O O   . PRO B 477  ? 0.3310 0.2644 0.1632 -0.0277 0.0018  0.0260  475  PRO B O   
12721 C CB  . PRO B 477  ? 0.3114 0.2594 0.1699 -0.0265 0.0023  0.0221  475  PRO B CB  
12722 C CG  . PRO B 477  ? 0.3250 0.2814 0.1890 -0.0305 0.0068  0.0240  475  PRO B CG  
12723 C CD  . PRO B 477  ? 0.3044 0.2577 0.1592 -0.0350 0.0089  0.0280  475  PRO B CD  
12724 N N   . VAL B 478  ? 0.3156 0.2391 0.1514 -0.0237 -0.0072 0.0236  476  VAL B N   
12725 C CA  . VAL B 478  ? 0.3062 0.2232 0.1327 -0.0212 -0.0098 0.0232  476  VAL B CA  
12726 C C   . VAL B 478  ? 0.3420 0.2590 0.1738 -0.0161 -0.0137 0.0192  476  VAL B C   
12727 O O   . VAL B 478  ? 0.3836 0.2982 0.2206 -0.0150 -0.0173 0.0184  476  VAL B O   
12728 C CB  . VAL B 478  ? 0.3162 0.2216 0.1320 -0.0232 -0.0132 0.0265  476  VAL B CB  
12729 C CG1 . VAL B 478  ? 0.4084 0.3075 0.2145 -0.0204 -0.0160 0.0260  476  VAL B CG1 
12730 C CG2 . VAL B 478  ? 0.3733 0.2787 0.1842 -0.0290 -0.0092 0.0307  476  VAL B CG2 
12731 N N   . GLY B 479  ? 0.3873 0.3071 0.2181 -0.0132 -0.0130 0.0167  477  GLY B N   
12732 C CA  . GLY B 479  ? 0.3856 0.3052 0.2211 -0.0088 -0.0169 0.0131  477  GLY B CA  
12733 C C   . GLY B 479  ? 0.3711 0.2955 0.2069 -0.0062 -0.0150 0.0102  477  GLY B C   
12734 O O   . GLY B 479  ? 0.3811 0.3098 0.2144 -0.0074 -0.0101 0.0106  477  GLY B O   
12735 N N   . THR B 480  ? 0.4436 0.3671 0.2825 -0.0026 -0.0189 0.0071  478  THR B N   
12736 C CA  . THR B 480  ? 0.4687 0.3955 0.3084 0.0001  -0.0182 0.0038  478  THR B CA  
12737 C C   . THR B 480  ? 0.4063 0.3422 0.2562 0.0005  -0.0142 0.0019  478  THR B C   
12738 O O   . THR B 480  ? 0.3989 0.3388 0.2561 -0.0012 -0.0125 0.0029  478  THR B O   
12739 C CB  . THR B 480  ? 0.4467 0.3699 0.2876 0.0033  -0.0241 0.0013  478  THR B CB  
12740 O OG1 . THR B 480  ? 0.4919 0.4181 0.3436 0.0041  -0.0259 0.0003  478  THR B OG1 
12741 C CG2 . THR B 480  ? 0.4672 0.3814 0.2984 0.0034  -0.0285 0.0032  478  THR B CG2 
12742 N N   . HIS B 481  ? 0.4691 0.4078 0.3191 0.0027  -0.0129 -0.0009 479  HIS B N   
12743 C CA  . HIS B 481  ? 0.4434 0.3901 0.3027 0.0036  -0.0094 -0.0029 479  HIS B CA  
12744 C C   . HIS B 481  ? 0.4278 0.3769 0.2979 0.0044  -0.0119 -0.0042 479  HIS B C   
12745 O O   . HIS B 481  ? 0.4240 0.3791 0.3019 0.0034  -0.0091 -0.0039 479  HIS B O   
12746 C CB  . HIS B 481  ? 0.4192 0.3666 0.2759 0.0062  -0.0086 -0.0061 479  HIS B CB  
12747 C CG  . HIS B 481  ? 0.4707 0.4173 0.3177 0.0057  -0.0050 -0.0052 479  HIS B CG  
12748 N ND1 . HIS B 481  ? 0.5012 0.4484 0.3447 0.0080  -0.0033 -0.0078 479  HIS B ND1 
12749 C CD2 . HIS B 481  ? 0.4427 0.3878 0.2825 0.0031  -0.0026 -0.0019 479  HIS B CD2 
12750 C CE1 . HIS B 481  ? 0.5370 0.4835 0.3716 0.0071  0.0002  -0.0063 479  HIS B CE1 
12751 N NE2 . HIS B 481  ? 0.5028 0.4481 0.3350 0.0040  0.0007  -0.0026 479  HIS B NE2 
12752 N N   . GLU B 482  ? 0.4678 0.4127 0.3384 0.0061  -0.0172 -0.0055 480  GLU B N   
12753 C CA  . GLU B 482  ? 0.3974 0.3449 0.2781 0.0071  -0.0194 -0.0069 480  GLU B CA  
12754 C C   . GLU B 482  ? 0.4423 0.3907 0.3270 0.0049  -0.0187 -0.0044 480  GLU B C   
12755 O O   . GLU B 482  ? 0.4257 0.3794 0.3192 0.0047  -0.0172 -0.0050 480  GLU B O   
12756 C CB  . GLU B 482  ? 0.5488 0.4918 0.4288 0.0092  -0.0252 -0.0084 480  GLU B CB  
12757 C CG  . GLU B 482  ? 0.5746 0.5200 0.4645 0.0102  -0.0277 -0.0094 480  GLU B CG  
12758 C CD  . GLU B 482  ? 0.7233 0.6648 0.6127 0.0122  -0.0335 -0.0105 480  GLU B CD  
12759 O OE1 . GLU B 482  ? 0.7787 0.7158 0.6604 0.0130  -0.0359 -0.0108 480  GLU B OE1 
12760 O OE2 . GLU B 482  ? 0.7443 0.6874 0.6410 0.0131  -0.0357 -0.0111 480  GLU B OE2 
12761 N N   . THR B 483  ? 0.4240 0.3669 0.3016 0.0030  -0.0198 -0.0016 481  THR B N   
12762 C CA  . THR B 483  ? 0.4467 0.3890 0.3271 0.0007  -0.0197 0.0007  481  THR B CA  
12763 C C   . THR B 483  ? 0.4048 0.3534 0.2885 -0.0020 -0.0144 0.0021  481  THR B C   
12764 O O   . THR B 483  ? 0.4226 0.3739 0.3129 -0.0033 -0.0137 0.0027  481  THR B O   
12765 C CB  . THR B 483  ? 0.4472 0.3810 0.3185 -0.0007 -0.0223 0.0035  481  THR B CB  
12766 O OG1 . THR B 483  ? 0.5332 0.4660 0.3961 -0.0031 -0.0191 0.0058  481  THR B OG1 
12767 C CG2 . THR B 483  ? 0.4282 0.3563 0.2957 0.0023  -0.0277 0.0022  481  THR B CG2 
12768 N N   . LEU B 484  ? 0.4069 0.3577 0.2859 -0.0029 -0.0105 0.0027  482  LEU B N   
12769 C CA  . LEU B 484  ? 0.3936 0.3512 0.2760 -0.0053 -0.0054 0.0042  482  LEU B CA  
12770 C C   . LEU B 484  ? 0.3771 0.3426 0.2697 -0.0036 -0.0035 0.0017  482  LEU B C   
12771 O O   . LEU B 484  ? 0.3681 0.3391 0.2671 -0.0053 -0.0010 0.0026  482  LEU B O   
12772 C CB  . LEU B 484  ? 0.4124 0.3706 0.2868 -0.0066 -0.0016 0.0056  482  LEU B CB  
12773 C CG  . LEU B 484  ? 0.4068 0.3678 0.2790 -0.0039 0.0006  0.0032  482  LEU B CG  
12774 C CD1 . LEU B 484  ? 0.4082 0.3787 0.2880 -0.0036 0.0055  0.0023  482  LEU B CD1 
12775 C CD2 . LEU B 484  ? 0.4638 0.4208 0.3244 -0.0049 0.0020  0.0048  482  LEU B CD2 
12776 N N   . LEU B 485  ? 0.3949 0.3607 0.2891 -0.0002 -0.0048 -0.0014 483  LEU B N   
12777 C CA  . LEU B 485  ? 0.3686 0.3411 0.2719 0.0015  -0.0030 -0.0038 483  LEU B CA  
12778 C C   . LEU B 485  ? 0.4081 0.3820 0.3199 0.0016  -0.0053 -0.0042 483  LEU B C   
12779 O O   . LEU B 485  ? 0.3733 0.3532 0.2929 0.0021  -0.0033 -0.0053 483  LEU B O   
12780 C CB  . LEU B 485  ? 0.3739 0.3454 0.2757 0.0047  -0.0040 -0.0069 483  LEU B CB  
12781 C CG  . LEU B 485  ? 0.3911 0.3631 0.2861 0.0054  -0.0008 -0.0073 483  LEU B CG  
12782 C CD1 . LEU B 485  ? 0.4022 0.3716 0.2952 0.0085  -0.0028 -0.0105 483  LEU B CD1 
12783 C CD2 . LEU B 485  ? 0.3972 0.3771 0.2969 0.0051  0.0046  -0.0069 483  LEU B CD2 
12784 N N   . ALA B 486  ? 0.3639 0.3322 0.2742 0.0011  -0.0092 -0.0034 484  ALA B N   
12785 C CA  . ALA B 486  ? 0.3771 0.3462 0.2950 0.0018  -0.0116 -0.0044 484  ALA B CA  
12786 C C   . ALA B 486  ? 0.3809 0.3550 0.3049 -0.0003 -0.0090 -0.0032 484  ALA B C   
12787 O O   . ALA B 486  ? 0.4585 0.4366 0.3905 0.0007  -0.0091 -0.0046 484  ALA B O   
12788 C CB  . ALA B 486  ? 0.4162 0.3780 0.3304 0.0020  -0.0162 -0.0037 484  ALA B CB  
12789 N N   . TYR B 487  ? 0.3842 0.3584 0.3047 -0.0035 -0.0068 -0.0004 485  TYR B N   
12790 C CA  . TYR B 487  ? 0.3765 0.3554 0.3025 -0.0060 -0.0046 0.0010  485  TYR B CA  
12791 C C   . TYR B 487  ? 0.4131 0.3974 0.3379 -0.0082 0.0000  0.0027  485  TYR B C   
12792 O O   . TYR B 487  ? 0.3712 0.3584 0.2980 -0.0114 0.0018  0.0048  485  TYR B O   
12793 C CB  . TYR B 487  ? 0.4058 0.3791 0.3300 -0.0083 -0.0073 0.0029  485  TYR B CB  
12794 C CG  . TYR B 487  ? 0.4183 0.3880 0.3456 -0.0057 -0.0114 0.0010  485  TYR B CG  
12795 C CD1 . TYR B 487  ? 0.4579 0.4319 0.3936 -0.0047 -0.0115 -0.0006 485  TYR B CD1 
12796 C CD2 . TYR B 487  ? 0.4596 0.4218 0.3812 -0.0041 -0.0153 0.0007  485  TYR B CD2 
12797 C CE1 . TYR B 487  ? 0.4720 0.4434 0.4107 -0.0023 -0.0149 -0.0023 485  TYR B CE1 
12798 C CE2 . TYR B 487  ? 0.4767 0.4365 0.4017 -0.0016 -0.0189 -0.0010 485  TYR B CE2 
12799 C CZ  . TYR B 487  ? 0.5441 0.5087 0.4776 -0.0007 -0.0186 -0.0026 485  TYR B CZ  
12800 O OH  . TYR B 487  ? 0.6276 0.5904 0.5645 0.0019  -0.0219 -0.0043 485  TYR B OH  
12801 N N   . LEU B 488  ? 0.3977 0.3837 0.3193 -0.0066 0.0021  0.0018  486  LEU B N   
12802 C CA  . LEU B 488  ? 0.3414 0.3334 0.2621 -0.0081 0.0069  0.0032  486  LEU B CA  
12803 C C   . LEU B 488  ? 0.3332 0.3340 0.2632 -0.0083 0.0097  0.0029  486  LEU B C   
12804 O O   . LEU B 488  ? 0.3548 0.3611 0.2858 -0.0108 0.0130  0.0050  486  LEU B O   
12805 C CB  . LEU B 488  ? 0.3536 0.3453 0.2690 -0.0056 0.0086  0.0018  486  LEU B CB  
12806 C CG  . LEU B 488  ? 0.3538 0.3516 0.2674 -0.0068 0.0138  0.0032  486  LEU B CG  
12807 C CD1 . LEU B 488  ? 0.4122 0.4093 0.3218 -0.0114 0.0149  0.0070  486  LEU B CD1 
12808 C CD2 . LEU B 488  ? 0.3573 0.3537 0.2643 -0.0042 0.0153  0.0017  486  LEU B CD2 
12809 N N   . VAL B 489  ? 0.3157 0.3182 0.2524 -0.0058 0.0082  0.0006  487  VAL B N   
12810 C CA  . VAL B 489  ? 0.2933 0.3038 0.2385 -0.0058 0.0105  0.0004  487  VAL B CA  
12811 C C   . VAL B 489  ? 0.3339 0.3461 0.2815 -0.0098 0.0106  0.0029  487  VAL B C   
12812 O O   . VAL B 489  ? 0.3073 0.3267 0.2584 -0.0115 0.0137  0.0043  487  VAL B O   
12813 C CB  . VAL B 489  ? 0.2759 0.2869 0.2273 -0.0027 0.0086  -0.0024 487  VAL B CB  
12814 C CG1 . VAL B 489  ? 0.2941 0.3122 0.2540 -0.0033 0.0101  -0.0022 487  VAL B CG1 
12815 C CG2 . VAL B 489  ? 0.3556 0.3665 0.3055 0.0009  0.0094  -0.0048 487  VAL B CG2 
12816 N N   . ARG B 490  ? 0.3279 0.3336 0.2737 -0.0111 0.0070  0.0034  488  ARG B N   
12817 C CA  . ARG B 490  ? 0.3448 0.3510 0.2922 -0.0151 0.0067  0.0057  488  ARG B CA  
12818 C C   . ARG B 490  ? 0.3345 0.3423 0.2774 -0.0189 0.0094  0.0087  488  ARG B C   
12819 O O   . ARG B 490  ? 0.3281 0.3411 0.2744 -0.0221 0.0112  0.0105  488  ARG B O   
12820 C CB  . ARG B 490  ? 0.3279 0.3256 0.2730 -0.0155 0.0023  0.0057  488  ARG B CB  
12821 C CG  . ARG B 490  ? 0.3436 0.3401 0.2894 -0.0195 0.0015  0.0078  488  ARG B CG  
12822 C CD  . ARG B 490  ? 0.3601 0.3470 0.3020 -0.0194 -0.0028 0.0076  488  ARG B CD  
12823 N NE  . ARG B 490  ? 0.3812 0.3606 0.3142 -0.0199 -0.0041 0.0089  488  ARG B NE  
12824 C CZ  . ARG B 490  ? 0.3947 0.3664 0.3237 -0.0175 -0.0077 0.0079  488  ARG B CZ  
12825 N NH1 . ARG B 490  ? 0.3391 0.3102 0.2727 -0.0142 -0.0102 0.0054  488  ARG B NH1 
12826 N NH2 . ARG B 490  ? 0.3891 0.3540 0.3095 -0.0183 -0.0089 0.0095  488  ARG B NH2 
12827 N N   . ARG B 491  ? 0.3633 0.3669 0.2983 -0.0186 0.0098  0.0093  489  ARG B N   
12828 C CA  . ARG B 491  ? 0.3283 0.3333 0.2583 -0.0223 0.0126  0.0123  489  ARG B CA  
12829 C C   . ARG B 491  ? 0.3810 0.3967 0.3154 -0.0222 0.0176  0.0125  489  ARG B C   
12830 O O   . ARG B 491  ? 0.3792 0.3998 0.3142 -0.0261 0.0202  0.0151  489  ARG B O   
12831 C CB  . ARG B 491  ? 0.3942 0.3919 0.3142 -0.0218 0.0118  0.0128  489  ARG B CB  
12832 C CG  . ARG B 491  ? 0.4488 0.4468 0.3627 -0.0260 0.0146  0.0162  489  ARG B CG  
12833 C CD  . ARG B 491  ? 0.4786 0.4678 0.3870 -0.0297 0.0114  0.0187  489  ARG B CD  
12834 N NE  . ARG B 491  ? 0.5473 0.5268 0.4470 -0.0279 0.0084  0.0183  489  ARG B NE  
12835 C CZ  . ARG B 491  ? 0.5352 0.5049 0.4293 -0.0293 0.0046  0.0197  489  ARG B CZ  
12836 N NH1 . ARG B 491  ? 0.5310 0.4985 0.4268 -0.0328 0.0032  0.0214  489  ARG B NH1 
12837 N NH2 . ARG B 491  ? 0.5030 0.4646 0.3893 -0.0272 0.0019  0.0193  489  ARG B NH2 
12838 N N   . LEU B 492  ? 0.3398 0.3592 0.2771 -0.0178 0.0188  0.0099  490  LEU B N   
12839 C CA  . LEU B 492  ? 0.3502 0.3796 0.2917 -0.0170 0.0235  0.0098  490  LEU B CA  
12840 C C   . LEU B 492  ? 0.3665 0.4039 0.3173 -0.0184 0.0244  0.0104  490  LEU B C   
12841 O O   . LEU B 492  ? 0.3894 0.4355 0.3433 -0.0200 0.0281  0.0120  490  LEU B O   
12842 C CB  . LEU B 492  ? 0.4003 0.4303 0.3420 -0.0117 0.0242  0.0067  490  LEU B CB  
12843 C CG  . LEU B 492  ? 0.3832 0.4065 0.3155 -0.0102 0.0238  0.0060  490  LEU B CG  
12844 C CD1 . LEU B 492  ? 0.4208 0.4431 0.3534 -0.0051 0.0235  0.0024  490  LEU B CD1 
12845 C CD2 . LEU B 492  ? 0.3973 0.4240 0.3243 -0.0122 0.0280  0.0082  490  LEU B CD2 
12846 N N   . LEU B 493  ? 0.3586 0.3935 0.3139 -0.0179 0.0210  0.0092  491  LEU B N   
12847 C CA  . LEU B 493  ? 0.3187 0.3605 0.2823 -0.0194 0.0214  0.0098  491  LEU B CA  
12848 C C   . LEU B 493  ? 0.3669 0.4101 0.3298 -0.0251 0.0218  0.0131  491  LEU B C   
12849 O O   . LEU B 493  ? 0.3760 0.4275 0.3452 -0.0270 0.0235  0.0142  491  LEU B O   
12850 C CB  . LEU B 493  ? 0.3519 0.3898 0.3193 -0.0176 0.0177  0.0078  491  LEU B CB  
12851 C CG  . LEU B 493  ? 0.4117 0.4541 0.3854 -0.0132 0.0183  0.0052  491  LEU B CG  
12852 C CD1 . LEU B 493  ? 0.4357 0.4774 0.4059 -0.0096 0.0199  0.0035  491  LEU B CD1 
12853 C CD2 . LEU B 493  ? 0.3745 0.4121 0.3508 -0.0117 0.0146  0.0034  491  LEU B CD2 
12854 N N   . GLU B 494  ? 0.3722 0.4073 0.3276 -0.0280 0.0201  0.0147  492  GLU B N   
12855 C CA  . GLU B 494  ? 0.3451 0.3802 0.2990 -0.0338 0.0202  0.0179  492  GLU B CA  
12856 C C   . GLU B 494  ? 0.3836 0.4296 0.3404 -0.0363 0.0249  0.0200  492  GLU B C   
12857 O O   . GLU B 494  ? 0.3675 0.4191 0.3291 -0.0402 0.0254  0.0218  492  GLU B O   
12858 C CB  . GLU B 494  ? 0.3540 0.3785 0.2979 -0.0361 0.0183  0.0195  492  GLU B CB  
12859 C CG  . GLU B 494  ? 0.3258 0.3394 0.2669 -0.0348 0.0133  0.0182  492  GLU B CG  
12860 C CD  . GLU B 494  ? 0.4042 0.4075 0.3351 -0.0357 0.0114  0.0195  492  GLU B CD  
12861 O OE1 . GLU B 494  ? 0.4438 0.4478 0.3694 -0.0385 0.0140  0.0219  492  GLU B OE1 
12862 O OE2 . GLU B 494  ? 0.4821 0.4767 0.4101 -0.0336 0.0075  0.0181  492  GLU B OE2 
12863 N N   . ASN B 495  ? 0.3546 0.4040 0.3089 -0.0339 0.0282  0.0197  493  ASN B N   
12864 C CA  . ASN B 495  ? 0.3966 0.4568 0.3534 -0.0357 0.0331  0.0216  493  ASN B CA  
12865 C C   . ASN B 495  ? 0.4240 0.4932 0.3867 -0.0306 0.0361  0.0193  493  ASN B C   
12866 O O   . ASN B 495  ? 0.3990 0.4775 0.3636 -0.0310 0.0404  0.0205  493  ASN B O   
12867 C CB  . ASN B 495  ? 0.3520 0.4089 0.2996 -0.0379 0.0351  0.0237  493  ASN B CB  
12868 C CG  . ASN B 495  ? 0.3899 0.4373 0.3310 -0.0431 0.0322  0.0262  493  ASN B CG  
12869 O OD1 . ASN B 495  ? 0.3504 0.4004 0.2940 -0.0483 0.0320  0.0287  493  ASN B OD1 
12870 N ND2 . ASN B 495  ? 0.3561 0.3922 0.2887 -0.0416 0.0295  0.0255  493  ASN B ND2 
12871 N N   . GLY B 496  ? 0.4523 0.5191 0.4181 -0.0260 0.0339  0.0162  494  GLY B N   
12872 C CA  . GLY B 496  ? 0.4526 0.5263 0.4230 -0.0209 0.0365  0.0140  494  GLY B CA  
12873 C C   . GLY B 496  ? 0.4785 0.5582 0.4583 -0.0191 0.0357  0.0128  494  GLY B C   
12874 O O   . GLY B 496  ? 0.4873 0.5716 0.4708 -0.0146 0.0375  0.0109  494  GLY B O   
12875 N N   . ALA B 497  ? 0.4319 0.5111 0.4154 -0.0226 0.0331  0.0139  495  ALA B N   
12876 C CA  . ALA B 497  ? 0.4136 0.4985 0.4056 -0.0213 0.0322  0.0130  495  ALA B CA  
12877 C C   . ALA B 497  ? 0.4042 0.5019 0.4028 -0.0230 0.0356  0.0150  495  ALA B C   
12878 O O   . ALA B 497  ? 0.4103 0.5122 0.4070 -0.0264 0.0381  0.0174  495  ALA B O   
12879 C CB  . ALA B 497  ? 0.3935 0.4723 0.3863 -0.0240 0.0279  0.0132  495  ALA B CB  
12880 N N   . ASN B 498  ? 0.4082 0.5123 0.4145 -0.0206 0.0354  0.0140  496  ASN B N   
12881 C CA  . ASN B 498  ? 0.3810 0.4983 0.3943 -0.0211 0.0386  0.0154  496  ASN B CA  
12882 C C   . ASN B 498  ? 0.4125 0.5342 0.4275 -0.0278 0.0385  0.0186  496  ASN B C   
12883 O O   . ASN B 498  ? 0.3726 0.5048 0.3909 -0.0295 0.0418  0.0206  496  ASN B O   
12884 C CB  . ASN B 498  ? 0.4443 0.5662 0.4651 -0.0174 0.0376  0.0138  496  ASN B CB  
12885 C CG  . ASN B 498  ? 0.5232 0.6588 0.5520 -0.0182 0.0400  0.0155  496  ASN B CG  
12886 O OD1 . ASN B 498  ? 0.5299 0.6694 0.5632 -0.0221 0.0382  0.0170  496  ASN B OD1 
12887 N ND2 . ASN B 498  ? 0.6006 0.7439 0.6313 -0.0144 0.0439  0.0151  496  ASN B ND2 
12888 N N   . SER B 499  ? 0.3521 0.4663 0.3648 -0.0317 0.0347  0.0192  497  SER B N   
12889 C CA  . SER B 499  ? 0.3269 0.4434 0.3403 -0.0385 0.0341  0.0222  497  SER B CA  
12890 C C   . SER B 499  ? 0.2760 0.3864 0.2812 -0.0426 0.0347  0.0241  497  SER B C   
12891 O O   . SER B 499  ? 0.3481 0.4595 0.3528 -0.0487 0.0343  0.0268  497  SER B O   
12892 C CB  . SER B 499  ? 0.3965 0.5074 0.4113 -0.0407 0.0295  0.0217  497  SER B CB  
12893 O OG  . SER B 499  ? 0.4051 0.5031 0.4135 -0.0390 0.0266  0.0199  497  SER B OG  
12894 N N   . SER B 500  ? 0.3033 0.4070 0.3017 -0.0394 0.0356  0.0229  498  SER B N   
12895 C CA  . SER B 500  ? 0.2683 0.3653 0.2580 -0.0429 0.0360  0.0248  498  SER B CA  
12896 C C   . SER B 500  ? 0.2901 0.3971 0.2805 -0.0458 0.0407  0.0275  498  SER B C   
12897 O O   . SER B 500  ? 0.3254 0.4424 0.3205 -0.0424 0.0443  0.0268  498  SER B O   
12898 C CB  . SER B 500  ? 0.3450 0.4325 0.3273 -0.0385 0.0355  0.0227  498  SER B CB  
12899 O OG  . SER B 500  ? 0.3676 0.4456 0.3488 -0.0365 0.0311  0.0205  498  SER B OG  
12900 N N   . PHE B 501  ? 0.2496 0.3536 0.2352 -0.0520 0.0406  0.0305  499  PHE B N   
12901 C CA  . PHE B 501  ? 0.2644 0.3779 0.2503 -0.0554 0.0452  0.0334  499  PHE B CA  
12902 C C   . PHE B 501  ? 0.3543 0.4693 0.3360 -0.0508 0.0492  0.0323  499  PHE B C   
12903 O O   . PHE B 501  ? 0.2962 0.4232 0.2821 -0.0497 0.0537  0.0329  499  PHE B O   
12904 C CB  . PHE B 501  ? 0.2713 0.3788 0.2509 -0.0629 0.0442  0.0368  499  PHE B CB  
12905 C CG  . PHE B 501  ? 0.2799 0.3968 0.2593 -0.0672 0.0489  0.0401  499  PHE B CG  
12906 C CD1 . PHE B 501  ? 0.3389 0.4533 0.3104 -0.0663 0.0520  0.0408  499  PHE B CD1 
12907 C CD2 . PHE B 501  ? 0.3167 0.4451 0.3037 -0.0722 0.0503  0.0425  499  PHE B CD2 
12908 C CE1 . PHE B 501  ? 0.3179 0.4413 0.2891 -0.0703 0.0567  0.0439  499  PHE B CE1 
12909 C CE2 . PHE B 501  ? 0.2999 0.4379 0.2872 -0.0763 0.0549  0.0456  499  PHE B CE2 
12910 C CZ  . PHE B 501  ? 0.3204 0.4559 0.2998 -0.0754 0.0582  0.0463  499  PHE B CZ  
12911 N N   . VAL B 502  ? 0.3168 0.4199 0.2900 -0.0479 0.0475  0.0306  500  VAL B N   
12912 C CA  . VAL B 502  ? 0.3490 0.4524 0.3168 -0.0441 0.0510  0.0298  500  VAL B CA  
12913 C C   . VAL B 502  ? 0.4058 0.5174 0.3799 -0.0374 0.0533  0.0269  500  VAL B C   
12914 O O   . VAL B 502  ? 0.4477 0.5664 0.4214 -0.0351 0.0579  0.0268  500  VAL B O   
12915 C CB  . VAL B 502  ? 0.3795 0.4681 0.3369 -0.0426 0.0480  0.0286  500  VAL B CB  
12916 C CG1 . VAL B 502  ? 0.4183 0.5066 0.3700 -0.0380 0.0511  0.0271  500  VAL B CG1 
12917 C CG2 . VAL B 502  ? 0.3492 0.4301 0.2994 -0.0491 0.0463  0.0318  500  VAL B CG2 
12918 N N   . HIS B 503  ? 0.3309 0.4416 0.3108 -0.0343 0.0503  0.0245  501  HIS B N   
12919 C CA  . HIS B 503  ? 0.3945 0.5124 0.3806 -0.0281 0.0522  0.0219  501  HIS B CA  
12920 C C   . HIS B 503  ? 0.3939 0.5271 0.3887 -0.0292 0.0559  0.0236  501  HIS B C   
12921 O O   . HIS B 503  ? 0.3644 0.5056 0.3615 -0.0249 0.0598  0.0226  501  HIS B O   
12922 C CB  . HIS B 503  ? 0.4229 0.5354 0.4125 -0.0251 0.0480  0.0193  501  HIS B CB  
12923 C CG  . HIS B 503  ? 0.4319 0.5507 0.4276 -0.0190 0.0494  0.0168  501  HIS B CG  
12924 N ND1 . HIS B 503  ? 0.4499 0.5793 0.4552 -0.0187 0.0502  0.0173  501  HIS B ND1 
12925 C CD2 . HIS B 503  ? 0.4729 0.5883 0.4662 -0.0130 0.0501  0.0139  501  HIS B CD2 
12926 C CE1 . HIS B 503  ? 0.4213 0.5534 0.4297 -0.0126 0.0513  0.0148  501  HIS B CE1 
12927 N NE2 . HIS B 503  ? 0.4483 0.5719 0.4495 -0.0091 0.0513  0.0126  501  HIS B NE2 
12928 N N   . ARG B 504  ? 0.3216 0.4593 0.3213 -0.0348 0.0546  0.0261  502  ARG B N   
12929 C CA  . ARG B 504  ? 0.3490 0.5020 0.3579 -0.0361 0.0576  0.0277  502  ARG B CA  
12930 C C   . ARG B 504  ? 0.3999 0.5614 0.4070 -0.0377 0.0630  0.0299  502  ARG B C   
12931 O O   . ARG B 504  ? 0.3724 0.5472 0.3864 -0.0356 0.0668  0.0302  502  ARG B O   
12932 C CB  . ARG B 504  ? 0.3554 0.5103 0.3691 -0.0423 0.0545  0.0299  502  ARG B CB  
12933 C CG  . ARG B 504  ? 0.3748 0.5249 0.3923 -0.0401 0.0500  0.0277  502  ARG B CG  
12934 C CD  . ARG B 504  ? 0.3438 0.4907 0.3624 -0.0465 0.0462  0.0295  502  ARG B CD  
12935 N NE  . ARG B 504  ? 0.3739 0.5328 0.3986 -0.0520 0.0479  0.0326  502  ARG B NE  
12936 C CZ  . ARG B 504  ? 0.3108 0.4825 0.3452 -0.0510 0.0488  0.0328  502  ARG B CZ  
12937 N NH1 . ARG B 504  ? 0.4031 0.5777 0.4423 -0.0444 0.0487  0.0302  502  ARG B NH1 
12938 N NH2 . ARG B 504  ? 0.3923 0.5741 0.4319 -0.0568 0.0498  0.0357  502  ARG B NH2 
12939 N N   . ILE B 505  ? 0.3135 0.4677 0.3115 -0.0414 0.0635  0.0316  503  ILE B N   
12940 C CA  . ILE B 505  ? 0.3520 0.5142 0.3479 -0.0433 0.0688  0.0339  503  ILE B CA  
12941 C C   . ILE B 505  ? 0.3924 0.5565 0.3854 -0.0362 0.0727  0.0314  503  ILE B C   
12942 O O   . ILE B 505  ? 0.3401 0.5149 0.3345 -0.0357 0.0779  0.0325  503  ILE B O   
12943 C CB  . ILE B 505  ? 0.3261 0.4796 0.3126 -0.0499 0.0681  0.0367  503  ILE B CB  
12944 C CG1 . ILE B 505  ? 0.4287 0.5924 0.4144 -0.0533 0.0738  0.0398  503  ILE B CG1 
12945 C CG2 . ILE B 505  ? 0.3645 0.5028 0.3403 -0.0469 0.0659  0.0348  503  ILE B CG2 
12946 C CD1 . ILE B 505  ? 0.4352 0.5953 0.4164 -0.0620 0.0730  0.0438  503  ILE B CD1 
12947 N N   . ASN B 506  ? 0.3683 0.5226 0.3577 -0.0306 0.0702  0.0279  504  ASN B N   
12948 C CA  . ASN B 506  ? 0.4174 0.5728 0.4045 -0.0234 0.0733  0.0250  504  ASN B CA  
12949 C C   . ASN B 506  ? 0.4279 0.5927 0.4249 -0.0180 0.0741  0.0230  504  ASN B C   
12950 O O   . ASN B 506  ? 0.4475 0.6125 0.4432 -0.0114 0.0762  0.0203  504  ASN B O   
12951 C CB  . ASN B 506  ? 0.4567 0.5969 0.4347 -0.0202 0.0701  0.0223  504  ASN B CB  
12952 C CG  . ASN B 506  ? 0.5509 0.6829 0.5177 -0.0236 0.0706  0.0239  504  ASN B CG  
12953 O OD1 . ASN B 506  ? 0.6377 0.7754 0.6013 -0.0246 0.0753  0.0255  504  ASN B OD1 
12954 N ND2 . ASN B 506  ? 0.6035 0.7223 0.5643 -0.0254 0.0658  0.0236  504  ASN B ND2 
12955 N N   . ASP B 507  ? 0.4555 0.6273 0.4617 -0.0205 0.0724  0.0242  505  ASP B N   
12956 C CA  . ASP B 507  ? 0.4357 0.6169 0.4515 -0.0157 0.0730  0.0227  505  ASP B CA  
12957 C C   . ASP B 507  ? 0.4994 0.6923 0.5221 -0.0167 0.0760  0.0245  505  ASP B C   
12958 O O   . ASP B 507  ? 0.4685 0.6657 0.4954 -0.0227 0.0748  0.0272  505  ASP B O   
12959 C CB  . ASP B 507  ? 0.4417 0.6197 0.4631 -0.0171 0.0678  0.0224  505  ASP B CB  
12960 C CG  . ASP B 507  ? 0.4839 0.6698 0.5143 -0.0117 0.0678  0.0207  505  ASP B CG  
12961 O OD1 . ASP B 507  ? 0.4913 0.6839 0.5246 -0.0074 0.0710  0.0199  505  ASP B OD1 
12962 O OD2 . ASP B 507  ? 0.5107 0.6926 0.5444 -0.0117 0.0636  0.0198  505  ASP B OD2 
12963 N N   . PRO B 508  ? 0.5419 0.7387 0.5658 -0.0109 0.0792  0.0228  506  PRO B N   
12964 C CA  . PRO B 508  ? 0.5408 0.7481 0.5713 -0.0117 0.0818  0.0242  506  PRO B CA  
12965 C C   . PRO B 508  ? 0.5440 0.7589 0.5855 -0.0119 0.0793  0.0246  506  PRO B C   
12966 O O   . PRO B 508  ? 0.5761 0.8000 0.6235 -0.0139 0.0807  0.0264  506  PRO B O   
12967 C CB  . PRO B 508  ? 0.5824 0.7903 0.6105 -0.0046 0.0856  0.0217  506  PRO B CB  
12968 C CG  . PRO B 508  ? 0.6069 0.8068 0.6317 0.0010  0.0836  0.0185  506  PRO B CG  
12969 C CD  . PRO B 508  ? 0.5349 0.7268 0.5542 -0.0034 0.0806  0.0193  506  PRO B CD  
12970 N N   . LYS B 509  ? 0.5221 0.7337 0.5663 -0.0098 0.0757  0.0232  507  LYS B N   
12971 C CA  . LYS B 509  ? 0.5348 0.7525 0.5886 -0.0103 0.0728  0.0236  507  LYS B CA  
12972 C C   . LYS B 509  ? 0.5346 0.7531 0.5904 -0.0183 0.0698  0.0264  507  LYS B C   
12973 O O   . LYS B 509  ? 0.6018 0.8244 0.6648 -0.0193 0.0669  0.0268  507  LYS B O   
12974 C CB  . LYS B 509  ? 0.4959 0.7091 0.5511 -0.0047 0.0701  0.0209  507  LYS B CB  
12975 N N   . VAL B 510  ? 0.5053 0.7193 0.5546 -0.0241 0.0703  0.0283  508  VAL B N   
12976 C CA  . VAL B 510  ? 0.4560 0.6695 0.5061 -0.0322 0.0676  0.0311  508  VAL B CA  
12977 C C   . VAL B 510  ? 0.4521 0.6708 0.5018 -0.0369 0.0704  0.0338  508  VAL B C   
12978 O O   . VAL B 510  ? 0.4506 0.6666 0.4934 -0.0369 0.0736  0.0342  508  VAL B O   
12979 C CB  . VAL B 510  ? 0.4395 0.6420 0.4817 -0.0354 0.0653  0.0313  508  VAL B CB  
12980 C CG1 . VAL B 510  ? 0.4006 0.6015 0.4429 -0.0440 0.0624  0.0342  508  VAL B CG1 
12981 C CG2 . VAL B 510  ? 0.4001 0.5980 0.4430 -0.0306 0.0627  0.0285  508  VAL B CG2 
12982 N N   . SER B 511  ? 0.4141 0.6402 0.4709 -0.0410 0.0690  0.0357  509  SER B N   
12983 C CA  . SER B 511  ? 0.3799 0.6121 0.4375 -0.0455 0.0717  0.0383  509  SER B CA  
12984 C C   . SER B 511  ? 0.4138 0.6389 0.4645 -0.0536 0.0705  0.0409  509  SER B C   
12985 O O   . SER B 511  ? 0.4071 0.6239 0.4543 -0.0565 0.0669  0.0410  509  SER B O   
12986 C CB  . SER B 511  ? 0.4334 0.6765 0.5011 -0.0468 0.0706  0.0392  509  SER B CB  
12987 O OG  . SER B 511  ? 0.4885 0.7295 0.5581 -0.0530 0.0662  0.0407  509  SER B OG  
12988 N N   . ILE B 512  ? 0.3610 0.5892 0.4095 -0.0572 0.0736  0.0432  510  ILE B N   
12989 C CA  . ILE B 512  ? 0.4081 0.6298 0.4505 -0.0654 0.0724  0.0461  510  ILE B CA  
12990 C C   . ILE B 512  ? 0.4495 0.6725 0.4972 -0.0712 0.0680  0.0475  510  ILE B C   
12991 O O   . ILE B 512  ? 0.4030 0.6170 0.4455 -0.0769 0.0648  0.0489  510  ILE B O   
12992 C CB  . ILE B 512  ? 0.4249 0.6503 0.4644 -0.0679 0.0768  0.0482  510  ILE B CB  
12993 C CG1 . ILE B 512  ? 0.4349 0.6569 0.4674 -0.0622 0.0808  0.0466  510  ILE B CG1 
12994 C CG2 . ILE B 512  ? 0.4019 0.6203 0.4351 -0.0767 0.0753  0.0514  510  ILE B CG2 
12995 C CD1 . ILE B 512  ? 0.4660 0.6901 0.4940 -0.0645 0.0853  0.0486  510  ILE B CD1 
12996 N N   . ASP B 513  ? 0.4020 0.6355 0.4597 -0.0697 0.0674  0.0471  511  ASP B N   
12997 C CA  . ASP B 513  ? 0.4459 0.6807 0.5087 -0.0746 0.0629  0.0481  511  ASP B CA  
12998 C C   . ASP B 513  ? 0.4296 0.6548 0.4896 -0.0744 0.0586  0.0467  511  ASP B C   
12999 O O   . ASP B 513  ? 0.3994 0.6181 0.4568 -0.0806 0.0549  0.0480  511  ASP B O   
13000 C CB  . ASP B 513  ? 0.4719 0.7194 0.5455 -0.0715 0.0630  0.0475  511  ASP B CB  
13001 C CG  . ASP B 513  ? 0.5319 0.7894 0.6095 -0.0749 0.0658  0.0498  511  ASP B CG  
13002 O OD1 . ASP B 513  ? 0.5672 0.8217 0.6407 -0.0821 0.0658  0.0523  511  ASP B OD1 
13003 O OD2 . ASP B 513  ? 0.5568 0.8251 0.6417 -0.0705 0.0680  0.0490  511  ASP B OD2 
13004 N N   . GLU B 514  ? 0.3894 0.6131 0.4497 -0.0672 0.0588  0.0439  512  GLU B N   
13005 C CA  . GLU B 514  ? 0.3954 0.6105 0.4534 -0.0666 0.0550  0.0424  512  GLU B CA  
13006 C C   . GLU B 514  ? 0.3902 0.5930 0.4378 -0.0709 0.0542  0.0434  512  GLU B C   
13007 O O   . GLU B 514  ? 0.3758 0.5710 0.4211 -0.0744 0.0503  0.0435  512  GLU B O   
13008 C CB  . GLU B 514  ? 0.4362 0.6521 0.4961 -0.0579 0.0559  0.0392  512  GLU B CB  
13009 C CG  . GLU B 514  ? 0.4504 0.6770 0.5197 -0.0530 0.0563  0.0381  512  GLU B CG  
13010 C CD  . GLU B 514  ? 0.5051 0.7311 0.5753 -0.0443 0.0574  0.0350  512  GLU B CD  
13011 O OE1 . GLU B 514  ? 0.6134 0.8337 0.6829 -0.0425 0.0544  0.0334  512  GLU B OE1 
13012 O OE2 . GLU B 514  ? 0.5167 0.7478 0.5880 -0.0393 0.0610  0.0341  512  GLU B OE2 
13013 N N   . LEU B 515  ? 0.3699 0.5703 0.4110 -0.0708 0.0578  0.0442  513  LEU B N   
13014 C CA  . LEU B 515  ? 0.3486 0.5367 0.3790 -0.0743 0.0571  0.0452  513  LEU B CA  
13015 C C   . LEU B 515  ? 0.3808 0.5638 0.4078 -0.0832 0.0548  0.0483  513  LEU B C   
13016 O O   . LEU B 515  ? 0.3673 0.5385 0.3862 -0.0868 0.0523  0.0490  513  LEU B O   
13017 C CB  . LEU B 515  ? 0.3099 0.4966 0.3336 -0.0712 0.0615  0.0450  513  LEU B CB  
13018 C CG  . LEU B 515  ? 0.3280 0.5151 0.3516 -0.0627 0.0632  0.0417  513  LEU B CG  
13019 C CD1 . LEU B 515  ? 0.3527 0.5406 0.3709 -0.0594 0.0680  0.0415  513  LEU B CD1 
13020 C CD2 . LEU B 515  ? 0.3505 0.5252 0.3680 -0.0616 0.0596  0.0401  513  LEU B CD2 
13021 N N   . ILE B 516  ? 0.3342 0.5253 0.3667 -0.0868 0.0553  0.0500  514  ILE B N   
13022 C CA  . ILE B 516  ? 0.3184 0.5049 0.3478 -0.0953 0.0531  0.0529  514  ILE B CA  
13023 C C   . ILE B 516  ? 0.3373 0.5246 0.3725 -0.0985 0.0484  0.0527  514  ILE B C   
13024 O O   . ILE B 516  ? 0.3746 0.5588 0.4083 -0.1055 0.0461  0.0549  514  ILE B O   
13025 C CB  . ILE B 516  ? 0.3816 0.5755 0.4122 -0.0982 0.0566  0.0552  514  ILE B CB  
13026 C CG1 . ILE B 516  ? 0.3662 0.5749 0.4085 -0.0964 0.0576  0.0548  514  ILE B CG1 
13027 C CG2 . ILE B 516  ? 0.4171 0.6104 0.4420 -0.0946 0.0614  0.0552  514  ILE B CG2 
13028 C CD1 . ILE B 516  ? 0.4591 0.6760 0.5034 -0.0997 0.0610  0.0572  514  ILE B CD1 
13029 N N   . ALA B 517  ? 0.3393 0.5303 0.3805 -0.0935 0.0468  0.0503  515  ALA B N   
13030 C CA  . ALA B 517  ? 0.3778 0.5682 0.4234 -0.0962 0.0421  0.0499  515  ALA B CA  
13031 C C   . ALA B 517  ? 0.3504 0.5267 0.3879 -0.1020 0.0382  0.0508  515  ALA B C   
13032 O O   . ALA B 517  ? 0.3545 0.5208 0.3841 -0.1012 0.0383  0.0504  515  ALA B O   
13033 C CB  . ALA B 517  ? 0.3507 0.5450 0.4023 -0.0893 0.0411  0.0469  515  ALA B CB  
13034 N N   . ASP B 518  ? 0.3237 0.4985 0.3625 -0.1079 0.0346  0.0519  516  ASP B N   
13035 C CA  . ASP B 518  ? 0.3326 0.4932 0.3633 -0.1139 0.0306  0.0529  516  ASP B CA  
13036 C C   . ASP B 518  ? 0.3227 0.4775 0.3539 -0.1118 0.0267  0.0505  516  ASP B C   
13037 O O   . ASP B 518  ? 0.2958 0.4560 0.3337 -0.1115 0.0243  0.0495  516  ASP B O   
13038 C CB  . ASP B 518  ? 0.3103 0.4715 0.3417 -0.1212 0.0285  0.0551  516  ASP B CB  
13039 C CG  . ASP B 518  ? 0.3966 0.5419 0.4185 -0.1274 0.0245  0.0561  516  ASP B CG  
13040 O OD1 . ASP B 518  ? 0.3372 0.4711 0.3528 -0.1260 0.0228  0.0550  516  ASP B OD1 
13041 O OD2 . ASP B 518  ? 0.3992 0.5430 0.4198 -0.1337 0.0230  0.0581  516  ASP B OD2 
13042 N N   . PRO B 519  ? 0.2836 0.4275 0.3079 -0.1103 0.0260  0.0496  517  PRO B N   
13043 C CA  . PRO B 519  ? 0.3167 0.4534 0.3411 -0.1070 0.0219  0.0467  517  PRO B CA  
13044 C C   . PRO B 519  ? 0.3236 0.4556 0.3478 -0.1132 0.0172  0.0473  517  PRO B C   
13045 O O   . PRO B 519  ? 0.3002 0.4326 0.3284 -0.1107 0.0143  0.0451  517  PRO B O   
13046 C CB  . PRO B 519  ? 0.3242 0.4448 0.3384 -0.1029 0.0210  0.0449  517  PRO B CB  
13047 C CG  . PRO B 519  ? 0.3124 0.4354 0.3230 -0.1030 0.0255  0.0468  517  PRO B CG  
13048 C CD  . PRO B 519  ? 0.3086 0.4434 0.3234 -0.1101 0.0280  0.0505  517  PRO B CD  
13049 N N   . VAL B 520  ? 0.2991 0.4254 0.3181 -0.1204 0.0161  0.0498  518  VAL B N   
13050 C CA  . VAL B 520  ? 0.2904 0.4093 0.3074 -0.1257 0.0112  0.0499  518  VAL B CA  
13051 C C   . VAL B 520  ? 0.3352 0.4663 0.3619 -0.1255 0.0102  0.0494  518  VAL B C   
13052 O O   . VAL B 520  ? 0.3203 0.4487 0.3484 -0.1259 0.0063  0.0478  518  VAL B O   
13053 C CB  . VAL B 520  ? 0.3420 0.4514 0.3508 -0.1325 0.0103  0.0525  518  VAL B CB  
13054 C CG1 . VAL B 520  ? 0.3358 0.4368 0.3420 -0.1377 0.0051  0.0524  518  VAL B CG1 
13055 C CG2 . VAL B 520  ? 0.3382 0.4347 0.3368 -0.1323 0.0111  0.0532  518  VAL B CG2 
13056 N N   . GLU B 521  ? 0.3166 0.4611 0.3497 -0.1246 0.0137  0.0506  519  GLU B N   
13057 C CA  . GLU B 521  ? 0.3036 0.4600 0.3457 -0.1244 0.0128  0.0503  519  GLU B CA  
13058 C C   . GLU B 521  ? 0.3394 0.5033 0.3886 -0.1171 0.0131  0.0477  519  GLU B C   
13059 O O   . GLU B 521  ? 0.3572 0.5265 0.4121 -0.1167 0.0107  0.0469  519  GLU B O   
13060 C CB  . GLU B 521  ? 0.3545 0.5226 0.4011 -0.1259 0.0164  0.0525  519  GLU B CB  
13061 C CG  . GLU B 521  ? 0.3552 0.5171 0.3957 -0.1335 0.0159  0.0552  519  GLU B CG  
13062 C CD  . GLU B 521  ? 0.4178 0.5714 0.4553 -0.1394 0.0106  0.0553  519  GLU B CD  
13063 O OE1 . GLU B 521  ? 0.4275 0.5866 0.4709 -0.1387 0.0081  0.0541  519  GLU B OE1 
13064 O OE2 . GLU B 521  ? 0.4620 0.6031 0.4907 -0.1446 0.0088  0.0566  519  GLU B OE2 
13065 N N   . VAL B 522  ? 0.3444 0.5085 0.3931 -0.1114 0.0159  0.0465  520  VAL B N   
13066 C CA  . VAL B 522  ? 0.3075 0.4773 0.3621 -0.1045 0.0160  0.0440  520  VAL B CA  
13067 C C   . VAL B 522  ? 0.3474 0.5080 0.3996 -0.1051 0.0113  0.0422  520  VAL B C   
13068 O O   . VAL B 522  ? 0.3415 0.5068 0.3991 -0.1029 0.0091  0.0409  520  VAL B O   
13069 C CB  . VAL B 522  ? 0.2975 0.4687 0.3513 -0.0983 0.0201  0.0431  520  VAL B CB  
13070 C CG1 . VAL B 522  ? 0.3329 0.5086 0.3921 -0.0912 0.0198  0.0404  520  VAL B CG1 
13071 C CG2 . VAL B 522  ? 0.3670 0.5476 0.4232 -0.0973 0.0248  0.0446  520  VAL B CG2 
13072 N N   . VAL B 523  ? 0.2775 0.4245 0.3212 -0.1081 0.0095  0.0422  521  VAL B N   
13073 C CA  . VAL B 523  ? 0.2856 0.4211 0.3254 -0.1078 0.0048  0.0400  521  VAL B CA  
13074 C C   . VAL B 523  ? 0.3155 0.4523 0.3573 -0.1137 0.0010  0.0408  521  VAL B C   
13075 O O   . VAL B 523  ? 0.2892 0.4253 0.3332 -0.1123 -0.0021 0.0389  521  VAL B O   
13076 C CB  . VAL B 523  ? 0.2898 0.4072 0.3183 -0.1077 0.0033  0.0392  521  VAL B CB  
13077 C CG1 . VAL B 523  ? 0.2747 0.3796 0.2986 -0.1081 -0.0018 0.0371  521  VAL B CG1 
13078 C CG2 . VAL B 523  ? 0.2979 0.4122 0.3241 -0.0999 0.0061  0.0374  521  VAL B CG2 
13079 N N   . ARG B 524  ? 0.3056 0.4427 0.3457 -0.1193 0.0012  0.0432  522  ARG B N   
13080 C CA  . ARG B 524  ? 0.3175 0.4534 0.3578 -0.1243 -0.0026 0.0436  522  ARG B CA  
13081 C C   . ARG B 524  ? 0.3588 0.5071 0.4084 -0.1211 -0.0032 0.0426  522  ARG B C   
13082 O O   . ARG B 524  ? 0.3642 0.5099 0.4139 -0.1230 -0.0071 0.0417  522  ARG B O   
13083 C CB  . ARG B 524  ? 0.3001 0.4361 0.3379 -0.1305 -0.0018 0.0465  522  ARG B CB  
13084 C CG  . ARG B 524  ? 0.3619 0.4940 0.3981 -0.1366 -0.0060 0.0470  522  ARG B CG  
13085 C CD  . ARG B 524  ? 0.3883 0.5248 0.4247 -0.1423 -0.0047 0.0500  522  ARG B CD  
13086 N NE  . ARG B 524  ? 0.4160 0.5447 0.4451 -0.1448 -0.0026 0.0517  522  ARG B NE  
13087 C CZ  . ARG B 524  ? 0.3774 0.4901 0.3965 -0.1490 -0.0053 0.0521  522  ARG B CZ  
13088 N NH1 . ARG B 524  ? 0.4119 0.5144 0.4268 -0.1509 -0.0101 0.0506  522  ARG B NH1 
13089 N NH2 . ARG B 524  ? 0.4095 0.5159 0.4221 -0.1509 -0.0032 0.0539  522  ARG B NH2 
13090 N N   . ALA B 525  ? 0.3319 0.4931 0.3888 -0.1161 0.0007  0.0427  523  ALA B N   
13091 C CA  . ALA B 525  ? 0.3304 0.5039 0.3960 -0.1131 0.0004  0.0422  523  ALA B CA  
13092 C C   . ALA B 525  ? 0.3580 0.5328 0.4268 -0.1064 -0.0003 0.0397  523  ALA B C   
13093 O O   . ALA B 525  ? 0.3883 0.5729 0.4641 -0.1031 -0.0005 0.0392  523  ALA B O   
13094 C CB  . ALA B 525  ? 0.2897 0.4765 0.3615 -0.1113 0.0049  0.0438  523  ALA B CB  
13095 N N   . MET B 526  ? 0.3324 0.4977 0.3962 -0.1044 -0.0009 0.0381  524  MET B N   
13096 C CA  A MET B 526  ? 0.3524 0.5185 0.4189 -0.0983 -0.0017 0.0356  524  MET B CA  
13097 C CA  B MET B 526  ? 0.3523 0.5186 0.4189 -0.0982 -0.0016 0.0357  524  MET B CA  
13098 C C   . MET B 526  ? 0.3534 0.5166 0.4200 -0.0999 -0.0064 0.0345  524  MET B C   
13099 O O   . MET B 526  ? 0.2973 0.4525 0.3589 -0.1059 -0.0096 0.0350  524  MET B O   
13100 C CB  A MET B 526  ? 0.3477 0.5043 0.4087 -0.0963 -0.0011 0.0343  524  MET B CB  
13101 C CB  B MET B 526  ? 0.3476 0.5047 0.4089 -0.0960 -0.0009 0.0343  524  MET B CB  
13102 C CG  A MET B 526  ? 0.3659 0.5248 0.4263 -0.0926 0.0037  0.0348  524  MET B CG  
13103 C CG  B MET B 526  ? 0.3635 0.5221 0.4234 -0.0940 0.0037  0.0353  524  MET B CG  
13104 S SD  A MET B 526  ? 0.4241 0.5986 0.4942 -0.0850 0.0074  0.0343  524  MET B SD  
13105 S SD  B MET B 526  ? 0.3661 0.5108 0.4184 -0.0863 0.0046  0.0323  524  MET B SD  
13106 C CE  A MET B 526  ? 0.3633 0.5320 0.4332 -0.0782 0.0049  0.0308  524  MET B CE  
13107 C CE  B MET B 526  ? 0.3669 0.5204 0.4266 -0.0776 0.0058  0.0301  524  MET B CE  
13108 N N   . PRO B 527  ? 0.3707 0.5397 0.4425 -0.0946 -0.0071 0.0330  525  PRO B N   
13109 C CA  . PRO B 527  ? 0.3830 0.5493 0.4546 -0.0960 -0.0116 0.0319  525  PRO B CA  
13110 C C   . PRO B 527  ? 0.3498 0.5019 0.4135 -0.0986 -0.0150 0.0303  525  PRO B C   
13111 O O   . PRO B 527  ? 0.3302 0.4767 0.3908 -0.1026 -0.0189 0.0300  525  PRO B O   
13112 C CB  . PRO B 527  ? 0.4027 0.5771 0.4806 -0.0889 -0.0109 0.0305  525  PRO B CB  
13113 C CG  . PRO B 527  ? 0.3812 0.5570 0.4598 -0.0837 -0.0070 0.0300  525  PRO B CG  
13114 C CD  . PRO B 527  ? 0.3915 0.5683 0.4686 -0.0870 -0.0039 0.0320  525  PRO B CD  
13115 N N   . VAL B 528  ? 0.3535 0.4988 0.4135 -0.0958 -0.0137 0.0291  526  VAL B N   
13116 C CA  . VAL B 528  ? 0.2996 0.4277 0.3500 -0.0957 -0.0163 0.0270  526  VAL B CA  
13117 C C   . VAL B 528  ? 0.2787 0.3988 0.3232 -0.0963 -0.0140 0.0277  526  VAL B C   
13118 O O   . VAL B 528  ? 0.3174 0.4375 0.3619 -0.0906 -0.0109 0.0269  526  VAL B O   
13119 C CB  . VAL B 528  ? 0.3179 0.4408 0.3670 -0.0884 -0.0170 0.0239  526  VAL B CB  
13120 C CG1 . VAL B 528  ? 0.3126 0.4183 0.3520 -0.0877 -0.0191 0.0218  526  VAL B CG1 
13121 C CG2 . VAL B 528  ? 0.3259 0.4556 0.3798 -0.0883 -0.0197 0.0234  526  VAL B CG2 
13122 N N   . VAL B 529  ? 0.2754 0.3886 0.3146 -0.1032 -0.0156 0.0292  527  VAL B N   
13123 C CA  . VAL B 529  ? 0.2424 0.3478 0.2754 -0.1043 -0.0136 0.0302  527  VAL B CA  
13124 C C   . VAL B 529  ? 0.2521 0.3437 0.2781 -0.0984 -0.0141 0.0274  527  VAL B C   
13125 O O   . VAL B 529  ? 0.2658 0.3472 0.2870 -0.0978 -0.0175 0.0253  527  VAL B O   
13126 C CB  . VAL B 529  ? 0.2829 0.3825 0.3111 -0.1132 -0.0158 0.0324  527  VAL B CB  
13127 C CG1 . VAL B 529  ? 0.2680 0.3571 0.2883 -0.1139 -0.0142 0.0333  527  VAL B CG1 
13128 C CG2 . VAL B 529  ? 0.2905 0.4046 0.3259 -0.1186 -0.0147 0.0353  527  VAL B CG2 
13129 N N   . GLY B 530  ? 0.2481 0.3396 0.2733 -0.0940 -0.0107 0.0273  528  GLY B N   
13130 C CA  . GLY B 530  ? 0.2369 0.3160 0.2557 -0.0887 -0.0111 0.0249  528  GLY B CA  
13131 C C   . GLY B 530  ? 0.2280 0.3081 0.2497 -0.0814 -0.0111 0.0220  528  GLY B C   
13132 O O   . GLY B 530  ? 0.2302 0.2996 0.2466 -0.0776 -0.0122 0.0198  528  GLY B O   
13133 N N   . ALA B 531  ? 0.2002 0.2927 0.2299 -0.0793 -0.0100 0.0220  529  ALA B N   
13134 C CA  . ALA B 531  ? 0.2238 0.3167 0.2558 -0.0726 -0.0100 0.0195  529  ALA B CA  
13135 C C   . ALA B 531  ? 0.1989 0.2887 0.2292 -0.0666 -0.0073 0.0183  529  ALA B C   
13136 O O   . ALA B 531  ? 0.2156 0.3092 0.2465 -0.0667 -0.0043 0.0197  529  ALA B O   
13137 C CB  . ALA B 531  ? 0.2391 0.3462 0.2800 -0.0714 -0.0092 0.0200  529  ALA B CB  
13138 N N   . LYS B 532  ? 0.2047 0.2875 0.2327 -0.0617 -0.0084 0.0157  530  LYS B N   
13139 C CA  . LYS B 532  ? 0.1833 0.2631 0.2101 -0.0559 -0.0063 0.0142  530  LYS B CA  
13140 C C   . LYS B 532  ? 0.2031 0.2947 0.2366 -0.0525 -0.0029 0.0148  530  LYS B C   
13141 O O   . LYS B 532  ? 0.1890 0.2905 0.2287 -0.0527 -0.0026 0.0155  530  LYS B O   
13142 C CB  . LYS B 532  ? 0.2035 0.2761 0.2283 -0.0516 -0.0081 0.0114  530  LYS B CB  
13143 C CG  . LYS B 532  ? 0.2572 0.3279 0.2819 -0.0453 -0.0063 0.0096  530  LYS B CG  
13144 C CD  . LYS B 532  ? 0.2535 0.3189 0.2773 -0.0418 -0.0082 0.0071  530  LYS B CD  
13145 C CE  . LYS B 532  ? 0.2022 0.2756 0.2316 -0.0405 -0.0083 0.0069  530  LYS B CE  
13146 N NZ  . LYS B 532  ? 0.2172 0.2998 0.2523 -0.0370 -0.0054 0.0074  530  LYS B NZ  
13147 N N   . HIS B 533  ? 0.1706 0.2608 0.2025 -0.0493 -0.0004 0.0145  531  HIS B N   
13148 C CA  . HIS B 533  ? 0.1596 0.2591 0.1968 -0.0451 0.0028  0.0145  531  HIS B CA  
13149 C C   . HIS B 533  ? 0.1740 0.2765 0.2154 -0.0408 0.0021  0.0128  531  HIS B C   
13150 O O   . HIS B 533  ? 0.1814 0.2763 0.2201 -0.0386 0.0002  0.0109  531  HIS B O   
13151 C CB  . HIS B 533  ? 0.1707 0.2651 0.2039 -0.0418 0.0049  0.0137  531  HIS B CB  
13152 C CG  . HIS B 533  ? 0.1958 0.2991 0.2331 -0.0385 0.0085  0.0141  531  HIS B CG  
13153 N ND1 . HIS B 533  ? 0.1947 0.3036 0.2369 -0.0337 0.0095  0.0129  531  HIS B ND1 
13154 C CD2 . HIS B 533  ? 0.2774 0.3846 0.3140 -0.0392 0.0115  0.0155  531  HIS B CD2 
13155 C CE1 . HIS B 533  ? 0.2863 0.4020 0.3308 -0.0314 0.0128  0.0134  531  HIS B CE1 
13156 N NE2 . HIS B 533  ? 0.3481 0.4632 0.3894 -0.0347 0.0142  0.0149  531  HIS B NE2 
13157 N N   . ASP B 534  ? 0.1950 0.3090 0.2432 -0.0396 0.0036  0.0137  532  ASP B N   
13158 C CA  . ASP B 534  ? 0.2349 0.3520 0.2870 -0.0358 0.0028  0.0125  532  ASP B CA  
13159 C C   . ASP B 534  ? 0.2235 0.3358 0.2742 -0.0298 0.0039  0.0103  532  ASP B C   
13160 O O   . ASP B 534  ? 0.2437 0.3547 0.2955 -0.0269 0.0027  0.0090  532  ASP B O   
13161 C CB  . ASP B 534  ? 0.2061 0.3366 0.2657 -0.0352 0.0043  0.0140  532  ASP B CB  
13162 C CG  . ASP B 534  ? 0.4430 0.5795 0.5053 -0.0411 0.0026  0.0160  532  ASP B CG  
13163 O OD1 . ASP B 534  ? 0.4677 0.5987 0.5273 -0.0441 -0.0006 0.0155  532  ASP B OD1 
13164 O OD2 . ASP B 534  ? 0.5002 0.6469 0.5670 -0.0428 0.0046  0.0179  532  ASP B OD2 
13165 N N   . ARG B 535  ? 0.1754 0.2851 0.2235 -0.0280 0.0061  0.0100  533  ARG B N   
13166 C CA  . ARG B 535  ? 0.1863 0.2924 0.2334 -0.0225 0.0073  0.0081  533  ARG B CA  
13167 C C   . ARG B 535  ? 0.1786 0.2731 0.2195 -0.0220 0.0059  0.0065  533  ARG B C   
13168 O O   . ARG B 535  ? 0.2226 0.3136 0.2622 -0.0180 0.0068  0.0050  533  ARG B O   
13169 C CB  . ARG B 535  ? 0.2675 0.3790 0.3160 -0.0200 0.0107  0.0086  533  ARG B CB  
13170 C CG  . ARG B 535  ? 0.3108 0.4341 0.3661 -0.0185 0.0124  0.0097  533  ARG B CG  
13171 C CD  . ARG B 535  ? 0.4040 0.5319 0.4601 -0.0155 0.0160  0.0099  533  ARG B CD  
13172 N N   . ILE B 536  ? 0.1529 0.2413 0.1900 -0.0259 0.0036  0.0068  534  ILE B N   
13173 C CA  . ILE B 536  ? 0.1516 0.2292 0.1831 -0.0252 0.0020  0.0052  534  ILE B CA  
13174 C C   . ILE B 536  ? 0.1559 0.2295 0.1868 -0.0259 -0.0008 0.0042  534  ILE B C   
13175 O O   . ILE B 536  ? 0.1684 0.2428 0.1993 -0.0299 -0.0024 0.0052  534  ILE B O   
13176 C CB  . ILE B 536  ? 0.1638 0.2361 0.1901 -0.0287 0.0018  0.0063  534  ILE B CB  
13177 C CG1 . ILE B 536  ? 0.2054 0.2816 0.2317 -0.0276 0.0048  0.0072  534  ILE B CG1 
13178 C CG2 . ILE B 536  ? 0.1818 0.2429 0.2025 -0.0276 -0.0003 0.0046  534  ILE B CG2 
13179 C CD1 . ILE B 536  ? 0.2889 0.3612 0.3102 -0.0314 0.0050  0.0087  534  ILE B CD1 
13180 N N   . ALA B 537  ? 0.1578 0.2271 0.1882 -0.0222 -0.0014 0.0022  535  ALA B N   
13181 C CA  . ALA B 537  ? 0.1457 0.2115 0.1754 -0.0224 -0.0037 0.0011  535  ALA B CA  
13182 C C   . ALA B 537  ? 0.1337 0.1898 0.1576 -0.0243 -0.0059 0.0004  535  ALA B C   
13183 O O   . ALA B 537  ? 0.1509 0.2014 0.1715 -0.0228 -0.0057 -0.0004 535  ALA B O   
13184 C CB  . ALA B 537  ? 0.1536 0.2191 0.1851 -0.0178 -0.0033 -0.0006 535  ALA B CB  
13185 N N   . LEU B 538  ? 0.1488 0.2027 0.1711 -0.0273 -0.0081 0.0005  536  LEU B N   
13186 C CA  . LEU B 538  ? 0.1305 0.1746 0.1473 -0.0280 -0.0103 -0.0007 536  LEU B CA  
13187 C C   . LEU B 538  ? 0.1507 0.1910 0.1671 -0.0233 -0.0103 -0.0030 536  LEU B C   
13188 O O   . LEU B 538  ? 0.1574 0.2025 0.1777 -0.0206 -0.0093 -0.0036 536  LEU B O   
13189 C CB  . LEU B 538  ? 0.1591 0.2015 0.1744 -0.0314 -0.0127 -0.0007 536  LEU B CB  
13190 C CG  . LEU B 538  ? 0.1771 0.2209 0.1914 -0.0369 -0.0135 0.0015  536  LEU B CG  
13191 C CD1 . LEU B 538  ? 0.2390 0.2822 0.2526 -0.0398 -0.0160 0.0013  536  LEU B CD1 
13192 C CD2 . LEU B 538  ? 0.1871 0.2226 0.1955 -0.0390 -0.0142 0.0020  536  LEU B CD2 
13193 N N   . PRO B 539  ? 0.1418 0.1738 0.1537 -0.0223 -0.0114 -0.0042 537  PRO B N   
13194 C CA  . PRO B 539  ? 0.1339 0.1632 0.1460 -0.0179 -0.0113 -0.0063 537  PRO B CA  
13195 C C   . PRO B 539  ? 0.1493 0.1803 0.1632 -0.0168 -0.0118 -0.0075 537  PRO B C   
13196 O O   . PRO B 539  ? 0.1479 0.1814 0.1647 -0.0135 -0.0106 -0.0084 537  PRO B O   
13197 C CB  . PRO B 539  ? 0.1475 0.1676 0.1541 -0.0178 -0.0130 -0.0072 537  PRO B CB  
13198 C CG  . PRO B 539  ? 0.1629 0.1818 0.1670 -0.0212 -0.0130 -0.0053 537  PRO B CG  
13199 C CD  . PRO B 539  ? 0.1599 0.1851 0.1665 -0.0248 -0.0126 -0.0035 537  PRO B CD  
13200 N N   . ALA B 540  ? 0.1574 0.1869 0.1695 -0.0196 -0.0135 -0.0073 538  ALA B N   
13201 C CA  . ALA B 540  ? 0.1608 0.1916 0.1739 -0.0186 -0.0140 -0.0083 538  ALA B CA  
13202 C C   . ALA B 540  ? 0.2159 0.2555 0.2344 -0.0176 -0.0125 -0.0074 538  ALA B C   
13203 O O   . ALA B 540  ? 0.1939 0.2349 0.2137 -0.0157 -0.0124 -0.0083 538  ALA B O   
13204 C CB  . ALA B 540  ? 0.2027 0.2301 0.2123 -0.0221 -0.0164 -0.0083 538  ALA B CB  
13205 N N   . GLU B 541  ? 0.1626 0.2081 0.1842 -0.0189 -0.0112 -0.0056 539  GLU B N   
13206 C CA  . GLU B 541  ? 0.1742 0.2281 0.2009 -0.0181 -0.0100 -0.0046 539  GLU B CA  
13207 C C   . GLU B 541  ? 0.1448 0.2020 0.1746 -0.0147 -0.0076 -0.0046 539  GLU B C   
13208 O O   . GLU B 541  ? 0.1706 0.2347 0.2044 -0.0139 -0.0063 -0.0035 539  GLU B O   
13209 C CB  . GLU B 541  ? 0.2007 0.2599 0.2289 -0.0221 -0.0105 -0.0026 539  GLU B CB  
13210 C CG  . GLU B 541  ? 0.2436 0.2988 0.2683 -0.0258 -0.0132 -0.0027 539  GLU B CG  
13211 C CD  . GLU B 541  ? 0.3341 0.3943 0.3603 -0.0305 -0.0141 -0.0007 539  GLU B CD  
13212 O OE1 . GLU B 541  ? 0.3485 0.4161 0.3787 -0.0310 -0.0125 0.0010  539  GLU B OE1 
13213 O OE2 . GLU B 541  ? 0.3637 0.4205 0.3868 -0.0338 -0.0165 -0.0008 539  GLU B OE2 
13214 N N   . LEU B 542  ? 0.1328 0.1848 0.1605 -0.0124 -0.0071 -0.0059 540  LEU B N   
13215 C CA  . LEU B 542  ? 0.1601 0.2142 0.1901 -0.0094 -0.0051 -0.0061 540  LEU B CA  
13216 C C   . LEU B 542  ? 0.1681 0.2268 0.2018 -0.0068 -0.0040 -0.0062 540  LEU B C   
13217 O O   . LEU B 542  ? 0.1899 0.2522 0.2261 -0.0049 -0.0023 -0.0058 540  LEU B O   
13218 C CB  . LEU B 542  ? 0.2171 0.2649 0.2446 -0.0073 -0.0053 -0.0078 540  LEU B CB  
13219 C CG  . LEU B 542  ? 0.2487 0.2921 0.2729 -0.0081 -0.0056 -0.0078 540  LEU B CG  
13220 C CD1 . LEU B 542  ? 0.1586 0.1980 0.1819 -0.0051 -0.0056 -0.0094 540  LEU B CD1 
13221 C CD2 . LEU B 542  ? 0.1867 0.2344 0.2120 -0.0092 -0.0041 -0.0062 540  LEU B CD2 
13222 N N   . PHE B 543  ? 0.1458 0.2040 0.1795 -0.0066 -0.0050 -0.0068 541  PHE B N   
13223 C CA  . PHE B 543  ? 0.1476 0.2090 0.1841 -0.0041 -0.0042 -0.0068 541  PHE B CA  
13224 C C   . PHE B 543  ? 0.1472 0.2143 0.1859 -0.0054 -0.0048 -0.0054 541  PHE B C   
13225 O O   . PHE B 543  ? 0.1777 0.2473 0.2182 -0.0036 -0.0045 -0.0052 541  PHE B O   
13226 C CB  . PHE B 543  ? 0.1481 0.2051 0.1829 -0.0026 -0.0047 -0.0085 541  PHE B CB  
13227 C CG  . PHE B 543  ? 0.1562 0.2080 0.1890 -0.0015 -0.0045 -0.0098 541  PHE B CG  
13228 C CD1 . PHE B 543  ? 0.1837 0.2360 0.2178 0.0001  -0.0032 -0.0099 541  PHE B CD1 
13229 C CD2 . PHE B 543  ? 0.1296 0.1762 0.1592 -0.0021 -0.0058 -0.0111 541  PHE B CD2 
13230 C CE1 . PHE B 543  ? 0.1590 0.2069 0.1915 0.0010  -0.0033 -0.0112 541  PHE B CE1 
13231 C CE2 . PHE B 543  ? 0.1606 0.2029 0.1888 -0.0008 -0.0059 -0.0123 541  PHE B CE2 
13232 C CZ  . PHE B 543  ? 0.1802 0.2234 0.2099 0.0006  -0.0047 -0.0123 541  PHE B CZ  
13233 N N   . GLY B 544  ? 0.1546 0.2241 0.1933 -0.0085 -0.0056 -0.0043 542  GLY B N   
13234 C CA  . GLY B 544  ? 0.1591 0.2349 0.2004 -0.0099 -0.0063 -0.0028 542  GLY B CA  
13235 C C   . GLY B 544  ? 0.1839 0.2587 0.2241 -0.0099 -0.0079 -0.0032 542  GLY B C   
13236 O O   . GLY B 544  ? 0.2053 0.2744 0.2417 -0.0109 -0.0092 -0.0045 542  GLY B O   
13237 N N   . ASP B 545  ? 0.2137 0.2942 0.2570 -0.0086 -0.0078 -0.0022 543  ASP B N   
13238 C CA  . ASP B 545  ? 0.2186 0.2990 0.2608 -0.0089 -0.0094 -0.0023 543  ASP B CA  
13239 C C   . ASP B 545  ? 0.2092 0.2843 0.2490 -0.0064 -0.0089 -0.0039 543  ASP B C   
13240 O O   . ASP B 545  ? 0.2434 0.3168 0.2808 -0.0068 -0.0102 -0.0043 543  ASP B O   
13241 C CB  . ASP B 545  ? 0.2515 0.3395 0.2977 -0.0078 -0.0096 -0.0007 543  ASP B CB  
13242 C CG  . ASP B 545  ? 0.4120 0.5068 0.4613 -0.0106 -0.0103 0.0010  543  ASP B CG  
13243 O OD1 . ASP B 545  ? 0.3996 0.4926 0.4471 -0.0142 -0.0113 0.0009  543  ASP B OD1 
13244 O OD2 . ASP B 545  ? 0.5315 0.6334 0.5850 -0.0091 -0.0100 0.0024  543  ASP B OD2 
13245 N N   . ALA B 546  ? 0.1969 0.2694 0.2369 -0.0040 -0.0071 -0.0047 544  ALA B N   
13246 C CA  . ALA B 546  ? 0.1954 0.2642 0.2341 -0.0016 -0.0064 -0.0058 544  ALA B CA  
13247 C C   . ALA B 546  ? 0.2037 0.2666 0.2382 -0.0027 -0.0074 -0.0075 544  ALA B C   
13248 O O   . ALA B 546  ? 0.1898 0.2510 0.2225 -0.0019 -0.0076 -0.0081 544  ALA B O   
13249 C CB  . ALA B 546  ? 0.1850 0.2526 0.2250 0.0008  -0.0044 -0.0063 544  ALA B CB  
13250 N N   . ARG B 547  ? 0.1492 0.2089 0.1819 -0.0043 -0.0079 -0.0082 545  ARG B N   
13251 C CA  . ARG B 547  ? 0.1594 0.2130 0.1880 -0.0048 -0.0089 -0.0099 545  ARG B CA  
13252 C C   . ARG B 547  ? 0.1588 0.2095 0.1855 -0.0070 -0.0098 -0.0100 545  ARG B C   
13253 O O   . ARG B 547  ? 0.1548 0.2078 0.1834 -0.0077 -0.0092 -0.0090 545  ARG B O   
13254 C CB  . ARG B 547  ? 0.2032 0.2537 0.2314 -0.0020 -0.0075 -0.0113 545  ARG B CB  
13255 C CG  . ARG B 547  ? 0.1925 0.2430 0.2228 -0.0007 -0.0062 -0.0114 545  ARG B CG  
13256 C CD  . ARG B 547  ? 0.2338 0.2818 0.2641 0.0017  -0.0051 -0.0128 545  ARG B CD  
13257 N NE  . ARG B 547  ? 0.2409 0.2895 0.2734 0.0030  -0.0039 -0.0128 545  ARG B NE  
13258 C CZ  . ARG B 547  ? 0.1995 0.2451 0.2314 0.0035  -0.0040 -0.0137 545  ARG B CZ  
13259 N NH1 . ARG B 547  ? 0.1699 0.2114 0.1989 0.0031  -0.0051 -0.0149 545  ARG B NH1 
13260 N NH2 . ARG B 547  ? 0.2150 0.2615 0.2487 0.0045  -0.0030 -0.0135 545  ARG B NH2 
13261 N N   . THR B 548  ? 0.1397 0.1848 0.1622 -0.0080 -0.0112 -0.0113 546  THR B N   
13262 C CA  . THR B 548  ? 0.1243 0.1650 0.1439 -0.0101 -0.0124 -0.0116 546  THR B CA  
13263 C C   . THR B 548  ? 0.1157 0.1520 0.1344 -0.0078 -0.0116 -0.0129 546  THR B C   
13264 O O   . THR B 548  ? 0.1332 0.1670 0.1510 -0.0054 -0.0112 -0.0144 546  THR B O   
13265 C CB  . THR B 548  ? 0.1312 0.1673 0.1461 -0.0122 -0.0146 -0.0124 546  THR B CB  
13266 O OG1 . THR B 548  ? 0.2000 0.2407 0.2160 -0.0145 -0.0156 -0.0111 546  THR B OG1 
13267 C CG2 . THR B 548  ? 0.1646 0.1949 0.1759 -0.0145 -0.0160 -0.0126 546  THR B CG2 
13268 N N   . ASN B 549  ? 0.1294 0.1651 0.1484 -0.0085 -0.0114 -0.0122 547  ASN B N   
13269 C CA  . ASN B 549  ? 0.1163 0.1479 0.1343 -0.0064 -0.0110 -0.0133 547  ASN B CA  
13270 C C   . ASN B 549  ? 0.1369 0.1613 0.1501 -0.0065 -0.0126 -0.0149 547  ASN B C   
13271 O O   . ASN B 549  ? 0.1638 0.1852 0.1737 -0.0090 -0.0143 -0.0147 547  ASN B O   
13272 C CB  . ASN B 549  ? 0.1267 0.1590 0.1452 -0.0075 -0.0105 -0.0121 547  ASN B CB  
13273 C CG  . ASN B 549  ? 0.1169 0.1462 0.1350 -0.0052 -0.0101 -0.0130 547  ASN B CG  
13274 O OD1 . ASN B 549  ? 0.1437 0.1719 0.1625 -0.0025 -0.0097 -0.0145 547  ASN B OD1 
13275 N ND2 . ASN B 549  ? 0.1332 0.1616 0.1503 -0.0063 -0.0100 -0.0121 547  ASN B ND2 
13276 N N   . SER B 550  ? 0.1184 0.1400 0.1312 -0.0035 -0.0123 -0.0165 548  SER B N   
13277 C CA  . SER B 550  ? 0.1438 0.1583 0.1521 -0.0029 -0.0138 -0.0180 548  SER B CA  
13278 C C   . SER B 550  ? 0.1685 0.1783 0.1736 -0.0048 -0.0152 -0.0173 548  SER B C   
13279 O O   . SER B 550  ? 0.1543 0.1664 0.1611 -0.0057 -0.0145 -0.0159 548  SER B O   
13280 C CB  . SER B 550  ? 0.1390 0.1524 0.1482 0.0009  -0.0131 -0.0198 548  SER B CB  
13281 O OG  . SER B 550  ? 0.1443 0.1594 0.1561 0.0020  -0.0123 -0.0194 548  SER B OG  
13282 N N   . ALA B 551  ? 0.1648 0.1677 0.1649 -0.0056 -0.0171 -0.0182 549  ALA B N   
13283 C CA  . ALA B 551  ? 0.1815 0.1785 0.1776 -0.0075 -0.0187 -0.0174 549  ALA B CA  
13284 C C   . ALA B 551  ? 0.1950 0.1860 0.1885 -0.0043 -0.0195 -0.0190 549  ALA B C   
13285 O O   . ALA B 551  ? 0.1818 0.1707 0.1745 -0.0014 -0.0196 -0.0210 549  ALA B O   
13286 C CB  . ALA B 551  ? 0.1848 0.1773 0.1763 -0.0110 -0.0206 -0.0171 549  ALA B CB  
13287 N N   . GLY B 552  ? 0.1930 0.1814 0.1852 -0.0047 -0.0200 -0.0180 550  GLY B N   
13288 C CA  . GLY B 552  ? 0.1887 0.1709 0.1780 -0.0019 -0.0212 -0.0192 550  GLY B CA  
13289 C C   . GLY B 552  ? 0.1843 0.1572 0.1668 -0.0036 -0.0236 -0.0191 550  GLY B C   
13290 O O   . GLY B 552  ? 0.2173 0.1878 0.1970 -0.0067 -0.0245 -0.0188 550  GLY B O   
13291 N N   . LEU B 553  ? 0.2031 0.1702 0.1826 -0.0018 -0.0249 -0.0193 551  LEU B N   
13292 C CA  . LEU B 553  ? 0.2205 0.1774 0.1929 -0.0029 -0.0274 -0.0192 551  LEU B CA  
13293 C C   . LEU B 553  ? 0.2165 0.1708 0.1871 -0.0032 -0.0280 -0.0176 551  LEU B C   
13294 O O   . LEU B 553  ? 0.2404 0.1983 0.2144 -0.0002 -0.0272 -0.0180 551  LEU B O   
13295 C CB  . LEU B 553  ? 0.2316 0.1822 0.2010 0.0013  -0.0288 -0.0217 551  LEU B CB  
13296 C CG  . LEU B 553  ? 0.2454 0.1968 0.2148 0.0017  -0.0284 -0.0235 551  LEU B CG  
13297 C CD1 . LEU B 553  ? 0.2714 0.2180 0.2388 0.0067  -0.0292 -0.0262 551  LEU B CD1 
13298 C CD2 . LEU B 553  ? 0.3019 0.2485 0.2665 -0.0030 -0.0298 -0.0226 551  LEU B CD2 
13299 N N   . ASP B 554  ? 0.2199 0.1678 0.1851 -0.0069 -0.0295 -0.0159 552  ASP B N   
13300 C CA  . ASP B 554  ? 0.2298 0.1751 0.1926 -0.0079 -0.0300 -0.0140 552  ASP B CA  
13301 C C   . ASP B 554  ? 0.2174 0.1525 0.1743 -0.0050 -0.0326 -0.0149 552  ASP B C   
13302 O O   . ASP B 554  ? 0.2295 0.1554 0.1800 -0.0067 -0.0347 -0.0147 552  ASP B O   
13303 C CB  . ASP B 554  ? 0.2386 0.1831 0.1987 -0.0139 -0.0299 -0.0114 552  ASP B CB  
13304 C CG  . ASP B 554  ? 0.2320 0.1741 0.1892 -0.0152 -0.0301 -0.0092 552  ASP B CG  
13305 O OD1 . ASP B 554  ? 0.2593 0.2002 0.2164 -0.0115 -0.0304 -0.0098 552  ASP B OD1 
13306 O OD2 . ASP B 554  ? 0.2679 0.2095 0.2229 -0.0202 -0.0299 -0.0069 552  ASP B OD2 
13307 N N   . LEU B 555  ? 0.2092 0.1457 0.1682 -0.0005 -0.0326 -0.0158 553  LEU B N   
13308 C CA  . LEU B 555  ? 0.2405 0.1682 0.1947 0.0031  -0.0351 -0.0168 553  LEU B CA  
13309 C C   . LEU B 555  ? 0.2679 0.1885 0.2160 0.0010  -0.0368 -0.0145 553  LEU B C   
13310 O O   . LEU B 555  ? 0.2550 0.1685 0.1991 0.0041  -0.0390 -0.0149 553  LEU B O   
13311 C CB  . LEU B 555  ? 0.2297 0.1626 0.1891 0.0086  -0.0347 -0.0187 553  LEU B CB  
13312 C CG  . LEU B 555  ? 0.2215 0.1605 0.1863 0.0111  -0.0331 -0.0211 553  LEU B CG  
13313 C CD1 . LEU B 555  ? 0.2472 0.1908 0.2169 0.0162  -0.0329 -0.0227 553  LEU B CD1 
13314 C CD2 . LEU B 555  ? 0.2783 0.2104 0.2387 0.0116  -0.0344 -0.0226 553  LEU B CD2 
13315 N N   . SER B 556  ? 0.2328 0.1553 0.1801 -0.0042 -0.0357 -0.0120 554  SER B N   
13316 C CA  . SER B 556  ? 0.2496 0.1643 0.1899 -0.0072 -0.0371 -0.0095 554  SER B CA  
13317 C C   . SER B 556  ? 0.2497 0.1571 0.1844 -0.0120 -0.0384 -0.0084 554  SER B C   
13318 O O   . SER B 556  ? 0.2716 0.1715 0.1998 -0.0151 -0.0397 -0.0062 554  SER B O   
13319 C CB  . SER B 556  ? 0.2574 0.1789 0.2000 -0.0100 -0.0350 -0.0073 554  SER B CB  
13320 O OG  . SER B 556  ? 0.2514 0.1792 0.1970 -0.0146 -0.0329 -0.0061 554  SER B OG  
13321 N N   . ASN B 557  ? 0.2455 0.1546 0.1821 -0.0127 -0.0381 -0.0098 555  ASN B N   
13322 C CA  . ASN B 557  ? 0.2557 0.1586 0.1874 -0.0176 -0.0393 -0.0090 555  ASN B CA  
13323 C C   . ASN B 557  ? 0.2879 0.1787 0.2130 -0.0148 -0.0423 -0.0108 555  ASN B C   
13324 O O   . ASN B 557  ? 0.2790 0.1707 0.2063 -0.0103 -0.0424 -0.0136 555  ASN B O   
13325 C CB  . ASN B 557  ? 0.2550 0.1668 0.1924 -0.0200 -0.0374 -0.0095 555  ASN B CB  
13326 C CG  . ASN B 557  ? 0.2590 0.1656 0.1920 -0.0254 -0.0388 -0.0086 555  ASN B CG  
13327 O OD1 . ASN B 557  ? 0.2693 0.1654 0.1959 -0.0250 -0.0413 -0.0097 555  ASN B OD1 
13328 N ND2 . ASN B 557  ? 0.2720 0.1860 0.2083 -0.0306 -0.0373 -0.0066 555  ASN B ND2 
13329 N N   . GLU B 558  ? 0.2740 0.1532 0.1908 -0.0175 -0.0447 -0.0093 556  GLU B N   
13330 C CA  . GLU B 558  ? 0.2960 0.1625 0.2057 -0.0144 -0.0478 -0.0111 556  GLU B CA  
13331 C C   . GLU B 558  ? 0.3066 0.1712 0.2156 -0.0148 -0.0483 -0.0133 556  GLU B C   
13332 O O   . GLU B 558  ? 0.3284 0.1868 0.2347 -0.0100 -0.0497 -0.0159 556  GLU B O   
13333 C CB  . GLU B 558  ? 0.3510 0.2045 0.2511 -0.0177 -0.0504 -0.0087 556  GLU B CB  
13334 C CG  . GLU B 558  ? 0.3246 0.1764 0.2228 -0.0163 -0.0508 -0.0068 556  GLU B CG  
13335 C CD  . GLU B 558  ? 0.3495 0.1997 0.2484 -0.0085 -0.0519 -0.0088 556  GLU B CD  
13336 O OE1 . GLU B 558  ? 0.3339 0.1820 0.2334 -0.0036 -0.0528 -0.0118 556  GLU B OE1 
13337 O OE2 . GLU B 558  ? 0.3369 0.1885 0.2359 -0.0072 -0.0518 -0.0074 556  GLU B OE2 
13338 N N   . GLU B 559  ? 0.2829 0.1525 0.1940 -0.0204 -0.0472 -0.0123 557  GLU B N   
13339 C CA  . GLU B 559  ? 0.2968 0.1652 0.2073 -0.0207 -0.0477 -0.0146 557  GLU B CA  
13340 C C   . GLU B 559  ? 0.2774 0.1540 0.1945 -0.0147 -0.0459 -0.0174 557  GLU B C   
13341 O O   . GLU B 559  ? 0.2937 0.1654 0.2083 -0.0111 -0.0469 -0.0203 557  GLU B O   
13342 C CB  . GLU B 559  ? 0.3278 0.2018 0.2404 -0.0277 -0.0469 -0.0129 557  GLU B CB  
13343 C CG  . GLU B 559  ? 0.3969 0.2630 0.3030 -0.0346 -0.0488 -0.0101 557  GLU B CG  
13344 C CD  . GLU B 559  ? 0.4709 0.3451 0.3807 -0.0413 -0.0478 -0.0085 557  GLU B CD  
13345 O OE1 . GLU B 559  ? 0.5272 0.4102 0.4428 -0.0403 -0.0464 -0.0100 557  GLU B OE1 
13346 O OE2 . GLU B 559  ? 0.4429 0.3150 0.3500 -0.0476 -0.0484 -0.0056 557  GLU B OE2 
13347 N N   . THR B 560  ? 0.2611 0.1499 0.1863 -0.0137 -0.0432 -0.0168 558  THR B N   
13348 C CA  . THR B 560  ? 0.2645 0.1616 0.1962 -0.0085 -0.0413 -0.0192 558  THR B CA  
13349 C C   . THR B 560  ? 0.2700 0.1618 0.1999 -0.0019 -0.0424 -0.0213 558  THR B C   
13350 O O   . THR B 560  ? 0.2716 0.1643 0.2029 0.0023  -0.0420 -0.0240 558  THR B O   
13351 C CB  . THR B 560  ? 0.2589 0.1688 0.1988 -0.0091 -0.0384 -0.0177 558  THR B CB  
13352 O OG1 . THR B 560  ? 0.2683 0.1834 0.2101 -0.0149 -0.0374 -0.0158 558  THR B OG1 
13353 C CG2 . THR B 560  ? 0.2805 0.1989 0.2272 -0.0042 -0.0364 -0.0200 558  THR B CG2 
13354 N N   . LEU B 561  ? 0.2467 0.1334 0.1737 -0.0007 -0.0437 -0.0200 559  LEU B N   
13355 C CA  . LEU B 561  ? 0.2613 0.1436 0.1870 0.0059  -0.0450 -0.0220 559  LEU B CA  
13356 C C   . LEU B 561  ? 0.2912 0.1621 0.2098 0.0080  -0.0473 -0.0241 559  LEU B C   
13357 O O   . LEU B 561  ? 0.2897 0.1604 0.2094 0.0139  -0.0473 -0.0268 559  LEU B O   
13358 C CB  . LEU B 561  ? 0.2762 0.1546 0.1993 0.0064  -0.0463 -0.0200 559  LEU B CB  
13359 C CG  . LEU B 561  ? 0.2483 0.1378 0.1783 0.0057  -0.0441 -0.0185 559  LEU B CG  
13360 C CD1 . LEU B 561  ? 0.2652 0.1496 0.1912 0.0057  -0.0456 -0.0164 559  LEU B CD1 
13361 C CD2 . LEU B 561  ? 0.2591 0.1584 0.1971 0.0108  -0.0423 -0.0207 559  LEU B CD2 
13362 N N   . ALA B 562  ? 0.2993 0.1607 0.2106 0.0033  -0.0492 -0.0230 560  ALA B N   
13363 C CA  . ALA B 562  ? 0.2982 0.1472 0.2017 0.0051  -0.0516 -0.0251 560  ALA B CA  
13364 C C   . ALA B 562  ? 0.3389 0.1922 0.2449 0.0066  -0.0502 -0.0279 560  ALA B C   
13365 O O   . ALA B 562  ? 0.3358 0.1843 0.2394 0.0120  -0.0509 -0.0308 560  ALA B O   
13366 C CB  . ALA B 562  ? 0.3213 0.1590 0.2162 -0.0010 -0.0540 -0.0230 560  ALA B CB  
13367 N N   . SER B 563  ? 0.3103 0.1729 0.2212 0.0023  -0.0482 -0.0271 561  SER B N   
13368 C CA  . SER B 563  ? 0.2967 0.1635 0.2098 0.0035  -0.0469 -0.0296 561  SER B CA  
13369 C C   . SER B 563  ? 0.3160 0.1922 0.2363 0.0098  -0.0445 -0.0316 561  SER B C   
13370 O O   . SER B 563  ? 0.3283 0.2038 0.2480 0.0137  -0.0441 -0.0344 561  SER B O   
13371 C CB  . SER B 563  ? 0.3241 0.1984 0.2405 -0.0029 -0.0457 -0.0280 561  SER B CB  
13372 O OG  . SER B 563  ? 0.3588 0.2455 0.2836 -0.0037 -0.0432 -0.0261 561  SER B OG  
13373 N N   . LEU B 564  ? 0.2848 0.1697 0.2118 0.0108  -0.0430 -0.0302 562  LEU B N   
13374 C CA  A LEU B 564  ? 0.2919 0.1854 0.2257 0.0164  -0.0409 -0.0319 562  LEU B CA  
13375 C CA  B LEU B 564  ? 0.2918 0.1853 0.2256 0.0165  -0.0409 -0.0319 562  LEU B CA  
13376 C C   . LEU B 564  ? 0.3327 0.2190 0.2630 0.0229  -0.0424 -0.0342 562  LEU B C   
13377 O O   . LEU B 564  ? 0.3149 0.2050 0.2480 0.0276  -0.0411 -0.0368 562  LEU B O   
13378 C CB  A LEU B 564  ? 0.3106 0.2135 0.2513 0.0158  -0.0394 -0.0298 562  LEU B CB  
13379 C CB  B LEU B 564  ? 0.3109 0.2135 0.2515 0.0160  -0.0395 -0.0299 562  LEU B CB  
13380 C CG  A LEU B 564  ? 0.2893 0.2028 0.2382 0.0203  -0.0371 -0.0311 562  LEU B CG  
13381 C CG  B LEU B 564  ? 0.2948 0.2095 0.2427 0.0129  -0.0367 -0.0288 562  LEU B CG  
13382 C CD1 A LEU B 564  ? 0.2724 0.1930 0.2251 0.0203  -0.0348 -0.0326 562  LEU B CD1 
13383 C CD1 B LEU B 564  ? 0.2533 0.1752 0.2068 0.0137  -0.0355 -0.0273 562  LEU B CD1 
13384 C CD2 A LEU B 564  ? 0.2709 0.1922 0.2254 0.0189  -0.0360 -0.0290 562  LEU B CD2 
13385 C CD2 B LEU B 564  ? 0.2741 0.1950 0.2258 0.0154  -0.0347 -0.0310 562  LEU B CD2 
13386 N N   . THR B 565  ? 0.3193 0.1955 0.2436 0.0234  -0.0452 -0.0333 563  THR B N   
13387 C CA  . THR B 565  ? 0.2964 0.1650 0.2169 0.0298  -0.0470 -0.0355 563  THR B CA  
13388 C C   . THR B 565  ? 0.3383 0.2020 0.2548 0.0323  -0.0470 -0.0386 563  THR B C   
13389 O O   . THR B 565  ? 0.3280 0.1939 0.2467 0.0385  -0.0462 -0.0412 563  THR B O   
13390 C CB  . THR B 565  ? 0.3211 0.1769 0.2335 0.0289  -0.0503 -0.0339 563  THR B CB  
13391 O OG1 . THR B 565  ? 0.3268 0.1874 0.2427 0.0272  -0.0502 -0.0312 563  THR B OG1 
13392 C CG2 . THR B 565  ? 0.3808 0.2281 0.2888 0.0360  -0.0524 -0.0362 563  THR B CG2 
13393 N N   . GLU B 566  ? 0.3264 0.1841 0.2374 0.0274  -0.0478 -0.0384 564  GLU B N   
13394 C CA  . GLU B 566  ? 0.3520 0.2037 0.2580 0.0296  -0.0481 -0.0414 564  GLU B CA  
13395 C C   . GLU B 566  ? 0.3484 0.2118 0.2611 0.0314  -0.0448 -0.0432 564  GLU B C   
13396 O O   . GLU B 566  ? 0.3456 0.2080 0.2574 0.0368  -0.0441 -0.0462 564  GLU B O   
13397 C CB  . GLU B 566  ? 0.3954 0.2369 0.2931 0.0234  -0.0503 -0.0406 564  GLU B CB  
13398 C CG  . GLU B 566  ? 0.4541 0.2814 0.3432 0.0219  -0.0538 -0.0391 564  GLU B CG  
13399 C CD  . GLU B 566  ? 0.5488 0.3681 0.4342 0.0295  -0.0554 -0.0410 564  GLU B CD  
13400 O OE1 . GLU B 566  ? 0.5907 0.4074 0.4742 0.0349  -0.0551 -0.0444 564  GLU B OE1 
13401 O OE2 . GLU B 566  ? 0.5589 0.3746 0.4433 0.0301  -0.0570 -0.0392 564  GLU B OE2 
13402 N N   . ALA B 567  ? 0.3131 0.1877 0.2327 0.0272  -0.0427 -0.0413 565  ALA B N   
13403 C CA  . ALA B 567  ? 0.2888 0.1744 0.2147 0.0286  -0.0396 -0.0427 565  ALA B CA  
13404 C C   . ALA B 567  ? 0.3281 0.2210 0.2603 0.0351  -0.0377 -0.0441 565  ALA B C   
13405 O O   . ALA B 567  ? 0.3008 0.1981 0.2351 0.0388  -0.0358 -0.0465 565  ALA B O   
13406 C CB  . ALA B 567  ? 0.3138 0.2092 0.2454 0.0229  -0.0379 -0.0402 565  ALA B CB  
13407 N N   . LEU B 568  ? 0.2791 0.1736 0.2144 0.0365  -0.0384 -0.0427 566  LEU B N   
13408 C CA  . LEU B 568  ? 0.2870 0.1888 0.2287 0.0424  -0.0370 -0.0439 566  LEU B CA  
13409 C C   . LEU B 568  ? 0.3208 0.2154 0.2580 0.0489  -0.0381 -0.0469 566  LEU B C   
13410 O O   . LEU B 568  ? 0.3025 0.2036 0.2440 0.0536  -0.0360 -0.0491 566  LEU B O   
13411 C CB  . LEU B 568  ? 0.2829 0.1872 0.2281 0.0421  -0.0379 -0.0417 566  LEU B CB  
13412 C CG  . LEU B 568  ? 0.2902 0.2032 0.2409 0.0368  -0.0364 -0.0389 566  LEU B CG  
13413 C CD1 . LEU B 568  ? 0.3353 0.2483 0.2873 0.0366  -0.0378 -0.0369 566  LEU B CD1 
13414 C CD2 . LEU B 568  ? 0.2923 0.2182 0.2515 0.0375  -0.0331 -0.0396 566  LEU B CD2 
13415 N N   . ARG B 569  ? 0.2918 0.1731 0.2205 0.0493  -0.0413 -0.0470 567  ARG B N   
13416 C CA  . ARG B 569  ? 0.3313 0.2039 0.2543 0.0555  -0.0425 -0.0500 567  ARG B CA  
13417 C C   . ARG B 569  ? 0.3359 0.2098 0.2576 0.0567  -0.0405 -0.0527 567  ARG B C   
13418 O O   . ARG B 569  ? 0.3423 0.2189 0.2656 0.0629  -0.0391 -0.0554 567  ARG B O   
13419 C CB  . ARG B 569  ? 0.3472 0.2037 0.2597 0.0542  -0.0464 -0.0494 567  ARG B CB  
13420 C CG  . ARG B 569  ? 0.4421 0.2952 0.3543 0.0548  -0.0487 -0.0473 567  ARG B CG  
13421 C CD  . ARG B 569  ? 0.5097 0.3456 0.4106 0.0536  -0.0525 -0.0467 567  ARG B CD  
13422 N NE  . ARG B 569  ? 0.5655 0.3978 0.4654 0.0537  -0.0548 -0.0443 567  ARG B NE  
13423 C CZ  . ARG B 569  ? 0.5960 0.4154 0.4873 0.0506  -0.0579 -0.0425 567  ARG B CZ  
13424 N NH1 . ARG B 569  ? 0.6593 0.4680 0.5423 0.0465  -0.0592 -0.0427 567  ARG B NH1 
13425 N NH2 . ARG B 569  ? 0.6426 0.4594 0.5333 0.0513  -0.0598 -0.0403 567  ARG B NH2 
13426 N N   . GLU B 570  ? 0.2951 0.1675 0.2137 0.0508  -0.0403 -0.0520 568  GLU B N   
13427 C CA  . GLU B 570  ? 0.3205 0.1930 0.2366 0.0516  -0.0387 -0.0545 568  GLU B CA  
13428 C C   . GLU B 570  ? 0.3227 0.2096 0.2478 0.0541  -0.0348 -0.0554 568  GLU B C   
13429 O O   . GLU B 570  ? 0.3581 0.2459 0.2820 0.0581  -0.0331 -0.0582 568  GLU B O   
13430 C CB  . GLU B 570  ? 0.3466 0.2151 0.2580 0.0442  -0.0396 -0.0532 568  GLU B CB  
13431 C CG  . GLU B 570  ? 0.4335 0.2858 0.3342 0.0420  -0.0435 -0.0532 568  GLU B CG  
13432 C CD  . GLU B 570  ? 0.5263 0.3765 0.4244 0.0336  -0.0447 -0.0509 568  GLU B CD  
13433 O OE1 . GLU B 570  ? 0.5065 0.3673 0.4104 0.0300  -0.0426 -0.0497 568  GLU B OE1 
13434 O OE2 . GLU B 570  ? 0.6052 0.4432 0.4954 0.0305  -0.0479 -0.0501 568  GLU B OE2 
13435 N N   . SER B 571  ? 0.3019 0.2001 0.2357 0.0517  -0.0332 -0.0530 569  SER B N   
13436 C CA  . SER B 571  ? 0.2977 0.2095 0.2402 0.0536  -0.0296 -0.0535 569  SER B CA  
13437 C C   . SER B 571  ? 0.3235 0.2384 0.2691 0.0610  -0.0285 -0.0558 569  SER B C   
13438 O O   . SER B 571  ? 0.3275 0.2501 0.2769 0.0638  -0.0255 -0.0575 569  SER B O   
13439 C CB  . SER B 571  ? 0.2980 0.2198 0.2486 0.0496  -0.0285 -0.0504 569  SER B CB  
13440 O OG  . SER B 571  ? 0.3126 0.2361 0.2670 0.0521  -0.0295 -0.0496 569  SER B OG  
13441 N N   . ALA B 572  ? 0.3039 0.2129 0.2478 0.0644  -0.0309 -0.0559 570  ALA B N   
13442 C CA  . ALA B 572  ? 0.3190 0.2314 0.2663 0.0718  -0.0302 -0.0580 570  ALA B CA  
13443 C C   . ALA B 572  ? 0.3618 0.2675 0.3027 0.0768  -0.0299 -0.0615 570  ALA B C   
13444 O O   . ALA B 572  ? 0.3912 0.3022 0.3358 0.0830  -0.0282 -0.0636 570  ALA B O   
13445 C CB  . ALA B 572  ? 0.3354 0.2432 0.2825 0.0740  -0.0333 -0.0569 570  ALA B CB  
13446 N N   . ALA B 573  ? 0.3309 0.2253 0.2623 0.0742  -0.0314 -0.0622 571  ALA B N   
13447 C CA  . ALA B 573  ? 0.3527 0.2404 0.2773 0.0783  -0.0310 -0.0653 571  ALA B CA  
13448 C C   . ALA B 573  ? 0.3379 0.2327 0.2640 0.0780  -0.0275 -0.0670 571  ALA B C   
13449 O O   . ALA B 573  ? 0.3818 0.2749 0.3044 0.0809  -0.0261 -0.0688 571  ALA B O   
13450 C CB  . ALA B 573  ? 0.3902 0.2622 0.3036 0.0752  -0.0344 -0.0651 571  ALA B CB  
13451 N N   . MET B 574  ? 0.3200 0.2250 0.2525 0.0730  -0.0255 -0.0649 572  MET B N   
13452 C CA  . MET B 574  ? 0.3220 0.2342 0.2560 0.0719  -0.0222 -0.0658 572  MET B CA  
13453 C C   . MET B 574  ? 0.3184 0.2422 0.2600 0.0775  -0.0186 -0.0673 572  MET B C   
13454 O O   . MET B 574  ? 0.3220 0.2523 0.2708 0.0801  -0.0184 -0.0665 572  MET B O   
13455 C CB  . MET B 574  ? 0.3215 0.2405 0.2598 0.0647  -0.0215 -0.0626 572  MET B CB  
13456 C CG  . MET B 574  ? 0.3349 0.2442 0.2663 0.0585  -0.0246 -0.0611 572  MET B CG  
13457 S SD  . MET B 574  ? 0.3679 0.2862 0.3062 0.0510  -0.0242 -0.0570 572  MET B SD  
13458 C CE  . MET B 574  ? 0.3886 0.2945 0.3177 0.0447  -0.0280 -0.0559 572  MET B CE  
13459 N N   . LYS B 575  ? 0.2873 0.2137 0.2269 0.0793  -0.0157 -0.0694 573  LYS B N   
13460 C CA  . LYS B 575  ? 0.2627 0.2014 0.2099 0.0835  -0.0117 -0.0704 573  LYS B CA  
13461 C C   . LYS B 575  ? 0.2682 0.2193 0.2235 0.0788  -0.0092 -0.0679 573  LYS B C   
13462 O O   . LYS B 575  ? 0.2707 0.2229 0.2236 0.0752  -0.0078 -0.0676 573  LYS B O   
13463 C CB  . LYS B 575  ? 0.2986 0.2358 0.2407 0.0861  -0.0095 -0.0725 573  LYS B CB  
13464 C CG  . LYS B 575  ? 0.3088 0.2595 0.2589 0.0893  -0.0050 -0.0728 573  LYS B CG  
13465 C CD  . LYS B 575  ? 0.3511 0.2989 0.2954 0.0921  -0.0029 -0.0749 573  LYS B CD  
13466 C CE  . LYS B 575  ? 0.4653 0.4266 0.4172 0.0948  0.0018  -0.0750 573  LYS B CE  
13467 N NZ  . LYS B 575  ? 0.4956 0.4656 0.4574 0.0972  0.0020  -0.0737 573  LYS B NZ  
13468 N N   . TRP B 576  ? 0.2534 0.2137 0.2181 0.0789  -0.0087 -0.0661 574  TRP B N   
13469 C CA  . TRP B 576  ? 0.2192 0.1910 0.1921 0.0747  -0.0065 -0.0636 574  TRP B CA  
13470 C C   . TRP B 576  ? 0.2091 0.1927 0.1885 0.0781  -0.0023 -0.0647 574  TRP B C   
13471 O O   . TRP B 576  ? 0.2405 0.2281 0.2242 0.0833  -0.0017 -0.0660 574  TRP B O   
13472 C CB  . TRP B 576  ? 0.2079 0.1825 0.1869 0.0725  -0.0084 -0.0610 574  TRP B CB  
13473 C CG  . TRP B 576  ? 0.2289 0.1935 0.2023 0.0685  -0.0121 -0.0594 574  TRP B CG  
13474 C CD1 . TRP B 576  ? 0.2957 0.2519 0.2658 0.0700  -0.0155 -0.0594 574  TRP B CD1 
13475 C CD2 . TRP B 576  ? 0.2146 0.1769 0.1853 0.0621  -0.0128 -0.0574 574  TRP B CD2 
13476 N NE1 . TRP B 576  ? 0.2781 0.2270 0.2435 0.0647  -0.0181 -0.0575 574  TRP B NE1 
13477 C CE2 . TRP B 576  ? 0.2599 0.2128 0.2260 0.0599  -0.0165 -0.0563 574  TRP B CE2 
13478 C CE3 . TRP B 576  ? 0.2081 0.1757 0.1800 0.0582  -0.0107 -0.0564 574  TRP B CE3 
13479 C CZ2 . TRP B 576  ? 0.2816 0.2309 0.2446 0.0537  -0.0179 -0.0542 574  TRP B CZ2 
13480 C CZ3 . TRP B 576  ? 0.2434 0.2072 0.2122 0.0524  -0.0123 -0.0544 574  TRP B CZ3 
13481 C CH2 . TRP B 576  ? 0.3041 0.2593 0.2689 0.0502  -0.0158 -0.0533 574  TRP B CH2 
13482 N N   . THR B 577  ? 0.2136 0.2028 0.1939 0.0751  0.0006  -0.0640 575  THR B N   
13483 C CA  . THR B 577  ? 0.2047 0.2053 0.1910 0.0774  0.0048  -0.0646 575  THR B CA  
13484 C C   . THR B 577  ? 0.2053 0.2146 0.1975 0.0720  0.0067  -0.0617 575  THR B C   
13485 O O   . THR B 577  ? 0.2104 0.2164 0.2005 0.0668  0.0051  -0.0597 575  THR B O   
13486 C CB  . THR B 577  ? 0.2317 0.2297 0.2113 0.0804  0.0072  -0.0674 575  THR B CB  
13487 O OG1 . THR B 577  ? 0.2560 0.2494 0.2295 0.0754  0.0068  -0.0664 575  THR B OG1 
13488 C CG2 . THR B 577  ? 0.2537 0.2417 0.2264 0.0851  0.0052  -0.0699 575  THR B CG2 
13489 N N   . ALA B 578  ? 0.1960 0.2168 0.1958 0.0733  0.0101  -0.0615 576  ALA B N   
13490 C CA  . ALA B 578  ? 0.1538 0.1829 0.1587 0.0687  0.0124  -0.0590 576  ALA B CA  
13491 C C   . ALA B 578  ? 0.1688 0.2062 0.1759 0.0712  0.0169  -0.0602 576  ALA B C   
13492 O O   . ALA B 578  ? 0.2002 0.2431 0.2118 0.0758  0.0184  -0.0618 576  ALA B O   
13493 C CB  . ALA B 578  ? 0.1766 0.2120 0.1903 0.0665  0.0114  -0.0567 576  ALA B CB  
13494 N N   . LEU B 579  ? 0.1787 0.2170 0.1826 0.0683  0.0191  -0.0595 577  LEU B N   
13495 C CA  . LEU B 579  ? 0.1732 0.2183 0.1775 0.0701  0.0235  -0.0605 577  LEU B CA  
13496 C C   . LEU B 579  ? 0.1495 0.2020 0.1580 0.0652  0.0258  -0.0576 577  LEU B C   
13497 O O   . LEU B 579  ? 0.1446 0.1946 0.1530 0.0605  0.0238  -0.0552 577  LEU B O   
13498 C CB  . LEU B 579  ? 0.2279 0.2651 0.2215 0.0718  0.0240  -0.0628 577  LEU B CB  
13499 C CG  . LEU B 579  ? 0.2813 0.3073 0.2677 0.0755  0.0208  -0.0655 577  LEU B CG  
13500 C CD1 . LEU B 579  ? 0.2754 0.2929 0.2505 0.0757  0.0210  -0.0673 577  LEU B CD1 
13501 C CD2 . LEU B 579  ? 0.2876 0.3168 0.2780 0.0809  0.0217  -0.0670 577  LEU B CD2 
13502 N N   . PRO B 580  ? 0.1622 0.2238 0.1743 0.0662  0.0301  -0.0577 578  PRO B N   
13503 C CA  . PRO B 580  ? 0.1497 0.2163 0.1633 0.0615  0.0324  -0.0550 578  PRO B CA  
13504 C C   . PRO B 580  ? 0.1514 0.2104 0.1551 0.0597  0.0321  -0.0551 578  PRO B C   
13505 O O   . PRO B 580  ? 0.1754 0.2329 0.1731 0.0623  0.0342  -0.0571 578  PRO B O   
13506 C CB  . PRO B 580  ? 0.1503 0.2278 0.1692 0.0637  0.0372  -0.0555 578  PRO B CB  
13507 C CG  . PRO B 580  ? 0.1710 0.2496 0.1931 0.0686  0.0367  -0.0575 578  PRO B CG  
13508 C CD  . PRO B 580  ? 0.1805 0.2477 0.1949 0.0713  0.0331  -0.0598 578  PRO B CD  
13509 N N   . GLN B 581  ? 0.1595 0.2135 0.1612 0.0553  0.0292  -0.0530 579  GLN B N   
13510 C CA  . GLN B 581  ? 0.1693 0.2159 0.1620 0.0531  0.0280  -0.0529 579  GLN B CA  
13511 C C   . GLN B 581  ? 0.1608 0.2125 0.1544 0.0493  0.0304  -0.0502 579  GLN B C   
13512 O O   . GLN B 581  ? 0.1842 0.2368 0.1811 0.0453  0.0290  -0.0474 579  GLN B O   
13513 C CB  . GLN B 581  ? 0.1807 0.2192 0.1708 0.0507  0.0233  -0.0521 579  GLN B CB  
13514 C CG  . GLN B 581  ? 0.2014 0.2337 0.1897 0.0541  0.0207  -0.0545 579  GLN B CG  
13515 C CD  . GLN B 581  ? 0.2574 0.2824 0.2365 0.0574  0.0206  -0.0576 579  GLN B CD  
13516 O OE1 . GLN B 581  ? 0.2588 0.2829 0.2320 0.0569  0.0224  -0.0581 579  GLN B OE1 
13517 N NE2 . GLN B 581  ? 0.3177 0.3367 0.2947 0.0608  0.0185  -0.0598 579  GLN B NE2 
13518 N N   . LEU B 582  ? 0.1854 0.2403 0.1760 0.0507  0.0341  -0.0510 580  LEU B N   
13519 C CA  . LEU B 582  ? 0.1844 0.2432 0.1745 0.0472  0.0364  -0.0485 580  LEU B CA  
13520 C C   . LEU B 582  ? 0.1937 0.2448 0.1742 0.0453  0.0346  -0.0483 580  LEU B C   
13521 O O   . LEU B 582  ? 0.2350 0.2782 0.2092 0.0466  0.0319  -0.0503 580  LEU B O   
13522 C CB  . LEU B 582  ? 0.2000 0.2667 0.1918 0.0493  0.0415  -0.0490 580  LEU B CB  
13523 C CG  . LEU B 582  ? 0.2269 0.3038 0.2296 0.0494  0.0438  -0.0480 580  LEU B CG  
13524 C CD1 . LEU B 582  ? 0.2391 0.3166 0.2471 0.0529  0.0420  -0.0500 580  LEU B CD1 
13525 C CD2 . LEU B 582  ? 0.3000 0.3849 0.3036 0.0506  0.0491  -0.0481 580  LEU B CD2 
13526 N N   . ALA B 583  ? 0.2021 0.2555 0.1815 0.0419  0.0359  -0.0457 581  ALA B N   
13527 C CA  . ALA B 583  ? 0.2206 0.2675 0.1914 0.0397  0.0338  -0.0451 581  ALA B CA  
13528 C C   . ALA B 583  ? 0.2742 0.3161 0.2356 0.0427  0.0345  -0.0482 581  ALA B C   
13529 O O   . ALA B 583  ? 0.3344 0.3685 0.2882 0.0417  0.0315  -0.0490 581  ALA B O   
13530 C CB  . ALA B 583  ? 0.2539 0.3047 0.2251 0.0362  0.0356  -0.0418 581  ALA B CB  
13531 N N   . THR B 584  ? 0.1965 0.2426 0.1581 0.0462  0.0385  -0.0502 582  THR B N   
13532 C CA  . THR B 584  ? 0.2525 0.2945 0.2050 0.0496  0.0399  -0.0533 582  THR B CA  
13533 C C   . THR B 584  ? 0.2466 0.2833 0.1974 0.0539  0.0382  -0.0569 582  THR B C   
13534 O O   . THR B 584  ? 0.2838 0.3165 0.2270 0.0573  0.0393  -0.0600 582  THR B O   
13535 C CB  . THR B 584  ? 0.2599 0.3099 0.2135 0.0515  0.0456  -0.0535 582  THR B CB  
13536 O OG1 . THR B 584  ? 0.3045 0.3632 0.2690 0.0524  0.0476  -0.0528 582  THR B OG1 
13537 C CG2 . THR B 584  ? 0.3732 0.4256 0.3243 0.0475  0.0472  -0.0504 582  THR B CG2 
13538 N N   . GLY B 585  ? 0.2406 0.2770 0.1979 0.0540  0.0356  -0.0567 583  GLY B N   
13539 C CA  . GLY B 585  ? 0.2196 0.2507 0.1755 0.0581  0.0338  -0.0599 583  GLY B CA  
13540 C C   . GLY B 585  ? 0.2094 0.2476 0.1754 0.0606  0.0351  -0.0600 583  GLY B C   
13541 O O   . GLY B 585  ? 0.2441 0.2916 0.2183 0.0590  0.0374  -0.0577 583  GLY B O   
13542 N N   . PRO B 586  ? 0.2113 0.2449 0.1767 0.0645  0.0332  -0.0625 584  PRO B N   
13543 C CA  . PRO B 586  ? 0.1964 0.2366 0.1712 0.0674  0.0340  -0.0628 584  PRO B CA  
13544 C C   . PRO B 586  ? 0.2253 0.2746 0.2033 0.0713  0.0391  -0.0642 584  PRO B C   
13545 O O   . PRO B 586  ? 0.2578 0.3047 0.2291 0.0738  0.0412  -0.0661 584  PRO B O   
13546 C CB  . PRO B 586  ? 0.2291 0.2601 0.2002 0.0708  0.0305  -0.0654 584  PRO B CB  
13547 C CG  . PRO B 586  ? 0.2891 0.3105 0.2482 0.0718  0.0297  -0.0677 584  PRO B CG  
13548 C CD  . PRO B 586  ? 0.2669 0.2886 0.2229 0.0663  0.0299  -0.0652 584  PRO B CD  
13549 N N   . ALA B 587  ? 0.1908 0.2504 0.1794 0.0710  0.0409  -0.0626 585  ALA B N   
13550 C CA  . ALA B 587  ? 0.1938 0.2620 0.1879 0.0724  0.0450  -0.0619 585  ALA B CA  
13551 C C   . ALA B 587  ? 0.1922 0.2605 0.1908 0.0763  0.0439  -0.0631 585  ALA B C   
13552 O O   . ALA B 587  ? 0.2060 0.2706 0.2067 0.0770  0.0402  -0.0634 585  ALA B O   
13553 C CB  . ALA B 587  ? 0.2149 0.2938 0.2180 0.0685  0.0473  -0.0588 585  ALA B CB  
13554 N N   . ALA B 588  ? 0.2118 0.2845 0.2117 0.0789  0.0473  -0.0637 586  ALA B N   
13555 C CA  . ALA B 588  ? 0.2014 0.2761 0.2066 0.0828  0.0468  -0.0646 586  ALA B CA  
13556 C C   . ALA B 588  ? 0.1945 0.2791 0.2117 0.0809  0.0468  -0.0622 586  ALA B C   
13557 O O   . ALA B 588  ? 0.2470 0.3387 0.2689 0.0769  0.0487  -0.0598 586  ALA B O   
13558 C CB  . ALA B 588  ? 0.2119 0.2895 0.2155 0.0860  0.0507  -0.0659 586  ALA B CB  
13559 N N   . GLY B 589  ? 0.2155 0.3001 0.2372 0.0838  0.0445  -0.0627 587  GLY B N   
13560 C CA  . GLY B 589  ? 0.2213 0.3152 0.2541 0.0823  0.0444  -0.0606 587  GLY B CA  
13561 C C   . GLY B 589  ? 0.2390 0.3322 0.2754 0.0863  0.0419  -0.0616 587  GLY B C   
13562 O O   . GLY B 589  ? 0.2669 0.3531 0.2975 0.0905  0.0408  -0.0639 587  GLY B O   
13563 N N   . GLU B 590  ? 0.2442 0.3444 0.2899 0.0848  0.0408  -0.0598 588  GLU B N   
13564 C CA  . GLU B 590  ? 0.2477 0.3482 0.2976 0.0883  0.0382  -0.0603 588  GLU B CA  
13565 C C   . GLU B 590  ? 0.2386 0.3290 0.2842 0.0888  0.0332  -0.0610 588  GLU B C   
13566 O O   . GLU B 590  ? 0.2353 0.3245 0.2816 0.0850  0.0313  -0.0596 588  GLU B O   
13567 C CB  . GLU B 590  ? 0.3071 0.4189 0.3683 0.0864  0.0387  -0.0582 588  GLU B CB  
13568 C CG  . GLU B 590  ? 0.3909 0.5127 0.4573 0.0871  0.0432  -0.0578 588  GLU B CG  
13569 C CD  . GLU B 590  ? 0.4445 0.5658 0.5101 0.0930  0.0437  -0.0600 588  GLU B CD  
13570 O OE1 . GLU B 590  ? 0.4689 0.5893 0.5374 0.0958  0.0405  -0.0604 588  GLU B OE1 
13571 O OE2 . GLU B 590  ? 0.5646 0.6863 0.6265 0.0949  0.0472  -0.0612 588  GLU B OE2 
13572 N N   . THR B 591  ? 0.2240 0.3074 0.2653 0.0933  0.0310  -0.0629 589  THR B N   
13573 C CA  . THR B 591  ? 0.2242 0.2965 0.2597 0.0940  0.0264  -0.0637 589  THR B CA  
13574 C C   . THR B 591  ? 0.2452 0.3182 0.2857 0.0963  0.0231  -0.0633 589  THR B C   
13575 O O   . THR B 591  ? 0.2625 0.3405 0.3071 0.0998  0.0241  -0.0638 589  THR B O   
13576 C CB  . THR B 591  ? 0.2226 0.2839 0.2474 0.0970  0.0260  -0.0662 589  THR B CB  
13577 O OG1 . THR B 591  ? 0.2826 0.3433 0.3025 0.0945  0.0288  -0.0664 589  THR B OG1 
13578 C CG2 . THR B 591  ? 0.2738 0.3231 0.2923 0.0972  0.0212  -0.0668 589  THR B CG2 
13579 N N   . ARG B 592  ? 0.2184 0.2866 0.2585 0.0944  0.0193  -0.0625 590  ARG B N   
13580 C CA  . ARG B 592  ? 0.2031 0.2704 0.2465 0.0964  0.0157  -0.0622 590  ARG B CA  
13581 C C   . ARG B 592  ? 0.2247 0.2804 0.2616 0.0956  0.0114  -0.0624 590  ARG B C   
13582 O O   . ARG B 592  ? 0.2397 0.2902 0.2716 0.0927  0.0112  -0.0624 590  ARG B O   
13583 C CB  . ARG B 592  ? 0.2841 0.3625 0.3380 0.0938  0.0159  -0.0600 590  ARG B CB  
13584 C CG  . ARG B 592  ? 0.2543 0.3337 0.3098 0.0885  0.0153  -0.0583 590  ARG B CG  
13585 C CD  . ARG B 592  ? 0.3246 0.4109 0.3887 0.0865  0.0135  -0.0565 590  ARG B CD  
13586 N NE  . ARG B 592  ? 0.3183 0.4064 0.3842 0.0812  0.0136  -0.0549 590  ARG B NE  
13587 C CZ  . ARG B 592  ? 0.3021 0.3838 0.3653 0.0794  0.0104  -0.0545 590  ARG B CZ  
13588 N NH1 . ARG B 592  ? 0.2671 0.3396 0.3251 0.0821  0.0068  -0.0555 590  ARG B NH1 
13589 N NH2 . ARG B 592  ? 0.3308 0.4150 0.3962 0.0747  0.0108  -0.0531 590  ARG B NH2 
13590 N N   . THR B 593  ? 0.2490 0.3008 0.2860 0.0983  0.0078  -0.0625 591  THR B N   
13591 C CA  . THR B 593  ? 0.2340 0.2746 0.2649 0.0976  0.0036  -0.0625 591  THR B CA  
13592 C C   . THR B 593  ? 0.2333 0.2773 0.2692 0.0934  0.0020  -0.0605 591  THR B C   
13593 O O   . THR B 593  ? 0.2457 0.3003 0.2903 0.0918  0.0031  -0.0591 591  THR B O   
13594 C CB  . THR B 593  ? 0.2580 0.2922 0.2862 0.1021  0.0004  -0.0633 591  THR B CB  
13595 O OG1 . THR B 593  ? 0.3064 0.3499 0.3435 0.1032  -0.0001 -0.0622 591  THR B OG1 
13596 C CG2 . THR B 593  ? 0.3269 0.3568 0.3496 0.1064  0.0019  -0.0654 591  THR B CG2 
13597 N N   . VAL B 594  ? 0.2221 0.2568 0.2522 0.0915  -0.0008 -0.0604 592  VAL B N   
13598 C CA  . VAL B 594  ? 0.2194 0.2548 0.2525 0.0879  -0.0029 -0.0588 592  VAL B CA  
13599 C C   . VAL B 594  ? 0.2488 0.2754 0.2782 0.0899  -0.0075 -0.0588 592  VAL B C   
13600 O O   . VAL B 594  ? 0.2398 0.2549 0.2606 0.0914  -0.0093 -0.0599 592  VAL B O   
13601 C CB  . VAL B 594  ? 0.2182 0.2500 0.2475 0.0839  -0.0023 -0.0587 592  VAL B CB  
13602 C CG1 . VAL B 594  ? 0.2236 0.2563 0.2561 0.0801  -0.0044 -0.0569 592  VAL B CG1 
13603 C CG2 . VAL B 594  ? 0.2274 0.2670 0.2591 0.0823  0.0022  -0.0588 592  VAL B CG2 
13604 N N   . LEU B 595  ? 0.2529 0.2844 0.2885 0.0898  -0.0093 -0.0575 593  LEU B N   
13605 C CA  . LEU B 595  ? 0.2511 0.2755 0.2838 0.0921  -0.0135 -0.0572 593  LEU B CA  
13606 C C   . LEU B 595  ? 0.2156 0.2365 0.2479 0.0887  -0.0163 -0.0558 593  LEU B C   
13607 O O   . LEU B 595  ? 0.2497 0.2775 0.2874 0.0850  -0.0151 -0.0548 593  LEU B O   
13608 C CB  . LEU B 595  ? 0.2634 0.2953 0.3027 0.0951  -0.0140 -0.0569 593  LEU B CB  
13609 C CG  . LEU B 595  ? 0.2544 0.2911 0.2952 0.0987  -0.0112 -0.0582 593  LEU B CG  
13610 C CD1 . LEU B 595  ? 0.2814 0.3260 0.3294 0.1014  -0.0120 -0.0577 593  LEU B CD1 
13611 C CD2 . LEU B 595  ? 0.2690 0.2942 0.3003 0.1022  -0.0119 -0.0599 593  LEU B CD2 
13612 N N   . ASN B 596  ? 0.1970 0.2067 0.2226 0.0899  -0.0200 -0.0558 594  ASN B N   
13613 C CA  . ASN B 596  ? 0.2054 0.2105 0.2298 0.0871  -0.0230 -0.0544 594  ASN B CA  
13614 C C   . ASN B 596  ? 0.2064 0.2202 0.2388 0.0870  -0.0242 -0.0531 594  ASN B C   
13615 O O   . ASN B 596  ? 0.2059 0.2205 0.2394 0.0904  -0.0258 -0.0532 594  ASN B O   
13616 C CB  . ASN B 596  ? 0.2249 0.2155 0.2395 0.0885  -0.0266 -0.0544 594  ASN B CB  
13617 C CG  . ASN B 596  ? 0.2310 0.2154 0.2420 0.0833  -0.0290 -0.0518 594  ASN B CG  
13618 O OD1 . ASN B 596  ? 0.2380 0.2287 0.2542 0.0802  -0.0292 -0.0500 594  ASN B OD1 
13619 N ND2 . ASN B 596  ? 0.2884 0.2600 0.2899 0.0822  -0.0310 -0.0514 594  ASN B ND2 
13620 N N   . PRO B 597  ? 0.1790 0.1988 0.2161 0.0823  -0.0235 -0.0515 595  PRO B N   
13621 C CA  . PRO B 597  ? 0.1960 0.2236 0.2405 0.0825  -0.0251 -0.0506 595  PRO B CA  
13622 C C   . PRO B 597  ? 0.2072 0.2274 0.2479 0.0843  -0.0295 -0.0499 595  PRO B C   
13623 O O   . PRO B 597  ? 0.2276 0.2534 0.2733 0.0857  -0.0312 -0.0495 595  PRO B O   
13624 C CB  . PRO B 597  ? 0.1961 0.2283 0.2435 0.0760  -0.0234 -0.0487 595  PRO B CB  
13625 C CG  . PRO B 597  ? 0.2408 0.2656 0.2813 0.0724  -0.0220 -0.0481 595  PRO B CG  
13626 C CD  . PRO B 597  ? 0.1977 0.2177 0.2335 0.0763  -0.0212 -0.0501 595  PRO B CD  
13627 N N   . GLY B 598  ? 0.2133 0.2210 0.2446 0.0833  -0.0314 -0.0493 596  GLY B N   
13628 C CA  . GLY B 598  ? 0.2391 0.2385 0.2656 0.0848  -0.0356 -0.0484 596  GLY B CA  
13629 C C   . GLY B 598  ? 0.2533 0.2479 0.2768 0.0912  -0.0376 -0.0500 596  GLY B C   
13630 O O   . GLY B 598  ? 0.2677 0.2565 0.2879 0.0930  -0.0412 -0.0491 596  GLY B O   
13631 N N   . ASP B 599  ? 0.2305 0.2275 0.2545 0.0933  -0.0348 -0.0515 597  ASP B N   
13632 C CA  . ASP B 599  ? 0.2688 0.2613 0.2891 0.0980  -0.0359 -0.0524 597  ASP B CA  
13633 C C   . ASP B 599  ? 0.2619 0.2606 0.2849 0.0996  -0.0318 -0.0540 597  ASP B C   
13634 O O   . ASP B 599  ? 0.2534 0.2466 0.2712 0.0989  -0.0302 -0.0550 597  ASP B O   
13635 C CB  . ASP B 599  ? 0.2782 0.2547 0.2872 0.0987  -0.0386 -0.0524 597  ASP B CB  
13636 C CG  . ASP B 599  ? 0.3503 0.3211 0.3549 0.1036  -0.0402 -0.0532 597  ASP B CG  
13637 O OD1 . ASP B 599  ? 0.3060 0.2851 0.3160 0.1068  -0.0384 -0.0542 597  ASP B OD1 
13638 O OD2 . ASP B 599  ? 0.3855 0.3433 0.3812 0.1042  -0.0433 -0.0527 597  ASP B OD2 
13639 N N   . HIS B 600  ? 0.2629 0.2732 0.2941 0.1014  -0.0302 -0.0542 598  HIS B N   
13640 C CA  . HIS B 600  ? 0.2654 0.2829 0.3000 0.1025  -0.0261 -0.0555 598  HIS B CA  
13641 C C   . HIS B 600  ? 0.2694 0.2790 0.2970 0.1066  -0.0258 -0.0571 598  HIS B C   
13642 O O   . HIS B 600  ? 0.3042 0.3177 0.3328 0.1074  -0.0223 -0.0583 598  HIS B O   
13643 C CB  . HIS B 600  ? 0.2808 0.3123 0.3257 0.1033  -0.0246 -0.0551 598  HIS B CB  
13644 C CG  . HIS B 600  ? 0.3063 0.3470 0.3584 0.0986  -0.0235 -0.0538 598  HIS B CG  
13645 N ND1 . HIS B 600  ? 0.3098 0.3630 0.3713 0.0981  -0.0222 -0.0532 598  HIS B ND1 
13646 C CD2 . HIS B 600  ? 0.2223 0.2613 0.2735 0.0941  -0.0234 -0.0530 598  HIS B CD2 
13647 C CE1 . HIS B 600  ? 0.3216 0.3800 0.3873 0.0934  -0.0215 -0.0521 598  HIS B CE1 
13648 N NE2 . HIS B 600  ? 0.2701 0.3202 0.3298 0.0911  -0.0222 -0.0520 598  HIS B NE2 
13649 N N   . ARG B 601  ? 0.2890 0.2872 0.3093 0.1091  -0.0295 -0.0572 599  ARG B N   
13650 C CA  . ARG B 601  ? 0.3094 0.2982 0.3219 0.1126  -0.0296 -0.0587 599  ARG B CA  
13651 C C   . ARG B 601  ? 0.3190 0.2989 0.3238 0.1098  -0.0285 -0.0594 599  ARG B C   
13652 O O   . ARG B 601  ? 0.3357 0.3090 0.3343 0.1121  -0.0278 -0.0609 599  ARG B O   
13653 C CB  . ARG B 601  ? 0.3168 0.2955 0.3233 0.1156  -0.0340 -0.0583 599  ARG B CB  
13654 C CG  . ARG B 601  ? 0.3693 0.3559 0.3827 0.1185  -0.0355 -0.0577 599  ARG B CG  
13655 C CD  . ARG B 601  ? 0.3733 0.3493 0.3804 0.1205  -0.0403 -0.0568 599  ARG B CD  
13656 N NE  . ARG B 601  ? 0.3939 0.3620 0.3962 0.1163  -0.0427 -0.0553 599  ARG B NE  
13657 C CZ  . ARG B 601  ? 0.4064 0.3639 0.4020 0.1168  -0.0469 -0.0541 599  ARG B CZ  
13658 N NH1 . ARG B 601  ? 0.4491 0.4022 0.4418 0.1213  -0.0492 -0.0544 599  ARG B NH1 
13659 N NH2 . ARG B 601  ? 0.4020 0.3531 0.3937 0.1126  -0.0486 -0.0526 599  ARG B NH2 
13660 N N   . ASP B 602  ? 0.2972 0.2766 0.3021 0.1050  -0.0285 -0.0583 600  ASP B N   
13661 C CA  . ASP B 602  ? 0.3227 0.2939 0.3205 0.1019  -0.0279 -0.0588 600  ASP B CA  
13662 C C   . ASP B 602  ? 0.3066 0.2874 0.3093 0.1002  -0.0233 -0.0596 600  ASP B C   
13663 O O   . ASP B 602  ? 0.3023 0.2920 0.3117 0.0971  -0.0219 -0.0587 600  ASP B O   
13664 C CB  . ASP B 602  ? 0.3200 0.2850 0.3151 0.0978  -0.0305 -0.0572 600  ASP B CB  
13665 C CG  . ASP B 602  ? 0.3480 0.3041 0.3356 0.0943  -0.0301 -0.0577 600  ASP B CG  
13666 O OD1 . ASP B 602  ? 0.3614 0.3119 0.3432 0.0956  -0.0291 -0.0592 600  ASP B OD1 
13667 O OD2 . ASP B 602  ? 0.3758 0.3307 0.3633 0.0900  -0.0308 -0.0564 600  ASP B OD2 
13668 N N   . VAL B 603  ? 0.3247 0.3037 0.3238 0.1023  -0.0211 -0.0614 601  VAL B N   
13669 C CA  . VAL B 603  ? 0.2950 0.2819 0.2972 0.1008  -0.0168 -0.0621 601  VAL B CA  
13670 C C   . VAL B 603  ? 0.2867 0.2667 0.2830 0.0965  -0.0169 -0.0622 601  VAL B C   
13671 O O   . VAL B 603  ? 0.3531 0.3209 0.3401 0.0965  -0.0185 -0.0631 601  VAL B O   
13672 C CB  . VAL B 603  ? 0.2973 0.2847 0.2976 0.1049  -0.0145 -0.0640 601  VAL B CB  
13673 C CG1 . VAL B 603  ? 0.2798 0.2752 0.2829 0.1031  -0.0099 -0.0647 601  VAL B CG1 
13674 C CG2 . VAL B 603  ? 0.3266 0.3205 0.3326 0.1093  -0.0147 -0.0640 601  VAL B CG2 
13675 N N   . VAL B 604  ? 0.2340 0.2216 0.2357 0.0927  -0.0152 -0.0612 602  VAL B N   
13676 C CA  . VAL B 604  ? 0.2352 0.2171 0.2321 0.0886  -0.0154 -0.0612 602  VAL B CA  
13677 C C   . VAL B 604  ? 0.2561 0.2388 0.2500 0.0881  -0.0121 -0.0627 602  VAL B C   
13678 O O   . VAL B 604  ? 0.2563 0.2298 0.2420 0.0855  -0.0130 -0.0630 602  VAL B O   
13679 C CB  . VAL B 604  ? 0.2081 0.1975 0.2116 0.0832  -0.0151 -0.0584 602  VAL B CB  
13680 C CG1 . VAL B 604  ? 0.2153 0.1993 0.2138 0.0767  -0.0154 -0.0567 602  VAL B CG1 
13681 C CG2 . VAL B 604  ? 0.2257 0.2145 0.2320 0.0839  -0.0184 -0.0571 602  VAL B CG2 
13682 N N   . GLY B 605  ? 0.2218 0.2151 0.2214 0.0897  -0.0085 -0.0631 603  GLY B N   
13683 C CA  . GLY B 605  ? 0.2244 0.2190 0.2212 0.0890  -0.0053 -0.0643 603  GLY B CA  
13684 C C   . GLY B 605  ? 0.2352 0.2422 0.2393 0.0908  -0.0013 -0.0643 603  GLY B C   
13685 O O   . GLY B 605  ? 0.2478 0.2611 0.2583 0.0931  -0.0014 -0.0637 603  GLY B O   
13686 N N   . SER B 606  ? 0.2093 0.2200 0.2125 0.0895  0.0021  -0.0649 604  SER B N   
13687 C CA  A SER B 606  ? 0.2313 0.2530 0.2403 0.0908  0.0062  -0.0649 604  SER B CA  
13688 C CA  B SER B 606  ? 0.2313 0.2529 0.2402 0.0908  0.0062  -0.0649 604  SER B CA  
13689 C CA  C SER B 606  ? 0.2313 0.2531 0.2404 0.0908  0.0062  -0.0649 604  SER B CA  
13690 C C   . SER B 606  ? 0.2278 0.2571 0.2402 0.0867  0.0092  -0.0639 604  SER B C   
13691 O O   . SER B 606  ? 0.2350 0.2591 0.2418 0.0841  0.0090  -0.0642 604  SER B O   
13692 C CB  A SER B 606  ? 0.2615 0.2788 0.2642 0.0944  0.0079  -0.0670 604  SER B CB  
13693 C CB  B SER B 606  ? 0.2618 0.2785 0.2641 0.0944  0.0078  -0.0671 604  SER B CB  
13694 C CB  C SER B 606  ? 0.2612 0.2789 0.2643 0.0945  0.0079  -0.0670 604  SER B CB  
13695 O OG  A SER B 606  ? 0.2781 0.2910 0.2796 0.0988  0.0058  -0.0678 604  SER B OG  
13696 O OG  B SER B 606  ? 0.2336 0.2597 0.2393 0.0944  0.0123  -0.0672 604  SER B OG  
13697 O OG  C SER B 606  ? 0.2394 0.2500 0.2340 0.0928  0.0084  -0.0681 604  SER B OG  
13698 N N   . VAL B 607  ? 0.1943 0.2359 0.2158 0.0859  0.0119  -0.0625 605  VAL B N   
13699 C CA  . VAL B 607  ? 0.1815 0.2307 0.2066 0.0819  0.0149  -0.0612 605  VAL B CA  
13700 C C   . VAL B 607  ? 0.1826 0.2399 0.2104 0.0832  0.0193  -0.0614 605  VAL B C   
13701 O O   . VAL B 607  ? 0.1878 0.2503 0.2204 0.0859  0.0201  -0.0614 605  VAL B O   
13702 C CB  . VAL B 607  ? 0.1641 0.2204 0.1976 0.0785  0.0140  -0.0590 605  VAL B CB  
13703 C CG1 . VAL B 607  ? 0.1956 0.2589 0.2370 0.0803  0.0136  -0.0582 605  VAL B CG1 
13704 C CG2 . VAL B 607  ? 0.1524 0.2161 0.1892 0.0743  0.0172  -0.0576 605  VAL B CG2 
13705 N N   . THR B 608  ? 0.1921 0.2504 0.2165 0.0811  0.0221  -0.0615 606  THR B N   
13706 C CA  . THR B 608  ? 0.1833 0.2496 0.2102 0.0814  0.0267  -0.0613 606  THR B CA  
13707 C C   . THR B 608  ? 0.1710 0.2462 0.2044 0.0766  0.0286  -0.0589 606  THR B C   
13708 O O   . THR B 608  ? 0.1763 0.2490 0.2068 0.0734  0.0281  -0.0583 606  THR B O   
13709 C CB  . THR B 608  ? 0.1899 0.2500 0.2072 0.0826  0.0284  -0.0632 606  THR B CB  
13710 O OG1 . THR B 608  ? 0.2249 0.2763 0.2363 0.0869  0.0263  -0.0654 606  THR B OG1 
13711 C CG2 . THR B 608  ? 0.2047 0.2732 0.2242 0.0826  0.0333  -0.0628 606  THR B CG2 
13712 N N   . GLU B 609  ? 0.1846 0.2700 0.2267 0.0762  0.0306  -0.0574 607  GLU B N   
13713 C CA  . GLU B 609  ? 0.1780 0.2712 0.2267 0.0715  0.0318  -0.0549 607  GLU B CA  
13714 C C   . GLU B 609  ? 0.1841 0.2830 0.2325 0.0695  0.0365  -0.0542 607  GLU B C   
13715 O O   . GLU B 609  ? 0.1976 0.2969 0.2429 0.0722  0.0391  -0.0554 607  GLU B O   
13716 C CB  . GLU B 609  ? 0.2358 0.3360 0.2940 0.0713  0.0307  -0.0536 607  GLU B CB  
13717 C CG  . GLU B 609  ? 0.2534 0.3473 0.3111 0.0722  0.0259  -0.0540 607  GLU B CG  
13718 C CD  . GLU B 609  ? 0.2861 0.3859 0.3522 0.0720  0.0241  -0.0528 607  GLU B CD  
13719 O OE1 . GLU B 609  ? 0.3262 0.4334 0.3977 0.0734  0.0259  -0.0525 607  GLU B OE1 
13720 O OE2 . GLU B 609  ? 0.2807 0.3776 0.3479 0.0704  0.0208  -0.0521 607  GLU B OE2 
13721 N N   . THR B 610  ? 0.1886 0.2915 0.2398 0.0649  0.0374  -0.0521 608  THR B N   
13722 C CA  . THR B 610  ? 0.1567 0.2631 0.2060 0.0623  0.0412  -0.0511 608  THR B CA  
13723 C C   . THR B 610  ? 0.1570 0.2738 0.2137 0.0611  0.0447  -0.0494 608  THR B C   
13724 O O   . THR B 610  ? 0.2083 0.3308 0.2731 0.0592  0.0438  -0.0479 608  THR B O   
13725 C CB  . THR B 610  ? 0.1610 0.2664 0.2097 0.0577  0.0404  -0.0495 608  THR B CB  
13726 O OG1 . THR B 610  ? 0.1634 0.2591 0.2063 0.0582  0.0365  -0.0505 608  THR B OG1 
13727 C CG2 . THR B 610  ? 0.1584 0.2656 0.2029 0.0554  0.0440  -0.0486 608  THR B CG2 
13728 N N   . SER B 611  ? 0.1742 0.2935 0.2281 0.0620  0.0486  -0.0498 609  SER B N   
13729 C CA  . SER B 611  ? 0.1894 0.3187 0.2501 0.0601  0.0523  -0.0479 609  SER B CA  
13730 C C   . SER B 611  ? 0.1833 0.3159 0.2462 0.0544  0.0533  -0.0452 609  SER B C   
13731 O O   . SER B 611  ? 0.1868 0.3142 0.2441 0.0525  0.0524  -0.0450 609  SER B O   
13732 C CB  . SER B 611  ? 0.2239 0.3547 0.2806 0.0624  0.0564  -0.0490 609  SER B CB  
13733 O OG  . SER B 611  ? 0.2059 0.3332 0.2548 0.0606  0.0583  -0.0488 609  SER B OG  
13734 N N   . GLU B 612  ? 0.2121 0.3534 0.2830 0.0516  0.0551  -0.0430 610  GLU B N   
13735 C CA  . GLU B 612  ? 0.2093 0.3536 0.2822 0.0461  0.0563  -0.0403 610  GLU B CA  
13736 C C   . GLU B 612  ? 0.2363 0.3792 0.3020 0.0448  0.0598  -0.0398 610  GLU B C   
13737 O O   . GLU B 612  ? 0.1882 0.3288 0.2509 0.0413  0.0596  -0.0384 610  GLU B O   
13738 C CB  . GLU B 612  ? 0.2877 0.4415 0.3702 0.0434  0.0577  -0.0382 610  GLU B CB  
13739 C CG  . GLU B 612  ? 0.3159 0.4711 0.4056 0.0436  0.0539  -0.0382 610  GLU B CG  
13740 C CD  . GLU B 612  ? 0.4003 0.5647 0.4992 0.0404  0.0551  -0.0361 610  GLU B CD  
13741 O OE1 . GLU B 612  ? 0.4598 0.6274 0.5600 0.0357  0.0572  -0.0338 610  GLU B OE1 
13742 O OE2 . GLU B 612  ? 0.4625 0.6309 0.5672 0.0426  0.0538  -0.0367 610  GLU B OE2 
13743 N N   . GLU B 613  ? 0.2539 0.3980 0.3163 0.0476  0.0630  -0.0410 611  GLU B N   
13744 C CA  . GLU B 613  ? 0.2286 0.3707 0.2830 0.0468  0.0662  -0.0408 611  GLU B CA  
13745 C C   . GLU B 613  ? 0.2175 0.3503 0.2629 0.0474  0.0636  -0.0421 611  GLU B C   
13746 O O   . GLU B 613  ? 0.2362 0.3673 0.2768 0.0444  0.0646  -0.0407 611  GLU B O   
13747 C CB  . GLU B 613  ? 0.2726 0.4166 0.3246 0.0505  0.0695  -0.0424 611  GLU B CB  
13748 C CG  . GLU B 613  ? 0.2965 0.4370 0.3386 0.0507  0.0725  -0.0428 611  GLU B CG  
13749 C CD  . GLU B 613  ? 0.4723 0.6146 0.5122 0.0545  0.0759  -0.0447 611  GLU B CD  
13750 O OE1 . GLU B 613  ? 0.4852 0.6356 0.5325 0.0545  0.0784  -0.0438 611  GLU B OE1 
13751 O OE2 . GLU B 613  ? 0.5115 0.6469 0.5423 0.0577  0.0758  -0.0470 611  GLU B OE2 
13752 N N   . ASP B 614  ? 0.2148 0.3414 0.2576 0.0512  0.0603  -0.0446 612  ASP B N   
13753 C CA  . ASP B 614  ? 0.2107 0.3284 0.2452 0.0517  0.0576  -0.0460 612  ASP B CA  
13754 C C   . ASP B 614  ? 0.2098 0.3260 0.2466 0.0478  0.0548  -0.0441 612  ASP B C   
13755 O O   . ASP B 614  ? 0.1811 0.2894 0.2109 0.0454  0.0529  -0.0431 612  ASP B O   
13756 C CB  . ASP B 614  ? 0.1912 0.3020 0.2222 0.0566  0.0548  -0.0491 612  ASP B CB  
13757 C CG  . ASP B 614  ? 0.2500 0.3584 0.2744 0.0604  0.0572  -0.0513 612  ASP B CG  
13758 O OD1 . ASP B 614  ? 0.3083 0.4181 0.3282 0.0591  0.0606  -0.0506 612  ASP B OD1 
13759 O OD2 . ASP B 614  ? 0.2872 0.3919 0.3106 0.0646  0.0556  -0.0536 612  ASP B OD2 
13760 N N   . ALA B 615  ? 0.1790 0.3004 0.2250 0.0463  0.0536  -0.0430 613  ALA B N   
13761 C CA  . ALA B 615  ? 0.1677 0.2859 0.2155 0.0415  0.0508  -0.0402 613  ALA B CA  
13762 C C   . ALA B 615  ? 0.1811 0.3000 0.2264 0.0370  0.0531  -0.0372 613  ALA B C   
13763 O O   . ALA B 615  ? 0.1653 0.2772 0.2057 0.0342  0.0509  -0.0356 613  ALA B O   
13764 C CB  . ALA B 615  ? 0.1784 0.3029 0.2365 0.0406  0.0495  -0.0396 613  ALA B CB  
13765 N N   . ARG B 616  ? 0.1821 0.3095 0.2304 0.0362  0.0576  -0.0365 614  ARG B N   
13766 C CA  . ARG B 616  ? 0.2066 0.3342 0.2518 0.0320  0.0599  -0.0335 614  ARG B CA  
13767 C C   . ARG B 616  ? 0.1876 0.3076 0.2217 0.0327  0.0600  -0.0339 614  ARG B C   
13768 O O   . ARG B 616  ? 0.1901 0.3053 0.2198 0.0292  0.0591  -0.0315 614  ARG B O   
13769 C CB  . ARG B 616  ? 0.1996 0.3380 0.2500 0.0310  0.0649  -0.0327 614  ARG B CB  
13770 C CG  . ARG B 616  ? 0.2318 0.3769 0.2929 0.0284  0.0643  -0.0313 614  ARG B CG  
13771 C CD  . ARG B 616  ? 0.3379 0.4907 0.4035 0.0260  0.0683  -0.0292 614  ARG B CD  
13772 N NE  . ARG B 616  ? 0.3837 0.5400 0.4512 0.0299  0.0700  -0.0309 614  ARG B NE  
13773 C CZ  . ARG B 616  ? 0.3556 0.5156 0.4306 0.0317  0.0685  -0.0317 614  ARG B CZ  
13774 N NH1 . ARG B 616  ? 0.4074 0.5681 0.4886 0.0299  0.0651  -0.0311 614  ARG B NH1 
13775 N NH2 . ARG B 616  ? 0.3654 0.5286 0.4417 0.0355  0.0702  -0.0333 614  ARG B NH2 
13776 N N   . ARG B 617  ? 0.2020 0.3206 0.2314 0.0373  0.0609  -0.0370 615  ARG B N   
13777 C CA  . ARG B 617  ? 0.1977 0.3086 0.2161 0.0380  0.0607  -0.0377 615  ARG B CA  
13778 C C   . ARG B 617  ? 0.1767 0.2780 0.1911 0.0363  0.0557  -0.0370 615  ARG B C   
13779 O O   . ARG B 617  ? 0.1942 0.2904 0.2019 0.0339  0.0550  -0.0354 615  ARG B O   
13780 C CB  . ARG B 617  ? 0.2282 0.3384 0.2425 0.0436  0.0619  -0.0416 615  ARG B CB  
13781 C CG  . ARG B 617  ? 0.2949 0.3975 0.2974 0.0445  0.0619  -0.0427 615  ARG B CG  
13782 C CD  . ARG B 617  ? 0.3578 0.4623 0.3566 0.0497  0.0651  -0.0461 615  ARG B CD  
13783 N NE  . ARG B 617  ? 0.3355 0.4366 0.3349 0.0543  0.0626  -0.0495 615  ARG B NE  
13784 C CZ  . ARG B 617  ? 0.4111 0.5018 0.4026 0.0560  0.0590  -0.0515 615  ARG B CZ  
13785 N NH1 . ARG B 617  ? 0.3953 0.4786 0.3784 0.0533  0.0573  -0.0505 615  ARG B NH1 
13786 N NH2 . ARG B 617  ? 0.4045 0.4922 0.3967 0.0603  0.0570  -0.0544 615  ARG B NH2 
13787 N N   . ALA B 618  ? 0.1660 0.2651 0.1845 0.0375  0.0521  -0.0381 616  ALA B N   
13788 C CA  . ALA B 618  ? 0.1605 0.2513 0.1759 0.0358  0.0475  -0.0374 616  ALA B CA  
13789 C C   . ALA B 618  ? 0.1662 0.2565 0.1827 0.0309  0.0468  -0.0337 616  ALA B C   
13790 O O   . ALA B 618  ? 0.1669 0.2508 0.1778 0.0292  0.0445  -0.0326 616  ALA B O   
13791 C CB  . ALA B 618  ? 0.1524 0.2420 0.1729 0.0376  0.0443  -0.0388 616  ALA B CB  
13792 N N   . VAL B 619  ? 0.1775 0.2746 0.2013 0.0287  0.0487  -0.0318 617  VAL B N   
13793 C CA  . VAL B 619  ? 0.1569 0.2526 0.1811 0.0243  0.0479  -0.0284 617  VAL B CA  
13794 C C   . VAL B 619  ? 0.1836 0.2773 0.2004 0.0227  0.0500  -0.0268 617  VAL B C   
13795 O O   . VAL B 619  ? 0.1999 0.2884 0.2127 0.0204  0.0479  -0.0248 617  VAL B O   
13796 C CB  . VAL B 619  ? 0.1713 0.2738 0.2045 0.0219  0.0493  -0.0267 617  VAL B CB  
13797 C CG1 . VAL B 619  ? 0.2009 0.3008 0.2338 0.0176  0.0484  -0.0232 617  VAL B CG1 
13798 C CG2 . VAL B 619  ? 0.1721 0.2760 0.2121 0.0234  0.0468  -0.0282 617  VAL B CG2 
13799 N N   . ARG B 620  ? 0.1812 0.2790 0.1957 0.0241  0.0539  -0.0276 618  ARG B N   
13800 C CA  . ARG B 620  ? 0.2014 0.2970 0.2077 0.0229  0.0558  -0.0263 618  ARG B CA  
13801 C C   . ARG B 620  ? 0.2015 0.2886 0.1991 0.0242  0.0527  -0.0274 618  ARG B C   
13802 O O   . ARG B 620  ? 0.2067 0.2895 0.1987 0.0219  0.0517  -0.0253 618  ARG B O   
13803 C CB  . ARG B 620  ? 0.2587 0.3605 0.2640 0.0247  0.0609  -0.0274 618  ARG B CB  
13804 C CG  . ARG B 620  ? 0.3213 0.4324 0.3353 0.0227  0.0643  -0.0258 618  ARG B CG  
13805 C CD  . ARG B 620  ? 0.4023 0.5195 0.4140 0.0234  0.0697  -0.0259 618  ARG B CD  
13806 N NE  . ARG B 620  ? 0.4409 0.5577 0.4482 0.0283  0.0708  -0.0296 618  ARG B NE  
13807 C CZ  . ARG B 620  ? 0.3800 0.5024 0.3928 0.0320  0.0720  -0.0324 618  ARG B CZ  
13808 N NH1 . ARG B 620  ? 0.3595 0.4890 0.3828 0.0313  0.0722  -0.0319 618  ARG B NH1 
13809 N NH2 . ARG B 620  ? 0.4273 0.5479 0.4348 0.0367  0.0728  -0.0358 618  ARG B NH2 
13810 N N   . LEU B 621  ? 0.1895 0.2738 0.1860 0.0276  0.0509  -0.0307 619  LEU B N   
13811 C CA  . LEU B 621  ? 0.2192 0.2953 0.2076 0.0283  0.0475  -0.0318 619  LEU B CA  
13812 C C   . LEU B 621  ? 0.2233 0.2949 0.2127 0.0255  0.0434  -0.0297 619  LEU B C   
13813 O O   . LEU B 621  ? 0.2213 0.2877 0.2042 0.0242  0.0413  -0.0287 619  LEU B O   
13814 C CB  . LEU B 621  ? 0.2316 0.3050 0.2187 0.0324  0.0462  -0.0357 619  LEU B CB  
13815 C CG  . LEU B 621  ? 0.2216 0.2978 0.2058 0.0361  0.0499  -0.0384 619  LEU B CG  
13816 C CD1 . LEU B 621  ? 0.2280 0.3014 0.2122 0.0403  0.0482  -0.0420 619  LEU B CD1 
13817 C CD2 . LEU B 621  ? 0.2811 0.3534 0.2547 0.0360  0.0511  -0.0385 619  LEU B CD2 
13818 N N   . ALA B 622  ? 0.1809 0.2548 0.1784 0.0246  0.0421  -0.0289 620  ALA B N   
13819 C CA  . ALA B 622  ? 0.1515 0.2219 0.1505 0.0220  0.0385  -0.0268 620  ALA B CA  
13820 C C   . ALA B 622  ? 0.1892 0.2597 0.1863 0.0189  0.0394  -0.0234 620  ALA B C   
13821 O O   . ALA B 622  ? 0.1842 0.2501 0.1777 0.0174  0.0366  -0.0220 620  ALA B O   
13822 C CB  . ALA B 622  ? 0.1649 0.2381 0.1727 0.0218  0.0374  -0.0268 620  ALA B CB  
13823 N N   . ALA B 623  ? 0.1812 0.2568 0.1805 0.0177  0.0431  -0.0220 621  ALA B N   
13824 C CA  . ALA B 623  ? 0.1876 0.2626 0.1844 0.0148  0.0439  -0.0186 621  ALA B CA  
13825 C C   . ALA B 623  ? 0.1888 0.2594 0.1758 0.0150  0.0436  -0.0184 621  ALA B C   
13826 O O   . ALA B 623  ? 0.2085 0.2754 0.1922 0.0132  0.0416  -0.0161 621  ALA B O   
13827 C CB  . ALA B 623  ? 0.1964 0.2776 0.1969 0.0133  0.0482  -0.0172 621  ALA B CB  
13828 N N   . ASP B 624  ? 0.2111 0.2820 0.1934 0.0174  0.0454  -0.0209 622  ASP B N   
13829 C CA  . ASP B 624  ? 0.2404 0.3069 0.2128 0.0176  0.0451  -0.0209 622  ASP B CA  
13830 C C   . ASP B 624  ? 0.2645 0.3248 0.2336 0.0173  0.0401  -0.0210 622  ASP B C   
13831 O O   . ASP B 624  ? 0.3246 0.3815 0.2874 0.0160  0.0387  -0.0194 622  ASP B O   
13832 C CB  . ASP B 624  ? 0.2799 0.3472 0.2476 0.0207  0.0476  -0.0241 622  ASP B CB  
13833 C CG  . ASP B 624  ? 0.3667 0.4408 0.3367 0.0210  0.0529  -0.0238 622  ASP B CG  
13834 O OD1 . ASP B 624  ? 0.4151 0.4922 0.3876 0.0181  0.0547  -0.0206 622  ASP B OD1 
13835 O OD2 . ASP B 624  ? 0.4007 0.4771 0.3697 0.0240  0.0552  -0.0267 622  ASP B OD2 
13836 N N   . ALA B 625  ? 0.2465 0.3055 0.2197 0.0184  0.0374  -0.0228 623  ALA B N   
13837 C CA  . ALA B 625  ? 0.3430 0.3967 0.3136 0.0180  0.0329  -0.0231 623  ALA B CA  
13838 C C   . ALA B 625  ? 0.2775 0.3310 0.2530 0.0158  0.0304  -0.0204 623  ALA B C   
13839 O O   . ALA B 625  ? 0.2609 0.3108 0.2348 0.0151  0.0267  -0.0202 623  ALA B O   
13840 C CB  . ALA B 625  ? 0.3758 0.4274 0.3473 0.0203  0.0312  -0.0265 623  ALA B CB  
13841 N N   . ALA B 626  ? 0.2155 0.2728 0.1970 0.0145  0.0323  -0.0184 624  ALA B N   
13842 C CA  . ALA B 626  ? 0.2120 0.2688 0.1981 0.0127  0.0299  -0.0161 624  ALA B CA  
13843 C C   . ALA B 626  ? 0.2142 0.2675 0.1954 0.0114  0.0274  -0.0139 624  ALA B C   
13844 O O   . ALA B 626  ? 0.2113 0.2628 0.1945 0.0110  0.0241  -0.0135 624  ALA B O   
13845 C CB  . ALA B 626  ? 0.1807 0.2414 0.1728 0.0114  0.0325  -0.0143 624  ALA B CB  
13846 N N   . PRO B 627  ? 0.2122 0.2646 0.1871 0.0108  0.0286  -0.0124 625  PRO B N   
13847 C CA  . PRO B 627  ? 0.2313 0.2805 0.2019 0.0097  0.0257  -0.0103 625  PRO B CA  
13848 C C   . PRO B 627  ? 0.2341 0.2803 0.2015 0.0103  0.0220  -0.0120 625  PRO B C   
13849 O O   . PRO B 627  ? 0.2272 0.2720 0.1950 0.0095  0.0187  -0.0105 625  PRO B O   
13850 C CB  . PRO B 627  ? 0.2749 0.3238 0.2387 0.0092  0.0281  -0.0087 625  PRO B CB  
13851 C CG  . PRO B 627  ? 0.2943 0.3470 0.2614 0.0091  0.0325  -0.0089 625  PRO B CG  
13852 C CD  . PRO B 627  ? 0.2509 0.3055 0.2230 0.0107  0.0328  -0.0121 625  PRO B CD  
13853 N N   . ASP B 628  ? 0.2354 0.2803 0.1992 0.0117  0.0223  -0.0150 626  ASP B N   
13854 C CA  . ASP B 628  ? 0.2582 0.2996 0.2183 0.0119  0.0186  -0.0166 626  ASP B CA  
13855 C C   . ASP B 628  ? 0.2283 0.2698 0.1948 0.0116  0.0159  -0.0171 626  ASP B C   
13856 O O   . ASP B 628  ? 0.2502 0.2898 0.2157 0.0107  0.0124  -0.0167 626  ASP B O   
13857 C CB  . ASP B 628  ? 0.2634 0.3026 0.2177 0.0135  0.0195  -0.0200 626  ASP B CB  
13858 C CG  . ASP B 628  ? 0.3612 0.3999 0.3080 0.0138  0.0219  -0.0197 626  ASP B CG  
13859 O OD1 . ASP B 628  ? 0.3510 0.3895 0.2948 0.0124  0.0213  -0.0170 626  ASP B OD1 
13860 O OD2 . ASP B 628  ? 0.4254 0.4640 0.3692 0.0157  0.0244  -0.0222 626  ASP B OD2 
13861 N N   . TRP B 629  ? 0.2086 0.2524 0.1816 0.0123  0.0176  -0.0179 627  TRP B N   
13862 C CA  . TRP B 629  ? 0.1882 0.2319 0.1668 0.0121  0.0153  -0.0182 627  TRP B CA  
13863 C C   . TRP B 629  ? 0.1848 0.2299 0.1674 0.0106  0.0140  -0.0152 627  TRP B C   
13864 O O   . TRP B 629  ? 0.1849 0.2291 0.1690 0.0099  0.0110  -0.0148 627  TRP B O   
13865 C CB  . TRP B 629  ? 0.1670 0.2127 0.1510 0.0135  0.0173  -0.0200 627  TRP B CB  
13866 C CG  . TRP B 629  ? 0.1522 0.1975 0.1414 0.0132  0.0150  -0.0203 627  TRP B CG  
13867 C CD1 . TRP B 629  ? 0.1542 0.2022 0.1504 0.0130  0.0156  -0.0194 627  TRP B CD1 
13868 C CD2 . TRP B 629  ? 0.1571 0.1992 0.1448 0.0130  0.0118  -0.0215 627  TRP B CD2 
13869 N NE1 . TRP B 629  ? 0.1530 0.1995 0.1517 0.0128  0.0131  -0.0200 627  TRP B NE1 
13870 C CE2 . TRP B 629  ? 0.1381 0.1812 0.1320 0.0127  0.0107  -0.0212 627  TRP B CE2 
13871 C CE3 . TRP B 629  ? 0.1941 0.2324 0.1755 0.0127  0.0095  -0.0228 627  TRP B CE3 
13872 C CZ2 . TRP B 629  ? 0.1617 0.2023 0.1556 0.0121  0.0078  -0.0219 627  TRP B CZ2 
13873 C CZ3 . TRP B 629  ? 0.1833 0.2190 0.1651 0.0120  0.0064  -0.0235 627  TRP B CZ3 
13874 C CH2 . TRP B 629  ? 0.1947 0.2317 0.1828 0.0116  0.0057  -0.0230 627  TRP B CH2 
13875 N N   . ALA B 630  ? 0.1697 0.2167 0.1537 0.0101  0.0162  -0.0130 628  ALA B N   
13876 C CA  . ALA B 630  ? 0.1769 0.2245 0.1638 0.0091  0.0149  -0.0102 628  ALA B CA  
13877 C C   . ALA B 630  ? 0.2160 0.2618 0.1985 0.0085  0.0118  -0.0089 628  ALA B C   
13878 O O   . ALA B 630  ? 0.2074 0.2537 0.1929 0.0081  0.0096  -0.0074 628  ALA B O   
13879 C CB  . ALA B 630  ? 0.1891 0.2379 0.1766 0.0085  0.0178  -0.0080 628  ALA B CB  
13880 N N   . ALA B 631  ? 0.2139 0.2580 0.1895 0.0086  0.0115  -0.0096 629  ALA B N   
13881 C CA  . ALA B 631  ? 0.1887 0.2315 0.1600 0.0079  0.0083  -0.0085 629  ALA B CA  
13882 C C   . ALA B 631  ? 0.2232 0.2651 0.1950 0.0074  0.0049  -0.0100 629  ALA B C   
13883 O O   . ALA B 631  ? 0.2518 0.2934 0.2215 0.0066  0.0018  -0.0089 629  ALA B O   
13884 C CB  . ALA B 631  ? 0.2243 0.2652 0.1872 0.0079  0.0090  -0.0086 629  ALA B CB  
13885 N N   . VAL B 632  ? 0.2025 0.2439 0.1771 0.0079  0.0052  -0.0124 630  VAL B N   
13886 C CA  . VAL B 632  ? 0.1899 0.2304 0.1657 0.0071  0.0020  -0.0135 630  VAL B CA  
13887 C C   . VAL B 632  ? 0.1991 0.2423 0.1812 0.0065  0.0007  -0.0113 630  VAL B C   
13888 O O   . VAL B 632  ? 0.2066 0.2515 0.1940 0.0072  0.0026  -0.0108 630  VAL B O   
13889 C CB  . VAL B 632  ? 0.1983 0.2371 0.1752 0.0078  0.0027  -0.0165 630  VAL B CB  
13890 C CG1 . VAL B 632  ? 0.2001 0.2376 0.1780 0.0066  -0.0006 -0.0173 630  VAL B CG1 
13891 C CG2 . VAL B 632  ? 0.2290 0.2651 0.1995 0.0089  0.0042  -0.0187 630  VAL B CG2 
13892 N N   . PRO B 633  ? 0.1774 0.2214 0.1593 0.0054  -0.0024 -0.0101 631  PRO B N   
13893 C CA  . PRO B 633  ? 0.1798 0.2269 0.1675 0.0053  -0.0033 -0.0080 631  PRO B CA  
13894 C C   . PRO B 633  ? 0.1782 0.2259 0.1717 0.0055  -0.0027 -0.0090 631  PRO B C   
13895 O O   . PRO B 633  ? 0.1679 0.2138 0.1608 0.0051  -0.0032 -0.0112 631  PRO B O   
13896 C CB  . PRO B 633  ? 0.2128 0.2609 0.1990 0.0040  -0.0070 -0.0071 631  PRO B CB  
13897 C CG  . PRO B 633  ? 0.2433 0.2890 0.2220 0.0036  -0.0077 -0.0078 631  PRO B CG  
13898 C CD  . PRO B 633  ? 0.1944 0.2370 0.1704 0.0043  -0.0052 -0.0104 631  PRO B CD  
13899 N N   . PRO B 634  ? 0.1807 0.2305 0.1794 0.0061  -0.0018 -0.0075 632  PRO B N   
13900 C CA  . PRO B 634  ? 0.1752 0.2255 0.1791 0.0063  -0.0012 -0.0084 632  PRO B CA  
13901 C C   . PRO B 634  ? 0.1576 0.2079 0.1622 0.0051  -0.0035 -0.0095 632  PRO B C   
13902 O O   . PRO B 634  ? 0.1412 0.1901 0.1470 0.0052  -0.0031 -0.0112 632  PRO B O   
13903 C CB  . PRO B 634  ? 0.1652 0.2177 0.1735 0.0071  -0.0007 -0.0062 632  PRO B CB  
13904 C CG  . PRO B 634  ? 0.2426 0.2946 0.2479 0.0076  0.0004  -0.0046 632  PRO B CG  
13905 C CD  . PRO B 634  ? 0.2160 0.2671 0.2155 0.0069  -0.0011 -0.0049 632  PRO B CD  
13906 N N   . SER B 635  ? 0.1772 0.2291 0.1811 0.0040  -0.0061 -0.0083 633  SER B N   
13907 C CA  . SER B 635  ? 0.2081 0.2601 0.2127 0.0024  -0.0084 -0.0091 633  SER B CA  
13908 C C   . SER B 635  ? 0.1881 0.2360 0.1879 0.0016  -0.0089 -0.0116 633  SER B C   
13909 O O   . SER B 635  ? 0.1688 0.2151 0.1692 0.0006  -0.0098 -0.0129 633  SER B O   
13910 C CB  . SER B 635  ? 0.2627 0.3181 0.2676 0.0012  -0.0111 -0.0074 633  SER B CB  
13911 O OG  . SER B 635  ? 0.3274 0.3818 0.3271 0.0009  -0.0122 -0.0071 633  SER B OG  
13912 N N   . GLU B 636  ? 0.1697 0.2153 0.1641 0.0021  -0.0084 -0.0124 634  GLU B N   
13913 C CA  . GLU B 636  ? 0.1616 0.2027 0.1510 0.0017  -0.0088 -0.0150 634  GLU B CA  
13914 C C   . GLU B 636  ? 0.1771 0.2163 0.1678 0.0035  -0.0062 -0.0168 634  GLU B C   
13915 O O   . GLU B 636  ? 0.1479 0.1836 0.1369 0.0033  -0.0068 -0.0188 634  GLU B O   
13916 C CB  . GLU B 636  ? 0.1817 0.2210 0.1644 0.0018  -0.0091 -0.0153 634  GLU B CB  
13917 C CG  . GLU B 636  ? 0.2479 0.2821 0.2247 0.0019  -0.0092 -0.0182 634  GLU B CG  
13918 C CD  . GLU B 636  ? 0.3184 0.3497 0.2939 0.0000  -0.0122 -0.0195 634  GLU B CD  
13919 O OE1 . GLU B 636  ? 0.3160 0.3496 0.2934 -0.0022 -0.0148 -0.0180 634  GLU B OE1 
13920 O OE2 . GLU B 636  ? 0.3258 0.3525 0.2983 0.0006  -0.0119 -0.0220 634  GLU B OE2 
13921 N N   . ARG B 637  ? 0.1405 0.1818 0.1343 0.0050  -0.0035 -0.0160 635  ARG B N   
13922 C CA  . ARG B 637  ? 0.1409 0.1814 0.1371 0.0065  -0.0013 -0.0175 635  ARG B CA  
13923 C C   . ARG B 637  ? 0.1418 0.1823 0.1421 0.0060  -0.0024 -0.0177 635  ARG B C   
13924 O O   . ARG B 637  ? 0.1340 0.1720 0.1341 0.0066  -0.0023 -0.0197 635  ARG B O   
13925 C CB  . ARG B 637  ? 0.1341 0.1773 0.1334 0.0077  0.0016  -0.0163 635  ARG B CB  
13926 C CG  . ARG B 637  ? 0.1465 0.1897 0.1415 0.0080  0.0029  -0.0158 635  ARG B CG  
13927 C CD  . ARG B 637  ? 0.1422 0.1875 0.1399 0.0089  0.0060  -0.0148 635  ARG B CD  
13928 N NE  . ARG B 637  ? 0.1530 0.2004 0.1556 0.0086  0.0060  -0.0127 635  ARG B NE  
13929 C CZ  . ARG B 637  ? 0.1715 0.2200 0.1741 0.0084  0.0068  -0.0104 635  ARG B CZ  
13930 N NH1 . ARG B 637  ? 0.2200 0.2679 0.2177 0.0083  0.0073  -0.0096 635  ARG B NH1 
13931 N NH2 . ARG B 637  ? 0.1782 0.2279 0.1853 0.0085  0.0071  -0.0089 635  ARG B NH2 
13932 N N   . ALA B 638  ? 0.1277 0.1709 0.1315 0.0049  -0.0036 -0.0158 636  ALA B N   
13933 C CA  . ALA B 638  ? 0.1219 0.1654 0.1292 0.0042  -0.0046 -0.0158 636  ALA B CA  
13934 C C   . ALA B 638  ? 0.1179 0.1580 0.1218 0.0027  -0.0069 -0.0172 636  ALA B C   
13935 O O   . ALA B 638  ? 0.1302 0.1683 0.1352 0.0026  -0.0072 -0.0181 636  ALA B O   
13936 C CB  . ALA B 638  ? 0.1373 0.1847 0.1485 0.0036  -0.0052 -0.0134 636  ALA B CB  
13937 N N   . ALA B 639  ? 0.1375 0.1766 0.1370 0.0014  -0.0087 -0.0172 637  ALA B N   
13938 C CA  . ALA B 639  ? 0.1317 0.1668 0.1274 -0.0005 -0.0111 -0.0185 637  ALA B CA  
13939 C C   . ALA B 639  ? 0.1320 0.1618 0.1241 0.0010  -0.0103 -0.0212 637  ALA B C   
13940 O O   . ALA B 639  ? 0.1506 0.1766 0.1411 0.0001  -0.0118 -0.0223 637  ALA B O   
13941 C CB  . ALA B 639  ? 0.1358 0.1709 0.1272 -0.0022 -0.0133 -0.0180 637  ALA B CB  
13942 N N   . CYS B 640  ? 0.1389 0.1686 0.1299 0.0034  -0.0079 -0.0221 638  CYS B N   
13943 C CA  . CYS B 640  ? 0.1359 0.1616 0.1246 0.0054  -0.0068 -0.0246 638  CYS B CA  
13944 C C   . CYS B 640  ? 0.1281 0.1537 0.1212 0.0062  -0.0064 -0.0249 638  CYS B C   
13945 O O   . CYS B 640  ? 0.1360 0.1572 0.1270 0.0067  -0.0073 -0.0267 638  CYS B O   
13946 C CB  . CYS B 640  ? 0.1422 0.1693 0.1300 0.0077  -0.0039 -0.0253 638  CYS B CB  
13947 S SG  . CYS B 640  ? 0.1679 0.1937 0.1487 0.0074  -0.0042 -0.0256 638  CYS B SG  
13948 N N   . LEU B 641  ? 0.1138 0.1440 0.1128 0.0064  -0.0050 -0.0232 639  LEU B N   
13949 C CA  . LEU B 641  ? 0.1016 0.1318 0.1046 0.0071  -0.0048 -0.0234 639  LEU B CA  
13950 C C   . LEU B 641  ? 0.1225 0.1500 0.1246 0.0050  -0.0073 -0.0232 639  LEU B C   
13951 O O   . LEU B 641  ? 0.1308 0.1549 0.1324 0.0056  -0.0078 -0.0244 639  LEU B O   
13952 C CB  . LEU B 641  ? 0.1396 0.1747 0.1483 0.0073  -0.0032 -0.0215 639  LEU B CB  
13953 C CG  . LEU B 641  ? 0.1323 0.1697 0.1436 0.0094  -0.0006 -0.0219 639  LEU B CG  
13954 C CD1 . LEU B 641  ? 0.1602 0.1980 0.1683 0.0100  0.0008  -0.0222 639  LEU B CD1 
13955 C CD2 . LEU B 641  ? 0.1235 0.1647 0.1400 0.0092  0.0004  -0.0200 639  LEU B CD2 
13956 N N   . ASP B 642  ? 0.1177 0.1469 0.1196 0.0025  -0.0089 -0.0216 640  ASP B N   
13957 C CA  . ASP B 642  ? 0.1251 0.1523 0.1263 0.0001  -0.0112 -0.0212 640  ASP B CA  
13958 C C   . ASP B 642  ? 0.1184 0.1388 0.1136 -0.0005 -0.0129 -0.0232 640  ASP B C   
13959 O O   . ASP B 642  ? 0.1460 0.1628 0.1403 -0.0014 -0.0141 -0.0236 640  ASP B O   
13960 C CB  . ASP B 642  ? 0.1405 0.1717 0.1430 -0.0025 -0.0125 -0.0191 640  ASP B CB  
13961 C CG  . ASP B 642  ? 0.1345 0.1714 0.1429 -0.0022 -0.0113 -0.0170 640  ASP B CG  
13962 O OD1 . ASP B 642  ? 0.1308 0.1679 0.1422 -0.0009 -0.0100 -0.0171 640  ASP B OD1 
13963 O OD2 . ASP B 642  ? 0.1814 0.2225 0.1915 -0.0033 -0.0119 -0.0153 640  ASP B OD2 
13964 N N   . ARG B 643  ? 0.1331 0.1513 0.1236 0.0001  -0.0131 -0.0245 641  ARG B N   
13965 C CA  . ARG B 643  ? 0.1373 0.1482 0.1215 0.0000  -0.0147 -0.0267 641  ARG B CA  
13966 C C   . ARG B 643  ? 0.1457 0.1530 0.1298 0.0029  -0.0135 -0.0285 641  ARG B C   
13967 O O   . ARG B 643  ? 0.1444 0.1457 0.1252 0.0025  -0.0152 -0.0296 641  ARG B O   
13968 C CB  . ARG B 643  ? 0.1408 0.1499 0.1196 0.0004  -0.0148 -0.0279 641  ARG B CB  
13969 C CG  . ARG B 643  ? 0.1729 0.1829 0.1495 -0.0030 -0.0173 -0.0267 641  ARG B CG  
13970 C CD  . ARG B 643  ? 0.2094 0.2164 0.1794 -0.0026 -0.0177 -0.0283 641  ARG B CD  
13971 N NE  . ARG B 643  ? 0.1973 0.2084 0.1685 -0.0002 -0.0150 -0.0279 641  ARG B NE  
13972 C CZ  . ARG B 643  ? 0.2053 0.2215 0.1782 -0.0011 -0.0150 -0.0259 641  ARG B CZ  
13973 N NH1 . ARG B 643  ? 0.2176 0.2361 0.1915 -0.0042 -0.0175 -0.0242 641  ARG B NH1 
13974 N NH2 . ARG B 643  ? 0.2370 0.2561 0.2104 0.0011  -0.0124 -0.0256 641  ARG B NH2 
13975 N N   . ALA B 644  ? 0.1313 0.1424 0.1192 0.0058  -0.0108 -0.0287 642  ALA B N   
13976 C CA  . ALA B 644  ? 0.1499 0.1587 0.1386 0.0087  -0.0099 -0.0303 642  ALA B CA  
13977 C C   . ALA B 644  ? 0.1533 0.1611 0.1446 0.0078  -0.0110 -0.0295 642  ALA B C   
13978 O O   . ALA B 644  ? 0.1476 0.1502 0.1367 0.0091  -0.0119 -0.0309 642  ALA B O   
13979 C CB  . ALA B 644  ? 0.1297 0.1438 0.1226 0.0114  -0.0068 -0.0304 642  ALA B CB  
13980 N N   . ALA B 645  ? 0.1332 0.1454 0.1287 0.0057  -0.0110 -0.0272 643  ALA B N   
13981 C CA  . ALA B 645  ? 0.1343 0.1458 0.1320 0.0046  -0.0120 -0.0262 643  ALA B CA  
13982 C C   . ALA B 645  ? 0.1444 0.1495 0.1371 0.0023  -0.0146 -0.0265 643  ALA B C   
13983 O O   . ALA B 645  ? 0.1468 0.1478 0.1385 0.0026  -0.0155 -0.0269 643  ALA B O   
13984 C CB  . ALA B 645  ? 0.1364 0.1541 0.1391 0.0029  -0.0113 -0.0238 643  ALA B CB  
13985 N N   . GLU B 646  ? 0.1412 0.1451 0.1304 -0.0002 -0.0161 -0.0263 644  GLU B N   
13986 C CA  . GLU B 646  ? 0.1626 0.1599 0.1466 -0.0029 -0.0188 -0.0267 644  GLU B CA  
13987 C C   . GLU B 646  ? 0.1848 0.1740 0.1635 -0.0005 -0.0195 -0.0292 644  GLU B C   
13988 O O   . GLU B 646  ? 0.1811 0.1642 0.1567 -0.0015 -0.0213 -0.0294 644  GLU B O   
13989 C CB  . GLU B 646  ? 0.1764 0.1738 0.1573 -0.0059 -0.0205 -0.0263 644  GLU B CB  
13990 C CG  . GLU B 646  ? 0.2205 0.2255 0.2061 -0.0086 -0.0204 -0.0237 644  GLU B CG  
13991 C CD  . GLU B 646  ? 0.3001 0.3061 0.2883 -0.0112 -0.0212 -0.0219 644  GLU B CD  
13992 O OE1 . GLU B 646  ? 0.4124 0.4124 0.3967 -0.0134 -0.0232 -0.0222 644  GLU B OE1 
13993 O OE2 . GLU B 646  ? 0.3125 0.3252 0.3065 -0.0110 -0.0197 -0.0201 644  GLU B OE2 
13994 N N   . LEU B 647  ? 0.1682 0.1573 0.1456 0.0028  -0.0180 -0.0311 645  LEU B N   
13995 C CA  . LEU B 647  ? 0.1765 0.1583 0.1490 0.0058  -0.0185 -0.0337 645  LEU B CA  
13996 C C   . LEU B 647  ? 0.1729 0.1540 0.1483 0.0083  -0.0179 -0.0339 645  LEU B C   
13997 O O   . LEU B 647  ? 0.1976 0.1712 0.1688 0.0092  -0.0196 -0.0351 645  LEU B O   
13998 C CB  . LEU B 647  ? 0.1760 0.1590 0.1469 0.0089  -0.0166 -0.0356 645  LEU B CB  
13999 C CG  . LEU B 647  ? 0.1737 0.1559 0.1402 0.0069  -0.0174 -0.0359 645  LEU B CG  
14000 C CD1 . LEU B 647  ? 0.1914 0.1749 0.1562 0.0103  -0.0151 -0.0378 645  LEU B CD1 
14001 C CD2 . LEU B 647  ? 0.2385 0.2117 0.1976 0.0045  -0.0206 -0.0369 645  LEU B CD2 
14002 N N   . MET B 648  ? 0.1556 0.1439 0.1377 0.0095  -0.0158 -0.0328 646  MET B N   
14003 C CA  . MET B 648  ? 0.1502 0.1381 0.1351 0.0117  -0.0156 -0.0329 646  MET B CA  
14004 C C   . MET B 648  ? 0.1727 0.1569 0.1564 0.0090  -0.0177 -0.0314 646  MET B C   
14005 O O   . MET B 648  ? 0.1954 0.1748 0.1775 0.0106  -0.0187 -0.0321 646  MET B O   
14006 C CB  . MET B 648  ? 0.1676 0.1639 0.1597 0.0131  -0.0131 -0.0319 646  MET B CB  
14007 C CG  . MET B 648  ? 0.1772 0.1771 0.1708 0.0162  -0.0108 -0.0334 646  MET B CG  
14008 S SD  . MET B 648  ? 0.1689 0.1769 0.1707 0.0178  -0.0085 -0.0324 646  MET B SD  
14009 C CE  . MET B 648  ? 0.1659 0.1776 0.1683 0.0205  -0.0058 -0.0340 646  MET B CE  
14010 N N   . GLN B 649  ? 0.1706 0.1570 0.1549 0.0049  -0.0184 -0.0294 647  GLN B N   
14011 C CA  . GLN B 649  ? 0.1905 0.1735 0.1734 0.0019  -0.0202 -0.0279 647  GLN B CA  
14012 C C   . GLN B 649  ? 0.1884 0.1614 0.1639 0.0011  -0.0227 -0.0291 647  GLN B C   
14013 O O   . GLN B 649  ? 0.2180 0.1855 0.1912 0.0011  -0.0241 -0.0289 647  GLN B O   
14014 C CB  . GLN B 649  ? 0.1778 0.1661 0.1632 -0.0022 -0.0202 -0.0256 647  GLN B CB  
14015 C CG  . GLN B 649  ? 0.1874 0.1739 0.1722 -0.0056 -0.0216 -0.0236 647  GLN B CG  
14016 C CD  . GLN B 649  ? 0.1570 0.1468 0.1462 -0.0041 -0.0202 -0.0227 647  GLN B CD  
14017 O OE1 . GLN B 649  ? 0.1744 0.1716 0.1688 -0.0043 -0.0185 -0.0214 647  GLN B OE1 
14018 N NE2 . GLN B 649  ? 0.1759 0.1599 0.1626 -0.0024 -0.0211 -0.0234 647  GLN B NE2 
14019 N N   . ALA B 650  ? 0.1852 0.1551 0.1563 0.0005  -0.0235 -0.0304 648  ALA B N   
14020 C CA  . ALA B 650  ? 0.1817 0.1414 0.1451 -0.0006 -0.0262 -0.0317 648  ALA B CA  
14021 C C   . ALA B 650  ? 0.2326 0.1857 0.1928 0.0041  -0.0263 -0.0340 648  ALA B C   
14022 O O   . ALA B 650  ? 0.2913 0.2355 0.2461 0.0037  -0.0285 -0.0345 648  ALA B O   
14023 C CB  . ALA B 650  ? 0.2274 0.1857 0.1868 -0.0024 -0.0270 -0.0326 648  ALA B CB  
14024 N N   . ARG B 651  ? 0.2144 0.1722 0.1782 0.0085  -0.0240 -0.0354 649  ARG B N   
14025 C CA  . ARG B 651  ? 0.1976 0.1508 0.1593 0.0135  -0.0239 -0.0377 649  ARG B CA  
14026 C C   . ARG B 651  ? 0.2272 0.1832 0.1937 0.0158  -0.0233 -0.0369 649  ARG B C   
14027 O O   . ARG B 651  ? 0.2393 0.1939 0.2060 0.0204  -0.0229 -0.0387 649  ARG B O   
14028 C CB  . ARG B 651  ? 0.2186 0.1751 0.1807 0.0170  -0.0218 -0.0398 649  ARG B CB  
14029 C CG  . ARG B 651  ? 0.2233 0.1758 0.1795 0.0147  -0.0228 -0.0407 649  ARG B CG  
14030 C CD  . ARG B 651  ? 0.2456 0.2015 0.2015 0.0176  -0.0206 -0.0426 649  ARG B CD  
14031 N NE  . ARG B 651  ? 0.2543 0.2069 0.2046 0.0147  -0.0219 -0.0430 649  ARG B NE  
14032 C CZ  . ARG B 651  ? 0.2572 0.2125 0.2061 0.0157  -0.0203 -0.0441 649  ARG B CZ  
14033 N NH1 . ARG B 651  ? 0.2609 0.2221 0.2136 0.0196  -0.0172 -0.0450 649  ARG B NH1 
14034 N NH2 . ARG B 651  ? 0.2612 0.2133 0.2048 0.0126  -0.0220 -0.0443 649  ARG B NH2 
14035 N N   . MET B 652  ? 0.1941 0.1540 0.1644 0.0127  -0.0233 -0.0344 650  MET B N   
14036 C CA  . MET B 652  ? 0.2080 0.1708 0.1828 0.0147  -0.0228 -0.0336 650  MET B CA  
14037 C C   . MET B 652  ? 0.2221 0.1770 0.1930 0.0179  -0.0246 -0.0349 650  MET B C   
14038 O O   . MET B 652  ? 0.2327 0.1905 0.2070 0.0220  -0.0237 -0.0359 650  MET B O   
14039 C CB  . MET B 652  ? 0.2014 0.1676 0.1789 0.0107  -0.0229 -0.0308 650  MET B CB  
14040 C CG  . MET B 652  ? 0.1964 0.1644 0.1773 0.0124  -0.0228 -0.0300 650  MET B CG  
14041 S SD  . MET B 652  ? 0.2301 0.2022 0.2138 0.0081  -0.0225 -0.0269 650  MET B SD  
14042 C CE  . MET B 652  ? 0.2086 0.1918 0.1994 0.0077  -0.0196 -0.0263 650  MET B CE  
14043 N N   . PRO B 653  ? 0.2254 0.1704 0.1892 0.0164  -0.0271 -0.0350 651  PRO B N   
14044 C CA  . PRO B 653  ? 0.2528 0.1899 0.2128 0.0200  -0.0289 -0.0361 651  PRO B CA  
14045 C C   . PRO B 653  ? 0.2462 0.1832 0.2064 0.0259  -0.0281 -0.0390 651  PRO B C   
14046 O O   . PRO B 653  ? 0.2745 0.2115 0.2365 0.0299  -0.0283 -0.0397 651  PRO B O   
14047 C CB  . PRO B 653  ? 0.2462 0.1721 0.1977 0.0167  -0.0318 -0.0358 651  PRO B CB  
14048 C CG  . PRO B 653  ? 0.2684 0.1984 0.2214 0.0106  -0.0315 -0.0334 651  PRO B CG  
14049 C CD  . PRO B 653  ? 0.2537 0.1939 0.2126 0.0113  -0.0288 -0.0339 651  PRO B CD  
14050 N N   . THR B 654  ? 0.2367 0.1740 0.1951 0.0265  -0.0271 -0.0408 652  THR B N   
14051 C CA  . THR B 654  ? 0.2362 0.1743 0.1949 0.0322  -0.0258 -0.0436 652  THR B CA  
14052 C C   . THR B 654  ? 0.2855 0.2351 0.2531 0.0347  -0.0230 -0.0434 652  THR B C   
14053 O O   . THR B 654  ? 0.2633 0.2143 0.2331 0.0396  -0.0225 -0.0449 652  THR B O   
14054 C CB  . THR B 654  ? 0.2626 0.1982 0.2167 0.0318  -0.0253 -0.0454 652  THR B CB  
14055 O OG1 . THR B 654  ? 0.2922 0.2164 0.2377 0.0293  -0.0282 -0.0456 652  THR B OG1 
14056 C CG2 . THR B 654  ? 0.2805 0.2168 0.2343 0.0378  -0.0236 -0.0484 652  THR B CG2 
14057 N N   . LEU B 655  ? 0.2218 0.1796 0.1945 0.0313  -0.0213 -0.0416 653  LEU B N   
14058 C CA  . LEU B 655  ? 0.2243 0.1925 0.2053 0.0330  -0.0188 -0.0412 653  LEU B CA  
14059 C C   . LEU B 655  ? 0.2256 0.1945 0.2098 0.0346  -0.0199 -0.0405 653  LEU B C   
14060 O O   . LEU B 655  ? 0.2357 0.2104 0.2251 0.0381  -0.0187 -0.0413 653  LEU B O   
14061 C CB  . LEU B 655  ? 0.2218 0.1972 0.2068 0.0288  -0.0173 -0.0392 653  LEU B CB  
14062 C CG  . LEU B 655  ? 0.2274 0.2038 0.2102 0.0272  -0.0161 -0.0396 653  LEU B CG  
14063 C CD1 . LEU B 655  ? 0.2268 0.2095 0.2133 0.0231  -0.0151 -0.0373 653  LEU B CD1 
14064 C CD2 . LEU B 655  ? 0.2539 0.2343 0.2383 0.0311  -0.0137 -0.0417 653  LEU B CD2 
14065 N N   . LEU B 656  ? 0.2392 0.2025 0.2203 0.0321  -0.0222 -0.0389 654  LEU B N   
14066 C CA  . LEU B 656  ? 0.2481 0.2107 0.2309 0.0337  -0.0235 -0.0382 654  LEU B CA  
14067 C C   . LEU B 656  ? 0.2598 0.2189 0.2413 0.0393  -0.0245 -0.0404 654  LEU B C   
14068 O O   . LEU B 656  ? 0.2555 0.2192 0.2419 0.0423  -0.0244 -0.0406 654  LEU B O   
14069 C CB  . LEU B 656  ? 0.2728 0.2284 0.2509 0.0300  -0.0259 -0.0362 654  LEU B CB  
14070 C CG  . LEU B 656  ? 0.2694 0.2279 0.2484 0.0245  -0.0253 -0.0339 654  LEU B CG  
14071 C CD1 . LEU B 656  ? 0.2924 0.2437 0.2665 0.0215  -0.0276 -0.0320 654  LEU B CD1 
14072 C CD2 . LEU B 656  ? 0.2701 0.2389 0.2567 0.0241  -0.0231 -0.0328 654  LEU B CD2 
14073 N N   . GLY B 657  ? 0.2725 0.2228 0.2471 0.0408  -0.0258 -0.0420 655  GLY B N   
14074 C CA  . GLY B 657  ? 0.2924 0.2387 0.2652 0.0466  -0.0269 -0.0442 655  GLY B CA  
14075 C C   . GLY B 657  ? 0.2603 0.2162 0.2400 0.0508  -0.0243 -0.0459 655  GLY B C   
14076 O O   . GLY B 657  ? 0.2642 0.2221 0.2469 0.0552  -0.0248 -0.0467 655  GLY B O   
14077 N N   . LEU B 658  ? 0.2351 0.1977 0.2177 0.0493  -0.0215 -0.0462 656  LEU B N   
14078 C CA  . LEU B 658  ? 0.2394 0.2112 0.2282 0.0529  -0.0188 -0.0476 656  LEU B CA  
14079 C C   . LEU B 658  ? 0.2616 0.2430 0.2589 0.0522  -0.0179 -0.0461 656  LEU B C   
14080 O O   . LEU B 658  ? 0.2432 0.2304 0.2458 0.0561  -0.0172 -0.0471 656  LEU B O   
14081 C CB  . LEU B 658  ? 0.2287 0.2036 0.2168 0.0514  -0.0162 -0.0483 656  LEU B CB  
14082 C CG  . LEU B 658  ? 0.2345 0.2188 0.2283 0.0546  -0.0129 -0.0497 656  LEU B CG  
14083 C CD1 . LEU B 658  ? 0.2263 0.2085 0.2191 0.0610  -0.0132 -0.0524 656  LEU B CD1 
14084 C CD2 . LEU B 658  ? 0.2203 0.2061 0.2120 0.0525  -0.0107 -0.0500 656  LEU B CD2 
14085 N N   . ILE B 659  ? 0.2208 0.2039 0.2196 0.0474  -0.0180 -0.0437 657  ILE B N   
14086 C CA  . ILE B 659  ? 0.1695 0.1606 0.1755 0.0465  -0.0174 -0.0423 657  ILE B CA  
14087 C C   . ILE B 659  ? 0.2096 0.1984 0.2161 0.0494  -0.0199 -0.0424 657  ILE B C   
14088 O O   . ILE B 659  ? 0.2297 0.2254 0.2425 0.0515  -0.0195 -0.0426 657  ILE B O   
14089 C CB  . ILE B 659  ? 0.2037 0.1961 0.2102 0.0411  -0.0172 -0.0398 657  ILE B CB  
14090 C CG1 . ILE B 659  ? 0.1887 0.1854 0.1962 0.0389  -0.0146 -0.0397 657  ILE B CG1 
14091 C CG2 . ILE B 659  ? 0.2273 0.2257 0.2398 0.0404  -0.0172 -0.0385 657  ILE B CG2 
14092 C CD1 . ILE B 659  ? 0.2007 0.1963 0.2066 0.0338  -0.0147 -0.0375 657  ILE B CD1 
14093 N N   . ILE B 660  ? 0.2049 0.1838 0.2047 0.0492  -0.0227 -0.0420 658  ILE B N   
14094 C CA  . ILE B 660  ? 0.1917 0.1673 0.1910 0.0520  -0.0254 -0.0420 658  ILE B CA  
14095 C C   . ILE B 660  ? 0.1914 0.1699 0.1937 0.0581  -0.0253 -0.0443 658  ILE B C   
14096 O O   . ILE B 660  ? 0.2235 0.2070 0.2308 0.0605  -0.0260 -0.0443 658  ILE B O   
14097 C CB  . ILE B 660  ? 0.2352 0.1985 0.2257 0.0509  -0.0283 -0.0413 658  ILE B CB  
14098 C CG1 . ILE B 660  ? 0.2443 0.2061 0.2331 0.0451  -0.0286 -0.0387 658  ILE B CG1 
14099 C CG2 . ILE B 660  ? 0.2386 0.1968 0.2272 0.0553  -0.0312 -0.0418 658  ILE B CG2 
14100 C CD1 . ILE B 660  ? 0.2651 0.2153 0.2451 0.0428  -0.0309 -0.0378 658  ILE B CD1 
14101 N N   . ARG B 661  ? 0.1979 0.1736 0.1971 0.0608  -0.0244 -0.0464 659  ARG B N   
14102 C CA  . ARG B 661  ? 0.2021 0.1792 0.2030 0.0672  -0.0245 -0.0487 659  ARG B CA  
14103 C C   . ARG B 661  ? 0.2082 0.1982 0.2180 0.0688  -0.0213 -0.0496 659  ARG B C   
14104 O O   . ARG B 661  ? 0.2141 0.2095 0.2289 0.0730  -0.0216 -0.0505 659  ARG B O   
14105 C CB  . ARG B 661  ? 0.2449 0.2129 0.2381 0.0699  -0.0249 -0.0507 659  ARG B CB  
14106 C CG  . ARG B 661  ? 0.2869 0.2418 0.2717 0.0699  -0.0286 -0.0502 659  ARG B CG  
14107 C CD  . ARG B 661  ? 0.3569 0.3013 0.3332 0.0722  -0.0294 -0.0522 659  ARG B CD  
14108 N NE  . ARG B 661  ? 0.3276 0.2743 0.3054 0.0790  -0.0284 -0.0551 659  ARG B NE  
14109 C CZ  . ARG B 661  ? 0.3272 0.2743 0.3031 0.0807  -0.0261 -0.0573 659  ARG B CZ  
14110 N NH1 . ARG B 661  ? 0.3298 0.2750 0.3021 0.0761  -0.0247 -0.0570 659  ARG B NH1 
14111 N NH2 . ARG B 661  ? 0.3383 0.2876 0.3156 0.0874  -0.0251 -0.0600 659  ARG B NH2 
14112 N N   . GLU B 662  ? 0.1915 0.1867 0.2033 0.0654  -0.0183 -0.0492 660  GLU B N   
14113 C CA  . GLU B 662  ? 0.2001 0.2070 0.2197 0.0667  -0.0152 -0.0499 660  GLU B CA  
14114 C C   . GLU B 662  ? 0.1938 0.2090 0.2209 0.0642  -0.0151 -0.0481 660  GLU B C   
14115 O O   . GLU B 662  ? 0.1992 0.2231 0.2335 0.0667  -0.0143 -0.0487 660  GLU B O   
14116 C CB  . GLU B 662  ? 0.2071 0.2160 0.2254 0.0642  -0.0121 -0.0501 660  GLU B CB  
14117 C CG  . GLU B 662  ? 0.2164 0.2372 0.2425 0.0647  -0.0086 -0.0504 660  GLU B CG  
14118 C CD  . GLU B 662  ? 0.2055 0.2283 0.2300 0.0622  -0.0055 -0.0504 660  GLU B CD  
14119 O OE1 . GLU B 662  ? 0.2149 0.2338 0.2358 0.0578  -0.0058 -0.0489 660  GLU B OE1 
14120 O OE2 . GLU B 662  ? 0.2102 0.2390 0.2373 0.0648  -0.0027 -0.0518 660  GLU B OE2 
14121 N N   . ALA B 663  ? 0.1857 0.1985 0.2115 0.0594  -0.0161 -0.0459 661  ALA B N   
14122 C CA  . ALA B 663  ? 0.1673 0.1874 0.1996 0.0568  -0.0158 -0.0444 661  ALA B CA  
14123 C C   . ALA B 663  ? 0.1684 0.1858 0.2006 0.0573  -0.0191 -0.0435 661  ALA B C   
14124 O O   . ALA B 663  ? 0.1925 0.2155 0.2298 0.0556  -0.0192 -0.0424 661  ALA B O   
14125 C CB  . ALA B 663  ? 0.1833 0.2037 0.2147 0.0514  -0.0143 -0.0425 661  ALA B CB  
14126 N N   . GLY B 664  ? 0.1766 0.1851 0.2028 0.0597  -0.0218 -0.0440 662  GLY B N   
14127 C CA  . GLY B 664  ? 0.1964 0.2018 0.2219 0.0606  -0.0250 -0.0432 662  GLY B CA  
14128 C C   . GLY B 664  ? 0.2063 0.2074 0.2285 0.0559  -0.0262 -0.0409 662  GLY B C   
14129 O O   . GLY B 664  ? 0.2176 0.2189 0.2409 0.0558  -0.0283 -0.0399 662  GLY B O   
14130 N N   . LYS B 665  ? 0.2015 0.1990 0.2197 0.0520  -0.0250 -0.0399 663  LYS B N   
14131 C CA  . LYS B 665  ? 0.1921 0.1871 0.2080 0.0474  -0.0255 -0.0377 663  LYS B CA  
14132 C C   . LYS B 665  ? 0.1603 0.1445 0.1682 0.0467  -0.0282 -0.0369 663  LYS B C   
14133 O O   . LYS B 665  ? 0.2132 0.1906 0.2161 0.0488  -0.0291 -0.0379 663  LYS B O   
14134 C CB  . LYS B 665  ? 0.2045 0.2024 0.2211 0.0433  -0.0228 -0.0369 663  LYS B CB  
14135 C CG  . LYS B 665  ? 0.2049 0.2128 0.2289 0.0430  -0.0202 -0.0372 663  LYS B CG  
14136 C CD  . LYS B 665  ? 0.2120 0.2223 0.2367 0.0384  -0.0183 -0.0356 663  LYS B CD  
14137 C CE  . LYS B 665  ? 0.2498 0.2693 0.2815 0.0381  -0.0160 -0.0358 663  LYS B CE  
14138 N NZ  . LYS B 665  ? 0.2003 0.2221 0.2330 0.0340  -0.0145 -0.0342 663  LYS B NZ  
14139 N N   . SER B 666  ? 0.2106 0.1928 0.2168 0.0437  -0.0292 -0.0349 664  SER B N   
14140 C CA  . SER B 666  ? 0.2267 0.1991 0.2251 0.0417  -0.0312 -0.0336 664  SER B CA  
14141 C C   . SER B 666  ? 0.2239 0.1938 0.2191 0.0379  -0.0297 -0.0330 664  SER B C   
14142 O O   . SER B 666  ? 0.2225 0.1989 0.2217 0.0360  -0.0272 -0.0330 664  SER B O   
14143 C CB  . SER B 666  ? 0.2620 0.2341 0.2599 0.0393  -0.0324 -0.0316 664  SER B CB  
14144 O OG  . SER B 666  ? 0.2586 0.2368 0.2599 0.0355  -0.0300 -0.0305 664  SER B OG  
14145 N N   . ALA B 667  ? 0.2276 0.1879 0.2153 0.0366  -0.0315 -0.0323 665  ALA B N   
14146 C CA  . ALA B 667  ? 0.2282 0.1861 0.2127 0.0324  -0.0305 -0.0315 665  ALA B CA  
14147 C C   . ALA B 667  ? 0.2227 0.1862 0.2101 0.0280  -0.0288 -0.0295 665  ALA B C   
14148 O O   . ALA B 667  ? 0.2078 0.1752 0.1970 0.0255  -0.0268 -0.0294 665  ALA B O   
14149 C CB  . ALA B 667  ? 0.2883 0.2346 0.2643 0.0312  -0.0329 -0.0309 665  ALA B CB  
14150 N N   . LEU B 668  ? 0.2147 0.1788 0.2025 0.0271  -0.0295 -0.0281 666  LEU B N   
14151 C CA  . LEU B 668  ? 0.2064 0.1760 0.1970 0.0234  -0.0278 -0.0263 666  LEU B CA  
14152 C C   . LEU B 668  ? 0.1904 0.1694 0.1881 0.0238  -0.0252 -0.0271 666  LEU B C   
14153 O O   . LEU B 668  ? 0.2023 0.1849 0.2014 0.0208  -0.0234 -0.0263 666  LEU B O   
14154 C CB  . LEU B 668  ? 0.2855 0.2544 0.2755 0.0235  -0.0291 -0.0252 666  LEU B CB  
14155 C CG  . LEU B 668  ? 0.2968 0.2692 0.2877 0.0197  -0.0277 -0.0232 666  LEU B CG  
14156 C CD1 . LEU B 668  ? 0.3819 0.3492 0.3675 0.0157  -0.0278 -0.0215 666  LEU B CD1 
14157 C CD2 . LEU B 668  ? 0.3976 0.3697 0.3881 0.0206  -0.0289 -0.0225 666  LEU B CD2 
14158 N N   . ASN B 669  ? 0.1859 0.1691 0.1880 0.0274  -0.0251 -0.0286 667  ASN B N   
14159 C CA  . ASN B 669  ? 0.1761 0.1680 0.1847 0.0274  -0.0227 -0.0292 667  ASN B CA  
14160 C C   . ASN B 669  ? 0.1706 0.1634 0.1794 0.0276  -0.0211 -0.0303 667  ASN B C   
14161 O O   . ASN B 669  ? 0.1765 0.1750 0.1887 0.0260  -0.0189 -0.0300 667  ASN B O   
14162 C CB  . ASN B 669  ? 0.1897 0.1861 0.2032 0.0308  -0.0230 -0.0305 667  ASN B CB  
14163 C CG  . ASN B 669  ? 0.2039 0.2009 0.2180 0.0303  -0.0243 -0.0294 667  ASN B CG  
14164 O OD1 . ASN B 669  ? 0.2526 0.2502 0.2661 0.0272  -0.0235 -0.0279 667  ASN B OD1 
14165 N ND2 . ASN B 669  ? 0.2229 0.2197 0.2381 0.0334  -0.0262 -0.0303 667  ASN B ND2 
14166 N N   . ALA B 670  ? 0.1743 0.1613 0.1789 0.0295  -0.0223 -0.0315 668  ALA B N   
14167 C CA  . ALA B 670  ? 0.1734 0.1607 0.1772 0.0296  -0.0209 -0.0326 668  ALA B CA  
14168 C C   . ALA B 670  ? 0.1650 0.1512 0.1663 0.0251  -0.0203 -0.0311 668  ALA B C   
14169 O O   . ALA B 670  ? 0.1573 0.1476 0.1605 0.0242  -0.0184 -0.0313 668  ALA B O   
14170 C CB  . ALA B 670  ? 0.1991 0.1793 0.1981 0.0327  -0.0225 -0.0343 668  ALA B CB  
14171 N N   . ILE B 671  ? 0.1639 0.1450 0.1612 0.0224  -0.0218 -0.0295 669  ILE B N   
14172 C CA  . ILE B 671  ? 0.1717 0.1530 0.1674 0.0180  -0.0212 -0.0279 669  ILE B CA  
14173 C C   . ILE B 671  ? 0.1787 0.1685 0.1802 0.0165  -0.0189 -0.0269 669  ILE B C   
14174 O O   . ILE B 671  ? 0.1723 0.1654 0.1749 0.0147  -0.0176 -0.0266 669  ILE B O   
14175 C CB  . ILE B 671  ? 0.1735 0.1488 0.1645 0.0152  -0.0230 -0.0261 669  ILE B CB  
14176 C CG1 . ILE B 671  ? 0.2206 0.1861 0.2048 0.0160  -0.0254 -0.0270 669  ILE B CG1 
14177 C CG2 . ILE B 671  ? 0.2121 0.1898 0.2031 0.0106  -0.0221 -0.0242 669  ILE B CG2 
14178 C CD1 . ILE B 671  ? 0.2667 0.2253 0.2458 0.0139  -0.0274 -0.0253 669  ILE B CD1 
14179 N N   . ALA B 672  ? 0.1606 0.1539 0.1655 0.0173  -0.0186 -0.0264 670  ALA B N   
14180 C CA  . ALA B 672  ? 0.1692 0.1698 0.1791 0.0161  -0.0166 -0.0255 670  ALA B CA  
14181 C C   . ALA B 672  ? 0.1792 0.1849 0.1930 0.0176  -0.0148 -0.0267 670  ALA B C   
14182 O O   . ALA B 672  ? 0.1804 0.1906 0.1967 0.0160  -0.0131 -0.0259 670  ALA B O   
14183 C CB  . ALA B 672  ? 0.1864 0.1889 0.1987 0.0170  -0.0169 -0.0252 670  ALA B CB  
14184 N N   . GLU B 673  ? 0.1646 0.1696 0.1788 0.0208  -0.0150 -0.0285 671  GLU B N   
14185 C CA  . GLU B 673  ? 0.1620 0.1721 0.1797 0.0221  -0.0131 -0.0296 671  GLU B CA  
14186 C C   . GLU B 673  ? 0.1482 0.1572 0.1631 0.0206  -0.0124 -0.0296 671  GLU B C   
14187 O O   . GLU B 673  ? 0.1481 0.1619 0.1656 0.0196  -0.0105 -0.0292 671  GLU B O   
14188 C CB  . GLU B 673  ? 0.1760 0.1862 0.1949 0.0260  -0.0133 -0.0316 671  GLU B CB  
14189 C CG  . GLU B 673  ? 0.2137 0.2286 0.2352 0.0271  -0.0111 -0.0326 671  GLU B CG  
14190 C CD  . GLU B 673  ? 0.1926 0.2121 0.2187 0.0303  -0.0104 -0.0340 671  GLU B CD  
14191 O OE1 . GLU B 673  ? 0.2117 0.2294 0.2380 0.0326  -0.0121 -0.0347 671  GLU B OE1 
14192 O OE2 . GLU B 673  ? 0.1493 0.1743 0.1789 0.0305  -0.0081 -0.0343 671  GLU B OE2 
14193 N N   . VAL B 674  ? 0.1329 0.1352 0.1422 0.0202  -0.0140 -0.0300 672  VAL B N   
14194 C CA  . VAL B 674  ? 0.1418 0.1427 0.1481 0.0183  -0.0137 -0.0300 672  VAL B CA  
14195 C C   . VAL B 674  ? 0.1447 0.1488 0.1522 0.0146  -0.0131 -0.0279 672  VAL B C   
14196 O O   . VAL B 674  ? 0.1340 0.1415 0.1425 0.0135  -0.0119 -0.0276 672  VAL B O   
14197 C CB  . VAL B 674  ? 0.1389 0.1313 0.1385 0.0183  -0.0158 -0.0309 672  VAL B CB  
14198 C CG1 . VAL B 674  ? 0.1460 0.1370 0.1423 0.0162  -0.0158 -0.0310 672  VAL B CG1 
14199 C CG2 . VAL B 674  ? 0.1627 0.1522 0.1612 0.0227  -0.0163 -0.0331 672  VAL B CG2 
14200 N N   . ARG B 675  ? 0.1360 0.1395 0.1438 0.0129  -0.0139 -0.0264 673  ARG B N   
14201 C CA  . ARG B 675  ? 0.1435 0.1510 0.1531 0.0098  -0.0131 -0.0244 673  ARG B CA  
14202 C C   . ARG B 675  ? 0.1156 0.1301 0.1304 0.0106  -0.0109 -0.0241 673  ARG B C   
14203 O O   . ARG B 675  ? 0.1218 0.1395 0.1376 0.0089  -0.0101 -0.0232 673  ARG B O   
14204 C CB  . ARG B 675  ? 0.1440 0.1504 0.1534 0.0084  -0.0139 -0.0230 673  ARG B CB  
14205 C CG  . ARG B 675  ? 0.1539 0.1537 0.1579 0.0063  -0.0159 -0.0224 673  ARG B CG  
14206 C CD  . ARG B 675  ? 0.1382 0.1385 0.1423 0.0043  -0.0160 -0.0205 673  ARG B CD  
14207 N NE  . ARG B 675  ? 0.1506 0.1566 0.1574 0.0019  -0.0146 -0.0190 673  ARG B NE  
14208 C CZ  . ARG B 675  ? 0.1467 0.1558 0.1552 0.0007  -0.0138 -0.0174 673  ARG B CZ  
14209 N NH1 . ARG B 675  ? 0.1848 0.1918 0.1924 0.0015  -0.0142 -0.0173 673  ARG B NH1 
14210 N NH2 . ARG B 675  ? 0.1444 0.1588 0.1554 -0.0012 -0.0126 -0.0161 673  ARG B NH2 
14211 N N   . GLU B 676  ? 0.1242 0.1408 0.1422 0.0130  -0.0102 -0.0250 674  GLU B N   
14212 C CA  . GLU B 676  ? 0.1220 0.1447 0.1448 0.0134  -0.0082 -0.0246 674  GLU B CA  
14213 C C   . GLU B 676  ? 0.1236 0.1481 0.1463 0.0138  -0.0070 -0.0252 674  GLU B C   
14214 O O   . GLU B 676  ? 0.1141 0.1425 0.1389 0.0129  -0.0056 -0.0243 674  GLU B O   
14215 C CB  . GLU B 676  ? 0.1268 0.1511 0.1528 0.0156  -0.0080 -0.0255 674  GLU B CB  
14216 C CG  . GLU B 676  ? 0.1595 0.1894 0.1901 0.0156  -0.0061 -0.0250 674  GLU B CG  
14217 C CD  . GLU B 676  ? 0.2797 0.3113 0.3136 0.0171  -0.0062 -0.0257 674  GLU B CD  
14218 O OE1 . GLU B 676  ? 0.3052 0.3339 0.3378 0.0177  -0.0079 -0.0260 674  GLU B OE1 
14219 O OE2 . GLU B 676  ? 0.3123 0.3479 0.3499 0.0174  -0.0048 -0.0258 674  GLU B OE2 
14220 N N   . ALA B 677  ? 0.1125 0.1340 0.1326 0.0154  -0.0074 -0.0269 675  ALA B N   
14221 C CA  . ALA B 677  ? 0.1103 0.1332 0.1295 0.0158  -0.0063 -0.0275 675  ALA B CA  
14222 C C   . ALA B 677  ? 0.1120 0.1343 0.1286 0.0131  -0.0067 -0.0263 675  ALA B C   
14223 O O   . ALA B 677  ? 0.1101 0.1359 0.1279 0.0125  -0.0054 -0.0256 675  ALA B O   
14224 C CB  . ALA B 677  ? 0.1312 0.1501 0.1471 0.0182  -0.0068 -0.0296 675  ALA B CB  
14225 N N   . ILE B 678  ? 0.1149 0.1331 0.1282 0.0113  -0.0086 -0.0258 676  ILE B N   
14226 C CA  . ILE B 678  ? 0.1078 0.1262 0.1193 0.0083  -0.0093 -0.0245 676  ILE B CA  
14227 C C   . ILE B 678  ? 0.1114 0.1355 0.1271 0.0071  -0.0081 -0.0226 676  ILE B C   
14228 O O   . ILE B 678  ? 0.1114 0.1383 0.1274 0.0060  -0.0076 -0.0217 676  ILE B O   
14229 C CB  . ILE B 678  ? 0.1158 0.1289 0.1234 0.0062  -0.0115 -0.0242 676  ILE B CB  
14230 C CG1 . ILE B 678  ? 0.1311 0.1375 0.1336 0.0075  -0.0129 -0.0261 676  ILE B CG1 
14231 C CG2 . ILE B 678  ? 0.1423 0.1570 0.1493 0.0027  -0.0123 -0.0224 676  ILE B CG2 
14232 C CD1 . ILE B 678  ? 0.1383 0.1385 0.1372 0.0062  -0.0150 -0.0259 676  ILE B CD1 
14233 N N   . ASP B 679  ? 0.0973 0.1230 0.1160 0.0075  -0.0077 -0.0219 677  ASP B N   
14234 C CA  . ASP B 679  ? 0.1206 0.1511 0.1430 0.0067  -0.0066 -0.0203 677  ASP B CA  
14235 C C   . ASP B 679  ? 0.0945 0.1287 0.1195 0.0079  -0.0048 -0.0203 677  ASP B C   
14236 O O   . ASP B 679  ? 0.1075 0.1450 0.1338 0.0070  -0.0042 -0.0189 677  ASP B O   
14237 C CB  . ASP B 679  ? 0.1168 0.1474 0.1411 0.0071  -0.0065 -0.0199 677  ASP B CB  
14238 C CG  . ASP B 679  ? 0.1361 0.1635 0.1577 0.0054  -0.0080 -0.0193 677  ASP B CG  
14239 O OD1 . ASP B 679  ? 0.1726 0.1992 0.1921 0.0032  -0.0089 -0.0186 677  ASP B OD1 
14240 O OD2 . ASP B 679  ? 0.1694 0.1951 0.1912 0.0061  -0.0084 -0.0195 677  ASP B OD2 
14241 N N   . PHE B 680  ? 0.1000 0.1342 0.1259 0.0100  -0.0039 -0.0217 678  PHE B N   
14242 C CA  . PHE B 680  ? 0.0877 0.1253 0.1157 0.0108  -0.0021 -0.0215 678  PHE B CA  
14243 C C   . PHE B 680  ? 0.1023 0.1401 0.1276 0.0099  -0.0021 -0.0211 678  PHE B C   
14244 O O   . PHE B 680  ? 0.1052 0.1459 0.1318 0.0094  -0.0011 -0.0199 678  PHE B O   
14245 C CB  . PHE B 680  ? 0.0838 0.1216 0.1130 0.0129  -0.0012 -0.0232 678  PHE B CB  
14246 C CG  . PHE B 680  ? 0.0905 0.1299 0.1235 0.0138  -0.0008 -0.0233 678  PHE B CG  
14247 C CD1 . PHE B 680  ? 0.1022 0.1443 0.1382 0.0131  0.0001  -0.0221 678  PHE B CD1 
14248 C CD2 . PHE B 680  ? 0.1139 0.1519 0.1473 0.0154  -0.0014 -0.0248 678  PHE B CD2 
14249 C CE1 . PHE B 680  ? 0.1245 0.1677 0.1636 0.0137  0.0003  -0.0224 678  PHE B CE1 
14250 C CE2 . PHE B 680  ? 0.1325 0.1722 0.1694 0.0161  -0.0013 -0.0250 678  PHE B CE2 
14251 C CZ  . PHE B 680  ? 0.1099 0.1522 0.1496 0.0151  -0.0005 -0.0238 678  PHE B CZ  
14252 N N   . LEU B 681  ? 0.0933 0.1276 0.1146 0.0098  -0.0032 -0.0223 679  LEU B N   
14253 C CA  . LEU B 681  ? 0.0963 0.1304 0.1145 0.0089  -0.0035 -0.0221 679  LEU B CA  
14254 C C   . LEU B 681  ? 0.0966 0.1329 0.1154 0.0067  -0.0042 -0.0201 679  LEU B C   
14255 O O   . LEU B 681  ? 0.1141 0.1530 0.1330 0.0064  -0.0036 -0.0191 679  LEU B O   
14256 C CB  . LEU B 681  ? 0.1140 0.1430 0.1273 0.0088  -0.0050 -0.0237 679  LEU B CB  
14257 C CG  . LEU B 681  ? 0.1035 0.1307 0.1158 0.0116  -0.0040 -0.0259 679  LEU B CG  
14258 C CD1 . LEU B 681  ? 0.1220 0.1429 0.1293 0.0118  -0.0059 -0.0275 679  LEU B CD1 
14259 C CD2 . LEU B 681  ? 0.1329 0.1622 0.1442 0.0125  -0.0022 -0.0263 679  LEU B CD2 
14260 N N   . ARG B 682  ? 0.0873 0.1228 0.1064 0.0052  -0.0055 -0.0194 680  ARG B N   
14261 C CA  . ARG B 682  ? 0.0993 0.1377 0.1193 0.0032  -0.0063 -0.0175 680  ARG B CA  
14262 C C   . ARG B 682  ? 0.0994 0.1422 0.1236 0.0039  -0.0049 -0.0160 680  ARG B C   
14263 O O   . ARG B 682  ? 0.1079 0.1539 0.1330 0.0032  -0.0050 -0.0146 680  ARG B O   
14264 C CB  . ARG B 682  ? 0.1101 0.1466 0.1291 0.0012  -0.0079 -0.0171 680  ARG B CB  
14265 C CG  . ARG B 682  ? 0.1198 0.1514 0.1338 -0.0002 -0.0098 -0.0182 680  ARG B CG  
14266 C CD  . ARG B 682  ? 0.1160 0.1453 0.1290 -0.0023 -0.0113 -0.0177 680  ARG B CD  
14267 N NE  . ARG B 682  ? 0.1206 0.1445 0.1284 -0.0040 -0.0134 -0.0187 680  ARG B NE  
14268 C CZ  . ARG B 682  ? 0.1370 0.1565 0.1423 -0.0057 -0.0148 -0.0187 680  ARG B CZ  
14269 N NH1 . ARG B 682  ? 0.1509 0.1711 0.1583 -0.0059 -0.0144 -0.0178 680  ARG B NH1 
14270 N NH2 . ARG B 682  ? 0.1742 0.1881 0.1743 -0.0072 -0.0168 -0.0197 680  ARG B NH2 
14271 N N   . TYR B 683  ? 0.1010 0.1440 0.1278 0.0054  -0.0037 -0.0164 681  TYR B N   
14272 C CA  . TYR B 683  ? 0.1032 0.1496 0.1335 0.0061  -0.0024 -0.0152 681  TYR B CA  
14273 C C   . TYR B 683  ? 0.0971 0.1450 0.1277 0.0070  -0.0012 -0.0148 681  TYR B C   
14274 O O   . TYR B 683  ? 0.0954 0.1458 0.1272 0.0069  -0.0009 -0.0133 681  TYR B O   
14275 C CB  . TYR B 683  ? 0.0999 0.1455 0.1323 0.0072  -0.0017 -0.0159 681  TYR B CB  
14276 C CG  . TYR B 683  ? 0.0931 0.1410 0.1285 0.0080  -0.0004 -0.0149 681  TYR B CG  
14277 C CD1 . TYR B 683  ? 0.1063 0.1561 0.1431 0.0077  -0.0004 -0.0137 681  TYR B CD1 
14278 C CD2 . TYR B 683  ? 0.0954 0.1437 0.1322 0.0091  0.0009  -0.0152 681  TYR B CD2 
14279 C CE1 . TYR B 683  ? 0.1250 0.1762 0.1641 0.0087  0.0007  -0.0129 681  TYR B CE1 
14280 C CE2 . TYR B 683  ? 0.0979 0.1475 0.1370 0.0097  0.0019  -0.0144 681  TYR B CE2 
14281 C CZ  . TYR B 683  ? 0.1094 0.1601 0.1494 0.0097  0.0017  -0.0133 681  TYR B CZ  
14282 O OH  . TYR B 683  ? 0.1467 0.1979 0.1883 0.0105  0.0027  -0.0126 681  TYR B OH  
14283 N N   . TYR B 684  ? 0.0986 0.1451 0.1280 0.0079  -0.0004 -0.0161 682  TYR B N   
14284 C CA  . TYR B 684  ? 0.0881 0.1360 0.1175 0.0084  0.0009  -0.0155 682  TYR B CA  
14285 C C   . TYR B 684  ? 0.1061 0.1545 0.1326 0.0075  0.0000  -0.0147 682  TYR B C   
14286 O O   . TYR B 684  ? 0.1098 0.1599 0.1364 0.0076  0.0006  -0.0133 682  TYR B O   
14287 C CB  . TYR B 684  ? 0.0998 0.1468 0.1287 0.0095  0.0022  -0.0171 682  TYR B CB  
14288 C CG  . TYR B 684  ? 0.0910 0.1383 0.1232 0.0104  0.0030  -0.0177 682  TYR B CG  
14289 C CD1 . TYR B 684  ? 0.1018 0.1506 0.1371 0.0104  0.0035  -0.0166 682  TYR B CD1 
14290 C CD2 . TYR B 684  ? 0.0973 0.1436 0.1297 0.0115  0.0031  -0.0196 682  TYR B CD2 
14291 C CE1 . TYR B 684  ? 0.1076 0.1565 0.1457 0.0109  0.0040  -0.0173 682  TYR B CE1 
14292 C CE2 . TYR B 684  ? 0.1027 0.1497 0.1383 0.0122  0.0036  -0.0202 682  TYR B CE2 
14293 C CZ  . TYR B 684  ? 0.1041 0.1523 0.1424 0.0118  0.0040  -0.0190 682  TYR B CZ  
14294 O OH  . TYR B 684  ? 0.0991 0.1478 0.1404 0.0123  0.0041  -0.0197 682  TYR B OH  
14295 N N   . ALA B 685  ? 0.0972 0.1438 0.1208 0.0064  -0.0017 -0.0153 683  ALA B N   
14296 C CA  . ALA B 685  ? 0.0978 0.1452 0.1189 0.0051  -0.0031 -0.0144 683  ALA B CA  
14297 C C   . ALA B 685  ? 0.1010 0.1521 0.1249 0.0046  -0.0036 -0.0123 683  ALA B C   
14298 O O   . ALA B 685  ? 0.1057 0.1587 0.1290 0.0046  -0.0037 -0.0110 683  ALA B O   
14299 C CB  . ALA B 685  ? 0.1085 0.1530 0.1262 0.0036  -0.0050 -0.0155 683  ALA B CB  
14300 N N   . GLU B 686  ? 0.0908 0.1428 0.1173 0.0042  -0.0038 -0.0119 684  GLU B N   
14301 C CA  . GLU B 686  ? 0.1308 0.1867 0.1602 0.0040  -0.0041 -0.0100 684  GLU B CA  
14302 C C   . GLU B 686  ? 0.1170 0.1744 0.1485 0.0059  -0.0025 -0.0090 684  GLU B C   
14303 O O   . GLU B 686  ? 0.1139 0.1738 0.1460 0.0062  -0.0028 -0.0074 684  GLU B O   
14304 C CB  . GLU B 686  ? 0.1518 0.2084 0.1832 0.0033  -0.0044 -0.0099 684  GLU B CB  
14305 C CG  . GLU B 686  ? 0.1583 0.2195 0.1931 0.0037  -0.0042 -0.0081 684  GLU B CG  
14306 C CD  . GLU B 686  ? 0.2305 0.2953 0.2652 0.0025  -0.0058 -0.0066 684  GLU B CD  
14307 O OE1 . GLU B 686  ? 0.2026 0.2662 0.2344 0.0009  -0.0073 -0.0071 684  GLU B OE1 
14308 O OE2 . GLU B 686  ? 0.2353 0.3043 0.2729 0.0034  -0.0056 -0.0051 684  GLU B OE2 
14309 N N   . GLN B 687  ? 0.0940 0.1494 0.1264 0.0070  -0.0010 -0.0099 685  GLN B N   
14310 C CA  . GLN B 687  ? 0.0853 0.1413 0.1193 0.0084  0.0005  -0.0090 685  GLN B CA  
14311 C C   . GLN B 687  ? 0.1126 0.1687 0.1443 0.0086  0.0006  -0.0081 685  GLN B C   
14312 O O   . GLN B 687  ? 0.1259 0.1831 0.1583 0.0094  0.0009  -0.0065 685  GLN B O   
14313 C CB  . GLN B 687  ? 0.1133 0.1674 0.1486 0.0091  0.0019  -0.0102 685  GLN B CB  
14314 C CG  . GLN B 687  ? 0.1110 0.1649 0.1484 0.0092  0.0017  -0.0107 685  GLN B CG  
14315 C CD  . GLN B 687  ? 0.1264 0.1821 0.1657 0.0099  0.0018  -0.0094 685  GLN B CD  
14316 O OE1 . GLN B 687  ? 0.1422 0.1980 0.1823 0.0109  0.0027  -0.0085 685  GLN B OE1 
14317 N NE2 . GLN B 687  ? 0.1919 0.2491 0.2318 0.0093  0.0010  -0.0092 685  GLN B NE2 
14318 N N   . THR B 688  ? 0.0977 0.1524 0.1263 0.0079  0.0004  -0.0091 686  THR B N   
14319 C CA  . THR B 688  ? 0.1050 0.1597 0.1307 0.0079  0.0004  -0.0084 686  THR B CA  
14320 C C   . THR B 688  ? 0.0989 0.1559 0.1241 0.0075  -0.0013 -0.0067 686  THR B C   
14321 O O   . THR B 688  ? 0.1364 0.1943 0.1611 0.0083  -0.0012 -0.0050 686  THR B O   
14322 C CB  . THR B 688  ? 0.1144 0.1670 0.1364 0.0074  0.0004  -0.0101 686  THR B CB  
14323 O OG1 . THR B 688  ? 0.1195 0.1708 0.1424 0.0081  0.0022  -0.0114 686  THR B OG1 
14324 C CG2 . THR B 688  ? 0.1368 0.1893 0.1549 0.0072  0.0002  -0.0093 686  THR B CG2 
14325 N N   . ARG B 689  ? 0.1039 0.1621 0.1293 0.0063  -0.0031 -0.0069 687  ARG B N   
14326 C CA  . ARG B 689  ? 0.1058 0.1672 0.1313 0.0057  -0.0050 -0.0054 687  ARG B CA  
14327 C C   . ARG B 689  ? 0.1248 0.1891 0.1540 0.0072  -0.0046 -0.0035 687  ARG B C   
14328 O O   . ARG B 689  ? 0.1569 0.2239 0.1862 0.0076  -0.0058 -0.0019 687  ARG B O   
14329 C CB  . ARG B 689  ? 0.1354 0.1977 0.1609 0.0037  -0.0069 -0.0060 687  ARG B CB  
14330 C CG  . ARG B 689  ? 0.1447 0.2038 0.1655 0.0021  -0.0081 -0.0075 687  ARG B CG  
14331 C CD  . ARG B 689  ? 0.1453 0.2050 0.1660 -0.0003 -0.0102 -0.0078 687  ARG B CD  
14332 N NE  . ARG B 689  ? 0.1578 0.2170 0.1809 -0.0006 -0.0097 -0.0084 687  ARG B NE  
14333 C CZ  . ARG B 689  ? 0.1529 0.2079 0.1740 -0.0013 -0.0097 -0.0102 687  ARG B CZ  
14334 N NH1 . ARG B 689  ? 0.1467 0.1976 0.1633 -0.0014 -0.0100 -0.0118 687  ARG B NH1 
14335 N NH2 . ARG B 689  ? 0.1589 0.2135 0.1821 -0.0016 -0.0093 -0.0104 687  ARG B NH2 
14336 N N   . ARG B 690  ? 0.1133 0.1770 0.1453 0.0082  -0.0031 -0.0039 688  ARG B N   
14337 C CA  A ARG B 690  ? 0.1163 0.1820 0.1513 0.0100  -0.0025 -0.0024 688  ARG B CA  
14338 C CA  B ARG B 690  ? 0.1168 0.1825 0.1518 0.0100  -0.0025 -0.0024 688  ARG B CA  
14339 C C   . ARG B 690  ? 0.1208 0.1845 0.1548 0.0116  -0.0014 -0.0014 688  ARG B C   
14340 O O   . ARG B 690  ? 0.1305 0.1955 0.1660 0.0133  -0.0014 0.0001  688  ARG B O   
14341 C CB  A ARG B 690  ? 0.1163 0.1815 0.1540 0.0104  -0.0014 -0.0033 688  ARG B CB  
14342 C CB  B ARG B 690  ? 0.1169 0.1822 0.1546 0.0104  -0.0014 -0.0033 688  ARG B CB  
14343 C CG  A ARG B 690  ? 0.1378 0.2051 0.1768 0.0090  -0.0023 -0.0038 688  ARG B CG  
14344 C CG  B ARG B 690  ? 0.1384 0.2059 0.1774 0.0089  -0.0024 -0.0038 688  ARG B CG  
14345 C CD  A ARG B 690  ? 0.1622 0.2347 0.2038 0.0094  -0.0032 -0.0022 688  ARG B CD  
14346 C CD  B ARG B 690  ? 0.1629 0.2356 0.2040 0.0091  -0.0036 -0.0021 688  ARG B CD  
14347 N NE  A ARG B 690  ? 0.1489 0.2225 0.1929 0.0119  -0.0021 -0.0013 688  ARG B NE  
14348 N NE  B ARG B 690  ? 0.1678 0.2417 0.2108 0.0117  -0.0027 -0.0008 688  ARG B NE  
14349 C CZ  A ARG B 690  ? 0.1549 0.2303 0.1996 0.0137  -0.0023 0.0002  688  ARG B CZ  
14350 C CZ  B ARG B 690  ? 0.1562 0.2305 0.2015 0.0131  -0.0015 -0.0010 688  ARG B CZ  
14351 N NH1 A ARG B 690  ? 0.1561 0.2331 0.1994 0.0133  -0.0038 0.0013  688  ARG B NH1 
14352 N NH1 B ARG B 690  ? 0.1683 0.2421 0.2143 0.0121  -0.0010 -0.0021 688  ARG B NH1 
14353 N NH2 A ARG B 690  ? 0.1308 0.2060 0.1771 0.0162  -0.0011 0.0007  688  ARG B NH2 
14354 N NH2 B ARG B 690  ? 0.1375 0.2121 0.1840 0.0157  -0.0008 0.0001  688  ARG B NH2 
14355 N N   . THR B 691  ? 0.1051 0.1657 0.1365 0.0111  -0.0004 -0.0022 689  THR B N   
14356 C CA  . THR B 691  ? 0.1327 0.1911 0.1635 0.0123  0.0011  -0.0012 689  THR B CA  
14357 C C   . THR B 691  ? 0.1511 0.2080 0.1780 0.0119  0.0013  -0.0005 689  THR B C   
14358 O O   . THR B 691  ? 0.1693 0.2253 0.1952 0.0129  0.0015  0.0013  689  THR B O   
14359 C CB  . THR B 691  ? 0.1392 0.1952 0.1715 0.0122  0.0029  -0.0026 689  THR B CB  
14360 O OG1 . THR B 691  ? 0.1376 0.1928 0.1688 0.0109  0.0033  -0.0044 689  THR B OG1 
14361 C CG2 . THR B 691  ? 0.1404 0.1971 0.1760 0.0129  0.0029  -0.0030 689  THR B CG2 
14362 N N   . LEU B 692  ? 0.1360 0.1922 0.1604 0.0106  0.0014  -0.0018 690  LEU B N   
14363 C CA  . LEU B 692  ? 0.1413 0.1956 0.1621 0.0104  0.0025  -0.0014 690  LEU B CA  
14364 C C   . LEU B 692  ? 0.1440 0.1989 0.1612 0.0104  0.0010  0.0002  690  LEU B C   
14365 O O   . LEU B 692  ? 0.1761 0.2327 0.1921 0.0098  -0.0010 -0.0001 690  LEU B O   
14366 C CB  . LEU B 692  ? 0.1318 0.1851 0.1509 0.0094  0.0035  -0.0036 690  LEU B CB  
14367 C CG  . LEU B 692  ? 0.1320 0.1847 0.1544 0.0095  0.0051  -0.0051 690  LEU B CG  
14368 C CD1 . LEU B 692  ? 0.1539 0.2059 0.1742 0.0090  0.0062  -0.0071 690  LEU B CD1 
14369 C CD2 . LEU B 692  ? 0.1755 0.2272 0.1996 0.0099  0.0067  -0.0040 690  LEU B CD2 
14370 N N   . GLY B 693  ? 0.1443 0.1976 0.1595 0.0110  0.0019  0.0020  691  GLY B N   
14371 C CA  . GLY B 693  ? 0.1699 0.2232 0.1812 0.0113  0.0005  0.0038  691  GLY B CA  
14372 C C   . GLY B 693  ? 0.1759 0.2266 0.1829 0.0108  0.0024  0.0044  691  GLY B C   
14373 O O   . GLY B 693  ? 0.1805 0.2299 0.1878 0.0102  0.0047  0.0033  691  GLY B O   
14374 N N   . PRO B 694  ? 0.2127 0.2627 0.2154 0.0111  0.0013  0.0064  692  PRO B N   
14375 C CA  . PRO B 694  ? 0.1895 0.2371 0.1870 0.0104  0.0030  0.0069  692  PRO B CA  
14376 C C   . PRO B 694  ? 0.2180 0.2632 0.2164 0.0102  0.0058  0.0078  692  PRO B C   
14377 O O   . PRO B 694  ? 0.2542 0.2984 0.2502 0.0091  0.0081  0.0073  692  PRO B O   
14378 C CB  . PRO B 694  ? 0.2415 0.2888 0.2347 0.0110  0.0009  0.0093  692  PRO B CB  
14379 C CG  . PRO B 694  ? 0.2497 0.3002 0.2456 0.0117  -0.0022 0.0091  692  PRO B CG  
14380 C CD  . PRO B 694  ? 0.2101 0.2620 0.2124 0.0121  -0.0016 0.0080  692  PRO B CD  
14381 N N   . GLY B 695  ? 0.2043 0.2486 0.2061 0.0111  0.0057  0.0090  693  GLY B N   
14382 C CA  . GLY B 695  ? 0.2105 0.2521 0.2131 0.0107  0.0080  0.0099  693  GLY B CA  
14383 C C   . GLY B 695  ? 0.2019 0.2441 0.2087 0.0097  0.0099  0.0077  693  GLY B C   
14384 O O   . GLY B 695  ? 0.2469 0.2870 0.2548 0.0090  0.0116  0.0084  693  GLY B O   
14385 N N   . HIS B 696  ? 0.1966 0.2416 0.2059 0.0096  0.0094  0.0053  694  HIS B N   
14386 C CA  . HIS B 696  ? 0.1545 0.2002 0.1677 0.0089  0.0110  0.0032  694  HIS B CA  
14387 C C   . HIS B 696  ? 0.2046 0.2515 0.2158 0.0080  0.0126  0.0016  694  HIS B C   
14388 O O   . HIS B 696  ? 0.2206 0.2691 0.2320 0.0081  0.0120  -0.0004 694  HIS B O   
14389 C CB  . HIS B 696  ? 0.1536 0.2010 0.1708 0.0097  0.0094  0.0016  694  HIS B CB  
14390 C CG  . HIS B 696  ? 0.1411 0.1881 0.1598 0.0110  0.0078  0.0030  694  HIS B CG  
14391 N ND1 . HIS B 696  ? 0.1502 0.1993 0.1691 0.0119  0.0056  0.0032  694  HIS B ND1 
14392 C CD2 . HIS B 696  ? 0.1614 0.2062 0.1814 0.0118  0.0081  0.0044  694  HIS B CD2 
14393 C CE1 . HIS B 696  ? 0.1603 0.2091 0.1809 0.0133  0.0047  0.0045  694  HIS B CE1 
14394 N NE2 . HIS B 696  ? 0.1712 0.2169 0.1922 0.0134  0.0062  0.0052  694  HIS B NE2 
14395 N N   . GLY B 697  ? 0.2007 0.2466 0.2097 0.0070  0.0148  0.0027  695  GLY B N   
14396 C CA  . GLY B 697  ? 0.2053 0.2526 0.2117 0.0064  0.0167  0.0015  695  GLY B CA  
14397 C C   . GLY B 697  ? 0.1853 0.2347 0.1958 0.0061  0.0182  -0.0009 695  GLY B C   
14398 O O   . GLY B 697  ? 0.1834 0.2331 0.1985 0.0058  0.0186  -0.0011 695  GLY B O   
14399 N N   . PRO B 698  ? 0.1870 0.2381 0.1959 0.0064  0.0190  -0.0029 696  PRO B N   
14400 C CA  . PRO B 698  ? 0.1780 0.2314 0.1908 0.0066  0.0203  -0.0053 696  PRO B CA  
14401 C C   . PRO B 698  ? 0.1720 0.2272 0.1868 0.0054  0.0234  -0.0048 696  PRO B C   
14402 O O   . PRO B 698  ? 0.2068 0.2613 0.2187 0.0043  0.0250  -0.0027 696  PRO B O   
14403 C CB  . PRO B 698  ? 0.2323 0.2861 0.2416 0.0076  0.0202  -0.0074 696  PRO B CB  
14404 C CG  . PRO B 698  ? 0.2754 0.3278 0.2785 0.0073  0.0204  -0.0058 696  PRO B CG  
14405 C CD  . PRO B 698  ? 0.2445 0.2950 0.2476 0.0069  0.0184  -0.0033 696  PRO B CD  
14406 N N   . LEU B 699  ? 0.1440 0.2017 0.1638 0.0056  0.0242  -0.0065 697  LEU B N   
14407 C CA  . LEU B 699  ? 0.1434 0.2039 0.1659 0.0043  0.0270  -0.0063 697  LEU B CA  
14408 C C   . LEU B 699  ? 0.1650 0.2280 0.1845 0.0047  0.0296  -0.0072 697  LEU B C   
14409 O O   . LEU B 699  ? 0.1617 0.2261 0.1802 0.0032  0.0322  -0.0057 697  LEU B O   
14410 C CB  . LEU B 699  ? 0.1485 0.2114 0.1774 0.0045  0.0268  -0.0081 697  LEU B CB  
14411 C CG  . LEU B 699  ? 0.1542 0.2148 0.1862 0.0041  0.0246  -0.0076 697  LEU B CG  
14412 C CD1 . LEU B 699  ? 0.1642 0.2273 0.2019 0.0044  0.0243  -0.0095 697  LEU B CD1 
14413 C CD2 . LEU B 699  ? 0.2185 0.2769 0.2501 0.0022  0.0253  -0.0049 697  LEU B CD2 
14414 N N   . GLY B 700  ? 0.1369 0.2003 0.1547 0.0066  0.0289  -0.0095 698  GLY B N   
14415 C CA  . GLY B 700  ? 0.1338 0.1998 0.1495 0.0076  0.0314  -0.0111 698  GLY B CA  
14416 C C   . GLY B 700  ? 0.1517 0.2200 0.1711 0.0095  0.0311  -0.0141 698  GLY B C   
14417 O O   . GLY B 700  ? 0.1476 0.2144 0.1697 0.0101  0.0286  -0.0150 698  GLY B O   
14418 N N   . PRO B 701  ? 0.1395 0.2114 0.1591 0.0106  0.0338  -0.0156 699  PRO B N   
14419 C CA  . PRO B 701  ? 0.1357 0.2096 0.1585 0.0130  0.0335  -0.0186 699  PRO B CA  
14420 C C   . PRO B 701  ? 0.1328 0.2086 0.1630 0.0125  0.0323  -0.0187 699  PRO B C   
14421 O O   . PRO B 701  ? 0.1504 0.2292 0.1848 0.0105  0.0337  -0.0172 699  PRO B O   
14422 C CB  . PRO B 701  ? 0.1406 0.2194 0.1633 0.0140  0.0372  -0.0196 699  PRO B CB  
14423 C CG  . PRO B 701  ? 0.1725 0.2497 0.1887 0.0127  0.0388  -0.0177 699  PRO B CG  
14424 C CD  . PRO B 701  ? 0.1374 0.2118 0.1540 0.0100  0.0373  -0.0148 699  PRO B CD  
14425 N N   . ILE B 702  ? 0.1146 0.1881 0.1459 0.0140  0.0295  -0.0203 700  ILE B N   
14426 C CA  A ILE B 702  ? 0.1039 0.1786 0.1413 0.0137  0.0281  -0.0206 700  ILE B CA  
14427 C CA  B ILE B 702  ? 0.1040 0.1786 0.1413 0.0137  0.0280  -0.0206 700  ILE B CA  
14428 C C   . ILE B 702  ? 0.1238 0.2009 0.1639 0.0164  0.0281  -0.0234 700  ILE B C   
14429 O O   . ILE B 702  ? 0.1209 0.1955 0.1573 0.0186  0.0272  -0.0252 700  ILE B O   
14430 C CB  A ILE B 702  ? 0.1123 0.1823 0.1489 0.0131  0.0248  -0.0199 700  ILE B CB  
14431 C CB  B ILE B 702  ? 0.1124 0.1823 0.1489 0.0132  0.0247  -0.0200 700  ILE B CB  
14432 C CG1 A ILE B 702  ? 0.1262 0.1947 0.1618 0.0107  0.0249  -0.0171 700  ILE B CG1 
14433 C CG1 B ILE B 702  ? 0.1328 0.2002 0.1666 0.0112  0.0245  -0.0174 700  ILE B CG1 
14434 C CG2 A ILE B 702  ? 0.1152 0.1860 0.1572 0.0135  0.0231  -0.0209 700  ILE B CG2 
14435 C CG2 B ILE B 702  ? 0.1155 0.1864 0.1578 0.0131  0.0232  -0.0205 700  ILE B CG2 
14436 C CD1 A ILE B 702  ? 0.1164 0.1810 0.1514 0.0102  0.0220  -0.0162 700  ILE B CD1 
14437 C CD1 B ILE B 702  ? 0.1262 0.1954 0.1633 0.0090  0.0258  -0.0154 700  ILE B CD1 
14438 N N   . VAL B 703  ? 0.1141 0.1960 0.1605 0.0162  0.0290  -0.0236 701  VAL B N   
14439 C CA  . VAL B 703  ? 0.1014 0.1862 0.1513 0.0189  0.0287  -0.0261 701  VAL B CA  
14440 C C   . VAL B 703  ? 0.1240 0.2060 0.1762 0.0191  0.0253  -0.0265 701  VAL B C   
14441 O O   . VAL B 703  ? 0.1166 0.1990 0.1723 0.0170  0.0245  -0.0252 701  VAL B O   
14442 C CB  . VAL B 703  ? 0.1005 0.1930 0.1564 0.0185  0.0315  -0.0261 701  VAL B CB  
14443 C CG1 . VAL B 703  ? 0.1331 0.2289 0.1937 0.0213  0.0306  -0.0284 701  VAL B CG1 
14444 C CG2 . VAL B 703  ? 0.1283 0.2237 0.1813 0.0186  0.0351  -0.0258 701  VAL B CG2 
14445 N N   . CYS B 704  ? 0.0954 0.1739 0.1450 0.0216  0.0234  -0.0284 702  CYS B N   
14446 C CA  . CYS B 704  ? 0.0870 0.1624 0.1380 0.0219  0.0202  -0.0288 702  CYS B CA  
14447 C C   . CYS B 704  ? 0.1089 0.1869 0.1635 0.0247  0.0197  -0.0309 702  CYS B C   
14448 O O   . CYS B 704  ? 0.1145 0.1916 0.1665 0.0275  0.0199  -0.0327 702  CYS B O   
14449 C CB  . CYS B 704  ? 0.1005 0.1691 0.1455 0.0222  0.0180  -0.0289 702  CYS B CB  
14450 S SG  . CYS B 704  ? 0.1197 0.1854 0.1605 0.0193  0.0180  -0.0265 702  CYS B SG  
14451 N N   . ILE B 705  ? 0.1159 0.1969 0.1762 0.0240  0.0189  -0.0306 703  ILE B N   
14452 C CA  . ILE B 705  ? 0.1013 0.1856 0.1658 0.0266  0.0181  -0.0324 703  ILE B CA  
14453 C C   . ILE B 705  ? 0.1139 0.1938 0.1783 0.0267  0.0146  -0.0325 703  ILE B C   
14454 O O   . ILE B 705  ? 0.1018 0.1809 0.1678 0.0242  0.0136  -0.0311 703  ILE B O   
14455 C CB  . ILE B 705  ? 0.0937 0.1860 0.1653 0.0255  0.0199  -0.0320 703  ILE B CB  
14456 C CG1 . ILE B 705  ? 0.1317 0.2285 0.2030 0.0254  0.0237  -0.0317 703  ILE B CG1 
14457 C CG2 . ILE B 705  ? 0.1260 0.2220 0.2025 0.0282  0.0185  -0.0337 703  ILE B CG2 
14458 C CD1 . ILE B 705  ? 0.1504 0.2547 0.2281 0.0230  0.0258  -0.0306 703  ILE B CD1 
14459 N N   . SER B 706  ? 0.1092 0.1859 0.1713 0.0297  0.0129  -0.0342 704  SER B N   
14460 C CA  . SER B 706  ? 0.1328 0.2039 0.1928 0.0299  0.0097  -0.0343 704  SER B CA  
14461 C C   . SER B 706  ? 0.1250 0.1978 0.1884 0.0326  0.0079  -0.0357 704  SER B C   
14462 O O   . SER B 706  ? 0.1237 0.2010 0.1899 0.0353  0.0091  -0.0371 704  SER B O   
14463 C CB  . SER B 706  ? 0.1336 0.1977 0.1865 0.0306  0.0087  -0.0347 704  SER B CB  
14464 O OG  . SER B 706  ? 0.1305 0.1945 0.1813 0.0337  0.0096  -0.0366 704  SER B OG  
14465 N N   . PRO B 707  ? 0.1163 0.1858 0.1796 0.0321  0.0052  -0.0354 705  PRO B N   
14466 C CA  . PRO B 707  ? 0.1304 0.2014 0.1969 0.0344  0.0031  -0.0364 705  PRO B CA  
14467 C C   . PRO B 707  ? 0.1318 0.1972 0.1939 0.0377  0.0012  -0.0379 705  PRO B C   
14468 O O   . PRO B 707  ? 0.1547 0.2141 0.2109 0.0377  0.0010  -0.0379 705  PRO B O   
14469 C CB  . PRO B 707  ? 0.1403 0.2095 0.2077 0.0318  0.0012  -0.0351 705  PRO B CB  
14470 C CG  . PRO B 707  ? 0.1662 0.2296 0.2281 0.0297  0.0011  -0.0339 705  PRO B CG  
14471 C CD  . PRO B 707  ? 0.1353 0.2002 0.1959 0.0292  0.0039  -0.0337 705  PRO B CD  
14472 N N   . TRP B 708  ? 0.1177 0.1849 0.1828 0.0406  -0.0005 -0.0390 706  TRP B N   
14473 C CA  . TRP B 708  ? 0.1296 0.1909 0.1904 0.0440  -0.0027 -0.0403 706  TRP B CA  
14474 C C   . TRP B 708  ? 0.1291 0.1834 0.1860 0.0428  -0.0058 -0.0394 706  TRP B C   
14475 O O   . TRP B 708  ? 0.1598 0.2075 0.2117 0.0449  -0.0076 -0.0401 706  TRP B O   
14476 C CB  . TRP B 708  ? 0.1303 0.1964 0.1956 0.0482  -0.0033 -0.0420 706  TRP B CB  
14477 C CG  . TRP B 708  ? 0.1439 0.2162 0.2159 0.0473  -0.0043 -0.0414 706  TRP B CG  
14478 C CD1 . TRP B 708  ? 0.1696 0.2511 0.2487 0.0463  -0.0024 -0.0413 706  TRP B CD1 
14479 C CD2 . TRP B 708  ? 0.1404 0.2097 0.2122 0.0469  -0.0077 -0.0409 706  TRP B CD2 
14480 N NE1 . TRP B 708  ? 0.1656 0.2501 0.2491 0.0453  -0.0046 -0.0408 706  TRP B NE1 
14481 C CE2 . TRP B 708  ? 0.1727 0.2498 0.2517 0.0457  -0.0078 -0.0406 706  TRP B CE2 
14482 C CE3 . TRP B 708  ? 0.1472 0.2081 0.2133 0.0472  -0.0106 -0.0405 706  TRP B CE3 
14483 C CZ2 . TRP B 708  ? 0.1625 0.2389 0.2428 0.0450  -0.0108 -0.0401 706  TRP B CZ2 
14484 C CZ3 . TRP B 708  ? 0.1599 0.2203 0.2273 0.0466  -0.0134 -0.0399 706  TRP B CZ3 
14485 C CH2 . TRP B 708  ? 0.1557 0.2237 0.2300 0.0456  -0.0135 -0.0398 706  TRP B CH2 
14486 N N   . ASN B 709  ? 0.1351 0.1902 0.1937 0.0396  -0.0063 -0.0379 707  ASN B N   
14487 C CA  . ASN B 709  ? 0.1528 0.2018 0.2078 0.0387  -0.0091 -0.0371 707  ASN B CA  
14488 C C   . ASN B 709  ? 0.1577 0.2004 0.2067 0.0361  -0.0090 -0.0359 707  ASN B C   
14489 O O   . ASN B 709  ? 0.1815 0.2182 0.2263 0.0358  -0.0112 -0.0355 707  ASN B O   
14490 C CB  . ASN B 709  ? 0.1564 0.2088 0.2156 0.0368  -0.0101 -0.0362 707  ASN B CB  
14491 C CG  . ASN B 709  ? 0.1736 0.2286 0.2344 0.0330  -0.0081 -0.0348 707  ASN B CG  
14492 O OD1 . ASN B 709  ? 0.1775 0.2341 0.2382 0.0321  -0.0057 -0.0346 707  ASN B OD1 
14493 N ND2 . ASN B 709  ? 0.1578 0.2127 0.2196 0.0310  -0.0093 -0.0339 707  ASN B ND2 
14494 N N   . PHE B 710  ? 0.1424 0.1867 0.1911 0.0342  -0.0066 -0.0354 708  PHE B N   
14495 C CA  . PHE B 710  ? 0.1346 0.1737 0.1779 0.0321  -0.0065 -0.0345 708  PHE B CA  
14496 C C   . PHE B 710  ? 0.1387 0.1785 0.1804 0.0330  -0.0045 -0.0354 708  PHE B C   
14497 O O   . PHE B 710  ? 0.1281 0.1703 0.1702 0.0310  -0.0025 -0.0345 708  PHE B O   
14498 C CB  . PHE B 710  ? 0.1389 0.1788 0.1827 0.0286  -0.0059 -0.0326 708  PHE B CB  
14499 C CG  . PHE B 710  ? 0.1804 0.2180 0.2238 0.0277  -0.0079 -0.0319 708  PHE B CG  
14500 C CD1 . PHE B 710  ? 0.2060 0.2375 0.2443 0.0268  -0.0095 -0.0312 708  PHE B CD1 
14501 C CD2 . PHE B 710  ? 0.1885 0.2298 0.2363 0.0278  -0.0084 -0.0319 708  PHE B CD2 
14502 C CE1 . PHE B 710  ? 0.2466 0.2758 0.2839 0.0260  -0.0112 -0.0304 708  PHE B CE1 
14503 C CE2 . PHE B 710  ? 0.1954 0.2339 0.2419 0.0272  -0.0104 -0.0313 708  PHE B CE2 
14504 C CZ  . PHE B 710  ? 0.1844 0.2170 0.2257 0.0264  -0.0117 -0.0305 708  PHE B CZ  
14505 N N   . PRO B 711  ? 0.1385 0.1760 0.1781 0.0363  -0.0050 -0.0371 709  PRO B N   
14506 C CA  . PRO B 711  ? 0.1338 0.1728 0.1724 0.0379  -0.0029 -0.0384 709  PRO B CA  
14507 C C   . PRO B 711  ? 0.1295 0.1636 0.1622 0.0361  -0.0026 -0.0380 709  PRO B C   
14508 O O   . PRO B 711  ? 0.1398 0.1753 0.1712 0.0369  -0.0006 -0.0389 709  PRO B O   
14509 C CB  . PRO B 711  ? 0.1802 0.2173 0.2180 0.0423  -0.0040 -0.0404 709  PRO B CB  
14510 C CG  . PRO B 711  ? 0.1536 0.1837 0.1878 0.0420  -0.0073 -0.0399 709  PRO B CG  
14511 C CD  . PRO B 711  ? 0.1496 0.1823 0.1871 0.0389  -0.0077 -0.0380 709  PRO B CD  
14512 N N   . LEU B 712  ? 0.1291 0.1581 0.1582 0.0335  -0.0044 -0.0368 710  LEU B N   
14513 C CA  . LEU B 712  ? 0.1319 0.1577 0.1564 0.0310  -0.0041 -0.0360 710  LEU B CA  
14514 C C   . LEU B 712  ? 0.1343 0.1630 0.1609 0.0275  -0.0034 -0.0338 710  LEU B C   
14515 O O   . LEU B 712  ? 0.1413 0.1719 0.1674 0.0259  -0.0019 -0.0332 710  LEU B O   
14516 C CB  . LEU B 712  ? 0.1429 0.1604 0.1611 0.0307  -0.0066 -0.0363 710  LEU B CB  
14517 C CG  . LEU B 712  ? 0.1395 0.1538 0.1530 0.0278  -0.0068 -0.0356 710  LEU B CG  
14518 C CD1 . LEU B 712  ? 0.1547 0.1691 0.1657 0.0293  -0.0052 -0.0371 710  LEU B CD1 
14519 C CD2 . LEU B 712  ? 0.1844 0.1907 0.1924 0.0266  -0.0095 -0.0354 710  LEU B CD2 
14520 N N   . ALA B 713  ? 0.1209 0.1501 0.1499 0.0263  -0.0045 -0.0327 711  ALA B N   
14521 C CA  . ALA B 713  ? 0.1266 0.1575 0.1567 0.0232  -0.0041 -0.0307 711  ALA B CA  
14522 C C   . ALA B 713  ? 0.1177 0.1548 0.1523 0.0227  -0.0017 -0.0301 711  ALA B C   
14523 O O   . ALA B 713  ? 0.1253 0.1636 0.1593 0.0208  -0.0007 -0.0290 711  ALA B O   
14524 C CB  . ALA B 713  ? 0.1381 0.1674 0.1688 0.0223  -0.0057 -0.0298 711  ALA B CB  
14525 N N   . ILE B 714  ? 0.1338 0.1749 0.1729 0.0241  -0.0011 -0.0308 712  ILE B N   
14526 C CA  . ILE B 714  ? 0.1315 0.1780 0.1747 0.0232  0.0011  -0.0300 712  ILE B CA  
14527 C C   . ILE B 714  ? 0.1243 0.1727 0.1665 0.0239  0.0032  -0.0307 712  ILE B C   
14528 O O   . ILE B 714  ? 0.1339 0.1848 0.1767 0.0223  0.0049  -0.0296 712  ILE B O   
14529 C CB  . ILE B 714  ? 0.1202 0.1707 0.1687 0.0239  0.0010  -0.0304 712  ILE B CB  
14530 C CG1 . ILE B 714  ? 0.1254 0.1738 0.1741 0.0226  -0.0008 -0.0295 712  ILE B CG1 
14531 C CG2 . ILE B 714  ? 0.1458 0.2017 0.1983 0.0228  0.0034  -0.0298 712  ILE B CG2 
14532 C CD1 . ILE B 714  ? 0.1819 0.2335 0.2352 0.0230  -0.0013 -0.0298 712  ILE B CD1 
14533 N N   . PHE B 715  ? 0.1165 0.1635 0.1567 0.0265  0.0030  -0.0325 713  PHE B N   
14534 C CA  . PHE B 715  ? 0.1215 0.1692 0.1594 0.0274  0.0049  -0.0333 713  PHE B CA  
14535 C C   . PHE B 715  ? 0.1119 0.1569 0.1455 0.0250  0.0050  -0.0320 713  PHE B C   
14536 O O   . PHE B 715  ? 0.1225 0.1703 0.1563 0.0240  0.0069  -0.0313 713  PHE B O   
14537 C CB  . PHE B 715  ? 0.1296 0.1739 0.1645 0.0306  0.0040  -0.0355 713  PHE B CB  
14538 C CG  . PHE B 715  ? 0.1276 0.1718 0.1591 0.0319  0.0058  -0.0367 713  PHE B CG  
14539 C CD1 . PHE B 715  ? 0.1385 0.1884 0.1731 0.0337  0.0084  -0.0375 713  PHE B CD1 
14540 C CD2 . PHE B 715  ? 0.1367 0.1750 0.1616 0.0313  0.0048  -0.0369 713  PHE B CD2 
14541 C CE1 . PHE B 715  ? 0.1678 0.2175 0.1987 0.0350  0.0102  -0.0387 713  PHE B CE1 
14542 C CE2 . PHE B 715  ? 0.1552 0.1929 0.1762 0.0325  0.0063  -0.0382 713  PHE B CE2 
14543 C CZ  . PHE B 715  ? 0.1536 0.1968 0.1774 0.0345  0.0091  -0.0391 713  PHE B CZ  
14544 N N   . THR B 716  ? 0.1287 0.1685 0.1586 0.0240  0.0027  -0.0317 714  THR B N   
14545 C CA  . THR B 716  ? 0.1308 0.1683 0.1568 0.0217  0.0024  -0.0306 714  THR B CA  
14546 C C   . THR B 716  ? 0.1146 0.1554 0.1433 0.0194  0.0032  -0.0284 714  THR B C   
14547 O O   . THR B 716  ? 0.1130 0.1546 0.1401 0.0182  0.0041  -0.0274 714  THR B O   
14548 C CB  . THR B 716  ? 0.1324 0.1641 0.1544 0.0209  -0.0003 -0.0306 714  THR B CB  
14549 O OG1 . THR B 716  ? 0.1598 0.1874 0.1784 0.0232  -0.0011 -0.0327 714  THR B OG1 
14550 C CG2 . THR B 716  ? 0.1507 0.1808 0.1692 0.0183  -0.0009 -0.0294 714  THR B CG2 
14551 N N   . GLY B 717  ? 0.1031 0.1454 0.1356 0.0188  0.0027  -0.0275 715  GLY B N   
14552 C CA  . GLY B 717  ? 0.1125 0.1570 0.1472 0.0168  0.0033  -0.0256 715  GLY B CA  
14553 C C   . GLY B 717  ? 0.1026 0.1510 0.1392 0.0166  0.0057  -0.0250 715  GLY B C   
14554 O O   . GLY B 717  ? 0.1153 0.1642 0.1508 0.0153  0.0063  -0.0235 715  GLY B O   
14555 N N   . GLN B 718  ? 0.0999 0.1512 0.1394 0.0179  0.0070  -0.0260 716  GLN B N   
14556 C CA  . GLN B 718  ? 0.0982 0.1533 0.1395 0.0174  0.0094  -0.0253 716  GLN B CA  
14557 C C   . GLN B 718  ? 0.1113 0.1656 0.1484 0.0174  0.0105  -0.0252 716  GLN B C   
14558 O O   . GLN B 718  ? 0.1097 0.1649 0.1459 0.0160  0.0115  -0.0236 716  GLN B O   
14559 C CB  . GLN B 718  ? 0.1134 0.1725 0.1590 0.0187  0.0107  -0.0264 716  GLN B CB  
14560 C CG  . GLN B 718  ? 0.1214 0.1816 0.1714 0.0184  0.0095  -0.0264 716  GLN B CG  
14561 C CD  . GLN B 718  ? 0.1290 0.1940 0.1838 0.0194  0.0106  -0.0274 716  GLN B CD  
14562 O OE1 . GLN B 718  ? 0.1299 0.1973 0.1888 0.0182  0.0106  -0.0268 716  GLN B OE1 
14563 N NE2 . GLN B 718  ? 0.1151 0.1816 0.1695 0.0217  0.0114  -0.0290 716  GLN B NE2 
14564 N N   . ILE B 719  ? 0.1000 0.1523 0.1339 0.0191  0.0100  -0.0270 717  ILE B N   
14565 C CA  . ILE B 719  ? 0.1134 0.1646 0.1425 0.0193  0.0109  -0.0273 717  ILE B CA  
14566 C C   . ILE B 719  ? 0.1065 0.1551 0.1321 0.0173  0.0096  -0.0258 717  ILE B C   
14567 O O   . ILE B 719  ? 0.1139 0.1632 0.1372 0.0165  0.0107  -0.0248 717  ILE B O   
14568 C CB  . ILE B 719  ? 0.1097 0.1582 0.1356 0.0217  0.0104  -0.0298 717  ILE B CB  
14569 C CG1 . ILE B 719  ? 0.1143 0.1669 0.1440 0.0240  0.0123  -0.0312 717  ILE B CG1 
14570 C CG2 . ILE B 719  ? 0.1766 0.2223 0.1963 0.0217  0.0106  -0.0302 717  ILE B CG2 
14571 C CD1 . ILE B 719  ? 0.2065 0.2562 0.2338 0.0269  0.0114  -0.0336 717  ILE B CD1 
14572 N N   . ALA B 720  ? 0.1162 0.1619 0.1412 0.0166  0.0072  -0.0255 718  ALA B N   
14573 C CA  . ALA B 720  ? 0.1046 0.1484 0.1267 0.0147  0.0058  -0.0241 718  ALA B CA  
14574 C C   . ALA B 720  ? 0.1082 0.1549 0.1325 0.0134  0.0067  -0.0219 718  ALA B C   
14575 O O   . ALA B 720  ? 0.1179 0.1646 0.1397 0.0124  0.0067  -0.0207 718  ALA B O   
14576 C CB  . ALA B 720  ? 0.1075 0.1485 0.1294 0.0140  0.0034  -0.0242 718  ALA B CB  
14577 N N   . ALA B 721  ? 0.1051 0.1539 0.1340 0.0133  0.0074  -0.0212 719  ALA B N   
14578 C CA  . ALA B 721  ? 0.0957 0.1464 0.1265 0.0122  0.0083  -0.0192 719  ALA B CA  
14579 C C   . ALA B 721  ? 0.1099 0.1622 0.1393 0.0122  0.0104  -0.0186 719  ALA B C   
14580 O O   . ALA B 721  ? 0.1075 0.1597 0.1350 0.0113  0.0104  -0.0169 719  ALA B O   
14581 C CB  . ALA B 721  ? 0.1156 0.1676 0.1510 0.0122  0.0086  -0.0190 719  ALA B CB  
14582 N N   . ALA B 722  ? 0.0995 0.1534 0.1298 0.0131  0.0121  -0.0199 720  ALA B N   
14583 C CA  . ALA B 722  ? 0.0962 0.1519 0.1250 0.0129  0.0144  -0.0193 720  ALA B CA  
14584 C C   . ALA B 722  ? 0.1052 0.1589 0.1281 0.0129  0.0139  -0.0192 720  ALA B C   
14585 O O   . ALA B 722  ? 0.1118 0.1657 0.1326 0.0120  0.0147  -0.0175 720  ALA B O   
14586 C CB  . ALA B 722  ? 0.0872 0.1457 0.1182 0.0141  0.0164  -0.0209 720  ALA B CB  
14587 N N   . LEU B 723  ? 0.1083 0.1596 0.1283 0.0138  0.0125  -0.0209 721  LEU B N   
14588 C CA  . LEU B 723  ? 0.1193 0.1682 0.1333 0.0136  0.0118  -0.0211 721  LEU B CA  
14589 C C   . LEU B 723  ? 0.1203 0.1684 0.1330 0.0120  0.0100  -0.0190 721  LEU B C   
14590 O O   . LEU B 723  ? 0.1237 0.1717 0.1327 0.0114  0.0103  -0.0179 721  LEU B O   
14591 C CB  . LEU B 723  ? 0.1189 0.1645 0.1300 0.0146  0.0101  -0.0234 721  LEU B CB  
14592 C CG  . LEU B 723  ? 0.1300 0.1757 0.1406 0.0169  0.0117  -0.0258 721  LEU B CG  
14593 C CD1 . LEU B 723  ? 0.1446 0.1860 0.1526 0.0178  0.0094  -0.0278 721  LEU B CD1 
14594 C CD2 . LEU B 723  ? 0.1340 0.1805 0.1404 0.0175  0.0138  -0.0262 721  LEU B CD2 
14595 N N   . VAL B 724  ? 0.1054 0.1532 0.1209 0.0113  0.0082  -0.0184 722  VAL B N   
14596 C CA  . VAL B 724  ? 0.1087 0.1562 0.1231 0.0100  0.0064  -0.0166 722  VAL B CA  
14597 C C   . VAL B 724  ? 0.1149 0.1644 0.1308 0.0097  0.0075  -0.0143 722  VAL B C   
14598 O O   . VAL B 724  ? 0.1140 0.1635 0.1278 0.0090  0.0064  -0.0127 722  VAL B O   
14599 C CB  . VAL B 724  ? 0.1202 0.1672 0.1370 0.0095  0.0043  -0.0166 722  VAL B CB  
14600 C CG1 . VAL B 724  ? 0.1136 0.1623 0.1356 0.0096  0.0050  -0.0156 722  VAL B CG1 
14601 C CG2 . VAL B 724  ? 0.1094 0.1561 0.1240 0.0082  0.0021  -0.0155 722  VAL B CG2 
14602 N N   . ALA B 725  ? 0.1150 0.1658 0.1341 0.0100  0.0095  -0.0140 723  ALA B N   
14603 C CA  . ALA B 725  ? 0.1045 0.1563 0.1242 0.0095  0.0108  -0.0119 723  ALA B CA  
14604 C C   . ALA B 725  ? 0.1455 0.1973 0.1609 0.0094  0.0123  -0.0114 723  ALA B C   
14605 O O   . ALA B 725  ? 0.1672 0.2192 0.1822 0.0089  0.0134  -0.0094 723  ALA B O   
14606 C CB  . ALA B 725  ? 0.1183 0.1713 0.1427 0.0095  0.0123  -0.0118 723  ALA B CB  
14607 N N   . GLY B 726  ? 0.1187 0.1697 0.1304 0.0099  0.0124  -0.0131 724  GLY B N   
14608 C CA  . GLY B 726  ? 0.1278 0.1785 0.1345 0.0099  0.0137  -0.0128 724  GLY B CA  
14609 C C   . GLY B 726  ? 0.1505 0.2029 0.1574 0.0104  0.0168  -0.0138 724  GLY B C   
14610 O O   . GLY B 726  ? 0.1545 0.2071 0.1575 0.0102  0.0184  -0.0131 724  GLY B O   
14611 N N   . ASN B 727  ? 0.1274 0.1814 0.1387 0.0112  0.0177  -0.0154 725  ASN B N   
14612 C CA  . ASN B 727  ? 0.1244 0.1812 0.1374 0.0118  0.0207  -0.0164 725  ASN B CA  
14613 C C   . ASN B 727  ? 0.1303 0.1867 0.1413 0.0137  0.0209  -0.0193 725  ASN B C   
14614 O O   . ASN B 727  ? 0.1419 0.1966 0.1539 0.0145  0.0188  -0.0207 725  ASN B O   
14615 C CB  . ASN B 727  ? 0.1247 0.1840 0.1444 0.0114  0.0214  -0.0161 725  ASN B CB  
14616 C CG  . ASN B 727  ? 0.1410 0.1997 0.1625 0.0097  0.0209  -0.0135 725  ASN B CG  
14617 O OD1 . ASN B 727  ? 0.1376 0.1969 0.1582 0.0086  0.0227  -0.0117 725  ASN B OD1 
14618 N ND2 . ASN B 727  ? 0.1385 0.1958 0.1625 0.0096  0.0186  -0.0133 725  ASN B ND2 
14619 N N   . PRO B 728  ? 0.1280 0.1857 0.1361 0.0146  0.0234  -0.0202 726  PRO B N   
14620 C CA  . PRO B 728  ? 0.1168 0.1745 0.1239 0.0169  0.0239  -0.0232 726  PRO B CA  
14621 C C   . PRO B 728  ? 0.1419 0.2032 0.1559 0.0179  0.0249  -0.0241 726  PRO B C   
14622 O O   . PRO B 728  ? 0.1341 0.1988 0.1529 0.0165  0.0262  -0.0225 726  PRO B O   
14623 C CB  . PRO B 728  ? 0.1552 0.2140 0.1574 0.0176  0.0267  -0.0235 726  PRO B CB  
14624 C CG  . PRO B 728  ? 0.1583 0.2201 0.1624 0.0155  0.0289  -0.0207 726  PRO B CG  
14625 C CD  . PRO B 728  ? 0.1319 0.1918 0.1383 0.0136  0.0262  -0.0185 726  PRO B CD  
14626 N N   . VAL B 729  ? 0.1048 0.1650 0.1192 0.0201  0.0239  -0.0267 727  VAL B N   
14627 C CA  . VAL B 729  ? 0.1064 0.1693 0.1273 0.0211  0.0238  -0.0276 727  VAL B CA  
14628 C C   . VAL B 729  ? 0.1309 0.1964 0.1524 0.0241  0.0258  -0.0301 727  VAL B C   
14629 O O   . VAL B 729  ? 0.1350 0.1976 0.1513 0.0261  0.0256  -0.0321 727  VAL B O   
14630 C CB  . VAL B 729  ? 0.1152 0.1741 0.1366 0.0211  0.0203  -0.0281 727  VAL B CB  
14631 C CG1 . VAL B 729  ? 0.1314 0.1922 0.1581 0.0229  0.0199  -0.0296 727  VAL B CG1 
14632 C CG2 . VAL B 729  ? 0.1262 0.1843 0.1491 0.0185  0.0188  -0.0256 727  VAL B CG2 
14633 N N   . LEU B 730  ? 0.1057 0.1769 0.1337 0.0244  0.0275  -0.0301 728  LEU B N   
14634 C CA  . LEU B 730  ? 0.1141 0.1889 0.1447 0.0276  0.0290  -0.0325 728  LEU B CA  
14635 C C   . LEU B 730  ? 0.1294 0.2038 0.1648 0.0284  0.0264  -0.0332 728  LEU B C   
14636 O O   . LEU B 730  ? 0.1283 0.2057 0.1693 0.0266  0.0261  -0.0318 728  LEU B O   
14637 C CB  . LEU B 730  ? 0.1410 0.2235 0.1760 0.0271  0.0327  -0.0318 728  LEU B CB  
14638 C CG  . LEU B 730  ? 0.1411 0.2251 0.1720 0.0260  0.0359  -0.0307 728  LEU B CG  
14639 C CD1 . LEU B 730  ? 0.1607 0.2402 0.1836 0.0284  0.0359  -0.0326 728  LEU B CD1 
14640 C CD2 . LEU B 730  ? 0.1633 0.2454 0.1930 0.0221  0.0354  -0.0276 728  LEU B CD2 
14641 N N   . ALA B 731  ? 0.1114 0.1815 0.1440 0.0310  0.0243  -0.0354 729  ALA B N   
14642 C CA  . ALA B 731  ? 0.1087 0.1770 0.1445 0.0318  0.0215  -0.0359 729  ALA B CA  
14643 C C   . ALA B 731  ? 0.1350 0.2078 0.1753 0.0352  0.0224  -0.0379 729  ALA B C   
14644 O O   . ALA B 731  ? 0.1421 0.2138 0.1793 0.0385  0.0231  -0.0401 729  ALA B O   
14645 C CB  . ALA B 731  ? 0.1510 0.2112 0.1807 0.0322  0.0184  -0.0367 729  ALA B CB  
14646 N N   . LYS B 732  ? 0.1214 0.1993 0.1688 0.0345  0.0223  -0.0372 730  LYS B N   
14647 C CA  . LYS B 732  ? 0.1442 0.2275 0.1970 0.0375  0.0229  -0.0388 730  LYS B CA  
14648 C C   . LYS B 732  ? 0.1246 0.2049 0.1794 0.0383  0.0193  -0.0392 730  LYS B C   
14649 O O   . LYS B 732  ? 0.1447 0.2269 0.2039 0.0360  0.0182  -0.0378 730  LYS B O   
14650 C CB  . LYS B 732  ? 0.1402 0.2326 0.2000 0.0359  0.0256  -0.0377 730  LYS B CB  
14651 C CG  . LYS B 732  ? 0.1755 0.2753 0.2396 0.0393  0.0280  -0.0395 730  LYS B CG  
14652 C CD  . LYS B 732  ? 0.1846 0.2851 0.2522 0.0428  0.0256  -0.0413 730  LYS B CD  
14653 C CE  . LYS B 732  ? 0.1734 0.2770 0.2476 0.0406  0.0237  -0.0400 730  LYS B CE  
14654 N NZ  . LYS B 732  ? 0.1991 0.3032 0.2763 0.0442  0.0211  -0.0418 730  LYS B NZ  
14655 N N   . PRO B 733  ? 0.1096 0.1848 0.1607 0.0415  0.0174  -0.0411 731  PRO B N   
14656 C CA  . PRO B 733  ? 0.1264 0.1980 0.1785 0.0423  0.0139  -0.0413 731  PRO B CA  
14657 C C   . PRO B 733  ? 0.1088 0.1869 0.1680 0.0446  0.0137  -0.0422 731  PRO B C   
14658 O O   . PRO B 733  ? 0.1354 0.2204 0.1983 0.0466  0.0163  -0.0431 731  PRO B O   
14659 C CB  . PRO B 733  ? 0.1450 0.2084 0.1899 0.0450  0.0122  -0.0431 731  PRO B CB  
14660 C CG  . PRO B 733  ? 0.1477 0.2135 0.1907 0.0477  0.0151  -0.0448 731  PRO B CG  
14661 C CD  . PRO B 733  ? 0.1530 0.2248 0.1982 0.0447  0.0183  -0.0432 731  PRO B CD  
14662 N N   . ALA B 734  ? 0.1231 0.1991 0.1840 0.0443  0.0107  -0.0418 732  ALA B N   
14663 C CA  . ALA B 734  ? 0.1245 0.2061 0.1918 0.0468  0.0098  -0.0427 732  ALA B CA  
14664 C C   . ALA B 734  ? 0.1477 0.2299 0.2143 0.0521  0.0103  -0.0452 732  ALA B C   
14665 O O   . ALA B 734  ? 0.1445 0.2194 0.2043 0.0542  0.0095  -0.0464 732  ALA B O   
14666 C CB  . ALA B 734  ? 0.1257 0.2030 0.1931 0.0462  0.0060  -0.0421 732  ALA B CB  
14667 N N   . GLU B 735  ? 0.1251 0.2162 0.1987 0.0543  0.0115  -0.0460 733  GLU B N   
14668 C CA  . GLU B 735  ? 0.1301 0.2225 0.2036 0.0596  0.0120  -0.0481 733  GLU B CA  
14669 C C   . GLU B 735  ? 0.1436 0.2278 0.2128 0.0631  0.0083  -0.0495 733  GLU B C   
14670 O O   . GLU B 735  ? 0.1442 0.2239 0.2085 0.0668  0.0083  -0.0511 733  GLU B O   
14671 C CB  . GLU B 735  ? 0.1606 0.2623 0.2419 0.0595  0.0131  -0.0472 733  GLU B CB  
14672 C CG  . GLU B 735  ? 0.2510 0.3541 0.3321 0.0640  0.0140  -0.0484 733  GLU B CG  
14673 C CD  . GLU B 735  ? 0.2866 0.3999 0.3759 0.0636  0.0155  -0.0474 733  GLU B CD  
14674 O OE1 . GLU B 735  ? 0.2818 0.4005 0.3766 0.0596  0.0155  -0.0457 733  GLU B OE1 
14675 O OE2 . GLU B 735  ? 0.3665 0.4825 0.4567 0.0672  0.0167  -0.0483 733  GLU B OE2 
14676 N N   . GLU B 736  ? 0.1477 0.2287 0.2175 0.0614  0.0050  -0.0484 734  GLU B N   
14677 C CA  . GLU B 736  ? 0.1380 0.2111 0.2037 0.0643  0.0013  -0.0492 734  GLU B CA  
14678 C C   . GLU B 736  ? 0.1566 0.2180 0.2126 0.0637  0.0001  -0.0493 734  GLU B C   
14679 O O   . GLU B 736  ? 0.1892 0.2434 0.2405 0.0669  -0.0023 -0.0505 734  GLU B O   
14680 C CB  . GLU B 736  ? 0.1505 0.2240 0.2196 0.0622  -0.0018 -0.0478 734  GLU B CB  
14681 C CG  . GLU B 736  ? 0.1979 0.2821 0.2762 0.0626  -0.0015 -0.0476 734  GLU B CG  
14682 C CD  . GLU B 736  ? 0.2068 0.2986 0.2906 0.0579  0.0009  -0.0461 734  GLU B CD  
14683 O OE1 . GLU B 736  ? 0.1743 0.2641 0.2551 0.0547  0.0030  -0.0451 734  GLU B OE1 
14684 O OE2 . GLU B 736  ? 0.2546 0.3529 0.3446 0.0566  0.0004  -0.0451 734  GLU B OE2 
14685 N N   . THR B 737  ? 0.1597 0.2189 0.2124 0.0595  0.0015  -0.0480 735  THR B N   
14686 C CA  . THR B 737  ? 0.1630 0.2117 0.2072 0.0577  -0.0001 -0.0476 735  THR B CA  
14687 C C   . THR B 737  ? 0.1519 0.1992 0.1917 0.0564  0.0025  -0.0479 735  THR B C   
14688 O O   . THR B 737  ? 0.1659 0.2104 0.2029 0.0523  0.0025  -0.0463 735  THR B O   
14689 C CB  . THR B 737  ? 0.1349 0.1810 0.1791 0.0533  -0.0021 -0.0453 735  THR B CB  
14690 O OG1 . THR B 737  ? 0.1465 0.1996 0.1957 0.0497  0.0001  -0.0438 735  THR B OG1 
14691 C CG2 . THR B 737  ? 0.1452 0.1903 0.1915 0.0547  -0.0052 -0.0452 735  THR B CG2 
14692 N N   . PRO B 738  ? 0.1556 0.2048 0.1945 0.0600  0.0046  -0.0499 736  PRO B N   
14693 C CA  . PRO B 738  ? 0.1466 0.1945 0.1808 0.0588  0.0071  -0.0502 736  PRO B CA  
14694 C C   . PRO B 738  ? 0.1490 0.1858 0.1738 0.0584  0.0051  -0.0508 736  PRO B C   
14695 O O   . PRO B 738  ? 0.1511 0.1860 0.1717 0.0560  0.0063  -0.0504 736  PRO B O   
14696 C CB  . PRO B 738  ? 0.1600 0.2139 0.1965 0.0632  0.0100  -0.0523 736  PRO B CB  
14697 C CG  . PRO B 738  ? 0.1641 0.2164 0.2019 0.0680  0.0078  -0.0540 736  PRO B CG  
14698 C CD  . PRO B 738  ? 0.1402 0.1935 0.1825 0.0655  0.0051  -0.0520 736  PRO B CD  
14699 N N   . LEU B 739  ? 0.1565 0.1857 0.1777 0.0608  0.0020  -0.0518 737  LEU B N   
14700 C CA  . LEU B 739  ? 0.1538 0.1722 0.1656 0.0608  0.0003  -0.0528 737  LEU B CA  
14701 C C   . LEU B 739  ? 0.1456 0.1597 0.1544 0.0552  -0.0012 -0.0505 737  LEU B C   
14702 O O   . LEU B 739  ? 0.1563 0.1659 0.1591 0.0532  -0.0010 -0.0507 737  LEU B O   
14703 C CB  . LEU B 739  ? 0.1647 0.1756 0.1731 0.0647  -0.0026 -0.0544 737  LEU B CB  
14704 C CG  . LEU B 739  ? 0.1685 0.1836 0.1800 0.0710  -0.0014 -0.0567 737  LEU B CG  
14705 C CD1 . LEU B 739  ? 0.1892 0.1964 0.1975 0.0746  -0.0049 -0.0577 737  LEU B CD1 
14706 C CD2 . LEU B 739  ? 0.1954 0.2105 0.2030 0.0737  0.0014  -0.0590 737  LEU B CD2 
14707 N N   . ILE B 740  ? 0.1576 0.1733 0.1703 0.0525  -0.0027 -0.0485 738  ILE B N   
14708 C CA  . ILE B 740  ? 0.1548 0.1672 0.1651 0.0475  -0.0039 -0.0463 738  ILE B CA  
14709 C C   . ILE B 740  ? 0.1504 0.1686 0.1626 0.0445  -0.0012 -0.0451 738  ILE B C   
14710 O O   . ILE B 740  ? 0.1563 0.1712 0.1645 0.0411  -0.0017 -0.0441 738  ILE B O   
14711 C CB  . ILE B 740  ? 0.1718 0.1846 0.1855 0.0457  -0.0060 -0.0445 738  ILE B CB  
14712 C CG1 . ILE B 740  ? 0.1784 0.1876 0.1892 0.0407  -0.0072 -0.0424 738  ILE B CG1 
14713 C CG2 . ILE B 740  ? 0.1847 0.2073 0.2069 0.0456  -0.0042 -0.0437 738  ILE B CG2 
14714 C CD1 . ILE B 740  ? 0.2052 0.2046 0.2079 0.0399  -0.0093 -0.0429 738  ILE B CD1 
14715 N N   . ALA B 741  ? 0.1556 0.1825 0.1738 0.0455  0.0015  -0.0452 739  ALA B N   
14716 C CA  . ALA B 741  ? 0.1659 0.1978 0.1852 0.0430  0.0042  -0.0441 739  ALA B CA  
14717 C C   . ALA B 741  ? 0.1454 0.1732 0.1578 0.0437  0.0051  -0.0454 739  ALA B C   
14718 O O   . ALA B 741  ? 0.1462 0.1731 0.1558 0.0405  0.0055  -0.0442 739  ALA B O   
14719 C CB  . ALA B 741  ? 0.1773 0.2188 0.2039 0.0442  0.0070  -0.0440 739  ALA B CB  
14720 N N   . ALA B 742  ? 0.1387 0.1645 0.1485 0.0480  0.0056  -0.0480 740  ALA B N   
14721 C CA  . ALA B 742  ? 0.1417 0.1628 0.1442 0.0489  0.0063  -0.0496 740  ALA B CA  
14722 C C   . ALA B 742  ? 0.1639 0.1759 0.1593 0.0459  0.0033  -0.0491 740  ALA B C   
14723 O O   . ALA B 742  ? 0.1640 0.1740 0.1546 0.0439  0.0037  -0.0490 740  ALA B O   
14724 C CB  . ALA B 742  ? 0.1524 0.1715 0.1526 0.0544  0.0069  -0.0527 740  ALA B CB  
14725 N N   . GLU B 743  ? 0.1622 0.1692 0.1571 0.0452  0.0002  -0.0486 741  GLU B N   
14726 C CA  . GLU B 743  ? 0.1728 0.1716 0.1615 0.0420  -0.0026 -0.0479 741  GLU B CA  
14727 C C   . GLU B 743  ? 0.1628 0.1651 0.1535 0.0370  -0.0025 -0.0452 741  GLU B C   
14728 O O   . GLU B 743  ? 0.1679 0.1663 0.1536 0.0343  -0.0035 -0.0448 741  GLU B O   
14729 C CB  . GLU B 743  ? 0.1992 0.1921 0.1871 0.0425  -0.0057 -0.0479 741  GLU B CB  
14730 C CG  . GLU B 743  ? 0.1928 0.1773 0.1746 0.0388  -0.0087 -0.0469 741  GLU B CG  
14731 C CD  . GLU B 743  ? 0.2396 0.2157 0.2126 0.0393  -0.0098 -0.0489 741  GLU B CD  
14732 O OE1 . GLU B 743  ? 0.2289 0.2044 0.1996 0.0433  -0.0083 -0.0514 741  GLU B OE1 
14733 O OE2 . GLU B 743  ? 0.2810 0.2512 0.2493 0.0356  -0.0121 -0.0481 741  GLU B OE2 
14734 N N   . GLY B 744  ? 0.1511 0.1608 0.1492 0.0360  -0.0012 -0.0434 742  GLY B N   
14735 C CA  . GLY B 744  ? 0.1549 0.1683 0.1551 0.0319  -0.0008 -0.0409 742  GLY B CA  
14736 C C   . GLY B 744  ? 0.1327 0.1484 0.1306 0.0313  0.0013  -0.0410 742  GLY B C   
14737 O O   . GLY B 744  ? 0.1543 0.1689 0.1497 0.0281  0.0005  -0.0396 742  GLY B O   
14738 N N   . VAL B 745  ? 0.1350 0.1540 0.1335 0.0342  0.0039  -0.0425 743  VAL B N   
14739 C CA  . VAL B 745  ? 0.1414 0.1621 0.1369 0.0337  0.0059  -0.0426 743  VAL B CA  
14740 C C   . VAL B 745  ? 0.1578 0.1707 0.1445 0.0334  0.0041  -0.0440 743  VAL B C   
14741 O O   . VAL B 745  ? 0.1752 0.1876 0.1585 0.0310  0.0041  -0.0431 743  VAL B O   
14742 C CB  . VAL B 745  ? 0.1507 0.1772 0.1489 0.0370  0.0094  -0.0439 743  VAL B CB  
14743 C CG1 . VAL B 745  ? 0.1458 0.1725 0.1389 0.0370  0.0114  -0.0445 743  VAL B CG1 
14744 C CG2 . VAL B 745  ? 0.1645 0.1991 0.1710 0.0361  0.0111  -0.0421 743  VAL B CG2 
14745 N N   . ARG B 746  ? 0.1426 0.1489 0.1253 0.0358  0.0024  -0.0462 744  ARG B N   
14746 C CA  . ARG B 746  ? 0.1662 0.1639 0.1401 0.0351  0.0003  -0.0476 744  ARG B CA  
14747 C C   . ARG B 746  ? 0.1578 0.1534 0.1304 0.0302  -0.0022 -0.0453 744  ARG B C   
14748 O O   . ARG B 746  ? 0.1786 0.1714 0.1458 0.0281  -0.0031 -0.0454 744  ARG B O   
14749 C CB  . ARG B 746  ? 0.1859 0.1758 0.1559 0.0380  -0.0017 -0.0499 744  ARG B CB  
14750 C CG  . ARG B 746  ? 0.1893 0.1800 0.1590 0.0435  0.0005  -0.0526 744  ARG B CG  
14751 C CD  . ARG B 746  ? 0.2009 0.1825 0.1660 0.0461  -0.0022 -0.0546 744  ARG B CD  
14752 N NE  . ARG B 746  ? 0.2173 0.2006 0.1835 0.0519  -0.0002 -0.0571 744  ARG B NE  
14753 C CZ  . ARG B 746  ? 0.1769 0.1640 0.1492 0.0547  0.0000  -0.0571 744  ARG B CZ  
14754 N NH1 . ARG B 746  ? 0.1883 0.1754 0.1646 0.0526  -0.0021 -0.0551 744  ARG B NH1 
14755 N NH2 . ARG B 746  ? 0.2250 0.2163 0.1996 0.0598  0.0025  -0.0591 744  ARG B NH2 
14756 N N   . ILE B 747  ? 0.1435 0.1406 0.1209 0.0283  -0.0035 -0.0434 745  ILE B N   
14757 C CA  . ILE B 747  ? 0.1414 0.1369 0.1181 0.0238  -0.0059 -0.0413 745  ILE B CA  
14758 C C   . ILE B 747  ? 0.1517 0.1534 0.1308 0.0213  -0.0046 -0.0393 745  ILE B C   
14759 O O   . ILE B 747  ? 0.1557 0.1556 0.1313 0.0184  -0.0061 -0.0384 745  ILE B O   
14760 C CB  . ILE B 747  ? 0.1421 0.1376 0.1231 0.0228  -0.0074 -0.0399 745  ILE B CB  
14761 C CG1 . ILE B 747  ? 0.1567 0.1434 0.1327 0.0242  -0.0097 -0.0417 745  ILE B CG1 
14762 C CG2 . ILE B 747  ? 0.1664 0.1637 0.1491 0.0184  -0.0087 -0.0372 745  ILE B CG2 
14763 C CD1 . ILE B 747  ? 0.1921 0.1784 0.1718 0.0243  -0.0109 -0.0407 745  ILE B CD1 
14764 N N   . LEU B 748  ? 0.1477 0.1566 0.1326 0.0225  -0.0018 -0.0384 746  LEU B N   
14765 C CA  . LEU B 748  ? 0.1520 0.1661 0.1388 0.0204  -0.0006 -0.0364 746  LEU B CA  
14766 C C   . LEU B 748  ? 0.1412 0.1537 0.1218 0.0206  0.0001  -0.0373 746  LEU B C   
14767 O O   . LEU B 748  ? 0.1431 0.1564 0.1220 0.0180  -0.0007 -0.0358 746  LEU B O   
14768 C CB  . LEU B 748  ? 0.1503 0.1716 0.1440 0.0215  0.0022  -0.0353 746  LEU B CB  
14769 C CG  . LEU B 748  ? 0.1790 0.2028 0.1787 0.0201  0.0015  -0.0334 746  LEU B CG  
14770 C CD1 . LEU B 748  ? 0.1772 0.2066 0.1831 0.0219  0.0039  -0.0333 746  LEU B CD1 
14771 C CD2 . LEU B 748  ? 0.1861 0.2119 0.1866 0.0169  0.0007  -0.0310 746  LEU B CD2 
14772 N N   . ARG B 749  ? 0.1424 0.1526 0.1194 0.0238  0.0014  -0.0399 747  ARG B N   
14773 C CA  . ARG B 749  ? 0.1447 0.1527 0.1149 0.0240  0.0019  -0.0411 747  ARG B CA  
14774 C C   . ARG B 749  ? 0.1510 0.1518 0.1144 0.0216  -0.0016 -0.0416 747  ARG B C   
14775 O O   . ARG B 749  ? 0.1742 0.1746 0.1336 0.0196  -0.0023 -0.0409 747  ARG B O   
14776 C CB  . ARG B 749  ? 0.1730 0.1803 0.1409 0.0283  0.0043  -0.0439 747  ARG B CB  
14777 C CG  . ARG B 749  ? 0.1943 0.2097 0.1679 0.0299  0.0082  -0.0432 747  ARG B CG  
14778 C CD  . ARG B 749  ? 0.2287 0.2441 0.1993 0.0339  0.0109  -0.0459 747  ARG B CD  
14779 N NE  . ARG B 749  ? 0.1915 0.2153 0.1681 0.0353  0.0147  -0.0452 747  ARG B NE  
14780 C CZ  . ARG B 749  ? 0.2608 0.2867 0.2358 0.0386  0.0178  -0.0471 747  ARG B CZ  
14781 N NH1 . ARG B 749  ? 0.2577 0.2778 0.2252 0.0411  0.0175  -0.0499 747  ARG B NH1 
14782 N NH2 . ARG B 749  ? 0.2628 0.2969 0.2440 0.0393  0.0212  -0.0462 747  ARG B NH2 
14783 N N   . GLU B 750  ? 0.1586 0.1537 0.1207 0.0216  -0.0040 -0.0426 748  GLU B N   
14784 C CA  . GLU B 750  ? 0.1828 0.1709 0.1386 0.0188  -0.0075 -0.0430 748  GLU B CA  
14785 C C   . GLU B 750  ? 0.1618 0.1533 0.1200 0.0145  -0.0091 -0.0400 748  GLU B C   
14786 O O   . GLU B 750  ? 0.1887 0.1772 0.1418 0.0118  -0.0114 -0.0399 748  GLU B O   
14787 C CB  . GLU B 750  ? 0.1909 0.1726 0.1456 0.0193  -0.0098 -0.0440 748  GLU B CB  
14788 C CG  . GLU B 750  ? 0.2161 0.1898 0.1640 0.0162  -0.0135 -0.0445 748  GLU B CG  
14789 C CD  . GLU B 750  ? 0.2381 0.2040 0.1835 0.0170  -0.0155 -0.0458 748  GLU B CD  
14790 O OE1 . GLU B 750  ? 0.2655 0.2317 0.2136 0.0207  -0.0141 -0.0468 748  GLU B OE1 
14791 O OE2 . GLU B 750  ? 0.3351 0.2946 0.2759 0.0137  -0.0187 -0.0457 748  GLU B OE2 
14792 N N   . ALA B 751  ? 0.1591 0.1572 0.1251 0.0138  -0.0080 -0.0377 749  ALA B N   
14793 C CA  . ALA B 751  ? 0.1404 0.1426 0.1098 0.0103  -0.0092 -0.0348 749  ALA B CA  
14794 C C   . ALA B 751  ? 0.1543 0.1610 0.1233 0.0096  -0.0080 -0.0335 749  ALA B C   
14795 O O   . ALA B 751  ? 0.1885 0.1986 0.1599 0.0070  -0.0092 -0.0312 749  ALA B O   
14796 C CB  . ALA B 751  ? 0.1595 0.1664 0.1367 0.0103  -0.0083 -0.0331 749  ALA B CB  
14797 N N   . GLY B 752  ? 0.1521 0.1592 0.1185 0.0121  -0.0057 -0.0349 750  GLY B N   
14798 C CA  . GLY B 752  ? 0.1793 0.1899 0.1443 0.0114  -0.0047 -0.0336 750  GLY B CA  
14799 C C   . GLY B 752  ? 0.1614 0.1776 0.1303 0.0135  -0.0009 -0.0329 750  GLY B C   
14800 O O   . GLY B 752  ? 0.1874 0.2060 0.1545 0.0131  0.0002  -0.0318 750  GLY B O   
14801 N N   . ILE B 753  ? 0.1543 0.1727 0.1285 0.0155  0.0010  -0.0333 751  ILE B N   
14802 C CA  . ILE B 753  ? 0.1606 0.1844 0.1384 0.0171  0.0046  -0.0326 751  ILE B CA  
14803 C C   . ILE B 753  ? 0.1770 0.1995 0.1496 0.0195  0.0068  -0.0348 751  ILE B C   
14804 O O   . ILE B 753  ? 0.1952 0.2143 0.1655 0.0219  0.0068  -0.0374 751  ILE B O   
14805 C CB  . ILE B 753  ? 0.1274 0.1545 0.1126 0.0183  0.0058  -0.0324 751  ILE B CB  
14806 C CG1 . ILE B 753  ? 0.1440 0.1717 0.1336 0.0161  0.0037  -0.0305 751  ILE B CG1 
14807 C CG2 . ILE B 753  ? 0.1572 0.1900 0.1461 0.0193  0.0093  -0.0315 751  ILE B CG2 
14808 C CD1 . ILE B 753  ? 0.1664 0.1979 0.1584 0.0139  0.0037  -0.0276 751  ILE B CD1 
14809 N N   . PRO B 754  ? 0.1854 0.2104 0.1557 0.0193  0.0086  -0.0339 752  PRO B N   
14810 C CA  . PRO B 754  ? 0.2225 0.2465 0.1873 0.0216  0.0110  -0.0359 752  PRO B CA  
14811 C C   . PRO B 754  ? 0.2127 0.2399 0.1816 0.0247  0.0142  -0.0374 752  PRO B C   
14812 O O   . PRO B 754  ? 0.1824 0.2146 0.1589 0.0246  0.0155  -0.0361 752  PRO B O   
14813 C CB  . PRO B 754  ? 0.2351 0.2621 0.1978 0.0202  0.0125  -0.0338 752  PRO B CB  
14814 C CG  . PRO B 754  ? 0.2466 0.2744 0.2119 0.0171  0.0098  -0.0310 752  PRO B CG  
14815 C CD  . PRO B 754  ? 0.1768 0.2053 0.1488 0.0169  0.0085  -0.0308 752  PRO B CD  
14816 N N   . ALA B 755  ? 0.2277 0.2524 0.1915 0.0276  0.0155  -0.0403 753  ALA B N   
14817 C CA  . ALA B 755  ? 0.2073 0.2356 0.1750 0.0309  0.0186  -0.0419 753  ALA B CA  
14818 C C   . ALA B 755  ? 0.2025 0.2388 0.1757 0.0305  0.0223  -0.0398 753  ALA B C   
14819 O O   . ALA B 755  ? 0.2157 0.2568 0.1960 0.0316  0.0239  -0.0397 753  ALA B O   
14820 C CB  . ALA B 755  ? 0.2759 0.3004 0.2364 0.0343  0.0198  -0.0453 753  ALA B CB  
14821 N N   . SER B 756  ? 0.1907 0.2283 0.1607 0.0286  0.0234  -0.0380 754  SER B N   
14822 C CA  . SER B 756  ? 0.2019 0.2462 0.1764 0.0277  0.0268  -0.0359 754  SER B CA  
14823 C C   . SER B 756  ? 0.1888 0.2363 0.1711 0.0253  0.0257  -0.0331 754  SER B C   
14824 O O   . SER B 756  ? 0.1892 0.2422 0.1768 0.0247  0.0283  -0.0316 754  SER B O   
14825 C CB  . SER B 756  ? 0.2388 0.2829 0.2070 0.0263  0.0280  -0.0345 754  SER B CB  
14826 O OG  . SER B 756  ? 0.2669 0.3073 0.2323 0.0237  0.0246  -0.0328 754  SER B OG  
14827 N N   . ALA B 757  ? 0.1530 0.1968 0.1358 0.0237  0.0220  -0.0325 755  ALA B N   
14828 C CA  . ALA B 757  ? 0.1371 0.1834 0.1267 0.0218  0.0209  -0.0302 755  ALA B CA  
14829 C C   . ALA B 757  ? 0.1273 0.1747 0.1231 0.0231  0.0204  -0.0313 755  ALA B C   
14830 O O   . ALA B 757  ? 0.1469 0.1970 0.1487 0.0218  0.0201  -0.0296 755  ALA B O   
14831 C CB  . ALA B 757  ? 0.1499 0.1926 0.1373 0.0193  0.0174  -0.0286 755  ALA B CB  
14832 N N   . LEU B 758  ? 0.1236 0.1688 0.1177 0.0258  0.0202  -0.0342 756  LEU B N   
14833 C CA  . LEU B 758  ? 0.1367 0.1826 0.1363 0.0273  0.0193  -0.0352 756  LEU B CA  
14834 C C   . LEU B 758  ? 0.1547 0.2013 0.1534 0.0311  0.0212  -0.0381 756  LEU B C   
14835 O O   . LEU B 758  ? 0.1445 0.1857 0.1374 0.0329  0.0200  -0.0403 756  LEU B O   
14836 C CB  . LEU B 758  ? 0.1374 0.1778 0.1357 0.0263  0.0155  -0.0354 756  LEU B CB  
14837 C CG  . LEU B 758  ? 0.1256 0.1659 0.1286 0.0279  0.0143  -0.0364 756  LEU B CG  
14838 C CD1 . LEU B 758  ? 0.1522 0.1987 0.1633 0.0272  0.0156  -0.0348 756  LEU B CD1 
14839 C CD2 . LEU B 758  ? 0.1598 0.1945 0.1608 0.0264  0.0106  -0.0362 756  LEU B CD2 
14840 N N   . GLN B 759  ? 0.1448 0.1979 0.1493 0.0322  0.0240  -0.0380 757  GLN B N   
14841 C CA  . GLN B 759  ? 0.1260 0.1815 0.1313 0.0361  0.0261  -0.0406 757  GLN B CA  
14842 C C   . GLN B 759  ? 0.1268 0.1850 0.1393 0.0375  0.0251  -0.0411 757  GLN B C   
14843 O O   . GLN B 759  ? 0.1499 0.2115 0.1685 0.0353  0.0247  -0.0391 757  GLN B O   
14844 C CB  . GLN B 759  ? 0.1410 0.2031 0.1474 0.0363  0.0304  -0.0401 757  GLN B CB  
14845 C CG  . GLN B 759  ? 0.1602 0.2193 0.1584 0.0353  0.0314  -0.0398 757  GLN B CG  
14846 C CD  . GLN B 759  ? 0.1340 0.1995 0.1331 0.0350  0.0357  -0.0388 757  GLN B CD  
14847 O OE1 . GLN B 759  ? 0.1680 0.2356 0.1648 0.0378  0.0386  -0.0408 757  GLN B OE1 
14848 N NE2 . GLN B 759  ? 0.1557 0.2243 0.1579 0.0315  0.0364  -0.0357 757  GLN B NE2 
14849 N N   . LEU B 760  ? 0.1372 0.1932 0.1486 0.0413  0.0245  -0.0438 758  LEU B N   
14850 C CA  . LEU B 760  ? 0.1397 0.1979 0.1573 0.0433  0.0234  -0.0445 758  LEU B CA  
14851 C C   . LEU B 760  ? 0.1454 0.2113 0.1678 0.0465  0.0267  -0.0459 758  LEU B C   
14852 O O   . LEU B 760  ? 0.1395 0.2051 0.1579 0.0497  0.0286  -0.0480 758  LEU B O   
14853 C CB  . LEU B 760  ? 0.1573 0.2074 0.1705 0.0455  0.0200  -0.0465 758  LEU B CB  
14854 C CG  . LEU B 760  ? 0.1414 0.1929 0.1603 0.0476  0.0184  -0.0471 758  LEU B CG  
14855 C CD1 . LEU B 760  ? 0.1684 0.2196 0.1911 0.0440  0.0160  -0.0447 758  LEU B CD1 
14856 C CD2 . LEU B 760  ? 0.1832 0.2273 0.1971 0.0514  0.0162  -0.0497 758  LEU B CD2 
14857 N N   . LEU B 761  ? 0.1221 0.1950 0.1529 0.0459  0.0272  -0.0448 759  LEU B N   
14858 C CA  . LEU B 761  ? 0.1280 0.2098 0.1648 0.0484  0.0303  -0.0458 759  LEU B CA  
14859 C C   . LEU B 761  ? 0.1281 0.2121 0.1713 0.0505  0.0282  -0.0465 759  LEU B C   
14860 O O   . LEU B 761  ? 0.1463 0.2352 0.1963 0.0482  0.0278  -0.0449 759  LEU B O   
14861 C CB  . LEU B 761  ? 0.1547 0.2442 0.1962 0.0450  0.0334  -0.0434 759  LEU B CB  
14862 C CG  . LEU B 761  ? 0.1527 0.2417 0.1888 0.0428  0.0360  -0.0422 759  LEU B CG  
14863 C CD1 . LEU B 761  ? 0.1659 0.2519 0.1947 0.0463  0.0376  -0.0447 759  LEU B CD1 
14864 C CD2 . LEU B 761  ? 0.1812 0.2640 0.2136 0.0388  0.0336  -0.0400 759  LEU B CD2 
14865 N N   . PRO B 762  ? 0.1346 0.2145 0.1753 0.0549  0.0266  -0.0490 760  PRO B N   
14866 C CA  . PRO B 762  ? 0.1575 0.2395 0.2040 0.0572  0.0244  -0.0497 760  PRO B CA  
14867 C C   . PRO B 762  ? 0.1577 0.2512 0.2127 0.0589  0.0273  -0.0500 760  PRO B C   
14868 O O   . PRO B 762  ? 0.1597 0.2578 0.2145 0.0597  0.0309  -0.0503 760  PRO B O   
14869 C CB  . PRO B 762  ? 0.1345 0.2087 0.1750 0.0619  0.0225  -0.0524 760  PRO B CB  
14870 C CG  . PRO B 762  ? 0.1489 0.2154 0.1799 0.0608  0.0227  -0.0528 760  PRO B CG  
14871 C CD  . PRO B 762  ? 0.1491 0.2214 0.1810 0.0579  0.0264  -0.0513 760  PRO B CD  
14872 N N   . GLY B 763  ? 0.1386 0.2359 0.2006 0.0586  0.0254  -0.0493 761  GLY B N   
14873 C CA  . GLY B 763  ? 0.1675 0.2731 0.2366 0.0590  0.0269  -0.0484 761  GLY B CA  
14874 C C   . GLY B 763  ? 0.1402 0.2505 0.2167 0.0558  0.0252  -0.0465 761  GLY B C   
14875 O O   . GLY B 763  ? 0.1814 0.2878 0.2575 0.0541  0.0225  -0.0461 761  GLY B O   
14876 N N   . ASP B 764  ? 0.2210 0.3399 0.3045 0.0551  0.0270  -0.0454 762  ASP B N   
14877 C CA  . ASP B 764  ? 0.2287 0.3524 0.3194 0.0524  0.0252  -0.0438 762  ASP B CA  
14878 C C   . ASP B 764  ? 0.2862 0.4137 0.3795 0.0471  0.0270  -0.0418 762  ASP B C   
14879 O O   . ASP B 764  ? 0.2008 0.3264 0.2899 0.0454  0.0291  -0.0415 762  ASP B O   
14880 C CB  . ASP B 764  ? 0.2563 0.3869 0.3531 0.0546  0.0255  -0.0438 762  ASP B CB  
14881 C CG  . ASP B 764  ? 0.2911 0.4292 0.3905 0.0542  0.0301  -0.0432 762  ASP B CG  
14882 O OD1 . ASP B 764  ? 0.2734 0.4127 0.3713 0.0511  0.0329  -0.0422 762  ASP B OD1 
14883 O OD2 . ASP B 764  ? 0.3663 0.5092 0.4693 0.0571  0.0308  -0.0438 762  ASP B OD2 
14884 N N   . GLY B 765  ? 0.2231 0.3561 0.3234 0.0443  0.0262  -0.0403 763  GLY B N   
14885 C CA  . GLY B 765  ? 0.2167 0.3527 0.3195 0.0391  0.0275  -0.0383 763  GLY B CA  
14886 C C   . GLY B 765  ? 0.1990 0.3407 0.3027 0.0373  0.0320  -0.0372 763  GLY B C   
14887 O O   . GLY B 765  ? 0.2309 0.3733 0.3345 0.0332  0.0335  -0.0357 763  GLY B O   
14888 N N   . ARG B 766  ? 0.2133 0.3590 0.3179 0.0402  0.0342  -0.0379 764  ARG B N   
14889 C CA  . ARG B 766  ? 0.2205 0.3710 0.3250 0.0387  0.0388  -0.0369 764  ARG B CA  
14890 C C   . ARG B 766  ? 0.1795 0.3244 0.2758 0.0389  0.0405  -0.0374 764  ARG B C   
14891 O O   . ARG B 766  ? 0.2102 0.3573 0.3054 0.0359  0.0437  -0.0360 764  ARG B O   
14892 C CB  . ARG B 766  ? 0.2905 0.4465 0.3977 0.0422  0.0408  -0.0377 764  ARG B CB  
14893 C CG  . ARG B 766  ? 0.3141 0.4759 0.4294 0.0426  0.0387  -0.0374 764  ARG B CG  
14894 C CD  . ARG B 766  ? 0.4403 0.6081 0.5586 0.0463  0.0409  -0.0382 764  ARG B CD  
14895 N NE  . ARG B 766  ? 0.5918 0.7672 0.7135 0.0435  0.0453  -0.0366 764  ARG B NE  
14896 C CZ  . ARG B 766  ? 0.6257 0.8099 0.7557 0.0412  0.0460  -0.0351 764  ARG B CZ  
14897 N NH1 . ARG B 766  ? 0.6347 0.8214 0.7705 0.0413  0.0425  -0.0350 764  ARG B NH1 
14898 N NH2 . ARG B 766  ? 0.6467 0.8373 0.7791 0.0386  0.0501  -0.0336 764  ARG B NH2 
14899 N N   . VAL B 767  ? 0.1879 0.3253 0.2781 0.0424  0.0385  -0.0394 765  VAL B N   
14900 C CA  . VAL B 767  ? 0.1788 0.3103 0.2611 0.0423  0.0395  -0.0400 765  VAL B CA  
14901 C C   . VAL B 767  ? 0.1531 0.2829 0.2353 0.0377  0.0386  -0.0383 765  VAL B C   
14902 O O   . VAL B 767  ? 0.1770 0.3052 0.2551 0.0349  0.0407  -0.0367 765  VAL B O   
14903 C CB  . VAL B 767  ? 0.1494 0.2729 0.2256 0.0466  0.0370  -0.0425 765  VAL B CB  
14904 C CG1 . VAL B 767  ? 0.1605 0.2777 0.2281 0.0462  0.0377  -0.0430 765  VAL B CG1 
14905 C CG2 . VAL B 767  ? 0.1821 0.3067 0.2581 0.0513  0.0378  -0.0442 765  VAL B CG2 
14906 N N   . GLY B 768  ? 0.1564 0.2837 0.2414 0.0364  0.0350  -0.0378 766  GLY B N   
14907 C CA  . GLY B 768  ? 0.1776 0.3007 0.2615 0.0316  0.0336  -0.0353 766  GLY B CA  
14908 C C   . GLY B 768  ? 0.1601 0.2893 0.2478 0.0274  0.0366  -0.0331 766  GLY B C   
14909 O O   . GLY B 768  ? 0.1520 0.2774 0.2357 0.0241  0.0373  -0.0311 766  GLY B O   
14910 N N   . ALA B 769  ? 0.1908 0.3298 0.2863 0.0274  0.0383  -0.0333 767  ALA B N   
14911 C CA  . ALA B 769  ? 0.1634 0.3082 0.2627 0.0230  0.0410  -0.0311 767  ALA B CA  
14912 C C   . ALA B 769  ? 0.1793 0.3248 0.2738 0.0224  0.0451  -0.0303 767  ALA B C   
14913 O O   . ALA B 769  ? 0.1914 0.3359 0.2843 0.0182  0.0466  -0.0278 767  ALA B O   
14914 C CB  . ALA B 769  ? 0.1940 0.3467 0.3013 0.0227  0.0412  -0.0307 767  ALA B CB  
14915 N N   . ALA B 770  ? 0.1641 0.3099 0.2552 0.0266  0.0468  -0.0321 768  ALA B N   
14916 C CA  . ALA B 770  ? 0.1605 0.3067 0.2462 0.0264  0.0507  -0.0317 768  ALA B CA  
14917 C C   . ALA B 770  ? 0.1727 0.3091 0.2498 0.0245  0.0494  -0.0303 768  ALA B C   
14918 O O   . ALA B 770  ? 0.1912 0.3271 0.2646 0.0218  0.0520  -0.0284 768  ALA B O   
14919 C CB  . ALA B 770  ? 0.1991 0.3450 0.2816 0.0315  0.0520  -0.0338 768  ALA B CB  
14920 N N   . LEU B 771  ? 0.1578 0.2861 0.2315 0.0258  0.0455  -0.0312 769  LEU B N   
14921 C CA  . LEU B 771  ? 0.1683 0.2878 0.2347 0.0238  0.0440  -0.0297 769  LEU B CA  
14922 C C   . LEU B 771  ? 0.1604 0.2793 0.2288 0.0188  0.0436  -0.0267 769  LEU B C   
14923 O O   . LEU B 771  ? 0.1724 0.2880 0.2359 0.0164  0.0446  -0.0247 769  LEU B O   
14924 C CB  . LEU B 771  ? 0.1329 0.2446 0.1958 0.0261  0.0399  -0.0312 769  LEU B CB  
14925 C CG  . LEU B 771  ? 0.1394 0.2489 0.1982 0.0308  0.0397  -0.0341 769  LEU B CG  
14926 C CD1 . LEU B 771  ? 0.1579 0.2605 0.2149 0.0326  0.0355  -0.0354 769  LEU B CD1 
14927 C CD2 . LEU B 771  ? 0.1573 0.2635 0.2079 0.0312  0.0418  -0.0342 769  LEU B CD2 
14928 N N   . VAL B 772  ? 0.1348 0.2564 0.2100 0.0174  0.0418  -0.0263 770  VAL B N   
14929 C CA  . VAL B 772  ? 0.1429 0.2630 0.2198 0.0129  0.0411  -0.0237 770  VAL B CA  
14930 C C   . VAL B 772  ? 0.1840 0.3087 0.2616 0.0096  0.0449  -0.0216 770  VAL B C   
14931 O O   . VAL B 772  ? 0.1984 0.3190 0.2728 0.0063  0.0450  -0.0191 770  VAL B O   
14932 C CB  . VAL B 772  ? 0.1411 0.2636 0.2250 0.0122  0.0385  -0.0242 770  VAL B CB  
14933 C CG1 . VAL B 772  ? 0.1505 0.2728 0.2369 0.0073  0.0384  -0.0216 770  VAL B CG1 
14934 C CG2 . VAL B 772  ? 0.1187 0.2347 0.2003 0.0145  0.0346  -0.0255 770  VAL B CG2 
14935 N N   . ALA B 773  ? 0.1724 0.3058 0.2541 0.0106  0.0481  -0.0224 771  ALA B N   
14936 C CA  . ALA B 773  ? 0.1731 0.3119 0.2562 0.0072  0.0520  -0.0203 771  ALA B CA  
14937 C C   . ALA B 773  ? 0.2292 0.3652 0.3044 0.0073  0.0548  -0.0194 771  ALA B C   
14938 O O   . ALA B 773  ? 0.2307 0.3693 0.3055 0.0039  0.0578  -0.0171 771  ALA B O   
14939 C CB  . ALA B 773  ? 0.1764 0.3265 0.2675 0.0082  0.0544  -0.0215 771  ALA B CB  
14940 N N   . ALA B 774  ? 0.1710 0.3017 0.2397 0.0109  0.0538  -0.0211 772  ALA B N   
14941 C CA  . ALA B 774  ? 0.1839 0.3120 0.2446 0.0113  0.0563  -0.0205 772  ALA B CA  
14942 C C   . ALA B 774  ? 0.1929 0.3155 0.2489 0.0072  0.0561  -0.0172 772  ALA B C   
14943 O O   . ALA B 774  ? 0.2363 0.3533 0.2922 0.0056  0.0529  -0.0161 772  ALA B O   
14944 C CB  . ALA B 774  ? 0.2222 0.3444 0.2766 0.0156  0.0544  -0.0230 772  ALA B CB  
14945 N N   . ALA B 775  ? 0.2647 0.3889 0.3165 0.0059  0.0598  -0.0157 773  ALA B N   
14946 C CA  . ALA B 775  ? 0.2164 0.3363 0.2642 0.0018  0.0601  -0.0122 773  ALA B CA  
14947 C C   . ALA B 775  ? 0.2092 0.3194 0.2503 0.0022  0.0565  -0.0116 773  ALA B C   
14948 O O   . ALA B 775  ? 0.2695 0.3752 0.3098 -0.0008 0.0550  -0.0090 773  ALA B O   
14949 C CB  . ALA B 775  ? 0.3452 0.4683 0.3886 0.0007  0.0647  -0.0108 773  ALA B CB  
14950 N N   . GLU B 776  ? 0.2119 0.3186 0.2484 0.0058  0.0550  -0.0138 774  GLU B N   
14951 C CA  . GLU B 776  ? 0.1911 0.2894 0.2212 0.0061  0.0518  -0.0132 774  GLU B CA  
14952 C C   . GLU B 776  ? 0.1845 0.2793 0.2179 0.0067  0.0475  -0.0141 774  GLU B C   
14953 O O   . GLU B 776  ? 0.1920 0.2804 0.2210 0.0068  0.0447  -0.0134 774  GLU B O   
14954 C CB  . GLU B 776  ? 0.2177 0.3136 0.2404 0.0091  0.0521  -0.0151 774  GLU B CB  
14955 C CG  . GLU B 776  ? 0.2742 0.3730 0.2922 0.0088  0.0563  -0.0144 774  GLU B CG  
14956 C CD  . GLU B 776  ? 0.3299 0.4363 0.3515 0.0112  0.0598  -0.0168 774  GLU B CD  
14957 O OE1 . GLU B 776  ? 0.2821 0.3920 0.3107 0.0128  0.0588  -0.0188 774  GLU B OE1 
14958 O OE2 . GLU B 776  ? 0.3690 0.4782 0.3866 0.0115  0.0635  -0.0167 774  GLU B OE2 
14959 N N   . THR B 777  ? 0.1713 0.2700 0.2121 0.0072  0.0470  -0.0154 775  THR B N   
14960 C CA  . THR B 777  ? 0.1445 0.2398 0.1881 0.0078  0.0430  -0.0162 775  THR B CA  
14961 C C   . THR B 777  ? 0.1622 0.2534 0.2057 0.0046  0.0414  -0.0134 775  THR B C   
14962 O O   . THR B 777  ? 0.1788 0.2722 0.2250 0.0016  0.0430  -0.0115 775  THR B O   
14963 C CB  . THR B 777  ? 0.1528 0.2537 0.2042 0.0088  0.0429  -0.0180 775  THR B CB  
14964 O OG1 . THR B 777  ? 0.1920 0.2954 0.2427 0.0125  0.0438  -0.0208 775  THR B OG1 
14965 C CG2 . THR B 777  ? 0.1464 0.2438 0.2006 0.0088  0.0390  -0.0184 775  THR B CG2 
14966 N N   . ALA B 778  ? 0.1287 0.2137 0.1690 0.0053  0.0382  -0.0133 776  ALA B N   
14967 C CA  . ALA B 778  ? 0.1459 0.2263 0.1849 0.0031  0.0366  -0.0108 776  ALA B CA  
14968 C C   . ALA B 778  ? 0.1417 0.2200 0.1846 0.0032  0.0335  -0.0114 776  ALA B C   
14969 O O   . ALA B 778  ? 0.1481 0.2225 0.1904 0.0018  0.0320  -0.0096 776  ALA B O   
14970 C CB  . ALA B 778  ? 0.1494 0.2247 0.1810 0.0037  0.0356  -0.0098 776  ALA B CB  
14971 N N   . GLY B 779  ? 0.1299 0.2105 0.1765 0.0051  0.0325  -0.0139 777  GLY B N   
14972 C CA  . GLY B 779  ? 0.1373 0.2161 0.1873 0.0053  0.0297  -0.0145 777  GLY B CA  
14973 C C   . GLY B 779  ? 0.1262 0.2081 0.1796 0.0077  0.0290  -0.0172 777  GLY B C   
14974 O O   . GLY B 779  ? 0.1231 0.2067 0.1748 0.0098  0.0301  -0.0188 777  GLY B O   
14975 N N   . VAL B 780  ? 0.0952 0.1773 0.1530 0.0075  0.0271  -0.0178 778  VAL B N   
14976 C CA  . VAL B 780  ? 0.1033 0.1880 0.1647 0.0097  0.0261  -0.0202 778  VAL B CA  
14977 C C   . VAL B 780  ? 0.1130 0.1936 0.1746 0.0102  0.0228  -0.0206 778  VAL B C   
14978 O O   . VAL B 780  ? 0.1158 0.1943 0.1784 0.0082  0.0218  -0.0193 778  VAL B O   
14979 C CB  . VAL B 780  ? 0.1097 0.2011 0.1776 0.0089  0.0275  -0.0207 778  VAL B CB  
14980 C CG1 . VAL B 780  ? 0.1224 0.2161 0.1935 0.0117  0.0261  -0.0231 778  VAL B CG1 
14981 C CG2 . VAL B 780  ? 0.1048 0.2010 0.1726 0.0084  0.0312  -0.0201 778  VAL B CG2 
14982 N N   . MET B 781  ? 0.1047 0.1836 0.1648 0.0127  0.0212  -0.0224 779  MET B N   
14983 C CA  . MET B 781  ? 0.1133 0.1888 0.1736 0.0134  0.0182  -0.0230 779  MET B CA  
14984 C C   . MET B 781  ? 0.1072 0.1856 0.1711 0.0154  0.0175  -0.0251 779  MET B C   
14985 O O   . MET B 781  ? 0.1183 0.1979 0.1812 0.0178  0.0181  -0.0266 779  MET B O   
14986 C CB  . MET B 781  ? 0.1104 0.1807 0.1652 0.0143  0.0168  -0.0231 779  MET B CB  
14987 C CG  . MET B 781  ? 0.1276 0.1957 0.1788 0.0126  0.0175  -0.0211 779  MET B CG  
14988 S SD  . MET B 781  ? 0.1361 0.1994 0.1814 0.0135  0.0157  -0.0212 779  MET B SD  
14989 C CE  . MET B 781  ? 0.1278 0.1882 0.1743 0.0130  0.0131  -0.0208 779  MET B CE  
14990 N N   . PHE B 782  ? 0.1177 0.1975 0.1859 0.0146  0.0162  -0.0251 780  PHE B N   
14991 C CA  . PHE B 782  ? 0.0924 0.1760 0.1650 0.0164  0.0154  -0.0268 780  PHE B CA  
14992 C C   . PHE B 782  ? 0.1145 0.1949 0.1875 0.0167  0.0123  -0.0273 780  PHE B C   
14993 O O   . PHE B 782  ? 0.1482 0.2266 0.2215 0.0145  0.0114  -0.0261 780  PHE B O   
14994 C CB  . PHE B 782  ? 0.1137 0.2039 0.1922 0.0148  0.0171  -0.0265 780  PHE B CB  
14995 C CG  . PHE B 782  ? 0.1272 0.2219 0.2110 0.0164  0.0158  -0.0281 780  PHE B CG  
14996 C CD1 . PHE B 782  ? 0.1342 0.2328 0.2194 0.0195  0.0166  -0.0298 780  PHE B CD1 
14997 C CD2 . PHE B 782  ? 0.1538 0.2488 0.2410 0.0149  0.0137  -0.0279 780  PHE B CD2 
14998 C CE1 . PHE B 782  ? 0.1740 0.2771 0.2643 0.0213  0.0153  -0.0312 780  PHE B CE1 
14999 C CE2 . PHE B 782  ? 0.1510 0.2504 0.2431 0.0164  0.0122  -0.0293 780  PHE B CE2 
15000 C CZ  . PHE B 782  ? 0.1657 0.2693 0.2595 0.0197  0.0130  -0.0309 780  PHE B CZ  
15001 N N   . THR B 783  ? 0.1077 0.1873 0.1803 0.0194  0.0106  -0.0289 781  THR B N   
15002 C CA  . THR B 783  ? 0.1238 0.2011 0.1971 0.0199  0.0077  -0.0294 781  THR B CA  
15003 C C   . THR B 783  ? 0.1465 0.2283 0.2242 0.0222  0.0070  -0.0310 781  THR B C   
15004 O O   . THR B 783  ? 0.1601 0.2427 0.2370 0.0250  0.0074  -0.0323 781  THR B O   
15005 C CB  . THR B 783  ? 0.1265 0.1971 0.1942 0.0210  0.0060  -0.0295 781  THR B CB  
15006 O OG1 . THR B 783  ? 0.1524 0.2200 0.2167 0.0189  0.0067  -0.0280 781  THR B OG1 
15007 C CG2 . THR B 783  ? 0.1661 0.2342 0.2340 0.0213  0.0031  -0.0298 781  THR B CG2 
15008 N N   . GLY B 784  ? 0.1197 0.2046 0.2020 0.0210  0.0059  -0.0310 782  GLY B N   
15009 C CA  . GLY B 784  ? 0.1510 0.2416 0.2386 0.0230  0.0051  -0.0323 782  GLY B CA  
15010 C C   . GLY B 784  ? 0.1419 0.2363 0.2347 0.0206  0.0041  -0.0319 782  GLY B C   
15011 O O   . GLY B 784  ? 0.1560 0.2467 0.2472 0.0182  0.0030  -0.0310 782  GLY B O   
15012 N N   . SER B 785  ? 0.1682 0.2701 0.2671 0.0214  0.0045  -0.0327 783  SER B N   
15013 C CA  . SER B 785  ? 0.1807 0.2867 0.2850 0.0192  0.0030  -0.0326 783  SER B CA  
15014 C C   . SER B 785  ? 0.2090 0.3164 0.3148 0.0148  0.0048  -0.0310 783  SER B C   
15015 O O   . SER B 785  ? 0.1682 0.2766 0.2731 0.0137  0.0079  -0.0301 783  SER B O   
15016 C CB  . SER B 785  ? 0.1824 0.2969 0.2933 0.0214  0.0027  -0.0339 783  SER B CB  
15017 O OG  . SER B 785  ? 0.1977 0.3189 0.3121 0.0209  0.0062  -0.0337 783  SER B OG  
15018 N N   . THR B 786  ? 0.1782 0.2854 0.2862 0.0121  0.0028  -0.0307 784  THR B N   
15019 C CA  A THR B 786  ? 0.1780 0.2860 0.2875 0.0078  0.0043  -0.0292 784  THR B CA  
15020 C CA  B THR B 786  ? 0.1783 0.2863 0.2878 0.0078  0.0043  -0.0292 784  THR B CA  
15021 C C   . THR B 786  ? 0.1694 0.2864 0.2850 0.0066  0.0068  -0.0290 784  THR B C   
15022 O O   . THR B 786  ? 0.1963 0.3139 0.3117 0.0037  0.0095  -0.0275 784  THR B O   
15023 C CB  A THR B 786  ? 0.1997 0.3056 0.3102 0.0053  0.0013  -0.0292 784  THR B CB  
15024 C CB  B THR B 786  ? 0.1997 0.3054 0.3100 0.0054  0.0013  -0.0292 784  THR B CB  
15025 O OG1 A THR B 786  ? 0.2702 0.3829 0.3869 0.0059  -0.0006 -0.0304 784  THR B OG1 
15026 O OG1 B THR B 786  ? 0.1848 0.2931 0.2983 0.0011  0.0025  -0.0281 784  THR B OG1 
15027 C CG2 A THR B 786  ? 0.1661 0.2636 0.2705 0.0065  -0.0010 -0.0295 784  THR B CG2 
15028 C CG2 B THR B 786  ? 0.2457 0.3555 0.3601 0.0073  -0.0017 -0.0308 784  THR B CG2 
15029 N N   . GLU B 787  ? 0.1612 0.2857 0.2824 0.0087  0.0062  -0.0303 785  GLU B N   
15030 C CA  . GLU B 787  ? 0.1853 0.3195 0.3130 0.0077  0.0088  -0.0301 785  GLU B CA  
15031 C C   . GLU B 787  ? 0.1646 0.2994 0.2897 0.0087  0.0128  -0.0296 785  GLU B C   
15032 O O   . GLU B 787  ? 0.1950 0.3334 0.3219 0.0056  0.0157  -0.0282 785  GLU B O   
15033 C CB  . GLU B 787  ? 0.2082 0.3504 0.3423 0.0107  0.0072  -0.0318 785  GLU B CB  
15034 N N   . VAL B 788  ? 0.1833 0.3139 0.3035 0.0127  0.0129  -0.0305 786  VAL B N   
15035 C CA  . VAL B 788  ? 0.1664 0.2972 0.2835 0.0138  0.0164  -0.0302 786  VAL B CA  
15036 C C   . VAL B 788  ? 0.1325 0.2570 0.2442 0.0105  0.0177  -0.0283 786  VAL B C   
15037 O O   . VAL B 788  ? 0.1653 0.2920 0.2765 0.0089  0.0210  -0.0271 786  VAL B O   
15038 C CB  . VAL B 788  ? 0.1725 0.3000 0.2854 0.0188  0.0158  -0.0319 786  VAL B CB  
15039 C CG1 . VAL B 788  ? 0.1484 0.2745 0.2566 0.0197  0.0192  -0.0316 786  VAL B CG1 
15040 C CG2 . VAL B 788  ? 0.2458 0.3805 0.3643 0.0225  0.0150  -0.0338 786  VAL B CG2 
15041 N N   . ALA B 789  ? 0.1466 0.2633 0.2543 0.0095  0.0153  -0.0278 787  ALA B N   
15042 C CA  . ALA B 789  ? 0.1506 0.2614 0.2535 0.0067  0.0163  -0.0259 787  ALA B CA  
15043 C C   . ALA B 789  ? 0.1350 0.2493 0.2412 0.0023  0.0181  -0.0243 787  ALA B C   
15044 O O   . ALA B 789  ? 0.1392 0.2519 0.2425 0.0005  0.0205  -0.0226 787  ALA B O   
15045 C CB  . ALA B 789  ? 0.1353 0.2382 0.2343 0.0064  0.0133  -0.0258 787  ALA B CB  
15046 N N   . ARG B 790  ? 0.1560 0.2750 0.2682 0.0005  0.0167  -0.0246 788  ARG B N   
15047 C CA  . ARG B 790  ? 0.1499 0.2725 0.2656 -0.0041 0.0183  -0.0230 788  ARG B CA  
15048 C C   . ARG B 790  ? 0.1622 0.2922 0.2805 -0.0043 0.0222  -0.0225 788  ARG B C   
15049 O O   . ARG B 790  ? 0.1729 0.3028 0.2903 -0.0078 0.0246  -0.0205 788  ARG B O   
15050 C CB  . ARG B 790  ? 0.2135 0.3404 0.3355 -0.0060 0.0157  -0.0237 788  ARG B CB  
15051 C CG  . ARG B 790  ? 0.3169 0.4451 0.4416 -0.0115 0.0163  -0.0221 788  ARG B CG  
15052 C CD  . ARG B 790  ? 0.2997 0.4302 0.4293 -0.0133 0.0129  -0.0230 788  ARG B CD  
15053 N NE  . ARG B 790  ? 0.3053 0.4284 0.4309 -0.0112 0.0094  -0.0241 788  ARG B NE  
15054 C CZ  . ARG B 790  ? 0.3921 0.5061 0.5123 -0.0129 0.0080  -0.0234 788  ARG B CZ  
15055 N NH1 . ARG B 790  ? 0.3558 0.4663 0.4739 -0.0166 0.0096  -0.0216 788  ARG B NH1 
15056 N NH2 . ARG B 790  ? 0.4093 0.5175 0.5259 -0.0107 0.0051  -0.0245 788  ARG B NH2 
15057 N N   . LEU B 791  ? 0.1496 0.2859 0.2708 -0.0006 0.0230  -0.0241 789  LEU B N   
15058 C CA  . LEU B 791  ? 0.1448 0.2881 0.2680 -0.0004 0.0271  -0.0238 789  LEU B CA  
15059 C C   . LEU B 791  ? 0.1434 0.2811 0.2592 -0.0001 0.0295  -0.0226 789  LEU B C   
15060 O O   . LEU B 791  ? 0.1608 0.3013 0.2764 -0.0024 0.0329  -0.0211 789  LEU B O   
15061 C CB  . LEU B 791  ? 0.1700 0.3203 0.2971 0.0043  0.0272  -0.0260 789  LEU B CB  
15062 C CG  . LEU B 791  ? 0.2139 0.3717 0.3493 0.0043  0.0251  -0.0271 789  LEU B CG  
15063 C CD1 . LEU B 791  ? 0.2373 0.3978 0.3732 0.0097  0.0248  -0.0284 789  LEU B CD1 
15064 C CD2 . LEU B 791  ? 0.2445 0.4094 0.3856 -0.0005 0.0268  -0.0253 789  LEU B CD2 
15065 N N   . ILE B 792  ? 0.1429 0.2727 0.2524 0.0026  0.0278  -0.0233 790  ILE B N   
15066 C CA  . ILE B 792  ? 0.1372 0.2613 0.2395 0.0029  0.0296  -0.0222 790  ILE B CA  
15067 C C   . ILE B 792  ? 0.1515 0.2714 0.2513 -0.0016 0.0302  -0.0196 790  ILE B C   
15068 O O   . ILE B 792  ? 0.1635 0.2832 0.2603 -0.0030 0.0330  -0.0181 790  ILE B O   
15069 C CB  . ILE B 792  ? 0.1173 0.2339 0.2140 0.0062  0.0271  -0.0234 790  ILE B CB  
15070 C CG1 . ILE B 792  ? 0.1185 0.2385 0.2164 0.0107  0.0269  -0.0258 790  ILE B CG1 
15071 C CG2 . ILE B 792  ? 0.1242 0.2343 0.2136 0.0058  0.0281  -0.0220 790  ILE B CG2 
15072 C CD1 . ILE B 792  ? 0.1552 0.2681 0.2481 0.0138  0.0243  -0.0270 790  ILE B CD1 
15073 N N   . GLN B 793  ? 0.1489 0.2648 0.2496 -0.0037 0.0275  -0.0192 791  GLN B N   
15074 C CA  . GLN B 793  ? 0.1349 0.2460 0.2332 -0.0077 0.0277  -0.0168 791  GLN B CA  
15075 C C   . GLN B 793  ? 0.1451 0.2620 0.2468 -0.0115 0.0307  -0.0152 791  GLN B C   
15076 O O   . GLN B 793  ? 0.1574 0.2710 0.2551 -0.0138 0.0326  -0.0130 791  GLN B O   
15077 C CB  . GLN B 793  ? 0.1718 0.2788 0.2712 -0.0091 0.0243  -0.0171 791  GLN B CB  
15078 C CG  . GLN B 793  ? 0.2165 0.3168 0.3127 -0.0126 0.0239  -0.0150 791  GLN B CG  
15079 C CD  . GLN B 793  ? 0.3246 0.4233 0.4238 -0.0148 0.0210  -0.0155 791  GLN B CD  
15080 O OE1 . GLN B 793  ? 0.3583 0.4633 0.4634 -0.0153 0.0201  -0.0167 791  GLN B OE1 
15081 N NE2 . GLN B 793  ? 0.3598 0.4502 0.4546 -0.0159 0.0194  -0.0147 791  GLN B NE2 
15082 N N   . ALA B 794  ? 0.1656 0.2912 0.2745 -0.0121 0.0312  -0.0161 792  ALA B N   
15083 C CA  . ALA B 794  ? 0.1785 0.3106 0.2912 -0.0160 0.0343  -0.0144 792  ALA B CA  
15084 C C   . ALA B 794  ? 0.1740 0.3090 0.2839 -0.0149 0.0383  -0.0137 792  ALA B C   
15085 O O   . ALA B 794  ? 0.2091 0.3441 0.3174 -0.0184 0.0410  -0.0114 792  ALA B O   
15086 C CB  . ALA B 794  ? 0.2184 0.3604 0.3402 -0.0167 0.0338  -0.0157 792  ALA B CB  
15087 N N   . GLN B 795  ? 0.1723 0.3089 0.2807 -0.0101 0.0388  -0.0157 793  GLN B N   
15088 C CA  . GLN B 795  ? 0.1727 0.3114 0.2776 -0.0087 0.0425  -0.0153 793  GLN B CA  
15089 C C   . GLN B 795  ? 0.1405 0.2702 0.2370 -0.0099 0.0430  -0.0132 793  GLN B C   
15090 O O   . GLN B 795  ? 0.1713 0.3020 0.2652 -0.0119 0.0462  -0.0114 793  GLN B O   
15091 C CB  . GLN B 795  ? 0.2119 0.3528 0.3163 -0.0031 0.0425  -0.0180 793  GLN B CB  
15092 C CG  . GLN B 795  ? 0.2782 0.4211 0.3784 -0.0012 0.0463  -0.0180 793  GLN B CG  
15093 C CD  . GLN B 795  ? 0.3577 0.5100 0.4622 -0.0035 0.0505  -0.0169 793  GLN B CD  
15094 O OE1 . GLN B 795  ? 0.3570 0.5185 0.4690 -0.0028 0.0512  -0.0182 793  GLN B OE1 
15095 N NE2 . GLN B 795  ? 0.3470 0.4974 0.4469 -0.0064 0.0533  -0.0146 793  GLN B NE2 
15096 N N   . LEU B 796  ? 0.1388 0.2599 0.2310 -0.0087 0.0397  -0.0135 794  LEU B N   
15097 C CA  . LEU B 796  ? 0.1420 0.2550 0.2266 -0.0094 0.0398  -0.0116 794  LEU B CA  
15098 C C   . LEU B 796  ? 0.1718 0.2822 0.2556 -0.0142 0.0406  -0.0087 794  LEU B C   
15099 O O   . LEU B 796  ? 0.1938 0.3003 0.2720 -0.0153 0.0422  -0.0067 794  LEU B O   
15100 C CB  . LEU B 796  ? 0.1442 0.2497 0.2253 -0.0071 0.0361  -0.0126 794  LEU B CB  
15101 C CG  . LEU B 796  ? 0.1383 0.2434 0.2175 -0.0025 0.0351  -0.0150 794  LEU B CG  
15102 C CD1 . LEU B 796  ? 0.1461 0.2438 0.2220 -0.0011 0.0316  -0.0154 794  LEU B CD1 
15103 C CD2 . LEU B 796  ? 0.1447 0.2503 0.2191 -0.0009 0.0377  -0.0149 794  LEU B CD2 
15104 N N   . ALA B 797  ? 0.1896 0.3017 0.2787 -0.0172 0.0394  -0.0085 795  ALA B N   
15105 C CA  . ALA B 797  ? 0.2262 0.3347 0.3142 -0.0219 0.0398  -0.0058 795  ALA B CA  
15106 C C   . ALA B 797  ? 0.2357 0.3493 0.3242 -0.0250 0.0439  -0.0038 795  ALA B C   
15107 O O   . ALA B 797  ? 0.2806 0.3902 0.3666 -0.0289 0.0446  -0.0011 795  ALA B O   
15108 C CB  . ALA B 797  ? 0.2487 0.3573 0.3419 -0.0245 0.0372  -0.0062 795  ALA B CB  
15109 N N   . ASP B 798  ? 0.1964 0.3187 0.2879 -0.0232 0.0466  -0.0050 796  ASP B N   
15110 C CA  . ASP B 798  ? 0.2658 0.3932 0.3573 -0.0260 0.0508  -0.0030 796  ASP B CA  
15111 C C   . ASP B 798  ? 0.2543 0.3762 0.3371 -0.0252 0.0527  -0.0013 796  ASP B C   
15112 O O   . ASP B 798  ? 0.2917 0.4158 0.3728 -0.0281 0.0561  0.0009  796  ASP B O   
15113 C CB  . ASP B 798  ? 0.2174 0.3564 0.3150 -0.0241 0.0534  -0.0049 796  ASP B CB  
15114 C CG  . ASP B 798  ? 0.3379 0.4844 0.4385 -0.0282 0.0575  -0.0028 796  ASP B CG  
15115 O OD1 . ASP B 798  ? 0.3665 0.5132 0.4704 -0.0333 0.0572  -0.0010 796  ASP B OD1 
15116 O OD2 . ASP B 798  ? 0.3449 0.4967 0.4442 -0.0265 0.0612  -0.0030 796  ASP B OD2 
15117 N N   . ARG B 799  ? 0.2447 0.3596 0.3218 -0.0216 0.0505  -0.0023 797  ARG B N   
15118 C CA  . ARG B 799  ? 0.2620 0.3721 0.3308 -0.0202 0.0517  -0.0011 797  ARG B CA  
15119 C C   . ARG B 799  ? 0.2228 0.3225 0.2862 -0.0205 0.0487  0.0004  797  ARG B C   
15120 O O   . ARG B 799  ? 0.2123 0.3084 0.2780 -0.0209 0.0456  -0.0001 797  ARG B O   
15121 C CB  . ARG B 799  ? 0.2979 0.4102 0.3649 -0.0151 0.0519  -0.0038 797  ARG B CB  
15122 C CG  . ARG B 799  ? 0.3535 0.4760 0.4259 -0.0136 0.0547  -0.0057 797  ARG B CG  
15123 C CD  . ARG B 799  ? 0.3940 0.5169 0.4627 -0.0086 0.0551  -0.0082 797  ARG B CD  
15124 N NE  . ARG B 799  ? 0.3930 0.5125 0.4623 -0.0051 0.0513  -0.0107 797  ARG B NE  
15125 C CZ  . ARG B 799  ? 0.3916 0.5035 0.4546 -0.0030 0.0490  -0.0111 797  ARG B CZ  
15126 N NH1 . ARG B 799  ? 0.3069 0.4141 0.3626 -0.0036 0.0498  -0.0093 797  ARG B NH1 
15127 N NH2 . ARG B 799  ? 0.3052 0.4147 0.3693 -0.0003 0.0457  -0.0132 797  ARG B NH2 
15128 N N   . LEU B 800  ? 0.2279 0.3228 0.2837 -0.0201 0.0496  0.0021  798  LEU B N   
15129 C CA  . LEU B 800  ? 0.2221 0.3077 0.2721 -0.0194 0.0468  0.0033  798  LEU B CA  
15130 C C   . LEU B 800  ? 0.2336 0.3172 0.2776 -0.0158 0.0467  0.0026  798  LEU B C   
15131 O O   . LEU B 800  ? 0.2576 0.3457 0.3002 -0.0147 0.0493  0.0019  798  LEU B O   
15132 C CB  . LEU B 800  ? 0.2741 0.3542 0.3202 -0.0232 0.0476  0.0070  798  LEU B CB  
15133 C CG  . LEU B 800  ? 0.2713 0.3504 0.3216 -0.0273 0.0470  0.0082  798  LEU B CG  
15134 C CD1 . LEU B 800  ? 0.2925 0.3663 0.3379 -0.0311 0.0484  0.0119  798  LEU B CD1 
15135 C CD2 . LEU B 800  ? 0.2544 0.3287 0.3066 -0.0259 0.0430  0.0068  798  LEU B CD2 
15136 N N   . SER B 801  ? 0.2441 0.3211 0.2846 -0.0139 0.0435  0.0026  799  SER B N   
15137 C CA  . SER B 801  ? 0.2746 0.3489 0.3092 -0.0109 0.0427  0.0021  799  SER B CA  
15138 C C   . SER B 801  ? 0.3112 0.3832 0.3390 -0.0123 0.0448  0.0048  799  SER B C   
15139 O O   . SER B 801  ? 0.3006 0.3717 0.3280 -0.0156 0.0464  0.0073  799  SER B O   
15140 C CB  . SER B 801  ? 0.2700 0.3382 0.3031 -0.0092 0.0389  0.0019  799  SER B CB  
15141 O OG  . SER B 801  ? 0.3009 0.3632 0.3307 -0.0110 0.0381  0.0049  799  SER B OG  
15142 N N   . PRO B 802  ? 0.3043 0.3750 0.3264 -0.0099 0.0446  0.0043  800  PRO B N   
15143 C CA  . PRO B 802  ? 0.3604 0.4281 0.3752 -0.0110 0.0461  0.0070  800  PRO B CA  
15144 C C   . PRO B 802  ? 0.2884 0.3495 0.3006 -0.0129 0.0445  0.0102  800  PRO B C   
15145 O O   . PRO B 802  ? 0.3691 0.4282 0.3770 -0.0152 0.0464  0.0131  800  PRO B O   
15146 C CB  . PRO B 802  ? 0.3230 0.3893 0.3325 -0.0077 0.0447  0.0056  800  PRO B CB  
15147 C CG  . PRO B 802  ? 0.3321 0.4032 0.3463 -0.0054 0.0446  0.0019  800  PRO B CG  
15148 C CD  . PRO B 802  ? 0.3416 0.4140 0.3635 -0.0063 0.0434  0.0013  800  PRO B CD  
15149 N N   . ALA B 803  ? 0.3185 0.3759 0.3329 -0.0120 0.0412  0.0099  801  ALA B N   
15150 C CA  . ALA B 803  ? 0.2942 0.3448 0.3063 -0.0133 0.0396  0.0126  801  ALA B CA  
15151 C C   . ALA B 803  ? 0.3079 0.3583 0.3243 -0.0167 0.0405  0.0137  801  ALA B C   
15152 O O   . ALA B 803  ? 0.3411 0.3853 0.3559 -0.0178 0.0390  0.0157  801  ALA B O   
15153 C CB  . ALA B 803  ? 0.3372 0.3841 0.3495 -0.0105 0.0358  0.0117  801  ALA B CB  
15154 N N   . GLY B 804  ? 0.2669 0.3237 0.2886 -0.0183 0.0428  0.0124  802  GLY B N   
15155 C CA  . GLY B 804  ? 0.2695 0.3266 0.2955 -0.0220 0.0436  0.0133  802  GLY B CA  
15156 C C   . GLY B 804  ? 0.2684 0.3233 0.2992 -0.0215 0.0406  0.0118  802  GLY B C   
15157 O O   . GLY B 804  ? 0.2687 0.3192 0.3000 -0.0241 0.0399  0.0134  802  GLY B O   
15158 N N   . ARG B 805  ? 0.2443 0.3017 0.2780 -0.0183 0.0389  0.0089  803  ARG B N   
15159 C CA  . ARG B 805  ? 0.2338 0.2892 0.2713 -0.0174 0.0360  0.0073  803  ARG B CA  
15160 C C   . ARG B 805  ? 0.2064 0.2688 0.2503 -0.0164 0.0361  0.0043  803  ARG B C   
15161 O O   . ARG B 805  ? 0.2036 0.2717 0.2482 -0.0153 0.0379  0.0030  803  ARG B O   
15162 C CB  . ARG B 805  ? 0.2347 0.2851 0.2685 -0.0140 0.0332  0.0071  803  ARG B CB  
15163 C CG  . ARG B 805  ? 0.2986 0.3421 0.3262 -0.0143 0.0326  0.0101  803  ARG B CG  
15164 C CD  . ARG B 805  ? 0.2950 0.3328 0.3231 -0.0167 0.0318  0.0116  803  ARG B CD  
15165 N NE  . ARG B 805  ? 0.3505 0.3810 0.3725 -0.0164 0.0309  0.0144  803  ARG B NE  
15166 C CZ  . ARG B 805  ? 0.3341 0.3614 0.3522 -0.0192 0.0325  0.0174  803  ARG B CZ  
15167 N NH1 . ARG B 805  ? 0.3098 0.3412 0.3295 -0.0226 0.0354  0.0179  803  ARG B NH1 
15168 N NH2 . ARG B 805  ? 0.3456 0.3655 0.3581 -0.0185 0.0313  0.0199  803  ARG B NH2 
15169 N N   . PRO B 806  ? 0.1966 0.2586 0.2450 -0.0168 0.0342  0.0029  804  PRO B N   
15170 C CA  . PRO B 806  ? 0.1602 0.2286 0.2145 -0.0157 0.0339  0.0001  804  PRO B CA  
15171 C C   . PRO B 806  ? 0.1681 0.2381 0.2211 -0.0117 0.0332  -0.0020 804  PRO B C   
15172 O O   . PRO B 806  ? 0.1878 0.2532 0.2367 -0.0096 0.0315  -0.0018 804  PRO B O   
15173 C CB  . PRO B 806  ? 0.1880 0.2533 0.2454 -0.0163 0.0312  -0.0007 804  PRO B CB  
15174 C CG  . PRO B 806  ? 0.2189 0.2780 0.2734 -0.0193 0.0312  0.0019  804  PRO B CG  
15175 C CD  . PRO B 806  ? 0.2025 0.2581 0.2506 -0.0184 0.0322  0.0040  804  PRO B CD  
15176 N N   . ILE B 807  ? 0.1685 0.2453 0.2251 -0.0106 0.0345  -0.0039 805  ILE B N   
15177 C CA  A ILE B 807  ? 0.1676 0.2460 0.2234 -0.0070 0.0338  -0.0062 805  ILE B CA  
15178 C CA  B ILE B 807  ? 0.1672 0.2454 0.2228 -0.0070 0.0337  -0.0062 805  ILE B CA  
15179 C C   . ILE B 807  ? 0.1593 0.2360 0.2177 -0.0053 0.0306  -0.0080 805  ILE B C   
15180 O O   . ILE B 807  ? 0.1815 0.2609 0.2451 -0.0062 0.0300  -0.0090 805  ILE B O   
15181 C CB  A ILE B 807  ? 0.1628 0.2487 0.2216 -0.0062 0.0362  -0.0078 805  ILE B CB  
15182 C CB  B ILE B 807  ? 0.1623 0.2478 0.2204 -0.0061 0.0363  -0.0076 805  ILE B CB  
15183 C CG1 A ILE B 807  ? 0.1955 0.2837 0.2520 -0.0082 0.0398  -0.0059 805  ILE B CG1 
15184 C CG1 B ILE B 807  ? 0.1897 0.2764 0.2441 -0.0076 0.0396  -0.0057 805  ILE B CG1 
15185 C CG2 A ILE B 807  ? 0.1795 0.2658 0.2364 -0.0023 0.0354  -0.0101 805  ILE B CG2 
15186 C CG2 B ILE B 807  ? 0.1806 0.2666 0.2376 -0.0022 0.0351  -0.0102 805  ILE B CG2 
15187 C CD1 A ILE B 807  ? 0.1935 0.2785 0.2428 -0.0067 0.0404  -0.0051 805  ILE B CD1 
15188 C CD1 B ILE B 807  ? 0.2116 0.3063 0.2693 -0.0076 0.0427  -0.0067 805  ILE B CD1 
15189 N N   . PRO B 808  ? 0.1672 0.2396 0.2221 -0.0030 0.0285  -0.0085 806  PRO B N   
15190 C CA  . PRO B 808  ? 0.1414 0.2119 0.1984 -0.0017 0.0257  -0.0100 806  PRO B CA  
15191 C C   . PRO B 808  ? 0.1426 0.2177 0.2036 0.0000  0.0253  -0.0126 806  PRO B C   
15192 O O   . PRO B 808  ? 0.1545 0.2326 0.2148 0.0017  0.0264  -0.0137 806  PRO B O   
15193 C CB  . PRO B 808  ? 0.1610 0.2270 0.2131 0.0002  0.0241  -0.0097 806  PRO B CB  
15194 C CG  . PRO B 808  ? 0.2356 0.2997 0.2833 -0.0007 0.0255  -0.0075 806  PRO B CG  
15195 C CD  . PRO B 808  ? 0.1589 0.2276 0.2077 -0.0020 0.0285  -0.0073 806  PRO B CD  
15196 N N   . LEU B 809  ? 0.1550 0.2301 0.2197 -0.0003 0.0235  -0.0135 807  LEU B N   
15197 C CA  . LEU B 809  ? 0.1441 0.2224 0.2123 0.0016  0.0223  -0.0158 807  LEU B CA  
15198 C C   . LEU B 809  ? 0.1447 0.2186 0.2119 0.0028  0.0194  -0.0165 807  LEU B C   
15199 O O   . LEU B 809  ? 0.1604 0.2313 0.2280 0.0013  0.0182  -0.0157 807  LEU B O   
15200 C CB  . LEU B 809  ? 0.1505 0.2341 0.2248 0.0000  0.0228  -0.0163 807  LEU B CB  
15201 C CG  . LEU B 809  ? 0.1452 0.2321 0.2236 0.0019  0.0212  -0.0187 807  LEU B CG  
15202 C CD1 . LEU B 809  ? 0.1719 0.2612 0.2492 0.0051  0.0220  -0.0202 807  LEU B CD1 
15203 C CD2 . LEU B 809  ? 0.1678 0.2603 0.2525 -0.0001 0.0215  -0.0189 807  LEU B CD2 
15204 N N   . ILE B 810  ? 0.1082 0.1812 0.1736 0.0053  0.0182  -0.0179 808  ILE B N   
15205 C CA  . ILE B 810  ? 0.1258 0.1956 0.1908 0.0064  0.0156  -0.0187 808  ILE B CA  
15206 C C   . ILE B 810  ? 0.1353 0.2084 0.2040 0.0078  0.0146  -0.0207 808  ILE B C   
15207 O O   . ILE B 810  ? 0.1544 0.2296 0.2228 0.0098  0.0151  -0.0220 808  ILE B O   
15208 C CB  . ILE B 810  ? 0.1451 0.2113 0.2054 0.0080  0.0146  -0.0187 808  ILE B CB  
15209 C CG1 . ILE B 810  ? 0.1629 0.2264 0.2197 0.0070  0.0155  -0.0167 808  ILE B CG1 
15210 C CG2 . ILE B 810  ? 0.1864 0.2497 0.2465 0.0088  0.0122  -0.0194 808  ILE B CG2 
15211 C CD1 . ILE B 810  ? 0.2063 0.2670 0.2590 0.0083  0.0143  -0.0165 808  ILE B CD1 
15212 N N   . ALA B 811  ? 0.1575 0.2309 0.2293 0.0069  0.0132  -0.0211 809  ALA B N   
15213 C CA  . ALA B 811  ? 0.1650 0.2419 0.2407 0.0082  0.0120  -0.0229 809  ALA B CA  
15214 C C   . ALA B 811  ? 0.1667 0.2399 0.2415 0.0088  0.0092  -0.0235 809  ALA B C   
15215 O O   . ALA B 811  ? 0.2103 0.2805 0.2844 0.0072  0.0084  -0.0227 809  ALA B O   
15216 C CB  . ALA B 811  ? 0.1602 0.2425 0.2413 0.0062  0.0130  -0.0228 809  ALA B CB  
15217 N N   . GLU B 812  ? 0.1382 0.2113 0.2125 0.0113  0.0078  -0.0249 810  GLU B N   
15218 C CA  . GLU B 812  ? 0.1535 0.2236 0.2272 0.0120  0.0051  -0.0256 810  GLU B CA  
15219 C C   . GLU B 812  ? 0.1538 0.2281 0.2317 0.0132  0.0039  -0.0271 810  GLU B C   
15220 O O   . GLU B 812  ? 0.1409 0.2177 0.2197 0.0153  0.0044  -0.0281 810  GLU B O   
15221 C CB  . GLU B 812  ? 0.1987 0.2644 0.2676 0.0137  0.0042  -0.0258 810  GLU B CB  
15222 N N   . THR B 813  ? 0.1389 0.2136 0.2193 0.0119  0.0023  -0.0273 811  THR B N   
15223 C CA  . THR B 813  ? 0.1631 0.2430 0.2487 0.0125  0.0012  -0.0285 811  THR B CA  
15224 C C   . THR B 813  ? 0.1823 0.2603 0.2679 0.0131  -0.0020 -0.0294 811  THR B C   
15225 O O   . THR B 813  ? 0.2432 0.3251 0.3332 0.0126  -0.0033 -0.0300 811  THR B O   
15226 C CB  . THR B 813  ? 0.1643 0.2491 0.2546 0.0096  0.0026  -0.0279 811  THR B CB  
15227 O OG1 . THR B 813  ? 0.1542 0.2349 0.2427 0.0069  0.0024  -0.0268 811  THR B OG1 
15228 C CG2 . THR B 813  ? 0.2058 0.2941 0.2969 0.0094  0.0059  -0.0272 811  THR B CG2 
15229 N N   . GLY B 814  ? 0.2005 0.2727 0.2811 0.0142  -0.0034 -0.0293 812  GLY B N   
15230 C CA  . GLY B 814  ? 0.2121 0.2825 0.2921 0.0155  -0.0064 -0.0302 812  GLY B CA  
15231 C C   . GLY B 814  ? 0.1812 0.2487 0.2601 0.0136  -0.0080 -0.0300 812  GLY B C   
15232 O O   . GLY B 814  ? 0.1923 0.2577 0.2699 0.0114  -0.0069 -0.0291 812  GLY B O   
15233 N N   . GLY B 815  ? 0.1840 0.2509 0.2629 0.0146  -0.0108 -0.0309 813  GLY B N   
15234 C CA  . GLY B 815  ? 0.1773 0.2404 0.2539 0.0131  -0.0125 -0.0309 813  GLY B CA  
15235 C C   . GLY B 815  ? 0.2096 0.2734 0.2872 0.0142  -0.0158 -0.0320 813  GLY B C   
15236 O O   . GLY B 815  ? 0.3076 0.3740 0.3869 0.0165  -0.0168 -0.0326 813  GLY B O   
15237 N N   . GLN B 816  ? 0.1857 0.2469 0.2618 0.0126  -0.0175 -0.0322 814  GLN B N   
15238 C CA  . GLN B 816  ? 0.1741 0.2351 0.2501 0.0133  -0.0209 -0.0332 814  GLN B CA  
15239 C C   . GLN B 816  ? 0.1407 0.1946 0.2097 0.0134  -0.0218 -0.0329 814  GLN B C   
15240 O O   . GLN B 816  ? 0.1858 0.2371 0.2531 0.0117  -0.0228 -0.0332 814  GLN B O   
15241 C CB  . GLN B 816  ? 0.2070 0.2719 0.2877 0.0110  -0.0224 -0.0338 814  GLN B CB  
15242 C CG  . GLN B 816  ? 0.2418 0.3080 0.3235 0.0120  -0.0261 -0.0348 814  GLN B CG  
15243 C CD  . GLN B 816  ? 0.2960 0.3676 0.3818 0.0148  -0.0270 -0.0353 814  GLN B CD  
15244 O OE1 . GLN B 816  ? 0.2870 0.3560 0.3696 0.0176  -0.0269 -0.0352 814  GLN B OE1 
15245 N NE2 . GLN B 816  ? 0.3259 0.4050 0.4188 0.0141  -0.0276 -0.0359 814  GLN B NE2 
15246 N N   . ASN B 817  ? 0.1206 0.1714 0.1857 0.0154  -0.0214 -0.0324 815  ASN B N   
15247 C CA  . ASN B 817  ? 0.1118 0.1567 0.1707 0.0151  -0.0207 -0.0317 815  ASN B CA  
15248 C C   . ASN B 817  ? 0.1272 0.1683 0.1819 0.0156  -0.0235 -0.0322 815  ASN B C   
15249 O O   . ASN B 817  ? 0.1396 0.1809 0.1940 0.0173  -0.0258 -0.0326 815  ASN B O   
15250 C CB  . ASN B 817  ? 0.1112 0.1545 0.1676 0.0164  -0.0190 -0.0309 815  ASN B CB  
15251 C CG  . ASN B 817  ? 0.1340 0.1811 0.1942 0.0163  -0.0166 -0.0305 815  ASN B CG  
15252 O OD1 . ASN B 817  ? 0.1165 0.1647 0.1783 0.0145  -0.0148 -0.0301 815  ASN B OD1 
15253 N ND2 . ASN B 817  ? 0.1408 0.1896 0.2021 0.0181  -0.0167 -0.0308 815  ASN B ND2 
15254 N N   . ALA B 818  ? 0.1361 0.1734 0.1870 0.0143  -0.0233 -0.0321 816  ALA B N   
15255 C CA  . ALA B 818  ? 0.1245 0.1579 0.1707 0.0146  -0.0257 -0.0326 816  ALA B CA  
15256 C C   . ALA B 818  ? 0.1263 0.1548 0.1661 0.0152  -0.0244 -0.0317 816  ALA B C   
15257 O O   . ALA B 818  ? 0.1265 0.1546 0.1657 0.0149  -0.0216 -0.0308 816  ALA B O   
15258 C CB  . ALA B 818  ? 0.1528 0.1851 0.1989 0.0127  -0.0265 -0.0335 816  ALA B CB  
15259 N N   . MET B 819  ? 0.1284 0.1536 0.1635 0.0159  -0.0265 -0.0318 817  MET B N   
15260 C CA  . MET B 819  ? 0.1212 0.1418 0.1498 0.0161  -0.0255 -0.0310 817  MET B CA  
15261 C C   . MET B 819  ? 0.1376 0.1549 0.1620 0.0157  -0.0275 -0.0319 817  MET B C   
15262 O O   . MET B 819  ? 0.1650 0.1823 0.1894 0.0162  -0.0307 -0.0327 817  MET B O   
15263 C CB  . MET B 819  ? 0.1404 0.1592 0.1661 0.0174  -0.0260 -0.0300 817  MET B CB  
15264 C CG  . MET B 819  ? 0.1482 0.1627 0.1671 0.0172  -0.0250 -0.0291 817  MET B CG  
15265 S SD  . MET B 819  ? 0.1934 0.2049 0.2081 0.0182  -0.0260 -0.0277 817  MET B SD  
15266 C CE  . MET B 819  ? 0.1972 0.2115 0.2158 0.0179  -0.0233 -0.0269 817  MET B CE  
15267 N N   . ILE B 820  ? 0.1459 0.1603 0.1665 0.0151  -0.0258 -0.0319 818  ILE B N   
15268 C CA  . ILE B 820  ? 0.1473 0.1579 0.1628 0.0149  -0.0273 -0.0329 818  ILE B CA  
15269 C C   . ILE B 820  ? 0.1404 0.1473 0.1491 0.0156  -0.0265 -0.0319 818  ILE B C   
15270 O O   . ILE B 820  ? 0.1584 0.1655 0.1662 0.0157  -0.0236 -0.0307 818  ILE B O   
15271 C CB  . ILE B 820  ? 0.1434 0.1529 0.1590 0.0138  -0.0259 -0.0337 818  ILE B CB  
15272 C CG1 . ILE B 820  ? 0.1764 0.1895 0.1987 0.0125  -0.0269 -0.0345 818  ILE B CG1 
15273 C CG2 . ILE B 820  ? 0.1618 0.1663 0.1706 0.0138  -0.0272 -0.0348 818  ILE B CG2 
15274 C CD1 . ILE B 820  ? 0.2008 0.2122 0.2234 0.0112  -0.0256 -0.0352 818  ILE B CD1 
15275 N N   . VAL B 821  ? 0.1681 0.1720 0.1719 0.0161  -0.0292 -0.0323 819  VAL B N   
15276 C CA  . VAL B 821  ? 0.1633 0.1636 0.1602 0.0166  -0.0288 -0.0313 819  VAL B CA  
15277 C C   . VAL B 821  ? 0.1851 0.1814 0.1759 0.0165  -0.0299 -0.0325 819  VAL B C   
15278 O O   . VAL B 821  ? 0.2058 0.2014 0.1966 0.0164  -0.0333 -0.0338 819  VAL B O   
15279 C CB  . VAL B 821  ? 0.1793 0.1789 0.1752 0.0175  -0.0313 -0.0304 819  VAL B CB  
15280 C CG1 . VAL B 821  ? 0.2103 0.2056 0.1983 0.0177  -0.0309 -0.0292 819  VAL B CG1 
15281 C CG2 . VAL B 821  ? 0.1803 0.1835 0.1820 0.0178  -0.0303 -0.0296 819  VAL B CG2 
15282 N N   . ASP B 822  ? 0.1742 0.1680 0.1597 0.0166  -0.0273 -0.0321 820  ASP B N   
15283 C CA  . ASP B 822  ? 0.1951 0.1846 0.1738 0.0168  -0.0283 -0.0333 820  ASP B CA  
15284 C C   . ASP B 822  ? 0.2243 0.2106 0.1957 0.0172  -0.0288 -0.0321 820  ASP B C   
15285 O O   . ASP B 822  ? 0.2186 0.2056 0.1903 0.0173  -0.0286 -0.0304 820  ASP B O   
15286 C CB  . ASP B 822  ? 0.2016 0.1901 0.1790 0.0168  -0.0253 -0.0341 820  ASP B CB  
15287 C CG  . ASP B 822  ? 0.1950 0.1839 0.1697 0.0174  -0.0212 -0.0327 820  ASP B CG  
15288 O OD1 . ASP B 822  ? 0.2226 0.2118 0.1952 0.0174  -0.0206 -0.0310 820  ASP B OD1 
15289 O OD2 . ASP B 822  ? 0.2500 0.2390 0.2250 0.0179  -0.0186 -0.0332 820  ASP B OD2 
15290 N N   . SER B 823  ? 0.2334 0.2155 0.1976 0.0175  -0.0295 -0.0331 821  SER B N   
15291 C CA  . SER B 823  ? 0.2546 0.2332 0.2111 0.0178  -0.0303 -0.0321 821  SER B CA  
15292 C C   . SER B 823  ? 0.2632 0.2419 0.2164 0.0178  -0.0262 -0.0302 821  SER B C   
15293 O O   . SER B 823  ? 0.2899 0.2659 0.2367 0.0177  -0.0264 -0.0289 821  SER B O   
15294 C CB  . SER B 823  ? 0.2789 0.2529 0.2283 0.0180  -0.0325 -0.0338 821  SER B CB  
15295 O OG  . SER B 823  ? 0.3108 0.2835 0.2576 0.0183  -0.0296 -0.0350 821  SER B OG  
15296 N N   . SER B 824  ? 0.2126 0.1946 0.1698 0.0177  -0.0225 -0.0300 822  SER B N   
15297 C CA  . SER B 824  ? 0.2224 0.2057 0.1775 0.0175  -0.0186 -0.0281 822  SER B CA  
15298 C C   . SER B 824  ? 0.2515 0.2375 0.2109 0.0167  -0.0183 -0.0260 822  SER B C   
15299 O O   . SER B 824  ? 0.2528 0.2397 0.2102 0.0160  -0.0158 -0.0242 822  SER B O   
15300 C CB  . SER B 824  ? 0.2233 0.2088 0.1803 0.0182  -0.0148 -0.0287 822  SER B CB  
15301 O OG  . SER B 824  ? 0.1986 0.1881 0.1638 0.0180  -0.0142 -0.0287 822  SER B OG  
15302 N N   . ALA B 825  ? 0.2156 0.2031 0.1809 0.0166  -0.0207 -0.0263 823  ALA B N   
15303 C CA  . ALA B 825  ? 0.2294 0.2191 0.1987 0.0160  -0.0204 -0.0247 823  ALA B CA  
15304 C C   . ALA B 825  ? 0.2330 0.2192 0.1968 0.0156  -0.0220 -0.0231 823  ALA B C   
15305 O O   . ALA B 825  ? 0.2796 0.2620 0.2381 0.0160  -0.0246 -0.0235 823  ALA B O   
15306 C CB  . ALA B 825  ? 0.2278 0.2199 0.2043 0.0163  -0.0225 -0.0257 823  ALA B CB  
15307 N N   . LEU B 826  ? 0.2466 0.2338 0.2112 0.0146  -0.0206 -0.0211 824  LEU B N   
15308 C CA  . LEU B 826  ? 0.2721 0.2553 0.2315 0.0140  -0.0221 -0.0193 824  LEU B CA  
15309 C C   . LEU B 826  ? 0.2785 0.2606 0.2410 0.0149  -0.0258 -0.0197 824  LEU B C   
15310 O O   . LEU B 826  ? 0.2754 0.2605 0.2442 0.0150  -0.0255 -0.0199 824  LEU B O   
15311 C CB  . LEU B 826  ? 0.3171 0.3015 0.2760 0.0122  -0.0191 -0.0171 824  LEU B CB  
15312 C CG  . LEU B 826  ? 0.3620 0.3418 0.3146 0.0110  -0.0201 -0.0149 824  LEU B CG  
15313 C CD1 . LEU B 826  ? 0.3974 0.3727 0.3417 0.0113  -0.0213 -0.0148 824  LEU B CD1 
15314 C CD2 . LEU B 826  ? 0.4395 0.4214 0.3919 0.0087  -0.0167 -0.0128 824  LEU B CD2 
15315 N N   . ALA B 827  ? 0.2781 0.2560 0.2360 0.0158  -0.0293 -0.0199 825  ALA B N   
15316 C CA  . ALA B 827  ? 0.2361 0.2137 0.1973 0.0173  -0.0331 -0.0206 825  ALA B CA  
15317 C C   . ALA B 827  ? 0.2771 0.2543 0.2405 0.0172  -0.0331 -0.0193 825  ALA B C   
15318 O O   . ALA B 827  ? 0.2427 0.2225 0.2123 0.0184  -0.0342 -0.0203 825  ALA B O   
15319 C CB  . ALA B 827  ? 0.2757 0.2486 0.2307 0.0184  -0.0369 -0.0207 825  ALA B CB  
15320 N N   . GLU B 828  ? 0.2786 0.2523 0.2366 0.0158  -0.0319 -0.0172 826  GLU B N   
15321 C CA  . GLU B 828  ? 0.3078 0.2801 0.2670 0.0154  -0.0321 -0.0160 826  GLU B CA  
15322 C C   . GLU B 828  ? 0.2791 0.2567 0.2460 0.0150  -0.0297 -0.0166 826  GLU B C   
15323 O O   . GLU B 828  ? 0.2474 0.2253 0.2180 0.0159  -0.0308 -0.0170 826  GLU B O   
15324 C CB  . GLU B 828  ? 0.3344 0.3022 0.2865 0.0132  -0.0309 -0.0134 826  GLU B CB  
15325 C CG  . GLU B 828  ? 0.4002 0.3613 0.3442 0.0138  -0.0339 -0.0123 826  GLU B CG  
15326 C CD  . GLU B 828  ? 0.4460 0.4064 0.3850 0.0139  -0.0339 -0.0127 826  GLU B CD  
15327 O OE1 . GLU B 828  ? 0.4121 0.3769 0.3536 0.0136  -0.0314 -0.0139 826  GLU B OE1 
15328 O OE2 . GLU B 828  ? 0.4766 0.4315 0.4086 0.0144  -0.0366 -0.0118 826  GLU B OE2 
15329 N N   . GLN B 829  ? 0.2338 0.2155 0.2027 0.0138  -0.0263 -0.0168 827  GLN B N   
15330 C CA  . GLN B 829  ? 0.2419 0.2287 0.2178 0.0135  -0.0241 -0.0174 827  GLN B CA  
15331 C C   . GLN B 829  ? 0.2288 0.2187 0.2110 0.0153  -0.0256 -0.0194 827  GLN B C   
15332 O O   . GLN B 829  ? 0.2033 0.1955 0.1905 0.0157  -0.0255 -0.0198 827  GLN B O   
15333 C CB  . GLN B 829  ? 0.3104 0.3008 0.2868 0.0122  -0.0204 -0.0172 827  GLN B CB  
15334 C CG  . GLN B 829  ? 0.3834 0.3736 0.3566 0.0100  -0.0179 -0.0150 827  GLN B CG  
15335 C CD  . GLN B 829  ? 0.4345 0.4295 0.4098 0.0095  -0.0143 -0.0151 827  GLN B CD  
15336 O OE1 . GLN B 829  ? 0.3748 0.3716 0.3520 0.0108  -0.0139 -0.0168 827  GLN B OE1 
15337 N NE2 . GLN B 829  ? 0.4053 0.4022 0.3802 0.0075  -0.0118 -0.0134 827  GLN B NE2 
15338 N N   . VAL B 830  ? 0.2190 0.2092 0.2010 0.0163  -0.0269 -0.0208 828  VAL B N   
15339 C CA  . VAL B 830  ? 0.1865 0.1797 0.1743 0.0177  -0.0286 -0.0227 828  VAL B CA  
15340 C C   . VAL B 830  ? 0.1961 0.1884 0.1858 0.0192  -0.0313 -0.0228 828  VAL B C   
15341 O O   . VAL B 830  ? 0.1980 0.1939 0.1938 0.0200  -0.0311 -0.0237 828  VAL B O   
15342 C CB  . VAL B 830  ? 0.2101 0.2025 0.1959 0.0183  -0.0304 -0.0240 828  VAL B CB  
15343 C CG1 . VAL B 830  ? 0.2298 0.2256 0.2219 0.0194  -0.0326 -0.0258 828  VAL B CG1 
15344 C CG2 . VAL B 830  ? 0.2319 0.2251 0.2160 0.0172  -0.0275 -0.0242 828  VAL B CG2 
15345 N N   . VAL B 831  ? 0.2175 0.2049 0.2017 0.0199  -0.0339 -0.0220 829  VAL B N   
15346 C CA  . VAL B 831  ? 0.1883 0.1746 0.1740 0.0220  -0.0368 -0.0223 829  VAL B CA  
15347 C C   . VAL B 831  ? 0.1973 0.1839 0.1855 0.0219  -0.0354 -0.0217 829  VAL B C   
15348 O O   . VAL B 831  ? 0.2001 0.1894 0.1935 0.0236  -0.0362 -0.0228 829  VAL B O   
15349 C CB  . VAL B 831  ? 0.2053 0.1854 0.1838 0.0229  -0.0400 -0.0213 829  VAL B CB  
15350 C CG1 . VAL B 831  ? 0.2428 0.2207 0.2220 0.0252  -0.0427 -0.0213 829  VAL B CG1 
15351 C CG2 . VAL B 831  ? 0.2301 0.2107 0.2075 0.0236  -0.0423 -0.0224 829  VAL B CG2 
15352 N N   . GLY B 832  ? 0.2054 0.1897 0.1900 0.0199  -0.0331 -0.0201 830  GLY B N   
15353 C CA  . GLY B 832  ? 0.1853 0.1698 0.1721 0.0194  -0.0318 -0.0197 830  GLY B CA  
15354 C C   . GLY B 832  ? 0.2097 0.2006 0.2040 0.0196  -0.0299 -0.0210 830  GLY B C   
15355 O O   . GLY B 832  ? 0.2005 0.1925 0.1983 0.0208  -0.0301 -0.0217 830  GLY B O   
15356 N N   . ASP B 833  ? 0.2037 0.1985 0.2003 0.0186  -0.0279 -0.0215 831  ASP B N   
15357 C CA  . ASP B 833  ? 0.1802 0.1806 0.1836 0.0186  -0.0260 -0.0225 831  ASP B CA  
15358 C C   . ASP B 833  ? 0.1882 0.1916 0.1966 0.0206  -0.0278 -0.0242 831  ASP B C   
15359 O O   . ASP B 833  ? 0.1970 0.2043 0.2108 0.0210  -0.0267 -0.0250 831  ASP B O   
15360 C CB  . ASP B 833  ? 0.1722 0.1753 0.1762 0.0171  -0.0234 -0.0224 831  ASP B CB  
15361 C CG  . ASP B 833  ? 0.1903 0.1924 0.1911 0.0151  -0.0210 -0.0207 831  ASP B CG  
15362 O OD1 . ASP B 833  ? 0.2221 0.2221 0.2212 0.0145  -0.0210 -0.0197 831  ASP B OD1 
15363 O OD2 . ASP B 833  ? 0.2150 0.2184 0.2148 0.0142  -0.0191 -0.0204 831  ASP B OD2 
15364 N N   . VAL B 834  ? 0.1728 0.1748 0.1797 0.0218  -0.0306 -0.0248 832  VAL B N   
15365 C CA  . VAL B 834  ? 0.1555 0.1610 0.1676 0.0236  -0.0326 -0.0264 832  VAL B CA  
15366 C C   . VAL B 834  ? 0.1594 0.1643 0.1728 0.0258  -0.0341 -0.0266 832  VAL B C   
15367 O O   . VAL B 834  ? 0.1938 0.2032 0.2131 0.0270  -0.0339 -0.0277 832  VAL B O   
15368 C CB  . VAL B 834  ? 0.1667 0.1711 0.1766 0.0241  -0.0354 -0.0270 832  VAL B CB  
15369 C CG1 . VAL B 834  ? 0.2023 0.2101 0.2173 0.0262  -0.0382 -0.0284 832  VAL B CG1 
15370 C CG2 . VAL B 834  ? 0.1858 0.1917 0.1958 0.0222  -0.0338 -0.0274 832  VAL B CG2 
15371 N N   . ILE B 835  ? 0.1743 0.1733 0.1819 0.0264  -0.0356 -0.0255 833  ILE B N   
15372 C CA  . ILE B 835  ? 0.1976 0.1947 0.2054 0.0288  -0.0372 -0.0258 833  ILE B CA  
15373 C C   . ILE B 835  ? 0.1984 0.1979 0.2097 0.0285  -0.0346 -0.0260 833  ILE B C   
15374 O O   . ILE B 835  ? 0.2155 0.2178 0.2311 0.0306  -0.0350 -0.0272 833  ILE B O   
15375 C CB  . ILE B 835  ? 0.2130 0.2021 0.2127 0.0290  -0.0390 -0.0243 833  ILE B CB  
15376 C CG1 . ILE B 835  ? 0.2635 0.2500 0.2596 0.0299  -0.0422 -0.0241 833  ILE B CG1 
15377 C CG2 . ILE B 835  ? 0.2763 0.2621 0.2754 0.0312  -0.0402 -0.0244 833  ILE B CG2 
15378 C CD1 . ILE B 835  ? 0.2984 0.2859 0.2971 0.0335  -0.0457 -0.0252 833  ILE B CD1 
15379 N N   . THR B 836  ? 0.1911 0.1899 0.2006 0.0258  -0.0319 -0.0250 834  THR B N   
15380 C CA  A THR B 836  ? 0.1912 0.1924 0.2038 0.0252  -0.0295 -0.0252 834  THR B CA  
15381 C CA  B THR B 836  ? 0.1915 0.1928 0.2041 0.0253  -0.0295 -0.0252 834  THR B CA  
15382 C C   . THR B 836  ? 0.1948 0.2031 0.2145 0.0257  -0.0281 -0.0265 834  THR B C   
15383 O O   . THR B 836  ? 0.1960 0.2069 0.2195 0.0272  -0.0277 -0.0275 834  THR B O   
15384 C CB  A THR B 836  ? 0.2182 0.2180 0.2277 0.0222  -0.0271 -0.0237 834  THR B CB  
15385 C CB  B THR B 836  ? 0.2187 0.2184 0.2283 0.0223  -0.0271 -0.0237 834  THR B CB  
15386 O OG1 A THR B 836  ? 0.2579 0.2513 0.2607 0.0214  -0.0283 -0.0223 834  THR B OG1 
15387 O OG1 B THR B 836  ? 0.2081 0.2107 0.2186 0.0206  -0.0256 -0.0235 834  THR B OG1 
15388 C CG2 A THR B 836  ? 0.2042 0.2062 0.2163 0.0215  -0.0250 -0.0238 834  THR B CG2 
15389 C CG2 B THR B 836  ? 0.2544 0.2472 0.2570 0.0214  -0.0283 -0.0222 834  THR B CG2 
15390 N N   . SER B 837  ? 0.1700 0.1813 0.1916 0.0243  -0.0273 -0.0266 835  SER B N   
15391 C CA  . SER B 837  ? 0.1441 0.1615 0.1720 0.0240  -0.0257 -0.0276 835  SER B CA  
15392 C C   . SER B 837  ? 0.1472 0.1683 0.1800 0.0262  -0.0274 -0.0290 835  SER B C   
15393 O O   . SER B 837  ? 0.1581 0.1841 0.1961 0.0264  -0.0259 -0.0297 835  SER B O   
15394 C CB  . SER B 837  ? 0.1520 0.1707 0.1800 0.0222  -0.0248 -0.0274 835  SER B CB  
15395 O OG  . SER B 837  ? 0.1471 0.1636 0.1715 0.0204  -0.0229 -0.0262 835  SER B OG  
15396 N N   . ALA B 838  ? 0.1461 0.1656 0.1775 0.0279  -0.0304 -0.0294 836  ALA B N   
15397 C CA  . ALA B 838  ? 0.1532 0.1772 0.1899 0.0300  -0.0322 -0.0307 836  ALA B CA  
15398 C C   . ALA B 838  ? 0.1618 0.1856 0.1994 0.0330  -0.0330 -0.0313 836  ALA B C   
15399 O O   . ALA B 838  ? 0.1776 0.2070 0.2210 0.0346  -0.0329 -0.0324 836  ALA B O   
15400 C CB  . ALA B 838  ? 0.1885 0.2115 0.2238 0.0306  -0.0355 -0.0310 836  ALA B CB  
15401 N N   . PHE B 839  ? 0.1545 0.1717 0.1861 0.0338  -0.0338 -0.0305 837  PHE B N   
15402 C CA  . PHE B 839  ? 0.1758 0.1914 0.2072 0.0372  -0.0353 -0.0311 837  PHE B CA  
15403 C C   . PHE B 839  ? 0.1929 0.2051 0.2217 0.0371  -0.0334 -0.0309 837  PHE B C   
15404 O O   . PHE B 839  ? 0.2015 0.2129 0.2307 0.0401  -0.0342 -0.0318 837  PHE B O   
15405 C CB  . PHE B 839  ? 0.1915 0.2012 0.2176 0.0389  -0.0389 -0.0306 837  PHE B CB  
15406 C CG  . PHE B 839  ? 0.1967 0.2092 0.2247 0.0391  -0.0412 -0.0309 837  PHE B CG  
15407 C CD1 . PHE B 839  ? 0.2065 0.2267 0.2419 0.0405  -0.0419 -0.0323 837  PHE B CD1 
15408 C CD2 . PHE B 839  ? 0.2311 0.2387 0.2533 0.0376  -0.0428 -0.0298 837  PHE B CD2 
15409 C CE1 . PHE B 839  ? 0.1941 0.2168 0.2312 0.0403  -0.0443 -0.0327 837  PHE B CE1 
15410 C CE2 . PHE B 839  ? 0.2422 0.2521 0.2656 0.0377  -0.0451 -0.0302 837  PHE B CE2 
15411 C CZ  . PHE B 839  ? 0.2391 0.2565 0.2700 0.0390  -0.0460 -0.0317 837  PHE B CZ  
15412 N N   . ASP B 840  ? 0.1694 0.1797 0.1955 0.0340  -0.0312 -0.0298 838  ASP B N   
15413 C CA  . ASP B 840  ? 0.1729 0.1811 0.1973 0.0335  -0.0293 -0.0297 838  ASP B CA  
15414 C C   . ASP B 840  ? 0.1770 0.1911 0.2073 0.0353  -0.0278 -0.0312 838  ASP B C   
15415 O O   . ASP B 840  ? 0.1667 0.1875 0.2028 0.0349  -0.0267 -0.0318 838  ASP B O   
15416 C CB  . ASP B 840  ? 0.1920 0.1998 0.2146 0.0297  -0.0269 -0.0283 838  ASP B CB  
15417 C CG  . ASP B 840  ? 0.1981 0.2043 0.2192 0.0288  -0.0252 -0.0282 838  ASP B CG  
15418 O OD1 . ASP B 840  ? 0.2087 0.2194 0.2340 0.0294  -0.0234 -0.0291 838  ASP B OD1 
15419 O OD2 . ASP B 840  ? 0.2242 0.2246 0.2398 0.0274  -0.0256 -0.0270 838  ASP B OD2 
15420 N N   . SER B 841  ? 0.1895 0.2007 0.2179 0.0373  -0.0278 -0.0319 839  SER B N   
15421 C CA  . SER B 841  ? 0.1907 0.2070 0.2239 0.0393  -0.0262 -0.0334 839  SER B CA  
15422 C C   . SER B 841  ? 0.1717 0.1943 0.2109 0.0421  -0.0273 -0.0346 839  SER B C   
15423 O O   . SER B 841  ? 0.1758 0.2054 0.2209 0.0426  -0.0254 -0.0355 839  SER B O   
15424 C CB  . SER B 841  ? 0.1747 0.1956 0.2107 0.0365  -0.0229 -0.0331 839  SER B CB  
15425 O OG  . SER B 841  ? 0.2029 0.2186 0.2337 0.0342  -0.0221 -0.0320 839  SER B OG  
15426 N N   . ALA B 842  ? 0.1637 0.1839 0.2015 0.0438  -0.0304 -0.0345 840  ALA B N   
15427 C CA  . ALA B 842  ? 0.1543 0.1803 0.1977 0.0463  -0.0321 -0.0355 840  ALA B CA  
15428 C C   . ALA B 842  ? 0.1422 0.1762 0.1919 0.0438  -0.0306 -0.0355 840  ALA B C   
15429 O O   . ALA B 842  ? 0.1618 0.2033 0.2182 0.0453  -0.0305 -0.0366 840  ALA B O   
15430 C CB  . ALA B 842  ? 0.1870 0.2155 0.2332 0.0508  -0.0323 -0.0372 840  ALA B CB  
15431 N N   . GLY B 843  ? 0.1404 0.1730 0.1882 0.0400  -0.0293 -0.0343 841  GLY B N   
15432 C CA  . GLY B 843  ? 0.1651 0.2039 0.2179 0.0374  -0.0279 -0.0343 841  GLY B CA  
15433 C C   . GLY B 843  ? 0.1565 0.2014 0.2144 0.0369  -0.0248 -0.0348 841  GLY B C   
15434 O O   . GLY B 843  ? 0.1630 0.2136 0.2260 0.0351  -0.0238 -0.0349 841  GLY B O   
15435 N N   . GLN B 844  ? 0.1419 0.1854 0.1984 0.0383  -0.0232 -0.0352 842  GLN B N   
15436 C CA  . GLN B 844  ? 0.1540 0.2030 0.2147 0.0380  -0.0202 -0.0357 842  GLN B CA  
15437 C C   . GLN B 844  ? 0.1563 0.2037 0.2147 0.0346  -0.0176 -0.0346 842  GLN B C   
15438 O O   . GLN B 844  ? 0.2001 0.2472 0.2574 0.0348  -0.0155 -0.0347 842  GLN B O   
15439 C CB  . GLN B 844  ? 0.1498 0.1985 0.2100 0.0416  -0.0199 -0.0369 842  GLN B CB  
15440 C CG  . GLN B 844  ? 0.1558 0.2072 0.2192 0.0455  -0.0223 -0.0381 842  GLN B CG  
15441 C CD  . GLN B 844  ? 0.1539 0.2045 0.2164 0.0496  -0.0220 -0.0395 842  GLN B CD  
15442 O OE1 . GLN B 844  ? 0.1380 0.1951 0.2060 0.0525  -0.0218 -0.0408 842  GLN B OE1 
15443 N NE2 . GLN B 844  ? 0.1825 0.2253 0.2383 0.0498  -0.0218 -0.0394 842  GLN B NE2 
15444 N N   . ARG B 845  ? 0.1471 0.1929 0.2042 0.0318  -0.0178 -0.0335 843  ARG B N   
15445 C CA  . ARG B 845  ? 0.1262 0.1716 0.1822 0.0288  -0.0155 -0.0323 843  ARG B CA  
15446 C C   . ARG B 845  ? 0.1452 0.1956 0.2059 0.0268  -0.0147 -0.0322 843  ARG B C   
15447 O O   . ARG B 845  ? 0.1414 0.1928 0.2037 0.0267  -0.0166 -0.0324 843  ARG B O   
15448 C CB  . ARG B 845  ? 0.1345 0.1738 0.1848 0.0272  -0.0163 -0.0311 843  ARG B CB  
15449 C CG  . ARG B 845  ? 0.1469 0.1802 0.1917 0.0283  -0.0172 -0.0310 843  ARG B CG  
15450 C CD  . ARG B 845  ? 0.1626 0.1910 0.2024 0.0262  -0.0177 -0.0296 843  ARG B CD  
15451 N NE  . ARG B 845  ? 0.1901 0.2125 0.2244 0.0265  -0.0186 -0.0292 843  ARG B NE  
15452 C CZ  . ARG B 845  ? 0.1760 0.1963 0.2076 0.0248  -0.0173 -0.0283 843  ARG B CZ  
15453 N NH1 . ARG B 845  ? 0.1878 0.2116 0.2215 0.0229  -0.0150 -0.0278 843  ARG B NH1 
15454 N NH2 . ARG B 845  ? 0.2027 0.2172 0.2291 0.0248  -0.0184 -0.0280 843  ARG B NH2 
15455 N N   . CYS B 846  ? 0.1451 0.1983 0.2077 0.0251  -0.0120 -0.0317 844  CYS B N   
15456 C CA  . CYS B 846  ? 0.1586 0.2151 0.2248 0.0228  -0.0114 -0.0314 844  CYS B CA  
15457 C C   . CYS B 846  ? 0.1170 0.1695 0.1800 0.0211  -0.0124 -0.0306 844  CYS B C   
15458 O O   . CYS B 846  ? 0.1739 0.2280 0.2392 0.0196  -0.0128 -0.0306 844  CYS B O   
15459 C CB  . CYS B 846  ? 0.1887 0.2482 0.2568 0.0213  -0.0084 -0.0308 844  CYS B CB  
15460 S SG  . CYS B 846  ? 0.2638 0.3294 0.3364 0.0232  -0.0069 -0.0318 844  CYS B SG  
15461 N N   . SER B 847  ? 0.1229 0.1702 0.1806 0.0212  -0.0127 -0.0299 845  SER B N   
15462 C CA  . SER B 847  ? 0.1070 0.1504 0.1611 0.0199  -0.0134 -0.0292 845  SER B CA  
15463 C C   . SER B 847  ? 0.1101 0.1512 0.1624 0.0209  -0.0163 -0.0297 845  SER B C   
15464 O O   . SER B 847  ? 0.1286 0.1665 0.1776 0.0200  -0.0170 -0.0292 845  SER B O   
15465 C CB  . SER B 847  ? 0.1286 0.1683 0.1781 0.0195  -0.0124 -0.0281 845  SER B CB  
15466 O OG  . SER B 847  ? 0.1355 0.1732 0.1830 0.0212  -0.0135 -0.0285 845  SER B OG  
15467 N N   . ALA B 848  ? 0.1260 0.1685 0.1801 0.0230  -0.0180 -0.0306 846  ALA B N   
15468 C CA  . ALA B 848  ? 0.1343 0.1737 0.1856 0.0244  -0.0210 -0.0309 846  ALA B CA  
15469 C C   . ALA B 848  ? 0.1108 0.1506 0.1626 0.0232  -0.0225 -0.0311 846  ALA B C   
15470 O O   . ALA B 848  ? 0.1402 0.1839 0.1962 0.0219  -0.0219 -0.0315 846  ALA B O   
15471 C CB  . ALA B 848  ? 0.1279 0.1695 0.1818 0.0273  -0.0226 -0.0320 846  ALA B CB  
15472 N N   . LEU B 849  ? 0.1321 0.1673 0.1791 0.0235  -0.0245 -0.0308 847  LEU B N   
15473 C CA  . LEU B 849  ? 0.1273 0.1619 0.1736 0.0226  -0.0263 -0.0311 847  LEU B CA  
15474 C C   . LEU B 849  ? 0.1544 0.1931 0.2052 0.0239  -0.0289 -0.0323 847  LEU B C   
15475 O O   . LEU B 849  ? 0.1607 0.1990 0.2112 0.0263  -0.0309 -0.0326 847  LEU B O   
15476 C CB  . LEU B 849  ? 0.1340 0.1626 0.1734 0.0228  -0.0277 -0.0304 847  LEU B CB  
15477 C CG  . LEU B 849  ? 0.1325 0.1598 0.1700 0.0222  -0.0299 -0.0309 847  LEU B CG  
15478 C CD1 . LEU B 849  ? 0.1652 0.1938 0.2041 0.0200  -0.0282 -0.0311 847  LEU B CD1 
15479 C CD2 . LEU B 849  ? 0.1605 0.1819 0.1908 0.0225  -0.0311 -0.0300 847  LEU B CD2 
15480 N N   . ARG B 850  ? 0.1407 0.1834 0.1958 0.0223  -0.0289 -0.0329 848  ARG B N   
15481 C CA  . ARG B 850  ? 0.1374 0.1851 0.1978 0.0231  -0.0313 -0.0340 848  ARG B CA  
15482 C C   . ARG B 850  ? 0.1459 0.1921 0.2045 0.0222  -0.0343 -0.0345 848  ARG B C   
15483 O O   . ARG B 850  ? 0.1440 0.1926 0.2049 0.0236  -0.0374 -0.0353 848  ARG B O   
15484 C CB  . ARG B 850  ? 0.1624 0.2167 0.2297 0.0216  -0.0293 -0.0344 848  ARG B CB  
15485 C CG  . ARG B 850  ? 0.1423 0.1981 0.2111 0.0222  -0.0261 -0.0339 848  ARG B CG  
15486 C CD  . ARG B 850  ? 0.1427 0.1989 0.2115 0.0256  -0.0270 -0.0342 848  ARG B CD  
15487 N NE  . ARG B 850  ? 0.1484 0.2069 0.2191 0.0262  -0.0241 -0.0341 848  ARG B NE  
15488 C CZ  . ARG B 850  ? 0.1539 0.2119 0.2239 0.0291  -0.0241 -0.0345 848  ARG B CZ  
15489 N NH1 . ARG B 850  ? 0.1377 0.1926 0.2050 0.0316  -0.0269 -0.0348 848  ARG B NH1 
15490 N NH2 . ARG B 850  ? 0.1632 0.2232 0.2347 0.0295  -0.0214 -0.0345 848  ARG B NH2 
15491 N N   . VAL B 851  ? 0.1468 0.1889 0.2012 0.0201  -0.0336 -0.0342 849  VAL B N   
15492 C CA  . VAL B 851  ? 0.1590 0.1991 0.2111 0.0191  -0.0363 -0.0349 849  VAL B CA  
15493 C C   . VAL B 851  ? 0.1639 0.1969 0.2078 0.0188  -0.0358 -0.0342 849  VAL B C   
15494 O O   . VAL B 851  ? 0.1503 0.1814 0.1924 0.0175  -0.0330 -0.0337 849  VAL B O   
15495 C CB  . VAL B 851  ? 0.1851 0.2281 0.2411 0.0163  -0.0360 -0.0356 849  VAL B CB  
15496 C CG1 . VAL B 851  ? 0.2013 0.2421 0.2546 0.0154  -0.0395 -0.0365 849  VAL B CG1 
15497 C CG2 . VAL B 851  ? 0.2553 0.3059 0.3196 0.0162  -0.0357 -0.0360 849  VAL B CG2 
15498 N N   . LEU B 852  ? 0.1654 0.1949 0.2046 0.0202  -0.0384 -0.0341 850  LEU B N   
15499 C CA  . LEU B 852  ? 0.1317 0.1549 0.1630 0.0199  -0.0382 -0.0335 850  LEU B CA  
15500 C C   . LEU B 852  ? 0.1612 0.1827 0.1901 0.0186  -0.0403 -0.0345 850  LEU B C   
15501 O O   . LEU B 852  ? 0.1756 0.1987 0.2061 0.0190  -0.0438 -0.0354 850  LEU B O   
15502 C CB  . LEU B 852  ? 0.1788 0.1985 0.2055 0.0220  -0.0399 -0.0327 850  LEU B CB  
15503 C CG  . LEU B 852  ? 0.1693 0.1825 0.1873 0.0216  -0.0399 -0.0318 850  LEU B CG  
15504 C CD1 . LEU B 852  ? 0.1875 0.1993 0.2035 0.0203  -0.0358 -0.0309 850  LEU B CD1 
15505 C CD2 . LEU B 852  ? 0.2178 0.2275 0.2316 0.0235  -0.0420 -0.0309 850  LEU B CD2 
15506 N N   . CYS B 853  ? 0.1449 0.1631 0.1700 0.0171  -0.0382 -0.0345 851  CYS B N   
15507 C CA  . CYS B 853  ? 0.1598 0.1756 0.1819 0.0158  -0.0398 -0.0357 851  CYS B CA  
15508 C C   . CYS B 853  ? 0.1607 0.1703 0.1739 0.0163  -0.0398 -0.0352 851  CYS B C   
15509 O O   . CYS B 853  ? 0.1762 0.1835 0.1861 0.0162  -0.0366 -0.0344 851  CYS B O   
15510 C CB  . CYS B 853  ? 0.1593 0.1757 0.1838 0.0138  -0.0374 -0.0362 851  CYS B CB  
15511 S SG  . CYS B 853  ? 0.1899 0.2135 0.2244 0.0129  -0.0364 -0.0363 851  CYS B SG  
15512 N N   . LEU B 854  ? 0.1555 0.1628 0.1648 0.0169  -0.0434 -0.0358 852  LEU B N   
15513 C CA  . LEU B 854  ? 0.1816 0.1832 0.1821 0.0175  -0.0437 -0.0352 852  LEU B CA  
15514 C C   . LEU B 854  ? 0.2042 0.2022 0.1997 0.0165  -0.0451 -0.0366 852  LEU B C   
15515 O O   . LEU B 854  ? 0.2080 0.2071 0.2052 0.0159  -0.0485 -0.0380 852  LEU B O   
15516 C CB  . LEU B 854  ? 0.1819 0.1826 0.1803 0.0192  -0.0470 -0.0345 852  LEU B CB  
15517 C CG  . LEU B 854  ? 0.1941 0.1969 0.1960 0.0206  -0.0461 -0.0332 852  LEU B CG  
15518 C CD1 . LEU B 854  ? 0.1962 0.1972 0.1955 0.0225  -0.0498 -0.0327 852  LEU B CD1 
15519 C CD2 . LEU B 854  ? 0.2181 0.2185 0.2165 0.0202  -0.0420 -0.0317 852  LEU B CD2 
15520 N N   . GLN B 855  ? 0.1852 0.1790 0.1742 0.0163  -0.0425 -0.0364 853  GLN B N   
15521 C CA  . GLN B 855  ? 0.1814 0.1708 0.1642 0.0157  -0.0438 -0.0378 853  GLN B CA  
15522 C C   . GLN B 855  ? 0.2197 0.2067 0.1978 0.0164  -0.0482 -0.0381 853  GLN B C   
15523 O O   . GLN B 855  ? 0.2159 0.2018 0.1912 0.0176  -0.0488 -0.0366 853  GLN B O   
15524 C CB  . GLN B 855  ? 0.2172 0.2027 0.1933 0.0160  -0.0400 -0.0373 853  GLN B CB  
15525 C CG  . GLN B 855  ? 0.2388 0.2199 0.2092 0.0155  -0.0405 -0.0392 853  GLN B CG  
15526 C CD  . GLN B 855  ? 0.2648 0.2423 0.2282 0.0163  -0.0368 -0.0388 853  GLN B CD  
15527 O OE1 . GLN B 855  ? 0.2841 0.2636 0.2497 0.0166  -0.0330 -0.0377 853  GLN B OE1 
15528 N NE2 . GLN B 855  ? 0.2942 0.2667 0.2490 0.0166  -0.0381 -0.0398 853  GLN B NE2 
15529 N N   . GLU B 856  ? 0.2194 0.2053 0.1965 0.0155  -0.0514 -0.0399 854  GLU B N   
15530 C CA  . GLU B 856  ? 0.2485 0.2334 0.2229 0.0160  -0.0564 -0.0403 854  GLU B CA  
15531 C C   . GLU B 856  ? 0.2636 0.2433 0.2286 0.0173  -0.0566 -0.0391 854  GLU B C   
15532 O O   . GLU B 856  ? 0.2641 0.2438 0.2282 0.0186  -0.0596 -0.0382 854  GLU B O   
15533 C CB  . GLU B 856  ? 0.2933 0.2767 0.2664 0.0144  -0.0595 -0.0426 854  GLU B CB  
15534 C CG  . GLU B 856  ? 0.3077 0.2890 0.2762 0.0148  -0.0648 -0.0432 854  GLU B CG  
15535 C CD  . GLU B 856  ? 0.3873 0.3742 0.3629 0.0158  -0.0682 -0.0425 854  GLU B CD  
15536 O OE1 . GLU B 856  ? 0.3521 0.3451 0.3372 0.0153  -0.0672 -0.0425 854  GLU B OE1 
15537 O OE2 . GLU B 856  ? 0.3384 0.3237 0.3100 0.0171  -0.0719 -0.0421 854  GLU B OE2 
15538 N N   . ASP B 857  ? 0.2648 0.2402 0.2228 0.0172  -0.0534 -0.0390 855  ASP B N   
15539 C CA  . ASP B 857  ? 0.2995 0.2697 0.2477 0.0181  -0.0533 -0.0379 855  ASP B CA  
15540 C C   . ASP B 857  ? 0.2760 0.2469 0.2244 0.0191  -0.0523 -0.0354 855  ASP B C   
15541 O O   . ASP B 857  ? 0.3175 0.2843 0.2585 0.0198  -0.0536 -0.0342 855  ASP B O   
15542 C CB  . ASP B 857  ? 0.3549 0.3215 0.2967 0.0178  -0.0492 -0.0383 855  ASP B CB  
15543 N N   . VAL B 858  ? 0.2032 0.1785 0.1593 0.0192  -0.0500 -0.0345 856  VAL B N   
15544 C CA  . VAL B 858  ? 0.2502 0.2256 0.2063 0.0199  -0.0490 -0.0322 856  VAL B CA  
15545 C C   . VAL B 858  ? 0.1968 0.1761 0.1605 0.0209  -0.0515 -0.0320 856  VAL B C   
15546 O O   . VAL B 858  ? 0.2425 0.2216 0.2066 0.0217  -0.0510 -0.0303 856  VAL B O   
15547 C CB  . VAL B 858  ? 0.2458 0.2223 0.2028 0.0193  -0.0437 -0.0310 856  VAL B CB  
15548 C CG1 . VAL B 858  ? 0.2964 0.2690 0.2451 0.0188  -0.0410 -0.0308 856  VAL B CG1 
15549 C CG2 . VAL B 858  ? 0.2481 0.2296 0.2140 0.0187  -0.0415 -0.0320 856  VAL B CG2 
15550 N N   . ALA B 859  ? 0.2192 0.2022 0.1889 0.0208  -0.0543 -0.0337 857  ALA B N   
15551 C CA  . ALA B 859  ? 0.2171 0.2052 0.1953 0.0218  -0.0559 -0.0337 857  ALA B CA  
15552 C C   . ALA B 859  ? 0.2143 0.2005 0.1899 0.0238  -0.0594 -0.0325 857  ALA B C   
15553 O O   . ALA B 859  ? 0.2322 0.2201 0.2116 0.0251  -0.0589 -0.0315 857  ALA B O   
15554 C CB  . ALA B 859  ? 0.2378 0.2306 0.2227 0.0210  -0.0582 -0.0356 857  ALA B CB  
15555 N N   . ASP B 860  ? 0.2694 0.2516 0.2382 0.0243  -0.0630 -0.0327 858  ASP B N   
15556 C CA  . ASP B 860  ? 0.2548 0.2349 0.2212 0.0265  -0.0667 -0.0315 858  ASP B CA  
15557 C C   . ASP B 860  ? 0.2493 0.2249 0.2105 0.0270  -0.0643 -0.0292 858  ASP B C   
15558 O O   . ASP B 860  ? 0.2843 0.2600 0.2476 0.0289  -0.0656 -0.0282 858  ASP B O   
15559 C CB  . ASP B 860  ? 0.2711 0.2475 0.2306 0.0269  -0.0711 -0.0320 858  ASP B CB  
15560 C CG  . ASP B 860  ? 0.3557 0.3368 0.3209 0.0264  -0.0745 -0.0342 858  ASP B CG  
15561 O OD1 . ASP B 860  ? 0.3574 0.3451 0.3323 0.0269  -0.0750 -0.0349 858  ASP B OD1 
15562 O OD2 . ASP B 860  ? 0.3986 0.3770 0.3583 0.0254  -0.0767 -0.0353 858  ASP B OD2 
15563 N N   . ARG B 861  ? 0.2438 0.2154 0.1983 0.0255  -0.0609 -0.0283 859  ARG B N   
15564 C CA  A ARG B 861  ? 0.2657 0.2332 0.2153 0.0254  -0.0585 -0.0260 859  ARG B CA  
15565 C CA  B ARG B 861  ? 0.2655 0.2331 0.2152 0.0254  -0.0586 -0.0260 859  ARG B CA  
15566 C C   . ARG B 861  ? 0.2494 0.2206 0.2063 0.0254  -0.0557 -0.0255 859  ARG B C   
15567 O O   . ARG B 861  ? 0.2551 0.2240 0.2110 0.0263  -0.0561 -0.0240 859  ARG B O   
15568 C CB  A ARG B 861  ? 0.2915 0.2555 0.2335 0.0235  -0.0551 -0.0253 859  ARG B CB  
15569 C CB  B ARG B 861  ? 0.2916 0.2554 0.2334 0.0235  -0.0551 -0.0252 859  ARG B CB  
15570 C CG  A ARG B 861  ? 0.3246 0.2845 0.2609 0.0228  -0.0527 -0.0227 859  ARG B CG  
15571 C CG  B ARG B 861  ? 0.3413 0.3027 0.2802 0.0227  -0.0518 -0.0228 859  ARG B CG  
15572 C CD  A ARG B 861  ? 0.3944 0.3506 0.3218 0.0213  -0.0502 -0.0220 859  ARG B CD  
15573 C CD  B ARG B 861  ? 0.4009 0.3564 0.3289 0.0217  -0.0509 -0.0212 859  ARG B CD  
15574 N NE  A ARG B 861  ? 0.3801 0.3394 0.3096 0.0205  -0.0477 -0.0239 859  ARG B NE  
15575 N NE  B ARG B 861  ? 0.3912 0.3445 0.3169 0.0206  -0.0483 -0.0187 859  ARG B NE  
15576 C CZ  A ARG B 861  ? 0.3749 0.3379 0.3089 0.0195  -0.0433 -0.0240 859  ARG B CZ  
15577 C CZ  B ARG B 861  ? 0.3877 0.3437 0.3157 0.0190  -0.0436 -0.0181 859  ARG B CZ  
15578 N NH1 A ARG B 861  ? 0.3919 0.3566 0.3294 0.0189  -0.0409 -0.0225 859  ARG B NH1 
15579 N NH1 B ARG B 861  ? 0.3545 0.3150 0.2868 0.0184  -0.0409 -0.0197 859  ARG B NH1 
15580 N NH2 A ARG B 861  ? 0.3988 0.3635 0.3335 0.0191  -0.0414 -0.0258 859  ARG B NH2 
15581 N NH2 B ARG B 861  ? 0.3972 0.3511 0.3230 0.0177  -0.0419 -0.0158 859  ARG B NH2 
15582 N N   . ILE B 862  ? 0.2412 0.2177 0.2050 0.0244  -0.0530 -0.0268 860  ILE B N   
15583 C CA  . ILE B 862  ? 0.2161 0.1961 0.1866 0.0244  -0.0504 -0.0264 860  ILE B CA  
15584 C C   . ILE B 862  ? 0.2082 0.1909 0.1845 0.0266  -0.0535 -0.0269 860  ILE B C   
15585 O O   . ILE B 862  ? 0.2233 0.2055 0.2011 0.0275  -0.0528 -0.0259 860  ILE B O   
15586 C CB  . ILE B 862  ? 0.2089 0.1937 0.1850 0.0229  -0.0470 -0.0276 860  ILE B CB  
15587 C CG1 . ILE B 862  ? 0.2673 0.2494 0.2378 0.0212  -0.0433 -0.0268 860  ILE B CG1 
15588 C CG2 . ILE B 862  ? 0.2093 0.1985 0.1932 0.0231  -0.0451 -0.0275 860  ILE B CG2 
15589 C CD1 . ILE B 862  ? 0.2647 0.2503 0.2391 0.0200  -0.0403 -0.0280 860  ILE B CD1 
15590 N N   . LEU B 863  ? 0.2247 0.2102 0.2042 0.0276  -0.0571 -0.0284 861  LEU B N   
15591 C CA  . LEU B 863  ? 0.2437 0.2326 0.2292 0.0301  -0.0600 -0.0289 861  LEU B CA  
15592 C C   . LEU B 863  ? 0.2519 0.2354 0.2320 0.0323  -0.0625 -0.0273 861  LEU B C   
15593 O O   . LEU B 863  ? 0.2319 0.2164 0.2156 0.0343  -0.0628 -0.0271 861  LEU B O   
15594 C CB  . LEU B 863  ? 0.2489 0.2422 0.2388 0.0305  -0.0635 -0.0306 861  LEU B CB  
15595 C CG  . LEU B 863  ? 0.2994 0.2998 0.2981 0.0290  -0.0616 -0.0322 861  LEU B CG  
15596 C CD1 . LEU B 863  ? 0.3470 0.3504 0.3480 0.0284  -0.0650 -0.0338 861  LEU B CD1 
15597 C CD2 . LEU B 863  ? 0.3075 0.3132 0.3144 0.0305  -0.0606 -0.0323 861  LEU B CD2 
15598 N N   . THR B 864  ? 0.2435 0.2209 0.2147 0.0321  -0.0643 -0.0263 862  THR B N   
15599 C CA  . THR B 864  ? 0.2547 0.2257 0.2194 0.0339  -0.0667 -0.0246 862  THR B CA  
15600 C C   . THR B 864  ? 0.2463 0.2144 0.2098 0.0333  -0.0633 -0.0230 862  THR B C   
15601 O O   . THR B 864  ? 0.2515 0.2176 0.2155 0.0355  -0.0647 -0.0224 862  THR B O   
15602 C CB  . THR B 864  ? 0.3107 0.2752 0.2650 0.0331  -0.0683 -0.0235 862  THR B CB  
15603 O OG1 . THR B 864  ? 0.3280 0.2946 0.2830 0.0340  -0.0723 -0.0249 862  THR B OG1 
15604 C CG2 . THR B 864  ? 0.3269 0.2836 0.2733 0.0344  -0.0701 -0.0212 862  THR B CG2 
15605 N N   . MET B 865  ? 0.2293 0.1971 0.1910 0.0305  -0.0590 -0.0224 863  MET B N   
15606 C CA  . MET B 865  ? 0.2430 0.2084 0.2036 0.0294  -0.0559 -0.0209 863  MET B CA  
15607 C C   . MET B 865  ? 0.2116 0.1819 0.1808 0.0306  -0.0549 -0.0219 863  MET B C   
15608 O O   . MET B 865  ? 0.2453 0.2127 0.2138 0.0314  -0.0548 -0.0210 863  MET B O   
15609 C CB  . MET B 865  ? 0.2387 0.2044 0.1969 0.0262  -0.0515 -0.0203 863  MET B CB  
15610 C CG  . MET B 865  ? 0.2468 0.2093 0.2019 0.0246  -0.0487 -0.0184 863  MET B CG  
15611 S SD  . MET B 865  ? 0.3297 0.2943 0.2833 0.0212  -0.0435 -0.0178 863  MET B SD  
15612 C CE  . MET B 865  ? 0.3293 0.2899 0.2741 0.0209  -0.0450 -0.0175 863  MET B CE  
15613 N N   . LEU B 866  ? 0.2017 0.1792 0.1789 0.0307  -0.0542 -0.0238 864  LEU B N   
15614 C CA  . LEU B 866  ? 0.2120 0.1946 0.1974 0.0318  -0.0530 -0.0248 864  LEU B CA  
15615 C C   . LEU B 866  ? 0.2125 0.1945 0.1996 0.0353  -0.0565 -0.0251 864  LEU B C   
15616 O O   . LEU B 866  ? 0.2029 0.1842 0.1917 0.0365  -0.0557 -0.0249 864  LEU B O   
15617 C CB  . LEU B 866  ? 0.2072 0.1973 0.2001 0.0309  -0.0520 -0.0267 864  LEU B CB  
15618 C CG  . LEU B 866  ? 0.2578 0.2539 0.2594 0.0316  -0.0503 -0.0277 864  LEU B CG  
15619 C CD1 . LEU B 866  ? 0.2692 0.2639 0.2699 0.0301  -0.0464 -0.0267 864  LEU B CD1 
15620 C CD2 . LEU B 866  ? 0.2429 0.2455 0.2508 0.0304  -0.0496 -0.0292 864  LEU B CD2 
15621 N N   . LYS B 867  ? 0.2070 0.1889 0.1932 0.0371  -0.0606 -0.0256 865  LYS B N   
15622 C CA  . LYS B 867  ? 0.2064 0.1879 0.1942 0.0410  -0.0642 -0.0258 865  LYS B CA  
15623 C C   . LYS B 867  ? 0.2171 0.1897 0.1971 0.0420  -0.0649 -0.0240 865  LYS B C   
15624 O O   . LYS B 867  ? 0.2140 0.1856 0.1957 0.0446  -0.0656 -0.0241 865  LYS B O   
15625 C CB  . LYS B 867  ? 0.2337 0.2172 0.2222 0.0426  -0.0686 -0.0267 865  LYS B CB  
15626 C CG  . LYS B 867  ? 0.2546 0.2472 0.2518 0.0417  -0.0682 -0.0286 865  LYS B CG  
15627 C CD  . LYS B 867  ? 0.3057 0.3003 0.3032 0.0428  -0.0729 -0.0294 865  LYS B CD  
15628 C CE  . LYS B 867  ? 0.3079 0.3107 0.3133 0.0409  -0.0725 -0.0312 865  LYS B CE  
15629 N NZ  . LYS B 867  ? 0.3284 0.3323 0.3329 0.0412  -0.0770 -0.0320 865  LYS B NZ  
15630 N N   . GLY B 868  ? 0.2441 0.2101 0.2153 0.0397  -0.0645 -0.0222 866  GLY B N   
15631 C CA  . GLY B 868  ? 0.2394 0.1967 0.2028 0.0399  -0.0649 -0.0202 866  GLY B CA  
15632 C C   . GLY B 868  ? 0.2571 0.2139 0.2225 0.0389  -0.0615 -0.0199 866  GLY B C   
15633 O O   . GLY B 868  ? 0.2724 0.2241 0.2354 0.0408  -0.0627 -0.0193 866  GLY B O   
15634 N N   . ALA B 869  ? 0.2466 0.2084 0.2160 0.0361  -0.0574 -0.0204 867  ALA B N   
15635 C CA  . ALA B 869  ? 0.2350 0.1972 0.2068 0.0350  -0.0543 -0.0203 867  ALA B CA  
15636 C C   . ALA B 869  ? 0.2085 0.1746 0.1873 0.0382  -0.0550 -0.0220 867  ALA B C   
15637 O O   . ALA B 869  ? 0.2234 0.1862 0.2013 0.0390  -0.0544 -0.0217 867  ALA B O   
15638 C CB  . ALA B 869  ? 0.2334 0.2007 0.2083 0.0316  -0.0500 -0.0205 867  ALA B CB  
15639 N N   . LEU B 870  ? 0.1966 0.1697 0.1822 0.0401  -0.0563 -0.0238 868  LEU B N   
15640 C CA  . LEU B 870  ? 0.2084 0.1864 0.2012 0.0434  -0.0569 -0.0254 868  LEU B CA  
15641 C C   . LEU B 870  ? 0.2379 0.2098 0.2271 0.0471  -0.0599 -0.0251 868  LEU B C   
15642 O O   . LEU B 870  ? 0.2476 0.2197 0.2393 0.0491  -0.0592 -0.0259 868  LEU B O   
15643 C CB  . LEU B 870  ? 0.2298 0.2159 0.2297 0.0446  -0.0585 -0.0271 868  LEU B CB  
15644 C CG  . LEU B 870  ? 0.2772 0.2708 0.2861 0.0475  -0.0586 -0.0289 868  LEU B CG  
15645 C CD1 . LEU B 870  ? 0.3379 0.3379 0.3530 0.0451  -0.0545 -0.0297 868  LEU B CD1 
15646 C CD2 . LEU B 870  ? 0.3237 0.3223 0.3367 0.0498  -0.0623 -0.0299 868  LEU B CD2 
15647 N N   . HIS B 871  ? 0.2107 0.1767 0.1935 0.0482  -0.0634 -0.0240 869  HIS B N   
15648 C CA  . HIS B 871  ? 0.2468 0.2069 0.2262 0.0523  -0.0668 -0.0237 869  HIS B CA  
15649 C C   . HIS B 871  ? 0.2785 0.2292 0.2507 0.0513  -0.0658 -0.0222 869  HIS B C   
15650 O O   . HIS B 871  ? 0.3062 0.2510 0.2752 0.0548  -0.0683 -0.0221 869  HIS B O   
15651 C CB  . HIS B 871  ? 0.3146 0.2715 0.2895 0.0540  -0.0712 -0.0230 869  HIS B CB  
15652 C CG  . HIS B 871  ? 0.3550 0.3210 0.3378 0.0563  -0.0734 -0.0247 869  HIS B CG  
15653 N ND1 . HIS B 871  ? 0.3535 0.3247 0.3434 0.0606  -0.0749 -0.0264 869  HIS B ND1 
15654 C CD2 . HIS B 871  ? 0.3614 0.3324 0.3464 0.0547  -0.0743 -0.0252 869  HIS B CD2 
15655 C CE1 . HIS B 871  ? 0.3761 0.3556 0.3725 0.0614  -0.0766 -0.0276 869  HIS B CE1 
15656 N NE2 . HIS B 871  ? 0.4119 0.3911 0.4053 0.0578  -0.0764 -0.0270 869  HIS B NE2 
15657 N N   . GLU B 872  ? 0.2264 0.1757 0.1962 0.0469  -0.0622 -0.0212 870  GLU B N   
15658 C CA  . GLU B 872  ? 0.2443 0.1857 0.2080 0.0453  -0.0610 -0.0199 870  GLU B CA  
15659 C C   . GLU B 872  ? 0.2529 0.1977 0.2220 0.0455  -0.0583 -0.0213 870  GLU B C   
15660 O O   . GLU B 872  ? 0.2477 0.1863 0.2122 0.0439  -0.0572 -0.0204 870  GLU B O   
15661 C CB  . GLU B 872  ? 0.2471 0.1853 0.2051 0.0402  -0.0588 -0.0177 870  GLU B CB  
15662 C CG  . GLU B 872  ? 0.2771 0.2112 0.2287 0.0399  -0.0614 -0.0162 870  GLU B CG  
15663 C CD  . GLU B 872  ? 0.3126 0.2366 0.2564 0.0423  -0.0652 -0.0149 870  GLU B CD  
15664 O OE1 . GLU B 872  ? 0.3391 0.2571 0.2802 0.0428  -0.0652 -0.0145 870  GLU B OE1 
15665 O OE2 . GLU B 872  ? 0.3502 0.2716 0.2901 0.0438  -0.0684 -0.0142 870  GLU B OE2 
15666 N N   . LEU B 873  ? 0.2334 0.1877 0.2115 0.0471  -0.0571 -0.0233 871  LEU B N   
15667 C CA  . LEU B 873  ? 0.2195 0.1772 0.2024 0.0474  -0.0545 -0.0247 871  LEU B CA  
15668 C C   . LEU B 873  ? 0.2376 0.1917 0.2202 0.0523  -0.0566 -0.0258 871  LEU B C   
15669 O O   . LEU B 873  ? 0.2607 0.2145 0.2437 0.0563  -0.0599 -0.0263 871  LEU B O   
15670 C CB  . LEU B 873  ? 0.2184 0.1875 0.2109 0.0472  -0.0522 -0.0264 871  LEU B CB  
15671 C CG  . LEU B 873  ? 0.2916 0.2648 0.2853 0.0429  -0.0499 -0.0257 871  LEU B CG  
15672 C CD1 . LEU B 873  ? 0.2472 0.2309 0.2503 0.0431  -0.0481 -0.0274 871  LEU B CD1 
15673 C CD2 . LEU B 873  ? 0.2618 0.2314 0.2514 0.0389  -0.0470 -0.0243 871  LEU B CD2 
15674 N N   . HIS B 874  ? 0.2372 0.1889 0.2190 0.0520  -0.0547 -0.0263 872  HIS B N   
15675 C CA  . HIS B 874  ? 0.2467 0.1946 0.2278 0.0565  -0.0562 -0.0277 872  HIS B CA  
15676 C C   . HIS B 874  ? 0.2283 0.1854 0.2180 0.0582  -0.0536 -0.0300 872  HIS B C   
15677 O O   . HIS B 874  ? 0.2253 0.1853 0.2169 0.0550  -0.0503 -0.0301 872  HIS B O   
15678 C CB  . HIS B 874  ? 0.2494 0.1861 0.2219 0.0549  -0.0563 -0.0266 872  HIS B CB  
15679 C CG  . HIS B 874  ? 0.2960 0.2271 0.2664 0.0596  -0.0578 -0.0280 872  HIS B CG  
15680 N ND1 . HIS B 874  ? 0.4181 0.3526 0.3927 0.0656  -0.0599 -0.0297 872  HIS B ND1 
15681 C CD2 . HIS B 874  ? 0.3458 0.2684 0.3105 0.0594  -0.0577 -0.0281 872  HIS B CD2 
15682 C CE1 . HIS B 874  ? 0.4000 0.3280 0.3713 0.0691  -0.0608 -0.0309 872  HIS B CE1 
15683 N NE2 . HIS B 874  ? 0.3547 0.2750 0.3197 0.0654  -0.0595 -0.0299 872  HIS B NE2 
15684 N N   . ILE B 875  ? 0.2470 0.2086 0.2417 0.0633  -0.0552 -0.0317 873  ILE B N   
15685 C CA  . ILE B 875  ? 0.2302 0.2015 0.2334 0.0653  -0.0528 -0.0338 873  ILE B CA  
15686 C C   . ILE B 875  ? 0.2824 0.2494 0.2839 0.0701  -0.0534 -0.0354 873  ILE B C   
15687 O O   . ILE B 875  ? 0.2972 0.2595 0.2960 0.0745  -0.0568 -0.0356 873  ILE B O   
15688 C CB  . ILE B 875  ? 0.2625 0.2444 0.2742 0.0670  -0.0536 -0.0347 873  ILE B CB  
15689 C CG1 . ILE B 875  ? 0.3400 0.3266 0.3538 0.0621  -0.0523 -0.0336 873  ILE B CG1 
15690 C CG2 . ILE B 875  ? 0.2552 0.2464 0.2752 0.0698  -0.0514 -0.0369 873  ILE B CG2 
15691 C CD1 . ILE B 875  ? 0.3959 0.3766 0.4037 0.0605  -0.0551 -0.0318 873  ILE B CD1 
15692 N N   . GLY B 876  ? 0.2325 0.2010 0.2354 0.0696  -0.0503 -0.0365 874  GLY B N   
15693 C CA  . GLY B 876  ? 0.2641 0.2285 0.2651 0.0744  -0.0507 -0.0383 874  GLY B CA  
15694 C C   . GLY B 876  ? 0.2566 0.2228 0.2586 0.0730  -0.0471 -0.0395 874  GLY B C   
15695 O O   . GLY B 876  ? 0.2169 0.1887 0.2221 0.0685  -0.0441 -0.0389 874  GLY B O   
15696 N N   . ARG B 877  ? 0.2711 0.2322 0.2700 0.0771  -0.0473 -0.0412 875  ARG B N   
15697 C CA  . ARG B 877  ? 0.2576 0.2186 0.2558 0.0761  -0.0442 -0.0424 875  ARG B CA  
15698 C C   . ARG B 877  ? 0.2514 0.2056 0.2433 0.0699  -0.0435 -0.0406 875  ARG B C   
15699 O O   . ARG B 877  ? 0.2944 0.2387 0.2789 0.0684  -0.0459 -0.0391 875  ARG B O   
15700 C CB  . ARG B 877  ? 0.2842 0.2385 0.2782 0.0818  -0.0453 -0.0445 875  ARG B CB  
15701 C CG  . ARG B 877  ? 0.2882 0.2443 0.2826 0.0819  -0.0419 -0.0464 875  ARG B CG  
15702 C CD  . ARG B 877  ? 0.3534 0.3036 0.3441 0.0883  -0.0429 -0.0488 875  ARG B CD  
15703 N NE  . ARG B 877  ? 0.4128 0.3484 0.3926 0.0871  -0.0444 -0.0486 875  ARG B NE  
15704 C CZ  . ARG B 877  ? 0.4729 0.4002 0.4470 0.0920  -0.0455 -0.0506 875  ARG B CZ  
15705 N NH1 . ARG B 877  ? 0.3930 0.3270 0.3715 0.0966  -0.0444 -0.0520 875  ARG B NH1 
15706 N NH2 . ARG B 877  ? 0.4396 0.3533 0.4037 0.0899  -0.0470 -0.0503 875  ARG B NH2 
15707 N N   . THR B 878  ? 0.2405 0.2004 0.2355 0.0663  -0.0401 -0.0407 876  THR B N   
15708 C CA  . THR B 878  ? 0.2378 0.1950 0.2295 0.0600  -0.0391 -0.0387 876  THR B CA  
15709 C C   . THR B 878  ? 0.2800 0.2270 0.2635 0.0582  -0.0392 -0.0387 876  THR B C   
15710 O O   . THR B 878  ? 0.2885 0.2349 0.2703 0.0530  -0.0378 -0.0374 876  THR B O   
15711 C CB  . THR B 878  ? 0.2472 0.2152 0.2459 0.0569  -0.0356 -0.0386 876  THR B CB  
15712 O OG1 . THR B 878  ? 0.2661 0.2391 0.2684 0.0594  -0.0333 -0.0407 876  THR B OG1 
15713 C CG2 . THR B 878  ? 0.2658 0.2421 0.2712 0.0569  -0.0358 -0.0379 876  THR B CG2 
15714 N N   . ASP B 879  ? 0.3018 0.2404 0.2799 0.0622  -0.0411 -0.0401 877  ASP B N   
15715 C CA  . ASP B 879  ? 0.2833 0.2109 0.2528 0.0598  -0.0417 -0.0399 877  ASP B CA  
15716 C C   . ASP B 879  ? 0.3192 0.2358 0.2809 0.0578  -0.0449 -0.0378 877  ASP B C   
15717 O O   . ASP B 879  ? 0.3108 0.2160 0.2642 0.0575  -0.0466 -0.0380 877  ASP B O   
15718 C CB  . ASP B 879  ? 0.3471 0.2706 0.3139 0.0646  -0.0416 -0.0427 877  ASP B CB  
15719 C CG  . ASP B 879  ? 0.3664 0.2859 0.3319 0.0712  -0.0442 -0.0440 877  ASP B CG  
15720 O OD1 . ASP B 879  ? 0.4005 0.3250 0.3706 0.0731  -0.0454 -0.0433 877  ASP B OD1 
15721 O OD2 . ASP B 879  ? 0.3923 0.3034 0.3520 0.0747  -0.0452 -0.0459 877  ASP B OD2 
15722 N N   . ARG B 880  ? 0.2959 0.2153 0.2596 0.0563  -0.0458 -0.0359 878  ARG B N   
15723 C CA  . ARG B 880  ? 0.2834 0.1935 0.2399 0.0532  -0.0483 -0.0334 878  ARG B CA  
15724 C C   . ARG B 880  ? 0.2856 0.2020 0.2451 0.0476  -0.0466 -0.0311 878  ARG B C   
15725 O O   . ARG B 880  ? 0.2770 0.2036 0.2439 0.0480  -0.0452 -0.0312 878  ARG B O   
15726 C CB  . ARG B 880  ? 0.3226 0.2285 0.2772 0.0578  -0.0517 -0.0332 878  ARG B CB  
15727 C CG  . ARG B 880  ? 0.3549 0.2539 0.3061 0.0640  -0.0535 -0.0354 878  ARG B CG  
15728 C CD  . ARG B 880  ? 0.4688 0.3619 0.4168 0.0683  -0.0573 -0.0349 878  ARG B CD  
15729 N NE  . ARG B 880  ? 0.6406 0.5291 0.5868 0.0751  -0.0588 -0.0374 878  ARG B NE  
15730 C CZ  . ARG B 880  ? 0.6400 0.5191 0.5805 0.0795  -0.0624 -0.0373 878  ARG B CZ  
15731 N NH1 . ARG B 880  ? 0.6935 0.5662 0.6289 0.0776  -0.0652 -0.0347 878  ARG B NH1 
15732 N NH2 . ARG B 880  ? 0.6521 0.5278 0.5916 0.0860  -0.0634 -0.0398 878  ARG B NH2 
15733 N N   . LEU B 881  ? 0.2657 0.1758 0.2193 0.0423  -0.0468 -0.0291 879  LEU B N   
15734 C CA  . LEU B 881  ? 0.2563 0.1716 0.2120 0.0369  -0.0451 -0.0268 879  LEU B CA  
15735 C C   . LEU B 881  ? 0.2659 0.1842 0.2234 0.0377  -0.0461 -0.0256 879  LEU B C   
15736 O O   . LEU B 881  ? 0.2625 0.1887 0.2246 0.0351  -0.0442 -0.0247 879  LEU B O   
15737 C CB  . LEU B 881  ? 0.2930 0.1999 0.2413 0.0315  -0.0456 -0.0247 879  LEU B CB  
15738 C CG  . LEU B 881  ? 0.2647 0.1762 0.2142 0.0257  -0.0437 -0.0223 879  LEU B CG  
15739 C CD1 . LEU B 881  ? 0.2705 0.1913 0.2262 0.0237  -0.0405 -0.0231 879  LEU B CD1 
15740 C CD2 . LEU B 881  ? 0.2811 0.1827 0.2222 0.0211  -0.0451 -0.0200 879  LEU B CD2 
15741 N N   . SER B 882  ? 0.2459 0.1579 0.1997 0.0415  -0.0492 -0.0257 880  SER B N   
15742 C CA  . SER B 882  ? 0.2348 0.1485 0.1892 0.0424  -0.0507 -0.0245 880  SER B CA  
15743 C C   . SER B 882  ? 0.2502 0.1755 0.2139 0.0455  -0.0498 -0.0260 880  SER B C   
15744 O O   . SER B 882  ? 0.2653 0.1932 0.2302 0.0459  -0.0510 -0.0252 880  SER B O   
15745 C CB  . SER B 882  ? 0.2813 0.1844 0.2286 0.0458  -0.0547 -0.0240 880  SER B CB  
15746 O OG  . SER B 882  ? 0.3316 0.2346 0.2811 0.0518  -0.0558 -0.0265 880  SER B OG  
15747 N N   . VAL B 883  ? 0.2452 0.1771 0.2149 0.0477  -0.0479 -0.0282 881  VAL B N   
15748 C CA  . VAL B 883  ? 0.2366 0.1795 0.2151 0.0504  -0.0471 -0.0296 881  VAL B CA  
15749 C C   . VAL B 883  ? 0.2303 0.1816 0.2138 0.0461  -0.0443 -0.0288 881  VAL B C   
15750 O O   . VAL B 883  ? 0.2480 0.2007 0.2318 0.0427  -0.0417 -0.0286 881  VAL B O   
15751 C CB  . VAL B 883  ? 0.2465 0.1933 0.2296 0.0546  -0.0461 -0.0323 881  VAL B CB  
15752 C CG1 . VAL B 883  ? 0.2449 0.2042 0.2377 0.0560  -0.0445 -0.0335 881  VAL B CG1 
15753 C CG2 . VAL B 883  ? 0.2670 0.2063 0.2459 0.0600  -0.0492 -0.0333 881  VAL B CG2 
15754 N N   . ASP B 884  ? 0.2131 0.1699 0.2003 0.0463  -0.0449 -0.0285 882  ASP B N   
15755 C CA  . ASP B 884  ? 0.2043 0.1688 0.1960 0.0428  -0.0424 -0.0279 882  ASP B CA  
15756 C C   . ASP B 884  ? 0.2706 0.2455 0.2713 0.0444  -0.0406 -0.0297 882  ASP B C   
15757 O O   . ASP B 884  ? 0.2485 0.2291 0.2529 0.0415  -0.0378 -0.0296 882  ASP B O   
15758 C CB  . ASP B 884  ? 0.2191 0.1830 0.2091 0.0418  -0.0442 -0.0265 882  ASP B CB  
15759 C CG  . ASP B 884  ? 0.2537 0.2077 0.2347 0.0400  -0.0459 -0.0244 882  ASP B CG  
15760 O OD1 . ASP B 884  ? 0.2583 0.2094 0.2359 0.0361  -0.0441 -0.0232 882  ASP B OD1 
15761 O OD2 . ASP B 884  ? 0.2511 0.2002 0.2283 0.0423  -0.0491 -0.0240 882  ASP B OD2 
15762 N N   . VAL B 885  ? 0.2314 0.2091 0.2358 0.0489  -0.0422 -0.0312 883  VAL B N   
15763 C CA  . VAL B 885  ? 0.2219 0.2100 0.2351 0.0505  -0.0406 -0.0328 883  VAL B CA  
15764 C C   . VAL B 885  ? 0.1887 0.1772 0.2036 0.0552  -0.0410 -0.0347 883  VAL B C   
15765 O O   . VAL B 885  ? 0.2105 0.1943 0.2226 0.0590  -0.0440 -0.0351 883  VAL B O   
15766 C CB  . VAL B 885  ? 0.2520 0.2456 0.2694 0.0510  -0.0423 -0.0328 883  VAL B CB  
15767 C CG1 . VAL B 885  ? 0.2746 0.2791 0.3013 0.0520  -0.0406 -0.0343 883  VAL B CG1 
15768 C CG2 . VAL B 885  ? 0.2696 0.2620 0.2843 0.0466  -0.0419 -0.0311 883  VAL B CG2 
15769 N N   . GLY B 886  ? 0.1917 0.1853 0.2106 0.0552  -0.0380 -0.0359 884  GLY B N   
15770 C CA  . GLY B 886  ? 0.1934 0.1885 0.2144 0.0597  -0.0377 -0.0379 884  GLY B CA  
15771 C C   . GLY B 886  ? 0.1817 0.1877 0.2118 0.0623  -0.0372 -0.0392 884  GLY B C   
15772 O O   . GLY B 886  ? 0.1783 0.1896 0.2126 0.0612  -0.0381 -0.0387 884  GLY B O   
15773 N N   . PRO B 887  ? 0.1778 0.1876 0.2111 0.0656  -0.0356 -0.0411 885  PRO B N   
15774 C CA  . PRO B 887  ? 0.1797 0.2005 0.2220 0.0683  -0.0349 -0.0424 885  PRO B CA  
15775 C C   . PRO B 887  ? 0.1656 0.1955 0.2142 0.0644  -0.0316 -0.0421 885  PRO B C   
15776 O O   . PRO B 887  ? 0.1666 0.1947 0.2128 0.0604  -0.0294 -0.0412 885  PRO B O   
15777 C CB  . PRO B 887  ? 0.1717 0.1919 0.2136 0.0732  -0.0340 -0.0444 885  PRO B CB  
15778 C CG  . PRO B 887  ? 0.1811 0.1933 0.2159 0.0706  -0.0323 -0.0441 885  PRO B CG  
15779 C CD  . PRO B 887  ? 0.1929 0.1965 0.2211 0.0670  -0.0344 -0.0420 885  PRO B CD  
15780 N N   . VAL B 888  ? 0.1592 0.1993 0.2161 0.0656  -0.0315 -0.0428 886  VAL B N   
15781 C CA  . VAL B 888  ? 0.1471 0.1963 0.2105 0.0629  -0.0281 -0.0428 886  VAL B CA  
15782 C C   . VAL B 888  ? 0.1378 0.1905 0.2031 0.0657  -0.0252 -0.0444 886  VAL B C   
15783 O O   . VAL B 888  ? 0.1581 0.2074 0.2210 0.0703  -0.0261 -0.0457 886  VAL B O   
15784 C CB  . VAL B 888  ? 0.1492 0.2079 0.2207 0.0623  -0.0291 -0.0428 886  VAL B CB  
15785 C CG1 . VAL B 888  ? 0.1589 0.2135 0.2276 0.0594  -0.0318 -0.0413 886  VAL B CG1 
15786 C CG2 . VAL B 888  ? 0.1813 0.2456 0.2579 0.0676  -0.0308 -0.0443 886  VAL B CG2 
15787 N N   . ILE B 889  ? 0.1463 0.2051 0.2153 0.0629  -0.0216 -0.0443 887  ILE B N   
15788 C CA  . ILE B 889  ? 0.1471 0.2063 0.2149 0.0643  -0.0185 -0.0454 887  ILE B CA  
15789 C C   . ILE B 889  ? 0.1503 0.2163 0.2232 0.0696  -0.0178 -0.0474 887  ILE B C   
15790 O O   . ILE B 889  ? 0.1589 0.2215 0.2280 0.0725  -0.0166 -0.0486 887  ILE B O   
15791 C CB  . ILE B 889  ? 0.1557 0.2190 0.2254 0.0596  -0.0150 -0.0444 887  ILE B CB  
15792 C CG1 . ILE B 889  ? 0.1527 0.2154 0.2200 0.0607  -0.0118 -0.0455 887  ILE B CG1 
15793 C CG2 . ILE B 889  ? 0.1587 0.2328 0.2373 0.0578  -0.0140 -0.0441 887  ILE B CG2 
15794 C CD1 . ILE B 889  ? 0.1798 0.2314 0.2379 0.0608  -0.0127 -0.0455 887  ILE B CD1 
15795 N N   . THR B 890  ? 0.1669 0.2412 0.2467 0.0694  -0.0182 -0.0469 888  THR B N   
15796 C CA  . THR B 890  ? 0.1482 0.2288 0.2319 0.0722  -0.0168 -0.0474 888  THR B CA  
15797 C C   . THR B 890  ? 0.1616 0.2463 0.2496 0.0734  -0.0198 -0.0469 888  THR B C   
15798 O O   . THR B 890  ? 0.1659 0.2503 0.2551 0.0712  -0.0224 -0.0461 888  THR B O   
15799 C CB  . THR B 890  ? 0.1915 0.2816 0.2808 0.0697  -0.0126 -0.0470 888  THR B CB  
15800 O OG1 . THR B 890  ? 0.1726 0.2684 0.2673 0.0653  -0.0127 -0.0457 888  THR B OG1 
15801 C CG2 . THR B 890  ? 0.1703 0.2572 0.2554 0.0688  -0.0093 -0.0475 888  THR B CG2 
15802 N N   . SER B 891  ? 0.1766 0.2654 0.2672 0.0769  -0.0194 -0.0475 889  SER B N   
15803 C CA  . SER B 891  ? 0.1586 0.2533 0.2547 0.0779  -0.0218 -0.0470 889  SER B CA  
15804 C C   . SER B 891  ? 0.2288 0.3334 0.3327 0.0734  -0.0206 -0.0459 889  SER B C   
15805 O O   . SER B 891  ? 0.2039 0.3111 0.3110 0.0724  -0.0236 -0.0453 889  SER B O   
15806 C CB  . SER B 891  ? 0.2138 0.3116 0.3115 0.0827  -0.0212 -0.0478 889  SER B CB  
15807 O OG  . SER B 891  ? 0.3536 0.4583 0.4550 0.0823  -0.0167 -0.0481 889  SER B OG  
15808 N N   . GLU B 892  ? 0.1927 0.3024 0.2994 0.0706  -0.0166 -0.0456 890  GLU B N   
15809 C CA  . GLU B 892  ? 0.1870 0.3052 0.3005 0.0660  -0.0155 -0.0445 890  GLU B CA  
15810 C C   . GLU B 892  ? 0.2234 0.3375 0.3352 0.0623  -0.0178 -0.0438 890  GLU B C   
15811 O O   . GLU B 892  ? 0.2310 0.3497 0.3473 0.0597  -0.0196 -0.0431 890  GLU B O   
15812 C CB  . GLU B 892  ? 0.2524 0.3755 0.3680 0.0637  -0.0106 -0.0441 890  GLU B CB  
15813 N N   . ALA B 893  ? 0.1847 0.2904 0.2900 0.0619  -0.0179 -0.0441 891  ALA B N   
15814 C CA  . ALA B 893  ? 0.1799 0.2814 0.2833 0.0588  -0.0201 -0.0436 891  ALA B CA  
15815 C C   . ALA B 893  ? 0.2209 0.3199 0.3236 0.0605  -0.0248 -0.0435 891  ALA B C   
15816 O O   . ALA B 893  ? 0.2091 0.3100 0.3142 0.0577  -0.0268 -0.0430 891  ALA B O   
15817 C CB  . ALA B 893  ? 0.1858 0.2787 0.2823 0.0588  -0.0194 -0.0439 891  ALA B CB  
15818 N N   . LYS B 894  ? 0.1923 0.2866 0.2913 0.0652  -0.0267 -0.0442 892  LYS B N   
15819 C CA  . LYS B 894  ? 0.1927 0.2841 0.2905 0.0672  -0.0312 -0.0441 892  LYS B CA  
15820 C C   . LYS B 894  ? 0.2366 0.3373 0.3418 0.0661  -0.0324 -0.0437 892  LYS B C   
15821 O O   . LYS B 894  ? 0.2307 0.3312 0.3365 0.0646  -0.0356 -0.0432 892  LYS B O   
15822 C CB  . LYS B 894  ? 0.1864 0.2717 0.2792 0.0725  -0.0326 -0.0449 892  LYS B CB  
15823 C CG  . LYS B 894  ? 0.2085 0.2910 0.2999 0.0751  -0.0373 -0.0446 892  LYS B CG  
15824 C CD  . LYS B 894  ? 0.2214 0.2961 0.3067 0.0803  -0.0386 -0.0453 892  LYS B CD  
15825 C CE  . LYS B 894  ? 0.3374 0.4095 0.4213 0.0830  -0.0433 -0.0450 892  LYS B CE  
15826 N NZ  . LYS B 894  ? 0.4266 0.4894 0.5034 0.0877  -0.0449 -0.0454 892  LYS B NZ  
15827 N N   . ASP B 895  ? 0.1969 0.3060 0.3078 0.0668  -0.0297 -0.0438 893  ASP B N   
15828 C CA  . ASP B 895  ? 0.2226 0.3410 0.3410 0.0658  -0.0308 -0.0433 893  ASP B CA  
15829 C C   . ASP B 895  ? 0.2199 0.3420 0.3418 0.0601  -0.0308 -0.0425 893  ASP B C   
15830 O O   . ASP B 895  ? 0.2672 0.3927 0.3924 0.0588  -0.0338 -0.0421 893  ASP B O   
15831 C CB  . ASP B 895  ? 0.2541 0.3810 0.3781 0.0673  -0.0275 -0.0434 893  ASP B CB  
15832 C CG  . ASP B 895  ? 0.2684 0.3928 0.3900 0.0732  -0.0281 -0.0442 893  ASP B CG  
15833 O OD1 . ASP B 895  ? 0.3205 0.4373 0.4369 0.0760  -0.0316 -0.0446 893  ASP B OD1 
15834 O OD2 . ASP B 895  ? 0.3196 0.4495 0.4445 0.0751  -0.0250 -0.0445 893  ASP B OD2 
15835 N N   . ASN B 896  ? 0.2141 0.3356 0.3353 0.0568  -0.0276 -0.0422 894  ASN B N   
15836 C CA  . ASN B 896  ? 0.2145 0.3389 0.3387 0.0515  -0.0275 -0.0416 894  ASN B CA  
15837 C C   . ASN B 896  ? 0.2271 0.3448 0.3471 0.0504  -0.0314 -0.0416 894  ASN B C   
15838 O O   . ASN B 896  ? 0.2406 0.3613 0.3637 0.0473  -0.0334 -0.0413 894  ASN B O   
15839 C CB  . ASN B 896  ? 0.2503 0.3747 0.3739 0.0486  -0.0232 -0.0413 894  ASN B CB  
15840 C CG  . ASN B 896  ? 0.3575 0.4848 0.4842 0.0431  -0.0228 -0.0405 894  ASN B CG  
15841 O OD1 . ASN B 896  ? 0.3959 0.5175 0.5189 0.0410  -0.0235 -0.0405 894  ASN B OD1 
15842 N ND2 . ASN B 896  ? 0.4490 0.5851 0.5825 0.0407  -0.0217 -0.0399 894  ASN B ND2 
15843 N N   . ILE B 897  ? 0.2013 0.3099 0.3142 0.0527  -0.0325 -0.0420 895  ILE B N   
15844 C CA  . ILE B 897  ? 0.2450 0.3469 0.3534 0.0521  -0.0363 -0.0419 895  ILE B CA  
15845 C C   . ILE B 897  ? 0.2740 0.3771 0.3834 0.0540  -0.0406 -0.0419 895  ILE B C   
15846 O O   . ILE B 897  ? 0.2072 0.3099 0.3167 0.0517  -0.0435 -0.0417 895  ILE B O   
15847 C CB  . ILE B 897  ? 0.1888 0.2804 0.2889 0.0542  -0.0363 -0.0419 895  ILE B CB  
15848 C CG1 . ILE B 897  ? 0.1995 0.2886 0.2970 0.0511  -0.0319 -0.0413 895  ILE B CG1 
15849 C CG2 . ILE B 897  ? 0.2125 0.2952 0.3053 0.0531  -0.0397 -0.0410 895  ILE B CG2 
15850 C CD1 . ILE B 897  ? 0.1792 0.2594 0.2690 0.0533  -0.0310 -0.0413 895  ILE B CD1 
15851 N N   . GLU B 898  ? 0.2407 0.3449 0.3506 0.0582  -0.0412 -0.0422 896  GLU B N   
15852 C CA  . GLU B 898  ? 0.2667 0.3719 0.3774 0.0604  -0.0454 -0.0421 896  GLU B CA  
15853 C C   . GLU B 898  ? 0.2933 0.4082 0.4117 0.0575  -0.0459 -0.0418 896  GLU B C   
15854 O O   . GLU B 898  ? 0.2727 0.3878 0.3913 0.0571  -0.0499 -0.0416 896  GLU B O   
15855 C CB  . GLU B 898  ? 0.2570 0.3608 0.3662 0.0658  -0.0456 -0.0425 896  GLU B CB  
15856 C CG  . GLU B 898  ? 0.2613 0.3537 0.3617 0.0688  -0.0470 -0.0427 896  GLU B CG  
15857 C CD  . GLU B 898  ? 0.3684 0.4584 0.4667 0.0741  -0.0470 -0.0432 896  GLU B CD  
15858 O OE1 . GLU B 898  ? 0.4008 0.4986 0.5048 0.0756  -0.0449 -0.0435 896  GLU B OE1 
15859 O OE2 . GLU B 898  ? 0.4404 0.5206 0.5312 0.0768  -0.0490 -0.0432 896  GLU B OE2 
15860 N N   . LYS B 899  ? 0.2562 0.3791 0.3808 0.0552  -0.0421 -0.0416 897  LYS B N   
15861 C CA  . LYS B 899  ? 0.2591 0.3909 0.3909 0.0517  -0.0427 -0.0411 897  LYS B CA  
15862 C C   . LYS B 899  ? 0.2924 0.4214 0.4227 0.0474  -0.0450 -0.0410 897  LYS B C   
15863 O O   . LYS B 899  ? 0.3221 0.4549 0.4556 0.0455  -0.0479 -0.0408 897  LYS B O   
15864 C CB  . LYS B 899  ? 0.3010 0.4408 0.4389 0.0495  -0.0380 -0.0407 897  LYS B CB  
15865 C CG  . LYS B 899  ? 0.3649 0.5140 0.5104 0.0454  -0.0385 -0.0401 897  LYS B CG  
15866 C CD  . LYS B 899  ? 0.4055 0.5631 0.5572 0.0438  -0.0340 -0.0394 897  LYS B CD  
15867 C CE  . LYS B 899  ? 0.4782 0.6346 0.6293 0.0390  -0.0308 -0.0390 897  LYS B CE  
15868 N NZ  . LYS B 899  ? 0.5070 0.6730 0.6653 0.0360  -0.0275 -0.0381 897  LYS B NZ  
15869 N N   . HIS B 900  ? 0.2367 0.3587 0.3618 0.0458  -0.0439 -0.0412 898  HIS B N   
15870 C CA  . HIS B 900  ? 0.2631 0.3816 0.3860 0.0420  -0.0461 -0.0412 898  HIS B CA  
15871 C C   . HIS B 900  ? 0.2742 0.3866 0.3919 0.0440  -0.0511 -0.0414 898  HIS B C   
15872 O O   . HIS B 900  ? 0.2602 0.3732 0.3784 0.0415  -0.0543 -0.0415 898  HIS B O   
15873 C CB  . HIS B 900  ? 0.2385 0.3517 0.3576 0.0401  -0.0433 -0.0413 898  HIS B CB  
15874 C CG  . HIS B 900  ? 0.2392 0.3457 0.3529 0.0363  -0.0449 -0.0408 898  HIS B CG  
15875 N ND1 . HIS B 900  ? 0.2251 0.3346 0.3419 0.0316  -0.0449 -0.0407 898  HIS B ND1 
15876 C CD2 . HIS B 900  ? 0.2369 0.3330 0.3416 0.0365  -0.0462 -0.0403 898  HIS B CD2 
15877 C CE1 . HIS B 900  ? 0.2035 0.3047 0.3132 0.0293  -0.0460 -0.0403 898  HIS B CE1 
15878 N NE2 . HIS B 900  ? 0.2407 0.3341 0.3432 0.0322  -0.0467 -0.0400 898  HIS B NE2 
15879 N N   . ILE B 901  ? 0.2486 0.3545 0.3607 0.0483  -0.0520 -0.0415 899  ILE B N   
15880 C CA  . ILE B 901  ? 0.2432 0.3423 0.3492 0.0503  -0.0567 -0.0414 899  ILE B CA  
15881 C C   . ILE B 901  ? 0.3115 0.4156 0.4211 0.0512  -0.0601 -0.0413 899  ILE B C   
15882 O O   . ILE B 901  ? 0.2808 0.3823 0.3878 0.0501  -0.0640 -0.0413 899  ILE B O   
15883 C CB  . ILE B 901  ? 0.2636 0.3548 0.3632 0.0548  -0.0568 -0.0413 899  ILE B CB  
15884 C CG1 . ILE B 901  ? 0.2269 0.3115 0.3212 0.0530  -0.0531 -0.0409 899  ILE B CG1 
15885 C CG2 . ILE B 901  ? 0.2683 0.3524 0.3613 0.0570  -0.0617 -0.0410 899  ILE B CG2 
15886 C CD1 . ILE B 901  ? 0.2437 0.3195 0.3306 0.0565  -0.0530 -0.0405 899  ILE B CD1 
15887 N N   . GLU B 902  ? 0.2879 0.3994 0.4034 0.0532  -0.0587 -0.0413 900  GLU B N   
15888 C CA  . GLU B 902  ? 0.2635 0.3808 0.3832 0.0541  -0.0619 -0.0411 900  GLU B CA  
15889 C C   . GLU B 902  ? 0.3221 0.4460 0.4473 0.0490  -0.0627 -0.0410 900  GLU B C   
15890 O O   . GLU B 902  ? 0.3755 0.5005 0.5010 0.0484  -0.0667 -0.0409 900  GLU B O   
15891 C CB  . GLU B 902  ? 0.3492 0.4731 0.4741 0.0577  -0.0599 -0.0411 900  GLU B CB  
15892 C CG  . GLU B 902  ? 0.3721 0.4889 0.4913 0.0632  -0.0603 -0.0413 900  GLU B CG  
15893 C CD  . GLU B 902  ? 0.4294 0.5380 0.5416 0.0651  -0.0652 -0.0410 900  GLU B CD  
15894 O OE1 . GLU B 902  ? 0.4425 0.5546 0.5570 0.0653  -0.0687 -0.0408 900  GLU B OE1 
15895 O OE2 . GLU B 902  ? 0.4375 0.5362 0.5417 0.0662  -0.0656 -0.0410 900  GLU B OE2 
15896 N N   . ARG B 903  ? 0.2760 0.4037 0.4049 0.0451  -0.0590 -0.0410 901  ARG B N   
15897 C CA  . ARG B 903  ? 0.3426 0.4752 0.4758 0.0398  -0.0597 -0.0409 901  ARG B CA  
15898 C C   . ARG B 903  ? 0.3782 0.5033 0.5052 0.0376  -0.0634 -0.0413 901  ARG B C   
15899 O O   . ARG B 903  ? 0.3555 0.4830 0.4842 0.0349  -0.0666 -0.0414 901  ARG B O   
15900 C CB  . ARG B 903  ? 0.3631 0.4996 0.5003 0.0362  -0.0549 -0.0408 901  ARG B CB  
15901 C CG  . ARG B 903  ? 0.4174 0.5599 0.5600 0.0306  -0.0552 -0.0405 901  ARG B CG  
15902 C CD  . ARG B 903  ? 0.5143 0.6553 0.6567 0.0266  -0.0515 -0.0405 901  ARG B CD  
15903 N NE  . ARG B 903  ? 0.6557 0.8023 0.8034 0.0211  -0.0514 -0.0402 901  ARG B NE  
15904 C CZ  . ARG B 903  ? 0.6259 0.7692 0.7721 0.0166  -0.0504 -0.0404 901  ARG B CZ  
15905 N NH1 . ARG B 903  ? 0.6235 0.7586 0.7635 0.0171  -0.0494 -0.0410 901  ARG B NH1 
15906 N NH2 . ARG B 903  ? 0.6437 0.7920 0.7948 0.0116  -0.0504 -0.0401 901  ARG B NH2 
15907 N N   . MET B 904  ? 0.3671 0.4831 0.4867 0.0386  -0.0630 -0.0416 902  MET B N   
15908 C CA  . MET B 904  ? 0.3642 0.4725 0.4770 0.0370  -0.0665 -0.0419 902  MET B CA  
15909 C C   . MET B 904  ? 0.3997 0.5052 0.5088 0.0399  -0.0713 -0.0418 902  MET B C   
15910 O O   . MET B 904  ? 0.3379 0.4417 0.4447 0.0378  -0.0749 -0.0420 902  MET B O   
15911 C CB  . MET B 904  ? 0.3059 0.4051 0.4113 0.0374  -0.0643 -0.0417 902  MET B CB  
15912 C CG  . MET B 904  ? 0.3441 0.4438 0.4508 0.0340  -0.0590 -0.0414 902  MET B CG  
15913 S SD  . MET B 904  ? 0.3917 0.4931 0.5005 0.0275  -0.0589 -0.0416 902  MET B SD  
15914 C CE  . MET B 904  ? 0.3911 0.5065 0.5128 0.0263  -0.0570 -0.0421 902  MET B CE  
15915 N N   . ARG B 905  ? 0.4020 0.5062 0.5097 0.0449  -0.0715 -0.0414 903  ARG B N   
15916 C CA  . ARG B 905  ? 0.3777 0.4789 0.4817 0.0480  -0.0760 -0.0410 903  ARG B CA  
15917 C C   . ARG B 905  ? 0.4124 0.5219 0.5227 0.0467  -0.0786 -0.0410 903  ARG B C   
15918 O O   . ARG B 905  ? 0.4449 0.5519 0.5518 0.0468  -0.0830 -0.0409 903  ARG B O   
15919 C CB  . ARG B 905  ? 0.4121 0.5106 0.5141 0.0536  -0.0754 -0.0407 903  ARG B CB  
15920 C CG  . ARG B 905  ? 0.4381 0.5292 0.5327 0.0569  -0.0799 -0.0402 903  ARG B CG  
15921 C CD  . ARG B 905  ? 0.4732 0.5634 0.5675 0.0623  -0.0797 -0.0399 903  ARG B CD  
15922 N NE  . ARG B 905  ? 0.3461 0.4323 0.4382 0.0639  -0.0759 -0.0401 903  ARG B NE  
15923 C CZ  . ARG B 905  ? 0.3791 0.4549 0.4625 0.0656  -0.0765 -0.0396 903  ARG B CZ  
15924 N NH1 . ARG B 905  ? 0.3739 0.4419 0.4497 0.0658  -0.0804 -0.0390 903  ARG B NH1 
15925 N NH2 . ARG B 905  ? 0.3261 0.3991 0.4082 0.0669  -0.0731 -0.0398 903  ARG B NH2 
15926 N N   . GLY B 906  ? 0.3705 0.4899 0.4898 0.0455  -0.0758 -0.0409 904  GLY B N   
15927 C CA  . GLY B 906  ? 0.4510 0.5793 0.5772 0.0438  -0.0780 -0.0407 904  GLY B CA  
15928 C C   . GLY B 906  ? 0.4175 0.5451 0.5427 0.0386  -0.0806 -0.0410 904  GLY B C   
15929 O O   . GLY B 906  ? 0.3712 0.5032 0.4991 0.0376  -0.0841 -0.0409 904  GLY B O   
15930 N N   . LEU B 907  ? 0.4009 0.5229 0.5221 0.0354  -0.0791 -0.0416 905  LEU B N   
15931 C CA  . LEU B 907  ? 0.3997 0.5194 0.5187 0.0305  -0.0813 -0.0421 905  LEU B CA  
15932 C C   . LEU B 907  ? 0.3407 0.4507 0.4500 0.0315  -0.0855 -0.0424 905  LEU B C   
15933 O O   . LEU B 907  ? 0.4782 0.5845 0.5838 0.0278  -0.0875 -0.0430 905  LEU B O   
15934 C CB  . LEU B 907  ? 0.4294 0.5475 0.5486 0.0265  -0.0776 -0.0426 905  LEU B CB  
15935 C CG  . LEU B 907  ? 0.4181 0.5453 0.5463 0.0246  -0.0732 -0.0422 905  LEU B CG  
15936 C CD1 . LEU B 907  ? 0.4434 0.5677 0.5708 0.0213  -0.0695 -0.0426 905  LEU B CD1 
15937 C CD2 . LEU B 907  ? 0.4339 0.5702 0.5695 0.0215  -0.0749 -0.0418 905  LEU B CD2 
15938 N N   . GLY B 908  ? 0.3826 0.4879 0.4870 0.0365  -0.0869 -0.0419 906  GLY B N   
15939 C CA  . GLY B 908  ? 0.3530 0.4491 0.4478 0.0377  -0.0909 -0.0418 906  GLY B CA  
15940 C C   . GLY B 908  ? 0.4195 0.5056 0.5055 0.0372  -0.0898 -0.0421 906  GLY B C   
15941 O O   . GLY B 908  ? 0.4013 0.4796 0.4787 0.0372  -0.0929 -0.0420 906  GLY B O   
15942 N N   . ARG B 909  ? 0.3960 0.4823 0.4839 0.0368  -0.0854 -0.0422 907  ARG B N   
15943 C CA  . ARG B 909  ? 0.2737 0.3501 0.3527 0.0358  -0.0830 -0.0418 907  ARG B CA  
15944 C C   . ARG B 909  ? 0.2943 0.3636 0.3664 0.0402  -0.0833 -0.0408 907  ARG B C   
15945 O O   . ARG B 909  ? 0.3452 0.4183 0.4214 0.0443  -0.0839 -0.0407 907  ARG B O   
15946 C CB  . ARG B 909  ? 0.3392 0.4178 0.4219 0.0331  -0.0773 -0.0418 907  ARG B CB  
15947 C CG  . ARG B 909  ? 0.4043 0.4910 0.4951 0.0291  -0.0775 -0.0427 907  ARG B CG  
15948 C CD  . ARG B 909  ? 0.4340 0.5231 0.5286 0.0262  -0.0723 -0.0426 907  ARG B CD  
15949 N NE  . ARG B 909  ? 0.4913 0.5828 0.5886 0.0212  -0.0729 -0.0433 907  ARG B NE  
15950 C CZ  . ARG B 909  ? 0.5184 0.6150 0.6219 0.0180  -0.0697 -0.0433 907  ARG B CZ  
15951 N NH1 . ARG B 909  ? 0.4541 0.5550 0.5622 0.0193  -0.0656 -0.0428 907  ARG B NH1 
15952 N NH2 . ARG B 909  ? 0.4360 0.5333 0.5407 0.0133  -0.0707 -0.0439 907  ARG B NH2 
15953 N N   . LYS B 910  ? 0.2516 0.3104 0.3130 0.0393  -0.0830 -0.0400 908  LYS B N   
15954 C CA  . LYS B 910  ? 0.2987 0.3497 0.3525 0.0429  -0.0835 -0.0388 908  LYS B CA  
15955 C C   . LYS B 910  ? 0.3241 0.3744 0.3791 0.0441  -0.0787 -0.0382 908  LYS B C   
15956 O O   . LYS B 910  ? 0.3043 0.3534 0.3589 0.0411  -0.0743 -0.0381 908  LYS B O   
15957 C CB  . LYS B 910  ? 0.3152 0.3557 0.3573 0.0412  -0.0840 -0.0379 908  LYS B CB  
15958 C CG  . LYS B 910  ? 0.4092 0.4484 0.4477 0.0406  -0.0892 -0.0384 908  LYS B CG  
15959 C CD  . LYS B 910  ? 0.4775 0.5057 0.5034 0.0396  -0.0893 -0.0373 908  LYS B CD  
15960 C CE  . LYS B 910  ? 0.4829 0.5040 0.5023 0.0427  -0.0884 -0.0356 908  LYS B CE  
15961 N NZ  . LYS B 910  ? 0.5672 0.5782 0.5743 0.0421  -0.0895 -0.0344 908  LYS B NZ  
15962 N N   . VAL B 911  ? 0.3083 0.3591 0.3646 0.0486  -0.0797 -0.0379 909  VAL B N   
15963 C CA  . VAL B 911  ? 0.2426 0.2930 0.3003 0.0503  -0.0758 -0.0376 909  VAL B CA  
15964 C C   . VAL B 911  ? 0.2942 0.3349 0.3430 0.0535  -0.0770 -0.0364 909  VAL B C   
15965 O O   . VAL B 911  ? 0.3478 0.3878 0.3957 0.0572  -0.0812 -0.0363 909  VAL B O   
15966 C CB  . VAL B 911  ? 0.2777 0.3385 0.3461 0.0530  -0.0755 -0.0387 909  VAL B CB  
15967 C CG1 . VAL B 911  ? 0.2727 0.3323 0.3415 0.0550  -0.0716 -0.0386 909  VAL B CG1 
15968 C CG2 . VAL B 911  ? 0.2752 0.3457 0.3524 0.0494  -0.0744 -0.0397 909  VAL B CG2 
15969 N N   . GLU B 912  ? 0.2834 0.3168 0.3259 0.0519  -0.0735 -0.0354 910  GLU B N   
15970 C CA  . GLU B 912  ? 0.3094 0.3332 0.3434 0.0541  -0.0739 -0.0341 910  GLU B CA  
15971 C C   . GLU B 912  ? 0.3414 0.3658 0.3781 0.0559  -0.0706 -0.0342 910  GLU B C   
15972 O O   . GLU B 912  ? 0.2681 0.2955 0.3080 0.0534  -0.0664 -0.0346 910  GLU B O   
15973 C CB  . GLU B 912  ? 0.3428 0.3580 0.3673 0.0507  -0.0724 -0.0327 910  GLU B CB  
15974 C CG  . GLU B 912  ? 0.3202 0.3250 0.3351 0.0522  -0.0733 -0.0310 910  GLU B CG  
15975 C CD  . GLU B 912  ? 0.3586 0.3591 0.3679 0.0542  -0.0785 -0.0304 910  GLU B CD  
15976 O OE1 . GLU B 912  ? 0.3879 0.3931 0.4001 0.0537  -0.0811 -0.0312 910  GLU B OE1 
15977 O OE2 . GLU B 912  ? 0.4015 0.3938 0.4035 0.0562  -0.0801 -0.0290 910  GLU B OE2 
15978 N N   . GLN B 913  ? 0.3100 0.3310 0.3447 0.0604  -0.0726 -0.0340 911  GLN B N   
15979 C CA  . GLN B 913  ? 0.2867 0.3072 0.3229 0.0625  -0.0698 -0.0344 911  GLN B CA  
15980 C C   . GLN B 913  ? 0.3524 0.3619 0.3795 0.0650  -0.0713 -0.0332 911  GLN B C   
15981 O O   . GLN B 913  ? 0.3539 0.3590 0.3767 0.0674  -0.0756 -0.0325 911  GLN B O   
15982 C CB  . GLN B 913  ? 0.2828 0.3132 0.3290 0.0663  -0.0704 -0.0361 911  GLN B CB  
15983 C CG  . GLN B 913  ? 0.3118 0.3532 0.3675 0.0636  -0.0679 -0.0372 911  GLN B CG  
15984 C CD  . GLN B 913  ? 0.3491 0.4004 0.4144 0.0673  -0.0677 -0.0387 911  GLN B CD  
15985 O OE1 . GLN B 913  ? 0.3602 0.4141 0.4278 0.0711  -0.0710 -0.0391 911  GLN B OE1 
15986 N NE2 . GLN B 913  ? 0.2721 0.3288 0.3426 0.0659  -0.0633 -0.0394 911  GLN B NE2 
15987 N N   . ILE B 914  ? 0.3280 0.3326 0.3519 0.0642  -0.0680 -0.0328 912  ILE B N   
15988 C CA  . ILE B 914  ? 0.3337 0.3282 0.3499 0.0668  -0.0694 -0.0319 912  ILE B CA  
15989 C C   . ILE B 914  ? 0.4178 0.4150 0.4382 0.0728  -0.0714 -0.0332 912  ILE B C   
15990 O O   . ILE B 914  ? 0.3704 0.3768 0.3996 0.0742  -0.0695 -0.0349 912  ILE B O   
15991 C CB  . ILE B 914  ? 0.4325 0.4215 0.4444 0.0640  -0.0655 -0.0312 912  ILE B CB  
15992 C CG1 . ILE B 914  ? 0.3947 0.3863 0.4071 0.0584  -0.0622 -0.0307 912  ILE B CG1 
15993 C CG2 . ILE B 914  ? 0.4353 0.4116 0.4365 0.0645  -0.0672 -0.0295 912  ILE B CG2 
15994 C CD1 . ILE B 914  ? 0.3423 0.3299 0.3517 0.0557  -0.0584 -0.0301 912  ILE B CD1 
15995 N N   . GLY B 915  ? 0.3952 0.3844 0.4093 0.0764  -0.0751 -0.0325 913  GLY B N   
15996 C CA  . GLY B 915  ? 0.4169 0.4069 0.4338 0.0826  -0.0768 -0.0337 913  GLY B CA  
15997 C C   . GLY B 915  ? 0.4202 0.4056 0.4349 0.0832  -0.0735 -0.0343 913  GLY B C   
15998 O O   . GLY B 915  ? 0.4955 0.4715 0.5022 0.0802  -0.0722 -0.0330 913  GLY B O   
15999 N N   . LEU B 916  ? 0.3769 0.3696 0.3990 0.0869  -0.0722 -0.0363 914  LEU B N   
16000 C CA  . LEU B 916  ? 0.4031 0.3924 0.4237 0.0879  -0.0691 -0.0372 914  LEU B CA  
16001 C C   . LEU B 916  ? 0.4494 0.4300 0.4643 0.0933  -0.0717 -0.0374 914  LEU B C   
16002 O O   . LEU B 916  ? 0.4467 0.4299 0.4633 0.0963  -0.0738 -0.0376 914  LEU B O   
16003 C CB  . LEU B 916  ? 0.3823 0.3838 0.4132 0.0886  -0.0656 -0.0392 914  LEU B CB  
16004 C CG  . LEU B 916  ? 0.3787 0.3891 0.4156 0.0830  -0.0624 -0.0391 914  LEU B CG  
16005 C CD1 . LEU B 916  ? 0.4013 0.4225 0.4474 0.0842  -0.0589 -0.0409 914  LEU B CD1 
16006 C CD2 . LEU B 916  ? 0.3934 0.3965 0.4235 0.0773  -0.0600 -0.0375 914  LEU B CD2 
16007 N N   . ALA B 917  ? 0.3597 0.3298 0.3671 0.0931  -0.0707 -0.0372 915  ALA B N   
16008 C CA  . ALA B 917  ? 0.3817 0.3425 0.3826 0.0972  -0.0723 -0.0374 915  ALA B CA  
16009 C C   . ALA B 917  ? 0.4168 0.3857 0.4242 0.1005  -0.0698 -0.0396 915  ALA B C   
16010 O O   . ALA B 917  ? 0.4055 0.3846 0.4207 0.0994  -0.0663 -0.0408 915  ALA B O   
16011 C CB  . ALA B 917  ? 0.4610 0.4085 0.4523 0.0955  -0.0717 -0.0366 915  ALA B CB  
16012 N N   . SER B 918  ? 0.4322 0.3962 0.4359 0.1048  -0.0717 -0.0398 916  SER B N   
16013 C CA  . SER B 918  ? 0.4709 0.4425 0.4806 0.1085  -0.0697 -0.0418 916  SER B CA  
16014 C C   . SER B 918  ? 0.4040 0.3746 0.4131 0.1081  -0.0657 -0.0432 916  SER B C   
16015 O O   . SER B 918  ? 0.4108 0.3906 0.4267 0.1099  -0.0629 -0.0448 916  SER B O   
16016 C CB  . SER B 918  ? 0.5097 0.4751 0.5148 0.1133  -0.0727 -0.0417 916  SER B CB  
16017 O OG  . SER B 918  ? 0.5888 0.5391 0.5827 0.1138  -0.0739 -0.0412 916  SER B OG  
16018 N N   . GLU B 919  ? 0.4588 0.4186 0.4601 0.1056  -0.0655 -0.0426 917  GLU B N   
16019 C CA  . GLU B 919  ? 0.4383 0.3967 0.4386 0.1050  -0.0619 -0.0440 917  GLU B CA  
16020 C C   . GLU B 919  ? 0.3979 0.3690 0.4074 0.1023  -0.0580 -0.0448 917  GLU B C   
16021 O O   . GLU B 919  ? 0.3782 0.3510 0.3886 0.1023  -0.0546 -0.0462 917  GLU B O   
16022 C CB  . GLU B 919  ? 0.4140 0.3582 0.4041 0.1022  -0.0628 -0.0429 917  GLU B CB  
16023 C CG  . GLU B 919  ? 0.5550 0.4849 0.5346 0.1045  -0.0658 -0.0423 917  GLU B CG  
16024 C CD  . GLU B 919  ? 0.6575 0.5817 0.6328 0.1046  -0.0701 -0.0402 917  GLU B CD  
16025 O OE1 . GLU B 919  ? 0.5754 0.5057 0.5550 0.1024  -0.0708 -0.0391 917  GLU B OE1 
16026 O OE2 . GLU B 919  ? 0.6700 0.5834 0.6372 0.1068  -0.0728 -0.0396 917  GLU B OE2 
16027 N N   . THR B 920  ? 0.3623 0.3421 0.3783 0.0999  -0.0583 -0.0440 918  THR B N   
16028 C CA  . THR B 920  ? 0.3367 0.3283 0.3613 0.0971  -0.0546 -0.0447 918  THR B CA  
16029 C C   . THR B 920  ? 0.3132 0.3170 0.3464 0.0994  -0.0522 -0.0460 918  THR B C   
16030 O O   . THR B 920  ? 0.2985 0.3112 0.3379 0.0973  -0.0486 -0.0467 918  THR B O   
16031 C CB  . THR B 920  ? 0.3314 0.3276 0.3596 0.0935  -0.0559 -0.0434 918  THR B CB  
16032 O OG1 . THR B 920  ? 0.3250 0.3248 0.3557 0.0952  -0.0590 -0.0428 918  THR B OG1 
16033 C CG2 . THR B 920  ? 0.3400 0.3250 0.3595 0.0898  -0.0572 -0.0416 918  THR B CG2 
16034 N N   . GLY B 921  ? 0.2898 0.2942 0.3234 0.1036  -0.0541 -0.0463 919  GLY B N   
16035 C CA  . GLY B 921  ? 0.3294 0.3455 0.3714 0.1059  -0.0519 -0.0474 919  GLY B CA  
16036 C C   . GLY B 921  ? 0.3354 0.3539 0.3784 0.1067  -0.0476 -0.0489 919  GLY B C   
16037 O O   . GLY B 921  ? 0.3003 0.3302 0.3512 0.1071  -0.0448 -0.0496 919  GLY B O   
16038 N N   . VAL B 922  ? 0.2803 0.2880 0.3151 0.1068  -0.0471 -0.0494 920  VAL B N   
16039 C CA  . VAL B 922  ? 0.2780 0.2872 0.3128 0.1076  -0.0432 -0.0509 920  VAL B CA  
16040 C C   . VAL B 922  ? 0.2770 0.2922 0.3157 0.1030  -0.0396 -0.0509 920  VAL B C   
16041 O O   . VAL B 922  ? 0.2797 0.2984 0.3197 0.1032  -0.0360 -0.0520 920  VAL B O   
16042 C CB  . VAL B 922  ? 0.3014 0.2966 0.3257 0.1097  -0.0440 -0.0516 920  VAL B CB  
16043 C CG1 . VAL B 922  ? 0.3478 0.3383 0.3689 0.1148  -0.0468 -0.0519 920  VAL B CG1 
16044 C CG2 . VAL B 922  ? 0.3056 0.2895 0.3222 0.1063  -0.0462 -0.0505 920  VAL B CG2 
16045 N N   . GLY B 923  ? 0.2578 0.2743 0.2981 0.0990  -0.0406 -0.0496 921  GLY B N   
16046 C CA  . GLY B 923  ? 0.2337 0.2566 0.2783 0.0946  -0.0375 -0.0495 921  GLY B CA  
16047 C C   . GLY B 923  ? 0.1987 0.2330 0.2523 0.0921  -0.0374 -0.0486 921  GLY B C   
16048 O O   . GLY B 923  ? 0.2589 0.2980 0.3164 0.0941  -0.0392 -0.0483 921  GLY B O   
16049 N N   . THR B 924  ? 0.2020 0.2408 0.2588 0.0876  -0.0354 -0.0481 922  THR B N   
16050 C CA  . THR B 924  ? 0.1839 0.2331 0.2488 0.0846  -0.0351 -0.0473 922  THR B CA  
16051 C C   . THR B 924  ? 0.1762 0.2210 0.2387 0.0813  -0.0374 -0.0462 922  THR B C   
16052 O O   . THR B 924  ? 0.1943 0.2384 0.2560 0.0775  -0.0354 -0.0458 922  THR B O   
16053 C CB  . THR B 924  ? 0.1745 0.2334 0.2456 0.0820  -0.0305 -0.0476 922  THR B CB  
16054 O OG1 . THR B 924  ? 0.1907 0.2446 0.2574 0.0803  -0.0282 -0.0479 922  THR B OG1 
16055 C CG2 . THR B 924  ? 0.1972 0.2620 0.2717 0.0853  -0.0284 -0.0485 922  THR B CG2 
16056 N N   . PHE B 925  ? 0.1992 0.2408 0.2601 0.0824  -0.0415 -0.0454 923  PHE B N   
16057 C CA  . PHE B 925  ? 0.1946 0.2309 0.2516 0.0789  -0.0437 -0.0439 923  PHE B CA  
16058 C C   . PHE B 925  ? 0.1969 0.2412 0.2603 0.0773  -0.0455 -0.0434 923  PHE B C   
16059 O O   . PHE B 925  ? 0.2185 0.2682 0.2861 0.0798  -0.0470 -0.0437 923  PHE B O   
16060 C CB  . PHE B 925  ? 0.2100 0.2337 0.2577 0.0809  -0.0472 -0.0431 923  PHE B CB  
16061 C CG  . PHE B 925  ? 0.2166 0.2304 0.2564 0.0813  -0.0459 -0.0433 923  PHE B CG  
16062 C CD1 . PHE B 925  ? 0.2301 0.2425 0.2694 0.0865  -0.0456 -0.0451 923  PHE B CD1 
16063 C CD2 . PHE B 925  ? 0.2001 0.2060 0.2331 0.0763  -0.0450 -0.0418 923  PHE B CD2 
16064 C CE1 . PHE B 925  ? 0.2112 0.2138 0.2428 0.0867  -0.0446 -0.0455 923  PHE B CE1 
16065 C CE2 . PHE B 925  ? 0.2268 0.2238 0.2527 0.0763  -0.0441 -0.0419 923  PHE B CE2 
16066 C CZ  . PHE B 925  ? 0.2380 0.2328 0.2629 0.0813  -0.0440 -0.0438 923  PHE B CZ  
16067 N N   . VAL B 926  ? 0.2046 0.2483 0.2669 0.0718  -0.0447 -0.0420 924  VAL B N   
16068 C CA  . VAL B 926  ? 0.2131 0.2612 0.2787 0.0696  -0.0469 -0.0413 924  VAL B CA  
16069 C C   . VAL B 926  ? 0.2380 0.2757 0.2948 0.0671  -0.0490 -0.0396 924  VAL B C   
16070 O O   . VAL B 926  ? 0.2282 0.2600 0.2796 0.0638  -0.0469 -0.0387 924  VAL B O   
16071 C CB  . VAL B 926  ? 0.1856 0.2423 0.2577 0.0651  -0.0440 -0.0412 924  VAL B CB  
16072 C CG1 . VAL B 926  ? 0.1870 0.2466 0.2612 0.0624  -0.0466 -0.0406 924  VAL B CG1 
16073 C CG2 . VAL B 926  ? 0.2007 0.2682 0.2817 0.0672  -0.0417 -0.0427 924  VAL B CG2 
16074 N N   . PRO B 927  ? 0.2275 0.2630 0.2824 0.0686  -0.0532 -0.0391 925  PRO B N   
16075 C CA  . PRO B 927  ? 0.2582 0.2838 0.3041 0.0662  -0.0550 -0.0374 925  PRO B CA  
16076 C C   . PRO B 927  ? 0.2328 0.2601 0.2789 0.0606  -0.0531 -0.0366 925  PRO B C   
16077 O O   . PRO B 927  ? 0.2229 0.2588 0.2760 0.0590  -0.0526 -0.0372 925  PRO B O   
16078 C CB  . PRO B 927  ? 0.2670 0.2918 0.3123 0.0695  -0.0599 -0.0373 925  PRO B CB  
16079 C CG  . PRO B 927  ? 0.2773 0.3144 0.3331 0.0713  -0.0604 -0.0388 925  PRO B CG  
16080 C CD  . PRO B 927  ? 0.2133 0.2554 0.2740 0.0725  -0.0565 -0.0400 925  PRO B CD  
16081 N N   . PRO B 928  ? 0.2597 0.2789 0.2983 0.0574  -0.0521 -0.0352 926  PRO B N   
16082 C CA  . PRO B 928  ? 0.2466 0.2665 0.2844 0.0527  -0.0509 -0.0343 926  PRO B CA  
16083 C C   . PRO B 928  ? 0.2321 0.2551 0.2717 0.0528  -0.0543 -0.0344 926  PRO B C   
16084 O O   . PRO B 928  ? 0.2834 0.3024 0.3194 0.0554  -0.0580 -0.0341 926  PRO B O   
16085 C CB  . PRO B 928  ? 0.2331 0.2429 0.2615 0.0506  -0.0505 -0.0326 926  PRO B CB  
16086 C CG  . PRO B 928  ? 0.3065 0.3125 0.3329 0.0527  -0.0492 -0.0329 926  PRO B CG  
16087 C CD  . PRO B 928  ? 0.2897 0.2994 0.3206 0.0578  -0.0515 -0.0344 926  PRO B CD  
16088 N N   . THR B 929  ? 0.1878 0.2177 0.2329 0.0500  -0.0531 -0.0349 927  THR B N   
16089 C CA  . THR B 929  ? 0.2270 0.2619 0.2758 0.0499  -0.0561 -0.0354 927  THR B CA  
16090 C C   . THR B 929  ? 0.2527 0.2869 0.2996 0.0454  -0.0551 -0.0349 927  THR B C   
16091 O O   . THR B 929  ? 0.2198 0.2551 0.2678 0.0425  -0.0514 -0.0348 927  THR B O   
16092 C CB  . THR B 929  ? 0.2524 0.2981 0.3116 0.0513  -0.0558 -0.0369 927  THR B CB  
16093 O OG1 . THR B 929  ? 0.2288 0.2753 0.2897 0.0561  -0.0565 -0.0375 927  THR B OG1 
16094 C CG2 . THR B 929  ? 0.2269 0.2783 0.2904 0.0509  -0.0592 -0.0375 927  THR B CG2 
16095 N N   . ILE B 930  ? 0.2492 0.2813 0.2930 0.0449  -0.0585 -0.0347 928  ILE B N   
16096 C CA  . ILE B 930  ? 0.2605 0.2920 0.3023 0.0411  -0.0580 -0.0346 928  ILE B CA  
16097 C C   . ILE B 930  ? 0.2223 0.2607 0.2701 0.0409  -0.0611 -0.0358 928  ILE B C   
16098 O O   . ILE B 930  ? 0.2624 0.3012 0.3101 0.0436  -0.0652 -0.0360 928  ILE B O   
16099 C CB  . ILE B 930  ? 0.2265 0.2487 0.2581 0.0403  -0.0592 -0.0333 928  ILE B CB  
16100 C CG1 . ILE B 930  ? 0.2687 0.2846 0.2948 0.0399  -0.0562 -0.0320 928  ILE B CG1 
16101 C CG2 . ILE B 930  ? 0.2812 0.3030 0.3108 0.0368  -0.0590 -0.0335 928  ILE B CG2 
16102 C CD1 . ILE B 930  ? 0.2750 0.2820 0.2911 0.0393  -0.0574 -0.0305 928  ILE B CD1 
16103 N N   . ILE B 931  ? 0.2185 0.2620 0.2713 0.0378  -0.0592 -0.0365 929  ILE B N   
16104 C CA  . ILE B 931  ? 0.2226 0.2730 0.2815 0.0368  -0.0618 -0.0376 929  ILE B CA  
16105 C C   . ILE B 931  ? 0.2541 0.3015 0.3092 0.0329  -0.0619 -0.0377 929  ILE B C   
16106 O O   . ILE B 931  ? 0.2579 0.3042 0.3126 0.0301  -0.0582 -0.0375 929  ILE B O   
16107 C CB  . ILE B 931  ? 0.2101 0.2702 0.2792 0.0364  -0.0598 -0.0384 929  ILE B CB  
16108 C CG1 . ILE B 931  ? 0.2298 0.2930 0.3025 0.0407  -0.0595 -0.0385 929  ILE B CG1 
16109 C CG2 . ILE B 931  ? 0.3214 0.3888 0.3970 0.0348  -0.0626 -0.0394 929  ILE B CG2 
16110 C CD1 . ILE B 931  ? 0.2520 0.3255 0.3348 0.0406  -0.0574 -0.0394 929  ILE B CD1 
16111 N N   . GLU B 932  ? 0.2381 0.2840 0.2904 0.0328  -0.0661 -0.0380 930  GLU B N   
16112 C CA  . GLU B 932  ? 0.2455 0.2880 0.2936 0.0293  -0.0664 -0.0384 930  GLU B CA  
16113 C C   . GLU B 932  ? 0.2500 0.3001 0.3060 0.0268  -0.0674 -0.0397 930  GLU B C   
16114 O O   . GLU B 932  ? 0.2794 0.3355 0.3409 0.0279  -0.0710 -0.0404 930  GLU B O   
16115 C CB  . GLU B 932  ? 0.2547 0.2909 0.2945 0.0303  -0.0704 -0.0382 930  GLU B CB  
16116 C CG  . GLU B 932  ? 0.3029 0.3309 0.3341 0.0319  -0.0690 -0.0367 930  GLU B CG  
16117 C CD  . GLU B 932  ? 0.3774 0.3995 0.4007 0.0335  -0.0731 -0.0361 930  GLU B CD  
16118 O OE1 . GLU B 932  ? 0.3303 0.3506 0.3501 0.0318  -0.0755 -0.0368 930  GLU B OE1 
16119 O OE2 . GLU B 932  ? 0.3518 0.3703 0.3718 0.0364  -0.0740 -0.0350 930  GLU B OE2 
16120 N N   . LEU B 933  ? 0.2298 0.2794 0.2862 0.0233  -0.0643 -0.0399 931  LEU B N   
16121 C CA  . LEU B 933  ? 0.2254 0.2808 0.2884 0.0201  -0.0646 -0.0410 931  LEU B CA  
16122 C C   . LEU B 933  ? 0.3413 0.3914 0.3985 0.0171  -0.0661 -0.0417 931  LEU B C   
16123 O O   . LEU B 933  ? 0.2807 0.3228 0.3291 0.0172  -0.0652 -0.0413 931  LEU B O   
16124 C CB  . LEU B 933  ? 0.2787 0.3375 0.3468 0.0184  -0.0598 -0.0406 931  LEU B CB  
16125 C CG  . LEU B 933  ? 0.2908 0.3544 0.3641 0.0210  -0.0572 -0.0400 931  LEU B CG  
16126 C CD1 . LEU B 933  ? 0.2990 0.3649 0.3760 0.0186  -0.0526 -0.0397 931  LEU B CD1 
16127 C CD2 . LEU B 933  ? 0.3264 0.3986 0.4076 0.0230  -0.0601 -0.0406 931  LEU B CD2 
16128 N N   . GLU B 934  ? 0.3387 0.3935 0.4011 0.0142  -0.0680 -0.0428 932  GLU B N   
16129 C CA  . GLU B 934  ? 0.3443 0.3941 0.4017 0.0110  -0.0694 -0.0437 932  GLU B CA  
16130 C C   . GLU B 934  ? 0.4151 0.4611 0.4707 0.0085  -0.0649 -0.0436 932  GLU B C   
16131 O O   . GLU B 934  ? 0.4183 0.4564 0.4656 0.0081  -0.0638 -0.0436 932  GLU B O   
16132 C CB  . GLU B 934  ? 0.3939 0.4498 0.4574 0.0086  -0.0736 -0.0449 932  GLU B CB  
16133 N N   . LYS B 935  ? 0.3887 0.4405 0.4519 0.0069  -0.0622 -0.0433 933  LYS B N   
16134 C CA  . LYS B 935  ? 0.3904 0.4390 0.4524 0.0046  -0.0581 -0.0430 933  LYS B CA  
16135 C C   . LYS B 935  ? 0.3661 0.4192 0.4334 0.0056  -0.0540 -0.0418 933  LYS B C   
16136 O O   . LYS B 935  ? 0.3481 0.4081 0.4217 0.0074  -0.0544 -0.0416 933  LYS B O   
16137 C CB  . LYS B 935  ? 0.4439 0.4933 0.5084 0.0003  -0.0593 -0.0440 933  LYS B CB  
16138 C CG  . LYS B 935  ? 0.4506 0.5099 0.5253 -0.0015 -0.0614 -0.0444 933  LYS B CG  
16139 C CD  . LYS B 935  ? 0.4171 0.4757 0.4926 -0.0060 -0.0638 -0.0455 933  LYS B CD  
16140 N N   . LEU B 936  ? 0.3855 0.4345 0.4501 0.0047  -0.0500 -0.0412 934  LEU B N   
16141 C CA  . LEU B 936  ? 0.3665 0.4189 0.4350 0.0057  -0.0460 -0.0401 934  LEU B CA  
16142 C C   . LEU B 936  ? 0.3819 0.4431 0.4600 0.0040  -0.0456 -0.0401 934  LEU B C   
16143 O O   . LEU B 936  ? 0.3735 0.4399 0.4562 0.0058  -0.0438 -0.0395 934  LEU B O   
16144 C CB  . LEU B 936  ? 0.3527 0.3994 0.4167 0.0048  -0.0422 -0.0394 934  LEU B CB  
16145 C CG  . LEU B 936  ? 0.3334 0.3802 0.3972 0.0069  -0.0385 -0.0381 934  LEU B CG  
16146 C CD1 . LEU B 936  ? 0.3757 0.4151 0.4320 0.0072  -0.0362 -0.0376 934  LEU B CD1 
16147 C CD2 . LEU B 936  ? 0.4240 0.4764 0.4945 0.0056  -0.0357 -0.0375 934  LEU B CD2 
16148 N N   . SER B 937  ? 0.3720 0.4349 0.4529 0.0004  -0.0473 -0.0408 935  SER B N   
16149 C CA  . SER B 937  ? 0.4045 0.4761 0.4946 -0.0017 -0.0468 -0.0407 935  SER B CA  
16150 C C   . SER B 937  ? 0.3834 0.4637 0.4802 0.0004  -0.0493 -0.0410 935  SER B C   
16151 O O   . SER B 937  ? 0.4068 0.4957 0.5119 -0.0008 -0.0485 -0.0408 935  SER B O   
16152 C CB  . SER B 937  ? 0.4366 0.5073 0.5277 -0.0064 -0.0483 -0.0413 935  SER B CB  
16153 O OG  . SER B 937  ? 0.4514 0.5211 0.5407 -0.0070 -0.0531 -0.0426 935  SER B OG  
16154 N N   . ASP B 938  ? 0.3405 0.4189 0.4338 0.0036  -0.0523 -0.0415 936  ASP B N   
16155 C CA  . ASP B 938  ? 0.3570 0.4429 0.4561 0.0066  -0.0545 -0.0417 936  ASP B CA  
16156 C C   . ASP B 938  ? 0.4020 0.4914 0.5040 0.0096  -0.0509 -0.0409 936  ASP B C   
16157 O O   . ASP B 938  ? 0.3571 0.4544 0.4656 0.0119  -0.0518 -0.0410 936  ASP B O   
16158 C CB  . ASP B 938  ? 0.3573 0.4388 0.4506 0.0094  -0.0585 -0.0421 936  ASP B CB  
16159 C CG  . ASP B 938  ? 0.4487 0.5285 0.5401 0.0068  -0.0628 -0.0432 936  ASP B CG  
16160 O OD1 . ASP B 938  ? 0.4028 0.4863 0.4988 0.0028  -0.0633 -0.0437 936  ASP B OD1 
16161 O OD2 . ASP B 938  ? 0.4351 0.5095 0.5199 0.0086  -0.0659 -0.0435 936  ASP B OD2 
16162 N N   . LEU B 939  ? 0.3675 0.4513 0.4648 0.0099  -0.0470 -0.0400 937  LEU B N   
16163 C CA  . LEU B 939  ? 0.3173 0.4036 0.4167 0.0123  -0.0435 -0.0393 937  LEU B CA  
16164 C C   . LEU B 939  ? 0.3295 0.4206 0.4343 0.0092  -0.0401 -0.0388 937  LEU B C   
16165 O O   . LEU B 939  ? 0.3714 0.4578 0.4731 0.0065  -0.0380 -0.0383 937  LEU B O   
16166 C CB  . LEU B 939  ? 0.3436 0.4213 0.4347 0.0140  -0.0415 -0.0386 937  LEU B CB  
16167 C CG  . LEU B 939  ? 0.3113 0.3903 0.4034 0.0162  -0.0379 -0.0379 937  LEU B CG  
16168 C CD1 . LEU B 939  ? 0.2994 0.3844 0.3962 0.0198  -0.0393 -0.0384 937  LEU B CD1 
16169 C CD2 . LEU B 939  ? 0.3374 0.4078 0.4212 0.0175  -0.0365 -0.0372 937  LEU B CD2 
16170 N N   . GLN B 940  ? 0.3335 0.4340 0.4465 0.0099  -0.0394 -0.0389 938  GLN B N   
16171 C CA  . GLN B 940  ? 0.3886 0.4951 0.5078 0.0065  -0.0368 -0.0385 938  GLN B CA  
16172 C C   . GLN B 940  ? 0.4641 0.5739 0.5855 0.0082  -0.0324 -0.0378 938  GLN B C   
16173 O O   . GLN B 940  ? 0.4745 0.5893 0.6007 0.0055  -0.0298 -0.0372 938  GLN B O   
16174 C CB  . GLN B 940  ? 0.4664 0.5824 0.5940 0.0049  -0.0395 -0.0392 938  GLN B CB  
16175 C CG  . GLN B 940  ? 0.4521 0.5653 0.5783 0.0007  -0.0426 -0.0396 938  GLN B CG  
16176 C CD  . GLN B 940  ? 0.5601 0.6797 0.6915 0.0008  -0.0473 -0.0406 938  GLN B CD  
16177 O OE1 . GLN B 940  ? 0.5857 0.7151 0.7247 0.0027  -0.0477 -0.0408 938  GLN B OE1 
16178 N NE2 . GLN B 940  ? 0.5570 0.6713 0.6840 -0.0011 -0.0510 -0.0413 938  GLN B NE2 
16179 N N   . ARG B 941  ? 0.3707 0.4776 0.4885 0.0123  -0.0316 -0.0378 939  ARG B N   
16180 C CA  . ARG B 941  ? 0.4030 0.5117 0.5217 0.0138  -0.0275 -0.0372 939  ARG B CA  
16181 C C   . ARG B 941  ? 0.3834 0.4847 0.4949 0.0173  -0.0271 -0.0371 939  ARG B C   
16182 O O   . ARG B 941  ? 0.3041 0.4003 0.4110 0.0189  -0.0300 -0.0374 939  ARG B O   
16183 C CB  . ARG B 941  ? 0.4039 0.5233 0.5309 0.0157  -0.0269 -0.0377 939  ARG B CB  
16184 C CG  . ARG B 941  ? 0.4090 0.5306 0.5371 0.0205  -0.0298 -0.0388 939  ARG B CG  
16185 C CD  . ARG B 941  ? 0.4291 0.5606 0.5646 0.0230  -0.0279 -0.0392 939  ARG B CD  
16186 N NE  . ARG B 941  ? 0.4764 0.6091 0.6120 0.0274  -0.0303 -0.0396 939  ARG B NE  
16187 C CZ  . ARG B 941  ? 0.4143 0.5430 0.5458 0.0320  -0.0301 -0.0400 939  ARG B CZ  
16188 N NH1 . ARG B 941  ? 0.4369 0.5603 0.5639 0.0329  -0.0276 -0.0400 939  ARG B NH1 
16189 N NH2 . ARG B 941  ? 0.3663 0.4962 0.4983 0.0358  -0.0324 -0.0402 939  ARG B NH2 
16190 N N   . GLU B 942  ? 0.3971 0.4978 0.5074 0.0181  -0.0235 -0.0365 940  GLU B N   
16191 C CA  . GLU B 942  ? 0.4110 0.5050 0.5148 0.0210  -0.0230 -0.0364 940  GLU B CA  
16192 C C   . GLU B 942  ? 0.3233 0.4198 0.4285 0.0255  -0.0247 -0.0373 940  GLU B C   
16193 O O   . GLU B 942  ? 0.3585 0.4629 0.4701 0.0270  -0.0240 -0.0379 940  GLU B O   
16194 C CB  . GLU B 942  ? 0.4637 0.5561 0.5655 0.0204  -0.0189 -0.0356 940  GLU B CB  
16195 C CG  . GLU B 942  ? 0.4597 0.5437 0.5537 0.0218  -0.0184 -0.0351 940  GLU B CG  
16196 C CD  . GLU B 942  ? 0.5318 0.6145 0.6239 0.0211  -0.0147 -0.0342 940  GLU B CD  
16197 O OE1 . GLU B 942  ? 0.5593 0.6479 0.6559 0.0209  -0.0124 -0.0343 940  GLU B OE1 
16198 O OE2 . GLU B 942  ? 0.4662 0.5424 0.5525 0.0208  -0.0141 -0.0335 940  GLU B OE2 
16199 N N   . VAL B 943  ? 0.2352 0.3250 0.3346 0.0278  -0.0269 -0.0374 941  VAL B N   
16200 C CA  . VAL B 943  ? 0.2309 0.3209 0.3301 0.0323  -0.0289 -0.0382 941  VAL B CA  
16201 C C   . VAL B 943  ? 0.2263 0.3086 0.3184 0.0340  -0.0275 -0.0377 941  VAL B C   
16202 O O   . VAL B 943  ? 0.1992 0.2738 0.2847 0.0334  -0.0287 -0.0371 941  VAL B O   
16203 C CB  . VAL B 943  ? 0.2542 0.3427 0.3523 0.0333  -0.0335 -0.0386 941  VAL B CB  
16204 C CG1 . VAL B 943  ? 0.2400 0.3282 0.3377 0.0384  -0.0356 -0.0392 941  VAL B CG1 
16205 C CG2 . VAL B 943  ? 0.2647 0.3608 0.3698 0.0310  -0.0350 -0.0390 941  VAL B CG2 
16206 N N   . PHE B 944  ? 0.1868 0.2713 0.2802 0.0359  -0.0250 -0.0381 942  PHE B N   
16207 C CA  . PHE B 944  ? 0.1584 0.2363 0.2456 0.0365  -0.0230 -0.0376 942  PHE B CA  
16208 C C   . PHE B 944  ? 0.1941 0.2670 0.2771 0.0405  -0.0251 -0.0381 942  PHE B C   
16209 O O   . PHE B 944  ? 0.2029 0.2762 0.2858 0.0435  -0.0241 -0.0389 942  PHE B O   
16210 C CB  . PHE B 944  ? 0.1927 0.2749 0.2827 0.0361  -0.0191 -0.0377 942  PHE B CB  
16211 C CG  . PHE B 944  ? 0.1863 0.2624 0.2705 0.0347  -0.0168 -0.0368 942  PHE B CG  
16212 C CD1 . PHE B 944  ? 0.2027 0.2760 0.2846 0.0310  -0.0159 -0.0356 942  PHE B CD1 
16213 C CD2 . PHE B 944  ? 0.1904 0.2637 0.2713 0.0373  -0.0157 -0.0373 942  PHE B CD2 
16214 C CE1 . PHE B 944  ? 0.1778 0.2462 0.2547 0.0298  -0.0139 -0.0348 942  PHE B CE1 
16215 C CE2 . PHE B 944  ? 0.1993 0.2673 0.2749 0.0358  -0.0139 -0.0365 942  PHE B CE2 
16216 C CZ  . PHE B 944  ? 0.2083 0.2742 0.2822 0.0320  -0.0130 -0.0351 942  PHE B CZ  
16217 N N   . GLY B 945  ? 0.1744 0.2420 0.2532 0.0407  -0.0283 -0.0377 943  GLY B N   
16218 C CA  . GLY B 945  ? 0.1694 0.2314 0.2437 0.0442  -0.0308 -0.0380 943  GLY B CA  
16219 C C   . GLY B 945  ? 0.1796 0.2341 0.2474 0.0428  -0.0332 -0.0370 943  GLY B C   
16220 O O   . GLY B 945  ? 0.1901 0.2435 0.2566 0.0393  -0.0325 -0.0362 943  GLY B O   
16221 N N   . PRO B 946  ? 0.1578 0.2068 0.2211 0.0458  -0.0361 -0.0370 944  PRO B N   
16222 C CA  . PRO B 946  ? 0.1562 0.1972 0.2122 0.0444  -0.0381 -0.0358 944  PRO B CA  
16223 C C   . PRO B 946  ? 0.1818 0.2252 0.2396 0.0440  -0.0412 -0.0359 944  PRO B C   
16224 O O   . PRO B 946  ? 0.2078 0.2481 0.2628 0.0463  -0.0447 -0.0359 944  PRO B O   
16225 C CB  . PRO B 946  ? 0.1835 0.2177 0.2341 0.0478  -0.0398 -0.0357 944  PRO B CB  
16226 C CG  . PRO B 946  ? 0.1968 0.2368 0.2532 0.0520  -0.0406 -0.0373 944  PRO B CG  
16227 C CD  . PRO B 946  ? 0.1972 0.2464 0.2612 0.0505  -0.0373 -0.0380 944  PRO B CD  
16228 N N   . VAL B 947  ? 0.1683 0.2168 0.2303 0.0410  -0.0401 -0.0360 945  VAL B N   
16229 C CA  . VAL B 947  ? 0.1939 0.2458 0.2586 0.0402  -0.0430 -0.0364 945  VAL B CA  
16230 C C   . VAL B 947  ? 0.2292 0.2784 0.2909 0.0361  -0.0421 -0.0357 945  VAL B C   
16231 O O   . VAL B 947  ? 0.1936 0.2462 0.2586 0.0334  -0.0393 -0.0358 945  VAL B O   
16232 C CB  . VAL B 947  ? 0.1923 0.2545 0.2666 0.0408  -0.0430 -0.0376 945  VAL B CB  
16233 C CG1 . VAL B 947  ? 0.2285 0.2939 0.3053 0.0398  -0.0464 -0.0380 945  VAL B CG1 
16234 C CG2 . VAL B 947  ? 0.2423 0.3076 0.3197 0.0454  -0.0435 -0.0384 945  VAL B CG2 
16235 N N   . LEU B 948  ? 0.2029 0.2458 0.2581 0.0358  -0.0443 -0.0351 946  LEU B N   
16236 C CA  . LEU B 948  ? 0.1836 0.2234 0.2351 0.0324  -0.0436 -0.0346 946  LEU B CA  
16237 C C   . LEU B 948  ? 0.2345 0.2773 0.2883 0.0315  -0.0466 -0.0354 946  LEU B C   
16238 O O   . LEU B 948  ? 0.2333 0.2755 0.2861 0.0336  -0.0504 -0.0357 946  LEU B O   
16239 C CB  . LEU B 948  ? 0.1732 0.2044 0.2157 0.0324  -0.0439 -0.0334 946  LEU B CB  
16240 C CG  . LEU B 948  ? 0.2059 0.2338 0.2440 0.0294  -0.0433 -0.0330 946  LEU B CG  
16241 C CD1 . LEU B 948  ? 0.1857 0.2151 0.2255 0.0270  -0.0392 -0.0327 946  LEU B CD1 
16242 C CD2 . LEU B 948  ? 0.2404 0.2605 0.2697 0.0297  -0.0442 -0.0318 946  LEU B CD2 
16243 N N   . HIS B 949  ? 0.1757 0.2210 0.2320 0.0284  -0.0453 -0.0358 947  HIS B N   
16244 C CA  . HIS B 949  ? 0.1749 0.2218 0.2322 0.0268  -0.0480 -0.0365 947  HIS B CA  
16245 C C   . HIS B 949  ? 0.1962 0.2359 0.2456 0.0249  -0.0480 -0.0361 947  HIS B C   
16246 O O   . HIS B 949  ? 0.2054 0.2417 0.2517 0.0236  -0.0447 -0.0354 947  HIS B O   
16247 C CB  . HIS B 949  ? 0.2077 0.2617 0.2728 0.0244  -0.0468 -0.0373 947  HIS B CB  
16248 C CG  . HIS B 949  ? 0.2230 0.2846 0.2959 0.0262  -0.0461 -0.0376 947  HIS B CG  
16249 N ND1 . HIS B 949  ? 0.2041 0.2665 0.2782 0.0270  -0.0424 -0.0371 947  HIS B ND1 
16250 C CD2 . HIS B 949  ? 0.2440 0.3127 0.3235 0.0276  -0.0485 -0.0384 947  HIS B CD2 
16251 C CE1 . HIS B 949  ? 0.2218 0.2913 0.3028 0.0288  -0.0425 -0.0377 947  HIS B CE1 
16252 N NE2 . HIS B 949  ? 0.2243 0.2981 0.3090 0.0293  -0.0460 -0.0385 947  HIS B NE2 
16253 N N   . VAL B 950  ? 0.2019 0.2395 0.2481 0.0249  -0.0516 -0.0366 948  VAL B N   
16254 C CA  . VAL B 950  ? 0.2203 0.2510 0.2584 0.0235  -0.0517 -0.0363 948  VAL B CA  
16255 C C   . VAL B 950  ? 0.2267 0.2585 0.2656 0.0212  -0.0539 -0.0375 948  VAL B C   
16256 O O   . VAL B 950  ? 0.2642 0.2996 0.3065 0.0217  -0.0576 -0.0383 948  VAL B O   
16257 C CB  . VAL B 950  ? 0.2242 0.2490 0.2549 0.0256  -0.0540 -0.0355 948  VAL B CB  
16258 C CG1 . VAL B 950  ? 0.2380 0.2560 0.2600 0.0240  -0.0537 -0.0352 948  VAL B CG1 
16259 C CG2 . VAL B 950  ? 0.2335 0.2565 0.2630 0.0276  -0.0522 -0.0343 948  VAL B CG2 
16260 N N   . ILE B 951  ? 0.1805 0.2092 0.2164 0.0188  -0.0517 -0.0377 949  ILE B N   
16261 C CA  . ILE B 951  ? 0.1924 0.2201 0.2271 0.0165  -0.0539 -0.0390 949  ILE B CA  
16262 C C   . ILE B 951  ? 0.2026 0.2224 0.2276 0.0162  -0.0534 -0.0388 949  ILE B C   
16263 O O   . ILE B 951  ? 0.2125 0.2286 0.2330 0.0169  -0.0505 -0.0377 949  ILE B O   
16264 C CB  . ILE B 951  ? 0.2270 0.2583 0.2674 0.0137  -0.0520 -0.0396 949  ILE B CB  
16265 C CG1 . ILE B 951  ? 0.2164 0.2447 0.2546 0.0130  -0.0472 -0.0388 949  ILE B CG1 
16266 C CG2 . ILE B 951  ? 0.2864 0.3262 0.3366 0.0140  -0.0523 -0.0397 949  ILE B CG2 
16267 C CD1 . ILE B 951  ? 0.3354 0.3661 0.3783 0.0104  -0.0453 -0.0393 949  ILE B CD1 
16268 N N   . ARG B 952  ? 0.2012 0.2186 0.2229 0.0149  -0.0563 -0.0400 950  ARG B N   
16269 C CA  . ARG B 952  ? 0.2228 0.2329 0.2349 0.0146  -0.0561 -0.0402 950  ARG B CA  
16270 C C   . ARG B 952  ? 0.2056 0.2139 0.2172 0.0120  -0.0550 -0.0415 950  ARG B C   
16271 O O   . ARG B 952  ? 0.2605 0.2724 0.2777 0.0101  -0.0565 -0.0426 950  ARG B O   
16272 C CB  . ARG B 952  ? 0.2391 0.2466 0.2461 0.0155  -0.0609 -0.0407 950  ARG B CB  
16273 C CG  . ARG B 952  ? 0.2541 0.2634 0.2622 0.0182  -0.0629 -0.0396 950  ARG B CG  
16274 C CD  . ARG B 952  ? 0.3143 0.3231 0.3201 0.0190  -0.0685 -0.0402 950  ARG B CD  
16275 N NE  . ARG B 952  ? 0.3309 0.3321 0.3257 0.0193  -0.0695 -0.0400 950  ARG B NE  
16276 C CZ  . ARG B 952  ? 0.3390 0.3364 0.3279 0.0214  -0.0707 -0.0387 950  ARG B CZ  
16277 N NH1 . ARG B 952  ? 0.3134 0.3132 0.3058 0.0237  -0.0712 -0.0375 950  ARG B NH1 
16278 N NH2 . ARG B 952  ? 0.3287 0.3193 0.3075 0.0213  -0.0713 -0.0385 950  ARG B NH2 
16279 N N   . TYR B 953  ? 0.2052 0.2077 0.2098 0.0119  -0.0523 -0.0415 951  TYR B N   
16280 C CA  . TYR B 953  ? 0.2097 0.2094 0.2127 0.0099  -0.0512 -0.0428 951  TYR B CA  
16281 C C   . TYR B 953  ? 0.2207 0.2130 0.2134 0.0104  -0.0511 -0.0434 951  TYR B C   
16282 O O   . TYR B 953  ? 0.2168 0.2065 0.2041 0.0122  -0.0497 -0.0423 951  TYR B O   
16283 C CB  . TYR B 953  ? 0.2164 0.2177 0.2236 0.0094  -0.0467 -0.0421 951  TYR B CB  
16284 C CG  . TYR B 953  ? 0.2030 0.2015 0.2056 0.0110  -0.0427 -0.0408 951  TYR B CG  
16285 C CD1 . TYR B 953  ? 0.2019 0.2030 0.2062 0.0126  -0.0413 -0.0391 951  TYR B CD1 
16286 C CD2 . TYR B 953  ? 0.1918 0.1853 0.1886 0.0110  -0.0404 -0.0413 951  TYR B CD2 
16287 C CE1 . TYR B 953  ? 0.2138 0.2127 0.2142 0.0136  -0.0379 -0.0378 951  TYR B CE1 
16288 C CE2 . TYR B 953  ? 0.2076 0.1996 0.2009 0.0124  -0.0367 -0.0400 951  TYR B CE2 
16289 C CZ  . TYR B 953  ? 0.2078 0.2027 0.2030 0.0135  -0.0355 -0.0382 951  TYR B CZ  
16290 O OH  . TYR B 953  ? 0.2227 0.2164 0.2146 0.0146  -0.0321 -0.0370 951  TYR B OH  
16291 N N   . ARG B 954  ? 0.2611 0.2498 0.2509 0.0088  -0.0524 -0.0452 952  ARG B N   
16292 C CA  . ARG B 954  ? 0.2837 0.2652 0.2637 0.0093  -0.0516 -0.0462 952  ARG B CA  
16293 C C   . ARG B 954  ? 0.2650 0.2446 0.2441 0.0097  -0.0466 -0.0458 952  ARG B C   
16294 O O   . ARG B 954  ? 0.2655 0.2476 0.2507 0.0085  -0.0451 -0.0458 952  ARG B O   
16295 C CB  . ARG B 954  ? 0.3609 0.3387 0.3376 0.0074  -0.0554 -0.0485 952  ARG B CB  
16296 C CG  . ARG B 954  ? 0.3856 0.3663 0.3647 0.0066  -0.0608 -0.0490 952  ARG B CG  
16297 C CD  . ARG B 954  ? 0.4956 0.4745 0.4684 0.0088  -0.0625 -0.0482 952  ARG B CD  
16298 N NE  . ARG B 954  ? 0.5751 0.5465 0.5368 0.0097  -0.0614 -0.0488 952  ARG B NE  
16299 C CZ  . ARG B 954  ? 0.6149 0.5809 0.5696 0.0088  -0.0642 -0.0508 952  ARG B CZ  
16300 N NH1 . ARG B 954  ? 0.6303 0.5975 0.5880 0.0067  -0.0686 -0.0523 952  ARG B NH1 
16301 N NH2 . ARG B 954  ? 0.6294 0.5889 0.5739 0.0100  -0.0624 -0.0513 952  ARG B NH2 
16302 N N   . ARG B 955  ? 0.2992 0.2747 0.2707 0.0114  -0.0441 -0.0454 953  ARG B N   
16303 C CA  . ARG B 955  ? 0.3275 0.3024 0.2988 0.0123  -0.0393 -0.0448 953  ARG B CA  
16304 C C   . ARG B 955  ? 0.3218 0.2936 0.2934 0.0111  -0.0387 -0.0464 953  ARG B C   
16305 O O   . ARG B 955  ? 0.3030 0.2764 0.2785 0.0112  -0.0355 -0.0457 953  ARG B O   
16306 C CB  . ARG B 955  ? 0.3651 0.3364 0.3281 0.0142  -0.0368 -0.0442 953  ARG B CB  
16307 C CG  . ARG B 955  ? 0.3767 0.3480 0.3395 0.0154  -0.0317 -0.0435 953  ARG B CG  
16308 C CD  . ARG B 955  ? 0.3845 0.3617 0.3561 0.0152  -0.0295 -0.0417 953  ARG B CD  
16309 N NE  . ARG B 955  ? 0.4032 0.3807 0.3748 0.0164  -0.0250 -0.0410 953  ARG B NE  
16310 C CZ  . ARG B 955  ? 0.4394 0.4149 0.4115 0.0165  -0.0236 -0.0420 953  ARG B CZ  
16311 N NH1 . ARG B 955  ? 0.3896 0.3622 0.3619 0.0151  -0.0261 -0.0438 953  ARG B NH1 
16312 N NH2 . ARG B 955  ? 0.3765 0.3529 0.3489 0.0179  -0.0196 -0.0412 953  ARG B NH2 
16313 N N   . ASP B 956  ? 0.3295 0.2968 0.2968 0.0099  -0.0418 -0.0485 954  ASP B N   
16314 C CA  . ASP B 956  ? 0.3441 0.3077 0.3113 0.0086  -0.0416 -0.0501 954  ASP B CA  
16315 C C   . ASP B 956  ? 0.3200 0.2884 0.2969 0.0063  -0.0422 -0.0496 954  ASP B C   
16316 O O   . ASP B 956  ? 0.3576 0.3232 0.3352 0.0050  -0.0415 -0.0505 954  ASP B O   
16317 C CB  . ASP B 956  ? 0.3792 0.3365 0.3394 0.0075  -0.0453 -0.0526 954  ASP B CB  
16318 C CG  . ASP B 956  ? 0.5352 0.4872 0.4850 0.0098  -0.0443 -0.0533 954  ASP B CG  
16319 O OD1 . ASP B 956  ? 0.5736 0.5249 0.5209 0.0121  -0.0400 -0.0524 954  ASP B OD1 
16320 O OD2 . ASP B 956  ? 0.6248 0.5733 0.5687 0.0094  -0.0479 -0.0547 954  ASP B OD2 
16321 N N   . ASP B 957  ? 0.2807 0.2559 0.2646 0.0057  -0.0435 -0.0483 955  ASP B N   
16322 C CA  . ASP B 957  ? 0.3058 0.2864 0.2990 0.0036  -0.0439 -0.0478 955  ASP B CA  
16323 C C   . ASP B 957  ? 0.2535 0.2389 0.2521 0.0048  -0.0399 -0.0457 955  ASP B C   
16324 O O   . ASP B 957  ? 0.2512 0.2422 0.2578 0.0035  -0.0400 -0.0449 955  ASP B O   
16325 C CB  . ASP B 957  ? 0.3127 0.2983 0.3107 0.0023  -0.0482 -0.0479 955  ASP B CB  
16326 C CG  . ASP B 957  ? 0.4367 0.4186 0.4314 0.0001  -0.0525 -0.0501 955  ASP B CG  
16327 O OD1 . ASP B 957  ? 0.4088 0.3859 0.4012 -0.0016 -0.0524 -0.0514 955  ASP B OD1 
16328 O OD2 . ASP B 957  ? 0.4742 0.4580 0.4686 0.0001  -0.0563 -0.0505 955  ASP B OD2 
16329 N N   . LEU B 958  ? 0.2268 0.2104 0.2213 0.0072  -0.0366 -0.0448 956  LEU B N   
16330 C CA  . LEU B 958  ? 0.1943 0.1823 0.1935 0.0083  -0.0331 -0.0428 956  LEU B CA  
16331 C C   . LEU B 958  ? 0.2412 0.2307 0.2459 0.0069  -0.0314 -0.0424 956  LEU B C   
16332 O O   . LEU B 958  ? 0.2015 0.1966 0.2129 0.0065  -0.0304 -0.0411 956  LEU B O   
16333 C CB  . LEU B 958  ? 0.2196 0.2051 0.2131 0.0107  -0.0299 -0.0420 956  LEU B CB  
16334 C CG  . LEU B 958  ? 0.2129 0.2027 0.2107 0.0117  -0.0264 -0.0400 956  LEU B CG  
16335 C CD1 . LEU B 958  ? 0.2353 0.2303 0.2376 0.0117  -0.0276 -0.0387 956  LEU B CD1 
16336 C CD2 . LEU B 958  ? 0.2416 0.2292 0.2338 0.0138  -0.0234 -0.0394 956  LEU B CD2 
16337 N N   . ASP B 959  ? 0.2277 0.2120 0.2292 0.0062  -0.0309 -0.0435 957  ASP B N   
16338 C CA  . ASP B 959  ? 0.2387 0.2236 0.2447 0.0049  -0.0291 -0.0430 957  ASP B CA  
16339 C C   . ASP B 959  ? 0.2082 0.1977 0.2214 0.0020  -0.0314 -0.0429 957  ASP B C   
16340 O O   . ASP B 959  ? 0.2177 0.2115 0.2369 0.0012  -0.0297 -0.0416 957  ASP B O   
16341 C CB  . ASP B 959  ? 0.2406 0.2179 0.2410 0.0048  -0.0286 -0.0444 957  ASP B CB  
16342 C CG  . ASP B 959  ? 0.2334 0.2103 0.2369 0.0044  -0.0260 -0.0434 957  ASP B CG  
16343 O OD1 . ASP B 959  ? 0.2264 0.2069 0.2325 0.0060  -0.0230 -0.0416 957  ASP B OD1 
16344 O OD2 . ASP B 959  ? 0.2400 0.2127 0.2429 0.0023  -0.0271 -0.0443 957  ASP B OD2 
16345 N N   . ARG B 960  ? 0.2258 0.2149 0.2385 0.0003  -0.0353 -0.0443 958  ARG B N   
16346 C CA  . ARG B 960  ? 0.2382 0.2329 0.2583 -0.0024 -0.0376 -0.0443 958  ARG B CA  
16347 C C   . ARG B 960  ? 0.2474 0.2500 0.2737 -0.0013 -0.0370 -0.0428 958  ARG B C   
16348 O O   . ARG B 960  ? 0.2466 0.2550 0.2802 -0.0028 -0.0367 -0.0421 958  ARG B O   
16349 C CB  . ARG B 960  ? 0.2734 0.2661 0.2912 -0.0042 -0.0422 -0.0462 958  ARG B CB  
16350 C CG  . ARG B 960  ? 0.3468 0.3464 0.3725 -0.0069 -0.0451 -0.0462 958  ARG B CG  
16351 C CD  . ARG B 960  ? 0.4609 0.4575 0.4834 -0.0088 -0.0497 -0.0482 958  ARG B CD  
16352 N NE  . ARG B 960  ? 0.6150 0.6191 0.6443 -0.0103 -0.0532 -0.0482 958  ARG B NE  
16353 C CZ  . ARG B 960  ? 0.7030 0.7066 0.7302 -0.0111 -0.0577 -0.0497 958  ARG B CZ  
16354 N NH1 . ARG B 960  ? 0.6468 0.6423 0.6648 -0.0106 -0.0593 -0.0512 958  ARG B NH1 
16355 N NH2 . ARG B 960  ? 0.6860 0.6973 0.7204 -0.0122 -0.0607 -0.0496 958  ARG B NH2 
16356 N N   . LEU B 961  ? 0.1957 0.1986 0.2189 0.0014  -0.0369 -0.0424 959  LEU B N   
16357 C CA  . LEU B 961  ? 0.2024 0.2117 0.2306 0.0028  -0.0363 -0.0410 959  LEU B CA  
16358 C C   . LEU B 961  ? 0.1968 0.2087 0.2287 0.0033  -0.0324 -0.0395 959  LEU B C   
16359 O O   . LEU B 961  ? 0.2073 0.2252 0.2458 0.0030  -0.0320 -0.0387 959  LEU B O   
16360 C CB  . LEU B 961  ? 0.1829 0.1904 0.2058 0.0054  -0.0368 -0.0408 959  LEU B CB  
16361 C CG  . LEU B 961  ? 0.2016 0.2138 0.2279 0.0073  -0.0357 -0.0393 959  LEU B CG  
16362 C CD1 . LEU B 961  ? 0.2516 0.2700 0.2846 0.0067  -0.0384 -0.0395 959  LEU B CD1 
16363 C CD2 . LEU B 961  ? 0.1893 0.1985 0.2093 0.0094  -0.0358 -0.0388 959  LEU B CD2 
16364 N N   . VAL B 962  ? 0.1733 0.1809 0.2012 0.0041  -0.0295 -0.0391 960  VAL B N   
16365 C CA  . VAL B 962  ? 0.1713 0.1811 0.2025 0.0043  -0.0261 -0.0376 960  VAL B CA  
16366 C C   . VAL B 962  ? 0.1929 0.2054 0.2299 0.0017  -0.0261 -0.0375 960  VAL B C   
16367 O O   . VAL B 962  ? 0.1922 0.2096 0.2344 0.0015  -0.0245 -0.0363 960  VAL B O   
16368 C CB  . VAL B 962  ? 0.1891 0.1938 0.2148 0.0057  -0.0233 -0.0373 960  VAL B CB  
16369 C CG1 . VAL B 962  ? 0.2288 0.2355 0.2580 0.0058  -0.0202 -0.0358 960  VAL B CG1 
16370 C CG2 . VAL B 962  ? 0.1928 0.1964 0.2138 0.0082  -0.0227 -0.0370 960  VAL B CG2 
16371 N N   . ASP B 963  ? 0.1897 0.1990 0.2256 -0.0006 -0.0281 -0.0388 961  ASP B N   
16372 C CA  . ASP B 963  ? 0.2312 0.2432 0.2727 -0.0037 -0.0286 -0.0386 961  ASP B CA  
16373 C C   . ASP B 963  ? 0.2388 0.2591 0.2875 -0.0043 -0.0299 -0.0383 961  ASP B C   
16374 O O   . ASP B 963  ? 0.2808 0.3061 0.3354 -0.0055 -0.0284 -0.0373 961  ASP B O   
16375 C CB  . ASP B 963  ? 0.2466 0.2537 0.2855 -0.0064 -0.0313 -0.0402 961  ASP B CB  
16376 C CG  . ASP B 963  ? 0.3315 0.3306 0.3647 -0.0064 -0.0297 -0.0405 961  ASP B CG  
16377 O OD1 . ASP B 963  ? 0.3670 0.3653 0.3996 -0.0047 -0.0264 -0.0392 961  ASP B OD1 
16378 O OD2 . ASP B 963  ? 0.3595 0.3528 0.3885 -0.0079 -0.0319 -0.0421 961  ASP B OD2 
16379 N N   . ASP B 964  ? 0.2345 0.2562 0.2825 -0.0033 -0.0328 -0.0392 962  ASP B N   
16380 C CA  . ASP B 964  ? 0.2456 0.2751 0.3002 -0.0033 -0.0344 -0.0391 962  ASP B CA  
16381 C C   . ASP B 964  ? 0.2770 0.3110 0.3349 -0.0012 -0.0315 -0.0376 962  ASP B C   
16382 O O   . ASP B 964  ? 0.2493 0.2900 0.3139 -0.0018 -0.0311 -0.0372 962  ASP B O   
16383 C CB  . ASP B 964  ? 0.2538 0.2831 0.3059 -0.0019 -0.0380 -0.0401 962  ASP B CB  
16384 C CG  . ASP B 964  ? 0.3301 0.3565 0.3803 -0.0043 -0.0416 -0.0417 962  ASP B CG  
16385 O OD1 . ASP B 964  ? 0.3128 0.3384 0.3648 -0.0075 -0.0416 -0.0420 962  ASP B OD1 
16386 O OD2 . ASP B 964  ? 0.3614 0.3864 0.4082 -0.0032 -0.0447 -0.0426 962  ASP B OD2 
16387 N N   . VAL B 965  ? 0.1960 0.2265 0.2491 0.0012  -0.0294 -0.0369 963  VAL B N   
16388 C CA  . VAL B 965  ? 0.1737 0.2077 0.2292 0.0031  -0.0268 -0.0356 963  VAL B CA  
16389 C C   . VAL B 965  ? 0.2032 0.2393 0.2625 0.0015  -0.0240 -0.0347 963  VAL B C   
16390 O O   . VAL B 965  ? 0.2284 0.2700 0.2927 0.0017  -0.0228 -0.0340 963  VAL B O   
16391 C CB  . VAL B 965  ? 0.1745 0.2042 0.2240 0.0055  -0.0254 -0.0351 963  VAL B CB  
16392 C CG1 . VAL B 965  ? 0.1595 0.1922 0.2111 0.0069  -0.0227 -0.0337 963  VAL B CG1 
16393 C CG2 . VAL B 965  ? 0.1996 0.2278 0.2456 0.0070  -0.0281 -0.0357 963  VAL B CG2 
16394 N N   . ASN B 966  ? 0.1829 0.2142 0.2394 0.0001  -0.0228 -0.0346 964  ASN B N   
16395 C CA  . ASN B 966  ? 0.2153 0.2477 0.2744 -0.0015 -0.0202 -0.0335 964  ASN B CA  
16396 C C   . ASN B 966  ? 0.2416 0.2791 0.3071 -0.0043 -0.0211 -0.0336 964  ASN B C   
16397 O O   . ASN B 966  ? 0.2685 0.3092 0.3376 -0.0054 -0.0189 -0.0324 964  ASN B O   
16398 C CB  . ASN B 966  ? 0.2067 0.2320 0.2609 -0.0022 -0.0192 -0.0334 964  ASN B CB  
16399 C CG  . ASN B 966  ? 0.2174 0.2388 0.2662 0.0007  -0.0175 -0.0329 964  ASN B CG  
16400 O OD1 . ASN B 966  ? 0.2129 0.2371 0.2622 0.0026  -0.0163 -0.0322 964  ASN B OD1 
16401 N ND2 . ASN B 966  ? 0.2057 0.2207 0.2492 0.0009  -0.0174 -0.0334 964  ASN B ND2 
16402 N N   . ALA B 967  ? 0.2484 0.2870 0.3153 -0.0057 -0.0243 -0.0348 965  ALA B N   
16403 C CA  . ALA B 967  ? 0.2458 0.2893 0.3187 -0.0090 -0.0254 -0.0350 965  ALA B CA  
16404 C C   . ALA B 967  ? 0.2762 0.3287 0.3562 -0.0083 -0.0245 -0.0344 965  ALA B C   
16405 O O   . ALA B 967  ? 0.3027 0.3603 0.3884 -0.0111 -0.0242 -0.0341 965  ALA B O   
16406 C CB  . ALA B 967  ? 0.2587 0.3014 0.3312 -0.0104 -0.0295 -0.0366 965  ALA B CB  
16407 N N   . THR B 968  ? 0.2289 0.2835 0.3087 -0.0049 -0.0240 -0.0343 966  THR B N   
16408 C CA  . THR B 968  ? 0.2268 0.2894 0.3127 -0.0039 -0.0229 -0.0338 966  THR B CA  
16409 C C   . THR B 968  ? 0.2804 0.3448 0.3684 -0.0050 -0.0192 -0.0324 966  THR B C   
16410 O O   . THR B 968  ? 0.2656 0.3371 0.3594 -0.0053 -0.0181 -0.0321 966  THR B O   
16411 C CB  . THR B 968  ? 0.2506 0.3136 0.3348 0.0002  -0.0231 -0.0340 966  THR B CB  
16412 O OG1 . THR B 968  ? 0.2219 0.2809 0.3018 0.0016  -0.0202 -0.0330 966  THR B OG1 
16413 C CG2 . THR B 968  ? 0.2592 0.3187 0.3394 0.0015  -0.0265 -0.0351 966  THR B CG2 
16414 N N   . GLY B 969  ? 0.2423 0.3004 0.3255 -0.0056 -0.0173 -0.0316 967  GLY B N   
16415 C CA  . GLY B 969  ? 0.2542 0.3131 0.3383 -0.0063 -0.0139 -0.0301 967  GLY B CA  
16416 C C   . GLY B 969  ? 0.2366 0.2956 0.3187 -0.0032 -0.0118 -0.0294 967  GLY B C   
16417 O O   . GLY B 969  ? 0.2203 0.2786 0.3016 -0.0035 -0.0091 -0.0282 967  GLY B O   
16418 N N   . TYR B 970  ? 0.2080 0.2676 0.2890 -0.0003 -0.0131 -0.0302 968  TYR B N   
16419 C CA  . TYR B 970  ? 0.1594 0.2182 0.2379 0.0025  -0.0115 -0.0297 968  TYR B CA  
16420 C C   . TYR B 970  ? 0.1971 0.2489 0.2692 0.0033  -0.0113 -0.0293 968  TYR B C   
16421 O O   . TYR B 970  ? 0.2123 0.2599 0.2817 0.0024  -0.0126 -0.0298 968  TYR B O   
16422 C CB  . TYR B 970  ? 0.1957 0.2575 0.2755 0.0051  -0.0131 -0.0306 968  TYR B CB  
16423 C CG  . TYR B 970  ? 0.2077 0.2771 0.2939 0.0052  -0.0129 -0.0309 968  TYR B CG  
16424 C CD1 . TYR B 970  ? 0.2437 0.3163 0.3314 0.0063  -0.0103 -0.0303 968  TYR B CD1 
16425 C CD2 . TYR B 970  ? 0.2618 0.3355 0.3525 0.0044  -0.0152 -0.0319 968  TYR B CD2 
16426 C CE1 . TYR B 970  ? 0.2994 0.3794 0.3930 0.0067  -0.0097 -0.0307 968  TYR B CE1 
16427 C CE2 . TYR B 970  ? 0.3011 0.3826 0.3981 0.0047  -0.0148 -0.0322 968  TYR B CE2 
16428 C CZ  . TYR B 970  ? 0.3377 0.4224 0.4361 0.0060  -0.0119 -0.0316 968  TYR B CZ  
16429 O OH  . TYR B 970  ? 0.4050 0.4978 0.5097 0.0066  -0.0113 -0.0320 968  TYR B OH  
16430 N N   . GLY B 971  ? 0.1458 0.1966 0.2155 0.0050  -0.0095 -0.0285 969  GLY B N   
16431 C CA  . GLY B 971  ? 0.1577 0.2031 0.2221 0.0060  -0.0091 -0.0281 969  GLY B CA  
16432 C C   . GLY B 971  ? 0.1342 0.1799 0.1969 0.0078  -0.0076 -0.0273 969  GLY B C   
16433 O O   . GLY B 971  ? 0.1502 0.1945 0.2113 0.0078  -0.0057 -0.0262 969  GLY B O   
16434 N N   . LEU B 972  ? 0.1315 0.1788 0.1945 0.0095  -0.0087 -0.0279 970  LEU B N   
16435 C CA  . LEU B 972  ? 0.1271 0.1743 0.1883 0.0110  -0.0077 -0.0273 970  LEU B CA  
16436 C C   . LEU B 972  ? 0.1111 0.1541 0.1674 0.0120  -0.0085 -0.0271 970  LEU B C   
16437 O O   . LEU B 972  ? 0.1410 0.1817 0.1947 0.0118  -0.0072 -0.0262 970  LEU B O   
16438 C CB  . LEU B 972  ? 0.1269 0.1779 0.1909 0.0123  -0.0082 -0.0279 970  LEU B CB  
16439 C CG  . LEU B 972  ? 0.1338 0.1846 0.1961 0.0136  -0.0069 -0.0274 970  LEU B CG  
16440 C CD1 . LEU B 972  ? 0.1774 0.2281 0.2390 0.0126  -0.0045 -0.0262 970  LEU B CD1 
16441 C CD2 . LEU B 972  ? 0.1538 0.2084 0.2191 0.0151  -0.0072 -0.0283 970  LEU B CD2 
16442 N N   . THR B 973  ? 0.1049 0.1472 0.1600 0.0132  -0.0105 -0.0278 971  THR B N   
16443 C CA  . THR B 973  ? 0.1072 0.1456 0.1574 0.0138  -0.0111 -0.0275 971  THR B CA  
16444 C C   . THR B 973  ? 0.1263 0.1624 0.1748 0.0136  -0.0130 -0.0283 971  THR B C   
16445 O O   . THR B 973  ? 0.1288 0.1665 0.1799 0.0132  -0.0146 -0.0292 971  THR B O   
16446 C CB  . THR B 973  ? 0.1082 0.1460 0.1568 0.0153  -0.0120 -0.0274 971  THR B CB  
16447 O OG1 . THR B 973  ? 0.1131 0.1524 0.1639 0.0163  -0.0141 -0.0285 971  THR B OG1 
16448 C CG2 . THR B 973  ? 0.1256 0.1649 0.1750 0.0155  -0.0102 -0.0268 971  THR B CG2 
16449 N N   . PHE B 974  ? 0.1068 0.1393 0.1506 0.0137  -0.0129 -0.0278 972  PHE B N   
16450 C CA  . PHE B 974  ? 0.1049 0.1345 0.1458 0.0136  -0.0145 -0.0286 972  PHE B CA  
16451 C C   . PHE B 974  ? 0.1232 0.1496 0.1588 0.0143  -0.0143 -0.0279 972  PHE B C   
16452 O O   . PHE B 974  ? 0.1219 0.1480 0.1561 0.0142  -0.0123 -0.0268 972  PHE B O   
16453 C CB  . PHE B 974  ? 0.1255 0.1539 0.1665 0.0125  -0.0137 -0.0289 972  PHE B CB  
16454 C CG  . PHE B 974  ? 0.1211 0.1458 0.1580 0.0125  -0.0152 -0.0297 972  PHE B CG  
16455 C CD1 . PHE B 974  ? 0.1386 0.1633 0.1763 0.0120  -0.0179 -0.0310 972  PHE B CD1 
16456 C CD2 . PHE B 974  ? 0.1348 0.1563 0.1670 0.0130  -0.0139 -0.0293 972  PHE B CD2 
16457 C CE1 . PHE B 974  ? 0.1525 0.1733 0.1858 0.0119  -0.0194 -0.0319 972  PHE B CE1 
16458 C CE2 . PHE B 974  ? 0.1292 0.1470 0.1570 0.0131  -0.0151 -0.0303 972  PHE B CE2 
16459 C CZ  . PHE B 974  ? 0.1585 0.1757 0.1866 0.0125  -0.0180 -0.0316 972  PHE B CZ  
16460 N N   . GLY B 975  ? 0.1237 0.1478 0.1562 0.0148  -0.0165 -0.0284 973  GLY B N   
16461 C CA  . GLY B 975  ? 0.1294 0.1503 0.1564 0.0151  -0.0164 -0.0277 973  GLY B CA  
16462 C C   . GLY B 975  ? 0.1254 0.1431 0.1483 0.0150  -0.0172 -0.0284 973  GLY B C   
16463 O O   . GLY B 975  ? 0.1375 0.1548 0.1611 0.0148  -0.0193 -0.0297 973  GLY B O   
16464 N N   . LEU B 976  ? 0.1399 0.1555 0.1583 0.0152  -0.0157 -0.0277 974  LEU B N   
16465 C CA  . LEU B 976  ? 0.1399 0.1520 0.1532 0.0153  -0.0161 -0.0284 974  LEU B CA  
16466 C C   . LEU B 976  ? 0.1302 0.1404 0.1383 0.0156  -0.0156 -0.0272 974  LEU B C   
16467 O O   . LEU B 976  ? 0.1466 0.1582 0.1547 0.0154  -0.0133 -0.0259 974  LEU B O   
16468 C CB  . LEU B 976  ? 0.1543 0.1660 0.1673 0.0153  -0.0140 -0.0287 974  LEU B CB  
16469 C CG  . LEU B 976  ? 0.1553 0.1631 0.1624 0.0158  -0.0140 -0.0296 974  LEU B CG  
16470 C CD1 . LEU B 976  ? 0.1818 0.1872 0.1875 0.0155  -0.0171 -0.0312 974  LEU B CD1 
16471 C CD2 . LEU B 976  ? 0.1934 0.2009 0.2005 0.0163  -0.0114 -0.0298 974  LEU B CD2 
16472 N N   . HIS B 977  ? 0.1557 0.1629 0.1594 0.0158  -0.0178 -0.0276 975  HIS B N   
16473 C CA  . HIS B 977  ? 0.1440 0.1486 0.1417 0.0159  -0.0174 -0.0265 975  HIS B CA  
16474 C C   . HIS B 977  ? 0.1621 0.1637 0.1544 0.0162  -0.0172 -0.0274 975  HIS B C   
16475 O O   . HIS B 977  ? 0.1698 0.1690 0.1601 0.0164  -0.0198 -0.0287 975  HIS B O   
16476 C CB  . HIS B 977  ? 0.1781 0.1809 0.1741 0.0160  -0.0203 -0.0260 975  HIS B CB  
16477 C CG  . HIS B 977  ? 0.2012 0.2052 0.1989 0.0157  -0.0196 -0.0246 975  HIS B CG  
16478 N ND1 . HIS B 977  ? 0.2784 0.2803 0.2716 0.0151  -0.0188 -0.0229 975  HIS B ND1 
16479 C CD2 . HIS B 977  ? 0.2652 0.2719 0.2683 0.0158  -0.0197 -0.0246 975  HIS B CD2 
16480 C CE1 . HIS B 977  ? 0.2457 0.2485 0.2412 0.0147  -0.0187 -0.0220 975  HIS B CE1 
16481 N NE2 . HIS B 977  ? 0.2668 0.2724 0.2682 0.0153  -0.0191 -0.0230 975  HIS B NE2 
16482 N N   . THR B 978  ? 0.1571 0.1590 0.1469 0.0163  -0.0142 -0.0267 976  THR B N   
16483 C CA  . THR B 978  ? 0.1558 0.1549 0.1400 0.0169  -0.0132 -0.0274 976  THR B CA  
16484 C C   . THR B 978  ? 0.1576 0.1584 0.1399 0.0169  -0.0096 -0.0260 976  THR B C   
16485 O O   . THR B 978  ? 0.1785 0.1830 0.1651 0.0166  -0.0078 -0.0248 976  THR B O   
16486 C CB  . THR B 978  ? 0.1660 0.1645 0.1518 0.0174  -0.0132 -0.0293 976  THR B CB  
16487 O OG1 . THR B 978  ? 0.1951 0.1904 0.1747 0.0183  -0.0121 -0.0302 976  THR B OG1 
16488 C CG2 . THR B 978  ? 0.2057 0.2076 0.1969 0.0176  -0.0107 -0.0289 976  THR B CG2 
16489 N N   . ARG B 979  ? 0.1800 0.1785 0.1558 0.0174  -0.0087 -0.0260 977  ARG B N   
16490 C CA  . ARG B 979  ? 0.1863 0.1870 0.1604 0.0177  -0.0050 -0.0248 977  ARG B CA  
16491 C C   . ARG B 979  ? 0.1854 0.1864 0.1591 0.0193  -0.0027 -0.0262 977  ARG B C   
16492 O O   . ARG B 979  ? 0.2255 0.2291 0.1984 0.0200  0.0006  -0.0253 977  ARG B O   
16493 C CB  . ARG B 979  ? 0.2254 0.2239 0.1923 0.0172  -0.0047 -0.0238 977  ARG B CB  
16494 C CG  . ARG B 979  ? 0.2861 0.2842 0.2531 0.0155  -0.0064 -0.0220 977  ARG B CG  
16495 C CD  . ARG B 979  ? 0.3442 0.3392 0.3036 0.0149  -0.0064 -0.0209 977  ARG B CD  
16496 N NE  . ARG B 979  ? 0.3690 0.3633 0.3280 0.0132  -0.0077 -0.0189 977  ARG B NE  
16497 C CZ  . ARG B 979  ? 0.4118 0.4033 0.3644 0.0121  -0.0077 -0.0174 977  ARG B CZ  
16498 N NH1 . ARG B 979  ? 0.3602 0.3497 0.3060 0.0125  -0.0065 -0.0176 977  ARG B NH1 
16499 N NH2 . ARG B 979  ? 0.4055 0.3958 0.3580 0.0105  -0.0090 -0.0155 977  ARG B NH2 
16500 N N   . LEU B 980  ? 0.1707 0.1691 0.1451 0.0200  -0.0044 -0.0282 978  LEU B N   
16501 C CA  . LEU B 980  ? 0.1865 0.1828 0.1583 0.0218  -0.0029 -0.0299 978  LEU B CA  
16502 C C   . LEU B 980  ? 0.1790 0.1777 0.1568 0.0225  -0.0016 -0.0301 978  LEU B C   
16503 O O   . LEU B 980  ? 0.1888 0.1875 0.1711 0.0216  -0.0036 -0.0306 978  LEU B O   
16504 C CB  . LEU B 980  ? 0.1906 0.1814 0.1579 0.0219  -0.0058 -0.0321 978  LEU B CB  
16505 C CG  . LEU B 980  ? 0.2067 0.1948 0.1681 0.0212  -0.0078 -0.0318 978  LEU B CG  
16506 C CD1 . LEU B 980  ? 0.2341 0.2170 0.1917 0.0212  -0.0112 -0.0341 978  LEU B CD1 
16507 C CD2 . LEU B 980  ? 0.2141 0.2024 0.1697 0.0220  -0.0047 -0.0309 978  LEU B CD2 
16508 N N   . ASP B 981  ? 0.1798 0.1807 0.1576 0.0241  0.0017  -0.0297 979  ASP B N   
16509 C CA  . ASP B 981  ? 0.1776 0.1805 0.1606 0.0250  0.0030  -0.0297 979  ASP B CA  
16510 C C   . ASP B 981  ? 0.1808 0.1790 0.1636 0.0254  0.0012  -0.0318 979  ASP B C   
16511 O O   . ASP B 981  ? 0.1761 0.1754 0.1640 0.0250  0.0009  -0.0316 979  ASP B O   
16512 C CB  . ASP B 981  ? 0.1806 0.1863 0.1628 0.0272  0.0067  -0.0292 979  ASP B CB  
16513 C CG  . ASP B 981  ? 0.2104 0.2221 0.1949 0.0264  0.0087  -0.0268 979  ASP B CG  
16514 O OD1 . ASP B 981  ? 0.2154 0.2292 0.2031 0.0243  0.0073  -0.0255 979  ASP B OD1 
16515 O OD2 . ASP B 981  ? 0.2455 0.2600 0.2286 0.0281  0.0117  -0.0263 979  ASP B OD2 
16516 N N   . GLU B 982  ? 0.1774 0.1702 0.1542 0.0260  0.0001  -0.0337 980  GLU B N   
16517 C CA  . GLU B 982  ? 0.1832 0.1712 0.1599 0.0260  -0.0018 -0.0357 980  GLU B CA  
16518 C C   . GLU B 982  ? 0.1808 0.1693 0.1619 0.0234  -0.0051 -0.0356 980  GLU B C   
16519 O O   . GLU B 982  ? 0.1962 0.1839 0.1810 0.0227  -0.0059 -0.0361 980  GLU B O   
16520 C CB  . GLU B 982  ? 0.1997 0.1814 0.1684 0.0270  -0.0027 -0.0379 980  GLU B CB  
16521 C CG  . GLU B 982  ? 0.2513 0.2276 0.2195 0.0262  -0.0053 -0.0400 980  GLU B CG  
16522 C CD  . GLU B 982  ? 0.3240 0.2938 0.2844 0.0264  -0.0072 -0.0423 980  GLU B CD  
16523 O OE1 . GLU B 982  ? 0.4076 0.3775 0.3647 0.0257  -0.0086 -0.0422 980  GLU B OE1 
16524 O OE2 . GLU B 982  ? 0.3209 0.2852 0.2780 0.0274  -0.0074 -0.0442 980  GLU B OE2 
16525 N N   . THR B 983  ? 0.1762 0.1660 0.1570 0.0221  -0.0069 -0.0350 981  THR B N   
16526 C CA  . THR B 983  ? 0.1758 0.1668 0.1613 0.0200  -0.0099 -0.0350 981  THR B CA  
16527 C C   . THR B 983  ? 0.1547 0.1508 0.1475 0.0195  -0.0087 -0.0333 981  THR B C   
16528 O O   . THR B 983  ? 0.1816 0.1784 0.1789 0.0183  -0.0101 -0.0336 981  THR B O   
16529 C CB  . THR B 983  ? 0.1864 0.1774 0.1695 0.0193  -0.0121 -0.0346 981  THR B CB  
16530 O OG1 . THR B 983  ? 0.2221 0.2081 0.1982 0.0197  -0.0135 -0.0363 981  THR B OG1 
16531 C CG2 . THR B 983  ? 0.2050 0.1979 0.1932 0.0176  -0.0151 -0.0346 981  THR B CG2 
16532 N N   . ILE B 984  ? 0.1471 0.1466 0.1407 0.0202  -0.0061 -0.0316 982  ILE B N   
16533 C CA  . ILE B 984  ? 0.1641 0.1681 0.1639 0.0197  -0.0049 -0.0301 982  ILE B CA  
16534 C C   . ILE B 984  ? 0.1498 0.1531 0.1522 0.0202  -0.0040 -0.0306 982  ILE B C   
16535 O O   . ILE B 984  ? 0.1569 0.1617 0.1641 0.0191  -0.0048 -0.0303 982  ILE B O   
16536 C CB  . ILE B 984  ? 0.1616 0.1694 0.1614 0.0203  -0.0024 -0.0283 982  ILE B CB  
16537 C CG1 . ILE B 984  ? 0.2079 0.2159 0.2055 0.0192  -0.0036 -0.0275 982  ILE B CG1 
16538 C CG2 . ILE B 984  ? 0.1834 0.1955 0.1892 0.0199  -0.0013 -0.0269 982  ILE B CG2 
16539 C CD1 . ILE B 984  ? 0.2241 0.2353 0.2207 0.0193  -0.0013 -0.0257 982  ILE B CD1 
16540 N N   . ALA B 985  ? 0.1685 0.1690 0.1673 0.0220  -0.0024 -0.0314 983  ALA B N   
16541 C CA  . ALA B 985  ? 0.1839 0.1828 0.1844 0.0227  -0.0016 -0.0318 983  ALA B CA  
16542 C C   . ALA B 985  ? 0.1833 0.1785 0.1847 0.0211  -0.0042 -0.0332 983  ALA B C   
16543 O O   . ALA B 985  ? 0.1781 0.1739 0.1835 0.0202  -0.0043 -0.0327 983  ALA B O   
16544 C CB  . ALA B 985  ? 0.1855 0.1816 0.1814 0.0254  0.0005  -0.0325 983  ALA B CB  
16545 N N   . HIS B 986  ? 0.1737 0.1653 0.1711 0.0204  -0.0064 -0.0348 984  HIS B N   
16546 C CA  . HIS B 986  ? 0.1828 0.1714 0.1811 0.0184  -0.0092 -0.0361 984  HIS B CA  
16547 C C   . HIS B 986  ? 0.1694 0.1626 0.1743 0.0163  -0.0105 -0.0351 984  HIS B C   
16548 O O   . HIS B 986  ? 0.1951 0.1885 0.2038 0.0150  -0.0108 -0.0350 984  HIS B O   
16549 C CB  . HIS B 986  ? 0.1974 0.1821 0.1903 0.0181  -0.0116 -0.0379 984  HIS B CB  
16550 C CG  . HIS B 986  ? 0.2144 0.1966 0.2083 0.0157  -0.0149 -0.0393 984  HIS B CG  
16551 N ND1 . HIS B 986  ? 0.2998 0.2780 0.2888 0.0152  -0.0176 -0.0411 984  HIS B ND1 
16552 C CD2 . HIS B 986  ? 0.2287 0.2122 0.2280 0.0136  -0.0161 -0.0392 984  HIS B CD2 
16553 C CE1 . HIS B 986  ? 0.2582 0.2355 0.2498 0.0128  -0.0204 -0.0420 984  HIS B CE1 
16554 N NE2 . HIS B 986  ? 0.2519 0.2325 0.2499 0.0117  -0.0194 -0.0408 984  HIS B NE2 
16555 N N   . VAL B 987  ? 0.1514 0.1481 0.1574 0.0160  -0.0112 -0.0344 985  VAL B N   
16556 C CA  . VAL B 987  ? 0.1667 0.1675 0.1785 0.0144  -0.0127 -0.0337 985  VAL B CA  
16557 C C   . VAL B 987  ? 0.1746 0.1791 0.1914 0.0143  -0.0105 -0.0322 985  VAL B C   
16558 O O   . VAL B 987  ? 0.1955 0.2018 0.2168 0.0128  -0.0112 -0.0321 985  VAL B O   
16559 C CB  . VAL B 987  ? 0.1578 0.1608 0.1690 0.0145  -0.0140 -0.0333 985  VAL B CB  
16560 C CG1 . VAL B 987  ? 0.2157 0.2232 0.2329 0.0134  -0.0150 -0.0326 985  VAL B CG1 
16561 C CG2 . VAL B 987  ? 0.1727 0.1720 0.1793 0.0142  -0.0167 -0.0349 985  VAL B CG2 
16562 N N   . THR B 988  ? 0.1487 0.1548 0.1648 0.0158  -0.0080 -0.0310 986  THR B N   
16563 C CA  . THR B 988  ? 0.1538 0.1634 0.1745 0.0157  -0.0064 -0.0295 986  THR B CA  
16564 C C   . THR B 988  ? 0.1885 0.1959 0.2101 0.0155  -0.0056 -0.0296 986  THR B C   
16565 O O   . THR B 988  ? 0.2556 0.2654 0.2813 0.0147  -0.0050 -0.0287 986  THR B O   
16566 C CB  . THR B 988  ? 0.2086 0.2209 0.2286 0.0170  -0.0041 -0.0280 986  THR B CB  
16567 O OG1 . THR B 988  ? 0.2344 0.2445 0.2507 0.0188  -0.0025 -0.0282 986  THR B OG1 
16568 C CG2 . THR B 988  ? 0.2438 0.2579 0.2629 0.0167  -0.0050 -0.0276 986  THR B CG2 
16569 N N   . SER B 989  ? 0.1922 0.1946 0.2097 0.0163  -0.0056 -0.0308 987  SER B N   
16570 C CA  . SER B 989  ? 0.2227 0.2218 0.2405 0.0160  -0.0052 -0.0310 987  SER B CA  
16571 C C   . SER B 989  ? 0.2508 0.2489 0.2712 0.0133  -0.0074 -0.0317 987  SER B C   
16572 O O   . SER B 989  ? 0.3385 0.3353 0.3607 0.0123  -0.0069 -0.0312 987  SER B O   
16573 C CB  . SER B 989  ? 0.2485 0.2418 0.2606 0.0180  -0.0046 -0.0322 987  SER B CB  
16574 O OG  . SER B 989  ? 0.3231 0.3122 0.3315 0.0172  -0.0067 -0.0341 987  SER B OG  
16575 N N   . ARG B 990  ? 0.1918 0.1907 0.2125 0.0119  -0.0097 -0.0327 988  ARG B N   
16576 C CA  . ARG B 990  ? 0.2114 0.2099 0.2347 0.0092  -0.0120 -0.0335 988  ARG B CA  
16577 C C   . ARG B 990  ? 0.1935 0.1981 0.2227 0.0077  -0.0126 -0.0328 988  ARG B C   
16578 O O   . ARG B 990  ? 0.2095 0.2152 0.2423 0.0054  -0.0136 -0.0329 988  ARG B O   
16579 C CB  . ARG B 990  ? 0.2251 0.2197 0.2443 0.0087  -0.0146 -0.0355 988  ARG B CB  
16580 C CG  . ARG B 990  ? 0.3167 0.3046 0.3290 0.0103  -0.0141 -0.0367 988  ARG B CG  
16581 C CD  . ARG B 990  ? 0.3105 0.2929 0.3216 0.0091  -0.0144 -0.0374 988  ARG B CD  
16582 N NE  . ARG B 990  ? 0.2530 0.2321 0.2628 0.0066  -0.0177 -0.0392 988  ARG B NE  
16583 C CZ  . ARG B 990  ? 0.2403 0.2141 0.2489 0.0047  -0.0186 -0.0400 988  ARG B CZ  
16584 N NH1 . ARG B 990  ? 0.2792 0.2503 0.2877 0.0052  -0.0167 -0.0391 988  ARG B NH1 
16585 N NH2 . ARG B 990  ? 0.2535 0.2247 0.2609 0.0023  -0.0218 -0.0417 988  ARG B NH2 
16586 N N   . ILE B 991  ? 0.1757 0.1844 0.2060 0.0090  -0.0121 -0.0320 989  ILE B N   
16587 C CA  . ILE B 991  ? 0.1788 0.1931 0.2144 0.0081  -0.0126 -0.0314 989  ILE B CA  
16588 C C   . ILE B 991  ? 0.1748 0.1915 0.2141 0.0076  -0.0105 -0.0300 989  ILE B C   
16589 O O   . ILE B 991  ? 0.1979 0.2130 0.2354 0.0087  -0.0084 -0.0291 989  ILE B O   
16590 C CB  . ILE B 991  ? 0.1576 0.1741 0.1923 0.0097  -0.0127 -0.0310 989  ILE B CB  
16591 C CG1 . ILE B 991  ? 0.1935 0.2149 0.2328 0.0091  -0.0139 -0.0309 989  ILE B CG1 
16592 C CG2 . ILE B 991  ? 0.2100 0.2271 0.2434 0.0113  -0.0100 -0.0296 989  ILE B CG2 
16593 C CD1 . ILE B 991  ? 0.2389 0.2603 0.2791 0.0080  -0.0170 -0.0323 989  ILE B CD1 
16594 N N   . LYS B 992  ? 0.1624 0.1831 0.2066 0.0060  -0.0110 -0.0298 990  LYS B N   
16595 C CA  . LYS B 992  ? 0.1848 0.2082 0.2324 0.0053  -0.0090 -0.0284 990  LYS B CA  
16596 C C   . LYS B 992  ? 0.2115 0.2404 0.2625 0.0059  -0.0086 -0.0279 990  LYS B C   
16597 O O   . LYS B 992  ? 0.2574 0.2902 0.3126 0.0047  -0.0094 -0.0282 990  LYS B O   
16598 C CB  . LYS B 992  ? 0.2144 0.2374 0.2646 0.0025  -0.0095 -0.0286 990  LYS B CB  
16599 C CG  . LYS B 992  ? 0.2352 0.2516 0.2815 0.0018  -0.0099 -0.0292 990  LYS B CG  
16600 C CD  . LYS B 992  ? 0.3772 0.3904 0.4206 0.0033  -0.0076 -0.0280 990  LYS B CD  
16601 C CE  . LYS B 992  ? 0.4658 0.4723 0.5059 0.0024  -0.0079 -0.0284 990  LYS B CE  
16602 N NZ  . LYS B 992  ? 0.6061 0.6094 0.6433 0.0045  -0.0058 -0.0273 990  LYS B NZ  
16603 N N   . ALA B 993  ? 0.1747 0.2039 0.2238 0.0077  -0.0075 -0.0272 991  ALA B N   
16604 C CA  . ALA B 993  ? 0.1454 0.1789 0.1969 0.0085  -0.0072 -0.0268 991  ALA B CA  
16605 C C   . ALA B 993  ? 0.1393 0.1729 0.1894 0.0095  -0.0052 -0.0254 991  ALA B C   
16606 O O   . ALA B 993  ? 0.1634 0.1942 0.2103 0.0102  -0.0043 -0.0250 991  ALA B O   
16607 C CB  . ALA B 993  ? 0.1597 0.1934 0.2100 0.0095  -0.0092 -0.0276 991  ALA B CB  
16608 N N   . GLY B 994  ? 0.1227 0.1597 0.1751 0.0097  -0.0044 -0.0249 992  GLY B N   
16609 C CA  . GLY B 994  ? 0.1105 0.1481 0.1619 0.0103  -0.0026 -0.0236 992  GLY B CA  
16610 C C   . GLY B 994  ? 0.1046 0.1415 0.1532 0.0116  -0.0028 -0.0233 992  GLY B C   
16611 O O   . GLY B 994  ? 0.1083 0.1450 0.1555 0.0120  -0.0015 -0.0222 992  GLY B O   
16612 N N   . ASN B 995  ? 0.0971 0.1337 0.1450 0.0121  -0.0044 -0.0241 993  ASN B N   
16613 C CA  . ASN B 995  ? 0.1046 0.1403 0.1496 0.0128  -0.0046 -0.0238 993  ASN B CA  
16614 C C   . ASN B 995  ? 0.1080 0.1411 0.1503 0.0132  -0.0062 -0.0245 993  ASN B C   
16615 O O   . ASN B 995  ? 0.1304 0.1635 0.1733 0.0133  -0.0080 -0.0255 993  ASN B O   
16616 C CB  . ASN B 995  ? 0.1043 0.1417 0.1503 0.0132  -0.0051 -0.0239 993  ASN B CB  
16617 C CG  . ASN B 995  ? 0.1260 0.1653 0.1729 0.0130  -0.0035 -0.0229 993  ASN B CG  
16618 O OD1 . ASN B 995  ? 0.1148 0.1561 0.1645 0.0126  -0.0027 -0.0230 993  ASN B OD1 
16619 N ND2 . ASN B 995  ? 0.1351 0.1738 0.1797 0.0131  -0.0030 -0.0221 993  ASN B ND2 
16620 N N   . LEU B 996  ? 0.0980 0.1292 0.1373 0.0134  -0.0054 -0.0240 994  LEU B N   
16621 C CA  . LEU B 996  ? 0.0933 0.1218 0.1292 0.0137  -0.0065 -0.0246 994  LEU B CA  
16622 C C   . LEU B 996  ? 0.1388 0.1667 0.1717 0.0140  -0.0065 -0.0239 994  LEU B C   
16623 O O   . LEU B 996  ? 0.1316 0.1610 0.1645 0.0139  -0.0051 -0.0227 994  LEU B O   
16624 C CB  . LEU B 996  ? 0.1223 0.1488 0.1563 0.0140  -0.0055 -0.0248 994  LEU B CB  
16625 C CG  . LEU B 996  ? 0.1328 0.1592 0.1693 0.0135  -0.0051 -0.0251 994  LEU B CG  
16626 C CD1 . LEU B 996  ? 0.1791 0.2024 0.2127 0.0141  -0.0041 -0.0253 994  LEU B CD1 
16627 C CD2 . LEU B 996  ? 0.1759 0.2023 0.2145 0.0125  -0.0071 -0.0264 994  LEU B CD2 
16628 N N   . TYR B 997  ? 0.1172 0.1430 0.1474 0.0142  -0.0082 -0.0244 995  TYR B N   
16629 C CA  . TYR B 997  ? 0.1089 0.1335 0.1357 0.0142  -0.0084 -0.0235 995  TYR B CA  
16630 C C   . TYR B 997  ? 0.1276 0.1493 0.1499 0.0145  -0.0090 -0.0239 995  TYR B C   
16631 O O   . TYR B 997  ? 0.1248 0.1448 0.1465 0.0147  -0.0109 -0.0251 995  TYR B O   
16632 C CB  . TYR B 997  ? 0.1173 0.1416 0.1446 0.0143  -0.0102 -0.0237 995  TYR B CB  
16633 C CG  . TYR B 997  ? 0.1104 0.1374 0.1414 0.0142  -0.0094 -0.0234 995  TYR B CG  
16634 C CD1 . TYR B 997  ? 0.1461 0.1739 0.1765 0.0136  -0.0082 -0.0222 995  TYR B CD1 
16635 C CD2 . TYR B 997  ? 0.1236 0.1526 0.1585 0.0145  -0.0099 -0.0244 995  TYR B CD2 
16636 C CE1 . TYR B 997  ? 0.1403 0.1701 0.1734 0.0136  -0.0076 -0.0221 995  TYR B CE1 
16637 C CE2 . TYR B 997  ? 0.1322 0.1636 0.1700 0.0145  -0.0090 -0.0242 995  TYR B CE2 
16638 C CZ  . TYR B 997  ? 0.1404 0.1719 0.1770 0.0141  -0.0079 -0.0231 995  TYR B CZ  
16639 O OH  . TYR B 997  ? 0.1407 0.1741 0.1793 0.0141  -0.0071 -0.0230 995  TYR B OH  
16640 N N   . ILE B 998  ? 0.1112 0.1325 0.1304 0.0143  -0.0075 -0.0229 996  ILE B N   
16641 C CA  . ILE B 998  ? 0.1269 0.1456 0.1414 0.0147  -0.0076 -0.0231 996  ILE B CA  
16642 C C   . ILE B 998  ? 0.1216 0.1390 0.1322 0.0140  -0.0080 -0.0220 996  ILE B C   
16643 O O   . ILE B 998  ? 0.1322 0.1513 0.1428 0.0133  -0.0065 -0.0205 996  ILE B O   
16644 C CB  . ILE B 998  ? 0.1344 0.1540 0.1481 0.0152  -0.0051 -0.0229 996  ILE B CB  
16645 C CG1 . ILE B 998  ? 0.2001 0.2203 0.2172 0.0157  -0.0047 -0.0238 996  ILE B CG1 
16646 C CG2 . ILE B 998  ? 0.1536 0.1702 0.1619 0.0158  -0.0050 -0.0235 996  ILE B CG2 
16647 C CD1 . ILE B 998  ? 0.2392 0.2572 0.2567 0.0157  -0.0068 -0.0254 996  ILE B CD1 
16648 N N   . ASN B 999  ? 0.1269 0.1410 0.1341 0.0142  -0.0102 -0.0225 997  ASN B N   
16649 C CA  . ASN B 999  ? 0.1304 0.1420 0.1328 0.0136  -0.0109 -0.0214 997  ASN B CA  
16650 C C   . ASN B 999  ? 0.1245 0.1364 0.1282 0.0128  -0.0114 -0.0203 997  ASN B C   
16651 O O   . ASN B 999  ? 0.1508 0.1617 0.1515 0.0117  -0.0107 -0.0188 997  ASN B O   
16652 C CB  . ASN B 999  ? 0.1511 0.1628 0.1496 0.0132  -0.0085 -0.0204 997  ASN B CB  
16653 C CG  . ASN B 999  ? 0.1274 0.1371 0.1227 0.0142  -0.0084 -0.0217 997  ASN B CG  
16654 O OD1 . ASN B 999  ? 0.1609 0.1680 0.1549 0.0147  -0.0109 -0.0229 997  ASN B OD1 
16655 N ND2 . ASN B 999  ? 0.1422 0.1534 0.1362 0.0146  -0.0057 -0.0214 997  ASN B ND2 
16656 N N   . ARG B 1000 ? 0.1287 0.1418 0.1367 0.0133  -0.0126 -0.0211 998  ARG B N   
16657 C CA  . ARG B 1000 ? 0.1169 0.1297 0.1260 0.0130  -0.0133 -0.0205 998  ARG B CA  
16658 C C   . ARG B 1000 ? 0.1470 0.1603 0.1597 0.0143  -0.0153 -0.0219 998  ARG B C   
16659 O O   . ARG B 1000 ? 0.1660 0.1802 0.1805 0.0151  -0.0160 -0.0231 998  ARG B O   
16660 C CB  . ARG B 1000 ? 0.1398 0.1556 0.1514 0.0120  -0.0111 -0.0195 998  ARG B CB  
16661 C CG  . ARG B 1000 ? 0.1292 0.1488 0.1453 0.0124  -0.0094 -0.0202 998  ARG B CG  
16662 C CD  . ARG B 1000 ? 0.1287 0.1511 0.1479 0.0118  -0.0082 -0.0195 998  ARG B CD  
16663 N NE  . ARG B 1000 ? 0.1247 0.1463 0.1455 0.0123  -0.0098 -0.0202 998  ARG B NE  
16664 C CZ  . ARG B 1000 ? 0.1287 0.1519 0.1517 0.0120  -0.0093 -0.0200 998  ARG B CZ  
16665 N NH1 . ARG B 1000 ? 0.1345 0.1603 0.1586 0.0110  -0.0075 -0.0190 998  ARG B NH1 
16666 N NH2 . ARG B 1000 ? 0.1458 0.1681 0.1699 0.0128  -0.0107 -0.0209 998  ARG B NH2 
16667 N N   . ASN B 1001 ? 0.1396 0.1523 0.1532 0.0146  -0.0162 -0.0218 999  ASN B N   
16668 C CA  . ASN B 1001 ? 0.1322 0.1463 0.1497 0.0161  -0.0177 -0.0231 999  ASN B CA  
16669 C C   . ASN B 1001 ? 0.1295 0.1481 0.1523 0.0159  -0.0158 -0.0237 999  ASN B C   
16670 O O   . ASN B 1001 ? 0.1341 0.1543 0.1574 0.0149  -0.0136 -0.0229 999  ASN B O   
16671 C CB  . ASN B 1001 ? 0.1316 0.1433 0.1479 0.0168  -0.0192 -0.0229 999  ASN B CB  
16672 C CG  . ASN B 1001 ? 0.1884 0.2008 0.2055 0.0158  -0.0175 -0.0222 999  ASN B CG  
16673 O OD1 . ASN B 1001 ? 0.1564 0.1725 0.1772 0.0155  -0.0158 -0.0225 999  ASN B OD1 
16674 N ND2 . ASN B 1001 ? 0.2358 0.2442 0.2488 0.0153  -0.0184 -0.0213 999  ASN B ND2 
16675 N N   . ILE B 1002 ? 0.1242 0.1450 0.1511 0.0170  -0.0168 -0.0249 1000 ILE B N   
16676 C CA  . ILE B 1002 ? 0.1160 0.1409 0.1477 0.0167  -0.0151 -0.0253 1000 ILE B CA  
16677 C C   . ILE B 1002 ? 0.1306 0.1575 0.1651 0.0172  -0.0145 -0.0255 1000 ILE B C   
16678 O O   . ILE B 1002 ? 0.1249 0.1553 0.1636 0.0172  -0.0135 -0.0260 1000 ILE B O   
16679 C CB  . ILE B 1002 ? 0.1175 0.1440 0.1519 0.0169  -0.0162 -0.0265 1000 ILE B CB  
16680 C CG1 . ILE B 1002 ? 0.1221 0.1498 0.1590 0.0184  -0.0185 -0.0276 1000 ILE B CG1 
16681 C CG2 . ILE B 1002 ? 0.1439 0.1677 0.1745 0.0165  -0.0168 -0.0265 1000 ILE B CG2 
16682 C CD1 . ILE B 1002 ? 0.1477 0.1782 0.1883 0.0181  -0.0195 -0.0287 1000 ILE B CD1 
16683 N N   . ILE B 1003 ? 0.1401 0.1646 0.1721 0.0176  -0.0151 -0.0251 1001 ILE B N   
16684 C CA  . ILE B 1003 ? 0.1364 0.1622 0.1703 0.0184  -0.0147 -0.0255 1001 ILE B CA  
16685 C C   . ILE B 1003 ? 0.1275 0.1520 0.1590 0.0172  -0.0133 -0.0244 1001 ILE B C   
16686 O O   . ILE B 1003 ? 0.1406 0.1633 0.1691 0.0157  -0.0129 -0.0233 1001 ILE B O   
16687 C CB  . ILE B 1003 ? 0.1577 0.1815 0.1909 0.0205  -0.0170 -0.0264 1001 ILE B CB  
16688 C CG1 . ILE B 1003 ? 0.1746 0.1927 0.2020 0.0203  -0.0185 -0.0256 1001 ILE B CG1 
16689 C CG2 . ILE B 1003 ? 0.1526 0.1789 0.1891 0.0218  -0.0184 -0.0275 1001 ILE B CG2 
16690 C CD1 . ILE B 1003 ? 0.2187 0.2338 0.2446 0.0226  -0.0207 -0.0263 1001 ILE B CD1 
16691 N N   . GLY B 1004 ? 0.1441 0.1697 0.1770 0.0177  -0.0127 -0.0249 1002 GLY B N   
16692 C CA  . GLY B 1004 ? 0.1362 0.1604 0.1667 0.0165  -0.0119 -0.0240 1002 GLY B CA  
16693 C C   . GLY B 1004 ? 0.1417 0.1686 0.1733 0.0147  -0.0099 -0.0229 1002 GLY B C   
16694 O O   . GLY B 1004 ? 0.1644 0.1899 0.1934 0.0132  -0.0096 -0.0218 1002 GLY B O   
16695 N N   . ALA B 1005 ? 0.1265 0.1570 0.1618 0.0149  -0.0085 -0.0232 1003 ALA B N   
16696 C CA  . ALA B 1005 ? 0.1278 0.1607 0.1641 0.0137  -0.0067 -0.0222 1003 ALA B CA  
16697 C C   . ALA B 1005 ? 0.1473 0.1800 0.1822 0.0128  -0.0062 -0.0215 1003 ALA B C   
16698 O O   . ALA B 1005 ? 0.1875 0.2196 0.2221 0.0135  -0.0066 -0.0223 1003 ALA B O   
16699 C CB  . ALA B 1005 ? 0.1263 0.1624 0.1665 0.0140  -0.0055 -0.0226 1003 ALA B CB  
16700 N N   . VAL B 1006 ? 0.1183 0.1517 0.1522 0.0115  -0.0054 -0.0202 1004 VAL B N   
16701 C CA  . VAL B 1006 ? 0.1148 0.1482 0.1471 0.0102  -0.0053 -0.0194 1004 VAL B CA  
16702 C C   . VAL B 1006 ? 0.1105 0.1474 0.1451 0.0100  -0.0038 -0.0189 1004 VAL B C   
16703 O O   . VAL B 1006 ? 0.1034 0.1424 0.1398 0.0101  -0.0027 -0.0182 1004 VAL B O   
16704 C CB  . VAL B 1006 ? 0.1148 0.1472 0.1446 0.0086  -0.0056 -0.0181 1004 VAL B CB  
16705 C CG1 . VAL B 1006 ? 0.1320 0.1655 0.1610 0.0069  -0.0054 -0.0171 1004 VAL B CG1 
16706 C CG2 . VAL B 1006 ? 0.1330 0.1612 0.1597 0.0085  -0.0073 -0.0184 1004 VAL B CG2 
16707 N N   . VAL B 1007 ? 0.1062 0.1432 0.1404 0.0100  -0.0038 -0.0192 1005 VAL B N   
16708 C CA  . VAL B 1007 ? 0.1145 0.1543 0.1501 0.0098  -0.0025 -0.0186 1005 VAL B CA  
16709 C C   . VAL B 1007 ? 0.1100 0.1520 0.1460 0.0088  -0.0020 -0.0170 1005 VAL B C   
16710 O O   . VAL B 1007 ? 0.1063 0.1479 0.1406 0.0075  -0.0027 -0.0162 1005 VAL B O   
16711 C CB  . VAL B 1007 ? 0.1043 0.1431 0.1380 0.0096  -0.0029 -0.0191 1005 VAL B CB  
16712 C CG1 . VAL B 1007 ? 0.1265 0.1680 0.1609 0.0092  -0.0019 -0.0182 1005 VAL B CG1 
16713 C CG2 . VAL B 1007 ? 0.1285 0.1660 0.1624 0.0112  -0.0031 -0.0208 1005 VAL B CG2 
16714 N N   . GLY B 1008 ? 0.1072 0.1515 0.1454 0.0094  -0.0008 -0.0164 1006 GLY B N   
16715 C CA  . GLY B 1008 ? 0.1071 0.1538 0.1459 0.0090  -0.0002 -0.0149 1006 GLY B CA  
16716 C C   . GLY B 1008 ? 0.1089 0.1558 0.1477 0.0090  -0.0001 -0.0145 1006 GLY B C   
16717 O O   . GLY B 1008 ? 0.1347 0.1840 0.1743 0.0089  0.0006  -0.0133 1006 GLY B O   
16718 N N   . VAL B 1009 ? 0.1121 0.1565 0.1500 0.0091  -0.0007 -0.0154 1007 VAL B N   
16719 C CA  . VAL B 1009 ? 0.1052 0.1492 0.1423 0.0091  -0.0005 -0.0151 1007 VAL B CA  
16720 C C   . VAL B 1009 ? 0.1065 0.1489 0.1443 0.0104  -0.0004 -0.0162 1007 VAL B C   
16721 O O   . VAL B 1009 ? 0.1270 0.1699 0.1651 0.0111  0.0004  -0.0159 1007 VAL B O   
16722 C CB  . VAL B 1009 ? 0.1109 0.1529 0.1453 0.0078  -0.0017 -0.0150 1007 VAL B CB  
16723 C CG1 . VAL B 1009 ? 0.1210 0.1630 0.1544 0.0077  -0.0013 -0.0145 1007 VAL B CG1 
16724 C CG2 . VAL B 1009 ? 0.1197 0.1631 0.1535 0.0061  -0.0021 -0.0140 1007 VAL B CG2 
16725 N N   . GLN B 1010 ? 0.1034 0.1439 0.1412 0.0108  -0.0013 -0.0174 1008 GLN B N   
16726 C CA  . GLN B 1010 ? 0.0937 0.1336 0.1331 0.0117  -0.0013 -0.0184 1008 GLN B CA  
16727 C C   . GLN B 1010 ? 0.1283 0.1692 0.1697 0.0119  -0.0010 -0.0189 1008 GLN B C   
16728 O O   . GLN B 1010 ? 0.1309 0.1712 0.1727 0.0123  -0.0018 -0.0200 1008 GLN B O   
16729 C CB  . GLN B 1010 ? 0.1128 0.1502 0.1509 0.0120  -0.0027 -0.0195 1008 GLN B CB  
16730 C CG  . GLN B 1010 ? 0.1142 0.1502 0.1495 0.0117  -0.0030 -0.0189 1008 GLN B CG  
16731 C CD  . GLN B 1010 ? 0.1195 0.1539 0.1522 0.0108  -0.0040 -0.0185 1008 GLN B CD  
16732 O OE1 . GLN B 1010 ? 0.1283 0.1614 0.1608 0.0109  -0.0050 -0.0191 1008 GLN B OE1 
16733 N NE2 . GLN B 1010 ? 0.1232 0.1576 0.1539 0.0099  -0.0036 -0.0174 1008 GLN B NE2 
16734 N N   . PRO B 1011 ? 0.1094 0.1520 0.1521 0.0119  0.0002  -0.0182 1009 PRO B N   
16735 C CA  . PRO B 1011 ? 0.1239 0.1677 0.1685 0.0120  0.0008  -0.0185 1009 PRO B CA  
16736 C C   . PRO B 1011 ? 0.1246 0.1679 0.1709 0.0123  0.0004  -0.0197 1009 PRO B C   
16737 O O   . PRO B 1011 ? 0.1136 0.1558 0.1600 0.0124  0.0001  -0.0200 1009 PRO B O   
16738 C CB  . PRO B 1011 ? 0.1289 0.1736 0.1741 0.0120  0.0021  -0.0173 1009 PRO B CB  
16739 C CG  . PRO B 1011 ? 0.1222 0.1675 0.1660 0.0119  0.0021  -0.0162 1009 PRO B CG  
16740 C CD  . PRO B 1011 ? 0.1258 0.1696 0.1684 0.0119  0.0012  -0.0169 1009 PRO B CD  
16741 N N   . PHE B 1012 ? 0.0960 0.1403 0.1435 0.0125  0.0003  -0.0206 1010 PHE B N   
16742 C CA  . PHE B 1012 ? 0.1094 0.1539 0.1586 0.0129  -0.0006 -0.0219 1010 PHE B CA  
16743 C C   . PHE B 1012 ? 0.1100 0.1568 0.1624 0.0125  0.0004  -0.0221 1010 PHE B C   
16744 O O   . PHE B 1012 ? 0.1205 0.1690 0.1736 0.0124  0.0016  -0.0218 1010 PHE B O   
16745 C CB  . PHE B 1012 ? 0.1133 0.1573 0.1617 0.0138  -0.0016 -0.0228 1010 PHE B CB  
16746 C CG  . PHE B 1012 ? 0.1012 0.1457 0.1514 0.0147  -0.0029 -0.0241 1010 PHE B CG  
16747 C CD1 . PHE B 1012 ? 0.1489 0.1913 0.1980 0.0148  -0.0044 -0.0244 1010 PHE B CD1 
16748 C CD2 . PHE B 1012 ? 0.1454 0.1926 0.1985 0.0153  -0.0025 -0.0250 1010 PHE B CD2 
16749 C CE1 . PHE B 1012 ? 0.1275 0.1705 0.1783 0.0156  -0.0059 -0.0255 1010 PHE B CE1 
16750 C CE2 . PHE B 1012 ? 0.1605 0.2089 0.2159 0.0162  -0.0039 -0.0262 1010 PHE B CE2 
16751 C CZ  . PHE B 1012 ? 0.1582 0.2044 0.2124 0.0164  -0.0057 -0.0264 1010 PHE B CZ  
16752 N N   . GLY B 1013 ? 0.1138 0.1605 0.1679 0.0121  -0.0002 -0.0226 1011 GLY B N   
16753 C CA  . GLY B 1013 ? 0.1157 0.1647 0.1731 0.0113  0.0005  -0.0228 1011 GLY B CA  
16754 C C   . GLY B 1013 ? 0.1179 0.1654 0.1759 0.0104  0.0000  -0.0229 1011 GLY B C   
16755 O O   . GLY B 1013 ? 0.1214 0.1660 0.1769 0.0104  -0.0003 -0.0225 1011 GLY B O   
16756 N N   . GLY B 1014 ? 0.1485 0.1980 0.2097 0.0094  -0.0003 -0.0235 1012 GLY B N   
16757 C CA  . GLY B 1014 ? 0.1425 0.1903 0.2042 0.0082  -0.0010 -0.0238 1012 GLY B CA  
16758 C C   . GLY B 1014 ? 0.2093 0.2581 0.2732 0.0063  0.0002  -0.0231 1012 GLY B C   
16759 O O   . GLY B 1014 ? 0.2602 0.3105 0.3246 0.0059  0.0019  -0.0221 1012 GLY B O   
16760 N N   . ARG B 1015 ? 0.2009 0.2488 0.2660 0.0049  -0.0010 -0.0237 1013 ARG B N   
16761 C CA  . ARG B 1015 ? 0.2799 0.3273 0.3464 0.0025  -0.0002 -0.0231 1013 ARG B CA  
16762 C C   . ARG B 1015 ? 0.2190 0.2700 0.2899 0.0008  -0.0014 -0.0240 1013 ARG B C   
16763 O O   . ARG B 1015 ? 0.1731 0.2269 0.2458 0.0019  -0.0028 -0.0252 1013 ARG B O   
16764 C CB  . ARG B 1015 ? 0.2693 0.3107 0.3321 0.0022  -0.0007 -0.0229 1013 ARG B CB  
16765 C CG  . ARG B 1015 ? 0.2942 0.3332 0.3551 0.0031  -0.0029 -0.0242 1013 ARG B CG  
16766 C CD  . ARG B 1015 ? 0.3426 0.3764 0.4011 0.0020  -0.0037 -0.0246 1013 ARG B CD  
16767 N NE  . ARG B 1015 ? 0.3997 0.4345 0.4612 -0.0008 -0.0045 -0.0249 1013 ARG B NE  
16768 C CZ  . ARG B 1015 ? 0.4056 0.4428 0.4698 -0.0018 -0.0065 -0.0262 1013 ARG B CZ  
16769 N NH1 . ARG B 1015 ? 0.3185 0.3566 0.3821 -0.0001 -0.0081 -0.0273 1013 ARG B NH1 
16770 N NH2 . ARG B 1015 ? 0.4533 0.4918 0.5206 -0.0048 -0.0070 -0.0263 1013 ARG B NH2 
16771 N N   . GLY B 1016 ? 0.1823 0.2332 0.2548 -0.0018 -0.0008 -0.0234 1014 GLY B N   
16772 C CA  . GLY B 1016 ? 0.2100 0.2649 0.2872 -0.0039 -0.0020 -0.0243 1014 GLY B CA  
16773 C C   . GLY B 1016 ? 0.1930 0.2552 0.2748 -0.0031 -0.0013 -0.0246 1014 GLY B C   
16774 O O   . GLY B 1016 ? 0.2106 0.2752 0.2928 -0.0025 0.0010  -0.0237 1014 GLY B O   
16775 N N   . LEU B 1017 ? 0.1850 0.2509 0.2701 -0.0027 -0.0034 -0.0260 1015 LEU B N   
16776 C CA  . LEU B 1017 ? 0.1968 0.2698 0.2864 -0.0014 -0.0030 -0.0266 1015 LEU B CA  
16777 C C   . LEU B 1017 ? 0.1803 0.2527 0.2673 0.0021  -0.0025 -0.0268 1015 LEU B C   
16778 O O   . LEU B 1017 ? 0.1868 0.2643 0.2768 0.0038  -0.0019 -0.0274 1015 LEU B O   
16779 C CB  . LEU B 1017 ? 0.2231 0.2999 0.3168 -0.0017 -0.0057 -0.0280 1015 LEU B CB  
16780 C CG  . LEU B 1017 ? 0.2274 0.3060 0.3247 -0.0056 -0.0065 -0.0278 1015 LEU B CG  
16781 C CD1 . LEU B 1017 ? 0.2136 0.2952 0.3141 -0.0056 -0.0098 -0.0293 1015 LEU B CD1 
16782 C CD2 . LEU B 1017 ? 0.2499 0.3349 0.3520 -0.0075 -0.0038 -0.0268 1015 LEU B CD2 
16783 N N   . SER B 1018 ? 0.1448 0.2113 0.2264 0.0033  -0.0026 -0.0265 1016 SER B N   
16784 C CA  . SER B 1018 ? 0.1461 0.2116 0.2250 0.0061  -0.0023 -0.0266 1016 SER B CA  
16785 C C   . SER B 1018 ? 0.1417 0.2076 0.2194 0.0063  0.0005  -0.0255 1016 SER B C   
16786 O O   . SER B 1018 ? 0.1621 0.2279 0.2379 0.0084  0.0008  -0.0257 1016 SER B O   
16787 C CB  . SER B 1018 ? 0.1316 0.1912 0.2055 0.0072  -0.0037 -0.0267 1016 SER B CB  
16788 O OG  . SER B 1018 ? 0.1746 0.2338 0.2490 0.0074  -0.0063 -0.0278 1016 SER B OG  
16789 N N   . GLY B 1019 ? 0.1702 0.2360 0.2482 0.0041  0.0022  -0.0243 1017 GLY B N   
16790 C CA  . GLY B 1019 ? 0.2258 0.2928 0.3029 0.0042  0.0047  -0.0232 1017 GLY B CA  
16791 C C   . GLY B 1019 ? 0.1778 0.2413 0.2525 0.0024  0.0060  -0.0215 1017 GLY B C   
16792 O O   . GLY B 1019 ? 0.1887 0.2487 0.2625 0.0010  0.0051  -0.0213 1017 GLY B O   
16793 N N   . THR B 1020 ? 0.1603 0.2244 0.2335 0.0026  0.0081  -0.0205 1018 THR B N   
16794 C CA  . THR B 1020 ? 0.1908 0.2519 0.2616 0.0011  0.0095  -0.0187 1018 THR B CA  
16795 C C   . THR B 1020 ? 0.1768 0.2330 0.2430 0.0025  0.0090  -0.0180 1018 THR B C   
16796 O O   . THR B 1020 ? 0.1942 0.2469 0.2582 0.0016  0.0095  -0.0166 1018 THR B O   
16797 C CB  . THR B 1020 ? 0.1580 0.2224 0.2290 0.0007  0.0120  -0.0177 1018 THR B CB  
16798 O OG1 . THR B 1020 ? 0.1469 0.2121 0.2160 0.0032  0.0121  -0.0184 1018 THR B OG1 
16799 C CG2 . THR B 1020 ? 0.1887 0.2590 0.2647 -0.0007 0.0129  -0.0182 1018 THR B CG2 
16800 N N   . GLY B 1021 ? 0.1448 0.2008 0.2095 0.0047  0.0081  -0.0188 1019 GLY B N   
16801 C CA  . GLY B 1021 ? 0.1366 0.1898 0.1975 0.0059  0.0081  -0.0180 1019 GLY B CA  
16802 C C   . GLY B 1021 ? 0.1625 0.2167 0.2220 0.0057  0.0099  -0.0167 1019 GLY B C   
16803 O O   . GLY B 1021 ? 0.1532 0.2104 0.2144 0.0048  0.0113  -0.0166 1019 GLY B O   
16804 N N   . PRO B 1022 ? 0.1105 0.1626 0.1667 0.0067  0.0098  -0.0158 1020 PRO B N   
16805 C CA  . PRO B 1022 ? 0.1164 0.1660 0.1707 0.0078  0.0085  -0.0159 1020 PRO B CA  
16806 C C   . PRO B 1022 ? 0.1255 0.1760 0.1798 0.0090  0.0073  -0.0173 1020 PRO B C   
16807 O O   . PRO B 1022 ? 0.1310 0.1839 0.1864 0.0093  0.0075  -0.0183 1020 PRO B O   
16808 C CB  . PRO B 1022 ? 0.1410 0.1897 0.1925 0.0082  0.0091  -0.0143 1020 PRO B CB  
16809 C CG  . PRO B 1022 ? 0.1667 0.2177 0.2179 0.0079  0.0103  -0.0141 1020 PRO B CG  
16810 C CD  . PRO B 1022 ? 0.1413 0.1940 0.1954 0.0065  0.0112  -0.0145 1020 PRO B CD  
16811 N N   . LYS B 1023 ? 0.1093 0.1579 0.1623 0.0097  0.0061  -0.0174 1021 LYS B N   
16812 C CA  . LYS B 1023 ? 0.1095 0.1582 0.1619 0.0106  0.0048  -0.0186 1021 LYS B CA  
16813 C C   . LYS B 1023 ? 0.1028 0.1524 0.1534 0.0111  0.0050  -0.0185 1021 LYS B C   
16814 O O   . LYS B 1023 ? 0.1127 0.1621 0.1616 0.0110  0.0055  -0.0173 1021 LYS B O   
16815 C CB  . LYS B 1023 ? 0.1079 0.1544 0.1587 0.0111  0.0038  -0.0184 1021 LYS B CB  
16816 C CG  . LYS B 1023 ? 0.1059 0.1509 0.1576 0.0109  0.0032  -0.0190 1021 LYS B CG  
16817 C CD  . LYS B 1023 ? 0.1054 0.1485 0.1550 0.0115  0.0027  -0.0187 1021 LYS B CD  
16818 C CE  . LYS B 1023 ? 0.1159 0.1570 0.1654 0.0115  0.0018  -0.0196 1021 LYS B CE  
16819 N NZ  . LYS B 1023 ? 0.1045 0.1458 0.1542 0.0117  0.0004  -0.0209 1021 LYS B NZ  
16820 N N   . ALA B 1024 ? 0.1226 0.1728 0.1735 0.0117  0.0043  -0.0198 1022 ALA B N   
16821 C CA  . ALA B 1024 ? 0.1033 0.1530 0.1517 0.0123  0.0040  -0.0201 1022 ALA B CA  
16822 C C   . ALA B 1024 ? 0.1097 0.1574 0.1558 0.0121  0.0028  -0.0195 1022 ALA B C   
16823 O O   . ALA B 1024 ? 0.1369 0.1835 0.1833 0.0122  0.0020  -0.0196 1022 ALA B O   
16824 C CB  . ALA B 1024 ? 0.1191 0.1693 0.1682 0.0134  0.0034  -0.0217 1022 ALA B CB  
16825 N N   . GLY B 1025 ? 0.0891 0.1365 0.1328 0.0119  0.0027  -0.0189 1023 GLY B N   
16826 C CA  . GLY B 1025 ? 0.0986 0.1448 0.1405 0.0114  0.0017  -0.0183 1023 GLY B CA  
16827 C C   . GLY B 1025 ? 0.0981 0.1451 0.1409 0.0111  0.0021  -0.0169 1023 GLY B C   
16828 O O   . GLY B 1025 ? 0.1180 0.1646 0.1600 0.0108  0.0015  -0.0165 1023 GLY B O   
16829 N N   . GLY B 1026 ? 0.1150 0.1630 0.1590 0.0112  0.0033  -0.0162 1024 GLY B N   
16830 C CA  . GLY B 1026 ? 0.1003 0.1485 0.1448 0.0114  0.0037  -0.0150 1024 GLY B CA  
16831 C C   . GLY B 1026 ? 0.0936 0.1428 0.1377 0.0113  0.0045  -0.0137 1024 GLY B C   
16832 O O   . GLY B 1026 ? 0.0985 0.1482 0.1417 0.0110  0.0049  -0.0137 1024 GLY B O   
16833 N N   . PRO B 1027 ? 0.0864 0.1357 0.1307 0.0118  0.0048  -0.0125 1025 PRO B N   
16834 C CA  . PRO B 1027 ? 0.0727 0.1229 0.1161 0.0120  0.0052  -0.0109 1025 PRO B CA  
16835 C C   . PRO B 1027 ? 0.1075 0.1566 0.1508 0.0119  0.0062  -0.0103 1025 PRO B C   
16836 O O   . PRO B 1027 ? 0.1073 0.1569 0.1494 0.0120  0.0064  -0.0090 1025 PRO B O   
16837 C CB  . PRO B 1027 ? 0.1287 0.1794 0.1724 0.0130  0.0050  -0.0099 1025 PRO B CB  
16838 C CG  . PRO B 1027 ? 0.1255 0.1744 0.1701 0.0134  0.0052  -0.0109 1025 PRO B CG  
16839 C CD  . PRO B 1027 ? 0.1062 0.1547 0.1510 0.0125  0.0047  -0.0125 1025 PRO B CD  
16840 N N   . LEU B 1028 ? 0.1160 0.1639 0.1606 0.0115  0.0068  -0.0112 1026 LEU B N   
16841 C CA  . LEU B 1028 ? 0.0935 0.1405 0.1381 0.0109  0.0079  -0.0105 1026 LEU B CA  
16842 C C   . LEU B 1028 ? 0.1160 0.1645 0.1606 0.0101  0.0086  -0.0112 1026 LEU B C   
16843 O O   . LEU B 1028 ? 0.1263 0.1748 0.1708 0.0094  0.0098  -0.0105 1026 LEU B O   
16844 C CB  . LEU B 1028 ? 0.1163 0.1612 0.1624 0.0106  0.0082  -0.0109 1026 LEU B CB  
16845 C CG  . LEU B 1028 ? 0.1521 0.1949 0.1976 0.0118  0.0078  -0.0102 1026 LEU B CG  
16846 C CD1 . LEU B 1028 ? 0.1852 0.2253 0.2316 0.0113  0.0079  -0.0110 1026 LEU B CD1 
16847 C CD2 . LEU B 1028 ? 0.2386 0.2805 0.2824 0.0124  0.0082  -0.0083 1026 LEU B CD2 
16848 N N   . TYR B 1029 ? 0.0988 0.1485 0.1433 0.0103  0.0080  -0.0125 1027 TYR B N   
16849 C CA  . TYR B 1029 ? 0.1016 0.1527 0.1464 0.0099  0.0087  -0.0136 1027 TYR B CA  
16850 C C   . TYR B 1029 ? 0.1182 0.1699 0.1607 0.0097  0.0097  -0.0127 1027 TYR B C   
16851 O O   . TYR B 1029 ? 0.1044 0.1571 0.1475 0.0091  0.0111  -0.0127 1027 TYR B O   
16852 C CB  . TYR B 1029 ? 0.1036 0.1548 0.1480 0.0105  0.0075  -0.0152 1027 TYR B CB  
16853 C CG  . TYR B 1029 ? 0.1121 0.1645 0.1577 0.0108  0.0079  -0.0168 1027 TYR B CG  
16854 C CD1 . TYR B 1029 ? 0.0921 0.1452 0.1408 0.0108  0.0081  -0.0177 1027 TYR B CD1 
16855 C CD2 . TYR B 1029 ? 0.1029 0.1555 0.1464 0.0113  0.0079  -0.0177 1027 TYR B CD2 
16856 C CE1 . TYR B 1029 ? 0.0943 0.1492 0.1446 0.0114  0.0083  -0.0192 1027 TYR B CE1 
16857 C CE2 . TYR B 1029 ? 0.1032 0.1569 0.1478 0.0122  0.0082  -0.0194 1027 TYR B CE2 
16858 C CZ  . TYR B 1029 ? 0.1001 0.1552 0.1483 0.0123  0.0085  -0.0200 1027 TYR B CZ  
16859 O OH  . TYR B 1029 ? 0.1271 0.1839 0.1767 0.0134  0.0087  -0.0217 1027 TYR B OH  
16860 N N   . LEU B 1030 ? 0.1059 0.1574 0.1459 0.0099  0.0089  -0.0119 1028 LEU B N   
16861 C CA  . LEU B 1030 ? 0.0925 0.1444 0.1296 0.0097  0.0095  -0.0112 1028 LEU B CA  
16862 C C   . LEU B 1030 ? 0.1059 0.1574 0.1427 0.0092  0.0108  -0.0095 1028 LEU B C   
16863 O O   . LEU B 1030 ? 0.1151 0.1671 0.1501 0.0087  0.0121  -0.0091 1028 LEU B O   
16864 C CB  . LEU B 1030 ? 0.1192 0.1711 0.1538 0.0098  0.0080  -0.0107 1028 LEU B CB  
16865 C CG  . LEU B 1030 ? 0.1125 0.1643 0.1465 0.0099  0.0066  -0.0122 1028 LEU B CG  
16866 C CD1 . LEU B 1030 ? 0.1450 0.1970 0.1764 0.0095  0.0051  -0.0114 1028 LEU B CD1 
16867 C CD2 . LEU B 1030 ? 0.1390 0.1906 0.1721 0.0102  0.0074  -0.0140 1028 LEU B CD2 
16868 N N   . GLY B 1031 ? 0.1244 0.1746 0.1626 0.0093  0.0106  -0.0084 1029 GLY B N   
16869 C CA  . GLY B 1031 ? 0.1217 0.1704 0.1590 0.0088  0.0116  -0.0066 1029 GLY B CA  
16870 C C   . GLY B 1031 ? 0.1141 0.1632 0.1525 0.0075  0.0134  -0.0068 1029 GLY B C   
16871 O O   . GLY B 1031 ? 0.1489 0.1968 0.1857 0.0067  0.0145  -0.0051 1029 GLY B O   
16872 N N   . ARG B 1032 ? 0.1128 0.1635 0.1539 0.0072  0.0137  -0.0086 1030 ARG B N   
16873 C CA  . ARG B 1032 ? 0.1214 0.1737 0.1644 0.0059  0.0154  -0.0090 1030 ARG B CA  
16874 C C   . ARG B 1032 ? 0.1219 0.1764 0.1631 0.0058  0.0169  -0.0092 1030 ARG B C   
16875 O O   . ARG B 1032 ? 0.1332 0.1896 0.1756 0.0047  0.0188  -0.0090 1030 ARG B O   
16876 C CB  . ARG B 1032 ? 0.1488 0.2025 0.1957 0.0060  0.0149  -0.0109 1030 ARG B CB  
16877 C CG  . ARG B 1032 ? 0.1622 0.2180 0.2121 0.0045  0.0163  -0.0112 1030 ARG B CG  
16878 C CD  . ARG B 1032 ? 0.2055 0.2586 0.2558 0.0029  0.0165  -0.0097 1030 ARG B CD  
16879 N NE  . ARG B 1032 ? 0.2223 0.2778 0.2762 0.0010  0.0175  -0.0101 1030 ARG B NE  
16880 C CZ  . ARG B 1032 ? 0.2150 0.2707 0.2688 -0.0011 0.0193  -0.0086 1030 ARG B CZ  
16881 N NH1 . ARG B 1032 ? 0.2441 0.2972 0.2942 -0.0015 0.0201  -0.0065 1030 ARG B NH1 
16882 N NH2 . ARG B 1032 ? 0.2335 0.2922 0.2912 -0.0030 0.0201  -0.0091 1030 ARG B NH2 
16883 N N   . LEU B 1033 ? 0.1206 0.1751 0.1588 0.0069  0.0161  -0.0095 1031 LEU B N   
16884 C CA  . LEU B 1033 ? 0.1089 0.1651 0.1449 0.0073  0.0173  -0.0103 1031 LEU B CA  
16885 C C   . LEU B 1033 ? 0.1288 0.1838 0.1602 0.0070  0.0177  -0.0085 1031 LEU B C   
16886 O O   . LEU B 1033 ? 0.1339 0.1896 0.1620 0.0074  0.0182  -0.0091 1031 LEU B O   
16887 C CB  . LEU B 1033 ? 0.1143 0.1708 0.1499 0.0086  0.0159  -0.0124 1031 LEU B CB  
16888 C CG  . LEU B 1033 ? 0.1306 0.1880 0.1703 0.0091  0.0152  -0.0141 1031 LEU B CG  
16889 C CD1 . LEU B 1033 ? 0.1482 0.2048 0.1868 0.0104  0.0136  -0.0159 1031 LEU B CD1 
16890 C CD2 . LEU B 1033 ? 0.1919 0.2523 0.2348 0.0087  0.0170  -0.0148 1031 LEU B CD2 
16891 N N   . VAL B 1034 ? 0.1220 0.1749 0.1525 0.0064  0.0174  -0.0064 1032 VAL B N   
16892 C CA  . VAL B 1034 ? 0.1516 0.2030 0.1778 0.0061  0.0177  -0.0043 1032 VAL B CA  
16893 C C   . VAL B 1034 ? 0.1590 0.2089 0.1858 0.0047  0.0190  -0.0023 1032 VAL B C   
16894 O O   . VAL B 1034 ? 0.1629 0.2125 0.1934 0.0041  0.0191  -0.0026 1032 VAL B O   
16895 C CB  . VAL B 1034 ? 0.1486 0.1985 0.1728 0.0072  0.0152  -0.0034 1032 VAL B CB  
16896 C CG1 . VAL B 1034 ? 0.1571 0.2082 0.1800 0.0079  0.0139  -0.0052 1032 VAL B CG1 
16897 C CG2 . VAL B 1034 ? 0.1558 0.2045 0.1832 0.0076  0.0139  -0.0031 1032 VAL B CG2 
16898 N N   . THR B 1035 ? 0.1738 0.2223 0.1965 0.0041  0.0199  -0.0002 1033 THR B N   
16899 C CA  . THR B 1035 ? 0.1860 0.2324 0.2087 0.0024  0.0213  0.0018  1033 THR B CA  
16900 C C   . THR B 1035 ? 0.1997 0.2420 0.2219 0.0030  0.0195  0.0035  1033 THR B C   
16901 O O   . THR B 1035 ? 0.2319 0.2716 0.2549 0.0018  0.0202  0.0047  1033 THR B O   
16902 C CB  . THR B 1035 ? 0.2460 0.2921 0.2641 0.0013  0.0232  0.0036  1033 THR B CB  
16903 O OG1 . THR B 1035 ? 0.2777 0.3227 0.2910 0.0026  0.0218  0.0043  1033 THR B OG1 
16904 C CG2 . THR B 1035 ? 0.2274 0.2778 0.2467 0.0005  0.0257  0.0019  1033 THR B CG2 
16905 N N   . THR B 1036 ? 0.1787 0.2205 0.1997 0.0049  0.0174  0.0036  1034 THR B N   
16906 C CA  . THR B 1036 ? 0.2115 0.2502 0.2325 0.0062  0.0156  0.0049  1034 THR B CA  
16907 C C   . THR B 1036 ? 0.1845 0.2252 0.2085 0.0077  0.0139  0.0031  1034 THR B C   
16908 O O   . THR B 1036 ? 0.1924 0.2354 0.2154 0.0085  0.0128  0.0024  1034 THR B O   
16909 C CB  . THR B 1036 ? 0.2423 0.2790 0.2588 0.0071  0.0147  0.0073  1034 THR B CB  
16910 O OG1 . THR B 1036 ? 0.2748 0.3098 0.2877 0.0055  0.0165  0.0090  1034 THR B OG1 
16911 C CG2 . THR B 1036 ? 0.2727 0.3061 0.2894 0.0087  0.0131  0.0087  1034 THR B CG2 
16912 N N   . ALA B 1037 ? 0.1656 0.2053 0.1929 0.0080  0.0135  0.0022  1035 ALA B N   
16913 C CA  . ALA B 1037 ? 0.1545 0.1962 0.1846 0.0092  0.0122  0.0005  1035 ALA B CA  
16914 C C   . ALA B 1037 ? 0.1597 0.2012 0.1888 0.0111  0.0104  0.0015  1035 ALA B C   
16915 O O   . ALA B 1037 ? 0.1757 0.2144 0.2034 0.0120  0.0100  0.0034  1035 ALA B O   
16916 C CB  . ALA B 1037 ? 0.1736 0.2141 0.2070 0.0088  0.0124  -0.0007 1035 ALA B CB  
16917 N N   . PRO B 1038 ? 0.1174 0.1618 0.1473 0.0118  0.0091  0.0005  1036 PRO B N   
16918 C CA  . PRO B 1038 ? 0.1274 0.1728 0.1575 0.0135  0.0074  0.0014  1036 PRO B CA  
16919 C C   . PRO B 1038 ? 0.1266 0.1713 0.1595 0.0147  0.0072  0.0008  1036 PRO B C   
16920 O O   . PRO B 1038 ? 0.1326 0.1760 0.1672 0.0140  0.0081  -0.0005 1036 PRO B O   
16921 C CB  . PRO B 1038 ? 0.1486 0.1975 0.1786 0.0131  0.0064  0.0003  1036 PRO B CB  
16922 C CG  . PRO B 1038 ? 0.1655 0.2147 0.1969 0.0119  0.0073  -0.0019 1036 PRO B CG  
16923 C CD  . PRO B 1038 ? 0.1400 0.1870 0.1707 0.0110  0.0092  -0.0016 1036 PRO B CD  
16924 N N   . VAL B 1039 ? 0.1313 0.1772 0.1647 0.0165  0.0060  0.0017  1037 VAL B N   
16925 C CA  . VAL B 1039 ? 0.1345 0.1804 0.1703 0.0179  0.0058  0.0010  1037 VAL B CA  
16926 C C   . VAL B 1039 ? 0.1213 0.1709 0.1591 0.0173  0.0053  -0.0006 1037 VAL B C   
16927 O O   . VAL B 1039 ? 0.1264 0.1794 0.1642 0.0173  0.0042  -0.0002 1037 VAL B O   
16928 C CB  . VAL B 1039 ? 0.1402 0.1864 0.1759 0.0205  0.0050  0.0027  1037 VAL B CB  
16929 C CG1 . VAL B 1039 ? 0.1583 0.2047 0.1962 0.0221  0.0051  0.0018  1037 VAL B CG1 
16930 C CG2 . VAL B 1039 ? 0.1806 0.2221 0.2135 0.0211  0.0054  0.0044  1037 VAL B CG2 
16931 N N   . PRO B 1040 ? 0.1364 0.1853 0.1757 0.0165  0.0059  -0.0023 1038 PRO B N   
16932 C CA  . PRO B 1040 ? 0.1230 0.1747 0.1636 0.0158  0.0053  -0.0037 1038 PRO B CA  
16933 C C   . PRO B 1040 ? 0.1145 0.1690 0.1565 0.0171  0.0045  -0.0032 1038 PRO B C   
16934 O O   . PRO B 1040 ? 0.1199 0.1737 0.1623 0.0190  0.0048  -0.0023 1038 PRO B O   
16935 C CB  . PRO B 1040 ? 0.1633 0.2130 0.2049 0.0150  0.0060  -0.0054 1038 PRO B CB  
16936 C CG  . PRO B 1040 ? 0.1784 0.2250 0.2194 0.0147  0.0070  -0.0051 1038 PRO B CG  
16937 C CD  . PRO B 1040 ? 0.1458 0.1912 0.1855 0.0160  0.0069  -0.0031 1038 PRO B CD  
16938 N N   . PRO B 1041 ? 0.1127 0.1703 0.1554 0.0161  0.0037  -0.0037 1039 PRO B N   
16939 C CA  . PRO B 1041 ? 0.1168 0.1778 0.1613 0.0170  0.0033  -0.0033 1039 PRO B CA  
16940 C C   . PRO B 1041 ? 0.1230 0.1822 0.1684 0.0183  0.0043  -0.0040 1039 PRO B C   
16941 O O   . PRO B 1041 ? 0.1348 0.1911 0.1799 0.0176  0.0048  -0.0054 1039 PRO B O   
16942 C CB  . PRO B 1041 ? 0.1526 0.2156 0.1971 0.0150  0.0024  -0.0041 1039 PRO B CB  
16943 C CG  . PRO B 1041 ? 0.1701 0.2313 0.2124 0.0135  0.0021  -0.0046 1039 PRO B CG  
16944 C CD  . PRO B 1041 ? 0.1502 0.2079 0.1918 0.0141  0.0033  -0.0048 1039 PRO B CD  
16945 N N   . GLN B 1042 ? 0.1194 0.1806 0.1660 0.0204  0.0045  -0.0031 1040 GLN B N   
16946 C CA  . GLN B 1042 ? 0.1261 0.1861 0.1733 0.0220  0.0054  -0.0038 1040 GLN B CA  
16947 C C   . GLN B 1042 ? 0.1345 0.1889 0.1803 0.0228  0.0061  -0.0044 1040 GLN B C   
16948 O O   . GLN B 1042 ? 0.1443 0.1965 0.1898 0.0238  0.0068  -0.0054 1040 GLN B O   
16949 C CB  . GLN B 1042 ? 0.1830 0.2439 0.2306 0.0205  0.0055  -0.0052 1040 GLN B CB  
16950 C CG  . GLN B 1042 ? 0.2411 0.3070 0.2898 0.0191  0.0048  -0.0046 1040 GLN B CG  
16951 C CD  . GLN B 1042 ? 0.3078 0.3737 0.3563 0.0177  0.0050  -0.0057 1040 GLN B CD  
16952 O OE1 . GLN B 1042 ? 0.3657 0.4345 0.4153 0.0183  0.0055  -0.0055 1040 GLN B OE1 
16953 N NE2 . GLN B 1042 ? 0.3831 0.4456 0.4302 0.0160  0.0046  -0.0070 1040 GLN B NE2 
16954 N N   . HIS B 1043 ? 0.1188 0.1704 0.1633 0.0223  0.0060  -0.0039 1041 HIS B N   
16955 C CA  . HIS B 1043 ? 0.1165 0.1628 0.1597 0.0221  0.0066  -0.0044 1041 HIS B CA  
16956 C C   . HIS B 1043 ? 0.1334 0.1769 0.1756 0.0246  0.0069  -0.0033 1041 HIS B C   
16957 O O   . HIS B 1043 ? 0.1521 0.1944 0.1931 0.0250  0.0066  -0.0018 1041 HIS B O   
16958 C CB  . HIS B 1043 ? 0.1243 0.1695 0.1667 0.0199  0.0066  -0.0044 1041 HIS B CB  
16959 C CG  . HIS B 1043 ? 0.1582 0.1987 0.1998 0.0191  0.0072  -0.0048 1041 HIS B CG  
16960 N ND1 . HIS B 1043 ? 0.1354 0.1746 0.1777 0.0176  0.0075  -0.0065 1041 HIS B ND1 
16961 C CD2 . HIS B 1043 ? 0.1497 0.1864 0.1897 0.0194  0.0076  -0.0037 1041 HIS B CD2 
16962 C CE1 . HIS B 1043 ? 0.1309 0.1662 0.1724 0.0168  0.0079  -0.0064 1041 HIS B CE1 
16963 N NE2 . HIS B 1043 ? 0.1380 0.1716 0.1780 0.0178  0.0081  -0.0046 1041 HIS B NE2 
16964 N N   . SER B 1044 ? 0.1143 0.1561 0.1564 0.0265  0.0073  -0.0040 1042 SER B N   
16965 C CA  . SER B 1044 ? 0.1298 0.1679 0.1704 0.0292  0.0075  -0.0033 1042 SER B CA  
16966 C C   . SER B 1044 ? 0.1236 0.1589 0.1636 0.0305  0.0081  -0.0049 1042 SER B C   
16967 O O   . SER B 1044 ? 0.1390 0.1763 0.1798 0.0294  0.0083  -0.0063 1042 SER B O   
16968 C CB  . SER B 1044 ? 0.1407 0.1829 0.1823 0.0319  0.0072  -0.0017 1042 SER B CB  
16969 O OG  . SER B 1044 ? 0.1225 0.1697 0.1661 0.0331  0.0075  -0.0022 1042 SER B OG  
16970 N N   . SER B 1045 ? 0.1268 0.1572 0.1648 0.0329  0.0084  -0.0048 1043 SER B N   
16971 C CA  . SER B 1045 ? 0.1355 0.1627 0.1721 0.0346  0.0089  -0.0064 1043 SER B CA  
16972 C C   . SER B 1045 ? 0.1264 0.1505 0.1613 0.0386  0.0091  -0.0057 1043 SER B C   
16973 O O   . SER B 1045 ? 0.1428 0.1634 0.1762 0.0392  0.0087  -0.0042 1043 SER B O   
16974 C CB  . SER B 1045 ? 0.1374 0.1586 0.1722 0.0322  0.0087  -0.0078 1043 SER B CB  
16975 O OG  . SER B 1045 ? 0.1467 0.1640 0.1794 0.0339  0.0091  -0.0094 1043 SER B OG  
16976 N N   . VAL B 1046 ? 0.1366 0.1617 0.1712 0.0415  0.0099  -0.0066 1044 VAL B N   
16977 C CA  . VAL B 1046 ? 0.1621 0.1839 0.1949 0.0459  0.0102  -0.0062 1044 VAL B CA  
16978 C C   . VAL B 1046 ? 0.1407 0.1528 0.1693 0.0463  0.0102  -0.0076 1044 VAL B C   
16979 O O   . VAL B 1046 ? 0.1708 0.1782 0.1968 0.0500  0.0103  -0.0074 1044 VAL B O   
16980 C CB  . VAL B 1046 ? 0.1678 0.1951 0.2021 0.0495  0.0113  -0.0067 1044 VAL B CB  
16981 C CG1 . VAL B 1046 ? 0.1920 0.2290 0.2306 0.0492  0.0112  -0.0051 1044 VAL B CG1 
16982 C CG2 . VAL B 1046 ? 0.1778 0.2047 0.2111 0.0487  0.0122  -0.0089 1044 VAL B CG2 
16983 N N   . HIS B 1047 ? 0.1664 0.1753 0.1940 0.0427  0.0098  -0.0090 1045 HIS B N   
16984 C CA  . HIS B 1047 ? 0.1623 0.1621 0.1859 0.0426  0.0096  -0.0105 1045 HIS B CA  
16985 C C   . HIS B 1047 ? 0.1518 0.1453 0.1737 0.0406  0.0087  -0.0093 1045 HIS B C   
16986 O O   . HIS B 1047 ? 0.1853 0.1817 0.2092 0.0377  0.0083  -0.0079 1045 HIS B O   
16987 C CB  . HIS B 1047 ? 0.1868 0.1870 0.2106 0.0398  0.0095  -0.0126 1045 HIS B CB  
16988 C CG  . HIS B 1047 ? 0.2207 0.2268 0.2457 0.0415  0.0104  -0.0135 1045 HIS B CG  
16989 N ND1 . HIS B 1047 ? 0.2605 0.2652 0.2833 0.0456  0.0114  -0.0144 1045 HIS B ND1 
16990 C CD2 . HIS B 1047 ? 0.2700 0.2835 0.2981 0.0399  0.0107  -0.0134 1045 HIS B CD2 
16991 C CE1 . HIS B 1047 ? 0.2650 0.2765 0.2897 0.0460  0.0124  -0.0148 1045 HIS B CE1 
16992 N NE2 . HIS B 1047 ? 0.2388 0.2553 0.2666 0.0425  0.0119  -0.0141 1045 HIS B NE2 
16993 N N   . THR B 1048 ? 0.1771 0.1618 0.1949 0.0421  0.0084  -0.0098 1046 THR B N   
16994 C CA  . THR B 1048 ? 0.1704 0.1479 0.1857 0.0399  0.0075  -0.0087 1046 THR B CA  
16995 C C   . THR B 1048 ? 0.1695 0.1396 0.1820 0.0374  0.0069  -0.0106 1046 THR B C   
16996 O O   . THR B 1048 ? 0.2015 0.1671 0.2109 0.0397  0.0069  -0.0125 1046 THR B O   
16997 C CB  . THR B 1048 ? 0.2034 0.1759 0.2158 0.0438  0.0074  -0.0071 1046 THR B CB  
16998 O OG1 . THR B 1048 ? 0.2117 0.1920 0.2271 0.0466  0.0078  -0.0055 1046 THR B OG1 
16999 C CG2 . THR B 1048 ? 0.2204 0.1863 0.2306 0.0410  0.0066  -0.0053 1046 THR B CG2 
17000 N N   . ASP B 1049 ? 0.1693 0.1382 0.1826 0.0327  0.0063  -0.0102 1047 ASP B N   
17001 C CA  . ASP B 1049 ? 0.1860 0.1488 0.1972 0.0297  0.0055  -0.0120 1047 ASP B CA  
17002 C C   . ASP B 1049 ? 0.2040 0.1557 0.2096 0.0315  0.0049  -0.0122 1047 ASP B C   
17003 O O   . ASP B 1049 ? 0.2149 0.1626 0.2187 0.0323  0.0048  -0.0101 1047 ASP B O   
17004 C CB  . ASP B 1049 ? 0.1562 0.1208 0.1699 0.0244  0.0051  -0.0113 1047 ASP B CB  
17005 C CG  . ASP B 1049 ? 0.1898 0.1490 0.2021 0.0209  0.0040  -0.0130 1047 ASP B CG  
17006 O OD1 . ASP B 1049 ? 0.2059 0.1562 0.2143 0.0201  0.0034  -0.0127 1047 ASP B OD1 
17007 O OD2 . ASP B 1049 ? 0.1957 0.1592 0.2104 0.0190  0.0037  -0.0146 1047 ASP B OD2 
17008 N N   . PRO B 1050 ? 0.2055 0.1515 0.2077 0.0324  0.0044  -0.0146 1048 PRO B N   
17009 C CA  . PRO B 1050 ? 0.2201 0.1547 0.2163 0.0347  0.0037  -0.0150 1048 PRO B CA  
17010 C C   . PRO B 1050 ? 0.2351 0.1615 0.2288 0.0304  0.0025  -0.0142 1048 PRO B C   
17011 O O   . PRO B 1050 ? 0.2493 0.1665 0.2383 0.0321  0.0021  -0.0133 1048 PRO B O   
17012 C CB  . PRO B 1050 ? 0.2675 0.1993 0.2609 0.0365  0.0036  -0.0181 1048 PRO B CB  
17013 C CG  . PRO B 1050 ? 0.2400 0.1789 0.2374 0.0326  0.0033  -0.0192 1048 PRO B CG  
17014 C CD  . PRO B 1050 ? 0.2101 0.1595 0.2133 0.0318  0.0043  -0.0171 1048 PRO B CD  
17015 N N   . VAL B 1051 ? 0.2497 0.1791 0.2464 0.0249  0.0020  -0.0143 1049 VAL B N   
17016 C CA  . VAL B 1051 ? 0.2405 0.1633 0.2356 0.0202  0.0011  -0.0132 1049 VAL B CA  
17017 C C   . VAL B 1051 ? 0.2253 0.1495 0.2214 0.0198  0.0018  -0.0099 1049 VAL B C   
17018 O O   . VAL B 1051 ? 0.2382 0.1539 0.2305 0.0186  0.0013  -0.0084 1049 VAL B O   
17019 C CB  . VAL B 1051 ? 0.2400 0.1666 0.2386 0.0147  0.0003  -0.0143 1049 VAL B CB  
17020 C CG1 . VAL B 1051 ? 0.2315 0.1521 0.2288 0.0095  -0.0005 -0.0131 1049 VAL B CG1 
17021 C CG2 . VAL B 1051 ? 0.2749 0.1995 0.2717 0.0153  -0.0007 -0.0176 1049 VAL B CG2 
17022 N N   . LEU B 1052 ? 0.1934 0.1277 0.1940 0.0208  0.0030  -0.0087 1050 LEU B N   
17023 C CA  . LEU B 1052 ? 0.1819 0.1176 0.1828 0.0214  0.0036  -0.0056 1050 LEU B CA  
17024 C C   . LEU B 1052 ? 0.2376 0.1654 0.2335 0.0261  0.0033  -0.0046 1050 LEU B C   
17025 O O   . LEU B 1052 ? 0.2225 0.1444 0.2154 0.0254  0.0031  -0.0023 1050 LEU B O   
17026 C CB  . LEU B 1052 ? 0.1798 0.1273 0.1858 0.0226  0.0047  -0.0050 1050 LEU B CB  
17027 C CG  . LEU B 1052 ? 0.1759 0.1267 0.1826 0.0234  0.0053  -0.0020 1050 LEU B CG  
17028 C CD1 . LEU B 1052 ? 0.2136 0.1617 0.2175 0.0290  0.0051  -0.0009 1050 LEU B CD1 
17029 C CD2 . LEU B 1052 ? 0.1900 0.1371 0.1955 0.0189  0.0053  0.0000  1050 LEU B CD2 
17030 N N   . LEU B 1053 ? 0.2189 0.1465 0.2136 0.0311  0.0034  -0.0063 1051 LEU B N   
17031 C CA  . LEU B 1053 ? 0.2583 0.1787 0.2484 0.0363  0.0032  -0.0055 1051 LEU B CA  
17032 C C   . LEU B 1053 ? 0.2566 0.1634 0.2405 0.0349  0.0020  -0.0056 1051 LEU B C   
17033 O O   . LEU B 1053 ? 0.2749 0.1747 0.2549 0.0366  0.0015  -0.0035 1051 LEU B O   
17034 C CB  . LEU B 1053 ? 0.2463 0.1694 0.2364 0.0418  0.0037  -0.0077 1051 LEU B CB  
17035 C CG  . LEU B 1053 ? 0.2720 0.2077 0.2676 0.0441  0.0048  -0.0071 1051 LEU B CG  
17036 C CD1 . LEU B 1053 ? 0.2653 0.2038 0.2610 0.0486  0.0056  -0.0094 1051 LEU B CD1 
17037 C CD2 . LEU B 1053 ? 0.2961 0.2334 0.2920 0.0468  0.0048  -0.0042 1051 LEU B CD2 
17038 N N   . ASP B 1054 ? 0.2513 0.1536 0.2337 0.0317  0.0012  -0.0079 1052 ASP B N   
17039 C CA  . ASP B 1054 ? 0.2976 0.1866 0.2740 0.0296  -0.0001 -0.0081 1052 ASP B CA  
17040 C C   . ASP B 1054 ? 0.2640 0.1504 0.2402 0.0246  -0.0004 -0.0051 1052 ASP B C   
17041 O O   . ASP B 1054 ? 0.3043 0.1795 0.2749 0.0245  -0.0012 -0.0037 1052 ASP B O   
17042 C CB  . ASP B 1054 ? 0.2844 0.1706 0.2600 0.0265  -0.0010 -0.0112 1052 ASP B CB  
17043 C CG  . ASP B 1054 ? 0.3617 0.2466 0.3350 0.0317  -0.0009 -0.0141 1052 ASP B CG  
17044 O OD1 . ASP B 1054 ? 0.3379 0.2221 0.3094 0.0377  -0.0002 -0.0137 1052 ASP B OD1 
17045 O OD2 . ASP B 1054 ? 0.3623 0.2468 0.3353 0.0297  -0.0016 -0.0168 1052 ASP B OD2 
17046 N N   . PHE B 1055 ? 0.2573 0.1537 0.2393 0.0207  0.0005  -0.0040 1053 PHE B N   
17047 C CA  . PHE B 1055 ? 0.2488 0.1440 0.2308 0.0159  0.0006  -0.0011 1053 PHE B CA  
17048 C C   . PHE B 1055 ? 0.2794 0.1724 0.2589 0.0193  0.0010  0.0019  1053 PHE B C   
17049 O O   . PHE B 1055 ? 0.2792 0.1639 0.2545 0.0172  0.0005  0.0043  1053 PHE B O   
17050 C CB  . PHE B 1055 ? 0.2448 0.1522 0.2337 0.0118  0.0017  -0.0010 1053 PHE B CB  
17051 C CG  . PHE B 1055 ? 0.2143 0.1222 0.2040 0.0066  0.0023  0.0018  1053 PHE B CG  
17052 C CD1 . PHE B 1055 ? 0.2853 0.1844 0.2718 0.0019  0.0015  0.0025  1053 PHE B CD1 
17053 C CD2 . PHE B 1055 ? 0.2176 0.1347 0.2110 0.0064  0.0036  0.0037  1053 PHE B CD2 
17054 C CE1 . PHE B 1055 ? 0.2621 0.1621 0.2493 -0.0030 0.0023  0.0052  1053 PHE B CE1 
17055 C CE2 . PHE B 1055 ? 0.2463 0.1642 0.2401 0.0017  0.0044  0.0062  1053 PHE B CE2 
17056 C CZ  . PHE B 1055 ? 0.2658 0.1753 0.2566 -0.0030 0.0039  0.0070  1053 PHE B CZ  
17057 N N   . ALA B 1056 ? 0.2558 0.1557 0.2375 0.0246  0.0016  0.0020  1054 ALA B N   
17058 C CA  . ALA B 1056 ? 0.2530 0.1515 0.2325 0.0282  0.0016  0.0049  1054 ALA B CA  
17059 C C   . ALA B 1056 ? 0.2761 0.1610 0.2483 0.0316  0.0004  0.0054  1054 ALA B C   
17060 O O   . ALA B 1056 ? 0.3112 0.1899 0.2795 0.0317  0.0000  0.0083  1054 ALA B O   
17061 C CB  . ALA B 1056 ? 0.2534 0.1626 0.2371 0.0331  0.0023  0.0046  1054 ALA B CB  
17062 N N   . LYS B 1057 ? 0.2926 0.1723 0.2625 0.0345  -0.0001 0.0025  1055 LYS B N   
17063 C CA  . LYS B 1057 ? 0.3385 0.2043 0.3009 0.0379  -0.0013 0.0026  1055 LYS B CA  
17064 C C   . LYS B 1057 ? 0.3841 0.2383 0.3416 0.0323  -0.0023 0.0038  1055 LYS B C   
17065 O O   . LYS B 1057 ? 0.3900 0.2335 0.3415 0.0337  -0.0032 0.0059  1055 LYS B O   
17066 C CB  . LYS B 1057 ? 0.3363 0.1991 0.2970 0.0419  -0.0015 -0.0011 1055 LYS B CB  
17067 C CG  . LYS B 1057 ? 0.3818 0.2529 0.3454 0.0488  -0.0005 -0.0019 1055 LYS B CG  
17068 C CD  . LYS B 1057 ? 0.3569 0.2243 0.3180 0.0528  -0.0005 -0.0054 1055 LYS B CD  
17069 C CE  . LYS B 1057 ? 0.3679 0.2382 0.3311 0.0481  -0.0004 -0.0082 1055 LYS B CE  
17070 N NZ  . LYS B 1057 ? 0.4095 0.2784 0.3706 0.0527  0.0000  -0.0115 1055 LYS B NZ  
17071 N N   . TRP B 1058 ? 0.3457 0.2019 0.3057 0.0258  -0.0023 0.0027  1056 TRP B N   
17072 C CA  . TRP B 1058 ? 0.3833 0.2299 0.3395 0.0195  -0.0032 0.0040  1056 TRP B CA  
17073 C C   . TRP B 1058 ? 0.3630 0.2101 0.3188 0.0172  -0.0026 0.0081  1056 TRP B C   
17074 O O   . TRP B 1058 ? 0.3841 0.2195 0.3338 0.0156  -0.0035 0.0103  1056 TRP B O   
17075 C CB  . TRP B 1058 ? 0.3587 0.2102 0.3191 0.0131  -0.0032 0.0020  1056 TRP B CB  
17076 C CG  . TRP B 1058 ? 0.3993 0.2436 0.3574 0.0057  -0.0039 0.0034  1056 TRP B CG  
17077 C CD1 . TRP B 1058 ? 0.4764 0.3071 0.4284 0.0033  -0.0056 0.0026  1056 TRP B CD1 
17078 C CD2 . TRP B 1058 ? 0.3619 0.2127 0.3241 -0.0005 -0.0029 0.0058  1056 TRP B CD2 
17079 N NE1 . TRP B 1058 ? 0.4445 0.2729 0.3966 -0.0043 -0.0058 0.0045  1056 TRP B NE1 
17080 C CE2 . TRP B 1058 ? 0.4116 0.2527 0.3702 -0.0066 -0.0040 0.0064  1056 TRP B CE2 
17081 C CE3 . TRP B 1058 ? 0.3898 0.2535 0.3581 -0.0015 -0.0011 0.0073  1056 TRP B CE3 
17082 C CZ2 . TRP B 1058 ? 0.4123 0.2569 0.3736 -0.0137 -0.0031 0.0088  1056 TRP B CZ2 
17083 C CZ3 . TRP B 1058 ? 0.4062 0.2731 0.3769 -0.0081 -0.0002 0.0095  1056 TRP B CZ3 
17084 C CH2 . TRP B 1058 ? 0.4214 0.2792 0.3887 -0.0141 -0.0011 0.0102  1056 TRP B CH2 
17085 N N   . LEU B 1059 ? 0.3298 0.1899 0.2916 0.0172  -0.0012 0.0093  1057 LEU B N   
17086 C CA  . LEU B 1059 ? 0.3465 0.2075 0.3074 0.0158  -0.0006 0.0132  1057 LEU B CA  
17087 C C   . LEU B 1059 ? 0.4476 0.3004 0.4026 0.0217  -0.0015 0.0153  1057 LEU B C   
17088 O O   . LEU B 1059 ? 0.4179 0.2631 0.3681 0.0199  -0.0019 0.0185  1057 LEU B O   
17089 C CB  . LEU B 1059 ? 0.3213 0.1976 0.2893 0.0152  0.0010  0.0137  1057 LEU B CB  
17090 C CG  . LEU B 1059 ? 0.3210 0.2056 0.2947 0.0091  0.0020  0.0124  1057 LEU B CG  
17091 C CD1 . LEU B 1059 ? 0.2969 0.1957 0.2769 0.0102  0.0033  0.0123  1057 LEU B CD1 
17092 C CD2 . LEU B 1059 ? 0.3553 0.2356 0.3273 0.0022  0.0023  0.0147  1057 LEU B CD2 
17093 N N   . ASP B 1060 ? 0.4103 0.2647 0.3656 0.0287  -0.0019 0.0136  1058 ASP B N   
17094 C CA  . ASP B 1060 ? 0.4189 0.2654 0.3688 0.0351  -0.0029 0.0152  1058 ASP B CA  
17095 C C   . ASP B 1060 ? 0.4550 0.2843 0.3965 0.0339  -0.0044 0.0159  1058 ASP B C   
17096 O O   . ASP B 1060 ? 0.5401 0.3611 0.4762 0.0352  -0.0052 0.0190  1058 ASP B O   
17097 C CB  . ASP B 1060 ? 0.4538 0.3043 0.4055 0.0426  -0.0030 0.0126  1058 ASP B CB  
17098 C CG  . ASP B 1060 ? 0.4287 0.2947 0.3873 0.0452  -0.0019 0.0128  1058 ASP B CG  
17099 O OD1 . ASP B 1060 ? 0.4191 0.2905 0.3794 0.0438  -0.0016 0.0157  1058 ASP B OD1 
17100 O OD2 . ASP B 1060 ? 0.4165 0.2892 0.3787 0.0489  -0.0013 0.0101  1058 ASP B OD2 
17101 N N   . GLY B 1061 ? 0.4457 0.2687 0.3856 0.0315  -0.0049 0.0130  1059 GLY B N   
17102 C CA  . GLY B 1061 ? 0.4741 0.2799 0.4055 0.0305  -0.0065 0.0133  1059 GLY B CA  
17103 C C   . GLY B 1061 ? 0.5096 0.3090 0.4378 0.0236  -0.0068 0.0167  1059 GLY B C   
17104 O O   . GLY B 1061 ? 0.5315 0.3161 0.4518 0.0237  -0.0081 0.0184  1059 GLY B O   
17105 N N   . LYS B 1062 ? 0.5032 0.3133 0.4373 0.0178  -0.0053 0.0179  1060 LYS B N   
17106 C CA  . LYS B 1062 ? 0.5023 0.3084 0.4342 0.0109  -0.0051 0.0213  1060 LYS B CA  
17107 C C   . LYS B 1062 ? 0.5697 0.3775 0.5000 0.0129  -0.0046 0.0253  1060 LYS B C   
17108 O O   . LYS B 1062 ? 0.5809 0.3853 0.5087 0.0075  -0.0042 0.0286  1060 LYS B O   
17109 C CB  . LYS B 1062 ? 0.4996 0.3167 0.4385 0.0036  -0.0036 0.0205  1060 LYS B CB  
17110 C CG  . LYS B 1062 ? 0.4946 0.3092 0.4346 0.0001  -0.0044 0.0170  1060 LYS B CG  
17111 C CD  . LYS B 1062 ? 0.4493 0.2786 0.3980 -0.0045 -0.0029 0.0157  1060 LYS B CD  
17112 C CE  . LYS B 1062 ? 0.4856 0.3209 0.4368 -0.0100 -0.0013 0.0191  1060 LYS B CE  
17113 N NZ  . LYS B 1062 ? 0.4962 0.3233 0.4444 -0.0176 -0.0017 0.0206  1060 LYS B NZ  
17114 N N   . GLY B 1063 ? 0.5426 0.3557 0.4742 0.0202  -0.0046 0.0253  1061 GLY B N   
17115 C CA  . GLY B 1063 ? 0.4787 0.2947 0.4093 0.0222  -0.0044 0.0290  1061 GLY B CA  
17116 C C   . GLY B 1063 ? 0.5586 0.3889 0.4956 0.0181  -0.0025 0.0301  1061 GLY B C   
17117 O O   . GLY B 1063 ? 0.5418 0.3733 0.4770 0.0178  -0.0022 0.0335  1061 GLY B O   
17118 N N   . ALA B 1064 ? 0.4888 0.3297 0.4329 0.0152  -0.0013 0.0272  1062 ALA B N   
17119 C CA  . ALA B 1064 ? 0.4797 0.3343 0.4301 0.0116  0.0006  0.0278  1062 ALA B CA  
17120 C C   . ALA B 1064 ? 0.4879 0.3537 0.4426 0.0174  0.0008  0.0271  1062 ALA B C   
17121 O O   . ALA B 1064 ? 0.4359 0.3122 0.3970 0.0180  0.0015  0.0244  1062 ALA B O   
17122 C CB  . ALA B 1064 ? 0.4153 0.2756 0.3710 0.0060  0.0016  0.0251  1062 ALA B CB  
17123 N N   . ARG B 1065 ? 0.4830 0.3464 0.4341 0.0215  0.0000  0.0299  1063 ARG B N   
17124 C CA  . ARG B 1065 ? 0.4122 0.2839 0.3664 0.0281  -0.0004 0.0293  1063 ARG B CA  
17125 C C   . ARG B 1065 ? 0.4057 0.2926 0.3669 0.0263  0.0010  0.0287  1063 ARG B C   
17126 O O   . ARG B 1065 ? 0.4568 0.3527 0.4232 0.0293  0.0012  0.0262  1063 ARG B O   
17127 C CB  . ARG B 1065 ? 0.4684 0.3339 0.4169 0.0325  -0.0019 0.0327  1063 ARG B CB  
17128 N N   . ALA B 1066 ? 0.4098 0.2994 0.3707 0.0213  0.0022  0.0309  1064 ALA B N   
17129 C CA  . ALA B 1066 ? 0.4016 0.3047 0.3684 0.0195  0.0036  0.0302  1064 ALA B CA  
17130 C C   . ALA B 1066 ? 0.3823 0.2922 0.3554 0.0172  0.0046  0.0265  1064 ALA B C   
17131 O O   . ALA B 1066 ? 0.3592 0.2798 0.3377 0.0187  0.0050  0.0248  1064 ALA B O   
17132 C CB  . ALA B 1066 ? 0.4035 0.3072 0.3683 0.0143  0.0049  0.0331  1064 ALA B CB  
17133 N N   . GLU B 1067 ? 0.3849 0.2886 0.3572 0.0134  0.0048  0.0254  1065 GLU B N   
17134 C CA  . GLU B 1067 ? 0.3486 0.2584 0.3265 0.0111  0.0055  0.0220  1065 GLU B CA  
17135 C C   . GLU B 1067 ? 0.3338 0.2447 0.3136 0.0162  0.0045  0.0191  1065 GLU B C   
17136 O O   . GLU B 1067 ? 0.3175 0.2375 0.3028 0.0164  0.0051  0.0166  1065 GLU B O   
17137 C CB  . GLU B 1067 ? 0.3479 0.2511 0.3244 0.0052  0.0057  0.0218  1065 GLU B CB  
17138 C CG  . GLU B 1067 ? 0.3563 0.2623 0.3334 -0.0009 0.0074  0.0240  1065 GLU B CG  
17139 C CD  . GLU B 1067 ? 0.4213 0.3187 0.3915 -0.0016 0.0072  0.0280  1065 GLU B CD  
17140 O OE1 . GLU B 1067 ? 0.4638 0.3520 0.4287 0.0026  0.0056  0.0290  1065 GLU B OE1 
17141 O OE2 . GLU B 1067 ? 0.4197 0.3195 0.3897 -0.0062 0.0088  0.0302  1065 GLU B OE2 
17142 N N   . ALA B 1068 ? 0.3352 0.2366 0.3102 0.0204  0.0031  0.0193  1066 ALA B N   
17143 C CA  . ALA B 1068 ? 0.3279 0.2307 0.3044 0.0257  0.0025  0.0165  1066 ALA B CA  
17144 C C   . ALA B 1068 ? 0.3654 0.2797 0.3465 0.0297  0.0028  0.0164  1066 ALA B C   
17145 O O   . ALA B 1068 ? 0.2713 0.1925 0.2566 0.0315  0.0031  0.0138  1066 ALA B O   
17146 C CB  . ALA B 1068 ? 0.3438 0.2341 0.3140 0.0300  0.0011  0.0169  1066 ALA B CB  
17147 N N   . GLU B 1069 ? 0.3332 0.2492 0.3129 0.0311  0.0026  0.0193  1067 GLU B N   
17148 C CA  . GLU B 1069 ? 0.3213 0.2485 0.3053 0.0340  0.0027  0.0194  1067 GLU B CA  
17149 C C   . GLU B 1069 ? 0.3424 0.2802 0.3321 0.0300  0.0040  0.0179  1067 GLU B C   
17150 O O   . GLU B 1069 ? 0.2963 0.2429 0.2906 0.0320  0.0042  0.0161  1067 GLU B O   
17151 C CB  . GLU B 1069 ? 0.3570 0.2833 0.3378 0.0353  0.0020  0.0230  1067 GLU B CB  
17152 C CG  . GLU B 1069 ? 0.4043 0.3424 0.3892 0.0368  0.0020  0.0234  1067 GLU B CG  
17153 C CD  . GLU B 1069 ? 0.4624 0.4053 0.4497 0.0430  0.0010  0.0225  1067 GLU B CD  
17154 O OE1 . GLU B 1069 ? 0.4613 0.3991 0.4476 0.0466  0.0006  0.0212  1067 GLU B OE1 
17155 O OE2 . GLU B 1069 ? 0.5417 0.4937 0.5321 0.0444  0.0007  0.0231  1067 GLU B OE2 
17156 N N   . ALA B 1070 ? 0.3011 0.2382 0.2906 0.0243  0.0050  0.0185  1068 ALA B N   
17157 C CA  . ALA B 1070 ? 0.3153 0.2619 0.3100 0.0208  0.0062  0.0170  1068 ALA B CA  
17158 C C   . ALA B 1070 ? 0.2565 0.2055 0.2549 0.0209  0.0063  0.0135  1068 ALA B C   
17159 O O   . ALA B 1070 ? 0.2564 0.2144 0.2596 0.0210  0.0068  0.0118  1068 ALA B O   
17160 C CB  . ALA B 1070 ? 0.3698 0.3148 0.3636 0.0149  0.0074  0.0183  1068 ALA B CB  
17161 N N   . ALA B 1071 ? 0.2463 0.1867 0.2421 0.0210  0.0057  0.0125  1069 ALA B N   
17162 C CA  . ALA B 1071 ? 0.2157 0.1574 0.2140 0.0212  0.0056  0.0092  1069 ALA B CA  
17163 C C   . ALA B 1071 ? 0.2561 0.2030 0.2565 0.0266  0.0053  0.0078  1069 ALA B C   
17164 O O   . ALA B 1071 ? 0.2299 0.1839 0.2345 0.0265  0.0058  0.0056  1069 ALA B O   
17165 C CB  . ALA B 1071 ? 0.2558 0.1862 0.2499 0.0203  0.0048  0.0084  1069 ALA B CB  
17166 N N   . ARG B 1072 ? 0.2470 0.1905 0.2446 0.0314  0.0046  0.0092  1070 ARG B N   
17167 C CA  A ARG B 1072 ? 0.2435 0.1927 0.2434 0.0365  0.0045  0.0081  1070 ARG B CA  
17168 C CA  B ARG B 1072 ? 0.2437 0.1929 0.2435 0.0366  0.0045  0.0081  1070 ARG B CA  
17169 C C   . ARG B 1072 ? 0.2686 0.2297 0.2735 0.0360  0.0050  0.0083  1070 ARG B C   
17170 O O   . ARG B 1072 ? 0.2305 0.1986 0.2391 0.0374  0.0054  0.0065  1070 ARG B O   
17171 C CB  A ARG B 1072 ? 0.2682 0.2119 0.2643 0.0419  0.0036  0.0097  1070 ARG B CB  
17172 C CB  B ARG B 1072 ? 0.2678 0.2118 0.2640 0.0419  0.0036  0.0098  1070 ARG B CB  
17173 C CG  A ARG B 1072 ? 0.2987 0.2300 0.2895 0.0431  0.0030  0.0089  1070 ARG B CG  
17174 C CG  B ARG B 1072 ? 0.2974 0.2297 0.2885 0.0440  0.0030  0.0089  1070 ARG B CG  
17175 C CD  A ARG B 1072 ? 0.3073 0.2338 0.2949 0.0497  0.0021  0.0097  1070 ARG B CD  
17176 C CD  B ARG B 1072 ? 0.3031 0.2308 0.2909 0.0502  0.0020  0.0104  1070 ARG B CD  
17177 N NE  A ARG B 1072 ? 0.3061 0.2193 0.2876 0.0504  0.0014  0.0091  1070 ARG B NE  
17178 N NE  B ARG B 1072 ? 0.3264 0.2517 0.3116 0.0497  0.0013  0.0139  1070 ARG B NE  
17179 C CZ  A ARG B 1072 ? 0.2927 0.2021 0.2732 0.0511  0.0016  0.0061  1070 ARG B CZ  
17180 C CZ  B ARG B 1072 ? 0.3073 0.2211 0.2865 0.0488  0.0005  0.0157  1070 ARG B CZ  
17181 N NH1 A ARG B 1072 ? 0.3148 0.2327 0.2999 0.0516  0.0025  0.0036  1070 ARG B NH1 
17182 N NH1 B ARG B 1072 ? 0.3064 0.2095 0.2814 0.0484  0.0002  0.0144  1070 ARG B NH1 
17183 N NH2 A ARG B 1072 ? 0.3158 0.2122 0.2902 0.0512  0.0008  0.0057  1070 ARG B NH2 
17184 N NH2 B ARG B 1072 ? 0.2886 0.2013 0.2656 0.0481  0.0000  0.0190  1070 ARG B NH2 
17185 N N   . ASN B 1073 ? 0.2342 0.1974 0.2388 0.0337  0.0051  0.0106  1071 ASN B N   
17186 C CA  . ASN B 1073 ? 0.2364 0.2101 0.2452 0.0329  0.0055  0.0107  1071 ASN B CA  
17187 C C   . ASN B 1073 ? 0.2523 0.2313 0.2650 0.0293  0.0064  0.0084  1071 ASN B C   
17188 O O   . ASN B 1073 ? 0.2386 0.2256 0.2550 0.0300  0.0065  0.0073  1071 ASN B O   
17189 C CB  . ASN B 1073 ? 0.2742 0.2480 0.2809 0.0312  0.0054  0.0135  1071 ASN B CB  
17190 C CG  . ASN B 1073 ? 0.3647 0.3354 0.3682 0.0354  0.0041  0.0159  1071 ASN B CG  
17191 O OD1 . ASN B 1073 ? 0.3813 0.3528 0.3855 0.0400  0.0034  0.0153  1071 ASN B OD1 
17192 N ND2 . ASN B 1073 ? 0.3951 0.3623 0.3949 0.0340  0.0039  0.0186  1071 ASN B ND2 
17193 N N   . ALA B 1074 ? 0.2321 0.2066 0.2439 0.0254  0.0069  0.0077  1072 ALA B N   
17194 C CA  . ALA B 1074 ? 0.2238 0.2030 0.2393 0.0224  0.0075  0.0054  1072 ALA B CA  
17195 C C   . ALA B 1074 ? 0.2034 0.1841 0.2206 0.0250  0.0072  0.0029  1072 ALA B C   
17196 O O   . ALA B 1074 ? 0.1839 0.1716 0.2047 0.0245  0.0075  0.0013  1072 ALA B O   
17197 C CB  . ALA B 1074 ? 0.2182 0.1924 0.2327 0.0180  0.0078  0.0052  1072 ALA B CB  
17198 N N   . GLY B 1075 ? 0.1766 0.1504 0.1908 0.0278  0.0067  0.0024  1073 GLY B N   
17199 C CA  . GLY B 1075 ? 0.2152 0.1901 0.2303 0.0305  0.0066  0.0001  1073 GLY B CA  
17200 C C   . GLY B 1075 ? 0.2470 0.2306 0.2653 0.0334  0.0069  0.0000  1073 GLY B C   
17201 O O   . GLY B 1075 ? 0.2303 0.2188 0.2512 0.0335  0.0072  -0.0019 1073 GLY B O   
17202 N N   . SER B 1076 ? 0.2408 0.2266 0.2589 0.0356  0.0066  0.0022  1074 SER B N   
17203 C CA  . SER B 1076 ? 0.2322 0.2267 0.2536 0.0381  0.0066  0.0024  1074 SER B CA  
17204 C C   . SER B 1076 ? 0.2427 0.2448 0.2675 0.0347  0.0069  0.0022  1074 SER B C   
17205 O O   . SER B 1076 ? 0.2819 0.2905 0.3097 0.0351  0.0071  0.0010  1074 SER B O   
17206 C CB  . SER B 1076 ? 0.2614 0.2558 0.2815 0.0416  0.0059  0.0047  1074 SER B CB  
17207 O OG  . SER B 1076 ? 0.2995 0.2877 0.3167 0.0456  0.0057  0.0046  1074 SER B OG  
17208 N N   . SER B 1077 ? 0.2215 0.2225 0.2455 0.0313  0.0070  0.0033  1075 SER B N   
17209 C CA  . SER B 1077 ? 0.2669 0.2743 0.2935 0.0283  0.0073  0.0032  1075 SER B CA  
17210 C C   . SER B 1077 ? 0.2145 0.2244 0.2436 0.0260  0.0077  0.0008  1075 SER B C   
17211 O O   . SER B 1077 ? 0.2557 0.2718 0.2873 0.0250  0.0078  0.0001  1075 SER B O   
17212 C CB  . SER B 1077 ? 0.2630 0.2675 0.2875 0.0254  0.0075  0.0048  1075 SER B CB  
17213 O OG  . SER B 1077 ? 0.3824 0.3921 0.4090 0.0223  0.0080  0.0044  1075 SER B OG  
17214 N N   . SER B 1078 ? 0.1648 0.1694 0.1928 0.0253  0.0078  -0.0006 1076 SER B N   
17215 C CA  . SER B 1078 ? 0.1515 0.1579 0.1816 0.0231  0.0080  -0.0028 1076 SER B CA  
17216 C C   . SER B 1078 ? 0.1492 0.1612 0.1815 0.0248  0.0080  -0.0041 1076 SER B C   
17217 O O   . SER B 1078 ? 0.1658 0.1779 0.1975 0.0281  0.0079  -0.0040 1076 SER B O   
17218 C CB  . SER B 1078 ? 0.1656 0.1649 0.1936 0.0225  0.0078  -0.0040 1076 SER B CB  
17219 O OG  . SER B 1078 ? 0.1415 0.1425 0.1713 0.0210  0.0077  -0.0062 1076 SER B OG  
17220 N N   . ALA B 1079 ? 0.1416 0.1581 0.1764 0.0227  0.0080  -0.0053 1077 ALA B N   
17221 C CA  . ALA B 1079 ? 0.1143 0.1354 0.1508 0.0237  0.0080  -0.0065 1077 ALA B CA  
17222 C C   . ALA B 1079 ? 0.1332 0.1519 0.1694 0.0232  0.0079  -0.0086 1077 ALA B C   
17223 O O   . ALA B 1079 ? 0.1304 0.1526 0.1678 0.0233  0.0078  -0.0097 1077 ALA B O   
17224 C CB  . ALA B 1079 ? 0.1439 0.1711 0.1826 0.0221  0.0079  -0.0064 1077 ALA B CB  
17225 N N   . LEU B 1080 ? 0.1274 0.1400 0.1618 0.0223  0.0077  -0.0092 1078 LEU B N   
17226 C CA  . LEU B 1080 ? 0.1126 0.1223 0.1461 0.0220  0.0073  -0.0112 1078 LEU B CA  
17227 C C   . LEU B 1080 ? 0.1067 0.1173 0.1392 0.0252  0.0076  -0.0120 1078 LEU B C   
17228 O O   . LEU B 1080 ? 0.1289 0.1379 0.1600 0.0281  0.0080  -0.0112 1078 LEU B O   
17229 C CB  . LEU B 1080 ? 0.1149 0.1170 0.1458 0.0211  0.0069  -0.0115 1078 LEU B CB  
17230 C CG  . LEU B 1080 ? 0.1275 0.1253 0.1566 0.0209  0.0062  -0.0136 1078 LEU B CG  
17231 C CD1 . LEU B 1080 ? 0.1508 0.1517 0.1823 0.0179  0.0056  -0.0150 1078 LEU B CD1 
17232 C CD2 . LEU B 1080 ? 0.1576 0.1469 0.1834 0.0204  0.0057  -0.0136 1078 LEU B CD2 
17233 N N   . GLY B 1081 ? 0.1271 0.1401 0.1603 0.0247  0.0074  -0.0135 1079 GLY B N   
17234 C CA  . GLY B 1081 ? 0.1464 0.1607 0.1786 0.0275  0.0080  -0.0142 1079 GLY B CA  
17235 C C   . GLY B 1081 ? 0.1500 0.1715 0.1846 0.0281  0.0085  -0.0134 1079 GLY B C   
17236 O O   . GLY B 1081 ? 0.1628 0.1863 0.1969 0.0301  0.0091  -0.0138 1079 GLY B O   
17237 N N   . LEU B 1082 ? 0.1305 0.1558 0.1674 0.0264  0.0082  -0.0122 1080 LEU B N   
17238 C CA  A LEU B 1082 ? 0.1155 0.1472 0.1544 0.0262  0.0084  -0.0116 1080 LEU B CA  
17239 C CA  B LEU B 1082 ? 0.1158 0.1475 0.1547 0.0262  0.0084  -0.0116 1080 LEU B CA  
17240 C C   . LEU B 1082 ? 0.1373 0.1703 0.1761 0.0254  0.0083  -0.0130 1080 LEU B C   
17241 O O   . LEU B 1082 ? 0.1375 0.1679 0.1757 0.0237  0.0076  -0.0143 1080 LEU B O   
17242 C CB  A LEU B 1082 ? 0.1254 0.1596 0.1661 0.0240  0.0079  -0.0106 1080 LEU B CB  
17243 C CB  B LEU B 1082 ? 0.1255 0.1598 0.1661 0.0240  0.0079  -0.0106 1080 LEU B CB  
17244 C CG  A LEU B 1082 ? 0.1135 0.1535 0.1559 0.0230  0.0077  -0.0100 1080 LEU B CG  
17245 C CG  B LEU B 1082 ? 0.1153 0.1555 0.1577 0.0234  0.0078  -0.0100 1080 LEU B CG  
17246 C CD1 A LEU B 1082 ? 0.1216 0.1629 0.1647 0.0219  0.0074  -0.0088 1080 LEU B CD1 
17247 C CD1 B LEU B 1082 ? 0.1357 0.1795 0.1787 0.0257  0.0082  -0.0088 1080 LEU B CD1 
17248 C CD2 A LEU B 1082 ? 0.1271 0.1679 0.1698 0.0212  0.0072  -0.0114 1080 LEU B CD2 
17249 C CD2 B LEU B 1082 ? 0.1250 0.1667 0.1683 0.0214  0.0073  -0.0093 1080 LEU B CD2 
17250 N N   . ASP B 1083 ? 0.1506 0.1877 0.1898 0.0265  0.0088  -0.0127 1081 ASP B N   
17251 C CA  . ASP B 1083 ? 0.1825 0.2206 0.2210 0.0259  0.0089  -0.0139 1081 ASP B CA  
17252 C C   . ASP B 1083 ? 0.1629 0.2071 0.2030 0.0256  0.0092  -0.0128 1081 ASP B C   
17253 O O   . ASP B 1083 ? 0.2104 0.2577 0.2510 0.0276  0.0102  -0.0120 1081 ASP B O   
17254 C CB  . ASP B 1083 ? 0.1876 0.2222 0.2233 0.0281  0.0096  -0.0150 1081 ASP B CB  
17255 C CG  . ASP B 1083 ? 0.3028 0.3378 0.3369 0.0275  0.0097  -0.0161 1081 ASP B CG  
17256 O OD1 . ASP B 1083 ? 0.3381 0.3749 0.3729 0.0252  0.0089  -0.0162 1081 ASP B OD1 
17257 O OD2 . ASP B 1083 ? 0.3974 0.4306 0.4290 0.0296  0.0105  -0.0170 1081 ASP B OD2 
17258 N N   . LEU B 1084 ? 0.1497 0.1957 0.1908 0.0231  0.0084  -0.0127 1082 LEU B N   
17259 C CA  . LEU B 1084 ? 0.1704 0.2216 0.2130 0.0220  0.0083  -0.0115 1082 LEU B CA  
17260 C C   . LEU B 1084 ? 0.1617 0.2132 0.2032 0.0203  0.0079  -0.0121 1082 LEU B C   
17261 O O   . LEU B 1084 ? 0.1572 0.2051 0.1974 0.0194  0.0072  -0.0134 1082 LEU B O   
17262 C CB  . LEU B 1084 ? 0.1817 0.2340 0.2257 0.0206  0.0074  -0.0107 1082 LEU B CB  
17263 C CG  . LEU B 1084 ? 0.2076 0.2603 0.2526 0.0218  0.0075  -0.0096 1082 LEU B CG  
17264 C CD1 . LEU B 1084 ? 0.2048 0.2583 0.2504 0.0200  0.0067  -0.0090 1082 LEU B CD1 
17265 C CD2 . LEU B 1084 ? 0.2503 0.3073 0.2965 0.0238  0.0082  -0.0083 1082 LEU B CD2 
17266 N N   . GLU B 1085 ? 0.1453 0.2011 0.1875 0.0198  0.0083  -0.0112 1083 GLU B N   
17267 C CA  . GLU B 1085 ? 0.1353 0.1915 0.1764 0.0175  0.0077  -0.0113 1083 GLU B CA  
17268 C C   . GLU B 1085 ? 0.1406 0.1991 0.1831 0.0155  0.0067  -0.0104 1083 GLU B C   
17269 O O   . GLU B 1085 ? 0.2004 0.2631 0.2448 0.0156  0.0069  -0.0091 1083 GLU B O   
17270 C CB  . GLU B 1085 ? 0.1317 0.1906 0.1720 0.0177  0.0089  -0.0108 1083 GLU B CB  
17271 C CG  . GLU B 1085 ? 0.1696 0.2277 0.2081 0.0152  0.0080  -0.0109 1083 GLU B CG  
17272 C CD  . GLU B 1085 ? 0.2057 0.2659 0.2427 0.0149  0.0093  -0.0104 1083 GLU B CD  
17273 O OE1 . GLU B 1085 ? 0.2410 0.3026 0.2778 0.0171  0.0109  -0.0105 1083 GLU B OE1 
17274 O OE2 . GLU B 1085 ? 0.2327 0.2928 0.2683 0.0125  0.0086  -0.0099 1083 GLU B OE2 
17275 N N   . LEU B 1086 ? 0.1123 0.1680 0.1537 0.0138  0.0054  -0.0112 1084 LEU B N   
17276 C CA  . LEU B 1086 ? 0.1269 0.1835 0.1687 0.0120  0.0043  -0.0107 1084 LEU B CA  
17277 C C   . LEU B 1086 ? 0.1762 0.2341 0.2169 0.0099  0.0038  -0.0101 1084 LEU B C   
17278 O O   . LEU B 1086 ? 0.1732 0.2291 0.2119 0.0095  0.0038  -0.0105 1084 LEU B O   
17279 C CB  . LEU B 1086 ? 0.1385 0.1913 0.1796 0.0116  0.0033  -0.0119 1084 LEU B CB  
17280 C CG  . LEU B 1086 ? 0.1431 0.1944 0.1852 0.0130  0.0037  -0.0125 1084 LEU B CG  
17281 C CD1 . LEU B 1086 ? 0.1647 0.2133 0.2066 0.0124  0.0029  -0.0136 1084 LEU B CD1 
17282 C CD2 . LEU B 1086 ? 0.1892 0.2431 0.2328 0.0137  0.0042  -0.0112 1084 LEU B CD2 
17283 N N   . PRO B 1087 ? 0.1342 0.1950 0.1757 0.0083  0.0032  -0.0090 1085 PRO B N   
17284 C CA  . PRO B 1087 ? 0.1636 0.2251 0.2038 0.0058  0.0026  -0.0083 1085 PRO B CA  
17285 C C   . PRO B 1087 ? 0.1430 0.1992 0.1802 0.0046  0.0013  -0.0094 1085 PRO B C   
17286 O O   . PRO B 1087 ? 0.1773 0.2307 0.2142 0.0050  0.0004  -0.0104 1085 PRO B O   
17287 C CB  . PRO B 1087 ? 0.2077 0.2728 0.2494 0.0043  0.0018  -0.0072 1085 PRO B CB  
17288 C CG  . PRO B 1087 ? 0.2002 0.2676 0.2442 0.0065  0.0024  -0.0070 1085 PRO B CG  
17289 C CD  . PRO B 1087 ? 0.1495 0.2129 0.1929 0.0087  0.0030  -0.0083 1085 PRO B CD  
17290 N N   . GLY B 1088 ? 0.1527 0.2077 0.1878 0.0032  0.0012  -0.0091 1086 GLY B N   
17291 C CA  . GLY B 1088 ? 0.1598 0.2096 0.1919 0.0024  -0.0002 -0.0099 1086 GLY B CA  
17292 C C   . GLY B 1088 ? 0.1149 0.1640 0.1444 0.0002  -0.0003 -0.0089 1086 GLY B C   
17293 O O   . GLY B 1088 ? 0.1549 0.2084 0.1854 -0.0013 0.0005  -0.0074 1086 GLY B O   
17294 N N   . PRO B 1089 ? 0.1534 0.1974 0.1795 0.0000  -0.0013 -0.0096 1087 PRO B N   
17295 C CA  . PRO B 1089 ? 0.1477 0.1901 0.1706 -0.0023 -0.0016 -0.0085 1087 PRO B CA  
17296 C C   . PRO B 1089 ? 0.1449 0.1902 0.1678 -0.0018 0.0004  -0.0077 1087 PRO B C   
17297 O O   . PRO B 1089 ? 0.1604 0.2067 0.1846 0.0007  0.0015  -0.0086 1087 PRO B O   
17298 C CB  . PRO B 1089 ? 0.1774 0.2130 0.1968 -0.0018 -0.0034 -0.0096 1087 PRO B CB  
17299 C CG  . PRO B 1089 ? 0.2138 0.2490 0.2352 0.0012  -0.0032 -0.0113 1087 PRO B CG  
17300 C CD  . PRO B 1089 ? 0.1984 0.2380 0.2237 0.0018  -0.0024 -0.0113 1087 PRO B CD  
17301 N N   . VAL B 1090 ? 0.1362 0.1826 0.1573 -0.0044 0.0008  -0.0061 1088 VAL B N   
17302 C CA  . VAL B 1090 ? 0.1341 0.1824 0.1540 -0.0040 0.0027  -0.0055 1088 VAL B CA  
17303 C C   . VAL B 1090 ? 0.1584 0.2009 0.1746 -0.0024 0.0020  -0.0067 1088 VAL B C   
17304 O O   . VAL B 1090 ? 0.1561 0.1931 0.1702 -0.0023 -0.0001 -0.0076 1088 VAL B O   
17305 C CB  . VAL B 1090 ? 0.1611 0.2115 0.1794 -0.0075 0.0033  -0.0034 1088 VAL B CB  
17306 C CG1 . VAL B 1090 ? 0.1574 0.2143 0.1798 -0.0093 0.0038  -0.0022 1088 VAL B CG1 
17307 C CG2 . VAL B 1090 ? 0.1764 0.2198 0.1898 -0.0099 0.0012  -0.0031 1088 VAL B CG2 
17308 N N   . GLY B 1091 ? 0.1580 0.2020 0.1733 -0.0009 0.0037  -0.0068 1089 GLY B N   
17309 C CA  . GLY B 1091 ? 0.1444 0.1831 0.1558 0.0005  0.0030  -0.0079 1089 GLY B CA  
17310 C C   . GLY B 1091 ? 0.1475 0.1841 0.1606 0.0033  0.0020  -0.0100 1089 GLY B C   
17311 O O   . GLY B 1091 ? 0.1386 0.1706 0.1488 0.0043  0.0007  -0.0111 1089 GLY B O   
17312 N N   . GLU B 1092 ? 0.1556 0.1954 0.1731 0.0043  0.0024  -0.0104 1090 GLU B N   
17313 C CA  . GLU B 1092 ? 0.1403 0.1787 0.1597 0.0066  0.0018  -0.0122 1090 GLU B CA  
17314 C C   . GLU B 1092 ? 0.1388 0.1816 0.1619 0.0080  0.0035  -0.0121 1090 GLU B C   
17315 O O   . GLU B 1092 ? 0.1522 0.1994 0.1775 0.0071  0.0045  -0.0108 1090 GLU B O   
17316 C CB  . GLU B 1092 ? 0.1796 0.2157 0.2001 0.0061  -0.0002 -0.0128 1090 GLU B CB  
17317 C CG  . GLU B 1092 ? 0.2331 0.2660 0.2538 0.0078  -0.0016 -0.0145 1090 GLU B CG  
17318 C CD  . GLU B 1092 ? 0.2253 0.2560 0.2463 0.0073  -0.0034 -0.0149 1090 GLU B CD  
17319 O OE1 . GLU B 1092 ? 0.2087 0.2415 0.2323 0.0070  -0.0032 -0.0148 1090 GLU B OE1 
17320 O OE2 . GLU B 1092 ? 0.2581 0.2847 0.2764 0.0073  -0.0052 -0.0154 1090 GLU B OE2 
17321 N N   . ARG B 1093 ? 0.1260 0.1676 0.1497 0.0102  0.0037  -0.0135 1091 ARG B N   
17322 C CA  . ARG B 1093 ? 0.1236 0.1680 0.1505 0.0118  0.0050  -0.0136 1091 ARG B CA  
17323 C C   . ARG B 1093 ? 0.1124 0.1546 0.1411 0.0125  0.0037  -0.0148 1091 ARG B C   
17324 O O   . ARG B 1093 ? 0.1257 0.1643 0.1531 0.0130  0.0027  -0.0161 1091 ARG B O   
17325 C CB  . ARG B 1093 ? 0.1862 0.2307 0.2117 0.0138  0.0066  -0.0141 1091 ARG B CB  
17326 C CG  . ARG B 1093 ? 0.2692 0.3160 0.2974 0.0158  0.0078  -0.0142 1091 ARG B CG  
17327 C CD  . ARG B 1093 ? 0.3288 0.3756 0.3552 0.0180  0.0096  -0.0147 1091 ARG B CD  
17328 N NE  . ARG B 1093 ? 0.3420 0.3913 0.3664 0.0173  0.0109  -0.0137 1091 ARG B NE  
17329 C CZ  . ARG B 1093 ? 0.3176 0.3641 0.3377 0.0174  0.0111  -0.0144 1091 ARG B CZ  
17330 N NH1 . ARG B 1093 ? 0.4020 0.4431 0.4194 0.0183  0.0099  -0.0161 1091 ARG B NH1 
17331 N NH2 . ARG B 1093 ? 0.3516 0.4009 0.3700 0.0165  0.0125  -0.0132 1091 ARG B NH2 
17332 N N   . ASN B 1094 ? 0.0973 0.1419 0.1289 0.0123  0.0038  -0.0142 1092 ASN B N   
17333 C CA  . ASN B 1094 ? 0.1046 0.1476 0.1380 0.0125  0.0028  -0.0151 1092 ASN B CA  
17334 C C   . ASN B 1094 ? 0.1300 0.1745 0.1656 0.0140  0.0039  -0.0149 1092 ASN B C   
17335 O O   . ASN B 1094 ? 0.1335 0.1815 0.1708 0.0141  0.0047  -0.0138 1092 ASN B O   
17336 C CB  . ASN B 1094 ? 0.1163 0.1598 0.1503 0.0110  0.0017  -0.0146 1092 ASN B CB  
17337 C CG  . ASN B 1094 ? 0.1126 0.1531 0.1440 0.0099  0.0003  -0.0151 1092 ASN B CG  
17338 O OD1 . ASN B 1094 ? 0.1334 0.1711 0.1643 0.0106  -0.0008 -0.0163 1092 ASN B OD1 
17339 N ND2 . ASN B 1094 ? 0.1445 0.1855 0.1742 0.0083  0.0001  -0.0140 1092 ASN B ND2 
17340 N N   . LEU B 1095 ? 0.1208 0.1627 0.1563 0.0150  0.0037  -0.0161 1093 LEU B N   
17341 C CA  . LEU B 1095 ? 0.1133 0.1553 0.1500 0.0166  0.0048  -0.0160 1093 LEU B CA  
17342 C C   . LEU B 1095 ? 0.1108 0.1516 0.1493 0.0162  0.0041  -0.0164 1093 LEU B C   
17343 O O   . LEU B 1095 ? 0.1301 0.1694 0.1688 0.0153  0.0030  -0.0173 1093 LEU B O   
17344 C CB  . LEU B 1095 ? 0.1381 0.1773 0.1725 0.0180  0.0052  -0.0170 1093 LEU B CB  
17345 C CG  . LEU B 1095 ? 0.1910 0.2312 0.2231 0.0182  0.0059  -0.0168 1093 LEU B CG  
17346 C CD1 . LEU B 1095 ? 0.2700 0.3067 0.2991 0.0195  0.0061  -0.0181 1093 LEU B CD1 
17347 C CD2 . LEU B 1095 ? 0.2022 0.2469 0.2357 0.0189  0.0075  -0.0153 1093 LEU B CD2 
17348 N N   . TYR B 1096 ? 0.1098 0.1515 0.1496 0.0171  0.0050  -0.0156 1094 TYR B N   
17349 C CA  . TYR B 1096 ? 0.1145 0.1553 0.1558 0.0166  0.0047  -0.0156 1094 TYR B CA  
17350 C C   . TYR B 1096 ? 0.1190 0.1579 0.1601 0.0180  0.0055  -0.0154 1094 TYR B C   
17351 O O   . TYR B 1096 ? 0.1205 0.1607 0.1615 0.0195  0.0064  -0.0144 1094 TYR B O   
17352 C CB  . TYR B 1096 ? 0.0919 0.1358 0.1346 0.0158  0.0047  -0.0145 1094 TYR B CB  
17353 C CG  . TYR B 1096 ? 0.1036 0.1470 0.1474 0.0154  0.0048  -0.0142 1094 TYR B CG  
17354 C CD1 . TYR B 1096 ? 0.1031 0.1459 0.1477 0.0143  0.0042  -0.0150 1094 TYR B CD1 
17355 C CD2 . TYR B 1096 ? 0.1314 0.1753 0.1756 0.0164  0.0055  -0.0130 1094 TYR B CD2 
17356 C CE1 . TYR B 1096 ? 0.1087 0.1516 0.1543 0.0138  0.0046  -0.0146 1094 TYR B CE1 
17357 C CE2 . TYR B 1096 ? 0.1336 0.1768 0.1783 0.0158  0.0057  -0.0125 1094 TYR B CE2 
17358 C CZ  . TYR B 1096 ? 0.1277 0.1706 0.1731 0.0144  0.0054  -0.0133 1094 TYR B CZ  
17359 O OH  . TYR B 1096 ? 0.1330 0.1757 0.1788 0.0138  0.0059  -0.0127 1094 TYR B OH  
17360 N N   . THR B 1097 ? 0.0991 0.1347 0.1401 0.0176  0.0051  -0.0163 1095 THR B N   
17361 C CA  . THR B 1097 ? 0.1026 0.1348 0.1426 0.0188  0.0056  -0.0163 1095 THR B CA  
17362 C C   . THR B 1097 ? 0.1147 0.1449 0.1557 0.0175  0.0054  -0.0162 1095 THR B C   
17363 O O   . THR B 1097 ? 0.1318 0.1630 0.1743 0.0157  0.0048  -0.0167 1095 THR B O   
17364 C CB  . THR B 1097 ? 0.1391 0.1678 0.1767 0.0195  0.0053  -0.0178 1095 THR B CB  
17365 O OG1 . THR B 1097 ? 0.1803 0.2079 0.2181 0.0177  0.0040  -0.0191 1095 THR B OG1 
17366 C CG2 . THR B 1097 ? 0.1561 0.1868 0.1923 0.0208  0.0059  -0.0178 1095 THR B CG2 
17367 N N   . LEU B 1098 ? 0.1151 0.1429 0.1554 0.0184  0.0060  -0.0154 1096 LEU B N   
17368 C CA  . LEU B 1098 ? 0.1041 0.1295 0.1449 0.0170  0.0059  -0.0151 1096 LEU B CA  
17369 C C   . LEU B 1098 ? 0.1075 0.1272 0.1462 0.0171  0.0056  -0.0159 1096 LEU B C   
17370 O O   . LEU B 1098 ? 0.1221 0.1389 0.1586 0.0192  0.0060  -0.0158 1096 LEU B O   
17371 C CB  . LEU B 1098 ? 0.0908 0.1173 0.1319 0.0175  0.0066  -0.0132 1096 LEU B CB  
17372 C CG  . LEU B 1098 ? 0.0932 0.1247 0.1358 0.0170  0.0067  -0.0124 1096 LEU B CG  
17373 C CD1 . LEU B 1098 ? 0.1112 0.1431 0.1534 0.0176  0.0073  -0.0105 1096 LEU B CD1 
17374 C CD2 . LEU B 1098 ? 0.1181 0.1514 0.1624 0.0148  0.0064  -0.0132 1096 LEU B CD2 
17375 N N   . HIS B 1099 ? 0.1313 0.1494 0.1708 0.0148  0.0048  -0.0168 1097 HIS B N   
17376 C CA  . HIS B 1099 ? 0.1229 0.1356 0.1607 0.0141  0.0041  -0.0179 1097 HIS B CA  
17377 C C   . HIS B 1099 ? 0.1326 0.1434 0.1714 0.0117  0.0041  -0.0170 1097 HIS B C   
17378 O O   . HIS B 1099 ? 0.1473 0.1615 0.1882 0.0106  0.0048  -0.0159 1097 HIS B O   
17379 C CB  . HIS B 1099 ? 0.1337 0.1467 0.1718 0.0129  0.0027  -0.0197 1097 HIS B CB  
17380 C CG  . HIS B 1099 ? 0.1407 0.1554 0.1776 0.0148  0.0027  -0.0205 1097 HIS B CG  
17381 N ND1 . HIS B 1099 ? 0.2050 0.2161 0.2386 0.0162  0.0024  -0.0217 1097 HIS B ND1 
17382 C CD2 . HIS B 1099 ? 0.1792 0.1987 0.2174 0.0153  0.0030  -0.0201 1097 HIS B CD2 
17383 C CE1 . HIS B 1099 ? 0.2165 0.2304 0.2495 0.0174  0.0026  -0.0219 1097 HIS B CE1 
17384 N NE2 . HIS B 1099 ? 0.1860 0.2049 0.2219 0.0167  0.0029  -0.0209 1097 HIS B NE2 
17385 N N   . ALA B 1100 ? 0.1583 0.1633 0.1950 0.0109  0.0035  -0.0177 1098 ALA B N   
17386 C CA  . ALA B 1100 ? 0.1693 0.1725 0.2070 0.0079  0.0034  -0.0170 1098 ALA B CA  
17387 C C   . ALA B 1100 ? 0.1714 0.1796 0.2131 0.0052  0.0028  -0.0177 1098 ALA B C   
17388 O O   . ALA B 1100 ? 0.1923 0.2029 0.2350 0.0054  0.0018  -0.0192 1098 ALA B O   
17389 C CB  . ALA B 1100 ? 0.2005 0.1961 0.2351 0.0071  0.0024  -0.0178 1098 ALA B CB  
17390 N N   . ARG B 1101 ? 0.1822 0.1922 0.2262 0.0027  0.0035  -0.0165 1099 ARG B N   
17391 C CA  . ARG B 1101 ? 0.1929 0.2081 0.2410 0.0003  0.0031  -0.0171 1099 ARG B CA  
17392 C C   . ARG B 1101 ? 0.2106 0.2235 0.2595 -0.0023 0.0015  -0.0184 1099 ARG B C   
17393 O O   . ARG B 1101 ? 0.2217 0.2385 0.2735 -0.0031 0.0004  -0.0198 1099 ARG B O   
17394 C CB  . ARG B 1101 ? 0.2242 0.2429 0.2746 -0.0013 0.0047  -0.0154 1099 ARG B CB  
17395 C CG  . ARG B 1101 ? 0.2258 0.2486 0.2765 0.0007  0.0059  -0.0146 1099 ARG B CG  
17396 C CD  . ARG B 1101 ? 0.2515 0.2778 0.3039 -0.0009 0.0074  -0.0132 1099 ARG B CD  
17397 N NE  . ARG B 1101 ? 0.2877 0.3201 0.3442 -0.0020 0.0075  -0.0141 1099 ARG B NE  
17398 C CZ  . ARG B 1101 ? 0.3250 0.3621 0.3827 -0.0005 0.0079  -0.0145 1099 ARG B CZ  
17399 N NH1 . ARG B 1101 ? 0.2691 0.3056 0.3244 0.0020  0.0080  -0.0142 1099 ARG B NH1 
17400 N NH2 . ARG B 1101 ? 0.2790 0.3213 0.3402 -0.0013 0.0082  -0.0153 1099 ARG B NH2 
17401 N N   . GLY B 1102 ? 0.1701 0.1767 0.2164 -0.0037 0.0012  -0.0180 1100 GLY B N   
17402 C CA  . GLY B 1102 ? 0.1939 0.1983 0.2411 -0.0070 -0.0003 -0.0191 1100 GLY B CA  
17403 C C   . GLY B 1102 ? 0.1685 0.1682 0.2145 -0.0099 0.0001  -0.0176 1100 GLY B C   
17404 O O   . GLY B 1102 ? 0.1987 0.1922 0.2405 -0.0085 0.0007  -0.0166 1100 GLY B O   
17405 N N   . ARG B 1103 ? 0.1757 0.1782 0.2253 -0.0138 -0.0001 -0.0174 1101 ARG B N   
17406 C CA  . ARG B 1103 ? 0.1693 0.1676 0.2179 -0.0173 0.0004  -0.0157 1101 ARG B CA  
17407 C C   . ARG B 1103 ? 0.1557 0.1598 0.2073 -0.0185 0.0027  -0.0137 1101 ARG B C   
17408 O O   . ARG B 1103 ? 0.1711 0.1835 0.2279 -0.0195 0.0032  -0.0140 1101 ARG B O   
17409 C CB  . ARG B 1103 ? 0.1641 0.1612 0.2145 -0.0216 -0.0016 -0.0168 1101 ARG B CB  
17410 C CG  . ARG B 1103 ? 0.2035 0.1947 0.2519 -0.0255 -0.0012 -0.0150 1101 ARG B CG  
17411 C CD  . ARG B 1103 ? 0.2569 0.2444 0.3055 -0.0299 -0.0036 -0.0162 1101 ARG B CD  
17412 N NE  . ARG B 1103 ? 0.3034 0.2844 0.3479 -0.0280 -0.0059 -0.0185 1101 ARG B NE  
17413 C CZ  . ARG B 1103 ? 0.3510 0.3211 0.3891 -0.0277 -0.0069 -0.0188 1101 ARG B CZ  
17414 N NH1 . ARG B 1103 ? 0.2832 0.2467 0.3178 -0.0289 -0.0059 -0.0168 1101 ARG B NH1 
17415 N NH2 . ARG B 1103 ? 0.3240 0.2893 0.3586 -0.0259 -0.0090 -0.0212 1101 ARG B NH2 
17416 N N   . ILE B 1104 ? 0.1321 0.1320 0.1804 -0.0180 0.0041  -0.0116 1102 ILE B N   
17417 C CA  . ILE B 1104 ? 0.1449 0.1495 0.1948 -0.0188 0.0064  -0.0094 1102 ILE B CA  
17418 C C   . ILE B 1104 ? 0.1403 0.1433 0.1910 -0.0238 0.0070  -0.0079 1102 ILE B C   
17419 O O   . ILE B 1104 ? 0.1509 0.1456 0.1978 -0.0254 0.0062  -0.0072 1102 ILE B O   
17420 C CB  . ILE B 1104 ? 0.1516 0.1527 0.1972 -0.0154 0.0076  -0.0078 1102 ILE B CB  
17421 C CG1 . ILE B 1104 ? 0.1485 0.1504 0.1931 -0.0108 0.0068  -0.0093 1102 ILE B CG1 
17422 C CG2 . ILE B 1104 ? 0.1616 0.1679 0.2086 -0.0160 0.0098  -0.0059 1102 ILE B CG2 
17423 C CD1 . ILE B 1104 ? 0.1689 0.1794 0.2176 -0.0097 0.0071  -0.0105 1102 ILE B CD1 
17424 N N   . LEU B 1105 ? 0.1297 0.1407 0.1852 -0.0262 0.0085  -0.0073 1103 LEU B N   
17425 C CA  . LEU B 1105 ? 0.1382 0.1490 0.1947 -0.0311 0.0096  -0.0054 1103 LEU B CA  
17426 C C   . LEU B 1105 ? 0.1553 0.1621 0.2074 -0.0308 0.0115  -0.0026 1103 LEU B C   
17427 O O   . LEU B 1105 ? 0.1460 0.1570 0.1980 -0.0283 0.0132  -0.0019 1103 LEU B O   
17428 C CB  . LEU B 1105 ? 0.1420 0.1638 0.2054 -0.0334 0.0107  -0.0058 1103 LEU B CB  
17429 C CG  . LEU B 1105 ? 0.1559 0.1799 0.2214 -0.0386 0.0125  -0.0037 1103 LEU B CG  
17430 C CD1 . LEU B 1105 ? 0.1583 0.1763 0.2232 -0.0431 0.0105  -0.0037 1103 LEU B CD1 
17431 C CD2 . LEU B 1105 ? 0.1957 0.2317 0.2681 -0.0395 0.0141  -0.0041 1103 LEU B CD2 
17432 N N   . LEU B 1106 ? 0.1455 0.1437 0.1935 -0.0334 0.0111  -0.0010 1104 LEU B N   
17433 C CA  . LEU B 1106 ? 0.1552 0.1482 0.1982 -0.0333 0.0127  0.0019  1104 LEU B CA  
17434 C C   . LEU B 1106 ? 0.1633 0.1581 0.2079 -0.0389 0.0144  0.0041  1104 LEU B C   
17435 O O   . LEU B 1106 ? 0.1784 0.1706 0.2241 -0.0433 0.0134  0.0040  1104 LEU B O   
17436 C CB  . LEU B 1106 ? 0.1737 0.1546 0.2101 -0.0318 0.0110  0.0024  1104 LEU B CB  
17437 C CG  . LEU B 1106 ? 0.2279 0.2063 0.2609 -0.0257 0.0106  0.0019  1104 LEU B CG  
17438 C CD1 . LEU B 1106 ? 0.2132 0.1992 0.2501 -0.0225 0.0102  -0.0006 1104 LEU B CD1 
17439 C CD2 . LEU B 1106 ? 0.2028 0.1696 0.2301 -0.0245 0.0087  0.0017  1104 LEU B CD2 
17440 N N   . VAL B 1107 ? 0.1767 0.1760 0.2212 -0.0388 0.0169  0.0061  1105 VAL B N   
17441 C CA  . VAL B 1107 ? 0.1713 0.1730 0.2170 -0.0440 0.0191  0.0085  1105 VAL B CA  
17442 C C   . VAL B 1107 ? 0.1843 0.1791 0.2232 -0.0435 0.0203  0.0116  1105 VAL B C   
17443 O O   . VAL B 1107 ? 0.2061 0.2057 0.2446 -0.0421 0.0225  0.0129  1105 VAL B O   
17444 C CB  . VAL B 1107 ? 0.1637 0.1783 0.2159 -0.0447 0.0213  0.0078  1105 VAL B CB  
17445 C CG1 . VAL B 1107 ? 0.1945 0.2123 0.2487 -0.0504 0.0235  0.0101  1105 VAL B CG1 
17446 C CG2 . VAL B 1107 ? 0.1724 0.1933 0.2308 -0.0438 0.0196  0.0045  1105 VAL B CG2 
17447 N N   . PRO B 1108 ? 0.1839 0.1673 0.2172 -0.0443 0.0189  0.0129  1106 PRO B N   
17448 C CA  . PRO B 1108 ? 0.1953 0.1713 0.2217 -0.0435 0.0197  0.0160  1106 PRO B CA  
17449 C C   . PRO B 1108 ? 0.2247 0.2010 0.2504 -0.0492 0.0220  0.0191  1106 PRO B C   
17450 O O   . PRO B 1108 ? 0.2448 0.2247 0.2747 -0.0543 0.0225  0.0190  1106 PRO B O   
17451 C CB  . PRO B 1108 ? 0.2185 0.1818 0.2395 -0.0423 0.0170  0.0159  1106 PRO B CB  
17452 C CG  . PRO B 1108 ? 0.2091 0.1722 0.2337 -0.0460 0.0155  0.0138  1106 PRO B CG  
17453 C CD  . PRO B 1108 ? 0.2053 0.1812 0.2376 -0.0454 0.0161  0.0113  1106 PRO B CD  
17454 N N   . ALA B 1109 ? 0.2101 0.1823 0.2301 -0.0482 0.0232  0.0220  1107 ALA B N   
17455 C CA  . ALA B 1109 ? 0.2375 0.2069 0.2544 -0.0533 0.0252  0.0256  1107 ALA B CA  
17456 C C   . ALA B 1109 ? 0.3029 0.2580 0.3116 -0.0537 0.0238  0.0282  1107 ALA B C   
17457 O O   . ALA B 1109 ? 0.3123 0.2619 0.3187 -0.0592 0.0242  0.0304  1107 ALA B O   
17458 C CB  . ALA B 1109 ? 0.2636 0.2404 0.2802 -0.0524 0.0282  0.0273  1107 ALA B CB  
17459 N N   . THR B 1110 ? 0.2893 0.2380 0.2933 -0.0480 0.0219  0.0278  1108 THR B N   
17460 C CA  . THR B 1110 ? 0.2616 0.1965 0.2574 -0.0471 0.0204  0.0302  1108 THR B CA  
17461 C C   . THR B 1110 ? 0.2759 0.2039 0.2703 -0.0428 0.0174  0.0277  1108 THR B C   
17462 O O   . THR B 1110 ? 0.2477 0.1821 0.2468 -0.0394 0.0166  0.0245  1108 THR B O   
17463 C CB  . THR B 1110 ? 0.3072 0.2407 0.2976 -0.0437 0.0214  0.0329  1108 THR B CB  
17464 O OG1 . THR B 1110 ? 0.2981 0.2366 0.2902 -0.0372 0.0205  0.0308  1108 THR B OG1 
17465 C CG2 . THR B 1110 ? 0.3106 0.2518 0.3021 -0.0474 0.0246  0.0352  1108 THR B CG2 
17466 N N   . GLU B 1111 ? 0.3272 0.2417 0.3148 -0.0429 0.0157  0.0292  1109 GLU B N   
17467 C CA  . GLU B 1111 ? 0.3058 0.2124 0.2910 -0.0385 0.0129  0.0270  1109 GLU B CA  
17468 C C   . GLU B 1111 ? 0.2850 0.1957 0.2706 -0.0311 0.0125  0.0257  1109 GLU B C   
17469 O O   . GLU B 1111 ? 0.2692 0.1831 0.2580 -0.0278 0.0113  0.0225  1109 GLU B O   
17470 C CB  . GLU B 1111 ? 0.2936 0.1844 0.2703 -0.0393 0.0114  0.0292  1109 GLU B CB  
17471 C CG  . GLU B 1111 ? 0.3175 0.1994 0.2907 -0.0339 0.0087  0.0271  1109 GLU B CG  
17472 C CD  . GLU B 1111 ? 0.3578 0.2233 0.3224 -0.0348 0.0071  0.0291  1109 GLU B CD  
17473 O OE1 . GLU B 1111 ? 0.3964 0.2554 0.3600 -0.0398 0.0062  0.0287  1109 GLU B OE1 
17474 O OE2 . GLU B 1111 ? 0.4348 0.2939 0.3936 -0.0305 0.0066  0.0313  1109 GLU B OE2 
17475 N N   . SER B 1112 ? 0.3025 0.2132 0.2846 -0.0285 0.0133  0.0283  1110 SER B N   
17476 C CA  . SER B 1112 ? 0.2823 0.1978 0.2652 -0.0219 0.0128  0.0273  1110 SER B CA  
17477 C C   . SER B 1112 ? 0.2657 0.1948 0.2564 -0.0214 0.0138  0.0244  1110 SER B C   
17478 O O   . SER B 1112 ? 0.2622 0.1946 0.2551 -0.0167 0.0128  0.0220  1110 SER B O   
17479 C CB  . SER B 1112 ? 0.3117 0.2263 0.2900 -0.0201 0.0135  0.0307  1110 SER B CB  
17480 O OG  . SER B 1112 ? 0.3185 0.2379 0.2978 -0.0139 0.0128  0.0297  1110 SER B OG  
17481 N N   . GLY B 1113 ? 0.2528 0.1896 0.2474 -0.0260 0.0159  0.0248  1111 GLY B N   
17482 C CA  . GLY B 1113 ? 0.2325 0.1815 0.2343 -0.0255 0.0167  0.0220  1111 GLY B CA  
17483 C C   . GLY B 1113 ? 0.2342 0.1837 0.2398 -0.0250 0.0152  0.0186  1111 GLY B C   
17484 O O   . GLY B 1113 ? 0.2244 0.1802 0.2336 -0.0215 0.0147  0.0161  1111 GLY B O   
17485 N N   . LEU B 1114 ? 0.2341 0.1766 0.2386 -0.0286 0.0142  0.0184  1112 LEU B N   
17486 C CA  . LEU B 1114 ? 0.2016 0.1433 0.2087 -0.0282 0.0124  0.0151  1112 LEU B CA  
17487 C C   . LEU B 1114 ? 0.2172 0.1544 0.2215 -0.0219 0.0107  0.0137  1112 LEU B C   
17488 O O   . LEU B 1114 ? 0.2152 0.1574 0.2231 -0.0193 0.0100  0.0108  1112 LEU B O   
17489 C CB  . LEU B 1114 ? 0.2458 0.1793 0.2510 -0.0333 0.0114  0.0155  1112 LEU B CB  
17490 C CG  . LEU B 1114 ? 0.2439 0.1735 0.2499 -0.0332 0.0091  0.0123  1112 LEU B CG  
17491 C CD1 . LEU B 1114 ? 0.2503 0.1912 0.2636 -0.0331 0.0091  0.0093  1112 LEU B CD1 
17492 C CD2 . LEU B 1114 ? 0.2717 0.1926 0.2751 -0.0391 0.0081  0.0131  1112 LEU B CD2 
17493 N N   . TYR B 1115 ? 0.2310 0.1591 0.2290 -0.0193 0.0100  0.0157  1113 TYR B N   
17494 C CA  . TYR B 1115 ? 0.2327 0.1570 0.2282 -0.0130 0.0085  0.0144  1113 TYR B CA  
17495 C C   . TYR B 1115 ? 0.2224 0.1572 0.2219 -0.0089 0.0092  0.0133  1113 TYR B C   
17496 O O   . TYR B 1115 ? 0.2289 0.1654 0.2299 -0.0050 0.0082  0.0109  1113 TYR B O   
17497 C CB  . TYR B 1115 ? 0.2369 0.1503 0.2251 -0.0107 0.0078  0.0171  1113 TYR B CB  
17498 C CG  . TYR B 1115 ? 0.2695 0.1700 0.2524 -0.0138 0.0067  0.0179  1113 TYR B CG  
17499 C CD1 . TYR B 1115 ? 0.2805 0.1788 0.2650 -0.0175 0.0058  0.0157  1113 TYR B CD1 
17500 C CD2 . TYR B 1115 ? 0.3166 0.2068 0.2926 -0.0131 0.0062  0.0210  1113 TYR B CD2 
17501 C CE1 . TYR B 1115 ? 0.3483 0.2342 0.3275 -0.0207 0.0046  0.0164  1113 TYR B CE1 
17502 C CE2 . TYR B 1115 ? 0.3332 0.2106 0.3037 -0.0160 0.0050  0.0218  1113 TYR B CE2 
17503 C CZ  . TYR B 1115 ? 0.3565 0.2317 0.3286 -0.0199 0.0042  0.0195  1113 TYR B CZ  
17504 O OH  . TYR B 1115 ? 0.4273 0.2892 0.3935 -0.0231 0.0028  0.0203  1113 TYR B OH  
17505 N N   . HIS B 1116 ? 0.2151 0.1565 0.2159 -0.0096 0.0107  0.0151  1114 HIS B N   
17506 C CA  . HIS B 1116 ? 0.1971 0.1481 0.2014 -0.0061 0.0112  0.0141  1114 HIS B CA  
17507 C C   . HIS B 1116 ? 0.1986 0.1581 0.2092 -0.0073 0.0114  0.0111  1114 HIS B C   
17508 O O   . HIS B 1116 ? 0.2047 0.1689 0.2176 -0.0037 0.0109  0.0091  1114 HIS B O   
17509 C CB  . HIS B 1116 ? 0.2123 0.1680 0.2161 -0.0070 0.0127  0.0166  1114 HIS B CB  
17510 C CG  . HIS B 1116 ? 0.2444 0.1943 0.2425 -0.0039 0.0121  0.0193  1114 HIS B CG  
17511 N ND1 . HIS B 1116 ? 0.2749 0.2150 0.2674 -0.0056 0.0119  0.0220  1114 HIS B ND1 
17512 C CD2 . HIS B 1116 ? 0.2622 0.2148 0.2595 0.0007  0.0115  0.0198  1114 HIS B CD2 
17513 C CE1 . HIS B 1116 ? 0.3109 0.2478 0.2992 -0.0018 0.0111  0.0241  1114 HIS B CE1 
17514 N NE2 . HIS B 1116 ? 0.3170 0.2618 0.3084 0.0020  0.0109  0.0228  1114 HIS B NE2 
17515 N N   . GLN B 1117 ? 0.1975 0.1591 0.2109 -0.0123 0.0122  0.0107  1115 GLN B N   
17516 C CA  . GLN B 1117 ? 0.1779 0.1471 0.1972 -0.0134 0.0122  0.0078  1115 GLN B CA  
17517 C C   . GLN B 1117 ? 0.1796 0.1450 0.1988 -0.0113 0.0103  0.0053  1115 GLN B C   
17518 O O   . GLN B 1117 ? 0.1769 0.1481 0.1993 -0.0090 0.0099  0.0030  1115 GLN B O   
17519 C CB  . GLN B 1117 ? 0.1779 0.1499 0.2002 -0.0192 0.0132  0.0081  1115 GLN B CB  
17520 C CG  . GLN B 1117 ? 0.1941 0.1720 0.2175 -0.0213 0.0155  0.0102  1115 GLN B CG  
17521 C CD  . GLN B 1117 ? 0.2008 0.1822 0.2277 -0.0270 0.0166  0.0104  1115 GLN B CD  
17522 O OE1 . GLN B 1117 ? 0.2039 0.1816 0.2316 -0.0299 0.0155  0.0095  1115 GLN B OE1 
17523 N NE2 . GLN B 1117 ? 0.1727 0.1614 0.2018 -0.0287 0.0189  0.0115  1115 GLN B NE2 
17524 N N   . LEU B 1118 ? 0.1679 0.1232 0.1829 -0.0121 0.0091  0.0056  1116 LEU B N   
17525 C CA  . LEU B 1118 ? 0.1751 0.1256 0.1888 -0.0098 0.0074  0.0031  1116 LEU B CA  
17526 C C   . LEU B 1118 ? 0.1866 0.1382 0.1992 -0.0037 0.0071  0.0024  1116 LEU B C   
17527 O O   . LEU B 1118 ? 0.2122 0.1666 0.2267 -0.0015 0.0064  -0.0001 1116 LEU B O   
17528 C CB  . LEU B 1118 ? 0.2041 0.1424 0.2123 -0.0113 0.0062  0.0038  1116 LEU B CB  
17529 C CG  . LEU B 1118 ? 0.2850 0.2212 0.2944 -0.0174 0.0056  0.0033  1116 LEU B CG  
17530 C CD1 . LEU B 1118 ? 0.2997 0.2227 0.3027 -0.0190 0.0045  0.0046  1116 LEU B CD1 
17531 C CD2 . LEU B 1118 ? 0.2957 0.2352 0.3085 -0.0173 0.0044  -0.0001 1116 LEU B CD2 
17532 N N   . ALA B 1119 ? 0.1934 0.1433 0.2031 -0.0010 0.0075  0.0047  1117 ALA B N   
17533 C CA  . ALA B 1119 ? 0.1992 0.1512 0.2085 0.0047  0.0072  0.0042  1117 ALA B CA  
17534 C C   . ALA B 1119 ? 0.1812 0.1441 0.1958 0.0056  0.0078  0.0026  1117 ALA B C   
17535 O O   . ALA B 1119 ? 0.1992 0.1642 0.2148 0.0087  0.0073  0.0007  1117 ALA B O   
17536 C CB  . ALA B 1119 ? 0.2157 0.1650 0.2214 0.0071  0.0075  0.0071  1117 ALA B CB  
17537 N N   . ALA B 1120 ? 0.1828 0.1525 0.2004 0.0028  0.0090  0.0034  1118 ALA B N   
17538 C CA  . ALA B 1120 ? 0.1533 0.1327 0.1754 0.0035  0.0095  0.0020  1118 ALA B CA  
17539 C C   . ALA B 1120 ? 0.1707 0.1521 0.1958 0.0028  0.0088  -0.0009 1118 ALA B C   
17540 O O   . ALA B 1120 ? 0.1672 0.1529 0.1941 0.0054  0.0084  -0.0025 1118 ALA B O   
17541 C CB  . ALA B 1120 ? 0.1755 0.1609 0.1999 0.0004  0.0109  0.0032  1118 ALA B CB  
17542 N N   . ALA B 1121 ? 0.1554 0.1338 0.1809 -0.0009 0.0084  -0.0015 1119 ALA B N   
17543 C CA  . ALA B 1121 ? 0.1482 0.1287 0.1765 -0.0019 0.0075  -0.0042 1119 ALA B CA  
17544 C C   . ALA B 1121 ? 0.1443 0.1194 0.1697 0.0013  0.0062  -0.0059 1119 ALA B C   
17545 O O   . ALA B 1121 ? 0.1514 0.1301 0.1787 0.0027  0.0057  -0.0080 1119 ALA B O   
17546 C CB  . ALA B 1121 ? 0.1847 0.1636 0.2143 -0.0069 0.0073  -0.0043 1119 ALA B CB  
17547 N N   . LEU B 1122 ? 0.1616 0.1278 0.1822 0.0025  0.0058  -0.0050 1120 LEU B N   
17548 C CA  . LEU B 1122 ? 0.1579 0.1186 0.1754 0.0059  0.0047  -0.0067 1120 LEU B CA  
17549 C C   . LEU B 1122 ? 0.1601 0.1255 0.1782 0.0108  0.0052  -0.0069 1120 LEU B C   
17550 O O   . LEU B 1122 ? 0.1727 0.1386 0.1906 0.0131  0.0048  -0.0089 1120 LEU B O   
17551 C CB  . LEU B 1122 ? 0.1712 0.1208 0.1830 0.0064  0.0041  -0.0057 1120 LEU B CB  
17552 C CG  . LEU B 1122 ? 0.1710 0.1147 0.1816 0.0013  0.0034  -0.0055 1120 LEU B CG  
17553 C CD1 . LEU B 1122 ? 0.2300 0.1622 0.2344 0.0021  0.0028  -0.0041 1120 LEU B CD1 
17554 C CD2 . LEU B 1122 ? 0.2217 0.1650 0.2334 -0.0004 0.0020  -0.0084 1120 LEU B CD2 
17555 N N   . ALA B 1123 ? 0.1600 0.1288 0.1785 0.0122  0.0061  -0.0048 1121 ALA B N   
17556 C CA  . ALA B 1123 ? 0.1498 0.1235 0.1692 0.0165  0.0065  -0.0048 1121 ALA B CA  
17557 C C   . ALA B 1123 ? 0.1542 0.1361 0.1777 0.0163  0.0067  -0.0065 1121 ALA B C   
17558 O O   . ALA B 1123 ? 0.1555 0.1406 0.1795 0.0196  0.0068  -0.0072 1121 ALA B O   
17559 C CB  . ALA B 1123 ? 0.1581 0.1342 0.1774 0.0175  0.0071  -0.0021 1121 ALA B CB  
17560 N N   . THR B 1124 ? 0.1450 0.1304 0.1714 0.0126  0.0067  -0.0072 1122 THR B N   
17561 C CA  . THR B 1124 ? 0.1335 0.1259 0.1635 0.0122  0.0067  -0.0088 1122 THR B CA  
17562 C C   . THR B 1124 ? 0.1203 0.1106 0.1503 0.0110  0.0057  -0.0112 1122 THR B C   
17563 O O   . THR B 1124 ? 0.1421 0.1373 0.1749 0.0099  0.0054  -0.0125 1122 THR B O   
17564 C CB  . THR B 1124 ? 0.1506 0.1490 0.1838 0.0095  0.0074  -0.0080 1122 THR B CB  
17565 O OG1 . THR B 1124 ? 0.1342 0.1296 0.1672 0.0059  0.0075  -0.0071 1122 THR B OG1 
17566 C CG2 . THR B 1124 ? 0.1512 0.1529 0.1842 0.0113  0.0081  -0.0060 1122 THR B CG2 
17567 N N   . GLY B 1125 ? 0.1315 0.1138 0.1579 0.0113  0.0049  -0.0118 1123 GLY B N   
17568 C CA  . GLY B 1125 ? 0.1422 0.1216 0.1675 0.0109  0.0038  -0.0142 1123 GLY B CA  
17569 C C   . GLY B 1125 ? 0.1476 0.1262 0.1745 0.0064  0.0028  -0.0150 1123 GLY B C   
17570 O O   . GLY B 1125 ? 0.1689 0.1455 0.1951 0.0057  0.0015  -0.0170 1123 GLY B O   
17571 N N   . ASN B 1126 ? 0.1508 0.1307 0.1797 0.0033  0.0033  -0.0133 1124 ASN B N   
17572 C CA  . ASN B 1126 ? 0.1558 0.1371 0.1874 -0.0011 0.0026  -0.0139 1124 ASN B CA  
17573 C C   . ASN B 1126 ? 0.1600 0.1328 0.1885 -0.0038 0.0016  -0.0139 1124 ASN B C   
17574 O O   . ASN B 1126 ? 0.1804 0.1459 0.2046 -0.0026 0.0018  -0.0128 1124 ASN B O   
17575 C CB  . ASN B 1126 ? 0.1334 0.1213 0.1689 -0.0034 0.0039  -0.0122 1124 ASN B CB  
17576 C CG  . ASN B 1126 ? 0.1485 0.1444 0.1868 -0.0011 0.0047  -0.0124 1124 ASN B CG  
17577 O OD1 . ASN B 1126 ? 0.1684 0.1687 0.2093 -0.0010 0.0040  -0.0141 1124 ASN B OD1 
17578 N ND2 . ASN B 1126 ? 0.1353 0.1328 0.1730 0.0006  0.0060  -0.0106 1124 ASN B ND2 
17579 N N   . SER B 1127 ? 0.1687 0.1425 0.1995 -0.0076 0.0004  -0.0151 1125 SER B N   
17580 C CA  . SER B 1127 ? 0.1479 0.1154 0.1772 -0.0117 -0.0005 -0.0146 1125 SER B CA  
17581 C C   . SER B 1127 ? 0.1719 0.1445 0.2050 -0.0154 0.0009  -0.0125 1125 SER B C   
17582 O O   . SER B 1127 ? 0.1494 0.1302 0.1862 -0.0145 0.0023  -0.0118 1125 SER B O   
17583 C CB  . SER B 1127 ? 0.1920 0.1581 0.2218 -0.0142 -0.0027 -0.0170 1125 SER B CB  
17584 O OG  . SER B 1127 ? 0.2469 0.2226 0.2825 -0.0154 -0.0029 -0.0179 1125 SER B OG  
17585 N N   . VAL B 1128 ? 0.1872 0.1547 0.2192 -0.0195 0.0005  -0.0114 1126 VAL B N   
17586 C CA  . VAL B 1128 ? 0.1548 0.1269 0.1900 -0.0232 0.0021  -0.0092 1126 VAL B CA  
17587 C C   . VAL B 1128 ? 0.1622 0.1339 0.1997 -0.0290 0.0010  -0.0095 1126 VAL B C   
17588 O O   . VAL B 1128 ? 0.2051 0.1693 0.2396 -0.0305 -0.0011 -0.0107 1126 VAL B O   
17589 C CB  . VAL B 1128 ? 0.1773 0.1438 0.2082 -0.0227 0.0036  -0.0063 1126 VAL B CB  
17590 C CG1 . VAL B 1128 ? 0.1843 0.1528 0.2138 -0.0173 0.0047  -0.0058 1126 VAL B CG1 
17591 C CG2 . VAL B 1128 ? 0.1791 0.1331 0.2040 -0.0238 0.0022  -0.0059 1126 VAL B CG2 
17592 N N   . ALA B 1129 ? 0.1511 0.1310 0.1939 -0.0323 0.0024  -0.0083 1127 ALA B N   
17593 C CA  . ALA B 1129 ? 0.1780 0.1584 0.2234 -0.0384 0.0020  -0.0076 1127 ALA B CA  
17594 C C   . ALA B 1129 ? 0.1733 0.1543 0.2183 -0.0406 0.0046  -0.0044 1127 ALA B C   
17595 O O   . ALA B 1129 ? 0.1745 0.1635 0.2225 -0.0391 0.0067  -0.0035 1127 ALA B O   
17596 C CB  . ALA B 1129 ? 0.1888 0.1799 0.2416 -0.0403 0.0014  -0.0092 1127 ALA B CB  
17597 N N   . ILE B 1130 ? 0.1658 0.1377 0.2064 -0.0439 0.0043  -0.0027 1128 ILE B N   
17598 C CA  . ILE B 1130 ? 0.1739 0.1445 0.2127 -0.0460 0.0066  0.0007  1128 ILE B CA  
17599 C C   . ILE B 1130 ? 0.1718 0.1477 0.2154 -0.0526 0.0074  0.0018  1128 ILE B C   
17600 O O   . ILE B 1130 ? 0.1801 0.1530 0.2245 -0.0569 0.0054  0.0009  1128 ILE B O   
17601 C CB  . ILE B 1130 ? 0.1806 0.1373 0.2112 -0.0455 0.0059  0.0023  1128 ILE B CB  
17602 C CG1 . ILE B 1130 ? 0.2308 0.1824 0.2570 -0.0389 0.0048  0.0008  1128 ILE B CG1 
17603 C CG2 . ILE B 1130 ? 0.2183 0.1739 0.2464 -0.0468 0.0083  0.0059  1128 ILE B CG2 
17604 C CD1 . ILE B 1130 ? 0.2303 0.1678 0.2485 -0.0380 0.0036  0.0018  1128 ILE B CD1 
17605 N N   . ASP B 1131 ? 0.1723 0.1562 0.2189 -0.0536 0.0102  0.0037  1129 ASP B N   
17606 C CA  . ASP B 1131 ? 0.1747 0.1648 0.2261 -0.0598 0.0117  0.0052  1129 ASP B CA  
17607 C C   . ASP B 1131 ? 0.2001 0.1799 0.2470 -0.0652 0.0110  0.0073  1129 ASP B C   
17608 O O   . ASP B 1131 ? 0.2018 0.1738 0.2425 -0.0650 0.0121  0.0099  1129 ASP B O   
17609 C CB  . ASP B 1131 ? 0.1655 0.1638 0.2189 -0.0592 0.0152  0.0072  1129 ASP B CB  
17610 C CG  . ASP B 1131 ? 0.1699 0.1760 0.2286 -0.0653 0.0172  0.0087  1129 ASP B CG  
17611 O OD1 . ASP B 1131 ? 0.2065 0.2166 0.2704 -0.0689 0.0158  0.0073  1129 ASP B OD1 
17612 O OD2 . ASP B 1131 ? 0.2116 0.2200 0.2691 -0.0663 0.0202  0.0113  1129 ASP B OD2 
17613 N N   . ALA B 1132 ? 0.2112 0.1909 0.2611 -0.0703 0.0091  0.0063  1130 ALA B N   
17614 C CA  . ALA B 1132 ? 0.2091 0.1785 0.2547 -0.0760 0.0081  0.0081  1130 ALA B CA  
17615 C C   . ALA B 1132 ? 0.2214 0.1935 0.2675 -0.0808 0.0112  0.0119  1130 ALA B C   
17616 O O   . ALA B 1132 ? 0.2505 0.2120 0.2906 -0.0842 0.0111  0.0143  1130 ALA B O   
17617 C CB  . ALA B 1132 ? 0.2160 0.1857 0.2651 -0.0805 0.0052  0.0060  1130 ALA B CB  
17618 N N   . ALA B 1133 ? 0.2327 0.2185 0.2855 -0.0811 0.0140  0.0123  1131 ALA B N   
17619 C CA  . ALA B 1133 ? 0.2452 0.2345 0.2985 -0.0856 0.0174  0.0159  1131 ALA B CA  
17620 C C   . ALA B 1133 ? 0.2509 0.2320 0.2960 -0.0828 0.0191  0.0186  1131 ALA B C   
17621 O O   . ALA B 1133 ? 0.3126 0.2931 0.3558 -0.0867 0.0215  0.0219  1131 ALA B O   
17622 C CB  . ALA B 1133 ? 0.2916 0.2976 0.3537 -0.0856 0.0201  0.0154  1131 ALA B CB  
17623 N N   . SER B 1134 ? 0.2241 0.1990 0.2643 -0.0761 0.0178  0.0174  1132 SER B N   
17624 C CA  . SER B 1134 ? 0.2550 0.2217 0.2874 -0.0733 0.0189  0.0200  1132 SER B CA  
17625 C C   . SER B 1134 ? 0.2621 0.2145 0.2872 -0.0772 0.0177  0.0225  1132 SER B C   
17626 O O   . SER B 1134 ? 0.2908 0.2370 0.3097 -0.0769 0.0191  0.0256  1132 SER B O   
17627 C CB  . SER B 1134 ? 0.2325 0.1962 0.2619 -0.0654 0.0174  0.0180  1132 SER B CB  
17628 O OG  . SER B 1134 ? 0.2573 0.2115 0.2838 -0.0643 0.0141  0.0160  1132 SER B OG  
17629 N N   . GLY B 1135 ? 0.2429 0.1894 0.2681 -0.0808 0.0151  0.0212  1133 GLY B N   
17630 C CA  . GLY B 1135 ? 0.2826 0.2144 0.3003 -0.0846 0.0136  0.0233  1133 GLY B CA  
17631 C C   . GLY B 1135 ? 0.3188 0.2369 0.3275 -0.0789 0.0119  0.0234  1133 GLY B C   
17632 O O   . GLY B 1135 ? 0.3567 0.2621 0.3579 -0.0811 0.0113  0.0260  1133 GLY B O   
17633 N N   . LEU B 1136 ? 0.2863 0.2066 0.2954 -0.0717 0.0111  0.0208  1134 LEU B N   
17634 C CA  . LEU B 1136 ? 0.3316 0.2410 0.3330 -0.0655 0.0098  0.0210  1134 LEU B CA  
17635 C C   . LEU B 1136 ? 0.3365 0.2361 0.3347 -0.0634 0.0065  0.0181  1134 LEU B C   
17636 O O   . LEU B 1136 ? 0.3379 0.2312 0.3314 -0.0571 0.0054  0.0173  1134 LEU B O   
17637 C CB  . LEU B 1136 ? 0.2837 0.2016 0.2872 -0.0587 0.0112  0.0203  1134 LEU B CB  
17638 C CG  . LEU B 1136 ? 0.2952 0.2205 0.2997 -0.0594 0.0144  0.0232  1134 LEU B CG  
17639 C CD1 . LEU B 1136 ? 0.3035 0.2375 0.3106 -0.0529 0.0153  0.0218  1134 LEU B CD1 
17640 C CD2 . LEU B 1136 ? 0.3199 0.2341 0.3161 -0.0604 0.0149  0.0272  1134 LEU B CD2 
17641 N N   . GLN B 1137 ? 0.2895 0.1877 0.2898 -0.0686 0.0047  0.0166  1135 GLN B N   
17642 C CA  . GLN B 1137 ? 0.3448 0.2346 0.3422 -0.0667 0.0015  0.0134  1135 GLN B CA  
17643 C C   . GLN B 1137 ? 0.3857 0.2585 0.3729 -0.0638 0.0000  0.0143  1135 GLN B C   
17644 O O   . GLN B 1137 ? 0.3820 0.2492 0.3659 -0.0583 -0.0018 0.0118  1135 GLN B O   
17645 C CB  . GLN B 1137 ? 0.3478 0.2381 0.3486 -0.0738 -0.0002 0.0121  1135 GLN B CB  
17646 C CG  . GLN B 1137 ? 0.3411 0.2477 0.3521 -0.0751 0.0003  0.0100  1135 GLN B CG  
17647 C CD  . GLN B 1137 ? 0.3284 0.2465 0.3456 -0.0800 0.0033  0.0126  1135 GLN B CD  
17648 O OE1 . GLN B 1137 ? 0.3201 0.2357 0.3342 -0.0813 0.0055  0.0160  1135 GLN B OE1 
17649 N NE2 . GLN B 1137 ? 0.3419 0.2729 0.3679 -0.0825 0.0034  0.0109  1135 GLN B NE2 
17650 N N   . ALA B 1138 ? 0.3597 0.2244 0.3417 -0.0672 0.0007  0.0180  1136 ALA B N   
17651 C CA  . ALA B 1138 ? 0.4031 0.2510 0.3751 -0.0643 -0.0008 0.0191  1136 ALA B CA  
17652 C C   . ALA B 1138 ? 0.4125 0.2602 0.3817 -0.0554 -0.0002 0.0191  1136 ALA B C   
17653 O O   . ALA B 1138 ? 0.4269 0.2617 0.3884 -0.0512 -0.0018 0.0191  1136 ALA B O   
17654 C CB  . ALA B 1138 ? 0.4191 0.2588 0.3861 -0.0701 0.0000  0.0234  1136 ALA B CB  
17655 N N   . SER B 1139 ? 0.3498 0.2113 0.3250 -0.0524 0.0019  0.0190  1137 SER B N   
17656 C CA  . SER B 1139 ? 0.3838 0.2462 0.3570 -0.0445 0.0024  0.0191  1137 SER B CA  
17657 C C   . SER B 1139 ? 0.3696 0.2312 0.3429 -0.0384 0.0007  0.0153  1137 SER B C   
17658 O O   . SER B 1139 ? 0.4125 0.2724 0.3831 -0.0316 0.0007  0.0153  1137 SER B O   
17659 C CB  . SER B 1139 ? 0.3633 0.2406 0.3427 -0.0436 0.0051  0.0202  1137 SER B CB  
17660 O OG  . SER B 1139 ? 0.3890 0.2661 0.3668 -0.0479 0.0070  0.0241  1137 SER B OG  
17661 N N   . LEU B 1140 ? 0.3975 0.2606 0.3738 -0.0406 -0.0007 0.0121  1138 LEU B N   
17662 C CA  . LEU B 1140 ? 0.3817 0.2440 0.3578 -0.0353 -0.0022 0.0084  1138 LEU B CA  
17663 C C   . LEU B 1140 ? 0.4554 0.3030 0.4248 -0.0362 -0.0049 0.0068  1138 LEU B C   
17664 O O   . LEU B 1140 ? 0.5009 0.3484 0.4712 -0.0356 -0.0064 0.0033  1138 LEU B O   
17665 C CB  . LEU B 1140 ? 0.3996 0.2757 0.3841 -0.0361 -0.0019 0.0056  1138 LEU B CB  
17666 C CG  . LEU B 1140 ? 0.3788 0.2694 0.3698 -0.0343 0.0006  0.0065  1138 LEU B CG  
17667 C CD1 . LEU B 1140 ? 0.3640 0.2661 0.3621 -0.0340 0.0004  0.0034  1138 LEU B CD1 
17668 C CD2 . LEU B 1140 ? 0.3747 0.2645 0.3627 -0.0274 0.0014  0.0076  1138 LEU B CD2 
17669 N N   . LYS B 1141 ? 0.4915 0.3259 0.4536 -0.0376 -0.0055 0.0093  1139 LYS B N   
17670 C CA  . LYS B 1141 ? 0.5074 0.3262 0.4620 -0.0382 -0.0081 0.0078  1139 LYS B CA  
17671 C C   . LYS B 1141 ? 0.5636 0.3768 0.5138 -0.0295 -0.0090 0.0055  1139 LYS B C   
17672 O O   . LYS B 1141 ? 0.5453 0.3598 0.4943 -0.0235 -0.0078 0.0068  1139 LYS B O   
17673 C CB  . LYS B 1141 ? 0.5525 0.3583 0.5002 -0.0420 -0.0085 0.0114  1139 LYS B CB  
17674 N N   . ASN B 1142 ? 0.5377 0.3453 0.4857 -0.0290 -0.0110 0.0019  1140 ASN B N   
17675 C CA  . ASN B 1142 ? 0.5754 0.3761 0.5182 -0.0212 -0.0119 -0.0007 1140 ASN B CA  
17676 C C   . ASN B 1142 ? 0.5436 0.3577 0.4920 -0.0148 -0.0101 -0.0019 1140 ASN B C   
17677 O O   . ASN B 1142 ? 0.5124 0.3238 0.4576 -0.0075 -0.0098 -0.0021 1140 ASN B O   
17678 C CB  . ASN B 1142 ? 0.6221 0.4078 0.5558 -0.0176 -0.0125 0.0013  1140 ASN B CB  
17679 C CG  . ASN B 1142 ? 0.7176 0.4890 0.6451 -0.0242 -0.0143 0.0027  1140 ASN B CG  
17680 O OD1 . ASN B 1142 ? 0.7192 0.4852 0.6436 -0.0264 -0.0138 0.0065  1140 ASN B OD1 
17681 N ND2 . ASN B 1142 ? 0.6897 0.4546 0.6149 -0.0277 -0.0165 -0.0002 1140 ASN B ND2 
17682 N N   . LEU B 1143 ? 0.5012 0.3299 0.4581 -0.0175 -0.0091 -0.0025 1141 LEU B N   
17683 C CA  . LEU B 1143 ? 0.4465 0.2874 0.4086 -0.0121 -0.0077 -0.0040 1141 LEU B CA  
17684 C C   . LEU B 1143 ? 0.4330 0.2693 0.3916 -0.0069 -0.0088 -0.0076 1141 LEU B C   
17685 O O   . LEU B 1143 ? 0.5255 0.3536 0.4804 -0.0093 -0.0108 -0.0099 1141 LEU B O   
17686 C CB  . LEU B 1143 ? 0.4467 0.3022 0.4176 -0.0163 -0.0069 -0.0046 1141 LEU B CB  
17687 C CG  . LEU B 1143 ? 0.4670 0.3354 0.4444 -0.0169 -0.0045 -0.0021 1141 LEU B CG  
17688 C CD1 . LEU B 1143 ? 0.3746 0.2560 0.3598 -0.0192 -0.0042 -0.0040 1141 LEU B CD1 
17689 C CD2 . LEU B 1143 ? 0.4039 0.2752 0.3807 -0.0100 -0.0032 -0.0010 1141 LEU B CD2 
17690 N N   . PRO B 1144 ? 0.4549 0.2966 0.4145 0.0001  -0.0077 -0.0084 1142 PRO B N   
17691 C CA  . PRO B 1144 ? 0.4244 0.2648 0.3822 0.0046  -0.0083 -0.0120 1142 PRO B CA  
17692 C C   . PRO B 1144 ? 0.4379 0.2857 0.4004 0.0005  -0.0090 -0.0145 1142 PRO B C   
17693 O O   . PRO B 1144 ? 0.3693 0.2284 0.3388 -0.0031 -0.0081 -0.0135 1142 PRO B O   
17694 C CB  . PRO B 1144 ? 0.4288 0.2776 0.3891 0.0116  -0.0064 -0.0116 1142 PRO B CB  
17695 C CG  . PRO B 1144 ? 0.4493 0.2986 0.4099 0.0118  -0.0054 -0.0078 1142 PRO B CG  
17696 C CD  . PRO B 1144 ? 0.4454 0.2947 0.4079 0.0040  -0.0057 -0.0058 1142 PRO B CD  
17697 N N   . GLN B 1145 ? 0.4330 0.2739 0.3912 0.0013  -0.0106 -0.0178 1143 GLN B N   
17698 C CA  . GLN B 1145 ? 0.4010 0.2478 0.3628 -0.0022 -0.0116 -0.0203 1143 GLN B CA  
17699 C C   . GLN B 1145 ? 0.3836 0.2458 0.3527 0.0001  -0.0099 -0.0206 1143 GLN B C   
17700 O O   . GLN B 1145 ? 0.3716 0.2427 0.3466 -0.0040 -0.0102 -0.0210 1143 GLN B O   
17701 C CB  . GLN B 1145 ? 0.4144 0.2514 0.3695 -0.0003 -0.0135 -0.0240 1143 GLN B CB  
17702 N N   . THR B 1146 ? 0.4031 0.2686 0.3721 0.0066  -0.0082 -0.0203 1144 THR B N   
17703 C CA  . THR B 1146 ? 0.3761 0.2556 0.3517 0.0086  -0.0066 -0.0204 1144 THR B CA  
17704 C C   . THR B 1146 ? 0.3662 0.2555 0.3487 0.0044  -0.0057 -0.0178 1144 THR B C   
17705 O O   . THR B 1146 ? 0.3720 0.2718 0.3604 0.0027  -0.0054 -0.0185 1144 THR B O   
17706 C CB  . THR B 1146 ? 0.3839 0.2653 0.3584 0.0159  -0.0049 -0.0200 1144 THR B CB  
17707 O OG1 . THR B 1146 ? 0.4229 0.2999 0.3954 0.0172  -0.0043 -0.0172 1144 THR B OG1 
17708 C CG2 . THR B 1146 ? 0.4546 0.3286 0.4230 0.0205  -0.0054 -0.0230 1144 THR B CG2 
17709 N N   . VAL B 1147 ? 0.3147 0.2006 0.2963 0.0029  -0.0052 -0.0149 1145 VAL B N   
17710 C CA  . VAL B 1147 ? 0.2470 0.1418 0.2346 -0.0011 -0.0041 -0.0125 1145 VAL B CA  
17711 C C   . VAL B 1147 ? 0.3017 0.1968 0.2916 -0.0081 -0.0053 -0.0129 1145 VAL B C   
17712 O O   . VAL B 1147 ? 0.2729 0.1785 0.2693 -0.0111 -0.0047 -0.0126 1145 VAL B O   
17713 C CB  . VAL B 1147 ? 0.2712 0.1624 0.2566 -0.0003 -0.0031 -0.0091 1145 VAL B CB  
17714 C CG1 . VAL B 1147 ? 0.2996 0.2013 0.2911 -0.0036 -0.0016 -0.0067 1145 VAL B CG1 
17715 C CG2 . VAL B 1147 ? 0.3166 0.2065 0.2992 0.0070  -0.0023 -0.0088 1145 VAL B CG2 
17716 N N   . GLY B 1148 ? 0.3244 0.2082 0.3092 -0.0109 -0.0072 -0.0137 1146 GLY B N   
17717 C CA  . GLY B 1148 ? 0.3244 0.2085 0.3115 -0.0179 -0.0086 -0.0140 1146 GLY B CA  
17718 C C   . GLY B 1148 ? 0.3355 0.2289 0.3280 -0.0192 -0.0093 -0.0166 1146 GLY B C   
17719 O O   . GLY B 1148 ? 0.3166 0.2173 0.3148 -0.0242 -0.0095 -0.0161 1146 GLY B O   
17720 N N   . LEU B 1149 ? 0.3142 0.2076 0.3048 -0.0144 -0.0098 -0.0191 1147 LEU B N   
17721 C CA  . LEU B 1149 ? 0.3158 0.2173 0.3106 -0.0152 -0.0106 -0.0215 1147 LEU B CA  
17722 C C   . LEU B 1149 ? 0.3036 0.2192 0.3064 -0.0156 -0.0090 -0.0203 1147 LEU B C   
17723 O O   . LEU B 1149 ? 0.3320 0.2548 0.3393 -0.0177 -0.0099 -0.0217 1147 LEU B O   
17724 C CB  . LEU B 1149 ? 0.4086 0.3074 0.3993 -0.0097 -0.0110 -0.0242 1147 LEU B CB  
17725 C CG  . LEU B 1149 ? 0.4701 0.3548 0.4525 -0.0089 -0.0128 -0.0261 1147 LEU B CG  
17726 C CD1 . LEU B 1149 ? 0.5099 0.3933 0.4886 -0.0035 -0.0129 -0.0289 1147 LEU B CD1 
17727 C CD2 . LEU B 1149 ? 0.5218 0.4015 0.5034 -0.0155 -0.0155 -0.0270 1147 LEU B CD2 
17728 N N   . ARG B 1150 ? 0.2586 0.1779 0.2629 -0.0135 -0.0067 -0.0178 1148 ARG B N   
17729 C CA  . ARG B 1150 ? 0.2423 0.1741 0.2534 -0.0137 -0.0051 -0.0166 1148 ARG B CA  
17730 C C   . ARG B 1150 ? 0.2489 0.1844 0.2640 -0.0188 -0.0043 -0.0143 1148 ARG B C   
17731 O O   . ARG B 1150 ? 0.2280 0.1736 0.2485 -0.0192 -0.0029 -0.0134 1148 ARG B O   
17732 C CB  . ARG B 1150 ? 0.2401 0.1749 0.2509 -0.0083 -0.0031 -0.0154 1148 ARG B CB  
17733 C CG  . ARG B 1150 ? 0.2822 0.2185 0.2917 -0.0033 -0.0032 -0.0175 1148 ARG B CG  
17734 C CD  . ARG B 1150 ? 0.2365 0.1819 0.2496 -0.0002 -0.0013 -0.0164 1148 ARG B CD  
17735 N NE  . ARG B 1150 ? 0.2656 0.2115 0.2767 0.0050  -0.0010 -0.0177 1148 ARG B NE  
17736 C CZ  . ARG B 1150 ? 0.2601 0.2110 0.2725 0.0086  0.0005  -0.0165 1148 ARG B CZ  
17737 N NH1 . ARG B 1150 ? 0.2318 0.1872 0.2469 0.0078  0.0017  -0.0142 1148 ARG B NH1 
17738 N NH2 . ARG B 1150 ? 0.2106 0.1619 0.2212 0.0131  0.0009  -0.0177 1148 ARG B NH2 
17739 N N   . VAL B 1151 ? 0.2421 0.1694 0.2541 -0.0228 -0.0052 -0.0134 1149 VAL B N   
17740 C CA  . VAL B 1151 ? 0.2282 0.1580 0.2431 -0.0278 -0.0041 -0.0108 1149 VAL B CA  
17741 C C   . VAL B 1151 ? 0.2556 0.1865 0.2735 -0.0340 -0.0059 -0.0118 1149 VAL B C   
17742 O O   . VAL B 1151 ? 0.2906 0.2131 0.3046 -0.0356 -0.0082 -0.0134 1149 VAL B O   
17743 C CB  . VAL B 1151 ? 0.2682 0.1876 0.2771 -0.0280 -0.0036 -0.0083 1149 VAL B CB  
17744 C CG1 . VAL B 1151 ? 0.2854 0.2066 0.2967 -0.0341 -0.0027 -0.0056 1149 VAL B CG1 
17745 C CG2 . VAL B 1151 ? 0.2959 0.2156 0.3026 -0.0222 -0.0020 -0.0069 1149 VAL B CG2 
17746 N N   . SER B 1152 ? 0.2173 0.1588 0.2421 -0.0374 -0.0048 -0.0108 1150 SER B N   
17747 C CA  . SER B 1152 ? 0.2148 0.1583 0.2432 -0.0440 -0.0060 -0.0109 1150 SER B CA  
17748 C C   . SER B 1152 ? 0.2180 0.1667 0.2499 -0.0477 -0.0036 -0.0078 1150 SER B C   
17749 O O   . SER B 1152 ? 0.2375 0.1908 0.2702 -0.0450 -0.0012 -0.0061 1150 SER B O   
17750 C CB  . SER B 1152 ? 0.2549 0.2079 0.2894 -0.0444 -0.0074 -0.0134 1150 SER B CB  
17751 O OG  . SER B 1152 ? 0.3262 0.2911 0.3665 -0.0423 -0.0053 -0.0129 1150 SER B OG  
17752 N N   . TRP B 1153 ? 0.2418 0.1895 0.2753 -0.0542 -0.0044 -0.0070 1151 TRP B N   
17753 C CA  . TRP B 1153 ? 0.2391 0.1925 0.2763 -0.0587 -0.0021 -0.0041 1151 TRP B CA  
17754 C C   . TRP B 1153 ? 0.2468 0.2127 0.2930 -0.0625 -0.0023 -0.0051 1151 TRP B C   
17755 O O   . TRP B 1153 ? 0.2800 0.2454 0.3277 -0.0649 -0.0051 -0.0072 1151 TRP B O   
17756 C CB  . TRP B 1153 ? 0.2473 0.1896 0.2794 -0.0637 -0.0025 -0.0019 1151 TRP B CB  
17757 C CG  . TRP B 1153 ? 0.2647 0.1954 0.2884 -0.0599 -0.0020 -0.0004 1151 TRP B CG  
17758 C CD1 . TRP B 1153 ? 0.3052 0.2242 0.3219 -0.0562 -0.0040 -0.0020 1151 TRP B CD1 
17759 C CD2 . TRP B 1153 ? 0.2613 0.1911 0.2827 -0.0591 0.0006  0.0029  1151 TRP B CD2 
17760 N NE1 . TRP B 1153 ? 0.2858 0.1971 0.2963 -0.0530 -0.0028 0.0002  1151 TRP B NE1 
17761 C CE2 . TRP B 1153 ? 0.3111 0.2286 0.3242 -0.0548 -0.0001 0.0032  1151 TRP B CE2 
17762 C CE3 . TRP B 1153 ? 0.2350 0.1732 0.2602 -0.0615 0.0035  0.0056  1151 TRP B CE3 
17763 C CZ2 . TRP B 1153 ? 0.2983 0.2117 0.3071 -0.0529 0.0017  0.0063  1151 TRP B CZ2 
17764 C CZ3 . TRP B 1153 ? 0.2790 0.2129 0.2994 -0.0598 0.0055  0.0085  1151 TRP B CZ3 
17765 C CH2 . TRP B 1153 ? 0.3023 0.2240 0.3147 -0.0555 0.0044  0.0089  1151 TRP B CH2 
17766 N N   . SER B 1154 ? 0.1878 0.1650 0.2396 -0.0626 0.0004  -0.0037 1152 SER B N   
17767 C CA  . SER B 1154 ? 0.1893 0.1795 0.2500 -0.0651 0.0004  -0.0047 1152 SER B CA  
17768 C C   . SER B 1154 ? 0.1966 0.1925 0.2615 -0.0712 0.0026  -0.0021 1152 SER B C   
17769 O O   . SER B 1154 ? 0.1864 0.1838 0.2503 -0.0707 0.0057  0.0004  1152 SER B O   
17770 C CB  . SER B 1154 ? 0.1976 0.1978 0.2622 -0.0597 0.0018  -0.0059 1152 SER B CB  
17771 O OG  . SER B 1154 ? 0.1938 0.2064 0.2670 -0.0620 0.0017  -0.0068 1152 SER B OG  
17772 N N   . LYS B 1155 ? 0.1943 0.1938 0.2640 -0.0768 0.0009  -0.0026 1153 LYS B N   
17773 C CA  . LYS B 1155 ? 0.1840 0.1920 0.2597 -0.0829 0.0029  -0.0005 1153 LYS B CA  
17774 C C   . LYS B 1155 ? 0.2033 0.2275 0.2888 -0.0820 0.0037  -0.0018 1153 LYS B C   
17775 O O   . LYS B 1155 ? 0.2102 0.2436 0.3021 -0.0869 0.0052  -0.0005 1153 LYS B O   
17776 C CB  . LYS B 1155 ? 0.2392 0.2417 0.3147 -0.0902 0.0004  -0.0002 1153 LYS B CB  
17777 C CG  . LYS B 1155 ? 0.2952 0.2811 0.3609 -0.0919 -0.0004 0.0014  1153 LYS B CG  
17778 C CD  . LYS B 1155 ? 0.3544 0.3346 0.4198 -0.0994 -0.0032 0.0014  1153 LYS B CD  
17779 C CE  . LYS B 1155 ? 0.4783 0.4406 0.5332 -0.1007 -0.0043 0.0028  1153 LYS B CE  
17780 N NZ  . LYS B 1155 ? 0.4972 0.4516 0.5504 -0.1070 -0.0079 0.0019  1153 LYS B NZ  
17781 N N   . ASP B 1156 ? 0.1702 0.1980 0.2568 -0.0760 0.0028  -0.0043 1154 ASP B N   
17782 C CA  . ASP B 1156 ? 0.1632 0.2051 0.2586 -0.0748 0.0029  -0.0060 1154 ASP B CA  
17783 C C   . ASP B 1156 ? 0.1430 0.1858 0.2366 -0.0671 0.0030  -0.0078 1154 ASP B C   
17784 O O   . ASP B 1156 ? 0.1516 0.1908 0.2434 -0.0643 0.0000  -0.0102 1154 ASP B O   
17785 C CB  . ASP B 1156 ? 0.1782 0.2226 0.2780 -0.0784 -0.0008 -0.0079 1154 ASP B CB  
17786 C CG  . ASP B 1156 ? 0.1451 0.2049 0.2548 -0.0779 -0.0008 -0.0092 1154 ASP B CG  
17787 O OD1 . ASP B 1156 ? 0.1505 0.2168 0.2620 -0.0726 0.0012  -0.0097 1154 ASP B OD1 
17788 O OD2 . ASP B 1156 ? 0.1791 0.2441 0.2944 -0.0827 -0.0028 -0.0097 1154 ASP B OD2 
17789 N N   . TRP B 1157 ? 0.1364 0.1837 0.2302 -0.0640 0.0063  -0.0065 1155 TRP B N   
17790 C CA  . TRP B 1157 ? 0.1300 0.1763 0.2209 -0.0572 0.0065  -0.0078 1155 TRP B CA  
17791 C C   . TRP B 1157 ? 0.1509 0.2050 0.2470 -0.0543 0.0046  -0.0106 1155 TRP B C   
17792 O O   . TRP B 1157 ? 0.1531 0.2032 0.2461 -0.0500 0.0027  -0.0124 1155 TRP B O   
17793 C CB  . TRP B 1157 ? 0.1369 0.1871 0.2271 -0.0547 0.0103  -0.0061 1155 TRP B CB  
17794 C CG  . TRP B 1157 ? 0.1368 0.1796 0.2214 -0.0567 0.0123  -0.0032 1155 TRP B CG  
17795 C CD1 . TRP B 1157 ? 0.1674 0.1994 0.2468 -0.0599 0.0111  -0.0019 1155 TRP B CD1 
17796 C CD2 . TRP B 1157 ? 0.1476 0.1931 0.2309 -0.0556 0.0159  -0.0011 1155 TRP B CD2 
17797 N NE1 . TRP B 1157 ? 0.1552 0.1829 0.2301 -0.0608 0.0137  0.0010  1155 TRP B NE1 
17798 C CE2 . TRP B 1157 ? 0.1517 0.1878 0.2289 -0.0582 0.0166  0.0016  1155 TRP B CE2 
17799 C CE3 . TRP B 1157 ? 0.1627 0.2173 0.2490 -0.0525 0.0184  -0.0012 1155 TRP B CE3 
17800 C CZ2 . TRP B 1157 ? 0.1648 0.2007 0.2389 -0.0580 0.0197  0.0041  1155 TRP B CZ2 
17801 C CZ3 . TRP B 1157 ? 0.1504 0.2047 0.2334 -0.0523 0.0215  0.0012  1155 TRP B CZ3 
17802 C CH2 . TRP B 1157 ? 0.1962 0.2413 0.2731 -0.0550 0.0221  0.0039  1155 TRP B CH2 
17803 N N   . ALA B 1158 ? 0.1542 0.2197 0.2584 -0.0567 0.0049  -0.0109 1156 ALA B N   
17804 C CA  . ALA B 1158 ? 0.1471 0.2203 0.2563 -0.0535 0.0032  -0.0134 1156 ALA B CA  
17805 C C   . ALA B 1158 ? 0.1538 0.2225 0.2623 -0.0544 -0.0012 -0.0154 1156 ALA B C   
17806 O O   . ALA B 1158 ? 0.2051 0.2752 0.3138 -0.0504 -0.0031 -0.0176 1156 ALA B O   
17807 C CB  . ALA B 1158 ? 0.1103 0.1973 0.2286 -0.0553 0.0048  -0.0131 1156 ALA B CB  
17808 N N   . ALA B 1159 ? 0.1298 0.1926 0.2367 -0.0596 -0.0028 -0.0149 1157 ALA B N   
17809 C CA  . ALA B 1159 ? 0.1551 0.2128 0.2604 -0.0607 -0.0070 -0.0169 1157 ALA B CA  
17810 C C   . ALA B 1159 ? 0.1935 0.2388 0.2898 -0.0569 -0.0083 -0.0179 1157 ALA B C   
17811 O O   . ALA B 1159 ? 0.2005 0.2429 0.2951 -0.0552 -0.0114 -0.0201 1157 ALA B O   
17812 C CB  . ALA B 1159 ? 0.1772 0.2325 0.2837 -0.0679 -0.0085 -0.0161 1157 ALA B CB  
17813 N N   . ASP B 1160 ? 0.1859 0.2241 0.2764 -0.0555 -0.0058 -0.0162 1158 ASP B N   
17814 C CA  . ASP B 1160 ? 0.1939 0.2202 0.2759 -0.0523 -0.0067 -0.0167 1158 ASP B CA  
17815 C C   . ASP B 1160 ? 0.1826 0.2101 0.2626 -0.0457 -0.0057 -0.0175 1158 ASP B C   
17816 O O   . ASP B 1160 ? 0.2366 0.2555 0.3102 -0.0425 -0.0064 -0.0182 1158 ASP B O   
17817 C CB  . ASP B 1160 ? 0.1922 0.2097 0.2688 -0.0544 -0.0050 -0.0143 1158 ASP B CB  
17818 C CG  . ASP B 1160 ? 0.2196 0.2326 0.2961 -0.0610 -0.0066 -0.0138 1158 ASP B CG  
17819 O OD1 . ASP B 1160 ? 0.2997 0.3142 0.3788 -0.0633 -0.0096 -0.0156 1158 ASP B OD1 
17820 O OD2 . ASP B 1160 ? 0.2487 0.2563 0.3223 -0.0639 -0.0050 -0.0114 1158 ASP B OD2 
17821 N N   . GLY B 1161 ? 0.1707 0.2085 0.2561 -0.0437 -0.0040 -0.0174 1159 GLY B N   
17822 C CA  . GLY B 1161 ? 0.1648 0.2042 0.2488 -0.0379 -0.0033 -0.0183 1159 GLY B CA  
17823 C C   . GLY B 1161 ? 0.2445 0.2848 0.3290 -0.0357 -0.0063 -0.0208 1159 GLY B C   
17824 O O   . GLY B 1161 ? 0.2646 0.3033 0.3498 -0.0384 -0.0092 -0.0221 1159 GLY B O   
17825 N N   . PRO B 1162 ? 0.2638 0.3067 0.3479 -0.0309 -0.0059 -0.0216 1160 PRO B N   
17826 C CA  . PRO B 1162 ? 0.2120 0.2575 0.2956 -0.0277 -0.0030 -0.0205 1160 PRO B CA  
17827 C C   . PRO B 1162 ? 0.2042 0.2412 0.2811 -0.0261 -0.0017 -0.0193 1160 PRO B C   
17828 O O   . PRO B 1162 ? 0.2494 0.2784 0.3212 -0.0252 -0.0031 -0.0200 1160 PRO B O   
17829 C CB  . PRO B 1162 ? 0.2767 0.3261 0.3613 -0.0236 -0.0041 -0.0222 1160 PRO B CB  
17830 C CG  . PRO B 1162 ? 0.2869 0.3305 0.3683 -0.0234 -0.0072 -0.0239 1160 PRO B CG  
17831 C CD  . PRO B 1162 ? 0.3048 0.3470 0.3879 -0.0284 -0.0087 -0.0239 1160 PRO B CD  
17832 N N   . PHE B 1163 ? 0.1598 0.1986 0.2367 -0.0256 0.0012  -0.0174 1161 PHE B N   
17833 C CA  . PHE B 1163 ? 0.1683 0.2004 0.2393 -0.0235 0.0025  -0.0161 1161 PHE B CA  
17834 C C   . PHE B 1163 ? 0.1792 0.2140 0.2494 -0.0189 0.0033  -0.0166 1161 PHE B C   
17835 O O   . PHE B 1163 ? 0.1831 0.2245 0.2569 -0.0175 0.0030  -0.0177 1161 PHE B O   
17836 C CB  . PHE B 1163 ? 0.1616 0.1932 0.2323 -0.0263 0.0049  -0.0136 1161 PHE B CB  
17837 C CG  . PHE B 1163 ? 0.1450 0.1739 0.2166 -0.0313 0.0041  -0.0130 1161 PHE B CG  
17838 C CD1 . PHE B 1163 ? 0.1894 0.2091 0.2566 -0.0323 0.0021  -0.0135 1161 PHE B CD1 
17839 C CD2 . PHE B 1163 ? 0.1618 0.1976 0.2386 -0.0352 0.0054  -0.0121 1161 PHE B CD2 
17840 C CE1 . PHE B 1163 ? 0.2279 0.2446 0.2956 -0.0373 0.0011  -0.0131 1161 PHE B CE1 
17841 C CE2 . PHE B 1163 ? 0.1824 0.2159 0.2601 -0.0403 0.0046  -0.0114 1161 PHE B CE2 
17842 C CZ  . PHE B 1163 ? 0.1766 0.2003 0.2497 -0.0415 0.0023  -0.0119 1161 PHE B CZ  
17843 N N   . ALA B 1164 ? 0.1710 0.2004 0.2362 -0.0165 0.0041  -0.0157 1162 ALA B N   
17844 C CA  . ALA B 1164 ? 0.1897 0.2209 0.2537 -0.0125 0.0046  -0.0160 1162 ALA B CA  
17845 C C   . ALA B 1164 ? 0.1973 0.2299 0.2602 -0.0117 0.0070  -0.0141 1162 ALA B C   
17846 O O   . ALA B 1164 ? 0.2332 0.2671 0.2948 -0.0086 0.0075  -0.0141 1162 ALA B O   
17847 C CB  . ALA B 1164 ? 0.1922 0.2170 0.2515 -0.0098 0.0033  -0.0168 1162 ALA B CB  
17848 N N   . GLY B 1165 ? 0.1531 0.1855 0.2163 -0.0145 0.0085  -0.0123 1163 GLY B N   
17849 C CA  . GLY B 1165 ? 0.1539 0.1868 0.2154 -0.0140 0.0107  -0.0103 1163 GLY B CA  
17850 C C   . GLY B 1165 ? 0.1422 0.1722 0.2029 -0.0177 0.0117  -0.0084 1163 GLY B C   
17851 O O   . GLY B 1165 ? 0.1503 0.1774 0.2116 -0.0205 0.0106  -0.0086 1163 GLY B O   
17852 N N   . ALA B 1166 ? 0.1647 0.1952 0.2236 -0.0178 0.0138  -0.0063 1164 ALA B N   
17853 C CA  . ALA B 1166 ? 0.1595 0.1872 0.2172 -0.0215 0.0150  -0.0041 1164 ALA B CA  
17854 C C   . ALA B 1166 ? 0.1536 0.1778 0.2065 -0.0202 0.0164  -0.0018 1164 ALA B C   
17855 O O   . ALA B 1166 ? 0.1843 0.2120 0.2366 -0.0175 0.0173  -0.0018 1164 ALA B O   
17856 C CB  . ALA B 1166 ? 0.1500 0.1853 0.2129 -0.0250 0.0166  -0.0039 1164 ALA B CB  
17857 N N   . LEU B 1167 ? 0.1384 0.1554 0.1875 -0.0223 0.0165  0.0002  1165 LEU B N   
17858 C CA  . LEU B 1167 ? 0.1521 0.1653 0.1964 -0.0216 0.0177  0.0028  1165 LEU B CA  
17859 C C   . LEU B 1167 ? 0.1476 0.1600 0.1916 -0.0264 0.0194  0.0051  1165 LEU B C   
17860 O O   . LEU B 1167 ? 0.1837 0.1925 0.2282 -0.0298 0.0186  0.0051  1165 LEU B O   
17861 C CB  . LEU B 1167 ? 0.1717 0.1756 0.2107 -0.0191 0.0160  0.0033  1165 LEU B CB  
17862 C CG  . LEU B 1167 ? 0.1501 0.1542 0.1892 -0.0146 0.0144  0.0012  1165 LEU B CG  
17863 C CD1 . LEU B 1167 ? 0.1912 0.1863 0.2253 -0.0124 0.0131  0.0019  1165 LEU B CD1 
17864 C CD2 . LEU B 1167 ? 0.1586 0.1688 0.1983 -0.0117 0.0153  0.0012  1165 LEU B CD2 
17865 N N   . VAL B 1168 ? 0.1568 0.1726 0.1997 -0.0267 0.0217  0.0069  1166 VAL B N   
17866 C CA  . VAL B 1168 ? 0.1758 0.1928 0.2190 -0.0314 0.0238  0.0091  1166 VAL B CA  
17867 C C   . VAL B 1168 ? 0.1724 0.1841 0.2091 -0.0310 0.0250  0.0122  1166 VAL B C   
17868 O O   . VAL B 1168 ? 0.1873 0.1998 0.2215 -0.0272 0.0251  0.0123  1166 VAL B O   
17869 C CB  . VAL B 1168 ? 0.1777 0.2058 0.2265 -0.0325 0.0260  0.0081  1166 VAL B CB  
17870 C CG1 . VAL B 1168 ? 0.2004 0.2306 0.2498 -0.0375 0.0285  0.0105  1166 VAL B CG1 
17871 C CG2 . VAL B 1168 ? 0.1606 0.1940 0.2157 -0.0322 0.0245  0.0050  1166 VAL B CG2 
17872 N N   . GLU B 1169 ? 0.1782 0.1841 0.2120 -0.0349 0.0255  0.0147  1167 GLU B N   
17873 C CA  . GLU B 1169 ? 0.2047 0.2052 0.2321 -0.0352 0.0267  0.0180  1167 GLU B CA  
17874 C C   . GLU B 1169 ? 0.2148 0.2191 0.2431 -0.0403 0.0296  0.0201  1167 GLU B C   
17875 O O   . GLU B 1169 ? 0.2403 0.2452 0.2718 -0.0447 0.0298  0.0201  1167 GLU B O   
17876 C CB  . GLU B 1169 ? 0.2116 0.1999 0.2335 -0.0351 0.0246  0.0194  1167 GLU B CB  
17877 C CG  . GLU B 1169 ? 0.2233 0.2049 0.2381 -0.0358 0.0255  0.0232  1167 GLU B CG  
17878 C CD  . GLU B 1169 ? 0.2378 0.2068 0.2471 -0.0364 0.0236  0.0247  1167 GLU B CD  
17879 O OE1 . GLU B 1169 ? 0.2316 0.1967 0.2425 -0.0375 0.0218  0.0231  1167 GLU B OE1 
17880 O OE2 . GLU B 1169 ? 0.2650 0.2274 0.2680 -0.0357 0.0237  0.0276  1167 GLU B OE2 
17881 N N   . GLY B 1170 ? 0.2068 0.2138 0.2322 -0.0397 0.0318  0.0219  1168 GLY B N   
17882 C CA  . GLY B 1170 ? 0.2264 0.2361 0.2515 -0.0445 0.0348  0.0244  1168 GLY B CA  
17883 C C   . GLY B 1170 ? 0.2483 0.2639 0.2715 -0.0428 0.0374  0.0252  1168 GLY B C   
17884 O O   . GLY B 1170 ? 0.2312 0.2483 0.2531 -0.0381 0.0366  0.0239  1168 GLY B O   
17885 N N   . ASP B 1171 ? 0.2608 0.2798 0.2837 -0.0471 0.0405  0.0273  1169 ASP B N   
17886 C CA  . ASP B 1171 ? 0.2752 0.3001 0.2961 -0.0459 0.0434  0.0280  1169 ASP B CA  
17887 C C   . ASP B 1171 ? 0.2570 0.2938 0.2853 -0.0447 0.0448  0.0248  1169 ASP B C   
17888 O O   . ASP B 1171 ? 0.2219 0.2621 0.2566 -0.0446 0.0434  0.0222  1169 ASP B O   
17889 C CB  . ASP B 1171 ? 0.2812 0.3045 0.2979 -0.0507 0.0464  0.0318  1169 ASP B CB  
17890 C CG  . ASP B 1171 ? 0.2967 0.3257 0.3194 -0.0565 0.0486  0.0322  1169 ASP B CG  
17891 O OD1 . ASP B 1171 ? 0.2895 0.3245 0.3199 -0.0568 0.0478  0.0294  1169 ASP B OD1 
17892 O OD2 . ASP B 1171 ? 0.3487 0.3762 0.3681 -0.0610 0.0511  0.0355  1169 ASP B OD2 
17893 N N   . ALA B 1172 ? 0.2597 0.3025 0.2866 -0.0436 0.0476  0.0249  1170 ALA B N   
17894 C CA  . ALA B 1172 ? 0.2659 0.3192 0.2986 -0.0414 0.0488  0.0218  1170 ALA B CA  
17895 C C   . ALA B 1172 ? 0.2417 0.3026 0.2826 -0.0450 0.0502  0.0208  1170 ALA B C   
17896 O O   . ALA B 1172 ? 0.2452 0.3117 0.2925 -0.0431 0.0491  0.0176  1170 ALA B O   
17897 C CB  . ALA B 1172 ? 0.2699 0.3276 0.2988 -0.0400 0.0519  0.0224  1170 ALA B CB  
17898 N N   . GLU B 1173 ? 0.2372 0.2986 0.2781 -0.0503 0.0526  0.0235  1171 GLU B N   
17899 C CA  . GLU B 1173 ? 0.2302 0.2996 0.2793 -0.0542 0.0539  0.0227  1171 GLU B CA  
17900 C C   . GLU B 1173 ? 0.2185 0.2844 0.2719 -0.0548 0.0501  0.0211  1171 GLU B C   
17901 O O   . GLU B 1173 ? 0.2272 0.3008 0.2884 -0.0549 0.0497  0.0186  1171 GLU B O   
17902 C CB  . GLU B 1173 ? 0.2970 0.3667 0.3448 -0.0603 0.0570  0.0263  1171 GLU B CB  
17903 N N   . ARG B 1174 ? 0.2157 0.2702 0.2639 -0.0550 0.0473  0.0223  1172 ARG B N   
17904 C CA  . ARG B 1174 ? 0.2037 0.2539 0.2548 -0.0555 0.0438  0.0208  1172 ARG B CA  
17905 C C   . ARG B 1174 ? 0.2028 0.2559 0.2571 -0.0501 0.0414  0.0170  1172 ARG B C   
17906 O O   . ARG B 1174 ? 0.2140 0.2707 0.2745 -0.0505 0.0398  0.0147  1172 ARG B O   
17907 C CB  . ARG B 1174 ? 0.2496 0.2864 0.2936 -0.0564 0.0416  0.0230  1172 ARG B CB  
17908 C CG  . ARG B 1174 ? 0.2480 0.2786 0.2935 -0.0564 0.0378  0.0213  1172 ARG B CG  
17909 C CD  . ARG B 1174 ? 0.3010 0.3363 0.3532 -0.0616 0.0378  0.0207  1172 ARG B CD  
17910 N NE  . ARG B 1174 ? 0.2791 0.3076 0.3318 -0.0618 0.0340  0.0192  1172 ARG B NE  
17911 C CZ  . ARG B 1174 ? 0.2817 0.3138 0.3405 -0.0650 0.0328  0.0176  1172 ARG B CZ  
17912 N NH1 . ARG B 1174 ? 0.2808 0.3241 0.3466 -0.0682 0.0349  0.0174  1172 ARG B NH1 
17913 N NH2 . ARG B 1174 ? 0.2817 0.3065 0.3396 -0.0648 0.0293  0.0161  1172 ARG B NH2 
17914 N N   . ILE B 1175 ? 0.1958 0.2474 0.2460 -0.0452 0.0412  0.0165  1173 ILE B N   
17915 C CA  . ILE B 1175 ? 0.1923 0.2460 0.2448 -0.0403 0.0390  0.0132  1173 ILE B CA  
17916 C C   . ILE B 1175 ? 0.1797 0.2447 0.2397 -0.0398 0.0402  0.0107  1173 ILE B C   
17917 O O   . ILE B 1175 ? 0.1919 0.2592 0.2566 -0.0384 0.0381  0.0081  1173 ILE B O   
17918 C CB  . ILE B 1175 ? 0.2027 0.2534 0.2493 -0.0357 0.0388  0.0134  1173 ILE B CB  
17919 C CG1 . ILE B 1175 ? 0.2177 0.2572 0.2577 -0.0351 0.0367  0.0154  1173 ILE B CG1 
17920 C CG2 . ILE B 1175 ? 0.2268 0.2814 0.2764 -0.0311 0.0371  0.0101  1173 ILE B CG2 
17921 C CD1 . ILE B 1175 ? 0.2385 0.2753 0.2725 -0.0313 0.0365  0.0162  1173 ILE B CD1 
17922 N N   . ARG B 1176 ? 0.1979 0.2702 0.2590 -0.0410 0.0438  0.0115  1174 ARG B N   
17923 C CA  A ARG B 1176 ? 0.2081 0.2916 0.2764 -0.0402 0.0452  0.0092  1174 ARG B CA  
17924 C CA  B ARG B 1176 ? 0.2081 0.2916 0.2763 -0.0403 0.0453  0.0092  1174 ARG B CA  
17925 C C   . ARG B 1176 ? 0.1796 0.2671 0.2552 -0.0439 0.0443  0.0085  1174 ARG B C   
17926 O O   . ARG B 1176 ? 0.1820 0.2749 0.2635 -0.0420 0.0429  0.0057  1174 ARG B O   
17927 C CB  A ARG B 1176 ? 0.2061 0.2963 0.2737 -0.0408 0.0495  0.0103  1174 ARG B CB  
17928 C CB  B ARG B 1176 ? 0.2066 0.2967 0.2741 -0.0411 0.0496  0.0105  1174 ARG B CB  
17929 C CG  A ARG B 1176 ? 0.2178 0.3199 0.2930 -0.0399 0.0513  0.0080  1174 ARG B CG  
17930 C CG  B ARG B 1176 ? 0.2272 0.3285 0.3007 -0.0388 0.0514  0.0079  1174 ARG B CG  
17931 C CD  A ARG B 1176 ? 0.2476 0.3563 0.3215 -0.0401 0.0558  0.0089  1174 ARG B CD  
17932 C CD  B ARG B 1176 ? 0.2470 0.3553 0.3201 -0.0404 0.0562  0.0093  1174 ARG B CD  
17933 N NE  A ARG B 1176 ? 0.2513 0.3718 0.3330 -0.0390 0.0576  0.0066  1174 ARG B NE  
17934 N NE  B ARG B 1176 ? 0.2754 0.3779 0.3397 -0.0396 0.0576  0.0114  1174 ARG B NE  
17935 C CZ  A ARG B 1176 ? 0.2987 0.4271 0.3873 -0.0429 0.0594  0.0072  1174 ARG B CZ  
17936 C CZ  B ARG B 1176 ? 0.2883 0.3914 0.3485 -0.0353 0.0584  0.0102  1174 ARG B CZ  
17937 N NH1 A ARG B 1176 ? 0.3299 0.4556 0.4185 -0.0487 0.0596  0.0100  1174 ARG B NH1 
17938 N NH1 B ARG B 1176 ? 0.2943 0.4028 0.3581 -0.0311 0.0579  0.0068  1174 ARG B NH1 
17939 N NH2 A ARG B 1176 ? 0.2693 0.4088 0.3650 -0.0410 0.0608  0.0049  1174 ARG B NH2 
17940 N NH2 B ARG B 1176 ? 0.3375 0.4351 0.3894 -0.0351 0.0595  0.0123  1174 ARG B NH2 
17941 N N   . ALA B 1177 ? 0.1711 0.2556 0.2463 -0.0493 0.0449  0.0111  1175 ALA B N   
17942 C CA  . ALA B 1177 ? 0.1778 0.2658 0.2598 -0.0534 0.0438  0.0105  1175 ALA B CA  
17943 C C   . ALA B 1177 ? 0.1801 0.2630 0.2632 -0.0516 0.0394  0.0082  1175 ALA B C   
17944 O O   . ALA B 1177 ? 0.1870 0.2760 0.2769 -0.0518 0.0380  0.0061  1175 ALA B O   
17945 C CB  . ALA B 1177 ? 0.1990 0.2828 0.2790 -0.0598 0.0449  0.0139  1175 ALA B CB  
17946 N N   . VAL B 1178 ? 0.1883 0.2603 0.2647 -0.0497 0.0372  0.0088  1176 VAL B N   
17947 C CA  . VAL B 1178 ? 0.1755 0.2423 0.2522 -0.0478 0.0333  0.0067  1176 VAL B CA  
17948 C C   . VAL B 1178 ? 0.1774 0.2497 0.2572 -0.0427 0.0323  0.0035  1176 VAL B C   
17949 O O   . VAL B 1178 ? 0.1699 0.2442 0.2540 -0.0421 0.0298  0.0013  1176 VAL B O   
17950 C CB  . VAL B 1178 ? 0.1945 0.2487 0.2631 -0.0466 0.0316  0.0080  1176 VAL B CB  
17951 C CG1 . VAL B 1178 ? 0.1975 0.2469 0.2660 -0.0437 0.0279  0.0056  1176 VAL B CG1 
17952 C CG2 . VAL B 1178 ? 0.2092 0.2568 0.2748 -0.0520 0.0320  0.0109  1176 VAL B CG2 
17953 N N   . ASN B 1179 ? 0.1620 0.2363 0.2392 -0.0389 0.0340  0.0034  1177 ASN B N   
17954 C CA  . ASN B 1179 ? 0.1779 0.2567 0.2573 -0.0341 0.0330  0.0006  1177 ASN B CA  
17955 C C   . ASN B 1179 ? 0.1727 0.2619 0.2603 -0.0348 0.0334  -0.0013 1177 ASN B C   
17956 O O   . ASN B 1179 ? 0.1714 0.2624 0.2621 -0.0323 0.0311  -0.0038 1177 ASN B O   
17957 C CB  . ASN B 1179 ? 0.1972 0.2766 0.2722 -0.0308 0.0350  0.0010  1177 ASN B CB  
17958 C CG  . ASN B 1179 ? 0.2194 0.2989 0.2939 -0.0256 0.0332  -0.0015 1177 ASN B CG  
17959 O OD1 . ASN B 1179 ? 0.2357 0.3117 0.3107 -0.0242 0.0302  -0.0030 1177 ASN B OD1 
17960 N ND2 . ASN B 1179 ? 0.2123 0.2954 0.2853 -0.0229 0.0350  -0.0020 1177 ASN B ND2 
17961 N N   . LYS B 1180 ? 0.1719 0.2681 0.2630 -0.0381 0.0364  0.0000  1178 LYS B N   
17962 C CA  . LYS B 1180 ? 0.1603 0.2672 0.2599 -0.0389 0.0369  -0.0016 1178 LYS B CA  
17963 C C   . LYS B 1180 ? 0.1555 0.2616 0.2594 -0.0415 0.0336  -0.0025 1178 LYS B C   
17964 O O   . LYS B 1180 ? 0.1762 0.2879 0.2856 -0.0397 0.0319  -0.0049 1178 LYS B O   
17965 C CB  . LYS B 1180 ? 0.1806 0.2954 0.2831 -0.0424 0.0410  0.0002  1178 LYS B CB  
17966 C CG  . LYS B 1180 ? 0.1990 0.3165 0.2980 -0.0393 0.0443  0.0005  1178 LYS B CG  
17967 C CD  . LYS B 1180 ? 0.2777 0.4030 0.3792 -0.0429 0.0486  0.0024  1178 LYS B CD  
17968 C CE  . LYS B 1180 ? 0.3118 0.4498 0.4228 -0.0431 0.0496  0.0007  1178 LYS B CE  
17969 N NZ  . LYS B 1180 ? 0.3478 0.4910 0.4599 -0.0369 0.0501  -0.0021 1178 LYS B NZ  
17970 N N   . ALA B 1181 ? 0.1571 0.2558 0.2582 -0.0457 0.0326  -0.0007 1179 ALA B N   
17971 C CA  . ALA B 1181 ? 0.1522 0.2487 0.2564 -0.0484 0.0293  -0.0016 1179 ALA B CA  
17972 C C   . ALA B 1181 ? 0.1713 0.2630 0.2737 -0.0440 0.0257  -0.0041 1179 ALA B C   
17973 O O   . ALA B 1181 ? 0.1556 0.2502 0.2626 -0.0441 0.0232  -0.0061 1179 ALA B O   
17974 C CB  . ALA B 1181 ? 0.1639 0.2517 0.2640 -0.0535 0.0289  0.0009  1179 ALA B CB  
17975 N N   . ILE B 1182 ? 0.1589 0.2434 0.2547 -0.0403 0.0255  -0.0040 1180 ILE B N   
17976 C CA  . ILE B 1182 ? 0.1548 0.2349 0.2486 -0.0362 0.0225  -0.0061 1180 ILE B CA  
17977 C C   . ILE B 1182 ? 0.1579 0.2463 0.2565 -0.0325 0.0222  -0.0085 1180 ILE B C   
17978 O O   . ILE B 1182 ? 0.1495 0.2379 0.2501 -0.0309 0.0194  -0.0106 1180 ILE B O   
17979 C CB  . ILE B 1182 ? 0.1728 0.2441 0.2589 -0.0332 0.0225  -0.0052 1180 ILE B CB  
17980 C CG1 . ILE B 1182 ? 0.1835 0.2453 0.2649 -0.0363 0.0218  -0.0032 1180 ILE B CG1 
17981 C CG2 . ILE B 1182 ? 0.1773 0.2462 0.2620 -0.0286 0.0200  -0.0075 1180 ILE B CG2 
17982 C CD1 . ILE B 1182 ? 0.1945 0.2481 0.2685 -0.0335 0.0219  -0.0021 1180 ILE B CD1 
17983 N N   . ALA B 1183 ? 0.1494 0.2446 0.2494 -0.0310 0.0251  -0.0083 1181 ALA B N   
17984 C CA  . ALA B 1183 ? 0.2018 0.3044 0.3060 -0.0272 0.0249  -0.0107 1181 ALA B CA  
17985 C C   . ALA B 1183 ? 0.1966 0.3067 0.3086 -0.0291 0.0235  -0.0120 1181 ALA B C   
17986 O O   . ALA B 1183 ? 0.2165 0.3302 0.3316 -0.0259 0.0217  -0.0142 1181 ALA B O   
17987 C CB  . ALA B 1183 ? 0.1927 0.3011 0.2968 -0.0255 0.0285  -0.0102 1181 ALA B CB  
17988 N N   . ALA B 1184 ? 0.1372 0.2495 0.2524 -0.0343 0.0241  -0.0105 1182 ALA B N   
17989 C CA  . ALA B 1184 ? 0.1858 0.3058 0.3089 -0.0366 0.0226  -0.0116 1182 ALA B CA  
17990 C C   . ALA B 1184 ? 0.1599 0.2740 0.2825 -0.0376 0.0183  -0.0128 1182 ALA B C   
17991 O O   . ALA B 1184 ? 0.1612 0.2812 0.2901 -0.0394 0.0164  -0.0138 1182 ALA B O   
17992 C CB  . ALA B 1184 ? 0.1842 0.3097 0.3113 -0.0422 0.0251  -0.0095 1182 ALA B CB  
17993 N N   . LEU B 1185 ? 0.1323 0.2354 0.2479 -0.0365 0.0166  -0.0126 1183 LEU B N   
17994 C CA  . LEU B 1185 ? 0.1358 0.2331 0.2503 -0.0374 0.0127  -0.0138 1183 LEU B CA  
17995 C C   . LEU B 1185 ? 0.1511 0.2519 0.2682 -0.0332 0.0102  -0.0164 1183 LEU B C   
17996 O O   . LEU B 1185 ? 0.1911 0.2934 0.3069 -0.0287 0.0112  -0.0172 1183 LEU B O   
17997 C CB  . LEU B 1185 ? 0.1644 0.2493 0.2707 -0.0368 0.0119  -0.0131 1183 LEU B CB  
17998 C CG  . LEU B 1185 ? 0.1467 0.2258 0.2490 -0.0406 0.0138  -0.0104 1183 LEU B CG  
17999 C CD1 . LEU B 1185 ? 0.1640 0.2315 0.2582 -0.0385 0.0129  -0.0100 1183 LEU B CD1 
18000 C CD2 . LEU B 1185 ? 0.1437 0.2231 0.2492 -0.0465 0.0126  -0.0098 1183 LEU B CD2 
18001 N N   . PRO B 1186 ? 0.1889 0.2905 0.3091 -0.0347 0.0069  -0.0178 1184 PRO B N   
18002 C CA  . PRO B 1186 ? 0.2080 0.3120 0.3297 -0.0307 0.0043  -0.0201 1184 PRO B CA  
18003 C C   . PRO B 1186 ? 0.1518 0.2461 0.2661 -0.0272 0.0028  -0.0208 1184 PRO B C   
18004 O O   . PRO B 1186 ? 0.1897 0.2752 0.2981 -0.0282 0.0031  -0.0198 1184 PRO B O   
18005 C CB  . PRO B 1186 ? 0.2443 0.3510 0.3707 -0.0340 0.0011  -0.0211 1184 PRO B CB  
18006 C CG  . PRO B 1186 ? 0.2451 0.3450 0.3686 -0.0392 0.0011  -0.0196 1184 PRO B CG  
18007 C CD  . PRO B 1186 ? 0.1803 0.2803 0.3022 -0.0402 0.0052  -0.0173 1184 PRO B CD  
18008 N N   . GLY B 1187 ? 0.1824 0.2785 0.2971 -0.0230 0.0013  -0.0226 1185 GLY B N   
18009 C CA  . GLY B 1187 ? 0.1990 0.2870 0.3073 -0.0198 -0.0002 -0.0233 1185 GLY B CA  
18010 C C   . GLY B 1187 ? 0.1814 0.2669 0.2854 -0.0165 0.0022  -0.0226 1185 GLY B C   
18011 O O   . GLY B 1187 ? 0.2193 0.3106 0.3256 -0.0147 0.0043  -0.0225 1185 GLY B O   
18012 N N   . PRO B 1188 ? 0.1744 0.2514 0.2720 -0.0156 0.0020  -0.0222 1186 PRO B N   
18013 C CA  . PRO B 1188 ? 0.1722 0.2468 0.2656 -0.0123 0.0037  -0.0217 1186 PRO B CA  
18014 C C   . PRO B 1188 ? 0.1889 0.2655 0.2823 -0.0133 0.0070  -0.0199 1186 PRO B C   
18015 O O   . PRO B 1188 ? 0.2286 0.3052 0.3230 -0.0168 0.0082  -0.0186 1186 PRO B O   
18016 C CB  . PRO B 1188 ? 0.2140 0.2795 0.3012 -0.0117 0.0025  -0.0215 1186 PRO B CB  
18017 C CG  . PRO B 1188 ? 0.3007 0.3629 0.3881 -0.0154 0.0014  -0.0212 1186 PRO B CG  
18018 C CD  . PRO B 1188 ? 0.2399 0.3090 0.3336 -0.0173 0.0001  -0.0222 1186 PRO B CD  
18019 N N   . LEU B 1189 ? 0.1726 0.2503 0.2642 -0.0102 0.0085  -0.0199 1187 LEU B N   
18020 C CA  . LEU B 1189 ? 0.2130 0.2919 0.3033 -0.0106 0.0116  -0.0183 1187 LEU B CA  
18021 C C   . LEU B 1189 ? 0.2347 0.3057 0.3190 -0.0110 0.0120  -0.0167 1187 LEU B C   
18022 O O   . LEU B 1189 ? 0.2551 0.3218 0.3355 -0.0084 0.0111  -0.0171 1187 LEU B O   
18023 C CB  . LEU B 1189 ? 0.2250 0.3076 0.3152 -0.0072 0.0128  -0.0191 1187 LEU B CB  
18024 C CG  . LEU B 1189 ? 0.2733 0.3648 0.3694 -0.0068 0.0138  -0.0200 1187 LEU B CG  
18025 C CD1 . LEU B 1189 ? 0.3640 0.4585 0.4643 -0.0062 0.0110  -0.0218 1187 LEU B CD1 
18026 C CD2 . LEU B 1189 ? 0.2700 0.3636 0.3645 -0.0034 0.0154  -0.0206 1187 LEU B CD2 
18027 N N   . LEU B 1190 ? 0.2142 0.2833 0.2979 -0.0142 0.0133  -0.0150 1188 LEU B N   
18028 C CA  . LEU B 1190 ? 0.1893 0.2505 0.2674 -0.0144 0.0134  -0.0135 1188 LEU B CA  
18029 C C   . LEU B 1190 ? 0.1914 0.2520 0.2659 -0.0124 0.0153  -0.0122 1188 LEU B C   
18030 O O   . LEU B 1190 ? 0.2035 0.2688 0.2793 -0.0129 0.0176  -0.0116 1188 LEU B O   
18031 C CB  . LEU B 1190 ? 0.1849 0.2431 0.2628 -0.0185 0.0138  -0.0119 1188 LEU B CB  
18032 C CG  . LEU B 1190 ? 0.1814 0.2392 0.2623 -0.0212 0.0116  -0.0129 1188 LEU B CG  
18033 C CD1 . LEU B 1190 ? 0.1812 0.2336 0.2601 -0.0251 0.0120  -0.0111 1188 LEU B CD1 
18034 C CD2 . LEU B 1190 ? 0.2297 0.2834 0.3088 -0.0187 0.0088  -0.0148 1188 LEU B CD2 
18035 N N   . LEU B 1191 ? 0.1935 0.2485 0.2635 -0.0103 0.0145  -0.0120 1189 LEU B N   
18036 C CA  . LEU B 1191 ? 0.2009 0.2541 0.2668 -0.0089 0.0159  -0.0105 1189 LEU B CA  
18037 C C   . LEU B 1191 ? 0.2389 0.2879 0.3023 -0.0114 0.0170  -0.0081 1189 LEU B C   
18038 O O   . LEU B 1191 ? 0.2198 0.2625 0.2807 -0.0119 0.0157  -0.0076 1189 LEU B O   
18039 C CB  . LEU B 1191 ? 0.1951 0.2446 0.2577 -0.0057 0.0144  -0.0110 1189 LEU B CB  
18040 C CG  . LEU B 1191 ? 0.2113 0.2609 0.2707 -0.0036 0.0153  -0.0102 1189 LEU B CG  
18041 C CD1 . LEU B 1191 ? 0.2309 0.2785 0.2885 -0.0008 0.0136  -0.0112 1189 LEU B CD1 
18042 C CD2 . LEU B 1191 ? 0.1861 0.2321 0.2418 -0.0044 0.0165  -0.0078 1189 LEU B CD2 
18043 N N   . VAL B 1192 ? 0.1721 0.2240 0.2355 -0.0129 0.0193  -0.0067 1190 VAL B N   
18044 C CA  . VAL B 1192 ? 0.2159 0.2644 0.2771 -0.0158 0.0206  -0.0043 1190 VAL B CA  
18045 C C   . VAL B 1192 ? 0.2352 0.2804 0.2910 -0.0141 0.0215  -0.0025 1190 VAL B C   
18046 O O   . VAL B 1192 ? 0.2274 0.2762 0.2825 -0.0121 0.0225  -0.0028 1190 VAL B O   
18047 C CB  . VAL B 1192 ? 0.2093 0.2639 0.2742 -0.0190 0.0229  -0.0037 1190 VAL B CB  
18048 C CG1 . VAL B 1192 ? 0.1873 0.2380 0.2493 -0.0224 0.0244  -0.0009 1190 VAL B CG1 
18049 C CG2 . VAL B 1192 ? 0.2062 0.2648 0.2769 -0.0207 0.0217  -0.0055 1190 VAL B CG2 
18050 N N   . GLN B 1193 ? 0.1682 0.2062 0.2199 -0.0147 0.0210  -0.0007 1191 GLN B N   
18051 C CA  . GLN B 1193 ? 0.1492 0.1837 0.1957 -0.0135 0.0217  0.0015  1191 GLN B CA  
18052 C C   . GLN B 1193 ? 0.1691 0.2003 0.2134 -0.0170 0.0231  0.0041  1191 GLN B C   
18053 O O   . GLN B 1193 ? 0.1862 0.2131 0.2307 -0.0194 0.0224  0.0045  1191 GLN B O   
18054 C CB  . GLN B 1193 ? 0.1751 0.2038 0.2183 -0.0106 0.0197  0.0015  1191 GLN B CB  
18055 C CG  . GLN B 1193 ? 0.1900 0.2216 0.2346 -0.0074 0.0184  -0.0006 1191 GLN B CG  
18056 C CD  . GLN B 1193 ? 0.1694 0.1963 0.2105 -0.0044 0.0169  0.0000  1191 GLN B CD  
18057 O OE1 . GLN B 1193 ? 0.1821 0.2085 0.2202 -0.0029 0.0172  0.0014  1191 GLN B OE1 
18058 N NE2 . GLN B 1193 ? 0.1856 0.2093 0.2273 -0.0035 0.0153  -0.0012 1191 GLN B NE2 
18059 N N   . ALA B 1194 ? 0.1809 0.2133 0.2223 -0.0173 0.0250  0.0059  1192 ALA B N   
18060 C CA  . ALA B 1194 ? 0.1709 0.2002 0.2096 -0.0207 0.0267  0.0087  1192 ALA B CA  
18061 C C   . ALA B 1194 ? 0.2108 0.2350 0.2431 -0.0191 0.0267  0.0111  1192 ALA B C   
18062 O O   . ALA B 1194 ? 0.2304 0.2561 0.2608 -0.0158 0.0262  0.0107  1192 ALA B O   
18063 C CB  . ALA B 1194 ? 0.1840 0.2207 0.2257 -0.0234 0.0295  0.0089  1192 ALA B CB  
18064 N N   . ALA B 1195 ? 0.1885 0.2064 0.2170 -0.0216 0.0271  0.0138  1193 ALA B N   
18065 C CA  . ALA B 1195 ? 0.2201 0.2328 0.2422 -0.0205 0.0272  0.0165  1193 ALA B CA  
18066 C C   . ALA B 1195 ? 0.2663 0.2745 0.2852 -0.0247 0.0287  0.0196  1193 ALA B C   
18067 O O   . ALA B 1195 ? 0.2248 0.2311 0.2459 -0.0281 0.0287  0.0196  1193 ALA B O   
18068 C CB  . ALA B 1195 ? 0.2369 0.2428 0.2560 -0.0169 0.0244  0.0166  1193 ALA B CB  
18069 N N   . SER B 1196 ? 0.2418 0.2483 0.2554 -0.0247 0.0299  0.0222  1194 SER B N   
18070 C CA  . SER B 1196 ? 0.2543 0.2549 0.2636 -0.0284 0.0311  0.0255  1194 SER B CA  
18071 C C   . SER B 1196 ? 0.2541 0.2439 0.2588 -0.0271 0.0285  0.0270  1194 SER B C   
18072 O O   . SER B 1196 ? 0.2658 0.2534 0.2699 -0.0228 0.0262  0.0258  1194 SER B O   
18073 C CB  . SER B 1196 ? 0.2685 0.2706 0.2729 -0.0288 0.0332  0.0279  1194 SER B CB  
18074 O OG  . SER B 1196 ? 0.2959 0.2951 0.2959 -0.0243 0.0314  0.0284  1194 SER B OG  
18075 N N   . SER B 1197 ? 0.2697 0.2526 0.2711 -0.0310 0.0290  0.0296  1195 SER B N   
18076 C CA  . SER B 1197 ? 0.2741 0.2456 0.2701 -0.0296 0.0267  0.0313  1195 SER B CA  
18077 C C   . SER B 1197 ? 0.2824 0.2511 0.2728 -0.0252 0.0257  0.0329  1195 SER B C   
18078 O O   . SER B 1197 ? 0.2938 0.2566 0.2819 -0.0213 0.0232  0.0327  1195 SER B O   
18079 C CB  . SER B 1197 ? 0.2645 0.2287 0.2568 -0.0348 0.0276  0.0343  1195 SER B CB  
18080 O OG  . SER B 1197 ? 0.2882 0.2549 0.2858 -0.0393 0.0283  0.0329  1195 SER B OG  
18081 N N   . GLY B 1198 ? 0.2979 0.2711 0.2862 -0.0255 0.0276  0.0343  1196 GLY B N   
18082 C CA  . GLY B 1198 ? 0.3315 0.3028 0.3145 -0.0215 0.0264  0.0358  1196 GLY B CA  
18083 C C   . GLY B 1198 ? 0.3116 0.2876 0.2979 -0.0165 0.0245  0.0330  1196 GLY B C   
18084 O O   . GLY B 1198 ? 0.3472 0.3191 0.3303 -0.0125 0.0222  0.0337  1196 GLY B O   
18085 N N   . GLU B 1199 ? 0.3097 0.2945 0.3023 -0.0165 0.0253  0.0299  1197 GLU B N   
18086 C CA  . GLU B 1199 ? 0.3024 0.2915 0.2980 -0.0122 0.0235  0.0272  1197 GLU B CA  
18087 C C   . GLU B 1199 ? 0.3099 0.2937 0.3067 -0.0098 0.0210  0.0262  1197 GLU B C   
18088 O O   . GLU B 1199 ? 0.3120 0.2955 0.3082 -0.0055 0.0190  0.0256  1197 GLU B O   
18089 C CB  . GLU B 1199 ? 0.3226 0.3212 0.3244 -0.0128 0.0248  0.0241  1197 GLU B CB  
18090 C CG  . GLU B 1199 ? 0.3234 0.3260 0.3273 -0.0085 0.0230  0.0218  1197 GLU B CG  
18091 C CD  . GLU B 1199 ? 0.4142 0.4251 0.4240 -0.0087 0.0238  0.0185  1197 GLU B CD  
18092 O OE1 . GLU B 1199 ? 0.4151 0.4297 0.4277 -0.0117 0.0258  0.0179  1197 GLU B OE1 
18093 O OE2 . GLU B 1199 ? 0.4126 0.4264 0.4240 -0.0056 0.0222  0.0167  1197 GLU B OE2 
18094 N N   . ILE B 1200 ? 0.2555 0.2353 0.2538 -0.0124 0.0211  0.0258  1198 ILE B N   
18095 C CA  . ILE B 1200 ? 0.2503 0.2242 0.2489 -0.0101 0.0189  0.0247  1198 ILE B CA  
18096 C C   . ILE B 1200 ? 0.3163 0.2822 0.3089 -0.0070 0.0172  0.0272  1198 ILE B C   
18097 O O   . ILE B 1200 ? 0.2886 0.2529 0.2813 -0.0027 0.0152  0.0262  1198 ILE B O   
18098 C CB  . ILE B 1200 ? 0.2427 0.2129 0.2431 -0.0141 0.0192  0.0241  1198 ILE B CB  
18099 C CG1 . ILE B 1200 ? 0.2673 0.2464 0.2745 -0.0163 0.0204  0.0213  1198 ILE B CG1 
18100 C CG2 . ILE B 1200 ? 0.2553 0.2177 0.2545 -0.0117 0.0169  0.0233  1198 ILE B CG2 
18101 C CD1 . ILE B 1200 ? 0.2632 0.2399 0.2726 -0.0208 0.0207  0.0208  1198 ILE B CD1 
18102 N N   . ALA B 1201 ? 0.3230 0.2841 0.3100 -0.0089 0.0180  0.0306  1199 ALA B N   
18103 C CA  . ALA B 1201 ? 0.3427 0.2956 0.3235 -0.0059 0.0162  0.0332  1199 ALA B CA  
18104 C C   . ALA B 1201 ? 0.3305 0.2881 0.3107 -0.0013 0.0150  0.0333  1199 ALA B C   
18105 O O   . ALA B 1201 ? 0.3842 0.3377 0.3622 0.0030  0.0128  0.0339  1199 ALA B O   
18106 C CB  . ALA B 1201 ? 0.3650 0.3115 0.3397 -0.0095 0.0174  0.0369  1199 ALA B CB  
18107 N N   . ARG B 1202 ? 0.3385 0.3048 0.3208 -0.0020 0.0163  0.0325  1200 ARG B N   
18108 C CA  . ARG B 1202 ? 0.3586 0.3287 0.3393 0.0015  0.0151  0.0330  1200 ARG B CA  
18109 C C   . ARG B 1202 ? 0.3806 0.3584 0.3671 0.0044  0.0141  0.0298  1200 ARG B C   
18110 O O   . ARG B 1202 ? 0.3559 0.3359 0.3415 0.0080  0.0124  0.0300  1200 ARG B O   
18111 C CB  . ARG B 1202 ? 0.4080 0.3819 0.3859 -0.0009 0.0169  0.0345  1200 ARG B CB  
18112 C CG  . ARG B 1202 ? 0.3687 0.3511 0.3515 -0.0035 0.0192  0.0319  1200 ARG B CG  
18113 C CD  . ARG B 1202 ? 0.4628 0.4491 0.4424 -0.0051 0.0210  0.0332  1200 ARG B CD  
18114 N NE  . ARG B 1202 ? 0.4793 0.4737 0.4637 -0.0071 0.0231  0.0305  1200 ARG B NE  
18115 C CZ  . ARG B 1202 ? 0.4460 0.4420 0.4313 -0.0111 0.0260  0.0307  1200 ARG B CZ  
18116 N NH1 . ARG B 1202 ? 0.4242 0.4145 0.4057 -0.0142 0.0272  0.0336  1200 ARG B NH1 
18117 N NH2 . ARG B 1202 ? 0.4063 0.4101 0.3966 -0.0121 0.0276  0.0281  1200 ARG B NH2 
18118 N N   . ASN B 1203 ? 0.3218 0.3037 0.3138 0.0029  0.0150  0.0269  1201 ASN B N   
18119 C CA  . ASN B 1203 ? 0.3391 0.3284 0.3361 0.0051  0.0144  0.0239  1201 ASN B CA  
18120 C C   . ASN B 1203 ? 0.3496 0.3373 0.3502 0.0065  0.0134  0.0218  1201 ASN B C   
18121 O O   . ASN B 1203 ? 0.3232 0.3107 0.3266 0.0037  0.0144  0.0203  1201 ASN B O   
18122 C CB  . ASN B 1203 ? 0.3190 0.3157 0.3192 0.0023  0.0163  0.0222  1201 ASN B CB  
18123 C CG  . ASN B 1203 ? 0.3097 0.3134 0.3146 0.0043  0.0156  0.0192  1201 ASN B CG  
18124 O OD1 . ASN B 1203 ? 0.3308 0.3347 0.3364 0.0076  0.0136  0.0187  1201 ASN B OD1 
18125 N ND2 . ASN B 1203 ? 0.3550 0.3644 0.3631 0.0023  0.0171  0.0173  1201 ASN B ND2 
18126 N N   . PRO B 1204 ? 0.3381 0.3250 0.3390 0.0106  0.0114  0.0215  1202 PRO B N   
18127 C CA  . PRO B 1204 ? 0.3310 0.3165 0.3349 0.0121  0.0107  0.0193  1202 PRO B CA  
18128 C C   . PRO B 1204 ? 0.3278 0.3200 0.3372 0.0108  0.0114  0.0162  1202 PRO B C   
18129 O O   . PRO B 1204 ? 0.3261 0.3167 0.3378 0.0107  0.0112  0.0143  1202 PRO B O   
18130 C CB  . PRO B 1204 ? 0.3939 0.3796 0.3973 0.0171  0.0088  0.0197  1202 PRO B CB  
18131 C CG  . PRO B 1204 ? 0.4186 0.4081 0.4200 0.0179  0.0083  0.0215  1202 PRO B CG  
18132 C CD  . PRO B 1204 ? 0.3856 0.3728 0.3837 0.0141  0.0098  0.0233  1202 PRO B CD  
18133 N N   . ASP B 1205 ? 0.2737 0.2730 0.2850 0.0098  0.0122  0.0155  1203 ASP B N   
18134 C CA  . ASP B 1205 ? 0.3240 0.3291 0.3400 0.0086  0.0128  0.0127  1203 ASP B CA  
18135 C C   . ASP B 1205 ? 0.3094 0.3162 0.3264 0.0045  0.0147  0.0124  1203 ASP B C   
18136 O O   . ASP B 1205 ? 0.2957 0.3085 0.3159 0.0036  0.0155  0.0106  1203 ASP B O   
18137 C CB  . ASP B 1205 ? 0.2926 0.3044 0.3102 0.0104  0.0121  0.0118  1203 ASP B CB  
18138 C CG  . ASP B 1205 ? 0.3770 0.3889 0.3949 0.0142  0.0103  0.0117  1203 ASP B CG  
18139 O OD1 . ASP B 1205 ? 0.3802 0.3884 0.3986 0.0157  0.0098  0.0113  1203 ASP B OD1 
18140 O OD2 . ASP B 1205 ? 0.3640 0.3800 0.3817 0.0158  0.0094  0.0121  1203 ASP B OD2 
18141 N N   . ALA B 1206 ? 0.2810 0.2826 0.2953 0.0021  0.0156  0.0143  1204 ALA B N   
18142 C CA  . ALA B 1206 ? 0.2794 0.2833 0.2952 -0.0020 0.0177  0.0143  1204 ALA B CA  
18143 C C   . ALA B 1206 ? 0.2534 0.2611 0.2746 -0.0032 0.0178  0.0114  1204 ALA B C   
18144 O O   . ALA B 1206 ? 0.2738 0.2872 0.2978 -0.0050 0.0192  0.0102  1204 ALA B O   
18145 C CB  . ALA B 1206 ? 0.2824 0.2793 0.2946 -0.0047 0.0184  0.0167  1204 ALA B CB  
18146 N N   . TYR B 1207 ? 0.2183 0.2227 0.2407 -0.0019 0.0164  0.0101  1205 TYR B N   
18147 C CA  . TYR B 1207 ? 0.2167 0.2245 0.2437 -0.0024 0.0161  0.0072  1205 TYR B CA  
18148 C C   . TYR B 1207 ? 0.2185 0.2287 0.2466 0.0014  0.0146  0.0057  1205 TYR B C   
18149 O O   . TYR B 1207 ? 0.2891 0.2952 0.3151 0.0040  0.0134  0.0062  1205 TYR B O   
18150 C CB  . TYR B 1207 ? 0.2262 0.2285 0.2535 -0.0042 0.0155  0.0068  1205 TYR B CB  
18151 C CG  . TYR B 1207 ? 0.1783 0.1785 0.2049 -0.0085 0.0168  0.0084  1205 TYR B CG  
18152 C CD1 . TYR B 1207 ? 0.1732 0.1799 0.2033 -0.0114 0.0185  0.0079  1205 TYR B CD1 
18153 C CD2 . TYR B 1207 ? 0.1871 0.1791 0.2097 -0.0097 0.0165  0.0104  1205 TYR B CD2 
18154 C CE1 . TYR B 1207 ? 0.1872 0.1930 0.2171 -0.0156 0.0200  0.0095  1205 TYR B CE1 
18155 C CE2 . TYR B 1207 ? 0.2316 0.2217 0.2535 -0.0141 0.0178  0.0121  1205 TYR B CE2 
18156 C CZ  . TYR B 1207 ? 0.1966 0.1939 0.2223 -0.0172 0.0196  0.0116  1205 TYR B CZ  
18157 O OH  . TYR B 1207 ? 0.2286 0.2248 0.2540 -0.0218 0.0211  0.0134  1205 TYR B OH  
18158 N N   . CYS B 1208 ? 0.1565 0.1732 0.1878 0.0016  0.0149  0.0039  1206 CYS B N   
18159 C CA  . CYS B 1208 ? 0.1796 0.1992 0.2120 0.0046  0.0137  0.0026  1206 CYS B CA  
18160 C C   . CYS B 1208 ? 0.1769 0.1954 0.2115 0.0053  0.0127  0.0005  1206 CYS B C   
18161 O O   . CYS B 1208 ? 0.1598 0.1799 0.1972 0.0034  0.0129  -0.0010 1206 CYS B O   
18162 C CB  . CYS B 1208 ? 0.1869 0.2130 0.2211 0.0044  0.0143  0.0015  1206 CYS B CB  
18163 S SG  . CYS B 1208 ? 0.2366 0.2661 0.2717 0.0075  0.0128  0.0002  1206 CYS B SG  
18164 N N   . LEU B 1209 ? 0.1597 0.1758 0.1932 0.0081  0.0116  0.0005  1207 LEU B N   
18165 C CA  . LEU B 1209 ? 0.1436 0.1582 0.1784 0.0089  0.0107  -0.0014 1207 LEU B CA  
18166 C C   . LEU B 1209 ? 0.1463 0.1664 0.1842 0.0092  0.0104  -0.0035 1207 LEU B C   
18167 O O   . LEU B 1209 ? 0.1648 0.1843 0.2039 0.0093  0.0098  -0.0052 1207 LEU B O   
18168 C CB  . LEU B 1209 ? 0.1577 0.1683 0.1902 0.0120  0.0099  -0.0009 1207 LEU B CB  
18169 C CG  . LEU B 1209 ? 0.1791 0.1830 0.2079 0.0123  0.0099  0.0011  1207 LEU B CG  
18170 C CD1 . LEU B 1209 ? 0.1997 0.1998 0.2266 0.0160  0.0090  0.0012  1207 LEU B CD1 
18171 C CD2 . LEU B 1209 ? 0.2090 0.2082 0.2373 0.0089  0.0102  0.0010  1207 LEU B CD2 
18172 N N   . ASN B 1210 ? 0.1553 0.1804 0.1940 0.0094  0.0107  -0.0033 1208 ASN B N   
18173 C CA  . ASN B 1210 ? 0.1871 0.2169 0.2283 0.0096  0.0104  -0.0052 1208 ASN B CA  
18174 C C   . ASN B 1210 ? 0.1492 0.1797 0.1928 0.0076  0.0105  -0.0068 1208 ASN B C   
18175 O O   . ASN B 1210 ? 0.1982 0.2302 0.2434 0.0080  0.0097  -0.0086 1208 ASN B O   
18176 C CB  . ASN B 1210 ? 0.2122 0.2462 0.2532 0.0096  0.0107  -0.0048 1208 ASN B CB  
18177 C CG  . ASN B 1210 ? 0.2377 0.2721 0.2767 0.0116  0.0101  -0.0033 1208 ASN B CG  
18178 O OD1 . ASN B 1210 ? 0.2924 0.3239 0.3300 0.0131  0.0097  -0.0023 1208 ASN B OD1 
18179 N ND2 . ASN B 1210 ? 0.2984 0.3364 0.3371 0.0116  0.0100  -0.0033 1208 ASN B ND2 
18180 N N   . TRP B 1211 ? 0.1490 0.1787 0.1930 0.0052  0.0114  -0.0062 1209 TRP B N   
18181 C CA  . TRP B 1211 ? 0.1511 0.1829 0.1982 0.0031  0.0116  -0.0076 1209 TRP B CA  
18182 C C   . TRP B 1211 ? 0.1511 0.1789 0.1985 0.0019  0.0108  -0.0082 1209 TRP B C   
18183 O O   . TRP B 1211 ? 0.1850 0.2145 0.2351 0.0000  0.0107  -0.0093 1209 TRP B O   
18184 C CB  . TRP B 1211 ? 0.1758 0.2103 0.2237 0.0010  0.0132  -0.0067 1209 TRP B CB  
18185 C CG  . TRP B 1211 ? 0.1724 0.2093 0.2185 0.0022  0.0139  -0.0058 1209 TRP B CG  
18186 C CD1 . TRP B 1211 ? 0.1816 0.2175 0.2251 0.0016  0.0150  -0.0038 1209 TRP B CD1 
18187 C CD2 . TRP B 1211 ? 0.1861 0.2261 0.2323 0.0040  0.0133  -0.0069 1209 TRP B CD2 
18188 N NE1 . TRP B 1211 ? 0.1860 0.2245 0.2280 0.0030  0.0151  -0.0036 1209 TRP B NE1 
18189 C CE2 . TRP B 1211 ? 0.1993 0.2402 0.2430 0.0045  0.0140  -0.0055 1209 TRP B CE2 
18190 C CE3 . TRP B 1211 ? 0.1798 0.2216 0.2277 0.0052  0.0121  -0.0087 1209 TRP B CE3 
18191 C CZ2 . TRP B 1211 ? 0.2324 0.2759 0.2753 0.0059  0.0135  -0.0061 1209 TRP B CZ2 
18192 C CZ3 . TRP B 1211 ? 0.2003 0.2444 0.2474 0.0066  0.0118  -0.0092 1209 TRP B CZ3 
18193 C CH2 . TRP B 1211 ? 0.2222 0.2672 0.2669 0.0068  0.0124  -0.0079 1209 TRP B CH2 
18194 N N   . LEU B 1212 ? 0.1487 0.1712 0.1933 0.0033  0.0102  -0.0077 1210 LEU B N   
18195 C CA  . LEU B 1212 ? 0.1447 0.1622 0.1887 0.0023  0.0093  -0.0084 1210 LEU B CA  
18196 C C   . LEU B 1212 ? 0.1435 0.1597 0.1870 0.0044  0.0080  -0.0101 1210 LEU B C   
18197 O O   . LEU B 1212 ? 0.1395 0.1509 0.1816 0.0041  0.0072  -0.0108 1210 LEU B O   
18198 C CB  . LEU B 1212 ? 0.1300 0.1412 0.1705 0.0020  0.0096  -0.0065 1210 LEU B CB  
18199 C CG  . LEU B 1212 ? 0.1253 0.1367 0.1659 -0.0011 0.0109  -0.0047 1210 LEU B CG  
18200 C CD1 . LEU B 1212 ? 0.1771 0.1824 0.2136 -0.0006 0.0111  -0.0024 1210 LEU B CD1 
18201 C CD2 . LEU B 1212 ? 0.1767 0.1879 0.2198 -0.0046 0.0106  -0.0057 1210 LEU B CD2 
18202 N N   . VAL B 1213 ? 0.1609 0.1812 0.2052 0.0064  0.0079  -0.0108 1211 VAL B N   
18203 C CA  . VAL B 1213 ? 0.1375 0.1575 0.1814 0.0082  0.0069  -0.0124 1211 VAL B CA  
18204 C C   . VAL B 1213 ? 0.1576 0.1825 0.2045 0.0074  0.0065  -0.0138 1211 VAL B C   
18205 O O   . VAL B 1213 ? 0.1769 0.2057 0.2258 0.0062  0.0070  -0.0135 1211 VAL B O   
18206 C CB  . VAL B 1213 ? 0.1472 0.1675 0.1894 0.0112  0.0071  -0.0117 1211 VAL B CB  
18207 C CG1 . VAL B 1213 ? 0.1419 0.1568 0.1811 0.0126  0.0073  -0.0105 1211 VAL B CG1 
18208 C CG2 . VAL B 1213 ? 0.1603 0.1855 0.2034 0.0115  0.0077  -0.0106 1211 VAL B CG2 
18209 N N   . GLU B 1214 ? 0.1441 0.1683 0.1907 0.0081  0.0054  -0.0154 1212 GLU B N   
18210 C CA  . GLU B 1214 ? 0.1529 0.1809 0.2016 0.0078  0.0046  -0.0168 1212 GLU B CA  
18211 C C   . GLU B 1214 ? 0.1319 0.1613 0.1794 0.0100  0.0044  -0.0170 1212 GLU B C   
18212 O O   . GLU B 1214 ? 0.1311 0.1579 0.1762 0.0115  0.0043  -0.0171 1212 GLU B O   
18213 C CB  . GLU B 1214 ? 0.2021 0.2282 0.2513 0.0066  0.0032  -0.0184 1212 GLU B CB  
18214 C CG  . GLU B 1214 ? 0.2358 0.2655 0.2871 0.0064  0.0022  -0.0197 1212 GLU B CG  
18215 C CD  . GLU B 1214 ? 0.3928 0.4209 0.4445 0.0053  0.0005  -0.0213 1212 GLU B CD  
18216 O OE1 . GLU B 1214 ? 0.3826 0.4087 0.4350 0.0033  0.0002  -0.0213 1212 GLU B OE1 
18217 O OE2 . GLU B 1214 ? 0.4818 0.5104 0.5329 0.0062  -0.0008 -0.0225 1212 GLU B OE2 
18218 N N   . GLU B 1215 ? 0.1444 0.1778 0.1932 0.0100  0.0045  -0.0170 1213 GLU B N   
18219 C CA  . GLU B 1215 ? 0.1112 0.1460 0.1589 0.0115  0.0042  -0.0172 1213 GLU B CA  
18220 C C   . GLU B 1215 ? 0.1066 0.1410 0.1542 0.0115  0.0029  -0.0188 1213 GLU B C   
18221 O O   . GLU B 1215 ? 0.1329 0.1682 0.1822 0.0105  0.0021  -0.0197 1213 GLU B O   
18222 C CB  . GLU B 1215 ? 0.1233 0.1616 0.1719 0.0114  0.0045  -0.0167 1213 GLU B CB  
18223 C CG  . GLU B 1215 ? 0.1453 0.1845 0.1938 0.0113  0.0056  -0.0152 1213 GLU B CG  
18224 C CD  . GLU B 1215 ? 0.1269 0.1692 0.1760 0.0109  0.0058  -0.0151 1213 GLU B CD  
18225 O OE1 . GLU B 1215 ? 0.1473 0.1909 0.1980 0.0100  0.0061  -0.0156 1213 GLU B OE1 
18226 O OE2 . GLU B 1215 ? 0.1315 0.1750 0.1795 0.0117  0.0057  -0.0146 1213 GLU B OE2 
18227 N N   . VAL B 1216 ? 0.1011 0.1344 0.1465 0.0128  0.0027  -0.0189 1214 VAL B N   
18228 C CA  . VAL B 1216 ? 0.1026 0.1353 0.1470 0.0130  0.0015  -0.0202 1214 VAL B CA  
18229 C C   . VAL B 1216 ? 0.1081 0.1426 0.1512 0.0138  0.0017  -0.0196 1214 VAL B C   
18230 O O   . VAL B 1216 ? 0.1402 0.1750 0.1822 0.0148  0.0027  -0.0187 1214 VAL B O   
18231 C CB  . VAL B 1216 ? 0.1260 0.1550 0.1684 0.0134  0.0010  -0.0211 1214 VAL B CB  
18232 C CG1 . VAL B 1216 ? 0.1493 0.1776 0.1899 0.0136  -0.0003 -0.0222 1214 VAL B CG1 
18233 C CG2 . VAL B 1216 ? 0.1400 0.1672 0.1837 0.0119  0.0005  -0.0216 1214 VAL B CG2 
18234 N N   . SER B 1217 ? 0.0911 0.1266 0.1343 0.0134  0.0007  -0.0202 1215 SER B N   
18235 C CA  . SER B 1217 ? 0.0912 0.1277 0.1328 0.0138  0.0006  -0.0197 1215 SER B CA  
18236 C C   . SER B 1217 ? 0.0983 0.1326 0.1375 0.0140  -0.0004 -0.0206 1215 SER B C   
18237 O O   . SER B 1217 ? 0.1243 0.1573 0.1638 0.0137  -0.0017 -0.0218 1215 SER B O   
18238 C CB  . SER B 1217 ? 0.1082 0.1464 0.1508 0.0132  0.0001  -0.0197 1215 SER B CB  
18239 O OG  . SER B 1217 ? 0.1390 0.1769 0.1795 0.0131  -0.0006 -0.0195 1215 SER B OG  
18240 N N   . ALA B 1218 ? 0.0975 0.1317 0.1344 0.0145  0.0002  -0.0201 1216 ALA B N   
18241 C CA  . ALA B 1218 ? 0.1135 0.1458 0.1475 0.0147  -0.0006 -0.0207 1216 ALA B CA  
18242 C C   . ALA B 1218 ? 0.1259 0.1594 0.1582 0.0143  -0.0003 -0.0197 1216 ALA B C   
18243 O O   . ALA B 1218 ? 0.1494 0.1851 0.1820 0.0144  0.0010  -0.0185 1216 ALA B O   
18244 C CB  . ALA B 1218 ? 0.1346 0.1648 0.1665 0.0157  0.0002  -0.0212 1216 ALA B CB  
18245 N N   . SER B 1219 ? 0.1118 0.1437 0.1423 0.0138  -0.0018 -0.0201 1217 SER B N   
18246 C CA  . SER B 1219 ? 0.1118 0.1440 0.1402 0.0130  -0.0018 -0.0191 1217 SER B CA  
18247 C C   . SER B 1219 ? 0.1010 0.1308 0.1255 0.0132  -0.0022 -0.0193 1217 SER B C   
18248 O O   . SER B 1219 ? 0.1202 0.1473 0.1434 0.0134  -0.0040 -0.0204 1217 SER B O   
18249 C CB  . SER B 1219 ? 0.1196 0.1513 0.1485 0.0123  -0.0033 -0.0191 1217 SER B CB  
18250 O OG  . SER B 1219 ? 0.1375 0.1687 0.1639 0.0112  -0.0035 -0.0181 1217 SER B OG  
18251 N N   . ILE B 1220 ? 0.1044 0.1353 0.1270 0.0131  -0.0007 -0.0184 1218 ILE B N   
18252 C CA  . ILE B 1220 ? 0.1281 0.1570 0.1465 0.0133  -0.0006 -0.0185 1218 ILE B CA  
18253 C C   . ILE B 1220 ? 0.1277 0.1567 0.1436 0.0117  -0.0006 -0.0171 1218 ILE B C   
18254 O O   . ILE B 1220 ? 0.1366 0.1689 0.1537 0.0108  0.0008  -0.0157 1218 ILE B O   
18255 C CB  . ILE B 1220 ? 0.1751 0.2053 0.1930 0.0146  0.0016  -0.0185 1218 ILE B CB  
18256 C CG1 . ILE B 1220 ? 0.2100 0.2391 0.2298 0.0159  0.0014  -0.0199 1218 ILE B CG1 
18257 C CG2 . ILE B 1220 ? 0.1927 0.2207 0.2056 0.0149  0.0019  -0.0188 1218 ILE B CG2 
18258 C CD1 . ILE B 1220 ? 0.3149 0.3459 0.3356 0.0174  0.0036  -0.0196 1218 ILE B CD1 
18259 N N   . ASN B 1221 ? 0.1443 0.1697 0.1566 0.0113  -0.0022 -0.0173 1219 ASN B N   
18260 C CA  . ASN B 1221 ? 0.1365 0.1610 0.1455 0.0096  -0.0023 -0.0158 1219 ASN B CA  
18261 C C   . ASN B 1221 ? 0.1542 0.1798 0.1602 0.0096  -0.0002 -0.0151 1219 ASN B C   
18262 O O   . ASN B 1221 ? 0.1921 0.2149 0.1943 0.0103  -0.0006 -0.0157 1219 ASN B O   
18263 C CB  . ASN B 1221 ? 0.1493 0.1690 0.1552 0.0095  -0.0050 -0.0163 1219 ASN B CB  
18264 C CG  . ASN B 1221 ? 0.1636 0.1811 0.1651 0.0077  -0.0052 -0.0147 1219 ASN B CG  
18265 O OD1 . ASN B 1221 ? 0.1594 0.1795 0.1607 0.0062  -0.0034 -0.0132 1219 ASN B OD1 
18266 N ND2 . ASN B 1221 ? 0.1966 0.2093 0.1943 0.0078  -0.0076 -0.0149 1219 ASN B ND2 
18267 N N   . THR B 1222 ? 0.1475 0.1775 0.1551 0.0087  0.0019  -0.0137 1220 THR B N   
18268 C CA  . THR B 1222 ? 0.1551 0.1874 0.1605 0.0089  0.0043  -0.0129 1220 THR B CA  
18269 C C   . THR B 1222 ? 0.2015 0.2325 0.2025 0.0067  0.0045  -0.0113 1220 THR B C   
18270 O O   . THR B 1222 ? 0.2448 0.2780 0.2436 0.0066  0.0067  -0.0105 1220 THR B O   
18271 C CB  . THR B 1222 ? 0.1764 0.2149 0.1861 0.0092  0.0067  -0.0121 1220 THR B CB  
18272 O OG1 . THR B 1222 ? 0.1983 0.2392 0.2104 0.0070  0.0063  -0.0107 1220 THR B OG1 
18273 C CG2 . THR B 1222 ? 0.1877 0.2266 0.2008 0.0116  0.0068  -0.0136 1220 THR B CG2 
18274 N N   . ALA B 1223 ? 0.1731 0.2004 0.1725 0.0050  0.0022  -0.0109 1221 ALA B N   
18275 C CA  . ALA B 1223 ? 0.2020 0.2266 0.1963 0.0029  0.0018  -0.0094 1221 ALA B CA  
18276 C C   . ALA B 1223 ? 0.2501 0.2687 0.2393 0.0039  -0.0001 -0.0103 1221 ALA B C   
18277 O O   . ALA B 1223 ? 0.2651 0.2802 0.2493 0.0023  -0.0009 -0.0091 1221 ALA B O   
18278 C CB  . ALA B 1223 ? 0.2139 0.2371 0.2088 0.0005  0.0003  -0.0082 1221 ALA B CB  
18279 N N   . ALA B 1224 ? 0.2399 0.2572 0.2300 0.0064  -0.0010 -0.0123 1222 ALA B N   
18280 C CA  . ALA B 1224 ? 0.2492 0.2611 0.2353 0.0073  -0.0036 -0.0134 1222 ALA B CA  
18281 C C   . ALA B 1224 ? 0.3155 0.3249 0.2949 0.0069  -0.0029 -0.0127 1222 ALA B C   
18282 O O   . ALA B 1224 ? 0.3163 0.3207 0.2910 0.0069  -0.0052 -0.0127 1222 ALA B O   
18283 C CB  . ALA B 1224 ? 0.2782 0.2898 0.2670 0.0096  -0.0047 -0.0156 1222 ALA B CB  
18284 N N   . ALA B 1225 ? 0.2392 0.2522 0.2178 0.0068  0.0003  -0.0121 1223 ALA B N   
18285 C CA  . ALA B 1225 ? 0.2807 0.2917 0.2526 0.0066  0.0014  -0.0114 1223 ALA B CA  
18286 C C   . ALA B 1225 ? 0.3351 0.3445 0.3030 0.0037  0.0014  -0.0090 1223 ALA B C   
18287 O O   . ALA B 1225 ? 0.3136 0.3204 0.2751 0.0032  0.0019  -0.0082 1223 ALA B O   
18288 C CB  . ALA B 1225 ? 0.3033 0.3190 0.2756 0.0077  0.0051  -0.0116 1223 ALA B CB  
18289 N N   . GLY B 1226 ? 0.3056 0.3159 0.2765 0.0017  0.0008  -0.0077 1224 GLY B N   
18290 C CA  . GLY B 1226 ? 0.3015 0.3093 0.2685 -0.0014 0.0005  -0.0053 1224 GLY B CA  
18291 C C   . GLY B 1226 ? 0.3174 0.3307 0.2877 -0.0041 0.0028  -0.0034 1224 GLY B C   
18292 O O   . GLY B 1226 ? 0.3196 0.3308 0.2869 -0.0072 0.0024  -0.0013 1224 GLY B O   
18293 N N   . GLY B 1227 ? 0.2641 0.2841 0.2403 -0.0031 0.0050  -0.0039 1225 GLY B N   
18294 C CA  . GLY B 1227 ? 0.2588 0.2848 0.2390 -0.0056 0.0069  -0.0022 1225 GLY B CA  
18295 C C   . GLY B 1227 ? 0.2575 0.2896 0.2446 -0.0035 0.0082  -0.0035 1225 GLY B C   
18296 O O   . GLY B 1227 ? 0.2443 0.2756 0.2328 -0.0003 0.0078  -0.0056 1225 GLY B O   
18297 N N   . ASN B 1228 ? 0.2420 0.2803 0.2334 -0.0054 0.0098  -0.0020 1226 ASN B N   
18298 C CA  . ASN B 1228 ? 0.2499 0.2940 0.2480 -0.0038 0.0106  -0.0028 1226 ASN B CA  
18299 C C   . ASN B 1228 ? 0.2859 0.3379 0.2863 -0.0034 0.0142  -0.0018 1226 ASN B C   
18300 O O   . ASN B 1228 ? 0.2846 0.3412 0.2860 -0.0064 0.0155  0.0003  1226 ASN B O   
18301 C CB  . ASN B 1228 ? 0.2715 0.3159 0.2728 -0.0060 0.0088  -0.0021 1226 ASN B CB  
18302 C CG  . ASN B 1228 ? 0.2665 0.3164 0.2744 -0.0044 0.0093  -0.0028 1226 ASN B CG  
18303 O OD1 . ASN B 1228 ? 0.2762 0.3320 0.2870 -0.0027 0.0117  -0.0028 1226 ASN B OD1 
18304 N ND2 . ASN B 1228 ? 0.2560 0.3039 0.2660 -0.0049 0.0071  -0.0033 1226 ASN B ND2 
18305 N N   . ALA B 1229 ? 0.2566 0.3104 0.2580 0.0002  0.0158  -0.0034 1227 ALA B N   
18306 C CA  . ALA B 1229 ? 0.3056 0.3668 0.3089 0.0014  0.0193  -0.0027 1227 ALA B CA  
18307 C C   . ALA B 1229 ? 0.3192 0.3883 0.3290 0.0002  0.0202  -0.0014 1227 ALA B C   
18308 O O   . ALA B 1229 ? 0.2930 0.3690 0.3043 -0.0013 0.0227  0.0003  1227 ALA B O   
18309 C CB  . ALA B 1229 ? 0.3191 0.3796 0.3222 0.0059  0.0204  -0.0050 1227 ALA B CB  
18310 N N   . SER B 1230 ? 0.2940 0.3627 0.3079 0.0008  0.0182  -0.0021 1228 SER B N   
18311 C CA  . SER B 1230 ? 0.2863 0.3623 0.3062 -0.0002 0.0187  -0.0010 1228 SER B CA  
18312 C C   . SER B 1230 ? 0.3320 0.4105 0.3520 -0.0050 0.0184  0.0014  1228 SER B C   
18313 O O   . SER B 1230 ? 0.3159 0.4026 0.3398 -0.0063 0.0201  0.0030  1228 SER B O   
18314 C CB  . SER B 1230 ? 0.3608 0.4346 0.3839 0.0010  0.0163  -0.0022 1228 SER B CB  
18315 O OG  . SER B 1230 ? 0.4671 0.5402 0.4912 0.0052  0.0170  -0.0039 1228 SER B OG  
18316 N N   . LEU B 1231 ? 0.2780 0.3495 0.2937 -0.0077 0.0161  0.0016  1229 LEU B N   
18317 C CA  . LEU B 1231 ? 0.2884 0.3608 0.3034 -0.0126 0.0155  0.0039  1229 LEU B CA  
18318 C C   . LEU B 1231 ? 0.3264 0.4020 0.3387 -0.0147 0.0181  0.0057  1229 LEU B C   
18319 O O   . LEU B 1231 ? 0.3092 0.3874 0.3217 -0.0191 0.0182  0.0079  1229 LEU B O   
18320 C CB  . LEU B 1231 ? 0.2742 0.3373 0.2850 -0.0145 0.0122  0.0035  1229 LEU B CB  
18321 C CG  . LEU B 1231 ? 0.2653 0.3282 0.2795 -0.0156 0.0098  0.0032  1229 LEU B CG  
18322 C CD1 . LEU B 1231 ? 0.3427 0.4086 0.3618 -0.0119 0.0099  0.0015  1229 LEU B CD1 
18323 C CD2 . LEU B 1231 ? 0.2649 0.3183 0.2746 -0.0169 0.0066  0.0026  1229 LEU B CD2 
18324 N N   . MET B 1232 ? 0.3092 0.3847 0.3188 -0.0119 0.0203  0.0050  1230 MET B N   
18325 C CA  . MET B 1232 ? 0.3173 0.3973 0.3248 -0.0137 0.0234  0.0068  1230 MET B CA  
18326 C C   . MET B 1232 ? 0.3529 0.4446 0.3669 -0.0144 0.0259  0.0083  1230 MET B C   
18327 O O   . MET B 1232 ? 0.3363 0.4330 0.3497 -0.0174 0.0282  0.0104  1230 MET B O   
18328 C CB  . MET B 1232 ? 0.3118 0.3894 0.3148 -0.0101 0.0253  0.0054  1230 MET B CB  
18329 C CG  . MET B 1232 ? 0.3150 0.3819 0.3107 -0.0101 0.0230  0.0045  1230 MET B CG  
18330 S SD  . MET B 1232 ? 0.3814 0.4457 0.3723 -0.0054 0.0249  0.0024  1230 MET B SD  
18331 C CE  . MET B 1232 ? 0.3731 0.4439 0.3612 -0.0071 0.0294  0.0046  1230 MET B CE  
18332 N N   . ALA B 1233 ? 0.3223 0.4184 0.3424 -0.0119 0.0256  0.0073  1231 ALA B N   
18333 C CA  . ALA B 1233 ? 0.3568 0.4644 0.3838 -0.0123 0.0276  0.0087  1231 ALA B CA  
18334 C C   . ALA B 1233 ? 0.4467 0.5570 0.4773 -0.0168 0.0254  0.0103  1231 ALA B C   
18335 O O   . ALA B 1233 ? 0.4115 0.5319 0.4481 -0.0177 0.0266  0.0117  1231 ALA B O   
18336 C CB  . ALA B 1233 ? 0.4047 0.5159 0.4361 -0.0068 0.0283  0.0069  1231 ALA B CB  
18337 N N   . ILE B 1234 ? 0.3428 0.4447 0.3699 -0.0196 0.0221  0.0102  1232 ILE B N   
18338 C CA  . ILE B 1234 ? 0.3741 0.4769 0.4039 -0.0236 0.0196  0.0113  1232 ILE B CA  
18339 C C   . ILE B 1234 ? 0.4054 0.5063 0.4314 -0.0294 0.0194  0.0136  1232 ILE B C   
18340 O O   . ILE B 1234 ? 0.4048 0.4959 0.4242 -0.0307 0.0178  0.0134  1232 ILE B O   
18341 C CB  . ILE B 1234 ? 0.3313 0.4259 0.3599 -0.0223 0.0162  0.0094  1232 ILE B CB  
18342 C CG1 . ILE B 1234 ? 0.3743 0.4718 0.4073 -0.0173 0.0164  0.0076  1232 ILE B CG1 
18343 C CG2 . ILE B 1234 ? 0.3235 0.4171 0.3530 -0.0269 0.0134  0.0105  1232 ILE B CG2 
18344 C CD1 . ILE B 1234 ? 0.3173 0.4078 0.3496 -0.0159 0.0134  0.0058  1232 ILE B CD1 
18345 N N   . GLY B 1235 ? 0.3721 0.4821 0.4021 -0.0331 0.0207  0.0159  1233 GLY B N   
18346 C CA  . GLY B 1235 ? 0.3265 0.4354 0.3534 -0.0393 0.0204  0.0184  1233 GLY B CA  
18347 C C   . GLY B 1235 ? 0.3871 0.5022 0.4190 -0.0440 0.0190  0.0200  1233 GLY B C   
18348 O O   . GLY B 1235 ? 0.3068 0.4174 0.3357 -0.0494 0.0169  0.0214  1233 GLY B O   
18349 O OXT . GLY B 1235 ? 0.4202 0.5451 0.4593 -0.0424 0.0196  0.0200  1233 GLY B OXT 
# 
