data_9DL7
# 
_entry.id   9DL7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9DL7         pdb_00009dl7 10.2210/pdb9dl7/pdb 
WWPDB D_1000287796 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DL7 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-10 
_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                 3 
_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 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanner, J.J.' 1 ? 
'Meeks, K.R.'  2 ? 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Molecules 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            29 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-gamma-semialdehyde Dehydrogenase.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/molecules29225408 
_citation.pdbx_database_id_PubMed   39598797 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meeks, K.R.'  1 ? 
primary 'Bogner, A.N.' 2 ? 
primary 'Nix, J.C.'    3 ? 
primary 'Tanner, J.J.' 4 ? 
# 
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 'Bifunctional protein PutA'   131961.656 2    1.5.5.2,1.2.1.88 ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550    2    ?                ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120    8    ?                ? ? ? 
4 non-polymer syn 'TRIETHYLENE GLYCOL'          150.173    2    ?                ? ? ? 
5 non-polymer syn '1-(4-fluorophenyl)thiourea'  170.207    2    ?                ? ? ? 
6 non-polymer syn 'FORMIC ACID'                 46.025     12   ?                ? ? ? 
7 non-polymer syn 'SULFATE ION'                 96.063     26   ?                ? ? ? 
8 water       nat water                         18.015     1498 ?                ? ? ? 
# 
_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 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'DI(HYDROXYETHYL)ETHER'       PEG 
4 'TRIETHYLENE GLYCOL'          PGE 
5 '1-(4-fluorophenyl)thiourea'  8P4 
6 'FORMIC ACID'                 FMT 
7 'SULFATE ION'                 SO4 
8 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, SM11_chr0102' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    SM11 
_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     707241 
_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 
8P4 non-polymer         . '1-(4-fluorophenyl)thiourea'  ? 'C7 H7 F N2 S'      170.207 
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 
FMT non-polymer         . 'FORMIC ACID'                 ? 'C H2 O2'           46.025  
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   14   ALA ALA 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   ?    ?   ?   A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   ?    ?   ?   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  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  ?    ?   ?   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  ?    ?   ?   A . n 
A 1 493  LEU 493  491  ?    ?   ?   A . n 
A 1 494  GLU 494  492  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   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 ?    ?   ?   A . n 
A 1 1227 GLY 1227 1225 ?    ?   ?   A . n 
A 1 1228 ASN 1228 1226 ?    ?   ?   A . n 
A 1 1229 ALA 1229 1227 ?    ?   ?   A . n 
A 1 1230 SER 1230 1228 ?    ?   ?   A . n 
A 1 1231 LEU 1231 1229 ?    ?   ?   A . n 
A 1 1232 MET 1232 1230 ?    ?   ?   A . n 
A 1 1233 ALA 1233 1231 ?    ?   ?   A . n 
A 1 1234 ILE 1234 1232 ?    ?   ?   A . n 
A 1 1235 GLY 1235 1233 ?    ?   ?   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   14   ALA ALA 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   ?    ?   ?   B . n 
B 1 83   GLY 83   81   ?    ?   ?   B . n 
B 1 84   SER 84   82   ?    ?   ?   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  128  GLY GLY 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  ?    ?   ?   B . n 
B 1 138  GLY 138  136  ?    ?   ?   B . n 
B 1 139  SER 139  137  ?    ?   ?   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 ?    ?   ?   B . n 
B 1 1225 ALA 1225 1223 ?    ?   ?   B . n 
B 1 1226 GLY 1226 1224 ?    ?   ?   B . n 
B 1 1227 GLY 1227 1225 ?    ?   ?   B . n 
B 1 1228 ASN 1228 1226 ?    ?   ?   B . n 
B 1 1229 ALA 1229 1227 ?    ?   ?   B . n 
B 1 1230 SER 1230 1228 ?    ?   ?   B . n 
B 1 1231 LEU 1231 1229 ?    ?   ?   B . n 
B 1 1232 MET 1232 1230 ?    ?   ?   B . n 
B 1 1233 ALA 1233 1231 ?    ?   ?   B . n 
B 1 1234 ILE 1234 1232 ?    ?   ?   B . n 
B 1 1235 GLY 1235 1233 ?    ?   ?   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 8P4 ? ? 8P4 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD ? ? FAD ? ? '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 FAD 1   2001 2001 FAD FAD A . 
D  3 PEG 1   2002 2003 PEG PEG A . 
E  4 PGE 1   2003 2004 PGE PGE A . 
F  3 PEG 1   2004 2005 PEG PEG A . 
G  5 8P4 1   2005 2006 8P4 8P4 A . 
H  6 FMT 1   2006 2008 FMT FMT A . 
I  3 PEG 1   2007 2009 PEG PEG A . 
J  6 FMT 1   2008 2010 FMT FMT A . 
K  6 FMT 1   2009 2011 FMT FMT A . 
L  6 FMT 1   2010 2012 FMT FMT A . 
M  6 FMT 1   2011 2013 FMT FMT A . 
N  3 PEG 1   2012 2014 PEG PEG A . 
O  6 FMT 1   2013 2015 FMT FMT A . 
P  6 FMT 1   2014 2010 FMT FMT A . 
Q  7 SO4 1   2015 2    SO4 SO4 A . 
R  7 SO4 1   2016 3    SO4 SO4 A . 
S  7 SO4 1   2017 4    SO4 SO4 A . 
T  7 SO4 1   2018 6    SO4 SO4 A . 
U  7 SO4 1   2019 8    SO4 SO4 A . 
V  7 SO4 1   2020 9    SO4 SO4 A . 
W  7 SO4 1   2021 10   SO4 SO4 A . 
X  7 SO4 1   2022 11   SO4 SO4 A . 
Y  7 SO4 1   2023 12   SO4 SO4 A . 
Z  7 SO4 1   2024 13   SO4 SO4 A . 
AA 7 SO4 1   2025 18   SO4 SO4 A . 
BA 7 SO4 1   2026 21   SO4 SO4 A . 
CA 7 SO4 1   2027 23   SO4 SO4 A . 
DA 7 SO4 1   2028 24   SO4 SO4 A . 
EA 7 SO4 1   2029 26   SO4 SO4 A . 
FA 7 SO4 1   2030 29   SO4 SO4 A . 
GA 2 FAD 1   2001 2001 FAD FAD B . 
HA 4 PGE 1   2002 2002 PGE PGE B . 
IA 3 PEG 1   2003 2003 PEG PEG B . 
JA 3 PEG 1   2004 2005 PEG PEG B . 
KA 5 8P4 1   2005 2006 8P4 8P4 B . 
LA 6 FMT 1   2006 2008 FMT FMT B . 
MA 3 PEG 1   2007 2011 PEG PEG B . 
NA 6 FMT 1   2008 2012 FMT FMT B . 
OA 3 PEG 1   2009 2013 PEG PEG B . 
PA 6 FMT 1   2010 2014 FMT FMT B . 
QA 6 FMT 1   2011 2016 FMT FMT B . 
RA 6 FMT 1   2012 2017 FMT FMT B . 
SA 7 SO4 1   2013 1    SO4 SO4 B . 
TA 7 SO4 1   2014 5    SO4 SO4 B . 
UA 7 SO4 1   2015 7    SO4 SO4 B . 
VA 7 SO4 1   2016 14   SO4 SO4 B . 
WA 7 SO4 1   2017 15   SO4 SO4 B . 
XA 7 SO4 1   2018 16   SO4 SO4 B . 
YA 7 SO4 1   2019 17   SO4 SO4 B . 
ZA 7 SO4 1   2020 20   SO4 SO4 B . 
AB 7 SO4 1   2021 25   SO4 SO4 B . 
BB 7 SO4 1   2022 28   SO4 SO4 B . 
CB 8 HOH 1   2101 1190 HOH HOH A . 
CB 8 HOH 2   2102 596  HOH HOH A . 
CB 8 HOH 3   2103 1288 HOH HOH A . 
CB 8 HOH 4   2104 367  HOH HOH A . 
CB 8 HOH 5   2105 254  HOH HOH A . 
CB 8 HOH 6   2106 965  HOH HOH A . 
CB 8 HOH 7   2107 651  HOH HOH A . 
CB 8 HOH 8   2108 1217 HOH HOH A . 
CB 8 HOH 9   2109 1487 HOH HOH A . 
CB 8 HOH 10  2110 431  HOH HOH A . 
CB 8 HOH 11  2111 1426 HOH HOH A . 
CB 8 HOH 12  2112 353  HOH HOH A . 
CB 8 HOH 13  2113 1311 HOH HOH A . 
CB 8 HOH 14  2114 1566 HOH HOH A . 
CB 8 HOH 15  2115 1095 HOH HOH A . 
CB 8 HOH 16  2116 346  HOH HOH A . 
CB 8 HOH 17  2117 807  HOH HOH A . 
CB 8 HOH 18  2118 969  HOH HOH A . 
CB 8 HOH 19  2119 1077 HOH HOH A . 
CB 8 HOH 20  2120 1654 HOH HOH A . 
CB 8 HOH 21  2121 674  HOH HOH A . 
CB 8 HOH 22  2122 1053 HOH HOH A . 
CB 8 HOH 23  2123 1115 HOH HOH A . 
CB 8 HOH 24  2124 633  HOH HOH A . 
CB 8 HOH 25  2125 1611 HOH HOH A . 
CB 8 HOH 26  2126 602  HOH HOH A . 
CB 8 HOH 27  2127 1010 HOH HOH A . 
CB 8 HOH 28  2128 1376 HOH HOH A . 
CB 8 HOH 29  2129 895  HOH HOH A . 
CB 8 HOH 30  2130 334  HOH HOH A . 
CB 8 HOH 31  2131 617  HOH HOH A . 
CB 8 HOH 32  2132 1139 HOH HOH A . 
CB 8 HOH 33  2133 1175 HOH HOH A . 
CB 8 HOH 34  2134 1069 HOH HOH A . 
CB 8 HOH 35  2135 309  HOH HOH A . 
CB 8 HOH 36  2136 1271 HOH HOH A . 
CB 8 HOH 37  2137 962  HOH HOH A . 
CB 8 HOH 38  2138 704  HOH HOH A . 
CB 8 HOH 39  2139 713  HOH HOH A . 
CB 8 HOH 40  2140 398  HOH HOH A . 
CB 8 HOH 41  2141 1313 HOH HOH A . 
CB 8 HOH 42  2142 928  HOH HOH A . 
CB 8 HOH 43  2143 1498 HOH HOH A . 
CB 8 HOH 44  2144 152  HOH HOH A . 
CB 8 HOH 45  2145 1239 HOH HOH A . 
CB 8 HOH 46  2146 366  HOH HOH A . 
CB 8 HOH 47  2147 1427 HOH HOH A . 
CB 8 HOH 48  2148 165  HOH HOH A . 
CB 8 HOH 49  2149 991  HOH HOH A . 
CB 8 HOH 50  2150 1350 HOH HOH A . 
CB 8 HOH 51  2151 518  HOH HOH A . 
CB 8 HOH 52  2152 133  HOH HOH A . 
CB 8 HOH 53  2153 55   HOH HOH A . 
CB 8 HOH 54  2154 1617 HOH HOH A . 
CB 8 HOH 55  2155 771  HOH HOH A . 
CB 8 HOH 56  2156 82   HOH HOH A . 
CB 8 HOH 57  2157 439  HOH HOH A . 
CB 8 HOH 58  2158 103  HOH HOH A . 
CB 8 HOH 59  2159 816  HOH HOH A . 
CB 8 HOH 60  2160 101  HOH HOH A . 
CB 8 HOH 61  2161 554  HOH HOH A . 
CB 8 HOH 62  2162 114  HOH HOH A . 
CB 8 HOH 63  2163 540  HOH HOH A . 
CB 8 HOH 64  2164 650  HOH HOH A . 
CB 8 HOH 65  2165 192  HOH HOH A . 
CB 8 HOH 66  2166 1297 HOH HOH A . 
CB 8 HOH 67  2167 202  HOH HOH A . 
CB 8 HOH 68  2168 1000 HOH HOH A . 
CB 8 HOH 69  2169 530  HOH HOH A . 
CB 8 HOH 70  2170 661  HOH HOH A . 
CB 8 HOH 71  2171 388  HOH HOH A . 
CB 8 HOH 72  2172 413  HOH HOH A . 
CB 8 HOH 73  2173 1004 HOH HOH A . 
CB 8 HOH 74  2174 778  HOH HOH A . 
CB 8 HOH 75  2175 359  HOH HOH A . 
CB 8 HOH 76  2176 858  HOH HOH A . 
CB 8 HOH 77  2177 1316 HOH HOH A . 
CB 8 HOH 78  2178 502  HOH HOH A . 
CB 8 HOH 79  2179 792  HOH HOH A . 
CB 8 HOH 80  2180 253  HOH HOH A . 
CB 8 HOH 81  2181 606  HOH HOH A . 
CB 8 HOH 82  2182 494  HOH HOH A . 
CB 8 HOH 83  2183 669  HOH HOH A . 
CB 8 HOH 84  2184 1117 HOH HOH A . 
CB 8 HOH 85  2185 887  HOH HOH A . 
CB 8 HOH 86  2186 157  HOH HOH A . 
CB 8 HOH 87  2187 1334 HOH HOH A . 
CB 8 HOH 88  2188 131  HOH HOH A . 
CB 8 HOH 89  2189 323  HOH HOH A . 
CB 8 HOH 90  2190 1500 HOH HOH A . 
CB 8 HOH 91  2191 578  HOH HOH A . 
CB 8 HOH 92  2192 369  HOH HOH A . 
CB 8 HOH 93  2193 377  HOH HOH A . 
CB 8 HOH 94  2194 913  HOH HOH A . 
CB 8 HOH 95  2195 119  HOH HOH A . 
CB 8 HOH 96  2196 424  HOH HOH A . 
CB 8 HOH 97  2197 20   HOH HOH A . 
CB 8 HOH 98  2198 358  HOH HOH A . 
CB 8 HOH 99  2199 106  HOH HOH A . 
CB 8 HOH 100 2200 44   HOH HOH A . 
CB 8 HOH 101 2201 1250 HOH HOH A . 
CB 8 HOH 102 2202 1029 HOH HOH A . 
CB 8 HOH 103 2203 195  HOH HOH A . 
CB 8 HOH 104 2204 140  HOH HOH A . 
CB 8 HOH 105 2205 489  HOH HOH A . 
CB 8 HOH 106 2206 39   HOH HOH A . 
CB 8 HOH 107 2207 1537 HOH HOH A . 
CB 8 HOH 108 2208 910  HOH HOH A . 
CB 8 HOH 109 2209 340  HOH HOH A . 
CB 8 HOH 110 2210 1204 HOH HOH A . 
CB 8 HOH 111 2211 787  HOH HOH A . 
CB 8 HOH 112 2212 63   HOH HOH A . 
CB 8 HOH 113 2213 30   HOH HOH A . 
CB 8 HOH 114 2214 438  HOH HOH A . 
CB 8 HOH 115 2215 837  HOH HOH A . 
CB 8 HOH 116 2216 569  HOH HOH A . 
CB 8 HOH 117 2217 267  HOH HOH A . 
CB 8 HOH 118 2218 638  HOH HOH A . 
CB 8 HOH 119 2219 808  HOH HOH A . 
CB 8 HOH 120 2220 775  HOH HOH A . 
CB 8 HOH 121 2221 764  HOH HOH A . 
CB 8 HOH 122 2222 1121 HOH HOH A . 
CB 8 HOH 123 2223 49   HOH HOH A . 
CB 8 HOH 124 2224 1568 HOH HOH A . 
CB 8 HOH 125 2225 397  HOH HOH A . 
CB 8 HOH 126 2226 1553 HOH HOH A . 
CB 8 HOH 127 2227 1194 HOH HOH A . 
CB 8 HOH 128 2228 402  HOH HOH A . 
CB 8 HOH 129 2229 474  HOH HOH A . 
CB 8 HOH 130 2230 389  HOH HOH A . 
CB 8 HOH 131 2231 1353 HOH HOH A . 
CB 8 HOH 132 2232 825  HOH HOH A . 
CB 8 HOH 133 2233 33   HOH HOH A . 
CB 8 HOH 134 2234 1058 HOH HOH A . 
CB 8 HOH 135 2235 197  HOH HOH A . 
CB 8 HOH 136 2236 1171 HOH HOH A . 
CB 8 HOH 137 2237 1437 HOH HOH A . 
CB 8 HOH 138 2238 61   HOH HOH A . 
CB 8 HOH 139 2239 303  HOH HOH A . 
CB 8 HOH 140 2240 819  HOH HOH A . 
CB 8 HOH 141 2241 100  HOH HOH A . 
CB 8 HOH 142 2242 481  HOH HOH A . 
CB 8 HOH 143 2243 25   HOH HOH A . 
CB 8 HOH 144 2244 1497 HOH HOH A . 
CB 8 HOH 145 2245 1205 HOH HOH A . 
CB 8 HOH 146 2246 566  HOH HOH A . 
CB 8 HOH 147 2247 588  HOH HOH A . 
CB 8 HOH 148 2248 150  HOH HOH A . 
CB 8 HOH 149 2249 676  HOH HOH A . 
CB 8 HOH 150 2250 1616 HOH HOH A . 
CB 8 HOH 151 2251 1252 HOH HOH A . 
CB 8 HOH 152 2252 160  HOH HOH A . 
CB 8 HOH 153 2253 761  HOH HOH A . 
CB 8 HOH 154 2254 746  HOH HOH A . 
CB 8 HOH 155 2255 154  HOH HOH A . 
CB 8 HOH 156 2256 348  HOH HOH A . 
CB 8 HOH 157 2257 238  HOH HOH A . 
CB 8 HOH 158 2258 62   HOH HOH A . 
CB 8 HOH 159 2259 6    HOH HOH A . 
CB 8 HOH 160 2260 147  HOH HOH A . 
CB 8 HOH 161 2261 644  HOH HOH A . 
CB 8 HOH 162 2262 958  HOH HOH A . 
CB 8 HOH 163 2263 710  HOH HOH A . 
CB 8 HOH 164 2264 652  HOH HOH A . 
CB 8 HOH 165 2265 180  HOH HOH A . 
CB 8 HOH 166 2266 1100 HOH HOH A . 
CB 8 HOH 167 2267 1101 HOH HOH A . 
CB 8 HOH 168 2268 813  HOH HOH A . 
CB 8 HOH 169 2269 432  HOH HOH A . 
CB 8 HOH 170 2270 785  HOH HOH A . 
CB 8 HOH 171 2271 1531 HOH HOH A . 
CB 8 HOH 172 2272 1338 HOH HOH A . 
CB 8 HOH 173 2273 225  HOH HOH A . 
CB 8 HOH 174 2274 85   HOH HOH A . 
CB 8 HOH 175 2275 501  HOH HOH A . 
CB 8 HOH 176 2276 191  HOH HOH A . 
CB 8 HOH 177 2277 527  HOH HOH A . 
CB 8 HOH 178 2278 95   HOH HOH A . 
CB 8 HOH 179 2279 115  HOH HOH A . 
CB 8 HOH 180 2280 112  HOH HOH A . 
CB 8 HOH 181 2281 525  HOH HOH A . 
CB 8 HOH 182 2282 48   HOH HOH A . 
CB 8 HOH 183 2283 1622 HOH HOH A . 
CB 8 HOH 184 2284 719  HOH HOH A . 
CB 8 HOH 185 2285 255  HOH HOH A . 
CB 8 HOH 186 2286 80   HOH HOH A . 
CB 8 HOH 187 2287 344  HOH HOH A . 
CB 8 HOH 188 2288 1151 HOH HOH A . 
CB 8 HOH 189 2289 1118 HOH HOH A . 
CB 8 HOH 190 2290 812  HOH HOH A . 
CB 8 HOH 191 2291 261  HOH HOH A . 
CB 8 HOH 192 2292 247  HOH HOH A . 
CB 8 HOH 193 2293 949  HOH HOH A . 
CB 8 HOH 194 2294 460  HOH HOH A . 
CB 8 HOH 195 2295 129  HOH HOH A . 
CB 8 HOH 196 2296 914  HOH HOH A . 
CB 8 HOH 197 2297 341  HOH HOH A . 
CB 8 HOH 198 2298 515  HOH HOH A . 
CB 8 HOH 199 2299 116  HOH HOH A . 
CB 8 HOH 200 2300 1201 HOH HOH A . 
CB 8 HOH 201 2301 681  HOH HOH A . 
CB 8 HOH 202 2302 92   HOH HOH A . 
CB 8 HOH 203 2303 1512 HOH HOH A . 
CB 8 HOH 204 2304 508  HOH HOH A . 
CB 8 HOH 205 2305 41   HOH HOH A . 
CB 8 HOH 206 2306 88   HOH HOH A . 
CB 8 HOH 207 2307 791  HOH HOH A . 
CB 8 HOH 208 2308 563  HOH HOH A . 
CB 8 HOH 209 2309 680  HOH HOH A . 
CB 8 HOH 210 2310 639  HOH HOH A . 
CB 8 HOH 211 2311 1192 HOH HOH A . 
CB 8 HOH 212 2312 762  HOH HOH A . 
CB 8 HOH 213 2313 32   HOH HOH A . 
CB 8 HOH 214 2314 308  HOH HOH A . 
CB 8 HOH 215 2315 246  HOH HOH A . 
CB 8 HOH 216 2316 1452 HOH HOH A . 
CB 8 HOH 217 2317 322  HOH HOH A . 
CB 8 HOH 218 2318 320  HOH HOH A . 
CB 8 HOH 219 2319 107  HOH HOH A . 
CB 8 HOH 220 2320 929  HOH HOH A . 
CB 8 HOH 221 2321 113  HOH HOH A . 
CB 8 HOH 222 2322 616  HOH HOH A . 
CB 8 HOH 223 2323 478  HOH HOH A . 
CB 8 HOH 224 2324 1354 HOH HOH A . 
CB 8 HOH 225 2325 368  HOH HOH A . 
CB 8 HOH 226 2326 370  HOH HOH A . 
CB 8 HOH 227 2327 235  HOH HOH A . 
CB 8 HOH 228 2328 12   HOH HOH A . 
CB 8 HOH 229 2329 60   HOH HOH A . 
CB 8 HOH 230 2330 947  HOH HOH A . 
CB 8 HOH 231 2331 186  HOH HOH A . 
CB 8 HOH 232 2332 296  HOH HOH A . 
CB 8 HOH 233 2333 144  HOH HOH A . 
CB 8 HOH 234 2334 153  HOH HOH A . 
CB 8 HOH 235 2335 1538 HOH HOH A . 
CB 8 HOH 236 2336 1062 HOH HOH A . 
CB 8 HOH 237 2337 782  HOH HOH A . 
CB 8 HOH 238 2338 1634 HOH HOH A . 
CB 8 HOH 239 2339 87   HOH HOH A . 
CB 8 HOH 240 2340 663  HOH HOH A . 
CB 8 HOH 241 2341 935  HOH HOH A . 
CB 8 HOH 242 2342 934  HOH HOH A . 
CB 8 HOH 243 2343 237  HOH HOH A . 
CB 8 HOH 244 2344 1451 HOH HOH A . 
CB 8 HOH 245 2345 1078 HOH HOH A . 
CB 8 HOH 246 2346 1464 HOH HOH A . 
CB 8 HOH 247 2347 155  HOH HOH A . 
CB 8 HOH 248 2348 302  HOH HOH A . 
CB 8 HOH 249 2349 675  HOH HOH A . 
CB 8 HOH 250 2350 74   HOH HOH A . 
CB 8 HOH 251 2351 788  HOH HOH A . 
CB 8 HOH 252 2352 1279 HOH HOH A . 
CB 8 HOH 253 2353 646  HOH HOH A . 
CB 8 HOH 254 2354 821  HOH HOH A . 
CB 8 HOH 255 2355 834  HOH HOH A . 
CB 8 HOH 256 2356 124  HOH HOH A . 
CB 8 HOH 257 2357 454  HOH HOH A . 
CB 8 HOH 258 2358 715  HOH HOH A . 
CB 8 HOH 259 2359 16   HOH HOH A . 
CB 8 HOH 260 2360 1208 HOH HOH A . 
CB 8 HOH 261 2361 637  HOH HOH A . 
CB 8 HOH 262 2362 1331 HOH HOH A . 
CB 8 HOH 263 2363 936  HOH HOH A . 
CB 8 HOH 264 2364 848  HOH HOH A . 
CB 8 HOH 265 2365 600  HOH HOH A . 
CB 8 HOH 266 2366 1187 HOH HOH A . 
CB 8 HOH 267 2367 380  HOH HOH A . 
CB 8 HOH 268 2368 264  HOH HOH A . 
CB 8 HOH 269 2369 332  HOH HOH A . 
CB 8 HOH 270 2370 274  HOH HOH A . 
CB 8 HOH 271 2371 1307 HOH HOH A . 
CB 8 HOH 272 2372 215  HOH HOH A . 
CB 8 HOH 273 2373 466  HOH HOH A . 
CB 8 HOH 274 2374 1523 HOH HOH A . 
CB 8 HOH 275 2375 193  HOH HOH A . 
CB 8 HOH 276 2376 1247 HOH HOH A . 
CB 8 HOH 277 2377 673  HOH HOH A . 
CB 8 HOH 278 2378 99   HOH HOH A . 
CB 8 HOH 279 2379 72   HOH HOH A . 
CB 8 HOH 280 2380 917  HOH HOH A . 
CB 8 HOH 281 2381 483  HOH HOH A . 
CB 8 HOH 282 2382 557  HOH HOH A . 
CB 8 HOH 283 2383 479  HOH HOH A . 
CB 8 HOH 284 2384 1367 HOH HOH A . 
CB 8 HOH 285 2385 121  HOH HOH A . 
CB 8 HOH 286 2386 899  HOH HOH A . 
CB 8 HOH 287 2387 718  HOH HOH A . 
CB 8 HOH 288 2388 1016 HOH HOH A . 
CB 8 HOH 289 2389 898  HOH HOH A . 
CB 8 HOH 290 2390 937  HOH HOH A . 
CB 8 HOH 291 2391 570  HOH HOH A . 
CB 8 HOH 292 2392 838  HOH HOH A . 
CB 8 HOH 293 2393 231  HOH HOH A . 
CB 8 HOH 294 2394 243  HOH HOH A . 
CB 8 HOH 295 2395 53   HOH HOH A . 
CB 8 HOH 296 2396 622  HOH HOH A . 
CB 8 HOH 297 2397 360  HOH HOH A . 
CB 8 HOH 298 2398 68   HOH HOH A . 
CB 8 HOH 299 2399 181  HOH HOH A . 
CB 8 HOH 300 2400 797  HOH HOH A . 
CB 8 HOH 301 2401 990  HOH HOH A . 
CB 8 HOH 302 2402 384  HOH HOH A . 
CB 8 HOH 303 2403 1018 HOH HOH A . 
CB 8 HOH 304 2404 698  HOH HOH A . 
CB 8 HOH 305 2405 159  HOH HOH A . 
CB 8 HOH 306 2406 740  HOH HOH A . 
CB 8 HOH 307 2407 260  HOH HOH A . 
CB 8 HOH 308 2408 612  HOH HOH A . 
CB 8 HOH 309 2409 394  HOH HOH A . 
CB 8 HOH 310 2410 804  HOH HOH A . 
CB 8 HOH 311 2411 1150 HOH HOH A . 
CB 8 HOH 312 2412 434  HOH HOH A . 
CB 8 HOH 313 2413 495  HOH HOH A . 
CB 8 HOH 314 2414 176  HOH HOH A . 
CB 8 HOH 315 2415 451  HOH HOH A . 
CB 8 HOH 316 2416 531  HOH HOH A . 
CB 8 HOH 317 2417 924  HOH HOH A . 
CB 8 HOH 318 2418 523  HOH HOH A . 
CB 8 HOH 319 2419 964  HOH HOH A . 
CB 8 HOH 320 2420 528  HOH HOH A . 
CB 8 HOH 321 2421 75   HOH HOH A . 
CB 8 HOH 322 2422 1049 HOH HOH A . 
CB 8 HOH 323 2423 1161 HOH HOH A . 
CB 8 HOH 324 2424 822  HOH HOH A . 
CB 8 HOH 325 2425 705  HOH HOH A . 
CB 8 HOH 326 2426 817  HOH HOH A . 
CB 8 HOH 327 2427 647  HOH HOH A . 
CB 8 HOH 328 2428 453  HOH HOH A . 
CB 8 HOH 329 2429 91   HOH HOH A . 
CB 8 HOH 330 2430 1280 HOH HOH A . 
CB 8 HOH 331 2431 333  HOH HOH A . 
CB 8 HOH 332 2432 22   HOH HOH A . 
CB 8 HOH 333 2433 976  HOH HOH A . 
CB 8 HOH 334 2434 995  HOH HOH A . 
CB 8 HOH 335 2435 1128 HOH HOH A . 
CB 8 HOH 336 2436 654  HOH HOH A . 
CB 8 HOH 337 2437 542  HOH HOH A . 
CB 8 HOH 338 2438 1260 HOH HOH A . 
CB 8 HOH 339 2439 997  HOH HOH A . 
CB 8 HOH 340 2440 537  HOH HOH A . 
CB 8 HOH 341 2441 362  HOH HOH A . 
CB 8 HOH 342 2442 615  HOH HOH A . 
CB 8 HOH 343 2443 290  HOH HOH A . 
CB 8 HOH 344 2444 467  HOH HOH A . 
CB 8 HOH 345 2445 1557 HOH HOH A . 
CB 8 HOH 346 2446 158  HOH HOH A . 
CB 8 HOH 347 2447 459  HOH HOH A . 
CB 8 HOH 348 2448 184  HOH HOH A . 
CB 8 HOH 349 2449 627  HOH HOH A . 
CB 8 HOH 350 2450 529  HOH HOH A . 
CB 8 HOH 351 2451 728  HOH HOH A . 
CB 8 HOH 352 2452 104  HOH HOH A . 
CB 8 HOH 353 2453 513  HOH HOH A . 
CB 8 HOH 354 2454 375  HOH HOH A . 
CB 8 HOH 355 2455 921  HOH HOH A . 
CB 8 HOH 356 2456 516  HOH HOH A . 
CB 8 HOH 357 2457 605  HOH HOH A . 
CB 8 HOH 358 2458 737  HOH HOH A . 
CB 8 HOH 359 2459 108  HOH HOH A . 
CB 8 HOH 360 2460 357  HOH HOH A . 
CB 8 HOH 361 2461 993  HOH HOH A . 
CB 8 HOH 362 2462 841  HOH HOH A . 
CB 8 HOH 363 2463 607  HOH HOH A . 
CB 8 HOH 364 2464 932  HOH HOH A . 
CB 8 HOH 365 2465 559  HOH HOH A . 
CB 8 HOH 366 2466 696  HOH HOH A . 
CB 8 HOH 367 2467 1605 HOH HOH A . 
CB 8 HOH 368 2468 149  HOH HOH A . 
CB 8 HOH 369 2469 352  HOH HOH A . 
CB 8 HOH 370 2470 425  HOH HOH A . 
CB 8 HOH 371 2471 543  HOH HOH A . 
CB 8 HOH 372 2472 1433 HOH HOH A . 
CB 8 HOH 373 2473 310  HOH HOH A . 
CB 8 HOH 374 2474 31   HOH HOH A . 
CB 8 HOH 375 2475 59   HOH HOH A . 
CB 8 HOH 376 2476 1488 HOH HOH A . 
CB 8 HOH 377 2477 978  HOH HOH A . 
CB 8 HOH 378 2478 278  HOH HOH A . 
CB 8 HOH 379 2479 328  HOH HOH A . 
CB 8 HOH 380 2480 1385 HOH HOH A . 
CB 8 HOH 381 2481 229  HOH HOH A . 
CB 8 HOH 382 2482 998  HOH HOH A . 
CB 8 HOH 383 2483 26   HOH HOH A . 
CB 8 HOH 384 2484 1214 HOH HOH A . 
CB 8 HOH 385 2485 536  HOH HOH A . 
CB 8 HOH 386 2486 532  HOH HOH A . 
CB 8 HOH 387 2487 315  HOH HOH A . 
CB 8 HOH 388 2488 1570 HOH HOH A . 
CB 8 HOH 389 2489 941  HOH HOH A . 
CB 8 HOH 390 2490 1057 HOH HOH A . 
CB 8 HOH 391 2491 1110 HOH HOH A . 
CB 8 HOH 392 2492 17   HOH HOH A . 
CB 8 HOH 393 2493 774  HOH HOH A . 
CB 8 HOH 394 2494 381  HOH HOH A . 
CB 8 HOH 395 2495 1138 HOH HOH A . 
CB 8 HOH 396 2496 768  HOH HOH A . 
CB 8 HOH 397 2497 299  HOH HOH A . 
CB 8 HOH 398 2498 1184 HOH HOH A . 
CB 8 HOH 399 2499 405  HOH HOH A . 
CB 8 HOH 400 2500 199  HOH HOH A . 
CB 8 HOH 401 2501 428  HOH HOH A . 
CB 8 HOH 402 2502 441  HOH HOH A . 
CB 8 HOH 403 2503 820  HOH HOH A . 
CB 8 HOH 404 2504 470  HOH HOH A . 
CB 8 HOH 405 2505 1174 HOH HOH A . 
CB 8 HOH 406 2506 34   HOH HOH A . 
CB 8 HOH 407 2507 989  HOH HOH A . 
CB 8 HOH 408 2508 977  HOH HOH A . 
CB 8 HOH 409 2509 1509 HOH HOH A . 
CB 8 HOH 410 2510 1149 HOH HOH A . 
CB 8 HOH 411 2511 1340 HOH HOH A . 
CB 8 HOH 412 2512 292  HOH HOH A . 
CB 8 HOH 413 2513 423  HOH HOH A . 
CB 8 HOH 414 2514 1076 HOH HOH A . 
CB 8 HOH 415 2515 421  HOH HOH A . 
CB 8 HOH 416 2516 220  HOH HOH A . 
CB 8 HOH 417 2517 347  HOH HOH A . 
CB 8 HOH 418 2518 141  HOH HOH A . 
CB 8 HOH 419 2519 849  HOH HOH A . 
CB 8 HOH 420 2520 265  HOH HOH A . 
CB 8 HOH 421 2521 1373 HOH HOH A . 
CB 8 HOH 422 2522 850  HOH HOH A . 
CB 8 HOH 423 2523 1130 HOH HOH A . 
CB 8 HOH 424 2524 1525 HOH HOH A . 
CB 8 HOH 425 2525 918  HOH HOH A . 
CB 8 HOH 426 2526 1438 HOH HOH A . 
CB 8 HOH 427 2527 23   HOH HOH A . 
CB 8 HOH 428 2528 312  HOH HOH A . 
CB 8 HOH 429 2529 456  HOH HOH A . 
CB 8 HOH 430 2530 1267 HOH HOH A . 
CB 8 HOH 431 2531 118  HOH HOH A . 
CB 8 HOH 432 2532 901  HOH HOH A . 
CB 8 HOH 433 2533 232  HOH HOH A . 
CB 8 HOH 434 2534 620  HOH HOH A . 
CB 8 HOH 435 2535 148  HOH HOH A . 
CB 8 HOH 436 2536 204  HOH HOH A . 
CB 8 HOH 437 2537 878  HOH HOH A . 
CB 8 HOH 438 2538 46   HOH HOH A . 
CB 8 HOH 439 2539 593  HOH HOH A . 
CB 8 HOH 440 2540 1185 HOH HOH A . 
CB 8 HOH 441 2541 1227 HOH HOH A . 
CB 8 HOH 442 2542 1637 HOH HOH A . 
CB 8 HOH 443 2543 824  HOH HOH A . 
CB 8 HOH 444 2544 151  HOH HOH A . 
CB 8 HOH 445 2545 514  HOH HOH A . 
CB 8 HOH 446 2546 390  HOH HOH A . 
CB 8 HOH 447 2547 477  HOH HOH A . 
CB 8 HOH 448 2548 1410 HOH HOH A . 
CB 8 HOH 449 2549 1454 HOH HOH A . 
CB 8 HOH 450 2550 64   HOH HOH A . 
CB 8 HOH 451 2551 1309 HOH HOH A . 
CB 8 HOH 452 2552 226  HOH HOH A . 
CB 8 HOH 453 2553 86   HOH HOH A . 
CB 8 HOH 454 2554 137  HOH HOH A . 
CB 8 HOH 455 2555 597  HOH HOH A . 
CB 8 HOH 456 2556 94   HOH HOH A . 
CB 8 HOH 457 2557 1650 HOH HOH A . 
CB 8 HOH 458 2558 1477 HOH HOH A . 
CB 8 HOH 459 2559 170  HOH HOH A . 
CB 8 HOH 460 2560 442  HOH HOH A . 
CB 8 HOH 461 2561 1318 HOH HOH A . 
CB 8 HOH 462 2562 556  HOH HOH A . 
CB 8 HOH 463 2563 24   HOH HOH A . 
CB 8 HOH 464 2564 1182 HOH HOH A . 
CB 8 HOH 465 2565 682  HOH HOH A . 
CB 8 HOH 466 2566 66   HOH HOH A . 
CB 8 HOH 467 2567 482  HOH HOH A . 
CB 8 HOH 468 2568 979  HOH HOH A . 
CB 8 HOH 469 2569 610  HOH HOH A . 
CB 8 HOH 470 2570 221  HOH HOH A . 
CB 8 HOH 471 2571 946  HOH HOH A . 
CB 8 HOH 472 2572 445  HOH HOH A . 
CB 8 HOH 473 2573 579  HOH HOH A . 
CB 8 HOH 474 2574 1314 HOH HOH A . 
CB 8 HOH 475 2575 872  HOH HOH A . 
CB 8 HOH 476 2576 522  HOH HOH A . 
CB 8 HOH 477 2577 833  HOH HOH A . 
CB 8 HOH 478 2578 440  HOH HOH A . 
CB 8 HOH 479 2579 511  HOH HOH A . 
CB 8 HOH 480 2580 925  HOH HOH A . 
CB 8 HOH 481 2581 392  HOH HOH A . 
CB 8 HOH 482 2582 1202 HOH HOH A . 
CB 8 HOH 483 2583 1536 HOH HOH A . 
CB 8 HOH 484 2584 1384 HOH HOH A . 
CB 8 HOH 485 2585 444  HOH HOH A . 
CB 8 HOH 486 2586 378  HOH HOH A . 
CB 8 HOH 487 2587 580  HOH HOH A . 
CB 8 HOH 488 2588 986  HOH HOH A . 
CB 8 HOH 489 2589 386  HOH HOH A . 
CB 8 HOH 490 2590 161  HOH HOH A . 
CB 8 HOH 491 2591 43   HOH HOH A . 
CB 8 HOH 492 2592 1441 HOH HOH A . 
CB 8 HOH 493 2593 342  HOH HOH A . 
CB 8 HOH 494 2594 500  HOH HOH A . 
CB 8 HOH 495 2595 1037 HOH HOH A . 
CB 8 HOH 496 2596 145  HOH HOH A . 
CB 8 HOH 497 2597 447  HOH HOH A . 
CB 8 HOH 498 2598 801  HOH HOH A . 
CB 8 HOH 499 2599 135  HOH HOH A . 
CB 8 HOH 500 2600 1294 HOH HOH A . 
CB 8 HOH 501 2601 213  HOH HOH A . 
CB 8 HOH 502 2602 1097 HOH HOH A . 
CB 8 HOH 503 2603 1436 HOH HOH A . 
CB 8 HOH 504 2604 721  HOH HOH A . 
CB 8 HOH 505 2605 490  HOH HOH A . 
CB 8 HOH 506 2606 911  HOH HOH A . 
CB 8 HOH 507 2607 240  HOH HOH A . 
CB 8 HOH 508 2608 224  HOH HOH A . 
CB 8 HOH 509 2609 956  HOH HOH A . 
CB 8 HOH 510 2610 1249 HOH HOH A . 
CB 8 HOH 511 2611 69   HOH HOH A . 
CB 8 HOH 512 2612 1273 HOH HOH A . 
CB 8 HOH 513 2613 1006 HOH HOH A . 
CB 8 HOH 514 2614 385  HOH HOH A . 
CB 8 HOH 515 2615 642  HOH HOH A . 
CB 8 HOH 516 2616 1519 HOH HOH A . 
CB 8 HOH 517 2617 659  HOH HOH A . 
CB 8 HOH 518 2618 503  HOH HOH A . 
CB 8 HOH 519 2619 462  HOH HOH A . 
CB 8 HOH 520 2620 955  HOH HOH A . 
CB 8 HOH 521 2621 298  HOH HOH A . 
CB 8 HOH 522 2622 504  HOH HOH A . 
CB 8 HOH 523 2623 1209 HOH HOH A . 
CB 8 HOH 524 2624 1370 HOH HOH A . 
CB 8 HOH 525 2625 383  HOH HOH A . 
CB 8 HOH 526 2626 541  HOH HOH A . 
CB 8 HOH 527 2627 552  HOH HOH A . 
CB 8 HOH 528 2628 1423 HOH HOH A . 
CB 8 HOH 529 2629 1506 HOH HOH A . 
CB 8 HOH 530 2630 214  HOH HOH A . 
CB 8 HOH 531 2631 1515 HOH HOH A . 
CB 8 HOH 532 2632 1399 HOH HOH A . 
CB 8 HOH 533 2633 908  HOH HOH A . 
CB 8 HOH 534 2634 575  HOH HOH A . 
CB 8 HOH 535 2635 697  HOH HOH A . 
CB 8 HOH 536 2636 382  HOH HOH A . 
CB 8 HOH 537 2637 1013 HOH HOH A . 
CB 8 HOH 538 2638 1651 HOH HOH A . 
CB 8 HOH 539 2639 1093 HOH HOH A . 
CB 8 HOH 540 2640 1387 HOH HOH A . 
CB 8 HOH 541 2641 1173 HOH HOH A . 
CB 8 HOH 542 2642 164  HOH HOH A . 
CB 8 HOH 543 2643 313  HOH HOH A . 
CB 8 HOH 544 2644 409  HOH HOH A . 
CB 8 HOH 545 2645 1015 HOH HOH A . 
CB 8 HOH 546 2646 1596 HOH HOH A . 
CB 8 HOH 547 2647 1323 HOH HOH A . 
CB 8 HOH 548 2648 455  HOH HOH A . 
CB 8 HOH 549 2649 1460 HOH HOH A . 
CB 8 HOH 550 2650 758  HOH HOH A . 
CB 8 HOH 551 2651 1499 HOH HOH A . 
CB 8 HOH 552 2652 581  HOH HOH A . 
CB 8 HOH 553 2653 827  HOH HOH A . 
CB 8 HOH 554 2654 280  HOH HOH A . 
CB 8 HOH 555 2655 873  HOH HOH A . 
CB 8 HOH 556 2656 794  HOH HOH A . 
CB 8 HOH 557 2657 1413 HOH HOH A . 
CB 8 HOH 558 2658 609  HOH HOH A . 
CB 8 HOH 559 2659 379  HOH HOH A . 
CB 8 HOH 560 2660 480  HOH HOH A . 
CB 8 HOH 561 2661 636  HOH HOH A . 
CB 8 HOH 562 2662 268  HOH HOH A . 
CB 8 HOH 563 2663 1556 HOH HOH A . 
CB 8 HOH 564 2664 912  HOH HOH A . 
CB 8 HOH 565 2665 1450 HOH HOH A . 
CB 8 HOH 566 2666 558  HOH HOH A . 
CB 8 HOH 567 2667 727  HOH HOH A . 
CB 8 HOH 568 2668 649  HOH HOH A . 
CB 8 HOH 569 2669 671  HOH HOH A . 
CB 8 HOH 570 2670 707  HOH HOH A . 
CB 8 HOH 571 2671 832  HOH HOH A . 
CB 8 HOH 572 2672 975  HOH HOH A . 
CB 8 HOH 573 2673 1281 HOH HOH A . 
CB 8 HOH 574 2674 21   HOH HOH A . 
CB 8 HOH 575 2675 1111 HOH HOH A . 
CB 8 HOH 576 2676 885  HOH HOH A . 
CB 8 HOH 577 2677 664  HOH HOH A . 
CB 8 HOH 578 2678 1332 HOH HOH A . 
CB 8 HOH 579 2679 1197 HOH HOH A . 
CB 8 HOH 580 2680 626  HOH HOH A . 
CB 8 HOH 581 2681 1599 HOH HOH A . 
CB 8 HOH 582 2682 396  HOH HOH A . 
CB 8 HOH 583 2683 449  HOH HOH A . 
CB 8 HOH 584 2684 1292 HOH HOH A . 
CB 8 HOH 585 2685 843  HOH HOH A . 
CB 8 HOH 586 2686 1507 HOH HOH A . 
CB 8 HOH 587 2687 1156 HOH HOH A . 
CB 8 HOH 588 2688 1391 HOH HOH A . 
CB 8 HOH 589 2689 1256 HOH HOH A . 
CB 8 HOH 590 2690 1364 HOH HOH A . 
CB 8 HOH 591 2691 1299 HOH HOH A . 
CB 8 HOH 592 2692 276  HOH HOH A . 
CB 8 HOH 593 2693 1587 HOH HOH A . 
CB 8 HOH 594 2694 1346 HOH HOH A . 
CB 8 HOH 595 2695 1625 HOH HOH A . 
CB 8 HOH 596 2696 1244 HOH HOH A . 
CB 8 HOH 597 2697 1246 HOH HOH A . 
CB 8 HOH 598 2698 1609 HOH HOH A . 
CB 8 HOH 599 2699 194  HOH HOH A . 
CB 8 HOH 600 2700 1088 HOH HOH A . 
CB 8 HOH 601 2701 219  HOH HOH A . 
CB 8 HOH 602 2702 940  HOH HOH A . 
CB 8 HOH 603 2703 1120 HOH HOH A . 
CB 8 HOH 604 2704 1620 HOH HOH A . 
CB 8 HOH 605 2705 679  HOH HOH A . 
CB 8 HOH 606 2706 829  HOH HOH A . 
CB 8 HOH 607 2707 244  HOH HOH A . 
CB 8 HOH 608 2708 1439 HOH HOH A . 
CB 8 HOH 609 2709 1430 HOH HOH A . 
CB 8 HOH 610 2710 1278 HOH HOH A . 
CB 8 HOH 611 2711 1141 HOH HOH A . 
CB 8 HOH 612 2712 1565 HOH HOH A . 
CB 8 HOH 613 2713 711  HOH HOH A . 
CB 8 HOH 614 2714 343  HOH HOH A . 
CB 8 HOH 615 2715 686  HOH HOH A . 
CB 8 HOH 616 2716 1333 HOH HOH A . 
CB 8 HOH 617 2717 757  HOH HOH A . 
CB 8 HOH 618 2718 1063 HOH HOH A . 
CB 8 HOH 619 2719 1237 HOH HOH A . 
CB 8 HOH 620 2720 1388 HOH HOH A . 
CB 8 HOH 621 2721 1082 HOH HOH A . 
CB 8 HOH 622 2722 1343 HOH HOH A . 
CB 8 HOH 623 2723 1482 HOH HOH A . 
CB 8 HOH 624 2724 1306 HOH HOH A . 
CB 8 HOH 625 2725 798  HOH HOH A . 
CB 8 HOH 626 2726 922  HOH HOH A . 
CB 8 HOH 627 2727 863  HOH HOH A . 
CB 8 HOH 628 2728 1429 HOH HOH A . 
CB 8 HOH 629 2729 1025 HOH HOH A . 
CB 8 HOH 630 2730 371  HOH HOH A . 
CB 8 HOH 631 2731 1560 HOH HOH A . 
CB 8 HOH 632 2732 1593 HOH HOH A . 
CB 8 HOH 633 2733 1511 HOH HOH A . 
CB 8 HOH 634 2734 1458 HOH HOH A . 
CB 8 HOH 635 2735 1012 HOH HOH A . 
CB 8 HOH 636 2736 1563 HOH HOH A . 
CB 8 HOH 637 2737 1147 HOH HOH A . 
CB 8 HOH 638 2738 1096 HOH HOH A . 
CB 8 HOH 639 2739 1510 HOH HOH A . 
CB 8 HOH 640 2740 909  HOH HOH A . 
CB 8 HOH 641 2741 1041 HOH HOH A . 
CB 8 HOH 642 2742 1603 HOH HOH A . 
CB 8 HOH 643 2743 1264 HOH HOH A . 
CB 8 HOH 644 2744 571  HOH HOH A . 
CB 8 HOH 645 2745 364  HOH HOH A . 
CB 8 HOH 646 2746 1418 HOH HOH A . 
CB 8 HOH 647 2747 662  HOH HOH A . 
CB 8 HOH 648 2748 951  HOH HOH A . 
CB 8 HOH 649 2749 1545 HOH HOH A . 
CB 8 HOH 650 2750 1546 HOH HOH A . 
CB 8 HOH 651 2751 457  HOH HOH A . 
CB 8 HOH 652 2752 1629 HOH HOH A . 
CB 8 HOH 653 2753 1241 HOH HOH A . 
CB 8 HOH 654 2754 1255 HOH HOH A . 
CB 8 HOH 655 2755 847  HOH HOH A . 
CB 8 HOH 656 2756 1479 HOH HOH A . 
CB 8 HOH 657 2757 1291 HOH HOH A . 
CB 8 HOH 658 2758 1296 HOH HOH A . 
CB 8 HOH 659 2759 811  HOH HOH A . 
CB 8 HOH 660 2760 1275 HOH HOH A . 
CB 8 HOH 661 2761 488  HOH HOH A . 
CB 8 HOH 662 2762 1457 HOH HOH A . 
CB 8 HOH 663 2763 1181 HOH HOH A . 
CB 8 HOH 664 2764 994  HOH HOH A . 
CB 8 HOH 665 2765 1623 HOH HOH A . 
CB 8 HOH 666 2766 1098 HOH HOH A . 
CB 8 HOH 667 2767 1134 HOH HOH A . 
CB 8 HOH 668 2768 1293 HOH HOH A . 
CB 8 HOH 669 2769 1355 HOH HOH A . 
CB 8 HOH 670 2770 1312 HOH HOH A . 
CB 8 HOH 671 2771 1186 HOH HOH A . 
CB 8 HOH 672 2772 1050 HOH HOH A . 
CB 8 HOH 673 2773 793  HOH HOH A . 
CB 8 HOH 674 2774 857  HOH HOH A . 
CB 8 HOH 675 2775 640  HOH HOH A . 
CB 8 HOH 676 2776 1524 HOH HOH A . 
CB 8 HOH 677 2777 1153 HOH HOH A . 
CB 8 HOH 678 2778 1206 HOH HOH A . 
CB 8 HOH 679 2779 987  HOH HOH A . 
CB 8 HOH 680 2780 598  HOH HOH A . 
CB 8 HOH 681 2781 1257 HOH HOH A . 
CB 8 HOH 682 2782 1245 HOH HOH A . 
CB 8 HOH 683 2783 1133 HOH HOH A . 
CB 8 HOH 684 2784 486  HOH HOH A . 
CB 8 HOH 685 2785 463  HOH HOH A . 
CB 8 HOH 686 2786 1146 HOH HOH A . 
CB 8 HOH 687 2787 1610 HOH HOH A . 
CB 8 HOH 688 2788 395  HOH HOH A . 
CB 8 HOH 689 2789 1223 HOH HOH A . 
CB 8 HOH 690 2790 1645 HOH HOH A . 
CB 8 HOH 691 2791 1091 HOH HOH A . 
CB 8 HOH 692 2792 179  HOH HOH A . 
CB 8 HOH 693 2793 690  HOH HOH A . 
CB 8 HOH 694 2794 1263 HOH HOH A . 
CB 8 HOH 695 2795 1586 HOH HOH A . 
CB 8 HOH 696 2796 1232 HOH HOH A . 
CB 8 HOH 697 2797 1656 HOH HOH A . 
CB 8 HOH 698 2798 1369 HOH HOH A . 
CB 8 HOH 699 2799 625  HOH HOH A . 
CB 8 HOH 700 2800 1324 HOH HOH A . 
CB 8 HOH 701 2801 933  HOH HOH A . 
CB 8 HOH 702 2802 1109 HOH HOH A . 
CB 8 HOH 703 2803 1020 HOH HOH A . 
CB 8 HOH 704 2804 1501 HOH HOH A . 
CB 8 HOH 705 2805 1644 HOH HOH A . 
CB 8 HOH 706 2806 1514 HOH HOH A . 
CB 8 HOH 707 2807 1386 HOH HOH A . 
CB 8 HOH 708 2808 1183 HOH HOH A . 
CB 8 HOH 709 2809 415  HOH HOH A . 
CB 8 HOH 710 2810 1508 HOH HOH A . 
CB 8 HOH 711 2811 561  HOH HOH A . 
CB 8 HOH 712 2812 971  HOH HOH A . 
CB 8 HOH 713 2813 1642 HOH HOH A . 
CB 8 HOH 714 2814 1158 HOH HOH A . 
CB 8 HOH 715 2815 230  HOH HOH A . 
CB 8 HOH 716 2816 1579 HOH HOH A . 
CB 8 HOH 717 2817 1612 HOH HOH A . 
CB 8 HOH 718 2818 1191 HOH HOH A . 
CB 8 HOH 719 2819 844  HOH HOH A . 
CB 8 HOH 720 2820 1559 HOH HOH A . 
CB 8 HOH 721 2821 842  HOH HOH A . 
CB 8 HOH 722 2822 1600 HOH HOH A . 
CB 8 HOH 723 2823 1231 HOH HOH A . 
CB 8 HOH 724 2824 1123 HOH HOH A . 
CB 8 HOH 725 2825 1160 HOH HOH A . 
CB 8 HOH 726 2826 1113 HOH HOH A . 
CB 8 HOH 727 2827 1155 HOH HOH A . 
CB 8 HOH 728 2828 1061 HOH HOH A . 
CB 8 HOH 729 2829 1640 HOH HOH A . 
CB 8 HOH 730 2830 1392 HOH HOH A . 
CB 8 HOH 731 2831 1503 HOH HOH A . 
CB 8 HOH 732 2832 1027 HOH HOH A . 
CB 8 HOH 733 2833 1295 HOH HOH A . 
CB 8 HOH 734 2834 1262 HOH HOH A . 
CB 8 HOH 735 2835 1289 HOH HOH A . 
CB 8 HOH 736 2836 1132 HOH HOH A . 
CB 8 HOH 737 2837 1572 HOH HOH A . 
CB 8 HOH 738 2838 1059 HOH HOH A . 
CB 8 HOH 739 2839 750  HOH HOH A . 
CB 8 HOH 740 2840 1456 HOH HOH A . 
CB 8 HOH 741 2841 524  HOH HOH A . 
CB 8 HOH 742 2842 1421 HOH HOH A . 
CB 8 HOH 743 2843 1080 HOH HOH A . 
CB 8 HOH 744 2844 491  HOH HOH A . 
CB 8 HOH 745 2845 695  HOH HOH A . 
CB 8 HOH 746 2846 944  HOH HOH A . 
CB 8 HOH 747 2847 835  HOH HOH A . 
CB 8 HOH 748 2848 1070 HOH HOH A . 
CB 8 HOH 749 2849 691  HOH HOH A . 
CB 8 HOH 750 2850 1276 HOH HOH A . 
CB 8 HOH 751 2851 1079 HOH HOH A . 
CB 8 HOH 752 2852 1534 HOH HOH A . 
CB 8 HOH 753 2853 1159 HOH HOH A . 
CB 8 HOH 754 2854 923  HOH HOH A . 
CB 8 HOH 755 2855 297  HOH HOH A . 
CB 8 HOH 756 2856 539  HOH HOH A . 
CB 8 HOH 757 2857 1023 HOH HOH A . 
CB 8 HOH 758 2858 766  HOH HOH A . 
CB 8 HOH 759 2859 1618 HOH HOH A . 
CB 8 HOH 760 2860 1628 HOH HOH A . 
CB 8 HOH 761 2861 1315 HOH HOH A . 
CB 8 HOH 762 2862 996  HOH HOH A . 
CB 8 HOH 763 2863 1362 HOH HOH A . 
CB 8 HOH 764 2864 1493 HOH HOH A . 
CB 8 HOH 765 2865 733  HOH HOH A . 
CB 8 HOH 766 2866 1251 HOH HOH A . 
CB 8 HOH 767 2867 603  HOH HOH A . 
CB 8 HOH 768 2868 920  HOH HOH A . 
CB 8 HOH 769 2869 1045 HOH HOH A . 
DB 8 HOH 1   2101 183  HOH HOH B . 
DB 8 HOH 2   2102 1381 HOH HOH B . 
DB 8 HOH 3   2103 1574 HOH HOH B . 
DB 8 HOH 4   2104 1481 HOH HOH B . 
DB 8 HOH 5   2105 1042 HOH HOH B . 
DB 8 HOH 6   2106 1195 HOH HOH B . 
DB 8 HOH 7   2107 1471 HOH HOH B . 
DB 8 HOH 8   2108 926  HOH HOH B . 
DB 8 HOH 9   2109 547  HOH HOH B . 
DB 8 HOH 10  2110 984  HOH HOH B . 
DB 8 HOH 11  2111 809  HOH HOH B . 
DB 8 HOH 12  2112 1014 HOH HOH B . 
DB 8 HOH 13  2113 1052 HOH HOH B . 
DB 8 HOH 14  2114 738  HOH HOH B . 
DB 8 HOH 15  2115 1216 HOH HOH B . 
DB 8 HOH 16  2116 1226 HOH HOH B . 
DB 8 HOH 17  2117 983  HOH HOH B . 
DB 8 HOH 18  2118 852  HOH HOH B . 
DB 8 HOH 19  2119 881  HOH HOH B . 
DB 8 HOH 20  2120 1358 HOH HOH B . 
DB 8 HOH 21  2121 1177 HOH HOH B . 
DB 8 HOH 22  2122 1652 HOH HOH B . 
DB 8 HOH 23  2123 1220 HOH HOH B . 
DB 8 HOH 24  2124 448  HOH HOH B . 
DB 8 HOH 25  2125 269  HOH HOH B . 
DB 8 HOH 26  2126 307  HOH HOH B . 
DB 8 HOH 27  2127 1558 HOH HOH B . 
DB 8 HOH 28  2128 166  HOH HOH B . 
DB 8 HOH 29  2129 227  HOH HOH B . 
DB 8 HOH 30  2130 683  HOH HOH B . 
DB 8 HOH 31  2131 1578 HOH HOH B . 
DB 8 HOH 32  2132 553  HOH HOH B . 
DB 8 HOH 33  2133 1103 HOH HOH B . 
DB 8 HOH 34  2134 1476 HOH HOH B . 
DB 8 HOH 35  2135 548  HOH HOH B . 
DB 8 HOH 36  2136 365  HOH HOH B . 
DB 8 HOH 37  2137 545  HOH HOH B . 
DB 8 HOH 38  2138 748  HOH HOH B . 
DB 8 HOH 39  2139 784  HOH HOH B . 
DB 8 HOH 40  2140 800  HOH HOH B . 
DB 8 HOH 41  2141 685  HOH HOH B . 
DB 8 HOH 42  2142 1207 HOH HOH B . 
DB 8 HOH 43  2143 146  HOH HOH B . 
DB 8 HOH 44  2144 1157 HOH HOH B . 
DB 8 HOH 45  2145 1259 HOH HOH B . 
DB 8 HOH 46  2146 83   HOH HOH B . 
DB 8 HOH 47  2147 1327 HOH HOH B . 
DB 8 HOH 48  2148 125  HOH HOH B . 
DB 8 HOH 49  2149 1389 HOH HOH B . 
DB 8 HOH 50  2150 414  HOH HOH B . 
DB 8 HOH 51  2151 1535 HOH HOH B . 
DB 8 HOH 52  2152 331  HOH HOH B . 
DB 8 HOH 53  2153 138  HOH HOH B . 
DB 8 HOH 54  2154 780  HOH HOH B . 
DB 8 HOH 55  2155 1544 HOH HOH B . 
DB 8 HOH 56  2156 42   HOH HOH B . 
DB 8 HOH 57  2157 436  HOH HOH B . 
DB 8 HOH 58  2158 1419 HOH HOH B . 
DB 8 HOH 59  2159 656  HOH HOH B . 
DB 8 HOH 60  2160 1051 HOH HOH B . 
DB 8 HOH 61  2161 335  HOH HOH B . 
DB 8 HOH 62  2162 399  HOH HOH B . 
DB 8 HOH 63  2163 773  HOH HOH B . 
DB 8 HOH 64  2164 741  HOH HOH B . 
DB 8 HOH 65  2165 967  HOH HOH B . 
DB 8 HOH 66  2166 1435 HOH HOH B . 
DB 8 HOH 67  2167 1527 HOH HOH B . 
DB 8 HOH 68  2168 36   HOH HOH B . 
DB 8 HOH 69  2169 228  HOH HOH B . 
DB 8 HOH 70  2170 283  HOH HOH B . 
DB 8 HOH 71  2171 1489 HOH HOH B . 
DB 8 HOH 72  2172 1379 HOH HOH B . 
DB 8 HOH 73  2173 196  HOH HOH B . 
DB 8 HOH 74  2174 1631 HOH HOH B . 
DB 8 HOH 75  2175 604  HOH HOH B . 
DB 8 HOH 76  2176 324  HOH HOH B . 
DB 8 HOH 77  2177 81   HOH HOH B . 
DB 8 HOH 78  2178 1165 HOH HOH B . 
DB 8 HOH 79  2179 203  HOH HOH B . 
DB 8 HOH 80  2180 1124 HOH HOH B . 
DB 8 HOH 81  2181 712  HOH HOH B . 
DB 8 HOH 82  2182 123  HOH HOH B . 
DB 8 HOH 83  2183 736  HOH HOH B . 
DB 8 HOH 84  2184 208  HOH HOH B . 
DB 8 HOH 85  2185 1453 HOH HOH B . 
DB 8 HOH 86  2186 888  HOH HOH B . 
DB 8 HOH 87  2187 350  HOH HOH B . 
DB 8 HOH 88  2188 648  HOH HOH B . 
DB 8 HOH 89  2189 1176 HOH HOH B . 
DB 8 HOH 90  2190 815  HOH HOH B . 
DB 8 HOH 91  2191 321  HOH HOH B . 
DB 8 HOH 92  2192 550  HOH HOH B . 
DB 8 HOH 93  2193 618  HOH HOH B . 
DB 8 HOH 94  2194 611  HOH HOH B . 
DB 8 HOH 95  2195 931  HOH HOH B . 
DB 8 HOH 96  2196 1131 HOH HOH B . 
DB 8 HOH 97  2197 329  HOH HOH B . 
DB 8 HOH 98  2198 549  HOH HOH B . 
DB 8 HOH 99  2199 803  HOH HOH B . 
DB 8 HOH 100 2200 551  HOH HOH B . 
DB 8 HOH 101 2201 1269 HOH HOH B . 
DB 8 HOH 102 2202 27   HOH HOH B . 
DB 8 HOH 103 2203 205  HOH HOH B . 
DB 8 HOH 104 2204 519  HOH HOH B . 
DB 8 HOH 105 2205 291  HOH HOH B . 
DB 8 HOH 106 2206 635  HOH HOH B . 
DB 8 HOH 107 2207 9    HOH HOH B . 
DB 8 HOH 108 2208 393  HOH HOH B . 
DB 8 HOH 109 2209 209  HOH HOH B . 
DB 8 HOH 110 2210 823  HOH HOH B . 
DB 8 HOH 111 2211 688  HOH HOH B . 
DB 8 HOH 112 2212 499  HOH HOH B . 
DB 8 HOH 113 2213 828  HOH HOH B . 
DB 8 HOH 114 2214 89   HOH HOH B . 
DB 8 HOH 115 2215 533  HOH HOH B . 
DB 8 HOH 116 2216 485  HOH HOH B . 
DB 8 HOH 117 2217 745  HOH HOH B . 
DB 8 HOH 118 2218 874  HOH HOH B . 
DB 8 HOH 119 2219 796  HOH HOH B . 
DB 8 HOH 120 2220 282  HOH HOH B . 
DB 8 HOH 121 2221 1431 HOH HOH B . 
DB 8 HOH 122 2222 587  HOH HOH B . 
DB 8 HOH 123 2223 56   HOH HOH B . 
DB 8 HOH 124 2224 574  HOH HOH B . 
DB 8 HOH 125 2225 212  HOH HOH B . 
DB 8 HOH 126 2226 961  HOH HOH B . 
DB 8 HOH 127 2227 839  HOH HOH B . 
DB 8 HOH 128 2228 1032 HOH HOH B . 
DB 8 HOH 129 2229 749  HOH HOH B . 
DB 8 HOH 130 2230 860  HOH HOH B . 
DB 8 HOH 131 2231 1198 HOH HOH B . 
DB 8 HOH 132 2232 5    HOH HOH B . 
DB 8 HOH 133 2233 732  HOH HOH B . 
DB 8 HOH 134 2234 1330 HOH HOH B . 
DB 8 HOH 135 2235 805  HOH HOH B . 
DB 8 HOH 136 2236 759  HOH HOH B . 
DB 8 HOH 137 2237 1624 HOH HOH B . 
DB 8 HOH 138 2238 1148 HOH HOH B . 
DB 8 HOH 139 2239 1236 HOH HOH B . 
DB 8 HOH 140 2240 1463 HOH HOH B . 
DB 8 HOH 141 2241 953  HOH HOH B . 
DB 8 HOH 142 2242 484  HOH HOH B . 
DB 8 HOH 143 2243 387  HOH HOH B . 
DB 8 HOH 144 2244 139  HOH HOH B . 
DB 8 HOH 145 2245 223  HOH HOH B . 
DB 8 HOH 146 2246 952  HOH HOH B . 
DB 8 HOH 147 2247 930  HOH HOH B . 
DB 8 HOH 148 2248 744  HOH HOH B . 
DB 8 HOH 149 2249 1026 HOH HOH B . 
DB 8 HOH 150 2250 403  HOH HOH B . 
DB 8 HOH 151 2251 249  HOH HOH B . 
DB 8 HOH 152 2252 429  HOH HOH B . 
DB 8 HOH 153 2253 992  HOH HOH B . 
DB 8 HOH 154 2254 783  HOH HOH B . 
DB 8 HOH 155 2255 37   HOH HOH B . 
DB 8 HOH 156 2256 1377 HOH HOH B . 
DB 8 HOH 157 2257 468  HOH HOH B . 
DB 8 HOH 158 2258 903  HOH HOH B . 
DB 8 HOH 159 2259 417  HOH HOH B . 
DB 8 HOH 160 2260 182  HOH HOH B . 
DB 8 HOH 161 2261 1483 HOH HOH B . 
DB 8 HOH 162 2262 1065 HOH HOH B . 
DB 8 HOH 163 2263 3    HOH HOH B . 
DB 8 HOH 164 2264 234  HOH HOH B . 
DB 8 HOH 165 2265 1106 HOH HOH B . 
DB 8 HOH 166 2266 326  HOH HOH B . 
DB 8 HOH 167 2267 257  HOH HOH B . 
DB 8 HOH 168 2268 29   HOH HOH B . 
DB 8 HOH 169 2269 1403 HOH HOH B . 
DB 8 HOH 170 2270 4    HOH HOH B . 
DB 8 HOH 171 2271 1462 HOH HOH B . 
DB 8 HOH 172 2272 210  HOH HOH B . 
DB 8 HOH 173 2273 70   HOH HOH B . 
DB 8 HOH 174 2274 472  HOH HOH B . 
DB 8 HOH 175 2275 706  HOH HOH B . 
DB 8 HOH 176 2276 1411 HOH HOH B . 
DB 8 HOH 177 2277 376  HOH HOH B . 
DB 8 HOH 178 2278 288  HOH HOH B . 
DB 8 HOH 179 2279 592  HOH HOH B . 
DB 8 HOH 180 2280 35   HOH HOH B . 
DB 8 HOH 181 2281 251  HOH HOH B . 
DB 8 HOH 182 2282 1539 HOH HOH B . 
DB 8 HOH 183 2283 90   HOH HOH B . 
DB 8 HOH 184 2284 840  HOH HOH B . 
DB 8 HOH 185 2285 361  HOH HOH B . 
DB 8 HOH 186 2286 73   HOH HOH B . 
DB 8 HOH 187 2287 1105 HOH HOH B . 
DB 8 HOH 188 2288 586  HOH HOH B . 
DB 8 HOH 189 2289 325  HOH HOH B . 
DB 8 HOH 190 2290 410  HOH HOH B . 
DB 8 HOH 191 2291 1168 HOH HOH B . 
DB 8 HOH 192 2292 300  HOH HOH B . 
DB 8 HOH 193 2293 1518 HOH HOH B . 
DB 8 HOH 194 2294 722  HOH HOH B . 
DB 8 HOH 195 2295 327  HOH HOH B . 
DB 8 HOH 196 2296 211  HOH HOH B . 
DB 8 HOH 197 2297 576  HOH HOH B . 
DB 8 HOH 198 2298 1126 HOH HOH B . 
DB 8 HOH 199 2299 200  HOH HOH B . 
DB 8 HOH 200 2300 189  HOH HOH B . 
DB 8 HOH 201 2301 765  HOH HOH B . 
DB 8 HOH 202 2302 57   HOH HOH B . 
DB 8 HOH 203 2303 206  HOH HOH B . 
DB 8 HOH 204 2304 1212 HOH HOH B . 
DB 8 HOH 205 2305 289  HOH HOH B . 
DB 8 HOH 206 2306 11   HOH HOH B . 
DB 8 HOH 207 2307 412  HOH HOH B . 
DB 8 HOH 208 2308 565  HOH HOH B . 
DB 8 HOH 209 2309 407  HOH HOH B . 
DB 8 HOH 210 2310 1094 HOH HOH B . 
DB 8 HOH 211 2311 185  HOH HOH B . 
DB 8 HOH 212 2312 263  HOH HOH B . 
DB 8 HOH 213 2313 105  HOH HOH B . 
DB 8 HOH 214 2314 132  HOH HOH B . 
DB 8 HOH 215 2315 742  HOH HOH B . 
DB 8 HOH 216 2316 349  HOH HOH B . 
DB 8 HOH 217 2317 1188 HOH HOH B . 
DB 8 HOH 218 2318 487  HOH HOH B . 
DB 8 HOH 219 2319 716  HOH HOH B . 
DB 8 HOH 220 2320 316  HOH HOH B . 
DB 8 HOH 221 2321 1048 HOH HOH B . 
DB 8 HOH 222 2322 136  HOH HOH B . 
DB 8 HOH 223 2323 623  HOH HOH B . 
DB 8 HOH 224 2324 974  HOH HOH B . 
DB 8 HOH 225 2325 433  HOH HOH B . 
DB 8 HOH 226 2326 271  HOH HOH B . 
DB 8 HOH 227 2327 77   HOH HOH B . 
DB 8 HOH 228 2328 1615 HOH HOH B . 
DB 8 HOH 229 2329 175  HOH HOH B . 
DB 8 HOH 230 2330 109  HOH HOH B . 
DB 8 HOH 231 2331 52   HOH HOH B . 
DB 8 HOH 232 2332 666  HOH HOH B . 
DB 8 HOH 233 2333 521  HOH HOH B . 
DB 8 HOH 234 2334 1521 HOH HOH B . 
DB 8 HOH 235 2335 582  HOH HOH B . 
DB 8 HOH 236 2336 19   HOH HOH B . 
DB 8 HOH 237 2337 117  HOH HOH B . 
DB 8 HOH 238 2338 1193 HOH HOH B . 
DB 8 HOH 239 2339 1129 HOH HOH B . 
DB 8 HOH 240 2340 1361 HOH HOH B . 
DB 8 HOH 241 2341 471  HOH HOH B . 
DB 8 HOH 242 2342 356  HOH HOH B . 
DB 8 HOH 243 2343 954  HOH HOH B . 
DB 8 HOH 244 2344 988  HOH HOH B . 
DB 8 HOH 245 2345 318  HOH HOH B . 
DB 8 HOH 246 2346 689  HOH HOH B . 
DB 8 HOH 247 2347 177  HOH HOH B . 
DB 8 HOH 248 2348 285  HOH HOH B . 
DB 8 HOH 249 2349 446  HOH HOH B . 
DB 8 HOH 250 2350 1595 HOH HOH B . 
DB 8 HOH 251 2351 314  HOH HOH B . 
DB 8 HOH 252 2352 1655 HOH HOH B . 
DB 8 HOH 253 2353 1019 HOH HOH B . 
DB 8 HOH 254 2354 772  HOH HOH B . 
DB 8 HOH 255 2355 577  HOH HOH B . 
DB 8 HOH 256 2356 572  HOH HOH B . 
DB 8 HOH 257 2357 126  HOH HOH B . 
DB 8 HOH 258 2358 437  HOH HOH B . 
DB 8 HOH 259 2359 345  HOH HOH B . 
DB 8 HOH 260 2360 18   HOH HOH B . 
DB 8 HOH 261 2361 1363 HOH HOH B . 
DB 8 HOH 262 2362 419  HOH HOH B . 
DB 8 HOH 263 2363 250  HOH HOH B . 
DB 8 HOH 264 2364 1442 HOH HOH B . 
DB 8 HOH 265 2365 585  HOH HOH B . 
DB 8 HOH 266 2366 306  HOH HOH B . 
DB 8 HOH 267 2367 1480 HOH HOH B . 
DB 8 HOH 268 2368 599  HOH HOH B . 
DB 8 HOH 269 2369 1002 HOH HOH B . 
DB 8 HOH 270 2370 1112 HOH HOH B . 
DB 8 HOH 271 2371 781  HOH HOH B . 
DB 8 HOH 272 2372 458  HOH HOH B . 
DB 8 HOH 273 2373 890  HOH HOH B . 
DB 8 HOH 274 2374 836  HOH HOH B . 
DB 8 HOH 275 2375 601  HOH HOH B . 
DB 8 HOH 276 2376 660  HOH HOH B . 
DB 8 HOH 277 2377 248  HOH HOH B . 
DB 8 HOH 278 2378 416  HOH HOH B . 
DB 8 HOH 279 2379 1143 HOH HOH B . 
DB 8 HOH 280 2380 241  HOH HOH B . 
DB 8 HOH 281 2381 966  HOH HOH B . 
DB 8 HOH 282 2382 1517 HOH HOH B . 
DB 8 HOH 283 2383 427  HOH HOH B . 
DB 8 HOH 284 2384 13   HOH HOH B . 
DB 8 HOH 285 2385 1590 HOH HOH B . 
DB 8 HOH 286 2386 1282 HOH HOH B . 
DB 8 HOH 287 2387 163  HOH HOH B . 
DB 8 HOH 288 2388 111  HOH HOH B . 
DB 8 HOH 289 2389 889  HOH HOH B . 
DB 8 HOH 290 2390 1541 HOH HOH B . 
DB 8 HOH 291 2391 187  HOH HOH B . 
DB 8 HOH 292 2392 1005 HOH HOH B . 
DB 8 HOH 293 2393 767  HOH HOH B . 
DB 8 HOH 294 2394 493  HOH HOH B . 
DB 8 HOH 295 2395 1630 HOH HOH B . 
DB 8 HOH 296 2396 476  HOH HOH B . 
DB 8 HOH 297 2397 1092 HOH HOH B . 
DB 8 HOH 298 2398 28   HOH HOH B . 
DB 8 HOH 299 2399 1349 HOH HOH B . 
DB 8 HOH 300 2400 156  HOH HOH B . 
DB 8 HOH 301 2401 506  HOH HOH B . 
DB 8 HOH 302 2402 631  HOH HOH B . 
DB 8 HOH 303 2403 1011 HOH HOH B . 
DB 8 HOH 304 2404 168  HOH HOH B . 
DB 8 HOH 305 2405 919  HOH HOH B . 
DB 8 HOH 306 2406 143  HOH HOH B . 
DB 8 HOH 307 2407 54   HOH HOH B . 
DB 8 HOH 308 2408 304  HOH HOH B . 
DB 8 HOH 309 2409 169  HOH HOH B . 
DB 8 HOH 310 2410 608  HOH HOH B . 
DB 8 HOH 311 2411 38   HOH HOH B . 
DB 8 HOH 312 2412 672  HOH HOH B . 
DB 8 HOH 313 2413 1522 HOH HOH B . 
DB 8 HOH 314 2414 218  HOH HOH B . 
DB 8 HOH 315 2415 1378 HOH HOH B . 
DB 8 HOH 316 2416 236  HOH HOH B . 
DB 8 HOH 317 2417 337  HOH HOH B . 
DB 8 HOH 318 2418 190  HOH HOH B . 
DB 8 HOH 319 2419 1272 HOH HOH B . 
DB 8 HOH 320 2420 287  HOH HOH B . 
DB 8 HOH 321 2421 1588 HOH HOH B . 
DB 8 HOH 322 2422 93   HOH HOH B . 
DB 8 HOH 323 2423 1163 HOH HOH B . 
DB 8 HOH 324 2424 1196 HOH HOH B . 
DB 8 HOH 325 2425 294  HOH HOH B . 
DB 8 HOH 326 2426 355  HOH HOH B . 
DB 8 HOH 327 2427 354  HOH HOH B . 
DB 8 HOH 328 2428 509  HOH HOH B . 
DB 8 HOH 329 2429 372  HOH HOH B . 
DB 8 HOH 330 2430 534  HOH HOH B . 
DB 8 HOH 331 2431 272  HOH HOH B . 
DB 8 HOH 332 2432 1242 HOH HOH B . 
DB 8 HOH 333 2433 284  HOH HOH B . 
DB 8 HOH 334 2434 469  HOH HOH B . 
DB 8 HOH 335 2435 747  HOH HOH B . 
DB 8 HOH 336 2436 473  HOH HOH B . 
DB 8 HOH 337 2437 172  HOH HOH B . 
DB 8 HOH 338 2438 1526 HOH HOH B . 
DB 8 HOH 339 2439 972  HOH HOH B . 
DB 8 HOH 340 2440 84   HOH HOH B . 
DB 8 HOH 341 2441 58   HOH HOH B . 
DB 8 HOH 342 2442 122  HOH HOH B . 
DB 8 HOH 343 2443 624  HOH HOH B . 
DB 8 HOH 344 2444 259  HOH HOH B . 
DB 8 HOH 345 2445 657  HOH HOH B . 
DB 8 HOH 346 2446 1009 HOH HOH B . 
DB 8 HOH 347 2447 404  HOH HOH B . 
DB 8 HOH 348 2448 330  HOH HOH B . 
DB 8 HOH 349 2449 40   HOH HOH B . 
DB 8 HOH 350 2450 708  HOH HOH B . 
DB 8 HOH 351 2451 498  HOH HOH B . 
DB 8 HOH 352 2452 1235 HOH HOH B . 
DB 8 HOH 353 2453 573  HOH HOH B . 
DB 8 HOH 354 2454 1046 HOH HOH B . 
DB 8 HOH 355 2455 1108 HOH HOH B . 
DB 8 HOH 356 2456 50   HOH HOH B . 
DB 8 HOH 357 2457 1582 HOH HOH B . 
DB 8 HOH 358 2458 658  HOH HOH B . 
DB 8 HOH 359 2459 948  HOH HOH B . 
DB 8 HOH 360 2460 242  HOH HOH B . 
DB 8 HOH 361 2461 544  HOH HOH B . 
DB 8 HOH 362 2462 411  HOH HOH B . 
DB 8 HOH 363 2463 628  HOH HOH B . 
DB 8 HOH 364 2464 892  HOH HOH B . 
DB 8 HOH 365 2465 938  HOH HOH B . 
DB 8 HOH 366 2466 207  HOH HOH B . 
DB 8 HOH 367 2467 1585 HOH HOH B . 
DB 8 HOH 368 2468 266  HOH HOH B . 
DB 8 HOH 369 2469 526  HOH HOH B . 
DB 8 HOH 370 2470 173  HOH HOH B . 
DB 8 HOH 371 2471 496  HOH HOH B . 
DB 8 HOH 372 2472 130  HOH HOH B . 
DB 8 HOH 373 2473 980  HOH HOH B . 
DB 8 HOH 374 2474 127  HOH HOH B . 
DB 8 HOH 375 2475 1222 HOH HOH B . 
DB 8 HOH 376 2476 894  HOH HOH B . 
DB 8 HOH 377 2477 222  HOH HOH B . 
DB 8 HOH 378 2478 1608 HOH HOH B . 
DB 8 HOH 379 2479 643  HOH HOH B . 
DB 8 HOH 380 2480 188  HOH HOH B . 
DB 8 HOH 381 2481 102  HOH HOH B . 
DB 8 HOH 382 2482 336  HOH HOH B . 
DB 8 HOH 383 2483 735  HOH HOH B . 
DB 8 HOH 384 2484 420  HOH HOH B . 
DB 8 HOH 385 2485 1598 HOH HOH B . 
DB 8 HOH 386 2486 67   HOH HOH B . 
DB 8 HOH 387 2487 400  HOH HOH B . 
DB 8 HOH 388 2488 1520 HOH HOH B . 
DB 8 HOH 389 2489 239  HOH HOH B . 
DB 8 HOH 390 2490 1104 HOH HOH B . 
DB 8 HOH 391 2491 216  HOH HOH B . 
DB 8 HOH 392 2492 1341 HOH HOH B . 
DB 8 HOH 393 2493 1319 HOH HOH B . 
DB 8 HOH 394 2494 1028 HOH HOH B . 
DB 8 HOH 395 2495 1619 HOH HOH B . 
DB 8 HOH 396 2496 1086 HOH HOH B . 
DB 8 HOH 397 2497 1038 HOH HOH B . 
DB 8 HOH 398 2498 293  HOH HOH B . 
DB 8 HOH 399 2499 339  HOH HOH B . 
DB 8 HOH 400 2500 497  HOH HOH B . 
DB 8 HOH 401 2501 317  HOH HOH B . 
DB 8 HOH 402 2502 120  HOH HOH B . 
DB 8 HOH 403 2503 1485 HOH HOH B . 
DB 8 HOH 404 2504 701  HOH HOH B . 
DB 8 HOH 405 2505 1007 HOH HOH B . 
DB 8 HOH 406 2506 110  HOH HOH B . 
DB 8 HOH 407 2507 281  HOH HOH B . 
DB 8 HOH 408 2508 1573 HOH HOH B . 
DB 8 HOH 409 2509 1491 HOH HOH B . 
DB 8 HOH 410 2510 1170 HOH HOH B . 
DB 8 HOH 411 2511 97   HOH HOH B . 
DB 8 HOH 412 2512 591  HOH HOH B . 
DB 8 HOH 413 2513 98   HOH HOH B . 
DB 8 HOH 414 2514 1075 HOH HOH B . 
DB 8 HOH 415 2515 694  HOH HOH B . 
DB 8 HOH 416 2516 714  HOH HOH B . 
DB 8 HOH 417 2517 1258 HOH HOH B . 
DB 8 HOH 418 2518 670  HOH HOH B . 
DB 8 HOH 419 2519 279  HOH HOH B . 
DB 8 HOH 420 2520 1210 HOH HOH B . 
DB 8 HOH 421 2521 1089 HOH HOH B . 
DB 8 HOH 422 2522 665  HOH HOH B . 
DB 8 HOH 423 2523 1398 HOH HOH B . 
DB 8 HOH 424 2524 1372 HOH HOH B . 
DB 8 HOH 425 2525 1639 HOH HOH B . 
DB 8 HOH 426 2526 1211 HOH HOH B . 
DB 8 HOH 427 2527 1532 HOH HOH B . 
DB 8 HOH 428 2528 461  HOH HOH B . 
DB 8 HOH 429 2529 256  HOH HOH B . 
DB 8 HOH 430 2530 311  HOH HOH B . 
DB 8 HOH 431 2531 512  HOH HOH B . 
DB 8 HOH 432 2532 632  HOH HOH B . 
DB 8 HOH 433 2533 15   HOH HOH B . 
DB 8 HOH 434 2534 826  HOH HOH B . 
DB 8 HOH 435 2535 45   HOH HOH B . 
DB 8 HOH 436 2536 391  HOH HOH B . 
DB 8 HOH 437 2537 1167 HOH HOH B . 
DB 8 HOH 438 2538 430  HOH HOH B . 
DB 8 HOH 439 2539 743  HOH HOH B . 
DB 8 HOH 440 2540 1152 HOH HOH B . 
DB 8 HOH 441 2541 174  HOH HOH B . 
DB 8 HOH 442 2542 1371 HOH HOH B . 
DB 8 HOH 443 2543 960  HOH HOH B . 
DB 8 HOH 444 2544 517  HOH HOH B . 
DB 8 HOH 445 2545 1635 HOH HOH B . 
DB 8 HOH 446 2546 753  HOH HOH B . 
DB 8 HOH 447 2547 802  HOH HOH B . 
DB 8 HOH 448 2548 1580 HOH HOH B . 
DB 8 HOH 449 2549 584  HOH HOH B . 
DB 8 HOH 450 2550 756  HOH HOH B . 
DB 8 HOH 451 2551 1008 HOH HOH B . 
DB 8 HOH 452 2552 443  HOH HOH B . 
DB 8 HOH 453 2553 900  HOH HOH B . 
DB 8 HOH 454 2554 1081 HOH HOH B . 
DB 8 HOH 455 2555 1290 HOH HOH B . 
DB 8 HOH 456 2556 1135 HOH HOH B . 
DB 8 HOH 457 2557 134  HOH HOH B . 
DB 8 HOH 458 2558 999  HOH HOH B . 
DB 8 HOH 459 2559 1390 HOH HOH B . 
DB 8 HOH 460 2560 217  HOH HOH B . 
DB 8 HOH 461 2561 845  HOH HOH B . 
DB 8 HOH 462 2562 7    HOH HOH B . 
DB 8 HOH 463 2563 1478 HOH HOH B . 
DB 8 HOH 464 2564 1305 HOH HOH B . 
DB 8 HOH 465 2565 629  HOH HOH B . 
DB 8 HOH 466 2566 1366 HOH HOH B . 
DB 8 HOH 467 2567 301  HOH HOH B . 
DB 8 HOH 468 2568 1107 HOH HOH B . 
DB 8 HOH 469 2569 464  HOH HOH B . 
DB 8 HOH 470 2570 1448 HOH HOH B . 
DB 8 HOH 471 2571 546  HOH HOH B . 
DB 8 HOH 472 2572 8    HOH HOH B . 
DB 8 HOH 473 2573 198  HOH HOH B . 
DB 8 HOH 474 2574 233  HOH HOH B . 
DB 8 HOH 475 2575 790  HOH HOH B . 
DB 8 HOH 476 2576 799  HOH HOH B . 
DB 8 HOH 477 2577 1024 HOH HOH B . 
DB 8 HOH 478 2578 1621 HOH HOH B . 
DB 8 HOH 479 2579 1424 HOH HOH B . 
DB 8 HOH 480 2580 590  HOH HOH B . 
DB 8 HOH 481 2581 1547 HOH HOH B . 
DB 8 HOH 482 2582 1067 HOH HOH B . 
DB 8 HOH 483 2583 338  HOH HOH B . 
DB 8 HOH 484 2584 1571 HOH HOH B . 
DB 8 HOH 485 2585 1356 HOH HOH B . 
DB 8 HOH 486 2586 1329 HOH HOH B . 
DB 8 HOH 487 2587 319  HOH HOH B . 
DB 8 HOH 488 2588 65   HOH HOH B . 
DB 8 HOH 489 2589 1114 HOH HOH B . 
DB 8 HOH 490 2590 1357 HOH HOH B . 
DB 8 HOH 491 2591 957  HOH HOH B . 
DB 8 HOH 492 2592 76   HOH HOH B . 
DB 8 HOH 493 2593 891  HOH HOH B . 
DB 8 HOH 494 2594 1083 HOH HOH B . 
DB 8 HOH 495 2595 769  HOH HOH B . 
DB 8 HOH 496 2596 1396 HOH HOH B . 
DB 8 HOH 497 2597 520  HOH HOH B . 
DB 8 HOH 498 2598 201  HOH HOH B . 
DB 8 HOH 499 2599 1039 HOH HOH B . 
DB 8 HOH 500 2600 142  HOH HOH B . 
DB 8 HOH 501 2601 465  HOH HOH B . 
DB 8 HOH 502 2602 305  HOH HOH B . 
DB 8 HOH 503 2603 883  HOH HOH B . 
DB 8 HOH 504 2604 1084 HOH HOH B . 
DB 8 HOH 505 2605 709  HOH HOH B . 
DB 8 HOH 506 2606 252  HOH HOH B . 
DB 8 HOH 507 2607 1360 HOH HOH B . 
DB 8 HOH 508 2608 363  HOH HOH B . 
DB 8 HOH 509 2609 51   HOH HOH B . 
DB 8 HOH 510 2610 814  HOH HOH B . 
DB 8 HOH 511 2611 1647 HOH HOH B . 
DB 8 HOH 512 2612 789  HOH HOH B . 
DB 8 HOH 513 2613 884  HOH HOH B . 
DB 8 HOH 514 2614 734  HOH HOH B . 
DB 8 HOH 515 2615 286  HOH HOH B . 
DB 8 HOH 516 2616 435  HOH HOH B . 
DB 8 HOH 517 2617 1575 HOH HOH B . 
DB 8 HOH 518 2618 1344 HOH HOH B . 
DB 8 HOH 519 2619 595  HOH HOH B . 
DB 8 HOH 520 2620 677  HOH HOH B . 
DB 8 HOH 521 2621 273  HOH HOH B . 
DB 8 HOH 522 2622 1447 HOH HOH B . 
DB 8 HOH 523 2623 904  HOH HOH B . 
DB 8 HOH 524 2624 1034 HOH HOH B . 
DB 8 HOH 525 2625 1265 HOH HOH B . 
DB 8 HOH 526 2626 1636 HOH HOH B . 
DB 8 HOH 527 2627 1189 HOH HOH B . 
DB 8 HOH 528 2628 1380 HOH HOH B . 
DB 8 HOH 529 2629 245  HOH HOH B . 
DB 8 HOH 530 2630 1056 HOH HOH B . 
DB 8 HOH 531 2631 589  HOH HOH B . 
DB 8 HOH 532 2632 1576 HOH HOH B . 
DB 8 HOH 533 2633 262  HOH HOH B . 
DB 8 HOH 534 2634 1551 HOH HOH B . 
DB 8 HOH 535 2635 475  HOH HOH B . 
DB 8 HOH 536 2636 270  HOH HOH B . 
DB 8 HOH 537 2637 510  HOH HOH B . 
DB 8 HOH 538 2638 47   HOH HOH B . 
DB 8 HOH 539 2639 507  HOH HOH B . 
DB 8 HOH 540 2640 450  HOH HOH B . 
DB 8 HOH 541 2641 426  HOH HOH B . 
DB 8 HOH 542 2642 1351 HOH HOH B . 
DB 8 HOH 543 2643 730  HOH HOH B . 
DB 8 HOH 544 2644 1516 HOH HOH B . 
DB 8 HOH 545 2645 71   HOH HOH B . 
DB 8 HOH 546 2646 1320 HOH HOH B . 
DB 8 HOH 547 2647 78   HOH HOH B . 
DB 8 HOH 548 2648 1144 HOH HOH B . 
DB 8 HOH 549 2649 1298 HOH HOH B . 
DB 8 HOH 550 2650 982  HOH HOH B . 
DB 8 HOH 551 2651 178  HOH HOH B . 
DB 8 HOH 552 2652 568  HOH HOH B . 
DB 8 HOH 553 2653 167  HOH HOH B . 
DB 8 HOH 554 2654 755  HOH HOH B . 
DB 8 HOH 555 2655 1444 HOH HOH B . 
DB 8 HOH 556 2656 564  HOH HOH B . 
DB 8 HOH 557 2657 725  HOH HOH B . 
DB 8 HOH 558 2658 1496 HOH HOH B . 
DB 8 HOH 559 2659 786  HOH HOH B . 
DB 8 HOH 560 2660 1017 HOH HOH B . 
DB 8 HOH 561 2661 897  HOH HOH B . 
DB 8 HOH 562 2662 777  HOH HOH B . 
DB 8 HOH 563 2663 1649 HOH HOH B . 
DB 8 HOH 564 2664 1455 HOH HOH B . 
DB 8 HOH 565 2665 1253 HOH HOH B . 
DB 8 HOH 566 2666 1359 HOH HOH B . 
DB 8 HOH 567 2667 1375 HOH HOH B . 
DB 8 HOH 568 2668 1555 HOH HOH B . 
DB 8 HOH 569 2669 538  HOH HOH B . 
DB 8 HOH 570 2670 1472 HOH HOH B . 
DB 8 HOH 571 2671 1646 HOH HOH B . 
DB 8 HOH 572 2672 1200 HOH HOH B . 
DB 8 HOH 573 2673 1504 HOH HOH B . 
DB 8 HOH 574 2674 275  HOH HOH B . 
DB 8 HOH 575 2675 818  HOH HOH B . 
DB 8 HOH 576 2676 630  HOH HOH B . 
DB 8 HOH 577 2677 1486 HOH HOH B . 
DB 8 HOH 578 2678 452  HOH HOH B . 
DB 8 HOH 579 2679 1119 HOH HOH B . 
DB 8 HOH 580 2680 760  HOH HOH B . 
DB 8 HOH 581 2681 1074 HOH HOH B . 
DB 8 HOH 582 2682 1569 HOH HOH B . 
DB 8 HOH 583 2683 1215 HOH HOH B . 
DB 8 HOH 584 2684 1326 HOH HOH B . 
DB 8 HOH 585 2685 1055 HOH HOH B . 
DB 8 HOH 586 2686 1382 HOH HOH B . 
DB 8 HOH 587 2687 1248 HOH HOH B . 
DB 8 HOH 588 2688 1494 HOH HOH B . 
DB 8 HOH 589 2689 1643 HOH HOH B . 
DB 8 HOH 590 2690 855  HOH HOH B . 
DB 8 HOH 591 2691 950  HOH HOH B . 
DB 8 HOH 592 2692 1561 HOH HOH B . 
DB 8 HOH 593 2693 374  HOH HOH B . 
DB 8 HOH 594 2694 1495 HOH HOH B . 
DB 8 HOH 595 2695 1446 HOH HOH B . 
DB 8 HOH 596 2696 1627 HOH HOH B . 
DB 8 HOH 597 2697 1614 HOH HOH B . 
DB 8 HOH 598 2698 619  HOH HOH B . 
DB 8 HOH 599 2699 641  HOH HOH B . 
DB 8 HOH 600 2700 1594 HOH HOH B . 
DB 8 HOH 601 2701 1466 HOH HOH B . 
DB 8 HOH 602 2702 1179 HOH HOH B . 
DB 8 HOH 603 2703 418  HOH HOH B . 
DB 8 HOH 604 2704 1408 HOH HOH B . 
DB 8 HOH 605 2705 1402 HOH HOH B . 
DB 8 HOH 606 2706 1513 HOH HOH B . 
DB 8 HOH 607 2707 1577 HOH HOH B . 
DB 8 HOH 608 2708 406  HOH HOH B . 
DB 8 HOH 609 2709 1229 HOH HOH B . 
DB 8 HOH 610 2710 408  HOH HOH B . 
DB 8 HOH 611 2711 692  HOH HOH B . 
DB 8 HOH 612 2712 1169 HOH HOH B . 
DB 8 HOH 613 2713 1540 HOH HOH B . 
DB 8 HOH 614 2714 1033 HOH HOH B . 
DB 8 HOH 615 2715 1287 HOH HOH B . 
DB 8 HOH 616 2716 1085 HOH HOH B . 
DB 8 HOH 617 2717 1564 HOH HOH B . 
DB 8 HOH 618 2718 720  HOH HOH B . 
DB 8 HOH 619 2719 401  HOH HOH B . 
DB 8 HOH 620 2720 1591 HOH HOH B . 
DB 8 HOH 621 2721 1348 HOH HOH B . 
DB 8 HOH 622 2722 667  HOH HOH B . 
DB 8 HOH 623 2723 968  HOH HOH B . 
DB 8 HOH 624 2724 1658 HOH HOH B . 
DB 8 HOH 625 2725 1548 HOH HOH B . 
DB 8 HOH 626 2726 1420 HOH HOH B . 
DB 8 HOH 627 2727 1317 HOH HOH B . 
DB 8 HOH 628 2728 1127 HOH HOH B . 
DB 8 HOH 629 2729 896  HOH HOH B . 
DB 8 HOH 630 2730 776  HOH HOH B . 
DB 8 HOH 631 2731 1490 HOH HOH B . 
DB 8 HOH 632 2732 1345 HOH HOH B . 
DB 8 HOH 633 2733 583  HOH HOH B . 
DB 8 HOH 634 2734 1003 HOH HOH B . 
DB 8 HOH 635 2735 1542 HOH HOH B . 
DB 8 HOH 636 2736 1401 HOH HOH B . 
DB 8 HOH 637 2737 770  HOH HOH B . 
DB 8 HOH 638 2738 505  HOH HOH B . 
DB 8 HOH 639 2739 907  HOH HOH B . 
DB 8 HOH 640 2740 668  HOH HOH B . 
DB 8 HOH 641 2741 1022 HOH HOH B . 
DB 8 HOH 642 2742 915  HOH HOH B . 
DB 8 HOH 643 2743 973  HOH HOH B . 
DB 8 HOH 644 2744 1218 HOH HOH B . 
DB 8 HOH 645 2745 1549 HOH HOH B . 
DB 8 HOH 646 2746 1142 HOH HOH B . 
DB 8 HOH 647 2747 1054 HOH HOH B . 
DB 8 HOH 648 2748 1632 HOH HOH B . 
DB 8 HOH 649 2749 1592 HOH HOH B . 
DB 8 HOH 650 2750 1395 HOH HOH B . 
DB 8 HOH 651 2751 614  HOH HOH B . 
DB 8 HOH 652 2752 1233 HOH HOH B . 
DB 8 HOH 653 2753 1584 HOH HOH B . 
DB 8 HOH 654 2754 1047 HOH HOH B . 
DB 8 HOH 655 2755 693  HOH HOH B . 
DB 8 HOH 656 2756 1072 HOH HOH B . 
DB 8 HOH 657 2757 1467 HOH HOH B . 
DB 8 HOH 658 2758 1530 HOH HOH B . 
DB 8 HOH 659 2759 703  HOH HOH B . 
DB 8 HOH 660 2760 1613 HOH HOH B . 
DB 8 HOH 661 2761 1601 HOH HOH B . 
DB 8 HOH 662 2762 1243 HOH HOH B . 
DB 8 HOH 663 2763 1529 HOH HOH B . 
DB 8 HOH 664 2764 1274 HOH HOH B . 
DB 8 HOH 665 2765 830  HOH HOH B . 
DB 8 HOH 666 2766 1268 HOH HOH B . 
DB 8 HOH 667 2767 1425 HOH HOH B . 
DB 8 HOH 668 2768 1125 HOH HOH B . 
DB 8 HOH 669 2769 724  HOH HOH B . 
DB 8 HOH 670 2770 1415 HOH HOH B . 
DB 8 HOH 671 2771 1335 HOH HOH B . 
DB 8 HOH 672 2772 1528 HOH HOH B . 
DB 8 HOH 673 2773 981  HOH HOH B . 
DB 8 HOH 674 2774 1066 HOH HOH B . 
DB 8 HOH 675 2775 1414 HOH HOH B . 
DB 8 HOH 676 2776 634  HOH HOH B . 
DB 8 HOH 677 2777 717  HOH HOH B . 
DB 8 HOH 678 2778 751  HOH HOH B . 
DB 8 HOH 679 2779 1322 HOH HOH B . 
DB 8 HOH 680 2780 1303 HOH HOH B . 
DB 8 HOH 681 2781 1543 HOH HOH B . 
DB 8 HOH 682 2782 1166 HOH HOH B . 
DB 8 HOH 683 2783 1641 HOH HOH B . 
DB 8 HOH 684 2784 1145 HOH HOH B . 
DB 8 HOH 685 2785 1219 HOH HOH B . 
DB 8 HOH 686 2786 1581 HOH HOH B . 
DB 8 HOH 687 2787 1417 HOH HOH B . 
DB 8 HOH 688 2788 942  HOH HOH B . 
DB 8 HOH 689 2789 731  HOH HOH B . 
DB 8 HOH 690 2790 806  HOH HOH B . 
DB 8 HOH 691 2791 723  HOH HOH B . 
DB 8 HOH 692 2792 1087 HOH HOH B . 
DB 8 HOH 693 2793 1405 HOH HOH B . 
DB 8 HOH 694 2794 684  HOH HOH B . 
DB 8 HOH 695 2795 1122 HOH HOH B . 
DB 8 HOH 696 2796 1178 HOH HOH B . 
DB 8 HOH 697 2797 1533 HOH HOH B . 
DB 8 HOH 698 2798 1035 HOH HOH B . 
DB 8 HOH 699 2799 1459 HOH HOH B . 
DB 8 HOH 700 2800 1445 HOH HOH B . 
DB 8 HOH 701 2801 1043 HOH HOH B . 
DB 8 HOH 702 2802 1492 HOH HOH B . 
DB 8 HOH 703 2803 1633 HOH HOH B . 
DB 8 HOH 704 2804 1589 HOH HOH B . 
DB 8 HOH 705 2805 1310 HOH HOH B . 
DB 8 HOH 706 2806 1254 HOH HOH B . 
DB 8 HOH 707 2807 1394 HOH HOH B . 
DB 8 HOH 708 2808 1434 HOH HOH B . 
DB 8 HOH 709 2809 779  HOH HOH B . 
DB 8 HOH 710 2810 752  HOH HOH B . 
DB 8 HOH 711 2811 702  HOH HOH B . 
DB 8 HOH 712 2812 1342 HOH HOH B . 
DB 8 HOH 713 2813 1562 HOH HOH B . 
DB 8 HOH 714 2814 1283 HOH HOH B . 
DB 8 HOH 715 2815 613  HOH HOH B . 
DB 8 HOH 716 2816 1422 HOH HOH B . 
DB 8 HOH 717 2817 1583 HOH HOH B . 
DB 8 HOH 718 2818 535  HOH HOH B . 
DB 8 HOH 719 2819 1502 HOH HOH B . 
DB 8 HOH 720 2820 1657 HOH HOH B . 
DB 8 HOH 721 2821 1406 HOH HOH B . 
DB 8 HOH 722 2822 1552 HOH HOH B . 
DB 8 HOH 723 2823 1308 HOH HOH B . 
DB 8 HOH 724 2824 1400 HOH HOH B . 
DB 8 HOH 725 2825 846  HOH HOH B . 
DB 8 HOH 726 2826 1221 HOH HOH B . 
DB 8 HOH 727 2827 1449 HOH HOH B . 
DB 8 HOH 728 2828 1044 HOH HOH B . 
DB 8 HOH 729 2829 754  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 ASP 20   ? CG  ? A ASP 22   CG  
2   1 Y 1 A ASP 20   ? OD1 ? A ASP 22   OD1 
3   1 Y 1 A ASP 20   ? OD2 ? A ASP 22   OD2 
4   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
5   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
6   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
7   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
8   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
9   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
10  1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
11  1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
12  1 Y 1 A SER 66   ? OG  ? A SER 68   OG  
13  1 Y 1 A LYS 70   ? CG  ? A LYS 72   CG  
14  1 Y 1 A LYS 70   ? CD  ? A LYS 72   CD  
15  1 Y 1 A LYS 70   ? CE  ? A LYS 72   CE  
16  1 Y 1 A LYS 70   ? NZ  ? A LYS 72   NZ  
17  1 Y 1 A ILE 72   ? CG1 ? A ILE 74   CG1 
18  1 Y 1 A ILE 72   ? CG2 ? A ILE 74   CG2 
19  1 Y 1 A ILE 72   ? CD1 ? A ILE 74   CD1 
20  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
21  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
22  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
23  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
24  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
25  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
26  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
27  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
28  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
29  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
30  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
31  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
32  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
33  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
34  1 Y 1 A ASP 123  ? CG  ? A ASP 125  CG  
35  1 Y 1 A ASP 123  ? OD1 ? A ASP 125  OD1 
36  1 Y 1 A ASP 123  ? OD2 ? A ASP 125  OD2 
37  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
38  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
39  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
40  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
41  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
42  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
43  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
44  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
45  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
46  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
47  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
48  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
49  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
50  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
51  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
52  1 Y 1 A HIS 133  ? CG  ? A HIS 135  CG  
53  1 Y 1 A HIS 133  ? ND1 ? A HIS 135  ND1 
54  1 Y 1 A HIS 133  ? CD2 ? A HIS 135  CD2 
55  1 Y 1 A HIS 133  ? CE1 ? A HIS 135  CE1 
56  1 Y 1 A HIS 133  ? NE2 ? A HIS 135  NE2 
57  1 Y 1 A ARG 138  ? CG  ? A ARG 140  CG  
58  1 Y 1 A ARG 138  ? CD  ? A ARG 140  CD  
59  1 Y 1 A ARG 138  ? NE  ? A ARG 140  NE  
60  1 Y 1 A ARG 138  ? CZ  ? A ARG 140  CZ  
61  1 Y 1 A ARG 138  ? NH1 ? A ARG 140  NH1 
62  1 Y 1 A ARG 138  ? NH2 ? A ARG 140  NH2 
63  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
64  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
65  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
66  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
67  1 Y 1 A ARG 181  ? CG  ? A ARG 183  CG  
68  1 Y 1 A ARG 181  ? CD  ? A ARG 183  CD  
69  1 Y 1 A ARG 181  ? NE  ? A ARG 183  NE  
70  1 Y 1 A ARG 181  ? CZ  ? A ARG 183  CZ  
71  1 Y 1 A ARG 181  ? NH1 ? A ARG 183  NH1 
72  1 Y 1 A ARG 181  ? NH2 ? A ARG 183  NH2 
73  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
74  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
75  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
76  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
77  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
78  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
79  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
80  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
81  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
82  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
83  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
84  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
85  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
86  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
87  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
88  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
89  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
90  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
91  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
92  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
93  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
94  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
95  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
96  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
97  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
98  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
99  1 Y 1 A GLU 234  ? CG  ? A GLU 236  CG  
100 1 Y 1 A GLU 234  ? CD  ? A GLU 236  CD  
101 1 Y 1 A GLU 234  ? OE1 ? A GLU 236  OE1 
102 1 Y 1 A GLU 234  ? OE2 ? A GLU 236  OE2 
103 1 Y 1 A LEU 295  ? CG  ? A LEU 297  CG  
104 1 Y 1 A LEU 295  ? CD1 ? A LEU 297  CD1 
105 1 Y 1 A LEU 295  ? CD2 ? A LEU 297  CD2 
106 1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
107 1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
108 1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
109 1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
110 1 Y 1 A LEU 449  ? CG  ? A LEU 451  CG  
111 1 Y 1 A LEU 449  ? CD1 ? A LEU 451  CD1 
112 1 Y 1 A LEU 449  ? CD2 ? A LEU 451  CD2 
113 1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
114 1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
115 1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
116 1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
117 1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
118 1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
119 1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
120 1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
121 1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
122 1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
123 1 Y 1 A THR 481  ? OG1 ? A THR 483  OG1 
124 1 Y 1 A THR 481  ? CG2 ? A THR 483  CG2 
125 1 Y 1 A LEU 482  ? CG  ? A LEU 484  CG  
126 1 Y 1 A LEU 482  ? CD1 ? A LEU 484  CD1 
127 1 Y 1 A LEU 482  ? CD2 ? A LEU 484  CD2 
128 1 Y 1 A LEU 483  ? CG  ? A LEU 485  CG  
129 1 Y 1 A LEU 483  ? CD1 ? A LEU 485  CD1 
130 1 Y 1 A LEU 483  ? CD2 ? A LEU 485  CD2 
131 1 Y 1 A TYR 485  ? CG  ? A TYR 487  CG  
132 1 Y 1 A TYR 485  ? CD1 ? A TYR 487  CD1 
133 1 Y 1 A TYR 485  ? CD2 ? A TYR 487  CD2 
134 1 Y 1 A TYR 485  ? CE1 ? A TYR 487  CE1 
135 1 Y 1 A TYR 485  ? CE2 ? A TYR 487  CE2 
136 1 Y 1 A TYR 485  ? CZ  ? A TYR 487  CZ  
137 1 Y 1 A TYR 485  ? OH  ? A TYR 487  OH  
138 1 Y 1 A VAL 487  ? CG1 ? A VAL 489  CG1 
139 1 Y 1 A VAL 487  ? CG2 ? A VAL 489  CG2 
140 1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
141 1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
142 1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
143 1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
144 1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
145 1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
146 1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
147 1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
148 1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
149 1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
150 1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
151 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
152 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
153 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
154 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
155 1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
156 1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
157 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
158 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
159 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
160 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
161 1 Y 1 A GLU 564  ? CG  ? A GLU 566  CG  
162 1 Y 1 A GLU 564  ? CD  ? A GLU 566  CD  
163 1 Y 1 A GLU 564  ? OE1 ? A GLU 566  OE1 
164 1 Y 1 A GLU 564  ? OE2 ? A GLU 566  OE2 
165 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
166 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
167 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
168 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
169 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
170 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
171 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
172 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
173 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
174 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
175 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
176 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
177 1 Y 1 A ARG 764  ? CG  ? A ARG 766  CG  
178 1 Y 1 A ARG 764  ? CD  ? A ARG 766  CD  
179 1 Y 1 A ARG 764  ? NE  ? A ARG 766  NE  
180 1 Y 1 A ARG 764  ? CZ  ? A ARG 766  CZ  
181 1 Y 1 A ARG 764  ? NH1 ? A ARG 766  NH1 
182 1 Y 1 A ARG 764  ? NH2 ? A ARG 766  NH2 
183 1 Y 1 A GLU 810  ? CG  ? A GLU 812  CG  
184 1 Y 1 A GLU 810  ? CD  ? A GLU 812  CD  
185 1 Y 1 A GLU 810  ? OE1 ? A GLU 812  OE1 
186 1 Y 1 A GLU 810  ? OE2 ? A GLU 812  OE2 
187 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
188 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
189 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
190 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
191 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
192 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
193 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
194 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
195 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
196 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
197 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
198 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
199 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
200 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
201 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
202 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
203 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
204 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
205 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
206 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
207 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
208 1 Y 1 A LEU 934  ? CG  ? A LEU 936  CG  
209 1 Y 1 A LEU 934  ? CD1 ? A LEU 936  CD1 
210 1 Y 1 A LEU 934  ? CD2 ? A LEU 936  CD2 
211 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
212 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
213 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
214 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
215 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
216 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
217 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
218 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
219 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
220 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
221 1 Y 1 A LYS 990  ? CG  ? A LYS 992  CG  
222 1 Y 1 A LYS 990  ? CD  ? A LYS 992  CD  
223 1 Y 1 A LYS 990  ? CE  ? A LYS 992  CE  
224 1 Y 1 A LYS 990  ? NZ  ? A LYS 992  NZ  
225 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
226 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
227 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
228 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
229 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
230 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
231 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
232 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
233 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
234 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
235 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
236 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
237 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
238 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
239 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
240 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
241 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
242 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
243 1 Y 1 A GLU 1171 ? CG  ? A GLU 1173 CG  
244 1 Y 1 A GLU 1171 ? CD  ? A GLU 1173 CD  
245 1 Y 1 A GLU 1171 ? OE1 ? A GLU 1173 OE1 
246 1 Y 1 A GLU 1171 ? OE2 ? A GLU 1173 OE2 
247 1 Y 1 A GLU 1212 ? CG  ? A GLU 1214 CG  
248 1 Y 1 A GLU 1212 ? CD  ? A GLU 1214 CD  
249 1 Y 1 A GLU 1212 ? OE1 ? A GLU 1214 OE1 
250 1 Y 1 A GLU 1212 ? OE2 ? A GLU 1214 OE2 
251 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
252 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
253 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
254 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
255 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
256 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
257 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
258 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
259 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
260 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
261 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
262 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
263 1 Y 1 B ARG 69   ? CG  ? B ARG 71   CG  
264 1 Y 1 B ARG 69   ? CD  ? B ARG 71   CD  
265 1 Y 1 B ARG 69   ? NE  ? B ARG 71   NE  
266 1 Y 1 B ARG 69   ? CZ  ? B ARG 71   CZ  
267 1 Y 1 B ARG 69   ? NH1 ? B ARG 71   NH1 
268 1 Y 1 B ARG 69   ? NH2 ? B ARG 71   NH2 
269 1 Y 1 B LYS 70   ? CG  ? B LYS 72   CG  
270 1 Y 1 B LYS 70   ? CD  ? B LYS 72   CD  
271 1 Y 1 B LYS 70   ? CE  ? B LYS 72   CE  
272 1 Y 1 B LYS 70   ? NZ  ? B LYS 72   NZ  
273 1 Y 1 B ILE 72   ? CG1 ? B ILE 74   CG1 
274 1 Y 1 B ILE 72   ? CG2 ? B ILE 74   CG2 
275 1 Y 1 B ILE 72   ? CD1 ? B ILE 74   CD1 
276 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
277 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
278 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
279 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
280 1 Y 1 B LEU 75   ? CG  ? B LEU 77   CG  
281 1 Y 1 B LEU 75   ? CD1 ? B LEU 77   CD1 
282 1 Y 1 B LEU 75   ? CD2 ? B LEU 77   CD2 
283 1 Y 1 B HIS 79   ? CG  ? B HIS 81   CG  
284 1 Y 1 B HIS 79   ? ND1 ? B HIS 81   ND1 
285 1 Y 1 B HIS 79   ? CD2 ? B HIS 81   CD2 
286 1 Y 1 B HIS 79   ? CE1 ? B HIS 81   CE1 
287 1 Y 1 B HIS 79   ? NE2 ? B HIS 81   NE2 
288 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
289 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
290 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
291 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
292 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
293 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
294 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
295 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
296 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
297 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
298 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
299 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
300 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
301 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
302 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
303 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
304 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
305 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
306 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
307 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
308 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
309 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
310 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
311 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
312 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
313 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
314 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
315 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
316 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
317 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
318 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
319 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
320 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
321 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
322 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
323 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
324 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
325 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
326 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
327 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
328 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
329 1 Y 1 B LEU 155  ? CG  ? B LEU 157  CG  
330 1 Y 1 B LEU 155  ? CD1 ? B LEU 157  CD1 
331 1 Y 1 B LEU 155  ? CD2 ? B LEU 157  CD2 
332 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
333 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
334 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
335 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
336 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
337 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
338 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
339 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
340 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
341 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
342 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
343 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
344 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
345 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
346 1 Y 1 B GLU 210  ? CG  ? B GLU 212  CG  
347 1 Y 1 B GLU 210  ? CD  ? B GLU 212  CD  
348 1 Y 1 B GLU 210  ? OE1 ? B GLU 212  OE1 
349 1 Y 1 B GLU 210  ? OE2 ? B GLU 212  OE2 
350 1 Y 1 B GLU 213  ? CG  ? B GLU 215  CG  
351 1 Y 1 B GLU 213  ? CD  ? B GLU 215  CD  
352 1 Y 1 B GLU 213  ? OE1 ? B GLU 215  OE1 
353 1 Y 1 B GLU 213  ? OE2 ? B GLU 215  OE2 
354 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
355 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
356 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
357 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
358 1 Y 1 B GLU 258  ? CG  ? B GLU 260  CG  
359 1 Y 1 B GLU 258  ? CD  ? B GLU 260  CD  
360 1 Y 1 B GLU 258  ? OE1 ? B GLU 260  OE1 
361 1 Y 1 B GLU 258  ? OE2 ? B GLU 260  OE2 
362 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
363 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
364 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
365 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
366 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
367 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
368 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
369 1 Y 1 B LYS 443  ? CG  ? B LYS 445  CG  
370 1 Y 1 B LYS 443  ? CD  ? B LYS 445  CD  
371 1 Y 1 B LYS 443  ? CE  ? B LYS 445  CE  
372 1 Y 1 B LYS 443  ? NZ  ? B LYS 445  NZ  
373 1 Y 1 B LEU 449  ? CG  ? B LEU 451  CG  
374 1 Y 1 B LEU 449  ? CD1 ? B LEU 451  CD1 
375 1 Y 1 B LEU 449  ? CD2 ? B LEU 451  CD2 
376 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
377 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
378 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
379 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
380 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
381 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
382 1 Y 1 B LEU 466  ? CG  ? B LEU 468  CG  
383 1 Y 1 B LEU 466  ? CD1 ? B LEU 468  CD1 
384 1 Y 1 B LEU 466  ? CD2 ? B LEU 468  CD2 
385 1 Y 1 B ASP 467  ? CG  ? B ASP 469  CG  
386 1 Y 1 B ASP 467  ? OD1 ? B ASP 469  OD1 
387 1 Y 1 B ASP 467  ? OD2 ? B ASP 469  OD2 
388 1 Y 1 B HIS 479  ? CG  ? B HIS 481  CG  
389 1 Y 1 B HIS 479  ? ND1 ? B HIS 481  ND1 
390 1 Y 1 B HIS 479  ? CD2 ? B HIS 481  CD2 
391 1 Y 1 B HIS 479  ? CE1 ? B HIS 481  CE1 
392 1 Y 1 B HIS 479  ? NE2 ? B HIS 481  NE2 
393 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
394 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
395 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
396 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
397 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
398 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
399 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
400 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
401 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
402 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
403 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
404 1 Y 1 B LEU 486  ? CG  ? B LEU 488  CG  
405 1 Y 1 B LEU 486  ? CD1 ? B LEU 488  CD1 
406 1 Y 1 B LEU 486  ? CD2 ? B LEU 488  CD2 
407 1 Y 1 B ARG 488  ? CG  ? B ARG 490  CG  
408 1 Y 1 B ARG 488  ? CD  ? B ARG 490  CD  
409 1 Y 1 B ARG 488  ? NE  ? B ARG 490  NE  
410 1 Y 1 B ARG 488  ? CZ  ? B ARG 490  CZ  
411 1 Y 1 B ARG 488  ? NH1 ? B ARG 490  NH1 
412 1 Y 1 B ARG 488  ? NH2 ? B ARG 490  NH2 
413 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
414 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
415 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
416 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
417 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
418 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
419 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
420 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
421 1 Y 1 B ASN 504  ? CG  ? B ASN 506  CG  
422 1 Y 1 B ASN 504  ? OD1 ? B ASN 506  OD1 
423 1 Y 1 B ASN 504  ? ND2 ? B ASN 506  ND2 
424 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
425 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
426 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
427 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
428 1 Y 1 B ILE 510  ? CG1 ? B ILE 512  CG1 
429 1 Y 1 B ILE 510  ? CG2 ? B ILE 512  CG2 
430 1 Y 1 B ILE 510  ? CD1 ? B ILE 512  CD1 
431 1 Y 1 B LEU 513  ? CG  ? B LEU 515  CG  
432 1 Y 1 B LEU 513  ? CD1 ? B LEU 515  CD1 
433 1 Y 1 B LEU 513  ? CD2 ? B LEU 515  CD2 
434 1 Y 1 B ILE 514  ? CG1 ? B ILE 516  CG1 
435 1 Y 1 B ILE 514  ? CG2 ? B ILE 516  CG2 
436 1 Y 1 B ILE 514  ? CD1 ? B ILE 516  CD1 
437 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
438 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
439 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
440 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
441 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
442 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
443 1 Y 1 B GLU 568  ? CG  ? B GLU 570  CG  
444 1 Y 1 B GLU 568  ? CD  ? B GLU 570  CD  
445 1 Y 1 B GLU 568  ? OE1 ? B GLU 570  OE1 
446 1 Y 1 B GLU 568  ? OE2 ? B GLU 570  OE2 
447 1 Y 1 B GLU 588  ? CG  ? B GLU 590  CG  
448 1 Y 1 B GLU 588  ? CD  ? B GLU 590  CD  
449 1 Y 1 B GLU 588  ? OE1 ? B GLU 590  OE1 
450 1 Y 1 B GLU 588  ? OE2 ? B GLU 590  OE2 
451 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
452 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
453 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
454 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
455 1 Y 1 B ASP 622  ? CG  ? B ASP 624  CG  
456 1 Y 1 B ASP 622  ? OD1 ? B ASP 624  OD1 
457 1 Y 1 B ASP 622  ? OD2 ? B ASP 624  OD2 
458 1 Y 1 B ARG 764  ? CG  ? B ARG 766  CG  
459 1 Y 1 B ARG 764  ? CD  ? B ARG 766  CD  
460 1 Y 1 B ARG 764  ? NE  ? B ARG 766  NE  
461 1 Y 1 B ARG 764  ? CZ  ? B ARG 766  CZ  
462 1 Y 1 B ARG 764  ? NH1 ? B ARG 766  NH1 
463 1 Y 1 B ARG 764  ? NH2 ? B ARG 766  NH2 
464 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
465 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
466 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
467 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
468 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
469 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
470 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
471 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
472 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
473 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
474 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
475 1 Y 1 B LEU 905  ? CG  ? B LEU 907  CG  
476 1 Y 1 B LEU 905  ? CD1 ? B LEU 907  CD1 
477 1 Y 1 B LEU 905  ? CD2 ? B LEU 907  CD2 
478 1 Y 1 B ARG 907  ? CG  ? B ARG 909  CG  
479 1 Y 1 B ARG 907  ? CD  ? B ARG 909  CD  
480 1 Y 1 B ARG 907  ? NE  ? B ARG 909  NE  
481 1 Y 1 B ARG 907  ? CZ  ? B ARG 909  CZ  
482 1 Y 1 B ARG 907  ? NH1 ? B ARG 909  NH1 
483 1 Y 1 B ARG 907  ? NH2 ? B ARG 909  NH2 
484 1 Y 1 B LYS 908  ? CG  ? B LYS 910  CG  
485 1 Y 1 B LYS 908  ? CD  ? B LYS 910  CD  
486 1 Y 1 B LYS 908  ? CE  ? B LYS 910  CE  
487 1 Y 1 B LYS 908  ? NZ  ? B LYS 910  NZ  
488 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
489 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
490 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
491 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
492 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
493 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
494 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
495 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
496 1 Y 1 B LEU 934  ? CG  ? B LEU 936  CG  
497 1 Y 1 B LEU 934  ? CD1 ? B LEU 936  CD1 
498 1 Y 1 B LEU 934  ? CD2 ? B LEU 936  CD2 
499 1 Y 1 B SER 935  ? OG  ? B SER 937  OG  
500 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
501 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
502 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
503 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
504 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
505 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
506 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
507 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
508 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
509 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
510 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
511 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
512 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
513 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
514 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
515 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
516 1 Y 1 B LYS 990  ? CG  ? B LYS 992  CG  
517 1 Y 1 B LYS 990  ? CD  ? B LYS 992  CD  
518 1 Y 1 B LYS 990  ? CE  ? B LYS 992  CE  
519 1 Y 1 B LYS 990  ? NZ  ? B LYS 992  NZ  
520 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
521 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
522 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
523 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
524 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
525 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
526 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
527 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
528 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
529 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
530 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
531 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
532 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
533 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
534 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
535 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
536 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
537 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
538 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
539 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
540 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
541 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
542 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
543 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
544 1 Y 1 B GLU 1171 ? CG  ? B GLU 1173 CG  
545 1 Y 1 B GLU 1171 ? CD  ? B GLU 1173 CD  
546 1 Y 1 B GLU 1171 ? OE1 ? B GLU 1173 OE1 
547 1 Y 1 B GLU 1171 ? OE2 ? B GLU 1173 OE2 
548 1 Y 1 B LYS 1178 ? CG  ? B LYS 1180 CG  
549 1 Y 1 B LYS 1178 ? CD  ? B LYS 1180 CD  
550 1 Y 1 B LYS 1178 ? CE  ? B LYS 1180 CE  
551 1 Y 1 B LYS 1178 ? NZ  ? B LYS 1180 NZ  
552 1 Y 1 B GLU 1197 ? CG  ? B GLU 1199 CG  
553 1 Y 1 B GLU 1197 ? CD  ? B GLU 1199 CD  
554 1 Y 1 B GLU 1197 ? OE1 ? B GLU 1199 OE1 
555 1 Y 1 B GLU 1197 ? OE2 ? B GLU 1199 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          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .            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                     9DL7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.135 
_cell.length_a_esd                 ? 
_cell.length_b                     101.867 
_cell.length_b_esd                 ? 
_cell.length_c                     126.557 
_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                         9DL7 
_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                   9DL7 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.10 
_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              ? 
_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    
;Reservoir contained 0.1 M HEPES, pH 7.5, 0.1 M sodium formate, 0.1 M magnesium chloride, 0.2 M ammonium sulfate, and 20% (w/v) PEG 3350. Crystal was soaked in cryobuffer containing 19 mM 1-(4-fluorophenyl)thiourea and 20% PEG 200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-01 
_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   1.000018 
_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                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000018 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DL7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               46.97 
_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                                     503696 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.238 
_reflns.pdbx_Rpim_I_all                                0.096 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.981 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.217 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           89890 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12912 
_reflns_shell.percent_possible_obs                          99.8 
_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                               7.0 
_reflns_shell.pdbx_chi_squared                              0.40 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.6 
_reflns_shell.pdbx_Rrim_I_all                               2.544 
_reflns_shell.pdbx_Rpim_I_all                               0.953 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.397 
_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                                  2.356 
_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                                 9DL7 
_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                            1.72 
_refine.ls_d_res_low                             46.97 
_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                     503696 
_refine.ls_number_reflns_R_free                  10332 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.83 
_refine.ls_percent_reflns_R_free                 2.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2091 
_refine.ls_R_factor_R_free                       0.2400 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2084 
_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                          0.00 
_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                 27.69 
_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                            0.27 
_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        17530 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         370 
_refine_hist.number_atoms_solvent             1498 
_refine_hist.number_atoms_total               19398 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        46.97 
# 
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  ? 18303 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.813  ? 24956 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.356 ? 6570  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 2919  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 3240  ? 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' 1.72 1.74  . . 334 16724 99.00  . . . . 0.3025 . . . . . . . . . . . 0.3131 
'X-RAY DIFFRACTION' 1.74 1.76  . . 353 16784 100.00 . . . . 0.2920 . . . . . . . . . . . 0.3777 
'X-RAY DIFFRACTION' 1.76 1.78  . . 337 16746 100.00 . . . . 0.2840 . . . . . . . . . . . 0.3013 
'X-RAY DIFFRACTION' 1.78 1.80  . . 392 16812 100.00 . . . . 0.2788 . . . . . . . . . . . 0.3289 
'X-RAY DIFFRACTION' 1.80 1.83  . . 293 16741 100.00 . . . . 0.2864 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 1.83 1.85  . . 359 16794 100.00 . . . . 0.2922 . . . . . . . . . . . 0.3073 
'X-RAY DIFFRACTION' 1.85 1.88  . . 372 16601 99.00  . . . . 0.3327 . . . . . . . . . . . 0.3421 
'X-RAY DIFFRACTION' 1.88 1.91  . . 310 16356 97.00  . . . . 0.4165 . . . . . . . . . . . 0.4498 
'X-RAY DIFFRACTION' 1.91 1.94  . . 380 15893 95.00  . . . . 0.4379 . . . . . . . . . . . 0.4384 
'X-RAY DIFFRACTION' 1.94 1.97  . . 358 16616 99.00  . . . . 0.3596 . . . . . . . . . . . 0.4250 
'X-RAY DIFFRACTION' 1.97 2.00  . . 315 16772 100.00 . . . . 0.2712 . . . . . . . . . . . 0.3199 
'X-RAY DIFFRACTION' 2.00 2.04  . . 322 16740 99.00  . . . . 0.2560 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 2.04 2.08  . . 326 15538 92.00  . . . . 0.2912 . . . . . . . . . . . 0.3336 
'X-RAY DIFFRACTION' 2.08 2.12  . . 389 16606 99.00  . . . . 0.2335 . . . . . . . . . . . 0.2692 
'X-RAY DIFFRACTION' 2.12 2.17  . . 402 16732 100.00 . . . . 0.2048 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 2.17 2.22  . . 345 16672 100.00 . . . . 0.2140 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 2.22 2.27  . . 358 15858 95.00  . . . . 0.2458 . . . . . . . . . . . 0.3060 
'X-RAY DIFFRACTION' 2.27 2.33  . . 385 16618 99.00  . . . . 0.2066 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 2.33 2.40  . . 354 16712 99.00  . . . . 0.1910 . . . . . . . . . . . 0.2268 
'X-RAY DIFFRACTION' 2.40 2.48  . . 324 16786 99.00  . . . . 0.1874 . . . . . . . . . . . 0.2065 
'X-RAY DIFFRACTION' 2.48 2.57  . . 313 16655 99.00  . . . . 0.1938 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.57 2.67  . . 409 16459 98.00  . . . . 0.1998 . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 2.67 2.79  . . 330 16469 98.00  . . . . 0.1983 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 2.79 2.94  . . 310 16554 98.00  . . . . 0.1939 . . . . . . . . . . . 0.2322 
'X-RAY DIFFRACTION' 2.94 3.13  . . 316 16404 97.00  . . . . 0.1950 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 3.13 3.37  . . 364 16128 96.00  . . . . 0.1930 . . . . . . . . . . . 0.2253 
'X-RAY DIFFRACTION' 3.37 3.71  . . 330 15346 92.00  . . . . 0.1847 . . . . . . . . . . . 0.2138 
'X-RAY DIFFRACTION' 3.71 4.24  . . 309 15584 92.00  . . . . 0.1655 . . . . . . . . . . . 0.2006 
'X-RAY DIFFRACTION' 4.24 5.34  . . 306 16102 95.00  . . . . 0.1616 . . . . . . . . . . . 0.1861 
'X-RAY DIFFRACTION' 5.34 46.97 . . 337 16562 99.00  . . . . 0.1637 . . . . . . . . . . . 0.1796 
# 
_struct.entry_id                     9DL7 
_struct.title                        'Structure of proline utilization A complexed with 1-(4-fluorophenyl)thiourea' 
_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        9DL7 
_struct_keywords.text            
;FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGENASE, 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 4 ? 
F  N N 3 ? 
G  N N 5 ? 
H  N N 6 ? 
I  N N 3 ? 
J  N N 6 ? 
K  N N 6 ? 
L  N N 6 ? 
M  N N 6 ? 
N  N N 3 ? 
O  N N 6 ? 
P  N N 6 ? 
Q  N N 7 ? 
R  N N 7 ? 
S  N N 7 ? 
T  N N 7 ? 
U  N N 7 ? 
V  N N 7 ? 
W  N N 7 ? 
X  N N 7 ? 
Y  N N 7 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
FA N N 7 ? 
GA N N 2 ? 
HA N N 4 ? 
IA N N 3 ? 
JA N N 3 ? 
KA N N 5 ? 
LA N N 6 ? 
MA N N 3 ? 
NA N N 6 ? 
OA N N 3 ? 
PA N N 6 ? 
QA N N 6 ? 
RA N N 6 ? 
SA N N 7 ? 
TA N N 7 ? 
UA N N 7 ? 
VA N N 7 ? 
WA N N 7 ? 
XA N N 7 ? 
YA N N 7 ? 
ZA N N 7 ? 
AB N N 7 ? 
BB N N 7 ? 
CB N N 8 ? 
DB N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    F7X6I3_SINMM 
_struct_ref.pdbx_db_accession          F7X6I3 
_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 9DL7 A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9DL7 B 3 ? 1235 ? F7X6I3 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 9DL7 SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9DL7 MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9DL7 SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9DL7 MET B 2 ? UNP F7X6I3 ? ? '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_and_software_defined_assembly PISA dimeric   2 
2 author_defined_assembly              ?    monomeric 1 
3 author_defined_assembly              ?    monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 16350 ? 
1 MORE         -414  ? 
1 'SSA (A^2)'  79060 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 
;A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB
;
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,CB 
3 1 B,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,DB 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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   ? ALA A 56   ? PRO A 42   ALA A 54   1 ? 13 
HELX_P HELX_P3   AA3 SER A 59   ? GLY A 79   ? SER A 57   GLY A 77   1 ? 21 
HELX_P HELX_P4   AA4 VAL A 86   ? TYR A 93   ? VAL A 84   TYR A 91   1 ? 8  
HELX_P HELX_P5   AA5 SER A 96   ? ARG A 112  ? SER A 94   ARG A 110  1 ? 17 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 ILE A 127  ? GLY A 130  ? ILE A 125  GLY A 128  5 ? 4  
HELX_P HELX_P8   AA8 ASN A 131  ? LEU A 136  ? ASN A 129  LEU A 134  1 ? 6  
HELX_P HELX_P9   AA9 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P10  AB1 ASN A 162  ? GLY A 178  ? ASN A 160  GLY A 176  1 ? 17 
HELX_P HELX_P11  AB2 GLY A 178  ? GLN A 196  ? GLY A 176  GLN A 194  1 ? 19 
HELX_P HELX_P12  AB3 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P13  AB4 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P14  AB5 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P15  AB6 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P16  AB7 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P17  AB8 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P18  AB9 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P19  AC1 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P20  AC2 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P21  AC3 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P22  AC4 TYR A 375  ? GLY A 387  ? TYR A 373  GLY A 385  1 ? 13 
HELX_P HELX_P23  AC5 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P24  AC6 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P25  AC7 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P26  AC8 THR A 480  ? TYR A 487  ? THR A 478  TYR A 485  1 ? 8  
HELX_P HELX_P27  AC9 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P28  AD1 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P29  AD2 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P30  AD3 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P31  AD4 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P32  AD5 SER A 611  ? ALA A 631  ? SER A 609  ALA A 629  1 ? 21 
HELX_P HELX_P33  AD6 PRO A 633  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P34  AD7 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
HELX_P HELX_P35  AD8 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P36  AD9 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P37  AE1 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P38  AE2 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P39  AE3 SER A 785  ? ALA A 797  ? SER A 783  ALA A 795  1 ? 13 
HELX_P HELX_P40  AE4 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P41  AE5 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P42  AE6 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P43  AE7 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P44  AE8 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P45  AE9 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P46  AF1 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P47  AF2 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P48  AF3 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P49  AF4 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P50  AF5 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P51  AF6 ASP A 1049 ? GLY A 1063 ? ASP A 1047 GLY A 1061 1 ? 15 
HELX_P HELX_P52  AF7 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P53  AF8 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P54  AF9 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P55  AG1 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P56  AG2 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P57  AG3 ASP A 1156 ? ASP A 1160 ? ASP A 1154 ASP A 1158 5 ? 5  
HELX_P HELX_P58  AG4 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P59  AG5 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P60  AG6 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
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   ? GLY B 79   ? SER B 57   GLY B 77   1 ? 21 
HELX_P HELX_P64  AH1 VAL B 86   ? TYR B 93   ? VAL B 84   TYR B 91   1 ? 8  
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 ILE B 127  ? GLY B 130  ? ILE B 125  GLY B 128  5 ? 4  
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  ? LYS B 216  ? THR B 200  LYS B 214  1 ? 15 
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  ? ASP B 386  ? TYR B 373  ASP B 384  1 ? 12 
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 HIS B 481  ? LEU B 493  ? HIS B 479  LEU B 491  1 ? 13 
HELX_P HELX_P85  AJ4 GLU B 494  ? ALA B 497  ? GLU B 492  ALA B 495  5 ? 4  
HELX_P HELX_P86  AJ5 SER B 500  ? ILE B 505  ? SER B 498  ILE B 503  1 ? 6  
HELX_P HELX_P87  AJ6 SER B 511  ? ALA B 517  ? SER B 509  ALA B 515  1 ? 7  
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  ? MET B 574  ? ASN B 555  MET B 572  1 ? 18 
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  ? ALA B 797  ? SER B 783  ALA B 795  1 ? 13 
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 ? GLY B 1063 ? ASP B 1047 GLY B 1061 1 ? 15 
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  
# 
_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 -0.83 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 1.41  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -5.53 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 0.77  
# 
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  ALA A 1166 ? GLU A 1169 ? ALA A 1164 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  SER B 219  ? MET B 224  ? SER B 217  MET B 222  
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  ? VAL B 478  ? CYS B 470  VAL B 476  
AA7 9  SER B 219  ? MET B 224  ? SER B 217  MET B 222  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? THR B 608  ? ASP B 597  THR B 606  
AA8 3  THR B 591  ? ASN B 596  ? THR B 589  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 ? LEU B 1086 ? ASP B 1081 LEU B 1084 
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  ALA B 1166 ? GLU B 1169 ? ALA B 1164 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 GLY A 263  ? O GLY A 261  
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 LEU A 370  ? N LEU A 368  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 GLU A 1214 ? O GLU A 1212 N HIS A 1099 ? N HIS A 1097 
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 264  ? N ILE B 262  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 PHE B 339  ? N PHE B 337  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 LEU B 730  ? O LEU B 728  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 ASN B 1094 ? O ASN B 1092 N LEU B 1086 ? N LEU B 1084 
AB3 1 2  O SER B 1152 ? O SER B 1150 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                   9DL7 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLU 539  ? ? O  A HOH 2101 ? ? 2.03 
2  1 F1  B 8P4 2005 ? A O  B HOH 2582 ? ? 2.07 
3  1 OE1 B GLU 539  ? ? O  B HOH 2101 ? ? 2.07 
4  1 O   A HOH 2702 ? ? O  A HOH 2761 ? ? 2.12 
5  1 NH2 A ARG 202  ? ? O  A HOH 2102 ? ? 2.15 
6  1 O   A HOH 2609 ? ? O  B HOH 2504 ? ? 2.17 
7  1 OG  A SER 845  ? ? O2 A SO4 2016 ? ? 2.17 
8  1 O   A HOH 2853 ? ? O  A HOH 2867 ? ? 2.18 
9  1 O   A HOH 2183 ? ? O  A HOH 2725 ? ? 2.19 
10 1 O   A HOH 2523 ? ? O  A HOH 2741 ? ? 2.19 
11 1 OE1 B GLU 1212 ? ? O  B HOH 2102 ? ? 2.19 
12 1 O   B HOH 2459 ? ? O  B HOH 2733 ? ? 2.19 
13 1 OD1 A ASN 298  ? A O  A HOH 2103 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     2104 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     2715 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.14 
# 
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   ? ? -157.95 51.35   
2  1 LYS A 124  ? ? -142.71 -53.28  
3  1 GLU A 308  ? ? -124.47 -135.20 
4  1 VAL A 460  ? ? -126.13 -55.79  
5  1 LYS A 465  ? ? -117.48 -112.68 
6  1 ALA A 484  ? ? -56.73  -73.03  
7  1 ASP A 597  ? ? -168.31 99.42   
8  1 THR A 689  ? ? -134.79 -43.37  
9  1 THR A 811  ? ? -127.19 -165.84 
10 1 GLN A 814  ? ? -106.49 71.20   
11 1 GLN A 842  ? ? -91.05  30.23   
12 1 LEU A 970  ? ? -95.50  -83.21  
13 1 VAL A 1007 ? ? -121.70 -52.31  
14 1 ALA A 1222 ? ? -67.19  6.61    
15 1 ALA B 22   ? ? -153.75 63.71   
16 1 LYS B 124  ? ? -138.75 -49.74  
17 1 GLU B 308  ? ? -120.39 -134.05 
18 1 LYS B 465  ? ? -111.02 -121.04 
19 1 ASP B 597  ? ? -172.65 100.19  
20 1 THR B 689  ? ? -132.15 -40.56  
21 1 HIS B 694  ? ? -100.53 76.85   
22 1 GLN B 814  ? ? -118.57 76.03   
23 1 GLN B 842  ? ? -96.19  30.79   
24 1 LEU B 970  ? ? -95.69  -86.26  
# 
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 -25.7236 66.4408 93.4146 0.2407 ? -0.0034 ? 0.0053  ? 0.1986 ? 0.0227  ? 0.1960 ? 0.5087 ? -0.0420 
? 0.1440 ? 0.1428 ? 0.0347  ? 0.2421 ? -0.0089 ? -0.0218 ? 0.0066  ? 0.0300 ? 0.0262 ? -0.0029 ? 0.0058 ? 0.0134  ? -0.0199 ? 
2 'X-RAY DIFFRACTION' ? refined 5.9564   31.4122 91.4587 0.1658 ? 0.0002  ? -0.0193 ? 0.1973 ? -0.0144 ? 0.1636 ? 0.3158 ? -0.0187 
? 0.2186 ? 0.2837 ? -0.0684 ? 0.6337 ? 0.0419  ? -0.0564 ? -0.0362 ? 0.0659 ? 0.0343 ? -0.0148 ? 0.1084 ? -0.1285 ? -0.0705 ? 
# 
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 and peptide' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B and peptide' 
# 
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 HIS 79   ? A HIS 81   
17 1 Y 1 A SER 80   ? A SER 82   
18 1 Y 1 A GLY 81   ? A GLY 83   
19 1 Y 1 A SER 82   ? A SER 84   
20 1 Y 1 A GLY 135  ? A GLY 137  
21 1 Y 1 A GLY 136  ? A GLY 138  
22 1 Y 1 A SER 137  ? A SER 139  
23 1 Y 1 A LEU 490  ? A LEU 492  
24 1 Y 1 A LEU 491  ? A LEU 493  
25 1 Y 1 A GLU 492  ? A GLU 494  
26 1 Y 1 A ASN 493  ? A ASN 495  
27 1 Y 1 A GLY 1224 ? A GLY 1226 
28 1 Y 1 A GLY 1225 ? A GLY 1227 
29 1 Y 1 A ASN 1226 ? A ASN 1228 
30 1 Y 1 A ALA 1227 ? A ALA 1229 
31 1 Y 1 A SER 1228 ? A SER 1230 
32 1 Y 1 A LEU 1229 ? A LEU 1231 
33 1 Y 1 A MET 1230 ? A MET 1232 
34 1 Y 1 A ALA 1231 ? A ALA 1233 
35 1 Y 1 A ILE 1232 ? A ILE 1234 
36 1 Y 1 A GLY 1233 ? A GLY 1235 
37 1 Y 1 B SER -1   ? B SER 1    
38 1 Y 1 B MET 0    ? B MET 2    
39 1 Y 1 B MET 1    ? B MET 3    
40 1 Y 1 B SER 2    ? B SER 4    
41 1 Y 1 B PRO 3    ? B PRO 5    
42 1 Y 1 B ASN 4    ? B ASN 6    
43 1 Y 1 B PRO 5    ? B PRO 7    
44 1 Y 1 B LEU 6    ? B LEU 8    
45 1 Y 1 B GLN 7    ? B GLN 9    
46 1 Y 1 B LYS 8    ? B LYS 10   
47 1 Y 1 B PRO 9    ? B PRO 11   
48 1 Y 1 B ALA 10   ? B ALA 12   
49 1 Y 1 B ILE 11   ? B ILE 13   
50 1 Y 1 B ASP 12   ? B ASP 14   
51 1 Y 1 B ALA 13   ? B ALA 15   
52 1 Y 1 B SER 80   ? B SER 82   
53 1 Y 1 B GLY 81   ? B GLY 83   
54 1 Y 1 B SER 82   ? B SER 84   
55 1 Y 1 B GLY 135  ? B GLY 137  
56 1 Y 1 B GLY 136  ? B GLY 138  
57 1 Y 1 B SER 137  ? B SER 139  
58 1 Y 1 B ALA 1222 ? B ALA 1224 
59 1 Y 1 B ALA 1223 ? B ALA 1225 
60 1 Y 1 B GLY 1224 ? B GLY 1226 
61 1 Y 1 B GLY 1225 ? B GLY 1227 
62 1 Y 1 B ASN 1226 ? B ASN 1228 
63 1 Y 1 B ALA 1227 ? B ALA 1229 
64 1 Y 1 B SER 1228 ? B SER 1230 
65 1 Y 1 B LEU 1229 ? B LEU 1231 
66 1 Y 1 B MET 1230 ? B MET 1232 
67 1 Y 1 B ALA 1231 ? B ALA 1233 
68 1 Y 1 B ILE 1232 ? B ILE 1234 
69 1 Y 1 B GLY 1233 ? B GLY 1235 
# 
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 
8P4 N1     N N N 1   
8P4 C4     C Y N 2   
8P4 C5     C Y N 3   
8P4 C6     C Y N 4   
8P4 C7     C N N 5   
8P4 C1     C Y N 6   
8P4 C2     C Y N 7   
8P4 C3     C Y N 8   
8P4 N2     N N N 9   
8P4 S1     S N N 10  
8P4 F1     F N N 11  
8P4 H1     H N N 12  
8P4 H2     H N N 13  
8P4 H3     H N N 14  
8P4 H4     H N N 15  
8P4 H5     H N N 16  
8P4 H6     H N N 17  
8P4 H7     H N N 18  
ALA N      N N N 19  
ALA CA     C N S 20  
ALA C      C N N 21  
ALA O      O N N 22  
ALA CB     C N N 23  
ALA OXT    O N N 24  
ALA H      H N N 25  
ALA H2     H N N 26  
ALA HA     H N N 27  
ALA HB1    H N N 28  
ALA HB2    H N N 29  
ALA HB3    H N N 30  
ALA HXT    H N N 31  
ARG N      N N N 32  
ARG CA     C N S 33  
ARG C      C N N 34  
ARG O      O N N 35  
ARG CB     C N N 36  
ARG CG     C N N 37  
ARG CD     C N N 38  
ARG NE     N N N 39  
ARG CZ     C N N 40  
ARG NH1    N N N 41  
ARG NH2    N N N 42  
ARG OXT    O N N 43  
ARG H      H N N 44  
ARG H2     H N N 45  
ARG HA     H N N 46  
ARG HB2    H N N 47  
ARG HB3    H N N 48  
ARG HG2    H N N 49  
ARG HG3    H N N 50  
ARG HD2    H N N 51  
ARG HD3    H N N 52  
ARG HE     H N N 53  
ARG HH11   H N N 54  
ARG HH12   H N N 55  
ARG HH21   H N N 56  
ARG HH22   H N N 57  
ARG HXT    H N N 58  
ASN N      N N N 59  
ASN CA     C N S 60  
ASN C      C N N 61  
ASN O      O N N 62  
ASN CB     C N N 63  
ASN CG     C N N 64  
ASN OD1    O N N 65  
ASN ND2    N N N 66  
ASN OXT    O N N 67  
ASN H      H N N 68  
ASN H2     H N N 69  
ASN HA     H N N 70  
ASN HB2    H N N 71  
ASN HB3    H N N 72  
ASN HD21   H N N 73  
ASN HD22   H N N 74  
ASN HXT    H N N 75  
ASP N      N N N 76  
ASP CA     C N S 77  
ASP C      C N N 78  
ASP O      O N N 79  
ASP CB     C N N 80  
ASP CG     C N N 81  
ASP OD1    O N N 82  
ASP OD2    O N N 83  
ASP OXT    O N N 84  
ASP H      H N N 85  
ASP H2     H N N 86  
ASP HA     H N N 87  
ASP HB2    H N N 88  
ASP HB3    H N N 89  
ASP HD2    H N N 90  
ASP HXT    H N N 91  
CYS N      N N N 92  
CYS CA     C N R 93  
CYS C      C N N 94  
CYS O      O N N 95  
CYS CB     C N N 96  
CYS SG     S N N 97  
CYS OXT    O N N 98  
CYS H      H N N 99  
CYS H2     H N N 100 
CYS HA     H N N 101 
CYS HB2    H N N 102 
CYS HB3    H N N 103 
CYS HG     H N N 104 
CYS HXT    H N N 105 
FAD PA     P N R 106 
FAD O1A    O N N 107 
FAD O2A    O N N 108 
FAD O5B    O N N 109 
FAD C5B    C N N 110 
FAD C4B    C N R 111 
FAD O4B    O N N 112 
FAD C3B    C N S 113 
FAD O3B    O N N 114 
FAD C2B    C N R 115 
FAD O2B    O N N 116 
FAD C1B    C N R 117 
FAD N9A    N Y N 118 
FAD C8A    C Y N 119 
FAD N7A    N Y N 120 
FAD C5A    C Y N 121 
FAD C6A    C Y N 122 
FAD N6A    N N N 123 
FAD N1A    N Y N 124 
FAD C2A    C Y N 125 
FAD N3A    N Y N 126 
FAD C4A    C Y N 127 
FAD N1     N N N 128 
FAD C2     C N N 129 
FAD O2     O N N 130 
FAD N3     N N N 131 
FAD C4     C N N 132 
FAD O4     O N N 133 
FAD C4X    C N N 134 
FAD N5     N N N 135 
FAD C5X    C Y N 136 
FAD C6     C Y N 137 
FAD C7     C Y N 138 
FAD C7M    C N N 139 
FAD C8     C Y N 140 
FAD C8M    C N N 141 
FAD C9     C Y N 142 
FAD C9A    C Y N 143 
FAD N10    N N N 144 
FAD C10    C N N 145 
FAD "C1'"  C N N 146 
FAD "C2'"  C N S 147 
FAD "O2'"  O N N 148 
FAD "C3'"  C N S 149 
FAD "O3'"  O N N 150 
FAD "C4'"  C N R 151 
FAD "O4'"  O N N 152 
FAD "C5'"  C N N 153 
FAD "O5'"  O N N 154 
FAD P      P N R 155 
FAD O1P    O N N 156 
FAD O2P    O N N 157 
FAD O3P    O N N 158 
FAD HOA2   H N N 159 
FAD H51A   H N N 160 
FAD H52A   H N N 161 
FAD H4B    H N N 162 
FAD H3B    H N N 163 
FAD HO3A   H N N 164 
FAD H2B    H N N 165 
FAD HO2A   H N N 166 
FAD H1B    H N N 167 
FAD H8A    H N N 168 
FAD H61A   H N N 169 
FAD H62A   H N N 170 
FAD H2A    H N N 171 
FAD HN3    H N N 172 
FAD H6     H N N 173 
FAD HM71   H N N 174 
FAD HM72   H N N 175 
FAD HM73   H N N 176 
FAD HM81   H N N 177 
FAD HM82   H N N 178 
FAD HM83   H N N 179 
FAD H9     H N N 180 
FAD "H1'1" H N N 181 
FAD "H1'2" H N N 182 
FAD "H2'"  H N N 183 
FAD "HO2'" H N N 184 
FAD "H3'"  H N N 185 
FAD "HO3'" H N N 186 
FAD "H4'"  H N N 187 
FAD "HO4'" H N N 188 
FAD "H5'1" H N N 189 
FAD "H5'2" H N N 190 
FAD HOP2   H N N 191 
FMT C      C N N 192 
FMT O1     O N N 193 
FMT O2     O N N 194 
FMT H      H N N 195 
FMT HO2    H N N 196 
GLN N      N N N 197 
GLN CA     C N S 198 
GLN C      C N N 199 
GLN O      O N N 200 
GLN CB     C N N 201 
GLN CG     C N N 202 
GLN CD     C N N 203 
GLN OE1    O N N 204 
GLN NE2    N N N 205 
GLN OXT    O N N 206 
GLN H      H N N 207 
GLN H2     H N N 208 
GLN HA     H N N 209 
GLN HB2    H N N 210 
GLN HB3    H N N 211 
GLN HG2    H N N 212 
GLN HG3    H N N 213 
GLN HE21   H N N 214 
GLN HE22   H N N 215 
GLN HXT    H N N 216 
GLU N      N N N 217 
GLU CA     C N S 218 
GLU C      C N N 219 
GLU O      O N N 220 
GLU CB     C N N 221 
GLU CG     C N N 222 
GLU CD     C N N 223 
GLU OE1    O N N 224 
GLU OE2    O N N 225 
GLU OXT    O N N 226 
GLU H      H N N 227 
GLU H2     H N N 228 
GLU HA     H N N 229 
GLU HB2    H N N 230 
GLU HB3    H N N 231 
GLU HG2    H N N 232 
GLU HG3    H N N 233 
GLU HE2    H N N 234 
GLU HXT    H N N 235 
GLY N      N N N 236 
GLY CA     C N N 237 
GLY C      C N N 238 
GLY O      O N N 239 
GLY OXT    O N N 240 
GLY H      H N N 241 
GLY H2     H N N 242 
GLY HA2    H N N 243 
GLY HA3    H N N 244 
GLY HXT    H N N 245 
HIS N      N N N 246 
HIS CA     C N S 247 
HIS C      C N N 248 
HIS O      O N N 249 
HIS CB     C N N 250 
HIS CG     C Y N 251 
HIS ND1    N Y N 252 
HIS CD2    C Y N 253 
HIS CE1    C Y N 254 
HIS NE2    N Y N 255 
HIS OXT    O N N 256 
HIS H      H N N 257 
HIS H2     H N N 258 
HIS HA     H N N 259 
HIS HB2    H N N 260 
HIS HB3    H N N 261 
HIS HD1    H N N 262 
HIS HD2    H N N 263 
HIS HE1    H N N 264 
HIS HE2    H N N 265 
HIS HXT    H N N 266 
HOH O      O N N 267 
HOH H1     H N N 268 
HOH H2     H N N 269 
ILE N      N N N 270 
ILE CA     C N S 271 
ILE C      C N N 272 
ILE O      O N N 273 
ILE CB     C N S 274 
ILE CG1    C N N 275 
ILE CG2    C N N 276 
ILE CD1    C N N 277 
ILE OXT    O N N 278 
ILE H      H N N 279 
ILE H2     H N N 280 
ILE HA     H N N 281 
ILE HB     H N N 282 
ILE HG12   H N N 283 
ILE HG13   H N N 284 
ILE HG21   H N N 285 
ILE HG22   H N N 286 
ILE HG23   H N N 287 
ILE HD11   H N N 288 
ILE HD12   H N N 289 
ILE HD13   H N N 290 
ILE HXT    H N N 291 
LEU N      N N N 292 
LEU CA     C N S 293 
LEU C      C N N 294 
LEU O      O N N 295 
LEU CB     C N N 296 
LEU CG     C N N 297 
LEU CD1    C N N 298 
LEU CD2    C N N 299 
LEU OXT    O N N 300 
LEU H      H N N 301 
LEU H2     H N N 302 
LEU HA     H N N 303 
LEU HB2    H N N 304 
LEU HB3    H N N 305 
LEU HG     H N N 306 
LEU HD11   H N N 307 
LEU HD12   H N N 308 
LEU HD13   H N N 309 
LEU HD21   H N N 310 
LEU HD22   H N N 311 
LEU HD23   H N N 312 
LEU HXT    H N N 313 
LYS N      N N N 314 
LYS CA     C N S 315 
LYS C      C N N 316 
LYS O      O N N 317 
LYS CB     C N N 318 
LYS CG     C N N 319 
LYS CD     C N N 320 
LYS CE     C N N 321 
LYS NZ     N N N 322 
LYS OXT    O N N 323 
LYS H      H N N 324 
LYS H2     H N N 325 
LYS HA     H N N 326 
LYS HB2    H N N 327 
LYS HB3    H N N 328 
LYS HG2    H N N 329 
LYS HG3    H N N 330 
LYS HD2    H N N 331 
LYS HD3    H N N 332 
LYS HE2    H N N 333 
LYS HE3    H N N 334 
LYS HZ1    H N N 335 
LYS HZ2    H N N 336 
LYS HZ3    H N N 337 
LYS HXT    H N N 338 
MET N      N N N 339 
MET CA     C N S 340 
MET C      C N N 341 
MET O      O N N 342 
MET CB     C N N 343 
MET CG     C N N 344 
MET SD     S N N 345 
MET CE     C N N 346 
MET OXT    O N N 347 
MET H      H N N 348 
MET H2     H N N 349 
MET HA     H N N 350 
MET HB2    H N N 351 
MET HB3    H N N 352 
MET HG2    H N N 353 
MET HG3    H N N 354 
MET HE1    H N N 355 
MET HE2    H N N 356 
MET HE3    H N N 357 
MET HXT    H N N 358 
PEG C1     C N N 359 
PEG O1     O N N 360 
PEG C2     C N N 361 
PEG O2     O N N 362 
PEG C3     C N N 363 
PEG C4     C N N 364 
PEG O4     O N N 365 
PEG H11    H N N 366 
PEG H12    H N N 367 
PEG HO1    H N N 368 
PEG H21    H N N 369 
PEG H22    H N N 370 
PEG H31    H N N 371 
PEG H32    H N N 372 
PEG H41    H N N 373 
PEG H42    H N N 374 
PEG HO4    H N N 375 
PGE C1     C N N 376 
PGE O1     O N N 377 
PGE C2     C N N 378 
PGE O2     O N N 379 
PGE C3     C N N 380 
PGE C4     C N N 381 
PGE O4     O N N 382 
PGE C6     C N N 383 
PGE C5     C N N 384 
PGE O3     O N N 385 
PGE H1     H N N 386 
PGE H12    H N N 387 
PGE HO1    H N N 388 
PGE H2     H N N 389 
PGE H22    H N N 390 
PGE H3     H N N 391 
PGE H32    H N N 392 
PGE H4     H N N 393 
PGE H42    H N N 394 
PGE HO4    H N N 395 
PGE H6     H N N 396 
PGE H62    H N N 397 
PGE H5     H N N 398 
PGE H52    H N N 399 
PHE N      N N N 400 
PHE CA     C N S 401 
PHE C      C N N 402 
PHE O      O N N 403 
PHE CB     C N N 404 
PHE CG     C Y N 405 
PHE CD1    C Y N 406 
PHE CD2    C Y N 407 
PHE CE1    C Y N 408 
PHE CE2    C Y N 409 
PHE CZ     C Y N 410 
PHE OXT    O N N 411 
PHE H      H N N 412 
PHE H2     H N N 413 
PHE HA     H N N 414 
PHE HB2    H N N 415 
PHE HB3    H N N 416 
PHE HD1    H N N 417 
PHE HD2    H N N 418 
PHE HE1    H N N 419 
PHE HE2    H N N 420 
PHE HZ     H N N 421 
PHE HXT    H N N 422 
PRO N      N N N 423 
PRO CA     C N S 424 
PRO C      C N N 425 
PRO O      O N N 426 
PRO CB     C N N 427 
PRO CG     C N N 428 
PRO CD     C N N 429 
PRO OXT    O N N 430 
PRO H      H N N 431 
PRO HA     H N N 432 
PRO HB2    H N N 433 
PRO HB3    H N N 434 
PRO HG2    H N N 435 
PRO HG3    H N N 436 
PRO HD2    H N N 437 
PRO HD3    H N N 438 
PRO HXT    H N N 439 
SER N      N N N 440 
SER CA     C N S 441 
SER C      C N N 442 
SER O      O N N 443 
SER CB     C N N 444 
SER OG     O N N 445 
SER OXT    O N N 446 
SER H      H N N 447 
SER H2     H N N 448 
SER HA     H N N 449 
SER HB2    H N N 450 
SER HB3    H N N 451 
SER HG     H N N 452 
SER HXT    H N N 453 
SO4 S      S N N 454 
SO4 O1     O N N 455 
SO4 O2     O N N 456 
SO4 O3     O N N 457 
SO4 O4     O N N 458 
THR N      N N N 459 
THR CA     C N S 460 
THR C      C N N 461 
THR O      O N N 462 
THR CB     C N R 463 
THR OG1    O N N 464 
THR CG2    C N N 465 
THR OXT    O N N 466 
THR H      H N N 467 
THR H2     H N N 468 
THR HA     H N N 469 
THR HB     H N N 470 
THR HG1    H N N 471 
THR HG21   H N N 472 
THR HG22   H N N 473 
THR HG23   H N N 474 
THR HXT    H N N 475 
TRP N      N N N 476 
TRP CA     C N S 477 
TRP C      C N N 478 
TRP O      O N N 479 
TRP CB     C N N 480 
TRP CG     C Y N 481 
TRP CD1    C Y N 482 
TRP CD2    C Y N 483 
TRP NE1    N Y N 484 
TRP CE2    C Y N 485 
TRP CE3    C Y N 486 
TRP CZ2    C Y N 487 
TRP CZ3    C Y N 488 
TRP CH2    C Y N 489 
TRP OXT    O N N 490 
TRP H      H N N 491 
TRP H2     H N N 492 
TRP HA     H N N 493 
TRP HB2    H N N 494 
TRP HB3    H N N 495 
TRP HD1    H N N 496 
TRP HE1    H N N 497 
TRP HE3    H N N 498 
TRP HZ2    H N N 499 
TRP HZ3    H N N 500 
TRP HH2    H N N 501 
TRP HXT    H N N 502 
TYR N      N N N 503 
TYR CA     C N S 504 
TYR C      C N N 505 
TYR O      O N N 506 
TYR CB     C N N 507 
TYR CG     C Y N 508 
TYR CD1    C Y N 509 
TYR CD2    C Y N 510 
TYR CE1    C Y N 511 
TYR CE2    C Y N 512 
TYR CZ     C Y N 513 
TYR OH     O N N 514 
TYR OXT    O N N 515 
TYR H      H N N 516 
TYR H2     H N N 517 
TYR HA     H N N 518 
TYR HB2    H N N 519 
TYR HB3    H N N 520 
TYR HD1    H N N 521 
TYR HD2    H N N 522 
TYR HE1    H N N 523 
TYR HE2    H N N 524 
TYR HH     H N N 525 
TYR HXT    H N N 526 
VAL N      N N N 527 
VAL CA     C N S 528 
VAL C      C N N 529 
VAL O      O N N 530 
VAL CB     C N N 531 
VAL CG1    C N N 532 
VAL CG2    C N N 533 
VAL OXT    O N N 534 
VAL H      H N N 535 
VAL H2     H N N 536 
VAL HA     H N N 537 
VAL HB     H N N 538 
VAL HG11   H N N 539 
VAL HG12   H N N 540 
VAL HG13   H N N 541 
VAL HG21   H N N 542 
VAL HG22   H N N 543 
VAL HG23   H N N 544 
VAL HXT    H N N 545 
# 
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 
8P4 S1    C7     doub N N 1   
8P4 N2    C7     sing N N 2   
8P4 C7    N1     sing N N 3   
8P4 N1    C6     sing N N 4   
8P4 C5    C6     doub Y N 5   
8P4 C5    C4     sing Y N 6   
8P4 C6    C1     sing Y N 7   
8P4 C4    C3     doub Y N 8   
8P4 C1    C2     doub Y N 9   
8P4 C3    C2     sing Y N 10  
8P4 C3    F1     sing N N 11  
8P4 N1    H1     sing N N 12  
8P4 C4    H2     sing N N 13  
8P4 C5    H3     sing N N 14  
8P4 C1    H4     sing N N 15  
8P4 C2    H5     sing N N 16  
8P4 N2    H6     sing N N 17  
8P4 N2    H7     sing N N 18  
ALA N     CA     sing N N 19  
ALA N     H      sing N N 20  
ALA N     H2     sing N N 21  
ALA CA    C      sing N N 22  
ALA CA    CB     sing N N 23  
ALA CA    HA     sing N N 24  
ALA C     O      doub N N 25  
ALA C     OXT    sing N N 26  
ALA CB    HB1    sing N N 27  
ALA CB    HB2    sing N N 28  
ALA CB    HB3    sing N N 29  
ALA OXT   HXT    sing N N 30  
ARG N     CA     sing N N 31  
ARG N     H      sing N N 32  
ARG N     H2     sing N N 33  
ARG CA    C      sing N N 34  
ARG CA    CB     sing N N 35  
ARG CA    HA     sing N N 36  
ARG C     O      doub N N 37  
ARG C     OXT    sing N N 38  
ARG CB    CG     sing N N 39  
ARG CB    HB2    sing N N 40  
ARG CB    HB3    sing N N 41  
ARG CG    CD     sing N N 42  
ARG CG    HG2    sing N N 43  
ARG CG    HG3    sing N N 44  
ARG CD    NE     sing N N 45  
ARG CD    HD2    sing N N 46  
ARG CD    HD3    sing N N 47  
ARG NE    CZ     sing N N 48  
ARG NE    HE     sing N N 49  
ARG CZ    NH1    sing N N 50  
ARG CZ    NH2    doub N N 51  
ARG NH1   HH11   sing N N 52  
ARG NH1   HH12   sing N N 53  
ARG NH2   HH21   sing N N 54  
ARG NH2   HH22   sing N N 55  
ARG OXT   HXT    sing N N 56  
ASN N     CA     sing N N 57  
ASN N     H      sing N N 58  
ASN N     H2     sing N N 59  
ASN CA    C      sing N N 60  
ASN CA    CB     sing N N 61  
ASN CA    HA     sing N N 62  
ASN C     O      doub N N 63  
ASN C     OXT    sing N N 64  
ASN CB    CG     sing N N 65  
ASN CB    HB2    sing N N 66  
ASN CB    HB3    sing N N 67  
ASN CG    OD1    doub N N 68  
ASN CG    ND2    sing N N 69  
ASN ND2   HD21   sing N N 70  
ASN ND2   HD22   sing N N 71  
ASN OXT   HXT    sing N N 72  
ASP N     CA     sing N N 73  
ASP N     H      sing N N 74  
ASP N     H2     sing N N 75  
ASP CA    C      sing N N 76  
ASP CA    CB     sing N N 77  
ASP CA    HA     sing N N 78  
ASP C     O      doub N N 79  
ASP C     OXT    sing N N 80  
ASP CB    CG     sing N N 81  
ASP CB    HB2    sing N N 82  
ASP CB    HB3    sing N N 83  
ASP CG    OD1    doub N N 84  
ASP CG    OD2    sing N N 85  
ASP OD2   HD2    sing N N 86  
ASP OXT   HXT    sing N N 87  
CYS N     CA     sing N N 88  
CYS N     H      sing N N 89  
CYS N     H2     sing N N 90  
CYS CA    C      sing N N 91  
CYS CA    CB     sing N N 92  
CYS CA    HA     sing N N 93  
CYS C     O      doub N N 94  
CYS C     OXT    sing N N 95  
CYS CB    SG     sing N N 96  
CYS CB    HB2    sing N N 97  
CYS CB    HB3    sing N N 98  
CYS SG    HG     sing N N 99  
CYS OXT   HXT    sing N N 100 
FAD PA    O1A    doub N N 101 
FAD PA    O2A    sing N N 102 
FAD PA    O5B    sing N N 103 
FAD PA    O3P    sing N N 104 
FAD O2A   HOA2   sing N N 105 
FAD O5B   C5B    sing N N 106 
FAD C5B   C4B    sing N N 107 
FAD C5B   H51A   sing N N 108 
FAD C5B   H52A   sing N N 109 
FAD C4B   O4B    sing N N 110 
FAD C4B   C3B    sing N N 111 
FAD C4B   H4B    sing N N 112 
FAD O4B   C1B    sing N N 113 
FAD C3B   O3B    sing N N 114 
FAD C3B   C2B    sing N N 115 
FAD C3B   H3B    sing N N 116 
FAD O3B   HO3A   sing N N 117 
FAD C2B   O2B    sing N N 118 
FAD C2B   C1B    sing N N 119 
FAD C2B   H2B    sing N N 120 
FAD O2B   HO2A   sing N N 121 
FAD C1B   N9A    sing N N 122 
FAD C1B   H1B    sing N N 123 
FAD N9A   C8A    sing Y N 124 
FAD N9A   C4A    sing Y N 125 
FAD C8A   N7A    doub Y N 126 
FAD C8A   H8A    sing N N 127 
FAD N7A   C5A    sing Y N 128 
FAD C5A   C6A    sing Y N 129 
FAD C5A   C4A    doub Y N 130 
FAD C6A   N6A    sing N N 131 
FAD C6A   N1A    doub Y N 132 
FAD N6A   H61A   sing N N 133 
FAD N6A   H62A   sing N N 134 
FAD N1A   C2A    sing Y N 135 
FAD C2A   N3A    doub Y N 136 
FAD C2A   H2A    sing N N 137 
FAD N3A   C4A    sing Y N 138 
FAD N1    C2     sing N N 139 
FAD N1    C10    doub N N 140 
FAD C2    O2     doub N N 141 
FAD C2    N3     sing N N 142 
FAD N3    C4     sing N N 143 
FAD N3    HN3    sing N N 144 
FAD C4    O4     doub N N 145 
FAD C4    C4X    sing N N 146 
FAD C4X   N5     doub N N 147 
FAD C4X   C10    sing N N 148 
FAD N5    C5X    sing N N 149 
FAD C5X   C6     doub Y N 150 
FAD C5X   C9A    sing Y N 151 
FAD C6    C7     sing Y N 152 
FAD C6    H6     sing N N 153 
FAD C7    C7M    sing N N 154 
FAD C7    C8     doub Y N 155 
FAD C7M   HM71   sing N N 156 
FAD C7M   HM72   sing N N 157 
FAD C7M   HM73   sing N N 158 
FAD C8    C8M    sing N N 159 
FAD C8    C9     sing Y N 160 
FAD C8M   HM81   sing N N 161 
FAD C8M   HM82   sing N N 162 
FAD C8M   HM83   sing N N 163 
FAD C9    C9A    doub Y N 164 
FAD C9    H9     sing N N 165 
FAD C9A   N10    sing N N 166 
FAD N10   C10    sing N N 167 
FAD N10   "C1'"  sing N N 168 
FAD "C1'" "C2'"  sing N N 169 
FAD "C1'" "H1'1" sing N N 170 
FAD "C1'" "H1'2" sing N N 171 
FAD "C2'" "O2'"  sing N N 172 
FAD "C2'" "C3'"  sing N N 173 
FAD "C2'" "H2'"  sing N N 174 
FAD "O2'" "HO2'" sing N N 175 
FAD "C3'" "O3'"  sing N N 176 
FAD "C3'" "C4'"  sing N N 177 
FAD "C3'" "H3'"  sing N N 178 
FAD "O3'" "HO3'" sing N N 179 
FAD "C4'" "O4'"  sing N N 180 
FAD "C4'" "C5'"  sing N N 181 
FAD "C4'" "H4'"  sing N N 182 
FAD "O4'" "HO4'" sing N N 183 
FAD "C5'" "O5'"  sing N N 184 
FAD "C5'" "H5'1" sing N N 185 
FAD "C5'" "H5'2" sing N N 186 
FAD "O5'" P      sing N N 187 
FAD P     O1P    doub N N 188 
FAD P     O2P    sing N N 189 
FAD P     O3P    sing N N 190 
FAD O2P   HOP2   sing N N 191 
FMT C     O1     doub N N 192 
FMT C     O2     sing N N 193 
FMT C     H      sing N N 194 
FMT O2    HO2    sing N N 195 
GLN N     CA     sing N N 196 
GLN N     H      sing N N 197 
GLN N     H2     sing N N 198 
GLN CA    C      sing N N 199 
GLN CA    CB     sing N N 200 
GLN CA    HA     sing N N 201 
GLN C     O      doub N N 202 
GLN C     OXT    sing N N 203 
GLN CB    CG     sing N N 204 
GLN CB    HB2    sing N N 205 
GLN CB    HB3    sing N N 206 
GLN CG    CD     sing N N 207 
GLN CG    HG2    sing N N 208 
GLN CG    HG3    sing N N 209 
GLN CD    OE1    doub N N 210 
GLN CD    NE2    sing N N 211 
GLN NE2   HE21   sing N N 212 
GLN NE2   HE22   sing N N 213 
GLN OXT   HXT    sing N N 214 
GLU N     CA     sing N N 215 
GLU N     H      sing N N 216 
GLU N     H2     sing N N 217 
GLU CA    C      sing N N 218 
GLU CA    CB     sing N N 219 
GLU CA    HA     sing N N 220 
GLU C     O      doub N N 221 
GLU C     OXT    sing N N 222 
GLU CB    CG     sing N N 223 
GLU CB    HB2    sing N N 224 
GLU CB    HB3    sing N N 225 
GLU CG    CD     sing N N 226 
GLU CG    HG2    sing N N 227 
GLU CG    HG3    sing N N 228 
GLU CD    OE1    doub N N 229 
GLU CD    OE2    sing N N 230 
GLU OE2   HE2    sing N N 231 
GLU OXT   HXT    sing N N 232 
GLY N     CA     sing N N 233 
GLY N     H      sing N N 234 
GLY N     H2     sing N N 235 
GLY CA    C      sing N N 236 
GLY CA    HA2    sing N N 237 
GLY CA    HA3    sing N N 238 
GLY C     O      doub N N 239 
GLY C     OXT    sing N N 240 
GLY OXT   HXT    sing N N 241 
HIS N     CA     sing N N 242 
HIS N     H      sing N N 243 
HIS N     H2     sing N N 244 
HIS CA    C      sing N N 245 
HIS CA    CB     sing N N 246 
HIS CA    HA     sing N N 247 
HIS C     O      doub N N 248 
HIS C     OXT    sing N N 249 
HIS CB    CG     sing N N 250 
HIS CB    HB2    sing N N 251 
HIS CB    HB3    sing N N 252 
HIS CG    ND1    sing Y N 253 
HIS CG    CD2    doub Y N 254 
HIS ND1   CE1    doub Y N 255 
HIS ND1   HD1    sing N N 256 
HIS CD2   NE2    sing Y N 257 
HIS CD2   HD2    sing N N 258 
HIS CE1   NE2    sing Y N 259 
HIS CE1   HE1    sing N N 260 
HIS NE2   HE2    sing N N 261 
HIS OXT   HXT    sing N N 262 
HOH O     H1     sing N N 263 
HOH O     H2     sing N N 264 
ILE N     CA     sing N N 265 
ILE N     H      sing N N 266 
ILE N     H2     sing N N 267 
ILE CA    C      sing N N 268 
ILE CA    CB     sing N N 269 
ILE CA    HA     sing N N 270 
ILE C     O      doub N N 271 
ILE C     OXT    sing N N 272 
ILE CB    CG1    sing N N 273 
ILE CB    CG2    sing N N 274 
ILE CB    HB     sing N N 275 
ILE CG1   CD1    sing N N 276 
ILE CG1   HG12   sing N N 277 
ILE CG1   HG13   sing N N 278 
ILE CG2   HG21   sing N N 279 
ILE CG2   HG22   sing N N 280 
ILE CG2   HG23   sing N N 281 
ILE CD1   HD11   sing N N 282 
ILE CD1   HD12   sing N N 283 
ILE CD1   HD13   sing N N 284 
ILE OXT   HXT    sing N N 285 
LEU N     CA     sing N N 286 
LEU N     H      sing N N 287 
LEU N     H2     sing N N 288 
LEU CA    C      sing N N 289 
LEU CA    CB     sing N N 290 
LEU CA    HA     sing N N 291 
LEU C     O      doub N N 292 
LEU C     OXT    sing N N 293 
LEU CB    CG     sing N N 294 
LEU CB    HB2    sing N N 295 
LEU CB    HB3    sing N N 296 
LEU CG    CD1    sing N N 297 
LEU CG    CD2    sing N N 298 
LEU CG    HG     sing N N 299 
LEU CD1   HD11   sing N N 300 
LEU CD1   HD12   sing N N 301 
LEU CD1   HD13   sing N N 302 
LEU CD2   HD21   sing N N 303 
LEU CD2   HD22   sing N N 304 
LEU CD2   HD23   sing N N 305 
LEU OXT   HXT    sing N N 306 
LYS N     CA     sing N N 307 
LYS N     H      sing N N 308 
LYS N     H2     sing N N 309 
LYS CA    C      sing N N 310 
LYS CA    CB     sing N N 311 
LYS CA    HA     sing N N 312 
LYS C     O      doub N N 313 
LYS C     OXT    sing N N 314 
LYS CB    CG     sing N N 315 
LYS CB    HB2    sing N N 316 
LYS CB    HB3    sing N N 317 
LYS CG    CD     sing N N 318 
LYS CG    HG2    sing N N 319 
LYS CG    HG3    sing N N 320 
LYS CD    CE     sing N N 321 
LYS CD    HD2    sing N N 322 
LYS CD    HD3    sing N N 323 
LYS CE    NZ     sing N N 324 
LYS CE    HE2    sing N N 325 
LYS CE    HE3    sing N N 326 
LYS NZ    HZ1    sing N N 327 
LYS NZ    HZ2    sing N N 328 
LYS NZ    HZ3    sing N N 329 
LYS OXT   HXT    sing N N 330 
MET N     CA     sing N N 331 
MET N     H      sing N N 332 
MET N     H2     sing N N 333 
MET CA    C      sing N N 334 
MET CA    CB     sing N N 335 
MET CA    HA     sing N N 336 
MET C     O      doub N N 337 
MET C     OXT    sing N N 338 
MET CB    CG     sing N N 339 
MET CB    HB2    sing N N 340 
MET CB    HB3    sing N N 341 
MET CG    SD     sing N N 342 
MET CG    HG2    sing N N 343 
MET CG    HG3    sing N N 344 
MET SD    CE     sing N N 345 
MET CE    HE1    sing N N 346 
MET CE    HE2    sing N N 347 
MET CE    HE3    sing N N 348 
MET OXT   HXT    sing N N 349 
PEG C1    O1     sing N N 350 
PEG C1    C2     sing N N 351 
PEG C1    H11    sing N N 352 
PEG C1    H12    sing N N 353 
PEG O1    HO1    sing N N 354 
PEG C2    O2     sing N N 355 
PEG C2    H21    sing N N 356 
PEG C2    H22    sing N N 357 
PEG O2    C3     sing N N 358 
PEG C3    C4     sing N N 359 
PEG C3    H31    sing N N 360 
PEG C3    H32    sing N N 361 
PEG C4    O4     sing N N 362 
PEG C4    H41    sing N N 363 
PEG C4    H42    sing N N 364 
PEG O4    HO4    sing N N 365 
PGE C1    O1     sing N N 366 
PGE C1    C2     sing N N 367 
PGE C1    H1     sing N N 368 
PGE C1    H12    sing N N 369 
PGE O1    HO1    sing N N 370 
PGE C2    O2     sing N N 371 
PGE C2    H2     sing N N 372 
PGE C2    H22    sing N N 373 
PGE O2    C3     sing N N 374 
PGE C3    C4     sing N N 375 
PGE C3    H3     sing N N 376 
PGE C3    H32    sing N N 377 
PGE C4    O3     sing N N 378 
PGE C4    H4     sing N N 379 
PGE C4    H42    sing N N 380 
PGE O4    C6     sing N N 381 
PGE O4    HO4    sing N N 382 
PGE C6    C5     sing N N 383 
PGE C6    H6     sing N N 384 
PGE C6    H62    sing N N 385 
PGE C5    O3     sing N N 386 
PGE C5    H5     sing N N 387 
PGE C5    H52    sing N N 388 
PHE N     CA     sing N N 389 
PHE N     H      sing N N 390 
PHE N     H2     sing N N 391 
PHE CA    C      sing N N 392 
PHE CA    CB     sing N N 393 
PHE CA    HA     sing N N 394 
PHE C     O      doub N N 395 
PHE C     OXT    sing N N 396 
PHE CB    CG     sing N N 397 
PHE CB    HB2    sing N N 398 
PHE CB    HB3    sing N N 399 
PHE CG    CD1    doub Y N 400 
PHE CG    CD2    sing Y N 401 
PHE CD1   CE1    sing Y N 402 
PHE CD1   HD1    sing N N 403 
PHE CD2   CE2    doub Y N 404 
PHE CD2   HD2    sing N N 405 
PHE CE1   CZ     doub Y N 406 
PHE CE1   HE1    sing N N 407 
PHE CE2   CZ     sing Y N 408 
PHE CE2   HE2    sing N N 409 
PHE CZ    HZ     sing N N 410 
PHE OXT   HXT    sing N N 411 
PRO N     CA     sing N N 412 
PRO N     CD     sing N N 413 
PRO N     H      sing N N 414 
PRO CA    C      sing N N 415 
PRO CA    CB     sing N N 416 
PRO CA    HA     sing N N 417 
PRO C     O      doub N N 418 
PRO C     OXT    sing N N 419 
PRO CB    CG     sing N N 420 
PRO CB    HB2    sing N N 421 
PRO CB    HB3    sing N N 422 
PRO CG    CD     sing N N 423 
PRO CG    HG2    sing N N 424 
PRO CG    HG3    sing N N 425 
PRO CD    HD2    sing N N 426 
PRO CD    HD3    sing N N 427 
PRO OXT   HXT    sing N N 428 
SER N     CA     sing N N 429 
SER N     H      sing N N 430 
SER N     H2     sing N N 431 
SER CA    C      sing N N 432 
SER CA    CB     sing N N 433 
SER CA    HA     sing N N 434 
SER C     O      doub N N 435 
SER C     OXT    sing N N 436 
SER CB    OG     sing N N 437 
SER CB    HB2    sing N N 438 
SER CB    HB3    sing N N 439 
SER OG    HG     sing N N 440 
SER OXT   HXT    sing N N 441 
SO4 S     O1     doub N N 442 
SO4 S     O2     doub N N 443 
SO4 S     O3     sing N N 444 
SO4 S     O4     sing N N 445 
THR N     CA     sing N N 446 
THR N     H      sing N N 447 
THR N     H2     sing N N 448 
THR CA    C      sing N N 449 
THR CA    CB     sing N N 450 
THR CA    HA     sing N N 451 
THR C     O      doub N N 452 
THR C     OXT    sing N N 453 
THR CB    OG1    sing N N 454 
THR CB    CG2    sing N N 455 
THR CB    HB     sing N N 456 
THR OG1   HG1    sing N N 457 
THR CG2   HG21   sing N N 458 
THR CG2   HG22   sing N N 459 
THR CG2   HG23   sing N N 460 
THR OXT   HXT    sing N N 461 
TRP N     CA     sing N N 462 
TRP N     H      sing N N 463 
TRP N     H2     sing N N 464 
TRP CA    C      sing N N 465 
TRP CA    CB     sing N N 466 
TRP CA    HA     sing N N 467 
TRP C     O      doub N N 468 
TRP C     OXT    sing N N 469 
TRP CB    CG     sing N N 470 
TRP CB    HB2    sing N N 471 
TRP CB    HB3    sing N N 472 
TRP CG    CD1    doub Y N 473 
TRP CG    CD2    sing Y N 474 
TRP CD1   NE1    sing Y N 475 
TRP CD1   HD1    sing N N 476 
TRP CD2   CE2    doub Y N 477 
TRP CD2   CE3    sing Y N 478 
TRP NE1   CE2    sing Y N 479 
TRP NE1   HE1    sing N N 480 
TRP CE2   CZ2    sing Y N 481 
TRP CE3   CZ3    doub Y N 482 
TRP CE3   HE3    sing N N 483 
TRP CZ2   CH2    doub Y N 484 
TRP CZ2   HZ2    sing N N 485 
TRP CZ3   CH2    sing Y N 486 
TRP CZ3   HZ3    sing N N 487 
TRP CH2   HH2    sing N N 488 
TRP OXT   HXT    sing N N 489 
TYR N     CA     sing N N 490 
TYR N     H      sing N N 491 
TYR N     H2     sing N N 492 
TYR CA    C      sing N N 493 
TYR CA    CB     sing N N 494 
TYR CA    HA     sing N N 495 
TYR C     O      doub N N 496 
TYR C     OXT    sing N N 497 
TYR CB    CG     sing N N 498 
TYR CB    HB2    sing N N 499 
TYR CB    HB3    sing N N 500 
TYR CG    CD1    doub Y N 501 
TYR CG    CD2    sing Y N 502 
TYR CD1   CE1    sing Y N 503 
TYR CD1   HD1    sing N N 504 
TYR CD2   CE2    doub Y N 505 
TYR CD2   HD2    sing N N 506 
TYR CE1   CZ     doub Y N 507 
TYR CE1   HE1    sing N N 508 
TYR CE2   CZ     sing Y N 509 
TYR CE2   HE2    sing N N 510 
TYR CZ    OH     sing N N 511 
TYR OH    HH     sing N N 512 
TYR OXT   HXT    sing N N 513 
VAL N     CA     sing N N 514 
VAL N     H      sing N N 515 
VAL N     H2     sing N N 516 
VAL CA    C      sing N N 517 
VAL CA    CB     sing N N 518 
VAL CA    HA     sing N N 519 
VAL C     O      doub N N 520 
VAL C     OXT    sing N N 521 
VAL CB    CG1    sing N N 522 
VAL CB    CG2    sing N N 523 
VAL CB    HB     sing N N 524 
VAL CG1   HG11   sing N N 525 
VAL CG1   HG12   sing N N 526 
VAL CG1   HG13   sing N N 527 
VAL CG2   HG21   sing N N 528 
VAL CG2   HG22   sing N N 529 
VAL CG2   HG23   sing N N 530 
VAL OXT   HXT    sing N N 531 
# 
_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           1R01GM132640 
_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   6X9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DL7 
_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]   0.009888 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002907 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009817 
_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]   0.008236 
_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 
F 
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     . ALA A  1 16   ? -49.851 93.654  104.102 1.00 56.43 ? 14   ALA A N     1 
ATOM   2     C CA    . ALA A  1 16   ? -48.781 92.728  104.472 1.00 57.56 ? 14   ALA A CA    1 
ATOM   3     C C     . ALA A  1 16   ? -49.312 91.302  104.558 1.00 58.72 ? 14   ALA A C     1 
ATOM   4     O O     . ALA A  1 16   ? -50.090 90.982  105.455 1.00 60.41 ? 14   ALA A O     1 
ATOM   5     C CB    . ALA A  1 16   ? -48.146 93.142  105.799 1.00 55.62 ? 14   ALA A CB    1 
ATOM   6     N N     . PRO A  1 17   ? -48.895 90.447  103.623 1.00 54.20 ? 15   PRO A N     1 
ATOM   7     C CA    . PRO A  1 17   ? -49.406 89.071  103.609 1.00 48.66 ? 15   PRO A CA    1 
ATOM   8     C C     . PRO A  1 17   ? -48.955 88.308  104.845 1.00 48.19 ? 15   PRO A C     1 
ATOM   9     O O     . PRO A  1 17   ? -47.804 88.413  105.276 1.00 47.53 ? 15   PRO A O     1 
ATOM   10    C CB    . PRO A  1 17   ? -48.804 88.478  102.328 1.00 47.93 ? 15   PRO A CB    1 
ATOM   11    C CG    . PRO A  1 17   ? -48.356 89.652  101.515 1.00 45.63 ? 15   PRO A CG    1 
ATOM   12    C CD    . PRO A  1 17   ? -47.979 90.710  102.503 1.00 49.99 ? 15   PRO A CD    1 
ATOM   13    N N     . ALA A  1 18   ? -49.883 87.550  105.425 1.00 44.99 ? 16   ALA A N     1 
ATOM   14    C CA    . ALA A  1 18   ? -49.548 86.741  106.587 1.00 38.22 ? 16   ALA A CA    1 
ATOM   15    C C     . ALA A  1 18   ? -48.477 85.718  106.214 1.00 37.05 ? 16   ALA A C     1 
ATOM   16    O O     . ALA A  1 18   ? -48.554 85.099  105.144 1.00 29.89 ? 16   ALA A O     1 
ATOM   17    C CB    . ALA A  1 18   ? -50.789 86.032  107.126 1.00 37.00 ? 16   ALA A CB    1 
ATOM   18    N N     . PRO A  1 19   ? -47.459 85.529  107.055 1.00 34.21 ? 17   PRO A N     1 
ATOM   19    C CA    . PRO A  1 19   ? -46.389 84.584  106.712 1.00 29.41 ? 17   PRO A CA    1 
ATOM   20    C C     . PRO A  1 19   ? -46.924 83.168  106.537 1.00 29.36 ? 17   PRO A C     1 
ATOM   21    O O     . PRO A  1 19   ? -47.666 82.659  107.379 1.00 29.03 ? 17   PRO A O     1 
ATOM   22    C CB    . PRO A  1 19   ? -45.430 84.685  107.906 1.00 29.94 ? 17   PRO A CB    1 
ATOM   23    C CG    . PRO A  1 19   ? -45.694 86.039  108.486 1.00 33.87 ? 17   PRO A CG    1 
ATOM   24    C CD    . PRO A  1 19   ? -47.175 86.266  108.298 1.00 31.74 ? 17   PRO A CD    1 
ATOM   25    N N     . PHE A  1 20   ? -46.541 82.538  105.425 1.00 27.02 ? 18   PHE A N     1 
ATOM   26    C CA    . PHE A  1 20   ? -46.819 81.141  105.104 1.00 24.89 ? 18   PHE A CA    1 
ATOM   27    C C     . PHE A  1 20   ? -48.296 80.870  104.848 1.00 29.49 ? 18   PHE A C     1 
ATOM   28    O O     . PHE A  1 20   ? -48.688 79.705  104.741 1.00 28.58 ? 18   PHE A O     1 
ATOM   29    C CB    . PHE A  1 20   ? -46.323 80.186  106.199 1.00 26.52 ? 18   PHE A CB    1 
ATOM   30    C CG    . PHE A  1 20   ? -44.834 80.218  106.407 1.00 21.87 ? 18   PHE A CG    1 
ATOM   31    C CD1   . PHE A  1 20   ? -43.972 79.684  105.452 1.00 21.93 ? 18   PHE A CD1   1 
ATOM   32    C CD2   . PHE A  1 20   ? -44.292 80.760  107.566 1.00 25.35 ? 18   PHE A CD2   1 
ATOM   33    C CE1   . PHE A  1 20   ? -42.594 79.704  105.642 1.00 23.62 ? 18   PHE A CE1   1 
ATOM   34    C CE2   . PHE A  1 20   ? -42.914 80.783  107.755 1.00 23.61 ? 18   PHE A CE2   1 
ATOM   35    C CZ    . PHE A  1 20   ? -42.068 80.258  106.805 1.00 24.06 ? 18   PHE A CZ    1 
ATOM   36    N N     . ALA A  1 21   ? -49.131 81.907  104.753 1.00 26.43 ? 19   ALA A N     1 
ATOM   37    C CA    . ALA A  1 21   ? -50.553 81.683  104.505 1.00 33.92 ? 19   ALA A CA    1 
ATOM   38    C C     . ALA A  1 21   ? -50.803 81.070  103.131 1.00 32.04 ? 19   ALA A C     1 
ATOM   39    O O     . ALA A  1 21   ? -51.854 80.454  102.922 1.00 36.09 ? 19   ALA A O     1 
ATOM   40    C CB    . ALA A  1 21   ? -51.330 82.993  104.659 1.00 35.46 ? 19   ALA A CB    1 
ATOM   41    N N     . ASP A  1 22   ? -49.856 81.197  102.204 1.00 27.02 ? 20   ASP A N     1 
ATOM   42    C CA    . ASP A  1 22   ? -49.964 80.636  100.864 1.00 29.45 ? 20   ASP A CA    1 
ATOM   43    C C     . ASP A  1 22   ? -48.753 79.767  100.530 1.00 27.23 ? 20   ASP A C     1 
ATOM   44    O O     . ASP A  1 22   ? -48.276 79.760  99.394  1.00 27.47 ? 20   ASP A O     1 
ATOM   45    C CB    . ASP A  1 22   ? -50.126 81.747  99.829  1.00 31.13 ? 20   ASP A CB    1 
ATOM   46    N N     . PHE A  1 23   ? -48.240 79.014  101.509 1.00 24.77 ? 21   PHE A N     1 
ATOM   47    C CA    . PHE A  1 23   ? -46.968 78.324  101.326 1.00 25.31 ? 21   PHE A CA    1 
ATOM   48    C C     . PHE A  1 23   ? -47.016 77.357  100.147 1.00 23.47 ? 21   PHE A C     1 
ATOM   49    O O     . PHE A  1 23   ? -46.193 77.438  99.229  1.00 22.33 ? 21   PHE A O     1 
ATOM   50    C CB    . PHE A  1 23   ? -46.563 77.584  102.609 1.00 21.96 ? 21   PHE A CB    1 
ATOM   51    C CG    . PHE A  1 23   ? -45.313 76.757  102.450 1.00 21.02 ? 21   PHE A CG    1 
ATOM   52    C CD1   . PHE A  1 23   ? -44.105 77.367  102.135 1.00 24.00 ? 21   PHE A CD1   1 
ATOM   53    C CD2   . PHE A  1 23   ? -45.341 75.376  102.600 1.00 25.37 ? 21   PHE A CD2   1 
ATOM   54    C CE1   . PHE A  1 23   ? -42.952 76.630  101.964 1.00 21.15 ? 21   PHE A CE1   1 
ATOM   55    C CE2   . PHE A  1 23   ? -44.186 74.622  102.430 1.00 25.20 ? 21   PHE A CE2   1 
ATOM   56    C CZ    . PHE A  1 23   ? -42.983 75.253  102.115 1.00 22.24 ? 21   PHE A CZ    1 
ATOM   57    N N     . ALA A  1 24   ? -47.981 76.441  100.155 1.00 23.60 ? 22   ALA A N     1 
ATOM   58    C CA    . ALA A  1 24   ? -48.044 75.357  99.182  1.00 26.22 ? 22   ALA A CA    1 
ATOM   59    C C     . ALA A  1 24   ? -49.451 74.783  99.042  1.00 27.06 ? 22   ALA A C     1 
ATOM   60    O O     . ALA A  1 24   ? -49.619 73.555  99.112  1.00 26.15 ? 22   ALA A O     1 
ATOM   61    C CB    . ALA A  1 24   ? -47.089 74.227  99.579  1.00 26.55 ? 22   ALA A CB    1 
ATOM   62    N N     . PRO A  1 25   ? -50.472 75.607  98.822  1.00 28.85 ? 23   PRO A N     1 
ATOM   63    C CA    . PRO A  1 25   ? -51.841 75.076  98.721  1.00 28.14 ? 23   PRO A CA    1 
ATOM   64    C C     . PRO A  1 25   ? -51.935 74.086  97.577  1.00 26.08 ? 23   PRO A C     1 
ATOM   65    O O     . PRO A  1 25   ? -51.350 74.311  96.509  1.00 26.02 ? 23   PRO A O     1 
ATOM   66    C CB    . PRO A  1 25   ? -52.691 76.326  98.451  1.00 29.78 ? 23   PRO A CB    1 
ATOM   67    C CG    . PRO A  1 25   ? -51.756 77.267  97.784  1.00 31.13 ? 23   PRO A CG    1 
ATOM   68    C CD    . PRO A  1 25   ? -50.404 77.026  98.430  1.00 25.50 ? 23   PRO A CD    1 
ATOM   69    N N     . PRO A  1 26   ? -52.616 72.963  97.777  1.00 24.93 ? 24   PRO A N     1 
ATOM   70    C CA    . PRO A  1 26   ? -52.717 71.958  96.714  1.00 25.33 ? 24   PRO A CA    1 
ATOM   71    C C     . PRO A  1 26   ? -53.582 72.444  95.562  1.00 25.32 ? 24   PRO A C     1 
ATOM   72    O O     . PRO A  1 26   ? -54.408 73.352  95.698  1.00 23.26 ? 24   PRO A O     1 
ATOM   73    C CB    . PRO A  1 26   ? -53.370 70.766  97.417  1.00 26.75 ? 24   PRO A CB    1 
ATOM   74    C CG    . PRO A  1 26   ? -54.191 71.418  98.519  1.00 29.47 ? 24   PRO A CG    1 
ATOM   75    C CD    . PRO A  1 26   ? -53.338 72.557  98.996  1.00 29.73 ? 24   PRO A CD    1 
ATOM   76    N N     . VAL A  1 27   ? -53.371 71.810  94.405  1.00 26.11 ? 25   VAL A N     1 
ATOM   77    C CA    . VAL A  1 27   ? -54.165 72.135  93.220  1.00 26.71 ? 25   VAL A CA    1 
ATOM   78    C C     . VAL A  1 27   ? -55.651 71.934  93.499  1.00 28.33 ? 25   VAL A C     1 
ATOM   79    O O     . VAL A  1 27   ? -56.480 72.778  93.139  1.00 27.01 ? 25   VAL A O     1 
ATOM   80    C CB    . VAL A  1 27   ? -53.676 71.308  92.017  1.00 28.92 ? 25   VAL A CB    1 
ATOM   81    C CG1   . VAL A  1 27   ? -54.646 71.412  90.837  1.00 25.39 ? 25   VAL A CG1   1 
ATOM   82    C CG2   . VAL A  1 27   ? -52.284 71.774  91.616  1.00 26.39 ? 25   VAL A CG2   1 
ATOM   83    N N     . ARG A  1 28   ? -56.008 70.854  94.189  1.00 27.10 ? 26   ARG A N     1 
ATOM   84    C CA    . ARG A  1 28   ? -57.399 70.595  94.526  1.00 28.00 ? 26   ARG A CA    1 
ATOM   85    C C     . ARG A  1 28   ? -57.458 69.887  95.870  1.00 34.03 ? 26   ARG A C     1 
ATOM   86    O O     . ARG A  1 28   ? -56.466 69.290  96.304  1.00 29.97 ? 26   ARG A O     1 
ATOM   87    C CB    . ARG A  1 28   ? -58.084 69.746  93.442  1.00 33.28 ? 26   ARG A CB    1 
ATOM   88    C CG    . ARG A  1 28   ? -57.625 68.299  93.434  1.00 32.79 ? 26   ARG A CG    1 
ATOM   89    C CD    . ARG A  1 28   ? -58.276 67.487  92.326  1.00 32.88 ? 26   ARG A CD    1 
ATOM   90    N NE    . ARG A  1 28   ? -57.555 67.625  91.066  1.00 35.58 ? 26   ARG A NE    1 
ATOM   91    C CZ    . ARG A  1 28   ? -57.930 68.422  90.076  1.00 40.12 ? 26   ARG A CZ    1 
ATOM   92    N NH1   . ARG A  1 28   ? -59.054 69.122  90.139  1.00 41.05 ? 26   ARG A NH1   1 
ATOM   93    N NH2   . ARG A  1 28   ? -57.160 68.518  88.995  1.00 33.49 ? 26   ARG A NH2   1 
ATOM   94    N N     . PRO A  1 29   ? -58.607 69.931  96.553  1.00 32.45 ? 27   PRO A N     1 
ATOM   95    C CA    . PRO A  1 29   ? -58.755 69.134  97.777  1.00 33.48 ? 27   PRO A CA    1 
ATOM   96    C C     . PRO A  1 29   ? -58.524 67.659  97.480  1.00 30.61 ? 27   PRO A C     1 
ATOM   97    O O     . PRO A  1 29   ? -58.944 67.143  96.444  1.00 29.53 ? 27   PRO A O     1 
ATOM   98    C CB    . PRO A  1 29   ? -60.200 69.412  98.214  1.00 32.70 ? 27   PRO A CB    1 
ATOM   99    C CG    . PRO A  1 29   ? -60.549 70.717  97.578  1.00 35.44 ? 27   PRO A CG    1 
ATOM   100   C CD    . PRO A  1 29   ? -59.826 70.707  96.254  1.00 35.95 ? 27   PRO A CD    1 
ATOM   101   N N     . GLN A  1 30   ? -57.830 66.986  98.392  1.00 30.49 ? 28   GLN A N     1 
ATOM   102   C CA    . GLN A  1 30   ? -57.365 65.624  98.148  1.00 29.23 ? 28   GLN A CA    1 
ATOM   103   C C     . GLN A  1 30   ? -58.475 64.637  98.495  1.00 32.81 ? 28   GLN A C     1 
ATOM   104   O O     . GLN A  1 30   ? -58.842 64.485  99.664  1.00 29.93 ? 28   GLN A O     1 
ATOM   105   C CB    . GLN A  1 30   ? -56.104 65.341  98.962  1.00 27.13 ? 28   GLN A CB    1 
ATOM   106   C CG    . GLN A  1 30   ? -54.919 66.278  98.648  1.00 26.60 ? 28   GLN A CG    1 
ATOM   107   C CD    . GLN A  1 30   ? -54.370 66.079  97.242  1.00 28.42 ? 28   GLN A CD    1 
ATOM   108   O OE1   . GLN A  1 30   ? -53.679 65.101  96.970  1.00 26.31 ? 28   GLN A OE1   1 
ATOM   109   N NE2   . GLN A  1 30   ? -54.690 67.003  96.340  1.00 29.55 ? 28   GLN A NE2   1 
ATOM   110   N N     . SER A  1 31   ? -58.990 63.946  97.482  1.00 30.88 ? 29   SER A N     1 
ATOM   111   C CA    . SER A  1 31   ? -60.021 62.942  97.684  1.00 30.02 ? 29   SER A CA    1 
ATOM   112   C C     . SER A  1 31   ? -59.475 61.759  98.483  1.00 29.85 ? 29   SER A C     1 
ATOM   113   O O     . SER A  1 31   ? -58.266 61.585  98.652  1.00 25.99 ? 29   SER A O     1 
ATOM   114   C CB    . SER A  1 31   ? -60.562 62.455  96.340  1.00 30.36 ? 29   SER A CB    1 
ATOM   115   O OG    . SER A  1 31   ? -59.611 61.641  95.666  1.00 27.09 ? 29   SER A OG    1 
ATOM   116   N N     . THR A  1 32   ? -60.399 60.946  98.994  1.00 25.78 ? 30   THR A N     1 
ATOM   117   C CA    . THR A  1 32   ? -60.030 59.674  99.608  1.00 28.98 ? 30   THR A CA    1 
ATOM   118   C C     . THR A  1 32   ? -59.057 58.892  98.727  1.00 28.72 ? 30   THR A C     1 
ATOM   119   O O     . THR A  1 32   ? -58.044 58.379  99.208  1.00 23.81 ? 30   THR A O     1 
ATOM   120   C CB    . THR A  1 32   ? -61.287 58.848  99.881  1.00 32.13 ? 30   THR A CB    1 
ATOM   121   O OG1   . THR A  1 32   ? -62.181 59.608  100.699 1.00 34.53 ? 30   THR A OG1   1 
ATOM   122   C CG2   . THR A  1 32   ? -60.937 57.564  100.607 1.00 32.60 ? 30   THR A CG2   1 
ATOM   123   N N     . LEU A  1 33   ? -59.347 58.802  97.426  1.00 26.02 ? 31   LEU A N     1 
ATOM   124   C CA    . LEU A  1 33   ? -58.498 58.016  96.532  1.00 27.79 ? 31   LEU A CA    1 
ATOM   125   C C     . LEU A  1 33   ? -57.129 58.657  96.341  1.00 24.36 ? 31   LEU A C     1 
ATOM   126   O O     . LEU A  1 33   ? -56.124 57.949  96.216  1.00 23.10 ? 31   LEU A O     1 
ATOM   127   C CB    . LEU A  1 33   ? -59.185 57.831  95.185  1.00 25.55 ? 31   LEU A CB    1 
ATOM   128   C CG    . LEU A  1 33   ? -60.352 56.855  95.227  1.00 29.96 ? 31   LEU A CG    1 
ATOM   129   C CD1   . LEU A  1 33   ? -61.221 57.034  93.975  1.00 24.24 ? 31   LEU A CD1   1 
ATOM   130   C CD2   . LEU A  1 33   ? -59.824 55.427  95.350  1.00 27.16 ? 31   LEU A CD2   1 
ATOM   131   N N     . ARG A  1 34   ? -57.074 59.992  96.287  1.00 22.78 ? 32   ARG A N     1 
ATOM   132   C CA    . ARG A  1 34   ? -55.784 60.665  96.179  1.00 21.73 ? 32   ARG A CA    1 
ATOM   133   C C     . ARG A  1 34   ? -54.983 60.505  97.461  1.00 24.08 ? 32   ARG A C     1 
ATOM   134   O O     . ARG A  1 34   ? -53.759 60.352  97.416  1.00 23.25 ? 32   ARG A O     1 
ATOM   135   C CB    . ARG A  1 34   ? -55.970 62.149  95.869  1.00 25.75 ? 32   ARG A CB    1 
ATOM   136   C CG    . ARG A  1 34   ? -56.471 62.449  94.467  1.00 25.38 ? 32   ARG A CG    1 
ATOM   137   C CD    . ARG A  1 34   ? -55.377 62.254  93.411  1.00 24.96 ? 32   ARG A CD    1 
ATOM   138   N NE    . ARG A  1 34   ? -54.257 63.174  93.576  1.00 24.68 ? 32   ARG A NE    1 
ATOM   139   C CZ    . ARG A  1 34   ? -54.110 64.316  92.913  1.00 28.04 ? 32   ARG A CZ    1 
ATOM   140   N NH1   . ARG A  1 34   ? -55.024 64.742  92.054  1.00 27.00 ? 32   ARG A NH1   1 
ATOM   141   N NH2   . ARG A  1 34   ? -53.021 65.051  93.118  1.00 26.78 ? 32   ARG A NH2   1 
ATOM   142   N N     . ARG A  1 35   ? -55.655 60.560  98.617  1.00 24.26 ? 33   ARG A N     1 
ATOM   143   C CA    . ARG A  1 35   ? -54.939 60.398  99.875  1.00 28.15 ? 33   ARG A CA    1 
ATOM   144   C C     . ARG A  1 35   ? -54.362 58.993  100.014 1.00 25.49 ? 33   ARG A C     1 
ATOM   145   O O     . ARG A  1 35   ? -53.282 58.829  100.593 1.00 24.11 ? 33   ARG A O     1 
ATOM   146   C CB    . ARG A  1 35   ? -55.849 60.734  101.061 1.00 29.27 ? 33   ARG A CB    1 
ATOM   147   C CG    . ARG A  1 35   ? -56.320 62.190  101.097 1.00 33.98 ? 33   ARG A CG    1 
ATOM   148   C CD    . ARG A  1 35   ? -56.966 62.548  102.446 1.00 36.98 ? 33   ARG A CD    1 
ATOM   149   N NE    . ARG A  1 35   ? -55.961 62.956  103.423 1.00 44.56 ? 33   ARG A NE    1 
ATOM   150   C CZ    . ARG A  1 35   ? -56.190 63.168  104.713 1.00 48.50 ? 33   ARG A CZ    1 
ATOM   151   N NH1   . ARG A  1 35   ? -57.399 63.025  105.238 1.00 50.44 ? 33   ARG A NH1   1 
ATOM   152   N NH2   . ARG A  1 35   ? -55.177 63.524  105.500 1.00 47.40 ? 33   ARG A NH2   1 
ATOM   153   N N     . ALA A  1 36   ? -55.041 57.977  99.479  1.00 24.06 ? 34   ALA A N     1 
ATOM   154   C CA    . ALA A  1 36   ? -54.496 56.622  99.577  1.00 25.56 ? 34   ALA A CA    1 
ATOM   155   C C     . ALA A  1 36   ? -53.250 56.463  98.709  1.00 25.24 ? 34   ALA A C     1 
ATOM   156   O O     . ALA A  1 36   ? -52.344 55.690  99.046  1.00 23.39 ? 34   ALA A O     1 
ATOM   157   C CB    . ALA A  1 36   ? -55.560 55.594  99.184  1.00 24.99 ? 34   ALA A CB    1 
ATOM   158   N N     . ILE A  1 37   ? -53.197 57.186  97.590  1.00 22.48 ? 35   ILE A N     1 
ATOM   159   C CA    . ILE A  1 37   ? -51.972 57.269  96.802  1.00 20.83 ? 35   ILE A CA    1 
ATOM   160   C C     . ILE A  1 37   ? -50.837 57.859  97.635  1.00 24.47 ? 35   ILE A C     1 
ATOM   161   O O     . ILE A  1 37   ? -49.758 57.264  97.756  1.00 20.55 ? 35   ILE A O     1 
ATOM   162   C CB    . ILE A  1 37   ? -52.223 58.097  95.530  1.00 21.35 ? 35   ILE A CB    1 
ATOM   163   C CG1   . ILE A  1 37   ? -53.273 57.402  94.668  1.00 20.18 ? 35   ILE A CG1   1 
ATOM   164   C CG2   . ILE A  1 37   ? -50.909 58.318  94.766  1.00 20.64 ? 35   ILE A CG2   1 
ATOM   165   C CD1   . ILE A  1 37   ? -53.666 58.223  93.431  1.00 20.16 ? 35   ILE A CD1   1 
ATOM   166   N N     . THR A  1 38   ? -51.075 59.028  98.242  1.00 25.71 ? 36   THR A N     1 
ATOM   167   C CA    . THR A  1 38   ? -50.010 59.722  98.963  1.00 21.40 ? 36   THR A CA    1 
ATOM   168   C C     . THR A  1 38   ? -49.512 58.899  100.138 1.00 24.92 ? 36   THR A C     1 
ATOM   169   O O     . THR A  1 38   ? -48.304 58.861  100.413 1.00 21.97 ? 36   THR A O     1 
ATOM   170   C CB    . THR A  1 38   ? -50.502 61.085  99.448  1.00 24.06 ? 36   THR A CB    1 
ATOM   171   O OG1   . THR A  1 38   ? -51.047 61.813  98.343  1.00 25.14 ? 36   THR A OG1   1 
ATOM   172   C CG2   . THR A  1 38   ? -49.354 61.880  100.031 1.00 23.53 ? 36   THR A CG2   1 
ATOM   173   N N     . ALA A  1 39   ? -50.431 58.233  100.838 1.00 22.15 ? 37   ALA A N     1 
ATOM   174   C CA    . ALA A  1 39   ? -50.067 57.408  101.984 1.00 24.20 ? 37   ALA A CA    1 
ATOM   175   C C     . ALA A  1 39   ? -49.083 56.310  101.613 1.00 25.82 ? 37   ALA A C     1 
ATOM   176   O O     . ALA A  1 39   ? -48.282 55.895  102.455 1.00 25.18 ? 37   ALA A O     1 
ATOM   177   C CB    . ALA A  1 39   ? -51.326 56.793  102.617 1.00 25.38 ? 37   ALA A CB    1 
ATOM   178   N N     . ALA A  1 40   ? -49.122 55.831  100.373 1.00 22.09 ? 38   ALA A N     1 
ATOM   179   C CA    . ALA A  1 40   ? -48.277 54.731  99.917  1.00 22.83 ? 38   ALA A CA    1 
ATOM   180   C C     . ALA A  1 40   ? -46.936 55.184  99.342  1.00 23.82 ? 38   ALA A C     1 
ATOM   181   O O     . ALA A  1 40   ? -46.142 54.333  98.930  1.00 25.51 ? 38   ALA A O     1 
ATOM   182   C CB    . ALA A  1 40   ? -49.026 53.907  98.862  1.00 23.67 ? 38   ALA A CB    1 
ATOM   183   N N     . TYR A  1 41   ? -46.667 56.492  99.323  1.00 22.29 ? 39   TYR A N     1 
ATOM   184   C CA    . TYR A  1 41   ? -45.515 57.047  98.616  1.00 21.55 ? 39   TYR A CA    1 
ATOM   185   C C     . TYR A  1 41   ? -44.222 56.322  98.978  1.00 20.42 ? 39   TYR A C     1 
ATOM   186   O O     . TYR A  1 41   ? -43.496 55.849  98.099  1.00 21.74 ? 39   TYR A O     1 
ATOM   187   C CB    . TYR A  1 41   ? -45.425 58.547  98.930  1.00 21.69 ? 39   TYR A CB    1 
ATOM   188   C CG    . TYR A  1 41   ? -44.679 59.440  97.956  1.00 23.39 ? 39   TYR A CG    1 
ATOM   189   C CD1   . TYR A  1 41   ? -43.599 58.976  97.205  1.00 20.08 ? 39   TYR A CD1   1 
ATOM   190   C CD2   . TYR A  1 41   ? -45.040 60.778  97.826  1.00 25.34 ? 39   TYR A CD2   1 
ATOM   191   C CE1   . TYR A  1 41   ? -42.924 59.830  96.330  1.00 18.42 ? 39   TYR A CE1   1 
ATOM   192   C CE2   . TYR A  1 41   ? -44.384 61.627  96.978  1.00 20.03 ? 39   TYR A CE2   1 
ATOM   193   C CZ    . TYR A  1 41   ? -43.323 61.145  96.220  1.00 20.03 ? 39   TYR A CZ    1 
ATOM   194   O OH    . TYR A  1 41   ? -42.663 61.996  95.373  1.00 20.72 ? 39   TYR A OH    1 
ATOM   195   N N     . ARG A  1 42   ? -43.928 56.207  100.269 1.00 22.92 ? 40   ARG A N     1 
ATOM   196   C CA    . ARG A  1 42   ? -42.696 55.588  100.744 1.00 23.16 ? 40   ARG A CA    1 
ATOM   197   C C     . ARG A  1 42   ? -42.985 54.484  101.756 1.00 24.97 ? 40   ARG A C     1 
ATOM   198   O O     . ARG A  1 42   ? -42.227 54.271  102.710 1.00 25.23 ? 40   ARG A O     1 
ATOM   199   C CB    . ARG A  1 42   ? -41.765 56.646  101.334 1.00 27.12 ? 40   ARG A CB    1 
ATOM   200   C CG    . ARG A  1 42   ? -41.241 57.575  100.254 1.00 25.36 ? 40   ARG A CG    1 
ATOM   201   C CD    . ARG A  1 42   ? -40.573 58.821  100.776 1.00 24.97 ? 40   ARG A CD    1 
ATOM   202   N NE    . ARG A  1 42   ? -40.542 59.841  99.737  1.00 21.67 ? 40   ARG A NE    1 
ATOM   203   C CZ    . ARG A  1 42   ? -39.725 59.848  98.692  1.00 21.62 ? 40   ARG A CZ    1 
ATOM   204   N NH1   . ARG A  1 42   ? -38.773 58.939  98.546  1.00 21.51 ? 40   ARG A NH1   1 
ATOM   205   N NH2   . ARG A  1 42   ? -39.857 60.804  97.772  1.00 22.20 ? 40   ARG A NH2   1 
ATOM   206   N N     . ARG A  1 43   ? -44.058 53.740  101.541 1.00 22.72 ? 41   ARG A N     1 
ATOM   207   C CA    . ARG A  1 43   ? -44.436 52.682  102.472 1.00 29.19 ? 41   ARG A CA    1 
ATOM   208   C C     . ARG A  1 43   ? -43.371 51.587  102.495 1.00 25.08 ? 41   ARG A C     1 
ATOM   209   O O     . ARG A  1 43   ? -42.778 51.277  101.457 1.00 25.20 ? 41   ARG A O     1 
ATOM   210   C CB    . ARG A  1 43   ? -45.790 52.099  102.071 1.00 23.85 ? 41   ARG A CB    1 
ATOM   211   C CG    . ARG A  1 43   ? -46.274 50.909  102.875 1.00 25.71 ? 41   ARG A CG    1 
ATOM   212   C CD    . ARG A  1 43   ? -47.695 50.601  102.486 1.00 26.04 ? 41   ARG A CD    1 
ATOM   213   N NE    . ARG A  1 43   ? -48.584 51.720  102.779 1.00 25.19 ? 41   ARG A NE    1 
ATOM   214   C CZ    . ARG A  1 43   ? -49.717 51.951  102.128 1.00 29.77 ? 41   ARG A CZ    1 
ATOM   215   N NH1   . ARG A  1 43   ? -50.136 51.145  101.166 1.00 26.76 ? 41   ARG A NH1   1 
ATOM   216   N NH2   . ARG A  1 43   ? -50.452 53.009  102.455 1.00 25.80 ? 41   ARG A NH2   1 
ATOM   217   N N     . PRO A  1 44   ? -43.103 50.989  103.656 1.00 29.18 ? 42   PRO A N     1 
ATOM   218   C CA    . PRO A  1 44   ? -42.105 49.915  103.735 1.00 26.99 ? 42   PRO A CA    1 
ATOM   219   C C     . PRO A  1 44   ? -42.365 48.804  102.730 1.00 28.08 ? 42   PRO A C     1 
ATOM   220   O O     . PRO A  1 44   ? -43.502 48.389  102.516 1.00 26.41 ? 42   PRO A O     1 
ATOM   221   C CB    . PRO A  1 44   ? -42.260 49.411  105.176 1.00 27.27 ? 42   PRO A CB    1 
ATOM   222   C CG    . PRO A  1 44   ? -42.640 50.642  105.931 1.00 28.21 ? 42   PRO A CG    1 
ATOM   223   C CD    . PRO A  1 44   ? -43.578 51.395  104.993 1.00 27.98 ? 42   PRO A CD    1 
ATOM   224   N N     . GLU A  1 45   ? -41.284 48.310  102.120 1.00 28.57 ? 43   GLU A N     1 
ATOM   225   C CA    . GLU A  1 45   ? -41.416 47.263  101.113 1.00 27.23 ? 43   GLU A CA    1 
ATOM   226   C C     . GLU A  1 45   ? -42.048 45.999  101.683 1.00 25.62 ? 43   GLU A C     1 
ATOM   227   O O     . GLU A  1 45   ? -42.810 45.326  100.984 1.00 27.10 ? 43   GLU A O     1 
ATOM   228   C CB    . GLU A  1 45   ? -40.046 46.961  100.500 1.00 30.02 ? 43   GLU A CB    1 
ATOM   229   C CG    . GLU A  1 45   ? -40.045 47.069  98.991  1.00 30.78 ? 43   GLU A CG    1 
ATOM   230   C CD    . GLU A  1 45   ? -38.657 46.970  98.368  1.00 27.46 ? 43   GLU A CD    1 
ATOM   231   O OE1   . GLU A  1 45   ? -37.692 47.577  98.901  1.00 27.08 ? 43   GLU A OE1   1 
ATOM   232   O OE2   . GLU A  1 45   ? -38.545 46.291  97.326  1.00 27.13 ? 43   GLU A OE2   1 
ATOM   233   N N     . THR A  1 46   ? -41.766 45.671  102.952 1.00 27.24 ? 44   THR A N     1 
ATOM   234   C CA    . THR A  1 46   ? -42.414 44.530  103.598 1.00 29.25 ? 44   THR A CA    1 
ATOM   235   C C     . THR A  1 46   ? -43.918 44.720  103.770 1.00 30.95 ? 44   THR A C     1 
ATOM   236   O O     . THR A  1 46   ? -44.636 43.730  103.930 1.00 33.98 ? 44   THR A O     1 
ATOM   237   C CB    . THR A  1 46   ? -41.801 44.260  104.973 1.00 28.88 ? 44   THR A CB    1 
ATOM   238   O OG1   . THR A  1 46   ? -41.871 45.456  105.767 1.00 28.72 ? 44   THR A OG1   1 
ATOM   239   C CG2   . THR A  1 46   ? -40.346 43.810  104.844 1.00 30.82 ? 44   THR A CG2   1 
ATOM   240   N N     . GLU A  1 47   ? -44.411 45.955  103.762 1.00 28.60 ? 45   GLU A N     1 
ATOM   241   C CA    . GLU A  1 47   ? -45.851 46.170  103.829 1.00 30.72 ? 45   GLU A CA    1 
ATOM   242   C C     . GLU A  1 47   ? -46.491 46.221  102.453 1.00 28.11 ? 45   GLU A C     1 
ATOM   243   O O     . GLU A  1 47   ? -47.666 45.874  102.317 1.00 28.55 ? 45   GLU A O     1 
ATOM   244   C CB    . GLU A  1 47   ? -46.163 47.459  104.593 1.00 31.50 ? 45   GLU A CB    1 
ATOM   245   C CG    . GLU A  1 47   ? -45.560 47.478  105.989 1.00 34.77 ? 45   GLU A CG    1 
ATOM   246   C CD    . GLU A  1 47   ? -45.885 48.747  106.758 1.00 39.00 ? 45   GLU A CD    1 
ATOM   247   O OE1   . GLU A  1 47   ? -46.534 49.649  106.183 1.00 36.94 ? 45   GLU A OE1   1 
ATOM   248   O OE2   . GLU A  1 47   ? -45.493 48.835  107.945 1.00 48.08 ? 45   GLU A OE2   1 
ATOM   249   N N     . CYS A  1 48   ? -45.729 46.620  101.430 1.00 28.77 ? 46   CYS A N     1 
ATOM   250   C CA    . CYS A  1 48   ? -46.265 46.687  100.070 1.00 26.98 ? 46   CYS A CA    1 
ATOM   251   C C     . CYS A  1 48   ? -46.499 45.300  99.485  1.00 28.67 ? 46   CYS A C     1 
ATOM   252   O O     . CYS A  1 48   ? -47.517 45.061  98.823  1.00 29.08 ? 46   CYS A O     1 
ATOM   253   C CB    . CYS A  1 48   ? -45.303 47.451  99.164  1.00 23.12 ? 46   CYS A CB    1 
ATOM   254   S SG    . CYS A  1 48   ? -45.168 49.207  99.516  1.00 27.63 ? 46   CYS A SG    1 
ATOM   255   N N     . LEU A  1 49   ? -45.560 44.386  99.687  1.00 25.10 ? 47   LEU A N     1 
ATOM   256   C CA    . LEU A  1 49   ? -45.527 43.179  98.864  1.00 28.85 ? 47   LEU A CA    1 
ATOM   257   C C     . LEU A  1 49   ? -46.642 42.177  99.164  1.00 26.67 ? 47   LEU A C     1 
ATOM   258   O O     . LEU A  1 49   ? -47.216 41.646  98.204  1.00 29.95 ? 47   LEU A O     1 
ATOM   259   C CB    . LEU A  1 49   ? -44.155 42.497  98.959  1.00 27.56 ? 47   LEU A CB    1 
ATOM   260   C CG    . LEU A  1 49   ? -43.156 42.921  97.862  1.00 28.53 ? 47   LEU A CG    1 
ATOM   261   C CD1   . LEU A  1 49   ? -43.578 42.407  96.497  1.00 29.16 ? 47   LEU A CD1   1 
ATOM   262   C CD2   . LEU A  1 49   ? -43.030 44.425  97.794  1.00 25.67 ? 47   LEU A CD2   1 
ATOM   263   N N     . PRO A  1 50   ? -47.002 41.890  100.424 1.00 31.91 ? 48   PRO A N     1 
ATOM   264   C CA    . PRO A  1 50   ? -48.009 40.822  100.683 1.00 29.17 ? 48   PRO A CA    1 
ATOM   265   C C     . PRO A  1 50   ? -49.322 41.039  99.942  1.00 29.19 ? 48   PRO A C     1 
ATOM   266   O O     . PRO A  1 50   ? -49.842 40.079  99.354  1.00 29.39 ? 48   PRO A O     1 
ATOM   267   C CB    . PRO A  1 50   ? -48.194 40.863  102.210 1.00 32.95 ? 48   PRO A CB    1 
ATOM   268   C CG    . PRO A  1 50   ? -46.835 41.247  102.709 1.00 30.29 ? 48   PRO A CG    1 
ATOM   269   C CD    . PRO A  1 50   ? -46.360 42.313  101.689 1.00 28.36 ? 48   PRO A CD    1 
ATOM   270   N N     . PRO A  1 51   ? -49.906 42.250  99.926  1.00 28.33 ? 49   PRO A N     1 
ATOM   271   C CA    . PRO A  1 51   ? -51.132 42.417  99.127  1.00 31.18 ? 49   PRO A CA    1 
ATOM   272   C C     . PRO A  1 51   ? -50.892 42.306  97.632  1.00 30.36 ? 49   PRO A C     1 
ATOM   273   O O     . PRO A  1 51   ? -51.810 41.916  96.902  1.00 33.87 ? 49   PRO A O     1 
ATOM   274   C CB    . PRO A  1 51   ? -51.634 43.820  99.511  1.00 29.63 ? 49   PRO A CB    1 
ATOM   275   C CG    . PRO A  1 51   ? -50.444 44.527  100.008 1.00 31.42 ? 49   PRO A CG    1 
ATOM   276   C CD    . PRO A  1 51   ? -49.594 43.486  100.677 1.00 29.88 ? 49   PRO A CD    1 
ATOM   277   N N     . LEU A  1 52   ? -49.700 42.663  97.146  1.00 28.97 ? 50   LEU A N     1 
ATOM   278   C CA    . LEU A  1 52   ? -49.390 42.424  95.741  1.00 27.11 ? 50   LEU A CA    1 
ATOM   279   C C     . LEU A  1 52   ? -49.303 40.926  95.461  1.00 29.99 ? 50   LEU A C     1 
ATOM   280   O O     . LEU A  1 52   ? -49.903 40.427  94.500  1.00 29.72 ? 50   LEU A O     1 
ATOM   281   C CB    . LEU A  1 52   ? -48.093 43.146  95.353  1.00 26.46 ? 50   LEU A CB    1 
ATOM   282   C CG    . LEU A  1 52   ? -48.088 44.678  95.528  1.00 26.92 ? 50   LEU A CG    1 
ATOM   283   C CD1   . LEU A  1 52   ? -46.702 45.299  95.310  1.00 22.60 ? 50   LEU A CD1   1 
ATOM   284   C CD2   . LEU A  1 52   ? -49.119 45.332  94.588  1.00 24.72 ? 50   LEU A CD2   1 
ATOM   285   N N     . VAL A  1 53   ? -48.594 40.184  96.319  1.00 28.53 ? 51   VAL A N     1 
ATOM   286   C CA    . VAL A  1 53   ? -48.528 38.726  96.176  1.00 29.49 ? 51   VAL A CA    1 
ATOM   287   C C     . VAL A  1 53   ? -49.929 38.123  96.103  1.00 30.84 ? 51   VAL A C     1 
ATOM   288   O O     . VAL A  1 53   ? -50.227 37.304  95.227  1.00 33.60 ? 51   VAL A O     1 
ATOM   289   C CB    . VAL A  1 53   ? -47.712 38.109  97.329  1.00 30.63 ? 51   VAL A CB    1 
ATOM   290   C CG1   . VAL A  1 53   ? -47.821 36.593  97.299  1.00 32.23 ? 51   VAL A CG1   1 
ATOM   291   C CG2   . VAL A  1 53   ? -46.273 38.531  97.227  1.00 30.07 ? 51   VAL A CG2   1 
ATOM   292   N N     . GLU A  1 54   ? -50.817 38.531  97.015  1.00 30.90 ? 52   GLU A N     1 
ATOM   293   C CA    . GLU A  1 54   ? -52.164 37.970  97.022  1.00 33.58 ? 52   GLU A CA    1 
ATOM   294   C C     . GLU A  1 54   ? -52.907 38.318  95.741  1.00 33.76 ? 52   GLU A C     1 
ATOM   295   O O     . GLU A  1 54   ? -53.581 37.464  95.156  1.00 35.24 ? 52   GLU A O     1 
ATOM   296   C CB    . GLU A  1 54   ? -52.943 38.459  98.250  1.00 33.75 ? 52   GLU A CB    1 
ATOM   297   N N     . ALA A  1 55   ? -52.779 39.565  95.280  1.00 31.74 ? 53   ALA A N     1 
ATOM   298   C CA    . ALA A  1 55   ? -53.502 40.003  94.089  1.00 33.83 ? 53   ALA A CA    1 
ATOM   299   C C     . ALA A  1 55   ? -52.984 39.329  92.823  1.00 33.39 ? 53   ALA A C     1 
ATOM   300   O O     . ALA A  1 55   ? -53.746 39.136  91.869  1.00 32.69 ? 53   ALA A O     1 
ATOM   301   C CB    . ALA A  1 55   ? -53.408 41.527  93.957  1.00 30.37 ? 53   ALA A CB    1 
ATOM   302   N N     . ALA A  1 56   ? -51.700 38.979  92.786  1.00 33.48 ? 54   ALA A N     1 
ATOM   303   C CA    . ALA A  1 56   ? -51.091 38.349  91.622  1.00 31.15 ? 54   ALA A CA    1 
ATOM   304   C C     . ALA A  1 56   ? -51.202 36.831  91.646  1.00 34.04 ? 54   ALA A C     1 
ATOM   305   O O     . ALA A  1 56   ? -50.725 36.176  90.719  1.00 34.76 ? 54   ALA A O     1 
ATOM   306   C CB    . ALA A  1 56   ? -49.615 38.755  91.517  1.00 31.20 ? 54   ALA A CB    1 
ATOM   307   N N     . THR A  1 57   ? -51.836 36.261  92.669  1.00 38.11 ? 55   THR A N     1 
ATOM   308   C CA    . THR A  1 57   ? -51.886 34.811  92.813  1.00 36.98 ? 55   THR A CA    1 
ATOM   309   C C     . THR A  1 57   ? -52.883 34.202  91.837  1.00 38.79 ? 55   THR A C     1 
ATOM   310   O O     . THR A  1 57   ? -54.045 34.618  91.774  1.00 42.22 ? 55   THR A O     1 
ATOM   311   C CB    . THR A  1 57   ? -52.244 34.446  94.251  1.00 35.48 ? 55   THR A CB    1 
ATOM   312   O OG1   . THR A  1 57   ? -51.189 34.892  95.113  1.00 37.94 ? 55   THR A OG1   1 
ATOM   313   C CG2   . THR A  1 57   ? -52.419 32.935  94.399  1.00 37.28 ? 55   THR A CG2   1 
ATOM   314   N N     . GLN A  1 58   ? -52.425 33.216  91.070  1.00 38.15 ? 56   GLN A N     1 
ATOM   315   C CA    . GLN A  1 58   ? -53.252 32.536  90.089  1.00 42.38 ? 56   GLN A CA    1 
ATOM   316   C C     . GLN A  1 58   ? -53.310 31.046  90.403  1.00 40.85 ? 56   GLN A C     1 
ATOM   317   O O     . GLN A  1 58   ? -52.477 30.515  91.139  1.00 41.82 ? 56   GLN A O     1 
ATOM   318   C CB    . GLN A  1 58   ? -52.721 32.756  88.667  1.00 42.51 ? 56   GLN A CB    1 
ATOM   319   C CG    . GLN A  1 58   ? -52.576 34.222  88.283  1.00 39.19 ? 56   GLN A CG    1 
ATOM   320   C CD    . GLN A  1 58   ? -52.606 34.423  86.786  1.00 35.96 ? 56   GLN A CD    1 
ATOM   321   O OE1   . GLN A  1 58   ? -53.662 34.324  86.160  1.00 42.15 ? 56   GLN A OE1   1 
ATOM   322   N NE2   . GLN A  1 58   ? -51.449 34.695  86.198  1.00 39.57 ? 56   GLN A NE2   1 
ATOM   323   N N     . SER A  1 59   ? -54.303 30.378  89.819  1.00 42.38 ? 57   SER A N     1 
ATOM   324   C CA    . SER A  1 59   ? -54.538 28.972  90.107  1.00 45.95 ? 57   SER A CA    1 
ATOM   325   C C     . SER A  1 59   ? -53.381 28.114  89.607  1.00 45.14 ? 57   SER A C     1 
ATOM   326   O O     . SER A  1 59   ? -52.600 28.514  88.737  1.00 42.34 ? 57   SER A O     1 
ATOM   327   C CB    . SER A  1 59   ? -55.846 28.501  89.470  1.00 45.68 ? 57   SER A CB    1 
ATOM   328   O OG    . SER A  1 59   ? -55.717 28.381  88.063  1.00 45.29 ? 57   SER A OG    1 
ATOM   329   N N     . LYS A  1 60   ? -53.281 26.910  90.174  1.00 44.71 ? 58   LYS A N     1 
ATOM   330   C CA    . LYS A  1 60   ? -52.231 25.984  89.766  1.00 46.94 ? 58   LYS A CA    1 
ATOM   331   C C     . LYS A  1 60   ? -52.274 25.727  88.263  1.00 43.08 ? 58   LYS A C     1 
ATOM   332   O O     . LYS A  1 60   ? -51.242 25.783  87.584  1.00 44.18 ? 58   LYS A O     1 
ATOM   333   C CB    . LYS A  1 60   ? -52.360 24.672  90.541  1.00 45.33 ? 58   LYS A CB    1 
ATOM   334   C CG    . LYS A  1 60   ? -51.407 23.588  90.077  1.00 51.61 ? 58   LYS A CG    1 
ATOM   335   C CD    . LYS A  1 60   ? -49.959 24.021  90.224  1.00 51.96 ? 58   LYS A CD    1 
ATOM   336   C CE    . LYS A  1 60   ? -49.010 22.880  89.891  1.00 53.05 ? 58   LYS A CE    1 
ATOM   337   N NZ    . LYS A  1 60   ? -47.595 23.240  90.170  1.00 56.56 ? 58   LYS A NZ    1 
ATOM   338   N N     . GLU A  1 61   ? -53.464 25.444  87.724  1.00 43.45 ? 59   GLU A N     1 
ATOM   339   C CA    . GLU A  1 61   ? -53.586 25.192  86.292  1.00 41.19 ? 59   GLU A CA    1 
ATOM   340   C C     . GLU A  1 61   ? -53.115 26.389  85.477  1.00 43.64 ? 59   GLU A C     1 
ATOM   341   O O     . GLU A  1 61   ? -52.386 26.229  84.491  1.00 45.80 ? 59   GLU A O     1 
ATOM   342   C CB    . GLU A  1 61   ? -55.033 24.841  85.937  1.00 43.11 ? 59   GLU A CB    1 
ATOM   343   N N     . ILE A  1 62   ? -53.513 27.598  85.877  1.00 43.17 ? 60   ILE A N     1 
ATOM   344   C CA    . ILE A  1 62   ? -53.108 28.791  85.139  1.00 40.49 ? 60   ILE A CA    1 
ATOM   345   C C     . ILE A  1 62   ? -51.596 28.963  85.194  1.00 40.05 ? 60   ILE A C     1 
ATOM   346   O O     . ILE A  1 62   ? -50.960 29.320  84.195  1.00 42.36 ? 60   ILE A O     1 
ATOM   347   C CB    . ILE A  1 62   ? -53.844 30.030  85.680  1.00 38.88 ? 60   ILE A CB    1 
ATOM   348   C CG1   . ILE A  1 62   ? -55.304 30.019  85.216  1.00 43.01 ? 60   ILE A CG1   1 
ATOM   349   C CG2   . ILE A  1 62   ? -53.137 31.312  85.241  1.00 38.69 ? 60   ILE A CG2   1 
ATOM   350   C CD1   . ILE A  1 62   ? -56.094 31.220  85.660  1.00 40.77 ? 60   ILE A CD1   1 
ATOM   351   N N     . ARG A  1 63   ? -50.995 28.710  86.357  1.00 39.95 ? 61   ARG A N     1 
ATOM   352   C CA    . ARG A  1 63   ? -49.547 28.834  86.461  1.00 38.77 ? 61   ARG A CA    1 
ATOM   353   C C     . ARG A  1 63   ? -48.844 27.802  85.587  1.00 40.86 ? 61   ARG A C     1 
ATOM   354   O O     . ARG A  1 63   ? -47.813 28.105  84.975  1.00 41.46 ? 61   ARG A O     1 
ATOM   355   C CB    . ARG A  1 63   ? -49.106 28.718  87.921  1.00 39.92 ? 61   ARG A CB    1 
ATOM   356   C CG    . ARG A  1 63   ? -49.397 29.974  88.721  1.00 44.96 ? 61   ARG A CG    1 
ATOM   357   C CD    . ARG A  1 63   ? -48.854 29.912  90.138  1.00 42.41 ? 61   ARG A CD    1 
ATOM   358   N NE    . ARG A  1 63   ? -49.663 29.070  91.008  1.00 43.71 ? 61   ARG A NE    1 
ATOM   359   C CZ    . ARG A  1 63   ? -49.259 27.911  91.505  1.00 49.11 ? 61   ARG A CZ    1 
ATOM   360   N NH1   . ARG A  1 63   ? -48.053 27.432  91.248  1.00 54.00 ? 61   ARG A NH1   1 
ATOM   361   N NH2   . ARG A  1 63   ? -50.082 27.219  92.288  1.00 50.39 ? 61   ARG A NH2   1 
ATOM   362   N N     . ASP A  1 64   ? -49.397 26.588  85.498  1.00 42.78 ? 62   ASP A N     1 
ATOM   363   C CA    . ASP A  1 64   ? -48.824 25.568  84.622  1.00 43.46 ? 62   ASP A CA    1 
ATOM   364   C C     . ASP A  1 64   ? -48.909 25.989  83.159  1.00 41.22 ? 62   ASP A C     1 
ATOM   365   O O     . ASP A  1 64   ? -47.913 25.934  82.426  1.00 41.47 ? 62   ASP A O     1 
ATOM   366   C CB    . ASP A  1 64   ? -49.533 24.228  84.831  1.00 46.67 ? 62   ASP A CB    1 
ATOM   367   C CG    . ASP A  1 64   ? -49.089 23.516  86.100  1.00 46.00 ? 62   ASP A CG    1 
ATOM   368   O OD1   . ASP A  1 64   ? -48.350 24.115  86.907  1.00 47.27 ? 62   ASP A OD1   1 
ATOM   369   O OD2   . ASP A  1 64   ? -49.479 22.346  86.286  1.00 51.65 ? 62   ASP A OD2   1 
ATOM   370   N N     . ALA A  1 65   ? -50.098 26.408  82.714  1.00 39.21 ? 63   ALA A N     1 
ATOM   371   C CA    . ALA A  1 65   ? -50.253 26.870  81.340  1.00 40.06 ? 63   ALA A CA    1 
ATOM   372   C C     . ALA A  1 65   ? -49.361 28.074  81.056  1.00 39.65 ? 63   ALA A C     1 
ATOM   373   O O     . ALA A  1 65   ? -48.759 28.167  79.982  1.00 41.57 ? 63   ALA A O     1 
ATOM   374   C CB    . ALA A  1 65   ? -51.717 27.207  81.058  1.00 40.54 ? 63   ALA A CB    1 
ATOM   375   N N     . ALA A  1 66   ? -49.249 28.999  82.010  1.00 38.81 ? 64   ALA A N     1 
ATOM   376   C CA    . ALA A  1 66   ? -48.390 30.160  81.796  1.00 41.50 ? 64   ALA A CA    1 
ATOM   377   C C     . ALA A  1 66   ? -46.932 29.748  81.617  1.00 39.73 ? 64   ALA A C     1 
ATOM   378   O O     . ALA A  1 66   ? -46.235 30.282  80.748  1.00 39.68 ? 64   ALA A O     1 
ATOM   379   C CB    . ALA A  1 66   ? -48.533 31.151  82.952  1.00 38.03 ? 64   ALA A CB    1 
ATOM   380   N N     . ALA A  1 67   ? -46.451 28.800  82.428  1.00 40.24 ? 65   ALA A N     1 
ATOM   381   C CA    . ALA A  1 67   ? -45.063 28.364  82.292  1.00 43.52 ? 65   ALA A CA    1 
ATOM   382   C C     . ALA A  1 67   ? -44.821 27.681  80.950  1.00 41.20 ? 65   ALA A C     1 
ATOM   383   O O     . ALA A  1 67   ? -43.739 27.821  80.367  1.00 42.31 ? 65   ALA A O     1 
ATOM   384   C CB    . ALA A  1 67   ? -44.681 27.430  83.442  1.00 38.48 ? 65   ALA A CB    1 
ATOM   385   N N     . SER A  1 68   ? -45.817 26.958  80.437  1.00 42.35 ? 66   SER A N     1 
ATOM   386   C CA    . SER A  1 68   ? -45.680 26.335  79.125  1.00 42.97 ? 66   SER A CA    1 
ATOM   387   C C     . SER A  1 68   ? -45.616 27.387  78.024  1.00 43.37 ? 66   SER A C     1 
ATOM   388   O O     . SER A  1 68   ? -44.754 27.321  77.139  1.00 41.56 ? 66   SER A O     1 
ATOM   389   C CB    . SER A  1 68   ? -46.837 25.363  78.883  1.00 37.41 ? 66   SER A CB    1 
ATOM   390   N N     . THR A  1 69   ? -46.518 28.376  78.068  1.00 42.93 ? 67   THR A N     1 
ATOM   391   C CA    . THR A  1 69   ? -46.514 29.433  77.058  1.00 39.09 ? 67   THR A CA    1 
ATOM   392   C C     . THR A  1 69   ? -45.201 30.210  77.074  1.00 40.56 ? 67   THR A C     1 
ATOM   393   O O     . THR A  1 69   ? -44.629 30.499  76.015  1.00 40.77 ? 67   THR A O     1 
ATOM   394   C CB    . THR A  1 69   ? -47.701 30.374  77.277  1.00 35.90 ? 67   THR A CB    1 
ATOM   395   O OG1   . THR A  1 69   ? -48.914 29.625  77.218  1.00 37.28 ? 67   THR A OG1   1 
ATOM   396   C CG2   . THR A  1 69   ? -47.742 31.473  76.210  1.00 35.70 ? 67   THR A CG2   1 
ATOM   397   N N     . ALA A  1 70   ? -44.697 30.544  78.269  1.00 38.47 ? 68   ALA A N     1 
ATOM   398   C CA    . ALA A  1 70   ? -43.442 31.280  78.359  1.00 40.46 ? 68   ALA A CA    1 
ATOM   399   C C     . ALA A  1 70   ? -42.269 30.449  77.860  1.00 43.68 ? 68   ALA A C     1 
ATOM   400   O O     . ALA A  1 70   ? -41.332 30.999  77.267  1.00 42.15 ? 68   ALA A O     1 
ATOM   401   C CB    . ALA A  1 70   ? -43.194 31.739  79.795  1.00 37.65 ? 68   ALA A CB    1 
ATOM   402   N N     . ARG A  1 71   ? -42.298 29.133  78.097  1.00 43.50 ? 69   ARG A N     1 
ATOM   403   C CA    . ARG A  1 71   ? -41.237 28.271  77.585  1.00 45.13 ? 69   ARG A CA    1 
ATOM   404   C C     . ARG A  1 71   ? -41.261 28.223  76.064  1.00 42.00 ? 69   ARG A C     1 
ATOM   405   O O     . ARG A  1 71   ? -40.206 28.259  75.421  1.00 48.72 ? 69   ARG A O     1 
ATOM   406   C CB    . ARG A  1 71   ? -41.366 26.862  78.169  1.00 45.07 ? 69   ARG A CB    1 
ATOM   407   C CG    . ARG A  1 71   ? -40.420 25.853  77.536  1.00 48.41 ? 69   ARG A CG    1 
ATOM   408   C CD    . ARG A  1 71   ? -40.360 24.547  78.320  1.00 45.84 ? 69   ARG A CD    1 
ATOM   409   N NE    . ARG A  1 71   ? -39.404 24.619  79.418  1.00 49.72 ? 69   ARG A NE    1 
ATOM   410   C CZ    . ARG A  1 71   ? -38.087 24.588  79.265  1.00 51.31 ? 69   ARG A CZ    1 
ATOM   411   N NH1   . ARG A  1 71   ? -37.532 24.490  78.068  1.00 54.06 ? 69   ARG A NH1   1 
ATOM   412   N NH2   . ARG A  1 71   ? -37.307 24.669  80.339  1.00 54.03 ? 69   ARG A NH2   1 
ATOM   413   N N     . LYS A  1 72   ? -42.456 28.164  75.474  1.00 41.59 ? 70   LYS A N     1 
ATOM   414   C CA    . LYS A  1 72   ? -42.570 28.168  74.019  1.00 44.17 ? 70   LYS A CA    1 
ATOM   415   C C     . LYS A  1 72   ? -42.059 29.477  73.427  1.00 47.38 ? 70   LYS A C     1 
ATOM   416   O O     . LYS A  1 72   ? -41.350 29.474  72.414  1.00 47.62 ? 70   LYS A O     1 
ATOM   417   C CB    . LYS A  1 72   ? -44.021 27.923  73.605  1.00 41.28 ? 70   LYS A CB    1 
ATOM   418   N N     . LEU A  1 73   ? -42.397 30.609  74.052  1.00 45.36 ? 71   LEU A N     1 
ATOM   419   C CA    . LEU A  1 73   ? -41.939 31.899  73.544  1.00 43.17 ? 71   LEU A CA    1 
ATOM   420   C C     . LEU A  1 73   ? -40.427 32.046  73.682  1.00 44.64 ? 71   LEU A C     1 
ATOM   421   O O     . LEU A  1 73   ? -39.757 32.526  72.762  1.00 43.72 ? 71   LEU A O     1 
ATOM   422   C CB    . LEU A  1 73   ? -42.643 33.044  74.274  1.00 38.35 ? 71   LEU A CB    1 
ATOM   423   C CG    . LEU A  1 73   ? -44.161 33.150  74.190  1.00 38.99 ? 71   LEU A CG    1 
ATOM   424   C CD1   . LEU A  1 73   ? -44.637 34.199  75.181  1.00 41.44 ? 71   LEU A CD1   1 
ATOM   425   C CD2   . LEU A  1 73   ? -44.613 33.506  72.782  1.00 38.76 ? 71   LEU A CD2   1 
ATOM   426   N N     . ILE A  1 74   ? -39.872 31.656  74.835  1.00 43.45 ? 72   ILE A N     1 
ATOM   427   C CA    . ILE A  1 74   ? -38.441 31.833  75.059  1.00 45.65 ? 72   ILE A CA    1 
ATOM   428   C C     . ILE A  1 74   ? -37.642 30.896  74.165  1.00 52.23 ? 72   ILE A C     1 
ATOM   429   O O     . ILE A  1 74   ? -36.539 31.238  73.724  1.00 50.30 ? 72   ILE A O     1 
ATOM   430   C CB    . ILE A  1 74   ? -38.095 31.630  76.546  1.00 45.70 ? 72   ILE A CB    1 
ATOM   431   N N     . GLU A  1 75   ? -38.183 29.710  73.875  1.00 55.75 ? 73   GLU A N     1 
ATOM   432   C CA    . GLU A  1 75   ? -37.530 28.800  72.940  1.00 57.95 ? 73   GLU A CA    1 
ATOM   433   C C     . GLU A  1 75   ? -37.503 29.388  71.534  1.00 57.44 ? 73   GLU A C     1 
ATOM   434   O O     . GLU A  1 75   ? -36.460 29.388  70.871  1.00 59.51 ? 73   GLU A O     1 
ATOM   435   C CB    . GLU A  1 75   ? -38.230 27.439  72.957  1.00 55.09 ? 73   GLU A CB    1 
ATOM   436   C CG    . GLU A  1 75   ? -37.669 26.502  74.021  1.00 60.07 ? 73   GLU A CG    1 
ATOM   437   C CD    . GLU A  1 75   ? -38.531 25.280  74.288  1.00 63.21 ? 73   GLU A CD    1 
ATOM   438   O OE1   . GLU A  1 75   ? -39.636 25.175  73.712  1.00 59.36 ? 73   GLU A OE1   1 
ATOM   439   O OE2   . GLU A  1 75   ? -38.095 24.423  75.089  1.00 62.68 ? 73   GLU A OE2   1 
ATOM   440   N N     . ALA A  1 76   ? -38.641 29.904  71.066  1.00 52.59 ? 74   ALA A N     1 
ATOM   441   C CA    . ALA A  1 76   ? -38.673 30.601  69.783  1.00 52.18 ? 74   ALA A CA    1 
ATOM   442   C C     . ALA A  1 76   ? -37.653 31.734  69.743  1.00 53.05 ? 74   ALA A C     1 
ATOM   443   O O     . ALA A  1 76   ? -36.910 31.887  68.766  1.00 57.22 ? 74   ALA A O     1 
ATOM   444   C CB    . ALA A  1 76   ? -40.081 31.135  69.520  1.00 50.77 ? 74   ALA A CB    1 
ATOM   445   N N     . LEU A  1 77   ? -37.597 32.536  70.810  1.00 52.44 ? 75   LEU A N     1 
ATOM   446   C CA    . LEU A  1 77   ? -36.677 33.670  70.851  1.00 51.99 ? 75   LEU A CA    1 
ATOM   447   C C     . LEU A  1 77   ? -35.226 33.222  70.727  1.00 55.38 ? 75   LEU A C     1 
ATOM   448   O O     . LEU A  1 77   ? -34.428 33.859  70.029  1.00 52.95 ? 75   LEU A O     1 
ATOM   449   C CB    . LEU A  1 77   ? -36.874 34.453  72.147  1.00 50.89 ? 75   LEU A CB    1 
ATOM   450   C CG    . LEU A  1 77   ? -37.657 35.757  72.064  1.00 46.38 ? 75   LEU A CG    1 
ATOM   451   C CD1   . LEU A  1 77   ? -37.677 36.414  73.431  1.00 45.05 ? 75   LEU A CD1   1 
ATOM   452   C CD2   . LEU A  1 77   ? -37.025 36.672  71.033  1.00 48.71 ? 75   LEU A CD2   1 
ATOM   453   N N     . ARG A  1 78   ? -34.860 32.139  71.410  1.00 55.49 ? 76   ARG A N     1 
ATOM   454   C CA    . ARG A  1 78   ? -33.475 31.694  71.390  1.00 56.41 ? 76   ARG A CA    1 
ATOM   455   C C     . ARG A  1 78   ? -33.110 30.986  70.094  1.00 56.64 ? 76   ARG A C     1 
ATOM   456   O O     . ARG A  1 78   ? -31.924 30.900  69.767  1.00 59.46 ? 76   ARG A O     1 
ATOM   457   C CB    . ARG A  1 78   ? -33.199 30.793  72.596  1.00 55.71 ? 76   ARG A CB    1 
ATOM   458   C CG    . ARG A  1 78   ? -33.276 31.553  73.906  1.00 53.01 ? 76   ARG A CG    1 
ATOM   459   C CD    . ARG A  1 78   ? -32.676 30.793  75.066  1.00 47.53 ? 76   ARG A CD    1 
ATOM   460   N NE    . ARG A  1 78   ? -32.143 31.724  76.053  1.00 48.06 ? 76   ARG A NE    1 
ATOM   461   C CZ    . ARG A  1 78   ? -31.691 31.377  77.248  1.00 50.01 ? 76   ARG A CZ    1 
ATOM   462   N NH1   . ARG A  1 78   ? -31.717 30.119  77.660  1.00 49.52 ? 76   ARG A NH1   1 
ATOM   463   N NH2   . ARG A  1 78   ? -31.203 32.317  78.054  1.00 51.19 ? 76   ARG A NH2   1 
ATOM   464   N N     . GLY A  1 79   ? -34.097 30.509  69.343  1.00 55.78 ? 77   GLY A N     1 
ATOM   465   C CA    . GLY A  1 79   ? -33.830 29.883  68.066  1.00 59.09 ? 77   GLY A CA    1 
ATOM   466   C C     . GLY A  1 79   ? -33.860 30.852  66.901  1.00 59.33 ? 77   GLY A C     1 
ATOM   467   O O     . GLY A  1 79   ? -34.287 30.488  65.801  1.00 60.21 ? 77   GLY A O     1 
ATOM   468   N N     . LYS A  1 80   ? -33.412 32.085  67.132  1.00 61.58 ? 78   LYS A N     1 
ATOM   469   C CA    . LYS A  1 80   ? -33.327 33.099  66.084  1.00 61.53 ? 78   LYS A CA    1 
ATOM   470   C C     . LYS A  1 80   ? -32.593 34.332  66.603  1.00 60.30 ? 78   LYS A C     1 
ATOM   471   O O     . LYS A  1 80   ? -31.819 34.958  65.880  1.00 67.14 ? 78   LYS A O     1 
ATOM   472   C CB    . LYS A  1 80   ? -34.723 33.481  65.571  1.00 61.17 ? 78   LYS A CB    1 
ATOM   473   C CG    . LYS A  1 80   ? -35.666 34.011  66.638  1.00 58.50 ? 78   LYS A CG    1 
ATOM   474   C CD    . LYS A  1 80   ? -37.050 34.286  66.066  1.00 54.81 ? 78   LYS A CD    1 
ATOM   475   C CE    . LYS A  1 80   ? -37.943 34.997  67.079  1.00 50.66 ? 78   LYS A CE    1 
ATOM   476   N NZ    . LYS A  1 80   ? -39.298 35.315  66.526  1.00 44.54 ? 78   LYS A NZ    1 
ATOM   477   N N     . GLY A  1 85   ? -24.908 41.588  64.948  1.00 50.09 ? 83   GLY A N     1 
ATOM   478   C CA    . GLY A  1 85   ? -24.763 42.866  64.272  1.00 46.44 ? 83   GLY A CA    1 
ATOM   479   C C     . GLY A  1 85   ? -23.389 43.474  64.506  1.00 49.36 ? 83   GLY A C     1 
ATOM   480   O O     . GLY A  1 85   ? -22.429 43.167  63.795  1.00 43.59 ? 83   GLY A O     1 
ATOM   481   N N     . VAL A  1 86   ? -23.287 44.348  65.509  1.00 46.27 ? 84   VAL A N     1 
ATOM   482   C CA    . VAL A  1 86   ? -21.971 44.837  65.910  1.00 44.94 ? 84   VAL A CA    1 
ATOM   483   C C     . VAL A  1 86   ? -21.065 43.669  66.270  1.00 43.87 ? 84   VAL A C     1 
ATOM   484   O O     . VAL A  1 86   ? -19.849 43.720  66.047  1.00 40.74 ? 84   VAL A O     1 
ATOM   485   C CB    . VAL A  1 86   ? -22.102 45.839  67.074  1.00 45.25 ? 84   VAL A CB    1 
ATOM   486   C CG1   . VAL A  1 86   ? -20.738 46.363  67.492  1.00 46.48 ? 84   VAL A CG1   1 
ATOM   487   C CG2   . VAL A  1 86   ? -22.990 46.990  66.672  1.00 47.45 ? 84   VAL A CG2   1 
ATOM   488   N N     . GLU A  1 87   ? -21.642 42.587  66.802  1.00 45.88 ? 85   GLU A N     1 
ATOM   489   C CA    . GLU A  1 87   ? -20.839 41.436  67.200  1.00 44.64 ? 85   GLU A CA    1 
ATOM   490   C C     . GLU A  1 87   ? -20.194 40.772  65.995  1.00 42.66 ? 85   GLU A C     1 
ATOM   491   O O     . GLU A  1 87   ? -19.057 40.294  66.079  1.00 44.38 ? 85   GLU A O     1 
ATOM   492   C CB    . GLU A  1 87   ? -21.700 40.433  67.969  1.00 48.14 ? 85   GLU A CB    1 
ATOM   493   N N     . GLY A  1 88   ? -20.903 40.730  64.865  1.00 42.80 ? 86   GLY A N     1 
ATOM   494   C CA    . GLY A  1 88   ? -20.312 40.183  63.659  1.00 40.02 ? 86   GLY A CA    1 
ATOM   495   C C     . GLY A  1 88   ? -19.192 41.040  63.109  1.00 38.59 ? 86   GLY A C     1 
ATOM   496   O O     . GLY A  1 88   ? -18.238 40.519  62.523  1.00 37.76 ? 86   GLY A O     1 
ATOM   497   N N     . LEU A  1 89   ? -19.295 42.360  63.275  1.00 38.96 ? 87   LEU A N     1 
ATOM   498   C CA    . LEU A  1 89   ? -18.230 43.249  62.826  1.00 36.00 ? 87   LEU A CA    1 
ATOM   499   C C     . LEU A  1 89   ? -16.988 43.081  63.698  1.00 33.95 ? 87   LEU A C     1 
ATOM   500   O O     . LEU A  1 89   ? -15.868 42.964  63.189  1.00 32.48 ? 87   LEU A O     1 
ATOM   501   C CB    . LEU A  1 89   ? -18.725 44.696  62.848  1.00 41.00 ? 87   LEU A CB    1 
ATOM   502   C CG    . LEU A  1 89   ? -18.156 45.708  61.850  1.00 40.02 ? 87   LEU A CG    1 
ATOM   503   C CD1   . LEU A  1 89   ? -18.864 47.045  62.014  1.00 42.34 ? 87   LEU A CD1   1 
ATOM   504   C CD2   . LEU A  1 89   ? -16.655 45.880  62.008  1.00 43.36 ? 87   LEU A CD2   1 
ATOM   505   N N     . VAL A  1 90   ? -17.176 43.060  65.019  1.00 36.39 ? 88   VAL A N     1 
ATOM   506   C CA    . VAL A  1 90   ? -16.070 42.812  65.940  1.00 33.24 ? 88   VAL A CA    1 
ATOM   507   C C     . VAL A  1 90   ? -15.388 41.492  65.615  1.00 39.04 ? 88   VAL A C     1 
ATOM   508   O O     . VAL A  1 90   ? -14.151 41.390  65.613  1.00 34.40 ? 88   VAL A O     1 
ATOM   509   C CB    . VAL A  1 90   ? -16.585 42.842  67.390  1.00 34.40 ? 88   VAL A CB    1 
ATOM   510   C CG1   . VAL A  1 90   ? -15.542 42.291  68.334  1.00 36.67 ? 88   VAL A CG1   1 
ATOM   511   C CG2   . VAL A  1 90   ? -16.974 44.267  67.774  1.00 33.13 ? 88   VAL A CG2   1 
ATOM   512   N N     . GLN A  1 91   ? -16.182 40.458  65.328  1.00 38.11 ? 89   GLN A N     1 
ATOM   513   C CA    . GLN A  1 91   ? -15.612 39.158  64.995  1.00 38.22 ? 89   GLN A CA    1 
ATOM   514   C C     . GLN A  1 91   ? -14.854 39.215  63.676  1.00 37.31 ? 89   GLN A C     1 
ATOM   515   O O     . GLN A  1 91   ? -13.727 38.717  63.575  1.00 36.20 ? 89   GLN A O     1 
ATOM   516   C CB    . GLN A  1 91   ? -16.715 38.097  64.935  1.00 40.38 ? 89   GLN A CB    1 
ATOM   517   N N     . GLU A  1 92   ? -15.453 39.827  62.652  1.00 38.54 ? 90   GLU A N     1 
ATOM   518   C CA    . GLU A  1 92   ? -14.864 39.756  61.318  1.00 34.72 ? 90   GLU A CA    1 
ATOM   519   C C     . GLU A  1 92   ? -13.501 40.434  61.266  1.00 38.61 ? 90   GLU A C     1 
ATOM   520   O O     . GLU A  1 92   ? -12.587 39.958  60.581  1.00 34.63 ? 90   GLU A O     1 
ATOM   521   C CB    . GLU A  1 92   ? -15.811 40.374  60.288  1.00 37.86 ? 90   GLU A CB    1 
ATOM   522   C CG    . GLU A  1 92   ? -15.267 40.301  58.873  1.00 39.42 ? 90   GLU A CG    1 
ATOM   523   C CD    . GLU A  1 92   ? -16.185 40.925  57.852  1.00 43.49 ? 90   GLU A CD    1 
ATOM   524   O OE1   . GLU A  1 92   ? -17.198 41.545  58.254  1.00 44.84 ? 90   GLU A OE1   1 
ATOM   525   O OE2   . GLU A  1 92   ? -15.881 40.797  56.647  1.00 45.84 ? 90   GLU A OE2   1 
ATOM   526   N N     . TYR A  1 93   ? -13.331 41.536  61.993  1.00 37.31 ? 91   TYR A N     1 
ATOM   527   C CA    . TYR A  1 93   ? -12.087 42.283  61.937  1.00 32.62 ? 91   TYR A CA    1 
ATOM   528   C C     . TYR A  1 93   ? -11.233 42.089  63.183  1.00 33.59 ? 91   TYR A C     1 
ATOM   529   O O     . TYR A  1 93   ? -10.240 42.806  63.359  1.00 31.06 ? 91   TYR A O     1 
ATOM   530   C CB    . TYR A  1 93   ? -12.384 43.763  61.690  1.00 31.60 ? 91   TYR A CB    1 
ATOM   531   C CG    . TYR A  1 93   ? -12.871 44.008  60.277  1.00 32.83 ? 91   TYR A CG    1 
ATOM   532   C CD1   . TYR A  1 93   ? -11.968 44.228  59.238  1.00 30.98 ? 91   TYR A CD1   1 
ATOM   533   C CD2   . TYR A  1 93   ? -14.229 43.993  59.977  1.00 33.62 ? 91   TYR A CD2   1 
ATOM   534   C CE1   . TYR A  1 93   ? -12.402 44.434  57.935  1.00 35.88 ? 91   TYR A CE1   1 
ATOM   535   C CE2   . TYR A  1 93   ? -14.675 44.201  58.675  1.00 37.80 ? 91   TYR A CE2   1 
ATOM   536   C CZ    . TYR A  1 93   ? -13.756 44.425  57.665  1.00 36.18 ? 91   TYR A CZ    1 
ATOM   537   O OH    . TYR A  1 93   ? -14.199 44.637  56.379  1.00 39.45 ? 91   TYR A OH    1 
ATOM   538   N N     . SER A  1 94   ? -11.578 41.111  64.024  1.00 31.93 ? 92   SER A N     1 
ATOM   539   C CA    . SER A  1 94   ? -10.811 40.788  65.227  1.00 32.18 ? 92   SER A CA    1 
ATOM   540   C C     . SER A  1 94   ? -10.601 42.028  66.088  1.00 28.13 ? 92   SER A C     1 
ATOM   541   O O     . SER A  1 94   ? -9.510  42.269  66.610  1.00 32.55 ? 92   SER A O     1 
ATOM   542   C CB    . SER A  1 94   ? -9.471  40.133  64.877  1.00 35.75 ? 92   SER A CB    1 
ATOM   543   O OG    . SER A  1 94   ? -9.662  39.004  64.040  1.00 38.49 ? 92   SER A OG    1 
ATOM   544   N N     . LEU A  1 95   ? -11.664 42.815  66.236  1.00 29.26 ? 93   LEU A N     1 
ATOM   545   C CA    . LEU A  1 95   ? -11.607 44.053  66.996  1.00 27.71 ? 93   LEU A CA    1 
ATOM   546   C C     . LEU A  1 95   ? -11.667 43.765  68.485  1.00 26.14 ? 93   LEU A C     1 
ATOM   547   O O     . LEU A  1 95   ? -12.391 42.876  68.937  1.00 28.00 ? 93   LEU A O     1 
ATOM   548   C CB    . LEU A  1 95   ? -12.763 44.978  66.618  1.00 29.19 ? 93   LEU A CB    1 
ATOM   549   C CG    . LEU A  1 95   ? -12.892 45.432  65.166  1.00 29.14 ? 93   LEU A CG    1 
ATOM   550   C CD1   . LEU A  1 95   ? -14.077 46.386  65.039  1.00 29.25 ? 93   LEU A CD1   1 
ATOM   551   C CD2   . LEU A  1 95   ? -11.605 46.093  64.674  1.00 23.79 ? 93   LEU A CD2   1 
ATOM   552   N N     . SER A  1 96   ? -10.891 44.524  69.247  1.00 25.53 ? 94   SER A N     1 
ATOM   553   C CA    . SER A  1 96   ? -11.070 44.564  70.683  1.00 28.64 ? 94   SER A CA    1 
ATOM   554   C C     . SER A  1 96   ? -12.304 45.402  71.013  1.00 25.28 ? 94   SER A C     1 
ATOM   555   O O     . SER A  1 96   ? -12.876 46.069  70.146  1.00 25.16 ? 94   SER A O     1 
ATOM   556   C CB    . SER A  1 96   ? -9.826  45.141  71.347  1.00 23.32 ? 94   SER A CB    1 
ATOM   557   O OG    . SER A  1 96   ? -9.683  46.496  70.965  1.00 22.55 ? 94   SER A OG    1 
ATOM   558   N N     . SER A  1 97   ? -12.712 45.366  72.284  1.00 22.02 ? 95   SER A N     1 
ATOM   559   C CA    . SER A  1 97   ? -13.860 46.165  72.711  1.00 28.92 ? 95   SER A CA    1 
ATOM   560   C C     . SER A  1 97   ? -13.612 47.647  72.478  1.00 25.23 ? 95   SER A C     1 
ATOM   561   O O     . SER A  1 97   ? -14.468 48.349  71.931  1.00 23.40 ? 95   SER A O     1 
ATOM   562   C CB    . SER A  1 97   ? -14.190 45.896  74.180  1.00 32.41 ? 95   SER A CB    1 
ATOM   563   O OG    . SER A  1 97   ? -14.741 44.602  74.324  1.00 37.37 ? 95   SER A OG    1 
ATOM   564   N N     . GLN A  1 98   ? -12.439 48.144  72.878  1.00 22.19 ? 96   GLN A N     1 
ATOM   565   C CA    . GLN A  1 98   ? -12.158 49.562  72.665  1.00 24.20 ? 96   GLN A CA    1 
ATOM   566   C C     . GLN A  1 98   ? -12.099 49.915  71.184  1.00 22.69 ? 96   GLN A C     1 
ATOM   567   O O     . GLN A  1 98   ? -12.496 51.018  70.805  1.00 21.59 ? 96   GLN A O     1 
ATOM   568   C CB    . GLN A  1 98   ? -10.859 49.957  73.364  1.00 23.62 ? 96   GLN A CB    1 
ATOM   569   C CG    . GLN A  1 98   ? -11.009 50.000  74.873  1.00 24.06 ? 96   GLN A CG    1 
ATOM   570   C CD    . GLN A  1 98   ? -11.972 51.090  75.320  1.00 24.83 ? 96   GLN A CD    1 
ATOM   571   O OE1   . GLN A  1 98   ? -13.191 50.897  75.344  1.00 24.70 ? 96   GLN A OE1   1 
ATOM   572   N NE2   . GLN A  1 98   ? -11.428 52.249  75.660  1.00 24.56 ? 96   GLN A NE2   1 
ATOM   573   N N     . GLU A  1 99   ? -11.614 49.002  70.330  1.00 24.17 ? 97   GLU A N     1 
ATOM   574   C CA    . GLU A  1 99   ? -11.593 49.289  68.898  1.00 23.32 ? 97   GLU A CA    1 
ATOM   575   C C     . GLU A  1 99   ? -13.002 49.353  68.328  1.00 23.69 ? 97   GLU A C     1 
ATOM   576   O O     . GLU A  1 99   ? -13.307 50.231  67.509  1.00 24.30 ? 97   GLU A O     1 
ATOM   577   C CB    . GLU A  1 99   ? -10.772 48.238  68.144  1.00 22.58 ? 97   GLU A CB    1 
ATOM   578   C CG    . GLU A  1 99   ? -9.281  48.320  68.462  1.00 22.72 ? 97   GLU A CG    1 
ATOM   579   C CD    . GLU A  1 99   ? -8.464  47.163  67.909  1.00 23.22 ? 97   GLU A CD    1 
ATOM   580   O OE1   . GLU A  1 99   ? -9.053  46.161  67.450  1.00 24.67 ? 97   GLU A OE1   1 
ATOM   581   O OE2   . GLU A  1 99   ? -7.215  47.255  67.965  1.00 26.21 ? 97   GLU A OE2   1 
ATOM   582   N N     . GLY A  1 100  ? -13.867 48.424  68.729  1.00 23.08 ? 98   GLY A N     1 
ATOM   583   C CA    . GLY A  1 100  ? -15.254 48.494  68.289  1.00 24.12 ? 98   GLY A CA    1 
ATOM   584   C C     . GLY A  1 100  ? -15.923 49.795  68.702  1.00 24.84 ? 98   GLY A C     1 
ATOM   585   O O     . GLY A  1 100  ? -16.635 50.415  67.910  1.00 22.70 ? 98   GLY A O     1 
ATOM   586   N N     . VAL A  1 101  ? -15.695 50.230  69.947  1.00 22.09 ? 99   VAL A N     1 
ATOM   587   C CA    . VAL A  1 101  ? -16.261 51.496  70.412  1.00 23.96 ? 99   VAL A CA    1 
ATOM   588   C C     . VAL A  1 101  ? -15.700 52.655  69.598  1.00 26.64 ? 99   VAL A C     1 
ATOM   589   O O     . VAL A  1 101  ? -16.440 53.534  69.135  1.00 23.03 ? 99   VAL A O     1 
ATOM   590   C CB    . VAL A  1 101  ? -15.979 51.698  71.914  1.00 20.46 ? 99   VAL A CB    1 
ATOM   591   C CG1   . VAL A  1 101  ? -16.428 53.101  72.352  1.00 20.52 ? 99   VAL A CG1   1 
ATOM   592   C CG2   . VAL A  1 101  ? -16.675 50.635  72.753  1.00 24.29 ? 99   VAL A CG2   1 
ATOM   593   N N     . ALA A  1 102  ? -14.374 52.682  69.428  1.00 22.14 ? 100  ALA A N     1 
ATOM   594   C CA    . ALA A  1 102  ? -13.747 53.773  68.687  1.00 23.45 ? 100  ALA A CA    1 
ATOM   595   C C     . ALA A  1 102  ? -14.226 53.807  67.253  1.00 22.85 ? 100  ALA A C     1 
ATOM   596   O O     . ALA A  1 102  ? -14.460 54.886  66.696  1.00 26.65 ? 100  ALA A O     1 
ATOM   597   C CB    . ALA A  1 102  ? -12.226 53.649  68.728  1.00 21.35 ? 100  ALA A CB    1 
ATOM   598   N N     . LEU A  1 103  ? -14.341 52.634  66.625  1.00 24.39 ? 101  LEU A N     1 
ATOM   599   C CA    . LEU A  1 103  ? -14.855 52.565  65.261  1.00 24.80 ? 101  LEU A CA    1 
ATOM   600   C C     . LEU A  1 103  ? -16.254 53.162  65.169  1.00 25.42 ? 101  LEU A C     1 
ATOM   601   O O     . LEU A  1 103  ? -16.550 53.940  64.253  1.00 24.74 ? 101  LEU A O     1 
ATOM   602   C CB    . LEU A  1 103  ? -14.862 51.116  64.784  1.00 24.56 ? 101  LEU A CB    1 
ATOM   603   C CG    . LEU A  1 103  ? -15.441 50.887  63.390  1.00 27.37 ? 101  LEU A CG    1 
ATOM   604   C CD1   . LEU A  1 103  ? -14.618 51.638  62.369  1.00 23.69 ? 101  LEU A CD1   1 
ATOM   605   C CD2   . LEU A  1 103  ? -15.457 49.410  63.076  1.00 27.57 ? 101  LEU A CD2   1 
ATOM   606   N N     . MET A  1 104  ? -17.136 52.797  66.100  1.00 23.49 ? 102  MET A N     1 
ATOM   607   C CA    . MET A  1 104  ? -18.501 53.325  66.051  1.00 26.73 ? 102  MET A CA    1 
ATOM   608   C C     . MET A  1 104  ? -18.515 54.832  66.292  1.00 24.83 ? 102  MET A C     1 
ATOM   609   O O     . MET A  1 104  ? -19.331 55.547  65.701  1.00 26.07 ? 102  MET A O     1 
ATOM   610   C CB    . MET A  1 104  ? -19.402 52.602  67.059  1.00 23.98 ? 102  MET A CB    1 
ATOM   611   C CG    . MET A  1 104  ? -19.564 51.111  66.791  1.00 26.68 ? 102  MET A CG    1 
ATOM   612   S SD    . MET A  1 104  ? -20.020 50.731  65.067  1.00 32.46 ? 102  MET A SD    1 
ATOM   613   C CE    . MET A  1 104  ? -21.770 51.105  65.084  1.00 38.23 ? 102  MET A CE    1 
ATOM   614   N N     . CYS A  1 105  ? -17.616 55.339  67.149  1.00 20.80 ? 103  CYS A N     1 
ATOM   615   C CA    . CYS A  1 105  ? -17.518 56.788  67.325  1.00 24.18 ? 103  CYS A CA    1 
ATOM   616   C C     . CYS A  1 105  ? -17.058 57.458  66.044  1.00 29.78 ? 103  CYS A C     1 
ATOM   617   O O     . CYS A  1 105  ? -17.507 58.563  65.712  1.00 29.82 ? 103  CYS A O     1 
ATOM   618   C CB    . CYS A  1 105  ? -16.550 57.143  68.459  1.00 24.94 ? 103  CYS A CB    1 
ATOM   619   S SG    . CYS A  1 105  ? -17.087 56.652  70.062  1.00 24.34 ? 103  CYS A SG    1 
ATOM   620   N N     . LEU A  1 106  ? -16.148 56.805  65.315  1.00 27.12 ? 104  LEU A N     1 
ATOM   621   C CA    . LEU A  1 106  ? -15.678 57.357  64.055  1.00 25.47 ? 104  LEU A CA    1 
ATOM   622   C C     . LEU A  1 106  ? -16.782 57.333  63.017  1.00 30.78 ? 104  LEU A C     1 
ATOM   623   O O     . LEU A  1 106  ? -16.966 58.308  62.277  1.00 31.17 ? 104  LEU A O     1 
ATOM   624   C CB    . LEU A  1 106  ? -14.468 56.577  63.551  1.00 26.13 ? 104  LEU A CB    1 
ATOM   625   C CG    . LEU A  1 106  ? -14.067 56.916  62.109  1.00 28.60 ? 104  LEU A CG    1 
ATOM   626   C CD1   . LEU A  1 106  ? -13.566 58.358  62.016  1.00 25.57 ? 104  LEU A CD1   1 
ATOM   627   C CD2   . LEU A  1 106  ? -13.043 55.933  61.563  1.00 28.08 ? 104  LEU A CD2   1 
ATOM   628   N N     . ALA A  1 107  ? -17.516 56.219  62.946  1.00 26.28 ? 105  ALA A N     1 
ATOM   629   C CA    . ALA A  1 107  ? -18.641 56.121  62.023  1.00 29.73 ? 105  ALA A CA    1 
ATOM   630   C C     . ALA A  1 107  ? -19.678 57.200  62.307  1.00 35.05 ? 105  ALA A C     1 
ATOM   631   O O     . ALA A  1 107  ? -20.176 57.855  61.386  1.00 34.88 ? 105  ALA A O     1 
ATOM   632   C CB    . ALA A  1 107  ? -19.268 54.733  62.114  1.00 28.47 ? 105  ALA A CB    1 
ATOM   633   N N     . GLU A  1 108  ? -20.019 57.396  63.585  1.00 31.93 ? 106  GLU A N     1 
ATOM   634   C CA    . GLU A  1 108  ? -20.960 58.447  63.956  1.00 37.04 ? 106  GLU A CA    1 
ATOM   635   C C     . GLU A  1 108  ? -20.519 59.798  63.400  1.00 38.24 ? 106  GLU A C     1 
ATOM   636   O O     . GLU A  1 108  ? -21.307 60.517  62.772  1.00 35.50 ? 106  GLU A O     1 
ATOM   637   C CB    . GLU A  1 108  ? -21.096 58.503  65.482  1.00 33.91 ? 106  GLU A CB    1 
ATOM   638   C CG    . GLU A  1 108  ? -21.848 59.721  66.013  1.00 37.86 ? 106  GLU A CG    1 
ATOM   639   C CD    . GLU A  1 108  ? -21.537 60.012  67.472  1.00 43.06 ? 106  GLU A CD    1 
ATOM   640   O OE1   . GLU A  1 108  ? -21.138 59.076  68.209  1.00 38.75 ? 106  GLU A OE1   1 
ATOM   641   O OE2   . GLU A  1 108  ? -21.681 61.188  67.883  1.00 43.70 ? 106  GLU A OE2   1 
ATOM   642   N N     . ALA A  1 109  ? -19.243 60.141  63.595  1.00 33.64 ? 107  ALA A N     1 
ATOM   643   C CA    . ALA A  1 109  ? -18.748 61.439  63.147  1.00 40.88 ? 107  ALA A CA    1 
ATOM   644   C C     . ALA A  1 109  ? -18.744 61.543  61.629  1.00 41.66 ? 107  ALA A C     1 
ATOM   645   O O     . ALA A  1 109  ? -19.045 62.609  61.077  1.00 41.67 ? 107  ALA A O     1 
ATOM   646   C CB    . ALA A  1 109  ? -17.348 61.686  63.697  1.00 43.68 ? 107  ALA A CB    1 
ATOM   647   N N     . LEU A  1 110  ? -18.378 60.460  60.939  1.00 35.25 ? 108  LEU A N     1 
ATOM   648   C CA    . LEU A  1 110  ? -18.433 60.462  59.480  1.00 39.89 ? 108  LEU A CA    1 
ATOM   649   C C     . LEU A  1 110  ? -19.859 60.650  58.980  1.00 43.56 ? 108  LEU A C     1 
ATOM   650   O O     . LEU A  1 110  ? -20.086 61.320  57.965  1.00 44.68 ? 108  LEU A O     1 
ATOM   651   C CB    . LEU A  1 110  ? -17.848 59.166  58.925  1.00 35.22 ? 108  LEU A CB    1 
ATOM   652   C CG    . LEU A  1 110  ? -16.333 59.036  59.057  1.00 33.96 ? 108  LEU A CG    1 
ATOM   653   C CD1   . LEU A  1 110  ? -15.926 57.587  58.887  1.00 30.32 ? 108  LEU A CD1   1 
ATOM   654   C CD2   . LEU A  1 110  ? -15.630 59.929  58.030  1.00 34.58 ? 108  LEU A CD2   1 
ATOM   655   N N     . LEU A  1 111  ? -20.832 60.055  59.671  1.00 40.58 ? 109  LEU A N     1 
ATOM   656   C CA    . LEU A  1 111  ? -22.230 60.206  59.281  1.00 45.24 ? 109  LEU A CA    1 
ATOM   657   C C     . LEU A  1 111  ? -22.752 61.618  59.515  1.00 47.87 ? 109  LEU A C     1 
ATOM   658   O O     . LEU A  1 111  ? -23.785 61.982  58.945  1.00 52.03 ? 109  LEU A O     1 
ATOM   659   C CB    . LEU A  1 111  ? -23.096 59.190  60.028  1.00 41.05 ? 109  LEU A CB    1 
ATOM   660   C CG    . LEU A  1 111  ? -22.915 57.750  59.545  1.00 37.56 ? 109  LEU A CG    1 
ATOM   661   C CD1   . LEU A  1 111  ? -23.613 56.771  60.462  1.00 38.13 ? 109  LEU A CD1   1 
ATOM   662   C CD2   . LEU A  1 111  ? -23.425 57.608  58.124  1.00 40.19 ? 109  LEU A CD2   1 
ATOM   663   N N     . ARG A  1 112  ? -22.062 62.424  60.327  1.00 47.83 ? 110  ARG A N     1 
ATOM   664   C CA    . ARG A  1 112  ? -22.438 63.826  60.461  1.00 48.82 ? 110  ARG A CA    1 
ATOM   665   C C     . ARG A  1 112  ? -22.091 64.640  59.220  1.00 56.25 ? 110  ARG A C     1 
ATOM   666   O O     . ARG A  1 112  ? -22.674 65.711  59.014  1.00 58.32 ? 110  ARG A O     1 
ATOM   667   C CB    . ARG A  1 112  ? -21.778 64.439  61.691  1.00 48.01 ? 110  ARG A CB    1 
ATOM   668   C CG    . ARG A  1 112  ? -22.449 64.044  62.995  1.00 52.91 ? 110  ARG A CG    1 
ATOM   669   C CD    . ARG A  1 112  ? -22.059 64.984  64.114  1.00 55.42 ? 110  ARG A CD    1 
ATOM   670   N NE    . ARG A  1 112  ? -20.632 64.921  64.397  1.00 58.47 ? 110  ARG A NE    1 
ATOM   671   C CZ    . ARG A  1 112  ? -20.092 64.184  65.359  1.00 62.96 ? 110  ARG A CZ    1 
ATOM   672   N NH1   . ARG A  1 112  ? -20.837 63.439  66.162  1.00 60.14 ? 110  ARG A NH1   1 
ATOM   673   N NH2   . ARG A  1 112  ? -18.772 64.200  65.527  1.00 64.22 ? 110  ARG A NH2   1 
ATOM   674   N N     . ILE A  1 113  ? -21.164 64.162  58.395  1.00 56.86 ? 111  ILE A N     1 
ATOM   675   C CA    . ILE A  1 113  ? -20.882 64.783  57.103  1.00 55.49 ? 111  ILE A CA    1 
ATOM   676   C C     . ILE A  1 113  ? -22.125 64.643  56.234  1.00 62.50 ? 111  ILE A C     1 
ATOM   677   O O     . ILE A  1 113  ? -22.593 63.518  55.999  1.00 61.70 ? 111  ILE A O     1 
ATOM   678   C CB    . ILE A  1 113  ? -19.652 64.153  56.433  1.00 54.46 ? 111  ILE A CB    1 
ATOM   679   C CG1   . ILE A  1 113  ? -18.392 64.502  57.226  1.00 45.27 ? 111  ILE A CG1   1 
ATOM   680   C CG2   . ILE A  1 113  ? -19.541 64.598  54.980  1.00 53.80 ? 111  ILE A CG2   1 
ATOM   681   C CD1   . ILE A  1 113  ? -17.177 63.778  56.758  1.00 45.79 ? 111  ILE A CD1   1 
ATOM   682   N N     . PRO A  1 114  ? -22.687 65.748  55.737  1.00 66.70 ? 112  PRO A N     1 
ATOM   683   C CA    . PRO A  1 114  ? -23.979 65.651  55.034  1.00 64.63 ? 112  PRO A CA    1 
ATOM   684   C C     . PRO A  1 114  ? -23.926 64.832  53.754  1.00 66.15 ? 112  PRO A C     1 
ATOM   685   O O     . PRO A  1 114  ? -24.700 63.880  53.599  1.00 65.89 ? 112  PRO A O     1 
ATOM   686   C CB    . PRO A  1 114  ? -24.328 67.123  54.767  1.00 69.12 ? 112  PRO A CB    1 
ATOM   687   C CG    . PRO A  1 114  ? -22.995 67.824  54.723  1.00 69.46 ? 112  PRO A CG    1 
ATOM   688   C CD    . PRO A  1 114  ? -22.156 67.124  55.753  1.00 61.41 ? 112  PRO A CD    1 
ATOM   689   N N     . ASP A  1 115  ? -23.021 65.166  52.839  1.00 67.40 ? 113  ASP A N     1 
ATOM   690   C CA    . ASP A  1 115  ? -23.021 64.609  51.492  1.00 64.52 ? 113  ASP A CA    1 
ATOM   691   C C     . ASP A  1 115  ? -22.290 63.273  51.444  1.00 62.02 ? 113  ASP A C     1 
ATOM   692   O O     . ASP A  1 115  ? -21.128 63.179  51.851  1.00 60.65 ? 113  ASP A O     1 
ATOM   693   C CB    . ASP A  1 115  ? -22.376 65.596  50.521  1.00 62.78 ? 113  ASP A CB    1 
ATOM   694   C CG    . ASP A  1 115  ? -22.098 64.981  49.171  1.00 68.96 ? 113  ASP A CG    1 
ATOM   695   O OD1   . ASP A  1 115  ? -23.061 64.549  48.501  1.00 72.55 ? 113  ASP A OD1   1 
ATOM   696   O OD2   . ASP A  1 115  ? -20.914 64.927  48.779  1.00 69.40 ? 113  ASP A OD2   1 
ATOM   697   N N     . THR A  1 116  ? -22.964 62.251  50.904  1.00 61.00 ? 114  THR A N     1 
ATOM   698   C CA    . THR A  1 116  ? -22.401 60.903  50.891  1.00 59.15 ? 114  THR A CA    1 
ATOM   699   C C     . THR A  1 116  ? -21.080 60.852  50.132  1.00 60.67 ? 114  THR A C     1 
ATOM   700   O O     . THR A  1 116  ? -20.095 60.285  50.618  1.00 60.59 ? 114  THR A O     1 
ATOM   701   C CB    . THR A  1 116  ? -23.399 59.916  50.287  1.00 60.07 ? 114  THR A CB    1 
ATOM   702   O OG1   . THR A  1 116  ? -24.543 59.806  51.142  1.00 60.36 ? 114  THR A OG1   1 
ATOM   703   C CG2   . THR A  1 116  ? -22.759 58.543  50.130  1.00 62.11 ? 114  THR A CG2   1 
ATOM   704   N N     . ALA A  1 117  ? -21.037 61.434  48.932  1.00 60.75 ? 115  ALA A N     1 
ATOM   705   C CA    . ALA A  1 117  ? -19.807 61.384  48.147  1.00 60.84 ? 115  ALA A CA    1 
ATOM   706   C C     . ALA A  1 117  ? -18.660 62.104  48.847  1.00 58.22 ? 115  ALA A C     1 
ATOM   707   O O     . ALA A  1 117  ? -17.499 61.698  48.714  1.00 56.52 ? 115  ALA A O     1 
ATOM   708   C CB    . ALA A  1 117  ? -20.039 61.978  46.757  1.00 61.95 ? 115  ALA A CB    1 
ATOM   709   N N     . THR A  1 118  ? -18.961 63.173  49.588  1.00 59.09 ? 116  THR A N     1 
ATOM   710   C CA    . THR A  1 118  ? -17.928 63.849  50.366  1.00 58.70 ? 116  THR A CA    1 
ATOM   711   C C     . THR A  1 118  ? -17.381 62.927  51.447  1.00 55.50 ? 116  THR A C     1 
ATOM   712   O O     . THR A  1 118  ? -16.163 62.783  51.599  1.00 53.66 ? 116  THR A O     1 
ATOM   713   C CB    . THR A  1 118  ? -18.490 65.129  50.987  1.00 56.35 ? 116  THR A CB    1 
ATOM   714   O OG1   . THR A  1 118  ? -18.944 66.001  49.946  1.00 64.91 ? 116  THR A OG1   1 
ATOM   715   C CG2   . THR A  1 118  ? -17.426 65.840  51.806  1.00 50.96 ? 116  THR A CG2   1 
ATOM   716   N N     . ARG A  1 119  ? -18.278 62.292  52.205  1.00 53.81 ? 117  ARG A N     1 
ATOM   717   C CA    . ARG A  1 119  ? -17.868 61.345  53.237  1.00 54.02 ? 117  ARG A CA    1 
ATOM   718   C C     . ARG A  1 119  ? -17.008 60.228  52.655  1.00 53.69 ? 117  ARG A C     1 
ATOM   719   O O     . ARG A  1 119  ? -15.955 59.886  53.208  1.00 48.84 ? 117  ARG A O     1 
ATOM   720   C CB    . ARG A  1 119  ? -19.107 60.769  53.924  1.00 53.57 ? 117  ARG A CB    1 
ATOM   721   C CG    . ARG A  1 119  ? -18.808 59.798  55.051  1.00 47.69 ? 117  ARG A CG    1 
ATOM   722   C CD    . ARG A  1 119  ? -20.073 59.111  55.533  1.00 46.52 ? 117  ARG A CD    1 
ATOM   723   N NE    . ARG A  1 119  ? -21.199 60.035  55.561  1.00 49.39 ? 117  ARG A NE    1 
ATOM   724   C CZ    . ARG A  1 119  ? -22.323 59.861  54.880  1.00 52.75 ? 117  ARG A CZ    1 
ATOM   725   N NH1   . ARG A  1 119  ? -22.538 58.765  54.172  1.00 50.41 ? 117  ARG A NH1   1 
ATOM   726   N NH2   . ARG A  1 119  ? -23.256 60.809  54.914  1.00 60.08 ? 117  ARG A NH2   1 
ATOM   727   N N     . ASP A  1 120  ? -17.445 59.648  51.532  1.00 53.50 ? 118  ASP A N     1 
ATOM   728   C CA    . ASP A  1 120  ? -16.688 58.573  50.900  1.00 50.74 ? 118  ASP A CA    1 
ATOM   729   C C     . ASP A  1 120  ? -15.328 59.053  50.416  1.00 52.36 ? 118  ASP A C     1 
ATOM   730   O O     . ASP A  1 120  ? -14.360 58.282  50.425  1.00 51.89 ? 118  ASP A O     1 
ATOM   731   C CB    . ASP A  1 120  ? -17.483 57.980  49.738  1.00 54.79 ? 118  ASP A CB    1 
ATOM   732   C CG    . ASP A  1 120  ? -18.812 57.397  50.180  1.00 62.58 ? 118  ASP A CG    1 
ATOM   733   O OD1   . ASP A  1 120  ? -19.142 57.502  51.382  1.00 57.44 ? 118  ASP A OD1   1 
ATOM   734   O OD2   . ASP A  1 120  ? -19.527 56.831  49.325  1.00 66.64 ? 118  ASP A OD2   1 
ATOM   735   N N     . ALA A  1 121  ? -15.235 60.315  49.987  1.00 52.73 ? 119  ALA A N     1 
ATOM   736   C CA    . ALA A  1 121  ? -13.947 60.868  49.583  1.00 54.94 ? 119  ALA A CA    1 
ATOM   737   C C     . ALA A  1 121  ? -13.030 61.057  50.783  1.00 49.68 ? 119  ALA A C     1 
ATOM   738   O O     . ALA A  1 121  ? -11.824 60.796  50.700  1.00 50.90 ? 119  ALA A O     1 
ATOM   739   C CB    . ALA A  1 121  ? -14.148 62.195  48.852  1.00 52.10 ? 119  ALA A CB    1 
ATOM   740   N N     . LEU A  1 122  ? -13.583 61.520  51.905  1.00 52.45 ? 120  LEU A N     1 
ATOM   741   C CA    . LEU A  1 122  ? -12.773 61.701  53.104  1.00 48.12 ? 120  LEU A CA    1 
ATOM   742   C C     . LEU A  1 122  ? -12.269 60.363  53.629  1.00 47.76 ? 120  LEU A C     1 
ATOM   743   O O     . LEU A  1 122  ? -11.131 60.264  54.104  1.00 47.07 ? 120  LEU A O     1 
ATOM   744   C CB    . LEU A  1 122  ? -13.582 62.430  54.174  1.00 51.67 ? 120  LEU A CB    1 
ATOM   745   C CG    . LEU A  1 122  ? -12.775 62.958  55.362  1.00 48.48 ? 120  LEU A CG    1 
ATOM   746   C CD1   . LEU A  1 122  ? -11.757 63.984  54.890  1.00 52.53 ? 120  LEU A CD1   1 
ATOM   747   C CD2   . LEU A  1 122  ? -13.694 63.548  56.417  1.00 50.47 ? 120  LEU A CD2   1 
ATOM   748   N N     . ILE A  1 123  ? -13.102 59.324  53.548  1.00 47.13 ? 121  ILE A N     1 
ATOM   749   C CA    . ILE A  1 123  ? -12.689 57.997  53.991  1.00 47.75 ? 121  ILE A CA    1 
ATOM   750   C C     . ILE A  1 123  ? -11.549 57.481  53.122  1.00 50.01 ? 121  ILE A C     1 
ATOM   751   O O     . ILE A  1 123  ? -10.500 57.062  53.626  1.00 44.22 ? 121  ILE A O     1 
ATOM   752   C CB    . ILE A  1 123  ? -13.891 57.035  53.985  1.00 44.70 ? 121  ILE A CB    1 
ATOM   753   C CG1   . ILE A  1 123  ? -14.893 57.422  55.080  1.00 44.35 ? 121  ILE A CG1   1 
ATOM   754   C CG2   . ILE A  1 123  ? -13.433 55.595  54.150  1.00 43.06 ? 121  ILE A CG2   1 
ATOM   755   C CD1   . ILE A  1 123  ? -16.176 56.625  55.044  1.00 41.27 ? 121  ILE A CD1   1 
ATOM   756   N N     . ARG A  1 124  ? -11.728 57.535  51.799  1.00 49.32 ? 122  ARG A N     1 
ATOM   757   C CA    . ARG A  1 124  ? -10.734 56.984  50.880  1.00 51.69 ? 122  ARG A CA    1 
ATOM   758   C C     . ARG A  1 124  ? -9.436  57.784  50.899  1.00 51.46 ? 122  ARG A C     1 
ATOM   759   O O     . ARG A  1 124  ? -8.345  57.204  50.929  1.00 52.79 ? 122  ARG A O     1 
ATOM   760   C CB    . ARG A  1 124  ? -11.308 56.932  49.463  1.00 49.14 ? 122  ARG A CB    1 
ATOM   761   N N     . ASP A  1 125  ? -9.529  59.113  50.894  1.00 58.86 ? 123  ASP A N     1 
ATOM   762   C CA    . ASP A  1 125  ? -8.370  59.963  50.666  1.00 58.79 ? 123  ASP A CA    1 
ATOM   763   C C     . ASP A  1 125  ? -7.758  60.540  51.938  1.00 57.41 ? 123  ASP A C     1 
ATOM   764   O O     . ASP A  1 125  ? -6.696  61.165  51.860  1.00 67.27 ? 123  ASP A O     1 
ATOM   765   C CB    . ASP A  1 125  ? -8.744  61.113  49.718  1.00 61.18 ? 123  ASP A CB    1 
ATOM   766   N N     . LYS A  1 126  ? -8.374  60.346  53.102  1.00 50.87 ? 124  LYS A N     1 
ATOM   767   C CA    . LYS A  1 126  ? -7.839  60.973  54.306  1.00 53.17 ? 124  LYS A CA    1 
ATOM   768   C C     . LYS A  1 126  ? -7.958  60.089  55.546  1.00 56.29 ? 124  LYS A C     1 
ATOM   769   O O     . LYS A  1 126  ? -6.961  59.861  56.239  1.00 57.07 ? 124  LYS A O     1 
ATOM   770   C CB    . LYS A  1 126  ? -8.532  62.316  54.546  1.00 54.01 ? 124  LYS A CB    1 
ATOM   771   N N     . ILE A  1 127  ? -9.166  59.597  55.845  1.00 54.49 ? 125  ILE A N     1 
ATOM   772   C CA    . ILE A  1 127  ? -9.370  58.818  57.067  1.00 50.49 ? 125  ILE A CA    1 
ATOM   773   C C     . ILE A  1 127  ? -8.609  57.500  56.996  1.00 51.00 ? 125  ILE A C     1 
ATOM   774   O O     . ILE A  1 127  ? -7.832  57.164  57.898  1.00 51.11 ? 125  ILE A O     1 
ATOM   775   C CB    . ILE A  1 127  ? -10.867 58.576  57.322  1.00 44.34 ? 125  ILE A CB    1 
ATOM   776   C CG1   . ILE A  1 127  ? -11.629 59.899  57.436  1.00 45.68 ? 125  ILE A CG1   1 
ATOM   777   C CG2   . ILE A  1 127  ? -11.052 57.739  58.586  1.00 42.28 ? 125  ILE A CG2   1 
ATOM   778   C CD1   . ILE A  1 127  ? -11.182 60.770  58.576  1.00 45.68 ? 125  ILE A CD1   1 
ATOM   779   N N     . ALA A  1 128  ? -8.823  56.730  55.925  1.00 49.05 ? 126  ALA A N     1 
ATOM   780   C CA    . ALA A  1 128  ? -8.167  55.435  55.781  1.00 46.95 ? 126  ALA A CA    1 
ATOM   781   C C     . ALA A  1 128  ? -6.650  55.538  55.723  1.00 50.56 ? 126  ALA A C     1 
ATOM   782   O O     . ALA A  1 128  ? -5.978  54.503  55.798  1.00 43.93 ? 126  ALA A O     1 
ATOM   783   C CB    . ALA A  1 128  ? -8.672  54.717  54.530  1.00 44.55 ? 126  ALA A CB    1 
ATOM   784   N N     . ASP A  1 129  ? -6.098  56.744  55.585  1.00 53.71 ? 127  ASP A N     1 
ATOM   785   C CA    . ASP A  1 129  ? -4.659  56.962  55.601  1.00 55.96 ? 127  ASP A CA    1 
ATOM   786   C C     . ASP A  1 129  ? -4.137  57.289  56.993  1.00 55.98 ? 127  ASP A C     1 
ATOM   787   O O     . ASP A  1 129  ? -2.982  57.701  57.130  1.00 58.26 ? 127  ASP A O     1 
ATOM   788   C CB    . ASP A  1 129  ? -4.282  58.084  54.627  1.00 55.27 ? 127  ASP A CB    1 
ATOM   789   N N     . GLY A  1 130  ? -4.962  57.111  58.027  1.00 58.68 ? 128  GLY A N     1 
ATOM   790   C CA    . GLY A  1 130  ? -4.590  57.427  59.387  1.00 55.21 ? 128  GLY A CA    1 
ATOM   791   C C     . GLY A  1 130  ? -4.873  58.853  59.809  1.00 62.29 ? 128  GLY A C     1 
ATOM   792   O O     . GLY A  1 130  ? -5.018  59.111  61.010  1.00 60.25 ? 128  GLY A O     1 
ATOM   793   N N     . ASN A  1 131  ? -4.959  59.784  58.860  1.00 75.06 ? 129  ASN A N     1 
ATOM   794   C CA    . ASN A  1 131  ? -5.216  61.185  59.170  1.00 76.33 ? 129  ASN A CA    1 
ATOM   795   C C     . ASN A  1 131  ? -6.669  61.389  59.577  1.00 75.45 ? 129  ASN A C     1 
ATOM   796   O O     . ASN A  1 131  ? -7.414  62.108  58.901  1.00 80.20 ? 129  ASN A O     1 
ATOM   797   C CB    . ASN A  1 131  ? -4.869  62.073  57.970  1.00 66.66 ? 129  ASN A CB    1 
ATOM   798   N N     . TRP A  1 132  ? -7.085  60.758  60.677  1.00 62.26 ? 130  TRP A N     1 
ATOM   799   C CA    . TRP A  1 132  ? -8.455  60.903  61.152  1.00 59.30 ? 130  TRP A CA    1 
ATOM   800   C C     . TRP A  1 132  ? -8.618  62.071  62.112  1.00 60.72 ? 130  TRP A C     1 
ATOM   801   O O     . TRP A  1 132  ? -9.712  62.645  62.199  1.00 60.44 ? 130  TRP A O     1 
ATOM   802   C CB    . TRP A  1 132  ? -8.937  59.602  61.818  1.00 57.08 ? 130  TRP A CB    1 
ATOM   803   C CG    . TRP A  1 132  ? -8.166  59.125  63.051  1.00 45.96 ? 130  TRP A CG    1 
ATOM   804   C CD1   . TRP A  1 132  ? -7.176  58.178  63.090  1.00 41.70 ? 130  TRP A CD1   1 
ATOM   805   C CD2   . TRP A  1 132  ? -8.363  59.548  64.410  1.00 42.28 ? 130  TRP A CD2   1 
ATOM   806   N NE1   . TRP A  1 132  ? -6.744  57.995  64.385  1.00 38.47 ? 130  TRP A NE1   1 
ATOM   807   C CE2   . TRP A  1 132  ? -7.449  58.826  65.213  1.00 34.55 ? 130  TRP A CE2   1 
ATOM   808   C CE3   . TRP A  1 132  ? -9.215  60.471  65.024  1.00 42.54 ? 130  TRP A CE3   1 
ATOM   809   C CZ2   . TRP A  1 132  ? -7.367  59.002  66.595  1.00 31.96 ? 130  TRP A CZ2   1 
ATOM   810   C CZ3   . TRP A  1 132  ? -9.134  60.644  66.391  1.00 39.99 ? 130  TRP A CZ3   1 
ATOM   811   C CH2   . TRP A  1 132  ? -8.216  59.914  67.164  1.00 33.11 ? 130  TRP A CH2   1 
ATOM   812   N N     . LYS A  1 133  ? -7.553  62.435  62.829  1.00 62.69 ? 131  LYS A N     1 
ATOM   813   C CA    . LYS A  1 133  ? -7.616  63.583  63.726  1.00 65.69 ? 131  LYS A CA    1 
ATOM   814   C C     . LYS A  1 133  ? -7.836  64.877  62.951  1.00 70.78 ? 131  LYS A C     1 
ATOM   815   O O     . LYS A  1 133  ? -8.561  65.768  63.409  1.00 70.61 ? 131  LYS A O     1 
ATOM   816   C CB    . LYS A  1 133  ? -6.334  63.661  64.556  1.00 61.62 ? 131  LYS A CB    1 
ATOM   817   N N     . SER A  1 134  ? -7.238  64.981  61.760  1.00 76.19 ? 132  SER A N     1 
ATOM   818   C CA    . SER A  1 134  ? -7.221  66.242  61.021  1.00 74.49 ? 132  SER A CA    1 
ATOM   819   C C     . SER A  1 134  ? -8.631  66.722  60.684  1.00 76.54 ? 132  SER A C     1 
ATOM   820   O O     . SER A  1 134  ? -8.971  67.889  60.911  1.00 75.58 ? 132  SER A O     1 
ATOM   821   C CB    . SER A  1 134  ? -6.388  66.083  59.748  1.00 72.88 ? 132  SER A CB    1 
ATOM   822   N N     . HIS A  1 135  ? -9.469  65.833  60.148  1.00 77.12 ? 133  HIS A N     1 
ATOM   823   C CA    . HIS A  1 135  ? -10.761 66.244  59.604  1.00 75.30 ? 133  HIS A CA    1 
ATOM   824   C C     . HIS A  1 135  ? -11.884 66.269  60.637  1.00 73.24 ? 133  HIS A C     1 
ATOM   825   O O     . HIS A  1 135  ? -12.825 67.060  60.497  1.00 71.55 ? 133  HIS A O     1 
ATOM   826   C CB    . HIS A  1 135  ? -11.158 65.322  58.446  1.00 68.95 ? 133  HIS A CB    1 
ATOM   827   N N     . LEU A  1 136  ? -11.814 65.434  61.667  1.00 72.20 ? 134  LEU A N     1 
ATOM   828   C CA    . LEU A  1 136  ? -12.923 65.296  62.605  1.00 68.66 ? 134  LEU A CA    1 
ATOM   829   C C     . LEU A  1 136  ? -12.479 65.529  64.053  1.00 68.84 ? 134  LEU A C     1 
ATOM   830   O O     . LEU A  1 136  ? -12.630 66.625  64.599  1.00 68.34 ? 134  LEU A O     1 
ATOM   831   C CB    . LEU A  1 136  ? -13.550 63.906  62.461  1.00 61.73 ? 134  LEU A CB    1 
ATOM   832   C CG    . LEU A  1 136  ? -13.813 63.415  61.034  1.00 59.56 ? 134  LEU A CG    1 
ATOM   833   C CD1   . LEU A  1 136  ? -13.945 61.901  60.996  1.00 48.65 ? 134  LEU A CD1   1 
ATOM   834   C CD2   . LEU A  1 136  ? -15.054 64.077  60.448  1.00 57.36 ? 134  LEU A CD2   1 
ATOM   835   N N     . ARG A  1 140  ? -14.739 69.360  68.888  1.00 33.14 ? 138  ARG A N     1 
ATOM   836   C CA    . ARG A  1 140  ? -15.213 68.357  69.832  1.00 36.91 ? 138  ARG A CA    1 
ATOM   837   C C     . ARG A  1 140  ? -14.533 67.009  69.584  1.00 39.75 ? 138  ARG A C     1 
ATOM   838   O O     . ARG A  1 140  ? -14.233 66.654  68.446  1.00 42.03 ? 138  ARG A O     1 
ATOM   839   C CB    . ARG A  1 140  ? -16.736 68.206  69.744  1.00 34.60 ? 138  ARG A CB    1 
ATOM   840   N N     . SER A  1 141  ? -14.286 66.271  70.664  1.00 39.12 ? 139  SER A N     1 
ATOM   841   C CA    . SER A  1 141  ? -13.706 64.939  70.561  1.00 35.48 ? 139  SER A CA    1 
ATOM   842   C C     . SER A  1 141  ? -14.576 64.028  69.698  1.00 34.23 ? 139  SER A C     1 
ATOM   843   O O     . SER A  1 141  ? -15.806 64.124  69.692  1.00 32.62 ? 139  SER A O     1 
ATOM   844   C CB    . SER A  1 141  ? -13.549 64.329  71.958  1.00 33.03 ? 139  SER A CB    1 
ATOM   845   O OG    . SER A  1 141  ? -12.998 63.027  71.901  1.00 32.04 ? 139  SER A OG    1 
ATOM   846   N N     . LEU A  1 142  ? -13.916 63.134  68.957  1.00 32.68 ? 140  LEU A N     1 
ATOM   847   C CA    . LEU A  1 142  ? -14.618 62.040  68.292  1.00 31.15 ? 140  LEU A CA    1 
ATOM   848   C C     . LEU A  1 142  ? -15.422 61.198  69.272  1.00 29.78 ? 140  LEU A C     1 
ATOM   849   O O     . LEU A  1 142  ? -16.411 60.559  68.890  1.00 27.08 ? 140  LEU A O     1 
ATOM   850   C CB    . LEU A  1 142  ? -13.617 61.123  67.592  1.00 32.24 ? 140  LEU A CB    1 
ATOM   851   C CG    . LEU A  1 142  ? -13.239 61.308  66.138  1.00 40.15 ? 140  LEU A CG    1 
ATOM   852   C CD1   . LEU A  1 142  ? -12.889 59.939  65.581  1.00 37.99 ? 140  LEU A CD1   1 
ATOM   853   C CD2   . LEU A  1 142  ? -14.369 61.927  65.373  1.00 40.31 ? 140  LEU A CD2   1 
ATOM   854   N N     . PHE A  1 143  ? -14.998 61.161  70.530  1.00 25.92 ? 141  PHE A N     1 
ATOM   855   C CA    . PHE A  1 143  ? -15.437 60.148  71.473  1.00 27.56 ? 141  PHE A CA    1 
ATOM   856   C C     . PHE A  1 143  ? -16.445 60.686  72.477  1.00 26.18 ? 141  PHE A C     1 
ATOM   857   O O     . PHE A  1 143  ? -16.632 60.085  73.540  1.00 21.38 ? 141  PHE A O     1 
ATOM   858   C CB    . PHE A  1 143  ? -14.206 59.553  72.169  1.00 23.88 ? 141  PHE A CB    1 
ATOM   859   C CG    . PHE A  1 143  ? -13.149 59.105  71.194  1.00 22.33 ? 141  PHE A CG    1 
ATOM   860   C CD1   . PHE A  1 143  ? -13.417 58.079  70.301  1.00 20.72 ? 141  PHE A CD1   1 
ATOM   861   C CD2   . PHE A  1 143  ? -11.915 59.735  71.132  1.00 21.64 ? 141  PHE A CD2   1 
ATOM   862   C CE1   . PHE A  1 143  ? -12.466 57.674  69.374  1.00 24.40 ? 141  PHE A CE1   1 
ATOM   863   C CE2   . PHE A  1 143  ? -10.962 59.329  70.212  1.00 24.29 ? 141  PHE A CE2   1 
ATOM   864   C CZ    . PHE A  1 143  ? -11.244 58.294  69.329  1.00 25.21 ? 141  PHE A CZ    1 
ATOM   865   N N     . VAL A  1 144  ? -17.126 61.788  72.147  1.00 26.79 ? 142  VAL A N     1 
ATOM   866   C CA    . VAL A  1 144  ? -18.037 62.403  73.115  1.00 28.72 ? 142  VAL A CA    1 
ATOM   867   C C     . VAL A  1 144  ? -19.165 61.453  73.505  1.00 25.92 ? 142  VAL A C     1 
ATOM   868   O O     . VAL A  1 144  ? -19.643 61.488  74.647  1.00 27.36 ? 142  VAL A O     1 
ATOM   869   C CB    . VAL A  1 144  ? -18.593 63.734  72.575  1.00 31.77 ? 142  VAL A CB    1 
ATOM   870   C CG1   . VAL A  1 144  ? -17.463 64.748  72.419  1.00 32.11 ? 142  VAL A CG1   1 
ATOM   871   C CG2   . VAL A  1 144  ? -19.342 63.518  71.261  1.00 30.48 ? 142  VAL A CG2   1 
ATOM   872   N N     . ASN A  1 145  ? -19.589 60.577  72.589  1.00 27.58 ? 143  ASN A N     1 
ATOM   873   C CA    . ASN A  1 145  ? -20.686 59.646  72.826  1.00 28.85 ? 143  ASN A CA    1 
ATOM   874   C C     . ASN A  1 145  ? -20.204 58.212  73.014  1.00 29.25 ? 143  ASN A C     1 
ATOM   875   O O     . ASN A  1 145  ? -20.995 57.270  72.874  1.00 26.44 ? 143  ASN A O     1 
ATOM   876   C CB    . ASN A  1 145  ? -21.698 59.716  71.682  1.00 30.90 ? 143  ASN A CB    1 
ATOM   877   C CG    . ASN A  1 145  ? -22.527 60.978  71.728  1.00 33.12 ? 143  ASN A CG    1 
ATOM   878   O OD1   . ASN A  1 145  ? -23.019 61.373  72.790  1.00 36.07 ? 143  ASN A OD1   1 
ATOM   879   N ND2   . ASN A  1 145  ? -22.666 61.633  70.588  1.00 37.19 ? 143  ASN A ND2   1 
ATOM   880   N N     . ALA A  1 146  ? -18.918 58.036  73.337  1.00 26.53 ? 144  ALA A N     1 
ATOM   881   C CA    . ALA A  1 146  ? -18.350 56.698  73.481  1.00 27.55 ? 144  ALA A CA    1 
ATOM   882   C C     . ALA A  1 146  ? -19.044 55.887  74.567  1.00 25.26 ? 144  ALA A C     1 
ATOM   883   O O     . ALA A  1 146  ? -19.097 54.654  74.471  1.00 28.03 ? 144  ALA A O     1 
ATOM   884   C CB    . ALA A  1 146  ? -16.852 56.793  73.794  1.00 24.41 ? 144  ALA A CB    1 
ATOM   885   N N     . ALA A  1 147  ? -19.538 56.543  75.623  1.00 25.20 ? 145  ALA A N     1 
ATOM   886   C CA    . ALA A  1 147  ? -20.234 55.809  76.677  1.00 28.75 ? 145  ALA A CA    1 
ATOM   887   C C     . ALA A  1 147  ? -21.419 55.044  76.107  1.00 29.09 ? 145  ALA A C     1 
ATOM   888   O O     . ALA A  1 147  ? -21.641 53.876  76.453  1.00 32.95 ? 145  ALA A O     1 
ATOM   889   C CB    . ALA A  1 147  ? -20.683 56.765  77.786  1.00 32.53 ? 145  ALA A CB    1 
ATOM   890   N N     . THR A  1 148  ? -22.159 55.671  75.193  1.00 26.15 ? 146  THR A N     1 
ATOM   891   C CA    . THR A  1 148  ? -23.293 55.010  74.556  1.00 27.48 ? 146  THR A CA    1 
ATOM   892   C C     . THR A  1 148  ? -22.832 53.856  73.679  1.00 29.07 ? 146  THR A C     1 
ATOM   893   O O     . THR A  1 148  ? -23.379 52.750  73.753  1.00 30.22 ? 146  THR A O     1 
ATOM   894   C CB    . THR A  1 148  ? -24.094 56.023  73.731  1.00 33.41 ? 146  THR A CB    1 
ATOM   895   O OG1   . THR A  1 148  ? -24.555 57.077  74.585  1.00 38.35 ? 146  THR A OG1   1 
ATOM   896   C CG2   . THR A  1 148  ? -25.289 55.352  73.064  1.00 35.57 ? 146  THR A CG2   1 
ATOM   897   N N     . TRP A  1 149  ? -21.819 54.091  72.842  1.00 26.91 ? 147  TRP A N     1 
ATOM   898   C CA    . TRP A  1 149  ? -21.288 53.009  72.019  1.00 26.47 ? 147  TRP A CA    1 
ATOM   899   C C     . TRP A  1 149  ? -20.644 51.924  72.875  1.00 25.33 ? 147  TRP A C     1 
ATOM   900   O O     . TRP A  1 149  ? -20.725 50.738  72.540  1.00 28.81 ? 147  TRP A O     1 
ATOM   901   C CB    . TRP A  1 149  ? -20.300 53.561  70.988  1.00 24.94 ? 147  TRP A CB    1 
ATOM   902   C CG    . TRP A  1 149  ? -20.983 54.407  69.947  1.00 26.65 ? 147  TRP A CG    1 
ATOM   903   C CD1   . TRP A  1 149  ? -20.792 55.741  69.712  1.00 30.49 ? 147  TRP A CD1   1 
ATOM   904   C CD2   . TRP A  1 149  ? -21.981 53.971  69.010  1.00 26.61 ? 147  TRP A CD2   1 
ATOM   905   N NE1   . TRP A  1 149  ? -21.605 56.160  68.675  1.00 29.27 ? 147  TRP A NE1   1 
ATOM   906   C CE2   . TRP A  1 149  ? -22.342 55.092  68.231  1.00 28.23 ? 147  TRP A CE2   1 
ATOM   907   C CE3   . TRP A  1 149  ? -22.593 52.743  68.747  1.00 27.88 ? 147  TRP A CE3   1 
ATOM   908   C CZ2   . TRP A  1 149  ? -23.300 55.019  67.213  1.00 31.06 ? 147  TRP A CZ2   1 
ATOM   909   C CZ3   . TRP A  1 149  ? -23.547 52.672  67.735  1.00 32.87 ? 147  TRP A CZ3   1 
ATOM   910   C CH2   . TRP A  1 149  ? -23.889 53.805  66.983  1.00 31.04 ? 147  TRP A CH2   1 
ATOM   911   N N     . GLY A  1 150  ? -19.995 52.305  73.978  1.00 24.47 ? 148  GLY A N     1 
ATOM   912   C CA    . GLY A  1 150  ? -19.511 51.299  74.909  1.00 24.61 ? 148  GLY A CA    1 
ATOM   913   C C     . GLY A  1 150  ? -20.616 50.375  75.383  1.00 30.99 ? 148  GLY A C     1 
ATOM   914   O O     . GLY A  1 150  ? -20.440 49.154  75.439  1.00 31.21 ? 148  GLY A O     1 
ATOM   915   N N     . LEU A  1 151  ? -21.779 50.943  75.718  1.00 30.93 ? 149  LEU A N     1 
ATOM   916   C CA    . LEU A  1 151  ? -22.899 50.112  76.152  1.00 32.74 ? 149  LEU A CA    1 
ATOM   917   C C     . LEU A  1 151  ? -23.385 49.223  75.012  1.00 31.14 ? 149  LEU A C     1 
ATOM   918   O O     . LEU A  1 151  ? -23.682 48.041  75.220  1.00 31.41 ? 149  LEU A O     1 
ATOM   919   C CB    . LEU A  1 151  ? -24.024 50.993  76.690  1.00 33.45 ? 149  LEU A CB    1 
ATOM   920   C CG    . LEU A  1 151  ? -25.244 50.310  77.318  1.00 38.08 ? 149  LEU A CG    1 
ATOM   921   C CD1   . LEU A  1 151  ? -24.843 49.388  78.471  1.00 36.10 ? 149  LEU A CD1   1 
ATOM   922   C CD2   . LEU A  1 151  ? -26.206 51.375  77.792  1.00 42.56 ? 149  LEU A CD2   1 
ATOM   923   N N     . VAL A  1 152  ? -23.431 49.770  73.798  1.00 29.20 ? 150  VAL A N     1 
ATOM   924   C CA    . VAL A  1 152  ? -23.786 48.974  72.621  1.00 31.15 ? 150  VAL A CA    1 
ATOM   925   C C     . VAL A  1 152  ? -22.802 47.822  72.429  1.00 33.73 ? 150  VAL A C     1 
ATOM   926   O O     . VAL A  1 152  ? -23.202 46.680  72.186  1.00 33.99 ? 150  VAL A O     1 
ATOM   927   C CB    . VAL A  1 152  ? -23.847 49.871  71.372  1.00 33.27 ? 150  VAL A CB    1 
ATOM   928   C CG1   . VAL A  1 152  ? -23.995 49.031  70.114  1.00 34.90 ? 150  VAL A CG1   1 
ATOM   929   C CG2   . VAL A  1 152  ? -24.984 50.878  71.488  1.00 34.43 ? 150  VAL A CG2   1 
ATOM   930   N N     . VAL A  1 153  ? -21.498 48.102  72.537  1.00 32.09 ? 151  VAL A N     1 
ATOM   931   C CA    . VAL A  1 153  ? -20.498 47.104  72.156  1.00 33.62 ? 151  VAL A CA    1 
ATOM   932   C C     . VAL A  1 153  ? -20.280 46.084  73.269  1.00 33.50 ? 151  VAL A C     1 
ATOM   933   O O     . VAL A  1 153  ? -20.144 44.882  73.005  1.00 34.26 ? 151  VAL A O     1 
ATOM   934   C CB    . VAL A  1 153  ? -19.178 47.790  71.747  1.00 28.99 ? 151  VAL A CB    1 
ATOM   935   C CG1   . VAL A  1 153  ? -18.076 46.762  71.523  1.00 30.02 ? 151  VAL A CG1   1 
ATOM   936   C CG2   . VAL A  1 153  ? -19.372 48.604  70.486  1.00 28.61 ? 151  VAL A CG2   1 
ATOM   937   N N     . THR A  1 154  ? -20.238 46.531  74.525  1.00 30.80 ? 152  THR A N     1 
ATOM   938   C CA    . THR A  1 154  ? -19.835 45.668  75.626  1.00 33.15 ? 152  THR A CA    1 
ATOM   939   C C     . THR A  1 154  ? -20.948 45.361  76.615  1.00 34.82 ? 152  THR A C     1 
ATOM   940   O O     . THR A  1 154  ? -20.766 44.480  77.463  1.00 35.94 ? 152  THR A O     1 
ATOM   941   C CB    . THR A  1 154  ? -18.667 46.295  76.407  1.00 34.14 ? 152  THR A CB    1 
ATOM   942   O OG1   . THR A  1 154  ? -19.142 47.429  77.145  1.00 37.87 ? 152  THR A OG1   1 
ATOM   943   C CG2   . THR A  1 154  ? -17.555 46.737  75.463  1.00 34.54 ? 152  THR A CG2   1 
ATOM   944   N N     . GLY A  1 155  ? -22.077 46.062  76.551  1.00 34.38 ? 153  GLY A N     1 
ATOM   945   C CA    . GLY A  1 155  ? -23.108 45.886  77.553  1.00 34.10 ? 153  GLY A CA    1 
ATOM   946   C C     . GLY A  1 155  ? -22.801 46.519  78.889  1.00 39.03 ? 153  GLY A C     1 
ATOM   947   O O     . GLY A  1 155  ? -23.562 46.326  79.843  1.00 43.39 ? 153  GLY A O     1 
ATOM   948   N N     . LYS A  1 156  ? -21.705 47.266  78.992  1.00 36.26 ? 154  LYS A N     1 
ATOM   949   C CA    . LYS A  1 156  ? -21.320 47.928  80.228  1.00 37.46 ? 154  LYS A CA    1 
ATOM   950   C C     . LYS A  1 156  ? -21.352 49.438  80.030  1.00 36.17 ? 154  LYS A C     1 
ATOM   951   O O     . LYS A  1 156  ? -21.007 49.940  78.957  1.00 34.58 ? 154  LYS A O     1 
ATOM   952   C CB    . LYS A  1 156  ? -19.932 47.479  80.683  1.00 34.77 ? 154  LYS A CB    1 
ATOM   953   N N     . LEU A  1 157  ? -21.778 50.161  81.062  1.00 36.51 ? 155  LEU A N     1 
ATOM   954   C CA    . LEU A  1 157  ? -21.871 51.613  81.007  1.00 38.06 ? 155  LEU A CA    1 
ATOM   955   C C     . LEU A  1 157  ? -20.797 52.235  81.889  1.00 39.86 ? 155  LEU A C     1 
ATOM   956   O O     . LEU A  1 157  ? -20.491 51.722  82.970  1.00 39.83 ? 155  LEU A O     1 
ATOM   957   C CB    . LEU A  1 157  ? -23.257 52.103  81.446  1.00 37.96 ? 155  LEU A CB    1 
ATOM   958   C CG    . LEU A  1 157  ? -23.547 53.589  81.185  1.00 43.43 ? 155  LEU A CG    1 
ATOM   959   C CD1   . LEU A  1 157  ? -23.458 53.906  79.702  1.00 38.79 ? 155  LEU A CD1   1 
ATOM   960   C CD2   . LEU A  1 157  ? -24.906 54.000  81.737  1.00 50.95 ? 155  LEU A CD2   1 
ATOM   961   N N     . THR A  1 158  ? -20.208 53.324  81.409  1.00 37.05 ? 156  THR A N     1 
ATOM   962   C CA    . THR A  1 158  ? -19.321 54.151  82.212  1.00 38.23 ? 156  THR A CA    1 
ATOM   963   C C     . THR A  1 158  ? -19.797 55.589  82.104  1.00 34.72 ? 156  THR A C     1 
ATOM   964   O O     . THR A  1 158  ? -20.393 55.978  81.098  1.00 35.63 ? 156  THR A O     1 
ATOM   965   C CB    . THR A  1 158  ? -17.855 54.045  81.756  1.00 40.00 ? 156  THR A CB    1 
ATOM   966   O OG1   . THR A  1 158  ? -17.725 54.572  80.430  1.00 43.04 ? 156  THR A OG1   1 
ATOM   967   C CG2   . THR A  1 158  ? -17.396 52.596  81.764  1.00 41.28 ? 156  THR A CG2   1 
ATOM   968   N N     . SER A  1 159  ? -19.557 56.378  83.153  1.00 34.48 ? 157  SER A N     1 
ATOM   969   C CA    . SER A  1 159  ? -20.003 57.767  83.092  1.00 33.99 ? 157  SER A CA    1 
ATOM   970   C C     . SER A  1 159  ? -19.082 58.607  82.217  1.00 30.40 ? 157  SER A C     1 
ATOM   971   O O     . SER A  1 159  ? -19.543 59.516  81.516  1.00 34.83 ? 157  SER A O     1 
ATOM   972   C CB    . SER A  1 159  ? -20.107 58.368  84.498  1.00 38.00 ? 157  SER A CB    1 
ATOM   973   O OG    . SER A  1 159  ? -18.842 58.483  85.131  1.00 41.65 ? 157  SER A OG    1 
ATOM   974   N N     . THR A  1 160  ? -17.787 58.313  82.230  1.00 31.89 ? 158  THR A N     1 
ATOM   975   C CA    . THR A  1 160  ? -16.823 59.033  81.418  1.00 26.95 ? 158  THR A CA    1 
ATOM   976   C C     . THR A  1 160  ? -16.031 58.064  80.547  1.00 29.25 ? 158  THR A C     1 
ATOM   977   O O     . THR A  1 160  ? -16.093 56.841  80.694  1.00 30.87 ? 158  THR A O     1 
ATOM   978   C CB    . THR A  1 160  ? -15.884 59.879  82.289  1.00 32.01 ? 158  THR A CB    1 
ATOM   979   O OG1   . THR A  1 160  ? -15.204 59.042  83.227  1.00 26.78 ? 158  THR A OG1   1 
ATOM   980   C CG2   . THR A  1 160  ? -16.670 60.941  83.037  1.00 30.26 ? 158  THR A CG2   1 
ATOM   981   N N     . VAL A  1 161  ? -15.259 58.650  79.646  1.00 25.79 ? 159  VAL A N     1 
ATOM   982   C CA    . VAL A  1 161  ? -14.749 57.991  78.457  1.00 25.46 ? 159  VAL A CA    1 
ATOM   983   C C     . VAL A  1 161  ? -13.231 58.066  78.493  1.00 24.57 ? 159  VAL A C     1 
ATOM   984   O O     . VAL A  1 161  ? -12.677 59.146  78.714  1.00 22.29 ? 159  VAL A O     1 
ATOM   985   C CB    . VAL A  1 161  ? -15.322 58.684  77.208  1.00 24.37 ? 159  VAL A CB    1 
ATOM   986   C CG1   . VAL A  1 161  ? -14.454 58.475  76.004  1.00 30.60 ? 159  VAL A CG1   1 
ATOM   987   C CG2   . VAL A  1 161  ? -16.782 58.235  76.984  1.00 30.62 ? 159  VAL A CG2   1 
ATOM   988   N N     . ASN A  1 162  ? -12.556 56.932  78.288  1.00 21.76 ? 160  ASN A N     1 
ATOM   989   C CA    . ASN A  1 162  ? -11.090 56.965  78.242  1.00 22.93 ? 160  ASN A CA    1 
ATOM   990   C C     . ASN A  1 162  ? -10.703 57.297  76.809  1.00 22.21 ? 160  ASN A C     1 
ATOM   991   O O     . ASN A  1 162  ? -10.518 56.411  75.966  1.00 19.95 ? 160  ASN A O     1 
ATOM   992   C CB    . ASN A  1 162  ? -10.463 55.661  78.730  1.00 20.79 ? 160  ASN A CB    1 
ATOM   993   C CG    . ASN A  1 162  ? -8.920  55.737  78.791  1.00 23.06 ? 160  ASN A CG    1 
ATOM   994   O OD1   . ASN A  1 162  ? -8.275  56.518  78.062  1.00 21.35 ? 160  ASN A OD1   1 
ATOM   995   N ND2   . ASN A  1 162  ? -8.330  54.935  79.667  1.00 21.92 ? 160  ASN A ND2   1 
ATOM   996   N N     . ASP A  1 163  ? -10.606 58.601  76.523  1.00 19.95 ? 161  ASP A N     1 
ATOM   997   C CA    . ASP A  1 163  ? -10.396 59.030  75.145  1.00 19.77 ? 161  ASP A CA    1 
ATOM   998   C C     . ASP A  1 163  ? -8.991  58.737  74.648  1.00 20.09 ? 161  ASP A C     1 
ATOM   999   O O     . ASP A  1 163  ? -8.788  58.639  73.437  1.00 20.36 ? 161  ASP A O     1 
ATOM   1000  C CB    . ASP A  1 163  ? -10.721 60.525  74.964  1.00 21.51 ? 161  ASP A CB    1 
ATOM   1001  C CG    . ASP A  1 163  ? -10.181 61.424  76.088  1.00 25.38 ? 161  ASP A CG    1 
ATOM   1002  O OD1   . ASP A  1 163  ? -10.182 61.029  77.272  1.00 21.37 ? 161  ASP A OD1   1 
ATOM   1003  O OD2   . ASP A  1 163  ? -9.792  62.567  75.764  1.00 27.96 ? 161  ASP A OD2   1 
ATOM   1004  N N     . ARG A  1 164  ? -8.011  58.596  75.542  1.00 20.10 ? 162  ARG A N     1 
ATOM   1005  C CA    . ARG A  1 164  ? -6.676  58.234  75.084  1.00 20.42 ? 162  ARG A CA    1 
ATOM   1006  C C     . ARG A  1 164  ? -6.629  56.776  74.665  1.00 20.63 ? 162  ARG A C     1 
ATOM   1007  O O     . ARG A  1 164  ? -5.991  56.432  73.660  1.00 21.22 ? 162  ARG A O     1 
ATOM   1008  C CB    . ARG A  1 164  ? -5.636  58.517  76.178  1.00 20.39 ? 162  ARG A CB    1 
ATOM   1009  C CG    . ARG A  1 164  ? -5.440  59.994  76.501  1.00 25.34 ? 162  ARG A CG    1 
ATOM   1010  C CD    . ARG A  1 164  ? -5.599  60.876  75.269  1.00 31.96 ? 162  ARG A CD    1 
ATOM   1011  N NE    . ARG A  1 164  ? -4.682  60.543  74.187  1.00 34.71 ? 162  ARG A NE    1 
ATOM   1012  C CZ    . ARG A  1 164  ? -4.900  60.862  72.916  1.00 35.74 ? 162  ARG A CZ    1 
ATOM   1013  N NH1   . ARG A  1 164  ? -5.982  61.537  72.549  1.00 34.37 ? 162  ARG A NH1   1 
ATOM   1014  N NH2   . ARG A  1 164  ? -4.018  60.489  71.989  1.00 31.69 ? 162  ARG A NH2   1 
ATOM   1015  N N     . SER A  1 165  ? -7.330  55.914  75.411  1.00 20.46 ? 163  SER A N     1 
ATOM   1016  C CA    . SER A  1 165  ? -7.473  54.515  75.023  1.00 21.06 ? 163  SER A CA    1 
ATOM   1017  C C     . SER A  1 165  ? -8.185  54.391  73.685  1.00 20.82 ? 163  SER A C     1 
ATOM   1018  O O     . SER A  1 165  ? -7.783  53.597  72.822  1.00 21.15 ? 163  SER A O     1 
ATOM   1019  C CB    . SER A  1 165  ? -8.263  53.756  76.097  1.00 20.45 ? 163  SER A CB    1 
ATOM   1020  O OG    . SER A  1 165  ? -8.382  52.385  75.761  1.00 22.57 ? 163  SER A OG    1 
ATOM   1021  N N     . LEU A  1 166  ? -9.266  55.151  73.512  1.00 20.59 ? 164  LEU A N     1 
ATOM   1022  C CA    . LEU A  1 166  ? -10.036 55.070  72.271  1.00 20.73 ? 164  LEU A CA    1 
ATOM   1023  C C     . LEU A  1 166  ? -9.247  55.630  71.092  1.00 21.04 ? 164  LEU A C     1 
ATOM   1024  O O     . LEU A  1 166  ? -9.332  55.108  69.971  1.00 21.33 ? 164  LEU A O     1 
ATOM   1025  C CB    . LEU A  1 166  ? -11.357 55.807  72.441  1.00 20.41 ? 164  LEU A CB    1 
ATOM   1026  C CG    . LEU A  1 166  ? -12.339 55.128  73.402  1.00 21.85 ? 164  LEU A CG    1 
ATOM   1027  C CD1   . LEU A  1 166  ? -13.495 56.041  73.683  1.00 23.87 ? 164  LEU A CD1   1 
ATOM   1028  C CD2   . LEU A  1 166  ? -12.817 53.782  72.858  1.00 20.37 ? 164  LEU A CD2   1 
ATOM   1029  N N     . ALA A  1 167  ? -8.487  56.705  71.312  1.00 21.01 ? 165  ALA A N     1 
ATOM   1030  C CA    . ALA A  1 167  ? -7.687  57.253  70.217  1.00 22.27 ? 165  ALA A CA    1 
ATOM   1031  C C     . ALA A  1 167  ? -6.598  56.271  69.792  1.00 21.72 ? 165  ALA A C     1 
ATOM   1032  O O     . ALA A  1 167  ? -6.355  56.081  68.595  1.00 22.08 ? 165  ALA A O     1 
ATOM   1033  C CB    . ALA A  1 167  ? -7.079  58.595  70.624  1.00 21.25 ? 165  ALA A CB    1 
ATOM   1034  N N     . ALA A  1 168  ? -5.943  55.627  70.760  1.00 21.68 ? 166  ALA A N     1 
ATOM   1035  C CA    . ALA A  1 168  ? -4.988  54.570  70.434  1.00 22.05 ? 166  ALA A CA    1 
ATOM   1036  C C     . ALA A  1 168  ? -5.664  53.431  69.678  1.00 22.24 ? 166  ALA A C     1 
ATOM   1037  O O     . ALA A  1 168  ? -5.115  52.913  68.698  1.00 22.65 ? 166  ALA A O     1 
ATOM   1038  C CB    . ALA A  1 168  ? -4.327  54.043  71.718  1.00 21.94 ? 166  ALA A CB    1 
ATOM   1039  N N     . ALA A  1 169  ? -6.858  53.022  70.124  1.00 21.97 ? 167  ALA A N     1 
ATOM   1040  C CA    . ALA A  1 169  ? -7.540  51.912  69.468  1.00 22.16 ? 167  ALA A CA    1 
ATOM   1041  C C     . ALA A  1 169  ? -7.906  52.273  68.036  1.00 22.40 ? 167  ALA A C     1 
ATOM   1042  O O     . ALA A  1 169  ? -7.753  51.455  67.124  1.00 22.78 ? 167  ALA A O     1 
ATOM   1043  C CB    . ALA A  1 169  ? -8.792  51.518  70.251  1.00 21.83 ? 167  ALA A CB    1 
ATOM   1044  N N     . LEU A  1 170  ? -8.378  53.499  67.821  1.00 22.84 ? 168  LEU A N     1 
ATOM   1045  C CA    . LEU A  1 170  ? -8.794  53.904  66.478  1.00 22.87 ? 168  LEU A CA    1 
ATOM   1046  C C     . LEU A  1 170  ? -7.601  53.928  65.527  1.00 22.89 ? 168  LEU A C     1 
ATOM   1047  O O     . LEU A  1 170  ? -7.673  53.411  64.407  1.00 25.15 ? 168  LEU A O     1 
ATOM   1048  C CB    . LEU A  1 170  ? -9.478  55.270  66.546  1.00 22.13 ? 168  LEU A CB    1 
ATOM   1049  C CG    . LEU A  1 170  ? -10.096 55.744  65.233  1.00 25.35 ? 168  LEU A CG    1 
ATOM   1050  C CD1   . LEU A  1 170  ? -11.079 54.706  64.708  1.00 24.13 ? 168  LEU A CD1   1 
ATOM   1051  C CD2   . LEU A  1 170  ? -10.788 57.078  65.442  1.00 28.29 ? 168  LEU A CD2   1 
ATOM   1052  N N     . THR A  1 171  ? -6.485  54.520  65.963  1.00 22.91 ? 169  THR A N     1 
ATOM   1053  C CA    . THR A  1 171  ? -5.261  54.488  65.166  1.00 23.38 ? 169  THR A CA    1 
ATOM   1054  C C     . THR A  1 171  ? -4.842  53.054  64.865  1.00 25.60 ? 169  THR A C     1 
ATOM   1055  O O     . THR A  1 171  ? -4.535  52.712  63.717  1.00 24.17 ? 169  THR A O     1 
ATOM   1056  C CB    . THR A  1 171  ? -4.140  55.229  65.905  1.00 26.70 ? 169  THR A CB    1 
ATOM   1057  O OG1   . THR A  1 171  ? -4.481  56.611  66.024  1.00 29.05 ? 169  THR A OG1   1 
ATOM   1058  C CG2   . THR A  1 171  ? -2.791  55.095  65.174  1.00 26.05 ? 169  THR A CG2   1 
ATOM   1059  N N     . ARG A  1 172  ? -4.854  52.190  65.891  1.00 23.54 ? 170  ARG A N     1 
ATOM   1060  C CA    . ARG A  1 172  ? -4.445  50.801  65.701  1.00 23.89 ? 170  ARG A CA    1 
ATOM   1061  C C     . ARG A  1 172  ? -5.312  50.109  64.654  1.00 24.13 ? 170  ARG A C     1 
ATOM   1062  O O     . ARG A  1 172  ? -4.796  49.474  63.732  1.00 24.61 ? 170  ARG A O     1 
ATOM   1063  C CB    . ARG A  1 172  ? -4.500  50.044  67.035  1.00 23.63 ? 170  ARG A CB    1 
ATOM   1064  C CG    . ARG A  1 172  ? -3.865  48.661  66.984  1.00 25.41 ? 170  ARG A CG    1 
ATOM   1065  C CD    . ARG A  1 172  ? -3.958  47.905  68.323  1.00 23.79 ? 170  ARG A CD    1 
ATOM   1066  N NE    . ARG A  1 172  ? -3.715  48.731  69.503  1.00 23.39 ? 170  ARG A NE    1 
ATOM   1067  C CZ    . ARG A  1 172  ? -4.662  49.182  70.316  1.00 22.93 ? 170  ARG A CZ    1 
ATOM   1068  N NH1   . ARG A  1 172  ? -5.947  48.963  70.072  1.00 22.79 ? 170  ARG A NH1   1 
ATOM   1069  N NH2   . ARG A  1 172  ? -4.310  49.864  71.406  1.00 22.63 ? 170  ARG A NH2   1 
ATOM   1070  N N     . LEU A  1 173  ? -6.637  50.219  64.778  1.00 23.82 ? 171  LEU A N     1 
ATOM   1071  C CA    . LEU A  1 173  ? -7.502  49.450  63.889  1.00 24.05 ? 171  LEU A CA    1 
ATOM   1072  C C     . LEU A  1 173  ? -7.452  49.988  62.466  1.00 24.83 ? 171  LEU A C     1 
ATOM   1073  O O     . LEU A  1 173  ? -7.538  49.216  61.508  1.00 24.81 ? 171  LEU A O     1 
ATOM   1074  C CB    . LEU A  1 173  ? -8.938  49.429  64.427  1.00 23.64 ? 171  LEU A CB    1 
ATOM   1075  C CG    . LEU A  1 173  ? -9.811  50.674  64.293  1.00 23.31 ? 171  LEU A CG    1 
ATOM   1076  C CD1   . LEU A  1 173  ? -10.578 50.650  62.958  1.00 25.35 ? 171  LEU A CD1   1 
ATOM   1077  C CD2   . LEU A  1 173  ? -10.792 50.807  65.453  1.00 24.53 ? 171  LEU A CD2   1 
ATOM   1078  N N     . ILE A  1 174  ? -7.318  51.301  62.301  1.00 24.26 ? 172  ILE A N     1 
ATOM   1079  C CA    . ILE A  1 174  ? -7.212  51.840  60.949  1.00 24.63 ? 172  ILE A CA    1 
ATOM   1080  C C     . ILE A  1 174  ? -5.894  51.415  60.315  1.00 26.84 ? 172  ILE A C     1 
ATOM   1081  O O     . ILE A  1 174  ? -5.859  50.984  59.158  1.00 29.13 ? 172  ILE A O     1 
ATOM   1082  C CB    . ILE A  1 174  ? -7.381  53.371  60.974  1.00 26.30 ? 172  ILE A CB    1 
ATOM   1083  C CG1   . ILE A  1 174  ? -8.821  53.719  61.361  1.00 28.34 ? 172  ILE A CG1   1 
ATOM   1084  C CG2   . ILE A  1 174  ? -7.029  53.965  59.616  1.00 28.33 ? 172  ILE A CG2   1 
ATOM   1085  C CD1   . ILE A  1 174  ? -9.075  55.204  61.565  1.00 28.74 ? 172  ILE A CD1   1 
ATOM   1086  N N     . SER A  1 175  ? -4.794  51.489  61.072  1.00 25.13 ? 173  SER A N     1 
ATOM   1087  C CA    . SER A  1 175  ? -3.501  51.106  60.514  1.00 25.65 ? 173  SER A CA    1 
ATOM   1088  C C     . SER A  1 175  ? -3.454  49.627  60.154  1.00 26.02 ? 173  SER A C     1 
ATOM   1089  O O     . SER A  1 175  ? -2.703  49.236  59.261  1.00 26.73 ? 173  SER A O     1 
ATOM   1090  C CB    . SER A  1 175  ? -2.374  51.437  61.493  1.00 26.05 ? 173  SER A CB    1 
ATOM   1091  O OG    . SER A  1 175  ? -2.248  52.836  61.702  1.00 31.99 ? 173  SER A OG    1 
ATOM   1092  N N     . ARG A  1 176  ? -4.249  48.798  60.831  1.00 25.76 ? 174  ARG A N     1 
ATOM   1093  C CA    . ARG A  1 176  ? -4.256  47.351  60.636  1.00 27.12 ? 174  ARG A CA    1 
ATOM   1094  C C     . ARG A  1 176  ? -5.226  46.916  59.541  1.00 27.34 ? 174  ARG A C     1 
ATOM   1095  O O     . ARG A  1 176  ? -4.892  46.047  58.722  1.00 28.84 ? 174  ARG A O     1 
ATOM   1096  C CB    . ARG A  1 176  ? -4.624  46.653  61.953  1.00 28.39 ? 174  ARG A CB    1 
ATOM   1097  C CG    . ARG A  1 176  ? -4.607  45.121  61.910  1.00 29.95 ? 174  ARG A CG    1 
ATOM   1098  C CD    . ARG A  1 176  ? -4.850  44.520  63.316  1.00 25.95 ? 174  ARG A CD    1 
ATOM   1099  N NE    . ARG A  1 176  ? -6.261  44.515  63.689  1.00 25.35 ? 174  ARG A NE    1 
ATOM   1100  C CZ    . ARG A  1 176  ? -6.808  45.225  64.669  1.00 29.04 ? 174  ARG A CZ    1 
ATOM   1101  N NH1   . ARG A  1 176  ? -6.075  45.978  65.484  1.00 25.31 ? 174  ARG A NH1   1 
ATOM   1102  N NH2   . ARG A  1 176  ? -8.125  45.166  64.852  1.00 30.37 ? 174  ARG A NH2   1 
ATOM   1103  N N     . CYS A  1 177  ? -6.418  47.518  59.495  1.00 30.58 ? 175  CYS A N     1 
ATOM   1104  C CA    . CYS A  1 177  ? -7.470  47.048  58.601  1.00 27.53 ? 175  CYS A CA    1 
ATOM   1105  C C     . CYS A  1 177  ? -7.847  48.033  57.503  1.00 33.12 ? 175  CYS A C     1 
ATOM   1106  O O     . CYS A  1 177  ? -8.471  47.617  56.525  1.00 32.01 ? 175  CYS A O     1 
ATOM   1107  C CB    . CYS A  1 177  ? -8.728  46.691  59.406  1.00 30.54 ? 175  CYS A CB    1 
ATOM   1108  S SG    . CYS A  1 177  ? -8.446  45.499  60.773  1.00 35.62 ? 175  CYS A SG    1 
ATOM   1109  N N     . GLY A  1 178  ? -7.504  49.315  57.639  1.00 31.16 ? 176  GLY A N     1 
ATOM   1110  C CA    . GLY A  1 178  ? -7.714  50.244  56.530  1.00 33.10 ? 176  GLY A CA    1 
ATOM   1111  C C     . GLY A  1 178  ? -9.171  50.580  56.220  1.00 29.83 ? 176  GLY A C     1 
ATOM   1112  O O     . GLY A  1 178  ? -10.087 50.403  57.029  1.00 29.60 ? 176  GLY A O     1 
ATOM   1113  N N     . GLU A  1 179  ? -9.366  51.099  55.009  1.00 34.34 ? 177  GLU A N     1 
ATOM   1114  C CA    . GLU A  1 179  ? -10.695 51.521  54.559  1.00 30.98 ? 177  GLU A CA    1 
ATOM   1115  C C     . GLU A  1 179  ? -11.792 50.467  54.719  1.00 31.84 ? 177  GLU A C     1 
ATOM   1116  O O     . GLU A  1 179  ? -12.921 50.847  55.081  1.00 31.50 ? 177  GLU A O     1 
ATOM   1117  C CB    . GLU A  1 179  ? -10.592 51.980  53.096  1.00 35.46 ? 177  GLU A CB    1 
ATOM   1118  C CG    . GLU A  1 179  ? -11.870 52.526  52.495  1.00 38.31 ? 177  GLU A CG    1 
ATOM   1119  C CD    . GLU A  1 179  ? -11.668 52.938  51.041  1.00 48.59 ? 177  GLU A CD    1 
ATOM   1120  O OE1   . GLU A  1 179  ? -10.551 53.389  50.708  1.00 49.45 ? 177  GLU A OE1   1 
ATOM   1121  O OE2   . GLU A  1 179  ? -12.612 52.800  50.231  1.00 54.41 ? 177  GLU A OE2   1 
ATOM   1122  N N     . PRO A  1 180  ? -11.563 49.171  54.455  1.00 29.13 ? 178  PRO A N     1 
ATOM   1123  C CA    . PRO A  1 180  ? -12.664 48.205  54.596  1.00 26.47 ? 178  PRO A CA    1 
ATOM   1124  C C     . PRO A  1 180  ? -13.356 48.217  55.949  1.00 31.60 ? 178  PRO A C     1 
ATOM   1125  O O     . PRO A  1 180  ? -14.586 48.074  56.007  1.00 30.54 ? 178  PRO A O     1 
ATOM   1126  C CB    . PRO A  1 180  ? -11.968 46.867  54.324  1.00 32.01 ? 178  PRO A CB    1 
ATOM   1127  C CG    . PRO A  1 180  ? -10.908 47.207  53.343  1.00 30.07 ? 178  PRO A CG    1 
ATOM   1128  C CD    . PRO A  1 180  ? -10.400 48.563  53.775  1.00 29.71 ? 178  PRO A CD    1 
ATOM   1129  N N     . VAL A  1 181  ? -12.612 48.376  57.046  1.00 27.83 ? 179  VAL A N     1 
ATOM   1130  C CA    . VAL A  1 181  ? -13.274 48.361  58.337  1.00 27.58 ? 179  VAL A CA    1 
ATOM   1131  C C     . VAL A  1 181  ? -14.002 49.684  58.597  1.00 27.68 ? 179  VAL A C     1 
ATOM   1132  O O     . VAL A  1 181  ? -15.022 49.701  59.289  1.00 27.98 ? 179  VAL A O     1 
ATOM   1133  C CB    . VAL A  1 181  ? -12.259 48.021  59.449  1.00 27.68 ? 179  VAL A CB    1 
ATOM   1134  C CG1   . VAL A  1 181  ? -11.317 49.198  59.729  1.00 26.50 ? 179  VAL A CG1   1 
ATOM   1135  C CG2   . VAL A  1 181  ? -12.984 47.565  60.699  1.00 29.05 ? 179  VAL A CG2   1 
ATOM   1136  N N     . ILE A  1 182  ? -13.505 50.798  58.050  1.00 28.23 ? 180  ILE A N     1 
ATOM   1137  C CA    . ILE A  1 182  ? -14.185 52.084  58.197  1.00 26.45 ? 180  ILE A CA    1 
ATOM   1138  C C     . ILE A  1 182  ? -15.530 52.052  57.470  1.00 29.20 ? 180  ILE A C     1 
ATOM   1139  O O     . ILE A  1 182  ? -16.563 52.465  58.009  1.00 29.87 ? 180  ILE A O     1 
ATOM   1140  C CB    . ILE A  1 182  ? -13.286 53.220  57.670  1.00 30.62 ? 180  ILE A CB    1 
ATOM   1141  C CG1   . ILE A  1 182  ? -11.984 53.296  58.479  1.00 27.26 ? 180  ILE A CG1   1 
ATOM   1142  C CG2   . ILE A  1 182  ? -14.011 54.560  57.699  1.00 28.31 ? 180  ILE A CG2   1 
ATOM   1143  C CD1   . ILE A  1 182  ? -10.925 54.153  57.840  1.00 28.39 ? 180  ILE A CD1   1 
ATOM   1144  N N     . ARG A  1 183  ? -15.534 51.536  56.243  1.00 30.40 ? 181  ARG A N     1 
ATOM   1145  C CA    . ARG A  1 183  ? -16.777 51.424  55.482  1.00 29.95 ? 181  ARG A CA    1 
ATOM   1146  C C     . ARG A  1 183  ? -17.793 50.528  56.188  1.00 32.16 ? 181  ARG A C     1 
ATOM   1147  O O     . ARG A  1 183  ? -18.985 50.851  56.241  1.00 36.18 ? 181  ARG A O     1 
ATOM   1148  C CB    . ARG A  1 183  ? -16.477 50.903  54.071  1.00 29.54 ? 181  ARG A CB    1 
ATOM   1149  N N     . ARG A  1 184  ? -17.342 49.401  56.745  1.00 31.05 ? 182  ARG A N     1 
ATOM   1150  C CA    . ARG A  1 184  ? -18.246 48.527  57.489  1.00 30.34 ? 182  ARG A CA    1 
ATOM   1151  C C     . ARG A  1 184  ? -18.771 49.202  58.753  1.00 34.19 ? 182  ARG A C     1 
ATOM   1152  O O     . ARG A  1 184  ? -19.948 49.053  59.101  1.00 32.61 ? 182  ARG A O     1 
ATOM   1153  C CB    . ARG A  1 184  ? -17.540 47.221  57.835  1.00 35.88 ? 182  ARG A CB    1 
ATOM   1154  C CG    . ARG A  1 184  ? -17.421 46.285  56.653  1.00 39.74 ? 182  ARG A CG    1 
ATOM   1155  C CD    . ARG A  1 184  ? -18.708 45.489  56.464  1.00 38.06 ? 182  ARG A CD    1 
ATOM   1156  N NE    . ARG A  1 184  ? -18.715 44.285  57.286  1.00 43.44 ? 182  ARG A NE    1 
ATOM   1157  C CZ    . ARG A  1 184  ? -19.472 44.101  58.359  1.00 44.87 ? 182  ARG A CZ    1 
ATOM   1158  N NH1   . ARG A  1 184  ? -20.346 45.013  58.756  1.00 49.84 ? 182  ARG A NH1   1 
ATOM   1159  N NH2   . ARG A  1 184  ? -19.357 42.967  59.046  1.00 39.87 ? 182  ARG A NH2   1 
ATOM   1160  N N     . GLY A  1 185  ? -17.915 49.930  59.466  1.00 31.19 ? 183  GLY A N     1 
ATOM   1161  C CA    . GLY A  1 185  ? -18.396 50.662  60.624  1.00 27.47 ? 183  GLY A CA    1 
ATOM   1162  C C     . GLY A  1 185  ? -19.463 51.673  60.251  1.00 33.37 ? 183  GLY A C     1 
ATOM   1163  O O     . GLY A  1 185  ? -20.507 51.767  60.903  1.00 28.12 ? 183  GLY A O     1 
ATOM   1164  N N     . VAL A  1 186  ? -19.222 52.427  59.179  1.00 30.69 ? 184  VAL A N     1 
ATOM   1165  C CA    . VAL A  1 186  ? -20.176 53.445  58.750  1.00 34.50 ? 184  VAL A CA    1 
ATOM   1166  C C     . VAL A  1 186  ? -21.519 52.813  58.417  1.00 32.33 ? 184  VAL A C     1 
ATOM   1167  O O     . VAL A  1 186  ? -22.576 53.335  58.792  1.00 35.90 ? 184  VAL A O     1 
ATOM   1168  C CB    . VAL A  1 186  ? -19.606 54.234  57.557  1.00 36.50 ? 184  VAL A CB    1 
ATOM   1169  C CG1   . VAL A  1 186  ? -20.704 55.035  56.866  1.00 33.72 ? 184  VAL A CG1   1 
ATOM   1170  C CG2   . VAL A  1 186  ? -18.473 55.140  58.023  1.00 33.26 ? 184  VAL A CG2   1 
ATOM   1171  N N     . ASP A  1 187  ? -21.503 51.678  57.717  1.00 35.71 ? 185  ASP A N     1 
ATOM   1172  C CA    . ASP A  1 187  ? -22.756 51.012  57.378  1.00 31.97 ? 185  ASP A CA    1 
ATOM   1173  C C     . ASP A  1 187  ? -23.479 50.535  58.630  1.00 35.24 ? 185  ASP A C     1 
ATOM   1174  O O     . ASP A  1 187  ? -24.702 50.671  58.740  1.00 34.08 ? 185  ASP A O     1 
ATOM   1175  C CB    . ASP A  1 187  ? -22.491 49.847  56.427  1.00 33.98 ? 185  ASP A CB    1 
ATOM   1176  C CG    . ASP A  1 187  ? -21.963 50.305  55.078  1.00 43.14 ? 185  ASP A CG    1 
ATOM   1177  O OD1   . ASP A  1 187  ? -22.140 51.494  54.733  1.00 50.23 ? 185  ASP A OD1   1 
ATOM   1178  O OD2   . ASP A  1 187  ? -21.377 49.475  54.354  1.00 47.82 ? 185  ASP A OD2   1 
ATOM   1179  N N     . MET A  1 188  ? -22.734 49.997  59.600  1.00 31.67 ? 186  MET A N     1 
ATOM   1180  C CA    . MET A  1 188  ? -23.354 49.516  60.829  1.00 34.06 ? 186  MET A CA    1 
ATOM   1181  C C     . MET A  1 188  ? -23.977 50.662  61.618  1.00 39.56 ? 186  MET A C     1 
ATOM   1182  O O     . MET A  1 188  ? -25.126 50.569  62.071  1.00 38.83 ? 186  MET A O     1 
ATOM   1183  C CB    . MET A  1 188  ? -22.316 48.781  61.679  1.00 39.67 ? 186  MET A CB    1 
ATOM   1184  C CG    . MET A  1 188  ? -22.893 48.163  62.944  1.00 40.86 ? 186  MET A CG    1 
ATOM   1185  S SD    . MET A  1 188  ? -23.843 46.679  62.566  1.00 58.47 ? 186  MET A SD    1 
ATOM   1186  C CE    . MET A  1 188  ? -22.544 45.671  61.837  1.00 48.92 ? 186  MET A CE    1 
ATOM   1187  N N     . ALA A  1 189  ? -23.229 51.755  61.804  1.00 35.79 ? 187  ALA A N     1 
ATOM   1188  C CA    . ALA A  1 189  ? -23.763 52.865  62.586  1.00 34.66 ? 187  ALA A CA    1 
ATOM   1189  C C     . ALA A  1 189  ? -24.978 53.483  61.912  1.00 37.65 ? 187  ALA A C     1 
ATOM   1190  O O     . ALA A  1 189  ? -25.895 53.948  62.600  1.00 36.85 ? 187  ALA A O     1 
ATOM   1191  C CB    . ALA A  1 189  ? -22.690 53.928  62.819  1.00 34.47 ? 187  ALA A CB    1 
ATOM   1192  N N     . MET A  1 190  ? -25.008 53.479  60.577  1.00 35.64 ? 188  MET A N     1 
ATOM   1193  C CA    . MET A  1 190  ? -26.123 54.078  59.849  1.00 40.07 ? 188  MET A CA    1 
ATOM   1194  C C     . MET A  1 190  ? -27.400 53.264  60.022  1.00 39.57 ? 188  MET A C     1 
ATOM   1195  O O     . MET A  1 190  ? -28.486 53.832  60.179  1.00 40.12 ? 188  MET A O     1 
ATOM   1196  C CB    . MET A  1 190  ? -25.768 54.211  58.369  1.00 37.11 ? 188  MET A CB    1 
ATOM   1197  C CG    . MET A  1 190  ? -26.722 55.089  57.577  1.00 41.61 ? 188  MET A CG    1 
ATOM   1198  S SD    . MET A  1 190  ? -26.366 55.028  55.803  1.00 53.01 ? 188  MET A SD    1 
ATOM   1199  C CE    . MET A  1 190  ? -25.774 56.698  55.499  1.00 46.52 ? 188  MET A CE    1 
ATOM   1200  N N     . ARG A  1 191  ? -27.290 51.935  59.990  1.00 36.25 ? 189  ARG A N     1 
ATOM   1201  C CA    . ARG A  1 191  ? -28.457 51.093  60.215  1.00 42.62 ? 189  ARG A CA    1 
ATOM   1202  C C     . ARG A  1 191  ? -28.937 51.193  61.659  1.00 43.43 ? 189  ARG A C     1 
ATOM   1203  O O     . ARG A  1 191  ? -30.146 51.195  61.920  1.00 41.00 ? 189  ARG A O     1 
ATOM   1204  C CB    . ARG A  1 191  ? -28.134 49.642  59.852  1.00 38.02 ? 189  ARG A CB    1 
ATOM   1205  N N     . MET A  1 192  ? -28.005 51.278  62.611  1.00 38.72 ? 190  MET A N     1 
ATOM   1206  C CA    . MET A  1 192  ? -28.398 51.298  64.014  1.00 38.78 ? 190  MET A CA    1 
ATOM   1207  C C     . MET A  1 192  ? -29.052 52.618  64.395  1.00 40.51 ? 190  MET A C     1 
ATOM   1208  O O     . MET A  1 192  ? -30.073 52.631  65.095  1.00 40.31 ? 190  MET A O     1 
ATOM   1209  C CB    . MET A  1 192  ? -27.187 51.040  64.902  1.00 38.95 ? 190  MET A CB    1 
ATOM   1210  C CG    . MET A  1 192  ? -26.585 49.662  64.741  1.00 38.03 ? 190  MET A CG    1 
ATOM   1211  S SD    . MET A  1 192  ? -25.455 49.364  66.107  1.00 51.49 ? 190  MET A SD    1 
ATOM   1212  C CE    . MET A  1 192  ? -26.635 48.990  67.408  1.00 43.73 ? 190  MET A CE    1 
ATOM   1213  N N     . MET A  1 193  ? -28.473 53.737  63.952  1.00 37.96 ? 191  MET A N     1 
ATOM   1214  C CA    . MET A  1 193  ? -28.960 55.053  64.352  1.00 42.92 ? 191  MET A CA    1 
ATOM   1215  C C     . MET A  1 193  ? -30.189 55.495  63.567  1.00 42.65 ? 191  MET A C     1 
ATOM   1216  O O     . MET A  1 193  ? -31.026 56.229  64.103  1.00 40.28 ? 191  MET A O     1 
ATOM   1217  C CB    . MET A  1 193  ? -27.856 56.092  64.188  1.00 40.59 ? 191  MET A CB    1 
ATOM   1218  C CG    . MET A  1 193  ? -26.757 55.976  65.229  1.00 42.42 ? 191  MET A CG    1 
ATOM   1219  S SD    . MET A  1 193  ? -25.763 57.473  65.333  1.00 51.47 ? 191  MET A SD    1 
ATOM   1220  C CE    . MET A  1 193  ? -24.984 57.497  63.722  1.00 42.95 ? 191  MET A CE    1 
ATOM   1221  N N     . GLY A  1 194  ? -30.309 55.081  62.311  1.00 40.59 ? 192  GLY A N     1 
ATOM   1222  C CA    . GLY A  1 194  ? -31.412 55.536  61.489  1.00 41.16 ? 192  GLY A CA    1 
ATOM   1223  C C     . GLY A  1 194  ? -32.567 54.563  61.380  1.00 42.72 ? 192  GLY A C     1 
ATOM   1224  O O     . GLY A  1 194  ? -33.651 54.928  60.898  1.00 39.01 ? 192  GLY A O     1 
ATOM   1225  N N     . GLU A  1 195  ? -32.344 53.314  61.824  1.00 36.23 ? 193  GLU A N     1 
ATOM   1226  C CA    . GLU A  1 195  ? -33.333 52.253  61.636  1.00 39.94 ? 193  GLU A CA    1 
ATOM   1227  C C     . GLU A  1 195  ? -33.591 51.411  62.876  1.00 37.65 ? 193  GLU A C     1 
ATOM   1228  O O     . GLU A  1 195  ? -34.698 50.873  63.001  1.00 29.58 ? 193  GLU A O     1 
ATOM   1229  C CB    . GLU A  1 195  ? -32.928 51.324  60.490  1.00 44.11 ? 193  GLU A CB    1 
ATOM   1230  C CG    . GLU A  1 195  ? -32.797 51.998  59.140  1.00 48.11 ? 193  GLU A CG    1 
ATOM   1231  C CD    . GLU A  1 195  ? -31.887 51.225  58.200  1.00 52.09 ? 193  GLU A CD    1 
ATOM   1232  O OE1   . GLU A  1 195  ? -31.731 49.997  58.399  1.00 50.29 ? 193  GLU A OE1   1 
ATOM   1233  O OE2   . GLU A  1 195  ? -31.320 51.849  57.272  1.00 53.36 ? 193  GLU A OE2   1 
ATOM   1234  N N     . GLN A  1 196  ? -32.618 51.261  63.781  1.00 41.29 ? 194  GLN A N     1 
ATOM   1235  C CA    . GLN A  1 196  ? -32.733 50.414  64.965  1.00 41.35 ? 194  GLN A CA    1 
ATOM   1236  C C     . GLN A  1 196  ? -33.008 51.209  66.236  1.00 39.89 ? 194  GLN A C     1 
ATOM   1237  O O     . GLN A  1 196  ? -33.884 50.844  67.027  1.00 41.33 ? 194  GLN A O     1 
ATOM   1238  C CB    . GLN A  1 196  ? -31.450 49.595  65.157  1.00 40.13 ? 194  GLN A CB    1 
ATOM   1239  N N     . PHE A  1 197  ? -32.258 52.284  66.459  1.00 35.58 ? 195  PHE A N     1 
ATOM   1240  C CA    . PHE A  1 197  ? -32.508 53.117  67.628  1.00 37.49 ? 195  PHE A CA    1 
ATOM   1241  C C     . PHE A  1 197  ? -33.779 53.931  67.450  1.00 33.55 ? 195  PHE A C     1 
ATOM   1242  O O     . PHE A  1 197  ? -34.537 54.128  68.402  1.00 34.67 ? 195  PHE A O     1 
ATOM   1243  C CB    . PHE A  1 197  ? -31.317 54.036  67.882  1.00 36.91 ? 195  PHE A CB    1 
ATOM   1244  C CG    . PHE A  1 197  ? -30.053 53.306  68.242  1.00 43.59 ? 195  PHE A CG    1 
ATOM   1245  C CD1   . PHE A  1 197  ? -30.102 52.028  68.777  1.00 43.37 ? 195  PHE A CD1   1 
ATOM   1246  C CD2   . PHE A  1 197  ? -28.817 53.895  68.039  1.00 42.40 ? 195  PHE A CD2   1 
ATOM   1247  C CE1   . PHE A  1 197  ? -28.939 51.355  69.108  1.00 39.23 ? 195  PHE A CE1   1 
ATOM   1248  C CE2   . PHE A  1 197  ? -27.651 53.224  68.374  1.00 41.89 ? 195  PHE A CE2   1 
ATOM   1249  C CZ    . PHE A  1 197  ? -27.719 51.959  68.911  1.00 38.16 ? 195  PHE A CZ    1 
ATOM   1250  N N     . VAL A  1 198  ? -34.028 54.412  66.245  1.00 32.91 ? 196  VAL A N     1 
ATOM   1251  C CA    . VAL A  1 198  ? -35.256 55.129  65.952  1.00 33.23 ? 196  VAL A CA    1 
ATOM   1252  C C     . VAL A  1 198  ? -35.978 54.386  64.844  1.00 31.79 ? 196  VAL A C     1 
ATOM   1253  O O     . VAL A  1 198  ? -35.362 53.729  63.999  1.00 33.59 ? 196  VAL A O     1 
ATOM   1254  C CB    . VAL A  1 198  ? -35.003 56.598  65.549  1.00 30.80 ? 196  VAL A CB    1 
ATOM   1255  C CG1   . VAL A  1 198  ? -34.301 57.353  66.675  1.00 34.85 ? 196  VAL A CG1   1 
ATOM   1256  C CG2   . VAL A  1 198  ? -34.214 56.667  64.264  1.00 33.63 ? 196  VAL A CG2   1 
ATOM   1257  N N     . THR A  1 199  ? -37.303 54.477  64.867  1.00 27.70 ? 197  THR A N     1 
ATOM   1258  C CA    . THR A  1 199  ? -38.081 54.008  63.729  1.00 29.63 ? 197  THR A CA    1 
ATOM   1259  C C     . THR A  1 199  ? -37.803 54.870  62.510  1.00 33.77 ? 197  THR A C     1 
ATOM   1260  O O     . THR A  1 199  ? -37.725 54.363  61.386  1.00 37.61 ? 197  THR A O     1 
ATOM   1261  C CB    . THR A  1 199  ? -39.564 54.014  64.086  1.00 32.01 ? 197  THR A CB    1 
ATOM   1262  O OG1   . THR A  1 199  ? -39.755 53.190  65.245  1.00 29.95 ? 197  THR A OG1   1 
ATOM   1263  C CG2   . THR A  1 199  ? -40.425 53.475  62.934  1.00 30.62 ? 197  THR A CG2   1 
ATOM   1264  N N     . GLY A  1 200  ? -37.631 56.168  62.717  1.00 32.96 ? 198  GLY A N     1 
ATOM   1265  C CA    . GLY A  1 200  ? -37.342 57.071  61.622  1.00 32.87 ? 198  GLY A CA    1 
ATOM   1266  C C     . GLY A  1 200  ? -36.722 58.344  62.146  1.00 34.67 ? 198  GLY A C     1 
ATOM   1267  O O     . GLY A  1 200  ? -36.844 58.682  63.329  1.00 34.29 ? 198  GLY A O     1 
ATOM   1268  N N     . GLU A  1 201  ? -36.036 59.041  61.241  1.00 34.40 ? 199  GLU A N     1 
ATOM   1269  C CA    . GLU A  1 201  ? -35.420 60.320  61.571  1.00 38.24 ? 199  GLU A CA    1 
ATOM   1270  C C     . GLU A  1 201  ? -36.469 61.417  61.722  1.00 34.75 ? 199  GLU A C     1 
ATOM   1271  O O     . GLU A  1 201  ? -36.296 62.336  62.527  1.00 32.80 ? 199  GLU A O     1 
ATOM   1272  C CB    . GLU A  1 201  ? -34.395 60.663  60.482  1.00 40.14 ? 199  GLU A CB    1 
ATOM   1273  C CG    . GLU A  1 201  ? -33.619 61.953  60.651  1.00 45.45 ? 199  GLU A CG    1 
ATOM   1274  C CD    . GLU A  1 201  ? -32.616 62.164  59.510  1.00 59.41 ? 199  GLU A CD    1 
ATOM   1275  O OE1   . GLU A  1 201  ? -31.881 61.205  59.176  1.00 60.26 ? 199  GLU A OE1   1 
ATOM   1276  O OE2   . GLU A  1 201  ? -32.573 63.277  58.936  1.00 61.46 ? 199  GLU A OE2   1 
ATOM   1277  N N     . THR A  1 202  ? -37.556 61.333  60.959  1.00 32.41 ? 200  THR A N     1 
ATOM   1278  C CA    . THR A  1 202  ? -38.672 62.262  61.039  1.00 34.36 ? 200  THR A CA    1 
ATOM   1279  C C     . THR A  1 202  ? -39.966 61.466  61.156  1.00 29.78 ? 200  THR A C     1 
ATOM   1280  O O     . THR A  1 202  ? -40.013 60.279  60.829  1.00 28.59 ? 200  THR A O     1 
ATOM   1281  C CB    . THR A  1 202  ? -38.740 63.159  59.804  1.00 31.22 ? 200  THR A CB    1 
ATOM   1282  O OG1   . THR A  1 202  ? -39.028 62.343  58.662  1.00 33.14 ? 200  THR A OG1   1 
ATOM   1283  C CG2   . THR A  1 202  ? -37.412 63.879  59.591  1.00 35.80 ? 200  THR A CG2   1 
ATOM   1284  N N     . ILE A  1 203  ? -41.028 62.131  61.613  1.00 27.99 ? 201  ILE A N     1 
ATOM   1285  C CA    . ILE A  1 203  ? -42.319 61.451  61.704  1.00 27.40 ? 201  ILE A CA    1 
ATOM   1286  C C     . ILE A  1 203  ? -42.742 60.938  60.332  1.00 27.76 ? 201  ILE A C     1 
ATOM   1287  O O     . ILE A  1 203  ? -43.276 59.830  60.207  1.00 29.91 ? 201  ILE A O     1 
ATOM   1288  C CB    . ILE A  1 203  ? -43.383 62.372  62.335  1.00 29.16 ? 201  ILE A CB    1 
ATOM   1289  C CG1   . ILE A  1 203  ? -44.666 61.585  62.644  1.00 23.14 ? 201  ILE A CG1   1 
ATOM   1290  C CG2   . ILE A  1 203  ? -43.692 63.582  61.443  1.00 28.89 ? 201  ILE A CG2   1 
ATOM   1291  C CD1   . ILE A  1 203  ? -44.437 60.398  63.573  1.00 22.05 ? 201  ILE A CD1   1 
ATOM   1292  N N     . ARG A  1 204  ? -42.447 61.698  59.277  1.00 27.56 ? 202  ARG A N     1 
ATOM   1293  C CA    . ARG A  1 204  ? -42.780 61.247  57.928  1.00 31.97 ? 202  ARG A CA    1 
ATOM   1294  C C     . ARG A  1 204  ? -42.066 59.945  57.594  1.00 33.94 ? 202  ARG A C     1 
ATOM   1295  O O     . ARG A  1 204  ? -42.676 59.001  57.079  1.00 31.71 ? 202  ARG A O     1 
ATOM   1296  C CB    . ARG A  1 204  ? -42.418 62.328  56.912  1.00 35.34 ? 202  ARG A CB    1 
ATOM   1297  C CG    . ARG A  1 204  ? -43.608 62.892  56.196  1.00 40.48 ? 202  ARG A CG    1 
ATOM   1298  C CD    . ARG A  1 204  ? -43.481 64.403  56.024  1.00 44.76 ? 202  ARG A CD    1 
ATOM   1299  N NE    . ARG A  1 204  ? -44.766 65.071  56.204  1.00 41.02 ? 202  ARG A NE    1 
ATOM   1300  C CZ    . ARG A  1 204  ? -45.212 65.540  57.363  1.00 39.14 ? 202  ARG A CZ    1 
ATOM   1301  N NH1   . ARG A  1 204  ? -44.491 65.454  58.474  1.00 33.44 ? 202  ARG A NH1   1 
ATOM   1302  N NH2   . ARG A  1 204  ? -46.406 66.120  57.408  1.00 38.11 ? 202  ARG A NH2   1 
ATOM   1303  N N     . GLU A  1 205  ? -40.763 59.879  57.888  1.00 31.37 ? 203  GLU A N     1 
ATOM   1304  C CA    . GLU A  1 205  ? -39.992 58.671  57.623  1.00 31.32 ? 203  GLU A CA    1 
ATOM   1305  C C     . GLU A  1 205  ? -40.483 57.511  58.476  1.00 29.90 ? 203  GLU A C     1 
ATOM   1306  O O     . GLU A  1 205  ? -40.652 56.392  57.985  1.00 32.55 ? 203  GLU A O     1 
ATOM   1307  C CB    . GLU A  1 205  ? -38.508 58.935  57.888  1.00 35.59 ? 203  GLU A CB    1 
ATOM   1308  C CG    . GLU A  1 205  ? -37.564 57.870  57.336  1.00 37.95 ? 203  GLU A CG    1 
ATOM   1309  C CD    . GLU A  1 205  ? -36.096 58.245  57.527  1.00 39.71 ? 203  GLU A CD    1 
ATOM   1310  O OE1   . GLU A  1 205  ? -35.625 58.229  58.682  1.00 38.27 ? 203  GLU A OE1   1 
ATOM   1311  O OE2   . GLU A  1 205  ? -35.421 58.572  56.524  1.00 49.40 ? 203  GLU A OE2   1 
ATOM   1312  N N     . ALA A  1 206  ? -40.696 57.758  59.768  1.00 29.34 ? 204  ALA A N     1 
ATOM   1313  C CA    . ALA A  1 206  ? -41.163 56.695  60.648  1.00 31.22 ? 204  ALA A CA    1 
ATOM   1314  C C     . ALA A  1 206  ? -42.510 56.151  60.189  1.00 29.18 ? 204  ALA A C     1 
ATOM   1315  O O     . ALA A  1 206  ? -42.738 54.933  60.212  1.00 26.51 ? 204  ALA A O     1 
ATOM   1316  C CB    . ALA A  1 206  ? -41.242 57.205  62.086  1.00 31.22 ? 204  ALA A CB    1 
ATOM   1317  N N     . LEU A  1 207  ? -43.411 57.035  59.754  1.00 26.16 ? 205  LEU A N     1 
ATOM   1318  C CA    . LEU A  1 207  ? -44.721 56.579  59.293  1.00 28.41 ? 205  LEU A CA    1 
ATOM   1319  C C     . LEU A  1 207  ? -44.599 55.699  58.058  1.00 32.89 ? 205  LEU A C     1 
ATOM   1320  O O     . LEU A  1 207  ? -45.367 54.744  57.888  1.00 30.83 ? 205  LEU A O     1 
ATOM   1321  C CB    . LEU A  1 207  ? -45.630 57.779  59.013  1.00 30.00 ? 205  LEU A CB    1 
ATOM   1322  C CG    . LEU A  1 207  ? -46.166 58.467  60.270  1.00 26.57 ? 205  LEU A CG    1 
ATOM   1323  C CD1   . LEU A  1 207  ? -46.799 59.806  59.934  1.00 27.25 ? 205  LEU A CD1   1 
ATOM   1324  C CD2   . LEU A  1 207  ? -47.171 57.571  60.989  1.00 23.51 ? 205  LEU A CD2   1 
ATOM   1325  N N     . LYS A  1 208  ? -43.654 56.013  57.168  1.00 30.99 ? 206  LYS A N     1 
ATOM   1326  C CA    . LYS A  1 208  ? -43.473 55.175  55.987  1.00 32.52 ? 206  LYS A CA    1 
ATOM   1327  C C     . LYS A  1 208  ? -42.955 53.800  56.372  1.00 29.17 ? 206  LYS A C     1 
ATOM   1328  O O     . LYS A  1 208  ? -43.335 52.800  55.756  1.00 34.96 ? 206  LYS A O     1 
ATOM   1329  C CB    . LYS A  1 208  ? -42.527 55.848  54.988  1.00 35.35 ? 206  LYS A CB    1 
ATOM   1330  N N     . ARG A  1 209  ? -42.120 53.726  57.407  1.00 32.80 ? 207  ARG A N     1 
ATOM   1331  C CA    . ARG A  1 209  ? -41.535 52.461  57.824  1.00 32.93 ? 207  ARG A CA    1 
ATOM   1332  C C     . ARG A  1 209  ? -42.466 51.615  58.685  1.00 35.47 ? 207  ARG A C     1 
ATOM   1333  O O     . ARG A  1 209  ? -42.189 50.425  58.875  1.00 34.03 ? 207  ARG A O     1 
ATOM   1334  C CB    . ARG A  1 209  ? -40.228 52.730  58.564  1.00 33.71 ? 207  ARG A CB    1 
ATOM   1335  C CG    . ARG A  1 209  ? -39.146 53.220  57.627  1.00 37.22 ? 207  ARG A CG    1 
ATOM   1336  C CD    . ARG A  1 209  ? -37.939 53.674  58.402  1.00 37.90 ? 207  ARG A CD    1 
ATOM   1337  N NE    . ARG A  1 209  ? -36.818 53.982  57.527  1.00 48.26 ? 207  ARG A NE    1 
ATOM   1338  C CZ    . ARG A  1 209  ? -35.607 54.295  57.965  1.00 49.87 ? 207  ARG A CZ    1 
ATOM   1339  N NH1   . ARG A  1 209  ? -35.340 54.362  59.260  1.00 42.96 ? 207  ARG A NH1   1 
ATOM   1340  N NH2   . ARG A  1 209  ? -34.642 54.541  57.083  1.00 49.44 ? 207  ARG A NH2   1 
ATOM   1341  N N     . SER A  1 210  ? -43.566 52.190  59.180  1.00 32.17 ? 208  SER A N     1 
ATOM   1342  C CA    . SER A  1 210  ? -44.521 51.450  59.997  1.00 29.29 ? 208  SER A CA    1 
ATOM   1343  C C     . SER A  1 210  ? -45.479 50.595  59.177  1.00 32.56 ? 208  SER A C     1 
ATOM   1344  O O     . SER A  1 210  ? -46.099 49.685  59.735  1.00 28.89 ? 208  SER A O     1 
ATOM   1345  C CB    . SER A  1 210  ? -45.343 52.414  60.849  1.00 29.12 ? 208  SER A CB    1 
ATOM   1346  O OG    . SER A  1 210  ? -44.508 53.275  61.600  1.00 28.54 ? 208  SER A OG    1 
ATOM   1347  N N     . LYS A  1 211  ? -45.624 50.869  57.879  1.00 31.00 ? 209  LYS A N     1 
ATOM   1348  C CA    . LYS A  1 211  ? -46.610 50.156  57.072  1.00 34.43 ? 209  LYS A CA    1 
ATOM   1349  C C     . LYS A  1 211  ? -46.392 48.646  57.122  1.00 36.97 ? 209  LYS A C     1 
ATOM   1350  O O     . LYS A  1 211  ? -47.358 47.871  57.149  1.00 36.44 ? 209  LYS A O     1 
ATOM   1351  C CB    . LYS A  1 211  ? -46.556 50.664  55.630  1.00 32.23 ? 209  LYS A CB    1 
ATOM   1352  N N     . GLU A  1 212  ? -45.132 48.213  57.160  1.00 34.93 ? 210  GLU A N     1 
ATOM   1353  C CA    . GLU A  1 212  ? -44.823 46.791  57.066  1.00 40.75 ? 210  GLU A CA    1 
ATOM   1354  C C     . GLU A  1 212  ? -45.399 46.014  58.246  1.00 39.56 ? 210  GLU A C     1 
ATOM   1355  O O     . GLU A  1 212  ? -46.167 45.064  58.064  1.00 38.51 ? 210  GLU A O     1 
ATOM   1356  C CB    . GLU A  1 212  ? -43.310 46.588  56.981  1.00 41.88 ? 210  GLU A CB    1 
ATOM   1357  C CG    . GLU A  1 212  ? -42.912 45.127  57.048  1.00 44.37 ? 210  GLU A CG    1 
ATOM   1358  C CD    . GLU A  1 212  ? -41.411 44.931  57.111  1.00 51.68 ? 210  GLU A CD    1 
ATOM   1359  O OE1   . GLU A  1 212  ? -40.688 45.938  57.273  1.00 56.05 ? 210  GLU A OE1   1 
ATOM   1360  O OE2   . GLU A  1 212  ? -40.953 43.771  57.002  1.00 57.19 ? 210  GLU A OE2   1 
ATOM   1361  N N     . LEU A  1 213  ? -45.023 46.392  59.471  1.00 40.34 ? 211  LEU A N     1 
ATOM   1362  C CA    . LEU A  1 213  ? -45.512 45.647  60.626  1.00 36.88 ? 211  LEU A CA    1 
ATOM   1363  C C     . LEU A  1 213  ? -46.973 45.946  60.931  1.00 35.34 ? 211  LEU A C     1 
ATOM   1364  O O     . LEU A  1 213  ? -47.637 45.124  61.568  1.00 36.32 ? 211  LEU A O     1 
ATOM   1365  C CB    . LEU A  1 213  ? -44.636 45.924  61.846  1.00 32.88 ? 211  LEU A CB    1 
ATOM   1366  C CG    . LEU A  1 213  ? -43.192 45.425  61.696  1.00 35.70 ? 211  LEU A CG    1 
ATOM   1367  C CD1   . LEU A  1 213  ? -42.377 45.743  62.936  1.00 33.49 ? 211  LEU A CD1   1 
ATOM   1368  C CD2   . LEU A  1 213  ? -43.143 43.935  61.408  1.00 38.22 ? 211  LEU A CD2   1 
ATOM   1369  N N     . GLU A  1 214  ? -47.495 47.089  60.482  1.00 32.86 ? 212  GLU A N     1 
ATOM   1370  C CA    . GLU A  1 214  ? -48.933 47.318  60.591  1.00 34.95 ? 212  GLU A CA    1 
ATOM   1371  C C     . GLU A  1 214  ? -49.708 46.316  59.746  1.00 35.16 ? 212  GLU A C     1 
ATOM   1372  O O     . GLU A  1 214  ? -50.760 45.829  60.162  1.00 32.63 ? 212  GLU A O     1 
ATOM   1373  C CB    . GLU A  1 214  ? -49.279 48.750  60.186  1.00 33.83 ? 212  GLU A CB    1 
ATOM   1374  C CG    . GLU A  1 214  ? -48.914 49.773  61.238  1.00 29.08 ? 212  GLU A CG    1 
ATOM   1375  C CD    . GLU A  1 214  ? -49.395 51.173  60.908  1.00 33.31 ? 212  GLU A CD    1 
ATOM   1376  O OE1   . GLU A  1 214  ? -49.796 51.419  59.749  1.00 33.83 ? 212  GLU A OE1   1 
ATOM   1377  O OE2   . GLU A  1 214  ? -49.379 52.033  61.812  1.00 34.66 ? 212  GLU A OE2   1 
ATOM   1378  N N     . GLU A  1 215  ? -49.194 45.985  58.562  1.00 38.71 ? 213  GLU A N     1 
ATOM   1379  C CA    . GLU A  1 215  ? -49.840 44.975  57.734  1.00 38.77 ? 213  GLU A CA    1 
ATOM   1380  C C     . GLU A  1 215  ? -49.757 43.583  58.357  1.00 41.51 ? 213  GLU A C     1 
ATOM   1381  O O     . GLU A  1 215  ? -50.515 42.694  57.956  1.00 42.72 ? 213  GLU A O     1 
ATOM   1382  C CB    . GLU A  1 215  ? -49.223 44.974  56.331  1.00 40.14 ? 213  GLU A CB    1 
ATOM   1383  N N     . LYS A  1 216  ? -48.864 43.374  59.324  1.00 46.34 ? 214  LYS A N     1 
ATOM   1384  C CA    . LYS A  1 216  ? -48.784 42.115  60.056  1.00 43.77 ? 214  LYS A CA    1 
ATOM   1385  C C     . LYS A  1 216  ? -49.541 42.143  61.381  1.00 45.21 ? 214  LYS A C     1 
ATOM   1386  O O     . LYS A  1 216  ? -49.497 41.156  62.121  1.00 47.96 ? 214  LYS A O     1 
ATOM   1387  C CB    . LYS A  1 216  ? -47.321 41.737  60.308  1.00 40.32 ? 214  LYS A CB    1 
ATOM   1388  N N     . GLY A  1 217  ? -50.222 43.239  61.704  1.00 35.01 ? 215  GLY A N     1 
ATOM   1389  C CA    . GLY A  1 217  ? -51.085 43.291  62.867  1.00 37.12 ? 215  GLY A CA    1 
ATOM   1390  C C     . GLY A  1 217  ? -50.563 44.077  64.055  1.00 36.76 ? 215  GLY A C     1 
ATOM   1391  O O     . GLY A  1 217  ? -51.193 44.046  65.119  1.00 39.07 ? 215  GLY A O     1 
ATOM   1392  N N     . PHE A  1 218  ? -49.441 44.767  63.919  1.00 34.43 ? 216  PHE A N     1 
ATOM   1393  C CA    . PHE A  1 218  ? -48.979 45.669  64.960  1.00 32.69 ? 216  PHE A CA    1 
ATOM   1394  C C     . PHE A  1 218  ? -49.634 47.034  64.799  1.00 29.83 ? 216  PHE A C     1 
ATOM   1395  O O     . PHE A  1 218  ? -50.201 47.361  63.758  1.00 30.87 ? 216  PHE A O     1 
ATOM   1396  C CB    . PHE A  1 218  ? -47.457 45.834  64.912  1.00 29.12 ? 216  PHE A CB    1 
ATOM   1397  C CG    . PHE A  1 218  ? -46.702 44.611  65.323  1.00 33.39 ? 216  PHE A CG    1 
ATOM   1398  C CD1   . PHE A  1 218  ? -46.545 43.552  64.451  1.00 33.50 ? 216  PHE A CD1   1 
ATOM   1399  C CD2   . PHE A  1 218  ? -46.145 44.524  66.582  1.00 28.49 ? 216  PHE A CD2   1 
ATOM   1400  C CE1   . PHE A  1 218  ? -45.848 42.425  64.828  1.00 37.26 ? 216  PHE A CE1   1 
ATOM   1401  C CE2   . PHE A  1 218  ? -45.438 43.400  66.967  1.00 34.66 ? 216  PHE A CE2   1 
ATOM   1402  C CZ    . PHE A  1 218  ? -45.290 42.353  66.096  1.00 35.19 ? 216  PHE A CZ    1 
ATOM   1403  N N     . SER A  1 219  ? -49.542 47.832  65.852  1.00 28.20 ? 217  SER A N     1 
ATOM   1404  C CA    . SER A  1 219  ? -49.860 49.247  65.805  1.00 26.78 ? 217  SER A CA    1 
ATOM   1405  C C     . SER A  1 219  ? -48.659 50.004  66.352  1.00 25.84 ? 217  SER A C     1 
ATOM   1406  O O     . SER A  1 219  ? -47.667 49.406  66.776  1.00 24.72 ? 217  SER A O     1 
ATOM   1407  C CB    . SER A  1 219  ? -51.146 49.567  66.587  1.00 28.84 ? 217  SER A CB    1 
ATOM   1408  O OG    . SER A  1 219  ? -51.020 49.238  67.960  1.00 29.27 ? 217  SER A OG    1 
ATOM   1409  N N     . TYR A  1 220  ? -48.753 51.328  66.345  1.00 23.98 ? 218  TYR A N     1 
ATOM   1410  C CA    . TYR A  1 220  ? -47.623 52.176  66.676  1.00 22.11 ? 218  TYR A CA    1 
ATOM   1411  C C     . TYR A  1 220  ? -48.050 53.298  67.606  1.00 23.61 ? 218  TYR A C     1 
ATOM   1412  O O     . TYR A  1 220  ? -49.190 53.759  67.566  1.00 24.18 ? 218  TYR A O     1 
ATOM   1413  C CB    . TYR A  1 220  ? -47.000 52.772  65.410  1.00 25.42 ? 218  TYR A CB    1 
ATOM   1414  C CG    . TYR A  1 220  ? -46.044 51.827  64.738  1.00 27.30 ? 218  TYR A CG    1 
ATOM   1415  C CD1   . TYR A  1 220  ? -46.486 50.909  63.791  1.00 25.97 ? 218  TYR A CD1   1 
ATOM   1416  C CD2   . TYR A  1 220  ? -44.698 51.830  65.080  1.00 23.69 ? 218  TYR A CD2   1 
ATOM   1417  C CE1   . TYR A  1 220  ? -45.602 50.030  63.188  1.00 27.84 ? 218  TYR A CE1   1 
ATOM   1418  C CE2   . TYR A  1 220  ? -43.808 50.960  64.487  1.00 27.13 ? 218  TYR A CE2   1 
ATOM   1419  C CZ    . TYR A  1 220  ? -44.259 50.069  63.540  1.00 27.68 ? 218  TYR A CZ    1 
ATOM   1420  O OH    . TYR A  1 220  ? -43.361 49.212  62.956  1.00 32.14 ? 218  TYR A OH    1 
ATOM   1421  N N     . SER A  1 221  ? -47.112 53.705  68.462  1.00 23.76 ? 219  SER A N     1 
ATOM   1422  C CA    . SER A  1 221  ? -47.183 54.942  69.229  1.00 24.72 ? 219  SER A CA    1 
ATOM   1423  C C     . SER A  1 221  ? -45.847 55.651  69.060  1.00 26.78 ? 219  SER A C     1 
ATOM   1424  O O     . SER A  1 221  ? -44.802 55.090  69.403  1.00 28.68 ? 219  SER A O     1 
ATOM   1425  C CB    . SER A  1 221  ? -47.462 54.660  70.711  1.00 23.74 ? 219  SER A CB    1 
ATOM   1426  O OG    . SER A  1 221  ? -47.517 55.863  71.464  1.00 29.62 ? 219  SER A OG    1 
ATOM   1427  N N     . TYR A  1 222  ? -45.870 56.875  68.546  1.00 24.69 ? 220  TYR A N     1 
ATOM   1428  C CA    . TYR A  1 222  ? -44.645 57.571  68.174  1.00 25.80 ? 220  TYR A CA    1 
ATOM   1429  C C     . TYR A  1 222  ? -44.195 58.491  69.296  1.00 25.20 ? 220  TYR A C     1 
ATOM   1430  O O     . TYR A  1 222  ? -45.003 59.233  69.858  1.00 22.66 ? 220  TYR A O     1 
ATOM   1431  C CB    . TYR A  1 222  ? -44.850 58.361  66.880  1.00 23.66 ? 220  TYR A CB    1 
ATOM   1432  C CG    . TYR A  1 222  ? -45.189 57.423  65.750  1.00 21.96 ? 220  TYR A CG    1 
ATOM   1433  C CD1   . TYR A  1 222  ? -44.197 56.676  65.129  1.00 22.32 ? 220  TYR A CD1   1 
ATOM   1434  C CD2   . TYR A  1 222  ? -46.506 57.241  65.349  1.00 23.84 ? 220  TYR A CD2   1 
ATOM   1435  C CE1   . TYR A  1 222  ? -44.504 55.787  64.104  1.00 26.06 ? 220  TYR A CE1   1 
ATOM   1436  C CE2   . TYR A  1 222  ? -46.826 56.354  64.340  1.00 22.97 ? 220  TYR A CE2   1 
ATOM   1437  C CZ    . TYR A  1 222  ? -45.824 55.634  63.724  1.00 23.04 ? 220  TYR A CZ    1 
ATOM   1438  O OH    . TYR A  1 222  ? -46.138 54.752  62.724  1.00 24.64 ? 220  TYR A OH    1 
ATOM   1439  N N     . ASP A  1 223  ? -42.902 58.433  69.609  1.00 25.90 ? 221  ASP A N     1 
ATOM   1440  C CA    . ASP A  1 223  ? -42.279 59.240  70.653  1.00 27.69 ? 221  ASP A CA    1 
ATOM   1441  C C     . ASP A  1 223  ? -41.302 60.203  69.987  1.00 31.09 ? 221  ASP A C     1 
ATOM   1442  O O     . ASP A  1 223  ? -40.276 59.777  69.440  1.00 28.97 ? 221  ASP A O     1 
ATOM   1443  C CB    . ASP A  1 223  ? -41.566 58.350  71.663  1.00 31.92 ? 221  ASP A CB    1 
ATOM   1444  C CG    . ASP A  1 223  ? -40.799 59.147  72.722  1.00 38.13 ? 221  ASP A CG    1 
ATOM   1445  O OD1   . ASP A  1 223  ? -40.916 60.394  72.781  1.00 38.75 ? 221  ASP A OD1   1 
ATOM   1446  O OD2   . ASP A  1 223  ? -40.078 58.503  73.509  1.00 40.30 ? 221  ASP A OD2   1 
ATOM   1447  N N     . MET A  1 224  ? -41.617 61.493  70.043  1.00 29.50 ? 222  MET A N     1 
ATOM   1448  C CA    . MET A  1 224  ? -40.807 62.516  69.398  1.00 33.89 ? 222  MET A CA    1 
ATOM   1449  C C     . MET A  1 224  ? -39.600 62.923  70.229  1.00 35.78 ? 222  MET A C     1 
ATOM   1450  O O     . MET A  1 224  ? -38.935 63.909  69.889  1.00 43.32 ? 222  MET A O     1 
ATOM   1451  C CB    . MET A  1 224  ? -41.665 63.739  69.078  1.00 31.79 ? 222  MET A CB    1 
ATOM   1452  C CG    . MET A  1 224  ? -42.845 63.407  68.159  1.00 32.65 ? 222  MET A CG    1 
ATOM   1453  S SD    . MET A  1 224  ? -42.323 62.771  66.554  1.00 37.97 ? 222  MET A SD    1 
ATOM   1454  C CE    . MET A  1 224  ? -41.495 64.222  65.910  1.00 33.12 ? 222  MET A CE    1 
ATOM   1455  N N     . LEU A  1 225  ? -39.336 62.206  71.317  1.00 37.60 ? 223  LEU A N     1 
ATOM   1456  C CA    . LEU A  1 225  ? -38.083 62.226  72.068  1.00 38.04 ? 223  LEU A CA    1 
ATOM   1457  C C     . LEU A  1 225  ? -37.834 63.522  72.832  1.00 38.80 ? 223  LEU A C     1 
ATOM   1458  O O     . LEU A  1 225  ? -36.744 63.699  73.380  1.00 42.58 ? 223  LEU A O     1 
ATOM   1459  C CB    . LEU A  1 225  ? -36.880 61.924  71.159  1.00 38.42 ? 223  LEU A CB    1 
ATOM   1460  C CG    . LEU A  1 225  ? -36.732 60.448  70.746  1.00 38.24 ? 223  LEU A CG    1 
ATOM   1461  C CD1   . LEU A  1 225  ? -35.403 60.162  70.030  1.00 36.16 ? 223  LEU A CD1   1 
ATOM   1462  C CD2   . LEU A  1 225  ? -36.915 59.516  71.948  1.00 35.23 ? 223  LEU A CD2   1 
ATOM   1463  N N     . GLY A  1 226  ? -38.804 64.428  72.906  1.00 39.94 ? 224  GLY A N     1 
ATOM   1464  C CA    . GLY A  1 226  ? -38.640 65.593  73.765  1.00 34.25 ? 224  GLY A CA    1 
ATOM   1465  C C     . GLY A  1 226  ? -38.766 65.215  75.234  1.00 34.84 ? 224  GLY A C     1 
ATOM   1466  O O     . GLY A  1 226  ? -39.579 64.368  75.611  1.00 34.64 ? 224  GLY A O     1 
ATOM   1467  N N     . GLU A  1 227  ? -37.926 65.834  76.070  1.00 34.93 ? 225  GLU A N     1 
ATOM   1468  C CA    . GLU A  1 227  ? -38.115 65.783  77.519  1.00 30.46 ? 225  GLU A CA    1 
ATOM   1469  C C     . GLU A  1 227  ? -37.215 66.805  78.193  1.00 30.48 ? 225  GLU A C     1 
ATOM   1470  O O     . GLU A  1 227  ? -36.203 67.239  77.636  1.00 34.11 ? 225  GLU A O     1 
ATOM   1471  C CB    . GLU A  1 227  ? -37.848 64.393  78.106  1.00 35.12 ? 225  GLU A CB    1 
ATOM   1472  C CG    . GLU A  1 227  ? -36.425 63.892  78.014  1.00 37.25 ? 225  GLU A CG    1 
ATOM   1473  C CD    . GLU A  1 227  ? -36.325 62.438  78.451  1.00 39.94 ? 225  GLU A CD    1 
ATOM   1474  O OE1   . GLU A  1 227  ? -36.366 62.178  79.677  1.00 42.10 ? 225  GLU A OE1   1 
ATOM   1475  O OE2   . GLU A  1 227  ? -36.242 61.557  77.569  1.00 40.57 ? 225  GLU A OE2   1 
ATOM   1476  N N     . ALA A  1 228  ? -37.616 67.183  79.403  1.00 28.75 ? 226  ALA A N     1 
ATOM   1477  C CA    . ALA A  1 228  ? -36.828 68.033  80.286  1.00 28.39 ? 226  ALA A CA    1 
ATOM   1478  C C     . ALA A  1 228  ? -36.434 69.334  79.586  1.00 28.73 ? 226  ALA A C     1 
ATOM   1479  O O     . ALA A  1 228  ? -35.260 69.668  79.443  1.00 28.15 ? 226  ALA A O     1 
ATOM   1480  C CB    . ALA A  1 228  ? -35.593 67.282  80.797  1.00 28.31 ? 226  ALA A CB    1 
ATOM   1481  N N     . ALA A  1 229  ? -37.447 70.065  79.139  1.00 24.87 ? 227  ALA A N     1 
ATOM   1482  C CA    . ALA A  1 229  ? -37.203 71.400  78.613  1.00 24.75 ? 227  ALA A CA    1 
ATOM   1483  C C     . ALA A  1 229  ? -36.542 72.279  79.671  1.00 23.63 ? 227  ALA A C     1 
ATOM   1484  O O     . ALA A  1 229  ? -36.946 72.296  80.840  1.00 23.28 ? 227  ALA A O     1 
ATOM   1485  C CB    . ALA A  1 229  ? -38.506 72.042  78.146  1.00 23.75 ? 227  ALA A CB    1 
ATOM   1486  N N     . THR A  1 230  ? -35.524 73.020  79.238  1.00 23.76 ? 228  THR A N     1 
ATOM   1487  C CA    . THR A  1 230  ? -34.744 73.924  80.077  1.00 28.33 ? 228  THR A CA    1 
ATOM   1488  C C     . THR A  1 230  ? -35.200 75.378  79.975  1.00 24.06 ? 228  THR A C     1 
ATOM   1489  O O     . THR A  1 230  ? -35.068 76.137  80.937  1.00 21.57 ? 228  THR A O     1 
ATOM   1490  C CB    . THR A  1 230  ? -33.259 73.815  79.680  1.00 29.58 ? 228  THR A CB    1 
ATOM   1491  O OG1   . THR A  1 230  ? -32.846 72.442  79.753  1.00 33.28 ? 228  THR A OG1   1 
ATOM   1492  C CG2   . THR A  1 230  ? -32.380 74.645  80.589  1.00 29.58 ? 228  THR A CG2   1 
ATOM   1493  N N     . THR A  1 231  ? -35.737 75.787  78.830  1.00 21.50 ? 229  THR A N     1 
ATOM   1494  C CA    . THR A  1 231  ? -36.114 77.167  78.577  1.00 21.33 ? 229  THR A CA    1 
ATOM   1495  C C     . THR A  1 231  ? -37.534 77.194  78.013  1.00 18.54 ? 229  THR A C     1 
ATOM   1496  O O     . THR A  1 231  ? -38.082 76.172  77.596  1.00 19.67 ? 229  THR A O     1 
ATOM   1497  C CB    . THR A  1 231  ? -35.157 77.835  77.578  1.00 21.14 ? 229  THR A CB    1 
ATOM   1498  O OG1   . THR A  1 231  ? -35.301 77.189  76.312  1.00 23.03 ? 229  THR A OG1   1 
ATOM   1499  C CG2   . THR A  1 231  ? -33.687 77.690  78.028  1.00 20.24 ? 229  THR A CG2   1 
ATOM   1500  N N     . ALA A  1 232  ? -38.127 78.383  78.015  1.00 19.58 ? 230  ALA A N     1 
ATOM   1501  C CA    . ALA A  1 232  ? -39.395 78.570  77.302  1.00 23.18 ? 230  ALA A CA    1 
ATOM   1502  C C     . ALA A  1 232  ? -39.269 78.186  75.829  1.00 25.19 ? 230  ALA A C     1 
ATOM   1503  O O     . ALA A  1 232  ? -40.191 77.592  75.249  1.00 23.58 ? 230  ALA A O     1 
ATOM   1504  C CB    . ALA A  1 232  ? -39.858 80.019  77.444  1.00 23.83 ? 230  ALA A CB    1 
ATOM   1505  N N     . ALA A  1 233  ? -38.135 78.513  75.200  1.00 24.96 ? 231  ALA A N     1 
ATOM   1506  C CA    . ALA A  1 233  ? -37.970 78.204  73.782  1.00 22.98 ? 231  ALA A CA    1 
ATOM   1507  C C     . ALA A  1 233  ? -37.906 76.701  73.547  1.00 25.58 ? 231  ALA A C     1 
ATOM   1508  O O     . ALA A  1 233  ? -38.425 76.201  72.544  1.00 25.96 ? 231  ALA A O     1 
ATOM   1509  C CB    . ALA A  1 233  ? -36.716 78.887  73.226  1.00 23.73 ? 231  ALA A CB    1 
ATOM   1510  N N     . ASP A  1 234  ? -37.271 75.961  74.452  1.00 21.01 ? 232  ASP A N     1 
ATOM   1511  C CA    . ASP A  1 234  ? -37.224 74.513  74.298  1.00 25.97 ? 232  ASP A CA    1 
ATOM   1512  C C     . ASP A  1 234  ? -38.610 73.915  74.422  1.00 21.59 ? 232  ASP A C     1 
ATOM   1513  O O     . ASP A  1 234  ? -38.967 73.007  73.666  1.00 25.19 ? 232  ASP A O     1 
ATOM   1514  C CB    . ASP A  1 234  ? -36.310 73.870  75.344  1.00 25.27 ? 232  ASP A CB    1 
ATOM   1515  C CG    . ASP A  1 234  ? -34.849 74.186  75.132  1.00 32.89 ? 232  ASP A CG    1 
ATOM   1516  O OD1   . ASP A  1 234  ? -34.424 74.339  73.968  1.00 32.03 ? 232  ASP A OD1   1 
ATOM   1517  O OD2   . ASP A  1 234  ? -34.120 74.269  76.154  1.00 37.01 ? 232  ASP A OD2   1 
ATOM   1518  N N     . ALA A  1 235  ? -39.394 74.392  75.388  1.00 20.07 ? 233  ALA A N     1 
ATOM   1519  C CA    . ALA A  1 235  ? -40.736 73.859  75.572  1.00 20.78 ? 233  ALA A CA    1 
ATOM   1520  C C     . ALA A  1 235  ? -41.588 74.145  74.355  1.00 22.91 ? 233  ALA A C     1 
ATOM   1521  O O     . ALA A  1 235  ? -42.362 73.289  73.921  1.00 22.25 ? 233  ALA A O     1 
ATOM   1522  C CB    . ALA A  1 235  ? -41.386 74.452  76.819  1.00 20.41 ? 233  ALA A CB    1 
ATOM   1523  N N     . GLU A  1 236  ? -41.436 75.343  73.780  1.00 21.52 ? 234  GLU A N     1 
ATOM   1524  C CA    . GLU A  1 236  ? -42.191 75.685  72.577  1.00 25.35 ? 234  GLU A CA    1 
ATOM   1525  C C     . GLU A  1 236  ? -41.745 74.839  71.390  1.00 24.75 ? 234  GLU A C     1 
ATOM   1526  O O     . GLU A  1 236  ? -42.575 74.429  70.567  1.00 25.36 ? 234  GLU A O     1 
ATOM   1527  C CB    . GLU A  1 236  ? -42.034 77.177  72.262  1.00 29.72 ? 234  GLU A CB    1 
ATOM   1528  N N     . ARG A  1 237  ? -40.440 74.580  71.273  1.00 21.52 ? 235  ARG A N     1 
ATOM   1529  C CA    . ARG A  1 237  ? -39.952 73.711  70.202  1.00 27.03 ? 235  ARG A CA    1 
ATOM   1530  C C     . ARG A  1 237  ? -40.531 72.304  70.328  1.00 26.41 ? 235  ARG A C     1 
ATOM   1531  O O     . ARG A  1 237  ? -41.017 71.729  69.345  1.00 23.57 ? 235  ARG A O     1 
ATOM   1532  C CB    . ARG A  1 237  ? -38.417 73.681  70.203  1.00 26.83 ? 235  ARG A CB    1 
ATOM   1533  C CG    . ARG A  1 237  ? -37.798 72.694  69.222  1.00 28.56 ? 235  ARG A CG    1 
ATOM   1534  C CD    . ARG A  1 237  ? -36.313 72.982  68.982  1.00 34.85 ? 235  ARG A CD    1 
ATOM   1535  N NE    . ARG A  1 237  ? -35.519 72.896  70.200  1.00 40.48 ? 235  ARG A NE    1 
ATOM   1536  C CZ    . ARG A  1 237  ? -34.933 71.791  70.638  1.00 47.84 ? 235  ARG A CZ    1 
ATOM   1537  N NH1   . ARG A  1 237  ? -35.044 70.644  69.983  1.00 50.64 ? 235  ARG A NH1   1 
ATOM   1538  N NH2   . ARG A  1 237  ? -34.207 71.839  71.755  1.00 43.14 ? 235  ARG A NH2   1 
ATOM   1539  N N     . TYR A  1 238  ? -40.521 71.740  71.535  1.00 23.15 ? 236  TYR A N     1 
ATOM   1540  C CA    . TYR A  1 238  ? -41.133 70.428  71.714  1.00 21.86 ? 236  TYR A CA    1 
ATOM   1541  C C     . TYR A  1 238  ? -42.635 70.471  71.441  1.00 24.12 ? 236  TYR A C     1 
ATOM   1542  O O     . TYR A  1 238  ? -43.191 69.524  70.874  1.00 26.41 ? 236  TYR A O     1 
ATOM   1543  C CB    . TYR A  1 238  ? -40.865 69.898  73.121  1.00 23.32 ? 236  TYR A CB    1 
ATOM   1544  C CG    . TYR A  1 238  ? -39.414 69.584  73.378  1.00 23.10 ? 236  TYR A CG    1 
ATOM   1545  C CD1   . TYR A  1 238  ? -38.631 68.976  72.402  1.00 31.30 ? 236  TYR A CD1   1 
ATOM   1546  C CD2   . TYR A  1 238  ? -38.818 69.912  74.586  1.00 26.53 ? 236  TYR A CD2   1 
ATOM   1547  C CE1   . TYR A  1 238  ? -37.293 68.692  72.631  1.00 34.15 ? 236  TYR A CE1   1 
ATOM   1548  C CE2   . TYR A  1 238  ? -37.483 69.641  74.821  1.00 30.42 ? 236  TYR A CE2   1 
ATOM   1549  C CZ    . TYR A  1 238  ? -36.730 69.028  73.844  1.00 34.89 ? 236  TYR A CZ    1 
ATOM   1550  O OH    . TYR A  1 238  ? -35.407 68.751  74.078  1.00 36.84 ? 236  TYR A OH    1 
ATOM   1551  N N     . TYR A  1 239  ? -43.312 71.552  71.847  1.00 20.42 ? 237  TYR A N     1 
ATOM   1552  C CA    . TYR A  1 239  ? -44.738 71.667  71.559  1.00 21.76 ? 237  TYR A CA    1 
ATOM   1553  C C     . TYR A  1 239  ? -44.981 71.635  70.058  1.00 27.34 ? 237  TYR A C     1 
ATOM   1554  O O     . TYR A  1 239  ? -45.861 70.915  69.573  1.00 21.99 ? 237  TYR A O     1 
ATOM   1555  C CB    . TYR A  1 239  ? -45.344 72.949  72.155  1.00 24.92 ? 237  TYR A CB    1 
ATOM   1556  C CG    . TYR A  1 239  ? -46.833 73.071  71.828  1.00 26.82 ? 237  TYR A CG    1 
ATOM   1557  C CD1   . TYR A  1 239  ? -47.262 73.608  70.611  1.00 27.05 ? 237  TYR A CD1   1 
ATOM   1558  C CD2   . TYR A  1 239  ? -47.798 72.588  72.695  1.00 22.38 ? 237  TYR A CD2   1 
ATOM   1559  C CE1   . TYR A  1 239  ? -48.601 73.686  70.291  1.00 27.05 ? 237  TYR A CE1   1 
ATOM   1560  C CE2   . TYR A  1 239  ? -49.157 72.680  72.388  1.00 25.79 ? 237  TYR A CE2   1 
ATOM   1561  C CZ    . TYR A  1 239  ? -49.546 73.219  71.179  1.00 28.37 ? 237  TYR A CZ    1 
ATOM   1562  O OH    . TYR A  1 239  ? -50.886 73.315  70.841  1.00 30.60 ? 237  TYR A OH    1 
ATOM   1563  N N     . ARG A  1 240  ? -44.233 72.430  69.301  1.00 23.71 ? 238  ARG A N     1 
ATOM   1564  C CA    . ARG A  1 240  ? -44.551 72.465  67.882  1.00 23.22 ? 238  ARG A CA    1 
ATOM   1565  C C     . ARG A  1 240  ? -44.148 71.162  67.199  1.00 25.54 ? 238  ARG A C     1 
ATOM   1566  O O     . ARG A  1 240  ? -44.771 70.779  66.203  1.00 23.93 ? 238  ARG A O     1 
ATOM   1567  C CB    . ARG A  1 240  ? -43.921 73.685  67.211  1.00 28.03 ? 238  ARG A CB    1 
ATOM   1568  C CG    . ARG A  1 240  ? -42.424 73.710  67.155  1.00 25.87 ? 238  ARG A CG    1 
ATOM   1569  C CD    . ARG A  1 240  ? -41.977 74.940  66.367  1.00 25.13 ? 238  ARG A CD    1 
ATOM   1570  N NE    . ARG A  1 240  ? -40.542 75.148  66.475  1.00 28.81 ? 238  ARG A NE    1 
ATOM   1571  C CZ    . ARG A  1 240  ? -39.961 75.983  67.329  1.00 30.48 ? 238  ARG A CZ    1 
ATOM   1572  N NH1   . ARG A  1 240  ? -40.670 76.726  68.168  1.00 26.48 ? 238  ARG A NH1   1 
ATOM   1573  N NH2   . ARG A  1 240  ? -38.635 76.071  67.344  1.00 36.86 ? 238  ARG A NH2   1 
ATOM   1574  N N     . ASP A  1 241  ? -43.157 70.446  67.744  1.00 25.38 ? 239  ASP A N     1 
ATOM   1575  C CA    . ASP A  1 241  ? -42.836 69.106  67.247  1.00 26.29 ? 239  ASP A CA    1 
ATOM   1576  C C     . ASP A  1 241  ? -43.990 68.133  67.490  1.00 24.05 ? 239  ASP A C     1 
ATOM   1577  O O     . ASP A  1 241  ? -44.351 67.348  66.605  1.00 23.18 ? 239  ASP A O     1 
ATOM   1578  C CB    . ASP A  1 241  ? -41.565 68.568  67.911  1.00 27.07 ? 239  ASP A CB    1 
ATOM   1579  C CG    . ASP A  1 241  ? -40.294 69.338  67.533  1.00 37.27 ? 239  ASP A CG    1 
ATOM   1580  O OD1   . ASP A  1 241  ? -40.315 70.177  66.599  1.00 34.83 ? 239  ASP A OD1   1 
ATOM   1581  O OD2   . ASP A  1 241  ? -39.256 69.093  68.205  1.00 41.68 ? 239  ASP A OD2   1 
ATOM   1582  N N     . TYR A  1 242  ? -44.559 68.149  68.702  1.00 20.83 ? 240  TYR A N     1 
ATOM   1583  C CA    . TYR A  1 242  ? -45.719 67.312  69.011  1.00 19.50 ? 240  TYR A CA    1 
ATOM   1584  C C     . TYR A  1 242  ? -46.899 67.636  68.104  1.00 19.10 ? 240  TYR A C     1 
ATOM   1585  O O     . TYR A  1 242  ? -47.562 66.738  67.575  1.00 20.17 ? 240  TYR A O     1 
ATOM   1586  C CB    . TYR A  1 242  ? -46.140 67.511  70.463  1.00 20.94 ? 240  TYR A CB    1 
ATOM   1587  C CG    . TYR A  1 242  ? -45.262 66.838  71.483  1.00 20.15 ? 240  TYR A CG    1 
ATOM   1588  C CD1   . TYR A  1 242  ? -44.571 65.669  71.190  1.00 23.62 ? 240  TYR A CD1   1 
ATOM   1589  C CD2   . TYR A  1 242  ? -45.164 67.353  72.761  1.00 20.78 ? 240  TYR A CD2   1 
ATOM   1590  C CE1   . TYR A  1 242  ? -43.777 65.044  72.163  1.00 27.23 ? 240  TYR A CE1   1 
ATOM   1591  C CE2   . TYR A  1 242  ? -44.373 66.748  73.721  1.00 23.83 ? 240  TYR A CE2   1 
ATOM   1592  C CZ    . TYR A  1 242  ? -43.693 65.596  73.425  1.00 21.74 ? 240  TYR A CZ    1 
ATOM   1593  O OH    . TYR A  1 242  ? -42.927 65.016  74.425  1.00 22.33 ? 240  TYR A OH    1 
ATOM   1594  N N     . GLU A  1 243  ? -47.191 68.928  67.944  1.00 20.67 ? 241  GLU A N     1 
ATOM   1595  C CA    . GLU A  1 243  ? -48.321 69.343  67.121  1.00 20.53 ? 241  GLU A CA    1 
ATOM   1596  C C     . GLU A  1 243  ? -48.158 68.862  65.686  1.00 23.20 ? 241  GLU A C     1 
ATOM   1597  O O     . GLU A  1 243  ? -49.112 68.353  65.081  1.00 19.95 ? 241  GLU A O     1 
ATOM   1598  C CB    . GLU A  1 243  ? -48.447 70.868  67.174  1.00 22.40 ? 241  GLU A CB    1 
ATOM   1599  C CG    . GLU A  1 243  ? -49.600 71.450  66.356  1.00 20.31 ? 241  GLU A CG    1 
ATOM   1600  C CD    . GLU A  1 243  ? -49.567 72.975  66.330  1.00 25.42 ? 241  GLU A CD    1 
ATOM   1601  O OE1   . GLU A  1 243  ? -48.478 73.562  66.510  1.00 28.86 ? 241  GLU A OE1   1 
ATOM   1602  O OE2   . GLU A  1 243  ? -50.632 73.589  66.142  1.00 27.51 ? 241  GLU A OE2   1 
ATOM   1603  N N     . SER A  1 244  ? -46.949 69.011  65.120  1.00 23.19 ? 242  SER A N     1 
ATOM   1604  C CA    . SER A  1 244  ? -46.723 68.578  63.741  1.00 21.32 ? 242  SER A CA    1 
ATOM   1605  C C     . SER A  1 244  ? -46.799 67.059  63.626  1.00 23.27 ? 242  SER A C     1 
ATOM   1606  O O     . SER A  1 244  ? -47.355 66.527  62.656  1.00 21.60 ? 242  SER A O     1 
ATOM   1607  C CB    . SER A  1 244  ? -45.376 69.110  63.225  1.00 23.80 ? 242  SER A CB    1 
ATOM   1608  O OG    . SER A  1 244  ? -44.279 68.619  63.982  1.00 28.95 ? 242  SER A OG    1 
ATOM   1609  N N     . ALA A  1 245  ? -46.270 66.344  64.616  1.00 20.49 ? 243  ALA A N     1 
ATOM   1610  C CA    . ALA A  1 245  ? -46.395 64.891  64.606  1.00 23.40 ? 243  ALA A CA    1 
ATOM   1611  C C     . ALA A  1 245  ? -47.854 64.448  64.704  1.00 19.79 ? 243  ALA A C     1 
ATOM   1612  O O     . ALA A  1 245  ? -48.261 63.497  64.032  1.00 21.81 ? 243  ALA A O     1 
ATOM   1613  C CB    . ALA A  1 245  ? -45.580 64.296  65.749  1.00 20.46 ? 243  ALA A CB    1 
ATOM   1614  N N     . ILE A  1 246  ? -48.663 65.121  65.534  1.00 19.67 ? 244  ILE A N     1 
ATOM   1615  C CA    . ILE A  1 246  ? -50.066 64.719  65.656  1.00 19.75 ? 244  ILE A CA    1 
ATOM   1616  C C     . ILE A  1 246  ? -50.777 64.843  64.312  1.00 22.42 ? 244  ILE A C     1 
ATOM   1617  O O     . ILE A  1 246  ? -51.517 63.940  63.904  1.00 20.21 ? 244  ILE A O     1 
ATOM   1618  C CB    . ILE A  1 246  ? -50.786 65.519  66.755  1.00 19.75 ? 244  ILE A CB    1 
ATOM   1619  C CG1   . ILE A  1 246  ? -50.241 65.135  68.141  1.00 19.74 ? 244  ILE A CG1   1 
ATOM   1620  C CG2   . ILE A  1 246  ? -52.308 65.254  66.690  1.00 22.83 ? 244  ILE A CG2   1 
ATOM   1621  C CD1   . ILE A  1 246  ? -50.963 65.804  69.301  1.00 21.44 ? 244  ILE A CD1   1 
ATOM   1622  N N     . HIS A  1 247  ? -50.522 65.932  63.580  1.00 20.17 ? 245  HIS A N     1 
ATOM   1623  C CA    . HIS A  1 247  ? -51.120 66.072  62.253  1.00 20.91 ? 245  HIS A CA    1 
ATOM   1624  C C     . HIS A  1 247  ? -50.644 64.962  61.324  1.00 21.60 ? 245  HIS A C     1 
ATOM   1625  O O     . HIS A  1 247  ? -51.441 64.370  60.589  1.00 25.17 ? 245  HIS A O     1 
ATOM   1626  C CB    . HIS A  1 247  ? -50.788 67.441  61.655  1.00 20.61 ? 245  HIS A CB    1 
ATOM   1627  C CG    . HIS A  1 247  ? -51.586 68.571  62.232  1.00 22.43 ? 245  HIS A CG    1 
ATOM   1628  N ND1   . HIS A  1 247  ? -52.932 68.727  61.992  1.00 21.49 ? 245  HIS A ND1   1 
ATOM   1629  C CD2   . HIS A  1 247  ? -51.219 69.623  63.007  1.00 20.40 ? 245  HIS A CD2   1 
ATOM   1630  C CE1   . HIS A  1 247  ? -53.363 69.820  62.594  1.00 25.12 ? 245  HIS A CE1   1 
ATOM   1631  N NE2   . HIS A  1 247  ? -52.345 70.378  63.223  1.00 22.13 ? 245  HIS A NE2   1 
ATOM   1632  N N     . ALA A  1 248  ? -49.339 64.681  61.332  1.00 20.60 ? 246  ALA A N     1 
ATOM   1633  C CA    . ALA A  1 248  ? -48.786 63.648  60.461  1.00 23.81 ? 246  ALA A CA    1 
ATOM   1634  C C     . ALA A  1 248  ? -49.359 62.281  60.805  1.00 22.70 ? 246  ALA A C     1 
ATOM   1635  O O     . ALA A  1 248  ? -49.735 61.511  59.916  1.00 23.42 ? 246  ALA A O     1 
ATOM   1636  C CB    . ALA A  1 248  ? -47.258 63.629  60.571  1.00 23.83 ? 246  ALA A CB    1 
ATOM   1637  N N     . ILE A  1 249  ? -49.406 61.954  62.097  1.00 20.53 ? 247  ILE A N     1 
ATOM   1638  C CA    . ILE A  1 249  ? -49.955 60.670  62.530  1.00 20.55 ? 247  ILE A CA    1 
ATOM   1639  C C     . ILE A  1 249  ? -51.448 60.587  62.225  1.00 24.21 ? 247  ILE A C     1 
ATOM   1640  O O     . ILE A  1 249  ? -51.936 59.569  61.723  1.00 24.48 ? 247  ILE A O     1 
ATOM   1641  C CB    . ILE A  1 249  ? -49.660 60.465  64.025  1.00 21.19 ? 247  ILE A CB    1 
ATOM   1642  C CG1   . ILE A  1 249  ? -48.150 60.371  64.223  1.00 22.06 ? 247  ILE A CG1   1 
ATOM   1643  C CG2   . ILE A  1 249  ? -50.389 59.232  64.571  1.00 21.35 ? 247  ILE A CG2   1 
ATOM   1644  C CD1   . ILE A  1 249  ? -47.723 60.599  65.671  1.00 19.77 ? 247  ILE A CD1   1 
ATOM   1645  N N     . GLY A  1 250  ? -52.193 61.656  62.512  1.00 22.33 ? 248  GLY A N     1 
ATOM   1646  C CA    . GLY A  1 250  ? -53.621 61.644  62.233  1.00 22.81 ? 248  GLY A CA    1 
ATOM   1647  C C     . GLY A  1 250  ? -53.945 61.533  60.757  1.00 24.18 ? 248  GLY A C     1 
ATOM   1648  O O     . GLY A  1 250  ? -54.959 60.927  60.389  1.00 22.02 ? 248  GLY A O     1 
ATOM   1649  N N     . LYS A  1 251  ? -53.105 62.124  59.892  1.00 26.55 ? 249  LYS A N     1 
ATOM   1650  C CA    . LYS A  1 251  ? -53.296 61.981  58.445  1.00 23.42 ? 249  LYS A CA    1 
ATOM   1651  C C     . LYS A  1 251  ? -53.045 60.551  57.998  1.00 25.24 ? 249  LYS A C     1 
ATOM   1652  O O     . LYS A  1 251  ? -53.784 60.003  57.166  1.00 26.58 ? 249  LYS A O     1 
ATOM   1653  C CB    . LYS A  1 251  ? -52.352 62.905  57.678  1.00 23.90 ? 249  LYS A CB    1 
ATOM   1654  C CG    . LYS A  1 251  ? -52.672 64.371  57.722  1.00 24.70 ? 249  LYS A CG    1 
ATOM   1655  C CD    . LYS A  1 251  ? -51.669 65.102  56.841  1.00 28.75 ? 249  LYS A CD    1 
ATOM   1656  C CE    . LYS A  1 251  ? -51.348 66.481  57.366  1.00 29.47 ? 249  LYS A CE    1 
ATOM   1657  N NZ    . LYS A  1 251  ? -50.173 67.038  56.615  1.00 31.39 ? 249  LYS A NZ    1 
ATOM   1658  N N     . ALA A  1 252  ? -51.986 59.944  58.530  1.00 24.02 ? 250  ALA A N     1 
ATOM   1659  C CA    . ALA A  1 252  ? -51.676 58.557  58.220  1.00 21.85 ? 250  ALA A CA    1 
ATOM   1660  C C     . ALA A  1 252  ? -52.711 57.614  58.817  1.00 22.89 ? 250  ALA A C     1 
ATOM   1661  O O     . ALA A  1 252  ? -53.052 56.596  58.203  1.00 26.82 ? 250  ALA A O     1 
ATOM   1662  C CB    . ALA A  1 252  ? -50.278 58.214  58.745  1.00 21.78 ? 250  ALA A CB    1 
ATOM   1663  N N     . SER A  1 253  ? -53.206 57.923  60.021  1.00 21.59 ? 251  SER A N     1 
ATOM   1664  C CA    . SER A  1 253  ? -54.206 57.064  60.649  1.00 24.15 ? 251  SER A CA    1 
ATOM   1665  C C     . SER A  1 253  ? -55.415 56.890  59.746  1.00 25.64 ? 251  SER A C     1 
ATOM   1666  O O     . SER A  1 253  ? -55.953 55.785  59.622  1.00 27.57 ? 251  SER A O     1 
ATOM   1667  C CB    . SER A  1 253  ? -54.654 57.639  61.984  1.00 23.43 ? 251  SER A CB    1 
ATOM   1668  O OG    . SER A  1 253  ? -55.639 56.802  62.547  1.00 24.05 ? 251  SER A OG    1 
ATOM   1669  N N     . ALA A  1 254  ? -55.846 57.976  59.109  1.00 23.24 ? 252  ALA A N     1 
ATOM   1670  C CA    . ALA A  1 254  ? -56.922 57.950  58.123  1.00 25.51 ? 252  ALA A CA    1 
ATOM   1671  C C     . ALA A  1 254  ? -58.177 57.276  58.672  1.00 27.27 ? 252  ALA A C     1 
ATOM   1672  O O     . ALA A  1 254  ? -58.813 56.454  58.004  1.00 26.77 ? 252  ALA A O     1 
ATOM   1673  C CB    . ALA A  1 254  ? -56.451 57.282  56.830  1.00 24.12 ? 252  ALA A CB    1 
ATOM   1674  N N     . GLY A  1 255  ? -58.543 57.635  59.902  1.00 24.91 ? 253  GLY A N     1 
ATOM   1675  C CA    . GLY A  1 255  ? -59.783 57.160  60.483  1.00 25.36 ? 253  GLY A CA    1 
ATOM   1676  C C     . GLY A  1 255  ? -59.761 55.750  61.029  1.00 29.50 ? 253  GLY A C     1 
ATOM   1677  O O     . GLY A  1 255  ? -60.827 55.171  61.239  1.00 28.95 ? 253  GLY A O     1 
ATOM   1678  N N     . ARG A  1 256  ? -58.583 55.173  61.281  1.00 27.25 ? 254  ARG A N     1 
ATOM   1679  C CA    . ARG A  1 256  ? -58.542 53.827  61.847  1.00 26.48 ? 254  ARG A CA    1 
ATOM   1680  C C     . ARG A  1 256  ? -58.918 53.796  63.323  1.00 29.04 ? 254  ARG A C     1 
ATOM   1681  O O     . ARG A  1 256  ? -59.175 52.713  63.860  1.00 27.40 ? 254  ARG A O     1 
ATOM   1682  C CB    . ARG A  1 256  ? -57.156 53.207  61.669  1.00 25.02 ? 254  ARG A CB    1 
ATOM   1683  C CG    . ARG A  1 256  ? -56.940 52.553  60.321  1.00 27.93 ? 254  ARG A CG    1 
ATOM   1684  C CD    . ARG A  1 256  ? -55.518 52.059  60.172  1.00 30.13 ? 254  ARG A CD    1 
ATOM   1685  N NE    . ARG A  1 256  ? -54.594 53.148  59.867  1.00 29.61 ? 254  ARG A NE    1 
ATOM   1686  C CZ    . ARG A  1 256  ? -53.274 53.018  59.826  1.00 31.70 ? 254  ARG A CZ    1 
ATOM   1687  N NH1   . ARG A  1 256  ? -52.682 51.885  60.166  1.00 33.90 ? 254  ARG A NH1   1 
ATOM   1688  N NH2   . ARG A  1 256  ? -52.529 54.050  59.433  1.00 30.94 ? 254  ARG A NH2   1 
ATOM   1689  N N     . GLY A  1 257  ? -58.937 54.941  63.998  1.00 23.23 ? 255  GLY A N     1 
ATOM   1690  C CA    . GLY A  1 257  ? -59.346 54.980  65.386  1.00 23.93 ? 255  GLY A CA    1 
ATOM   1691  C C     . GLY A  1 257  ? -58.189 54.695  66.317  1.00 24.61 ? 255  GLY A C     1 
ATOM   1692  O O     . GLY A  1 257  ? -57.060 54.416  65.905  1.00 25.85 ? 255  GLY A O     1 
ATOM   1693  N N     . ILE A  1 258  ? -58.498 54.742  67.615  1.00 24.05 ? 256  ILE A N     1 
ATOM   1694  C CA    . ILE A  1 258  ? -57.450 54.757  68.627  1.00 24.44 ? 256  ILE A CA    1 
ATOM   1695  C C     . ILE A  1 258  ? -56.875 53.379  68.925  1.00 24.47 ? 256  ILE A C     1 
ATOM   1696  O O     . ILE A  1 258  ? -55.800 53.286  69.527  1.00 23.71 ? 256  ILE A O     1 
ATOM   1697  C CB    . ILE A  1 258  ? -57.983 55.376  69.928  1.00 24.06 ? 256  ILE A CB    1 
ATOM   1698  C CG1   . ILE A  1 258  ? -59.086 54.490  70.505  1.00 25.51 ? 256  ILE A CG1   1 
ATOM   1699  C CG2   . ILE A  1 258  ? -58.464 56.833  69.693  1.00 22.90 ? 256  ILE A CG2   1 
ATOM   1700  C CD1   . ILE A  1 258  ? -59.794 55.102  71.679  1.00 28.68 ? 256  ILE A CD1   1 
ATOM   1701  N N     . TYR A  1 259  ? -57.557 52.304  68.544  1.00 26.42 ? 257  TYR A N     1 
ATOM   1702  C CA    . TYR A  1 259  ? -57.080 50.961  68.842  1.00 23.45 ? 257  TYR A CA    1 
ATOM   1703  C C     . TYR A  1 259  ? -56.296 50.370  67.685  1.00 27.04 ? 257  TYR A C     1 
ATOM   1704  O O     . TYR A  1 259  ? -55.186 49.877  67.876  1.00 28.79 ? 257  TYR A O     1 
ATOM   1705  C CB    . TYR A  1 259  ? -58.258 50.048  69.207  1.00 25.79 ? 257  TYR A CB    1 
ATOM   1706  C CG    . TYR A  1 259  ? -59.064 50.569  70.372  1.00 22.65 ? 257  TYR A CG    1 
ATOM   1707  C CD1   . TYR A  1 259  ? -58.449 50.914  71.568  1.00 24.40 ? 257  TYR A CD1   1 
ATOM   1708  C CD2   . TYR A  1 259  ? -60.441 50.764  70.261  1.00 26.18 ? 257  TYR A CD2   1 
ATOM   1709  C CE1   . TYR A  1 259  ? -59.173 51.419  72.625  1.00 23.42 ? 257  TYR A CE1   1 
ATOM   1710  C CE2   . TYR A  1 259  ? -61.179 51.262  71.320  1.00 25.73 ? 257  TYR A CE2   1 
ATOM   1711  C CZ    . TYR A  1 259  ? -60.535 51.583  72.504  1.00 24.67 ? 257  TYR A CZ    1 
ATOM   1712  O OH    . TYR A  1 259  ? -61.256 52.087  73.565  1.00 27.03 ? 257  TYR A OH    1 
ATOM   1713  N N     . GLU A  1 260  ? -56.854 50.421  66.475  1.00 29.45 ? 258  GLU A N     1 
ATOM   1714  C CA    . GLU A  1 260  ? -56.164 49.896  65.309  1.00 32.07 ? 258  GLU A CA    1 
ATOM   1715  C C     . GLU A  1 260  ? -55.204 50.899  64.682  1.00 29.94 ? 258  GLU A C     1 
ATOM   1716  O O     . GLU A  1 260  ? -54.280 50.485  63.976  1.00 38.08 ? 258  GLU A O     1 
ATOM   1717  C CB    . GLU A  1 260  ? -57.184 49.428  64.259  1.00 32.93 ? 258  GLU A CB    1 
ATOM   1718  C CG    . GLU A  1 260  ? -58.397 48.717  64.852  1.00 39.36 ? 258  GLU A CG    1 
ATOM   1719  C CD    . GLU A  1 260  ? -58.643 47.335  64.253  1.00 48.09 ? 258  GLU A CD    1 
ATOM   1720  O OE1   . GLU A  1 260  ? -57.661 46.675  63.843  1.00 49.19 ? 258  GLU A OE1   1 
ATOM   1721  O OE2   . GLU A  1 260  ? -59.821 46.912  64.195  1.00 51.01 ? 258  GLU A OE2   1 
ATOM   1722  N N     . GLY A  1 261  ? -55.389 52.198  64.927  1.00 27.32 ? 259  GLY A N     1 
ATOM   1723  C CA    . GLY A  1 261  ? -54.552 53.209  64.328  1.00 25.68 ? 259  GLY A CA    1 
ATOM   1724  C C     . GLY A  1 261  ? -53.427 53.654  65.247  1.00 26.71 ? 259  GLY A C     1 
ATOM   1725  O O     . GLY A  1 261  ? -53.380 53.309  66.429  1.00 25.96 ? 259  GLY A O     1 
ATOM   1726  N N     . PRO A  1 262  ? -52.496 54.430  64.705  1.00 25.33 ? 260  PRO A N     1 
ATOM   1727  C CA    . PRO A  1 262  ? -51.342 54.871  65.489  1.00 23.86 ? 260  PRO A CA    1 
ATOM   1728  C C     . PRO A  1 262  ? -51.699 56.026  66.408  1.00 21.28 ? 260  PRO A C     1 
ATOM   1729  O O     . PRO A  1 262  ? -52.682 56.738  66.212  1.00 22.84 ? 260  PRO A O     1 
ATOM   1730  C CB    . PRO A  1 262  ? -50.333 55.307  64.419  1.00 24.00 ? 260  PRO A CB    1 
ATOM   1731  C CG    . PRO A  1 262  ? -51.231 55.743  63.251  1.00 23.40 ? 260  PRO A CG    1 
ATOM   1732  C CD    . PRO A  1 262  ? -52.443 54.879  63.303  1.00 28.09 ? 260  PRO A CD    1 
ATOM   1733  N N     . GLY A  1 263  ? -50.882 56.172  67.448  1.00 20.13 ? 261  GLY A N     1 
ATOM   1734  C CA    . GLY A  1 263  ? -50.994 57.283  68.366  1.00 21.74 ? 261  GLY A CA    1 
ATOM   1735  C C     . GLY A  1 263  ? -49.658 57.930  68.671  1.00 21.47 ? 261  GLY A C     1 
ATOM   1736  O O     . GLY A  1 263  ? -48.645 57.638  68.021  1.00 20.45 ? 261  GLY A O     1 
ATOM   1737  N N     . ILE A  1 264  ? -49.659 58.835  69.639  1.00 19.40 ? 262  ILE A N     1 
ATOM   1738  C CA    . ILE A  1 264  ? -48.479 59.596  70.017  1.00 24.44 ? 262  ILE A CA    1 
ATOM   1739  C C     . ILE A  1 264  ? -48.307 59.489  71.523  1.00 21.93 ? 262  ILE A C     1 
ATOM   1740  O O     . ILE A  1 264  ? -49.278 59.302  72.265  1.00 19.71 ? 262  ILE A O     1 
ATOM   1741  C CB    . ILE A  1 264  ? -48.587 61.076  69.577  1.00 20.14 ? 262  ILE A CB    1 
ATOM   1742  C CG1   . ILE A  1 264  ? -47.236 61.789  69.685  1.00 19.48 ? 262  ILE A CG1   1 
ATOM   1743  C CG2   . ILE A  1 264  ? -49.671 61.823  70.392  1.00 19.08 ? 262  ILE A CG2   1 
ATOM   1744  C CD1   . ILE A  1 264  ? -47.221 63.214  69.074  1.00 21.75 ? 262  ILE A CD1   1 
ATOM   1745  N N     . SER A  1 265  ? -47.052 59.577  71.965  1.00 21.22 ? 263  SER A N     1 
ATOM   1746  C CA    . SER A  1 265  ? -46.679 59.622  73.373  1.00 23.46 ? 263  SER A CA    1 
ATOM   1747  C C     . SER A  1 265  ? -45.929 60.918  73.641  1.00 19.72 ? 263  SER A C     1 
ATOM   1748  O O     . SER A  1 265  ? -45.049 61.299  72.867  1.00 22.98 ? 263  SER A O     1 
ATOM   1749  C CB    . SER A  1 265  ? -45.800 58.438  73.753  1.00 22.99 ? 263  SER A CB    1 
ATOM   1750  O OG    . SER A  1 265  ? -46.556 57.239  73.823  1.00 29.70 ? 263  SER A OG    1 
ATOM   1751  N N     . ILE A  1 266  ? -46.282 61.597  74.726  1.00 20.09 ? 264  ILE A N     1 
ATOM   1752  C CA    . ILE A  1 266  ? -45.688 62.886  75.055  1.00 20.06 ? 264  ILE A CA    1 
ATOM   1753  C C     . ILE A  1 266  ? -45.175 62.817  76.486  1.00 22.00 ? 264  ILE A C     1 
ATOM   1754  O O     . ILE A  1 266  ? -45.665 62.035  77.308  1.00 19.96 ? 264  ILE A O     1 
ATOM   1755  C CB    . ILE A  1 266  ? -46.669 64.068  74.897  1.00 20.60 ? 264  ILE A CB    1 
ATOM   1756  C CG1   . ILE A  1 266  ? -47.841 63.931  75.874  1.00 22.36 ? 264  ILE A CG1   1 
ATOM   1757  C CG2   . ILE A  1 266  ? -47.203 64.164  73.452  1.00 22.92 ? 264  ILE A CG2   1 
ATOM   1758  C CD1   . ILE A  1 266  ? -48.654 65.225  76.039  1.00 26.90 ? 264  ILE A CD1   1 
ATOM   1759  N N     . LYS A  1 267  ? -44.179 63.639  76.776  1.00 21.33 ? 265  LYS A N     1 
ATOM   1760  C CA    . LYS A  1 267  ? -43.680 63.805  78.130  1.00 17.93 ? 265  LYS A CA    1 
ATOM   1761  C C     . LYS A  1 267  ? -44.016 65.215  78.593  1.00 19.49 ? 265  LYS A C     1 
ATOM   1762  O O     . LYS A  1 267  ? -43.741 66.184  77.883  1.00 19.24 ? 265  LYS A O     1 
ATOM   1763  C CB    . LYS A  1 267  ? -42.177 63.539  78.197  1.00 24.24 ? 265  LYS A CB    1 
ATOM   1764  C CG    . LYS A  1 267  ? -41.819 62.070  78.021  1.00 27.15 ? 265  LYS A CG    1 
ATOM   1765  C CD    . LYS A  1 267  ? -40.333 61.822  78.252  1.00 30.56 ? 265  LYS A CD    1 
ATOM   1766  C CE    . LYS A  1 267  ? -40.040 60.321  78.242  1.00 34.77 ? 265  LYS A CE    1 
ATOM   1767  N NZ    . LYS A  1 267  ? -40.626 59.673  77.024  1.00 33.64 ? 265  LYS A NZ    1 
ATOM   1768  N N     . LEU A  1 268  ? -44.658 65.325  79.760  1.00 17.68 ? 266  LEU A N     1 
ATOM   1769  C CA    . LEU A  1 268  ? -45.050 66.644  80.243  1.00 17.67 ? 266  LEU A CA    1 
ATOM   1770  C C     . LEU A  1 268  ? -43.843 67.541  80.493  1.00 19.46 ? 266  LEU A C     1 
ATOM   1771  O O     . LEU A  1 268  ? -43.930 68.762  80.307  1.00 18.12 ? 266  LEU A O     1 
ATOM   1772  C CB    . LEU A  1 268  ? -45.888 66.502  81.515  1.00 17.69 ? 266  LEU A CB    1 
ATOM   1773  C CG    . LEU A  1 268  ? -47.208 65.757  81.335  1.00 20.53 ? 266  LEU A CG    1 
ATOM   1774  C CD1   . LEU A  1 268  ? -47.946 65.601  82.652  1.00 21.48 ? 266  LEU A CD1   1 
ATOM   1775  C CD2   . LEU A  1 268  ? -48.059 66.510  80.327  1.00 18.10 ? 266  LEU A CD2   1 
ATOM   1776  N N     . SER A  1 269  ? -42.714 66.959  80.919  1.00 18.76 ? 267  SER A N     1 
ATOM   1777  C CA    . SER A  1 269  ? -41.509 67.745  81.151  1.00 21.71 ? 267  SER A CA    1 
ATOM   1778  C C     . SER A  1 269  ? -40.983 68.394  79.880  1.00 21.23 ? 267  SER A C     1 
ATOM   1779  O O     . SER A  1 269  ? -40.218 69.357  79.967  1.00 21.62 ? 267  SER A O     1 
ATOM   1780  C CB    . SER A  1 269  ? -40.409 66.871  81.779  1.00 20.01 ? 267  SER A CB    1 
ATOM   1781  O OG    . SER A  1 269  ? -39.838 65.993  80.821  1.00 21.42 ? 267  SER A OG    1 
ATOM   1782  N N     . ALA A  1 270  ? -41.381 67.900  78.702  1.00 20.25 ? 268  ALA A N     1 
ATOM   1783  C CA    . ALA A  1 270  ? -40.982 68.547  77.460  1.00 20.72 ? 268  ALA A CA    1 
ATOM   1784  C C     . ALA A  1 270  ? -41.746 69.847  77.222  1.00 20.48 ? 268  ALA A C     1 
ATOM   1785  O O     . ALA A  1 270  ? -41.283 70.687  76.450  1.00 19.68 ? 268  ALA A O     1 
ATOM   1786  C CB    . ALA A  1 270  ? -41.196 67.600  76.268  1.00 19.76 ? 268  ALA A CB    1 
ATOM   1787  N N     . LEU A  1 271  ? -42.900 70.034  77.871  1.00 18.91 ? 269  LEU A N     1 
ATOM   1788  C CA    . LEU A  1 271  ? -43.815 71.105  77.517  1.00 21.05 ? 269  LEU A CA    1 
ATOM   1789  C C     . LEU A  1 271  ? -43.762 72.306  78.454  1.00 20.29 ? 269  LEU A C     1 
ATOM   1790  O O     . LEU A  1 271  ? -44.447 73.298  78.202  1.00 20.49 ? 269  LEU A O     1 
ATOM   1791  C CB    . LEU A  1 271  ? -45.241 70.556  77.449  1.00 18.09 ? 269  LEU A CB    1 
ATOM   1792  C CG    . LEU A  1 271  ? -45.444 69.560  76.307  1.00 24.09 ? 269  LEU A CG    1 
ATOM   1793  C CD1   . LEU A  1 271  ? -46.846 69.030  76.379  1.00 23.06 ? 269  LEU A CD1   1 
ATOM   1794  C CD2   . LEU A  1 271  ? -45.165 70.215  74.942  1.00 23.12 ? 269  LEU A CD2   1 
ATOM   1795  N N     . HIS A  1 272  ? -42.970 72.250  79.524  1.00 17.76 ? 270  HIS A N     1 
ATOM   1796  C CA    . HIS A  1 272  ? -42.838 73.400  80.369  1.00 19.32 ? 270  HIS A CA    1 
ATOM   1797  C C     . HIS A  1 272  ? -41.480 73.292  81.050  1.00 17.89 ? 270  HIS A C     1 
ATOM   1798  O O     . HIS A  1 272  ? -41.118 72.200  81.486  1.00 20.29 ? 270  HIS A O     1 
ATOM   1799  C CB    . HIS A  1 272  ? -43.946 73.466  81.418  1.00 20.50 ? 270  HIS A CB    1 
ATOM   1800  C CG    . HIS A  1 272  ? -44.084 74.818  82.029  1.00 24.45 ? 270  HIS A CG    1 
ATOM   1801  N ND1   . HIS A  1 272  ? -43.190 75.304  82.958  1.00 25.40 ? 270  HIS A ND1   1 
ATOM   1802  C CD2   . HIS A  1 272  ? -44.978 75.811  81.806  1.00 24.96 ? 270  HIS A CD2   1 
ATOM   1803  C CE1   . HIS A  1 272  ? -43.540 76.533  83.298  1.00 25.42 ? 270  HIS A CE1   1 
ATOM   1804  N NE2   . HIS A  1 272  ? -44.620 76.866  82.612  1.00 24.98 ? 270  HIS A NE2   1 
ATOM   1805  N N     . PRO A  1 273  ? -40.711 74.384  81.152  1.00 20.44 ? 271  PRO A N     1 
ATOM   1806  C CA    . PRO A  1 273  ? -39.389 74.277  81.798  1.00 21.24 ? 271  PRO A CA    1 
ATOM   1807  C C     . PRO A  1 273  ? -39.454 74.121  83.306  1.00 27.03 ? 271  PRO A C     1 
ATOM   1808  O O     . PRO A  1 273  ? -38.450 73.726  83.913  1.00 20.34 ? 271  PRO A O     1 
ATOM   1809  C CB    . PRO A  1 273  ? -38.698 75.588  81.406  1.00 25.60 ? 271  PRO A CB    1 
ATOM   1810  C CG    . PRO A  1 273  ? -39.816 76.540  81.226  1.00 20.61 ? 271  PRO A CG    1 
ATOM   1811  C CD    . PRO A  1 273  ? -40.942 75.734  80.610  1.00 22.48 ? 271  PRO A CD    1 
ATOM   1812  N N     . ARG A  1 274  ? -40.590 74.417  83.937  1.00 22.43 ? 272  ARG A N     1 
ATOM   1813  C CA    . ARG A  1 274  ? -40.678 74.278  85.388  1.00 21.69 ? 272  ARG A CA    1 
ATOM   1814  C C     . ARG A  1 274  ? -41.797 73.320  85.764  1.00 23.59 ? 272  ARG A C     1 
ATOM   1815  O O     . ARG A  1 274  ? -42.739 73.691  86.473  1.00 21.71 ? 272  ARG A O     1 
ATOM   1816  C CB    . ARG A  1 274  ? -40.885 75.646  86.038  1.00 21.45 ? 272  ARG A CB    1 
ATOM   1817  C CG    . ARG A  1 274  ? -39.762 76.643  85.721  1.00 23.29 ? 272  ARG A CG    1 
ATOM   1818  C CD    . ARG A  1 274  ? -38.409 76.162  86.245  1.00 21.95 ? 272  ARG A CD    1 
ATOM   1819  N NE    . ARG A  1 274  ? -38.485 75.725  87.634  1.00 23.25 ? 272  ARG A NE    1 
ATOM   1820  C CZ    . ARG A  1 274  ? -38.426 76.543  88.678  1.00 22.90 ? 272  ARG A CZ    1 
ATOM   1821  N NH1   . ARG A  1 274  ? -38.327 77.851  88.525  1.00 23.32 ? 272  ARG A NH1   1 
ATOM   1822  N NH2   . ARG A  1 274  ? -38.473 76.036  89.906  1.00 20.54 ? 272  ARG A NH2   1 
ATOM   1823  N N     . TYR A  1 275  ? -41.707 72.086  85.284  1.00 20.99 ? 273  TYR A N     1 
ATOM   1824  C CA    . TYR A  1 275  ? -42.718 71.078  85.575  1.00 19.50 ? 273  TYR A CA    1 
ATOM   1825  C C     . TYR A  1 275  ? -42.383 70.417  86.910  1.00 22.43 ? 273  TYR A C     1 
ATOM   1826  O O     . TYR A  1 275  ? -41.588 69.477  86.971  1.00 22.56 ? 273  TYR A O     1 
ATOM   1827  C CB    . TYR A  1 275  ? -42.794 70.068  84.432  1.00 21.13 ? 273  TYR A CB    1 
ATOM   1828  C CG    . TYR A  1 275  ? -43.725 68.920  84.728  1.00 19.26 ? 273  TYR A CG    1 
ATOM   1829  C CD1   . TYR A  1 275  ? -45.011 69.149  85.218  1.00 20.66 ? 273  TYR A CD1   1 
ATOM   1830  C CD2   . TYR A  1 275  ? -43.322 67.609  84.523  1.00 20.03 ? 273  TYR A CD2   1 
ATOM   1831  C CE1   . TYR A  1 275  ? -45.869 68.098  85.501  1.00 21.25 ? 273  TYR A CE1   1 
ATOM   1832  C CE2   . TYR A  1 275  ? -44.162 66.548  84.811  1.00 20.48 ? 273  TYR A CE2   1 
ATOM   1833  C CZ    . TYR A  1 275  ? -45.433 66.800  85.292  1.00 22.62 ? 273  TYR A CZ    1 
ATOM   1834  O OH    . TYR A  1 275  ? -46.258 65.747  85.585  1.00 24.83 ? 273  TYR A OH    1 
ATOM   1835  N N     . SER A  1 276  ? -43.009 70.898  87.985  1.00 20.64 ? 274  SER A N     1 
ATOM   1836  C CA    . SER A  1 276  ? -42.725 70.369  89.314  1.00 22.13 ? 274  SER A CA    1 
ATOM   1837  C C     . SER A  1 276  ? -43.826 70.803  90.268  1.00 19.12 ? 274  SER A C     1 
ATOM   1838  O O     . SER A  1 276  ? -44.553 71.766  90.014  1.00 22.29 ? 274  SER A O     1 
ATOM   1839  C CB    . SER A  1 276  ? -41.360 70.838  89.832  1.00 23.43 ? 274  SER A CB    1 
ATOM   1840  O OG    . SER A  1 276  ? -41.440 72.200  90.214  1.00 25.11 ? 274  SER A OG    1 
ATOM   1841  N N     . ARG A  1 277  ? -43.946 70.061  91.371  1.00 19.73 ? 275  ARG A N     1 
ATOM   1842  C CA    . ARG A  1 277  ? -44.940 70.394  92.382  1.00 20.91 ? 275  ARG A CA    1 
ATOM   1843  C C     . ARG A  1 277  ? -44.711 71.790  92.951  1.00 22.96 ? 275  ARG A C     1 
ATOM   1844  O O     . ARG A  1 277  ? -45.672 72.501  93.249  1.00 19.44 ? 275  ARG A O     1 
ATOM   1845  C CB    . ARG A  1 277  ? -44.930 69.356  93.503  1.00 18.00 ? 275  ARG A CB    1 
ATOM   1846  C CG    . ARG A  1 277  ? -45.788 69.725  94.712  1.00 18.21 ? 275  ARG A CG    1 
ATOM   1847  C CD    . ARG A  1 277  ? -47.276 69.869  94.341  1.00 20.92 ? 275  ARG A CD    1 
ATOM   1848  N NE    . ARG A  1 277  ? -48.114 70.187  95.494  1.00 18.59 ? 275  ARG A NE    1 
ATOM   1849  C CZ    . ARG A  1 277  ? -48.320 71.412  95.960  1.00 20.98 ? 275  ARG A CZ    1 
ATOM   1850  N NH1   . ARG A  1 277  ? -47.723 72.463  95.425  1.00 22.31 ? 275  ARG A NH1   1 
ATOM   1851  N NH2   . ARG A  1 277  ? -49.153 71.588  96.984  1.00 21.61 ? 275  ARG A NH2   1 
ATOM   1852  N N     . ALA A  1 278  ? -43.449 72.196  93.129  1.00 20.21 ? 276  ALA A N     1 
ATOM   1853  C CA    . ALA A  1 278  ? -43.191 73.527  93.674  1.00 21.68 ? 276  ALA A CA    1 
ATOM   1854  C C     . ALA A  1 278  ? -43.757 74.617  92.778  1.00 21.23 ? 276  ALA A C     1 
ATOM   1855  O O     . ALA A  1 278  ? -44.068 75.716  93.255  1.00 23.98 ? 276  ALA A O     1 
ATOM   1856  C CB    . ALA A  1 278  ? -41.686 73.750  93.870  1.00 21.64 ? 276  ALA A CB    1 
ATOM   1857  N N     . GLN A  1 279  ? -43.897 74.331  91.486  1.00 22.86 ? 277  GLN A N     1 
ATOM   1858  C CA    . GLN A  1 279  ? -44.406 75.280  90.500  1.00 19.23 ? 277  GLN A CA    1 
ATOM   1859  C C     . GLN A  1 279  ? -45.805 74.895  90.017  1.00 23.93 ? 277  GLN A C     1 
ATOM   1860  O O     . GLN A  1 279  ? -46.162 75.160  88.866  1.00 24.39 ? 277  GLN A O     1 
ATOM   1861  C CB    . GLN A  1 279  ? -43.434 75.379  89.325  1.00 20.11 ? 277  GLN A CB    1 
ATOM   1862  C CG    . GLN A  1 279  ? -42.001 75.752  89.758  1.00 19.38 ? 277  GLN A CG    1 
ATOM   1863  C CD    . GLN A  1 279  ? -41.936 77.188  90.227  1.00 27.34 ? 277  GLN A CD    1 
ATOM   1864  O OE1   . GLN A  1 279  ? -42.507 78.079  89.599  1.00 27.55 ? 277  GLN A OE1   1 
ATOM   1865  N NE2   . GLN A  1 279  ? -41.265 77.419  91.349  1.00 21.95 ? 277  GLN A NE2   1 
ATOM   1866  N N     . ALA A  1 280  ? -46.609 74.290  90.902  1.00 21.89 ? 278  ALA A N     1 
ATOM   1867  C CA    . ALA A  1 280  ? -47.893 73.721  90.495  1.00 22.68 ? 278  ALA A CA    1 
ATOM   1868  C C     . ALA A  1 280  ? -48.794 74.770  89.867  1.00 22.53 ? 278  ALA A C     1 
ATOM   1869  O O     . ALA A  1 280  ? -49.500 74.484  88.892  1.00 21.74 ? 278  ALA A O     1 
ATOM   1870  C CB    . ALA A  1 280  ? -48.591 73.078  91.693  1.00 19.49 ? 278  ALA A CB    1 
ATOM   1871  N N     . ALA A  1 281  ? -48.782 75.994  90.410  1.00 22.50 ? 279  ALA A N     1 
ATOM   1872  C CA    . ALA A  1 281  ? -49.604 77.055  89.844  1.00 22.74 ? 279  ALA A CA    1 
ATOM   1873  C C     . ALA A  1 281  ? -49.250 77.303  88.383  1.00 24.56 ? 279  ALA A C     1 
ATOM   1874  O O     . ALA A  1 281  ? -50.138 77.390  87.522  1.00 24.30 ? 279  ALA A O     1 
ATOM   1875  C CB    . ALA A  1 281  ? -49.456 78.341  90.669  1.00 23.58 ? 279  ALA A CB    1 
ATOM   1876  N N     . ARG A  1 282  ? -47.952 77.410  88.074  1.00 21.80 ? 280  ARG A N     1 
ATOM   1877  C CA    . ARG A  1 282  ? -47.561 77.618  86.679  1.00 25.18 ? 280  ARG A CA    1 
ATOM   1878  C C     . ARG A  1 282  ? -47.872 76.391  85.832  1.00 22.80 ? 280  ARG A C     1 
ATOM   1879  O O     . ARG A  1 282  ? -48.201 76.520  84.644  1.00 22.66 ? 280  ARG A O     1 
ATOM   1880  C CB    . ARG A  1 282  ? -46.070 77.965  86.572  1.00 24.21 ? 280  ARG A CB    1 
ATOM   1881  C CG    . ARG A  1 282  ? -45.676 79.343  87.122  1.00 24.27 ? 280  ARG A CG    1 
ATOM   1882  C CD    . ARG A  1 282  ? -44.229 79.670  86.749  1.00 22.88 ? 280  ARG A CD    1 
ATOM   1883  N NE    . ARG A  1 282  ? -44.097 79.808  85.306  1.00 25.39 ? 280  ARG A NE    1 
ATOM   1884  C CZ    . ARG A  1 282  ? -42.952 79.818  84.636  1.00 28.29 ? 280  ARG A CZ    1 
ATOM   1885  N NH1   . ARG A  1 282  ? -41.779 79.727  85.259  1.00 23.68 ? 280  ARG A NH1   1 
ATOM   1886  N NH2   . ARG A  1 282  ? -42.983 79.914  83.306  1.00 23.61 ? 280  ARG A NH2   1 
ATOM   1887  N N     . VAL A  1 283  ? -47.775 75.202  86.423  1.00 21.49 ? 281  VAL A N     1 
ATOM   1888  C CA    . VAL A  1 283  ? -48.075 73.977  85.686  1.00 18.14 ? 281  VAL A CA    1 
ATOM   1889  C C     . VAL A  1 283  ? -49.547 73.957  85.281  1.00 21.02 ? 281  VAL A C     1 
ATOM   1890  O O     . VAL A  1 283  ? -49.879 73.688  84.123  1.00 21.31 ? 281  VAL A O     1 
ATOM   1891  C CB    . VAL A  1 283  ? -47.690 72.734  86.516  1.00 21.69 ? 281  VAL A CB    1 
ATOM   1892  C CG1   . VAL A  1 283  ? -48.321 71.462  85.910  1.00 22.41 ? 281  VAL A CG1   1 
ATOM   1893  C CG2   . VAL A  1 283  ? -46.161 72.584  86.597  1.00 21.35 ? 281  VAL A CG2   1 
ATOM   1894  N N     . MET A  1 284  ? -50.450 74.284  86.215  1.00 19.19 ? 282  MET A N     1 
ATOM   1895  C CA    . MET A  1 284  ? -51.873 74.288  85.861  1.00 22.28 ? 282  MET A CA    1 
ATOM   1896  C C     . MET A  1 284  ? -52.233 75.461  84.945  1.00 23.41 ? 282  MET A C     1 
ATOM   1897  O O     . MET A  1 284  ? -53.101 75.322  84.068  1.00 22.50 ? 282  MET A O     1 
ATOM   1898  C CB    . MET A  1 284  ? -52.730 74.313  87.129  1.00 21.74 ? 282  MET A CB    1 
ATOM   1899  C CG    . MET A  1 284  ? -52.450 73.159  88.099  1.00 21.10 ? 282  MET A CG    1 
ATOM   1900  S SD    . MET A  1 284  ? -52.618 71.499  87.382  1.00 26.09 ? 282  MET A SD    1 
ATOM   1901  C CE    . MET A  1 284  ? -54.370 71.438  86.997  1.00 22.84 ? 282  MET A CE    1 
ATOM   1902  N N     . GLY A  1 285  ? -51.573 76.609  85.108  1.00 25.37 ? 283  GLY A N     1 
ATOM   1903  C CA    . GLY A  1 285  ? -51.897 77.768  84.292  1.00 22.82 ? 283  GLY A CA    1 
ATOM   1904  C C     . GLY A  1 285  ? -51.257 77.782  82.922  1.00 24.35 ? 283  GLY A C     1 
ATOM   1905  O O     . GLY A  1 285  ? -51.811 78.377  81.992  1.00 24.62 ? 283  GLY A O     1 
ATOM   1906  N N     . GLU A  1 286  ? -50.105 77.133  82.758  1.00 19.71 ? 284  GLU A N     1 
ATOM   1907  C CA    . GLU A  1 286  ? -49.347 77.257  81.514  1.00 21.07 ? 284  GLU A CA    1 
ATOM   1908  C C     . GLU A  1 286  ? -49.132 75.943  80.789  1.00 25.83 ? 284  GLU A C     1 
ATOM   1909  O O     . GLU A  1 286  ? -49.196 75.905  79.558  1.00 28.12 ? 284  GLU A O     1 
ATOM   1910  C CB    . GLU A  1 286  ? -47.977 77.894  81.788  1.00 22.19 ? 284  GLU A CB    1 
ATOM   1911  C CG    . GLU A  1 286  ? -48.066 79.295  82.378  1.00 23.86 ? 284  GLU A CG    1 
ATOM   1912  C CD    . GLU A  1 286  ? -46.734 79.761  82.941  1.00 26.60 ? 284  GLU A CD    1 
ATOM   1913  O OE1   . GLU A  1 286  ? -45.675 79.357  82.407  1.00 26.12 ? 284  GLU A OE1   1 
ATOM   1914  O OE2   . GLU A  1 286  ? -46.757 80.522  83.923  1.00 27.65 ? 284  GLU A OE2   1 
ATOM   1915  N N     . LEU A  1 287  ? -48.831 74.870  81.515  1.00 18.94 ? 285  LEU A N     1 
ATOM   1916  C CA    . LEU A  1 287  ? -48.625 73.578  80.884  1.00 21.65 ? 285  LEU A CA    1 
ATOM   1917  C C     . LEU A  1 287  ? -49.953 72.910  80.534  1.00 19.80 ? 285  LEU A C     1 
ATOM   1918  O O     . LEU A  1 287  ? -50.096 72.359  79.439  1.00 22.26 ? 285  LEU A O     1 
ATOM   1919  C CB    . LEU A  1 287  ? -47.775 72.700  81.805  1.00 20.27 ? 285  LEU A CB    1 
ATOM   1920  C CG    . LEU A  1 287  ? -47.550 71.214  81.525  1.00 22.03 ? 285  LEU A CG    1 
ATOM   1921  C CD1   . LEU A  1 287  ? -47.272 70.970  80.104  1.00 25.74 ? 285  LEU A CD1   1 
ATOM   1922  C CD2   . LEU A  1 287  ? -46.367 70.721  82.355  1.00 21.86 ? 285  LEU A CD2   1 
ATOM   1923  N N     . LEU A  1 288  ? -50.934 72.947  81.444  1.00 21.48 ? 286  LEU A N     1 
ATOM   1924  C CA    . LEU A  1 288  ? -52.217 72.296  81.187  1.00 20.15 ? 286  LEU A CA    1 
ATOM   1925  C C     . LEU A  1 288  ? -52.878 72.768  79.897  1.00 23.76 ? 286  LEU A C     1 
ATOM   1926  O O     . LEU A  1 288  ? -53.253 71.909  79.082  1.00 21.87 ? 286  LEU A O     1 
ATOM   1927  C CB    . LEU A  1 288  ? -53.141 72.483  82.398  1.00 22.13 ? 286  LEU A CB    1 
ATOM   1928  C CG    . LEU A  1 288  ? -54.594 72.034  82.220  1.00 29.75 ? 286  LEU A CG    1 
ATOM   1929  C CD1   . LEU A  1 288  ? -54.687 70.544  81.920  1.00 21.57 ? 286  LEU A CD1   1 
ATOM   1930  C CD2   . LEU A  1 288  ? -55.373 72.394  83.470  1.00 34.27 ? 286  LEU A CD2   1 
ATOM   1931  N N     . PRO A  1 289  ? -53.017 74.073  79.617  1.00 23.85 ? 287  PRO A N     1 
ATOM   1932  C CA    . PRO A  1 289  ? -53.637 74.462  78.339  1.00 19.65 ? 287  PRO A CA    1 
ATOM   1933  C C     . PRO A  1 289  ? -52.898 73.942  77.121  1.00 21.42 ? 287  PRO A C     1 
ATOM   1934  O O     . PRO A  1 289  ? -53.541 73.707  76.084  1.00 19.90 ? 287  PRO A O     1 
ATOM   1935  C CB    . PRO A  1 289  ? -53.633 75.998  78.390  1.00 22.34 ? 287  PRO A CB    1 
ATOM   1936  C CG    . PRO A  1 289  ? -53.499 76.346  79.823  1.00 28.70 ? 287  PRO A CG    1 
ATOM   1937  C CD    . PRO A  1 289  ? -52.645 75.261  80.411  1.00 22.57 ? 287  PRO A CD    1 
ATOM   1938  N N     . ARG A  1 290  ? -51.577 73.749  77.212  1.00 20.06 ? 288  ARG A N     1 
ATOM   1939  C CA    . ARG A  1 290  ? -50.818 73.183  76.096  1.00 20.29 ? 288  ARG A CA    1 
ATOM   1940  C C     . ARG A  1 290  ? -51.164 71.719  75.875  1.00 20.16 ? 288  ARG A C     1 
ATOM   1941  O O     . ARG A  1 290  ? -51.376 71.293  74.737  1.00 22.76 ? 288  ARG A O     1 
ATOM   1942  C CB    . ARG A  1 290  ? -49.314 73.347  76.341  1.00 21.73 ? 288  ARG A CB    1 
ATOM   1943  C CG    . ARG A  1 290  ? -48.894 74.803  76.417  1.00 24.21 ? 288  ARG A CG    1 
ATOM   1944  C CD    . ARG A  1 290  ? -47.401 74.953  76.714  1.00 27.40 ? 288  ARG A CD    1 
ATOM   1945  N NE    . ARG A  1 290  ? -47.053 76.356  76.917  1.00 33.08 ? 288  ARG A NE    1 
ATOM   1946  C CZ    . ARG A  1 290  ? -46.085 76.794  77.717  1.00 35.42 ? 288  ARG A CZ    1 
ATOM   1947  N NH1   . ARG A  1 290  ? -45.334 75.961  78.422  1.00 25.27 ? 288  ARG A NH1   1 
ATOM   1948  N NH2   . ARG A  1 290  ? -45.866 78.104  77.814  1.00 33.02 ? 288  ARG A NH2   1 
ATOM   1949  N N     . VAL A  1 291  ? -51.197 70.916  76.943  1.00 18.49 ? 289  VAL A N     1 
ATOM   1950  C CA    . VAL A  1 291  ? -51.613 69.527  76.768  1.00 18.84 ? 289  VAL A CA    1 
ATOM   1951  C C     . VAL A  1 291  ? -53.039 69.466  76.233  1.00 19.00 ? 289  VAL A C     1 
ATOM   1952  O O     . VAL A  1 291  ? -53.359 68.630  75.378  1.00 20.86 ? 289  VAL A O     1 
ATOM   1953  C CB    . VAL A  1 291  ? -51.475 68.742  78.082  1.00 24.18 ? 289  VAL A CB    1 
ATOM   1954  C CG1   . VAL A  1 291  ? -51.766 67.249  77.834  1.00 20.86 ? 289  VAL A CG1   1 
ATOM   1955  C CG2   . VAL A  1 291  ? -50.077 68.935  78.646  1.00 23.69 ? 289  VAL A CG2   1 
ATOM   1956  N N     . LYS A  1 292  ? -53.917 70.349  76.720  1.00 20.85 ? 290  LYS A N     1 
ATOM   1957  C CA    . LYS A  1 292  ? -55.285 70.377  76.197  1.00 18.98 ? 290  LYS A CA    1 
ATOM   1958  C C     . LYS A  1 292  ? -55.302 70.680  74.704  1.00 20.12 ? 290  LYS A C     1 
ATOM   1959  O O     . LYS A  1 292  ? -56.054 70.048  73.952  1.00 21.54 ? 290  LYS A O     1 
ATOM   1960  C CB    . LYS A  1 292  ? -56.136 71.392  76.957  1.00 19.09 ? 290  LYS A CB    1 
ATOM   1961  C CG    . LYS A  1 292  ? -57.555 71.523  76.382  1.00 20.99 ? 290  LYS A CG    1 
ATOM   1962  C CD    . LYS A  1 292  ? -58.391 72.545  77.126  1.00 20.61 ? 290  LYS A CD    1 
ATOM   1963  C CE    . LYS A  1 292  ? -59.762 72.718  76.427  1.00 20.60 ? 290  LYS A CE    1 
ATOM   1964  N NZ    . LYS A  1 292  ? -60.717 73.412  77.319  1.00 25.04 ? 290  LYS A NZ    1 
ATOM   1965  N N     . ALA A  1 293  ? -54.473 71.622  74.238  1.00 20.57 ? 291  ALA A N     1 
ATOM   1966  C CA    . ALA A  1 293  ? -54.488 71.926  72.802  1.00 19.46 ? 291  ALA A CA    1 
ATOM   1967  C C     . ALA A  1 293  ? -54.016 70.732  71.973  1.00 19.28 ? 291  ALA A C     1 
ATOM   1968  O O     . ALA A  1 293  ? -54.583 70.440  70.910  1.00 20.98 ? 291  ALA A O     1 
ATOM   1969  C CB    . ALA A  1 293  ? -53.646 73.170  72.503  1.00 20.16 ? 291  ALA A CB    1 
ATOM   1970  N N     . LEU A  1 294  ? -53.001 70.011  72.457  1.00 19.04 ? 292  LEU A N     1 
ATOM   1971  C CA    . LEU A  1 294  ? -52.545 68.814  71.756  1.00 19.24 ? 292  LEU A CA    1 
ATOM   1972  C C     . LEU A  1 294  ? -53.609 67.722  71.785  1.00 19.15 ? 292  LEU A C     1 
ATOM   1973  O O     . LEU A  1 294  ? -53.842 67.039  70.778  1.00 19.27 ? 292  LEU A O     1 
ATOM   1974  C CB    . LEU A  1 294  ? -51.241 68.306  72.388  1.00 19.69 ? 292  LEU A CB    1 
ATOM   1975  C CG    . LEU A  1 294  ? -49.999 69.202  72.251  1.00 20.75 ? 292  LEU A CG    1 
ATOM   1976  C CD1   . LEU A  1 294  ? -48.805 68.589  72.986  1.00 20.08 ? 292  LEU A CD1   1 
ATOM   1977  C CD2   . LEU A  1 294  ? -49.663 69.394  70.786  1.00 18.92 ? 292  LEU A CD2   1 
ATOM   1978  N N     . ALA A  1 295  ? -54.258 67.532  72.940  1.00 19.07 ? 293  ALA A N     1 
ATOM   1979  C CA    . ALA A  1 295  ? -55.301 66.518  73.042  1.00 19.92 ? 293  ALA A CA    1 
ATOM   1980  C C     . ALA A  1 295  ? -56.477 66.842  72.126  1.00 19.42 ? 293  ALA A C     1 
ATOM   1981  O O     . ALA A  1 295  ? -57.067 65.937  71.524  1.00 20.74 ? 293  ALA A O     1 
ATOM   1982  C CB    . ALA A  1 295  ? -55.770 66.389  74.494  1.00 19.11 ? 293  ALA A CB    1 
ATOM   1983  N N     . LEU A  1 296  ? -56.822 68.127  71.996  1.00 19.48 ? 294  LEU A N     1 
ATOM   1984  C CA    . LEU A  1 296  ? -57.893 68.520  71.064  1.00 19.73 ? 294  LEU A CA    1 
ATOM   1985  C C     . LEU A  1 296  ? -57.561 68.135  69.626  1.00 21.14 ? 294  LEU A C     1 
ATOM   1986  O O     . LEU A  1 296  ? -58.451 67.721  68.865  1.00 22.62 ? 294  LEU A O     1 
ATOM   1987  C CB    . LEU A  1 296  ? -58.157 70.031  71.150  1.00 19.79 ? 294  LEU A CB    1 
ATOM   1988  C CG    . LEU A  1 296  ? -58.872 70.506  72.414  1.00 22.11 ? 294  LEU A CG    1 
ATOM   1989  C CD1   . LEU A  1 296  ? -58.818 72.035  72.550  1.00 20.15 ? 294  LEU A CD1   1 
ATOM   1990  C CD2   . LEU A  1 296  ? -60.323 69.993  72.459  1.00 24.94 ? 294  LEU A CD2   1 
ATOM   1991  N N     . LEU A  1 297  ? -56.295 68.303  69.217  1.00 19.75 ? 295  LEU A N     1 
ATOM   1992  C CA    . LEU A  1 297  ? -55.890 67.885  67.876  1.00 19.96 ? 295  LEU A CA    1 
ATOM   1993  C C     . LEU A  1 297  ? -55.922 66.365  67.739  1.00 22.13 ? 295  LEU A C     1 
ATOM   1994  O O     . LEU A  1 297  ? -56.406 65.839  66.729  1.00 20.80 ? 295  LEU A O     1 
ATOM   1995  C CB    . LEU A  1 297  ? -54.502 68.449  67.538  1.00 23.19 ? 295  LEU A CB    1 
ATOM   1996  N N     . ALA A  1 298  ? -55.458 65.636  68.765  1.00 19.72 ? 296  ALA A N     1 
ATOM   1997  C CA    . ALA A  1 298  ? -55.591 64.180  68.731  1.00 19.78 ? 296  ALA A CA    1 
ATOM   1998  C C     . ALA A  1 298  ? -57.053 63.758  68.693  1.00 22.75 ? 296  ALA A C     1 
ATOM   1999  O O     . ALA A  1 298  ? -57.403 62.782  68.018  1.00 21.71 ? 296  ALA A O     1 
ATOM   2000  C CB    . ALA A  1 298  ? -54.894 63.540  69.935  1.00 19.56 ? 296  ALA A CB    1 
ATOM   2001  N N     . LYS A  1 299  ? -57.922 64.476  69.418  1.00 19.96 ? 297  LYS A N     1 
ATOM   2002  C CA    . LYS A  1 299  ? -59.352 64.193  69.353  1.00 20.17 ? 297  LYS A CA    1 
ATOM   2003  C C     . LYS A  1 299  ? -59.876 64.338  67.933  1.00 24.53 ? 297  LYS A C     1 
ATOM   2004  O O     . LYS A  1 299  ? -60.629 63.485  67.451  1.00 25.25 ? 297  LYS A O     1 
ATOM   2005  C CB    . LYS A  1 299  ? -60.127 65.113  70.298  1.00 20.80 ? 297  LYS A CB    1 
ATOM   2006  C CG    . LYS A  1 299  ? -61.638 65.086  70.058  1.00 23.30 ? 297  LYS A CG    1 
ATOM   2007  C CD    . LYS A  1 299  ? -62.376 65.987  71.011  1.00 23.93 ? 297  LYS A CD    1 
ATOM   2008  C CE    . LYS A  1 299  ? -63.762 66.336  70.453  1.00 23.07 ? 297  LYS A CE    1 
ATOM   2009  N NZ    . LYS A  1 299  ? -64.516 67.115  71.451  1.00 28.18 ? 297  LYS A NZ    1 
ATOM   2010  N N     . ASN A  1 300  ? -59.466 65.401  67.229  1.00 21.68 ? 298  ASN A N     1 
ATOM   2011  C CA    A ASN A  1 300  ? -60.016 65.672  65.901  0.52 23.38 ? 298  ASN A CA    1 
ATOM   2012  C CA    B ASN A  1 300  ? -60.069 65.630  65.923  0.48 23.32 ? 298  ASN A CA    1 
ATOM   2013  C C     . ASN A  1 300  ? -59.634 64.599  64.889  1.00 23.23 ? 298  ASN A C     1 
ATOM   2014  O O     . ASN A  1 300  ? -60.384 64.342  63.936  1.00 24.15 ? 298  ASN A O     1 
ATOM   2015  C CB    A ASN A  1 300  ? -59.543 67.042  65.414  0.52 24.57 ? 298  ASN A CB    1 
ATOM   2016  C CB    B ASN A  1 300  ? -59.761 67.029  65.407  0.48 24.76 ? 298  ASN A CB    1 
ATOM   2017  C CG    A ASN A  1 300  ? -60.193 68.181  66.169  0.52 24.96 ? 298  ASN A CG    1 
ATOM   2018  C CG    B ASN A  1 300  ? -60.657 67.400  64.248  0.48 27.24 ? 298  ASN A CG    1 
ATOM   2019  O OD1   A ASN A  1 300  ? -61.218 68.002  66.825  0.52 27.46 ? 298  ASN A OD1   1 
ATOM   2020  O OD1   B ASN A  1 300  ? -61.770 67.884  64.449  0.48 31.05 ? 298  ASN A OD1   1 
ATOM   2021  N ND2   A ASN A  1 300  ? -59.609 69.362  66.069  0.52 27.90 ? 298  ASN A ND2   1 
ATOM   2022  N ND2   B ASN A  1 300  ? -60.203 67.128  63.035  0.48 24.02 ? 298  ASN A ND2   1 
ATOM   2023  N N     . TYR A  1 301  ? -58.462 63.993  65.047  1.00 20.70 ? 299  TYR A N     1 
ATOM   2024  C CA    . TYR A  1 301  ? -58.034 62.885  64.192  1.00 24.38 ? 299  TYR A CA    1 
ATOM   2025  C C     . TYR A  1 301  ? -58.381 61.515  64.758  1.00 24.04 ? 299  TYR A C     1 
ATOM   2026  O O     . TYR A  1 301  ? -58.186 60.512  64.058  1.00 24.09 ? 299  TYR A O     1 
ATOM   2027  C CB    . TYR A  1 301  ? -56.523 62.903  63.973  1.00 20.71 ? 299  TYR A CB    1 
ATOM   2028  C CG    . TYR A  1 301  ? -56.021 64.000  63.088  1.00 20.78 ? 299  TYR A CG    1 
ATOM   2029  C CD1   . TYR A  1 301  ? -56.165 63.925  61.708  1.00 21.16 ? 299  TYR A CD1   1 
ATOM   2030  C CD2   . TYR A  1 301  ? -55.392 65.109  63.630  1.00 20.66 ? 299  TYR A CD2   1 
ATOM   2031  C CE1   . TYR A  1 301  ? -55.692 64.924  60.892  1.00 23.13 ? 299  TYR A CE1   1 
ATOM   2032  C CE2   . TYR A  1 301  ? -54.905 66.117  62.818  1.00 25.17 ? 299  TYR A CE2   1 
ATOM   2033  C CZ    . TYR A  1 301  ? -55.074 66.019  61.449  1.00 25.20 ? 299  TYR A CZ    1 
ATOM   2034  O OH    . TYR A  1 301  ? -54.602 67.015  60.632  1.00 24.11 ? 299  TYR A OH    1 
ATOM   2035  N N     . ASP A  1 302  ? -58.836 61.458  66.011  1.00 22.00 ? 300  ASP A N     1 
ATOM   2036  C CA    . ASP A  1 302  ? -59.205 60.220  66.707  1.00 23.49 ? 300  ASP A CA    1 
ATOM   2037  C C     . ASP A  1 302  ? -58.018 59.259  66.789  1.00 22.59 ? 300  ASP A C     1 
ATOM   2038  O O     . ASP A  1 302  ? -58.072 58.105  66.358  1.00 23.20 ? 300  ASP A O     1 
ATOM   2039  C CB    . ASP A  1 302  ? -60.434 59.550  66.060  1.00 25.25 ? 300  ASP A CB    1 
ATOM   2040  C CG    . ASP A  1 302  ? -61.151 58.602  67.022  1.00 27.96 ? 300  ASP A CG    1 
ATOM   2041  O OD1   . ASP A  1 302  ? -61.206 58.925  68.230  1.00 27.33 ? 300  ASP A OD1   1 
ATOM   2042  O OD2   . ASP A  1 302  ? -61.664 57.542  66.574  1.00 27.66 ? 300  ASP A OD2   1 
ATOM   2043  N N     . ILE A  1 303  ? -56.933 59.760  67.381  1.00 20.81 ? 301  ILE A N     1 
ATOM   2044  C CA    . ILE A  1 303  ? -55.737 58.969  67.617  1.00 20.29 ? 301  ILE A CA    1 
ATOM   2045  C C     . ILE A  1 303  ? -55.482 58.965  69.115  1.00 20.05 ? 301  ILE A C     1 
ATOM   2046  O O     . ILE A  1 303  ? -56.026 59.773  69.864  1.00 19.94 ? 301  ILE A O     1 
ATOM   2047  C CB    . ILE A  1 303  ? -54.501 59.499  66.848  1.00 21.24 ? 301  ILE A CB    1 
ATOM   2048  C CG1   . ILE A  1 303  ? -54.060 60.869  67.397  1.00 19.98 ? 301  ILE A CG1   1 
ATOM   2049  C CG2   . ILE A  1 303  ? -54.807 59.601  65.347  1.00 21.59 ? 301  ILE A CG2   1 
ATOM   2050  C CD1   . ILE A  1 303  ? -52.621 61.255  67.035  1.00 21.55 ? 301  ILE A CD1   1 
ATOM   2051  N N     . GLY A  1 304  ? -54.656 58.030  69.549  1.00 24.18 ? 302  GLY A N     1 
ATOM   2052  C CA    . GLY A  1 304  ? -54.266 58.003  70.941  1.00 24.02 ? 302  GLY A CA    1 
ATOM   2053  C C     . GLY A  1 304  ? -53.262 59.094  71.266  1.00 20.85 ? 302  GLY A C     1 
ATOM   2054  O O     . GLY A  1 304  ? -52.416 59.470  70.450  1.00 19.49 ? 302  GLY A O     1 
ATOM   2055  N N     . LEU A  1 305  ? -53.365 59.610  72.489  1.00 21.42 ? 303  LEU A N     1 
ATOM   2056  C CA    . LEU A  1 305  ? -52.401 60.565  73.027  1.00 19.54 ? 303  LEU A CA    1 
ATOM   2057  C C     . LEU A  1 305  ? -52.077 60.084  74.426  1.00 18.98 ? 303  LEU A C     1 
ATOM   2058  O O     . LEU A  1 305  ? -52.933 60.134  75.316  1.00 19.00 ? 303  LEU A O     1 
ATOM   2059  C CB    . LEU A  1 305  ? -52.932 62.003  73.050  1.00 20.26 ? 303  LEU A CB    1 
ATOM   2060  C CG    . LEU A  1 305  ? -51.907 63.038  73.534  1.00 23.67 ? 303  LEU A CG    1 
ATOM   2061  C CD1   . LEU A  1 305  ? -52.019 64.362  72.793  1.00 23.31 ? 303  LEU A CD1   1 
ATOM   2062  C CD2   . LEU A  1 305  ? -52.055 63.278  75.046  1.00 25.05 ? 303  LEU A CD2   1 
ATOM   2063  N N     . ASN A  1 306  ? -50.848 59.636  74.615  1.00 18.89 ? 304  ASN A N     1 
ATOM   2064  C CA    . ASN A  1 306  ? -50.425 59.008  75.850  1.00 19.89 ? 304  ASN A CA    1 
ATOM   2065  C C     . ASN A  1 306  ? -49.482 59.949  76.591  1.00 18.55 ? 304  ASN A C     1 
ATOM   2066  O O     . ASN A  1 306  ? -48.557 60.502  75.989  1.00 22.63 ? 304  ASN A O     1 
ATOM   2067  C CB    . ASN A  1 306  ? -49.739 57.676  75.563  1.00 19.10 ? 304  ASN A CB    1 
ATOM   2068  C CG    . ASN A  1 306  ? -49.071 57.116  76.784  1.00 20.77 ? 304  ASN A CG    1 
ATOM   2069  O OD1   . ASN A  1 306  ? -47.869 57.317  76.987  1.00 24.22 ? 304  ASN A OD1   1 
ATOM   2070  N ND2   . ASN A  1 306  ? -49.848 56.465  77.636  1.00 18.89 ? 304  ASN A ND2   1 
ATOM   2071  N N     . ILE A  1 307  ? -49.740 60.133  77.883  1.00 18.51 ? 305  ILE A N     1 
ATOM   2072  C CA    . ILE A  1 307  ? -48.874 60.900  78.774  1.00 18.90 ? 305  ILE A CA    1 
ATOM   2073  C C     . ILE A  1 307  ? -47.895 59.935  79.429  1.00 21.52 ? 305  ILE A C     1 
ATOM   2074  O O     . ILE A  1 307  ? -48.290 59.124  80.270  1.00 19.62 ? 305  ILE A O     1 
ATOM   2075  C CB    . ILE A  1 307  ? -49.686 61.650  79.838  1.00 19.75 ? 305  ILE A CB    1 
ATOM   2076  C CG1   . ILE A  1 307  ? -50.680 62.618  79.173  1.00 23.52 ? 305  ILE A CG1   1 
ATOM   2077  C CG2   . ILE A  1 307  ? -48.757 62.364  80.828  1.00 22.29 ? 305  ILE A CG2   1 
ATOM   2078  C CD1   . ILE A  1 307  ? -51.622 63.264  80.150  1.00 26.70 ? 305  ILE A CD1   1 
ATOM   2079  N N     . ASP A  1 308  ? -46.612 60.048  79.068  1.00 20.94 ? 306  ASP A N     1 
ATOM   2080  C CA    . ASP A  1 308  ? -45.576 59.183  79.623  1.00 19.90 ? 306  ASP A CA    1 
ATOM   2081  C C     . ASP A  1 308  ? -45.325 59.527  81.079  1.00 22.09 ? 306  ASP A C     1 
ATOM   2082  O O     . ASP A  1 308  ? -45.534 60.662  81.518  1.00 20.41 ? 306  ASP A O     1 
ATOM   2083  C CB    . ASP A  1 308  ? -44.259 59.329  78.852  1.00 23.07 ? 306  ASP A CB    1 
ATOM   2084  C CG    . ASP A  1 308  ? -44.266 58.622  77.506  1.00 30.94 ? 306  ASP A CG    1 
ATOM   2085  O OD1   . ASP A  1 308  ? -45.195 57.833  77.226  1.00 31.98 ? 306  ASP A OD1   1 
ATOM   2086  O OD2   . ASP A  1 308  ? -43.324 58.858  76.719  1.00 34.59 ? 306  ASP A OD2   1 
ATOM   2087  N N     . ALA A  1 309  ? -44.844 58.533  81.825  1.00 19.23 ? 307  ALA A N     1 
ATOM   2088  C CA    . ALA A  1 309  ? -44.566 58.688  83.244  1.00 23.08 ? 307  ALA A CA    1 
ATOM   2089  C C     . ALA A  1 309  ? -43.081 58.943  83.457  1.00 22.38 ? 307  ALA A C     1 
ATOM   2090  O O     . ALA A  1 309  ? -42.228 58.347  82.786  1.00 19.98 ? 307  ALA A O     1 
ATOM   2091  C CB    . ALA A  1 309  ? -45.018 57.456  84.031  1.00 19.84 ? 307  ALA A CB    1 
ATOM   2092  N N     . GLU A  1 310  ? -42.781 59.835  84.403  1.00 22.01 ? 308  GLU A N     1 
ATOM   2093  C CA    . GLU A  1 310  ? -41.410 60.275  84.599  1.00 22.33 ? 308  GLU A CA    1 
ATOM   2094  C C     . GLU A  1 310  ? -40.996 60.038  86.046  1.00 19.93 ? 308  GLU A C     1 
ATOM   2095  O O     . GLU A  1 310  ? -41.240 58.954  86.595  1.00 20.35 ? 308  GLU A O     1 
ATOM   2096  C CB    . GLU A  1 310  ? -41.268 61.748  84.163  1.00 20.39 ? 308  GLU A CB    1 
ATOM   2097  C CG    . GLU A  1 310  ? -41.613 61.911  82.662  1.00 24.39 ? 308  GLU A CG    1 
ATOM   2098  C CD    . GLU A  1 310  ? -41.384 63.312  82.090  1.00 24.15 ? 308  GLU A CD    1 
ATOM   2099  O OE1   . GLU A  1 310  ? -40.214 63.677  81.862  1.00 24.06 ? 308  GLU A OE1   1 
ATOM   2100  O OE2   . GLU A  1 310  ? -42.381 64.025  81.838  1.00 23.47 ? 308  GLU A OE2   1 
ATOM   2101  N N     . GLU A  1 311  ? -40.345 61.014  86.668  1.00 19.06 ? 309  GLU A N     1 
ATOM   2102  C CA    . GLU A  1 311  ? -39.805 60.773  87.997  1.00 19.17 ? 309  GLU A CA    1 
ATOM   2103  C C     . GLU A  1 311  ? -40.929 60.668  89.025  1.00 17.59 ? 309  GLU A C     1 
ATOM   2104  O O     . GLU A  1 311  ? -42.032 61.176  88.835  1.00 18.24 ? 309  GLU A O     1 
ATOM   2105  C CB    . GLU A  1 311  ? -38.821 61.884  88.382  1.00 20.61 ? 309  GLU A CB    1 
ATOM   2106  C CG    . GLU A  1 311  ? -37.553 61.946  87.477  1.00 24.74 ? 309  GLU A CG    1 
ATOM   2107  C CD    . GLU A  1 311  ? -37.708 62.854  86.265  1.00 28.56 ? 309  GLU A CD    1 
ATOM   2108  O OE1   . GLU A  1 311  ? -38.847 63.250  85.936  1.00 25.16 ? 309  GLU A OE1   1 
ATOM   2109  O OE2   . GLU A  1 311  ? -36.680 63.173  85.626  1.00 31.33 ? 309  GLU A OE2   1 
ATOM   2110  N N     . ALA A  1 312  ? -40.617 60.025  90.159  1.00 18.73 ? 310  ALA A N     1 
ATOM   2111  C CA    . ALA A  1 312  ? -41.636 59.768  91.171  1.00 18.22 ? 310  ALA A CA    1 
ATOM   2112  C C     . ALA A  1 312  ? -42.251 61.052  91.715  1.00 17.81 ? 310  ALA A C     1 
ATOM   2113  O O     . ALA A  1 312  ? -43.418 61.044  92.116  1.00 20.70 ? 310  ALA A O     1 
ATOM   2114  C CB    . ALA A  1 312  ? -41.047 58.947  92.335  1.00 17.94 ? 310  ALA A CB    1 
ATOM   2115  N N     . ASP A  1 313  ? -41.487 62.155  91.773  1.00 19.05 ? 311  ASP A N     1 
ATOM   2116  C CA    . ASP A  1 313  ? -42.026 63.374  92.376  1.00 18.80 ? 311  ASP A CA    1 
ATOM   2117  C C     . ASP A  1 313  ? -42.916 64.151  91.418  1.00 18.86 ? 311  ASP A C     1 
ATOM   2118  O O     . ASP A  1 313  ? -43.393 65.234  91.775  1.00 19.81 ? 311  ASP A O     1 
ATOM   2119  C CB    . ASP A  1 313  ? -40.898 64.281  92.920  1.00 21.21 ? 311  ASP A CB    1 
ATOM   2120  C CG    . ASP A  1 313  ? -39.928 64.773  91.842  1.00 26.13 ? 311  ASP A CG    1 
ATOM   2121  O OD1   . ASP A  1 313  ? -40.104 64.480  90.644  1.00 21.45 ? 311  ASP A OD1   1 
ATOM   2122  O OD2   . ASP A  1 313  ? -38.960 65.476  92.206  1.00 25.47 ? 311  ASP A OD2   1 
ATOM   2123  N N     . ARG A  1 314  ? -43.131 63.619  90.220  1.00 18.18 ? 312  ARG A N     1 
ATOM   2124  C CA    . ARG A  1 314  ? -44.060 64.180  89.249  1.00 19.04 ? 312  ARG A CA    1 
ATOM   2125  C C     . ARG A  1 314  ? -45.316 63.341  89.080  1.00 17.80 ? 312  ARG A C     1 
ATOM   2126  O O     . ARG A  1 314  ? -46.240 63.781  88.382  1.00 20.52 ? 312  ARG A O     1 
ATOM   2127  C CB    . ARG A  1 314  ? -43.371 64.344  87.883  1.00 19.81 ? 312  ARG A CB    1 
ATOM   2128  C CG    . ARG A  1 314  ? -42.384 65.517  87.827  1.00 21.14 ? 312  ARG A CG    1 
ATOM   2129  C CD    . ARG A  1 314  ? -41.384 65.391  86.681  1.00 20.63 ? 312  ARG A CD    1 
ATOM   2130  N NE    . ARG A  1 314  ? -40.821 66.701  86.361  1.00 21.87 ? 312  ARG A NE    1 
ATOM   2131  C CZ    . ARG A  1 314  ? -39.792 66.908  85.549  1.00 22.98 ? 312  ARG A CZ    1 
ATOM   2132  N NH1   . ARG A  1 314  ? -39.126 65.898  85.002  1.00 23.23 ? 312  ARG A NH1   1 
ATOM   2133  N NH2   . ARG A  1 314  ? -39.426 68.161  85.270  1.00 21.61 ? 312  ARG A NH2   1 
ATOM   2134  N N     . LEU A  1 315  ? -45.377 62.151  89.685  1.00 18.59 ? 313  LEU A N     1 
ATOM   2135  C CA    . LEU A  1 315  ? -46.540 61.280  89.520  1.00 18.07 ? 313  LEU A CA    1 
ATOM   2136  C C     . LEU A  1 315  ? -47.835 61.998  89.904  1.00 22.62 ? 313  LEU A C     1 
ATOM   2137  O O     . LEU A  1 315  ? -48.752 62.151  89.081  1.00 20.07 ? 313  LEU A O     1 
ATOM   2138  C CB    . LEU A  1 315  ? -46.353 60.002  90.349  1.00 18.42 ? 313  LEU A CB    1 
ATOM   2139  C CG    . LEU A  1 315  ? -47.128 58.764  89.867  1.00 19.51 ? 313  LEU A CG    1 
ATOM   2140  C CD1   . LEU A  1 315  ? -46.734 57.504  90.668  1.00 20.75 ? 313  LEU A CD1   1 
ATOM   2141  C CD2   . LEU A  1 315  ? -48.688 58.935  89.856  1.00 24.36 ? 313  LEU A CD2   1 
ATOM   2142  N N     . GLU A  1 316  ? -47.924 62.453  91.157  1.00 21.16 ? 314  GLU A N     1 
ATOM   2143  C CA    . GLU A  1 316  ? -49.209 62.914  91.661  1.00 23.71 ? 314  GLU A CA    1 
ATOM   2144  C C     . GLU A  1 316  ? -49.597 64.250  91.045  1.00 23.74 ? 314  GLU A C     1 
ATOM   2145  O O     . GLU A  1 316  ? -50.786 64.507  90.838  1.00 23.51 ? 314  GLU A O     1 
ATOM   2146  C CB    . GLU A  1 316  ? -49.180 62.979  93.186  1.00 22.28 ? 314  GLU A CB    1 
ATOM   2147  C CG    . GLU A  1 316  ? -49.020 61.599  93.783  1.00 22.00 ? 314  GLU A CG    1 
ATOM   2148  C CD    . GLU A  1 316  ? -49.116 61.564  95.290  1.00 25.58 ? 314  GLU A CD    1 
ATOM   2149  O OE1   . GLU A  1 316  ? -49.857 62.381  95.886  1.00 25.89 ? 314  GLU A OE1   1 
ATOM   2150  O OE2   . GLU A  1 316  ? -48.446 60.691  95.878  1.00 24.04 ? 314  GLU A OE2   1 
ATOM   2151  N N     . LEU A  1 317  ? -48.613 65.088  90.707  1.00 20.70 ? 315  LEU A N     1 
ATOM   2152  C CA    . LEU A  1 317  ? -48.897 66.292  89.922  1.00 22.63 ? 315  LEU A CA    1 
ATOM   2153  C C     . LEU A  1 317  ? -49.482 65.948  88.550  1.00 18.16 ? 315  LEU A C     1 
ATOM   2154  O O     . LEU A  1 317  ? -50.421 66.608  88.085  1.00 19.60 ? 315  LEU A O     1 
ATOM   2155  C CB    . LEU A  1 317  ? -47.625 67.125  89.764  1.00 21.48 ? 315  LEU A CB    1 
ATOM   2156  C CG    . LEU A  1 317  ? -47.707 68.383  88.898  1.00 22.24 ? 315  LEU A CG    1 
ATOM   2157  C CD1   . LEU A  1 317  ? -48.719 69.387  89.470  1.00 19.72 ? 315  LEU A CD1   1 
ATOM   2158  C CD2   . LEU A  1 317  ? -46.334 69.009  88.796  1.00 24.50 ? 315  LEU A CD2   1 
ATOM   2159  N N     . SER A  1 318  ? -48.928 64.940  87.870  1.00 20.26 ? 316  SER A N     1 
ATOM   2160  C CA    . SER A  1 318  ? -49.491 64.555  86.576  1.00 19.77 ? 316  SER A CA    1 
ATOM   2161  C C     . SER A  1 318  ? -50.934 64.071  86.709  1.00 21.40 ? 316  SER A C     1 
ATOM   2162  O O     . SER A  1 318  ? -51.700 64.124  85.738  1.00 19.25 ? 316  SER A O     1 
ATOM   2163  C CB    . SER A  1 318  ? -48.626 63.472  85.911  1.00 20.40 ? 316  SER A CB    1 
ATOM   2164  O OG    . SER A  1 318  ? -48.801 62.212  86.551  1.00 21.04 ? 316  SER A OG    1 
ATOM   2165  N N     . LEU A  1 319  ? -51.322 63.572  87.881  1.00 18.51 ? 317  LEU A N     1 
ATOM   2166  C CA    . LEU A  1 319  ? -52.708 63.161  88.083  1.00 20.53 ? 317  LEU A CA    1 
ATOM   2167  C C     . LEU A  1 319  ? -53.650 64.359  88.089  1.00 20.78 ? 317  LEU A C     1 
ATOM   2168  O O     . LEU A  1 319  ? -54.782 64.268  87.601  1.00 23.32 ? 317  LEU A O     1 
ATOM   2169  C CB    . LEU A  1 319  ? -52.847 62.376  89.391  1.00 21.36 ? 317  LEU A CB    1 
ATOM   2170  C CG    . LEU A  1 319  ? -52.143 61.015  89.411  1.00 23.09 ? 317  LEU A CG    1 
ATOM   2171  C CD1   . LEU A  1 319  ? -52.265 60.395  90.788  1.00 19.69 ? 317  LEU A CD1   1 
ATOM   2172  C CD2   . LEU A  1 319  ? -52.713 60.091  88.318  1.00 19.30 ? 317  LEU A CD2   1 
ATOM   2173  N N     . ASP A  1 320  ? -53.204 65.494  88.626  1.00 22.64 ? 318  ASP A N     1 
ATOM   2174  C CA    . ASP A  1 320  ? -54.060 66.671  88.606  1.00 23.71 ? 318  ASP A CA    1 
ATOM   2175  C C     . ASP A  1 320  ? -54.326 67.123  87.180  1.00 22.22 ? 318  ASP A C     1 
ATOM   2176  O O     . ASP A  1 320  ? -55.427 67.586  86.872  1.00 23.46 ? 318  ASP A O     1 
ATOM   2177  C CB    . ASP A  1 320  ? -53.445 67.798  89.433  1.00 22.87 ? 318  ASP A CB    1 
ATOM   2178  C CG    . ASP A  1 320  ? -53.618 67.576  90.914  1.00 29.33 ? 318  ASP A CG    1 
ATOM   2179  O OD1   . ASP A  1 320  ? -54.776 67.393  91.343  1.00 28.96 ? 318  ASP A OD1   1 
ATOM   2180  O OD2   . ASP A  1 320  ? -52.600 67.553  91.654  1.00 28.28 ? 318  ASP A OD2   1 
ATOM   2181  N N     . LEU A  1 321  ? -53.329 67.013  86.299  1.00 21.13 ? 319  LEU A N     1 
ATOM   2182  C CA    . LEU A  1 321  ? -53.572 67.342  84.900  1.00 20.55 ? 319  LEU A CA    1 
ATOM   2183  C C     . LEU A  1 321  ? -54.491 66.319  84.251  1.00 20.54 ? 319  LEU A C     1 
ATOM   2184  O O     . LEU A  1 321  ? -55.382 66.688  83.476  1.00 22.33 ? 319  LEU A O     1 
ATOM   2185  C CB    . LEU A  1 321  ? -52.257 67.440  84.118  1.00 24.62 ? 319  LEU A CB    1 
ATOM   2186  C CG    . LEU A  1 321  ? -51.366 68.658  84.383  1.00 25.34 ? 319  LEU A CG    1 
ATOM   2187  C CD1   . LEU A  1 321  ? -50.263 68.287  85.351  1.00 27.59 ? 319  LEU A CD1   1 
ATOM   2188  C CD2   . LEU A  1 321  ? -50.800 69.174  83.081  1.00 25.99 ? 319  LEU A CD2   1 
ATOM   2189  N N     . LEU A  1 322  ? -54.285 65.034  84.541  1.00 20.00 ? 320  LEU A N     1 
ATOM   2190  C CA    . LEU A  1 322  ? -55.142 64.005  83.956  1.00 19.96 ? 320  LEU A CA    1 
ATOM   2191  C C     . LEU A  1 322  ? -56.596 64.229  84.353  1.00 19.01 ? 320  LEU A C     1 
ATOM   2192  O O     . LEU A  1 322  ? -57.502 64.092  83.525  1.00 20.44 ? 320  LEU A O     1 
ATOM   2193  C CB    . LEU A  1 322  ? -54.680 62.612  84.394  1.00 19.83 ? 320  LEU A CB    1 
ATOM   2194  C CG    . LEU A  1 322  ? -55.491 61.446  83.825  1.00 25.14 ? 320  LEU A CG    1 
ATOM   2195  C CD1   . LEU A  1 322  ? -55.249 61.336  82.310  1.00 20.40 ? 320  LEU A CD1   1 
ATOM   2196  C CD2   . LEU A  1 322  ? -55.140 60.142  84.533  1.00 20.49 ? 320  LEU A CD2   1 
ATOM   2197  N N     . GLU A  1 323  ? -56.825 64.612  85.609  1.00 20.37 ? 321  GLU A N     1 
ATOM   2198  C CA    . GLU A  1 323  ? -58.183 64.821  86.102  1.00 24.44 ? 321  GLU A CA    1 
ATOM   2199  C C     . GLU A  1 323  ? -58.857 65.988  85.386  1.00 24.65 ? 321  GLU A C     1 
ATOM   2200  O O     . GLU A  1 323  ? -60.005 65.875  84.948  1.00 23.67 ? 321  GLU A O     1 
ATOM   2201  C CB    . GLU A  1 323  ? -58.159 65.048  87.614  1.00 25.98 ? 321  GLU A CB    1 
ATOM   2202  C CG    . GLU A  1 323  ? -59.427 65.683  88.147  1.00 29.37 ? 321  GLU A CG    1 
ATOM   2203  C CD    . GLU A  1 323  ? -60.079 64.853  89.210  1.00 33.24 ? 321  GLU A CD    1 
ATOM   2204  O OE1   . GLU A  1 323  ? -59.378 64.042  89.833  1.00 41.23 ? 321  GLU A OE1   1 
ATOM   2205  O OE2   . GLU A  1 323  ? -61.295 65.006  89.431  1.00 38.71 ? 321  GLU A OE2   1 
ATOM   2206  N N     . VAL A  1 324  ? -58.151 67.111  85.234  1.00 22.29 ? 322  VAL A N     1 
ATOM   2207  C CA    . VAL A  1 324  ? -58.735 68.252  84.531  1.00 19.94 ? 322  VAL A CA    1 
ATOM   2208  C C     . VAL A  1 324  ? -59.053 67.878  83.090  1.00 21.99 ? 322  VAL A C     1 
ATOM   2209  O O     . VAL A  1 324  ? -60.151 68.157  82.585  1.00 27.03 ? 322  VAL A O     1 
ATOM   2210  C CB    . VAL A  1 324  ? -57.800 69.474  84.596  1.00 21.91 ? 322  VAL A CB    1 
ATOM   2211  C CG1   . VAL A  1 324  ? -58.368 70.607  83.758  1.00 26.24 ? 322  VAL A CG1   1 
ATOM   2212  C CG2   . VAL A  1 324  ? -57.612 69.910  86.025  1.00 23.34 ? 322  VAL A CG2   1 
ATOM   2213  N N     . LEU A  1 325  ? -58.097 67.248  82.401  1.00 20.65 ? 323  LEU A N     1 
ATOM   2214  C CA    . LEU A  1 325  ? -58.324 66.906  80.999  1.00 22.53 ? 323  LEU A CA    1 
ATOM   2215  C C     . LEU A  1 325  ? -59.505 65.955  80.852  1.00 21.90 ? 323  LEU A C     1 
ATOM   2216  O O     . LEU A  1 325  ? -60.350 66.127  79.966  1.00 20.40 ? 323  LEU A O     1 
ATOM   2217  C CB    . LEU A  1 325  ? -57.062 66.288  80.391  1.00 21.23 ? 323  LEU A CB    1 
ATOM   2218  C CG    . LEU A  1 325  ? -55.827 67.186  80.302  1.00 23.86 ? 323  LEU A CG    1 
ATOM   2219  C CD1   . LEU A  1 325  ? -54.587 66.353  80.080  1.00 20.45 ? 323  LEU A CD1   1 
ATOM   2220  C CD2   . LEU A  1 325  ? -56.012 68.200  79.187  1.00 18.93 ? 323  LEU A CD2   1 
ATOM   2221  N N     . CYS A  1 326  ? -59.577 64.933  81.702  1.00 22.83 ? 324  CYS A N     1 
ATOM   2222  C CA    . CYS A  1 326  ? -60.652 63.959  81.547  1.00 23.75 ? 324  CYS A CA    1 
ATOM   2223  C C     . CYS A  1 326  ? -62.017 64.548  81.882  1.00 24.88 ? 324  CYS A C     1 
ATOM   2224  O O     . CYS A  1 326  ? -63.034 64.049  81.385  1.00 22.96 ? 324  CYS A O     1 
ATOM   2225  C CB    . CYS A  1 326  ? -60.368 62.717  82.404  1.00 22.56 ? 324  CYS A CB    1 
ATOM   2226  S SG    . CYS A  1 326  ? -59.064 61.677  81.679  1.00 27.31 ? 324  CYS A SG    1 
ATOM   2227  N N     . LEU A  1 327  ? -62.061 65.611  82.680  1.00 23.71 ? 325  LEU A N     1 
ATOM   2228  C CA    . LEU A  1 327  ? -63.320 66.260  83.019  1.00 23.64 ? 325  LEU A CA    1 
ATOM   2229  C C     . LEU A  1 327  ? -63.633 67.440  82.107  1.00 24.54 ? 325  LEU A C     1 
ATOM   2230  O O     . LEU A  1 327  ? -64.709 68.031  82.232  1.00 23.62 ? 325  LEU A O     1 
ATOM   2231  C CB    . LEU A  1 327  ? -63.302 66.723  84.481  1.00 28.35 ? 325  LEU A CB    1 
ATOM   2232  C CG    . LEU A  1 327  ? -63.180 65.607  85.527  1.00 30.22 ? 325  LEU A CG    1 
ATOM   2233  C CD1   . LEU A  1 327  ? -62.965 66.182  86.926  1.00 32.39 ? 325  LEU A CD1   1 
ATOM   2234  C CD2   . LEU A  1 327  ? -64.395 64.706  85.505  1.00 31.58 ? 325  LEU A CD2   1 
ATOM   2235  N N     . ASP A  1 328  ? -62.736 67.777  81.180  1.00 23.68 ? 326  ASP A N     1 
ATOM   2236  C CA    . ASP A  1 328  ? -62.927 68.940  80.316  1.00 23.16 ? 326  ASP A CA    1 
ATOM   2237  C C     . ASP A  1 328  ? -63.892 68.589  79.189  1.00 21.36 ? 326  ASP A C     1 
ATOM   2238  O O     . ASP A  1 328  ? -63.614 67.695  78.390  1.00 24.61 ? 326  ASP A O     1 
ATOM   2239  C CB    . ASP A  1 328  ? -61.590 69.410  79.752  1.00 24.56 ? 326  ASP A CB    1 
ATOM   2240  C CG    . ASP A  1 328  ? -61.702 70.740  79.019  1.00 28.34 ? 326  ASP A CG    1 
ATOM   2241  O OD1   . ASP A  1 328  ? -62.629 70.908  78.199  1.00 28.43 ? 326  ASP A OD1   1 
ATOM   2242  O OD2   . ASP A  1 328  ? -60.868 71.630  79.277  1.00 28.19 ? 326  ASP A OD2   1 
ATOM   2243  N N     . GLY A  1 329  ? -65.022 69.297  79.128  1.00 23.62 ? 327  GLY A N     1 
ATOM   2244  C CA    . GLY A  1 329  ? -66.047 68.967  78.143  1.00 23.38 ? 327  GLY A CA    1 
ATOM   2245  C C     . GLY A  1 329  ? -65.597 69.136  76.703  1.00 25.09 ? 327  GLY A C     1 
ATOM   2246  O O     . GLY A  1 329  ? -66.107 68.456  75.804  1.00 23.54 ? 327  GLY A O     1 
ATOM   2247  N N     . ASP A  1 330  ? -64.637 70.031  76.454  1.00 23.84 ? 328  ASP A N     1 
ATOM   2248  C CA    . ASP A  1 330  ? -64.150 70.198  75.089  1.00 26.69 ? 328  ASP A CA    1 
ATOM   2249  C C     . ASP A  1 330  ? -63.511 68.938  74.538  1.00 21.48 ? 328  ASP A C     1 
ATOM   2250  O O     . ASP A  1 330  ? -63.408 68.803  73.317  1.00 22.44 ? 328  ASP A O     1 
ATOM   2251  C CB    . ASP A  1 330  ? -63.141 71.341  74.992  1.00 27.38 ? 328  ASP A CB    1 
ATOM   2252  C CG    . ASP A  1 330  ? -63.770 72.689  75.265  1.00 31.05 ? 328  ASP A CG    1 
ATOM   2253  O OD1   . ASP A  1 330  ? -64.992 72.833  75.018  1.00 34.49 ? 328  ASP A OD1   1 
ATOM   2254  O OD2   . ASP A  1 330  ? -63.051 73.598  75.730  1.00 32.26 ? 328  ASP A OD2   1 
ATOM   2255  N N     . LEU A  1 331  ? -63.076 68.021  75.399  1.00 21.21 ? 329  LEU A N     1 
ATOM   2256  C CA    . LEU A  1 331  ? -62.430 66.792  74.964  1.00 21.65 ? 329  LEU A CA    1 
ATOM   2257  C C     . LEU A  1 331  ? -63.389 65.604  74.911  1.00 24.82 ? 329  LEU A C     1 
ATOM   2258  O O     . LEU A  1 331  ? -62.954 64.481  74.635  1.00 22.85 ? 329  LEU A O     1 
ATOM   2259  C CB    . LEU A  1 331  ? -61.241 66.481  75.882  1.00 19.81 ? 329  LEU A CB    1 
ATOM   2260  C CG    . LEU A  1 331  ? -59.999 67.359  75.639  1.00 19.62 ? 329  LEU A CG    1 
ATOM   2261  C CD1   . LEU A  1 331  ? -59.000 67.180  76.768  1.00 19.41 ? 329  LEU A CD1   1 
ATOM   2262  C CD2   . LEU A  1 331  ? -59.332 67.035  74.307  1.00 19.61 ? 329  LEU A CD2   1 
ATOM   2263  N N     . SER A  1 332  ? -64.679 65.830  75.140  1.00 26.26 ? 330  SER A N     1 
ATOM   2264  C CA    . SER A  1 332  ? -65.641 64.737  75.219  1.00 26.40 ? 330  SER A CA    1 
ATOM   2265  C C     . SER A  1 332  ? -65.794 64.039  73.871  1.00 25.04 ? 330  SER A C     1 
ATOM   2266  O O     . SER A  1 332  ? -65.564 64.629  72.810  1.00 23.40 ? 330  SER A O     1 
ATOM   2267  C CB    . SER A  1 332  ? -67.005 65.251  75.695  1.00 26.89 ? 330  SER A CB    1 
ATOM   2268  O OG    . SER A  1 332  ? -67.534 66.239  74.826  1.00 31.35 ? 330  SER A OG    1 
ATOM   2269  N N     . GLY A  1 333  ? -66.179 62.761  73.925  1.00 23.26 ? 331  GLY A N     1 
ATOM   2270  C CA    . GLY A  1 333  ? -66.408 61.980  72.719  1.00 26.59 ? 331  GLY A CA    1 
ATOM   2271  C C     . GLY A  1 333  ? -65.175 61.303  72.159  1.00 24.36 ? 331  GLY A C     1 
ATOM   2272  O O     . GLY A  1 333  ? -65.253 60.678  71.093  1.00 22.72 ? 331  GLY A O     1 
ATOM   2273  N N     . TRP A  1 334  ? -64.049 61.389  72.855  1.00 23.78 ? 332  TRP A N     1 
ATOM   2274  C CA    . TRP A  1 334  ? -62.779 60.846  72.407  1.00 21.93 ? 332  TRP A CA    1 
ATOM   2275  C C     . TRP A  1 334  ? -62.199 60.040  73.552  1.00 22.17 ? 332  TRP A C     1 
ATOM   2276  O O     . TRP A  1 334  ? -62.069 60.565  74.659  1.00 23.60 ? 332  TRP A O     1 
ATOM   2277  C CB    . TRP A  1 334  ? -61.836 61.984  72.016  1.00 22.70 ? 332  TRP A CB    1 
ATOM   2278  C CG    . TRP A  1 334  ? -60.396 61.638  71.819  1.00 20.18 ? 332  TRP A CG    1 
ATOM   2279  C CD1   . TRP A  1 334  ? -59.850 60.909  70.804  1.00 22.63 ? 332  TRP A CD1   1 
ATOM   2280  C CD2   . TRP A  1 334  ? -59.303 62.072  72.638  1.00 19.91 ? 332  TRP A CD2   1 
ATOM   2281  N NE1   . TRP A  1 334  ? -58.484 60.857  70.940  1.00 20.15 ? 332  TRP A NE1   1 
ATOM   2282  C CE2   . TRP A  1 334  ? -58.122 61.562  72.061  1.00 19.83 ? 332  TRP A CE2   1 
ATOM   2283  C CE3   . TRP A  1 334  ? -59.214 62.852  73.791  1.00 19.76 ? 332  TRP A CE3   1 
ATOM   2284  C CZ2   . TRP A  1 334  ? -56.866 61.781  72.612  1.00 19.59 ? 332  TRP A CZ2   1 
ATOM   2285  C CZ3   . TRP A  1 334  ? -57.953 63.080  74.343  1.00 22.15 ? 332  TRP A CZ3   1 
ATOM   2286  C CH2   . TRP A  1 334  ? -56.801 62.548  73.748  1.00 19.70 ? 332  TRP A CH2   1 
ATOM   2287  N N     . ASN A  1 335  ? -61.855 58.777  73.286  1.00 20.76 ? 333  ASN A N     1 
ATOM   2288  C CA    . ASN A  1 335  ? -61.296 57.877  74.292  1.00 23.23 ? 333  ASN A CA    1 
ATOM   2289  C C     . ASN A  1 335  ? -59.792 57.663  74.111  1.00 23.47 ? 333  ASN A C     1 
ATOM   2290  O O     . ASN A  1 335  ? -59.233 56.690  74.642  1.00 23.00 ? 333  ASN A O     1 
ATOM   2291  C CB    . ASN A  1 335  ? -62.027 56.527  74.258  1.00 24.93 ? 333  ASN A CB    1 
ATOM   2292  C CG    . ASN A  1 335  ? -63.413 56.578  74.909  1.00 27.00 ? 333  ASN A CG    1 
ATOM   2293  O OD1   . ASN A  1 335  ? -63.637 57.283  75.892  1.00 25.98 ? 333  ASN A OD1   1 
ATOM   2294  N ND2   . ASN A  1 335  ? -64.347 55.831  74.347  1.00 28.21 ? 333  ASN A ND2   1 
ATOM   2295  N N     . GLY A  1 336  ? -59.128 58.540  73.356  1.00 20.32 ? 334  GLY A N     1 
ATOM   2296  C CA    . GLY A  1 336  ? -57.733 58.353  73.026  1.00 19.97 ? 334  GLY A CA    1 
ATOM   2297  C C     . GLY A  1 336  ? -56.749 58.789  74.093  1.00 21.92 ? 334  GLY A C     1 
ATOM   2298  O O     . GLY A  1 336  ? -55.554 58.541  73.926  1.00 19.95 ? 334  GLY A O     1 
ATOM   2299  N N     . MET A  1 337  ? -57.214 59.435  75.163  1.00 20.85 ? 335  MET A N     1 
ATOM   2300  C CA    A MET A  1 337  ? -56.309 59.895  76.207  0.44 20.47 ? 335  MET A CA    1 
ATOM   2301  C CA    B MET A  1 337  ? -56.302 59.891  76.202  0.56 20.46 ? 335  MET A CA    1 
ATOM   2302  C C     . MET A  1 337  ? -55.721 58.708  76.963  1.00 21.64 ? 335  MET A C     1 
ATOM   2303  O O     . MET A  1 337  ? -56.456 57.852  77.458  1.00 20.13 ? 335  MET A O     1 
ATOM   2304  C CB    A MET A  1 337  ? -57.040 60.830  77.168  0.44 22.66 ? 335  MET A CB    1 
ATOM   2305  C CB    B MET A  1 337  ? -57.007 60.831  77.171  0.56 22.77 ? 335  MET A CB    1 
ATOM   2306  C CG    A MET A  1 337  ? -56.143 61.418  78.247  0.44 24.41 ? 335  MET A CG    1 
ATOM   2307  C CG    B MET A  1 337  ? -56.137 61.169  78.371  0.56 24.66 ? 335  MET A CG    1 
ATOM   2308  S SD    A MET A  1 337  ? -54.859 62.489  77.585  0.44 25.66 ? 335  MET A SD    1 
ATOM   2309  S SD    B MET A  1 337  ? -56.037 62.935  78.663  0.56 25.86 ? 335  MET A SD    1 
ATOM   2310  C CE    A MET A  1 337  ? -55.741 64.040  77.396  0.44 21.73 ? 335  MET A CE    1 
ATOM   2311  C CE    B MET A  1 337  ? -55.316 63.473  77.106  0.56 21.73 ? 335  MET A CE    1 
ATOM   2312  N N     . GLY A  1 338  ? -54.384 58.677  77.063  1.00 21.33 ? 336  GLY A N     1 
ATOM   2313  C CA    . GLY A  1 338  ? -53.695 57.586  77.706  1.00 19.27 ? 336  GLY A CA    1 
ATOM   2314  C C     . GLY A  1 338  ? -52.760 58.097  78.786  1.00 18.98 ? 336  GLY A C     1 
ATOM   2315  O O     . GLY A  1 338  ? -52.390 59.269  78.817  1.00 18.81 ? 336  GLY A O     1 
ATOM   2316  N N     . PHE A  1 339  ? -52.438 57.198  79.714  1.00 19.01 ? 337  PHE A N     1 
ATOM   2317  C CA    . PHE A  1 339  ? -51.644 57.555  80.884  1.00 18.84 ? 337  PHE A CA    1 
ATOM   2318  C C     . PHE A  1 339  ? -50.825 56.345  81.318  1.00 19.07 ? 337  PHE A C     1 
ATOM   2319  O O     . PHE A  1 339  ? -51.360 55.235  81.435  1.00 21.32 ? 337  PHE A O     1 
ATOM   2320  C CB    . PHE A  1 339  ? -52.578 58.014  82.016  1.00 18.89 ? 337  PHE A CB    1 
ATOM   2321  C CG    . PHE A  1 339  ? -51.891 58.703  83.156  1.00 18.73 ? 337  PHE A CG    1 
ATOM   2322  C CD1   . PHE A  1 339  ? -51.620 60.068  83.099  1.00 22.56 ? 337  PHE A CD1   1 
ATOM   2323  C CD2   . PHE A  1 339  ? -51.563 57.997  84.298  1.00 18.78 ? 337  PHE A CD2   1 
ATOM   2324  C CE1   . PHE A  1 339  ? -51.004 60.704  84.167  1.00 22.10 ? 337  PHE A CE1   1 
ATOM   2325  C CE2   . PHE A  1 339  ? -50.949 58.636  85.375  1.00 22.96 ? 337  PHE A CE2   1 
ATOM   2326  C CZ    . PHE A  1 339  ? -50.674 59.985  85.299  1.00 20.86 ? 337  PHE A CZ    1 
ATOM   2327  N N     . VAL A  1 340  ? -49.532 56.564  81.559  1.00 21.40 ? 338  VAL A N     1 
ATOM   2328  C CA    . VAL A  1 340  ? -48.621 55.512  82.002  1.00 21.94 ? 338  VAL A CA    1 
ATOM   2329  C C     . VAL A  1 340  ? -48.601 55.459  83.525  1.00 19.70 ? 338  VAL A C     1 
ATOM   2330  O O     . VAL A  1 340  ? -48.554 56.500  84.201  1.00 19.68 ? 338  VAL A O     1 
ATOM   2331  C CB    . VAL A  1 340  ? -47.200 55.745  81.451  1.00 19.50 ? 338  VAL A CB    1 
ATOM   2332  C CG1   . VAL A  1 340  ? -46.249 54.666  81.941  1.00 19.75 ? 338  VAL A CG1   1 
ATOM   2333  C CG2   . VAL A  1 340  ? -47.193 55.808  79.944  1.00 18.80 ? 338  VAL A CG2   1 
ATOM   2334  N N     . VAL A  1 341  ? -48.620 54.240  84.065  1.00 20.34 ? 339  VAL A N     1 
ATOM   2335  C CA    . VAL A  1 341  ? -48.375 53.981  85.480  1.00 19.25 ? 339  VAL A CA    1 
ATOM   2336  C C     . VAL A  1 341  ? -47.212 52.996  85.592  1.00 20.12 ? 339  VAL A C     1 
ATOM   2337  O O     . VAL A  1 341  ? -47.118 52.034  84.826  1.00 19.54 ? 339  VAL A O     1 
ATOM   2338  C CB    . VAL A  1 341  ? -49.644 53.461  86.204  1.00 21.58 ? 339  VAL A CB    1 
ATOM   2339  C CG1   . VAL A  1 341  ? -50.846 54.378  85.928  1.00 21.18 ? 339  VAL A CG1   1 
ATOM   2340  C CG2   . VAL A  1 341  ? -49.993 52.056  85.780  1.00 27.35 ? 339  VAL A CG2   1 
ATOM   2341  N N     . GLN A  1 342  ? -46.325 53.232  86.558  1.00 18.89 ? 340  GLN A N     1 
ATOM   2342  C CA    . GLN A  1 342  ? -45.081 52.481  86.681  1.00 21.88 ? 340  GLN A CA    1 
ATOM   2343  C C     . GLN A  1 342  ? -45.211 51.444  87.794  1.00 19.14 ? 340  GLN A C     1 
ATOM   2344  O O     . GLN A  1 342  ? -45.363 51.803  88.968  1.00 20.64 ? 340  GLN A O     1 
ATOM   2345  C CB    . GLN A  1 342  ? -43.923 53.430  86.972  1.00 18.63 ? 340  GLN A CB    1 
ATOM   2346  C CG    . GLN A  1 342  ? -43.679 54.465  85.864  1.00 18.42 ? 340  GLN A CG    1 
ATOM   2347  C CD    . GLN A  1 342  ? -43.102 55.769  86.391  1.00 18.19 ? 340  GLN A CD    1 
ATOM   2348  O OE1   . GLN A  1 342  ? -43.646 56.374  87.307  1.00 18.18 ? 340  GLN A OE1   1 
ATOM   2349  N NE2   . GLN A  1 342  ? -41.980 56.202  85.808  1.00 19.95 ? 340  GLN A NE2   1 
ATOM   2350  N N     . ALA A  1 343  ? -45.116 50.166  87.430  1.00 19.37 ? 341  ALA A N     1 
ATOM   2351  C CA    . ALA A  1 343  ? -45.292 49.124  88.431  1.00 19.65 ? 341  ALA A CA    1 
ATOM   2352  C C     . ALA A  1 343  ? -44.121 49.046  89.400  1.00 21.31 ? 341  ALA A C     1 
ATOM   2353  O O     . ALA A  1 343  ? -44.268 48.460  90.476  1.00 21.68 ? 341  ALA A O     1 
ATOM   2354  C CB    . ALA A  1 343  ? -45.499 47.768  87.757  1.00 21.28 ? 341  ALA A CB    1 
ATOM   2355  N N     . TYR A  1 344  ? -42.962 49.609  89.063  1.00 19.80 ? 342  TYR A N     1 
ATOM   2356  C CA    . TYR A  1 344  ? -41.940 49.579  90.111  1.00 21.77 ? 342  TYR A CA    1 
ATOM   2357  C C     . TYR A  1 344  ? -42.225 50.578  91.231  1.00 22.72 ? 342  TYR A C     1 
ATOM   2358  O O     . TYR A  1 344  ? -41.441 50.649  92.189  1.00 21.49 ? 342  TYR A O     1 
ATOM   2359  C CB    . TYR A  1 344  ? -40.528 49.794  89.526  1.00 21.05 ? 342  TYR A CB    1 
ATOM   2360  C CG    . TYR A  1 344  ? -40.110 51.193  89.021  1.00 20.34 ? 342  TYR A CG    1 
ATOM   2361  C CD1   . TYR A  1 344  ? -40.996 52.266  88.984  1.00 21.16 ? 342  TYR A CD1   1 
ATOM   2362  C CD2   . TYR A  1 344  ? -38.810 51.401  88.552  1.00 20.27 ? 342  TYR A CD2   1 
ATOM   2363  C CE1   . TYR A  1 344  ? -40.591 53.518  88.516  1.00 20.51 ? 342  TYR A CE1   1 
ATOM   2364  C CE2   . TYR A  1 344  ? -38.404 52.626  88.077  1.00 22.55 ? 342  TYR A CE2   1 
ATOM   2365  C CZ    . TYR A  1 344  ? -39.293 53.684  88.064  1.00 21.10 ? 342  TYR A CZ    1 
ATOM   2366  O OH    . TYR A  1 344  ? -38.876 54.901  87.591  1.00 20.26 ? 342  TYR A OH    1 
ATOM   2367  N N     . GLY A  1 345  ? -43.315 51.333  91.140  1.00 19.24 ? 343  GLY A N     1 
ATOM   2368  C CA    . GLY A  1 345  ? -43.638 52.358  92.120  1.00 20.49 ? 343  GLY A CA    1 
ATOM   2369  C C     . GLY A  1 345  ? -44.594 51.809  93.159  1.00 22.85 ? 343  GLY A C     1 
ATOM   2370  O O     . GLY A  1 345  ? -45.500 51.040  92.840  1.00 22.74 ? 343  GLY A O     1 
ATOM   2371  N N     . LYS A  1 346  ? -44.367 52.193  94.417  1.00 19.64 ? 344  LYS A N     1 
ATOM   2372  C CA    . LYS A  1 346  ? -45.178 51.685  95.518  1.00 20.60 ? 344  LYS A CA    1 
ATOM   2373  C C     . LYS A  1 346  ? -46.617 52.190  95.475  1.00 22.67 ? 344  LYS A C     1 
ATOM   2374  O O     . LYS A  1 346  ? -47.493 51.596  96.115  1.00 22.51 ? 344  LYS A O     1 
ATOM   2375  C CB    . LYS A  1 346  ? -44.523 52.056  96.846  1.00 23.42 ? 344  LYS A CB    1 
ATOM   2376  C CG    . LYS A  1 346  ? -43.238 51.289  97.092  1.00 24.19 ? 344  LYS A CG    1 
ATOM   2377  C CD    . LYS A  1 346  ? -42.487 51.871  98.271  1.00 24.96 ? 344  LYS A CD    1 
ATOM   2378  C CE    . LYS A  1 346  ? -41.250 51.067  98.596  1.00 25.46 ? 344  LYS A CE    1 
ATOM   2379  N NZ    . LYS A  1 346  ? -40.554 51.625  99.798  1.00 25.20 ? 344  LYS A NZ    1 
ATOM   2380  N N     . ARG A  1 347  ? -46.886 53.262  94.736  1.00 20.53 ? 345  ARG A N     1 
ATOM   2381  C CA    . ARG A  1 347  ? -48.228 53.815  94.675  1.00 21.37 ? 345  ARG A CA    1 
ATOM   2382  C C     . ARG A  1 347  ? -49.063 53.208  93.563  1.00 21.00 ? 345  ARG A C     1 
ATOM   2383  O O     . ARG A  1 347  ? -50.276 53.441  93.523  1.00 22.45 ? 345  ARG A O     1 
ATOM   2384  C CB    . ARG A  1 347  ? -48.155 55.334  94.494  1.00 19.75 ? 345  ARG A CB    1 
ATOM   2385  C CG    . ARG A  1 347  ? -47.593 56.032  95.732  1.00 20.77 ? 345  ARG A CG    1 
ATOM   2386  C CD    . ARG A  1 347  ? -47.229 57.458  95.447  1.00 19.06 ? 345  ARG A CD    1 
ATOM   2387  N NE    . ARG A  1 347  ? -45.995 57.561  94.678  1.00 20.66 ? 345  ARG A NE    1 
ATOM   2388  C CZ    . ARG A  1 347  ? -45.560 58.691  94.139  1.00 21.49 ? 345  ARG A CZ    1 
ATOM   2389  N NH1   . ARG A  1 347  ? -46.231 59.822  94.282  1.00 18.75 ? 345  ARG A NH1   1 
ATOM   2390  N NH2   . ARG A  1 347  ? -44.430 58.685  93.432  1.00 20.29 ? 345  ARG A NH2   1 
ATOM   2391  N N     . CYS A  1 348  ? -48.444 52.420  92.687  1.00 19.69 ? 346  CYS A N     1 
ATOM   2392  C CA    . CYS A  1 348  ? -49.085 51.985  91.448  1.00 21.78 ? 346  CYS A CA    1 
ATOM   2393  C C     . CYS A  1 348  ? -50.515 51.458  91.607  1.00 20.36 ? 346  CYS A C     1 
ATOM   2394  O O     . CYS A  1 348  ? -51.390 51.913  90.860  1.00 21.96 ? 346  CYS A O     1 
ATOM   2395  C CB    . CYS A  1 348  ? -48.180 50.955  90.759  1.00 21.17 ? 346  CYS A CB    1 
ATOM   2396  S SG    . CYS A  1 348  ? -48.712 50.695  89.042  1.00 27.27 ? 346  CYS A SG    1 
ATOM   2397  N N     . PRO A  1 349  ? -50.832 50.528  92.519  1.00 21.85 ? 347  PRO A N     1 
ATOM   2398  C CA    . PRO A  1 349  ? -52.224 50.044  92.581  1.00 22.88 ? 347  PRO A CA    1 
ATOM   2399  C C     . PRO A  1 349  ? -53.211 51.109  93.031  1.00 22.08 ? 347  PRO A C     1 
ATOM   2400  O O     . PRO A  1 349  ? -54.364 51.105  92.581  1.00 24.44 ? 347  PRO A O     1 
ATOM   2401  C CB    . PRO A  1 349  ? -52.162 48.873  93.577  1.00 24.76 ? 347  PRO A CB    1 
ATOM   2402  C CG    . PRO A  1 349  ? -50.900 49.065  94.345  1.00 23.91 ? 347  PRO A CG    1 
ATOM   2403  C CD    . PRO A  1 349  ? -49.955 49.861  93.496  1.00 20.49 ? 347  PRO A CD    1 
ATOM   2404  N N     . PHE A  1 350  ? -52.788 52.026  93.898  1.00 23.58 ? 348  PHE A N     1 
ATOM   2405  C CA    . PHE A  1 350  ? -53.665 53.104  94.329  1.00 23.18 ? 348  PHE A CA    1 
ATOM   2406  C C     . PHE A  1 350  ? -53.818 54.146  93.240  1.00 20.83 ? 348  PHE A C     1 
ATOM   2407  O O     . PHE A  1 350  ? -54.891 54.748  93.105  1.00 23.27 ? 348  PHE A O     1 
ATOM   2408  C CB    . PHE A  1 350  ? -53.112 53.710  95.607  1.00 23.17 ? 348  PHE A CB    1 
ATOM   2409  C CG    . PHE A  1 350  ? -52.710 52.674  96.601  1.00 23.12 ? 348  PHE A CG    1 
ATOM   2410  C CD1   . PHE A  1 350  ? -53.666 52.087  97.422  1.00 25.95 ? 348  PHE A CD1   1 
ATOM   2411  C CD2   . PHE A  1 350  ? -51.390 52.235  96.677  1.00 22.88 ? 348  PHE A CD2   1 
ATOM   2412  C CE1   . PHE A  1 350  ? -53.311 51.106  98.316  1.00 29.59 ? 348  PHE A CE1   1 
ATOM   2413  C CE2   . PHE A  1 350  ? -51.033 51.248  97.566  1.00 24.62 ? 348  PHE A CE2   1 
ATOM   2414  C CZ    . PHE A  1 350  ? -51.990 50.690  98.388  1.00 27.35 ? 348  PHE A CZ    1 
ATOM   2415  N N     . VAL A  1 351  ? -52.769 54.347  92.436  1.00 19.96 ? 349  VAL A N     1 
ATOM   2416  C CA    . VAL A  1 351  ? -52.900 55.188  91.254  1.00 19.73 ? 349  VAL A CA    1 
ATOM   2417  C C     . VAL A  1 351  ? -53.899 54.569  90.300  1.00 19.91 ? 349  VAL A C     1 
ATOM   2418  O O     . VAL A  1 351  ? -54.731 55.265  89.716  1.00 21.81 ? 349  VAL A O     1 
ATOM   2419  C CB    . VAL A  1 351  ? -51.534 55.410  90.576  1.00 19.43 ? 349  VAL A CB    1 
ATOM   2420  C CG1   . VAL A  1 351  ? -51.696 56.266  89.308  1.00 19.23 ? 349  VAL A CG1   1 
ATOM   2421  C CG2   . VAL A  1 351  ? -50.576 56.086  91.541  1.00 19.30 ? 349  VAL A CG2   1 
ATOM   2422  N N     . LEU A  1 352  ? -53.834 53.247  90.127  1.00 21.72 ? 350  LEU A N     1 
ATOM   2423  C CA    . LEU A  1 352  ? -54.788 52.586  89.253  1.00 20.29 ? 350  LEU A CA    1 
ATOM   2424  C C     . LEU A  1 352  ? -56.215 52.714  89.787  1.00 24.16 ? 350  LEU A C     1 
ATOM   2425  O O     . LEU A  1 352  ? -57.151 52.949  89.012  1.00 23.16 ? 350  LEU A O     1 
ATOM   2426  C CB    . LEU A  1 352  ? -54.387 51.123  89.079  1.00 23.78 ? 350  LEU A CB    1 
ATOM   2427  C CG    . LEU A  1 352  ? -53.152 50.941  88.201  1.00 24.32 ? 350  LEU A CG    1 
ATOM   2428  C CD1   . LEU A  1 352  ? -52.711 49.485  88.181  1.00 25.51 ? 350  LEU A CD1   1 
ATOM   2429  C CD2   . LEU A  1 352  ? -53.465 51.431  86.783  1.00 21.61 ? 350  LEU A CD2   1 
ATOM   2430  N N     . ASP A  1 353  ? -56.412 52.545  91.101  1.00 22.57 ? 351  ASP A N     1 
ATOM   2431  C CA    . ASP A  1 353  ? -57.737 52.775  91.676  1.00 23.75 ? 351  ASP A CA    1 
ATOM   2432  C C     . ASP A  1 353  ? -58.255 54.160  91.316  1.00 23.69 ? 351  ASP A C     1 
ATOM   2433  O O     . ASP A  1 353  ? -59.423 54.324  90.941  1.00 25.84 ? 351  ASP A O     1 
ATOM   2434  C CB    . ASP A  1 353  ? -57.700 52.626  93.194  1.00 21.21 ? 351  ASP A CB    1 
ATOM   2435  C CG    . ASP A  1 353  ? -57.620 51.190  93.639  1.00 25.27 ? 351  ASP A CG    1 
ATOM   2436  O OD1   . ASP A  1 353  ? -57.842 50.290  92.807  1.00 27.13 ? 351  ASP A OD1   1 
ATOM   2437  O OD2   . ASP A  1 353  ? -57.305 50.972  94.827  1.00 33.37 ? 351  ASP A OD2   1 
ATOM   2438  N N     . PHE A  1 354  ? -57.398 55.175  91.456  1.00 21.35 ? 352  PHE A N     1 
ATOM   2439  C CA    . PHE A  1 354  ? -57.808 56.540  91.165  1.00 22.18 ? 352  PHE A CA    1 
ATOM   2440  C C     . PHE A  1 354  ? -58.166 56.701  89.697  1.00 20.26 ? 352  PHE A C     1 
ATOM   2441  O O     . PHE A  1 354  ? -59.178 57.328  89.363  1.00 21.68 ? 352  PHE A O     1 
ATOM   2442  C CB    . PHE A  1 354  ? -56.695 57.520  91.553  1.00 20.06 ? 352  PHE A CB    1 
ATOM   2443  C CG    . PHE A  1 354  ? -56.903 58.910  91.015  1.00 23.32 ? 352  PHE A CG    1 
ATOM   2444  C CD1   . PHE A  1 354  ? -57.684 59.823  91.705  1.00 24.47 ? 352  PHE A CD1   1 
ATOM   2445  C CD2   . PHE A  1 354  ? -56.301 59.308  89.828  1.00 21.80 ? 352  PHE A CD2   1 
ATOM   2446  C CE1   . PHE A  1 354  ? -57.888 61.114  91.206  1.00 28.16 ? 352  PHE A CE1   1 
ATOM   2447  C CE2   . PHE A  1 354  ? -56.504 60.595  89.318  1.00 24.25 ? 352  PHE A CE2   1 
ATOM   2448  C CZ    . PHE A  1 354  ? -57.292 61.497  90.016  1.00 24.94 ? 352  PHE A CZ    1 
ATOM   2449  N N     . ILE A  1 355  ? -57.362 56.115  88.804  1.00 20.12 ? 353  ILE A N     1 
ATOM   2450  C CA    . ILE A  1 355  ? -57.599 56.304  87.374  1.00 20.03 ? 353  ILE A CA    1 
ATOM   2451  C C     . ILE A  1 355  ? -58.880 55.599  86.949  1.00 21.21 ? 353  ILE A C     1 
ATOM   2452  O O     . ILE A  1 355  ? -59.648 56.116  86.124  1.00 22.02 ? 353  ILE A O     1 
ATOM   2453  C CB    . ILE A  1 355  ? -56.390 55.819  86.547  1.00 19.85 ? 353  ILE A CB    1 
ATOM   2454  C CG1   . ILE A  1 355  ? -55.170 56.713  86.794  1.00 21.12 ? 353  ILE A CG1   1 
ATOM   2455  C CG2   . ILE A  1 355  ? -56.736 55.834  85.046  1.00 19.83 ? 353  ILE A CG2   1 
ATOM   2456  C CD1   . ILE A  1 355  ? -53.895 56.221  86.094  1.00 21.24 ? 353  ILE A CD1   1 
ATOM   2457  N N     . ILE A  1 356  ? -59.114 54.394  87.473  1.00 21.30 ? 354  ILE A N     1 
ATOM   2458  C CA    . ILE A  1 356  ? -60.316 53.648  87.109  1.00 21.54 ? 354  ILE A CA    1 
ATOM   2459  C C     . ILE A  1 356  ? -61.559 54.403  87.564  1.00 22.05 ? 354  ILE A C     1 
ATOM   2460  O O     . ILE A  1 356  ? -62.552 54.487  86.832  1.00 22.13 ? 354  ILE A O     1 
ATOM   2461  C CB    . ILE A  1 356  ? -60.246 52.220  87.689  1.00 22.20 ? 354  ILE A CB    1 
ATOM   2462  C CG1   . ILE A  1 356  ? -59.113 51.433  87.014  1.00 22.85 ? 354  ILE A CG1   1 
ATOM   2463  C CG2   . ILE A  1 356  ? -61.589 51.489  87.543  1.00 26.12 ? 354  ILE A CG2   1 
ATOM   2464  C CD1   . ILE A  1 356  ? -58.707 50.140  87.746  1.00 22.16 ? 354  ILE A CD1   1 
ATOM   2465  N N     . ASP A  1 357  ? -61.509 54.993  88.764  1.00 22.73 ? 355  ASP A N     1 
ATOM   2466  C CA    . ASP A  1 357  ? -62.612 55.817  89.254  1.00 24.59 ? 355  ASP A CA    1 
ATOM   2467  C C     . ASP A  1 357  ? -62.779 57.079  88.415  1.00 25.91 ? 355  ASP A C     1 
ATOM   2468  O O     . ASP A  1 357  ? -63.908 57.509  88.139  1.00 24.20 ? 355  ASP A O     1 
ATOM   2469  C CB    . ASP A  1 357  ? -62.372 56.207  90.711  1.00 22.88 ? 355  ASP A CB    1 
ATOM   2470  C CG    . ASP A  1 357  ? -63.437 57.163  91.241  1.00 26.19 ? 355  ASP A CG    1 
ATOM   2471  O OD1   . ASP A  1 357  ? -64.539 56.685  91.559  1.00 28.53 ? 355  ASP A OD1   1 
ATOM   2472  O OD2   . ASP A  1 357  ? -63.183 58.391  91.318  1.00 28.03 ? 355  ASP A OD2   1 
ATOM   2473  N N     . LEU A  1 358  ? -61.666 57.696  88.019  1.00 23.58 ? 356  LEU A N     1 
ATOM   2474  C CA    . LEU A  1 358  ? -61.747 58.848  87.127  1.00 23.64 ? 356  LEU A CA    1 
ATOM   2475  C C     . LEU A  1 358  ? -62.377 58.454  85.801  1.00 23.42 ? 356  LEU A C     1 
ATOM   2476  O O     . LEU A  1 358  ? -63.195 59.199  85.246  1.00 20.61 ? 356  LEU A O     1 
ATOM   2477  C CB    . LEU A  1 358  ? -60.358 59.451  86.915  1.00 21.40 ? 356  LEU A CB    1 
ATOM   2478  C CG    . LEU A  1 358  ? -60.259 60.614  85.923  1.00 23.53 ? 356  LEU A CG    1 
ATOM   2479  C CD1   . LEU A  1 358  ? -61.173 61.760  86.365  1.00 23.35 ? 356  LEU A CD1   1 
ATOM   2480  C CD2   . LEU A  1 358  ? -58.788 61.069  85.744  1.00 20.09 ? 356  LEU A CD2   1 
ATOM   2481  N N     . ALA A  1 359  ? -62.025 57.274  85.287  1.00 22.96 ? 357  ALA A N     1 
ATOM   2482  C CA    . ALA A  1 359  ? -62.643 56.800  84.053  1.00 25.86 ? 357  ALA A CA    1 
ATOM   2483  C C     . ALA A  1 359  ? -64.154 56.638  84.214  1.00 25.73 ? 357  ALA A C     1 
ATOM   2484  O O     . ALA A  1 359  ? -64.928 57.007  83.317  1.00 25.66 ? 357  ALA A O     1 
ATOM   2485  C CB    . ALA A  1 359  ? -61.985 55.483  83.616  1.00 21.56 ? 357  ALA A CB    1 
ATOM   2486  N N     . ARG A  1 360  ? -64.596 56.085  85.349  1.00 23.09 ? 358  ARG A N     1 
ATOM   2487  C CA    . ARG A  1 360  ? -66.030 55.935  85.589  1.00 22.13 ? 358  ARG A CA    1 
ATOM   2488  C C     . ARG A  1 360  ? -66.727 57.289  85.686  1.00 25.67 ? 358  ARG A C     1 
ATOM   2489  O O     . ARG A  1 360  ? -67.783 57.500  85.078  1.00 30.26 ? 358  ARG A O     1 
ATOM   2490  C CB    . ARG A  1 360  ? -66.268 55.122  86.858  1.00 24.81 ? 358  ARG A CB    1 
ATOM   2491  C CG    . ARG A  1 360  ? -65.763 53.685  86.787  1.00 28.91 ? 358  ARG A CG    1 
ATOM   2492  C CD    . ARG A  1 360  ? -66.219 52.879  88.010  1.00 35.05 ? 358  ARG A CD    1 
ATOM   2493  N NE    . ARG A  1 360  ? -65.453 51.646  88.155  1.00 39.14 ? 358  ARG A NE    1 
ATOM   2494  C CZ    . ARG A  1 360  ? -65.739 50.513  87.527  1.00 43.52 ? 358  ARG A CZ    1 
ATOM   2495  N NH1   . ARG A  1 360  ? -66.789 50.415  86.722  1.00 38.52 ? 358  ARG A NH1   1 
ATOM   2496  N NH2   . ARG A  1 360  ? -64.954 49.453  87.710  1.00 39.59 ? 358  ARG A NH2   1 
ATOM   2497  N N     . ARG A  1 361  ? -66.150 58.222  86.447  1.00 24.50 ? 359  ARG A N     1 
ATOM   2498  C CA    . ARG A  1 361  ? -66.774 59.529  86.643  1.00 26.06 ? 359  ARG A CA    1 
ATOM   2499  C C     . ARG A  1 361  ? -66.888 60.291  85.332  1.00 23.74 ? 359  ARG A C     1 
ATOM   2500  O O     . ARG A  1 361  ? -67.939 60.864  85.019  1.00 27.37 ? 359  ARG A O     1 
ATOM   2501  C CB    . ARG A  1 361  ? -65.967 60.353  87.648  1.00 27.47 ? 359  ARG A CB    1 
ATOM   2502  C CG    . ARG A  1 361  ? -65.969 59.807  89.038  1.00 30.17 ? 359  ARG A CG    1 
ATOM   2503  C CD    . ARG A  1 361  ? -65.307 60.777  90.022  1.00 31.89 ? 359  ARG A CD    1 
ATOM   2504  N NE    . ARG A  1 361  ? -63.844 60.745  89.998  1.00 32.41 ? 359  ARG A NE    1 
ATOM   2505  C CZ    . ARG A  1 361  ? -63.069 61.792  89.736  1.00 30.61 ? 359  ARG A CZ    1 
ATOM   2506  N NH1   . ARG A  1 361  ? -63.576 62.957  89.369  1.00 28.55 ? 359  ARG A NH1   1 
ATOM   2507  N NH2   . ARG A  1 361  ? -61.750 61.674  89.876  1.00 28.06 ? 359  ARG A NH2   1 
ATOM   2508  N N     . SER A  1 362  ? -65.810 60.312  84.555  1.00 23.79 ? 360  SER A N     1 
ATOM   2509  C CA    . SER A  1 362  ? -65.769 61.095  83.333  1.00 22.70 ? 360  SER A CA    1 
ATOM   2510  C C     . SER A  1 362  ? -66.479 60.395  82.185  1.00 23.16 ? 360  SER A C     1 
ATOM   2511  O O     . SER A  1 362  ? -66.875 61.059  81.219  1.00 24.96 ? 360  SER A O     1 
ATOM   2512  C CB    . SER A  1 362  ? -64.309 61.391  82.943  1.00 26.96 ? 360  SER A CB    1 
ATOM   2513  O OG    . SER A  1 362  ? -63.591 60.203  82.636  1.00 22.24 ? 360  SER A OG    1 
ATOM   2514  N N     . GLY A  1 363  ? -66.654 59.080  82.266  1.00 22.76 ? 361  GLY A N     1 
ATOM   2515  C CA    . GLY A  1 363  ? -67.157 58.354  81.112  1.00 24.28 ? 361  GLY A CA    1 
ATOM   2516  C C     . GLY A  1 363  ? -66.150 58.139  80.000  1.00 26.86 ? 361  GLY A C     1 
ATOM   2517  O O     . GLY A  1 363  ? -66.536 57.733  78.901  1.00 26.87 ? 361  GLY A O     1 
ATOM   2518  N N     . ARG A  1 364  ? -64.870 58.406  80.241  1.00 27.14 ? 362  ARG A N     1 
ATOM   2519  C CA    . ARG A  1 364  ? -63.828 58.211  79.242  1.00 27.43 ? 362  ARG A CA    1 
ATOM   2520  C C     . ARG A  1 364  ? -63.090 56.912  79.531  1.00 29.22 ? 362  ARG A C     1 
ATOM   2521  O O     . ARG A  1 364  ? -62.699 56.657  80.675  1.00 27.99 ? 362  ARG A O     1 
ATOM   2522  C CB    . ARG A  1 364  ? -62.845 59.381  79.231  1.00 29.08 ? 362  ARG A CB    1 
ATOM   2523  C CG    . ARG A  1 364  ? -63.524 60.761  79.309  1.00 32.97 ? 362  ARG A CG    1 
ATOM   2524  C CD    . ARG A  1 364  ? -63.065 61.731  78.217  1.00 25.48 ? 362  ARG A CD    1 
ATOM   2525  N NE    . ARG A  1 364  ? -63.882 62.941  78.249  1.00 22.02 ? 362  ARG A NE    1 
ATOM   2526  C CZ    . ARG A  1 364  ? -63.409 64.169  78.423  1.00 25.03 ? 362  ARG A CZ    1 
ATOM   2527  N NH1   . ARG A  1 364  ? -62.103 64.412  78.466  1.00 19.92 ? 362  ARG A NH1   1 
ATOM   2528  N NH2   . ARG A  1 364  ? -64.266 65.184  78.548  1.00 20.51 ? 362  ARG A NH2   1 
ATOM   2529  N N     . ARG A  1 365  ? -62.900 56.099  78.495  1.00 24.36 ? 363  ARG A N     1 
ATOM   2530  C CA    . ARG A  1 365  ? -62.192 54.829  78.637  1.00 26.36 ? 363  ARG A CA    1 
ATOM   2531  C C     . ARG A  1 365  ? -60.693 55.102  78.561  1.00 24.53 ? 363  ARG A C     1 
ATOM   2532  O O     . ARG A  1 365  ? -60.075 55.048  77.492  1.00 25.66 ? 363  ARG A O     1 
ATOM   2533  C CB    . ARG A  1 365  ? -62.649 53.846  77.568  1.00 24.32 ? 363  ARG A CB    1 
ATOM   2534  C CG    . ARG A  1 365  ? -61.946 52.507  77.630  1.00 24.93 ? 363  ARG A CG    1 
ATOM   2535  C CD    . ARG A  1 365  ? -62.933 51.405  77.311  1.00 28.33 ? 363  ARG A CD    1 
ATOM   2536  N NE    . ARG A  1 365  ? -62.347 50.089  77.514  1.00 28.20 ? 363  ARG A NE    1 
ATOM   2537  C CZ    . ARG A  1 365  ? -61.675 49.431  76.584  1.00 26.59 ? 363  ARG A CZ    1 
ATOM   2538  N NH1   . ARG A  1 365  ? -61.526 49.921  75.368  1.00 27.69 ? 363  ARG A NH1   1 
ATOM   2539  N NH2   . ARG A  1 365  ? -61.127 48.260  76.886  1.00 26.90 ? 363  ARG A NH2   1 
ATOM   2540  N N     . ILE A  1 366  ? -60.095 55.411  79.715  1.00 22.87 ? 364  ILE A N     1 
ATOM   2541  C CA    . ILE A  1 366  ? -58.712 55.864  79.731  1.00 21.93 ? 364  ILE A CA    1 
ATOM   2542  C C     . ILE A  1 366  ? -57.800 54.733  79.276  1.00 21.28 ? 364  ILE A C     1 
ATOM   2543  O O     . ILE A  1 366  ? -57.949 53.577  79.697  1.00 22.31 ? 364  ILE A O     1 
ATOM   2544  C CB    . ILE A  1 366  ? -58.344 56.374  81.134  1.00 21.57 ? 364  ILE A CB    1 
ATOM   2545  C CG1   . ILE A  1 366  ? -59.233 57.573  81.507  1.00 24.49 ? 364  ILE A CG1   1 
ATOM   2546  C CG2   . ILE A  1 366  ? -56.852 56.752  81.211  1.00 22.61 ? 364  ILE A CG2   1 
ATOM   2547  C CD1   . ILE A  1 366  ? -59.090 58.043  82.976  1.00 22.97 ? 364  ILE A CD1   1 
ATOM   2548  N N     . MET A  1 367  ? -56.873 55.049  78.377  1.00 19.95 ? 365  MET A N     1 
ATOM   2549  C CA    . MET A  1 367  ? -55.866 54.073  77.972  1.00 19.97 ? 365  MET A CA    1 
ATOM   2550  C C     . MET A  1 367  ? -54.775 54.079  79.033  1.00 21.14 ? 365  MET A C     1 
ATOM   2551  O O     . MET A  1 367  ? -54.185 55.123  79.307  1.00 22.59 ? 365  MET A O     1 
ATOM   2552  C CB    . MET A  1 367  ? -55.306 54.412  76.592  1.00 19.90 ? 365  MET A CB    1 
ATOM   2553  C CG    . MET A  1 367  ? -56.416 54.583  75.524  1.00 22.79 ? 365  MET A CG    1 
ATOM   2554  S SD    . MET A  1 367  ? -55.836 55.031  73.872  1.00 26.98 ? 365  MET A SD    1 
ATOM   2555  C CE    . MET A  1 367  ? -55.522 53.427  73.147  1.00 26.11 ? 365  MET A CE    1 
ATOM   2556  N N     . VAL A  1 368  ? -54.554 52.944  79.684  1.00 21.91 ? 366  VAL A N     1 
ATOM   2557  C CA    . VAL A  1 368  ? -53.600 52.872  80.790  1.00 19.78 ? 366  VAL A CA    1 
ATOM   2558  C C     . VAL A  1 368  ? -52.455 51.981  80.348  1.00 20.38 ? 366  VAL A C     1 
ATOM   2559  O O     . VAL A  1 368  ? -52.644 50.775  80.145  1.00 20.82 ? 366  VAL A O     1 
ATOM   2560  C CB    . VAL A  1 368  ? -54.241 52.325  82.065  1.00 20.93 ? 366  VAL A CB    1 
ATOM   2561  C CG1   . VAL A  1 368  ? -53.181 52.272  83.171  1.00 19.83 ? 366  VAL A CG1   1 
ATOM   2562  C CG2   . VAL A  1 368  ? -55.440 53.165  82.475  1.00 22.01 ? 366  VAL A CG2   1 
ATOM   2563  N N     . ARG A  1 369  ? -51.265 52.560  80.190  1.00 20.52 ? 367  ARG A N     1 
ATOM   2564  C CA    . ARG A  1 369  ? -50.105 51.777  79.803  1.00 19.97 ? 367  ARG A CA    1 
ATOM   2565  C C     . ARG A  1 369  ? -49.394 51.372  81.083  1.00 22.57 ? 367  ARG A C     1 
ATOM   2566  O O     . ARG A  1 369  ? -48.909 52.229  81.818  1.00 21.52 ? 367  ARG A O     1 
ATOM   2567  C CB    . ARG A  1 369  ? -49.169 52.550  78.880  1.00 24.52 ? 367  ARG A CB    1 
ATOM   2568  C CG    . ARG A  1 369  ? -47.948 51.730  78.473  1.00 21.87 ? 367  ARG A CG    1 
ATOM   2569  C CD    . ARG A  1 369  ? -46.810 52.595  78.003  1.00 26.40 ? 367  ARG A CD    1 
ATOM   2570  N NE    . ARG A  1 369  ? -47.090 53.243  76.733  1.00 24.07 ? 367  ARG A NE    1 
ATOM   2571  C CZ    . ARG A  1 369  ? -46.511 54.367  76.328  1.00 29.33 ? 367  ARG A CZ    1 
ATOM   2572  N NH1   . ARG A  1 369  ? -45.586 54.970  77.060  1.00 28.04 ? 367  ARG A NH1   1 
ATOM   2573  N NH2   . ARG A  1 369  ? -46.876 54.904  75.164  1.00 26.47 ? 367  ARG A NH2   1 
ATOM   2574  N N     . LEU A  1 370  ? -49.356 50.077  81.354  1.00 21.38 ? 368  LEU A N     1 
ATOM   2575  C CA    . LEU A  1 370  ? -48.658 49.555  82.521  1.00 23.17 ? 368  LEU A CA    1 
ATOM   2576  C C     . LEU A  1 370  ? -47.226 49.225  82.113  1.00 22.41 ? 368  LEU A C     1 
ATOM   2577  O O     . LEU A  1 370  ? -47.004 48.428  81.197  1.00 22.33 ? 368  LEU A O     1 
ATOM   2578  C CB    . LEU A  1 370  ? -49.374 48.329  83.086  1.00 24.96 ? 368  LEU A CB    1 
ATOM   2579  C CG    . LEU A  1 370  ? -48.807 47.718  84.369  1.00 24.72 ? 368  LEU A CG    1 
ATOM   2580  C CD1   . LEU A  1 370  ? -48.938 48.678  85.537  1.00 25.05 ? 368  LEU A CD1   1 
ATOM   2581  C CD2   . LEU A  1 370  ? -49.508 46.395  84.691  1.00 24.94 ? 368  LEU A CD2   1 
ATOM   2582  N N     . VAL A  1 371  ? -46.258 49.851  82.786  1.00 20.36 ? 369  VAL A N     1 
ATOM   2583  C CA    . VAL A  1 371  ? -44.845 49.608  82.541  1.00 19.39 ? 369  VAL A CA    1 
ATOM   2584  C C     . VAL A  1 371  ? -44.213 49.265  83.877  1.00 20.15 ? 369  VAL A C     1 
ATOM   2585  O O     . VAL A  1 371  ? -44.813 49.448  84.936  1.00 21.09 ? 369  VAL A O     1 
ATOM   2586  C CB    . VAL A  1 371  ? -44.119 50.824  81.924  1.00 21.27 ? 369  VAL A CB    1 
ATOM   2587  C CG1   . VAL A  1 371  ? -44.871 51.346  80.723  1.00 21.60 ? 369  VAL A CG1   1 
ATOM   2588  C CG2   . VAL A  1 371  ? -43.977 51.932  82.962  1.00 20.56 ? 369  VAL A CG2   1 
ATOM   2589  N N     . LYS A  1 372  ? -42.974 48.796  83.822  1.00 21.76 ? 370  LYS A N     1 
ATOM   2590  C CA    . LYS A  1 372  ? -42.246 48.611  85.074  1.00 22.23 ? 370  LYS A CA    1 
ATOM   2591  C C     . LYS A  1 372  ? -41.640 49.935  85.547  1.00 20.68 ? 370  LYS A C     1 
ATOM   2592  O O     . LYS A  1 372  ? -42.031 50.457  86.593  1.00 24.13 ? 370  LYS A O     1 
ATOM   2593  C CB    . LYS A  1 372  ? -41.229 47.477  84.913  1.00 25.79 ? 370  LYS A CB    1 
ATOM   2594  C CG    . LYS A  1 372  ? -41.999 46.125  84.857  1.00 26.12 ? 370  LYS A CG    1 
ATOM   2595  C CD    . LYS A  1 372  ? -41.141 44.892  84.642  1.00 26.14 ? 370  LYS A CD    1 
ATOM   2596  C CE    . LYS A  1 372  ? -42.041 43.649  84.527  1.00 29.32 ? 370  LYS A CE    1 
ATOM   2597  N NZ    . LYS A  1 372  ? -41.292 42.421  84.148  1.00 29.45 ? 370  LYS A NZ    1 
ATOM   2598  N N     . GLY A  1 373  ? -40.773 50.545  84.760  1.00 20.32 ? 371  GLY A N     1 
ATOM   2599  C CA    . GLY A  1 373  ? -40.291 51.886  85.053  1.00 19.87 ? 371  GLY A CA    1 
ATOM   2600  C C     . GLY A  1 373  ? -38.837 52.099  84.639  1.00 21.06 ? 371  GLY A C     1 
ATOM   2601  O O     . GLY A  1 373  ? -38.008 51.210  84.693  1.00 24.72 ? 371  GLY A O     1 
ATOM   2602  N N     . ALA A  1 374  ? -38.525 53.332  84.230  1.00 19.12 ? 372  ALA A N     1 
ATOM   2603  C CA    . ALA A  1 374  ? -37.277 53.634  83.539  1.00 25.19 ? 372  ALA A CA    1 
ATOM   2604  C C     . ALA A  1 374  ? -36.283 54.459  84.348  1.00 23.54 ? 372  ALA A C     1 
ATOM   2605  O O     . ALA A  1 374  ? -35.181 54.726  83.851  1.00 22.16 ? 372  ALA A O     1 
ATOM   2606  C CB    . ALA A  1 374  ? -37.576 54.383  82.232  1.00 23.05 ? 372  ALA A CB    1 
ATOM   2607  N N     . TYR A  1 375  ? -36.627 54.871  85.567  1.00 20.49 ? 373  TYR A N     1 
ATOM   2608  C CA    . TYR A  1 375  ? -35.799 55.818  86.307  1.00 19.62 ? 373  TYR A CA    1 
ATOM   2609  C C     . TYR A  1 375  ? -35.254 55.228  87.604  1.00 20.57 ? 373  TYR A C     1 
ATOM   2610  O O     . TYR A  1 375  ? -34.928 55.985  88.521  1.00 20.02 ? 373  TYR A O     1 
ATOM   2611  C CB    . TYR A  1 375  ? -36.577 57.095  86.628  1.00 19.73 ? 373  TYR A CB    1 
ATOM   2612  C CG    . TYR A  1 375  ? -37.143 57.817  85.416  1.00 20.69 ? 373  TYR A CG    1 
ATOM   2613  C CD1   . TYR A  1 375  ? -38.329 57.387  84.813  1.00 22.57 ? 373  TYR A CD1   1 
ATOM   2614  C CD2   . TYR A  1 375  ? -36.499 58.926  84.880  1.00 26.44 ? 373  TYR A CD2   1 
ATOM   2615  C CE1   . TYR A  1 375  ? -38.848 58.037  83.690  1.00 23.96 ? 373  TYR A CE1   1 
ATOM   2616  C CE2   . TYR A  1 375  ? -37.019 59.592  83.760  1.00 29.41 ? 373  TYR A CE2   1 
ATOM   2617  C CZ    . TYR A  1 375  ? -38.192 59.143  83.182  1.00 28.06 ? 373  TYR A CZ    1 
ATOM   2618  O OH    . TYR A  1 375  ? -38.696 59.802  82.067  1.00 31.31 ? 373  TYR A OH    1 
ATOM   2619  N N     . TRP A  1 376  ? -35.140 53.900  87.693  1.00 18.44 ? 374  TRP A N     1 
ATOM   2620  C CA    . TRP A  1 376  ? -34.857 53.252  88.974  1.00 19.35 ? 374  TRP A CA    1 
ATOM   2621  C C     . TRP A  1 376  ? -33.601 53.809  89.645  1.00 22.49 ? 374  TRP A C     1 
ATOM   2622  O O     . TRP A  1 376  ? -33.647 54.232  90.806  1.00 22.04 ? 374  TRP A O     1 
ATOM   2623  C CB    . TRP A  1 376  ? -34.723 51.739  88.779  1.00 19.79 ? 374  TRP A CB    1 
ATOM   2624  C CG    . TRP A  1 376  ? -34.557 51.006  90.082  1.00 19.96 ? 374  TRP A CG    1 
ATOM   2625  C CD1   . TRP A  1 376  ? -35.551 50.666  90.955  1.00 23.12 ? 374  TRP A CD1   1 
ATOM   2626  C CD2   . TRP A  1 376  ? -33.330 50.546  90.671  1.00 24.03 ? 374  TRP A CD2   1 
ATOM   2627  N NE1   . TRP A  1 376  ? -35.021 50.030  92.055  1.00 23.10 ? 374  TRP A NE1   1 
ATOM   2628  C CE2   . TRP A  1 376  ? -33.664 49.928  91.896  1.00 22.97 ? 374  TRP A CE2   1 
ATOM   2629  C CE3   . TRP A  1 376  ? -31.991 50.580  90.275  1.00 27.57 ? 374  TRP A CE3   1 
ATOM   2630  C CZ2   . TRP A  1 376  ? -32.704 49.355  92.735  1.00 23.42 ? 374  TRP A CZ2   1 
ATOM   2631  C CZ3   . TRP A  1 376  ? -31.030 50.013  91.114  1.00 26.04 ? 374  TRP A CZ3   1 
ATOM   2632  C CH2   . TRP A  1 376  ? -31.397 49.405  92.325  1.00 26.67 ? 374  TRP A CH2   1 
ATOM   2633  N N     . ASP A  1 377  ? -32.465 53.794  88.933  1.00 22.28 ? 375  ASP A N     1 
ATOM   2634  C CA    . ASP A  1 377  ? -31.196 54.265  89.498  1.00 25.37 ? 375  ASP A CA    1 
ATOM   2635  C C     . ASP A  1 377  ? -31.315 55.684  90.033  1.00 21.03 ? 375  ASP A C     1 
ATOM   2636  O O     . ASP A  1 377  ? -30.820 56.001  91.121  1.00 19.86 ? 375  ASP A O     1 
ATOM   2637  C CB    . ASP A  1 377  ? -30.092 54.219  88.428  1.00 25.62 ? 375  ASP A CB    1 
ATOM   2638  C CG    . ASP A  1 377  ? -29.556 52.831  88.198  1.00 31.26 ? 375  ASP A CG    1 
ATOM   2639  O OD1   . ASP A  1 377  ? -29.283 52.137  89.196  1.00 43.10 ? 375  ASP A OD1   1 
ATOM   2640  O OD2   . ASP A  1 377  ? -29.398 52.431  87.022  1.00 41.25 ? 375  ASP A OD2   1 
ATOM   2641  N N     . ALA A  1 378  ? -31.959 56.554  89.269  1.00 22.60 ? 376  ALA A N     1 
ATOM   2642  C CA    . ALA A  1 378  ? -32.087 57.942  89.685  1.00 21.36 ? 376  ALA A CA    1 
ATOM   2643  C C     . ALA A  1 378  ? -32.978 58.075  90.914  1.00 19.13 ? 376  ALA A C     1 
ATOM   2644  O O     . ALA A  1 378  ? -32.727 58.946  91.754  1.00 19.67 ? 376  ALA A O     1 
ATOM   2645  C CB    . ALA A  1 378  ? -32.624 58.786  88.521  1.00 22.69 ? 376  ALA A CB    1 
ATOM   2646  N N     . GLU A  1 379  ? -34.010 57.219  91.045  1.00 20.13 ? 377  GLU A N     1 
ATOM   2647  C CA    . GLU A  1 379  ? -34.869 57.283  92.230  1.00 17.91 ? 377  GLU A CA    1 
ATOM   2648  C C     . GLU A  1 379  ? -34.113 56.856  93.480  1.00 18.31 ? 377  GLU A C     1 
ATOM   2649  O O     . GLU A  1 379  ? -34.277 57.463  94.549  1.00 18.66 ? 377  GLU A O     1 
ATOM   2650  C CB    . GLU A  1 379  ? -36.104 56.397  92.077  1.00 17.87 ? 377  GLU A CB    1 
ATOM   2651  C CG    . GLU A  1 379  ? -37.035 56.718  90.866  1.00 19.68 ? 377  GLU A CG    1 
ATOM   2652  C CD    . GLU A  1 379  ? -37.690 58.098  90.934  1.00 22.09 ? 377  GLU A CD    1 
ATOM   2653  O OE1   . GLU A  1 379  ? -37.621 58.781  91.979  1.00 21.70 ? 377  GLU A OE1   1 
ATOM   2654  O OE2   . GLU A  1 379  ? -38.295 58.505  89.922  1.00 21.05 ? 377  GLU A OE2   1 
ATOM   2655  N N     . ILE A  1 380  ? -33.317 55.790  93.374  1.00 17.91 ? 378  ILE A N     1 
ATOM   2656  C CA    . ILE A  1 380  ? -32.524 55.353  94.525  1.00 18.03 ? 378  ILE A CA    1 
ATOM   2657  C C     . ILE A  1 380  ? -31.597 56.473  94.972  1.00 20.90 ? 378  ILE A C     1 
ATOM   2658  O O     . ILE A  1 380  ? -31.520 56.802  96.159  1.00 21.68 ? 378  ILE A O     1 
ATOM   2659  C CB    . ILE A  1 380  ? -31.718 54.089  94.190  1.00 18.96 ? 378  ILE A CB    1 
ATOM   2660  C CG1   . ILE A  1 380  ? -32.629 52.958  93.724  1.00 23.17 ? 378  ILE A CG1   1 
ATOM   2661  C CG2   . ILE A  1 380  ? -30.844 53.686  95.421  1.00 19.55 ? 378  ILE A CG2   1 
ATOM   2662  C CD1   . ILE A  1 380  ? -33.772 52.623  94.686  1.00 20.79 ? 378  ILE A CD1   1 
ATOM   2663  N N     . LYS A  1 381  ? -30.859 57.059  94.021  1.00 17.95 ? 379  LYS A N     1 
ATOM   2664  C CA    . LYS A  1 381  ? -29.911 58.116  94.354  1.00 21.65 ? 379  LYS A CA    1 
ATOM   2665  C C     . LYS A  1 381  ? -30.611 59.324  94.959  1.00 19.79 ? 379  LYS A C     1 
ATOM   2666  O O     . LYS A  1 381  ? -30.136 59.898  95.938  1.00 18.87 ? 379  LYS A O     1 
ATOM   2667  C CB    . LYS A  1 381  ? -29.120 58.538  93.113  1.00 18.45 ? 379  LYS A CB    1 
ATOM   2668  C CG    . LYS A  1 381  ? -28.180 59.712  93.382  1.00 18.85 ? 379  LYS A CG    1 
ATOM   2669  C CD    . LYS A  1 381  ? -27.336 60.039  92.155  1.00 22.27 ? 379  LYS A CD    1 
ATOM   2670  C CE    . LYS A  1 381  ? -26.203 61.045  92.480  1.00 21.84 ? 379  LYS A CE    1 
ATOM   2671  N NZ    . LYS A  1 381  ? -25.422 61.396  91.254  1.00 20.56 ? 379  LYS A NZ    1 
ATOM   2672  N N     . ARG A  1 382  ? -31.739 59.728  94.391  1.00 18.17 ? 380  ARG A N     1 
ATOM   2673  C CA    . ARG A  1 382  ? -32.413 60.932  94.871  1.00 17.71 ? 380  ARG A CA    1 
ATOM   2674  C C     . ARG A  1 382  ? -32.913 60.757  96.297  1.00 18.86 ? 380  ARG A C     1 
ATOM   2675  O O     . ARG A  1 382  ? -32.789 61.673  97.119  1.00 21.33 ? 380  ARG A O     1 
ATOM   2676  C CB    . ARG A  1 382  ? -33.585 61.277  93.940  1.00 23.15 ? 380  ARG A CB    1 
ATOM   2677  C CG    . ARG A  1 382  ? -34.350 62.505  94.361  1.00 27.70 ? 380  ARG A CG    1 
ATOM   2678  C CD    . ARG A  1 382  ? -33.801 63.753  93.699  1.00 39.51 ? 380  ARG A CD    1 
ATOM   2679  N NE    . ARG A  1 382  ? -32.638 64.268  94.407  1.00 36.89 ? 380  ARG A NE    1 
ATOM   2680  C CZ    . ARG A  1 382  ? -31.917 65.307  94.007  1.00 45.79 ? 380  ARG A CZ    1 
ATOM   2681  N NH1   . ARG A  1 382  ? -32.211 65.965  92.895  1.00 51.38 ? 380  ARG A NH1   1 
ATOM   2682  N NH2   . ARG A  1 382  ? -30.876 65.697  94.741  1.00 47.00 ? 380  ARG A NH2   1 
ATOM   2683  N N     . ALA A  1 383  ? -33.496 59.589  96.608  1.00 18.58 ? 381  ALA A N     1 
ATOM   2684  C CA    . ALA A  1 383  ? -34.024 59.371  97.953  1.00 17.97 ? 381  ALA A CA    1 
ATOM   2685  C C     . ALA A  1 383  ? -32.901 59.398  98.971  1.00 18.48 ? 381  ALA A C     1 
ATOM   2686  O O     . ALA A  1 383  ? -33.051 59.960  100.067 1.00 20.40 ? 381  ALA A O     1 
ATOM   2687  C CB    . ALA A  1 383  ? -34.771 58.040  98.038  1.00 19.36 ? 381  ALA A CB    1 
ATOM   2688  N N     . GLN A  1 384  ? -31.757 58.815  98.611  1.00 19.18 ? 382  GLN A N     1 
ATOM   2689  C CA    . GLN A  1 384  ? -30.597 58.857  99.500  1.00 18.77 ? 382  GLN A CA    1 
ATOM   2690  C C     . GLN A  1 384  ? -30.106 60.291  99.695  1.00 21.80 ? 382  GLN A C     1 
ATOM   2691  O O     . GLN A  1 384  ? -29.862 60.720  100.825 1.00 25.17 ? 382  GLN A O     1 
ATOM   2692  C CB    . GLN A  1 384  ? -29.499 57.948  98.945  1.00 18.06 ? 382  GLN A CB    1 
ATOM   2693  C CG    . GLN A  1 384  ? -29.847 56.460  99.110  1.00 22.38 ? 382  GLN A CG    1 
ATOM   2694  C CD    . GLN A  1 384  ? -28.790 55.537  98.539  1.00 22.69 ? 382  GLN A CD    1 
ATOM   2695  O OE1   . GLN A  1 384  ? -27.984 55.942  97.708  1.00 23.70 ? 382  GLN A OE1   1 
ATOM   2696  N NE2   . GLN A  1 384  ? -28.804 54.279  98.971  1.00 24.02 ? 382  GLN A NE2   1 
ATOM   2697  N N     . LEU A  1 385  ? -29.993 61.065  98.612  1.00 20.29 ? 383  LEU A N     1 
ATOM   2698  C CA    . LEU A  1 385  ? -29.546 62.453  98.761  1.00 21.05 ? 383  LEU A CA    1 
ATOM   2699  C C     . LEU A  1 385  ? -30.474 63.254  99.673  1.00 23.66 ? 383  LEU A C     1 
ATOM   2700  O O     . LEU A  1 385  ? -30.015 64.100  100.455 1.00 22.54 ? 383  LEU A O     1 
ATOM   2701  C CB    . LEU A  1 385  ? -29.449 63.125  97.392  1.00 20.78 ? 383  LEU A CB    1 
ATOM   2702  C CG    . LEU A  1 385  ? -28.288 62.680  96.496  1.00 25.33 ? 383  LEU A CG    1 
ATOM   2703  C CD1   . LEU A  1 385  ? -28.385 63.334  95.133  1.00 26.12 ? 383  LEU A CD1   1 
ATOM   2704  C CD2   . LEU A  1 385  ? -26.974 63.009  97.171  1.00 26.48 ? 383  LEU A CD2   1 
ATOM   2705  N N     . ASP A  1 386  ? -31.778 63.027  99.572  1.00 21.61 ? 384  ASP A N     1 
ATOM   2706  C CA    . ASP A  1 386  ? -32.757 63.839  100.281 1.00 20.38 ? 384  ASP A CA    1 
ATOM   2707  C C     . ASP A  1 386  ? -33.069 63.302  101.667 1.00 22.14 ? 384  ASP A C     1 
ATOM   2708  O O     . ASP A  1 386  ? -33.877 63.908  102.380 1.00 19.74 ? 384  ASP A O     1 
ATOM   2709  C CB    . ASP A  1 386  ? -34.046 63.955  99.439  1.00 24.10 ? 384  ASP A CB    1 
ATOM   2710  C CG    . ASP A  1 386  ? -33.830 64.758  98.157  1.00 28.28 ? 384  ASP A CG    1 
ATOM   2711  O OD1   . ASP A  1 386  ? -32.853 65.543  98.100  1.00 29.82 ? 384  ASP A OD1   1 
ATOM   2712  O OD2   . ASP A  1 386  ? -34.626 64.609  97.198  1.00 25.01 ? 384  ASP A OD2   1 
ATOM   2713  N N     . GLY A  1 387  ? -32.443 62.199  102.072 1.00 21.58 ? 385  GLY A N     1 
ATOM   2714  C CA    . GLY A  1 387  ? -32.624 61.693  103.431 1.00 22.51 ? 385  GLY A CA    1 
ATOM   2715  C C     . GLY A  1 387  ? -34.056 61.322  103.746 1.00 21.99 ? 385  GLY A C     1 
ATOM   2716  O O     . GLY A  1 387  ? -34.539 61.574  104.857 1.00 22.79 ? 385  GLY A O     1 
ATOM   2717  N N     . LEU A  1 388  ? -34.759 60.752  102.779 1.00 21.39 ? 386  LEU A N     1 
ATOM   2718  C CA    . LEU A  1 388  ? -36.172 60.486  102.960 1.00 22.46 ? 386  LEU A CA    1 
ATOM   2719  C C     . LEU A  1 388  ? -36.374 59.137  103.641 1.00 25.03 ? 386  LEU A C     1 
ATOM   2720  O O     . LEU A  1 388  ? -35.450 58.329  103.768 1.00 26.37 ? 386  LEU A O     1 
ATOM   2721  C CB    . LEU A  1 388  ? -36.887 60.573  101.613 1.00 20.41 ? 386  LEU A CB    1 
ATOM   2722  C CG    . LEU A  1 388  ? -36.773 61.994  101.053 1.00 23.75 ? 386  LEU A CG    1 
ATOM   2723  C CD1   . LEU A  1 388  ? -37.505 62.130  99.713  1.00 21.40 ? 386  LEU A CD1   1 
ATOM   2724  C CD2   . LEU A  1 388  ? -37.251 63.051  102.072 1.00 23.28 ? 386  LEU A CD2   1 
ATOM   2725  N N     . ALA A  1 389  ? -37.605 58.918  104.109 1.00 23.61 ? 387  ALA A N     1 
ATOM   2726  C CA    . ALA A  1 389  ? -37.897 57.763  104.945 1.00 22.90 ? 387  ALA A CA    1 
ATOM   2727  C C     . ALA A  1 389  ? -37.618 56.451  104.219 1.00 25.09 ? 387  ALA A C     1 
ATOM   2728  O O     . ALA A  1 389  ? -37.128 55.490  104.818 1.00 25.38 ? 387  ALA A O     1 
ATOM   2729  C CB    . ALA A  1 389  ? -39.357 57.828  105.402 1.00 26.10 ? 387  ALA A CB    1 
ATOM   2730  N N     . ASP A  1 390  ? -37.924 56.388  102.931 1.00 20.04 ? 388  ASP A N     1 
ATOM   2731  C CA    . ASP A  1 390  ? -37.772 55.160  102.168 1.00 24.16 ? 388  ASP A CA    1 
ATOM   2732  C C     . ASP A  1 390  ? -37.775 55.546  100.698 1.00 22.01 ? 388  ASP A C     1 
ATOM   2733  O O     . ASP A  1 390  ? -37.890 56.725  100.348 1.00 21.03 ? 388  ASP A O     1 
ATOM   2734  C CB    . ASP A  1 390  ? -38.894 54.166  102.495 1.00 23.87 ? 388  ASP A CB    1 
ATOM   2735  C CG    . ASP A  1 390  ? -38.499 52.711  102.251 1.00 27.52 ? 388  ASP A CG    1 
ATOM   2736  O OD1   . ASP A  1 390  ? -37.720 52.424  101.319 1.00 29.43 ? 388  ASP A OD1   1 
ATOM   2737  O OD2   . ASP A  1 390  ? -38.981 51.847  103.009 1.00 31.41 ? 388  ASP A OD2   1 
ATOM   2738  N N     . PHE A  1 391  ? -37.653 54.548  99.851  1.00 20.24 ? 389  PHE A N     1 
ATOM   2739  C CA    . PHE A  1 391  ? -37.689 54.735  98.414  1.00 19.56 ? 389  PHE A CA    1 
ATOM   2740  C C     . PHE A  1 391  ? -39.127 54.739  97.920  1.00 22.11 ? 389  PHE A C     1 
ATOM   2741  O O     . PHE A  1 391  ? -40.002 54.129  98.539  1.00 20.02 ? 389  PHE A O     1 
ATOM   2742  C CB    . PHE A  1 391  ? -36.900 53.630  97.725  1.00 21.69 ? 389  PHE A CB    1 
ATOM   2743  C CG    . PHE A  1 391  ? -35.459 53.594  98.155  1.00 19.96 ? 389  PHE A CG    1 
ATOM   2744  C CD1   . PHE A  1 391  ? -34.562 54.532  97.664  1.00 20.11 ? 389  PHE A CD1   1 
ATOM   2745  C CD2   . PHE A  1 391  ? -35.014 52.658  99.073  1.00 25.32 ? 389  PHE A CD2   1 
ATOM   2746  C CE1   . PHE A  1 391  ? -33.237 54.529  98.067  1.00 24.19 ? 389  PHE A CE1   1 
ATOM   2747  C CE2   . PHE A  1 391  ? -33.684 52.646  99.475  1.00 22.07 ? 389  PHE A CE2   1 
ATOM   2748  C CZ    . PHE A  1 391  ? -32.800 53.580  98.973  1.00 23.97 ? 389  PHE A CZ    1 
ATOM   2749  N N     . PRO A  1 392  ? -39.378 55.482  96.840  1.00 19.91 ? 390  PRO A N     1 
ATOM   2750  C CA    . PRO A  1 392  ? -40.696 55.467  96.194  1.00 19.74 ? 390  PRO A CA    1 
ATOM   2751  C C     . PRO A  1 392  ? -40.846 54.352  95.174  1.00 21.41 ? 390  PRO A C     1 
ATOM   2752  O O     . PRO A  1 392  ? -41.895 54.262  94.522  1.00 21.89 ? 390  PRO A O     1 
ATOM   2753  C CB    . PRO A  1 392  ? -40.733 56.834  95.495  1.00 18.44 ? 390  PRO A CB    1 
ATOM   2754  C CG    . PRO A  1 392  ? -39.284 56.964  94.996  1.00 18.25 ? 390  PRO A CG    1 
ATOM   2755  C CD    . PRO A  1 392  ? -38.457 56.444  96.203  1.00 19.25 ? 390  PRO A CD    1 
ATOM   2756  N N     . VAL A  1 393  ? -39.813 53.532  95.018  1.00 20.46 ? 391  VAL A N     1 
ATOM   2757  C CA    . VAL A  1 393  ? -39.813 52.391  94.120  1.00 18.90 ? 391  VAL A CA    1 
ATOM   2758  C C     . VAL A  1 393  ? -39.349 51.181  94.914  1.00 23.08 ? 391  VAL A C     1 
ATOM   2759  O O     . VAL A  1 393  ? -38.748 51.303  95.985  1.00 21.56 ? 391  VAL A O     1 
ATOM   2760  C CB    . VAL A  1 393  ? -38.898 52.604  92.888  1.00 20.58 ? 391  VAL A CB    1 
ATOM   2761  C CG1   . VAL A  1 393  ? -39.427 53.748  92.019  1.00 22.20 ? 391  VAL A CG1   1 
ATOM   2762  C CG2   . VAL A  1 393  ? -37.454 52.892  93.344  1.00 19.04 ? 391  VAL A CG2   1 
ATOM   2763  N N     . PHE A  1 394  ? -39.622 50.005  94.367  1.00 20.44 ? 392  PHE A N     1 
ATOM   2764  C CA    . PHE A  1 394  ? -39.100 48.791  94.964  1.00 22.42 ? 392  PHE A CA    1 
ATOM   2765  C C     . PHE A  1 394  ? -37.588 48.729  94.762  1.00 23.81 ? 392  PHE A C     1 
ATOM   2766  O O     . PHE A  1 394  ? -37.022 49.422  93.908  1.00 22.18 ? 392  PHE A O     1 
ATOM   2767  C CB    . PHE A  1 394  ? -39.816 47.580  94.367  1.00 19.92 ? 392  PHE A CB    1 
ATOM   2768  C CG    . PHE A  1 394  ? -41.293 47.599  94.608  1.00 20.87 ? 392  PHE A CG    1 
ATOM   2769  C CD1   . PHE A  1 394  ? -41.793 47.483  95.891  1.00 20.30 ? 392  PHE A CD1   1 
ATOM   2770  C CD2   . PHE A  1 394  ? -42.177 47.789  93.571  1.00 21.44 ? 392  PHE A CD2   1 
ATOM   2771  C CE1   . PHE A  1 394  ? -43.153 47.519  96.134  1.00 22.69 ? 392  PHE A CE1   1 
ATOM   2772  C CE2   . PHE A  1 394  ? -43.539 47.833  93.804  1.00 23.31 ? 392  PHE A CE2   1 
ATOM   2773  C CZ    . PHE A  1 394  ? -44.030 47.689  95.087  1.00 20.40 ? 392  PHE A CZ    1 
ATOM   2774  N N     . THR A  1 395  ? -36.914 47.950  95.615  1.00 22.96 ? 393  THR A N     1 
ATOM   2775  C CA    . THR A  1 395  ? -35.470 47.788  95.498  1.00 25.81 ? 393  THR A CA    1 
ATOM   2776  C C     . THR A  1 395  ? -35.054 46.406  95.010  1.00 23.23 ? 393  THR A C     1 
ATOM   2777  O O     . THR A  1 395  ? -33.867 46.197  94.736  1.00 22.58 ? 393  THR A O     1 
ATOM   2778  C CB    . THR A  1 395  ? -34.763 48.070  96.837  1.00 24.56 ? 393  THR A CB    1 
ATOM   2779  O OG1   . THR A  1 395  ? -35.256 47.175  97.837  1.00 24.88 ? 393  THR A OG1   1 
ATOM   2780  C CG2   . THR A  1 395  ? -34.968 49.513  97.275  1.00 23.69 ? 393  THR A CG2   1 
ATOM   2781  N N     . ARG A  1 396  ? -35.985 45.467  94.896  1.00 25.05 ? 394  ARG A N     1 
ATOM   2782  C CA    . ARG A  1 396  ? -35.728 44.168  94.291  1.00 27.06 ? 394  ARG A CA    1 
ATOM   2783  C C     . ARG A  1 396  ? -36.512 44.072  92.992  1.00 25.25 ? 394  ARG A C     1 
ATOM   2784  O O     . ARG A  1 396  ? -37.710 44.372  92.964  1.00 24.91 ? 394  ARG A O     1 
ATOM   2785  C CB    . ARG A  1 396  ? -36.117 43.024  95.227  1.00 26.92 ? 394  ARG A CB    1 
ATOM   2786  C CG    . ARG A  1 396  ? -35.213 42.881  96.445  1.00 29.63 ? 394  ARG A CG    1 
ATOM   2787  C CD    . ARG A  1 396  ? -35.455 41.555  97.159  1.00 28.28 ? 394  ARG A CD    1 
ATOM   2788  N NE    . ARG A  1 396  ? -34.900 41.552  98.511  1.00 40.63 ? 394  ARG A NE    1 
ATOM   2789  C CZ    . ARG A  1 396  ? -33.839 40.847  98.895  1.00 46.66 ? 394  ARG A CZ    1 
ATOM   2790  N NH1   . ARG A  1 396  ? -33.181 40.069  98.048  1.00 48.99 ? 394  ARG A NH1   1 
ATOM   2791  N NH2   . ARG A  1 396  ? -33.428 40.926  100.162 1.00 35.87 ? 394  ARG A NH2   1 
ATOM   2792  N N     . LYS A  1 397  ? -35.833 43.659  91.925  1.00 24.46 ? 395  LYS A N     1 
ATOM   2793  C CA    . LYS A  1 397  ? -36.489 43.551  90.624  1.00 26.51 ? 395  LYS A CA    1 
ATOM   2794  C C     . LYS A  1 397  ? -37.683 42.608  90.674  1.00 25.74 ? 395  LYS A C     1 
ATOM   2795  O O     . LYS A  1 397  ? -38.693 42.831  89.994  1.00 25.92 ? 395  LYS A O     1 
ATOM   2796  C CB    . LYS A  1 397  ? -35.479 43.093  89.576  1.00 26.33 ? 395  LYS A CB    1 
ATOM   2797  C CG    . LYS A  1 397  ? -35.942 43.292  88.142  1.00 33.13 ? 395  LYS A CG    1 
ATOM   2798  C CD    . LYS A  1 397  ? -36.546 42.019  87.582  1.00 32.80 ? 395  LYS A CD    1 
ATOM   2799  C CE    . LYS A  1 397  ? -37.017 42.226  86.147  1.00 28.53 ? 395  LYS A CE    1 
ATOM   2800  N NZ    . LYS A  1 397  ? -37.560 40.960  85.578  1.00 30.49 ? 395  LYS A NZ    1 
ATOM   2801  N N     . ILE A  1 398  ? -37.589 41.537  91.465  1.00 25.58 ? 396  ILE A N     1 
ATOM   2802  C CA    . ILE A  1 398  ? -38.689 40.588  91.510  1.00 25.86 ? 396  ILE A CA    1 
ATOM   2803  C C     . ILE A  1 398  ? -39.928 41.199  92.162  1.00 24.56 ? 396  ILE A C     1 
ATOM   2804  O O     . ILE A  1 398  ? -41.050 40.767  91.891  1.00 25.39 ? 396  ILE A O     1 
ATOM   2805  C CB    . ILE A  1 398  ? -38.227 39.304  92.231  1.00 27.59 ? 396  ILE A CB    1 
ATOM   2806  C CG1   . ILE A  1 398  ? -39.103 38.121  91.827  1.00 32.83 ? 396  ILE A CG1   1 
ATOM   2807  C CG2   . ILE A  1 398  ? -38.263 39.495  93.725  1.00 28.49 ? 396  ILE A CG2   1 
ATOM   2808  C CD1   . ILE A  1 398  ? -38.561 36.783  92.271  1.00 35.98 ? 396  ILE A CD1   1 
ATOM   2809  N N     . HIS A  1 399  ? -39.754 42.206  93.015  1.00 22.88 ? 397  HIS A N     1 
ATOM   2810  C CA    . HIS A  1 399  ? -40.909 42.880  93.593  1.00 23.18 ? 397  HIS A CA    1 
ATOM   2811  C C     . HIS A  1 399  ? -41.659 43.666  92.528  1.00 22.92 ? 397  HIS A C     1 
ATOM   2812  O O     . HIS A  1 399  ? -42.897 43.633  92.474  1.00 24.43 ? 397  HIS A O     1 
ATOM   2813  C CB    . HIS A  1 399  ? -40.466 43.800  94.724  1.00 21.46 ? 397  HIS A CB    1 
ATOM   2814  C CG    . HIS A  1 399  ? -39.937 43.065  95.916  1.00 25.08 ? 397  HIS A CG    1 
ATOM   2815  N ND1   . HIS A  1 399  ? -39.312 43.699  96.966  1.00 26.85 ? 397  HIS A ND1   1 
ATOM   2816  C CD2   . HIS A  1 399  ? -39.950 41.745  96.224  1.00 26.93 ? 397  HIS A CD2   1 
ATOM   2817  C CE1   . HIS A  1 399  ? -38.957 42.800  97.871  1.00 25.19 ? 397  HIS A CE1   1 
ATOM   2818  N NE2   . HIS A  1 399  ? -39.327 41.607  97.443  1.00 25.81 ? 397  HIS A NE2   1 
ATOM   2819  N N     . THR A  1 400  ? -40.908 44.362  91.671  1.00 24.47 ? 398  THR A N     1 
ATOM   2820  C CA    . THR A  1 400  ? -41.500 45.037  90.522  1.00 24.93 ? 398  THR A CA    1 
ATOM   2821  C C     . THR A  1 400  ? -42.286 44.060  89.650  1.00 23.62 ? 398  THR A C     1 
ATOM   2822  O O     . THR A  1 400  ? -43.379 44.386  89.177  1.00 22.38 ? 398  THR A O     1 
ATOM   2823  C CB    . THR A  1 400  ? -40.391 45.745  89.731  1.00 24.49 ? 398  THR A CB    1 
ATOM   2824  O OG1   . THR A  1 400  ? -39.868 46.827  90.515  1.00 22.51 ? 398  THR A OG1   1 
ATOM   2825  C CG2   . THR A  1 400  ? -40.915 46.298  88.422  1.00 20.58 ? 398  THR A CG2   1 
ATOM   2826  N N     . ASP A  1 401  ? -41.762 42.844  89.445  1.00 25.55 ? 399  ASP A N     1 
ATOM   2827  C CA    . ASP A  1 401  ? -42.481 41.857  88.636  1.00 26.88 ? 399  ASP A CA    1 
ATOM   2828  C C     . ASP A  1 401  ? -43.798 41.442  89.295  1.00 26.65 ? 399  ASP A C     1 
ATOM   2829  O O     . ASP A  1 401  ? -44.827 41.317  88.617  1.00 26.68 ? 399  ASP A O     1 
ATOM   2830  C CB    . ASP A  1 401  ? -41.602 40.629  88.392  1.00 29.18 ? 399  ASP A CB    1 
ATOM   2831  C CG    . ASP A  1 401  ? -40.413 40.911  87.466  1.00 31.12 ? 399  ASP A CG    1 
ATOM   2832  O OD1   . ASP A  1 401  ? -40.487 41.826  86.609  1.00 32.70 ? 399  ASP A OD1   1 
ATOM   2833  O OD2   . ASP A  1 401  ? -39.399 40.189  87.591  1.00 33.83 ? 399  ASP A OD2   1 
ATOM   2834  N N     . VAL A  1 402  ? -43.787 41.207  90.612  1.00 29.25 ? 400  VAL A N     1 
ATOM   2835  C CA    . VAL A  1 402  ? -45.028 40.877  91.310  1.00 25.04 ? 400  VAL A CA    1 
ATOM   2836  C C     . VAL A  1 402  ? -45.996 42.051  91.250  1.00 27.15 ? 400  VAL A C     1 
ATOM   2837  O O     . VAL A  1 402  ? -47.197 41.878  90.985  1.00 23.79 ? 400  VAL A O     1 
ATOM   2838  C CB    . VAL A  1 402  ? -44.736 40.449  92.761  1.00 26.76 ? 400  VAL A CB    1 
ATOM   2839  C CG1   . VAL A  1 402  ? -46.044 40.249  93.528  1.00 30.60 ? 400  VAL A CG1   1 
ATOM   2840  C CG2   . VAL A  1 402  ? -43.923 39.164  92.772  1.00 27.43 ? 400  VAL A CG2   1 
ATOM   2841  N N     . SER A  1 403  ? -45.485 43.268  91.467  1.00 25.76 ? 401  SER A N     1 
ATOM   2842  C CA    . SER A  1 403  ? -46.320 44.461  91.359  1.00 23.66 ? 401  SER A CA    1 
ATOM   2843  C C     . SER A  1 403  ? -46.980 44.536  89.987  1.00 23.94 ? 401  SER A C     1 
ATOM   2844  O O     . SER A  1 403  ? -48.190 44.769  89.875  1.00 24.39 ? 401  SER A O     1 
ATOM   2845  C CB    . SER A  1 403  ? -45.482 45.712  91.630  1.00 23.42 ? 401  SER A CB    1 
ATOM   2846  O OG    . SER A  1 403  ? -46.255 46.900  91.539  1.00 22.07 ? 401  SER A OG    1 
ATOM   2847  N N     . TYR A  1 404  ? -46.199 44.293  88.932  1.00 21.92 ? 402  TYR A N     1 
ATOM   2848  C CA    . TYR A  1 404  ? -46.734 44.369  87.573  1.00 26.67 ? 402  TYR A CA    1 
ATOM   2849  C C     . TYR A  1 404  ? -47.887 43.388  87.371  1.00 24.80 ? 402  TYR A C     1 
ATOM   2850  O O     . TYR A  1 404  ? -48.948 43.751  86.848  1.00 23.81 ? 402  TYR A O     1 
ATOM   2851  C CB    . TYR A  1 404  ? -45.608 44.104  86.571  1.00 24.12 ? 402  TYR A CB    1 
ATOM   2852  C CG    . TYR A  1 404  ? -45.960 44.455  85.150  1.00 23.49 ? 402  TYR A CG    1 
ATOM   2853  C CD1   . TYR A  1 404  ? -46.715 43.587  84.368  1.00 25.78 ? 402  TYR A CD1   1 
ATOM   2854  C CD2   . TYR A  1 404  ? -45.531 45.647  84.589  1.00 23.97 ? 402  TYR A CD2   1 
ATOM   2855  C CE1   . TYR A  1 404  ? -47.042 43.907  83.063  1.00 27.22 ? 402  TYR A CE1   1 
ATOM   2856  C CE2   . TYR A  1 404  ? -45.845 45.973  83.288  1.00 24.42 ? 402  TYR A CE2   1 
ATOM   2857  C CZ    . TYR A  1 404  ? -46.602 45.101  82.528  1.00 23.90 ? 402  TYR A CZ    1 
ATOM   2858  O OH    . TYR A  1 404  ? -46.910 45.443  81.219  1.00 25.65 ? 402  TYR A OH    1 
ATOM   2859  N N     . ILE A  1 405  ? -47.693 42.133  87.777  1.00 22.70 ? 403  ILE A N     1 
ATOM   2860  C CA    . ILE A  1 405  ? -48.743 41.128  87.639  1.00 26.95 ? 403  ILE A CA    1 
ATOM   2861  C C     . ILE A  1 405  ? -49.951 41.502  88.491  1.00 25.86 ? 403  ILE A C     1 
ATOM   2862  O O     . ILE A  1 405  ? -51.103 41.380  88.054  1.00 25.13 ? 403  ILE A O     1 
ATOM   2863  C CB    . ILE A  1 405  ? -48.201 39.733  88.009  1.00 28.70 ? 403  ILE A CB    1 
ATOM   2864  C CG1   . ILE A  1 405  ? -46.952 39.393  87.179  1.00 30.05 ? 403  ILE A CG1   1 
ATOM   2865  C CG2   . ILE A  1 405  ? -49.286 38.677  87.823  1.00 26.52 ? 403  ILE A CG2   1 
ATOM   2866  C CD1   . ILE A  1 405  ? -47.231 39.147  85.714  1.00 33.71 ? 403  ILE A CD1   1 
ATOM   2867  N N     . ALA A  1 406  ? -49.704 41.979  89.712  1.00 26.38 ? 404  ALA A N     1 
ATOM   2868  C CA    . ALA A  1 406  ? -50.801 42.385  90.584  1.00 28.82 ? 404  ALA A CA    1 
ATOM   2869  C C     . ALA A  1 406  ? -51.610 43.507  89.947  1.00 27.22 ? 404  ALA A C     1 
ATOM   2870  O O     . ALA A  1 406  ? -52.844 43.486  89.959  1.00 29.22 ? 404  ALA A O     1 
ATOM   2871  C CB    . ALA A  1 406  ? -50.253 42.832  91.938  1.00 28.05 ? 404  ALA A CB    1 
ATOM   2872  N N     . CYS A  1 407  ? -50.920 44.501  89.386  1.00 25.80 ? 405  CYS A N     1 
ATOM   2873  C CA    . CYS A  1 407  ? -51.610 45.639  88.798  1.00 22.03 ? 405  CYS A CA    1 
ATOM   2874  C C     . CYS A  1 407  ? -52.308 45.252  87.505  1.00 26.77 ? 405  CYS A C     1 
ATOM   2875  O O     . CYS A  1 407  ? -53.380 45.785  87.204  1.00 23.89 ? 405  CYS A O     1 
ATOM   2876  C CB    . CYS A  1 407  ? -50.624 46.777  88.575  1.00 22.85 ? 405  CYS A CB    1 
ATOM   2877  S SG    . CYS A  1 407  ? -50.089 47.496  90.155  1.00 28.03 ? 405  CYS A SG    1 
ATOM   2878  N N     . ALA A  1 408  ? -51.715 44.332  86.738  1.00 26.63 ? 406  ALA A N     1 
ATOM   2879  C CA    . ALA A  1 408  ? -52.377 43.814  85.547  1.00 26.76 ? 406  ALA A CA    1 
ATOM   2880  C C     . ALA A  1 408  ? -53.682 43.111  85.903  1.00 25.96 ? 406  ALA A C     1 
ATOM   2881  O O     . ALA A  1 408  ? -54.675 43.237  85.181  1.00 26.82 ? 406  ALA A O     1 
ATOM   2882  C CB    . ALA A  1 408  ? -51.444 42.865  84.798  1.00 26.45 ? 406  ALA A CB    1 
ATOM   2883  N N     . ALA A  1 409  ? -53.701 42.369  87.011  1.00 26.46 ? 407  ALA A N     1 
ATOM   2884  C CA    . ALA A  1 409  ? -54.942 41.761  87.477  1.00 28.57 ? 407  ALA A CA    1 
ATOM   2885  C C     . ALA A  1 409  ? -56.008 42.814  87.745  1.00 27.16 ? 407  ALA A C     1 
ATOM   2886  O O     . ALA A  1 409  ? -57.176 42.635  87.388  1.00 27.10 ? 407  ALA A O     1 
ATOM   2887  C CB    . ALA A  1 409  ? -54.680 40.930  88.734  1.00 29.08 ? 407  ALA A CB    1 
ATOM   2888  N N     . LYS A  1 410  ? -55.626 43.919  88.381  1.00 26.46 ? 408  LYS A N     1 
ATOM   2889  C CA    . LYS A  1 410  ? -56.592 44.973  88.650  1.00 23.30 ? 408  LYS A CA    1 
ATOM   2890  C C     . LYS A  1 410  ? -57.106 45.572  87.353  1.00 25.44 ? 408  LYS A C     1 
ATOM   2891  O O     . LYS A  1 410  ? -58.304 45.851  87.217  1.00 26.65 ? 408  LYS A O     1 
ATOM   2892  C CB    . LYS A  1 410  ? -55.953 46.047  89.523  1.00 27.10 ? 408  LYS A CB    1 
ATOM   2893  C CG    . LYS A  1 410  ? -56.866 47.193  89.878  1.00 27.97 ? 408  LYS A CG    1 
ATOM   2894  C CD    . LYS A  1 410  ? -56.068 48.257  90.611  1.00 28.51 ? 408  LYS A CD    1 
ATOM   2895  C CE    . LYS A  1 410  ? -55.579 47.742  91.945  1.00 27.99 ? 408  LYS A CE    1 
ATOM   2896  N NZ    . LYS A  1 410  ? -56.722 47.609  92.900  1.00 28.53 ? 408  LYS A NZ    1 
ATOM   2897  N N     . LEU A  1 411  ? -56.206 45.761  86.386  1.00 25.35 ? 409  LEU A N     1 
ATOM   2898  C CA    . LEU A  1 411  ? -56.589 46.348  85.107  1.00 21.71 ? 409  LEU A CA    1 
ATOM   2899  C C     . LEU A  1 411  ? -57.505 45.422  84.318  1.00 24.54 ? 409  LEU A C     1 
ATOM   2900  O O     . LEU A  1 411  ? -58.465 45.879  83.682  1.00 24.58 ? 409  LEU A O     1 
ATOM   2901  C CB    . LEU A  1 411  ? -55.331 46.670  84.299  1.00 25.50 ? 409  LEU A CB    1 
ATOM   2902  C CG    . LEU A  1 411  ? -54.653 47.997  84.635  1.00 23.99 ? 409  LEU A CG    1 
ATOM   2903  C CD1   . LEU A  1 411  ? -53.285 48.058  83.978  1.00 26.16 ? 409  LEU A CD1   1 
ATOM   2904  C CD2   . LEU A  1 411  ? -55.530 49.145  84.164  1.00 20.83 ? 409  LEU A CD2   1 
ATOM   2905  N N     . LEU A  1 412  ? -57.211 44.123  84.326  1.00 24.52 ? 410  LEU A N     1 
ATOM   2906  C CA    . LEU A  1 412  ? -58.036 43.178  83.577  1.00 27.32 ? 410  LEU A CA    1 
ATOM   2907  C C     . LEU A  1 412  ? -59.438 43.038  84.153  1.00 26.84 ? 410  LEU A C     1 
ATOM   2908  O O     . LEU A  1 412  ? -60.348 42.628  83.431  1.00 29.77 ? 410  LEU A O     1 
ATOM   2909  C CB    . LEU A  1 412  ? -57.345 41.814  83.513  1.00 24.32 ? 410  LEU A CB    1 
ATOM   2910  C CG    . LEU A  1 412  ? -56.128 41.751  82.573  1.00 25.74 ? 410  LEU A CG    1 
ATOM   2911  C CD1   . LEU A  1 412  ? -55.413 40.427  82.653  1.00 29.25 ? 410  LEU A CD1   1 
ATOM   2912  C CD2   . LEU A  1 412  ? -56.551 42.027  81.134  1.00 28.80 ? 410  LEU A CD2   1 
ATOM   2913  N N     . ALA A  1 413  ? -59.641 43.376  85.421  1.00 24.42 ? 411  ALA A N     1 
ATOM   2914  C CA    . ALA A  1 413  ? -60.981 43.380  85.985  1.00 31.23 ? 411  ALA A CA    1 
ATOM   2915  C C     . ALA A  1 413  ? -61.752 44.634  85.622  1.00 30.40 ? 411  ALA A C     1 
ATOM   2916  O O     . ALA A  1 413  ? -62.921 44.754  85.999  1.00 28.35 ? 411  ALA A O     1 
ATOM   2917  C CB    . ALA A  1 413  ? -60.926 43.240  87.510  1.00 29.67 ? 411  ALA A CB    1 
ATOM   2918  N N     . ALA A  1 414  ? -61.129 45.572  84.907  1.00 26.88 ? 412  ALA A N     1 
ATOM   2919  C CA    . ALA A  1 414  ? -61.754 46.861  84.665  1.00 27.13 ? 412  ALA A CA    1 
ATOM   2920  C C     . ALA A  1 414  ? -61.726 47.227  83.187  1.00 26.31 ? 412  ALA A C     1 
ATOM   2921  O O     . ALA A  1 414  ? -61.733 48.409  82.845  1.00 25.09 ? 412  ALA A O     1 
ATOM   2922  C CB    . ALA A  1 414  ? -61.076 47.948  85.501  1.00 28.44 ? 412  ALA A CB    1 
ATOM   2923  N N     . THR A  1 415  ? -61.700 46.230  82.296  1.00 25.21 ? 413  THR A N     1 
ATOM   2924  C CA    . THR A  1 415  ? -61.591 46.535  80.871  1.00 27.69 ? 413  THR A CA    1 
ATOM   2925  C C     . THR A  1 415  ? -62.833 47.202  80.305  1.00 28.98 ? 413  THR A C     1 
ATOM   2926  O O     . THR A  1 415  ? -62.770 47.741  79.199  1.00 28.02 ? 413  THR A O     1 
ATOM   2927  C CB    . THR A  1 415  ? -61.281 45.278  80.044  1.00 30.40 ? 413  THR A CB    1 
ATOM   2928  O OG1   . THR A  1 415  ? -62.267 44.267  80.286  1.00 29.43 ? 413  THR A OG1   1 
ATOM   2929  C CG2   . THR A  1 415  ? -59.883 44.751  80.371  1.00 28.02 ? 413  THR A CG2   1 
ATOM   2930  N N     . ASP A  1 416  ? -63.952 47.191  81.024  1.00 30.08 ? 414  ASP A N     1 
ATOM   2931  C CA    . ASP A  1 416  ? -65.109 47.932  80.549  1.00 31.64 ? 414  ASP A CA    1 
ATOM   2932  C C     . ASP A  1 416  ? -64.928 49.441  80.695  1.00 30.57 ? 414  ASP A C     1 
ATOM   2933  O O     . ASP A  1 416  ? -65.546 50.197  79.941  1.00 28.58 ? 414  ASP A O     1 
ATOM   2934  C CB    . ASP A  1 416  ? -66.371 47.469  81.283  1.00 31.88 ? 414  ASP A CB    1 
ATOM   2935  C CG    . ASP A  1 416  ? -66.276 47.662  82.781  1.00 38.06 ? 414  ASP A CG    1 
ATOM   2936  O OD1   . ASP A  1 416  ? -65.163 47.492  83.342  1.00 38.65 ? 414  ASP A OD1   1 
ATOM   2937  O OD2   . ASP A  1 416  ? -67.312 47.987  83.400  1.00 46.32 ? 414  ASP A OD2   1 
ATOM   2938  N N     . VAL A  1 417  ? -64.081 49.907  81.612  1.00 26.21 ? 415  VAL A N     1 
ATOM   2939  C CA    . VAL A  1 417  ? -63.927 51.343  81.811  1.00 30.83 ? 415  VAL A CA    1 
ATOM   2940  C C     . VAL A  1 417  ? -62.531 51.861  81.490  1.00 25.66 ? 415  VAL A C     1 
ATOM   2941  O O     . VAL A  1 417  ? -62.364 53.085  81.352  1.00 27.09 ? 415  VAL A O     1 
ATOM   2942  C CB    . VAL A  1 417  ? -64.334 51.762  83.238  1.00 28.05 ? 415  VAL A CB    1 
ATOM   2943  C CG1   . VAL A  1 417  ? -65.792 51.381  83.498  1.00 34.24 ? 415  VAL A CG1   1 
ATOM   2944  C CG2   . VAL A  1 417  ? -63.418 51.132  84.265  1.00 30.75 ? 415  VAL A CG2   1 
ATOM   2945  N N     . VAL A  1 418  ? -61.511 51.007  81.388  1.00 24.23 ? 416  VAL A N     1 
ATOM   2946  C CA    . VAL A  1 418  ? -60.196 51.424  80.917  1.00 21.31 ? 416  VAL A CA    1 
ATOM   2947  C C     . VAL A  1 418  ? -59.721 50.436  79.861  1.00 22.40 ? 416  VAL A C     1 
ATOM   2948  O O     . VAL A  1 418  ? -60.220 49.316  79.748  1.00 26.60 ? 416  VAL A O     1 
ATOM   2949  C CB    . VAL A  1 418  ? -59.149 51.547  82.057  1.00 20.89 ? 416  VAL A CB    1 
ATOM   2950  C CG1   . VAL A  1 418  ? -59.613 52.546  83.111  1.00 24.34 ? 416  VAL A CG1   1 
ATOM   2951  C CG2   . VAL A  1 418  ? -58.874 50.198  82.704  1.00 21.13 ? 416  VAL A CG2   1 
ATOM   2952  N N     . PHE A  1 419  ? -58.768 50.890  79.057  1.00 20.96 ? 417  PHE A N     1 
ATOM   2953  C CA    . PHE A  1 419  ? -58.117 50.079  78.034  1.00 21.42 ? 417  PHE A CA    1 
ATOM   2954  C C     . PHE A  1 419  ? -56.716 49.751  78.525  1.00 22.56 ? 417  PHE A C     1 
ATOM   2955  O O     . PHE A  1 419  ? -55.826 50.612  78.467  1.00 22.61 ? 417  PHE A O     1 
ATOM   2956  C CB    . PHE A  1 419  ? -58.056 50.833  76.700  1.00 23.66 ? 417  PHE A CB    1 
ATOM   2957  C CG    . PHE A  1 419  ? -57.320 50.098  75.611  1.00 24.20 ? 417  PHE A CG    1 
ATOM   2958  C CD1   . PHE A  1 419  ? -57.765 48.864  75.170  1.00 25.83 ? 417  PHE A CD1   1 
ATOM   2959  C CD2   . PHE A  1 419  ? -56.185 50.647  75.023  1.00 20.78 ? 417  PHE A CD2   1 
ATOM   2960  C CE1   . PHE A  1 419  ? -57.093 48.184  74.171  1.00 24.74 ? 417  PHE A CE1   1 
ATOM   2961  C CE2   . PHE A  1 419  ? -55.516 49.979  74.022  1.00 22.29 ? 417  PHE A CE2   1 
ATOM   2962  C CZ    . PHE A  1 419  ? -55.963 48.741  73.596  1.00 24.76 ? 417  PHE A CZ    1 
ATOM   2963  N N     . PRO A  1 420  ? -56.462 48.545  79.034  1.00 21.83 ? 418  PRO A N     1 
ATOM   2964  C CA    . PRO A  1 420  ? -55.116 48.240  79.534  1.00 20.95 ? 418  PRO A CA    1 
ATOM   2965  C C     . PRO A  1 420  ? -54.146 47.970  78.394  1.00 23.24 ? 418  PRO A C     1 
ATOM   2966  O O     . PRO A  1 420  ? -54.502 47.397  77.359  1.00 22.69 ? 418  PRO A O     1 
ATOM   2967  C CB    . PRO A  1 420  ? -55.331 46.994  80.404  1.00 21.62 ? 418  PRO A CB    1 
ATOM   2968  C CG    . PRO A  1 420  ? -56.841 46.966  80.676  1.00 23.81 ? 418  PRO A CG    1 
ATOM   2969  C CD    . PRO A  1 420  ? -57.430 47.502  79.406  1.00 21.48 ? 418  PRO A CD    1 
ATOM   2970  N N     . GLN A  1 421  ? -52.904 48.397  78.602  1.00 21.36 ? 419  GLN A N     1 
ATOM   2971  C CA    . GLN A  1 421  ? -51.833 48.294  77.617  1.00 20.56 ? 419  GLN A CA    1 
ATOM   2972  C C     . GLN A  1 421  ? -50.612 47.762  78.346  1.00 23.70 ? 419  GLN A C     1 
ATOM   2973  O O     . GLN A  1 421  ? -49.981 48.497  79.113  1.00 23.56 ? 419  GLN A O     1 
ATOM   2974  C CB    . GLN A  1 421  ? -51.546 49.655  76.981  1.00 21.97 ? 419  GLN A CB    1 
ATOM   2975  C CG    . GLN A  1 421  ? -52.748 50.211  76.212  1.00 20.64 ? 419  GLN A CG    1 
ATOM   2976  C CD    . GLN A  1 421  ? -52.597 51.697  75.909  1.00 22.97 ? 419  GLN A CD    1 
ATOM   2977  O OE1   . GLN A  1 421  ? -52.390 52.505  76.812  1.00 22.51 ? 419  GLN A OE1   1 
ATOM   2978  N NE2   . GLN A  1 421  ? -52.680 52.056  74.633  1.00 20.08 ? 419  GLN A NE2   1 
ATOM   2979  N N     . PHE A  1 422  ? -50.295 46.489  78.129  1.00 20.80 ? 420  PHE A N     1 
ATOM   2980  C CA    . PHE A  1 422  ? -49.278 45.808  78.933  1.00 20.99 ? 420  PHE A CA    1 
ATOM   2981  C C     . PHE A  1 422  ? -47.942 45.892  78.205  1.00 24.23 ? 420  PHE A C     1 
ATOM   2982  O O     . PHE A  1 422  ? -47.627 45.081  77.334  1.00 24.42 ? 420  PHE A O     1 
ATOM   2983  C CB    . PHE A  1 422  ? -49.705 44.372  79.214  1.00 25.58 ? 420  PHE A CB    1 
ATOM   2984  C CG    . PHE A  1 422  ? -51.007 44.275  79.965  1.00 27.21 ? 420  PHE A CG    1 
ATOM   2985  C CD1   . PHE A  1 422  ? -51.101 44.730  81.273  1.00 27.93 ? 420  PHE A CD1   1 
ATOM   2986  C CD2   . PHE A  1 422  ? -52.144 43.757  79.353  1.00 25.42 ? 420  PHE A CD2   1 
ATOM   2987  C CE1   . PHE A  1 422  ? -52.300 44.660  81.961  1.00 25.82 ? 420  PHE A CE1   1 
ATOM   2988  C CE2   . PHE A  1 422  ? -53.339 43.688  80.036  1.00 26.47 ? 420  PHE A CE2   1 
ATOM   2989  C CZ    . PHE A  1 422  ? -53.420 44.135  81.343  1.00 26.16 ? 420  PHE A CZ    1 
ATOM   2990  N N     . ALA A  1 423  ? -47.147 46.896  78.582  1.00 22.47 ? 421  ALA A N     1 
ATOM   2991  C CA    . ALA A  1 423  ? -45.849 47.167  77.971  1.00 20.55 ? 421  ALA A CA    1 
ATOM   2992  C C     . ALA A  1 423  ? -44.807 46.313  78.677  1.00 28.00 ? 421  ALA A C     1 
ATOM   2993  O O     . ALA A  1 423  ? -44.450 46.597  79.827  1.00 26.81 ? 421  ALA A O     1 
ATOM   2994  C CB    . ALA A  1 423  ? -45.499 48.651  78.080  1.00 20.84 ? 421  ALA A CB    1 
ATOM   2995  N N     . THR A  1 424  ? -44.320 45.270  77.999  1.00 25.45 ? 422  THR A N     1 
ATOM   2996  C CA    . THR A  1 424  ? -43.255 44.456  78.582  1.00 25.68 ? 422  THR A CA    1 
ATOM   2997  C C     . THR A  1 424  ? -42.568 43.622  77.504  1.00 30.17 ? 422  THR A C     1 
ATOM   2998  O O     . THR A  1 424  ? -43.189 43.215  76.514  1.00 29.04 ? 422  THR A O     1 
ATOM   2999  C CB    . THR A  1 424  ? -43.775 43.537  79.696  1.00 32.54 ? 422  THR A CB    1 
ATOM   3000  O OG1   . THR A  1 424  ? -42.659 42.897  80.339  1.00 32.92 ? 422  THR A OG1   1 
ATOM   3001  C CG2   . THR A  1 424  ? -44.731 42.477  79.141  1.00 27.45 ? 422  THR A CG2   1 
ATOM   3002  N N     . HIS A  1 425  ? -41.266 43.395  77.707  1.00 27.17 ? 423  HIS A N     1 
ATOM   3003  C CA    . HIS A  1 425  ? -40.466 42.496  76.888  1.00 31.16 ? 423  HIS A CA    1 
ATOM   3004  C C     . HIS A  1 425  ? -40.191 41.180  77.594  1.00 34.03 ? 423  HIS A C     1 
ATOM   3005  O O     . HIS A  1 425  ? -39.429 40.359  77.078  1.00 36.06 ? 423  HIS A O     1 
ATOM   3006  C CB    . HIS A  1 425  ? -39.134 43.159  76.508  1.00 32.35 ? 423  HIS A CB    1 
ATOM   3007  C CG    . HIS A  1 425  ? -39.284 44.372  75.643  1.00 30.15 ? 423  HIS A CG    1 
ATOM   3008  N ND1   . HIS A  1 425  ? -38.543 45.519  75.831  1.00 33.75 ? 423  HIS A ND1   1 
ATOM   3009  C CD2   . HIS A  1 425  ? -40.113 44.625  74.601  1.00 30.24 ? 423  HIS A CD2   1 
ATOM   3010  C CE1   . HIS A  1 425  ? -38.898 46.421  74.931  1.00 34.08 ? 423  HIS A CE1   1 
ATOM   3011  N NE2   . HIS A  1 425  ? -39.845 45.901  74.170  1.00 28.31 ? 423  HIS A NE2   1 
ATOM   3012  N N     . ASN A  1 426  ? -40.783 40.973  78.765  1.00 31.20 ? 424  ASN A N     1 
ATOM   3013  C CA    . ASN A  1 426  ? -40.507 39.811  79.601  1.00 34.02 ? 424  ASN A CA    1 
ATOM   3014  C C     . ASN A  1 426  ? -41.505 38.721  79.226  1.00 33.10 ? 424  ASN A C     1 
ATOM   3015  O O     . ASN A  1 426  ? -42.711 38.874  79.441  1.00 34.50 ? 424  ASN A O     1 
ATOM   3016  C CB    . ASN A  1 426  ? -40.600 40.204  81.074  1.00 29.27 ? 424  ASN A CB    1 
ATOM   3017  C CG    . ASN A  1 426  ? -40.254 39.071  82.022  1.00 34.57 ? 424  ASN A CG    1 
ATOM   3018  O OD1   . ASN A  1 426  ? -40.644 37.923  81.813  1.00 33.53 ? 424  ASN A OD1   1 
ATOM   3019  N ND2   . ASN A  1 426  ? -39.537 39.403  83.099  1.00 27.50 ? 424  ASN A ND2   1 
ATOM   3020  N N     . ALA A  1 427  ? -41.002 37.624  78.657  1.00 32.42 ? 425  ALA A N     1 
ATOM   3021  C CA    . ALA A  1 427  ? -41.894 36.578  78.165  1.00 34.06 ? 425  ALA A CA    1 
ATOM   3022  C C     . ALA A  1 427  ? -42.690 35.926  79.288  1.00 34.57 ? 425  ALA A C     1 
ATOM   3023  O O     . ALA A  1 427  ? -43.811 35.467  79.056  1.00 29.99 ? 425  ALA A O     1 
ATOM   3024  C CB    . ALA A  1 427  ? -41.099 35.516  77.399  1.00 37.40 ? 425  ALA A CB    1 
ATOM   3025  N N     . GLN A  1 428  ? -42.131 35.866  80.501  1.00 33.13 ? 426  GLN A N     1 
ATOM   3026  C CA    . GLN A  1 428  ? -42.860 35.290  81.629  1.00 34.06 ? 426  GLN A CA    1 
ATOM   3027  C C     . GLN A  1 428  ? -44.003 36.200  82.063  1.00 33.74 ? 426  GLN A C     1 
ATOM   3028  O O     . GLN A  1 428  ? -45.114 35.728  82.336  1.00 31.42 ? 426  GLN A O     1 
ATOM   3029  C CB    . GLN A  1 428  ? -41.897 35.032  82.796  1.00 35.17 ? 426  GLN A CB    1 
ATOM   3030  C CG    . GLN A  1 428  ? -42.425 34.091  83.868  1.00 35.60 ? 426  GLN A CG    1 
ATOM   3031  C CD    . GLN A  1 428  ? -43.475 34.730  84.757  1.00 36.71 ? 426  GLN A CD    1 
ATOM   3032  O OE1   . GLN A  1 428  ? -43.394 35.917  85.076  1.00 38.17 ? 426  GLN A OE1   1 
ATOM   3033  N NE2   . GLN A  1 428  ? -44.478 33.950  85.144  1.00 32.81 ? 426  GLN A NE2   1 
ATOM   3034  N N     . THR A  1 429  ? -43.738 37.508  82.149  1.00 37.30 ? 427  THR A N     1 
ATOM   3035  C CA    . THR A  1 429  ? -44.790 38.480  82.436  1.00 29.63 ? 427  THR A CA    1 
ATOM   3036  C C     . THR A  1 429  ? -45.913 38.387  81.406  1.00 32.70 ? 427  THR A C     1 
ATOM   3037  O O     . THR A  1 429  ? -47.099 38.281  81.754  1.00 31.77 ? 427  THR A O     1 
ATOM   3038  C CB    . THR A  1 429  ? -44.187 39.887  82.454  1.00 33.69 ? 427  THR A CB    1 
ATOM   3039  O OG1   . THR A  1 429  ? -43.018 39.906  83.289  1.00 34.61 ? 427  THR A OG1   1 
ATOM   3040  C CG2   . THR A  1 429  ? -45.192 40.881  82.981  1.00 30.10 ? 427  THR A CG2   1 
ATOM   3041  N N     . LEU A  1 430  ? -45.542 38.409  80.124  1.00 29.93 ? 428  LEU A N     1 
ATOM   3042  C CA    . LEU A  1 430  ? -46.501 38.281  79.032  1.00 28.92 ? 428  LEU A CA    1 
ATOM   3043  C C     . LEU A  1 430  ? -47.372 37.041  79.194  1.00 31.86 ? 428  LEU A C     1 
ATOM   3044  O O     . LEU A  1 430  ? -48.605 37.119  79.127  1.00 34.08 ? 428  LEU A O     1 
ATOM   3045  C CB    . LEU A  1 430  ? -45.738 38.237  77.705  1.00 29.71 ? 428  LEU A CB    1 
ATOM   3046  C CG    . LEU A  1 430  ? -46.429 38.417  76.347  1.00 33.00 ? 428  LEU A CG    1 
ATOM   3047  C CD1   . LEU A  1 430  ? -45.341 38.585  75.300  1.00 33.17 ? 428  LEU A CD1   1 
ATOM   3048  C CD2   . LEU A  1 430  ? -47.321 37.254  75.971  1.00 33.53 ? 428  LEU A CD2   1 
ATOM   3049  N N     . ALA A  1 431  ? -46.741 35.879  79.393  1.00 32.25 ? 429  ALA A N     1 
ATOM   3050  C CA    . ALA A  1 431  ? -47.499 34.635  79.494  1.00 31.00 ? 429  ALA A CA    1 
ATOM   3051  C C     . ALA A  1 431  ? -48.457 34.668  80.677  1.00 30.17 ? 429  ALA A C     1 
ATOM   3052  O O     . ALA A  1 431  ? -49.607 34.228  80.567  1.00 30.11 ? 429  ALA A O     1 
ATOM   3053  C CB    . ALA A  1 431  ? -46.544 33.445  79.612  1.00 35.00 ? 429  ALA A CB    1 
ATOM   3054  N N     . ALA A  1 432  ? -47.999 35.195  81.815  1.00 31.00 ? 430  ALA A N     1 
ATOM   3055  C CA    . ALA A  1 432  ? -48.850 35.263  82.997  1.00 29.81 ? 430  ALA A CA    1 
ATOM   3056  C C     . ALA A  1 432  ? -50.101 36.094  82.728  1.00 29.03 ? 430  ALA A C     1 
ATOM   3057  O O     . ALA A  1 432  ? -51.212 35.701  83.100  1.00 32.89 ? 430  ALA A O     1 
ATOM   3058  C CB    . ALA A  1 432  ? -48.052 35.840  84.170  1.00 30.06 ? 430  ALA A CB    1 
ATOM   3059  N N     . ILE A  1 433  ? -49.939 37.233  82.056  1.00 32.36 ? 431  ILE A N     1 
ATOM   3060  C CA    . ILE A  1 433  ? -51.063 38.114  81.769  1.00 31.04 ? 431  ILE A CA    1 
ATOM   3061  C C     . ILE A  1 433  ? -51.964 37.500  80.715  1.00 31.78 ? 431  ILE A C     1 
ATOM   3062  O O     . ILE A  1 433  ? -53.196 37.527  80.834  1.00 30.23 ? 431  ILE A O     1 
ATOM   3063  C CB    . ILE A  1 433  ? -50.539 39.491  81.325  1.00 29.82 ? 431  ILE A CB    1 
ATOM   3064  C CG1   . ILE A  1 433  ? -49.820 40.169  82.484  1.00 26.97 ? 431  ILE A CG1   1 
ATOM   3065  C CG2   . ILE A  1 433  ? -51.664 40.339  80.782  1.00 30.85 ? 431  ILE A CG2   1 
ATOM   3066  C CD1   . ILE A  1 433  ? -49.415 41.577  82.193  1.00 33.04 ? 431  ILE A CD1   1 
ATOM   3067  N N     . TYR A  1 434  ? -51.361 36.956  79.659  1.00 31.46 ? 432  TYR A N     1 
ATOM   3068  C CA    . TYR A  1 434  ? -52.125 36.309  78.599  1.00 32.22 ? 432  TYR A CA    1 
ATOM   3069  C C     . TYR A  1 434  ? -53.071 35.252  79.164  1.00 34.53 ? 432  TYR A C     1 
ATOM   3070  O O     . TYR A  1 434  ? -54.257 35.211  78.815  1.00 30.23 ? 432  TYR A O     1 
ATOM   3071  C CB    . TYR A  1 434  ? -51.153 35.708  77.580  1.00 32.71 ? 432  TYR A CB    1 
ATOM   3072  C CG    . TYR A  1 434  ? -51.787 34.833  76.533  1.00 33.71 ? 432  TYR A CG    1 
ATOM   3073  C CD1   . TYR A  1 434  ? -52.560 35.374  75.512  1.00 32.89 ? 432  TYR A CD1   1 
ATOM   3074  C CD2   . TYR A  1 434  ? -51.588 33.458  76.551  1.00 35.34 ? 432  TYR A CD2   1 
ATOM   3075  C CE1   . TYR A  1 434  ? -53.142 34.555  74.546  1.00 34.50 ? 432  TYR A CE1   1 
ATOM   3076  C CE2   . TYR A  1 434  ? -52.152 32.640  75.596  1.00 35.22 ? 432  TYR A CE2   1 
ATOM   3077  C CZ    . TYR A  1 434  ? -52.928 33.187  74.598  1.00 39.06 ? 432  TYR A CZ    1 
ATOM   3078  O OH    . TYR A  1 434  ? -53.485 32.350  73.657  1.00 44.74 ? 432  TYR A OH    1 
ATOM   3079  N N     . HIS A  1 435  ? -52.573 34.396  80.061  1.00 30.98 ? 433  HIS A N     1 
ATOM   3080  C CA    . HIS A  1 435  ? -53.457 33.384  80.630  1.00 32.13 ? 433  HIS A CA    1 
ATOM   3081  C C     . HIS A  1 435  ? -54.394 33.975  81.676  1.00 36.41 ? 433  HIS A C     1 
ATOM   3082  O O     . HIS A  1 435  ? -55.508 33.471  81.864  1.00 34.60 ? 433  HIS A O     1 
ATOM   3083  C CB    . HIS A  1 435  ? -52.637 32.232  81.215  1.00 33.46 ? 433  HIS A CB    1 
ATOM   3084  C CG    . HIS A  1 435  ? -52.102 31.300  80.174  1.00 35.74 ? 433  HIS A CG    1 
ATOM   3085  N ND1   . HIS A  1 435  ? -52.890 30.360  79.545  1.00 37.98 ? 433  HIS A ND1   1 
ATOM   3086  C CD2   . HIS A  1 435  ? -50.871 31.191  79.621  1.00 39.64 ? 433  HIS A CD2   1 
ATOM   3087  C CE1   . HIS A  1 435  ? -52.164 29.703  78.658  1.00 34.82 ? 433  HIS A CE1   1 
ATOM   3088  N NE2   . HIS A  1 435  ? -50.934 30.181  78.691  1.00 34.23 ? 433  HIS A NE2   1 
ATOM   3089  N N     . MET A  1 436  ? -53.969 35.045  82.355  1.00 34.24 ? 434  MET A N     1 
ATOM   3090  C CA    . MET A  1 436  ? -54.849 35.698  83.317  1.00 33.97 ? 434  MET A CA    1 
ATOM   3091  C C     . MET A  1 436  ? -56.068 36.285  82.622  1.00 34.91 ? 434  MET A C     1 
ATOM   3092  O O     . MET A  1 436  ? -57.180 36.248  83.161  1.00 35.76 ? 434  MET A O     1 
ATOM   3093  C CB    . MET A  1 436  ? -54.083 36.787  84.071  1.00 31.02 ? 434  MET A CB    1 
ATOM   3094  C CG    . MET A  1 436  ? -54.940 37.582  85.033  1.00 33.26 ? 434  MET A CG    1 
ATOM   3095  S SD    . MET A  1 436  ? -54.014 38.851  85.921  1.00 37.77 ? 434  MET A SD    1 
ATOM   3096  C CE    . MET A  1 436  ? -52.855 37.845  86.839  1.00 34.76 ? 434  MET A CE    1 
ATOM   3097  N N     . ALA A  1 437  ? -55.879 36.809  81.408  1.00 32.62 ? 435  ALA A N     1 
ATOM   3098  C CA    . ALA A  1 437  ? -56.952 37.499  80.703  1.00 36.12 ? 435  ALA A CA    1 
ATOM   3099  C C     . ALA A  1 437  ? -58.039 36.555  80.195  1.00 37.01 ? 435  ALA A C     1 
ATOM   3100  O O     . ALA A  1 437  ? -59.156 37.010  79.919  1.00 33.58 ? 435  ALA A O     1 
ATOM   3101  C CB    . ALA A  1 437  ? -56.368 38.306  79.543  1.00 33.86 ? 435  ALA A CB    1 
ATOM   3102  N N     . GLY A  1 438  ? -57.747 35.266  80.061  1.00 37.60 ? 436  GLY A N     1 
ATOM   3103  C CA    . GLY A  1 438  ? -58.753 34.318  79.627  1.00 37.50 ? 436  GLY A CA    1 
ATOM   3104  C C     . GLY A  1 438  ? -58.950 34.305  78.120  1.00 43.35 ? 436  GLY A C     1 
ATOM   3105  O O     . GLY A  1 438  ? -58.233 34.954  77.350  1.00 35.46 ? 436  GLY A O     1 
ATOM   3106  N N     . LYS A  1 439  ? -59.984 33.563  77.702  1.00 44.42 ? 437  LYS A N     1 
ATOM   3107  C CA    . LYS A  1 439  ? -60.192 33.246  76.293  1.00 42.22 ? 437  LYS A CA    1 
ATOM   3108  C C     . LYS A  1 439  ? -61.041 34.268  75.547  1.00 46.61 ? 437  LYS A C     1 
ATOM   3109  O O     . LYS A  1 439  ? -60.940 34.350  74.318  1.00 47.37 ? 437  LYS A O     1 
ATOM   3110  C CB    . LYS A  1 439  ? -60.837 31.861  76.158  1.00 48.17 ? 437  LYS A CB    1 
ATOM   3111  N N     . ASP A  1 440  ? -61.879 35.035  76.239  1.00 43.06 ? 438  ASP A N     1 
ATOM   3112  C CA    . ASP A  1 440  ? -62.695 36.052  75.585  1.00 41.60 ? 438  ASP A CA    1 
ATOM   3113  C C     . ASP A  1 440  ? -61.821 37.246  75.225  1.00 41.59 ? 438  ASP A C     1 
ATOM   3114  O O     . ASP A  1 440  ? -61.322 37.943  76.114  1.00 41.38 ? 438  ASP A O     1 
ATOM   3115  C CB    . ASP A  1 440  ? -63.841 36.484  76.494  1.00 47.48 ? 438  ASP A CB    1 
ATOM   3116  C CG    . ASP A  1 440  ? -64.960 35.468  76.536  1.00 48.48 ? 438  ASP A CG    1 
ATOM   3117  O OD1   . ASP A  1 440  ? -64.830 34.414  75.873  1.00 46.41 ? 438  ASP A OD1   1 
ATOM   3118  O OD2   . ASP A  1 440  ? -65.968 35.725  77.229  1.00 52.29 ? 438  ASP A OD2   1 
ATOM   3119  N N     . PHE A  1 441  ? -61.636 37.494  73.928  1.00 35.86 ? 439  PHE A N     1 
ATOM   3120  C CA    . PHE A  1 441  ? -60.851 38.640  73.498  1.00 36.69 ? 439  PHE A CA    1 
ATOM   3121  C C     . PHE A  1 441  ? -61.506 39.316  72.304  1.00 36.06 ? 439  PHE A C     1 
ATOM   3122  O O     . PHE A  1 441  ? -62.181 38.680  71.492  1.00 33.64 ? 439  PHE A O     1 
ATOM   3123  C CB    . PHE A  1 441  ? -59.397 38.276  73.129  1.00 35.78 ? 439  PHE A CB    1 
ATOM   3124  C CG    . PHE A  1 441  ? -58.567 39.480  72.774  1.00 35.87 ? 439  PHE A CG    1 
ATOM   3125  C CD1   . PHE A  1 441  ? -58.052 40.293  73.769  1.00 31.62 ? 439  PHE A CD1   1 
ATOM   3126  C CD2   . PHE A  1 441  ? -58.360 39.841  71.454  1.00 35.32 ? 439  PHE A CD2   1 
ATOM   3127  C CE1   . PHE A  1 441  ? -57.320 41.428  73.454  1.00 27.88 ? 439  PHE A CE1   1 
ATOM   3128  C CE2   . PHE A  1 441  ? -57.632 40.982  71.139  1.00 29.80 ? 439  PHE A CE2   1 
ATOM   3129  C CZ    . PHE A  1 441  ? -57.116 41.770  72.148  1.00 29.18 ? 439  PHE A CZ    1 
ATOM   3130  N N     . HIS A  1 442  ? -61.282 40.620  72.208  1.00 35.58 ? 440  HIS A N     1 
ATOM   3131  C CA    . HIS A  1 442  ? -61.638 41.395  71.031  1.00 32.55 ? 440  HIS A CA    1 
ATOM   3132  C C     . HIS A  1 442  ? -60.728 42.613  70.988  1.00 33.80 ? 440  HIS A C     1 
ATOM   3133  O O     . HIS A  1 442  ? -60.259 43.090  72.028  1.00 32.49 ? 440  HIS A O     1 
ATOM   3134  C CB    . HIS A  1 442  ? -63.115 41.811  71.051  1.00 33.01 ? 440  HIS A CB    1 
ATOM   3135  C CG    . HIS A  1 442  ? -63.485 42.692  72.204  1.00 29.67 ? 440  HIS A CG    1 
ATOM   3136  N ND1   . HIS A  1 442  ? -63.349 44.065  72.170  1.00 33.72 ? 440  HIS A ND1   1 
ATOM   3137  C CD2   . HIS A  1 442  ? -64.009 42.397  73.418  1.00 28.07 ? 440  HIS A CD2   1 
ATOM   3138  C CE1   . HIS A  1 442  ? -63.763 44.577  73.317  1.00 29.58 ? 440  HIS A CE1   1 
ATOM   3139  N NE2   . HIS A  1 442  ? -64.170 43.586  74.090  1.00 33.37 ? 440  HIS A NE2   1 
ATOM   3140  N N     . VAL A  1 443  ? -60.456 43.097  69.774  1.00 34.86 ? 441  VAL A N     1 
ATOM   3141  C CA    . VAL A  1 443  ? -59.646 44.300  69.641  1.00 33.29 ? 441  VAL A CA    1 
ATOM   3142  C C     . VAL A  1 443  ? -60.326 45.430  70.395  1.00 33.01 ? 441  VAL A C     1 
ATOM   3143  O O     . VAL A  1 443  ? -61.535 45.644  70.260  1.00 33.02 ? 441  VAL A O     1 
ATOM   3144  C CB    . VAL A  1 443  ? -59.434 44.643  68.161  1.00 36.24 ? 441  VAL A CB    1 
ATOM   3145  C CG1   . VAL A  1 443  ? -58.878 46.047  68.026  1.00 30.78 ? 441  VAL A CG1   1 
ATOM   3146  C CG2   . VAL A  1 443  ? -58.495 43.633  67.531  1.00 40.23 ? 441  VAL A CG2   1 
ATOM   3147  N N     . GLY A  1 444  ? -59.553 46.142  71.219  1.00 27.25 ? 442  GLY A N     1 
ATOM   3148  C CA    . GLY A  1 444  ? -60.079 47.157  72.109  1.00 26.90 ? 442  GLY A CA    1 
ATOM   3149  C C     . GLY A  1 444  ? -60.298 46.705  73.540  1.00 27.79 ? 442  GLY A C     1 
ATOM   3150  O O     . GLY A  1 444  ? -60.541 47.552  74.409  1.00 29.75 ? 442  GLY A O     1 
ATOM   3151  N N     . LYS A  1 445  ? -60.221 45.402  73.816  1.00 28.32 ? 443  LYS A N     1 
ATOM   3152  C CA    . LYS A  1 445  ? -60.328 44.944  75.197  1.00 24.74 ? 443  LYS A CA    1 
ATOM   3153  C C     . LYS A  1 445  ? -59.051 45.252  75.976  1.00 27.32 ? 443  LYS A C     1 
ATOM   3154  O O     . LYS A  1 445  ? -59.101 45.837  77.066  1.00 26.33 ? 443  LYS A O     1 
ATOM   3155  C CB    . LYS A  1 445  ? -60.632 43.448  75.227  1.00 26.95 ? 443  LYS A CB    1 
ATOM   3156  C CG    . LYS A  1 445  ? -61.090 42.968  76.584  1.00 28.67 ? 443  LYS A CG    1 
ATOM   3157  C CD    . LYS A  1 445  ? -61.338 41.469  76.605  1.00 33.59 ? 443  LYS A CD    1 
ATOM   3158  C CE    . LYS A  1 445  ? -61.953 41.073  77.933  1.00 39.09 ? 443  LYS A CE    1 
ATOM   3159  N NZ    . LYS A  1 445  ? -62.122 39.608  78.032  1.00 43.97 ? 443  LYS A NZ    1 
ATOM   3160  N N     . TYR A  1 446  ? -57.898 44.850  75.438  1.00 26.50 ? 444  TYR A N     1 
ATOM   3161  C CA    . TYR A  1 446  ? -56.589 45.255  75.942  1.00 24.03 ? 444  TYR A CA    1 
ATOM   3162  C C     . TYR A  1 446  ? -55.577 45.004  74.828  1.00 25.57 ? 444  TYR A C     1 
ATOM   3163  O O     . TYR A  1 446  ? -55.909 44.461  73.773  1.00 25.04 ? 444  TYR A O     1 
ATOM   3164  C CB    . TYR A  1 446  ? -56.210 44.507  77.229  1.00 24.84 ? 444  TYR A CB    1 
ATOM   3165  C CG    . TYR A  1 446  ? -56.035 43.016  77.035  1.00 25.55 ? 444  TYR A CG    1 
ATOM   3166  C CD1   . TYR A  1 446  ? -54.803 42.476  76.682  1.00 28.88 ? 444  TYR A CD1   1 
ATOM   3167  C CD2   . TYR A  1 446  ? -57.109 42.151  77.199  1.00 29.90 ? 444  TYR A CD2   1 
ATOM   3168  C CE1   . TYR A  1 446  ? -54.646 41.101  76.497  1.00 31.50 ? 444  TYR A CE1   1 
ATOM   3169  C CE2   . TYR A  1 446  ? -56.967 40.792  77.012  1.00 29.44 ? 444  TYR A CE2   1 
ATOM   3170  C CZ    . TYR A  1 446  ? -55.739 40.274  76.659  1.00 33.99 ? 444  TYR A CZ    1 
ATOM   3171  O OH    . TYR A  1 446  ? -55.611 38.914  76.479  1.00 39.21 ? 444  TYR A OH    1 
ATOM   3172  N N     . GLU A  1 447  ? -54.329 45.386  75.073  1.00 21.73 ? 445  GLU A N     1 
ATOM   3173  C CA    . GLU A  1 447  ? -53.274 45.148  74.104  1.00 25.40 ? 445  GLU A CA    1 
ATOM   3174  C C     . GLU A  1 447  ? -51.969 44.976  74.857  1.00 21.78 ? 445  GLU A C     1 
ATOM   3175  O O     . GLU A  1 447  ? -51.868 45.297  76.040  1.00 24.92 ? 445  GLU A O     1 
ATOM   3176  C CB    . GLU A  1 447  ? -53.163 46.293  73.078  1.00 21.51 ? 445  GLU A CB    1 
ATOM   3177  C CG    . GLU A  1 447  ? -52.536 47.569  73.631  1.00 24.61 ? 445  GLU A CG    1 
ATOM   3178  C CD    . GLU A  1 447  ? -52.479 48.703  72.612  1.00 22.68 ? 445  GLU A CD    1 
ATOM   3179  O OE1   . GLU A  1 447  ? -53.124 48.591  71.541  1.00 24.14 ? 445  GLU A OE1   1 
ATOM   3180  O OE2   . GLU A  1 447  ? -51.793 49.713  72.881  1.00 22.28 ? 445  GLU A OE2   1 
ATOM   3181  N N     . PHE A  1 448  ? -50.978 44.441  74.163  1.00 25.99 ? 446  PHE A N     1 
ATOM   3182  C CA    . PHE A  1 448  ? -49.603 44.474  74.636  1.00 24.45 ? 446  PHE A CA    1 
ATOM   3183  C C     . PHE A  1 448  ? -48.865 45.612  73.953  1.00 23.92 ? 446  PHE A C     1 
ATOM   3184  O O     . PHE A  1 448  ? -49.343 46.186  72.973  1.00 24.67 ? 446  PHE A O     1 
ATOM   3185  C CB    . PHE A  1 448  ? -48.911 43.141  74.365  1.00 26.96 ? 446  PHE A CB    1 
ATOM   3186  C CG    . PHE A  1 448  ? -49.471 42.009  75.170  1.00 27.33 ? 446  PHE A CG    1 
ATOM   3187  C CD1   . PHE A  1 448  ? -49.037 41.789  76.468  1.00 27.94 ? 446  PHE A CD1   1 
ATOM   3188  C CD2   . PHE A  1 448  ? -50.447 41.185  74.643  1.00 28.49 ? 446  PHE A CD2   1 
ATOM   3189  C CE1   . PHE A  1 448  ? -49.560 40.758  77.221  1.00 29.16 ? 446  PHE A CE1   1 
ATOM   3190  C CE2   . PHE A  1 448  ? -50.975 40.154  75.390  1.00 29.86 ? 446  PHE A CE2   1 
ATOM   3191  C CZ    . PHE A  1 448  ? -50.527 39.937  76.682  1.00 31.48 ? 446  PHE A CZ    1 
ATOM   3192  N N     . GLN A  1 449  ? -47.688 45.941  74.485  1.00 21.98 ? 447  GLN A N     1 
ATOM   3193  C CA    . GLN A  1 449  ? -46.823 46.944  73.887  1.00 22.63 ? 447  GLN A CA    1 
ATOM   3194  C C     . GLN A  1 449  ? -45.366 46.527  74.039  1.00 25.92 ? 447  GLN A C     1 
ATOM   3195  O O     . GLN A  1 449  ? -45.010 45.770  74.944  1.00 25.38 ? 447  GLN A O     1 
ATOM   3196  C CB    . GLN A  1 449  ? -47.022 48.327  74.525  1.00 20.95 ? 447  GLN A CB    1 
ATOM   3197  C CG    . GLN A  1 449  ? -48.433 48.850  74.442  1.00 23.62 ? 447  GLN A CG    1 
ATOM   3198  C CD    . GLN A  1 449  ? -48.496 50.338  74.702  1.00 25.18 ? 447  GLN A CD    1 
ATOM   3199  O OE1   . GLN A  1 449  ? -47.572 50.918  75.270  1.00 21.42 ? 447  GLN A OE1   1 
ATOM   3200  N NE2   . GLN A  1 449  ? -49.581 50.965  74.286  1.00 20.14 ? 447  GLN A NE2   1 
ATOM   3201  N N     . CYS A  1 450  ? -44.527 47.058  73.145  1.00 23.32 ? 448  CYS A N     1 
ATOM   3202  C CA    . CYS A  1 450  ? -43.096 46.784  73.112  1.00 26.53 ? 448  CYS A CA    1 
ATOM   3203  C C     . CYS A  1 450  ? -42.388 47.970  72.468  1.00 26.59 ? 448  CYS A C     1 
ATOM   3204  O O     . CYS A  1 450  ? -43.015 48.833  71.854  1.00 27.74 ? 448  CYS A O     1 
ATOM   3205  C CB    . CYS A  1 450  ? -42.772 45.497  72.345  1.00 24.29 ? 448  CYS A CB    1 
ATOM   3206  S SG    . CYS A  1 450  ? -42.971 45.596  70.527  1.00 30.61 ? 448  CYS A SG    1 
ATOM   3207  N N     . LEU A  1 451  ? -41.067 48.010  72.622  1.00 28.92 ? 449  LEU A N     1 
ATOM   3208  C CA    . LEU A  1 451  ? -40.256 49.056  72.016  1.00 27.83 ? 449  LEU A CA    1 
ATOM   3209  C C     . LEU A  1 451  ? -39.812 48.651  70.615  1.00 27.18 ? 449  LEU A C     1 
ATOM   3210  O O     . LEU A  1 451  ? -39.542 47.481  70.343  1.00 28.32 ? 449  LEU A O     1 
ATOM   3211  C CB    . LEU A  1 451  ? -39.023 49.365  72.872  1.00 31.98 ? 449  LEU A CB    1 
ATOM   3212  N N     . HIS A  1 452  ? -39.741 49.643  69.728  1.00 26.93 ? 450  HIS A N     1 
ATOM   3213  C CA    . HIS A  1 452  ? -39.204 49.437  68.392  1.00 30.26 ? 450  HIS A CA    1 
ATOM   3214  C C     . HIS A  1 452  ? -37.786 48.884  68.454  1.00 32.57 ? 450  HIS A C     1 
ATOM   3215  O O     . HIS A  1 452  ? -36.954 49.348  69.236  1.00 28.62 ? 450  HIS A O     1 
ATOM   3216  C CB    . HIS A  1 452  ? -39.204 50.754  67.614  1.00 28.27 ? 450  HIS A CB    1 
ATOM   3217  C CG    . HIS A  1 452  ? -38.385 50.711  66.361  1.00 30.23 ? 450  HIS A CG    1 
ATOM   3218  N ND1   . HIS A  1 452  ? -38.892 50.272  65.157  1.00 32.16 ? 450  HIS A ND1   1 
ATOM   3219  C CD2   . HIS A  1 452  ? -37.088 51.027  66.133  1.00 31.57 ? 450  HIS A CD2   1 
ATOM   3220  C CE1   . HIS A  1 452  ? -37.946 50.336  64.235  1.00 31.60 ? 450  HIS A CE1   1 
ATOM   3221  N NE2   . HIS A  1 452  ? -36.841 50.786  64.803  1.00 32.49 ? 450  HIS A NE2   1 
ATOM   3222  N N     . GLY A  1 453  ? -37.514 47.893  67.607  1.00 39.58 ? 451  GLY A N     1 
ATOM   3223  C CA    . GLY A  1 453  ? -36.211 47.251  67.593  1.00 37.46 ? 451  GLY A CA    1 
ATOM   3224  C C     . GLY A  1 453  ? -36.100 46.127  68.603  1.00 41.10 ? 451  GLY A C     1 
ATOM   3225  O O     . GLY A  1 453  ? -35.624 45.035  68.283  1.00 51.58 ? 451  GLY A O     1 
ATOM   3226  N N     . MET A  1 454  ? -36.560 46.377  69.828  1.00 41.01 ? 452  MET A N     1 
ATOM   3227  C CA    . MET A  1 454  ? -36.319 45.446  70.924  1.00 37.89 ? 452  MET A CA    1 
ATOM   3228  C C     . MET A  1 454  ? -37.363 44.335  70.964  1.00 39.44 ? 452  MET A C     1 
ATOM   3229  O O     . MET A  1 454  ? -37.015 43.150  71.016  1.00 37.63 ? 452  MET A O     1 
ATOM   3230  C CB    . MET A  1 454  ? -36.290 46.208  72.250  1.00 34.60 ? 452  MET A CB    1 
ATOM   3231  C CG    . MET A  1 454  ? -35.717 45.411  73.406  1.00 36.82 ? 452  MET A CG    1 
ATOM   3232  S SD    . MET A  1 454  ? -33.969 45.071  73.143  1.00 62.31 ? 452  MET A SD    1 
ATOM   3233  C CE    . MET A  1 454  ? -33.319 46.741  73.052  1.00 50.44 ? 452  MET A CE    1 
ATOM   3234  N N     . GLY A  1 455  ? -38.649 44.693  70.917  1.00 35.60 ? 453  GLY A N     1 
ATOM   3235  C CA    . GLY A  1 455  ? -39.693 43.734  71.227  1.00 33.81 ? 453  GLY A CA    1 
ATOM   3236  C C     . GLY A  1 455  ? -40.274 42.932  70.082  1.00 35.06 ? 453  GLY A C     1 
ATOM   3237  O O     . GLY A  1 455  ? -41.007 41.966  70.335  1.00 35.10 ? 453  GLY A O     1 
ATOM   3238  N N     . GLU A  1 456  ? -39.997 43.306  68.832  1.00 37.10 ? 454  GLU A N     1 
ATOM   3239  C CA    . GLU A  1 456  ? -40.590 42.580  67.711  1.00 39.09 ? 454  GLU A CA    1 
ATOM   3240  C C     . GLU A  1 456  ? -40.275 41.089  67.712  1.00 39.10 ? 454  GLU A C     1 
ATOM   3241  O O     . GLU A  1 456  ? -41.198 40.303  67.435  1.00 40.54 ? 454  GLU A O     1 
ATOM   3242  C CB    . GLU A  1 456  ? -40.157 43.208  66.380  1.00 39.47 ? 454  GLU A CB    1 
ATOM   3243  C CG    . GLU A  1 456  ? -40.698 44.600  66.133  1.00 39.97 ? 454  GLU A CG    1 
ATOM   3244  C CD    . GLU A  1 456  ? -39.693 45.665  66.496  1.00 36.74 ? 454  GLU A CD    1 
ATOM   3245  O OE1   . GLU A  1 456  ? -38.842 45.384  67.364  1.00 36.06 ? 454  GLU A OE1   1 
ATOM   3246  O OE2   . GLU A  1 456  ? -39.745 46.771  65.912  1.00 41.10 ? 454  GLU A OE2   1 
ATOM   3247  N N     . PRO A  1 457  ? -39.040 40.629  67.981  1.00 38.95 ? 455  PRO A N     1 
ATOM   3248  C CA    . PRO A  1 457  ? -38.815 39.172  68.012  1.00 42.82 ? 455  PRO A CA    1 
ATOM   3249  C C     . PRO A  1 457  ? -39.776 38.444  68.934  1.00 39.06 ? 455  PRO A C     1 
ATOM   3250  O O     . PRO A  1 457  ? -40.304 37.389  68.567  1.00 36.23 ? 455  PRO A O     1 
ATOM   3251  C CB    . PRO A  1 457  ? -37.361 39.050  68.494  1.00 38.19 ? 455  PRO A CB    1 
ATOM   3252  C CG    . PRO A  1 457  ? -36.727 40.333  68.130  1.00 43.63 ? 455  PRO A CG    1 
ATOM   3253  C CD    . PRO A  1 457  ? -37.797 41.374  68.270  1.00 39.77 ? 455  PRO A CD    1 
ATOM   3254  N N     . LEU A  1 458  ? -40.042 38.998  70.116  1.00 38.11 ? 456  LEU A N     1 
ATOM   3255  C CA    . LEU A  1 458  ? -41.005 38.375  71.018  1.00 38.20 ? 456  LEU A CA    1 
ATOM   3256  C C     . LEU A  1 458  ? -42.420 38.455  70.457  1.00 37.07 ? 456  LEU A C     1 
ATOM   3257  O O     . LEU A  1 458  ? -43.118 37.441  70.353  1.00 37.23 ? 456  LEU A O     1 
ATOM   3258  C CB    . LEU A  1 458  ? -40.929 39.033  72.395  1.00 33.42 ? 456  LEU A CB    1 
ATOM   3259  C CG    . LEU A  1 458  ? -41.930 38.556  73.452  1.00 33.90 ? 456  LEU A CG    1 
ATOM   3260  C CD1   . LEU A  1 458  ? -41.887 37.041  73.613  1.00 34.65 ? 456  LEU A CD1   1 
ATOM   3261  C CD2   . LEU A  1 458  ? -41.650 39.244  74.786  1.00 32.94 ? 456  LEU A CD2   1 
ATOM   3262  N N     . TYR A  1 459  ? -42.859 39.650  70.079  1.00 36.34 ? 457  TYR A N     1 
ATOM   3263  C CA    . TYR A  1 459  ? -44.259 39.813  69.726  1.00 34.40 ? 457  TYR A CA    1 
ATOM   3264  C C     . TYR A  1 459  ? -44.591 39.336  68.323  1.00 34.63 ? 457  TYR A C     1 
ATOM   3265  O O     . TYR A  1 459  ? -45.778 39.211  68.003  1.00 38.39 ? 457  TYR A O     1 
ATOM   3266  C CB    . TYR A  1 459  ? -44.676 41.268  69.931  1.00 33.25 ? 457  TYR A CB    1 
ATOM   3267  C CG    . TYR A  1 459  ? -44.854 41.550  71.395  1.00 30.90 ? 457  TYR A CG    1 
ATOM   3268  C CD1   . TYR A  1 459  ? -46.014 41.162  72.051  1.00 31.30 ? 457  TYR A CD1   1 
ATOM   3269  C CD2   . TYR A  1 459  ? -43.848 42.144  72.135  1.00 30.73 ? 457  TYR A CD2   1 
ATOM   3270  C CE1   . TYR A  1 459  ? -46.181 41.389  73.397  1.00 28.41 ? 457  TYR A CE1   1 
ATOM   3271  C CE2   . TYR A  1 459  ? -44.006 42.383  73.482  1.00 29.94 ? 457  TYR A CE2   1 
ATOM   3272  C CZ    . TYR A  1 459  ? -45.179 42.003  74.113  1.00 29.63 ? 457  TYR A CZ    1 
ATOM   3273  O OH    . TYR A  1 459  ? -45.343 42.238  75.467  1.00 29.62 ? 457  TYR A OH    1 
ATOM   3274  N N     . GLU A  1 460  ? -43.591 39.034  67.491  1.00 36.92 ? 458  GLU A N     1 
ATOM   3275  C CA    . GLU A  1 460  ? -43.876 38.267  66.281  1.00 38.10 ? 458  GLU A CA    1 
ATOM   3276  C C     . GLU A  1 460  ? -44.382 36.870  66.611  1.00 40.78 ? 458  GLU A C     1 
ATOM   3277  O O     . GLU A  1 460  ? -45.033 36.239  65.771  1.00 43.59 ? 458  GLU A O     1 
ATOM   3278  C CB    . GLU A  1 460  ? -42.630 38.173  65.400  1.00 42.30 ? 458  GLU A CB    1 
ATOM   3279  C CG    . GLU A  1 460  ? -42.331 39.438  64.606  1.00 48.73 ? 458  GLU A CG    1 
ATOM   3280  C CD    . GLU A  1 460  ? -40.982 39.385  63.911  1.00 53.63 ? 458  GLU A CD    1 
ATOM   3281  O OE1   . GLU A  1 460  ? -40.255 38.378  64.091  1.00 53.55 ? 458  GLU A OE1   1 
ATOM   3282  O OE2   . GLU A  1 460  ? -40.648 40.355  63.190  1.00 57.88 ? 458  GLU A OE2   1 
ATOM   3283  N N     . GLU A  1 461  ? -44.097 36.379  67.817  1.00 39.90 ? 459  GLU A N     1 
ATOM   3284  C CA    . GLU A  1 461  ? -44.622 35.120  68.329  1.00 40.91 ? 459  GLU A CA    1 
ATOM   3285  C C     . GLU A  1 461  ? -45.979 35.280  69.010  1.00 43.91 ? 459  GLU A C     1 
ATOM   3286  O O     . GLU A  1 461  ? -46.470 34.320  69.614  1.00 41.82 ? 459  GLU A O     1 
ATOM   3287  C CB    . GLU A  1 461  ? -43.627 34.507  69.319  1.00 41.46 ? 459  GLU A CB    1 
ATOM   3288  C CG    . GLU A  1 461  ? -42.194 34.451  68.815  1.00 41.80 ? 459  GLU A CG    1 
ATOM   3289  C CD    . GLU A  1 461  ? -42.032 33.421  67.723  1.00 50.44 ? 459  GLU A CD    1 
ATOM   3290  O OE1   . GLU A  1 461  ? -42.868 32.493  67.675  1.00 47.17 ? 459  GLU A OE1   1 
ATOM   3291  O OE2   . GLU A  1 461  ? -41.086 33.542  66.910  1.00 51.33 ? 459  GLU A OE2   1 
ATOM   3292  N N     . VAL A  1 462  ? -46.589 36.466  68.927  1.00 39.16 ? 460  VAL A N     1 
ATOM   3293  C CA    . VAL A  1 462  ? -47.778 36.806  69.705  1.00 36.96 ? 460  VAL A CA    1 
ATOM   3294  C C     . VAL A  1 462  ? -48.887 37.288  68.780  1.00 37.98 ? 460  VAL A C     1 
ATOM   3295  O O     . VAL A  1 462  ? -50.000 36.751  68.790  1.00 38.60 ? 460  VAL A O     1 
ATOM   3296  C CB    . VAL A  1 462  ? -47.452 37.884  70.758  1.00 36.33 ? 460  VAL A CB    1 
ATOM   3297  C CG1   . VAL A  1 462  ? -48.722 38.335  71.471  1.00 33.25 ? 460  VAL A CG1   1 
ATOM   3298  C CG2   . VAL A  1 462  ? -46.413 37.374  71.747  1.00 36.29 ? 460  VAL A CG2   1 
ATOM   3299  N N     . VAL A  1 463  ? -48.582 38.316  67.985  1.00 36.09 ? 461  VAL A N     1 
ATOM   3300  C CA    . VAL A  1 463  ? -49.562 38.918  67.092  1.00 37.31 ? 461  VAL A CA    1 
ATOM   3301  C C     . VAL A  1 463  ? -49.936 37.938  65.989  1.00 40.68 ? 461  VAL A C     1 
ATOM   3302  O O     . VAL A  1 463  ? -49.087 37.201  65.469  1.00 44.24 ? 461  VAL A O     1 
ATOM   3303  C CB    . VAL A  1 463  ? -49.001 40.225  66.500  1.00 34.44 ? 461  VAL A CB    1 
ATOM   3304  C CG1   . VAL A  1 463  ? -50.000 40.861  65.554  1.00 36.94 ? 461  VAL A CG1   1 
ATOM   3305  C CG2   . VAL A  1 463  ? -48.617 41.193  67.614  1.00 28.54 ? 461  VAL A CG2   1 
ATOM   3306  N N     . GLY A  1 464  ? -51.204 37.928  65.627  1.00 40.21 ? 462  GLY A N     1 
ATOM   3307  C CA    . GLY A  1 464  ? -51.608 37.175  64.462  1.00 44.21 ? 462  GLY A CA    1 
ATOM   3308  C C     . GLY A  1 464  ? -52.396 35.932  64.837  1.00 46.87 ? 462  GLY A C     1 
ATOM   3309  O O     . GLY A  1 464  ? -52.170 35.305  65.882  1.00 46.22 ? 462  GLY A O     1 
ATOM   3310  N N     . ARG A  1 465  ? -53.329 35.560  63.959  1.00 47.37 ? 463  ARG A N     1 
ATOM   3311  C CA    . ARG A  1 465  ? -54.203 34.423  64.219  1.00 47.61 ? 463  ARG A CA    1 
ATOM   3312  C C     . ARG A  1 465  ? -53.435 33.113  64.313  1.00 47.94 ? 463  ARG A C     1 
ATOM   3313  O O     . ARG A  1 465  ? -53.961 32.137  64.860  1.00 51.45 ? 463  ARG A O     1 
ATOM   3314  C CB    . ARG A  1 465  ? -55.274 34.328  63.129  1.00 43.14 ? 463  ARG A CB    1 
ATOM   3315  N N     . GLY A  1 466  ? -52.210 33.064  63.798  1.00 48.00 ? 464  GLY A N     1 
ATOM   3316  C CA    . GLY A  1 466  ? -51.403 31.869  63.880  1.00 44.59 ? 464  GLY A CA    1 
ATOM   3317  C C     . GLY A  1 466  ? -50.540 31.775  65.109  1.00 52.82 ? 464  GLY A C     1 
ATOM   3318  O O     . GLY A  1 466  ? -49.832 30.781  65.295  1.00 51.34 ? 464  GLY A O     1 
ATOM   3319  N N     . LYS A  1 467  ? -50.577 32.789  65.969  1.00 47.81 ? 465  LYS A N     1 
ATOM   3320  C CA    . LYS A  1 467  ? -49.736 32.803  67.155  1.00 42.00 ? 465  LYS A CA    1 
ATOM   3321  C C     . LYS A  1 467  ? -50.602 32.804  68.407  1.00 44.68 ? 465  LYS A C     1 
ATOM   3322  O O     . LYS A  1 467  ? -51.285 31.816  68.688  1.00 49.13 ? 465  LYS A O     1 
ATOM   3323  C CB    . LYS A  1 467  ? -48.803 34.009  67.109  1.00 42.51 ? 465  LYS A CB    1 
ATOM   3324  C CG    . LYS A  1 467  ? -47.764 33.920  65.991  1.00 49.21 ? 465  LYS A CG    1 
ATOM   3325  C CD    . LYS A  1 467  ? -46.782 32.774  66.248  1.00 46.07 ? 465  LYS A CD    1 
ATOM   3326  C CE    . LYS A  1 467  ? -45.677 32.727  65.202  1.00 48.33 ? 465  LYS A CE    1 
ATOM   3327  N NZ    . LYS A  1 467  ? -44.524 31.906  65.668  1.00 49.95 ? 465  LYS A NZ    1 
ATOM   3328  N N     . LEU A  1 468  ? -50.586 33.897  69.164  1.00 42.22 ? 466  LEU A N     1 
ATOM   3329  C CA    . LEU A  1 468  ? -51.457 34.039  70.321  1.00 42.09 ? 466  LEU A CA    1 
ATOM   3330  C C     . LEU A  1 468  ? -52.667 34.920  70.035  1.00 42.32 ? 466  LEU A C     1 
ATOM   3331  O O     . LEU A  1 468  ? -53.581 34.983  70.866  1.00 37.77 ? 466  LEU A O     1 
ATOM   3332  C CB    . LEU A  1 468  ? -50.665 34.600  71.516  1.00 38.10 ? 466  LEU A CB    1 
ATOM   3333  C CG    . LEU A  1 468  ? -49.496 33.754  72.040  1.00 39.05 ? 466  LEU A CG    1 
ATOM   3334  C CD1   . LEU A  1 468  ? -48.896 34.375  73.294  1.00 37.35 ? 466  LEU A CD1   1 
ATOM   3335  C CD2   . LEU A  1 468  ? -49.923 32.310  72.307  1.00 42.40 ? 466  LEU A CD2   1 
ATOM   3336  N N     . ASP A  1 469  ? -52.687 35.587  68.878  1.00 43.65 ? 467  ASP A N     1 
ATOM   3337  C CA    . ASP A  1 469  ? -53.800 36.428  68.430  1.00 41.91 ? 467  ASP A CA    1 
ATOM   3338  C C     . ASP A  1 469  ? -54.110 37.544  69.428  1.00 35.39 ? 467  ASP A C     1 
ATOM   3339  O O     . ASP A  1 469  ? -55.268 37.821  69.748  1.00 35.19 ? 467  ASP A O     1 
ATOM   3340  C CB    . ASP A  1 469  ? -55.047 35.587  68.133  1.00 39.62 ? 467  ASP A CB    1 
ATOM   3341  C CG    . ASP A  1 469  ? -55.969 36.254  67.127  1.00 47.10 ? 467  ASP A CG    1 
ATOM   3342  O OD1   . ASP A  1 469  ? -55.552 37.275  66.534  1.00 46.03 ? 467  ASP A OD1   1 
ATOM   3343  O OD2   . ASP A  1 469  ? -57.102 35.764  66.927  1.00 53.46 ? 467  ASP A OD2   1 
ATOM   3344  N N     . ARG A  1 470  ? -53.056 38.197  69.905  1.00 36.57 ? 468  ARG A N     1 
ATOM   3345  C CA    . ARG A  1 470  ? -53.166 39.386  70.728  1.00 32.03 ? 468  ARG A CA    1 
ATOM   3346  C C     . ARG A  1 470  ? -52.395 40.528  70.079  1.00 29.36 ? 468  ARG A C     1 
ATOM   3347  O O     . ARG A  1 470  ? -51.255 40.325  69.636  1.00 31.34 ? 468  ARG A O     1 
ATOM   3348  C CB    . ARG A  1 470  ? -52.623 39.119  72.144  1.00 29.31 ? 468  ARG A CB    1 
ATOM   3349  C CG    . ARG A  1 470  ? -53.416 38.077  72.910  1.00 31.82 ? 468  ARG A CG    1 
ATOM   3350  C CD    . ARG A  1 470  ? -54.885 38.474  73.054  1.00 32.85 ? 468  ARG A CD    1 
ATOM   3351  N NE    . ARG A  1 470  ? -55.634 37.480  73.816  1.00 35.05 ? 468  ARG A NE    1 
ATOM   3352  C CZ    . ARG A  1 470  ? -56.366 36.513  73.277  1.00 39.14 ? 468  ARG A CZ    1 
ATOM   3353  N NH1   . ARG A  1 470  ? -56.490 36.389  71.964  1.00 37.45 ? 468  ARG A NH1   1 
ATOM   3354  N NH2   . ARG A  1 470  ? -57.003 35.660  74.074  1.00 35.94 ? 468  ARG A NH2   1 
ATOM   3355  N N     . PRO A  1 471  ? -52.970 41.725  69.994  1.00 30.47 ? 469  PRO A N     1 
ATOM   3356  C CA    . PRO A  1 471  ? -52.287 42.828  69.318  1.00 27.07 ? 469  PRO A CA    1 
ATOM   3357  C C     . PRO A  1 471  ? -51.169 43.405  70.170  1.00 30.67 ? 469  PRO A C     1 
ATOM   3358  O O     . PRO A  1 471  ? -51.185 43.325  71.401  1.00 29.46 ? 469  PRO A O     1 
ATOM   3359  C CB    . PRO A  1 471  ? -53.405 43.855  69.114  1.00 24.75 ? 469  PRO A CB    1 
ATOM   3360  C CG    . PRO A  1 471  ? -54.316 43.620  70.261  1.00 29.15 ? 469  PRO A CG    1 
ATOM   3361  C CD    . PRO A  1 471  ? -54.311 42.119  70.467  1.00 31.83 ? 469  PRO A CD    1 
ATOM   3362  N N     . CYS A  1 472  ? -50.191 44.002  69.490  1.00 27.13 ? 470  CYS A N     1 
ATOM   3363  C CA    . CYS A  1 472  ? -49.060 44.652  70.148  1.00 24.88 ? 470  CYS A CA    1 
ATOM   3364  C C     . CYS A  1 472  ? -48.840 46.016  69.516  1.00 24.49 ? 470  CYS A C     1 
ATOM   3365  O O     . CYS A  1 472  ? -48.790 46.133  68.286  1.00 28.42 ? 470  CYS A O     1 
ATOM   3366  C CB    . CYS A  1 472  ? -47.782 43.821  70.035  1.00 26.82 ? 470  CYS A CB    1 
ATOM   3367  S SG    . CYS A  1 472  ? -46.345 44.594  70.842  1.00 27.91 ? 470  CYS A SG    1 
ATOM   3368  N N     . ARG A  1 473  ? -48.718 47.041  70.351  1.00 23.28 ? 471  ARG A N     1 
ATOM   3369  C CA    . ARG A  1 473  ? -48.412 48.386  69.881  1.00 24.63 ? 471  ARG A CA    1 
ATOM   3370  C C     . ARG A  1 473  ? -46.929 48.665  70.084  1.00 24.60 ? 471  ARG A C     1 
ATOM   3371  O O     . ARG A  1 473  ? -46.395 48.469  71.183  1.00 25.85 ? 471  ARG A O     1 
ATOM   3372  C CB    . ARG A  1 473  ? -49.250 49.442  70.595  1.00 22.55 ? 471  ARG A CB    1 
ATOM   3373  C CG    . ARG A  1 473  ? -49.038 50.849  70.025  1.00 21.20 ? 471  ARG A CG    1 
ATOM   3374  C CD    . ARG A  1 473  ? -49.934 51.850  70.708  1.00 20.23 ? 471  ARG A CD    1 
ATOM   3375  N NE    . ARG A  1 473  ? -51.316 51.394  70.702  1.00 22.23 ? 471  ARG A NE    1 
ATOM   3376  C CZ    . ARG A  1 473  ? -52.167 51.601  69.704  1.00 23.89 ? 471  ARG A CZ    1 
ATOM   3377  N NH1   . ARG A  1 473  ? -51.857 52.380  68.676  1.00 24.29 ? 471  ARG A NH1   1 
ATOM   3378  N NH2   . ARG A  1 473  ? -53.354 51.006  69.732  1.00 23.91 ? 471  ARG A NH2   1 
ATOM   3379  N N     . ILE A  1 474  ? -46.279 49.142  69.030  1.00 24.16 ? 472  ILE A N     1 
ATOM   3380  C CA    . ILE A  1 474  ? -44.842 49.379  69.033  1.00 24.03 ? 472  ILE A CA    1 
ATOM   3381  C C     . ILE A  1 474  ? -44.577 50.829  69.399  1.00 23.46 ? 472  ILE A C     1 
ATOM   3382  O O     . ILE A  1 474  ? -45.059 51.744  68.728  1.00 25.06 ? 472  ILE A O     1 
ATOM   3383  C CB    . ILE A  1 474  ? -44.221 49.049  67.671  1.00 23.61 ? 472  ILE A CB    1 
ATOM   3384  C CG1   . ILE A  1 474  ? -44.289 47.551  67.396  1.00 30.01 ? 472  ILE A CG1   1 
ATOM   3385  C CG2   . ILE A  1 474  ? -42.773 49.559  67.635  1.00 25.16 ? 472  ILE A CG2   1 
ATOM   3386  C CD1   . ILE A  1 474  ? -43.965 47.189  65.958  1.00 31.43 ? 472  ILE A CD1   1 
ATOM   3387  N N     . TYR A  1 475  ? -43.811 51.039  70.465  1.00 20.45 ? 473  TYR A N     1 
ATOM   3388  C CA    . TYR A  1 475  ? -43.361 52.373  70.855  1.00 24.54 ? 473  TYR A CA    1 
ATOM   3389  C C     . TYR A  1 475  ? -42.187 52.767  69.961  1.00 28.27 ? 473  TYR A C     1 
ATOM   3390  O O     . TYR A  1 475  ? -41.106 52.171  70.037  1.00 24.65 ? 473  TYR A O     1 
ATOM   3391  C CB    . TYR A  1 475  ? -42.968 52.369  72.331  1.00 25.80 ? 473  TYR A CB    1 
ATOM   3392  C CG    . TYR A  1 475  ? -42.688 53.717  72.975  1.00 32.91 ? 473  TYR A CG    1 
ATOM   3393  C CD1   . TYR A  1 475  ? -43.709 54.454  73.572  1.00 30.57 ? 473  TYR A CD1   1 
ATOM   3394  C CD2   . TYR A  1 475  ? -41.393 54.230  73.025  1.00 34.22 ? 473  TYR A CD2   1 
ATOM   3395  C CE1   . TYR A  1 475  ? -43.451 55.681  74.175  1.00 31.66 ? 473  TYR A CE1   1 
ATOM   3396  C CE2   . TYR A  1 475  ? -41.124 55.451  73.621  1.00 33.71 ? 473  TYR A CE2   1 
ATOM   3397  C CZ    . TYR A  1 475  ? -42.150 56.170  74.200  1.00 35.57 ? 473  TYR A CZ    1 
ATOM   3398  O OH    . TYR A  1 475  ? -41.872 57.385  74.789  1.00 38.47 ? 473  TYR A OH    1 
ATOM   3399  N N     . ALA A  1 476  ? -42.393 53.774  69.120  1.00 24.79 ? 474  ALA A N     1 
ATOM   3400  C CA    . ALA A  1 476  ? -41.494 54.084  68.013  1.00 24.25 ? 474  ALA A CA    1 
ATOM   3401  C C     . ALA A  1 476  ? -40.802 55.418  68.246  1.00 23.93 ? 474  ALA A C     1 
ATOM   3402  O O     . ALA A  1 476  ? -41.410 56.476  68.020  1.00 23.28 ? 474  ALA A O     1 
ATOM   3403  C CB    . ALA A  1 476  ? -42.285 54.120  66.700  1.00 25.04 ? 474  ALA A CB    1 
ATOM   3404  N N     . PRO A  1 477  ? -39.547 55.435  68.702  1.00 24.41 ? 475  PRO A N     1 
ATOM   3405  C CA    . PRO A  1 477  ? -38.841 56.710  68.848  1.00 21.71 ? 475  PRO A CA    1 
ATOM   3406  C C     . PRO A  1 477  ? -38.579 57.337  67.489  1.00 24.49 ? 475  PRO A C     1 
ATOM   3407  O O     . PRO A  1 477  ? -38.343 56.652  66.496  1.00 27.73 ? 475  PRO A O     1 
ATOM   3408  C CB    . PRO A  1 477  ? -37.524 56.326  69.548  1.00 28.46 ? 475  PRO A CB    1 
ATOM   3409  C CG    . PRO A  1 477  ? -37.664 54.889  69.954  1.00 25.64 ? 475  PRO A CG    1 
ATOM   3410  C CD    . PRO A  1 477  ? -38.696 54.285  69.042  1.00 24.53 ? 475  PRO A CD    1 
ATOM   3411  N N     . VAL A  1 478  ? -38.631 58.661  67.453  1.00 27.60 ? 476  VAL A N     1 
ATOM   3412  C CA    . VAL A  1 478  ? -38.517 59.425  66.218  1.00 29.80 ? 476  VAL A CA    1 
ATOM   3413  C C     . VAL A  1 478  ? -37.566 60.582  66.480  1.00 31.44 ? 476  VAL A C     1 
ATOM   3414  O O     . VAL A  1 478  ? -37.813 61.393  67.378  1.00 30.87 ? 476  VAL A O     1 
ATOM   3415  C CB    . VAL A  1 478  ? -39.882 59.956  65.742  1.00 33.00 ? 476  VAL A CB    1 
ATOM   3416  C CG1   . VAL A  1 478  ? -39.708 60.772  64.462  1.00 34.12 ? 476  VAL A CG1   1 
ATOM   3417  C CG2   . VAL A  1 478  ? -40.890 58.819  65.541  1.00 23.46 ? 476  VAL A CG2   1 
ATOM   3418  N N     . GLY A  1 479  ? -36.494 60.668  65.710  1.00 32.58 ? 477  GLY A N     1 
ATOM   3419  C CA    . GLY A  1 479  ? -35.551 61.750  65.922  1.00 40.92 ? 477  GLY A CA    1 
ATOM   3420  C C     . GLY A  1 479  ? -34.228 61.500  65.236  1.00 40.36 ? 477  GLY A C     1 
ATOM   3421  O O     . GLY A  1 479  ? -33.915 60.392  64.800  1.00 35.34 ? 477  GLY A O     1 
ATOM   3422  N N     . THR A  1 480  ? -33.436 62.567  65.145  1.00 43.12 ? 478  THR A N     1 
ATOM   3423  C CA    . THR A  1 480  ? -32.157 62.538  64.446  1.00 49.82 ? 478  THR A CA    1 
ATOM   3424  C C     . THR A  1 480  ? -31.055 61.977  65.348  1.00 55.85 ? 478  THR A C     1 
ATOM   3425  O O     . THR A  1 480  ? -31.289 61.576  66.492  1.00 55.78 ? 478  THR A O     1 
ATOM   3426  C CB    . THR A  1 480  ? -31.780 63.936  63.960  1.00 45.37 ? 478  THR A CB    1 
ATOM   3427  O OG1   . THR A  1 480  ? -31.539 64.784  65.091  1.00 48.42 ? 478  THR A OG1   1 
ATOM   3428  C CG2   . THR A  1 480  ? -32.893 64.532  63.116  1.00 46.43 ? 478  THR A CG2   1 
ATOM   3429  N N     . HIS A  1 481  ? -29.821 61.974  64.820  1.00 63.46 ? 479  HIS A N     1 
ATOM   3430  C CA    . HIS A  1 481  ? -28.679 61.405  65.538  1.00 59.81 ? 479  HIS A CA    1 
ATOM   3431  C C     . HIS A  1 481  ? -28.347 62.195  66.796  1.00 61.52 ? 479  HIS A C     1 
ATOM   3432  O O     . HIS A  1 481  ? -27.897 61.612  67.791  1.00 65.86 ? 479  HIS A O     1 
ATOM   3433  C CB    . HIS A  1 481  ? -27.443 61.348  64.631  1.00 60.79 ? 479  HIS A CB    1 
ATOM   3434  C CG    . HIS A  1 481  ? -27.646 60.574  63.363  1.00 63.09 ? 479  HIS A CG    1 
ATOM   3435  N ND1   . HIS A  1 481  ? -26.669 60.471  62.394  1.00 60.87 ? 479  HIS A ND1   1 
ATOM   3436  C CD2   . HIS A  1 481  ? -28.707 59.869  62.903  1.00 60.85 ? 479  HIS A CD2   1 
ATOM   3437  C CE1   . HIS A  1 481  ? -27.121 59.737  61.393  1.00 65.50 ? 479  HIS A CE1   1 
ATOM   3438  N NE2   . HIS A  1 481  ? -28.355 59.359  61.676  1.00 68.38 ? 479  HIS A NE2   1 
ATOM   3439  N N     . GLU A  1 482  ? -28.543 63.514  66.769  1.00 59.48 ? 480  GLU A N     1 
ATOM   3440  C CA    . GLU A  1 482  ? -28.337 64.317  67.970  1.00 59.09 ? 480  GLU A CA    1 
ATOM   3441  C C     . GLU A  1 482  ? -29.289 63.889  69.081  1.00 58.53 ? 480  GLU A C     1 
ATOM   3442  O O     . GLU A  1 482  ? -28.858 63.562  70.193  1.00 62.10 ? 480  GLU A O     1 
ATOM   3443  C CB    . GLU A  1 482  ? -28.518 65.801  67.641  1.00 57.79 ? 480  GLU A CB    1 
ATOM   3444  N N     . THR A  1 483  ? -30.593 63.860  68.784  1.00 56.73 ? 481  THR A N     1 
ATOM   3445  C CA    . THR A  1 483  ? -31.595 63.573  69.808  1.00 58.57 ? 481  THR A CA    1 
ATOM   3446  C C     . THR A  1 483  ? -31.505 62.131  70.305  1.00 60.13 ? 481  THR A C     1 
ATOM   3447  O O     . THR A  1 483  ? -31.606 61.879  71.513  1.00 59.58 ? 481  THR A O     1 
ATOM   3448  C CB    . THR A  1 483  ? -32.994 63.868  69.260  1.00 53.40 ? 481  THR A CB    1 
ATOM   3449  N N     . LEU A  1 484  ? -31.320 61.173  69.391  1.00 61.00 ? 482  LEU A N     1 
ATOM   3450  C CA    . LEU A  1 484  ? -31.294 59.763  69.777  1.00 58.63 ? 482  LEU A CA    1 
ATOM   3451  C C     . LEU A  1 484  ? -30.184 59.482  70.785  1.00 61.56 ? 482  LEU A C     1 
ATOM   3452  O O     . LEU A  1 484  ? -30.430 58.915  71.857  1.00 59.33 ? 482  LEU A O     1 
ATOM   3453  C CB    . LEU A  1 484  ? -31.129 58.884  68.536  1.00 52.98 ? 482  LEU A CB    1 
ATOM   3454  N N     . LEU A  1 485  ? -28.951 59.883  70.458  1.00 60.91 ? 483  LEU A N     1 
ATOM   3455  C CA    . LEU A  1 485  ? -27.802 59.570  71.304  1.00 63.41 ? 483  LEU A CA    1 
ATOM   3456  C C     . LEU A  1 485  ? -27.888 60.226  72.677  1.00 67.19 ? 483  LEU A C     1 
ATOM   3457  O O     . LEU A  1 485  ? -27.179 59.800  73.599  1.00 61.95 ? 483  LEU A O     1 
ATOM   3458  C CB    . LEU A  1 485  ? -26.507 59.992  70.603  1.00 56.60 ? 483  LEU A CB    1 
ATOM   3459  N N     . ALA A  1 486  ? -28.740 61.244  72.833  1.00 74.87 ? 484  ALA A N     1 
ATOM   3460  C CA    . ALA A  1 486  ? -28.888 61.957  74.097  1.00 67.91 ? 484  ALA A CA    1 
ATOM   3461  C C     . ALA A  1 486  ? -29.255 61.010  75.235  1.00 68.98 ? 484  ALA A C     1 
ATOM   3462  O O     . ALA A  1 486  ? -28.415 60.710  76.089  1.00 72.30 ? 484  ALA A O     1 
ATOM   3463  C CB    . ALA A  1 486  ? -29.934 63.065  73.962  1.00 60.14 ? 484  ALA A CB    1 
ATOM   3464  N N     . TYR A  1 487  ? -30.496 60.523  75.255  1.00 61.84 ? 485  TYR A N     1 
ATOM   3465  C CA    . TYR A  1 487  ? -30.973 59.664  76.332  1.00 57.95 ? 485  TYR A CA    1 
ATOM   3466  C C     . TYR A  1 487  ? -31.039 58.197  75.927  1.00 60.56 ? 485  TYR A C     1 
ATOM   3467  O O     . TYR A  1 487  ? -31.853 57.442  76.470  1.00 59.73 ? 485  TYR A O     1 
ATOM   3468  C CB    . TYR A  1 487  ? -32.342 60.137  76.823  1.00 61.01 ? 485  TYR A CB    1 
ATOM   3469  N N     . LEU A  1 488  ? -30.192 57.768  74.986  1.00 59.81 ? 486  LEU A N     1 
ATOM   3470  C CA    . LEU A  1 488  ? -30.220 56.367  74.573  1.00 58.99 ? 486  LEU A CA    1 
ATOM   3471  C C     . LEU A  1 488  ? -29.658 55.451  75.654  1.00 57.59 ? 486  LEU A C     1 
ATOM   3472  O O     . LEU A  1 488  ? -30.037 54.273  75.729  1.00 52.17 ? 486  LEU A O     1 
ATOM   3473  C CB    . LEU A  1 488  ? -29.449 56.180  73.266  1.00 57.72 ? 486  LEU A CB    1 
ATOM   3474  C CG    . LEU A  1 488  ? -29.325 54.739  72.755  1.00 53.99 ? 486  LEU A CG    1 
ATOM   3475  C CD1   . LEU A  1 488  ? -30.688 54.082  72.631  1.00 52.56 ? 486  LEU A CD1   1 
ATOM   3476  C CD2   . LEU A  1 488  ? -28.598 54.701  71.432  1.00 47.04 ? 486  LEU A CD2   1 
ATOM   3477  N N     . VAL A  1 489  ? -28.754 55.968  76.493  1.00 57.23 ? 487  VAL A N     1 
ATOM   3478  C CA    . VAL A  1 489  ? -28.194 55.164  77.579  1.00 55.51 ? 487  VAL A CA    1 
ATOM   3479  C C     . VAL A  1 489  ? -29.318 54.592  78.432  1.00 58.08 ? 487  VAL A C     1 
ATOM   3480  O O     . VAL A  1 489  ? -29.434 53.373  78.608  1.00 59.86 ? 487  VAL A O     1 
ATOM   3481  C CB    . VAL A  1 489  ? -27.215 55.998  78.423  1.00 51.71 ? 487  VAL A CB    1 
ATOM   3482  N N     . ARG A  1 490  ? -30.182 55.476  78.946  1.00 57.82 ? 488  ARG A N     1 
ATOM   3483  C CA    . ARG A  1 490  ? -31.351 55.050  79.715  1.00 57.83 ? 488  ARG A CA    1 
ATOM   3484  C C     . ARG A  1 490  ? -32.183 54.022  78.949  1.00 58.21 ? 488  ARG A C     1 
ATOM   3485  O O     . ARG A  1 490  ? -32.712 53.074  79.542  1.00 55.87 ? 488  ARG A O     1 
ATOM   3486  C CB    . ARG A  1 490  ? -32.199 56.276  80.081  1.00 56.04 ? 488  ARG A CB    1 
ATOM   3487  C CG    . ARG A  1 490  ? -33.337 56.017  81.069  1.00 54.95 ? 488  ARG A CG    1 
ATOM   3488  C CD    . ARG A  1 490  ? -34.148 57.292  81.335  1.00 49.85 ? 488  ARG A CD    1 
ATOM   3489  N NE    . ARG A  1 490  ? -35.016 57.639  80.212  1.00 51.05 ? 488  ARG A NE    1 
ATOM   3490  C CZ    . ARG A  1 490  ? -35.435 58.867  79.931  1.00 48.29 ? 488  ARG A CZ    1 
ATOM   3491  N NH1   . ARG A  1 490  ? -35.052 59.911  80.647  1.00 37.99 ? 488  ARG A NH1   1 
ATOM   3492  N NH2   . ARG A  1 490  ? -36.254 59.052  78.896  1.00 44.18 ? 488  ARG A NH2   1 
ATOM   3493  N N     . ARG A  1 491  ? -32.289 54.180  77.632  1.00 56.39 ? 489  ARG A N     1 
ATOM   3494  C CA    . ARG A  1 491  ? -33.099 53.287  76.809  1.00 58.29 ? 489  ARG A CA    1 
ATOM   3495  C C     . ARG A  1 491  ? -32.522 51.880  76.786  1.00 54.78 ? 489  ARG A C     1 
ATOM   3496  O O     . ARG A  1 491  ? -33.184 50.945  76.349  1.00 58.97 ? 489  ARG A O     1 
ATOM   3497  C CB    . ARG A  1 491  ? -33.217 53.828  75.381  1.00 53.14 ? 489  ARG A CB    1 
ATOM   3498  N N     . GLY A  1 496  ? -30.555 46.684  79.439  1.00 65.64 ? 494  GLY A N     1 
ATOM   3499  C CA    . GLY A  1 496  ? -29.255 46.067  79.237  1.00 64.97 ? 494  GLY A CA    1 
ATOM   3500  C C     . GLY A  1 496  ? -28.468 45.783  80.507  1.00 72.13 ? 494  GLY A C     1 
ATOM   3501  O O     . GLY A  1 496  ? -27.251 45.601  80.458  1.00 73.37 ? 494  GLY A O     1 
ATOM   3502  N N     . ALA A  1 497  ? -29.155 45.748  81.646  1.00 62.93 ? 495  ALA A N     1 
ATOM   3503  C CA    . ALA A  1 497  ? -28.522 45.421  82.916  1.00 55.94 ? 495  ALA A CA    1 
ATOM   3504  C C     . ALA A  1 497  ? -28.672 43.931  83.214  1.00 52.60 ? 495  ALA A C     1 
ATOM   3505  O O     . ALA A  1 497  ? -29.506 43.236  82.627  1.00 53.13 ? 495  ALA A O     1 
ATOM   3506  C CB    . ALA A  1 497  ? -29.120 46.254  84.051  1.00 54.81 ? 495  ALA A CB    1 
ATOM   3507  N N     . ASN A  1 498  ? -27.848 43.445  84.149  1.00 51.83 ? 496  ASN A N     1 
ATOM   3508  C CA    . ASN A  1 498  ? -27.791 42.008  84.418  1.00 54.01 ? 496  ASN A CA    1 
ATOM   3509  C C     . ASN A  1 498  ? -29.149 41.447  84.828  1.00 48.95 ? 496  ASN A C     1 
ATOM   3510  O O     . ASN A  1 498  ? -29.429 40.266  84.589  1.00 47.38 ? 496  ASN A O     1 
ATOM   3511  C CB    . ASN A  1 498  ? -26.745 41.717  85.499  1.00 52.27 ? 496  ASN A CB    1 
ATOM   3512  N N     . SER A  1 499  ? -30.002 42.270  85.434  1.00 47.33 ? 497  SER A N     1 
ATOM   3513  C CA    . SER A  1 499  ? -31.323 41.836  85.868  1.00 45.68 ? 497  SER A CA    1 
ATOM   3514  C C     . SER A  1 499  ? -32.373 41.916  84.765  1.00 46.21 ? 497  SER A C     1 
ATOM   3515  O O     . SER A  1 499  ? -33.475 41.382  84.941  1.00 43.78 ? 497  SER A O     1 
ATOM   3516  C CB    . SER A  1 499  ? -31.779 42.666  87.081  1.00 41.64 ? 497  SER A CB    1 
ATOM   3517  O OG    . SER A  1 499  ? -31.667 44.063  86.835  1.00 42.13 ? 497  SER A OG    1 
ATOM   3518  N N     . SER A  1 500  ? -32.053 42.551  83.637  1.00 46.52 ? 498  SER A N     1 
ATOM   3519  C CA    . SER A  1 500  ? -33.023 42.727  82.565  1.00 43.40 ? 498  SER A CA    1 
ATOM   3520  C C     . SER A  1 500  ? -33.306 41.412  81.849  1.00 45.16 ? 498  SER A C     1 
ATOM   3521  O O     . SER A  1 500  ? -32.398 40.613  81.604  1.00 46.47 ? 498  SER A O     1 
ATOM   3522  C CB    . SER A  1 500  ? -32.520 43.760  81.561  1.00 46.07 ? 498  SER A CB    1 
ATOM   3523  O OG    . SER A  1 500  ? -32.436 45.035  82.166  1.00 54.11 ? 498  SER A OG    1 
ATOM   3524  N N     . PHE A  1 501  ? -34.582 41.198  81.506  1.00 39.67 ? 499  PHE A N     1 
ATOM   3525  C CA    . PHE A  1 501  ? -34.955 40.042  80.697  1.00 42.28 ? 499  PHE A CA    1 
ATOM   3526  C C     . PHE A  1 501  ? -34.191 40.020  79.381  1.00 46.51 ? 499  PHE A C     1 
ATOM   3527  O O     . PHE A  1 501  ? -33.706 38.965  78.955  1.00 47.64 ? 499  PHE A O     1 
ATOM   3528  C CB    . PHE A  1 501  ? -36.465 40.041  80.427  1.00 37.70 ? 499  PHE A CB    1 
ATOM   3529  C CG    . PHE A  1 501  ? -36.942 38.832  79.659  1.00 41.10 ? 499  PHE A CG    1 
ATOM   3530  C CD1   . PHE A  1 501  ? -37.304 37.673  80.325  1.00 40.07 ? 499  PHE A CD1   1 
ATOM   3531  C CD2   . PHE A  1 501  ? -37.016 38.851  78.270  1.00 41.97 ? 499  PHE A CD2   1 
ATOM   3532  C CE1   . PHE A  1 501  ? -37.735 36.559  79.630  1.00 38.84 ? 499  PHE A CE1   1 
ATOM   3533  C CE2   . PHE A  1 501  ? -37.443 37.737  77.567  1.00 40.28 ? 499  PHE A CE2   1 
ATOM   3534  C CZ    . PHE A  1 501  ? -37.803 36.589  78.248  1.00 41.90 ? 499  PHE A CZ    1 
ATOM   3535  N N     . VAL A  1 502  ? -34.083 41.173  78.714  1.00 44.78 ? 500  VAL A N     1 
ATOM   3536  C CA    . VAL A  1 502  ? -33.461 41.214  77.394  1.00 47.91 ? 500  VAL A CA    1 
ATOM   3537  C C     . VAL A  1 502  ? -31.990 40.848  77.489  1.00 49.88 ? 500  VAL A C     1 
ATOM   3538  O O     . VAL A  1 502  ? -31.435 40.224  76.576  1.00 57.49 ? 500  VAL A O     1 
ATOM   3539  C CB    . VAL A  1 502  ? -33.659 42.595  76.740  1.00 52.05 ? 500  VAL A CB    1 
ATOM   3540  N N     . HIS A  1 503  ? -31.335 41.220  78.589  1.00 48.91 ? 501  HIS A N     1 
ATOM   3541  C CA    . HIS A  1 503  ? -29.959 40.791  78.801  1.00 51.10 ? 501  HIS A CA    1 
ATOM   3542  C C     . HIS A  1 503  ? -29.896 39.311  79.170  1.00 54.03 ? 501  HIS A C     1 
ATOM   3543  O O     . HIS A  1 503  ? -29.047 38.572  78.657  1.00 54.67 ? 501  HIS A O     1 
ATOM   3544  C CB    . HIS A  1 503  ? -29.309 41.653  79.881  1.00 53.24 ? 501  HIS A CB    1 
ATOM   3545  C CG    . HIS A  1 503  ? -27.965 41.163  80.320  1.00 59.62 ? 501  HIS A CG    1 
ATOM   3546  N ND1   . HIS A  1 503  ? -27.806 40.156  81.249  1.00 60.52 ? 501  HIS A ND1   1 
ATOM   3547  C CD2   . HIS A  1 503  ? -26.716 41.545  79.962  1.00 60.07 ? 501  HIS A CD2   1 
ATOM   3548  C CE1   . HIS A  1 503  ? -26.518 39.936  81.442  1.00 61.65 ? 501  HIS A CE1   1 
ATOM   3549  N NE2   . HIS A  1 503  ? -25.835 40.765  80.673  1.00 64.78 ? 501  HIS A NE2   1 
ATOM   3550  N N     . ARG A  1 504  ? -30.808 38.854  80.033  1.00 50.06 ? 502  ARG A N     1 
ATOM   3551  C CA    . ARG A  1 504  ? -30.762 37.478  80.516  1.00 49.06 ? 502  ARG A CA    1 
ATOM   3552  C C     . ARG A  1 504  ? -31.153 36.474  79.439  1.00 53.37 ? 502  ARG A C     1 
ATOM   3553  O O     . ARG A  1 504  ? -30.608 35.366  79.410  1.00 52.38 ? 502  ARG A O     1 
ATOM   3554  C CB    . ARG A  1 504  ? -31.660 37.326  81.743  1.00 49.14 ? 502  ARG A CB    1 
ATOM   3555  C CG    . ARG A  1 504  ? -31.080 37.970  82.999  1.00 47.60 ? 502  ARG A CG    1 
ATOM   3556  C CD    . ARG A  1 504  ? -32.128 38.175  84.084  1.00 48.66 ? 502  ARG A CD    1 
ATOM   3557  N NE    . ARG A  1 504  ? -32.890 36.966  84.376  1.00 51.03 ? 502  ARG A NE    1 
ATOM   3558  C CZ    . ARG A  1 504  ? -32.440 35.959  85.113  1.00 54.49 ? 502  ARG A CZ    1 
ATOM   3559  N NH1   . ARG A  1 504  ? -31.205 35.949  85.588  1.00 51.33 ? 502  ARG A NH1   1 
ATOM   3560  N NH2   . ARG A  1 504  ? -33.251 34.938  85.382  1.00 55.15 ? 502  ARG A NH2   1 
ATOM   3561  N N     . ILE A  1 505  ? -32.089 36.827  78.549  1.00 51.24 ? 503  ILE A N     1 
ATOM   3562  C CA    . ILE A  1 505  ? -32.452 35.896  77.481  1.00 53.15 ? 503  ILE A CA    1 
ATOM   3563  C C     . ILE A  1 505  ? -31.247 35.622  76.587  1.00 55.76 ? 503  ILE A C     1 
ATOM   3564  O O     . ILE A  1 505  ? -31.086 34.507  76.070  1.00 53.81 ? 503  ILE A O     1 
ATOM   3565  C CB    . ILE A  1 505  ? -33.662 36.426  76.677  1.00 50.60 ? 503  ILE A CB    1 
ATOM   3566  C CG1   . ILE A  1 505  ? -34.102 35.409  75.625  1.00 48.24 ? 503  ILE A CG1   1 
ATOM   3567  C CG2   . ILE A  1 505  ? -33.332 37.741  75.997  1.00 51.16 ? 503  ILE A CG2   1 
ATOM   3568  C CD1   . ILE A  1 505  ? -35.478 34.831  75.857  1.00 47.07 ? 503  ILE A CD1   1 
ATOM   3569  N N     . ASN A  1 506  ? -30.364 36.614  76.422  1.00 54.10 ? 504  ASN A N     1 
ATOM   3570  C CA    . ASN A  1 506  ? -29.139 36.469  75.643  1.00 57.61 ? 504  ASN A CA    1 
ATOM   3571  C C     . ASN A  1 506  ? -28.010 35.787  76.408  1.00 58.98 ? 504  ASN A C     1 
ATOM   3572  O O     . ASN A  1 506  ? -26.966 35.506  75.811  1.00 57.31 ? 504  ASN A O     1 
ATOM   3573  C CB    . ASN A  1 506  ? -28.652 37.841  75.164  1.00 58.54 ? 504  ASN A CB    1 
ATOM   3574  C CG    . ASN A  1 506  ? -29.384 38.326  73.925  1.00 63.18 ? 504  ASN A CG    1 
ATOM   3575  O OD1   . ASN A  1 506  ? -30.415 37.774  73.538  1.00 63.54 ? 504  ASN A OD1   1 
ATOM   3576  N ND2   . ASN A  1 506  ? -28.846 39.364  73.293  1.00 65.90 ? 504  ASN A ND2   1 
ATOM   3577  N N     . ASP A  1 507  ? -28.185 35.525  77.703  1.00 57.06 ? 505  ASP A N     1 
ATOM   3578  C CA    . ASP A  1 507  ? -27.130 34.930  78.515  1.00 60.28 ? 505  ASP A CA    1 
ATOM   3579  C C     . ASP A  1 507  ? -27.176 33.413  78.384  1.00 61.96 ? 505  ASP A C     1 
ATOM   3580  O O     . ASP A  1 507  ? -28.189 32.803  78.753  1.00 57.43 ? 505  ASP A O     1 
ATOM   3581  C CB    . ASP A  1 507  ? -27.286 35.335  79.972  1.00 59.63 ? 505  ASP A CB    1 
ATOM   3582  C CG    . ASP A  1 507  ? -26.052 35.028  80.806  1.00 61.71 ? 505  ASP A CG    1 
ATOM   3583  O OD1   . ASP A  1 507  ? -25.385 34.005  80.542  1.00 61.91 ? 505  ASP A OD1   1 
ATOM   3584  O OD2   . ASP A  1 507  ? -25.751 35.815  81.730  1.00 61.96 ? 505  ASP A OD2   1 
ATOM   3585  N N     . PRO A  1 508  ? -26.114 32.767  77.889  1.00 68.40 ? 506  PRO A N     1 
ATOM   3586  C CA    . PRO A  1 508  ? -26.146 31.300  77.753  1.00 66.10 ? 506  PRO A CA    1 
ATOM   3587  C C     . PRO A  1 508  ? -26.109 30.564  79.083  1.00 63.72 ? 506  PRO A C     1 
ATOM   3588  O O     . PRO A  1 508  ? -26.503 29.392  79.131  1.00 64.09 ? 506  PRO A O     1 
ATOM   3589  C CB    . PRO A  1 508  ? -24.895 30.991  76.913  1.00 66.23 ? 506  PRO A CB    1 
ATOM   3590  C CG    . PRO A  1 508  ? -24.427 32.319  76.371  1.00 68.20 ? 506  PRO A CG    1 
ATOM   3591  C CD    . PRO A  1 508  ? -24.862 33.341  77.371  1.00 66.78 ? 506  PRO A CD    1 
ATOM   3592  N N     . LYS A  1 509  ? -25.646 31.204  80.155  1.00 59.24 ? 507  LYS A N     1 
ATOM   3593  C CA    . LYS A  1 509  ? -25.637 30.596  81.479  1.00 62.48 ? 507  LYS A CA    1 
ATOM   3594  C C     . LYS A  1 509  ? -26.984 30.707  82.190  1.00 60.06 ? 507  LYS A C     1 
ATOM   3595  O O     . LYS A  1 509  ? -27.079 30.345  83.366  1.00 60.60 ? 507  LYS A O     1 
ATOM   3596  C CB    . LYS A  1 509  ? -24.538 31.226  82.340  1.00 61.65 ? 507  LYS A CB    1 
ATOM   3597  N N     . VAL A  1 510  ? -28.017 31.205  81.515  1.00 59.09 ? 508  VAL A N     1 
ATOM   3598  C CA    . VAL A  1 510  ? -29.356 31.315  82.082  1.00 55.85 ? 508  VAL A CA    1 
ATOM   3599  C C     . VAL A  1 510  ? -30.249 30.324  81.350  1.00 55.58 ? 508  VAL A C     1 
ATOM   3600  O O     . VAL A  1 510  ? -30.440 30.430  80.133  1.00 58.07 ? 508  VAL A O     1 
ATOM   3601  C CB    . VAL A  1 510  ? -29.909 32.745  81.975  1.00 56.33 ? 508  VAL A CB    1 
ATOM   3602  C CG1   . VAL A  1 510  ? -31.357 32.794  82.444  1.00 53.01 ? 508  VAL A CG1   1 
ATOM   3603  C CG2   . VAL A  1 510  ? -29.050 33.707  82.783  1.00 51.01 ? 508  VAL A CG2   1 
ATOM   3604  N N     . SER A  1 511  ? -30.778 29.351  82.085  1.00 52.28 ? 509  SER A N     1 
ATOM   3605  C CA    . SER A  1 511  ? -31.682 28.379  81.502  1.00 51.39 ? 509  SER A CA    1 
ATOM   3606  C C     . SER A  1 511  ? -33.066 28.990  81.318  1.00 50.88 ? 509  SER A C     1 
ATOM   3607  O O     . SER A  1 511  ? -33.392 30.048  81.866  1.00 53.02 ? 509  SER A O     1 
ATOM   3608  C CB    . SER A  1 511  ? -31.778 27.137  82.383  1.00 55.83 ? 509  SER A CB    1 
ATOM   3609  O OG    . SER A  1 511  ? -32.464 27.429  83.589  1.00 53.00 ? 509  SER A OG    1 
ATOM   3610  N N     . ILE A  1 512  ? -33.892 28.302  80.532  1.00 47.52 ? 510  ILE A N     1 
ATOM   3611  C CA    . ILE A  1 512  ? -35.281 28.719  80.391  1.00 50.67 ? 510  ILE A CA    1 
ATOM   3612  C C     . ILE A  1 512  ? -36.009 28.577  81.719  1.00 51.40 ? 510  ILE A C     1 
ATOM   3613  O O     . ILE A  1 512  ? -36.812 29.437  82.098  1.00 49.11 ? 510  ILE A O     1 
ATOM   3614  C CB    . ILE A  1 512  ? -35.967 27.916  79.275  1.00 50.32 ? 510  ILE A CB    1 
ATOM   3615  C CG1   . ILE A  1 512  ? -35.233 28.134  77.952  1.00 49.32 ? 510  ILE A CG1   1 
ATOM   3616  C CG2   . ILE A  1 512  ? -37.429 28.309  79.160  1.00 48.90 ? 510  ILE A CG2   1 
ATOM   3617  C CD1   . ILE A  1 512  ? -35.784 27.322  76.821  1.00 53.78 ? 510  ILE A CD1   1 
ATOM   3618  N N     . ASP A  1 513  ? -35.721 27.500  82.457  1.00 49.81 ? 511  ASP A N     1 
ATOM   3619  C CA    . ASP A  1 513  ? -36.364 27.282  83.750  1.00 47.84 ? 511  ASP A CA    1 
ATOM   3620  C C     . ASP A  1 513  ? -36.148 28.468  84.680  1.00 47.07 ? 511  ASP A C     1 
ATOM   3621  O O     . ASP A  1 513  ? -37.038 28.823  85.464  1.00 49.02 ? 511  ASP A O     1 
ATOM   3622  C CB    . ASP A  1 513  ? -35.836 25.998  84.393  1.00 50.60 ? 511  ASP A CB    1 
ATOM   3623  C CG    . ASP A  1 513  ? -36.318 24.742  83.684  1.00 56.50 ? 511  ASP A CG    1 
ATOM   3624  O OD1   . ASP A  1 513  ? -37.467 24.734  83.186  1.00 54.67 ? 511  ASP A OD1   1 
ATOM   3625  O OD2   . ASP A  1 513  ? -35.547 23.758  83.632  1.00 62.62 ? 511  ASP A OD2   1 
ATOM   3626  N N     . GLU A  1 514  ? -34.970 29.093  84.610  1.00 48.06 ? 512  GLU A N     1 
ATOM   3627  C CA    . GLU A  1 514  ? -34.732 30.315  85.368  1.00 46.93 ? 512  GLU A CA    1 
ATOM   3628  C C     . GLU A  1 514  ? -35.552 31.477  84.824  1.00 46.86 ? 512  GLU A C     1 
ATOM   3629  O O     . GLU A  1 514  ? -35.913 32.386  85.578  1.00 47.70 ? 512  GLU A O     1 
ATOM   3630  C CB    . GLU A  1 514  ? -33.245 30.665  85.344  1.00 48.40 ? 512  GLU A CB    1 
ATOM   3631  C CG    . GLU A  1 514  ? -32.349 29.619  85.987  1.00 54.04 ? 512  GLU A CG    1 
ATOM   3632  C CD    . GLU A  1 514  ? -30.875 29.973  85.888  1.00 57.64 ? 512  GLU A CD    1 
ATOM   3633  O OE1   . GLU A  1 514  ? -30.539 30.889  85.107  1.00 62.39 ? 512  GLU A OE1   1 
ATOM   3634  O OE2   . GLU A  1 514  ? -30.053 29.342  86.590  1.00 62.06 ? 512  GLU A OE2   1 
ATOM   3635  N N     . LEU A  1 515  ? -35.853 31.462  83.525  1.00 47.88 ? 513  LEU A N     1 
ATOM   3636  C CA    . LEU A  1 515  ? -36.560 32.570  82.894  1.00 49.68 ? 513  LEU A CA    1 
ATOM   3637  C C     . LEU A  1 515  ? -38.071 32.455  83.053  1.00 44.49 ? 513  LEU A C     1 
ATOM   3638  O O     . LEU A  1 515  ? -38.768 33.478  83.077  1.00 41.96 ? 513  LEU A O     1 
ATOM   3639  C CB    . LEU A  1 515  ? -36.196 32.640  81.410  1.00 48.95 ? 513  LEU A CB    1 
ATOM   3640  C CG    . LEU A  1 515  ? -34.801 33.131  81.025  1.00 45.70 ? 513  LEU A CG    1 
ATOM   3641  C CD1   . LEU A  1 515  ? -34.565 32.888  79.543  1.00 45.46 ? 513  LEU A CD1   1 
ATOM   3642  C CD2   . LEU A  1 515  ? -34.626 34.608  81.351  1.00 44.43 ? 513  LEU A CD2   1 
ATOM   3643  N N     . ILE A  1 516  ? -38.599 31.236  83.152  1.00 42.07 ? 514  ILE A N     1 
ATOM   3644  C CA    . ILE A  1 516  ? -40.031 31.034  83.333  1.00 45.76 ? 514  ILE A CA    1 
ATOM   3645  C C     . ILE A  1 516  ? -40.402 30.893  84.808  1.00 39.57 ? 514  ILE A C     1 
ATOM   3646  O O     . ILE A  1 516  ? -41.549 30.572  85.127  1.00 42.11 ? 514  ILE A O     1 
ATOM   3647  C CB    . ILE A  1 516  ? -40.526 29.818  82.537  1.00 43.66 ? 514  ILE A CB    1 
ATOM   3648  C CG1   . ILE A  1 516  ? -39.918 28.530  83.080  1.00 41.20 ? 514  ILE A CG1   1 
ATOM   3649  C CG2   . ILE A  1 516  ? -40.194 29.977  81.056  1.00 47.19 ? 514  ILE A CG2   1 
ATOM   3650  C CD1   . ILE A  1 516  ? -40.597 27.277  82.556  1.00 44.33 ? 514  ILE A CD1   1 
ATOM   3651  N N     . ALA A  1 517  ? -39.454 31.123  85.717  1.00 39.20 ? 515  ALA A N     1 
ATOM   3652  C CA    . ALA A  1 517  ? -39.747 31.066  87.144  1.00 40.61 ? 515  ALA A CA    1 
ATOM   3653  C C     . ALA A  1 517  ? -40.788 32.115  87.511  1.00 41.23 ? 515  ALA A C     1 
ATOM   3654  O O     . ALA A  1 517  ? -40.678 33.277  87.110  1.00 36.51 ? 515  ALA A O     1 
ATOM   3655  C CB    . ALA A  1 517  ? -38.473 31.294  87.948  1.00 40.85 ? 515  ALA A CB    1 
ATOM   3656  N N     . ASP A  1 518  ? -41.788 31.700  88.273  1.00 40.27 ? 516  ASP A N     1 
ATOM   3657  C CA    . ASP A  1 518  ? -42.876 32.569  88.700  1.00 37.28 ? 516  ASP A CA    1 
ATOM   3658  C C     . ASP A  1 518  ? -42.406 33.532  89.782  1.00 36.79 ? 516  ASP A C     1 
ATOM   3659  O O     . ASP A  1 518  ? -42.205 33.102  90.925  1.00 34.84 ? 516  ASP A O     1 
ATOM   3660  C CB    . ASP A  1 518  ? -44.031 31.714  89.215  1.00 37.02 ? 516  ASP A CB    1 
ATOM   3661  C CG    . ASP A  1 518  ? -45.316 32.508  89.417  1.00 38.79 ? 516  ASP A CG    1 
ATOM   3662  O OD1   . ASP A  1 518  ? -45.275 33.762  89.432  1.00 36.37 ? 516  ASP A OD1   1 
ATOM   3663  O OD2   . ASP A  1 518  ? -46.380 31.873  89.553  1.00 38.01 ? 516  ASP A OD2   1 
ATOM   3664  N N     . PRO A  1 519  ? -42.264 34.832  89.497  1.00 32.97 ? 517  PRO A N     1 
ATOM   3665  C CA    . PRO A  1 519  ? -41.869 35.766  90.563  1.00 34.45 ? 517  PRO A CA    1 
ATOM   3666  C C     . PRO A  1 519  ? -42.837 35.783  91.738  1.00 32.83 ? 517  PRO A C     1 
ATOM   3667  O O     . PRO A  1 519  ? -42.406 35.985  92.880  1.00 31.21 ? 517  PRO A O     1 
ATOM   3668  C CB    . PRO A  1 519  ? -41.830 37.121  89.837  1.00 31.52 ? 517  PRO A CB    1 
ATOM   3669  C CG    . PRO A  1 519  ? -42.818 36.972  88.724  1.00 33.69 ? 517  PRO A CG    1 
ATOM   3670  C CD    . PRO A  1 519  ? -42.663 35.540  88.263  1.00 37.20 ? 517  PRO A CD    1 
ATOM   3671  N N     . VAL A  1 520  ? -44.132 35.567  91.487  1.00 32.48 ? 518  VAL A N     1 
ATOM   3672  C CA    . VAL A  1 520  ? -45.123 35.543  92.562  1.00 34.33 ? 518  VAL A CA    1 
ATOM   3673  C C     . VAL A  1 520  ? -44.805 34.440  93.564  1.00 37.20 ? 518  VAL A C     1 
ATOM   3674  O O     . VAL A  1 520  ? -44.833 34.657  94.781  1.00 36.15 ? 518  VAL A O     1 
ATOM   3675  C CB    . VAL A  1 520  ? -46.537 35.367  91.980  1.00 33.55 ? 518  VAL A CB    1 
ATOM   3676  C CG1   . VAL A  1 520  ? -47.575 35.294  93.101  1.00 35.89 ? 518  VAL A CG1   1 
ATOM   3677  C CG2   . VAL A  1 520  ? -46.851 36.489  91.007  1.00 33.30 ? 518  VAL A CG2   1 
ATOM   3678  N N     . GLU A  1 521  ? -44.523 33.232  93.068  1.00 38.57 ? 519  GLU A N     1 
ATOM   3679  C CA    . GLU A  1 521  ? -44.275 32.110  93.969  1.00 36.59 ? 519  GLU A CA    1 
ATOM   3680  C C     . GLU A  1 521  ? -42.880 32.151  94.574  1.00 35.49 ? 519  GLU A C     1 
ATOM   3681  O O     . GLU A  1 521  ? -42.686 31.641  95.682  1.00 38.64 ? 519  GLU A O     1 
ATOM   3682  C CB    . GLU A  1 521  ? -44.489 30.782  93.247  1.00 39.12 ? 519  GLU A CB    1 
ATOM   3683  C CG    . GLU A  1 521  ? -45.910 30.570  92.747  1.00 39.46 ? 519  GLU A CG    1 
ATOM   3684  C CD    . GLU A  1 521  ? -46.962 30.709  93.840  1.00 45.86 ? 519  GLU A CD    1 
ATOM   3685  O OE1   . GLU A  1 521  ? -46.665 30.441  95.028  1.00 45.49 ? 519  GLU A OE1   1 
ATOM   3686  O OE2   . GLU A  1 521  ? -48.102 31.093  93.504  1.00 52.39 ? 519  GLU A OE2   1 
ATOM   3687  N N     . VAL A  1 522  ? -41.908 32.745  93.874  1.00 32.72 ? 520  VAL A N     1 
ATOM   3688  C CA    . VAL A  1 522  ? -40.592 32.960  94.466  1.00 33.67 ? 520  VAL A CA    1 
ATOM   3689  C C     . VAL A  1 522  ? -40.695 33.919  95.647  1.00 38.88 ? 520  VAL A C     1 
ATOM   3690  O O     . VAL A  1 522  ? -40.172 33.651  96.734  1.00 37.93 ? 520  VAL A O     1 
ATOM   3691  C CB    . VAL A  1 522  ? -39.594 33.470  93.409  1.00 35.44 ? 520  VAL A CB    1 
ATOM   3692  C CG1   . VAL A  1 522  ? -38.232 33.726  94.048  1.00 32.46 ? 520  VAL A CG1   1 
ATOM   3693  C CG2   . VAL A  1 522  ? -39.459 32.473  92.269  1.00 35.62 ? 520  VAL A CG2   1 
ATOM   3694  N N     . VAL A  1 523  ? -41.372 35.055  95.453  1.00 35.43 ? 521  VAL A N     1 
ATOM   3695  C CA    . VAL A  1 523  ? -41.518 36.025  96.537  1.00 34.29 ? 521  VAL A CA    1 
ATOM   3696  C C     . VAL A  1 523  ? -42.272 35.413  97.714  1.00 38.41 ? 521  VAL A C     1 
ATOM   3697  O O     . VAL A  1 523  ? -41.917 35.632  98.877  1.00 37.89 ? 521  VAL A O     1 
ATOM   3698  C CB    . VAL A  1 523  ? -42.213 37.302  96.026  1.00 34.99 ? 521  VAL A CB    1 
ATOM   3699  C CG1   . VAL A  1 523  ? -42.652 38.171  97.193  1.00 32.35 ? 521  VAL A CG1   1 
ATOM   3700  C CG2   . VAL A  1 523  ? -41.275 38.079  95.129  1.00 31.86 ? 521  VAL A CG2   1 
ATOM   3701  N N     . ARG A  1 524  ? -43.317 34.630  97.432  1.00 37.33 ? 522  ARG A N     1 
ATOM   3702  C CA    . ARG A  1 524  ? -44.139 34.090  98.510  1.00 42.16 ? 522  ARG A CA    1 
ATOM   3703  C C     . ARG A  1 524  ? -43.338 33.165  99.418  1.00 41.24 ? 522  ARG A C     1 
ATOM   3704  O O     . ARG A  1 524  ? -43.641 33.053  100.610 1.00 43.55 ? 522  ARG A O     1 
ATOM   3705  C CB    . ARG A  1 524  ? -45.347 33.350  97.936  1.00 39.33 ? 522  ARG A CB    1 
ATOM   3706  C CG    . ARG A  1 524  ? -46.383 32.982  98.988  1.00 46.31 ? 522  ARG A CG    1 
ATOM   3707  C CD    . ARG A  1 524  ? -47.308 31.887  98.502  1.00 45.15 ? 522  ARG A CD    1 
ATOM   3708  N NE    . ARG A  1 524  ? -47.927 32.227  97.227  1.00 49.09 ? 522  ARG A NE    1 
ATOM   3709  C CZ    . ARG A  1 524  ? -49.082 32.865  97.100  1.00 42.63 ? 522  ARG A CZ    1 
ATOM   3710  N NH1   . ARG A  1 524  ? -49.770 33.265  98.153  1.00 44.13 ? 522  ARG A NH1   1 
ATOM   3711  N NH2   . ARG A  1 524  ? -49.565 33.093  95.884  1.00 45.33 ? 522  ARG A NH2   1 
ATOM   3712  N N     . ALA A  1 525  ? -42.301 32.525  98.889  1.00 40.57 ? 523  ALA A N     1 
ATOM   3713  C CA    . ALA A  1 525  ? -41.517 31.563  99.645  1.00 42.49 ? 523  ALA A CA    1 
ATOM   3714  C C     . ALA A  1 525  ? -40.295 32.177  100.312 1.00 42.33 ? 523  ALA A C     1 
ATOM   3715  O O     . ALA A  1 525  ? -39.539 31.453  100.963 1.00 41.16 ? 523  ALA A O     1 
ATOM   3716  C CB    . ALA A  1 525  ? -41.081 30.408  98.736  1.00 38.22 ? 523  ALA A CB    1 
ATOM   3717  N N     . MET A  1 526  ? -40.079 33.481  100.179 1.00 36.07 ? 524  MET A N     1 
ATOM   3718  C CA    . MET A  1 526  ? -38.918 34.087  100.807 1.00 42.88 ? 524  MET A CA    1 
ATOM   3719  C C     . MET A  1 526  ? -39.119 34.184  102.322 1.00 42.61 ? 524  MET A C     1 
ATOM   3720  O O     . MET A  1 526  ? -40.256 34.217  102.804 1.00 40.98 ? 524  MET A O     1 
ATOM   3721  C CB    . MET A  1 526  ? -38.652 35.466  100.212 1.00 41.27 ? 524  MET A CB    1 
ATOM   3722  C CG    . MET A  1 526  ? -38.243 35.395  98.760  1.00 39.00 ? 524  MET A CG    1 
ATOM   3723  S SD    . MET A  1 526  ? -37.799 36.991  98.084  1.00 49.72 ? 524  MET A SD    1 
ATOM   3724  C CE    . MET A  1 526  ? -37.301 36.512  96.433  1.00 40.97 ? 524  MET A CE    1 
ATOM   3725  N N     . PRO A  1 527  ? -38.024 34.214  103.094 1.00 39.81 ? 525  PRO A N     1 
ATOM   3726  C CA    . PRO A  1 527  ? -38.165 34.251  104.562 1.00 41.82 ? 525  PRO A CA    1 
ATOM   3727  C C     . PRO A  1 527  ? -38.886 35.486  105.066 1.00 43.56 ? 525  PRO A C     1 
ATOM   3728  O O     . PRO A  1 527  ? -39.687 35.393  106.004 1.00 43.82 ? 525  PRO A O     1 
ATOM   3729  C CB    . PRO A  1 527  ? -36.710 34.213  105.055 1.00 41.71 ? 525  PRO A CB    1 
ATOM   3730  C CG    . PRO A  1 527  ? -35.905 33.714  103.898 1.00 43.87 ? 525  PRO A CG    1 
ATOM   3731  C CD    . PRO A  1 527  ? -36.611 34.205  102.674 1.00 43.85 ? 525  PRO A CD    1 
ATOM   3732  N N     . VAL A  1 528  ? -38.608 36.650  104.482 1.00 43.14 ? 526  VAL A N     1 
ATOM   3733  C CA    . VAL A  1 528  ? -39.323 37.882  104.789 1.00 37.47 ? 526  VAL A CA    1 
ATOM   3734  C C     . VAL A  1 528  ? -39.865 38.411  103.471 1.00 34.88 ? 526  VAL A C     1 
ATOM   3735  O O     . VAL A  1 528  ? -39.096 38.889  102.628 1.00 34.51 ? 526  VAL A O     1 
ATOM   3736  C CB    . VAL A  1 528  ? -38.428 38.924  105.468 1.00 36.92 ? 526  VAL A CB    1 
ATOM   3737  C CG1   . VAL A  1 528  ? -39.278 40.114  105.924 1.00 39.66 ? 526  VAL A CG1   1 
ATOM   3738  C CG2   . VAL A  1 528  ? -37.671 38.303  106.638 1.00 38.98 ? 526  VAL A CG2   1 
ATOM   3739  N N     . VAL A  1 529  ? -41.181 38.305  103.281 1.00 33.56 ? 527  VAL A N     1 
ATOM   3740  C CA    . VAL A  1 529  ? -41.801 38.782  102.053 1.00 34.74 ? 527  VAL A CA    1 
ATOM   3741  C C     . VAL A  1 529  ? -41.636 40.293  101.969 1.00 33.23 ? 527  VAL A C     1 
ATOM   3742  O O     . VAL A  1 529  ? -41.955 41.021  102.918 1.00 33.03 ? 527  VAL A O     1 
ATOM   3743  C CB    . VAL A  1 529  ? -43.280 38.373  102.002 1.00 31.96 ? 527  VAL A CB    1 
ATOM   3744  C CG1   . VAL A  1 529  ? -43.975 39.038  100.814 1.00 34.54 ? 527  VAL A CG1   1 
ATOM   3745  C CG2   . VAL A  1 529  ? -43.408 36.842  101.927 1.00 35.76 ? 527  VAL A CG2   1 
ATOM   3746  N N     . GLY A  1 530  ? -41.096 40.767  100.846 1.00 32.59 ? 528  GLY A N     1 
ATOM   3747  C CA    . GLY A  1 530  ? -40.901 42.186  100.633 1.00 28.02 ? 528  GLY A CA    1 
ATOM   3748  C C     . GLY A  1 530  ? -39.670 42.791  101.266 1.00 29.59 ? 528  GLY A C     1 
ATOM   3749  O O     . GLY A  1 530  ? -39.570 44.023  101.316 1.00 26.23 ? 528  GLY A O     1 
ATOM   3750  N N     . ALA A  1 531  ? -38.734 41.976  101.761 1.00 30.04 ? 529  ALA A N     1 
ATOM   3751  C CA    . ALA A  1 531  ? -37.503 42.512  102.330 1.00 29.99 ? 529  ALA A CA    1 
ATOM   3752  C C     . ALA A  1 531  ? -36.767 43.385  101.314 1.00 32.70 ? 529  ALA A C     1 
ATOM   3753  O O     . ALA A  1 531  ? -36.676 43.052  100.131 1.00 29.42 ? 529  ALA A O     1 
ATOM   3754  C CB    . ALA A  1 531  ? -36.603 41.371  102.809 1.00 33.56 ? 529  ALA A CB    1 
ATOM   3755  N N     . LYS A  1 532  ? -36.264 44.523  101.787 1.00 28.09 ? 530  LYS A N     1 
ATOM   3756  C CA    . LYS A  1 532  ? -35.435 45.415  100.984 1.00 32.44 ? 530  LYS A CA    1 
ATOM   3757  C C     . LYS A  1 532  ? -34.213 44.679  100.433 1.00 29.47 ? 530  LYS A C     1 
ATOM   3758  O O     . LYS A  1 532  ? -33.724 43.715  101.024 1.00 27.45 ? 530  LYS A O     1 
ATOM   3759  C CB    . LYS A  1 532  ? -35.001 46.610  101.849 1.00 32.00 ? 530  LYS A CB    1 
ATOM   3760  C CG    . LYS A  1 532  ? -33.942 47.531  101.244 1.00 36.87 ? 530  LYS A CG    1 
ATOM   3761  C CD    . LYS A  1 532  ? -33.581 48.677  102.191 1.00 28.96 ? 530  LYS A CD    1 
ATOM   3762  C CE    . LYS A  1 532  ? -32.741 48.191  103.365 1.00 29.45 ? 530  LYS A CE    1 
ATOM   3763  N NZ    . LYS A  1 532  ? -31.427 47.668  102.918 1.00 27.79 ? 530  LYS A NZ    1 
ATOM   3764  N N     . HIS A  1 533  ? -33.724 45.130  99.277  1.00 29.11 ? 531  HIS A N     1 
ATOM   3765  C CA    . HIS A  1 533  ? -32.477 44.599  98.742  1.00 27.68 ? 531  HIS A CA    1 
ATOM   3766  C C     . HIS A  1 533  ? -31.353 44.761  99.758  1.00 30.22 ? 531  HIS A C     1 
ATOM   3767  O O     . HIS A  1 533  ? -31.195 45.826  100.357 1.00 28.37 ? 531  HIS A O     1 
ATOM   3768  C CB    . HIS A  1 533  ? -32.108 45.304  97.442  1.00 27.97 ? 531  HIS A CB    1 
ATOM   3769  C CG    . HIS A  1 533  ? -31.018 44.615  96.680  1.00 32.84 ? 531  HIS A CG    1 
ATOM   3770  N ND1   . HIS A  1 533  ? -29.708 44.587  97.115  1.00 29.21 ? 531  HIS A ND1   1 
ATOM   3771  C CD2   . HIS A  1 533  ? -31.047 43.913  95.522  1.00 31.74 ? 531  HIS A CD2   1 
ATOM   3772  C CE1   . HIS A  1 533  ? -28.976 43.905  96.253  1.00 32.73 ? 531  HIS A CE1   1 
ATOM   3773  N NE2   . HIS A  1 533  ? -29.764 43.480  95.279  1.00 37.71 ? 531  HIS A NE2   1 
ATOM   3774  N N     . ASP A  1 534  ? -30.568 43.694  99.940  1.00 32.44 ? 532  ASP A N     1 
ATOM   3775  C CA    . ASP A  1 534  ? -29.529 43.685  100.968 1.00 33.89 ? 532  ASP A CA    1 
ATOM   3776  C C     . ASP A  1 534  ? -28.447 44.729  100.731 1.00 32.44 ? 532  ASP A C     1 
ATOM   3777  O O     . ASP A  1 534  ? -27.815 45.184  101.691 1.00 34.37 ? 532  ASP A O     1 
ATOM   3778  C CB    . ASP A  1 534  ? -28.882 42.303  101.046 1.00 37.49 ? 532  ASP A CB    1 
ATOM   3779  C CG    . ASP A  1 534  ? -29.638 41.365  101.948 1.00 43.74 ? 532  ASP A CG    1 
ATOM   3780  O OD1   . ASP A  1 534  ? -30.585 41.834  102.616 1.00 43.24 ? 532  ASP A OD1   1 
ATOM   3781  O OD2   . ASP A  1 534  ? -29.279 40.167  102.001 1.00 54.80 ? 532  ASP A OD2   1 
ATOM   3782  N N     . ARG A  1 535  ? -28.193 45.102  99.480  1.00 27.13 ? 533  ARG A N     1 
ATOM   3783  C CA    . ARG A  1 535  ? -27.027 45.907  99.144  1.00 28.16 ? 533  ARG A CA    1 
ATOM   3784  C C     . ARG A  1 535  ? -27.367 47.374  98.905  1.00 32.08 ? 533  ARG A C     1 
ATOM   3785  O O     . ARG A  1 535  ? -26.486 48.151  98.518  1.00 29.78 ? 533  ARG A O     1 
ATOM   3786  C CB    . ARG A  1 535  ? -26.317 45.316  97.924  1.00 33.29 ? 533  ARG A CB    1 
ATOM   3787  N N     . ILE A  1 536  ? -28.612 47.776  99.146  1.00 25.64 ? 534  ILE A N     1 
ATOM   3788  C CA    A ILE A  1 536  ? -29.034 49.162  98.993  0.48 29.16 ? 534  ILE A CA    1 
ATOM   3789  C CA    B ILE A  1 536  ? -29.048 49.160  98.989  0.52 29.17 ? 534  ILE A CA    1 
ATOM   3790  C C     . ILE A  1 536  ? -29.363 49.711  100.372 1.00 28.63 ? 534  ILE A C     1 
ATOM   3791  O O     . ILE A  1 536  ? -30.176 49.132  101.106 1.00 29.01 ? 534  ILE A O     1 
ATOM   3792  C CB    A ILE A  1 536  ? -30.236 49.288  98.043  0.48 27.40 ? 534  ILE A CB    1 
ATOM   3793  C CB    B ILE A  1 536  ? -30.268 49.269  98.062  0.52 27.39 ? 534  ILE A CB    1 
ATOM   3794  C CG1   A ILE A  1 536  ? -29.904 48.645  96.694  0.48 27.49 ? 534  ILE A CG1   1 
ATOM   3795  C CG1   B ILE A  1 536  ? -29.920 48.757  96.661  0.52 27.50 ? 534  ILE A CG1   1 
ATOM   3796  C CG2   A ILE A  1 536  ? -30.616 50.753  97.864  0.48 27.87 ? 534  ILE A CG2   1 
ATOM   3797  C CG2   B ILE A  1 536  ? -30.762 50.710  98.006  0.52 27.88 ? 534  ILE A CG2   1 
ATOM   3798  C CD1   A ILE A  1 536  ? -31.077 48.592  95.752  0.48 25.41 ? 534  ILE A CD1   1 
ATOM   3799  C CD1   B ILE A  1 536  ? -29.117 49.733  95.846  0.52 25.40 ? 534  ILE A CD1   1 
ATOM   3800  N N     . ALA A  1 537  ? -28.723 50.820  100.729 1.00 26.59 ? 535  ALA A N     1 
ATOM   3801  C CA    . ALA A  1 537  ? -28.956 51.427  102.029 1.00 28.25 ? 535  ALA A CA    1 
ATOM   3802  C C     . ALA A  1 537  ? -30.196 52.311  101.991 1.00 24.61 ? 535  ALA A C     1 
ATOM   3803  O O     . ALA A  1 537  ? -30.360 53.122  101.073 1.00 24.38 ? 535  ALA A O     1 
ATOM   3804  C CB    . ALA A  1 537  ? -27.744 52.251  102.456 1.00 23.15 ? 535  ALA A CB    1 
ATOM   3805  N N     . LEU A  1 538  ? -31.056 52.161  102.995 1.00 23.15 ? 536  LEU A N     1 
ATOM   3806  C CA    . LEU A  1 538  ? -32.047 53.188  103.268 1.00 25.25 ? 536  LEU A CA    1 
ATOM   3807  C C     . LEU A  1 538  ? -31.322 54.511  103.501 1.00 25.47 ? 536  LEU A C     1 
ATOM   3808  O O     . LEU A  1 538  ? -30.189 54.521  103.994 1.00 25.14 ? 536  LEU A O     1 
ATOM   3809  C CB    . LEU A  1 538  ? -32.886 52.826  104.499 1.00 24.41 ? 536  LEU A CB    1 
ATOM   3810  C CG    . LEU A  1 538  ? -33.903 51.703  104.316 1.00 25.59 ? 536  LEU A CG    1 
ATOM   3811  C CD1   . LEU A  1 538  ? -34.568 51.338  105.647 1.00 31.63 ? 536  LEU A CD1   1 
ATOM   3812  C CD2   . LEU A  1 538  ? -34.948 52.100  103.283 1.00 27.97 ? 536  LEU A CD2   1 
ATOM   3813  N N     . PRO A  1 539  ? -31.929 55.639  103.126 1.00 22.38 ? 537  PRO A N     1 
ATOM   3814  C CA    . PRO A  1 539  ? -31.234 56.929  103.310 1.00 21.30 ? 537  PRO A CA    1 
ATOM   3815  C C     . PRO A  1 539  ? -30.707 57.142  104.728 1.00 21.31 ? 537  PRO A C     1 
ATOM   3816  O O     . PRO A  1 539  ? -29.565 57.592  104.883 1.00 23.36 ? 537  PRO A O     1 
ATOM   3817  C CB    . PRO A  1 539  ? -32.306 57.952  102.913 1.00 22.08 ? 537  PRO A CB    1 
ATOM   3818  C CG    . PRO A  1 539  ? -33.121 57.225  101.857 1.00 20.13 ? 537  PRO A CG    1 
ATOM   3819  C CD    . PRO A  1 539  ? -33.129 55.755  102.272 1.00 19.29 ? 537  PRO A CD    1 
ATOM   3820  N N     . ALA A  1 540  ? -31.484 56.788  105.760 1.00 19.38 ? 538  ALA A N     1 
ATOM   3821  C CA    . ALA A  1 540  ? -31.053 56.970  107.147 1.00 23.97 ? 538  ALA A CA    1 
ATOM   3822  C C     . ALA A  1 540  ? -29.857 56.101  107.518 1.00 25.20 ? 538  ALA A C     1 
ATOM   3823  O O     . ALA A  1 540  ? -29.214 56.352  108.551 1.00 25.52 ? 538  ALA A O     1 
ATOM   3824  C CB    . ALA A  1 540  ? -32.198 56.657  108.115 1.00 28.86 ? 538  ALA A CB    1 
ATOM   3825  N N     . GLU A  1 541  ? -29.564 55.071  106.726 1.00 23.28 ? 539  GLU A N     1 
ATOM   3826  C CA    . GLU A  1 541  ? -28.477 54.139  107.015 1.00 26.70 ? 539  GLU A CA    1 
ATOM   3827  C C     . GLU A  1 541  ? -27.290 54.338  106.076 1.00 26.24 ? 539  GLU A C     1 
ATOM   3828  O O     . GLU A  1 541  ? -26.422 53.468  105.978 1.00 23.30 ? 539  GLU A O     1 
ATOM   3829  C CB    . GLU A  1 541  ? -29.011 52.708  106.948 1.00 26.88 ? 539  GLU A CB    1 
ATOM   3830  C CG    . GLU A  1 541  ? -30.256 52.526  107.852 1.00 31.85 ? 539  GLU A CG    1 
ATOM   3831  C CD    . GLU A  1 541  ? -30.857 51.125  107.829 1.00 41.05 ? 539  GLU A CD    1 
ATOM   3832  O OE1   . GLU A  1 541  ? -30.404 50.281  107.029 1.00 45.64 ? 539  GLU A OE1   1 
ATOM   3833  O OE2   . GLU A  1 541  ? -31.796 50.868  108.615 1.00 43.92 ? 539  GLU A OE2   1 
ATOM   3834  N N     . LEU A  1 542  ? -27.223 55.495  105.413 1.00 23.08 ? 540  LEU A N     1 
ATOM   3835  C CA    A LEU A  1 542  ? -26.187 55.730  104.414 0.63 23.91 ? 540  LEU A CA    1 
ATOM   3836  C CA    B LEU A  1 542  ? -26.183 55.733  104.417 0.37 23.91 ? 540  LEU A CA    1 
ATOM   3837  C C     . LEU A  1 542  ? -24.785 55.589  105.002 1.00 24.48 ? 540  LEU A C     1 
ATOM   3838  O O     . LEU A  1 542  ? -23.849 55.209  104.291 1.00 25.30 ? 540  LEU A O     1 
ATOM   3839  C CB    A LEU A  1 542  ? -26.380 57.122  103.801 0.63 21.89 ? 540  LEU A CB    1 
ATOM   3840  C CB    B LEU A  1 542  ? -26.344 57.126  103.808 0.37 22.05 ? 540  LEU A CB    1 
ATOM   3841  C CG    A LEU A  1 542  ? -25.880 57.359  102.374 0.63 22.94 ? 540  LEU A CG    1 
ATOM   3842  C CG    B LEU A  1 542  ? -27.151 57.246  102.518 0.37 22.82 ? 540  LEU A CG    1 
ATOM   3843  C CD1   A LEU A  1 542  ? -26.505 56.364  101.410 0.63 23.81 ? 540  LEU A CD1   1 
ATOM   3844  C CD1   B LEU A  1 542  ? -26.980 58.638  101.925 0.37 20.53 ? 540  LEU A CD1   1 
ATOM   3845  C CD2   A LEU A  1 542  ? -26.169 58.792  101.931 0.63 20.10 ? 540  LEU A CD2   1 
ATOM   3846  C CD2   B LEU A  1 542  ? -26.739 56.172  101.524 0.37 23.70 ? 540  LEU A CD2   1 
ATOM   3847  N N     . PHE A  1 543  ? -24.617 55.881  106.287 1.00 22.78 ? 541  PHE A N     1 
ATOM   3848  C CA    . PHE A  1 543  ? -23.304 55.840  106.906 1.00 23.15 ? 541  PHE A CA    1 
ATOM   3849  C C     . PHE A  1 543  ? -23.116 54.627  107.810 1.00 26.86 ? 541  PHE A C     1 
ATOM   3850  O O     . PHE A  1 543  ? -22.122 54.567  108.537 1.00 28.38 ? 541  PHE A O     1 
ATOM   3851  C CB    . PHE A  1 543  ? -23.064 57.151  107.661 1.00 22.86 ? 541  PHE A CB    1 
ATOM   3852  C CG    . PHE A  1 543  ? -23.289 58.359  106.802 1.00 22.30 ? 541  PHE A CG    1 
ATOM   3853  C CD1   . PHE A  1 543  ? -22.649 58.462  105.581 1.00 22.82 ? 541  PHE A CD1   1 
ATOM   3854  C CD2   . PHE A  1 543  ? -24.190 59.345  107.167 1.00 25.28 ? 541  PHE A CD2   1 
ATOM   3855  C CE1   . PHE A  1 543  ? -22.867 59.542  104.751 1.00 23.07 ? 541  PHE A CE1   1 
ATOM   3856  C CE2   . PHE A  1 543  ? -24.412 60.445  106.341 1.00 21.23 ? 541  PHE A CE2   1 
ATOM   3857  C CZ    . PHE A  1 543  ? -23.755 60.540  105.134 1.00 26.39 ? 541  PHE A CZ    1 
ATOM   3858  N N     . GLY A  1 544  ? -24.031 53.657  107.767 1.00 29.70 ? 542  GLY A N     1 
ATOM   3859  C CA    . GLY A  1 544  ? -23.885 52.433  108.549 1.00 29.15 ? 542  GLY A CA    1 
ATOM   3860  C C     . GLY A  1 544  ? -23.806 52.678  110.048 1.00 34.52 ? 542  GLY A C     1 
ATOM   3861  O O     . GLY A  1 544  ? -24.545 53.492  110.620 1.00 29.81 ? 542  GLY A O     1 
ATOM   3862  N N     . ASP A  1 545  ? -22.889 51.952  110.701 1.00 32.12 ? 543  ASP A N     1 
ATOM   3863  C CA    . ASP A  1 545  ? -22.693 52.048  112.142 1.00 34.38 ? 543  ASP A CA    1 
ATOM   3864  C C     . ASP A  1 545  ? -22.001 53.332  112.580 1.00 31.74 ? 543  ASP A C     1 
ATOM   3865  O O     . ASP A  1 545  ? -21.994 53.625  113.778 1.00 33.75 ? 543  ASP A O     1 
ATOM   3866  C CB    . ASP A  1 545  ? -21.868 50.863  112.655 1.00 35.47 ? 543  ASP A CB    1 
ATOM   3867  C CG    . ASP A  1 545  ? -22.562 49.533  112.455 1.00 46.49 ? 543  ASP A CG    1 
ATOM   3868  O OD1   . ASP A  1 545  ? -23.802 49.518  112.280 1.00 50.08 ? 543  ASP A OD1   1 
ATOM   3869  O OD2   . ASP A  1 545  ? -21.864 48.496  112.478 1.00 55.91 ? 543  ASP A OD2   1 
ATOM   3870  N N     . ALA A  1 546  ? -21.388 54.080  111.664 1.00 29.99 ? 544  ALA A N     1 
ATOM   3871  C CA    . ALA A  1 546  ? -20.690 55.299  112.065 1.00 29.60 ? 544  ALA A CA    1 
ATOM   3872  C C     . ALA A  1 546  ? -21.651 56.297  112.699 1.00 32.02 ? 544  ALA A C     1 
ATOM   3873  O O     . ALA A  1 546  ? -21.388 56.827  113.783 1.00 29.75 ? 544  ALA A O     1 
ATOM   3874  C CB    . ALA A  1 546  ? -19.976 55.922  110.866 1.00 27.88 ? 544  ALA A CB    1 
ATOM   3875  N N     . ARG A  1 547  ? -22.779 56.559  112.042 1.00 29.94 ? 545  ARG A N     1 
ATOM   3876  C CA    . ARG A  1 547  ? -23.686 57.587  112.527 1.00 24.84 ? 545  ARG A CA    1 
ATOM   3877  C C     . ARG A  1 547  ? -24.961 57.534  111.706 1.00 27.46 ? 545  ARG A C     1 
ATOM   3878  O O     . ARG A  1 547  ? -24.976 57.019  110.586 1.00 24.38 ? 545  ARG A O     1 
ATOM   3879  C CB    . ARG A  1 547  ? -23.067 58.978  112.428 1.00 28.51 ? 545  ARG A CB    1 
ATOM   3880  C CG    . ARG A  1 547  ? -22.709 59.324  111.033 1.00 27.84 ? 545  ARG A CG    1 
ATOM   3881  C CD    . ARG A  1 547  ? -22.043 60.668  110.944 1.00 30.13 ? 545  ARG A CD    1 
ATOM   3882  N NE    . ARG A  1 547  ? -21.395 60.816  109.651 1.00 28.12 ? 545  ARG A NE    1 
ATOM   3883  C CZ    . ARG A  1 547  ? -21.815 61.638  108.700 1.00 25.07 ? 545  ARG A CZ    1 
ATOM   3884  N NH1   . ARG A  1 547  ? -22.867 62.421  108.881 1.00 27.15 ? 545  ARG A NH1   1 
ATOM   3885  N NH2   . ARG A  1 547  ? -21.169 61.669  107.542 1.00 27.60 ? 545  ARG A NH2   1 
ATOM   3886  N N     . THR A  1 548  ? -26.026 58.071  112.286 1.00 25.86 ? 546  THR A N     1 
ATOM   3887  C CA    . THR A  1 548  ? -27.332 58.108  111.643 1.00 22.59 ? 546  THR A CA    1 
ATOM   3888  C C     . THR A  1 548  ? -27.405 59.335  110.750 1.00 22.15 ? 546  THR A C     1 
ATOM   3889  O O     . THR A  1 548  ? -27.145 60.456  111.202 1.00 21.79 ? 546  THR A O     1 
ATOM   3890  C CB    . THR A  1 548  ? -28.450 58.148  112.685 1.00 26.12 ? 546  THR A CB    1 
ATOM   3891  O OG1   . THR A  1 548  ? -28.275 57.066  113.610 1.00 29.28 ? 546  THR A OG1   1 
ATOM   3892  C CG2   . THR A  1 548  ? -29.818 58.027  112.011 1.00 26.12 ? 546  THR A CG2   1 
ATOM   3893  N N     . ASN A  1 549  ? -27.754 59.116  109.482 1.00 22.20 ? 547  ASN A N     1 
ATOM   3894  C CA    . ASN A  1 549  ? -27.904 60.216  108.544 1.00 23.46 ? 547  ASN A CA    1 
ATOM   3895  C C     . ASN A  1 549  ? -29.050 61.121  108.985 1.00 21.55 ? 547  ASN A C     1 
ATOM   3896  O O     . ASN A  1 549  ? -30.012 60.670  109.605 1.00 23.16 ? 547  ASN A O     1 
ATOM   3897  C CB    . ASN A  1 549  ? -28.154 59.651  107.139 1.00 22.68 ? 547  ASN A CB    1 
ATOM   3898  C CG    . ASN A  1 549  ? -28.090 60.709  106.055 1.00 24.49 ? 547  ASN A CG    1 
ATOM   3899  O OD1   . ASN A  1 549  ? -27.622 61.817  106.281 1.00 20.03 ? 547  ASN A OD1   1 
ATOM   3900  N ND2   . ASN A  1 549  ? -28.563 60.361  104.861 1.00 20.17 ? 547  ASN A ND2   1 
ATOM   3901  N N     . SER A  1 550  ? -28.931 62.422  108.705 1.00 20.44 ? 548  SER A N     1 
ATOM   3902  C CA    . SER A  1 550  ? -30.056 63.303  108.992 1.00 19.37 ? 548  SER A CA    1 
ATOM   3903  C C     . SER A  1 550  ? -31.211 63.003  108.038 1.00 21.48 ? 548  SER A C     1 
ATOM   3904  O O     . SER A  1 550  ? -31.021 62.484  106.939 1.00 24.09 ? 548  SER A O     1 
ATOM   3905  C CB    . SER A  1 550  ? -29.661 64.773  108.858 1.00 21.23 ? 548  SER A CB    1 
ATOM   3906  O OG    . SER A  1 550  ? -29.106 65.010  107.575 1.00 21.98 ? 548  SER A OG    1 
ATOM   3907  N N     . ALA A  1 551  ? -32.420 63.328  108.477 1.00 20.63 ? 549  ALA A N     1 
ATOM   3908  C CA    . ALA A  1 551  ? -33.624 63.112  107.680 1.00 23.58 ? 549  ALA A CA    1 
ATOM   3909  C C     . ALA A  1 551  ? -34.108 64.436  107.108 1.00 23.52 ? 549  ALA A C     1 
ATOM   3910  O O     . ALA A  1 551  ? -34.057 65.471  107.779 1.00 22.44 ? 549  ALA A O     1 
ATOM   3911  C CB    . ALA A  1 551  ? -34.738 62.467  108.512 1.00 24.71 ? 549  ALA A CB    1 
ATOM   3912  N N     . GLY A  1 552  ? -34.564 64.403  105.860 1.00 21.03 ? 550  GLY A N     1 
ATOM   3913  C CA    . GLY A  1 552  ? -35.173 65.548  105.233 1.00 22.14 ? 550  GLY A CA    1 
ATOM   3914  C C     . GLY A  1 552  ? -36.687 65.446  105.229 1.00 22.50 ? 550  GLY A C     1 
ATOM   3915  O O     . GLY A  1 552  ? -37.294 64.668  105.972 1.00 24.22 ? 550  GLY A O     1 
ATOM   3916  N N     . LEU A  1 553  ? -37.305 66.238  104.363 1.00 23.01 ? 551  LEU A N     1 
ATOM   3917  C CA    . LEU A  1 553  ? -38.745 66.238  104.182 1.00 23.81 ? 551  LEU A CA    1 
ATOM   3918  C C     . LEU A  1 553  ? -39.022 66.217  102.692 1.00 23.10 ? 551  LEU A C     1 
ATOM   3919  O O     . LEU A  1 553  ? -38.272 66.798  101.904 1.00 22.67 ? 551  LEU A O     1 
ATOM   3920  C CB    . LEU A  1 553  ? -39.413 67.477  104.804 1.00 26.04 ? 551  LEU A CB    1 
ATOM   3921  C CG    . LEU A  1 553  ? -39.314 67.695  106.311 1.00 26.84 ? 551  LEU A CG    1 
ATOM   3922  C CD1   . LEU A  1 553  ? -39.870 69.084  106.646 1.00 25.20 ? 551  LEU A CD1   1 
ATOM   3923  C CD2   . LEU A  1 553  ? -40.046 66.591  107.079 1.00 27.44 ? 551  LEU A CD2   1 
ATOM   3924  N N     . ASP A  1 554  ? -40.105 65.552  102.310 1.00 24.65 ? 552  ASP A N     1 
ATOM   3925  C CA    . ASP A  1 554  ? -40.450 65.408  100.898 1.00 26.55 ? 552  ASP A CA    1 
ATOM   3926  C C     . ASP A  1 554  ? -41.418 66.529  100.543 1.00 20.50 ? 552  ASP A C     1 
ATOM   3927  O O     . ASP A  1 554  ? -42.587 66.496  100.922 1.00 21.39 ? 552  ASP A O     1 
ATOM   3928  C CB    . ASP A  1 554  ? -41.044 64.031  100.642 1.00 23.34 ? 552  ASP A CB    1 
ATOM   3929  C CG    . ASP A  1 554  ? -41.357 63.779  99.167  1.00 24.51 ? 552  ASP A CG    1 
ATOM   3930  O OD1   . ASP A  1 554  ? -41.184 64.692  98.317  1.00 25.29 ? 552  ASP A OD1   1 
ATOM   3931  O OD2   . ASP A  1 554  ? -41.760 62.639  98.868  1.00 26.20 ? 552  ASP A OD2   1 
ATOM   3932  N N     . LEU A  1 555  ? -40.918 67.547  99.850  1.00 24.28 ? 553  LEU A N     1 
ATOM   3933  C CA    . LEU A  1 555  ? -41.755 68.677  99.492  1.00 23.14 ? 553  LEU A CA    1 
ATOM   3934  C C     . LEU A  1 555  ? -42.650 68.383  98.299  1.00 25.70 ? 553  LEU A C     1 
ATOM   3935  O O     . LEU A  1 555  ? -43.338 69.297  97.832  1.00 23.49 ? 553  LEU A O     1 
ATOM   3936  C CB    . LEU A  1 555  ? -40.889 69.909  99.223  1.00 23.32 ? 553  LEU A CB    1 
ATOM   3937  C CG    . LEU A  1 555  ? -40.088 70.408  100.437 1.00 22.98 ? 553  LEU A CG    1 
ATOM   3938  C CD1   . LEU A  1 555  ? -39.399 71.726  100.124 1.00 28.71 ? 553  LEU A CD1   1 
ATOM   3939  C CD2   . LEU A  1 555  ? -41.005 70.560  101.664 1.00 24.04 ? 553  LEU A CD2   1 
ATOM   3940  N N     . SER A  1 556  ? -42.648 67.144  97.794  1.00 27.39 ? 554  SER A N     1 
ATOM   3941  C CA    . SER A  1 556  ? -43.625 66.696  96.803  1.00 24.98 ? 554  SER A CA    1 
ATOM   3942  C C     . SER A  1 556  ? -44.781 65.915  97.430  1.00 25.79 ? 554  SER A C     1 
ATOM   3943  O O     . SER A  1 556  ? -45.730 65.551  96.730  1.00 22.78 ? 554  SER A O     1 
ATOM   3944  C CB    . SER A  1 556  ? -42.935 65.844  95.738  1.00 23.74 ? 554  SER A CB    1 
ATOM   3945  O OG    . SER A  1 556  ? -42.751 64.511  96.198  1.00 24.92 ? 554  SER A OG    1 
ATOM   3946  N N     . ASN A  1 557  ? -44.734 65.671  98.730  1.00 23.61 ? 555  ASN A N     1 
ATOM   3947  C CA    . ASN A  1 557  ? -45.731 64.871  99.425  1.00 22.50 ? 555  ASN A CA    1 
ATOM   3948  C C     . ASN A  1 557  ? -46.776 65.819  100.014 1.00 25.73 ? 555  ASN A C     1 
ATOM   3949  O O     . ASN A  1 557  ? -46.435 66.704  100.806 1.00 22.70 ? 555  ASN A O     1 
ATOM   3950  C CB    . ASN A  1 557  ? -45.028 64.020  100.493 1.00 21.59 ? 555  ASN A CB    1 
ATOM   3951  C CG    . ASN A  1 557  ? -45.984 63.149  101.293 1.00 21.29 ? 555  ASN A CG    1 
ATOM   3952  O OD1   . ASN A  1 557  ? -46.986 63.629  101.817 1.00 23.16 ? 555  ASN A OD1   1 
ATOM   3953  N ND2   . ASN A  1 557  ? -45.674 61.854  101.387 1.00 22.72 ? 555  ASN A ND2   1 
ATOM   3954  N N     . GLU A  1 558  ? -48.045 65.665  99.593  1.00 27.16 ? 556  GLU A N     1 
ATOM   3955  C CA    . GLU A  1 558  ? -49.082 66.611  100.016 1.00 24.63 ? 556  GLU A CA    1 
ATOM   3956  C C     . GLU A  1 558  ? -49.334 66.556  101.513 1.00 24.50 ? 556  GLU A C     1 
ATOM   3957  O O     . GLU A  1 558  ? -49.639 67.583  102.131 1.00 25.53 ? 556  GLU A O     1 
ATOM   3958  C CB    . GLU A  1 558  ? -50.402 66.372  99.273  1.00 27.15 ? 556  GLU A CB    1 
ATOM   3959  C CG    . GLU A  1 558  ? -50.366 66.655  97.795  1.00 28.92 ? 556  GLU A CG    1 
ATOM   3960  C CD    . GLU A  1 558  ? -50.179 68.132  97.409  1.00 27.98 ? 556  GLU A CD    1 
ATOM   3961  O OE1   . GLU A  1 558  ? -50.229 69.036  98.273  1.00 27.15 ? 556  GLU A OE1   1 
ATOM   3962  O OE2   . GLU A  1 558  ? -49.982 68.383  96.199  1.00 26.44 ? 556  GLU A OE2   1 
ATOM   3963  N N     . GLU A  1 559  ? -49.244 65.369  102.117 1.00 24.08 ? 557  GLU A N     1 
ATOM   3964  C CA    . GLU A  1 559  ? -49.382 65.293  103.570 1.00 27.82 ? 557  GLU A CA    1 
ATOM   3965  C C     . GLU A  1 559  ? -48.279 66.086  104.256 1.00 26.02 ? 557  GLU A C     1 
ATOM   3966  O O     . GLU A  1 559  ? -48.540 66.822  105.214 1.00 24.63 ? 557  GLU A O     1 
ATOM   3967  C CB    . GLU A  1 559  ? -49.346 63.840  104.050 1.00 24.97 ? 557  GLU A CB    1 
ATOM   3968  C CG    . GLU A  1 559  ? -50.437 62.945  103.516 1.00 31.78 ? 557  GLU A CG    1 
ATOM   3969  C CD    . GLU A  1 559  ? -51.818 63.284  104.077 1.00 43.14 ? 557  GLU A CD    1 
ATOM   3970  O OE1   . GLU A  1 559  ? -51.903 63.842  105.197 1.00 43.43 ? 557  GLU A OE1   1 
ATOM   3971  O OE2   . GLU A  1 559  ? -52.826 62.989  103.387 1.00 45.01 ? 557  GLU A OE2   1 
ATOM   3972  N N     . THR A  1 560  ? -47.038 65.938  103.778 1.00 24.81 ? 558  THR A N     1 
ATOM   3973  C CA    . THR A  1 560  ? -45.925 66.711  104.327 1.00 24.07 ? 558  THR A CA    1 
ATOM   3974  C C     . THR A  1 560  ? -46.139 68.205  104.119 1.00 22.96 ? 558  THR A C     1 
ATOM   3975  O O     . THR A  1 560  ? -45.937 69.003  105.037 1.00 22.02 ? 558  THR A O     1 
ATOM   3976  C CB    . THR A  1 560  ? -44.603 66.269  103.682 1.00 20.88 ? 558  THR A CB    1 
ATOM   3977  O OG1   . THR A  1 560  ? -44.405 64.869  103.906 1.00 24.81 ? 558  THR A OG1   1 
ATOM   3978  C CG2   . THR A  1 560  ? -43.416 67.062  104.260 1.00 21.52 ? 558  THR A CG2   1 
ATOM   3979  N N     . LEU A  1 561  ? -46.590 68.607  102.930 1.00 21.02 ? 559  LEU A N     1 
ATOM   3980  C CA    . LEU A  1 561  ? -46.782 70.032  102.688 1.00 20.18 ? 559  LEU A CA    1 
ATOM   3981  C C     . LEU A  1 561  ? -47.870 70.607  103.588 1.00 22.23 ? 559  LEU A C     1 
ATOM   3982  O O     . LEU A  1 561  ? -47.752 71.745  104.066 1.00 25.17 ? 559  LEU A O     1 
ATOM   3983  C CB    . LEU A  1 561  ? -47.097 70.269  101.208 1.00 19.76 ? 559  LEU A CB    1 
ATOM   3984  C CG    . LEU A  1 561  ? -45.901 69.959  100.287 1.00 23.60 ? 559  LEU A CG    1 
ATOM   3985  C CD1   . LEU A  1 561  ? -46.282 70.019  98.798  1.00 20.81 ? 559  LEU A CD1   1 
ATOM   3986  C CD2   . LEU A  1 561  ? -44.721 70.890  100.573 1.00 21.00 ? 559  LEU A CD2   1 
ATOM   3987  N N     . ALA A  1 562  ? -48.942 69.838  103.826 1.00 21.69 ? 560  ALA A N     1 
ATOM   3988  C CA    . ALA A  1 562  ? -50.027 70.313  104.683 1.00 25.45 ? 560  ALA A CA    1 
ATOM   3989  C C     . ALA A  1 562  ? -49.558 70.449  106.119 1.00 26.03 ? 560  ALA A C     1 
ATOM   3990  O O     . ALA A  1 562  ? -49.801 71.471  106.776 1.00 26.23 ? 560  ALA A O     1 
ATOM   3991  C CB    . ALA A  1 562  ? -51.224 69.363  104.608 1.00 26.24 ? 560  ALA A CB    1 
ATOM   3992  N N     . SER A  1 563  ? -48.901 69.409  106.625 1.00 20.67 ? 561  SER A N     1 
ATOM   3993  C CA    . SER A  1 563  ? -48.352 69.463  107.976 1.00 26.44 ? 561  SER A CA    1 
ATOM   3994  C C     . SER A  1 563  ? -47.316 70.575  108.116 1.00 27.16 ? 561  SER A C     1 
ATOM   3995  O O     . SER A  1 563  ? -47.270 71.272  109.136 1.00 28.64 ? 561  SER A O     1 
ATOM   3996  C CB    . SER A  1 563  ? -47.743 68.101  108.319 1.00 28.51 ? 561  SER A CB    1 
ATOM   3997  O OG    . SER A  1 563  ? -46.790 68.220  109.356 1.00 39.47 ? 561  SER A OG    1 
ATOM   3998  N N     . LEU A  1 564  ? -46.467 70.755  107.104 1.00 25.12 ? 562  LEU A N     1 
ATOM   3999  C CA    . LEU A  1 564  ? -45.411 71.755  107.201 1.00 23.30 ? 562  LEU A CA    1 
ATOM   4000  C C     . LEU A  1 564  ? -45.990 73.166  107.134 1.00 24.12 ? 562  LEU A C     1 
ATOM   4001  O O     . LEU A  1 564  ? -45.543 74.057  107.856 1.00 25.91 ? 562  LEU A O     1 
ATOM   4002  C CB    . LEU A  1 564  ? -44.378 71.513  106.099 1.00 23.01 ? 562  LEU A CB    1 
ATOM   4003  C CG    . LEU A  1 564  ? -43.136 72.389  105.973 1.00 24.87 ? 562  LEU A CG    1 
ATOM   4004  C CD1   . LEU A  1 564  ? -42.352 72.437  107.287 1.00 21.82 ? 562  LEU A CD1   1 
ATOM   4005  C CD2   . LEU A  1 564  ? -42.261 71.857  104.857 1.00 22.71 ? 562  LEU A CD2   1 
ATOM   4006  N N     . THR A  1 565  ? -47.005 73.383  106.295 1.00 20.99 ? 563  THR A N     1 
ATOM   4007  C CA    . THR A  1 565  ? -47.659 74.690  106.249 1.00 26.38 ? 563  THR A CA    1 
ATOM   4008  C C     . THR A  1 565  ? -48.097 75.143  107.635 1.00 26.03 ? 563  THR A C     1 
ATOM   4009  O O     . THR A  1 565  ? -47.872 76.295  108.029 1.00 27.02 ? 563  THR A O     1 
ATOM   4010  C CB    . THR A  1 565  ? -48.870 74.640  105.317 1.00 24.78 ? 563  THR A CB    1 
ATOM   4011  O OG1   . THR A  1 565  ? -48.431 74.390  103.973 1.00 29.39 ? 563  THR A OG1   1 
ATOM   4012  C CG2   . THR A  1 565  ? -49.629 75.953  105.375 1.00 28.65 ? 563  THR A CG2   1 
ATOM   4013  N N     . GLU A  1 566  ? -48.736 74.241  108.385 1.00 22.98 ? 564  GLU A N     1 
ATOM   4014  C CA    . GLU A  1 566  ? -49.214 74.579  109.721 1.00 24.45 ? 564  GLU A CA    1 
ATOM   4015  C C     . GLU A  1 566  ? -48.050 74.839  110.670 1.00 28.57 ? 564  GLU A C     1 
ATOM   4016  O O     . GLU A  1 566  ? -48.054 75.818  111.424 1.00 28.78 ? 564  GLU A O     1 
ATOM   4017  C CB    . GLU A  1 566  ? -50.094 73.454  110.258 1.00 25.69 ? 564  GLU A CB    1 
ATOM   4018  N N     . ALA A  1 567  ? -47.043 73.964  110.652 1.00 28.12 ? 565  ALA A N     1 
ATOM   4019  C CA    . ALA A  1 567  ? -45.880 74.171  111.515 1.00 29.19 ? 565  ALA A CA    1 
ATOM   4020  C C     . ALA A  1 567  ? -45.163 75.479  111.180 1.00 27.28 ? 565  ALA A C     1 
ATOM   4021  O O     . ALA A  1 567  ? -44.671 76.174  112.079 1.00 26.25 ? 565  ALA A O     1 
ATOM   4022  C CB    . ALA A  1 567  ? -44.928 72.981  111.400 1.00 29.45 ? 565  ALA A CB    1 
ATOM   4023  N N     . LEU A  1 568  ? -45.093 75.830  109.892 1.00 24.86 ? 566  LEU A N     1 
ATOM   4024  C CA    . LEU A  1 568  ? -44.441 77.072  109.493 1.00 22.70 ? 566  LEU A CA    1 
ATOM   4025  C C     . LEU A  1 568  ? -45.245 78.296  109.928 1.00 25.33 ? 566  LEU A C     1 
ATOM   4026  O O     . LEU A  1 568  ? -44.671 79.274  110.425 1.00 23.52 ? 566  LEU A O     1 
ATOM   4027  C CB    . LEU A  1 568  ? -44.197 77.076  107.977 1.00 21.61 ? 566  LEU A CB    1 
ATOM   4028  C CG    . LEU A  1 568  ? -43.156 76.104  107.399 1.00 22.97 ? 566  LEU A CG    1 
ATOM   4029  C CD1   . LEU A  1 568  ? -43.118 76.159  105.860 1.00 20.09 ? 566  LEU A CD1   1 
ATOM   4030  C CD2   . LEU A  1 568  ? -41.766 76.375  107.922 1.00 23.52 ? 566  LEU A CD2   1 
ATOM   4031  N N     . ARG A  1 569  ? -46.578 78.261  109.764 1.00 26.92 ? 567  ARG A N     1 
ATOM   4032  C CA    . ARG A  1 569  ? -47.405 79.358  110.265 1.00 26.62 ? 567  ARG A CA    1 
ATOM   4033  C C     . ARG A  1 569  ? -47.249 79.516  111.772 1.00 27.68 ? 567  ARG A C     1 
ATOM   4034  O O     . ARG A  1 569  ? -47.210 80.640  112.289 1.00 26.99 ? 567  ARG A O     1 
ATOM   4035  C CB    . ARG A  1 569  ? -48.879 79.128  109.926 1.00 32.94 ? 567  ARG A CB    1 
ATOM   4036  C CG    . ARG A  1 569  ? -49.228 79.235  108.453 1.00 33.12 ? 567  ARG A CG    1 
ATOM   4037  C CD    . ARG A  1 569  ? -50.723 79.490  108.303 1.00 35.36 ? 567  ARG A CD    1 
ATOM   4038  N NE    . ARG A  1 569  ? -51.250 78.996  107.037 1.00 41.87 ? 567  ARG A NE    1 
ATOM   4039  C CZ    . ARG A  1 569  ? -52.457 79.290  106.567 1.00 46.21 ? 567  ARG A CZ    1 
ATOM   4040  N NH1   . ARG A  1 569  ? -53.271 80.111  107.215 1.00 47.01 ? 567  ARG A NH1   1 
ATOM   4041  N NH2   . ARG A  1 569  ? -52.852 78.756  105.414 1.00 44.15 ? 567  ARG A NH2   1 
ATOM   4042  N N     . GLU A  1 570  ? -47.163 78.398  112.492 1.00 26.51 ? 568  GLU A N     1 
ATOM   4043  C CA    . GLU A  1 570  ? -46.983 78.469  113.937 1.00 29.00 ? 568  GLU A CA    1 
ATOM   4044  C C     . GLU A  1 570  ? -45.646 79.114  114.301 1.00 30.88 ? 568  GLU A C     1 
ATOM   4045  O O     . GLU A  1 570  ? -45.567 79.895  115.260 1.00 25.92 ? 568  GLU A O     1 
ATOM   4046  C CB    . GLU A  1 570  ? -47.101 77.066  114.540 1.00 31.75 ? 568  GLU A CB    1 
ATOM   4047  C CG    . GLU A  1 570  ? -48.535 76.525  114.520 1.00 38.99 ? 568  GLU A CG    1 
ATOM   4048  C CD    . GLU A  1 570  ? -48.615 75.033  114.788 1.00 42.86 ? 568  GLU A CD    1 
ATOM   4049  O OE1   . GLU A  1 570  ? -47.549 74.397  114.943 1.00 50.49 ? 568  GLU A OE1   1 
ATOM   4050  O OE2   . GLU A  1 570  ? -49.743 74.495  114.843 1.00 50.11 ? 568  GLU A OE2   1 
ATOM   4051  N N     . SER A  1 571  ? -44.586 78.813  113.544 1.00 27.19 ? 569  SER A N     1 
ATOM   4052  C CA    . SER A  1 571  ? -43.281 79.392  113.856 1.00 28.03 ? 569  SER A CA    1 
ATOM   4053  C C     . SER A  1 571  ? -43.302 80.909  113.718 1.00 28.52 ? 569  SER A C     1 
ATOM   4054  O O     . SER A  1 571  ? -42.572 81.609  114.426 1.00 26.44 ? 569  SER A O     1 
ATOM   4055  C CB    . SER A  1 571  ? -42.201 78.787  112.954 1.00 23.06 ? 569  SER A CB    1 
ATOM   4056  O OG    . SER A  1 571  ? -42.335 79.256  111.613 1.00 28.52 ? 569  SER A OG    1 
ATOM   4057  N N     . ALA A  1 572  ? -44.157 81.439  112.839 1.00 27.93 ? 570  ALA A N     1 
ATOM   4058  C CA    . ALA A  1 572  ? -44.219 82.880  112.634 1.00 31.31 ? 570  ALA A CA    1 
ATOM   4059  C C     . ALA A  1 572  ? -45.064 83.591  113.683 1.00 33.02 ? 570  ALA A C     1 
ATOM   4060  O O     . ALA A  1 572  ? -45.031 84.825  113.744 1.00 33.87 ? 570  ALA A O     1 
ATOM   4061  C CB    . ALA A  1 572  ? -44.752 83.192  111.238 1.00 28.45 ? 570  ALA A CB    1 
ATOM   4062  N N     . ALA A  1 573  ? -45.807 82.844  114.499 1.00 31.28 ? 571  ALA A N     1 
ATOM   4063  C CA    . ALA A  1 573  ? -46.508 83.370  115.661 1.00 32.90 ? 571  ALA A CA    1 
ATOM   4064  C C     . ALA A  1 573  ? -45.677 83.283  116.935 1.00 36.50 ? 571  ALA A C     1 
ATOM   4065  O O     . ALA A  1 573  ? -46.172 83.635  118.009 1.00 42.42 ? 571  ALA A O     1 
ATOM   4066  C CB    . ALA A  1 573  ? -47.827 82.619  115.866 1.00 33.87 ? 571  ALA A CB    1 
ATOM   4067  N N     . MET A  1 574  ? -44.444 82.809  116.846 1.00 32.26 ? 572  MET A N     1 
ATOM   4068  C CA    . MET A  1 574  ? -43.582 82.685  118.010 1.00 35.77 ? 572  MET A CA    1 
ATOM   4069  C C     . MET A  1 574  ? -42.834 83.989  118.253 1.00 31.94 ? 572  MET A C     1 
ATOM   4070  O O     . MET A  1 574  ? -42.507 84.729  117.322 1.00 31.95 ? 572  MET A O     1 
ATOM   4071  C CB    . MET A  1 574  ? -42.609 81.520  117.827 1.00 32.37 ? 572  MET A CB    1 
ATOM   4072  C CG    . MET A  1 574  ? -43.305 80.172  117.922 1.00 34.02 ? 572  MET A CG    1 
ATOM   4073  S SD    . MET A  1 574  ? -42.249 78.768  117.571 1.00 38.98 ? 572  MET A SD    1 
ATOM   4074  C CE    . MET A  1 574  ? -43.411 77.416  117.746 1.00 42.04 ? 572  MET A CE    1 
ATOM   4075  N N     . LYS A  1 575  ? -42.580 84.275  119.526 1.00 33.48 ? 573  LYS A N     1 
ATOM   4076  C CA    . LYS A  1 575  ? -41.900 85.512  119.906 1.00 33.70 ? 573  LYS A CA    1 
ATOM   4077  C C     . LYS A  1 575  ? -40.402 85.232  120.036 1.00 31.40 ? 573  LYS A C     1 
ATOM   4078  O O     . LYS A  1 575  ? -39.819 85.206  121.122 1.00 31.75 ? 573  LYS A O     1 
ATOM   4079  C CB    . LYS A  1 575  ? -42.497 86.078  121.190 1.00 40.13 ? 573  LYS A CB    1 
ATOM   4080  N N     . TRP A  1 576  ? -39.779 85.020  118.878 1.00 25.35 ? 574  TRP A N     1 
ATOM   4081  C CA    . TRP A  1 576  ? -38.361 84.694  118.836 1.00 28.51 ? 574  TRP A CA    1 
ATOM   4082  C C     . TRP A  1 576  ? -37.532 85.827  119.429 1.00 26.86 ? 574  TRP A C     1 
ATOM   4083  O O     . TRP A  1 576  ? -37.757 87.001  119.126 1.00 29.72 ? 574  TRP A O     1 
ATOM   4084  C CB    . TRP A  1 576  ? -37.939 84.424  117.392 1.00 28.11 ? 574  TRP A CB    1 
ATOM   4085  C CG    . TRP A  1 576  ? -38.618 83.250  116.746 1.00 26.72 ? 574  TRP A CG    1 
ATOM   4086  C CD1   . TRP A  1 576  ? -39.578 83.284  115.749 1.00 25.55 ? 574  TRP A CD1   1 
ATOM   4087  C CD2   . TRP A  1 576  ? -38.370 81.865  117.011 1.00 24.28 ? 574  TRP A CD2   1 
ATOM   4088  N NE1   . TRP A  1 576  ? -39.932 82.005  115.397 1.00 26.00 ? 574  TRP A NE1   1 
ATOM   4089  C CE2   . TRP A  1 576  ? -39.215 81.115  116.157 1.00 25.51 ? 574  TRP A CE2   1 
ATOM   4090  C CE3   . TRP A  1 576  ? -37.528 81.185  117.898 1.00 23.88 ? 574  TRP A CE3   1 
ATOM   4091  C CZ2   . TRP A  1 576  ? -39.233 79.714  116.159 1.00 24.09 ? 574  TRP A CZ2   1 
ATOM   4092  C CZ3   . TRP A  1 576  ? -37.538 79.796  117.897 1.00 27.38 ? 574  TRP A CZ3   1 
ATOM   4093  C CH2   . TRP A  1 576  ? -38.389 79.073  117.036 1.00 29.34 ? 574  TRP A CH2   1 
ATOM   4094  N N     . THR A  1 577  ? -36.588 85.479  120.300 1.00 29.54 ? 575  THR A N     1 
ATOM   4095  C CA    . THR A  1 577  ? -35.691 86.464  120.892 1.00 28.28 ? 575  THR A CA    1 
ATOM   4096  C C     . THR A  1 577  ? -34.282 85.897  120.958 1.00 25.79 ? 575  THR A C     1 
ATOM   4097  O O     . THR A  1 577  ? -34.063 84.681  120.935 1.00 24.97 ? 575  THR A O     1 
ATOM   4098  C CB    . THR A  1 577  ? -36.103 86.891  122.316 1.00 33.61 ? 575  THR A CB    1 
ATOM   4099  O OG1   . THR A  1 577  ? -35.936 85.786  123.212 1.00 31.16 ? 575  THR A OG1   1 
ATOM   4100  C CG2   . THR A  1 577  ? -37.550 87.386  122.377 1.00 34.63 ? 575  THR A CG2   1 
ATOM   4101  N N     . ALA A  1 578  ? -33.318 86.803  121.057 1.00 27.20 ? 576  ALA A N     1 
ATOM   4102  C CA    . ALA A  1 578  ? -31.930 86.436  121.308 1.00 24.97 ? 576  ALA A CA    1 
ATOM   4103  C C     . ALA A  1 578  ? -31.387 87.423  122.323 1.00 26.79 ? 576  ALA A C     1 
ATOM   4104  O O     . ALA A  1 578  ? -31.566 88.634  122.172 1.00 27.21 ? 576  ALA A O     1 
ATOM   4105  C CB    . ALA A  1 578  ? -31.084 86.453  120.024 1.00 24.48 ? 576  ALA A CB    1 
ATOM   4106  N N     . LEU A  1 579  ? -30.752 86.907  123.361 1.00 29.02 ? 577  LEU A N     1 
ATOM   4107  C CA    . LEU A  1 579  ? -30.216 87.723  124.437 1.00 30.36 ? 577  LEU A CA    1 
ATOM   4108  C C     . LEU A  1 579  ? -28.766 87.339  124.663 1.00 27.39 ? 577  LEU A C     1 
ATOM   4109  O O     . LEU A  1 579  ? -28.346 86.236  124.300 1.00 25.74 ? 577  LEU A O     1 
ATOM   4110  C CB    . LEU A  1 579  ? -31.006 87.524  125.741 1.00 29.04 ? 577  LEU A CB    1 
ATOM   4111  C CG    . LEU A  1 579  ? -32.531 87.547  125.692 1.00 31.58 ? 577  LEU A CG    1 
ATOM   4112  C CD1   . LEU A  1 579  ? -33.091 87.306  127.086 1.00 38.07 ? 577  LEU A CD1   1 
ATOM   4113  C CD2   . LEU A  1 579  ? -33.037 88.857  125.123 1.00 34.14 ? 577  LEU A CD2   1 
ATOM   4114  N N     . PRO A  1 580  ? -27.969 88.229  125.250 1.00 27.09 ? 578  PRO A N     1 
ATOM   4115  C CA    . PRO A  1 580  ? -26.654 87.801  125.727 1.00 26.54 ? 578  PRO A CA    1 
ATOM   4116  C C     . PRO A  1 580  ? -26.859 86.801  126.842 1.00 32.72 ? 578  PRO A C     1 
ATOM   4117  O O     . PRO A  1 580  ? -27.371 87.163  127.905 1.00 32.64 ? 578  PRO A O     1 
ATOM   4118  C CB    . PRO A  1 580  ? -26.009 89.099  126.230 1.00 30.76 ? 578  PRO A CB    1 
ATOM   4119  C CG    . PRO A  1 580  ? -26.869 90.206  125.676 1.00 29.00 ? 578  PRO A CG    1 
ATOM   4120  C CD    . PRO A  1 580  ? -28.238 89.632  125.601 1.00 29.78 ? 578  PRO A CD    1 
ATOM   4121  N N     . GLN A  1 581  ? -26.524 85.543  126.589 1.00 29.42 ? 579  GLN A N     1 
ATOM   4122  C CA    . GLN A  1 581  ? -26.732 84.450  127.536 1.00 28.08 ? 579  GLN A CA    1 
ATOM   4123  C C     . GLN A  1 581  ? -25.381 84.101  128.143 1.00 31.31 ? 579  GLN A C     1 
ATOM   4124  O O     . GLN A  1 581  ? -24.653 83.246  127.633 1.00 26.95 ? 579  GLN A O     1 
ATOM   4125  C CB    . GLN A  1 581  ? -27.363 83.242  126.854 1.00 27.98 ? 579  GLN A CB    1 
ATOM   4126  C CG    . GLN A  1 581  ? -28.783 83.496  126.321 1.00 25.98 ? 579  GLN A CG    1 
ATOM   4127  C CD    . GLN A  1 581  ? -29.824 83.678  127.420 1.00 30.11 ? 579  GLN A CD    1 
ATOM   4128  O OE1   . GLN A  1 581  ? -29.531 83.544  128.606 1.00 35.36 ? 579  GLN A OE1   1 
ATOM   4129  N NE2   . GLN A  1 581  ? -31.046 83.994  127.023 1.00 30.60 ? 579  GLN A NE2   1 
ATOM   4130  N N     . LEU A  1 582  ? -25.058 84.769  129.246 1.00 32.46 ? 580  LEU A N     1 
ATOM   4131  C CA    . LEU A  1 582  ? -23.823 84.520  129.967 1.00 30.97 ? 580  LEU A CA    1 
ATOM   4132  C C     . LEU A  1 582  ? -23.982 83.332  130.918 1.00 32.74 ? 580  LEU A C     1 
ATOM   4133  O O     . LEU A  1 582  ? -25.081 82.827  131.150 1.00 31.28 ? 580  LEU A O     1 
ATOM   4134  C CB    . LEU A  1 582  ? -23.400 85.773  130.734 1.00 29.66 ? 580  LEU A CB    1 
ATOM   4135  C CG    . LEU A  1 582  ? -22.576 86.804  129.952 1.00 37.79 ? 580  LEU A CG    1 
ATOM   4136  C CD1   . LEU A  1 582  ? -23.389 87.449  128.848 1.00 35.34 ? 580  LEU A CD1   1 
ATOM   4137  C CD2   . LEU A  1 582  ? -22.006 87.877  130.888 1.00 40.00 ? 580  LEU A CD2   1 
ATOM   4138  N N     . ALA A  1 583  ? -22.858 82.887  131.481 1.00 31.09 ? 581  ALA A N     1 
ATOM   4139  C CA    . ALA A  1 583  ? -22.906 81.789  132.442 1.00 31.69 ? 581  ALA A CA    1 
ATOM   4140  C C     . ALA A  1 583  ? -23.771 82.137  133.648 1.00 39.54 ? 581  ALA A C     1 
ATOM   4141  O O     . ALA A  1 583  ? -24.420 81.257  134.226 1.00 39.89 ? 581  ALA A O     1 
ATOM   4142  C CB    . ALA A  1 583  ? -21.491 81.427  132.887 1.00 31.74 ? 581  ALA A CB    1 
ATOM   4143  N N     . THR A  1 584  ? -23.807 83.414  134.027 1.00 34.87 ? 582  THR A N     1 
ATOM   4144  C CA    . THR A  1 584  ? -24.551 83.891  135.183 1.00 37.78 ? 582  THR A CA    1 
ATOM   4145  C C     . THR A  1 584  ? -26.014 84.183  134.873 1.00 40.12 ? 582  THR A C     1 
ATOM   4146  O O     . THR A  1 584  ? -26.763 84.558  135.783 1.00 44.80 ? 582  THR A O     1 
ATOM   4147  C CB    . THR A  1 584  ? -23.881 85.151  135.733 1.00 41.90 ? 582  THR A CB    1 
ATOM   4148  O OG1   . THR A  1 584  ? -23.634 86.052  134.649 1.00 40.11 ? 582  THR A OG1   1 
ATOM   4149  C CG2   . THR A  1 584  ? -22.551 84.796  136.373 1.00 37.91 ? 582  THR A CG2   1 
ATOM   4150  N N     . GLY A  1 585  ? -26.436 84.020  133.621 1.00 34.50 ? 583  GLY A N     1 
ATOM   4151  C CA    . GLY A  1 585  ? -27.800 84.281  133.228 1.00 34.93 ? 583  GLY A CA    1 
ATOM   4152  C C     . GLY A  1 585  ? -27.884 85.283  132.095 1.00 36.97 ? 583  GLY A C     1 
ATOM   4153  O O     . GLY A  1 585  ? -26.864 85.747  131.569 1.00 34.08 ? 583  GLY A O     1 
ATOM   4154  N N     . PRO A  1 586  ? -29.107 85.624  131.687 1.00 36.93 ? 584  PRO A N     1 
ATOM   4155  C CA    . PRO A  1 586  ? -29.279 86.615  130.616 1.00 37.94 ? 584  PRO A CA    1 
ATOM   4156  C C     . PRO A  1 586  ? -28.786 87.977  131.073 1.00 38.37 ? 584  PRO A C     1 
ATOM   4157  O O     . PRO A  1 586  ? -28.796 88.292  132.259 1.00 39.97 ? 584  PRO A O     1 
ATOM   4158  C CB    . PRO A  1 586  ? -30.796 86.634  130.373 1.00 40.19 ? 584  PRO A CB    1 
ATOM   4159  C CG    . PRO A  1 586  ? -31.373 85.515  131.196 1.00 39.47 ? 584  PRO A CG    1 
ATOM   4160  C CD    . PRO A  1 586  ? -30.388 85.193  132.268 1.00 41.14 ? 584  PRO A CD    1 
ATOM   4161  N N     . ALA A  1 587  ? -28.337 88.787  130.121 1.00 35.35 ? 585  ALA A N     1 
ATOM   4162  C CA    . ALA A  1 587  ? -27.867 90.123  130.442 1.00 38.22 ? 585  ALA A CA    1 
ATOM   4163  C C     . ALA A  1 587  ? -28.733 91.163  129.744 1.00 40.46 ? 585  ALA A C     1 
ATOM   4164  O O     . ALA A  1 587  ? -29.407 90.880  128.751 1.00 40.63 ? 585  ALA A O     1 
ATOM   4165  C CB    . ALA A  1 587  ? -26.394 90.308  130.053 1.00 39.70 ? 585  ALA A CB    1 
ATOM   4166  N N     . ALA A  1 588  ? -28.728 92.370  130.300 1.00 40.74 ? 586  ALA A N     1 
ATOM   4167  C CA    . ALA A  1 588  ? -29.440 93.482  129.696 1.00 43.20 ? 586  ALA A CA    1 
ATOM   4168  C C     . ALA A  1 588  ? -28.592 94.118  128.599 1.00 35.95 ? 586  ALA A C     1 
ATOM   4169  O O     . ALA A  1 588  ? -27.371 93.942  128.537 1.00 40.96 ? 586  ALA A O     1 
ATOM   4170  C CB    . ALA A  1 588  ? -29.806 94.522  130.754 1.00 41.24 ? 586  ALA A CB    1 
ATOM   4171  N N     . GLY A  1 589  ? -29.251 94.863  127.723 1.00 39.14 ? 587  GLY A N     1 
ATOM   4172  C CA    . GLY A  1 589  ? -28.530 95.491  126.635 1.00 39.12 ? 587  GLY A CA    1 
ATOM   4173  C C     . GLY A  1 589  ? -29.471 96.238  125.723 1.00 37.20 ? 587  GLY A C     1 
ATOM   4174  O O     . GLY A  1 589  ? -30.663 96.379  126.005 1.00 36.28 ? 587  GLY A O     1 
ATOM   4175  N N     . GLU A  1 590  ? -28.905 96.730  124.623 1.00 36.69 ? 588  GLU A N     1 
ATOM   4176  C CA    . GLU A  1 590  ? -29.685 97.431  123.615 1.00 37.59 ? 588  GLU A CA    1 
ATOM   4177  C C     . GLU A  1 590  ? -30.471 96.422  122.786 1.00 37.76 ? 588  GLU A C     1 
ATOM   4178  O O     . GLU A  1 590  ? -29.895 95.480  122.230 1.00 37.23 ? 588  GLU A O     1 
ATOM   4179  C CB    . GLU A  1 590  ? -28.770 98.265  122.718 1.00 45.52 ? 588  GLU A CB    1 
ATOM   4180  N N     . THR A  1 591  ? -31.784 96.627  122.700 1.00 39.93 ? 589  THR A N     1 
ATOM   4181  C CA    . THR A  1 591  ? -32.710 95.701  122.054 1.00 34.70 ? 589  THR A CA    1 
ATOM   4182  C C     . THR A  1 591  ? -33.202 96.298  120.742 1.00 37.29 ? 589  THR A C     1 
ATOM   4183  O O     . THR A  1 591  ? -33.611 97.463  120.700 1.00 38.92 ? 589  THR A O     1 
ATOM   4184  C CB    . THR A  1 591  ? -33.898 95.392  122.983 1.00 36.58 ? 589  THR A CB    1 
ATOM   4185  O OG1   . THR A  1 591  ? -33.430 94.715  124.162 1.00 35.59 ? 589  THR A OG1   1 
ATOM   4186  C CG2   . THR A  1 591  ? -34.923 94.510  122.290 1.00 35.49 ? 589  THR A CG2   1 
ATOM   4187  N N     . ARG A  1 592  ? -33.170 95.503  119.673 1.00 36.32 ? 590  ARG A N     1 
ATOM   4188  C CA    . ARG A  1 592  ? -33.718 95.945  118.401 1.00 34.87 ? 590  ARG A CA    1 
ATOM   4189  C C     . ARG A  1 592  ? -34.439 94.785  117.728 1.00 32.85 ? 590  ARG A C     1 
ATOM   4190  O O     . ARG A  1 592  ? -34.284 93.622  118.107 1.00 31.79 ? 590  ARG A O     1 
ATOM   4191  C CB    . ARG A  1 592  ? -32.626 96.519  117.486 1.00 42.09 ? 590  ARG A CB    1 
ATOM   4192  C CG    . ARG A  1 592  ? -31.560 95.535  117.057 1.00 39.32 ? 590  ARG A CG    1 
ATOM   4193  C CD    . ARG A  1 592  ? -30.858 96.036  115.793 1.00 47.37 ? 590  ARG A CD    1 
ATOM   4194  N NE    . ARG A  1 592  ? -29.834 95.113  115.319 1.00 48.82 ? 590  ARG A NE    1 
ATOM   4195  C CZ    . ARG A  1 592  ? -30.053 94.099  114.490 1.00 49.51 ? 590  ARG A CZ    1 
ATOM   4196  N NH1   . ARG A  1 592  ? -31.259 93.845  114.002 1.00 43.02 ? 590  ARG A NH1   1 
ATOM   4197  N NH2   . ARG A  1 592  ? -29.037 93.316  114.145 1.00 46.68 ? 590  ARG A NH2   1 
ATOM   4198  N N     . THR A  1 593  ? -35.234 95.113  116.718 1.00 31.56 ? 591  THR A N     1 
ATOM   4199  C CA    . THR A  1 593  ? -36.018 94.102  116.031 1.00 33.49 ? 591  THR A CA    1 
ATOM   4200  C C     . THR A  1 593  ? -35.201 93.462  114.915 1.00 32.97 ? 591  THR A C     1 
ATOM   4201  O O     . THR A  1 593  ? -34.273 94.065  114.370 1.00 33.21 ? 591  THR A O     1 
ATOM   4202  C CB    . THR A  1 593  ? -37.304 94.713  115.475 1.00 35.73 ? 591  THR A CB    1 
ATOM   4203  O OG1   . THR A  1 593  ? -36.975 95.845  114.660 1.00 38.63 ? 591  THR A OG1   1 
ATOM   4204  C CG2   . THR A  1 593  ? -38.194 95.176  116.619 1.00 39.46 ? 591  THR A CG2   1 
ATOM   4205  N N     . VAL A  1 594  ? -35.541 92.215  114.603 1.00 28.21 ? 592  VAL A N     1 
ATOM   4206  C CA    . VAL A  1 594  ? -34.946 91.469  113.503 1.00 27.07 ? 592  VAL A CA    1 
ATOM   4207  C C     . VAL A  1 594  ? -36.006 91.355  112.418 1.00 27.81 ? 592  VAL A C     1 
ATOM   4208  O O     . VAL A  1 594  ? -37.147 90.960  112.696 1.00 27.94 ? 592  VAL A O     1 
ATOM   4209  C CB    . VAL A  1 594  ? -34.454 90.088  113.968 1.00 24.96 ? 592  VAL A CB    1 
ATOM   4210  C CG1   . VAL A  1 594  ? -33.865 89.292  112.818 1.00 24.81 ? 592  VAL A CG1   1 
ATOM   4211  C CG2   . VAL A  1 594  ? -33.415 90.254  115.093 1.00 28.76 ? 592  VAL A CG2   1 
ATOM   4212  N N     . LEU A  1 595  ? -35.648 91.745  111.201 1.00 25.12 ? 593  LEU A N     1 
ATOM   4213  C CA    . LEU A  1 595  ? -36.598 91.867  110.105 1.00 25.34 ? 593  LEU A CA    1 
ATOM   4214  C C     . LEU A  1 595  ? -36.365 90.775  109.073 1.00 26.15 ? 593  LEU A C     1 
ATOM   4215  O O     . LEU A  1 595  ? -35.241 90.303  108.886 1.00 25.39 ? 593  LEU A O     1 
ATOM   4216  C CB    . LEU A  1 595  ? -36.483 93.239  109.430 1.00 26.26 ? 593  LEU A CB    1 
ATOM   4217  C CG    . LEU A  1 595  ? -36.680 94.468  110.320 1.00 29.43 ? 593  LEU A CG    1 
ATOM   4218  C CD1   . LEU A  1 595  ? -36.656 95.759  109.499 1.00 30.83 ? 593  LEU A CD1   1 
ATOM   4219  C CD2   . LEU A  1 595  ? -37.975 94.351  111.116 1.00 26.63 ? 593  LEU A CD2   1 
ATOM   4220  N N     . ASN A  1 596  ? -37.442 90.391  108.400 1.00 22.74 ? 594  ASN A N     1 
ATOM   4221  C CA    . ASN A  1 596  ? -37.365 89.488  107.260 1.00 23.83 ? 594  ASN A CA    1 
ATOM   4222  C C     . ASN A  1 596  ? -36.666 90.214  106.119 1.00 22.64 ? 594  ASN A C     1 
ATOM   4223  O O     . ASN A  1 596  ? -37.139 91.281  105.700 1.00 26.76 ? 594  ASN A O     1 
ATOM   4224  C CB    . ASN A  1 596  ? -38.787 89.065  106.866 1.00 25.06 ? 594  ASN A CB    1 
ATOM   4225  C CG    . ASN A  1 596  ? -38.826 87.977  105.799 1.00 23.04 ? 594  ASN A CG    1 
ATOM   4226  O OD1   . ASN A  1 596  ? -37.932 87.864  104.966 1.00 23.83 ? 594  ASN A OD1   1 
ATOM   4227  N ND2   . ASN A  1 596  ? -39.891 87.187  105.816 1.00 25.17 ? 594  ASN A ND2   1 
ATOM   4228  N N     . PRO A  1 597  ? -35.542 89.709  105.602 1.00 23.06 ? 595  PRO A N     1 
ATOM   4229  C CA    . PRO A  1 597  ? -34.880 90.422  104.497 1.00 23.00 ? 595  PRO A CA    1 
ATOM   4230  C C     . PRO A  1 597  ? -35.737 90.481  103.243 1.00 24.31 ? 595  PRO A C     1 
ATOM   4231  O O     . PRO A  1 597  ? -35.608 91.428  102.456 1.00 23.12 ? 595  PRO A O     1 
ATOM   4232  C CB    . PRO A  1 597  ? -33.577 89.629  104.284 1.00 22.48 ? 595  PRO A CB    1 
ATOM   4233  C CG    . PRO A  1 597  ? -33.758 88.328  104.969 1.00 28.10 ? 595  PRO A CG    1 
ATOM   4234  C CD    . PRO A  1 597  ? -34.777 88.532  106.061 1.00 23.50 ? 595  PRO A CD    1 
ATOM   4235  N N     . GLY A  1 598  ? -36.643 89.518  103.062 1.00 26.24 ? 596  GLY A N     1 
ATOM   4236  C CA    . GLY A  1 598  ? -37.579 89.541  101.943 1.00 22.69 ? 596  GLY A CA    1 
ATOM   4237  C C     . GLY A  1 598  ? -38.740 90.505  102.085 1.00 28.42 ? 596  GLY A C     1 
ATOM   4238  O O     . GLY A  1 598  ? -39.447 90.759  101.101 1.00 26.89 ? 596  GLY A O     1 
ATOM   4239  N N     . ASP A  1 599  ? -38.951 91.047  103.282 1.00 26.93 ? 597  ASP A N     1 
ATOM   4240  C CA    . ASP A  1 599  ? -40.067 91.945  103.557 1.00 28.09 ? 597  ASP A CA    1 
ATOM   4241  C C     . ASP A  1 599  ? -39.856 92.604  104.911 1.00 26.13 ? 597  ASP A C     1 
ATOM   4242  O O     . ASP A  1 599  ? -40.158 92.002  105.948 1.00 25.19 ? 597  ASP A O     1 
ATOM   4243  C CB    . ASP A  1 599  ? -41.384 91.179  103.556 1.00 25.64 ? 597  ASP A CB    1 
ATOM   4244  C CG    . ASP A  1 599  ? -42.608 92.082  103.583 1.00 30.25 ? 597  ASP A CG    1 
ATOM   4245  O OD1   . ASP A  1 599  ? -42.529 93.273  103.981 1.00 28.75 ? 597  ASP A OD1   1 
ATOM   4246  O OD2   . ASP A  1 599  ? -43.677 91.570  103.202 1.00 33.58 ? 597  ASP A OD2   1 
ATOM   4247  N N     . HIS A  1 600  ? -39.362 93.837  104.913 1.00 23.69 ? 598  HIS A N     1 
ATOM   4248  C CA    . HIS A  1 600  ? -39.009 94.485  106.172 1.00 28.67 ? 598  HIS A CA    1 
ATOM   4249  C C     . HIS A  1 600  ? -40.213 94.799  107.047 1.00 29.51 ? 598  HIS A C     1 
ATOM   4250  O O     . HIS A  1 600  ? -40.023 95.131  108.222 1.00 33.20 ? 598  HIS A O     1 
ATOM   4251  C CB    . HIS A  1 600  ? -38.203 95.750  105.895 1.00 25.92 ? 598  HIS A CB    1 
ATOM   4252  C CG    . HIS A  1 600  ? -36.798 95.467  105.463 1.00 27.91 ? 598  HIS A CG    1 
ATOM   4253  N ND1   . HIS A  1 600  ? -35.866 96.459  105.254 1.00 31.82 ? 598  HIS A ND1   1 
ATOM   4254  C CD2   . HIS A  1 600  ? -36.170 94.295  105.196 1.00 26.94 ? 598  HIS A CD2   1 
ATOM   4255  C CE1   . HIS A  1 600  ? -34.723 95.914  104.876 1.00 33.53 ? 598  HIS A CE1   1 
ATOM   4256  N NE2   . HIS A  1 600  ? -34.880 94.602  104.833 1.00 30.18 ? 598  HIS A NE2   1 
ATOM   4257  N N     . ARG A  1 601  ? -41.436 94.670  106.528 1.00 26.33 ? 599  ARG A N     1 
ATOM   4258  C CA    . ARG A  1 601  ? -42.624 94.809  107.367 1.00 30.06 ? 599  ARG A CA    1 
ATOM   4259  C C     . ARG A  1 601  ? -42.816 93.623  108.301 1.00 27.23 ? 599  ARG A C     1 
ATOM   4260  O O     . ARG A  1 601  ? -43.537 93.742  109.295 1.00 31.52 ? 599  ARG A O     1 
ATOM   4261  C CB    . ARG A  1 601  ? -43.866 94.967  106.491 1.00 28.55 ? 599  ARG A CB    1 
ATOM   4262  C CG    . ARG A  1 601  ? -43.784 96.140  105.539 1.00 29.31 ? 599  ARG A CG    1 
ATOM   4263  C CD    . ARG A  1 601  ? -44.873 96.050  104.506 1.00 29.01 ? 599  ARG A CD    1 
ATOM   4264  N NE    . ARG A  1 601  ? -44.835 94.770  103.809 1.00 28.88 ? 599  ARG A NE    1 
ATOM   4265  C CZ    . ARG A  1 601  ? -45.723 94.408  102.899 1.00 37.91 ? 599  ARG A CZ    1 
ATOM   4266  N NH1   . ARG A  1 601  ? -46.720 95.209  102.557 1.00 37.42 ? 599  ARG A NH1   1 
ATOM   4267  N NH2   . ARG A  1 601  ? -45.607 93.220  102.313 1.00 37.11 ? 599  ARG A NH2   1 
ATOM   4268  N N     . ASP A  1 602  ? -42.213 92.480  107.985 1.00 26.73 ? 600  ASP A N     1 
ATOM   4269  C CA    . ASP A  1 602  ? -42.411 91.234  108.721 1.00 26.01 ? 600  ASP A CA    1 
ATOM   4270  C C     . ASP A  1 602  ? -41.354 91.184  109.817 1.00 28.21 ? 600  ASP A C     1 
ATOM   4271  O O     . ASP A  1 602  ? -40.175 90.929  109.551 1.00 29.55 ? 600  ASP A O     1 
ATOM   4272  C CB    . ASP A  1 602  ? -42.324 90.053  107.759 1.00 25.90 ? 600  ASP A CB    1 
ATOM   4273  C CG    . ASP A  1 602  ? -42.433 88.704  108.446 1.00 28.85 ? 600  ASP A CG    1 
ATOM   4274  O OD1   . ASP A  1 602  ? -43.000 88.623  109.550 1.00 31.53 ? 600  ASP A OD1   1 
ATOM   4275  O OD2   . ASP A  1 602  ? -41.932 87.711  107.862 1.00 29.73 ? 600  ASP A OD2   1 
ATOM   4276  N N     . VAL A  1 603  ? -41.777 91.453  111.050 1.00 30.34 ? 601  VAL A N     1 
ATOM   4277  C CA    . VAL A  1 603  ? -40.892 91.405  112.211 1.00 29.48 ? 601  VAL A CA    1 
ATOM   4278  C C     . VAL A  1 603  ? -40.762 89.957  112.667 1.00 29.47 ? 601  VAL A C     1 
ATOM   4279  O O     . VAL A  1 603  ? -41.760 89.309  112.998 1.00 31.26 ? 601  VAL A O     1 
ATOM   4280  C CB    . VAL A  1 603  ? -41.420 92.289  113.349 1.00 25.65 ? 601  VAL A CB    1 
ATOM   4281  C CG1   . VAL A  1 603  ? -40.452 92.269  114.534 1.00 29.58 ? 601  VAL A CG1   1 
ATOM   4282  C CG2   . VAL A  1 603  ? -41.637 93.712  112.864 1.00 34.35 ? 601  VAL A CG2   1 
ATOM   4283  N N     . VAL A  1 604  ? -39.531 89.451  112.698 1.00 28.35 ? 602  VAL A N     1 
ATOM   4284  C CA    . VAL A  1 604  ? -39.314 88.051  113.059 1.00 25.82 ? 602  VAL A CA    1 
ATOM   4285  C C     . VAL A  1 604  ? -39.093 87.890  114.560 1.00 28.17 ? 602  VAL A C     1 
ATOM   4286  O O     . VAL A  1 604  ? -39.501 86.877  115.142 1.00 27.13 ? 602  VAL A O     1 
ATOM   4287  C CB    . VAL A  1 604  ? -38.130 87.477  112.267 1.00 28.13 ? 602  VAL A CB    1 
ATOM   4288  C CG1   . VAL A  1 604  ? -38.012 85.970  112.494 1.00 27.61 ? 602  VAL A CG1   1 
ATOM   4289  C CG2   . VAL A  1 604  ? -38.261 87.819  110.773 1.00 24.73 ? 602  VAL A CG2   1 
ATOM   4290  N N     . GLY A  1 605  ? -38.461 88.867  115.191 1.00 26.64 ? 603  GLY A N     1 
ATOM   4291  C CA    . GLY A  1 605  ? -38.158 88.767  116.603 1.00 29.29 ? 603  GLY A CA    1 
ATOM   4292  C C     . GLY A  1 605  ? -37.394 89.985  117.060 1.00 28.46 ? 603  GLY A C     1 
ATOM   4293  O O     . GLY A  1 605  ? -37.383 91.018  116.389 1.00 28.61 ? 603  GLY A O     1 
ATOM   4294  N N     . SER A  1 606  ? -36.758 89.862  118.215 1.00 27.98 ? 604  SER A N     1 
ATOM   4295  C CA    . SER A  1 606  ? -35.971 90.958  118.747 1.00 29.92 ? 604  SER A CA    1 
ATOM   4296  C C     . SER A  1 606  ? -34.671 90.403  119.306 1.00 29.33 ? 604  SER A C     1 
ATOM   4297  O O     . SER A  1 606  ? -34.637 89.290  119.837 1.00 29.11 ? 604  SER A O     1 
ATOM   4298  C CB    . SER A  1 606  ? -36.745 91.723  119.828 1.00 35.63 ? 604  SER A CB    1 
ATOM   4299  O OG    . SER A  1 606  ? -36.959 90.896  120.951 1.00 41.50 ? 604  SER A OG    1 
ATOM   4300  N N     . VAL A  1 607  ? -33.598 91.166  119.162 1.00 25.96 ? 605  VAL A N     1 
ATOM   4301  C CA    . VAL A  1 607  ? -32.301 90.773  119.684 1.00 26.05 ? 605  VAL A CA    1 
ATOM   4302  C C     . VAL A  1 607  ? -31.851 91.821  120.693 1.00 31.35 ? 605  VAL A C     1 
ATOM   4303  O O     . VAL A  1 607  ? -32.008 93.027  120.469 1.00 29.73 ? 605  VAL A O     1 
ATOM   4304  C CB    . VAL A  1 607  ? -31.264 90.599  118.553 1.00 25.23 ? 605  VAL A CB    1 
ATOM   4305  C CG1   . VAL A  1 607  ? -31.239 91.825  117.657 1.00 27.77 ? 605  VAL A CG1   1 
ATOM   4306  C CG2   . VAL A  1 607  ? -29.888 90.342  119.145 1.00 25.09 ? 605  VAL A CG2   1 
ATOM   4307  N N     . THR A  1 608  ? -31.336 91.354  121.824 1.00 27.96 ? 606  THR A N     1 
ATOM   4308  C CA    . THR A  1 608  ? -30.670 92.207  122.799 1.00 34.13 ? 606  THR A CA    1 
ATOM   4309  C C     . THR A  1 608  ? -29.178 91.974  122.643 1.00 30.52 ? 606  THR A C     1 
ATOM   4310  O O     . THR A  1 608  ? -28.715 90.836  122.760 1.00 28.10 ? 606  THR A O     1 
ATOM   4311  C CB    . THR A  1 608  ? -31.119 91.881  124.221 1.00 32.64 ? 606  THR A CB    1 
ATOM   4312  O OG1   . THR A  1 608  ? -32.513 92.176  124.357 1.00 34.50 ? 606  THR A OG1   1 
ATOM   4313  C CG2   . THR A  1 608  ? -30.318 92.698  125.231 1.00 34.11 ? 606  THR A CG2   1 
ATOM   4314  N N     . GLU A  1 609  ? -28.431 93.034  122.366 1.00 31.04 ? 607  GLU A N     1 
ATOM   4315  C CA    . GLU A  1 609  ? -27.054 92.872  121.934 1.00 30.32 ? 607  GLU A CA    1 
ATOM   4316  C C     . GLU A  1 609  ? -26.099 93.068  123.101 1.00 31.04 ? 607  GLU A C     1 
ATOM   4317  O O     . GLU A  1 609  ? -26.406 93.761  124.072 1.00 32.30 ? 607  GLU A O     1 
ATOM   4318  C CB    . GLU A  1 609  ? -26.743 93.815  120.767 1.00 34.26 ? 607  GLU A CB    1 
ATOM   4319  C CG    . GLU A  1 609  ? -27.454 93.328  119.481 1.00 37.10 ? 607  GLU A CG    1 
ATOM   4320  C CD    . GLU A  1 609  ? -27.112 94.118  118.220 1.00 41.70 ? 607  GLU A CD    1 
ATOM   4321  O OE1   . GLU A  1 609  ? -26.864 95.340  118.312 1.00 43.41 ? 607  GLU A OE1   1 
ATOM   4322  O OE2   . GLU A  1 609  ? -27.099 93.503  117.128 1.00 40.24 ? 607  GLU A OE2   1 
ATOM   4323  N N     . THR A  1 610  ? -24.954 92.402  123.010 1.00 31.05 ? 608  THR A N     1 
ATOM   4324  C CA    . THR A  1 610  ? -24.028 92.291  124.130 1.00 31.54 ? 608  THR A CA    1 
ATOM   4325  C C     . THR A  1 610  ? -23.177 93.545  124.250 1.00 31.22 ? 608  THR A C     1 
ATOM   4326  O O     . THR A  1 610  ? -22.667 94.063  123.257 1.00 33.59 ? 608  THR A O     1 
ATOM   4327  C CB    . THR A  1 610  ? -23.124 91.070  123.936 1.00 32.00 ? 608  THR A CB    1 
ATOM   4328  O OG1   . THR A  1 610  ? -23.926 89.930  123.613 1.00 29.02 ? 608  THR A OG1   1 
ATOM   4329  C CG2   . THR A  1 610  ? -22.323 90.770  125.197 1.00 32.21 ? 608  THR A CG2   1 
ATOM   4330  N N     . SER A  1 611  ? -23.018 94.031  125.476 1.00 36.89 ? 609  SER A N     1 
ATOM   4331  C CA    . SER A  1 611  ? -22.095 95.128  125.700 1.00 36.99 ? 609  SER A CA    1 
ATOM   4332  C C     . SER A  1 611  ? -20.664 94.610  125.637 1.00 38.87 ? 609  SER A C     1 
ATOM   4333  O O     . SER A  1 611  ? -20.389 93.438  125.913 1.00 36.70 ? 609  SER A O     1 
ATOM   4334  C CB    . SER A  1 611  ? -22.360 95.799  127.050 1.00 37.75 ? 609  SER A CB    1 
ATOM   4335  O OG    . SER A  1 611  ? -21.888 94.995  128.118 1.00 36.92 ? 609  SER A OG    1 
ATOM   4336  N N     . GLU A  1 612  ? -19.750 95.497  125.248 1.00 37.89 ? 610  GLU A N     1 
ATOM   4337  C CA    . GLU A  1 612  ? -18.337 95.135  125.214 1.00 39.79 ? 610  GLU A CA    1 
ATOM   4338  C C     . GLU A  1 612  ? -17.870 94.620  126.575 1.00 37.03 ? 610  GLU A C     1 
ATOM   4339  O O     . GLU A  1 612  ? -17.095 93.658  126.654 1.00 33.93 ? 610  GLU A O     1 
ATOM   4340  C CB    . GLU A  1 612  ? -17.524 96.350  124.769 1.00 42.99 ? 610  GLU A CB    1 
ATOM   4341  C CG    . GLU A  1 612  ? -16.052 96.110  124.545 1.00 46.78 ? 610  GLU A CG    1 
ATOM   4342  C CD    . GLU A  1 612  ? -15.295 97.411  124.318 1.00 57.09 ? 610  GLU A CD    1 
ATOM   4343  O OE1   . GLU A  1 612  ? -15.785 98.254  123.533 1.00 64.26 ? 610  GLU A OE1   1 
ATOM   4344  O OE2   . GLU A  1 612  ? -14.222 97.597  124.935 1.00 56.53 ? 610  GLU A OE2   1 
ATOM   4345  N N     . GLU A  1 613  ? -18.371 95.220  127.657 1.00 31.35 ? 611  GLU A N     1 
ATOM   4346  C CA    . GLU A  1 613  ? -18.012 94.757  128.995 1.00 36.52 ? 611  GLU A CA    1 
ATOM   4347  C C     . GLU A  1 613  ? -18.493 93.330  129.240 1.00 34.58 ? 611  GLU A C     1 
ATOM   4348  O O     . GLU A  1 613  ? -17.759 92.514  129.806 1.00 32.84 ? 611  GLU A O     1 
ATOM   4349  C CB    . GLU A  1 613  ? -18.579 95.705  130.054 1.00 36.42 ? 611  GLU A CB    1 
ATOM   4350  N N     . ASP A  1 614  ? -19.714 92.999  128.803 1.00 37.04 ? 612  ASP A N     1 
ATOM   4351  C CA    . ASP A  1 614  ? -20.238 91.657  129.049 1.00 32.48 ? 612  ASP A CA    1 
ATOM   4352  C C     . ASP A  1 614  ? -19.554 90.602  128.182 1.00 30.76 ? 612  ASP A C     1 
ATOM   4353  O O     . ASP A  1 614  ? -19.411 89.453  128.611 1.00 31.03 ? 612  ASP A O     1 
ATOM   4354  C CB    . ASP A  1 614  ? -21.756 91.636  128.852 1.00 37.21 ? 612  ASP A CB    1 
ATOM   4355  C CG    . ASP A  1 614  ? -22.500 92.241  130.036 1.00 37.13 ? 612  ASP A CG    1 
ATOM   4356  O OD1   . ASP A  1 614  ? -21.901 92.331  131.132 1.00 45.74 ? 612  ASP A OD1   1 
ATOM   4357  O OD2   . ASP A  1 614  ? -23.671 92.637  129.879 1.00 41.28 ? 612  ASP A OD2   1 
ATOM   4358  N N     . ALA A  1 615  ? -19.112 90.965  126.977 1.00 30.99 ? 613  ALA A N     1 
ATOM   4359  C CA    . ALA A  1 615  ? -18.319 90.042  126.170 1.00 28.81 ? 613  ALA A CA    1 
ATOM   4360  C C     . ALA A  1 615  ? -17.040 89.638  126.899 1.00 30.89 ? 613  ALA A C     1 
ATOM   4361  O O     . ALA A  1 615  ? -16.700 88.450  126.974 1.00 28.41 ? 613  ALA A O     1 
ATOM   4362  C CB    . ALA A  1 615  ? -17.995 90.678  124.818 1.00 32.30 ? 613  ALA A CB    1 
ATOM   4363  N N     . ARG A  1 616  ? -16.320 90.620  127.450 1.00 30.40 ? 614  ARG A N     1 
ATOM   4364  C CA    . ARG A  1 616  ? -15.098 90.321  128.195 1.00 33.44 ? 614  ARG A CA    1 
ATOM   4365  C C     . ARG A  1 616  ? -15.397 89.531  129.462 1.00 32.75 ? 614  ARG A C     1 
ATOM   4366  O O     . ARG A  1 616  ? -14.603 88.672  129.870 1.00 30.51 ? 614  ARG A O     1 
ATOM   4367  C CB    . ARG A  1 616  ? -14.366 91.617  128.544 1.00 32.97 ? 614  ARG A CB    1 
ATOM   4368  C CG    . ARG A  1 616  ? -13.887 92.405  127.333 1.00 41.76 ? 614  ARG A CG    1 
ATOM   4369  C CD    . ARG A  1 616  ? -12.928 93.503  127.748 1.00 43.01 ? 614  ARG A CD    1 
ATOM   4370  N NE    . ARG A  1 616  ? -13.497 94.343  128.795 1.00 47.46 ? 614  ARG A NE    1 
ATOM   4371  C CZ    . ARG A  1 616  ? -14.299 95.376  128.567 1.00 47.90 ? 614  ARG A CZ    1 
ATOM   4372  N NH1   . ARG A  1 616  ? -14.633 95.731  127.338 1.00 49.69 ? 614  ARG A NH1   1 
ATOM   4373  N NH2   . ARG A  1 616  ? -14.776 96.069  129.599 1.00 52.84 ? 614  ARG A NH2   1 
ATOM   4374  N N     . ARG A  1 617  ? -16.529 89.819  130.106 1.00 28.54 ? 615  ARG A N     1 
ATOM   4375  C CA    . ARG A  1 617  ? -16.935 89.064  131.285 1.00 30.68 ? 615  ARG A CA    1 
ATOM   4376  C C     . ARG A  1 617  ? -17.239 87.617  130.929 1.00 30.40 ? 615  ARG A C     1 
ATOM   4377  O O     . ARG A  1 617  ? -16.894 86.698  131.680 1.00 29.61 ? 615  ARG A O     1 
ATOM   4378  C CB    . ARG A  1 617  ? -18.152 89.729  131.937 1.00 33.13 ? 615  ARG A CB    1 
ATOM   4379  C CG    . ARG A  1 617  ? -18.668 89.000  133.165 1.00 40.47 ? 615  ARG A CG    1 
ATOM   4380  C CD    . ARG A  1 617  ? -19.313 89.951  134.175 1.00 45.22 ? 615  ARG A CD    1 
ATOM   4381  N NE    . ARG A  1 617  ? -20.576 90.488  133.691 1.00 49.94 ? 615  ARG A NE    1 
ATOM   4382  C CZ    . ARG A  1 617  ? -21.758 89.926  133.912 1.00 52.95 ? 615  ARG A CZ    1 
ATOM   4383  N NH1   . ARG A  1 617  ? -21.873 88.814  134.624 1.00 48.73 ? 615  ARG A NH1   1 
ATOM   4384  N NH2   . ARG A  1 617  ? -22.852 90.494  133.408 1.00 43.93 ? 615  ARG A NH2   1 
ATOM   4385  N N     . ALA A  1 618  ? -17.878 87.392  129.777 1.00 29.27 ? 616  ALA A N     1 
ATOM   4386  C CA    . ALA A  1 618  ? -18.174 86.030  129.349 1.00 30.09 ? 616  ALA A CA    1 
ATOM   4387  C C     . ALA A  1 618  ? -16.899 85.214  129.161 1.00 27.39 ? 616  ALA A C     1 
ATOM   4388  O O     . ALA A  1 618  ? -16.854 84.034  129.527 1.00 26.92 ? 616  ALA A O     1 
ATOM   4389  C CB    . ALA A  1 618  ? -19.004 86.056  128.059 1.00 26.78 ? 616  ALA A CB    1 
ATOM   4390  N N     . VAL A  1 619  ? -15.852 85.816  128.586 1.00 28.44 ? 617  VAL A N     1 
ATOM   4391  C CA    . VAL A  1 619  ? -14.605 85.076  128.394 1.00 26.71 ? 617  VAL A CA    1 
ATOM   4392  C C     . VAL A  1 619  ? -14.012 84.690  129.741 1.00 27.15 ? 617  VAL A C     1 
ATOM   4393  O O     . VAL A  1 619  ? -13.519 83.568  129.917 1.00 27.00 ? 617  VAL A O     1 
ATOM   4394  C CB    . VAL A  1 619  ? -13.596 85.880  127.547 1.00 26.59 ? 617  VAL A CB    1 
ATOM   4395  C CG1   . VAL A  1 619  ? -12.275 85.118  127.420 1.00 26.72 ? 617  VAL A CG1   1 
ATOM   4396  C CG2   . VAL A  1 619  ? -14.163 86.178  126.162 1.00 26.15 ? 617  VAL A CG2   1 
ATOM   4397  N N     . ARG A  1 620  ? -14.059 85.603  130.718 1.00 27.73 ? 618  ARG A N     1 
ATOM   4398  C CA    . ARG A  1 620  ? -13.529 85.262  132.036 1.00 29.68 ? 618  ARG A CA    1 
ATOM   4399  C C     . ARG A  1 620  ? -14.378 84.187  132.703 1.00 31.47 ? 618  ARG A C     1 
ATOM   4400  O O     . ARG A  1 620  ? -13.843 83.294  133.369 1.00 32.53 ? 618  ARG A O     1 
ATOM   4401  C CB    . ARG A  1 620  ? -13.442 86.510  132.916 1.00 34.82 ? 618  ARG A CB    1 
ATOM   4402  C CG    . ARG A  1 620  ? -12.674 87.658  132.275 1.00 42.00 ? 618  ARG A CG    1 
ATOM   4403  C CD    . ARG A  1 620  ? -12.338 88.754  133.292 1.00 46.84 ? 618  ARG A CD    1 
ATOM   4404  N NE    . ARG A  1 620  ? -13.494 89.125  134.099 1.00 51.31 ? 618  ARG A NE    1 
ATOM   4405  C CZ    . ARG A  1 620  ? -14.320 90.125  133.824 1.00 46.06 ? 618  ARG A CZ    1 
ATOM   4406  N NH1   . ARG A  1 620  ? -14.137 90.906  132.769 1.00 40.93 ? 618  ARG A NH1   1 
ATOM   4407  N NH2   . ARG A  1 620  ? -15.358 90.346  134.627 1.00 47.27 ? 618  ARG A NH2   1 
ATOM   4408  N N     . LEU A  1 621  ? -15.700 84.240  132.516 1.00 29.17 ? 619  LEU A N     1 
ATOM   4409  C CA    . LEU A  1 621  ? -16.556 83.179  133.039 1.00 31.36 ? 619  LEU A CA    1 
ATOM   4410  C C     . LEU A  1 621  ? -16.263 81.850  132.354 1.00 31.15 ? 619  LEU A C     1 
ATOM   4411  O O     . LEU A  1 621  ? -16.256 80.796  133.004 1.00 29.67 ? 619  LEU A O     1 
ATOM   4412  C CB    . LEU A  1 621  ? -18.031 83.548  132.871 1.00 30.95 ? 619  LEU A CB    1 
ATOM   4413  C CG    . LEU A  1 621  ? -18.597 84.674  133.728 1.00 32.36 ? 619  LEU A CG    1 
ATOM   4414  C CD1   . LEU A  1 621  ? -20.001 85.027  133.253 1.00 35.04 ? 619  LEU A CD1   1 
ATOM   4415  C CD2   . LEU A  1 621  ? -18.608 84.259  135.192 1.00 35.72 ? 619  LEU A CD2   1 
ATOM   4416  N N     . ALA A  1 622  ? -16.029 81.877  131.036 1.00 27.48 ? 620  ALA A N     1 
ATOM   4417  C CA    . ALA A  1 622  ? -15.675 80.654  130.317 1.00 26.95 ? 620  ALA A CA    1 
ATOM   4418  C C     . ALA A  1 622  ? -14.333 80.095  130.791 1.00 30.06 ? 620  ALA A C     1 
ATOM   4419  O O     . ALA A  1 622  ? -14.201 78.883  130.990 1.00 30.00 ? 620  ALA A O     1 
ATOM   4420  C CB    . ALA A  1 622  ? -15.661 80.914  128.806 1.00 26.07 ? 620  ALA A CB    1 
ATOM   4421  N N     . ALA A  1 623  ? -13.335 80.962  131.010 1.00 30.84 ? 621  ALA A N     1 
ATOM   4422  C CA    . ALA A  1 623  ? -12.057 80.491  131.534 1.00 30.21 ? 621  ALA A CA    1 
ATOM   4423  C C     . ALA A  1 623  ? -12.232 79.839  132.898 1.00 32.65 ? 621  ALA A C     1 
ATOM   4424  O O     . ALA A  1 623  ? -11.622 78.798  133.180 1.00 32.39 ? 621  ALA A O     1 
ATOM   4425  C CB    . ALA A  1 623  ? -11.054 81.645  131.617 1.00 27.56 ? 621  ALA A CB    1 
ATOM   4426  N N     . ASP A  1 624  ? -13.069 80.432  133.756 1.00 32.02 ? 622  ASP A N     1 
ATOM   4427  C CA    A ASP A  1 624  ? -13.284 79.872  135.086 0.49 35.43 ? 622  ASP A CA    1 
ATOM   4428  C CA    B ASP A  1 624  ? -13.287 79.875  135.088 0.51 35.43 ? 622  ASP A CA    1 
ATOM   4429  C C     . ASP A  1 624  ? -13.904 78.483  135.006 1.00 34.76 ? 622  ASP A C     1 
ATOM   4430  O O     . ASP A  1 624  ? -13.572 77.600  135.801 1.00 38.85 ? 622  ASP A O     1 
ATOM   4431  C CB    A ASP A  1 624  ? -14.169 80.801  135.917 0.49 36.48 ? 622  ASP A CB    1 
ATOM   4432  C CB    B ASP A  1 624  ? -14.178 80.811  135.907 0.51 36.49 ? 622  ASP A CB    1 
ATOM   4433  C CG    A ASP A  1 624  ? -13.558 82.174  136.108 0.49 36.35 ? 622  ASP A CG    1 
ATOM   4434  C CG    B ASP A  1 624  ? -13.947 80.687  137.405 0.51 37.51 ? 622  ASP A CG    1 
ATOM   4435  O OD1   A ASP A  1 624  ? -12.321 82.300  135.983 0.49 40.09 ? 622  ASP A OD1   1 
ATOM   4436  O OD1   B ASP A  1 624  ? -13.458 79.633  137.859 0.51 39.37 ? 622  ASP A OD1   1 
ATOM   4437  O OD2   A ASP A  1 624  ? -14.319 83.126  136.383 0.49 38.42 ? 622  ASP A OD2   1 
ATOM   4438  O OD2   B ASP A  1 624  ? -14.258 81.651  138.133 0.51 42.27 ? 622  ASP A OD2   1 
ATOM   4439  N N     . ALA A  1 625  ? -14.797 78.271  134.048 1.00 34.13 ? 623  ALA A N     1 
ATOM   4440  C CA    . ALA A  1 625  ? -15.501 77.007  133.888 1.00 36.37 ? 623  ALA A CA    1 
ATOM   4441  C C     . ALA A  1 625  ? -14.768 75.993  133.021 1.00 32.54 ? 623  ALA A C     1 
ATOM   4442  O O     . ALA A  1 625  ? -15.234 74.852  132.919 1.00 35.13 ? 623  ALA A O     1 
ATOM   4443  C CB    . ALA A  1 625  ? -16.879 77.260  133.278 1.00 37.63 ? 623  ALA A CB    1 
ATOM   4444  N N     . ALA A  1 626  ? -13.657 76.376  132.384 1.00 32.06 ? 624  ALA A N     1 
ATOM   4445  C CA    . ALA A  1 626  ? -12.987 75.473  131.449 1.00 30.13 ? 624  ALA A CA    1 
ATOM   4446  C C     . ALA A  1 626  ? -12.597 74.135  132.068 1.00 29.38 ? 624  ALA A C     1 
ATOM   4447  O O     . ALA A  1 626  ? -12.884 73.094  131.454 1.00 31.67 ? 624  ALA A O     1 
ATOM   4448  C CB    . ALA A  1 626  ? -11.773 76.176  130.832 1.00 32.60 ? 624  ALA A CB    1 
ATOM   4449  N N     . PRO A  1 627  ? -11.948 74.073  133.239 1.00 33.73 ? 625  PRO A N     1 
ATOM   4450  C CA    . PRO A  1 627  ? -11.591 72.751  133.791 1.00 33.29 ? 625  PRO A CA    1 
ATOM   4451  C C     . PRO A  1 627  ? -12.790 71.849  134.017 1.00 34.21 ? 625  PRO A C     1 
ATOM   4452  O O     . PRO A  1 627  ? -12.705 70.635  133.787 1.00 34.26 ? 625  PRO A O     1 
ATOM   4453  C CB    . PRO A  1 627  ? -10.908 73.100  135.123 1.00 32.93 ? 625  PRO A CB    1 
ATOM   4454  C CG    . PRO A  1 627  ? -10.525 74.541  135.005 1.00 32.42 ? 625  PRO A CG    1 
ATOM   4455  C CD    . PRO A  1 627  ? -11.538 75.173  134.135 1.00 33.70 ? 625  PRO A CD    1 
ATOM   4456  N N     . ASP A  1 628  ? -13.908 72.419  134.471 1.00 30.94 ? 626  ASP A N     1 
ATOM   4457  C CA    . ASP A  1 628  ? -15.105 71.625  134.718 1.00 29.69 ? 626  ASP A CA    1 
ATOM   4458  C C     . ASP A  1 628  ? -15.616 70.974  133.437 1.00 34.30 ? 626  ASP A C     1 
ATOM   4459  O O     . ASP A  1 628  ? -15.962 69.785  133.428 1.00 33.03 ? 626  ASP A O     1 
ATOM   4460  C CB    . ASP A  1 628  ? -16.183 72.511  135.340 1.00 32.86 ? 626  ASP A CB    1 
ATOM   4461  C CG    . ASP A  1 628  ? -15.703 73.214  136.605 1.00 44.69 ? 626  ASP A CG    1 
ATOM   4462  O OD1   . ASP A  1 628  ? -14.724 74.000  136.528 1.00 46.65 ? 626  ASP A OD1   1 
ATOM   4463  O OD2   . ASP A  1 628  ? -16.298 72.974  137.673 1.00 40.73 ? 626  ASP A OD2   1 
ATOM   4464  N N     . TRP A  1 629  ? -15.664 71.731  132.341 1.00 28.46 ? 627  TRP A N     1 
ATOM   4465  C CA    . TRP A  1 629  ? -16.142 71.146  131.093 1.00 26.98 ? 627  TRP A CA    1 
ATOM   4466  C C     . TRP A  1 629  ? -15.118 70.174  130.507 1.00 30.59 ? 627  TRP A C     1 
ATOM   4467  O O     . TRP A  1 629  ? -15.490 69.135  129.947 1.00 28.31 ? 627  TRP A O     1 
ATOM   4468  C CB    . TRP A  1 629  ? -16.494 72.251  130.096 1.00 28.11 ? 627  TRP A CB    1 
ATOM   4469  C CG    . TRP A  1 629  ? -16.979 71.712  128.788 1.00 27.21 ? 627  TRP A CG    1 
ATOM   4470  C CD1   . TRP A  1 629  ? -16.395 71.879  127.561 1.00 26.91 ? 627  TRP A CD1   1 
ATOM   4471  C CD2   . TRP A  1 629  ? -18.133 70.886  128.577 1.00 29.40 ? 627  TRP A CD2   1 
ATOM   4472  N NE1   . TRP A  1 629  ? -17.128 71.222  126.597 1.00 29.03 ? 627  TRP A NE1   1 
ATOM   4473  C CE2   . TRP A  1 629  ? -18.195 70.601  127.192 1.00 25.99 ? 627  TRP A CE2   1 
ATOM   4474  C CE3   . TRP A  1 629  ? -19.115 70.356  129.420 1.00 27.82 ? 627  TRP A CE3   1 
ATOM   4475  C CZ2   . TRP A  1 629  ? -19.204 69.813  126.634 1.00 28.27 ? 627  TRP A CZ2   1 
ATOM   4476  C CZ3   . TRP A  1 629  ? -20.118 69.570  128.861 1.00 27.64 ? 627  TRP A CZ3   1 
ATOM   4477  C CH2   . TRP A  1 629  ? -20.155 69.309  127.484 1.00 27.08 ? 627  TRP A CH2   1 
ATOM   4478  N N     . ALA A  1 630  ? -13.819 70.482  130.640 1.00 28.53 ? 628  ALA A N     1 
ATOM   4479  C CA    . ALA A  1 630  ? -12.798 69.563  130.153 1.00 28.20 ? 628  ALA A CA    1 
ATOM   4480  C C     . ALA A  1 630  ? -12.853 68.231  130.892 1.00 31.30 ? 628  ALA A C     1 
ATOM   4481  O O     . ALA A  1 630  ? -12.486 67.196  130.329 1.00 30.59 ? 628  ALA A O     1 
ATOM   4482  C CB    . ALA A  1 630  ? -11.410 70.186  130.296 1.00 31.85 ? 628  ALA A CB    1 
ATOM   4483  N N     . ALA A  1 631  ? -13.332 68.236  132.141 1.00 30.50 ? 629  ALA A N     1 
ATOM   4484  C CA    . ALA A  1 631  ? -13.413 67.021  132.939 1.00 32.46 ? 629  ALA A CA    1 
ATOM   4485  C C     . ALA A  1 631  ? -14.581 66.126  132.556 1.00 32.56 ? 629  ALA A C     1 
ATOM   4486  O O     . ALA A  1 631  ? -14.597 64.962  132.960 1.00 34.56 ? 629  ALA A O     1 
ATOM   4487  C CB    . ALA A  1 631  ? -13.506 67.364  134.432 1.00 37.10 ? 629  ALA A CB    1 
ATOM   4488  N N     . VAL A  1 632  ? -15.549 66.623  131.799 1.00 30.02 ? 630  VAL A N     1 
ATOM   4489  C CA    . VAL A  1 632  ? -16.622 65.735  131.336 1.00 28.62 ? 630  VAL A CA    1 
ATOM   4490  C C     . VAL A  1 632  ? -16.038 64.760  130.321 1.00 31.59 ? 630  VAL A C     1 
ATOM   4491  O O     . VAL A  1 632  ? -15.370 65.194  129.363 1.00 29.35 ? 630  VAL A O     1 
ATOM   4492  C CB    . VAL A  1 632  ? -17.775 66.547  130.741 1.00 26.22 ? 630  VAL A CB    1 
ATOM   4493  C CG1   . VAL A  1 632  ? -18.826 65.621  130.122 1.00 26.01 ? 630  VAL A CG1   1 
ATOM   4494  C CG2   . VAL A  1 632  ? -18.410 67.421  131.840 1.00 29.25 ? 630  VAL A CG2   1 
ATOM   4495  N N     . PRO A  1 633  ? -16.204 63.454  130.514 1.00 28.91 ? 631  PRO A N     1 
ATOM   4496  C CA    . PRO A  1 633  ? -15.588 62.473  129.611 1.00 25.45 ? 631  PRO A CA    1 
ATOM   4497  C C     . PRO A  1 633  ? -16.005 62.716  128.170 1.00 27.10 ? 631  PRO A C     1 
ATOM   4498  O O     . PRO A  1 633  ? -17.170 63.056  127.903 1.00 28.10 ? 631  PRO A O     1 
ATOM   4499  C CB    . PRO A  1 633  ? -16.125 61.131  130.129 1.00 26.74 ? 631  PRO A CB    1 
ATOM   4500  C CG    . PRO A  1 633  ? -16.482 61.391  131.574 1.00 30.53 ? 631  PRO A CG    1 
ATOM   4501  C CD    . PRO A  1 633  ? -16.960 62.820  131.612 1.00 28.24 ? 631  PRO A CD    1 
ATOM   4502  N N     . PRO A  1 634  ? -15.077 62.551  127.214 1.00 26.49 ? 632  PRO A N     1 
ATOM   4503  C CA    . PRO A  1 634  ? -15.411 62.831  125.804 1.00 23.97 ? 632  PRO A CA    1 
ATOM   4504  C C     . PRO A  1 634  ? -16.664 62.124  125.319 1.00 26.37 ? 632  PRO A C     1 
ATOM   4505  O O     . PRO A  1 634  ? -17.437 62.709  124.546 1.00 24.28 ? 632  PRO A O     1 
ATOM   4506  C CB    . PRO A  1 634  ? -14.152 62.362  125.058 1.00 26.98 ? 632  PRO A CB    1 
ATOM   4507  C CG    . PRO A  1 634  ? -13.044 62.516  126.073 1.00 32.71 ? 632  PRO A CG    1 
ATOM   4508  C CD    . PRO A  1 634  ? -13.665 62.159  127.388 1.00 27.52 ? 632  PRO A CD    1 
ATOM   4509  N N     . SER A  1 635  ? -16.916 60.891  125.767 1.00 26.28 ? 633  SER A N     1 
ATOM   4510  C CA    . SER A  1 635  ? -18.112 60.191  125.294 1.00 28.17 ? 633  SER A CA    1 
ATOM   4511  C C     . SER A  1 635  ? -19.391 60.862  125.788 1.00 28.52 ? 633  SER A C     1 
ATOM   4512  O O     . SER A  1 635  ? -20.422 60.827  125.099 1.00 25.58 ? 633  SER A O     1 
ATOM   4513  C CB    . SER A  1 635  ? -18.082 58.727  125.735 1.00 30.07 ? 633  SER A CB    1 
ATOM   4514  O OG    . SER A  1 635  ? -18.184 58.630  127.138 1.00 37.82 ? 633  SER A OG    1 
ATOM   4515  N N     . GLU A  1 636  ? -19.343 61.489  126.959 1.00 26.53 ? 634  GLU A N     1 
ATOM   4516  C CA    . GLU A  1 636  ? -20.515 62.189  127.465 1.00 28.74 ? 634  GLU A CA    1 
ATOM   4517  C C     . GLU A  1 636  ? -20.688 63.537  126.783 1.00 27.43 ? 634  GLU A C     1 
ATOM   4518  O O     . GLU A  1 636  ? -21.822 63.960  126.523 1.00 28.99 ? 634  GLU A O     1 
ATOM   4519  C CB    . GLU A  1 636  ? -20.419 62.367  128.977 1.00 29.03 ? 634  GLU A CB    1 
ATOM   4520  C CG    . GLU A  1 636  ? -20.660 61.081  129.758 1.00 39.18 ? 634  GLU A CG    1 
ATOM   4521  C CD    . GLU A  1 636  ? -22.105 60.576  129.678 1.00 46.70 ? 634  GLU A CD    1 
ATOM   4522  O OE1   . GLU A  1 636  ? -22.991 61.301  129.151 1.00 43.75 ? 634  GLU A OE1   1 
ATOM   4523  O OE2   . GLU A  1 636  ? -22.355 59.443  130.156 1.00 53.97 ? 634  GLU A OE2   1 
ATOM   4524  N N     . ARG A  1 637  ? -19.578 64.220  126.484 1.00 25.15 ? 635  ARG A N     1 
ATOM   4525  C CA    . ARG A  1 637  ? -19.664 65.406  125.641 1.00 24.59 ? 635  ARG A CA    1 
ATOM   4526  C C     . ARG A  1 637  ? -20.289 65.056  124.296 1.00 23.75 ? 635  ARG A C     1 
ATOM   4527  O O     . ARG A  1 637  ? -21.148 65.793  123.794 1.00 23.21 ? 635  ARG A O     1 
ATOM   4528  C CB    . ARG A  1 637  ? -18.285 66.039  125.462 1.00 23.75 ? 635  ARG A CB    1 
ATOM   4529  C CG    . ARG A  1 637  ? -17.578 66.357  126.807 1.00 24.23 ? 635  ARG A CG    1 
ATOM   4530  C CD    . ARG A  1 637  ? -16.415 67.330  126.646 1.00 26.74 ? 635  ARG A CD    1 
ATOM   4531  N NE    . ARG A  1 637  ? -15.391 66.851  125.729 1.00 27.68 ? 635  ARG A NE    1 
ATOM   4532  C CZ    . ARG A  1 637  ? -14.188 66.414  126.079 1.00 30.19 ? 635  ARG A CZ    1 
ATOM   4533  N NH1   . ARG A  1 637  ? -13.817 66.341  127.347 1.00 29.64 ? 635  ARG A NH1   1 
ATOM   4534  N NH2   . ARG A  1 637  ? -13.330 66.050  125.128 1.00 26.20 ? 635  ARG A NH2   1 
ATOM   4535  N N     . ALA A  1 638  ? -19.892 63.917  123.715 1.00 23.21 ? 636  ALA A N     1 
ATOM   4536  C CA    . ALA A  1 638  ? -20.474 63.483  122.442 1.00 22.80 ? 636  ALA A CA    1 
ATOM   4537  C C     . ALA A  1 638  ? -21.956 63.155  122.584 1.00 24.73 ? 636  ALA A C     1 
ATOM   4538  O O     . ALA A  1 638  ? -22.745 63.402  121.660 1.00 22.64 ? 636  ALA A O     1 
ATOM   4539  C CB    . ALA A  1 638  ? -19.712 62.269  121.901 1.00 22.67 ? 636  ALA A CB    1 
ATOM   4540  N N     . ALA A  1 639  ? -22.349 62.569  123.719 1.00 26.37 ? 637  ALA A N     1 
ATOM   4541  C CA    . ALA A  1 639  ? -23.760 62.289  123.958 1.00 26.83 ? 637  ALA A CA    1 
ATOM   4542  C C     . ALA A  1 639  ? -24.585 63.569  123.949 1.00 26.76 ? 637  ALA A C     1 
ATOM   4543  O O     . ALA A  1 639  ? -25.705 63.582  123.425 1.00 28.21 ? 637  ALA A O     1 
ATOM   4544  C CB    . ALA A  1 639  ? -23.943 61.535  125.276 1.00 28.28 ? 637  ALA A CB    1 
ATOM   4545  N N     . CYS A  1 640  ? -24.040 64.664  124.499 1.00 24.38 ? 638  CYS A N     1 
ATOM   4546  C CA    . CYS A  1 640  ? -24.738 65.944  124.420 1.00 24.15 ? 638  CYS A CA    1 
ATOM   4547  C C     . CYS A  1 640  ? -24.974 66.329  122.968 1.00 25.36 ? 638  CYS A C     1 
ATOM   4548  O O     . CYS A  1 640  ? -26.084 66.719  122.586 1.00 26.07 ? 638  CYS A O     1 
ATOM   4549  C CB    . CYS A  1 640  ? -23.950 67.047  125.120 1.00 24.55 ? 638  CYS A CB    1 
ATOM   4550  S SG    . CYS A  1 640  ? -23.770 66.880  126.898 1.00 28.86 ? 638  CYS A SG    1 
ATOM   4551  N N     . LEU A  1 641  ? -23.930 66.221  122.138 1.00 24.76 ? 639  LEU A N     1 
ATOM   4552  C CA    . LEU A  1 641  ? -24.091 66.544  120.722 1.00 22.24 ? 639  LEU A CA    1 
ATOM   4553  C C     . LEU A  1 641  ? -25.133 65.649  120.074 1.00 23.57 ? 639  LEU A C     1 
ATOM   4554  O O     . LEU A  1 641  ? -25.978 66.128  119.312 1.00 21.87 ? 639  LEU A O     1 
ATOM   4555  C CB    . LEU A  1 641  ? -22.756 66.418  119.987 1.00 23.18 ? 639  LEU A CB    1 
ATOM   4556  C CG    . LEU A  1 641  ? -21.830 67.630  119.931 1.00 21.92 ? 639  LEU A CG    1 
ATOM   4557  C CD1   . LEU A  1 641  ? -21.426 68.072  121.318 1.00 24.81 ? 639  LEU A CD1   1 
ATOM   4558  C CD2   . LEU A  1 641  ? -20.604 67.301  119.054 1.00 21.97 ? 639  LEU A CD2   1 
ATOM   4559  N N     . ASP A  1 642  ? -25.097 64.346  120.369 1.00 22.23 ? 640  ASP A N     1 
ATOM   4560  C CA    . ASP A  1 642  ? -26.071 63.439  119.764 1.00 24.26 ? 640  ASP A CA    1 
ATOM   4561  C C     . ASP A  1 642  ? -27.488 63.760  120.224 1.00 23.17 ? 640  ASP A C     1 
ATOM   4562  O O     . ASP A  1 642  ? -28.437 63.687  119.431 1.00 22.13 ? 640  ASP A O     1 
ATOM   4563  C CB    . ASP A  1 642  ? -25.711 61.987  120.083 1.00 24.22 ? 640  ASP A CB    1 
ATOM   4564  C CG    . ASP A  1 642  ? -24.651 61.434  119.137 1.00 27.45 ? 640  ASP A CG    1 
ATOM   4565  O OD1   . ASP A  1 642  ? -24.514 61.989  118.022 1.00 24.78 ? 640  ASP A OD1   1 
ATOM   4566  O OD2   . ASP A  1 642  ? -23.971 60.446  119.497 1.00 26.61 ? 640  ASP A OD2   1 
ATOM   4567  N N     . ARG A  1 643  ? -27.653 64.117  121.503 1.00 22.76 ? 641  ARG A N     1 
ATOM   4568  C CA    . ARG A  1 643  ? -28.971 64.524  121.980 1.00 23.00 ? 641  ARG A CA    1 
ATOM   4569  C C     . ARG A  1 643  ? -29.420 65.809  121.299 1.00 25.00 ? 641  ARG A C     1 
ATOM   4570  O O     . ARG A  1 643  ? -30.593 65.945  120.945 1.00 27.65 ? 641  ARG A O     1 
ATOM   4571  C CB    . ARG A  1 643  ? -28.972 64.682  123.503 1.00 29.54 ? 641  ARG A CB    1 
ATOM   4572  C CG    . ARG A  1 643  ? -29.079 63.355  124.248 1.00 27.80 ? 641  ARG A CG    1 
ATOM   4573  C CD    . ARG A  1 643  ? -29.277 63.559  125.757 1.00 28.60 ? 641  ARG A CD    1 
ATOM   4574  N NE    . ARG A  1 643  ? -28.157 64.274  126.356 1.00 26.38 ? 641  ARG A NE    1 
ATOM   4575  C CZ    . ARG A  1 643  ? -27.140 63.687  126.975 1.00 29.85 ? 641  ARG A CZ    1 
ATOM   4576  N NH1   . ARG A  1 643  ? -27.048 62.370  127.064 1.00 26.08 ? 641  ARG A NH1   1 
ATOM   4577  N NH2   . ARG A  1 643  ? -26.185 64.440  127.512 1.00 27.90 ? 641  ARG A NH2   1 
ATOM   4578  N N     . ALA A  1 644  ? -28.494 66.749  121.078 1.00 24.00 ? 642  ALA A N     1 
ATOM   4579  C CA    . ALA A  1 644  ? -28.850 67.979  120.372 1.00 23.40 ? 642  ALA A CA    1 
ATOM   4580  C C     . ALA A  1 644  ? -29.327 67.687  118.958 1.00 21.93 ? 642  ALA A C     1 
ATOM   4581  O O     . ALA A  1 644  ? -30.288 68.304  118.480 1.00 22.31 ? 642  ALA A O     1 
ATOM   4582  C CB    . ALA A  1 644  ? -27.660 68.936  120.331 1.00 23.89 ? 642  ALA A CB    1 
ATOM   4583  N N     . ALA A  1 645  ? -28.662 66.753  118.272 1.00 24.54 ? 643  ALA A N     1 
ATOM   4584  C CA    . ALA A  1 645  ? -29.069 66.384  116.918 1.00 22.93 ? 643  ALA A CA    1 
ATOM   4585  C C     . ALA A  1 645  ? -30.495 65.850  116.890 1.00 24.49 ? 643  ALA A C     1 
ATOM   4586  O O     . ALA A  1 645  ? -31.258 66.149  115.962 1.00 24.90 ? 643  ALA A O     1 
ATOM   4587  C CB    . ALA A  1 645  ? -28.112 65.331  116.351 1.00 23.43 ? 643  ALA A CB    1 
ATOM   4588  N N     . GLU A  1 646  ? -30.854 65.020  117.872 1.00 23.38 ? 644  GLU A N     1 
ATOM   4589  C CA    . GLU A  1 646  ? -32.220 64.512  117.969 1.00 27.98 ? 644  GLU A CA    1 
ATOM   4590  C C     . GLU A  1 646  ? -33.223 65.639  118.178 1.00 27.58 ? 644  GLU A C     1 
ATOM   4591  O O     . GLU A  1 646  ? -34.293 65.648  117.559 1.00 27.00 ? 644  GLU A O     1 
ATOM   4592  C CB    . GLU A  1 646  ? -32.327 63.498  119.111 1.00 27.28 ? 644  GLU A CB    1 
ATOM   4593  C CG    . GLU A  1 646  ? -31.457 62.288  118.930 1.00 34.12 ? 644  GLU A CG    1 
ATOM   4594  C CD    . GLU A  1 646  ? -31.881 61.472  117.738 1.00 36.31 ? 644  GLU A CD    1 
ATOM   4595  O OE1   . GLU A  1 646  ? -33.107 61.389  117.498 1.00 45.57 ? 644  GLU A OE1   1 
ATOM   4596  O OE2   . GLU A  1 646  ? -30.999 60.940  117.029 1.00 41.57 ? 644  GLU A OE2   1 
ATOM   4597  N N     . LEU A  1 647  ? -32.902 66.591  119.058 1.00 24.89 ? 645  LEU A N     1 
ATOM   4598  C CA    . LEU A  1 647  ? -33.786 67.731  119.272 1.00 25.70 ? 645  LEU A CA    1 
ATOM   4599  C C     . LEU A  1 647  ? -33.926 68.566  118.007 1.00 26.15 ? 645  LEU A C     1 
ATOM   4600  O O     . LEU A  1 647  ? -35.036 68.984  117.653 1.00 27.98 ? 645  LEU A O     1 
ATOM   4601  C CB    . LEU A  1 647  ? -33.277 68.586  120.440 1.00 23.55 ? 645  LEU A CB    1 
ATOM   4602  C CG    . LEU A  1 647  ? -33.322 67.915  121.818 1.00 27.10 ? 645  LEU A CG    1 
ATOM   4603  C CD1   . LEU A  1 647  ? -32.596 68.765  122.866 1.00 27.47 ? 645  LEU A CD1   1 
ATOM   4604  C CD2   . LEU A  1 647  ? -34.754 67.624  122.267 1.00 31.11 ? 645  LEU A CD2   1 
ATOM   4605  N N     . MET A  1 648  ? -32.822 68.801  117.288 1.00 23.98 ? 646  MET A N     1 
ATOM   4606  C CA    . MET A  1 648  ? -32.930 69.580  116.057 1.00 27.03 ? 646  MET A CA    1 
ATOM   4607  C C     . MET A  1 648  ? -33.767 68.855  115.018 1.00 23.92 ? 646  MET A C     1 
ATOM   4608  O O     . MET A  1 648  ? -34.562 69.483  114.315 1.00 22.90 ? 646  MET A O     1 
ATOM   4609  C CB    . MET A  1 648  ? -31.553 69.891  115.480 1.00 23.98 ? 646  MET A CB    1 
ATOM   4610  C CG    . MET A  1 648  ? -30.842 70.974  116.237 1.00 28.56 ? 646  MET A CG    1 
ATOM   4611  S SD    . MET A  1 648  ? -29.543 71.751  115.268 1.00 28.56 ? 646  MET A SD    1 
ATOM   4612  C CE    . MET A  1 648  ? -28.759 72.657  116.595 1.00 26.86 ? 646  MET A CE    1 
ATOM   4613  N N     . GLN A  1 649  ? -33.590 67.534  114.905 1.00 25.33 ? 647  GLN A N     1 
ATOM   4614  C CA    . GLN A  1 649  ? -34.357 66.760  113.931 1.00 22.91 ? 647  GLN A CA    1 
ATOM   4615  C C     . GLN A  1 649  ? -35.847 66.805  114.246 1.00 25.21 ? 647  GLN A C     1 
ATOM   4616  O O     . GLN A  1 649  ? -36.681 66.988  113.349 1.00 24.03 ? 647  GLN A O     1 
ATOM   4617  C CB    . GLN A  1 649  ? -33.861 65.315  113.916 1.00 25.07 ? 647  GLN A CB    1 
ATOM   4618  C CG    . GLN A  1 649  ? -34.571 64.443  112.907 1.00 23.55 ? 647  GLN A CG    1 
ATOM   4619  C CD    . GLN A  1 649  ? -34.051 64.670  111.501 1.00 24.37 ? 647  GLN A CD    1 
ATOM   4620  O OE1   . GLN A  1 649  ? -33.002 64.163  111.131 1.00 23.36 ? 647  GLN A OE1   1 
ATOM   4621  N NE2   . GLN A  1 649  ? -34.783 65.447  110.720 1.00 27.08 ? 647  GLN A NE2   1 
ATOM   4622  N N     . ALA A  1 650  ? -36.195 66.631  115.524 1.00 26.06 ? 648  ALA A N     1 
ATOM   4623  C CA    . ALA A  1 650  ? -37.592 66.690  115.946 1.00 30.97 ? 648  ALA A CA    1 
ATOM   4624  C C     . ALA A  1 650  ? -38.177 68.077  115.720 1.00 29.83 ? 648  ALA A C     1 
ATOM   4625  O O     . ALA A  1 650  ? -39.341 68.211  115.334 1.00 30.54 ? 648  ALA A O     1 
ATOM   4626  C CB    . ALA A  1 650  ? -37.705 66.297  117.420 1.00 28.67 ? 648  ALA A CB    1 
ATOM   4627  N N     . ARG A  1 651  ? -37.377 69.118  115.935 1.00 29.46 ? 649  ARG A N     1 
ATOM   4628  C CA    . ARG A  1 651  ? -37.822 70.495  115.800 1.00 26.71 ? 649  ARG A CA    1 
ATOM   4629  C C     . ARG A  1 651  ? -37.639 71.046  114.393 1.00 26.48 ? 649  ARG A C     1 
ATOM   4630  O O     . ARG A  1 651  ? -37.807 72.254  114.190 1.00 27.33 ? 649  ARG A O     1 
ATOM   4631  C CB    . ARG A  1 651  ? -37.074 71.369  116.809 1.00 29.84 ? 649  ARG A CB    1 
ATOM   4632  C CG    . ARG A  1 651  ? -37.795 72.639  117.199 1.00 35.76 ? 649  ARG A CG    1 
ATOM   4633  C CD    . ARG A  1 651  ? -37.459 73.059  118.632 1.00 35.09 ? 649  ARG A CD    1 
ATOM   4634  N NE    . ARG A  1 651  ? -37.886 74.432  118.878 1.00 35.51 ? 649  ARG A NE    1 
ATOM   4635  C CZ    . ARG A  1 651  ? -39.136 74.798  119.126 1.00 39.52 ? 649  ARG A CZ    1 
ATOM   4636  N NH1   . ARG A  1 651  ? -40.126 73.920  119.143 1.00 38.11 ? 649  ARG A NH1   1 
ATOM   4637  N NH2   . ARG A  1 651  ? -39.400 76.081  119.362 1.00 44.04 ? 649  ARG A NH2   1 
ATOM   4638  N N     . MET A  1 652  ? -37.311 70.197  113.416 1.00 25.97 ? 650  MET A N     1 
ATOM   4639  C CA    . MET A  1 652  ? -36.958 70.721  112.098 1.00 24.41 ? 650  MET A CA    1 
ATOM   4640  C C     . MET A  1 652  ? -38.031 71.618  111.507 1.00 25.51 ? 650  MET A C     1 
ATOM   4641  O O     . MET A  1 652  ? -37.685 72.714  111.034 1.00 25.05 ? 650  MET A O     1 
ATOM   4642  C CB    . MET A  1 652  ? -36.615 69.579  111.136 1.00 24.86 ? 650  MET A CB    1 
ATOM   4643  C CG    . MET A  1 652  ? -36.266 70.082  109.739 1.00 24.92 ? 650  MET A CG    1 
ATOM   4644  S SD    . MET A  1 652  ? -35.837 68.776  108.570 1.00 28.54 ? 650  MET A SD    1 
ATOM   4645  C CE    . MET A  1 652  ? -34.155 68.418  109.071 1.00 25.21 ? 650  MET A CE    1 
ATOM   4646  N N     . PRO A  1 653  ? -39.322 71.249  111.495 1.00 24.72 ? 651  PRO A N     1 
ATOM   4647  C CA    . PRO A  1 653  ? -40.301 72.142  110.848 1.00 26.46 ? 651  PRO A CA    1 
ATOM   4648  C C     . PRO A  1 653  ? -40.298 73.553  111.421 1.00 23.15 ? 651  PRO A C     1 
ATOM   4649  O O     . PRO A  1 653  ? -40.338 74.522  110.655 1.00 22.65 ? 651  PRO A O     1 
ATOM   4650  C CB    . PRO A  1 653  ? -41.636 71.419  111.082 1.00 25.06 ? 651  PRO A CB    1 
ATOM   4651  C CG    . PRO A  1 653  ? -41.250 69.955  111.112 1.00 25.43 ? 651  PRO A CG    1 
ATOM   4652  C CD    . PRO A  1 653  ? -39.959 69.995  111.946 1.00 23.03 ? 651  PRO A CD    1 
ATOM   4653  N N     . THR A  1 654  ? -40.209 73.693  112.746 1.00 26.86 ? 652  THR A N     1 
ATOM   4654  C CA    . THR A  1 654  ? -40.161 75.017  113.364 1.00 25.54 ? 652  THR A CA    1 
ATOM   4655  C C     . THR A  1 654  ? -38.871 75.758  113.015 1.00 27.01 ? 652  THR A C     1 
ATOM   4656  O O     . THR A  1 654  ? -38.904 76.958  112.707 1.00 24.98 ? 652  THR A O     1 
ATOM   4657  C CB    . THR A  1 654  ? -40.306 74.889  114.880 1.00 27.16 ? 652  THR A CB    1 
ATOM   4658  O OG1   . THR A  1 654  ? -41.524 74.200  115.189 1.00 28.33 ? 652  THR A OG1   1 
ATOM   4659  C CG2   . THR A  1 654  ? -40.321 76.263  115.530 1.00 31.36 ? 652  THR A CG2   1 
ATOM   4660  N N     . LEU A  1 655  ? -37.723 75.069  113.089 1.00 25.15 ? 653  LEU A N     1 
ATOM   4661  C CA    . LEU A  1 655  ? -36.450 75.686  112.713 1.00 25.44 ? 653  LEU A CA    1 
ATOM   4662  C C     . LEU A  1 655  ? -36.470 76.183  111.272 1.00 23.82 ? 653  LEU A C     1 
ATOM   4663  O O     . LEU A  1 655  ? -35.918 77.251  110.981 1.00 23.03 ? 653  LEU A O     1 
ATOM   4664  C CB    . LEU A  1 655  ? -35.296 74.703  112.917 1.00 22.85 ? 653  LEU A CB    1 
ATOM   4665  C CG    . LEU A  1 655  ? -35.152 74.196  114.342 1.00 24.78 ? 653  LEU A CG    1 
ATOM   4666  C CD1   . LEU A  1 655  ? -34.027 73.176  114.428 1.00 28.64 ? 653  LEU A CD1   1 
ATOM   4667  C CD2   . LEU A  1 655  ? -34.893 75.367  115.274 1.00 29.79 ? 653  LEU A CD2   1 
ATOM   4668  N N     . LEU A  1 656  ? -37.101 75.422  110.358 1.00 22.15 ? 654  LEU A N     1 
ATOM   4669  C CA    . LEU A  1 656  ? -37.260 75.863  108.971 1.00 25.33 ? 654  LEU A CA    1 
ATOM   4670  C C     . LEU A  1 656  ? -37.950 77.212  108.897 1.00 26.27 ? 654  LEU A C     1 
ATOM   4671  O O     . LEU A  1 656  ? -37.527 78.102  108.145 1.00 26.20 ? 654  LEU A O     1 
ATOM   4672  C CB    . LEU A  1 656  ? -38.085 74.849  108.169 1.00 24.94 ? 654  LEU A CB    1 
ATOM   4673  C CG    . LEU A  1 656  ? -37.593 73.416  108.053 1.00 28.10 ? 654  LEU A CG    1 
ATOM   4674  C CD1   . LEU A  1 656  ? -38.527 72.613  107.159 1.00 21.65 ? 654  LEU A CD1   1 
ATOM   4675  C CD2   . LEU A  1 656  ? -36.185 73.416  107.507 1.00 23.48 ? 654  LEU A CD2   1 
ATOM   4676  N N     . GLY A  1 657  ? -39.054 77.359  109.636 1.00 22.66 ? 655  GLY A N     1 
ATOM   4677  C CA    . GLY A  1 657  ? -39.802 78.600  109.590 1.00 25.84 ? 655  GLY A CA    1 
ATOM   4678  C C     . GLY A  1 657  ? -38.970 79.783  110.023 1.00 23.11 ? 655  GLY A C     1 
ATOM   4679  O O     . GLY A  1 657  ? -39.031 80.852  109.417 1.00 23.65 ? 655  GLY A O     1 
ATOM   4680  N N     . LEU A  1 658  ? -38.163 79.602  111.070 1.00 22.18 ? 656  LEU A N     1 
ATOM   4681  C CA    . LEU A  1 658  ? -37.290 80.681  111.503 1.00 22.59 ? 656  LEU A CA    1 
ATOM   4682  C C     . LEU A  1 658  ? -36.216 80.985  110.462 1.00 21.46 ? 656  LEU A C     1 
ATOM   4683  O O     . LEU A  1 658  ? -35.954 82.154  110.161 1.00 22.36 ? 656  LEU A O     1 
ATOM   4684  C CB    . LEU A  1 658  ? -36.658 80.324  112.851 1.00 21.63 ? 656  LEU A CB    1 
ATOM   4685  C CG    . LEU A  1 658  ? -35.925 81.464  113.542 1.00 26.84 ? 656  LEU A CG    1 
ATOM   4686  C CD1   . LEU A  1 658  ? -36.791 82.718  113.571 1.00 25.80 ? 656  LEU A CD1   1 
ATOM   4687  C CD2   . LEU A  1 658  ? -35.570 81.015  114.960 1.00 22.23 ? 656  LEU A CD2   1 
ATOM   4688  N N     . ILE A  1 659  ? -35.598 79.951  109.887 1.00 21.48 ? 657  ILE A N     1 
ATOM   4689  C CA    . ILE A  1 659  ? -34.523 80.187  108.928 1.00 20.75 ? 657  ILE A CA    1 
ATOM   4690  C C     . ILE A  1 659  ? -35.059 80.881  107.683 1.00 20.96 ? 657  ILE A C     1 
ATOM   4691  O O     . ILE A  1 659  ? -34.399 81.747  107.106 1.00 20.34 ? 657  ILE A O     1 
ATOM   4692  C CB    . ILE A  1 659  ? -33.824 78.866  108.584 1.00 20.18 ? 657  ILE A CB    1 
ATOM   4693  C CG1   . ILE A  1 659  ? -33.109 78.347  109.849 1.00 21.62 ? 657  ILE A CG1   1 
ATOM   4694  C CG2   . ILE A  1 659  ? -32.806 79.085  107.455 1.00 19.91 ? 657  ILE A CG2   1 
ATOM   4695  C CD1   . ILE A  1 659  ? -32.484 76.987  109.675 1.00 25.88 ? 657  ILE A CD1   1 
ATOM   4696  N N     . ILE A  1 660  ? -36.257 80.501  107.251 1.00 22.37 ? 658  ILE A N     1 
ATOM   4697  C CA    . ILE A  1 660  ? -36.850 81.078  106.045 1.00 20.18 ? 658  ILE A CA    1 
ATOM   4698  C C     . ILE A  1 660  ? -37.060 82.580  106.214 1.00 22.57 ? 658  ILE A C     1 
ATOM   4699  O O     . ILE A  1 660  ? -36.705 83.381  105.334 1.00 22.68 ? 658  ILE A O     1 
ATOM   4700  C CB    . ILE A  1 660  ? -38.164 80.351  105.716 1.00 21.88 ? 658  ILE A CB    1 
ATOM   4701  C CG1   . ILE A  1 660  ? -37.866 78.959  105.140 1.00 24.35 ? 658  ILE A CG1   1 
ATOM   4702  C CG2   . ILE A  1 660  ? -39.047 81.198  104.786 1.00 22.87 ? 658  ILE A CG2   1 
ATOM   4703  C CD1   . ILE A  1 660  ? -39.076 78.061  105.054 1.00 25.67 ? 658  ILE A CD1   1 
ATOM   4704  N N     . ARG A  1 661  ? -37.633 82.984  107.355 1.00 21.74 ? 659  ARG A N     1 
ATOM   4705  C CA    . ARG A  1 661  ? -37.971 84.386  107.589 1.00 25.30 ? 659  ARG A CA    1 
ATOM   4706  C C     . ARG A  1 661  ? -36.785 85.214  108.088 1.00 26.03 ? 659  ARG A C     1 
ATOM   4707  O O     . ARG A  1 661  ? -36.638 86.371  107.680 1.00 26.72 ? 659  ARG A O     1 
ATOM   4708  C CB    . ARG A  1 661  ? -39.154 84.480  108.563 1.00 23.43 ? 659  ARG A CB    1 
ATOM   4709  C CG    . ARG A  1 661  ? -40.485 84.081  107.903 1.00 25.50 ? 659  ARG A CG    1 
ATOM   4710  C CD    . ARG A  1 661  ? -41.662 84.011  108.890 1.00 24.39 ? 659  ARG A CD    1 
ATOM   4711  N NE    . ARG A  1 661  ? -41.962 85.294  109.514 1.00 25.51 ? 659  ARG A NE    1 
ATOM   4712  C CZ    . ARG A  1 661  ? -41.910 85.516  110.821 1.00 27.52 ? 659  ARG A CZ    1 
ATOM   4713  N NH1   . ARG A  1 661  ? -41.568 84.562  111.671 1.00 27.84 ? 659  ARG A NH1   1 
ATOM   4714  N NH2   . ARG A  1 661  ? -42.212 86.726  111.291 1.00 26.18 ? 659  ARG A NH2   1 
ATOM   4715  N N     . GLU A  1 662  ? -35.932 84.667  108.969 1.00 21.39 ? 660  GLU A N     1 
ATOM   4716  C CA    . GLU A  1 662  ? -34.817 85.476  109.464 1.00 23.09 ? 660  GLU A CA    1 
ATOM   4717  C C     . GLU A  1 662  ? -33.708 85.619  108.426 1.00 23.50 ? 660  GLU A C     1 
ATOM   4718  O O     . GLU A  1 662  ? -33.121 86.693  108.289 1.00 22.25 ? 660  GLU A O     1 
ATOM   4719  C CB    . GLU A  1 662  ? -34.235 84.894  110.758 1.00 25.41 ? 660  GLU A CB    1 
ATOM   4720  C CG    . GLU A  1 662  ? -33.060 85.719  111.301 1.00 24.95 ? 660  GLU A CG    1 
ATOM   4721  C CD    . GLU A  1 662  ? -32.492 85.192  112.610 1.00 27.45 ? 660  GLU A CD    1 
ATOM   4722  O OE1   . GLU A  1 662  ? -32.319 83.966  112.745 1.00 27.11 ? 660  GLU A OE1   1 
ATOM   4723  O OE2   . GLU A  1 662  ? -32.190 86.015  113.502 1.00 26.45 ? 660  GLU A OE2   1 
ATOM   4724  N N     . ALA A  1 663  ? -33.401 84.561  107.683 1.00 21.30 ? 661  ALA A N     1 
ATOM   4725  C CA    . ALA A  1 663  ? -32.242 84.588  106.807 1.00 24.68 ? 661  ALA A CA    1 
ATOM   4726  C C     . ALA A  1 663  ? -32.615 84.723  105.342 1.00 23.38 ? 661  ALA A C     1 
ATOM   4727  O O     . ALA A  1 663  ? -31.717 84.851  104.501 1.00 23.00 ? 661  ALA A O     1 
ATOM   4728  C CB    . ALA A  1 663  ? -31.390 83.332  107.018 1.00 25.21 ? 661  ALA A CB    1 
ATOM   4729  N N     . GLY A  1 664  ? -33.906 84.714  105.022 1.00 24.29 ? 662  GLY A N     1 
ATOM   4730  C CA    . GLY A  1 664  ? -34.347 84.837  103.640 1.00 21.75 ? 662  GLY A CA    1 
ATOM   4731  C C     . GLY A  1 664  ? -34.113 83.614  102.785 1.00 21.12 ? 662  GLY A C     1 
ATOM   4732  O O     . GLY A  1 664  ? -33.961 83.743  101.569 1.00 24.55 ? 662  GLY A O     1 
ATOM   4733  N N     . LYS A  1 665  ? -34.082 82.428  103.377 1.00 22.79 ? 663  LYS A N     1 
ATOM   4734  C CA    . LYS A  1 665  ? -33.794 81.214  102.622 1.00 25.53 ? 663  LYS A CA    1 
ATOM   4735  C C     . LYS A  1 665  ? -35.087 80.531  102.186 1.00 24.57 ? 663  LYS A C     1 
ATOM   4736  O O     . LYS A  1 665  ? -36.128 80.669  102.829 1.00 21.73 ? 663  LYS A O     1 
ATOM   4737  C CB    . LYS A  1 665  ? -32.950 80.245  103.458 1.00 24.87 ? 663  LYS A CB    1 
ATOM   4738  C CG    . LYS A  1 665  ? -31.720 80.893  104.063 1.00 25.43 ? 663  LYS A CG    1 
ATOM   4739  C CD    . LYS A  1 665  ? -30.806 79.853  104.664 1.00 31.64 ? 663  LYS A CD    1 
ATOM   4740  C CE    . LYS A  1 665  ? -29.414 79.927  104.071 1.00 30.44 ? 663  LYS A CE    1 
ATOM   4741  N NZ    . LYS A  1 665  ? -28.608 78.738  104.485 1.00 30.16 ? 663  LYS A NZ    1 
ATOM   4742  N N     . SER A  1 666  ? -35.005 79.788  101.085 1.00 23.03 ? 664  SER A N     1 
ATOM   4743  C CA    . SER A  1 666  ? -36.120 78.983  100.620 1.00 26.53 ? 664  SER A CA    1 
ATOM   4744  C C     . SER A  1 666  ? -36.274 77.728  101.484 1.00 25.20 ? 664  SER A C     1 
ATOM   4745  O O     . SER A  1 666  ? -35.376 77.343  102.252 1.00 23.59 ? 664  SER A O     1 
ATOM   4746  C CB    . SER A  1 666  ? -35.915 78.601  99.156  1.00 25.69 ? 664  SER A CB    1 
ATOM   4747  O OG    . SER A  1 666  ? -34.786 77.754  99.042  1.00 28.59 ? 664  SER A OG    1 
ATOM   4748  N N     . ALA A  1 667  ? -37.432 77.073  101.348 1.00 21.72 ? 665  ALA A N     1 
ATOM   4749  C CA    . ALA A  1 667  ? -37.715 75.911  102.190 1.00 26.82 ? 665  ALA A CA    1 
ATOM   4750  C C     . ALA A  1 667  ? -36.705 74.793  101.965 1.00 25.18 ? 665  ALA A C     1 
ATOM   4751  O O     . ALA A  1 667  ? -36.225 74.187  102.929 1.00 22.89 ? 665  ALA A O     1 
ATOM   4752  C CB    . ALA A  1 667  ? -39.137 75.391  101.948 1.00 23.12 ? 665  ALA A CB    1 
ATOM   4753  N N     . LEU A  1 668  ? -36.377 74.494  100.704 1.00 22.19 ? 666  LEU A N     1 
ATOM   4754  C CA    A LEU A  1 668  ? -35.420 73.423  100.436 0.50 24.02 ? 666  LEU A CA    1 
ATOM   4755  C CA    B LEU A  1 668  ? -35.414 73.430  100.423 0.50 24.02 ? 666  LEU A CA    1 
ATOM   4756  C C     . LEU A  1 668  ? -34.060 73.726  101.057 1.00 23.17 ? 666  LEU A C     1 
ATOM   4757  O O     . LEU A  1 668  ? -33.419 72.834  101.612 1.00 23.38 ? 666  LEU A O     1 
ATOM   4758  C CB    A LEU A  1 668  ? -35.283 73.197  98.930  0.50 25.71 ? 666  LEU A CB    1 
ATOM   4759  C CB    B LEU A  1 668  ? -35.259 73.242  98.912  0.50 25.71 ? 666  LEU A CB    1 
ATOM   4760  C CG    A LEU A  1 668  ? -34.523 71.942  98.496  0.50 27.01 ? 666  LEU A CG    1 
ATOM   4761  C CG    B LEU A  1 668  ? -36.239 72.276  98.248  0.50 25.62 ? 666  LEU A CG    1 
ATOM   4762  C CD1   A LEU A  1 668  ? -35.009 70.728  99.269  0.50 26.64 ? 666  LEU A CD1   1 
ATOM   4763  C CD1   B LEU A  1 668  ? -36.261 72.457  96.737  0.50 25.23 ? 666  LEU A CD1   1 
ATOM   4764  C CD2   A LEU A  1 668  ? -34.702 71.726  97.007  0.50 25.64 ? 666  LEU A CD2   1 
ATOM   4765  C CD2   B LEU A  1 668  ? -35.866 70.845  98.610  0.50 28.13 ? 666  LEU A CD2   1 
ATOM   4766  N N     . ASN A  1 669  ? -33.613 74.982  100.985 1.00 22.59 ? 667  ASN A N     1 
ATOM   4767  C CA    . ASN A  1 669  ? -32.313 75.342  101.539 1.00 22.91 ? 667  ASN A CA    1 
ATOM   4768  C C     . ASN A  1 669  ? -32.317 75.353  103.058 1.00 23.31 ? 667  ASN A C     1 
ATOM   4769  O O     . ASN A  1 669  ? -31.290 75.046  103.675 1.00 21.20 ? 667  ASN A O     1 
ATOM   4770  C CB    . ASN A  1 669  ? -31.870 76.698  101.011 1.00 23.64 ? 667  ASN A CB    1 
ATOM   4771  C CG    . ASN A  1 669  ? -31.398 76.618  99.576  1.00 30.98 ? 667  ASN A CG    1 
ATOM   4772  O OD1   . ASN A  1 669  ? -30.702 75.675  99.196  1.00 35.00 ? 667  ASN A OD1   1 
ATOM   4773  N ND2   . ASN A  1 669  ? -31.780 77.591  98.773  1.00 27.81 ? 667  ASN A ND2   1 
ATOM   4774  N N     . ALA A  1 670  ? -33.450 75.699  103.676 1.00 20.64 ? 668  ALA A N     1 
ATOM   4775  C CA    . ALA A  1 670  ? -33.540 75.589  105.128 1.00 22.57 ? 668  ALA A CA    1 
ATOM   4776  C C     . ALA A  1 670  ? -33.499 74.131  105.577 1.00 22.97 ? 668  ALA A C     1 
ATOM   4777  O O     . ALA A  1 670  ? -32.881 73.812  106.602 1.00 20.41 ? 668  ALA A O     1 
ATOM   4778  C CB    . ALA A  1 670  ? -34.802 76.290  105.642 1.00 22.81 ? 668  ALA A CB    1 
ATOM   4779  N N     . ILE A  1 671  ? -34.146 73.228  104.837 1.00 21.43 ? 669  ILE A N     1 
ATOM   4780  C CA    . ILE A  1 671  ? -34.049 71.806  105.179 1.00 19.00 ? 669  ILE A CA    1 
ATOM   4781  C C     . ILE A  1 671  ? -32.590 71.355  105.153 1.00 19.15 ? 669  ILE A C     1 
ATOM   4782  O O     . ILE A  1 671  ? -32.102 70.690  106.079 1.00 21.91 ? 669  ILE A O     1 
ATOM   4783  C CB    . ILE A  1 671  ? -34.916 70.963  104.231 1.00 21.45 ? 669  ILE A CB    1 
ATOM   4784  C CG1   . ILE A  1 671  ? -36.392 71.285  104.474 1.00 23.77 ? 669  ILE A CG1   1 
ATOM   4785  C CG2   . ILE A  1 671  ? -34.641 69.457  104.443 1.00 20.18 ? 669  ILE A CG2   1 
ATOM   4786  C CD1   . ILE A  1 671  ? -37.323 70.803  103.377 1.00 21.26 ? 669  ILE A CD1   1 
ATOM   4787  N N     . ALA A  1 672  ? -31.876 71.709  104.083 1.00 18.52 ? 670  ALA A N     1 
ATOM   4788  C CA    . ALA A  1 672  ? -30.476 71.329  103.960 1.00 23.54 ? 670  ALA A CA    1 
ATOM   4789  C C     . ALA A  1 672  ? -29.660 71.922  105.097 1.00 18.87 ? 670  ALA A C     1 
ATOM   4790  O O     . ALA A  1 672  ? -28.777 71.260  105.647 1.00 21.49 ? 670  ALA A O     1 
ATOM   4791  C CB    . ALA A  1 672  ? -29.932 71.776  102.603 1.00 24.63 ? 670  ALA A CB    1 
ATOM   4792  N N     . GLU A  1 673  ? -29.970 73.164  105.480 1.00 21.80 ? 671  GLU A N     1 
ATOM   4793  C CA    . GLU A  1 673  ? -29.273 73.797  106.594 1.00 21.60 ? 671  GLU A CA    1 
ATOM   4794  C C     . GLU A  1 673  ? -29.503 73.055  107.909 1.00 26.46 ? 671  GLU A C     1 
ATOM   4795  O O     . GLU A  1 673  ? -28.555 72.812  108.672 1.00 21.23 ? 671  GLU A O     1 
ATOM   4796  C CB    . GLU A  1 673  ? -29.721 75.247  106.725 1.00 23.41 ? 671  GLU A CB    1 
ATOM   4797  C CG    . GLU A  1 673  ? -29.163 75.906  107.975 1.00 25.84 ? 671  GLU A CG    1 
ATOM   4798  C CD    . GLU A  1 673  ? -28.371 77.156  107.664 1.00 26.72 ? 671  GLU A CD    1 
ATOM   4799  O OE1   . GLU A  1 673  ? -28.627 77.782  106.614 1.00 34.32 ? 671  GLU A OE1   1 
ATOM   4800  O OE2   . GLU A  1 673  ? -27.484 77.509  108.468 1.00 25.28 ? 671  GLU A OE2   1 
ATOM   4801  N N     . VAL A  1 674  ? -30.759 72.707  108.215 1.00 20.21 ? 672  VAL A N     1 
ATOM   4802  C CA    . VAL A  1 674  ? -31.003 71.980  109.462 1.00 20.51 ? 672  VAL A CA    1 
ATOM   4803  C C     . VAL A  1 674  ? -30.356 70.596  109.407 1.00 20.89 ? 672  VAL A C     1 
ATOM   4804  O O     . VAL A  1 674  ? -29.729 70.148  110.375 1.00 19.62 ? 672  VAL A O     1 
ATOM   4805  C CB    . VAL A  1 674  ? -32.512 71.897  109.772 1.00 20.70 ? 672  VAL A CB    1 
ATOM   4806  C CG1   . VAL A  1 674  ? -32.753 71.060  111.031 1.00 20.57 ? 672  VAL A CG1   1 
ATOM   4807  C CG2   . VAL A  1 674  ? -33.099 73.305  109.947 1.00 20.34 ? 672  VAL A CG2   1 
ATOM   4808  N N     . ARG A  1 675  ? -30.483 69.903  108.273 1.00 19.81 ? 673  ARG A N     1 
ATOM   4809  C CA    . ARG A  1 675  ? -29.780 68.633  108.099 1.00 22.76 ? 673  ARG A CA    1 
ATOM   4810  C C     . ARG A  1 675  ? -28.267 68.783  108.300 1.00 22.09 ? 673  ARG A C     1 
ATOM   4811  O O     . ARG A  1 675  ? -27.629 67.921  108.915 1.00 21.66 ? 673  ARG A O     1 
ATOM   4812  C CB    . ARG A  1 675  ? -30.083 68.061  106.711 1.00 20.64 ? 673  ARG A CB    1 
ATOM   4813  C CG    . ARG A  1 675  ? -31.498 67.500  106.600 1.00 20.80 ? 673  ARG A CG    1 
ATOM   4814  C CD    . ARG A  1 675  ? -31.647 66.712  105.311 1.00 21.27 ? 673  ARG A CD    1 
ATOM   4815  N NE    . ARG A  1 675  ? -30.870 65.477  105.354 1.00 24.66 ? 673  ARG A NE    1 
ATOM   4816  C CZ    . ARG A  1 675  ? -30.461 64.804  104.285 1.00 23.40 ? 673  ARG A CZ    1 
ATOM   4817  N NH1   . ARG A  1 675  ? -30.712 65.235  103.055 1.00 21.14 ? 673  ARG A NH1   1 
ATOM   4818  N NH2   . ARG A  1 675  ? -29.791 63.665  104.453 1.00 18.45 ? 673  ARG A NH2   1 
ATOM   4819  N N     . GLU A  1 676  ? -27.678 69.869  107.788 1.00 19.50 ? 674  GLU A N     1 
ATOM   4820  C CA    . GLU A  1 676  ? -26.235 70.060  107.914 1.00 19.74 ? 674  GLU A CA    1 
ATOM   4821  C C     . GLU A  1 676  ? -25.844 70.234  109.370 1.00 19.27 ? 674  GLU A C     1 
ATOM   4822  O O     . GLU A  1 676  ? -24.817 69.699  109.813 1.00 20.70 ? 674  GLU A O     1 
ATOM   4823  C CB    . GLU A  1 676  ? -25.776 71.278  107.102 1.00 18.86 ? 674  GLU A CB    1 
ATOM   4824  C CG    . GLU A  1 676  ? -24.249 71.433  107.031 1.00 26.36 ? 674  GLU A CG    1 
ATOM   4825  C CD    . GLU A  1 676  ? -23.821 72.592  106.125 1.00 33.43 ? 674  GLU A CD    1 
ATOM   4826  O OE1   . GLU A  1 676  ? -24.668 73.089  105.354 1.00 40.86 ? 674  GLU A OE1   1 
ATOM   4827  O OE2   . GLU A  1 676  ? -22.642 73.008  106.181 1.00 42.93 ? 674  GLU A OE2   1 
ATOM   4828  N N     . ALA A  1 677  ? -26.669 70.954  110.139 1.00 19.89 ? 675  ALA A N     1 
ATOM   4829  C CA    . ALA A  1 677  ? -26.404 71.113  111.569 1.00 19.83 ? 675  ALA A CA    1 
ATOM   4830  C C     . ALA A  1 677  ? -26.453 69.768  112.274 1.00 19.93 ? 675  ALA A C     1 
ATOM   4831  O O     . ALA A  1 677  ? -25.572 69.434  113.079 1.00 20.10 ? 675  ALA A O     1 
ATOM   4832  C CB    . ALA A  1 677  ? -27.421 72.075  112.189 1.00 20.04 ? 675  ALA A CB    1 
ATOM   4833  N N     . ILE A  1 678  ? -27.482 68.975  111.971 1.00 20.67 ? 676  ILE A N     1 
ATOM   4834  C CA    . ILE A  1 678  ? -27.614 67.647  112.564 1.00 21.76 ? 676  ILE A CA    1 
ATOM   4835  C C     . ILE A  1 678  ? -26.420 66.775  112.191 1.00 19.87 ? 676  ILE A C     1 
ATOM   4836  O O     . ILE A  1 678  ? -25.908 66.013  113.013 1.00 20.07 ? 676  ILE A O     1 
ATOM   4837  C CB    . ILE A  1 678  ? -28.937 67.001  112.110 1.00 19.95 ? 676  ILE A CB    1 
ATOM   4838  C CG1   . ILE A  1 678  ? -30.143 67.723  112.715 1.00 23.63 ? 676  ILE A CG1   1 
ATOM   4839  C CG2   . ILE A  1 678  ? -28.962 65.502  112.433 1.00 20.10 ? 676  ILE A CG2   1 
ATOM   4840  C CD1   . ILE A  1 678  ? -31.426 67.449  111.931 1.00 23.00 ? 676  ILE A CD1   1 
ATOM   4841  N N     . ASP A  1 679  ? -26.003 66.836  110.924 1.00 20.13 ? 677  ASP A N     1 
ATOM   4842  C CA    . ASP A  1 679  ? -24.867 66.040  110.465 1.00 22.78 ? 677  ASP A CA    1 
ATOM   4843  C C     . ASP A  1 679  ? -23.580 66.430  111.196 1.00 20.22 ? 677  ASP A C     1 
ATOM   4844  O O     . ASP A  1 679  ? -22.821 65.554  111.629 1.00 19.68 ? 677  ASP A O     1 
ATOM   4845  C CB    . ASP A  1 679  ? -24.703 66.198  108.948 1.00 19.10 ? 677  ASP A CB    1 
ATOM   4846  C CG    . ASP A  1 679  ? -25.843 65.548  108.149 1.00 23.48 ? 677  ASP A CG    1 
ATOM   4847  O OD1   . ASP A  1 679  ? -26.516 64.635  108.670 1.00 21.16 ? 677  ASP A OD1   1 
ATOM   4848  O OD2   . ASP A  1 679  ? -26.027 65.930  106.971 1.00 24.05 ? 677  ASP A OD2   1 
ATOM   4849  N N     . PHE A  1 680  ? -23.330 67.739  111.365 1.00 19.61 ? 678  PHE A N     1 
ATOM   4850  C CA    . PHE A  1 680  ? -22.153 68.189  112.113 1.00 19.79 ? 678  PHE A CA    1 
ATOM   4851  C C     . PHE A  1 680  ? -22.162 67.637  113.530 1.00 20.12 ? 678  PHE A C     1 
ATOM   4852  O O     . PHE A  1 680  ? -21.130 67.186  114.048 1.00 20.24 ? 678  PHE A O     1 
ATOM   4853  C CB    . PHE A  1 680  ? -22.113 69.715  112.195 1.00 19.84 ? 678  PHE A CB    1 
ATOM   4854  C CG    . PHE A  1 680  ? -21.480 70.396  111.024 1.00 19.60 ? 678  PHE A CG    1 
ATOM   4855  C CD1   . PHE A  1 680  ? -20.232 70.023  110.566 1.00 19.49 ? 678  PHE A CD1   1 
ATOM   4856  C CD2   . PHE A  1 680  ? -22.125 71.471  110.423 1.00 19.51 ? 678  PHE A CD2   1 
ATOM   4857  C CE1   . PHE A  1 680  ? -19.645 70.688  109.504 1.00 22.81 ? 678  PHE A CE1   1 
ATOM   4858  C CE2   . PHE A  1 680  ? -21.552 72.150  109.362 1.00 22.64 ? 678  PHE A CE2   1 
ATOM   4859  C CZ    . PHE A  1 680  ? -20.307 71.766  108.898 1.00 22.93 ? 678  PHE A CZ    1 
ATOM   4860  N N     . LEU A  1 681  ? -23.312 67.740  114.205 1.00 20.57 ? 679  LEU A N     1 
ATOM   4861  C CA    . LEU A  1 681  ? -23.401 67.275  115.586 1.00 20.67 ? 679  LEU A CA    1 
ATOM   4862  C C     . LEU A  1 681  ? -23.057 65.797  115.674 1.00 20.70 ? 679  LEU A C     1 
ATOM   4863  O O     . LEU A  1 681  ? -22.218 65.380  116.488 1.00 22.37 ? 679  LEU A O     1 
ATOM   4864  C CB    . LEU A  1 681  ? -24.808 67.547  116.132 1.00 21.31 ? 679  LEU A CB    1 
ATOM   4865  C CG    . LEU A  1 681  ? -25.168 69.024  116.350 1.00 22.24 ? 679  LEU A CG    1 
ATOM   4866  C CD1   . LEU A  1 681  ? -26.674 69.211  116.430 1.00 23.08 ? 679  LEU A CD1   1 
ATOM   4867  C CD2   . LEU A  1 681  ? -24.530 69.509  117.651 1.00 21.32 ? 679  LEU A CD2   1 
ATOM   4868  N N     . ARG A  1 682  ? -23.681 64.990  114.818 1.00 20.50 ? 680  ARG A N     1 
ATOM   4869  C CA    . ARG A  1 682  ? -23.465 63.549  114.858 1.00 20.56 ? 680  ARG A CA    1 
ATOM   4870  C C     . ARG A  1 682  ? -22.083 63.167  114.356 1.00 20.42 ? 680  ARG A C     1 
ATOM   4871  O O     . ARG A  1 682  ? -21.502 62.196  114.845 1.00 21.87 ? 680  ARG A O     1 
ATOM   4872  C CB    . ARG A  1 682  ? -24.536 62.847  114.032 1.00 20.40 ? 680  ARG A CB    1 
ATOM   4873  C CG    . ARG A  1 682  ? -25.897 62.839  114.729 1.00 23.52 ? 680  ARG A CG    1 
ATOM   4874  C CD    . ARG A  1 682  ? -26.967 62.249  113.829 1.00 25.11 ? 680  ARG A CD    1 
ATOM   4875  N NE    . ARG A  1 682  ? -28.280 62.259  114.465 1.00 23.40 ? 680  ARG A NE    1 
ATOM   4876  C CZ    . ARG A  1 682  ? -29.425 62.097  113.810 1.00 28.52 ? 680  ARG A CZ    1 
ATOM   4877  N NH1   . ARG A  1 682  ? -29.452 61.931  112.496 1.00 22.40 ? 680  ARG A NH1   1 
ATOM   4878  N NH2   . ARG A  1 682  ? -30.570 62.120  114.489 1.00 27.35 ? 680  ARG A NH2   1 
ATOM   4879  N N     . TYR A  1 683  ? -21.553 63.904  113.379 1.00 20.13 ? 681  TYR A N     1 
ATOM   4880  C CA    . TYR A  1 683  ? -20.227 63.591  112.858 1.00 20.63 ? 681  TYR A CA    1 
ATOM   4881  C C     . TYR A  1 683  ? -19.151 63.881  113.897 1.00 20.26 ? 681  TYR A C     1 
ATOM   4882  O O     . TYR A  1 683  ? -18.307 63.019  114.191 1.00 20.38 ? 681  TYR A O     1 
ATOM   4883  C CB    . TYR A  1 683  ? -19.961 64.382  111.584 1.00 19.69 ? 681  TYR A CB    1 
ATOM   4884  C CG    . TYR A  1 683  ? -18.584 64.160  111.005 1.00 19.71 ? 681  TYR A CG    1 
ATOM   4885  C CD1   . TYR A  1 683  ? -18.296 63.021  110.266 1.00 19.48 ? 681  TYR A CD1   1 
ATOM   4886  C CD2   . TYR A  1 683  ? -17.565 65.077  111.230 1.00 19.63 ? 681  TYR A CD2   1 
ATOM   4887  C CE1   . TYR A  1 683  ? -17.039 62.817  109.741 1.00 19.65 ? 681  TYR A CE1   1 
ATOM   4888  C CE2   . TYR A  1 683  ? -16.307 64.884  110.714 1.00 19.56 ? 681  TYR A CE2   1 
ATOM   4889  C CZ    . TYR A  1 683  ? -16.044 63.753  109.969 1.00 19.45 ? 681  TYR A CZ    1 
ATOM   4890  O OH    . TYR A  1 683  ? -14.776 63.548  109.458 1.00 23.82 ? 681  TYR A OH    1 
ATOM   4891  N N     . TYR A  1 684  ? -19.169 65.089  114.479 1.00 20.37 ? 682  TYR A N     1 
ATOM   4892  C CA    . TYR A  1 684  ? -18.143 65.408  115.477 1.00 20.63 ? 682  TYR A CA    1 
ATOM   4893  C C     . TYR A  1 684  ? -18.313 64.564  116.740 1.00 22.20 ? 682  TYR A C     1 
ATOM   4894  O O     . TYR A  1 684  ? -17.328 64.292  117.450 1.00 21.20 ? 682  TYR A O     1 
ATOM   4895  C CB    . TYR A  1 684  ? -18.174 66.901  115.820 1.00 20.75 ? 682  TYR A CB    1 
ATOM   4896  C CG    . TYR A  1 684  ? -17.818 67.820  114.660 1.00 20.42 ? 682  TYR A CG    1 
ATOM   4897  C CD1   . TYR A  1 684  ? -16.769 67.515  113.794 1.00 20.22 ? 682  TYR A CD1   1 
ATOM   4898  C CD2   . TYR A  1 684  ? -18.527 69.005  114.450 1.00 20.38 ? 682  TYR A CD2   1 
ATOM   4899  C CE1   . TYR A  1 684  ? -16.440 68.359  112.731 1.00 20.66 ? 682  TYR A CE1   1 
ATOM   4900  C CE2   . TYR A  1 684  ? -18.203 69.857  113.408 1.00 20.15 ? 682  TYR A CE2   1 
ATOM   4901  C CZ    . TYR A  1 684  ? -17.165 69.526  112.546 1.00 19.96 ? 682  TYR A CZ    1 
ATOM   4902  O OH    . TYR A  1 684  ? -16.848 70.363  111.492 1.00 21.51 ? 682  TYR A OH    1 
ATOM   4903  N N     . ALA A  1 685  ? -19.541 64.140  117.043 1.00 21.09 ? 683  ALA A N     1 
ATOM   4904  C CA    . ALA A  1 685  ? -19.732 63.202  118.149 1.00 21.44 ? 683  ALA A CA    1 
ATOM   4905  C C     . ALA A  1 685  ? -19.056 61.875  117.844 1.00 21.43 ? 683  ALA A C     1 
ATOM   4906  O O     . ALA A  1 685  ? -18.335 61.330  118.681 1.00 21.71 ? 683  ALA A O     1 
ATOM   4907  C CB    . ALA A  1 685  ? -21.217 62.989  118.439 1.00 23.63 ? 683  ALA A CB    1 
ATOM   4908  N N     . GLU A  1 686  ? -19.264 61.343  116.638 1.00 21.12 ? 684  GLU A N     1 
ATOM   4909  C CA    . GLU A  1 686  ? -18.595 60.091  116.284 1.00 26.03 ? 684  GLU A CA    1 
ATOM   4910  C C     . GLU A  1 686  ? -17.078 60.261  116.187 1.00 21.51 ? 684  GLU A C     1 
ATOM   4911  O O     . GLU A  1 686  ? -16.326 59.383  116.635 1.00 24.88 ? 684  GLU A O     1 
ATOM   4912  C CB    . GLU A  1 686  ? -19.158 59.527  114.976 1.00 23.55 ? 684  GLU A CB    1 
ATOM   4913  C CG    . GLU A  1 686  ? -18.381 58.326  114.427 1.00 24.24 ? 684  GLU A CG    1 
ATOM   4914  C CD    . GLU A  1 686  ? -18.498 57.033  115.260 1.00 32.94 ? 684  GLU A CD    1 
ATOM   4915  O OE1   . GLU A  1 686  ? -19.263 56.983  116.247 1.00 31.51 ? 684  GLU A OE1   1 
ATOM   4916  O OE2   . GLU A  1 686  ? -17.800 56.049  114.917 1.00 36.36 ? 684  GLU A OE2   1 
ATOM   4917  N N     . GLN A  1 687  ? -16.598 61.385  115.644 1.00 20.87 ? 685  GLN A N     1 
ATOM   4918  C CA    . GLN A  1 687  ? -15.151 61.579  115.565 1.00 21.29 ? 685  GLN A CA    1 
ATOM   4919  C C     . GLN A  1 687  ? -14.546 61.627  116.961 1.00 21.48 ? 685  GLN A C     1 
ATOM   4920  O O     . GLN A  1 687  ? -13.438 61.122  117.189 1.00 21.97 ? 685  GLN A O     1 
ATOM   4921  C CB    . GLN A  1 687  ? -14.814 62.857  114.788 1.00 24.99 ? 685  GLN A CB    1 
ATOM   4922  C CG    . GLN A  1 687  ? -15.139 62.745  113.301 1.00 20.25 ? 685  GLN A CG    1 
ATOM   4923  C CD    . GLN A  1 687  ? -14.436 61.560  112.650 1.00 23.37 ? 685  GLN A CD    1 
ATOM   4924  O OE1   . GLN A  1 687  ? -13.204 61.457  112.673 1.00 22.99 ? 685  GLN A OE1   1 
ATOM   4925  N NE2   . GLN A  1 687  ? -15.219 60.640  112.093 1.00 26.19 ? 685  GLN A NE2   1 
ATOM   4926  N N     . THR A  1 688  ? -15.276 62.215  117.906 1.00 21.45 ? 686  THR A N     1 
ATOM   4927  C CA    . THR A  1 688  ? -14.821 62.250  119.296 1.00 21.86 ? 686  THR A CA    1 
ATOM   4928  C C     . THR A  1 688  ? -14.738 60.842  119.877 1.00 22.30 ? 686  THR A C     1 
ATOM   4929  O O     . THR A  1 688  ? -13.749 60.480  120.536 1.00 22.38 ? 686  THR A O     1 
ATOM   4930  C CB    . THR A  1 688  ? -15.773 63.129  120.122 1.00 23.02 ? 686  THR A CB    1 
ATOM   4931  O OG1   . THR A  1 688  ? -15.661 64.494  119.700 1.00 22.44 ? 686  THR A OG1   1 
ATOM   4932  C CG2   . THR A  1 688  ? -15.447 63.058  121.596 1.00 22.52 ? 686  THR A CG2   1 
ATOM   4933  N N     . ARG A  1 689  ? -15.782 60.037  119.664 1.00 22.21 ? 687  ARG A N     1 
ATOM   4934  C CA    . ARG A  1 689  ? -15.774 58.659  120.146 1.00 23.89 ? 687  ARG A CA    1 
ATOM   4935  C C     . ARG A  1 689  ? -14.678 57.832  119.489 1.00 27.49 ? 687  ARG A C     1 
ATOM   4936  O O     . ARG A  1 689  ? -14.257 56.825  120.062 1.00 25.26 ? 687  ARG A O     1 
ATOM   4937  C CB    . ARG A  1 689  ? -17.130 57.990  119.912 1.00 25.61 ? 687  ARG A CB    1 
ATOM   4938  C CG    . ARG A  1 689  ? -18.262 58.496  120.820 1.00 24.56 ? 687  ARG A CG    1 
ATOM   4939  C CD    . ARG A  1 689  ? -19.503 57.636  120.657 1.00 25.95 ? 687  ARG A CD    1 
ATOM   4940  N NE    . ARG A  1 689  ? -20.037 57.748  119.303 1.00 28.52 ? 687  ARG A NE    1 
ATOM   4941  C CZ    . ARG A  1 689  ? -21.009 58.576  118.936 1.00 30.33 ? 687  ARG A CZ    1 
ATOM   4942  N NH1   . ARG A  1 689  ? -21.604 59.374  119.808 1.00 28.13 ? 687  ARG A NH1   1 
ATOM   4943  N NH2   . ARG A  1 689  ? -21.393 58.601  117.659 1.00 25.21 ? 687  ARG A NH2   1 
ATOM   4944  N N     . ARG A  1 690  ? -14.214 58.231  118.302 1.00 22.33 ? 688  ARG A N     1 
ATOM   4945  C CA    . ARG A  1 690  ? -13.129 57.516  117.643 1.00 24.25 ? 688  ARG A CA    1 
ATOM   4946  C C     . ARG A  1 690  ? -11.746 57.917  118.151 1.00 25.47 ? 688  ARG A C     1 
ATOM   4947  O O     . ARG A  1 690  ? -10.804 57.146  117.958 1.00 24.89 ? 688  ARG A O     1 
ATOM   4948  C CB    . ARG A  1 690  ? -13.172 57.738  116.124 1.00 24.15 ? 688  ARG A CB    1 
ATOM   4949  C CG    . ARG A  1 690  ? -14.374 57.132  115.401 1.00 27.58 ? 688  ARG A CG    1 
ATOM   4950  C CD    . ARG A  1 690  ? -14.313 55.602  115.347 1.00 31.48 ? 688  ARG A CD    1 
ATOM   4951  N NE    . ARG A  1 690  ? -13.160 55.120  114.590 1.00 30.67 ? 688  ARG A NE    1 
ATOM   4952  C CZ    . ARG A  1 690  ? -12.148 54.449  115.124 1.00 32.56 ? 688  ARG A CZ    1 
ATOM   4953  N NH1   . ARG A  1 690  ? -12.142 54.111  116.408 1.00 31.16 ? 688  ARG A NH1   1 
ATOM   4954  N NH2   . ARG A  1 690  ? -11.119 54.102  114.353 1.00 28.49 ? 688  ARG A NH2   1 
ATOM   4955  N N     . THR A  1 691  ? -11.590 59.096  118.801 1.00 22.05 ? 689  THR A N     1 
ATOM   4956  C CA    . THR A  1 691  ? -10.247 59.662  118.915 1.00 22.84 ? 689  THR A CA    1 
ATOM   4957  C C     . THR A  1 691  ? -9.881  60.188  120.294 1.00 28.30 ? 689  THR A C     1 
ATOM   4958  O O     . THR A  1 691  ? -8.744  59.990  120.720 1.00 25.79 ? 689  THR A O     1 
ATOM   4959  C CB    . THR A  1 691  ? -10.017 60.814  117.915 1.00 25.79 ? 689  THR A CB    1 
ATOM   4960  O OG1   . THR A  1 691  ? -11.014 61.824  118.096 1.00 24.18 ? 689  THR A OG1   1 
ATOM   4961  C CG2   . THR A  1 691  ? -10.035 60.319  116.458 1.00 22.72 ? 689  THR A CG2   1 
ATOM   4962  N N     . LEU A  1 692  ? -10.771 60.907  120.974 1.00 25.05 ? 690  LEU A N     1 
ATOM   4963  C CA    . LEU A  1 692  ? -10.314 61.754  122.075 1.00 23.44 ? 690  LEU A CA    1 
ATOM   4964  C C     . LEU A  1 692  ? -10.176 60.971  123.378 1.00 29.14 ? 690  LEU A C     1 
ATOM   4965  O O     . LEU A  1 692  ? -11.028 60.146  123.728 1.00 26.41 ? 690  LEU A O     1 
ATOM   4966  C CB    . LEU A  1 692  ? -11.245 62.951  122.266 1.00 27.94 ? 690  LEU A CB    1 
ATOM   4967  C CG    . LEU A  1 692  ? -11.259 63.916  121.071 1.00 26.47 ? 690  LEU A CG    1 
ATOM   4968  C CD1   . LEU A  1 692  ? -12.019 65.187  121.428 1.00 28.25 ? 690  LEU A CD1   1 
ATOM   4969  C CD2   . LEU A  1 692  ? -9.850  64.243  120.631 1.00 27.56 ? 690  LEU A CD2   1 
ATOM   4970  N N     . GLY A  1 693  ? -9.077  61.232  124.076 1.00 27.33 ? 691  GLY A N     1 
ATOM   4971  C CA    . GLY A  1 693  ? -8.802  60.646  125.370 1.00 29.23 ? 691  GLY A CA    1 
ATOM   4972  C C     . GLY A  1 693  ? -8.283  61.708  126.323 1.00 36.21 ? 691  GLY A C     1 
ATOM   4973  O O     . GLY A  1 693  ? -8.296  62.900  126.009 1.00 35.14 ? 691  GLY A O     1 
ATOM   4974  N N     . PRO A  1 694  ? -7.806  61.298  127.503 1.00 39.93 ? 692  PRO A N     1 
ATOM   4975  C CA    . PRO A  1 694  ? -7.358  62.298  128.489 1.00 39.71 ? 692  PRO A CA    1 
ATOM   4976  C C     . PRO A  1 694  ? -6.121  63.071  128.055 1.00 37.27 ? 692  PRO A C     1 
ATOM   4977  O O     . PRO A  1 694  ? -5.932  64.208  128.502 1.00 39.93 ? 692  PRO A O     1 
ATOM   4978  C CB    . PRO A  1 694  ? -7.079  61.460  129.748 1.00 42.39 ? 692  PRO A CB    1 
ATOM   4979  C CG    . PRO A  1 694  ? -7.788  60.146  129.531 1.00 44.15 ? 692  PRO A CG    1 
ATOM   4980  C CD    . PRO A  1 694  ? -7.766  59.926  128.037 1.00 41.89 ? 692  PRO A CD    1 
ATOM   4981  N N     . GLY A  1 695  ? -5.273  62.500  127.198 1.00 33.05 ? 693  GLY A N     1 
ATOM   4982  C CA    . GLY A  1 695  ? -4.072  63.183  126.755 1.00 30.75 ? 693  GLY A CA    1 
ATOM   4983  C C     . GLY A  1 695  ? -4.303  64.269  125.727 1.00 35.27 ? 693  GLY A C     1 
ATOM   4984  O O     . GLY A  1 695  ? -3.358  64.996  125.396 1.00 34.85 ? 693  GLY A O     1 
ATOM   4985  N N     . HIS A  1 696  ? -5.529  64.400  125.213 1.00 29.07 ? 694  HIS A N     1 
ATOM   4986  C CA    . HIS A  1 696  ? -5.833  65.415  124.210 1.00 31.24 ? 694  HIS A CA    1 
ATOM   4987  C C     . HIS A  1 696  ? -6.549  66.546  124.940 1.00 34.24 ? 694  HIS A C     1 
ATOM   4988  O O     . HIS A  1 696  ? -7.778  66.630  124.985 1.00 34.15 ? 694  HIS A O     1 
ATOM   4989  C CB    . HIS A  1 696  ? -6.656  64.817  123.073 1.00 30.60 ? 694  HIS A CB    1 
ATOM   4990  C CG    . HIS A  1 696  ? -6.099  63.525  122.546 1.00 30.29 ? 694  HIS A CG    1 
ATOM   4991  N ND1   . HIS A  1 696  ? -6.726  62.310  122.731 1.00 26.62 ? 694  HIS A ND1   1 
ATOM   4992  C CD2   . HIS A  1 696  ? -4.964  63.260  121.852 1.00 27.54 ? 694  HIS A CD2   1 
ATOM   4993  C CE1   . HIS A  1 696  ? -6.009  61.355  122.166 1.00 28.97 ? 694  HIS A CE1   1 
ATOM   4994  N NE2   . HIS A  1 696  ? -4.936  61.905  121.626 1.00 30.62 ? 694  HIS A NE2   1 
ATOM   4995  N N     . GLY A  1 697  ? -5.748  67.406  125.558 1.00 31.43 ? 695  GLY A N     1 
ATOM   4996  C CA    . GLY A  1 697  ? -6.267  68.453  126.399 1.00 30.34 ? 695  GLY A CA    1 
ATOM   4997  C C     . GLY A  1 697  ? -6.881  69.566  125.578 1.00 25.80 ? 695  GLY A C     1 
ATOM   4998  O O     . GLY A  1 697  ? -6.463  69.849  124.453 1.00 31.16 ? 695  GLY A O     1 
ATOM   4999  N N     . PRO A  1 698  ? -7.897  70.213  126.122 1.00 30.30 ? 696  PRO A N     1 
ATOM   5000  C CA    . PRO A  1 698  ? -8.513  71.335  125.411 1.00 27.88 ? 696  PRO A CA    1 
ATOM   5001  C C     . PRO A  1 698  ? -7.585  72.541  125.357 1.00 27.58 ? 696  PRO A C     1 
ATOM   5002  O O     . PRO A  1 698  ? -6.649  72.694  126.141 1.00 28.77 ? 696  PRO A O     1 
ATOM   5003  C CB    . PRO A  1 698  ? -9.768  71.636  126.240 1.00 29.68 ? 696  PRO A CB    1 
ATOM   5004  C CG    . PRO A  1 698  ? -10.018 70.373  127.014 1.00 35.71 ? 696  PRO A CG    1 
ATOM   5005  C CD    . PRO A  1 698  ? -8.649  69.847  127.331 1.00 32.69 ? 696  PRO A CD    1 
ATOM   5006  N N     . LEU A  1 699  ? -7.859  73.404  124.390 1.00 25.86 ? 697  LEU A N     1 
ATOM   5007  C CA    . LEU A  1 699  ? -7.156  74.677  124.311 1.00 23.97 ? 697  LEU A CA    1 
ATOM   5008  C C     . LEU A  1 699  ? -7.597  75.626  125.416 1.00 25.64 ? 697  LEU A C     1 
ATOM   5009  O O     . LEU A  1 699  ? -6.764  76.320  126.011 1.00 26.92 ? 697  LEU A O     1 
ATOM   5010  C CB    . LEU A  1 699  ? -7.403  75.320  122.945 1.00 26.51 ? 697  LEU A CB    1 
ATOM   5011  C CG    . LEU A  1 699  ? -6.972  74.555  121.706 1.00 27.40 ? 697  LEU A CG    1 
ATOM   5012  C CD1   . LEU A  1 699  ? -7.581  75.232  120.486 1.00 25.71 ? 697  LEU A CD1   1 
ATOM   5013  C CD2   . LEU A  1 699  ? -5.456  74.504  121.617 1.00 30.20 ? 697  LEU A CD2   1 
ATOM   5014  N N     . GLY A  1 700  ? -8.901  75.656  125.717 1.00 24.44 ? 698  GLY A N     1 
ATOM   5015  C CA    . GLY A  1 700  ? -9.481  76.656  126.589 1.00 24.82 ? 698  GLY A CA    1 
ATOM   5016  C C     . GLY A  1 700  ? -10.651 77.337  125.902 1.00 25.56 ? 698  GLY A C     1 
ATOM   5017  O O     . GLY A  1 700  ? -11.179 76.828  124.907 1.00 25.66 ? 698  GLY A O     1 
ATOM   5018  N N     . PRO A  1 701  ? -11.071 78.503  126.399 1.00 25.20 ? 699  PRO A N     1 
ATOM   5019  C CA    . PRO A  1 701  ? -12.206 79.204  125.772 1.00 24.76 ? 699  PRO A CA    1 
ATOM   5020  C C     . PRO A  1 701  ? -11.963 79.472  124.292 1.00 24.62 ? 699  PRO A C     1 
ATOM   5021  O O     . PRO A  1 701  ? -10.931 80.022  123.896 1.00 24.31 ? 699  PRO A O     1 
ATOM   5022  C CB    . PRO A  1 701  ? -12.304 80.505  126.574 1.00 25.24 ? 699  PRO A CB    1 
ATOM   5023  C CG    . PRO A  1 701  ? -11.717 80.152  127.936 1.00 26.11 ? 699  PRO A CG    1 
ATOM   5024  C CD    . PRO A  1 701  ? -10.598 79.188  127.618 1.00 26.15 ? 699  PRO A CD    1 
ATOM   5025  N N     . ILE A  1 702  ? -12.940 79.090  123.471 1.00 23.95 ? 700  ILE A N     1 
ATOM   5026  C CA    . ILE A  1 702  ? -12.870 79.252  122.026 1.00 23.52 ? 700  ILE A CA    1 
ATOM   5027  C C     . ILE A  1 702  ? -13.951 80.233  121.607 1.00 23.50 ? 700  ILE A C     1 
ATOM   5028  O O     . ILE A  1 702  ? -15.113 80.095  122.008 1.00 23.57 ? 700  ILE A O     1 
ATOM   5029  C CB    . ILE A  1 702  ? -13.023 77.904  121.292 1.00 23.10 ? 700  ILE A CB    1 
ATOM   5030  C CG1   . ILE A  1 702  ? -11.817 77.009  121.622 1.00 23.13 ? 700  ILE A CG1   1 
ATOM   5031  C CG2   . ILE A  1 702  ? -13.140 78.132  119.792 1.00 22.68 ? 700  ILE A CG2   1 
ATOM   5032  C CD1   . ILE A  1 702  ? -11.646 75.817  120.689 1.00 27.24 ? 700  ILE A CD1   1 
ATOM   5033  N N     . VAL A  1 703  ? -13.563 81.234  120.833 1.00 23.45 ? 701  VAL A N     1 
ATOM   5034  C CA    . VAL A  1 703  ? -14.509 82.196  120.295 1.00 23.42 ? 701  VAL A CA    1 
ATOM   5035  C C     . VAL A  1 703  ? -14.957 81.678  118.937 1.00 22.93 ? 701  VAL A C     1 
ATOM   5036  O O     . VAL A  1 703  ? -14.123 81.384  118.073 1.00 22.67 ? 701  VAL A O     1 
ATOM   5037  C CB    . VAL A  1 703  ? -13.873 83.590  120.177 1.00 23.68 ? 701  VAL A CB    1 
ATOM   5038  C CG1   . VAL A  1 703  ? -14.845 84.534  119.527 1.00 23.65 ? 701  VAL A CG1   1 
ATOM   5039  C CG2   . VAL A  1 703  ? -13.522 84.118  121.548 1.00 24.21 ? 701  VAL A CG2   1 
ATOM   5040  N N     . CYS A  1 704  ? -16.266 81.547  118.761 1.00 22.82 ? 702  CYS A N     1 
ATOM   5041  C CA    . CYS A  1 704  ? -16.852 81.038  117.534 1.00 22.37 ? 702  CYS A CA    1 
ATOM   5042  C C     . CYS A  1 704  ? -17.642 82.174  116.901 1.00 22.39 ? 702  CYS A C     1 
ATOM   5043  O O     . CYS A  1 704  ? -18.627 82.648  117.478 1.00 22.61 ? 702  CYS A O     1 
ATOM   5044  C CB    . CYS A  1 704  ? -17.736 79.819  117.803 1.00 22.23 ? 702  CYS A CB    1 
ATOM   5045  S SG    . CYS A  1 704  ? -16.851 78.377  118.467 1.00 23.42 ? 702  CYS A SG    1 
ATOM   5046  N N     . ILE A  1 705  ? -17.192 82.617  115.732 1.00 22.18 ? 703  ILE A N     1 
ATOM   5047  C CA    . ILE A  1 705  ? -17.793 83.734  115.023 1.00 22.20 ? 703  ILE A CA    1 
ATOM   5048  C C     . ILE A  1 705  ? -18.378 83.168  113.750 1.00 21.77 ? 703  ILE A C     1 
ATOM   5049  O O     . ILE A  1 705  ? -17.650 82.621  112.918 1.00 21.50 ? 703  ILE A O     1 
ATOM   5050  C CB    . ILE A  1 705  ? -16.782 84.846  114.716 1.00 22.91 ? 703  ILE A CB    1 
ATOM   5051  C CG1   . ILE A  1 705  ? -16.183 85.387  116.017 1.00 24.78 ? 703  ILE A CG1   1 
ATOM   5052  C CG2   . ILE A  1 705  ? -17.468 85.958  113.901 1.00 24.79 ? 703  ILE A CG2   1 
ATOM   5053  C CD1   . ILE A  1 705  ? -15.040 86.377  115.815 1.00 28.71 ? 703  ILE A CD1   1 
ATOM   5054  N N     . SER A  1 706  ? -19.678 83.280  113.612 1.00 21.73 ? 704  SER A N     1 
ATOM   5055  C CA    . SER A  1 706  ? -20.378 82.589  112.546 1.00 21.34 ? 704  SER A CA    1 
ATOM   5056  C C     . SER A  1 706  ? -21.034 83.588  111.606 1.00 21.95 ? 704  SER A C     1 
ATOM   5057  O O     . SER A  1 706  ? -21.282 84.744  111.976 1.00 22.25 ? 704  SER A O     1 
ATOM   5058  C CB    . SER A  1 706  ? -21.421 81.623  113.121 1.00 22.09 ? 704  SER A CB    1 
ATOM   5059  O OG    . SER A  1 706  ? -22.267 82.265  114.050 1.00 24.34 ? 704  SER A OG    1 
ATOM   5060  N N     . PRO A  1 707  ? -21.293 83.180  110.369 1.00 22.02 ? 705  PRO A N     1 
ATOM   5061  C CA    . PRO A  1 707  ? -21.855 84.081  109.359 1.00 23.83 ? 705  PRO A CA    1 
ATOM   5062  C C     . PRO A  1 707  ? -23.381 84.023  109.270 1.00 23.07 ? 705  PRO A C     1 
ATOM   5063  O O     . PRO A  1 707  ? -24.050 83.178  109.872 1.00 22.47 ? 705  PRO A O     1 
ATOM   5064  C CB    . PRO A  1 707  ? -21.219 83.552  108.069 1.00 23.13 ? 705  PRO A CB    1 
ATOM   5065  C CG    . PRO A  1 707  ? -21.203 82.074  108.296 1.00 21.52 ? 705  PRO A CG    1 
ATOM   5066  C CD    . PRO A  1 707  ? -20.892 81.888  109.785 1.00 22.13 ? 705  PRO A CD    1 
ATOM   5067  N N     . TRP A  1 708  ? -23.929 84.951  108.488 1.00 23.72 ? 706  TRP A N     1 
ATOM   5068  C CA    . TRP A  1 708  ? -25.376 85.068  108.344 1.00 22.92 ? 706  TRP A CA    1 
ATOM   5069  C C     . TRP A  1 708  ? -25.933 84.176  107.247 1.00 22.19 ? 706  TRP A C     1 
ATOM   5070  O O     . TRP A  1 708  ? -27.153 83.986  107.188 1.00 22.39 ? 706  TRP A O     1 
ATOM   5071  C CB    . TRP A  1 708  ? -25.772 86.529  108.058 1.00 24.40 ? 706  TRP A CB    1 
ATOM   5072  C CG    . TRP A  1 708  ? -24.944 87.142  106.975 1.00 26.32 ? 706  TRP A CG    1 
ATOM   5073  C CD1   . TRP A  1 708  ? -23.861 87.958  107.129 1.00 28.56 ? 706  TRP A CD1   1 
ATOM   5074  C CD2   . TRP A  1 708  ? -25.107 86.954  105.570 1.00 21.41 ? 706  TRP A CD2   1 
ATOM   5075  N NE1   . TRP A  1 708  ? -23.353 88.310  105.901 1.00 28.25 ? 706  TRP A NE1   1 
ATOM   5076  C CE2   . TRP A  1 708  ? -24.103 87.706  104.927 1.00 25.18 ? 706  TRP A CE2   1 
ATOM   5077  C CE3   . TRP A  1 708  ? -26.028 86.245  104.788 1.00 25.63 ? 706  TRP A CE3   1 
ATOM   5078  C CZ2   . TRP A  1 708  ? -23.968 87.741  103.541 1.00 23.58 ? 706  TRP A CZ2   1 
ATOM   5079  C CZ3   . TRP A  1 708  ? -25.898 86.286  103.411 1.00 24.84 ? 706  TRP A CZ3   1 
ATOM   5080  C CH2   . TRP A  1 708  ? -24.876 87.031  102.801 1.00 29.83 ? 706  TRP A CH2   1 
ATOM   5081  N N     . ASN A  1 709  ? -25.076 83.632  106.379 1.00 22.72 ? 707  ASN A N     1 
ATOM   5082  C CA    . ASN A  1 709  ? -25.549 82.858  105.234 1.00 23.02 ? 707  ASN A CA    1 
ATOM   5083  C C     . ASN A  1 709  ? -25.801 81.394  105.558 1.00 25.81 ? 707  ASN A C     1 
ATOM   5084  O O     . ASN A  1 709  ? -26.556 80.732  104.832 1.00 24.02 ? 707  ASN A O     1 
ATOM   5085  C CB    . ASN A  1 709  ? -24.557 82.962  104.063 1.00 23.23 ? 707  ASN A CB    1 
ATOM   5086  C CG    . ASN A  1 709  ? -23.204 82.304  104.349 1.00 26.18 ? 707  ASN A CG    1 
ATOM   5087  O OD1   . ASN A  1 709  ? -22.760 82.199  105.497 1.00 28.92 ? 707  ASN A OD1   1 
ATOM   5088  N ND2   . ASN A  1 709  ? -22.537 81.864  103.287 1.00 25.30 ? 707  ASN A ND2   1 
ATOM   5089  N N     . PHE A  1 710  ? -25.177 80.866  106.608 1.00 22.25 ? 708  PHE A N     1 
ATOM   5090  C CA    . PHE A  1 710  ? -25.529 79.564  107.173 1.00 22.81 ? 708  PHE A CA    1 
ATOM   5091  C C     . PHE A  1 710  ? -25.681 79.752  108.674 1.00 25.37 ? 708  PHE A C     1 
ATOM   5092  O O     . PHE A  1 710  ? -24.841 79.305  109.469 1.00 22.59 ? 708  PHE A O     1 
ATOM   5093  C CB    . PHE A  1 710  ? -24.496 78.494  106.825 1.00 25.61 ? 708  PHE A CB    1 
ATOM   5094  C CG    . PHE A  1 710  ? -24.500 78.124  105.368 1.00 25.61 ? 708  PHE A CG    1 
ATOM   5095  C CD1   . PHE A  1 710  ? -25.441 77.241  104.872 1.00 31.09 ? 708  PHE A CD1   1 
ATOM   5096  C CD2   . PHE A  1 710  ? -23.581 78.683  104.493 1.00 33.63 ? 708  PHE A CD2   1 
ATOM   5097  C CE1   . PHE A  1 710  ? -25.462 76.904  103.522 1.00 32.13 ? 708  PHE A CE1   1 
ATOM   5098  C CE2   . PHE A  1 710  ? -23.589 78.346  103.136 1.00 34.15 ? 708  PHE A CE2   1 
ATOM   5099  C CZ    . PHE A  1 710  ? -24.530 77.462  102.658 1.00 34.55 ? 708  PHE A CZ    1 
ATOM   5100  N N     . PRO A  1 711  ? -26.761 80.420  109.090 1.00 24.42 ? 709  PRO A N     1 
ATOM   5101  C CA    . PRO A  1 711  ? -26.864 80.901  110.468 1.00 23.79 ? 709  PRO A CA    1 
ATOM   5102  C C     . PRO A  1 711  ? -27.196 79.830  111.486 1.00 22.54 ? 709  PRO A C     1 
ATOM   5103  O O     . PRO A  1 711  ? -27.137 80.115  112.691 1.00 22.05 ? 709  PRO A O     1 
ATOM   5104  C CB    . PRO A  1 711  ? -27.988 81.934  110.379 1.00 24.65 ? 709  PRO A CB    1 
ATOM   5105  C CG    . PRO A  1 711  ? -28.887 81.373  109.318 1.00 21.33 ? 709  PRO A CG    1 
ATOM   5106  C CD    . PRO A  1 711  ? -27.940 80.804  108.284 1.00 23.91 ? 709  PRO A CD    1 
ATOM   5107  N N     . LEU A  1 712  ? -27.540 78.622  111.059 1.00 23.88 ? 710  LEU A N     1 
ATOM   5108  C CA    . LEU A  1 712  ? -27.635 77.489  111.972 1.00 20.48 ? 710  LEU A CA    1 
ATOM   5109  C C     . LEU A  1 712  ? -26.530 76.466  111.761 1.00 22.00 ? 710  LEU A C     1 
ATOM   5110  O O     . LEU A  1 712  ? -25.936 76.003  112.734 1.00 21.37 ? 710  LEU A O     1 
ATOM   5111  C CB    . LEU A  1 712  ? -28.992 76.793  111.833 1.00 20.48 ? 710  LEU A CB    1 
ATOM   5112  C CG    . LEU A  1 712  ? -29.232 75.599  112.768 1.00 24.37 ? 710  LEU A CG    1 
ATOM   5113  C CD1   . LEU A  1 712  ? -29.187 76.062  114.215 1.00 20.95 ? 710  LEU A CD1   1 
ATOM   5114  C CD2   . LEU A  1 712  ? -30.557 74.947  112.482 1.00 25.13 ? 710  LEU A CD2   1 
ATOM   5115  N N     . ALA A  1 713  ? -26.218 76.143  110.505 1.00 20.05 ? 711  ALA A N     1 
ATOM   5116  C CA    . ALA A  1 713  ? -25.343 75.012  110.218 1.00 21.47 ? 711  ALA A CA    1 
ATOM   5117  C C     . ALA A  1 713  ? -23.895 75.327  110.580 1.00 20.77 ? 711  ALA A C     1 
ATOM   5118  O O     . ALA A  1 713  ? -23.250 74.565  111.307 1.00 23.28 ? 711  ALA A O     1 
ATOM   5119  C CB    . ALA A  1 713  ? -25.458 74.620  108.747 1.00 22.50 ? 711  ALA A CB    1 
ATOM   5120  N N     . ILE A  1 714  ? -23.357 76.437  110.065 1.00 21.18 ? 712  ILE A N     1 
ATOM   5121  C CA    . ILE A  1 714  ? -21.965 76.764  110.373 1.00 19.96 ? 712  ILE A CA    1 
ATOM   5122  C C     . ILE A  1 714  ? -21.839 77.203  111.825 1.00 22.13 ? 712  ILE A C     1 
ATOM   5123  O O     . ILE A  1 714  ? -20.856 76.877  112.505 1.00 21.88 ? 712  ILE A O     1 
ATOM   5124  C CB    . ILE A  1 714  ? -21.421 77.820  109.395 1.00 22.01 ? 712  ILE A CB    1 
ATOM   5125  C CG1   . ILE A  1 714  ? -21.287 77.193  108.005 1.00 26.68 ? 712  ILE A CG1   1 
ATOM   5126  C CG2   . ILE A  1 714  ? -20.055 78.354  109.884 1.00 20.19 ? 712  ILE A CG2   1 
ATOM   5127  C CD1   . ILE A  1 714  ? -20.668 78.112  106.957 1.00 32.61 ? 712  ILE A CD1   1 
ATOM   5128  N N     . PHE A  1 715  ? -22.838 77.938  112.319 1.00 21.42 ? 713  PHE A N     1 
ATOM   5129  C CA    . PHE A  1 715  ? -22.965 78.232  113.742 1.00 24.28 ? 713  PHE A CA    1 
ATOM   5130  C C     . PHE A  1 715  ? -22.803 76.964  114.581 1.00 21.48 ? 713  PHE A C     1 
ATOM   5131  O O     . PHE A  1 715  ? -21.934 76.881  115.457 1.00 21.47 ? 713  PHE A O     1 
ATOM   5132  C CB    . PHE A  1 715  ? -24.329 78.883  114.002 1.00 21.82 ? 713  PHE A CB    1 
ATOM   5133  C CG    . PHE A  1 715  ? -24.596 79.178  115.451 1.00 23.93 ? 713  PHE A CG    1 
ATOM   5134  C CD1   . PHE A  1 715  ? -24.096 80.329  116.040 1.00 24.25 ? 713  PHE A CD1   1 
ATOM   5135  C CD2   . PHE A  1 715  ? -25.352 78.309  116.222 1.00 25.56 ? 713  PHE A CD2   1 
ATOM   5136  C CE1   . PHE A  1 715  ? -24.340 80.608  117.390 1.00 26.20 ? 713  PHE A CE1   1 
ATOM   5137  C CE2   . PHE A  1 715  ? -25.603 78.576  117.569 1.00 25.83 ? 713  PHE A CE2   1 
ATOM   5138  C CZ    . PHE A  1 715  ? -25.104 79.727  118.150 1.00 22.89 ? 713  PHE A CZ    1 
ATOM   5139  N N     . THR A  1 716  ? -23.636 75.960  114.304 1.00 21.16 ? 714  THR A N     1 
ATOM   5140  C CA    . THR A  1 716  ? -23.617 74.716  115.073 1.00 21.23 ? 714  THR A CA    1 
ATOM   5141  C C     . THR A  1 716  ? -22.311 73.951  114.899 1.00 20.94 ? 714  THR A C     1 
ATOM   5142  O O     . THR A  1 716  ? -21.780 73.373  115.860 1.00 22.38 ? 714  THR A O     1 
ATOM   5143  C CB    . THR A  1 716  ? -24.782 73.842  114.633 1.00 22.15 ? 714  THR A CB    1 
ATOM   5144  O OG1   . THR A  1 716  ? -26.013 74.552  114.851 1.00 20.86 ? 714  THR A OG1   1 
ATOM   5145  C CG2   . THR A  1 716  ? -24.777 72.514  115.411 1.00 20.82 ? 714  THR A CG2   1 
ATOM   5146  N N     . GLY A  1 717  ? -21.819 73.873  113.666 1.00 20.42 ? 715  GLY A N     1 
ATOM   5147  C CA    . GLY A  1 717  ? -20.621 73.098  113.403 1.00 21.94 ? 715  GLY A CA    1 
ATOM   5148  C C     . GLY A  1 717  ? -19.432 73.580  114.210 1.00 20.54 ? 715  GLY A C     1 
ATOM   5149  O O     . GLY A  1 717  ? -18.782 72.795  114.903 1.00 20.79 ? 715  GLY A O     1 
ATOM   5150  N N     . GLN A  1 718  ? -19.139 74.882  114.144 1.00 20.64 ? 716  GLN A N     1 
ATOM   5151  C CA    . GLN A  1 718  ? -17.992 75.401  114.899 1.00 20.90 ? 716  GLN A CA    1 
ATOM   5152  C C     . GLN A  1 718  ? -18.174 75.156  116.384 1.00 22.61 ? 716  GLN A C     1 
ATOM   5153  O O     . GLN A  1 718  ? -17.253 74.702  117.078 1.00 21.41 ? 716  GLN A O     1 
ATOM   5154  C CB    . GLN A  1 718  ? -17.801 76.899  114.631 1.00 21.00 ? 716  GLN A CB    1 
ATOM   5155  C CG    . GLN A  1 718  ? -17.471 77.201  113.173 1.00 23.20 ? 716  GLN A CG    1 
ATOM   5156  C CD    . GLN A  1 718  ? -17.270 78.684  112.908 1.00 22.45 ? 716  GLN A CD    1 
ATOM   5157  O OE1   . GLN A  1 718  ? -16.428 79.061  112.094 1.00 22.85 ? 716  GLN A OE1   1 
ATOM   5158  N NE2   . GLN A  1 718  ? -18.029 79.531  113.602 1.00 21.11 ? 716  GLN A NE2   1 
ATOM   5159  N N     . ILE A  1 719  ? -19.365 75.460  116.893 1.00 21.41 ? 717  ILE A N     1 
ATOM   5160  C CA    . ILE A  1 719  ? -19.603 75.365  118.328 1.00 23.33 ? 717  ILE A CA    1 
ATOM   5161  C C     . ILE A  1 719  ? -19.495 73.919  118.788 1.00 21.81 ? 717  ILE A C     1 
ATOM   5162  O O     . ILE A  1 719  ? -18.853 73.613  119.800 1.00 22.09 ? 717  ILE A O     1 
ATOM   5163  C CB    . ILE A  1 719  ? -20.974 75.974  118.664 1.00 25.30 ? 717  ILE A CB    1 
ATOM   5164  C CG1   . ILE A  1 719  ? -20.917 77.486  118.473 1.00 27.43 ? 717  ILE A CG1   1 
ATOM   5165  C CG2   . ILE A  1 719  ? -21.415 75.602  120.071 1.00 29.49 ? 717  ILE A CG2   1 
ATOM   5166  C CD1   . ILE A  1 719  ? -22.234 78.119  118.617 1.00 32.25 ? 717  ILE A CD1   1 
ATOM   5167  N N     . ALA A  1 720  ? -20.128 73.009  118.051 1.00 21.53 ? 718  ALA A N     1 
ATOM   5168  C CA    . ALA A  1 720  ? -20.138 71.600  118.430 1.00 21.55 ? 718  ALA A CA    1 
ATOM   5169  C C     . ALA A  1 720  ? -18.731 71.029  118.454 1.00 21.53 ? 718  ALA A C     1 
ATOM   5170  O O     . ALA A  1 720  ? -18.366 70.282  119.370 1.00 22.55 ? 718  ALA A O     1 
ATOM   5171  C CB    . ALA A  1 720  ? -21.019 70.814  117.446 1.00 21.23 ? 718  ALA A CB    1 
ATOM   5172  N N     . ALA A  1 721  ? -17.921 71.365  117.447 1.00 21.26 ? 719  ALA A N     1 
ATOM   5173  C CA    . ALA A  1 721  ? -16.543 70.887  117.423 1.00 21.25 ? 719  ALA A CA    1 
ATOM   5174  C C     . ALA A  1 721  ? -15.774 71.387  118.639 1.00 21.63 ? 719  ALA A C     1 
ATOM   5175  O O     . ALA A  1 721  ? -15.135 70.600  119.347 1.00 21.95 ? 719  ALA A O     1 
ATOM   5176  C CB    . ALA A  1 721  ? -15.843 71.322  116.137 1.00 20.95 ? 719  ALA A CB    1 
ATOM   5177  N N     . ALA A  1 722  ? -15.824 72.694  118.899 1.00 21.79 ? 720  ALA A N     1 
ATOM   5178  C CA    . ALA A  1 722  ? -15.099 73.237  120.047 1.00 22.18 ? 720  ALA A CA    1 
ATOM   5179  C C     . ALA A  1 722  ? -15.596 72.625  121.354 1.00 23.77 ? 720  ALA A C     1 
ATOM   5180  O O     . ALA A  1 722  ? -14.794 72.251  122.222 1.00 22.79 ? 720  ALA A O     1 
ATOM   5181  C CB    . ALA A  1 722  ? -15.236 74.758  120.091 1.00 22.32 ? 720  ALA A CB    1 
ATOM   5182  N N     . LEU A  1 723  ? -16.922 72.541  121.520 1.00 22.55 ? 721  LEU A N     1 
ATOM   5183  C CA    . LEU A  1 723  ? -17.490 71.985  122.749 1.00 22.92 ? 721  LEU A CA    1 
ATOM   5184  C C     . LEU A  1 723  ? -17.056 70.541  122.953 1.00 24.20 ? 721  LEU A C     1 
ATOM   5185  O O     . LEU A  1 723  ? -16.624 70.155  124.045 1.00 25.76 ? 721  LEU A O     1 
ATOM   5186  C CB    . LEU A  1 723  ? -19.013 72.056  122.706 1.00 22.91 ? 721  LEU A CB    1 
ATOM   5187  C CG    . LEU A  1 723  ? -19.697 73.401  122.914 1.00 23.48 ? 721  LEU A CG    1 
ATOM   5188  C CD1   . LEU A  1 723  ? -21.190 73.216  122.729 1.00 25.14 ? 721  LEU A CD1   1 
ATOM   5189  C CD2   . LEU A  1 723  ? -19.373 73.902  124.324 1.00 23.59 ? 721  LEU A CD2   1 
ATOM   5190  N N     . VAL A  1 724  ? -17.187 69.714  121.912 1.00 22.54 ? 722  VAL A N     1 
ATOM   5191  C CA    . VAL A  1 724  ? -16.906 68.298  122.102 1.00 22.58 ? 722  VAL A CA    1 
ATOM   5192  C C     . VAL A  1 724  ? -15.411 68.043  122.281 1.00 22.68 ? 722  VAL A C     1 
ATOM   5193  O O     . VAL A  1 724  ? -15.025 67.069  122.944 1.00 25.64 ? 722  VAL A O     1 
ATOM   5194  C CB    . VAL A  1 724  ? -17.520 67.493  120.941 1.00 22.20 ? 722  VAL A CB    1 
ATOM   5195  C CG1   . VAL A  1 724  ? -16.591 67.476  119.725 1.00 22.51 ? 722  VAL A CG1   1 
ATOM   5196  C CG2   . VAL A  1 724  ? -17.902 66.081  121.414 1.00 24.83 ? 722  VAL A CG2   1 
ATOM   5197  N N     . ALA A  1 725  ? -14.549 68.922  121.761 1.00 24.06 ? 723  ALA A N     1 
ATOM   5198  C CA    . ALA A  1 725  ? -13.116 68.816  122.031 1.00 25.11 ? 723  ALA A CA    1 
ATOM   5199  C C     . ALA A  1 725  ? -12.760 69.179  123.468 1.00 27.74 ? 723  ALA A C     1 
ATOM   5200  O O     . ALA A  1 725  ? -11.578 69.092  123.835 1.00 23.79 ? 723  ALA A O     1 
ATOM   5201  C CB    . ALA A  1 725  ? -12.326 69.700  121.057 1.00 25.19 ? 723  ALA A CB    1 
ATOM   5202  N N     . GLY A  1 726  ? -13.739 69.558  124.286 1.00 23.37 ? 724  GLY A N     1 
ATOM   5203  C CA    . GLY A  1 726  ? -13.512 69.888  125.678 1.00 23.87 ? 724  GLY A CA    1 
ATOM   5204  C C     . GLY A  1 726  ? -13.342 71.360  125.982 1.00 24.94 ? 724  GLY A C     1 
ATOM   5205  O O     . GLY A  1 726  ? -12.880 71.698  127.081 1.00 26.00 ? 724  GLY A O     1 
ATOM   5206  N N     . ASN A  1 727  ? -13.692 72.245  125.049 1.00 25.44 ? 725  ASN A N     1 
ATOM   5207  C CA    . ASN A  1 727  ? -13.492 73.675  125.228 1.00 25.88 ? 725  ASN A CA    1 
ATOM   5208  C C     . ASN A  1 727  ? -14.812 74.368  125.529 1.00 24.76 ? 725  ASN A C     1 
ATOM   5209  O O     . ASN A  1 727  ? -15.830 74.072  124.893 1.00 23.80 ? 725  ASN A O     1 
ATOM   5210  C CB    . ASN A  1 727  ? -12.896 74.313  123.970 1.00 25.41 ? 725  ASN A CB    1 
ATOM   5211  C CG    . ASN A  1 727  ? -11.631 73.627  123.498 1.00 27.83 ? 725  ASN A CG    1 
ATOM   5212  O OD1   . ASN A  1 727  ? -10.554 73.840  124.056 1.00 24.57 ? 725  ASN A OD1   1 
ATOM   5213  N ND2   . ASN A  1 727  ? -11.748 72.821  122.440 1.00 22.99 ? 725  ASN A ND2   1 
ATOM   5214  N N     . PRO A  1 728  ? -14.866 75.320  126.445 1.00 24.47 ? 726  PRO A N     1 
ATOM   5215  C CA    . PRO A  1 728  ? -16.062 76.167  126.528 1.00 24.58 ? 726  PRO A CA    1 
ATOM   5216  C C     . PRO A  1 728  ? -16.031 77.196  125.412 1.00 24.29 ? 726  PRO A C     1 
ATOM   5217  O O     . PRO A  1 728  ? -14.970 77.542  124.885 1.00 25.29 ? 726  PRO A O     1 
ATOM   5218  C CB    . PRO A  1 728  ? -15.952 76.816  127.916 1.00 25.17 ? 726  PRO A CB    1 
ATOM   5219  C CG    . PRO A  1 728  ? -14.499 76.824  128.206 1.00 25.29 ? 726  PRO A CG    1 
ATOM   5220  C CD    . PRO A  1 728  ? -13.863 75.653  127.477 1.00 24.90 ? 726  PRO A CD    1 
ATOM   5221  N N     . VAL A  1 729  ? -17.221 77.660  125.029 1.00 24.21 ? 727  VAL A N     1 
ATOM   5222  C CA    . VAL A  1 729  ? -17.415 78.402  123.787 1.00 23.88 ? 727  VAL A CA    1 
ATOM   5223  C C     . VAL A  1 729  ? -18.074 79.744  124.071 1.00 24.16 ? 727  VAL A C     1 
ATOM   5224  O O     . VAL A  1 729  ? -19.010 79.842  124.874 1.00 24.46 ? 727  VAL A O     1 
ATOM   5225  C CB    . VAL A  1 729  ? -18.265 77.595  122.777 1.00 23.43 ? 727  VAL A CB    1 
ATOM   5226  C CG1   . VAL A  1 729  ? -18.732 78.483  121.622 1.00 23.17 ? 727  VAL A CG1   1 
ATOM   5227  C CG2   . VAL A  1 729  ? -17.488 76.411  122.260 1.00 23.13 ? 727  VAL A CG2   1 
ATOM   5228  N N     . LEU A  1 730  ? -17.582 80.778  123.404 1.00 24.10 ? 728  LEU A N     1 
ATOM   5229  C CA    . LEU A  1 730  ? -18.257 82.066  123.318 1.00 24.28 ? 728  LEU A CA    1 
ATOM   5230  C C     . LEU A  1 730  ? -18.785 82.136  121.897 1.00 23.83 ? 728  LEU A C     1 
ATOM   5231  O O     . LEU A  1 730  ? -17.992 82.199  120.954 1.00 23.65 ? 728  LEU A O     1 
ATOM   5232  C CB    . LEU A  1 730  ? -17.323 83.238  123.590 1.00 24.60 ? 728  LEU A CB    1 
ATOM   5233  C CG    . LEU A  1 730  ? -16.602 83.325  124.948 1.00 25.08 ? 728  LEU A CG    1 
ATOM   5234  C CD1   . LEU A  1 730  ? -17.596 82.989  126.069 1.00 26.49 ? 728  LEU A CD1   1 
ATOM   5235  C CD2   . LEU A  1 730  ? -15.378 82.419  124.984 1.00 24.94 ? 728  LEU A CD2   1 
ATOM   5236  N N     . ALA A  1 731  ? -20.105 82.104  121.748 1.00 24.69 ? 729  ALA A N     1 
ATOM   5237  C CA    . ALA A  1 731  ? -20.745 82.024  120.436 1.00 23.35 ? 729  ALA A CA    1 
ATOM   5238  C C     . ALA A  1 731  ? -21.221 83.411  120.036 1.00 23.66 ? 729  ALA A C     1 
ATOM   5239  O O     . ALA A  1 731  ? -22.181 83.937  120.619 1.00 25.89 ? 729  ALA A O     1 
ATOM   5240  C CB    . ALA A  1 731  ? -21.912 81.041  120.451 1.00 23.20 ? 729  ALA A CB    1 
ATOM   5241  N N     . LYS A  1 732  ? -20.569 83.989  119.022 1.00 24.91 ? 730  LYS A N     1 
ATOM   5242  C CA    . LYS A  1 732  ? -20.938 85.300  118.498 1.00 23.42 ? 730  LYS A CA    1 
ATOM   5243  C C     . LYS A  1 732  ? -21.570 85.096  117.128 1.00 22.99 ? 730  LYS A C     1 
ATOM   5244  O O     . LYS A  1 732  ? -20.846 84.877  116.148 1.00 22.68 ? 730  LYS A O     1 
ATOM   5245  C CB    . LYS A  1 732  ? -19.714 86.213  118.390 1.00 25.51 ? 730  LYS A CB    1 
ATOM   5246  C CG    . LYS A  1 732  ? -19.975 87.688  118.669 1.00 27.53 ? 730  LYS A CG    1 
ATOM   5247  C CD    . LYS A  1 732  ? -21.004 88.283  117.703 1.00 30.96 ? 730  LYS A CD    1 
ATOM   5248  C CE    . LYS A  1 732  ? -20.405 88.516  116.335 1.00 30.07 ? 730  LYS A CE    1 
ATOM   5249  N NZ    . LYS A  1 732  ? -21.338 89.285  115.460 1.00 31.41 ? 730  LYS A NZ    1 
ATOM   5250  N N     . PRO A  1 733  ? -22.893 85.145  117.012 1.00 22.98 ? 731  PRO A N     1 
ATOM   5251  C CA    . PRO A  1 733  ? -23.537 84.998  115.703 1.00 22.60 ? 731  PRO A CA    1 
ATOM   5252  C C     . PRO A  1 733  ? -23.519 86.303  114.922 1.00 23.82 ? 731  PRO A C     1 
ATOM   5253  O O     . PRO A  1 733  ? -23.320 87.385  115.472 1.00 26.35 ? 731  PRO A O     1 
ATOM   5254  C CB    . PRO A  1 733  ? -24.971 84.597  116.063 1.00 22.63 ? 731  PRO A CB    1 
ATOM   5255  C CG    . PRO A  1 733  ? -25.223 85.229  117.375 1.00 24.54 ? 731  PRO A CG    1 
ATOM   5256  C CD    . PRO A  1 733  ? -23.878 85.331  118.094 1.00 23.34 ? 731  PRO A CD    1 
ATOM   5257  N N     . ALA A  1 734  ? -23.728 86.182  113.609 1.00 22.33 ? 732  ALA A N     1 
ATOM   5258  C CA    . ALA A  1 734  ? -23.819 87.372  112.774 1.00 24.59 ? 732  ALA A CA    1 
ATOM   5259  C C     . ALA A  1 734  ? -24.907 88.308  113.292 1.00 22.77 ? 732  ALA A C     1 
ATOM   5260  O O     . ALA A  1 734  ? -25.937 87.872  113.810 1.00 24.50 ? 732  ALA A O     1 
ATOM   5261  C CB    . ALA A  1 734  ? -24.115 86.990  111.325 1.00 23.83 ? 732  ALA A CB    1 
ATOM   5262  N N     . GLU A  1 735  ? -24.673 89.615  113.127 1.00 23.07 ? 733  GLU A N     1 
ATOM   5263  C CA    . GLU A  1 735  ? -25.631 90.609  113.592 1.00 26.93 ? 733  GLU A CA    1 
ATOM   5264  C C     . GLU A  1 735  ? -26.993 90.427  112.932 1.00 26.31 ? 733  GLU A C     1 
ATOM   5265  O O     . GLU A  1 735  ? -28.024 90.702  113.550 1.00 23.54 ? 733  GLU A O     1 
ATOM   5266  C CB    . GLU A  1 735  ? -25.096 92.009  113.305 1.00 29.32 ? 733  GLU A CB    1 
ATOM   5267  C CG    . GLU A  1 735  ? -25.805 93.109  114.065 1.00 40.93 ? 733  GLU A CG    1 
ATOM   5268  C CD    . GLU A  1 735  ? -25.281 94.490  113.709 1.00 44.10 ? 733  GLU A CD    1 
ATOM   5269  O OE1   . GLU A  1 735  ? -24.255 94.564  112.993 1.00 49.73 ? 733  GLU A OE1   1 
ATOM   5270  O OE2   . GLU A  1 735  ? -25.899 95.492  114.137 1.00 52.28 ? 733  GLU A OE2   1 
ATOM   5271  N N     . GLU A  1 736  ? -27.006 89.932  111.693 1.00 26.82 ? 734  GLU A N     1 
ATOM   5272  C CA    . GLU A  1 736  ? -28.223 89.800  110.902 1.00 26.17 ? 734  GLU A CA    1 
ATOM   5273  C C     . GLU A  1 736  ? -29.100 88.622  111.329 1.00 28.18 ? 734  GLU A C     1 
ATOM   5274  O O     . GLU A  1 736  ? -30.321 88.659  111.098 1.00 24.53 ? 734  GLU A O     1 
ATOM   5275  C CB    . GLU A  1 736  ? -27.851 89.645  109.424 1.00 25.06 ? 734  GLU A CB    1 
ATOM   5276  C CG    . GLU A  1 736  ? -27.130 90.839  108.809 1.00 30.31 ? 734  GLU A CG    1 
ATOM   5277  C CD    . GLU A  1 736  ? -25.601 90.800  108.942 1.00 34.40 ? 734  GLU A CD    1 
ATOM   5278  O OE1   . GLU A  1 736  ? -25.059 89.960  109.693 1.00 28.14 ? 734  GLU A OE1   1 
ATOM   5279  O OE2   . GLU A  1 736  ? -24.936 91.620  108.271 1.00 38.92 ? 734  GLU A OE2   1 
ATOM   5280  N N     . THR A  1 737  ? -28.512 87.568  111.937 1.00 22.96 ? 735  THR A N     1 
ATOM   5281  C CA    . THR A  1 737  ? -29.218 86.296  112.161 1.00 23.41 ? 735  THR A CA    1 
ATOM   5282  C C     . THR A  1 737  ? -29.069 85.777  113.596 1.00 22.68 ? 735  THR A C     1 
ATOM   5283  O O     . THR A  1 737  ? -28.734 84.614  113.812 1.00 23.68 ? 735  THR A O     1 
ATOM   5284  C CB    . THR A  1 737  ? -28.735 85.229  111.172 1.00 22.48 ? 735  THR A CB    1 
ATOM   5285  O OG1   . THR A  1 737  ? -27.303 85.092  111.233 1.00 22.80 ? 735  THR A OG1   1 
ATOM   5286  C CG2   . THR A  1 737  ? -29.124 85.571  109.755 1.00 23.29 ? 735  THR A CG2   1 
ATOM   5287  N N     . PRO A  1 738  ? -29.359 86.604  114.606 1.00 22.82 ? 736  PRO A N     1 
ATOM   5288  C CA    . PRO A  1 738  ? -29.208 86.137  115.999 1.00 24.85 ? 736  PRO A CA    1 
ATOM   5289  C C     . PRO A  1 738  ? -30.272 85.145  116.467 1.00 25.61 ? 736  PRO A C     1 
ATOM   5290  O O     . PRO A  1 738  ? -30.001 84.384  117.404 1.00 23.87 ? 736  PRO A O     1 
ATOM   5291  C CB    . PRO A  1 738  ? -29.297 87.437  116.806 1.00 23.62 ? 736  PRO A CB    1 
ATOM   5292  C CG    . PRO A  1 738  ? -30.235 88.290  115.979 1.00 23.63 ? 736  PRO A CG    1 
ATOM   5293  C CD    . PRO A  1 738  ? -29.852 87.994  114.551 1.00 25.12 ? 736  PRO A CD    1 
ATOM   5294  N N     . LEU A  1 739  ? -31.470 85.126  115.869 1.00 22.95 ? 737  LEU A N     1 
ATOM   5295  C CA    . LEU A  1 739  ? -32.560 84.367  116.476 1.00 23.78 ? 737  LEU A CA    1 
ATOM   5296  C C     . LEU A  1 739  ? -32.357 82.866  116.327 1.00 22.69 ? 737  LEU A C     1 
ATOM   5297  O O     . LEU A  1 739  ? -32.564 82.115  117.284 1.00 22.86 ? 737  LEU A O     1 
ATOM   5298  C CB    . LEU A  1 739  ? -33.905 84.784  115.873 1.00 23.62 ? 737  LEU A CB    1 
ATOM   5299  C CG    . LEU A  1 739  ? -34.203 86.283  115.954 1.00 23.83 ? 737  LEU A CG    1 
ATOM   5300  C CD1   . LEU A  1 739  ? -35.434 86.610  115.131 1.00 25.60 ? 737  LEU A CD1   1 
ATOM   5301  C CD2   . LEU A  1 739  ? -34.381 86.747  117.395 1.00 24.98 ? 737  LEU A CD2   1 
ATOM   5302  N N     . ILE A  1 740  ? -31.970 82.403  115.137 1.00 23.70 ? 738  ILE A N     1 
ATOM   5303  C CA    . ILE A  1 740  ? -31.715 80.974  114.989 1.00 21.95 ? 738  ILE A CA    1 
ATOM   5304  C C     . ILE A  1 740  ? -30.491 80.562  115.813 1.00 22.04 ? 738  ILE A C     1 
ATOM   5305  O O     . ILE A  1 740  ? -30.432 79.440  116.319 1.00 24.56 ? 738  ILE A O     1 
ATOM   5306  C CB    . ILE A  1 740  ? -31.587 80.595  113.499 1.00 26.15 ? 738  ILE A CB    1 
ATOM   5307  C CG1   . ILE A  1 740  ? -31.461 79.077  113.332 1.00 27.31 ? 738  ILE A CG1   1 
ATOM   5308  C CG2   . ILE A  1 740  ? -30.413 81.298  112.840 1.00 25.03 ? 738  ILE A CG2   1 
ATOM   5309  C CD1   . ILE A  1 740  ? -32.764 78.308  113.537 1.00 26.38 ? 738  ILE A CD1   1 
ATOM   5310  N N     . ALA A  1 741  ? -29.533 81.473  116.020 1.00 22.20 ? 739  ALA A N     1 
ATOM   5311  C CA    . ALA A  1 741  ? -28.394 81.161  116.883 1.00 23.45 ? 739  ALA A CA    1 
ATOM   5312  C C     . ALA A  1 741  ? -28.845 80.931  118.317 1.00 23.81 ? 739  ALA A C     1 
ATOM   5313  O O     . ALA A  1 741  ? -28.422 79.967  118.965 1.00 23.24 ? 739  ALA A O     1 
ATOM   5314  C CB    . ALA A  1 741  ? -27.369 82.289  116.843 1.00 22.48 ? 739  ALA A CB    1 
ATOM   5315  N N     . ALA A  1 742  ? -29.667 81.845  118.847 1.00 23.11 ? 740  ALA A N     1 
ATOM   5316  C CA    . ALA A  1 742  ? -30.183 81.687  120.203 1.00 25.96 ? 740  ALA A CA    1 
ATOM   5317  C C     . ALA A  1 742  ? -30.968 80.390  120.347 1.00 24.90 ? 740  ALA A C     1 
ATOM   5318  O O     . ALA A  1 742  ? -30.856 79.700  121.363 1.00 25.94 ? 740  ALA A O     1 
ATOM   5319  C CB    . ALA A  1 742  ? -31.062 82.883  120.577 1.00 24.28 ? 740  ALA A CB    1 
ATOM   5320  N N     . GLU A  1 743  ? -31.770 80.042  119.333 1.00 23.12 ? 741  GLU A N     1 
ATOM   5321  C CA    . GLU A  1 743  ? -32.482 78.769  119.365 1.00 24.04 ? 741  GLU A CA    1 
ATOM   5322  C C     . GLU A  1 743  ? -31.522 77.581  119.306 1.00 26.46 ? 741  GLU A C     1 
ATOM   5323  O O     . GLU A  1 743  ? -31.766 76.550  119.939 1.00 26.21 ? 741  GLU A O     1 
ATOM   5324  C CB    . GLU A  1 743  ? -33.487 78.712  118.216 1.00 22.71 ? 741  GLU A CB    1 
ATOM   5325  C CG    . GLU A  1 743  ? -34.191 77.369  118.072 1.00 30.07 ? 741  GLU A CG    1 
ATOM   5326  C CD    . GLU A  1 743  ? -35.104 77.012  119.243 1.00 29.06 ? 741  GLU A CD    1 
ATOM   5327  O OE1   . GLU A  1 743  ? -35.324 77.855  120.151 1.00 28.91 ? 741  GLU A OE1   1 
ATOM   5328  O OE2   . GLU A  1 743  ? -35.595 75.861  119.265 1.00 32.63 ? 741  GLU A OE2   1 
ATOM   5329  N N     . GLY A  1 744  ? -30.439 77.692  118.530 1.00 25.16 ? 742  GLY A N     1 
ATOM   5330  C CA    . GLY A  1 744  ? -29.432 76.644  118.544 1.00 22.28 ? 742  GLY A CA    1 
ATOM   5331  C C     . GLY A  1 744  ? -28.773 76.488  119.905 1.00 24.71 ? 742  GLY A C     1 
ATOM   5332  O O     . GLY A  1 744  ? -28.545 75.370  120.364 1.00 22.69 ? 742  GLY A O     1 
ATOM   5333  N N     . VAL A  1 745  ? -28.474 77.606  120.576 1.00 22.99 ? 743  VAL A N     1 
ATOM   5334  C CA    . VAL A  1 745  ? -27.894 77.510  121.919 1.00 26.30 ? 743  VAL A CA    1 
ATOM   5335  C C     . VAL A  1 745  ? -28.891 76.898  122.896 1.00 25.24 ? 743  VAL A C     1 
ATOM   5336  O O     . VAL A  1 745  ? -28.521 76.053  123.724 1.00 26.59 ? 743  VAL A O     1 
ATOM   5337  C CB    . VAL A  1 745  ? -27.392 78.885  122.396 1.00 24.31 ? 743  VAL A CB    1 
ATOM   5338  C CG1   . VAL A  1 745  ? -27.131 78.883  123.907 1.00 24.32 ? 743  VAL A CG1   1 
ATOM   5339  C CG2   . VAL A  1 745  ? -26.112 79.242  121.644 1.00 23.44 ? 743  VAL A CG2   1 
ATOM   5340  N N     . ARG A  1 746  ? -30.167 77.309  122.822 1.00 24.42 ? 744  ARG A N     1 
ATOM   5341  C CA    . ARG A  1 746  ? -31.193 76.720  123.683 1.00 29.89 ? 744  ARG A CA    1 
ATOM   5342  C C     . ARG A  1 746  ? -31.229 75.201  123.539 1.00 27.52 ? 744  ARG A C     1 
ATOM   5343  O O     . ARG A  1 746  ? -31.295 74.474  124.535 1.00 27.05 ? 744  ARG A O     1 
ATOM   5344  C CB    . ARG A  1 746  ? -32.576 77.302  123.358 1.00 25.36 ? 744  ARG A CB    1 
ATOM   5345  C CG    . ARG A  1 746  ? -33.652 76.866  124.360 1.00 31.31 ? 744  ARG A CG    1 
ATOM   5346  C CD    . ARG A  1 746  ? -35.089 77.165  123.891 1.00 32.67 ? 744  ARG A CD    1 
ATOM   5347  N NE    . ARG A  1 746  ? -35.440 76.368  122.722 1.00 33.72 ? 744  ARG A NE    1 
ATOM   5348  C CZ    . ARG A  1 746  ? -35.765 75.082  122.766 1.00 37.81 ? 744  ARG A CZ    1 
ATOM   5349  N NH1   . ARG A  1 746  ? -35.846 74.430  123.915 1.00 38.06 ? 744  ARG A NH1   1 
ATOM   5350  N NH2   . ARG A  1 746  ? -36.004 74.432  121.628 1.00 35.23 ? 744  ARG A NH2   1 
ATOM   5351  N N     . ILE A  1 747  ? -31.175 74.708  122.300 1.00 26.23 ? 745  ILE A N     1 
ATOM   5352  C CA    . ILE A  1 747  ? -31.214 73.266  122.066 1.00 25.31 ? 745  ILE A CA    1 
ATOM   5353  C C     . ILE A  1 747  ? -29.967 72.585  122.626 1.00 26.50 ? 745  ILE A C     1 
ATOM   5354  O O     . ILE A  1 747  ? -30.057 71.535  123.276 1.00 25.66 ? 745  ILE A O     1 
ATOM   5355  C CB    . ILE A  1 747  ? -31.412 73.001  120.565 1.00 25.93 ? 745  ILE A CB    1 
ATOM   5356  C CG1   . ILE A  1 747  ? -32.866 73.340  120.197 1.00 27.18 ? 745  ILE A CG1   1 
ATOM   5357  C CG2   . ILE A  1 747  ? -31.045 71.564  120.217 1.00 25.53 ? 745  ILE A CG2   1 
ATOM   5358  C CD1   . ILE A  1 747  ? -33.172 73.291  118.726 1.00 26.21 ? 745  ILE A CD1   1 
ATOM   5359  N N     . LEU A  1 748  ? -28.783 73.168  122.401 1.00 28.60 ? 746  LEU A N     1 
ATOM   5360  C CA    . LEU A  1 748  ? -27.559 72.577  122.948 1.00 25.92 ? 746  LEU A CA    1 
ATOM   5361  C C     . LEU A  1 748  ? -27.572 72.556  124.470 1.00 27.34 ? 746  LEU A C     1 
ATOM   5362  O O     . LEU A  1 748  ? -27.103 71.590  125.087 1.00 24.58 ? 746  LEU A O     1 
ATOM   5363  C CB    . LEU A  1 748  ? -26.330 73.327  122.437 1.00 23.11 ? 746  LEU A CB    1 
ATOM   5364  C CG    . LEU A  1 748  ? -25.906 72.917  121.023 1.00 27.35 ? 746  LEU A CG    1 
ATOM   5365  C CD1   . LEU A  1 748  ? -24.960 73.936  120.396 1.00 33.28 ? 746  LEU A CD1   1 
ATOM   5366  C CD2   . LEU A  1 748  ? -25.264 71.551  121.066 1.00 27.74 ? 746  LEU A CD2   1 
ATOM   5367  N N     . ARG A  1 749  ? -28.071 73.618  125.102 1.00 24.54 ? 747  ARG A N     1 
ATOM   5368  C CA    . ARG A  1 749  ? -28.183 73.582  126.558 1.00 26.71 ? 747  ARG A CA    1 
ATOM   5369  C C     . ARG A  1 749  ? -29.199 72.535  127.008 1.00 28.73 ? 747  ARG A C     1 
ATOM   5370  O O     . ARG A  1 749  ? -28.939 71.779  127.948 1.00 27.45 ? 747  ARG A O     1 
ATOM   5371  C CB    . ARG A  1 749  ? -28.536 74.968  127.098 1.00 30.67 ? 747  ARG A CB    1 
ATOM   5372  C CG    . ARG A  1 749  ? -27.343 75.920  127.136 1.00 31.70 ? 747  ARG A CG    1 
ATOM   5373  C CD    . ARG A  1 749  ? -27.733 77.249  127.725 1.00 32.92 ? 747  ARG A CD    1 
ATOM   5374  N NE    . ARG A  1 749  ? -26.623 78.193  127.734 1.00 28.78 ? 747  ARG A NE    1 
ATOM   5375  C CZ    . ARG A  1 749  ? -26.658 79.355  128.372 1.00 33.23 ? 747  ARG A CZ    1 
ATOM   5376  N NH1   . ARG A  1 749  ? -27.742 79.752  129.023 1.00 32.56 ? 747  ARG A NH1   1 
ATOM   5377  N NH2   . ARG A  1 749  ? -25.575 80.129  128.372 1.00 31.66 ? 747  ARG A NH2   1 
ATOM   5378  N N     . GLU A  1 750  ? -30.354 72.458  126.337 1.00 27.25 ? 748  GLU A N     1 
ATOM   5379  C CA    . GLU A  1 750  ? -31.321 71.413  126.661 1.00 27.86 ? 748  GLU A CA    1 
ATOM   5380  C C     . GLU A  1 750  ? -30.712 70.018  126.506 1.00 25.85 ? 748  GLU A C     1 
ATOM   5381  O O     . GLU A  1 750  ? -31.038 69.103  127.272 1.00 28.39 ? 748  GLU A O     1 
ATOM   5382  C CB    . GLU A  1 750  ? -32.566 71.559  125.778 1.00 28.46 ? 748  GLU A CB    1 
ATOM   5383  C CG    . GLU A  1 750  ? -33.649 70.542  126.077 1.00 32.06 ? 748  GLU A CG    1 
ATOM   5384  C CD    . GLU A  1 750  ? -34.844 70.644  125.140 1.00 35.50 ? 748  GLU A CD    1 
ATOM   5385  O OE1   . GLU A  1 750  ? -35.015 71.694  124.487 1.00 42.02 ? 748  GLU A OE1   1 
ATOM   5386  O OE2   . GLU A  1 750  ? -35.608 69.662  125.044 1.00 41.34 ? 748  GLU A OE2   1 
ATOM   5387  N N     . ALA A  1 751  ? -29.802 69.839  125.541 1.00 25.22 ? 749  ALA A N     1 
ATOM   5388  C CA    . ALA A  1 751  ? -29.162 68.542  125.354 1.00 25.83 ? 749  ALA A CA    1 
ATOM   5389  C C     . ALA A  1 751  ? -28.118 68.240  126.424 1.00 25.54 ? 749  ALA A C     1 
ATOM   5390  O O     . ALA A  1 751  ? -27.614 67.113  126.474 1.00 26.86 ? 749  ALA A O     1 
ATOM   5391  C CB    . ALA A  1 751  ? -28.513 68.468  123.968 1.00 27.02 ? 749  ALA A CB    1 
ATOM   5392  N N     . GLY A  1 752  ? -27.766 69.211  127.254 1.00 25.16 ? 750  GLY A N     1 
ATOM   5393  C CA    . GLY A  1 752  ? -26.869 68.942  128.360 1.00 30.48 ? 750  GLY A CA    1 
ATOM   5394  C C     . GLY A  1 752  ? -25.620 69.796  128.429 1.00 27.16 ? 750  GLY A C     1 
ATOM   5395  O O     . GLY A  1 752  ? -24.847 69.647  129.377 1.00 27.92 ? 750  GLY A O     1 
ATOM   5396  N N     . ILE A  1 753  ? -25.387 70.674  127.455 1.00 27.73 ? 751  ILE A N     1 
ATOM   5397  C CA    . ILE A  1 753  ? -24.230 71.571  127.527 1.00 24.81 ? 751  ILE A CA    1 
ATOM   5398  C C     . ILE A  1 753  ? -24.476 72.573  128.648 1.00 26.26 ? 751  ILE A C     1 
ATOM   5399  O O     . ILE A  1 753  ? -25.473 73.301  128.604 1.00 28.72 ? 751  ILE A O     1 
ATOM   5400  C CB    . ILE A  1 753  ? -23.973 72.308  126.199 1.00 25.81 ? 751  ILE A CB    1 
ATOM   5401  C CG1   . ILE A  1 753  ? -23.775 71.322  125.050 1.00 24.19 ? 751  ILE A CG1   1 
ATOM   5402  C CG2   . ILE A  1 753  ? -22.744 73.206  126.330 1.00 25.35 ? 751  ILE A CG2   1 
ATOM   5403  C CD1   . ILE A  1 753  ? -22.495 70.522  125.140 1.00 23.77 ? 751  ILE A CD1   1 
ATOM   5404  N N     . PRO A  1 754  ? -23.606 72.660  129.659 1.00 27.47 ? 752  PRO A N     1 
ATOM   5405  C CA    . PRO A  1 754  ? -23.823 73.645  130.724 1.00 28.42 ? 752  PRO A CA    1 
ATOM   5406  C C     . PRO A  1 754  ? -23.745 75.069  130.198 1.00 32.52 ? 752  PRO A C     1 
ATOM   5407  O O     . PRO A  1 754  ? -23.026 75.373  129.237 1.00 28.13 ? 752  PRO A O     1 
ATOM   5408  C CB    . PRO A  1 754  ? -22.691 73.359  131.718 1.00 28.37 ? 752  PRO A CB    1 
ATOM   5409  C CG    . PRO A  1 754  ? -22.311 71.952  131.472 1.00 32.53 ? 752  PRO A CG    1 
ATOM   5410  C CD    . PRO A  1 754  ? -22.522 71.718  129.990 1.00 27.37 ? 752  PRO A CD    1 
ATOM   5411  N N     . ALA A  1 755  ? -24.495 75.946  130.867 1.00 32.52 ? 753  ALA A N     1 
ATOM   5412  C CA    . ALA A  1 755  ? -24.490 77.369  130.553 1.00 28.69 ? 753  ALA A CA    1 
ATOM   5413  C C     . ALA A  1 755  ? -23.087 77.959  130.585 1.00 29.81 ? 753  ALA A C     1 
ATOM   5414  O O     . ALA A  1 755  ? -22.778 78.873  129.811 1.00 31.98 ? 753  ALA A O     1 
ATOM   5415  C CB    . ALA A  1 755  ? -25.401 78.112  131.534 1.00 27.09 ? 753  ALA A CB    1 
ATOM   5416  N N     . SER A  1 756  ? -22.224 77.465  131.475 1.00 26.81 ? 754  SER A N     1 
ATOM   5417  C CA    . SER A  1 756  ? -20.876 78.006  131.554 1.00 27.23 ? 754  SER A CA    1 
ATOM   5418  C C     . SER A  1 756  ? -20.007 77.545  130.395 1.00 30.49 ? 754  SER A C     1 
ATOM   5419  O O     . SER A  1 756  ? -18.988 78.184  130.113 1.00 30.18 ? 754  SER A O     1 
ATOM   5420  C CB    . SER A  1 756  ? -20.234 77.618  132.886 1.00 30.92 ? 754  SER A CB    1 
ATOM   5421  O OG    . SER A  1 756  ? -20.196 76.210  133.022 1.00 32.40 ? 754  SER A OG    1 
ATOM   5422  N N     . ALA A  1 757  ? -20.394 76.466  129.708 1.00 25.90 ? 755  ALA A N     1 
ATOM   5423  C CA    . ALA A  1 757  ? -19.645 75.970  128.560 1.00 25.45 ? 755  ALA A CA    1 
ATOM   5424  C C     . ALA A  1 757  ? -20.118 76.567  127.245 1.00 24.93 ? 755  ALA A C     1 
ATOM   5425  O O     . ALA A  1 757  ? -19.396 76.494  126.247 1.00 24.53 ? 755  ALA A O     1 
ATOM   5426  C CB    . ALA A  1 757  ? -19.739 74.438  128.480 1.00 25.20 ? 755  ALA A CB    1 
ATOM   5427  N N     . LEU A  1 758  ? -21.299 77.166  127.214 1.00 25.01 ? 756  LEU A N     1 
ATOM   5428  C CA    . LEU A  1 758  ? -21.814 77.710  125.956 1.00 24.61 ? 756  LEU A CA    1 
ATOM   5429  C C     . LEU A  1 758  ? -22.534 79.019  126.256 1.00 24.91 ? 756  LEU A C     1 
ATOM   5430  O O     . LEU A  1 758  ? -23.651 79.018  126.788 1.00 25.74 ? 756  LEU A O     1 
ATOM   5431  C CB    . LEU A  1 758  ? -22.719 76.700  125.284 1.00 24.88 ? 756  LEU A CB    1 
ATOM   5432  C CG    . LEU A  1 758  ? -23.391 77.196  124.019 1.00 23.90 ? 756  LEU A CG    1 
ATOM   5433  C CD1   . LEU A  1 758  ? -22.345 77.840  123.094 1.00 23.62 ? 756  LEU A CD1   1 
ATOM   5434  C CD2   . LEU A  1 758  ? -24.029 75.998  123.368 1.00 26.22 ? 756  LEU A CD2   1 
ATOM   5435  N N     . GLN A  1 759  ? -21.887 80.131  125.916 1.00 25.57 ? 757  GLN A N     1 
ATOM   5436  C CA    . GLN A  1 759  ? -22.447 81.457  126.122 1.00 25.23 ? 757  GLN A CA    1 
ATOM   5437  C C     . GLN A  1 759  ? -22.711 82.124  124.777 1.00 24.86 ? 757  GLN A C     1 
ATOM   5438  O O     . GLN A  1 759  ? -21.876 82.066  123.866 1.00 25.19 ? 757  GLN A O     1 
ATOM   5439  C CB    . GLN A  1 759  ? -21.515 82.318  126.979 1.00 25.69 ? 757  GLN A CB    1 
ATOM   5440  C CG    . GLN A  1 759  ? -21.340 81.774  128.388 1.00 26.12 ? 757  GLN A CG    1 
ATOM   5441  C CD    . GLN A  1 759  ? -20.339 82.572  129.191 1.00 28.82 ? 757  GLN A CD    1 
ATOM   5442  O OE1   . GLN A  1 759  ? -20.704 83.503  129.916 1.00 27.88 ? 757  GLN A OE1   1 
ATOM   5443  N NE2   . GLN A  1 759  ? -19.065 82.216  129.060 1.00 26.41 ? 757  GLN A NE2   1 
ATOM   5444  N N     . LEU A  1 760  ? -23.882 82.736  124.656 1.00 25.49 ? 758  LEU A N     1 
ATOM   5445  C CA    . LEU A  1 760  ? -24.309 83.397  123.429 1.00 24.66 ? 758  LEU A CA    1 
ATOM   5446  C C     . LEU A  1 760  ? -24.133 84.903  123.575 1.00 25.00 ? 758  LEU A C     1 
ATOM   5447  O O     . LEU A  1 760  ? -24.610 85.496  124.546 1.00 27.33 ? 758  LEU A O     1 
ATOM   5448  C CB    . LEU A  1 760  ? -25.769 83.068  123.112 1.00 24.55 ? 758  LEU A CB    1 
ATOM   5449  C CG    . LEU A  1 760  ? -26.293 83.675  121.800 1.00 24.23 ? 758  LEU A CG    1 
ATOM   5450  C CD1   . LEU A  1 760  ? -25.806 82.883  120.566 1.00 24.85 ? 758  LEU A CD1   1 
ATOM   5451  C CD2   . LEU A  1 760  ? -27.811 83.771  121.800 1.00 24.94 ? 758  LEU A CD2   1 
ATOM   5452  N N     . LEU A  1 761  ? -23.465 85.523  122.603 1.00 27.43 ? 759  LEU A N     1 
ATOM   5453  C CA    . LEU A  1 761  ? -23.131 86.946  122.667 1.00 26.35 ? 759  LEU A CA    1 
ATOM   5454  C C     . LEU A  1 761  ? -23.536 87.614  121.361 1.00 24.85 ? 759  LEU A C     1 
ATOM   5455  O O     . LEU A  1 761  ? -22.693 87.854  120.488 1.00 27.54 ? 759  LEU A O     1 
ATOM   5456  C CB    . LEU A  1 761  ? -21.638 87.157  122.937 1.00 25.69 ? 759  LEU A CB    1 
ATOM   5457  C CG    . LEU A  1 761  ? -20.993 86.650  124.233 1.00 27.56 ? 759  LEU A CG    1 
ATOM   5458  C CD1   . LEU A  1 761  ? -21.810 87.066  125.442 1.00 27.03 ? 759  LEU A CD1   1 
ATOM   5459  C CD2   . LEU A  1 761  ? -20.771 85.141  124.209 1.00 29.32 ? 759  LEU A CD2   1 
ATOM   5460  N N     . PRO A  1 762  ? -24.815 87.932  121.195 1.00 25.48 ? 760  PRO A N     1 
ATOM   5461  C CA    . PRO A  1 762  ? -25.252 88.607  119.964 1.00 24.70 ? 760  PRO A CA    1 
ATOM   5462  C C     . PRO A  1 762  ? -24.705 90.025  119.885 1.00 29.98 ? 760  PRO A C     1 
ATOM   5463  O O     . PRO A  1 762  ? -24.414 90.661  120.900 1.00 28.37 ? 760  PRO A O     1 
ATOM   5464  C CB    . PRO A  1 762  ? -26.782 88.625  120.084 1.00 26.42 ? 760  PRO A CB    1 
ATOM   5465  C CG    . PRO A  1 762  ? -27.127 87.650  121.188 1.00 24.92 ? 760  PRO A CG    1 
ATOM   5466  C CD    . PRO A  1 762  ? -25.936 87.620  122.100 1.00 25.18 ? 760  PRO A CD    1 
ATOM   5467  N N     . GLY A  1 763  ? -24.562 90.518  118.664 1.00 26.91 ? 761  GLY A N     1 
ATOM   5468  C CA    . GLY A  1 763  ? -24.154 91.890  118.454 1.00 31.10 ? 761  GLY A CA    1 
ATOM   5469  C C     . GLY A  1 763  ? -23.336 92.034  117.186 1.00 34.12 ? 761  GLY A C     1 
ATOM   5470  O O     . GLY A  1 763  ? -23.261 91.125  116.357 1.00 32.34 ? 761  GLY A O     1 
ATOM   5471  N N     . ASP A  1 764  ? -22.723 93.204  117.053 1.00 35.50 ? 762  ASP A N     1 
ATOM   5472  C CA    . ASP A  1 764  ? -21.963 93.535  115.858 1.00 37.94 ? 762  ASP A CA    1 
ATOM   5473  C C     . ASP A  1 764  ? -20.478 93.236  116.080 1.00 41.35 ? 762  ASP A C     1 
ATOM   5474  O O     . ASP A  1 764  ? -20.107 92.461  116.975 1.00 36.64 ? 762  ASP A O     1 
ATOM   5475  C CB    . ASP A  1 764  ? -22.222 94.996  115.461 1.00 42.35 ? 762  ASP A CB    1 
ATOM   5476  C CG    . ASP A  1 764  ? -21.975 95.974  116.597 1.00 43.43 ? 762  ASP A CG    1 
ATOM   5477  O OD1   . ASP A  1 764  ? -20.902 95.912  117.242 1.00 46.14 ? 762  ASP A OD1   1 
ATOM   5478  O OD2   . ASP A  1 764  ? -22.857 96.824  116.830 1.00 46.70 ? 762  ASP A OD2   1 
ATOM   5479  N N     . GLY A  1 765  ? -19.620 93.847  115.260 1.00 38.59 ? 763  GLY A N     1 
ATOM   5480  C CA    . GLY A  1 765  ? -18.205 93.540  115.288 1.00 35.45 ? 763  GLY A CA    1 
ATOM   5481  C C     . GLY A  1 765  ? -17.506 93.998  116.542 1.00 35.47 ? 763  GLY A C     1 
ATOM   5482  O O     . GLY A  1 765  ? -16.453 93.450  116.888 1.00 38.30 ? 763  GLY A O     1 
ATOM   5483  N N     . ARG A  1 766  ? -18.056 95.006  117.222 1.00 36.51 ? 764  ARG A N     1 
ATOM   5484  C CA    . ARG A  1 766  ? -17.517 95.387  118.525 1.00 38.84 ? 764  ARG A CA    1 
ATOM   5485  C C     . ARG A  1 766  ? -17.518 94.196  119.481 1.00 36.67 ? 764  ARG A C     1 
ATOM   5486  O O     . ARG A  1 766  ? -16.569 94.005  120.252 1.00 31.73 ? 764  ARG A O     1 
ATOM   5487  C CB    . ARG A  1 766  ? -18.315 96.555  119.105 1.00 36.43 ? 764  ARG A CB    1 
ATOM   5488  N N     . VAL A  1 767  ? -18.564 93.369  119.421 1.00 35.32 ? 765  VAL A N     1 
ATOM   5489  C CA    . VAL A  1 767  ? -18.606 92.152  120.228 1.00 32.50 ? 765  VAL A CA    1 
ATOM   5490  C C     . VAL A  1 767  ? -17.554 91.158  119.750 1.00 31.32 ? 765  VAL A C     1 
ATOM   5491  O O     . VAL A  1 767  ? -16.808 90.587  120.551 1.00 31.74 ? 765  VAL A O     1 
ATOM   5492  C CB    . VAL A  1 767  ? -20.017 91.533  120.201 1.00 32.31 ? 765  VAL A CB    1 
ATOM   5493  C CG1   . VAL A  1 767  ? -20.074 90.316  121.101 1.00 29.05 ? 765  VAL A CG1   1 
ATOM   5494  C CG2   . VAL A  1 767  ? -21.063 92.566  120.616 1.00 32.53 ? 765  VAL A CG2   1 
ATOM   5495  N N     . GLY A  1 768  ? -17.486 90.925  118.439 1.00 30.12 ? 766  GLY A N     1 
ATOM   5496  C CA    . GLY A  1 768  ? -16.474 90.025  117.914 1.00 30.72 ? 766  GLY A CA    1 
ATOM   5497  C C     . GLY A  1 768  ? -15.071 90.450  118.296 1.00 30.86 ? 766  GLY A C     1 
ATOM   5498  O O     . GLY A  1 768  ? -14.261 89.629  118.726 1.00 28.39 ? 766  GLY A O     1 
ATOM   5499  N N     . ALA A  1 769  ? -14.780 91.747  118.185 1.00 31.89 ? 767  ALA A N     1 
ATOM   5500  C CA    . ALA A  1 769  ? -13.436 92.240  118.461 1.00 31.39 ? 767  ALA A CA    1 
ATOM   5501  C C     . ALA A  1 769  ? -13.087 92.104  119.937 1.00 33.30 ? 767  ALA A C     1 
ATOM   5502  O O     . ALA A  1 769  ? -11.958 91.735  120.282 1.00 31.97 ? 767  ALA A O     1 
ATOM   5503  C CB    . ALA A  1 769  ? -13.304 93.695  118.011 1.00 30.61 ? 767  ALA A CB    1 
ATOM   5504  N N     . ALA A  1 770  ? -14.045 92.399  120.819 1.00 31.31 ? 768  ALA A N     1 
ATOM   5505  C CA    . ALA A  1 770  ? -13.806 92.259  122.253 1.00 32.17 ? 768  ALA A CA    1 
ATOM   5506  C C     . ALA A  1 770  ? -13.500 90.811  122.617 1.00 32.20 ? 768  ALA A C     1 
ATOM   5507  O O     . ALA A  1 770  ? -12.598 90.535  123.418 1.00 30.72 ? 768  ALA A O     1 
ATOM   5508  C CB    . ALA A  1 770  ? -15.018 92.768  123.034 1.00 32.44 ? 768  ALA A CB    1 
ATOM   5509  N N     . LEU A  1 771  ? -14.242 89.871  122.033 1.00 30.35 ? 769  LEU A N     1 
ATOM   5510  C CA    . LEU A  1 771  ? -14.004 88.458  122.303 1.00 27.79 ? 769  LEU A CA    1 
ATOM   5511  C C     . LEU A  1 771  ? -12.624 88.027  121.819 1.00 29.09 ? 769  LEU A C     1 
ATOM   5512  O O     . LEU A  1 771  ? -11.883 87.345  122.539 1.00 31.61 ? 769  LEU A O     1 
ATOM   5513  C CB    . LEU A  1 771  ? -15.103 87.620  121.640 1.00 26.80 ? 769  LEU A CB    1 
ATOM   5514  C CG    . LEU A  1 771  ? -16.520 87.806  122.188 1.00 25.93 ? 769  LEU A CG    1 
ATOM   5515  C CD1   . LEU A  1 771  ? -17.541 87.132  121.271 1.00 24.69 ? 769  LEU A CD1   1 
ATOM   5516  C CD2   . LEU A  1 771  ? -16.640 87.260  123.597 1.00 26.94 ? 769  LEU A CD2   1 
ATOM   5517  N N     . VAL A  1 772  ? -12.254 88.430  120.601 1.00 26.45 ? 770  VAL A N     1 
ATOM   5518  C CA    . VAL A  1 772  ? -10.981 88.001  120.031 1.00 28.86 ? 770  VAL A CA    1 
ATOM   5519  C C     . VAL A  1 772  ? -9.816  88.542  120.858 1.00 30.47 ? 770  VAL A C     1 
ATOM   5520  O O     . VAL A  1 772  ? -8.830  87.838  121.105 1.00 29.51 ? 770  VAL A O     1 
ATOM   5521  C CB    . VAL A  1 772  ? -10.894 88.428  118.552 1.00 29.00 ? 770  VAL A CB    1 
ATOM   5522  C CG1   . VAL A  1 772  ? -9.484  88.243  118.011 1.00 30.41 ? 770  VAL A CG1   1 
ATOM   5523  C CG2   . VAL A  1 772  ? -11.881 87.624  117.731 1.00 28.73 ? 770  VAL A CG2   1 
ATOM   5524  N N     . ALA A  1 773  ? -9.924  89.781  121.326 1.00 29.45 ? 771  ALA A N     1 
ATOM   5525  C CA    . ALA A  1 773  ? -8.819  90.391  122.050 1.00 27.33 ? 771  ALA A CA    1 
ATOM   5526  C C     . ALA A  1 773  ? -8.702  89.925  123.496 1.00 35.70 ? 771  ALA A C     1 
ATOM   5527  O O     . ALA A  1 773  ? -7.673  90.202  124.128 1.00 36.42 ? 771  ALA A O     1 
ATOM   5528  C CB    . ALA A  1 773  ? -8.952  91.915  122.022 1.00 31.36 ? 771  ALA A CB    1 
ATOM   5529  N N     . ALA A  1 774  ? -9.712  89.248  124.046 1.00 31.14 ? 772  ALA A N     1 
ATOM   5530  C CA    . ALA A  1 774  ? -9.680  88.915  125.470 1.00 31.44 ? 772  ALA A CA    1 
ATOM   5531  C C     . ALA A  1 774  ? -8.502  87.998  125.771 1.00 29.66 ? 772  ALA A C     1 
ATOM   5532  O O     . ALA A  1 774  ? -8.167  87.112  124.984 1.00 31.40 ? 772  ALA A O     1 
ATOM   5533  C CB    . ALA A  1 774  ? -10.997 88.265  125.906 1.00 30.47 ? 772  ALA A CB    1 
ATOM   5534  N N     . ALA A  1 775  ? -7.854  88.224  126.922 1.00 31.36 ? 773  ALA A N     1 
ATOM   5535  C CA    . ALA A  1 775  ? -6.604  87.522  127.195 1.00 30.60 ? 773  ALA A CA    1 
ATOM   5536  C C     . ALA A  1 775  ? -6.800  86.017  127.328 1.00 31.81 ? 773  ALA A C     1 
ATOM   5537  O O     . ALA A  1 775  ? -5.905  85.245  126.958 1.00 30.20 ? 773  ALA A O     1 
ATOM   5538  C CB    . ALA A  1 775  ? -5.942  88.080  128.458 1.00 31.98 ? 773  ALA A CB    1 
ATOM   5539  N N     . GLU A  1 776  ? -7.945  85.573  127.837 1.00 30.66 ? 774  GLU A N     1 
ATOM   5540  C CA    . GLU A  1 776  ? -8.168  84.150  128.056 1.00 26.62 ? 774  GLU A CA    1 
ATOM   5541  C C     . GLU A  1 776  ? -8.746  83.437  126.837 1.00 26.95 ? 774  GLU A C     1 
ATOM   5542  O O     . GLU A  1 776  ? -9.060  82.243  126.919 1.00 27.56 ? 774  GLU A O     1 
ATOM   5543  C CB    . GLU A  1 776  ? -9.065  83.947  129.271 1.00 29.46 ? 774  GLU A CB    1 
ATOM   5544  C CG    . GLU A  1 776  ? -8.308  84.223  130.581 1.00 32.51 ? 774  GLU A CG    1 
ATOM   5545  C CD    . GLU A  1 776  ? -9.216  84.637  131.716 1.00 40.96 ? 774  GLU A CD    1 
ATOM   5546  O OE1   . GLU A  1 776  ? -10.146 85.432  131.470 1.00 46.93 ? 774  GLU A OE1   1 
ATOM   5547  O OE2   . GLU A  1 776  ? -9.000  84.165  132.853 1.00 51.55 ? 774  GLU A OE2   1 
ATOM   5548  N N     . THR A  1 777  ? -8.857  84.124  125.705 1.00 27.97 ? 775  THR A N     1 
ATOM   5549  C CA    . THR A  1 777  ? -9.279  83.464  124.477 1.00 26.30 ? 775  THR A CA    1 
ATOM   5550  C C     . THR A  1 777  ? -8.148  82.582  123.951 1.00 28.63 ? 775  THR A C     1 
ATOM   5551  O O     . THR A  1 777  ? -7.030  83.058  123.712 1.00 27.23 ? 775  THR A O     1 
ATOM   5552  C CB    . THR A  1 777  ? -9.700  84.511  123.450 1.00 25.94 ? 775  THR A CB    1 
ATOM   5553  O OG1   . THR A  1 777  ? -10.858 85.190  123.942 1.00 26.07 ? 775  THR A OG1   1 
ATOM   5554  C CG2   . THR A  1 777  ? -10.004 83.863  122.093 1.00 24.49 ? 775  THR A CG2   1 
ATOM   5555  N N     . ALA A  1 778  ? -8.428  81.285  123.815 1.00 25.45 ? 776  ALA A N     1 
ATOM   5556  C CA    . ALA A  1 778  ? -7.415  80.295  123.498 1.00 24.42 ? 776  ALA A CA    1 
ATOM   5557  C C     . ALA A  1 778  ? -7.478  79.806  122.060 1.00 24.40 ? 776  ALA A C     1 
ATOM   5558  O O     . ALA A  1 778  ? -6.581  79.074  121.630 1.00 29.13 ? 776  ALA A O     1 
ATOM   5559  C CB    . ALA A  1 778  ? -7.528  79.095  124.458 1.00 24.53 ? 776  ALA A CB    1 
ATOM   5560  N N     . GLY A  1 779  ? -8.485  80.218  121.302 1.00 24.04 ? 777  GLY A N     1 
ATOM   5561  C CA    . GLY A  1 779  ? -8.667  79.773  119.936 1.00 23.20 ? 777  GLY A CA    1 
ATOM   5562  C C     . GLY A  1 779  ? -9.851  80.513  119.351 1.00 23.08 ? 777  GLY A C     1 
ATOM   5563  O O     . GLY A  1 779  ? -10.747 80.936  120.089 1.00 23.31 ? 777  GLY A O     1 
ATOM   5564  N N     . VAL A  1 780  ? -9.854  80.707  118.033 1.00 23.74 ? 778  VAL A N     1 
ATOM   5565  C CA    . VAL A  1 780  ? -10.914 81.433  117.344 1.00 22.65 ? 778  VAL A CA    1 
ATOM   5566  C C     . VAL A  1 780  ? -11.306 80.621  116.131 1.00 22.18 ? 778  VAL A C     1 
ATOM   5567  O O     . VAL A  1 780  ? -10.440 80.196  115.364 1.00 21.98 ? 778  VAL A O     1 
ATOM   5568  C CB    . VAL A  1 780  ? -10.475 82.840  116.900 1.00 23.54 ? 778  VAL A CB    1 
ATOM   5569  C CG1   . VAL A  1 780  ? -11.583 83.508  116.088 1.00 22.69 ? 778  VAL A CG1   1 
ATOM   5570  C CG2   . VAL A  1 780  ? -10.087 83.686  118.106 1.00 23.33 ? 778  VAL A CG2   1 
ATOM   5571  N N     . MET A  1 781  ? -12.599 80.398  115.970 1.00 22.03 ? 779  MET A N     1 
ATOM   5572  C CA    . MET A  1 781  ? -13.151 79.779  114.781 1.00 21.61 ? 779  MET A CA    1 
ATOM   5573  C C     . MET A  1 781  ? -14.007 80.833  114.102 1.00 21.59 ? 779  MET A C     1 
ATOM   5574  O O     . MET A  1 781  ? -14.951 81.348  114.706 1.00 21.77 ? 779  MET A O     1 
ATOM   5575  C CB    . MET A  1 781  ? -13.958 78.536  115.150 1.00 21.48 ? 779  MET A CB    1 
ATOM   5576  C CG    . MET A  1 781  ? -13.131 77.520  115.919 1.00 21.56 ? 779  MET A CG    1 
ATOM   5577  S SD    . MET A  1 781  ? -14.162 76.208  116.600 1.00 24.78 ? 779  MET A SD    1 
ATOM   5578  C CE    . MET A  1 781  ? -14.347 75.172  115.148 1.00 21.05 ? 779  MET A CE    1 
ATOM   5579  N N     . PHE A  1 782  ? -13.643 81.189  112.873 1.00 21.39 ? 780  PHE A N     1 
ATOM   5580  C CA    . PHE A  1 782  ? -14.274 82.284  112.158 1.00 21.41 ? 780  PHE A CA    1 
ATOM   5581  C C     . PHE A  1 782  ? -14.663 81.784  110.784 1.00 21.10 ? 780  PHE A C     1 
ATOM   5582  O O     . PHE A  1 782  ? -13.837 81.192  110.081 1.00 20.82 ? 780  PHE A O     1 
ATOM   5583  C CB    . PHE A  1 782  ? -13.331 83.482  112.020 1.00 22.26 ? 780  PHE A CB    1 
ATOM   5584  C CG    . PHE A  1 782  ? -13.850 84.575  111.116 1.00 21.69 ? 780  PHE A CG    1 
ATOM   5585  C CD1   . PHE A  1 782  ? -14.716 85.548  111.608 1.00 23.48 ? 780  PHE A CD1   1 
ATOM   5586  C CD2   . PHE A  1 782  ? -13.456 84.638  109.783 1.00 22.05 ? 780  PHE A CD2   1 
ATOM   5587  C CE1   . PHE A  1 782  ? -15.189 86.558  110.796 1.00 23.45 ? 780  PHE A CE1   1 
ATOM   5588  C CE2   . PHE A  1 782  ? -13.920 85.647  108.958 1.00 24.98 ? 780  PHE A CE2   1 
ATOM   5589  C CZ    . PHE A  1 782  ? -14.792 86.608  109.460 1.00 26.29 ? 780  PHE A CZ    1 
ATOM   5590  N N     . THR A  1 783  ? -15.905 82.025  110.411 1.00 22.51 ? 781  THR A N     1 
ATOM   5591  C CA    . THR A  1 783  ? -16.341 81.870  109.034 1.00 24.50 ? 781  THR A CA    1 
ATOM   5592  C C     . THR A  1 783  ? -16.949 83.193  108.599 1.00 22.61 ? 781  THR A C     1 
ATOM   5593  O O     . THR A  1 783  ? -17.916 83.665  109.209 1.00 23.72 ? 781  THR A O     1 
ATOM   5594  C CB    . THR A  1 783  ? -17.339 80.722  108.881 1.00 25.23 ? 781  THR A CB    1 
ATOM   5595  O OG1   . THR A  1 783  ? -16.757 79.512  109.388 1.00 23.49 ? 781  THR A OG1   1 
ATOM   5596  C CG2   . THR A  1 783  ? -17.676 80.519  107.418 1.00 24.26 ? 781  THR A CG2   1 
ATOM   5597  N N     . GLY A  1 784  ? -16.384 83.783  107.548 1.00 23.78 ? 782  GLY A N     1 
ATOM   5598  C CA    . GLY A  1 784  ? -16.805 85.105  107.106 1.00 25.44 ? 782  GLY A CA    1 
ATOM   5599  C C     . GLY A  1 784  ? -15.901 85.607  105.997 1.00 25.11 ? 782  GLY A C     1 
ATOM   5600  O O     . GLY A  1 784  ? -15.279 84.817  105.291 1.00 27.17 ? 782  GLY A O     1 
ATOM   5601  N N     . SER A  1 785  ? -15.832 86.931  105.861 1.00 26.42 ? 783  SER A N     1 
ATOM   5602  C CA    . SER A  1 785  ? -15.043 87.530  104.792 1.00 29.79 ? 783  SER A CA    1 
ATOM   5603  C C     . SER A  1 785  ? -13.545 87.418  105.070 1.00 29.93 ? 783  SER A C     1 
ATOM   5604  O O     . SER A  1 785  ? -13.106 87.384  106.223 1.00 28.33 ? 783  SER A O     1 
ATOM   5605  C CB    . SER A  1 785  ? -15.426 88.997  104.631 1.00 33.79 ? 783  SER A CB    1 
ATOM   5606  O OG    . SER A  1 785  ? -15.304 89.665  105.868 1.00 34.94 ? 783  SER A OG    1 
ATOM   5607  N N     . THR A  1 786  ? -12.751 87.383  103.990 1.00 31.30 ? 784  THR A N     1 
ATOM   5608  C CA    . THR A  1 786  ? -11.296 87.360  104.146 1.00 32.41 ? 784  THR A CA    1 
ATOM   5609  C C     . THR A  1 786  ? -10.779 88.595  104.872 1.00 29.92 ? 784  THR A C     1 
ATOM   5610  O O     . THR A  1 786  ? -9.784  88.511  105.608 1.00 30.77 ? 784  THR A O     1 
ATOM   5611  C CB    . THR A  1 786  ? -10.583 87.267  102.793 1.00 34.83 ? 784  THR A CB    1 
ATOM   5612  O OG1   . THR A  1 786  ? -10.847 88.451  102.034 1.00 43.35 ? 784  THR A OG1   1 
ATOM   5613  C CG2   . THR A  1 786  ? -11.016 86.057  102.006 1.00 31.34 ? 784  THR A CG2   1 
ATOM   5614  N N     . GLU A  1 787  ? -11.411 89.752  104.656 1.00 32.34 ? 785  GLU A N     1 
ATOM   5615  C CA    . GLU A  1 787  ? -10.897 90.982  105.253 1.00 34.63 ? 785  GLU A CA    1 
ATOM   5616  C C     . GLU A  1 787  ? -11.030 90.955  106.772 1.00 30.09 ? 785  GLU A C     1 
ATOM   5617  O O     . GLU A  1 787  ? -10.085 91.308  107.487 1.00 30.03 ? 785  GLU A O     1 
ATOM   5618  C CB    . GLU A  1 787  ? -11.601 92.204  104.649 1.00 36.58 ? 785  GLU A CB    1 
ATOM   5619  C CG    . GLU A  1 787  ? -13.115 92.078  104.543 1.00 42.55 ? 785  GLU A CG    1 
ATOM   5620  C CD    . GLU A  1 787  ? -13.755 93.224  103.768 1.00 49.99 ? 785  GLU A CD    1 
ATOM   5621  O OE1   . GLU A  1 787  ? -13.179 93.638  102.742 1.00 53.74 ? 785  GLU A OE1   1 
ATOM   5622  O OE2   . GLU A  1 787  ? -14.829 93.717  104.186 1.00 51.70 ? 785  GLU A OE2   1 
ATOM   5623  N N     . VAL A  1 788  ? -12.181 90.511  107.284 1.00 31.15 ? 786  VAL A N     1 
ATOM   5624  C CA    . VAL A  1 788  ? -12.346 90.395  108.732 1.00 29.11 ? 786  VAL A CA    1 
ATOM   5625  C C     . VAL A  1 788  ? -11.443 89.301  109.288 1.00 26.18 ? 786  VAL A C     1 
ATOM   5626  O O     . VAL A  1 788  ? -10.873 89.445  110.376 1.00 28.01 ? 786  VAL A O     1 
ATOM   5627  C CB    . VAL A  1 788  ? -13.824 90.149  109.088 1.00 33.43 ? 786  VAL A CB    1 
ATOM   5628  C CG1   . VAL A  1 788  ? -13.979 89.807  110.565 1.00 29.19 ? 786  VAL A CG1   1 
ATOM   5629  C CG2   . VAL A  1 788  ? -14.659 91.376  108.745 1.00 39.43 ? 786  VAL A CG2   1 
ATOM   5630  N N     . ALA A  1 789  ? -11.305 88.183  108.564 1.00 26.30 ? 787  ALA A N     1 
ATOM   5631  C CA    . ALA A  1 789  ? -10.389 87.140  109.015 1.00 25.25 ? 787  ALA A CA    1 
ATOM   5632  C C     . ALA A  1 789  ? -8.970  87.678  109.149 1.00 23.78 ? 787  ALA A C     1 
ATOM   5633  O O     . ALA A  1 789  ? -8.248  87.331  110.093 1.00 24.91 ? 787  ALA A O     1 
ATOM   5634  C CB    . ALA A  1 789  ? -10.427 85.952  108.054 1.00 26.85 ? 787  ALA A CB    1 
ATOM   5635  N N     . ARG A  1 790  ? -8.551  88.544  108.220 1.00 26.34 ? 788  ARG A N     1 
ATOM   5636  C CA    . ARG A  1 790  ? -7.199  89.101  108.296 1.00 29.66 ? 788  ARG A CA    1 
ATOM   5637  C C     . ARG A  1 790  ? -7.058  90.042  109.490 1.00 26.95 ? 788  ARG A C     1 
ATOM   5638  O O     . ARG A  1 790  ? -5.998  90.099  110.131 1.00 29.81 ? 788  ARG A O     1 
ATOM   5639  C CB    . ARG A  1 790  ? -6.868  89.818  106.986 1.00 31.14 ? 788  ARG A CB    1 
ATOM   5640  C CG    . ARG A  1 790  ? -5.414  90.177  106.799 1.00 38.58 ? 788  ARG A CG    1 
ATOM   5641  C CD    . ARG A  1 790  ? -5.207  90.857  105.448 1.00 36.32 ? 788  ARG A CD    1 
ATOM   5642  N NE    . ARG A  1 790  ? -5.595  89.992  104.341 1.00 38.79 ? 788  ARG A NE    1 
ATOM   5643  C CZ    . ARG A  1 790  ? -4.803  89.074  103.804 1.00 43.03 ? 788  ARG A CZ    1 
ATOM   5644  N NH1   . ARG A  1 790  ? -3.577  88.860  104.269 1.00 42.18 ? 788  ARG A NH1   1 
ATOM   5645  N NH2   . ARG A  1 790  ? -5.248  88.357  102.774 1.00 46.10 ? 788  ARG A NH2   1 
ATOM   5646  N N     . LEU A  1 791  ? -8.126  90.771  109.823 1.00 26.57 ? 789  LEU A N     1 
ATOM   5647  C CA    . LEU A  1 791  ? -8.090  91.624  111.010 1.00 29.61 ? 789  LEU A CA    1 
ATOM   5648  C C     . LEU A  1 791  ? -8.015  90.793  112.284 1.00 27.48 ? 789  LEU A C     1 
ATOM   5649  O O     . LEU A  1 791  ? -7.347  91.186  113.248 1.00 28.05 ? 789  LEU A O     1 
ATOM   5650  C CB    . LEU A  1 791  ? -9.313  92.537  111.047 1.00 31.07 ? 789  LEU A CB    1 
ATOM   5651  C CG    . LEU A  1 791  ? -9.359  93.667  110.018 1.00 34.82 ? 789  LEU A CG    1 
ATOM   5652  C CD1   . LEU A  1 791  ? -10.747 94.289  110.002 1.00 37.33 ? 789  LEU A CD1   1 
ATOM   5653  C CD2   . LEU A  1 791  ? -8.303  94.716  110.349 1.00 34.46 ? 789  LEU A CD2   1 
ATOM   5654  N N     . ILE A  1 792  ? -8.697  89.647  112.312 1.00 25.21 ? 790  ILE A N     1 
ATOM   5655  C CA    . ILE A  1 792  ? -8.617  88.771  113.475 1.00 26.78 ? 790  ILE A CA    1 
ATOM   5656  C C     . ILE A  1 792  ? -7.213  88.199  113.607 1.00 25.93 ? 790  ILE A C     1 
ATOM   5657  O O     . ILE A  1 792  ? -6.632  88.180  114.702 1.00 24.47 ? 790  ILE A O     1 
ATOM   5658  C CB    . ILE A  1 792  ? -9.685  87.664  113.390 1.00 25.79 ? 790  ILE A CB    1 
ATOM   5659  C CG1   . ILE A  1 792  ? -11.073 88.271  113.610 1.00 27.36 ? 790  ILE A CG1   1 
ATOM   5660  C CG2   . ILE A  1 792  ? -9.409  86.552  114.405 1.00 23.16 ? 790  ILE A CG2   1 
ATOM   5661  C CD1   . ILE A  1 792  ? -12.226 87.360  113.213 1.00 25.57 ? 790  ILE A CD1   1 
ATOM   5662  N N     . GLN A  1 793  ? -6.643  87.738  112.491 1.00 24.11 ? 791  GLN A N     1 
ATOM   5663  C CA    . GLN A  1 793  ? -5.280  87.213  112.506 1.00 25.50 ? 791  GLN A CA    1 
ATOM   5664  C C     . GLN A  1 793  ? -4.301  88.227  113.087 1.00 26.58 ? 791  GLN A C     1 
ATOM   5665  O O     . GLN A  1 793  ? -3.424  87.871  113.885 1.00 26.88 ? 791  GLN A O     1 
ATOM   5666  C CB    . GLN A  1 793  ? -4.875  86.820  111.089 1.00 27.92 ? 791  GLN A CB    1 
ATOM   5667  C CG    . GLN A  1 793  ? -3.391  86.536  110.897 1.00 31.47 ? 791  GLN A CG    1 
ATOM   5668  C CD    . GLN A  1 793  ? -2.985  86.648  109.434 1.00 39.20 ? 791  GLN A CD    1 
ATOM   5669  O OE1   . GLN A  1 793  ? -3.418  87.564  108.722 1.00 39.42 ? 791  GLN A OE1   1 
ATOM   5670  N NE2   . GLN A  1 793  ? -2.167  85.708  108.971 1.00 38.56 ? 791  GLN A NE2   1 
ATOM   5671  N N     . ALA A  1 794  ? -4.439  89.500  112.701 1.00 29.61 ? 792  ALA A N     1 
ATOM   5672  C CA    . ALA A  1 794  ? -3.524  90.522  113.207 1.00 29.60 ? 792  ALA A CA    1 
ATOM   5673  C C     . ALA A  1 794  ? -3.679  90.712  114.712 1.00 31.08 ? 792  ALA A C     1 
ATOM   5674  O O     . ALA A  1 794  ? -2.688  90.940  115.418 1.00 30.32 ? 792  ALA A O     1 
ATOM   5675  C CB    . ALA A  1 794  ? -3.751  91.843  112.471 1.00 33.64 ? 792  ALA A CB    1 
ATOM   5676  N N     . GLN A  1 795  ? -4.909  90.628  115.221 1.00 30.32 ? 793  GLN A N     1 
ATOM   5677  C CA    . GLN A  1 795  ? -5.114  90.754  116.661 1.00 29.98 ? 793  GLN A CA    1 
ATOM   5678  C C     . GLN A  1 795  ? -4.544  89.555  117.400 1.00 31.84 ? 793  GLN A C     1 
ATOM   5679  O O     . GLN A  1 795  ? -3.973  89.701  118.488 1.00 33.35 ? 793  GLN A O     1 
ATOM   5680  C CB    . GLN A  1 795  ? -6.603  90.907  116.976 1.00 35.19 ? 793  GLN A CB    1 
ATOM   5681  C CG    . GLN A  1 795  ? -7.186  92.258  116.603 1.00 40.08 ? 793  GLN A CG    1 
ATOM   5682  C CD    . GLN A  1 795  ? -6.461  93.398  117.292 1.00 47.47 ? 793  GLN A CD    1 
ATOM   5683  O OE1   . GLN A  1 795  ? -6.267  93.385  118.515 1.00 44.27 ? 793  GLN A OE1   1 
ATOM   5684  N NE2   . GLN A  1 795  ? -6.033  94.386  116.504 1.00 43.32 ? 793  GLN A NE2   1 
ATOM   5685  N N     . LEU A  1 796  ? -4.671  88.364  116.816 1.00 28.01 ? 794  LEU A N     1 
ATOM   5686  C CA    . LEU A  1 796  ? -4.188  87.163  117.488 1.00 28.82 ? 794  LEU A CA    1 
ATOM   5687  C C     . LEU A  1 796  ? -2.666  87.058  117.458 1.00 33.08 ? 794  LEU A C     1 
ATOM   5688  O O     . LEU A  1 796  ? -2.079  86.409  118.334 1.00 35.37 ? 794  LEU A O     1 
ATOM   5689  C CB    . LEU A  1 796  ? -4.806  85.919  116.845 1.00 28.29 ? 794  LEU A CB    1 
ATOM   5690  C CG    . LEU A  1 796  ? -6.310  85.722  117.020 1.00 26.14 ? 794  LEU A CG    1 
ATOM   5691  C CD1   . LEU A  1 796  ? -6.714  84.379  116.425 1.00 26.98 ? 794  LEU A CD1   1 
ATOM   5692  C CD2   . LEU A  1 796  ? -6.702  85.815  118.486 1.00 31.08 ? 794  LEU A CD2   1 
ATOM   5693  N N     . ALA A  1 797  ? -2.011  87.660  116.461 1.00 28.47 ? 795  ALA A N     1 
ATOM   5694  C CA    . ALA A  1 797  ? -0.561  87.526  116.352 1.00 33.65 ? 795  ALA A CA    1 
ATOM   5695  C C     . ALA A  1 797  ? 0.157   88.222  117.497 1.00 34.72 ? 795  ALA A C     1 
ATOM   5696  O O     . ALA A  1 797  ? 1.334   87.937  117.749 1.00 38.88 ? 795  ALA A O     1 
ATOM   5697  C CB    . ALA A  1 797  ? -0.070  88.082  115.017 1.00 29.41 ? 795  ALA A CB    1 
ATOM   5698  N N     . ASP A  1 798  ? -0.535  89.114  118.200 1.00 32.13 ? 796  ASP A N     1 
ATOM   5699  C CA    . ASP A  1 798  ? 0.023   89.792  119.360 1.00 35.16 ? 796  ASP A CA    1 
ATOM   5700  C C     . ASP A  1 798  ? 0.073   88.909  120.601 1.00 37.77 ? 796  ASP A C     1 
ATOM   5701  O O     . ASP A  1 798  ? 0.726   89.287  121.585 1.00 33.67 ? 796  ASP A O     1 
ATOM   5702  C CB    . ASP A  1 798  ? -0.804  91.045  119.646 1.00 33.07 ? 796  ASP A CB    1 
ATOM   5703  C CG    . ASP A  1 798  ? -0.100  92.005  120.580 1.00 42.94 ? 796  ASP A CG    1 
ATOM   5704  O OD1   . ASP A  1 798  ? 1.050   92.389  120.272 1.00 45.90 ? 796  ASP A OD1   1 
ATOM   5705  O OD2   . ASP A  1 798  ? -0.695  92.372  121.619 1.00 47.31 ? 796  ASP A OD2   1 
ATOM   5706  N N     . ARG A  1 799  ? -0.583  87.747  120.583 1.00 34.28 ? 797  ARG A N     1 
ATOM   5707  C CA    . ARG A  1 799  ? -0.783  86.950  121.784 1.00 36.94 ? 797  ARG A CA    1 
ATOM   5708  C C     . ARG A  1 799  ? -0.188  85.556  121.622 1.00 32.09 ? 797  ARG A C     1 
ATOM   5709  O O     . ARG A  1 799  ? -0.033  85.039  120.509 1.00 32.01 ? 797  ARG A O     1 
ATOM   5710  C CB    . ARG A  1 799  ? -2.283  86.838  122.133 1.00 41.30 ? 797  ARG A CB    1 
ATOM   5711  C CG    . ARG A  1 799  ? -3.030  88.173  122.175 1.00 41.49 ? 797  ARG A CG    1 
ATOM   5712  C CD    . ARG A  1 799  ? -4.204  88.158  123.170 1.00 38.81 ? 797  ARG A CD    1 
ATOM   5713  N NE    . ARG A  1 799  ? -5.424  87.577  122.621 1.00 44.30 ? 797  ARG A NE    1 
ATOM   5714  C CZ    . ARG A  1 799  ? -5.802  86.319  122.809 1.00 38.58 ? 797  ARG A CZ    1 
ATOM   5715  N NH1   . ARG A  1 799  ? -5.086  85.483  123.542 1.00 37.99 ? 797  ARG A NH1   1 
ATOM   5716  N NH2   . ARG A  1 799  ? -6.924  85.887  122.242 1.00 32.00 ? 797  ARG A NH2   1 
ATOM   5717  N N     . LEU A  1 800  ? 0.137   84.947  122.762 1.00 31.66 ? 798  LEU A N     1 
ATOM   5718  C CA    . LEU A  1 800  ? 0.578   83.563  122.815 1.00 31.18 ? 798  LEU A CA    1 
ATOM   5719  C C     . LEU A  1 800  ? -0.276  82.796  123.815 1.00 31.69 ? 798  LEU A C     1 
ATOM   5720  O O     . LEU A  1 800  ? -0.855  83.376  124.735 1.00 28.55 ? 798  LEU A O     1 
ATOM   5721  C CB    . LEU A  1 800  ? 2.064   83.459  123.207 1.00 32.80 ? 798  LEU A CB    1 
ATOM   5722  C CG    . LEU A  1 800  ? 3.085   83.903  122.159 1.00 33.06 ? 798  LEU A CG    1 
ATOM   5723  C CD1   . LEU A  1 800  ? 4.500   83.812  122.726 1.00 32.72 ? 798  LEU A CD1   1 
ATOM   5724  C CD2   . LEU A  1 800  ? 2.972   83.062  120.893 1.00 32.06 ? 798  LEU A CD2   1 
ATOM   5725  N N     . SER A  1 801  ? -0.345  81.484  123.628 1.00 31.72 ? 799  SER A N     1 
ATOM   5726  C CA    . SER A  1 801  ? -1.079  80.620  124.536 1.00 34.48 ? 799  SER A CA    1 
ATOM   5727  C C     . SER A  1 801  ? -0.329  80.541  125.859 1.00 42.85 ? 799  SER A C     1 
ATOM   5728  O O     . SER A  1 801  ? 0.828   80.960  125.950 1.00 39.04 ? 799  SER A O     1 
ATOM   5729  C CB    . SER A  1 801  ? -1.253  79.229  123.924 1.00 37.68 ? 799  SER A CB    1 
ATOM   5730  O OG    . SER A  1 801  ? -0.035  78.495  123.953 1.00 39.47 ? 799  SER A OG    1 
ATOM   5731  N N     . PRO A  1 802  ? -0.972  80.028  126.916 1.00 44.78 ? 800  PRO A N     1 
ATOM   5732  C CA    . PRO A  1 802  ? -0.231  79.779  128.164 1.00 43.07 ? 800  PRO A CA    1 
ATOM   5733  C C     . PRO A  1 802  ? 1.012   78.930  127.968 1.00 43.78 ? 800  PRO A C     1 
ATOM   5734  O O     . PRO A  1 802  ? 1.984   79.094  128.713 1.00 50.87 ? 800  PRO A O     1 
ATOM   5735  C CB    . PRO A  1 802  ? -1.267  79.073  129.046 1.00 45.04 ? 800  PRO A CB    1 
ATOM   5736  C CG    . PRO A  1 802  ? -2.584  79.586  128.553 1.00 46.52 ? 800  PRO A CG    1 
ATOM   5737  C CD    . PRO A  1 802  ? -2.420  79.794  127.073 1.00 41.33 ? 800  PRO A CD    1 
ATOM   5738  N N     . ALA A  1 803  ? 1.020   78.038  126.979 1.00 41.96 ? 801  ALA A N     1 
ATOM   5739  C CA    . ALA A  1 803  ? 2.181   77.212  126.682 1.00 42.09 ? 801  ALA A CA    1 
ATOM   5740  C C     . ALA A  1 803  ? 3.164   77.880  125.726 1.00 45.92 ? 801  ALA A C     1 
ATOM   5741  O O     . ALA A  1 803  ? 4.174   77.265  125.373 1.00 45.27 ? 801  ALA A O     1 
ATOM   5742  C CB    . ALA A  1 803  ? 1.738   75.864  126.104 1.00 43.52 ? 801  ALA A CB    1 
ATOM   5743  N N     . GLY A  1 804  ? 2.902   79.114  125.300 1.00 43.66 ? 802  GLY A N     1 
ATOM   5744  C CA    . GLY A  1 804  ? 3.824   79.822  124.434 1.00 36.45 ? 802  GLY A CA    1 
ATOM   5745  C C     . GLY A  1 804  ? 3.661   79.552  122.957 1.00 36.31 ? 802  GLY A C     1 
ATOM   5746  O O     . GLY A  1 804  ? 4.592   79.821  122.186 1.00 36.22 ? 802  GLY A O     1 
ATOM   5747  N N     . ARG A  1 805  ? 2.512   79.039  122.533 1.00 34.99 ? 803  ARG A N     1 
ATOM   5748  C CA    . ARG A  1 805  ? 2.228   78.764  121.138 1.00 34.99 ? 803  ARG A CA    1 
ATOM   5749  C C     . ARG A  1 805  ? 1.287   79.813  120.571 1.00 30.60 ? 803  ARG A C     1 
ATOM   5750  O O     . ARG A  1 805  ? 0.565   80.484  121.315 1.00 31.09 ? 803  ARG A O     1 
ATOM   5751  C CB    . ARG A  1 805  ? 1.593   77.378  120.977 1.00 35.62 ? 803  ARG A CB    1 
ATOM   5752  C CG    . ARG A  1 805  ? 2.456   76.241  121.461 1.00 39.11 ? 803  ARG A CG    1 
ATOM   5753  C CD    . ARG A  1 805  ? 2.067   74.916  120.820 1.00 39.08 ? 803  ARG A CD    1 
ATOM   5754  N NE    . ARG A  1 805  ? 2.869   73.841  121.389 1.00 50.62 ? 803  ARG A NE    1 
ATOM   5755  C CZ    . ARG A  1 805  ? 2.579   73.225  122.527 1.00 54.84 ? 803  ARG A CZ    1 
ATOM   5756  N NH1   . ARG A  1 805  ? 1.459   73.485  123.186 1.00 51.92 ? 803  ARG A NH1   1 
ATOM   5757  N NH2   . ARG A  1 805  ? 3.433   72.330  123.017 1.00 53.63 ? 803  ARG A NH2   1 
ATOM   5758  N N     . PRO A  1 806  ? 1.275   79.986  119.250 1.00 27.88 ? 804  PRO A N     1 
ATOM   5759  C CA    . PRO A  1 806  ? 0.274   80.866  118.635 1.00 30.19 ? 804  PRO A CA    1 
ATOM   5760  C C     . PRO A  1 806  ? -1.138  80.411  118.972 1.00 32.34 ? 804  PRO A C     1 
ATOM   5761  O O     . PRO A  1 806  ? -1.393  79.221  119.183 1.00 27.14 ? 804  PRO A O     1 
ATOM   5762  C CB    . PRO A  1 806  ? 0.559   80.731  117.135 1.00 28.66 ? 804  PRO A CB    1 
ATOM   5763  C CG    . PRO A  1 806  ? 2.021   80.375  117.064 1.00 31.78 ? 804  PRO A CG    1 
ATOM   5764  C CD    . PRO A  1 806  ? 2.253   79.487  118.268 1.00 31.58 ? 804  PRO A CD    1 
ATOM   5765  N N     . ILE A  1 807  ? -2.054  81.379  119.037 1.00 28.50 ? 805  ILE A N     1 
ATOM   5766  C CA    . ILE A  1 807  ? -3.477  81.098  119.237 1.00 29.07 ? 805  ILE A CA    1 
ATOM   5767  C C     . ILE A  1 807  ? -4.036  80.527  117.941 1.00 26.86 ? 805  ILE A C     1 
ATOM   5768  O O     . ILE A  1 807  ? -3.967  81.190  116.894 1.00 26.05 ? 805  ILE A O     1 
ATOM   5769  C CB    . ILE A  1 807  ? -4.272  82.344  119.661 1.00 26.09 ? 805  ILE A CB    1 
ATOM   5770  C CG1   . ILE A  1 807  ? -3.617  83.023  120.865 1.00 31.63 ? 805  ILE A CG1   1 
ATOM   5771  C CG2   . ILE A  1 807  ? -5.696  81.947  120.031 1.00 25.35 ? 805  ILE A CG2   1 
ATOM   5772  C CD1   . ILE A  1 807  ? -3.486  82.118  122.062 1.00 31.20 ? 805  ILE A CD1   1 
ATOM   5773  N N     . PRO A  1 808  ? -4.579  79.310  117.957 1.00 28.07 ? 806  PRO A N     1 
ATOM   5774  C CA    . PRO A  1 808  ? -5.102  78.723  116.720 1.00 26.62 ? 806  PRO A CA    1 
ATOM   5775  C C     . PRO A  1 808  ? -6.271  79.530  116.185 1.00 24.50 ? 806  PRO A C     1 
ATOM   5776  O O     . PRO A  1 808  ? -7.186  79.898  116.923 1.00 23.34 ? 806  PRO A O     1 
ATOM   5777  C CB    . PRO A  1 808  ? -5.544  77.318  117.150 1.00 25.66 ? 806  PRO A CB    1 
ATOM   5778  C CG    . PRO A  1 808  ? -4.756  77.026  118.373 1.00 28.78 ? 806  PRO A CG    1 
ATOM   5779  C CD    . PRO A  1 808  ? -4.605  78.351  119.075 1.00 27.31 ? 806  PRO A CD    1 
ATOM   5780  N N     . LEU A  1 809  ? -6.251  79.769  114.878 1.00 27.23 ? 807  LEU A N     1 
ATOM   5781  C CA    . LEU A  1 809  ? -7.362  80.381  114.174 1.00 22.90 ? 807  LEU A CA    1 
ATOM   5782  C C     . LEU A  1 809  ? -7.759  79.458  113.035 1.00 22.25 ? 807  LEU A C     1 
ATOM   5783  O O     . LEU A  1 809  ? -6.915  79.098  112.207 1.00 21.42 ? 807  LEU A O     1 
ATOM   5784  C CB    . LEU A  1 809  ? -6.976  81.757  113.637 1.00 26.42 ? 807  LEU A CB    1 
ATOM   5785  C CG    . LEU A  1 809  ? -7.906  82.362  112.586 1.00 23.87 ? 807  LEU A CG    1 
ATOM   5786  C CD1   . LEU A  1 809  ? -9.210  82.890  113.210 1.00 23.92 ? 807  LEU A CD1   1 
ATOM   5787  C CD2   . LEU A  1 809  ? -7.163  83.461  111.867 1.00 28.72 ? 807  LEU A CD2   1 
ATOM   5788  N N     . ILE A  1 810  ? -9.026  79.052  113.023 1.00 21.59 ? 808  ILE A N     1 
ATOM   5789  C CA    . ILE A  1 810  ? -9.627  78.345  111.905 1.00 23.08 ? 808  ILE A CA    1 
ATOM   5790  C C     . ILE A  1 810  ? -10.513 79.357  111.214 1.00 21.50 ? 808  ILE A C     1 
ATOM   5791  O O     . ILE A  1 810  ? -11.545 79.758  111.766 1.00 23.37 ? 808  ILE A O     1 
ATOM   5792  C CB    . ILE A  1 810  ? -10.455 77.131  112.337 1.00 22.35 ? 808  ILE A CB    1 
ATOM   5793  C CG1   . ILE A  1 810  ? -9.664  76.176  113.210 1.00 24.66 ? 808  ILE A CG1   1 
ATOM   5794  C CG2   . ILE A  1 810  ? -10.961 76.394  111.115 1.00 23.77 ? 808  ILE A CG2   1 
ATOM   5795  C CD1   . ILE A  1 810  ? -10.511 74.987  113.614 1.00 25.70 ? 808  ILE A CD1   1 
ATOM   5796  N N     . ALA A  1 811  ? -10.120 79.754  110.009 1.00 25.50 ? 809  ALA A N     1 
ATOM   5797  C CA    . ALA A  1 811  ? -10.791 80.803  109.260 1.00 23.43 ? 809  ALA A CA    1 
ATOM   5798  C C     . ALA A  1 811  ? -11.190 80.233  107.916 1.00 23.51 ? 809  ALA A C     1 
ATOM   5799  O O     . ALA A  1 811  ? -10.329 79.798  107.143 1.00 25.62 ? 809  ALA A O     1 
ATOM   5800  C CB    . ALA A  1 811  ? -9.898  82.027  109.078 1.00 25.40 ? 809  ALA A CB    1 
ATOM   5801  N N     . GLU A  1 812  ? -12.492 80.221  107.659 1.00 23.03 ? 810  GLU A N     1 
ATOM   5802  C CA    . GLU A  1 812  ? -13.052 79.765  106.399 1.00 25.48 ? 810  GLU A CA    1 
ATOM   5803  C C     . GLU A  1 812  ? -13.610 80.996  105.697 1.00 25.18 ? 810  GLU A C     1 
ATOM   5804  O O     . GLU A  1 812  ? -14.462 81.703  106.249 1.00 23.11 ? 810  GLU A O     1 
ATOM   5805  C CB    . GLU A  1 812  ? -14.133 78.706  106.622 1.00 27.74 ? 810  GLU A CB    1 
ATOM   5806  N N     . THR A  1 813  ? -13.098 81.276  104.503 1.00 26.81 ? 811  THR A N     1 
ATOM   5807  C CA    . THR A  1 813  ? -13.375 82.559  103.882 1.00 25.59 ? 811  THR A CA    1 
ATOM   5808  C C     . THR A  1 813  ? -13.920 82.332  102.475 1.00 26.72 ? 811  THR A C     1 
ATOM   5809  O O     . THR A  1 813  ? -14.316 81.212  102.137 1.00 27.87 ? 811  THR A O     1 
ATOM   5810  C CB    . THR A  1 813  ? -12.112 83.439  103.913 1.00 32.64 ? 811  THR A CB    1 
ATOM   5811  O OG1   . THR A  1 813  ? -10.966 82.703  103.446 1.00 29.55 ? 811  THR A OG1   1 
ATOM   5812  C CG2   . THR A  1 813  ? -11.819 83.927  105.346 1.00 29.89 ? 811  THR A CG2   1 
ATOM   5813  N N     . GLY A  1 814  ? -13.963 83.368  101.650 1.00 32.06 ? 812  GLY A N     1 
ATOM   5814  C CA    . GLY A  1 814  ? -14.681 83.258  100.399 1.00 34.99 ? 812  GLY A CA    1 
ATOM   5815  C C     . GLY A  1 814  ? -13.955 82.398  99.378  1.00 36.28 ? 812  GLY A C     1 
ATOM   5816  O O     . GLY A  1 814  ? -12.951 81.734  99.648  1.00 33.65 ? 812  GLY A O     1 
ATOM   5817  N N     . GLY A  1 815  ? -14.518 82.393  98.175  1.00 25.22 ? 813  GLY A N     1 
ATOM   5818  C CA    . GLY A  1 815  ? -13.830 81.861  97.017  1.00 29.54 ? 813  GLY A CA    1 
ATOM   5819  C C     . GLY A  1 815  ? -14.319 82.566  95.771  1.00 26.90 ? 813  GLY A C     1 
ATOM   5820  O O     . GLY A  1 815  ? -15.403 83.150  95.746  1.00 29.47 ? 813  GLY A O     1 
ATOM   5821  N N     . GLN A  1 816  ? -13.493 82.517  94.738  1.00 24.89 ? 814  GLN A N     1 
ATOM   5822  C CA    . GLN A  1 816  ? -13.870 82.980  93.407  1.00 25.04 ? 814  GLN A CA    1 
ATOM   5823  C C     . GLN A  1 816  ? -14.080 81.747  92.537  1.00 22.72 ? 814  GLN A C     1 
ATOM   5824  O O     . GLN A  1 816  ? -13.277 81.433  91.651  1.00 22.75 ? 814  GLN A O     1 
ATOM   5825  C CB    . GLN A  1 816  ? -12.798 83.893  92.837  1.00 27.70 ? 814  GLN A CB    1 
ATOM   5826  C CG    . GLN A  1 816  ? -13.227 84.652  91.604  1.00 27.98 ? 814  GLN A CG    1 
ATOM   5827  C CD    . GLN A  1 816  ? -14.182 85.771  91.947  1.00 38.30 ? 814  GLN A CD    1 
ATOM   5828  O OE1   . GLN A  1 816  ? -15.378 85.540  92.159  1.00 34.79 ? 814  GLN A OE1   1 
ATOM   5829  N NE2   . GLN A  1 816  ? -13.660 86.997  92.014  1.00 36.62 ? 814  GLN A NE2   1 
ATOM   5830  N N     . ASN A  1 817  ? -15.168 81.035  92.817  1.00 24.13 ? 815  ASN A N     1 
ATOM   5831  C CA    . ASN A  1 817  ? -15.299 79.651  92.375  1.00 18.75 ? 815  ASN A CA    1 
ATOM   5832  C C     . ASN A  1 817  ? -15.654 79.581  90.902  1.00 20.63 ? 815  ASN A C     1 
ATOM   5833  O O     . ASN A  1 817  ? -16.486 80.349  90.415  1.00 22.72 ? 815  ASN A O     1 
ATOM   5834  C CB    . ASN A  1 817  ? -16.352 78.942  93.209  1.00 18.56 ? 815  ASN A CB    1 
ATOM   5835  C CG    . ASN A  1 817  ? -16.140 79.182  94.677  1.00 21.09 ? 815  ASN A CG    1 
ATOM   5836  O OD1   . ASN A  1 817  ? -15.039 78.975  95.182  1.00 20.29 ? 815  ASN A OD1   1 
ATOM   5837  N ND2   . ASN A  1 817  ? -17.160 79.670  95.353  1.00 19.59 ? 815  ASN A ND2   1 
ATOM   5838  N N     . ALA A  1 818  ? -15.014 78.648  90.202  1.00 20.45 ? 816  ALA A N     1 
ATOM   5839  C CA    . ALA A  1 818  ? -15.135 78.531  88.761  1.00 20.90 ? 816  ALA A CA    1 
ATOM   5840  C C     . ALA A  1 818  ? -15.648 77.155  88.383  1.00 18.40 ? 816  ALA A C     1 
ATOM   5841  O O     . ALA A  1 818  ? -15.528 76.183  89.129  1.00 19.40 ? 816  ALA A O     1 
ATOM   5842  C CB    . ALA A  1 818  ? -13.792 78.788  88.057  1.00 23.09 ? 816  ALA A CB    1 
ATOM   5843  N N     . MET A  1 819  ? -16.238 77.093  87.197  1.00 18.38 ? 817  MET A N     1 
ATOM   5844  C CA    . MET A  1 819  ? -16.590 75.842  86.561  1.00 18.39 ? 817  MET A CA    1 
ATOM   5845  C C     . MET A  1 819  ? -16.058 75.887  85.140  1.00 18.35 ? 817  MET A C     1 
ATOM   5846  O O     . MET A  1 819  ? -16.245 76.891  84.446  1.00 22.91 ? 817  MET A O     1 
ATOM   5847  C CB    . MET A  1 819  ? -18.107 75.636  86.527  1.00 18.05 ? 817  MET A CB    1 
ATOM   5848  C CG    . MET A  1 819  ? -18.501 74.309  85.931  1.00 22.62 ? 817  MET A CG    1 
ATOM   5849  S SD    . MET A  1 819  ? -20.285 74.172  85.778  1.00 24.94 ? 817  MET A SD    1 
ATOM   5850  C CE    . MET A  1 819  ? -20.730 73.888  87.486  1.00 23.15 ? 817  MET A CE    1 
ATOM   5851  N N     . ILE A  1 820  ? -15.412 74.811  84.709  1.00 18.80 ? 818  ILE A N     1 
ATOM   5852  C CA    . ILE A  1 820  ? -14.949 74.678  83.333  1.00 19.12 ? 818  ILE A CA    1 
ATOM   5853  C C     . ILE A  1 820  ? -15.822 73.653  82.626  1.00 18.59 ? 818  ILE A C     1 
ATOM   5854  O O     . ILE A  1 820  ? -16.027 72.543  83.127  1.00 18.15 ? 818  ILE A O     1 
ATOM   5855  C CB    . ILE A  1 820  ? -13.464 74.287  83.265  1.00 21.23 ? 818  ILE A CB    1 
ATOM   5856  C CG1   . ILE A  1 820  ? -12.607 75.368  83.936  1.00 21.27 ? 818  ILE A CG1   1 
ATOM   5857  C CG2   . ILE A  1 820  ? -13.051 74.076  81.816  1.00 20.60 ? 818  ILE A CG2   1 
ATOM   5858  C CD1   . ILE A  1 820  ? -11.101 75.155  83.809  1.00 23.26 ? 818  ILE A CD1   1 
ATOM   5859  N N     . VAL A  1 821  ? -16.323 74.023  81.448  1.00 18.42 ? 819  VAL A N     1 
ATOM   5860  C CA    . VAL A  1 821  ? -17.224 73.189  80.669  1.00 20.94 ? 819  VAL A CA    1 
ATOM   5861  C C     . VAL A  1 821  ? -16.617 73.048  79.286  1.00 21.89 ? 819  VAL A C     1 
ATOM   5862  O O     . VAL A  1 821  ? -16.377 74.059  78.617  1.00 20.77 ? 819  VAL A O     1 
ATOM   5863  C CB    . VAL A  1 821  ? -18.631 73.804  80.561  1.00 21.67 ? 819  VAL A CB    1 
ATOM   5864  C CG1   . VAL A  1 821  ? -19.501 72.985  79.605  1.00 18.61 ? 819  VAL A CG1   1 
ATOM   5865  C CG2   . VAL A  1 821  ? -19.273 73.925  81.942  1.00 19.96 ? 819  VAL A CG2   1 
ATOM   5866  N N     . ASP A  1 822  ? -16.392 71.811  78.840  1.00 21.79 ? 820  ASP A N     1 
ATOM   5867  C CA    . ASP A  1 822  ? -15.868 71.628  77.496  1.00 21.99 ? 820  ASP A CA    1 
ATOM   5868  C C     . ASP A  1 822  ? -16.990 71.188  76.548  1.00 25.68 ? 820  ASP A C     1 
ATOM   5869  O O     . ASP A  1 822  ? -18.151 71.042  76.932  1.00 20.77 ? 820  ASP A O     1 
ATOM   5870  C CB    . ASP A  1 822  ? -14.675 70.663  77.496  1.00 21.68 ? 820  ASP A CB    1 
ATOM   5871  C CG    . ASP A  1 822  ? -15.063 69.195  77.720  1.00 22.58 ? 820  ASP A CG    1 
ATOM   5872  O OD1   . ASP A  1 822  ? -16.237 68.822  77.559  1.00 22.34 ? 820  ASP A OD1   1 
ATOM   5873  O OD2   . ASP A  1 822  ? -14.147 68.395  78.037  1.00 23.77 ? 820  ASP A OD2   1 
ATOM   5874  N N     . SER A  1 823  ? -16.623 70.960  75.289  1.00 21.50 ? 821  SER A N     1 
ATOM   5875  C CA    . SER A  1 823  ? -17.618 70.642  74.271  1.00 22.54 ? 821  SER A CA    1 
ATOM   5876  C C     . SER A  1 823  ? -18.191 69.232  74.402  1.00 24.09 ? 821  SER A C     1 
ATOM   5877  O O     . SER A  1 823  ? -19.079 68.872  73.623  1.00 26.09 ? 821  SER A O     1 
ATOM   5878  C CB    . SER A  1 823  ? -17.001 70.831  72.875  1.00 26.02 ? 821  SER A CB    1 
ATOM   5879  O OG    . SER A  1 823  ? -15.895 69.966  72.703  1.00 26.11 ? 821  SER A OG    1 
ATOM   5880  N N     . SER A  1 824  ? -17.699 68.411  75.327  1.00 24.82 ? 822  SER A N     1 
ATOM   5881  C CA    . SER A  1 824  ? -18.267 67.079  75.501  1.00 21.50 ? 822  SER A CA    1 
ATOM   5882  C C     . SER A  1 824  ? -19.377 67.036  76.545  1.00 25.93 ? 822  SER A C     1 
ATOM   5883  O O     . SER A  1 824  ? -20.055 66.012  76.666  1.00 24.17 ? 822  SER A O     1 
ATOM   5884  C CB    . SER A  1 824  ? -17.177 66.080  75.885  1.00 23.51 ? 822  SER A CB    1 
ATOM   5885  O OG    . SER A  1 824  ? -16.809 66.275  77.239  1.00 21.55 ? 822  SER A OG    1 
ATOM   5886  N N     . ALA A  1 825  ? -19.567 68.111  77.303  1.00 22.17 ? 823  ALA A N     1 
ATOM   5887  C CA    . ALA A  1 825  ? -20.558 68.134  78.366  1.00 23.05 ? 823  ALA A CA    1 
ATOM   5888  C C     . ALA A  1 825  ? -21.972 68.253  77.798  1.00 21.97 ? 823  ALA A C     1 
ATOM   5889  O O     . ALA A  1 825  ? -22.186 68.803  76.718  1.00 25.47 ? 823  ALA A O     1 
ATOM   5890  C CB    . ALA A  1 825  ? -20.268 69.298  79.318  1.00 22.21 ? 823  ALA A CB    1 
ATOM   5891  N N     . LEU A  1 826  ? -22.945 67.717  78.533  1.00 25.97 ? 824  LEU A N     1 
ATOM   5892  C CA    . LEU A  1 826  ? -24.346 67.804  78.126  1.00 29.34 ? 824  LEU A CA    1 
ATOM   5893  C C     . LEU A  1 826  ? -24.907 69.156  78.557  1.00 29.82 ? 824  LEU A C     1 
ATOM   5894  O O     . LEU A  1 826  ? -25.010 69.442  79.759  1.00 24.79 ? 824  LEU A O     1 
ATOM   5895  C CB    . LEU A  1 826  ? -25.154 66.657  78.729  1.00 33.66 ? 824  LEU A CB    1 
ATOM   5896  C CG    . LEU A  1 826  ? -26.649 66.562  78.394  1.00 38.11 ? 824  LEU A CG    1 
ATOM   5897  C CD1   . LEU A  1 826  ? -26.864 66.557  76.891  1.00 38.83 ? 824  LEU A CD1   1 
ATOM   5898  C CD2   . LEU A  1 826  ? -27.255 65.311  79.013  1.00 43.19 ? 824  LEU A CD2   1 
ATOM   5899  N N     . ALA A  1 827  ? -25.267 69.982  77.570  1.00 25.53 ? 825  ALA A N     1 
ATOM   5900  C CA    . ALA A  1 827  ? -25.692 71.355  77.830  1.00 25.41 ? 825  ALA A CA    1 
ATOM   5901  C C     . ALA A  1 827  ? -26.798 71.429  78.877  1.00 28.40 ? 825  ALA A C     1 
ATOM   5902  O O     . ALA A  1 827  ? -26.750 72.275  79.782  1.00 25.80 ? 825  ALA A O     1 
ATOM   5903  C CB    . ALA A  1 827  ? -26.152 72.007  76.520  1.00 28.41 ? 825  ALA A CB    1 
ATOM   5904  N N     . GLU A  1 828  ? -27.802 70.551  78.778  1.00 25.65 ? 826  GLU A N     1 
ATOM   5905  C CA    . GLU A  1 828  ? -28.930 70.621  79.706  1.00 27.57 ? 826  GLU A CA    1 
ATOM   5906  C C     . GLU A  1 828  ? -28.490 70.354  81.138  1.00 26.70 ? 826  GLU A C     1 
ATOM   5907  O O     . GLU A  1 828  ? -28.973 70.998  82.076  1.00 25.57 ? 826  GLU A O     1 
ATOM   5908  C CB    . GLU A  1 828  ? -30.020 69.631  79.302  1.00 30.40 ? 826  GLU A CB    1 
ATOM   5909  C CG    . GLU A  1 828  ? -30.806 70.014  78.052  1.00 35.46 ? 826  GLU A CG    1 
ATOM   5910  C CD    . GLU A  1 828  ? -30.078 69.699  76.747  1.00 37.82 ? 826  GLU A CD    1 
ATOM   5911  O OE1   . GLU A  1 828  ? -28.938 69.188  76.783  1.00 34.92 ? 826  GLU A OE1   1 
ATOM   5912  O OE2   . GLU A  1 828  ? -30.655 69.969  75.669  1.00 47.63 ? 826  GLU A OE2   1 
ATOM   5913  N N     . GLN A  1 829  ? -27.587 69.393  81.326  1.00 26.89 ? 827  GLN A N     1 
ATOM   5914  C CA    . GLN A  1 829  ? -27.052 69.111  82.657  1.00 28.28 ? 827  GLN A CA    1 
ATOM   5915  C C     . GLN A  1 829  ? -26.189 70.263  83.156  1.00 23.73 ? 827  GLN A C     1 
ATOM   5916  O O     . GLN A  1 829  ? -26.264 70.647  84.330  1.00 26.81 ? 827  GLN A O     1 
ATOM   5917  C CB    . GLN A  1 829  ? -26.261 67.803  82.604  1.00 25.14 ? 827  GLN A CB    1 
ATOM   5918  C CG    . GLN A  1 829  ? -25.528 67.421  83.859  1.00 33.21 ? 827  GLN A CG    1 
ATOM   5919  C CD    . GLN A  1 829  ? -24.738 66.124  83.683  1.00 36.92 ? 827  GLN A CD    1 
ATOM   5920  O OE1   . GLN A  1 829  ? -24.536 65.654  82.560  1.00 39.66 ? 827  GLN A OE1   1 
ATOM   5921  N NE2   . GLN A  1 829  ? -24.301 65.539  84.794  1.00 43.59 ? 827  GLN A NE2   1 
ATOM   5922  N N     . VAL A  1 830  ? -25.360 70.822  82.275  1.00 24.94 ? 828  VAL A N     1 
ATOM   5923  C CA    . VAL A  1 830  ? -24.547 71.989  82.623  1.00 24.62 ? 828  VAL A CA    1 
ATOM   5924  C C     . VAL A  1 830  ? -25.432 73.143  83.085  1.00 21.23 ? 828  VAL A C     1 
ATOM   5925  O O     . VAL A  1 830  ? -25.138 73.818  84.075  1.00 20.92 ? 828  VAL A O     1 
ATOM   5926  C CB    . VAL A  1 830  ? -23.686 72.408  81.420  1.00 21.60 ? 828  VAL A CB    1 
ATOM   5927  C CG1   . VAL A  1 830  ? -23.106 73.809  81.631  1.00 22.67 ? 828  VAL A CG1   1 
ATOM   5928  C CG2   . VAL A  1 830  ? -22.584 71.371  81.135  1.00 22.32 ? 828  VAL A CG2   1 
ATOM   5929  N N     . VAL A  1 831  ? -26.502 73.424  82.341  1.00 20.53 ? 829  VAL A N     1 
ATOM   5930  C CA    . VAL A  1 831  ? -27.315 74.592  82.668  1.00 20.83 ? 829  VAL A CA    1 
ATOM   5931  C C     . VAL A  1 831  ? -27.981 74.421  84.028  1.00 21.74 ? 829  VAL A C     1 
ATOM   5932  O O     . VAL A  1 831  ? -27.994 75.353  84.844  1.00 20.92 ? 829  VAL A O     1 
ATOM   5933  C CB    . VAL A  1 831  ? -28.336 74.853  81.546  1.00 20.43 ? 829  VAL A CB    1 
ATOM   5934  C CG1   . VAL A  1 831  ? -29.389 75.884  81.990  1.00 23.47 ? 829  VAL A CG1   1 
ATOM   5935  C CG2   . VAL A  1 831  ? -27.599 75.321  80.297  1.00 21.57 ? 829  VAL A CG2   1 
ATOM   5936  N N     . GLY A  1 832  ? -28.489 73.222  84.322  1.00 17.89 ? 830  GLY A N     1 
ATOM   5937  C CA    . GLY A  1 832  ? -29.111 73.005  85.619  1.00 19.11 ? 830  GLY A CA    1 
ATOM   5938  C C     . GLY A  1 832  ? -28.107 73.127  86.754  1.00 20.79 ? 830  GLY A C     1 
ATOM   5939  O O     . GLY A  1 832  ? -28.393 73.726  87.797  1.00 18.69 ? 830  GLY A O     1 
ATOM   5940  N N     . ASP A  1 833  ? -26.905 72.604  86.546  1.00 17.26 ? 831  ASP A N     1 
ATOM   5941  C CA    . ASP A  1 833  ? -25.874 72.707  87.585  1.00 17.72 ? 831  ASP A CA    1 
ATOM   5942  C C     . ASP A  1 833  ? -25.363 74.130  87.735  1.00 19.00 ? 831  ASP A C     1 
ATOM   5943  O O     . ASP A  1 833  ? -24.986 74.541  88.841  1.00 20.27 ? 831  ASP A O     1 
ATOM   5944  C CB    . ASP A  1 833  ? -24.736 71.743  87.262  1.00 18.67 ? 831  ASP A CB    1 
ATOM   5945  C CG    . ASP A  1 833  ? -25.166 70.290  87.390  1.00 22.35 ? 831  ASP A CG    1 
ATOM   5946  O OD1   . ASP A  1 833  ? -26.194 70.053  88.058  1.00 21.53 ? 831  ASP A OD1   1 
ATOM   5947  O OD2   . ASP A  1 833  ? -24.502 69.399  86.821  1.00 24.65 ? 831  ASP A OD2   1 
ATOM   5948  N N     . VAL A  1 834  ? -25.353 74.900  86.644  1.00 18.32 ? 832  VAL A N     1 
ATOM   5949  C CA    . VAL A  1 834  ? -24.898 76.286  86.707  1.00 20.27 ? 832  VAL A CA    1 
ATOM   5950  C C     . VAL A  1 834  ? -25.940 77.170  87.393  1.00 21.70 ? 832  VAL A C     1 
ATOM   5951  O O     . VAL A  1 834  ? -25.611 77.977  88.270  1.00 17.86 ? 832  VAL A O     1 
ATOM   5952  C CB    . VAL A  1 834  ? -24.579 76.804  85.291  1.00 19.22 ? 832  VAL A CB    1 
ATOM   5953  C CG1   . VAL A  1 834  ? -24.505 78.295  85.304  1.00 18.79 ? 832  VAL A CG1   1 
ATOM   5954  C CG2   . VAL A  1 834  ? -23.256 76.199  84.765  1.00 19.12 ? 832  VAL A CG2   1 
ATOM   5955  N N     . ILE A  1 835  ? -27.204 77.063  86.968  1.00 19.57 ? 833  ILE A N     1 
ATOM   5956  C CA    . ILE A  1 835  ? -28.291 77.832  87.579  1.00 21.46 ? 833  ILE A CA    1 
ATOM   5957  C C     . ILE A  1 835  ? -28.318 77.611  89.080  1.00 22.20 ? 833  ILE A C     1 
ATOM   5958  O O     . ILE A  1 835  ? -28.373 78.561  89.870  1.00 19.53 ? 833  ILE A O     1 
ATOM   5959  C CB    . ILE A  1 835  ? -29.645 77.455  86.945  1.00 24.10 ? 833  ILE A CB    1 
ATOM   5960  C CG1   . ILE A  1 835  ? -29.765 78.045  85.537  1.00 24.06 ? 833  ILE A CG1   1 
ATOM   5961  C CG2   . ILE A  1 835  ? -30.805 77.881  87.857  1.00 23.00 ? 833  ILE A CG2   1 
ATOM   5962  C CD1   . ILE A  1 835  ? -29.762 79.553  85.501  1.00 23.76 ? 833  ILE A CD1   1 
ATOM   5963  N N     . THR A  1 836  ? -28.270 76.348  89.492  1.00 19.55 ? 834  THR A N     1 
ATOM   5964  C CA    . THR A  1 836  ? -28.253 76.026  90.912  1.00 21.72 ? 834  THR A CA    1 
ATOM   5965  C C     . THR A  1 836  ? -26.995 76.560  91.602  1.00 21.03 ? 834  THR A C     1 
ATOM   5966  O O     . THR A  1 836  ? -27.082 77.152  92.684  1.00 20.82 ? 834  THR A O     1 
ATOM   5967  C CB    . THR A  1 836  ? -28.356 74.507  91.085  1.00 19.20 ? 834  THR A CB    1 
ATOM   5968  O OG1   . THR A  1 836  ? -29.649 74.063  90.673  1.00 24.89 ? 834  THR A OG1   1 
ATOM   5969  C CG2   . THR A  1 836  ? -28.133 74.115  92.518  1.00 21.77 ? 834  THR A CG2   1 
ATOM   5970  N N     . SER A  1 837  ? -25.807 76.339  91.010  1.00 17.64 ? 835  SER A N     1 
ATOM   5971  C CA    . SER A  1 837  ? -24.572 76.703  91.723  1.00 17.74 ? 835  SER A CA    1 
ATOM   5972  C C     . SER A  1 837  ? -24.412 78.211  91.852  1.00 19.95 ? 835  SER A C     1 
ATOM   5973  O O     . SER A  1 837  ? -23.847 78.694  92.839  1.00 18.91 ? 835  SER A O     1 
ATOM   5974  C CB    . SER A  1 837  ? -23.337 76.136  91.021  1.00 17.71 ? 835  SER A CB    1 
ATOM   5975  O OG    . SER A  1 837  ? -23.341 74.710  90.990  1.00 18.57 ? 835  SER A OG    1 
ATOM   5976  N N     . ALA A  1 838  ? -24.881 78.971  90.869  1.00 18.03 ? 836  ALA A N     1 
ATOM   5977  C CA    . ALA A  1 838  ? -24.694 80.417  90.911  1.00 18.63 ? 836  ALA A CA    1 
ATOM   5978  C C     . ALA A  1 838  ? -25.795 81.138  91.676  1.00 18.38 ? 836  ALA A C     1 
ATOM   5979  O O     . ALA A  1 838  ? -25.528 82.145  92.333  1.00 21.26 ? 836  ALA A O     1 
ATOM   5980  C CB    . ALA A  1 838  ? -24.607 80.974  89.486  1.00 20.22 ? 836  ALA A CB    1 
ATOM   5981  N N     . PHE A  1 839  ? -27.047 80.676  91.588  1.00 18.52 ? 837  PHE A N     1 
ATOM   5982  C CA    . PHE A  1 839  ? -28.149 81.500  92.056  1.00 19.52 ? 837  PHE A CA    1 
ATOM   5983  C C     . PHE A  1 839  ? -28.891 80.928  93.248  1.00 20.36 ? 837  PHE A C     1 
ATOM   5984  O O     . PHE A  1 839  ? -29.651 81.666  93.888  1.00 19.83 ? 837  PHE A O     1 
ATOM   5985  C CB    . PHE A  1 839  ? -29.116 81.758  90.892  1.00 21.28 ? 837  PHE A CB    1 
ATOM   5986  C CG    . PHE A  1 839  ? -28.442 82.395  89.704  1.00 24.15 ? 837  PHE A CG    1 
ATOM   5987  C CD1   . PHE A  1 839  ? -27.690 83.548  89.860  1.00 22.84 ? 837  PHE A CD1   1 
ATOM   5988  C CD2   . PHE A  1 839  ? -28.531 81.827  88.442  1.00 23.50 ? 837  PHE A CD2   1 
ATOM   5989  C CE1   . PHE A  1 839  ? -27.043 84.139  88.773  1.00 20.18 ? 837  PHE A CE1   1 
ATOM   5990  C CE2   . PHE A  1 839  ? -27.890 82.403  87.363  1.00 20.47 ? 837  PHE A CE2   1 
ATOM   5991  C CZ    . PHE A  1 839  ? -27.152 83.568  87.521  1.00 24.80 ? 837  PHE A CZ    1 
ATOM   5992  N N     . ASP A  1 840  ? -28.665 79.657  93.595  1.00 20.57 ? 838  ASP A N     1 
ATOM   5993  C CA    . ASP A  1 840  ? -29.240 79.116  94.814  1.00 20.56 ? 838  ASP A CA    1 
ATOM   5994  C C     . ASP A  1 840  ? -28.841 79.977  96.000  1.00 21.25 ? 838  ASP A C     1 
ATOM   5995  O O     . ASP A  1 840  ? -27.697 80.421  96.092  1.00 20.70 ? 838  ASP A O     1 
ATOM   5996  C CB    . ASP A  1 840  ? -28.769 77.683  95.034  1.00 23.13 ? 838  ASP A CB    1 
ATOM   5997  C CG    . ASP A  1 840  ? -29.245 77.113  96.338  1.00 29.72 ? 838  ASP A CG    1 
ATOM   5998  O OD1   . ASP A  1 840  ? -28.619 77.399  97.386  1.00 30.01 ? 838  ASP A OD1   1 
ATOM   5999  O OD2   . ASP A  1 840  ? -30.250 76.378  96.312  1.00 30.92 ? 838  ASP A OD2   1 
ATOM   6000  N N     . SER A  1 841  ? -29.804 80.234  96.892  1.00 18.50 ? 839  SER A N     1 
ATOM   6001  C CA    . SER A  1 841  ? -29.571 81.050  98.080  1.00 21.41 ? 839  SER A CA    1 
ATOM   6002  C C     . SER A  1 841  ? -29.104 82.449  97.699  1.00 20.52 ? 839  SER A C     1 
ATOM   6003  O O     . SER A  1 841  ? -28.321 83.080  98.419  1.00 25.13 ? 839  SER A O     1 
ATOM   6004  C CB    . SER A  1 841  ? -28.563 80.383  99.025  1.00 23.27 ? 839  SER A CB    1 
ATOM   6005  O OG    . SER A  1 841  ? -28.998 79.090  99.400  1.00 24.06 ? 839  SER A OG    1 
ATOM   6006  N N     . ALA A  1 842  ? -29.560 82.924  96.542  1.00 19.46 ? 840  ALA A N     1 
ATOM   6007  C CA    . ALA A  1 842  ? -29.194 84.242  96.017  1.00 19.20 ? 840  ALA A CA    1 
ATOM   6008  C C     . ALA A  1 842  ? -27.681 84.396  95.872  1.00 20.65 ? 840  ALA A C     1 
ATOM   6009  O O     . ALA A  1 842  ? -27.147 85.491  96.035  1.00 23.93 ? 840  ALA A O     1 
ATOM   6010  C CB    . ALA A  1 842  ? -29.768 85.373  96.887  1.00 20.07 ? 840  ALA A CB    1 
ATOM   6011  N N     . GLY A  1 843  ? -26.987 83.300  95.553  1.00 19.40 ? 841  GLY A N     1 
ATOM   6012  C CA    . GLY A  1 843  ? -25.550 83.327  95.392  1.00 20.15 ? 841  GLY A CA    1 
ATOM   6013  C C     . GLY A  1 843  ? -24.796 83.606  96.670  1.00 20.70 ? 841  GLY A C     1 
ATOM   6014  O O     . GLY A  1 843  ? -23.601 83.902  96.626  1.00 21.51 ? 841  GLY A O     1 
ATOM   6015  N N     . GLN A  1 844  ? -25.461 83.523  97.814  1.00 19.96 ? 842  GLN A N     1 
ATOM   6016  C CA    . GLN A  1 844  ? -24.810 83.810  99.085  1.00 22.15 ? 842  GLN A CA    1 
ATOM   6017  C C     . GLN A  1 844  ? -24.202 82.567  99.723  1.00 25.00 ? 842  GLN A C     1 
ATOM   6018  O O     . GLN A  1 844  ? -24.124 82.485  100.955 1.00 30.74 ? 842  GLN A O     1 
ATOM   6019  C CB    . GLN A  1 844  ? -25.802 84.498  100.028 1.00 21.76 ? 842  GLN A CB    1 
ATOM   6020  C CG    . GLN A  1 844  ? -26.324 85.853  99.486  1.00 21.90 ? 842  GLN A CG    1 
ATOM   6021  C CD    . GLN A  1 844  ? -27.392 86.483  100.371 1.00 24.04 ? 842  GLN A CD    1 
ATOM   6022  O OE1   . GLN A  1 844  ? -27.357 87.688  100.648 1.00 23.66 ? 842  GLN A OE1   1 
ATOM   6023  N NE2   . GLN A  1 844  ? -28.329 85.664  100.848 1.00 24.93 ? 842  GLN A NE2   1 
ATOM   6024  N N     . ARG A  1 845  ? -23.765 81.596  98.922  1.00 26.62 ? 843  ARG A N     1 
ATOM   6025  C CA    . ARG A  1 845  ? -22.947 80.498  99.413  1.00 24.75 ? 843  ARG A CA    1 
ATOM   6026  C C     . ARG A  1 845  ? -21.480 80.812  99.178  1.00 22.08 ? 843  ARG A C     1 
ATOM   6027  O O     . ARG A  1 845  ? -21.110 81.387  98.149  1.00 24.94 ? 843  ARG A O     1 
ATOM   6028  C CB    . ARG A  1 845  ? -23.291 79.175  98.731  1.00 24.88 ? 843  ARG A CB    1 
ATOM   6029  C CG    . ARG A  1 845  ? -24.666 78.649  99.057  1.00 27.97 ? 843  ARG A CG    1 
ATOM   6030  C CD    . ARG A  1 845  ? -24.903 77.362  98.309  1.00 27.99 ? 843  ARG A CD    1 
ATOM   6031  N NE    . ARG A  1 845  ? -26.235 76.836  98.550  1.00 31.01 ? 843  ARG A NE    1 
ATOM   6032  C CZ    . ARG A  1 845  ? -26.514 75.864  99.407  1.00 30.56 ? 843  ARG A CZ    1 
ATOM   6033  N NH1   . ARG A  1 845  ? -25.568 75.293  100.145 1.00 31.44 ? 843  ARG A NH1   1 
ATOM   6034  N NH2   . ARG A  1 845  ? -27.768 75.442  99.515  1.00 33.49 ? 843  ARG A NH2   1 
ATOM   6035  N N     . CYS A  1 846  ? -20.641 80.435  100.144 1.00 21.89 ? 844  CYS A N     1 
ATOM   6036  C CA    . CYS A  1 846  ? -19.207 80.563  99.945  1.00 23.94 ? 844  CYS A CA    1 
ATOM   6037  C C     . CYS A  1 846  ? -18.747 79.748  98.740  1.00 20.97 ? 844  CYS A C     1 
ATOM   6038  O O     . CYS A  1 846  ? -17.803 80.137  98.052  1.00 24.68 ? 844  CYS A O     1 
ATOM   6039  C CB    . CYS A  1 846  ? -18.459 80.116  101.212 1.00 27.04 ? 844  CYS A CB    1 
ATOM   6040  S SG    . CYS A  1 846  ? -18.928 81.065  102.695 1.00 51.13 ? 844  CYS A SG    1 
ATOM   6041  N N     . SER A  1 847  ? -19.419 78.633  98.469  1.00 22.38 ? 845  SER A N     1 
ATOM   6042  C CA    . SER A  1 847  ? -19.146 77.744  97.344  1.00 20.42 ? 845  SER A CA    1 
ATOM   6043  C C     . SER A  1 847  ? -19.802 78.175  96.033  1.00 22.97 ? 845  SER A C     1 
ATOM   6044  O O     . SER A  1 847  ? -19.638 77.469  95.030  1.00 18.71 ? 845  SER A O     1 
ATOM   6045  C CB    . SER A  1 847  ? -19.644 76.353  97.691  1.00 25.48 ? 845  SER A CB    1 
ATOM   6046  O OG    . SER A  1 847  ? -20.974 76.459  98.161  1.00 29.00 ? 845  SER A OG    1 
ATOM   6047  N N     . ALA A  1 848  ? -20.545 79.279  96.020  1.00 19.64 ? 846  ALA A N     1 
ATOM   6048  C CA    . ALA A  1 848  ? -21.354 79.622  94.853  1.00 21.33 ? 846  ALA A CA    1 
ATOM   6049  C C     . ALA A  1 848  ? -20.478 79.804  93.621  1.00 20.45 ? 846  ALA A C     1 
ATOM   6050  O O     . ALA A  1 848  ? -19.336 80.253  93.698  1.00 20.66 ? 846  ALA A O     1 
ATOM   6051  C CB    . ALA A  1 848  ? -22.168 80.903  95.105  1.00 19.41 ? 846  ALA A CB    1 
ATOM   6052  N N     . LEU A  1 849  ? -21.035 79.449  92.468  1.00 18.64 ? 847  LEU A N     1 
ATOM   6053  C CA    . LEU A  1 849  ? -20.303 79.541  91.216  1.00 18.56 ? 847  LEU A CA    1 
ATOM   6054  C C     . LEU A  1 849  ? -20.218 80.999  90.804  1.00 20.54 ? 847  LEU A C     1 
ATOM   6055  O O     . LEU A  1 849  ? -21.249 81.653  90.603  1.00 24.43 ? 847  LEU A O     1 
ATOM   6056  C CB    . LEU A  1 849  ? -21.007 78.725  90.134  1.00 18.18 ? 847  LEU A CB    1 
ATOM   6057  C CG    . LEU A  1 849  ? -20.450 78.897  88.722  1.00 18.25 ? 847  LEU A CG    1 
ATOM   6058  C CD1   . LEU A  1 849  ? -19.008 78.388  88.591  1.00 18.28 ? 847  LEU A CD1   1 
ATOM   6059  C CD2   . LEU A  1 849  ? -21.386 78.203  87.724  1.00 18.11 ? 847  LEU A CD2   1 
ATOM   6060  N N     . ARG A  1 850  ? -19.000 81.513  90.701  1.00 19.25 ? 848  ARG A N     1 
ATOM   6061  C CA    . ARG A  1 850  ? -18.789 82.906  90.332  1.00 20.50 ? 848  ARG A CA    1 
ATOM   6062  C C     . ARG A  1 850  ? -18.355 83.088  88.886  1.00 20.27 ? 848  ARG A C     1 
ATOM   6063  O O     . ARG A  1 850  ? -18.656 84.126  88.295  1.00 21.48 ? 848  ARG A O     1 
ATOM   6064  C CB    . ARG A  1 850  ? -17.734 83.543  91.237  1.00 23.39 ? 848  ARG A CB    1 
ATOM   6065  C CG    . ARG A  1 850  ? -18.010 83.324  92.712  1.00 23.38 ? 848  ARG A CG    1 
ATOM   6066  C CD    . ARG A  1 850  ? -19.342 83.944  93.093  1.00 22.06 ? 848  ARG A CD    1 
ATOM   6067  N NE    . ARG A  1 850  ? -19.542 83.911  94.536  1.00 23.92 ? 848  ARG A NE    1 
ATOM   6068  C CZ    . ARG A  1 850  ? -20.706 84.116  95.133  1.00 24.74 ? 848  ARG A CZ    1 
ATOM   6069  N NH1   . ARG A  1 850  ? -21.811 84.381  94.435  1.00 19.83 ? 848  ARG A NH1   1 
ATOM   6070  N NH2   . ARG A  1 850  ? -20.770 84.052  96.461  1.00 22.53 ? 848  ARG A NH2   1 
ATOM   6071  N N     . VAL A  1 851  ? -17.622 82.133  88.318  1.00 19.06 ? 849  VAL A N     1 
ATOM   6072  C CA    . VAL A  1 851  ? -17.086 82.277  86.969  1.00 22.35 ? 849  VAL A CA    1 
ATOM   6073  C C     . VAL A  1 851  ? -17.315 80.978  86.218  1.00 21.46 ? 849  VAL A C     1 
ATOM   6074  O O     . VAL A  1 851  ? -16.786 79.930  86.604  1.00 19.31 ? 849  VAL A O     1 
ATOM   6075  C CB    . VAL A  1 851  ? -15.592 82.632  86.938  1.00 23.19 ? 849  VAL A CB    1 
ATOM   6076  C CG1   . VAL A  1 851  ? -15.179 82.959  85.499  1.00 23.47 ? 849  VAL A CG1   1 
ATOM   6077  C CG2   . VAL A  1 851  ? -15.296 83.806  87.827  1.00 23.48 ? 849  VAL A CG2   1 
ATOM   6078  N N     . LEU A  1 852  ? -18.093 81.050  85.142  1.00 20.16 ? 850  LEU A N     1 
ATOM   6079  C CA    . LEU A  1 852  ? -18.311 79.926  84.246  1.00 20.12 ? 850  LEU A CA    1 
ATOM   6080  C C     . LEU A  1 852  ? -17.429 80.080  83.011  1.00 19.36 ? 850  LEU A C     1 
ATOM   6081  O O     . LEU A  1 852  ? -17.453 81.126  82.354  1.00 19.37 ? 850  LEU A O     1 
ATOM   6082  C CB    . LEU A  1 852  ? -19.786 79.850  83.842  1.00 18.99 ? 850  LEU A CB    1 
ATOM   6083  C CG    . LEU A  1 852  ? -20.151 78.713  82.900  1.00 19.49 ? 850  LEU A CG    1 
ATOM   6084  C CD1   . LEU A  1 852  ? -19.894 77.340  83.511  1.00 18.31 ? 850  LEU A CD1   1 
ATOM   6085  C CD2   . LEU A  1 852  ? -21.621 78.869  82.522  1.00 19.40 ? 850  LEU A CD2   1 
ATOM   6086  N N     . CYS A  1 853  ? -16.663 79.041  82.696  1.00 18.94 ? 851  CYS A N     1 
ATOM   6087  C CA    . CYS A  1 853  ? -15.717 79.063  81.580  1.00 19.40 ? 851  CYS A CA    1 
ATOM   6088  C C     . CYS A  1 853  ? -16.207 78.065  80.542  1.00 22.03 ? 851  CYS A C     1 
ATOM   6089  O O     . CYS A  1 853  ? -16.235 76.856  80.799  1.00 19.99 ? 851  CYS A O     1 
ATOM   6090  C CB    . CYS A  1 853  ? -14.300 78.727  82.030  1.00 21.11 ? 851  CYS A CB    1 
ATOM   6091  S SG    . CYS A  1 853  ? -13.755 79.578  83.518  1.00 26.82 ? 851  CYS A SG    1 
ATOM   6092  N N     . LEU A  1 854  ? -16.606 78.570  79.380  1.00 21.94 ? 852  LEU A N     1 
ATOM   6093  C CA    . LEU A  1 854  ? -17.246 77.757  78.360  1.00 21.98 ? 852  LEU A CA    1 
ATOM   6094  C C     . LEU A  1 854  ? -16.310 77.594  77.174  1.00 20.20 ? 852  LEU A C     1 
ATOM   6095  O O     . LEU A  1 854  ? -15.808 78.585  76.638  1.00 20.86 ? 852  LEU A O     1 
ATOM   6096  C CB    . LEU A  1 854  ? -18.564 78.391  77.893  1.00 21.57 ? 852  LEU A CB    1 
ATOM   6097  C CG    . LEU A  1 854  ? -19.671 78.491  78.952  1.00 25.17 ? 852  LEU A CG    1 
ATOM   6098  C CD1   . LEU A  1 854  ? -20.940 79.167  78.392  1.00 19.51 ? 852  LEU A CD1   1 
ATOM   6099  C CD2   . LEU A  1 854  ? -20.000 77.109  79.541  1.00 22.67 ? 852  LEU A CD2   1 
ATOM   6100  N N     . GLN A  1 855  ? -16.103 76.355  76.744  1.00 20.36 ? 853  GLN A N     1 
ATOM   6101  C CA    . GLN A  1 855  ? -15.311 76.155  75.539  1.00 21.57 ? 853  GLN A CA    1 
ATOM   6102  C C     . GLN A  1 855  ? -16.009 76.840  74.375  1.00 21.73 ? 853  GLN A C     1 
ATOM   6103  O O     . GLN A  1 855  ? -17.235 76.783  74.249  1.00 22.66 ? 853  GLN A O     1 
ATOM   6104  C CB    . GLN A  1 855  ? -15.114 74.674  75.231  1.00 21.80 ? 853  GLN A CB    1 
ATOM   6105  C CG    . GLN A  1 855  ? -14.067 74.459  74.158  1.00 22.67 ? 853  GLN A CG    1 
ATOM   6106  C CD    . GLN A  1 855  ? -13.918 73.011  73.752  1.00 27.78 ? 853  GLN A CD    1 
ATOM   6107  O OE1   . GLN A  1 855  ? -13.928 72.111  74.591  1.00 29.59 ? 853  GLN A OE1   1 
ATOM   6108  N NE2   . GLN A  1 855  ? -13.769 72.778  72.456  1.00 26.74 ? 853  GLN A NE2   1 
ATOM   6109  N N     . GLU A  1 856  ? -15.208 77.500  73.546  1.00 23.36 ? 854  GLU A N     1 
ATOM   6110  C CA    . GLU A  1 856  ? -15.742 78.443  72.571  1.00 29.53 ? 854  GLU A CA    1 
ATOM   6111  C C     . GLU A  1 856  ? -16.737 77.779  71.629  1.00 30.29 ? 854  GLU A C     1 
ATOM   6112  O O     . GLU A  1 856  ? -17.730 78.407  71.235  1.00 30.93 ? 854  GLU A O     1 
ATOM   6113  C CB    . GLU A  1 856  ? -14.587 79.087  71.794  1.00 29.05 ? 854  GLU A CB    1 
ATOM   6114  C CG    . GLU A  1 856  ? -15.032 79.996  70.650  1.00 37.11 ? 854  GLU A CG    1 
ATOM   6115  C CD    . GLU A  1 856  ? -15.753 81.242  71.141  1.00 39.88 ? 854  GLU A CD    1 
ATOM   6116  O OE1   . GLU A  1 856  ? -15.433 81.711  72.256  1.00 40.94 ? 854  GLU A OE1   1 
ATOM   6117  O OE2   . GLU A  1 856  ? -16.653 81.744  70.427  1.00 39.56 ? 854  GLU A OE2   1 
ATOM   6118  N N     . ASP A  1 857  ? -16.505 76.511  71.270  1.00 26.86 ? 855  ASP A N     1 
ATOM   6119  C CA    . ASP A  1 857  ? -17.368 75.854  70.289  1.00 27.41 ? 855  ASP A CA    1 
ATOM   6120  C C     . ASP A  1 857  ? -18.798 75.690  70.792  1.00 28.95 ? 855  ASP A C     1 
ATOM   6121  O O     . ASP A  1 857  ? -19.728 75.622  69.979  1.00 32.18 ? 855  ASP A O     1 
ATOM   6122  C CB    . ASP A  1 857  ? -16.795 74.487  69.905  1.00 34.72 ? 855  ASP A CB    1 
ATOM   6123  N N     . VAL A  1 858  ? -19.006 75.612  72.112  1.00 24.00 ? 856  VAL A N     1 
ATOM   6124  C CA    . VAL A  1 858  ? -20.341 75.407  72.660  1.00 23.14 ? 856  VAL A CA    1 
ATOM   6125  C C     . VAL A  1 858  ? -20.825 76.602  73.471  1.00 24.77 ? 856  VAL A C     1 
ATOM   6126  O O     . VAL A  1 858  ? -21.906 76.544  74.059  1.00 26.35 ? 856  VAL A O     1 
ATOM   6127  C CB    . VAL A  1 858  ? -20.412 74.122  73.511  1.00 27.90 ? 856  VAL A CB    1 
ATOM   6128  C CG1   . VAL A  1 858  ? -20.225 72.870  72.632  1.00 26.27 ? 856  VAL A CG1   1 
ATOM   6129  C CG2   . VAL A  1 858  ? -19.363 74.166  74.627  1.00 24.26 ? 856  VAL A CG2   1 
ATOM   6130  N N     . ALA A  1 859  ? -20.045 77.682  73.516  1.00 26.67 ? 857  ALA A N     1 
ATOM   6131  C CA    . ALA A  1 859  ? -20.357 78.792  74.413  1.00 25.82 ? 857  ALA A CA    1 
ATOM   6132  C C     . ALA A  1 859  ? -21.693 79.439  74.063  1.00 27.97 ? 857  ALA A C     1 
ATOM   6133  O O     . ALA A  1 859  ? -22.504 79.720  74.949  1.00 27.51 ? 857  ALA A O     1 
ATOM   6134  C CB    . ALA A  1 859  ? -19.235 79.828  74.374  1.00 25.13 ? 857  ALA A CB    1 
ATOM   6135  N N     . ASP A  1 860  ? -21.935 79.700  72.774  1.00 25.89 ? 858  ASP A N     1 
ATOM   6136  C CA    . ASP A  1 860  ? -23.151 80.415  72.394  1.00 27.71 ? 858  ASP A CA    1 
ATOM   6137  C C     . ASP A  1 860  ? -24.393 79.597  72.717  1.00 25.52 ? 858  ASP A C     1 
ATOM   6138  O O     . ASP A  1 860  ? -25.362 80.122  73.278  1.00 26.60 ? 858  ASP A O     1 
ATOM   6139  C CB    . ASP A  1 860  ? -23.110 80.780  70.907  1.00 29.45 ? 858  ASP A CB    1 
ATOM   6140  C CG    . ASP A  1 860  ? -22.199 81.965  70.619  1.00 36.32 ? 858  ASP A CG    1 
ATOM   6141  O OD1   . ASP A  1 860  ? -22.094 82.869  71.473  1.00 40.67 ? 858  ASP A OD1   1 
ATOM   6142  O OD2   . ASP A  1 860  ? -21.585 81.990  69.534  1.00 43.17 ? 858  ASP A OD2   1 
ATOM   6143  N N     . ARG A  1 861  ? -24.361 78.296  72.421  1.00 24.77 ? 859  ARG A N     1 
ATOM   6144  C CA    . ARG A  1 861  ? -25.504 77.432  72.683  1.00 26.09 ? 859  ARG A CA    1 
ATOM   6145  C C     . ARG A  1 861  ? -25.803 77.335  74.176  1.00 25.91 ? 859  ARG A C     1 
ATOM   6146  O O     . ARG A  1 861  ? -26.963 77.409  74.603  1.00 24.42 ? 859  ARG A O     1 
ATOM   6147  C CB    . ARG A  1 861  ? -25.242 76.041  72.094  1.00 28.91 ? 859  ARG A CB    1 
ATOM   6148  C CG    . ARG A  1 861  ? -26.217 74.994  72.569  1.00 34.64 ? 859  ARG A CG    1 
ATOM   6149  C CD    . ARG A  1 861  ? -26.528 73.979  71.483  1.00 45.72 ? 859  ARG A CD    1 
ATOM   6150  N NE    . ARG A  1 861  ? -27.624 73.102  71.881  1.00 51.20 ? 859  ARG A NE    1 
ATOM   6151  C CZ    . ARG A  1 861  ? -27.482 72.030  72.650  1.00 46.59 ? 859  ARG A CZ    1 
ATOM   6152  N NH1   . ARG A  1 861  ? -26.299 71.671  73.124  1.00 48.49 ? 859  ARG A NH1   1 
ATOM   6153  N NH2   . ARG A  1 861  ? -28.553 71.303  72.954  1.00 45.56 ? 859  ARG A NH2   1 
ATOM   6154  N N     . ILE A  1 862  ? -24.765 77.152  74.986  1.00 21.82 ? 860  ILE A N     1 
ATOM   6155  C CA    . ILE A  1 862  ? -24.975 77.041  76.423  1.00 22.34 ? 860  ILE A CA    1 
ATOM   6156  C C     . ILE A  1 862  ? -25.421 78.380  77.007  1.00 19.86 ? 860  ILE A C     1 
ATOM   6157  O O     . ILE A  1 862  ? -26.326 78.432  77.851  1.00 21.84 ? 860  ILE A O     1 
ATOM   6158  C CB    . ILE A  1 862  ? -23.691 76.508  77.082  1.00 22.98 ? 860  ILE A CB    1 
ATOM   6159  C CG1   . ILE A  1 862  ? -23.475 75.044  76.672  1.00 25.57 ? 860  ILE A CG1   1 
ATOM   6160  C CG2   . ILE A  1 862  ? -23.769 76.655  78.571  1.00 24.29 ? 860  ILE A CG2   1 
ATOM   6161  C CD1   . ILE A  1 862  ? -22.226 74.403  77.242  1.00 27.53 ? 860  ILE A CD1   1 
ATOM   6162  N N     . LEU A  1 863  ? -24.831 79.484  76.543  1.00 22.15 ? 861  LEU A N     1 
ATOM   6163  C CA    . LEU A  1 863  ? -25.237 80.797  77.046  1.00 23.11 ? 861  LEU A CA    1 
ATOM   6164  C C     . LEU A  1 863  ? -26.708 81.071  76.752  1.00 21.88 ? 861  LEU A C     1 
ATOM   6165  O O     . LEU A  1 863  ? -27.430 81.580  77.609  1.00 20.14 ? 861  LEU A O     1 
ATOM   6166  C CB    . LEU A  1 863  ? -24.370 81.899  76.444  1.00 25.12 ? 861  LEU A CB    1 
ATOM   6167  C CG    . LEU A  1 863  ? -23.352 82.588  77.352  1.00 35.24 ? 861  LEU A CG    1 
ATOM   6168  C CD1   . LEU A  1 863  ? -22.515 83.557  76.527  1.00 33.97 ? 861  LEU A CD1   1 
ATOM   6169  C CD2   . LEU A  1 863  ? -24.032 83.309  78.523  1.00 29.04 ? 861  LEU A CD2   1 
ATOM   6170  N N     . THR A  1 864  ? -27.162 80.756  75.537  1.00 22.03 ? 862  THR A N     1 
ATOM   6171  C CA    . THR A  1 864  ? -28.563 80.975  75.189  1.00 22.82 ? 862  THR A CA    1 
ATOM   6172  C C     . THR A  1 864  ? -29.482 80.182  76.102  1.00 19.56 ? 862  THR A C     1 
ATOM   6173  O O     . THR A  1 864  ? -30.492 80.699  76.588  1.00 21.44 ? 862  THR A O     1 
ATOM   6174  C CB    . THR A  1 864  ? -28.789 80.593  73.723  1.00 24.28 ? 862  THR A CB    1 
ATOM   6175  O OG1   . THR A  1 864  ? -28.091 81.525  72.888  1.00 25.79 ? 862  THR A OG1   1 
ATOM   6176  C CG2   . THR A  1 864  ? -30.283 80.594  73.375  1.00 28.55 ? 862  THR A CG2   1 
ATOM   6177  N N     . MET A  1 865  ? -29.135 78.922  76.355  1.00 21.31 ? 863  MET A N     1 
ATOM   6178  C CA    . MET A  1 865  ? -29.920 78.092  77.253  1.00 21.89 ? 863  MET A CA    1 
ATOM   6179  C C     . MET A  1 865  ? -29.863 78.626  78.677  1.00 20.43 ? 863  MET A C     1 
ATOM   6180  O O     . MET A  1 865  ? -30.877 78.641  79.378  1.00 20.35 ? 863  MET A O     1 
ATOM   6181  C CB    . MET A  1 865  ? -29.409 76.653  77.178  1.00 22.40 ? 863  MET A CB    1 
ATOM   6182  C CG    . MET A  1 865  ? -30.276 75.616  77.895  1.00 27.54 ? 863  MET A CG    1 
ATOM   6183  S SD    . MET A  1 865  ? -29.677 73.928  77.548  1.00 41.53 ? 863  MET A SD    1 
ATOM   6184  C CE    . MET A  1 865  ? -29.085 74.173  75.878  1.00 25.78 ? 863  MET A CE    1 
ATOM   6185  N N     . LEU A  1 866  ? -28.687 79.095  79.103  1.00 21.25 ? 864  LEU A N     1 
ATOM   6186  C CA    A LEU A  1 866  ? -28.546 79.646  80.449  0.55 19.97 ? 864  LEU A CA    1 
ATOM   6187  C CA    B LEU A  1 866  ? -28.534 79.662  80.444  0.45 20.44 ? 864  LEU A CA    1 
ATOM   6188  C C     . LEU A  1 866  ? -29.432 80.873  80.646  1.00 21.00 ? 864  LEU A C     1 
ATOM   6189  O O     . LEU A  1 866  ? -30.080 81.022  81.690  1.00 18.93 ? 864  LEU A O     1 
ATOM   6190  C CB    A LEU A  1 866  ? -27.084 79.996  80.712  0.55 21.03 ? 864  LEU A CB    1 
ATOM   6191  C CB    B LEU A  1 866  ? -27.087 80.072  80.670  0.45 20.11 ? 864  LEU A CB    1 
ATOM   6192  C CG    A LEU A  1 866  ? -26.793 80.358  82.162  0.55 22.03 ? 864  LEU A CG    1 
ATOM   6193  C CG    B LEU A  1 866  ? -26.091 79.018  81.098  0.45 20.53 ? 864  LEU A CG    1 
ATOM   6194  C CD1   A LEU A  1 866  ? -27.147 79.173  83.037  0.55 20.55 ? 864  LEU A CD1   1 
ATOM   6195  C CD1   B LEU A  1 866  ? -24.816 79.738  81.385  0.45 20.47 ? 864  LEU A CD1   1 
ATOM   6196  C CD2   A LEU A  1 866  ? -25.331 80.729  82.329  0.55 18.79 ? 864  LEU A CD2   1 
ATOM   6197  C CD2   B LEU A  1 866  ? -26.611 78.303  82.332  0.45 20.12 ? 864  LEU A CD2   1 
ATOM   6198  N N     . LYS A  1 867  ? -29.436 81.783  79.672  1.00 19.01 ? 865  LYS A N     1 
ATOM   6199  C CA    . LYS A  1 867  ? -30.283 82.964  79.777  1.00 21.37 ? 865  LYS A CA    1 
ATOM   6200  C C     . LYS A  1 867  ? -31.755 82.577  79.811  1.00 21.03 ? 865  LYS A C     1 
ATOM   6201  O O     . LYS A  1 867  ? -32.522 83.110  80.616  1.00 20.70 ? 865  LYS A O     1 
ATOM   6202  C CB    . LYS A  1 867  ? -29.994 83.921  78.616  1.00 20.90 ? 865  LYS A CB    1 
ATOM   6203  C CG    . LYS A  1 867  ? -28.572 84.476  78.651  1.00 23.08 ? 865  LYS A CG    1 
ATOM   6204  C CD    . LYS A  1 867  ? -28.293 85.392  77.474  1.00 27.81 ? 865  LYS A CD    1 
ATOM   6205  C CE    . LYS A  1 867  ? -26.867 85.930  77.530  1.00 33.60 ? 865  LYS A CE    1 
ATOM   6206  N NZ    . LYS A  1 867  ? -26.445 86.589  76.247  1.00 34.76 ? 865  LYS A NZ    1 
ATOM   6207  N N     . GLY A  1 868  ? -32.163 81.627  78.964  1.00 20.68 ? 866  GLY A N     1 
ATOM   6208  C CA    . GLY A  1 868  ? -33.544 81.176  79.006  1.00 21.81 ? 866  GLY A CA    1 
ATOM   6209  C C     . GLY A  1 868  ? -33.919 80.566  80.343  1.00 19.65 ? 866  GLY A C     1 
ATOM   6210  O O     . GLY A  1 868  ? -35.016 80.804  80.861  1.00 22.62 ? 866  GLY A O     1 
ATOM   6211  N N     . ALA A  1 869  ? -33.014 79.765  80.923  1.00 19.61 ? 867  ALA A N     1 
ATOM   6212  C CA    . ALA A  1 869  ? -33.275 79.178  82.233  1.00 20.20 ? 867  ALA A CA    1 
ATOM   6213  C C     . ALA A  1 869  ? -33.326 80.248  83.317  1.00 20.68 ? 867  ALA A C     1 
ATOM   6214  O O     . ALA A  1 869  ? -34.106 80.141  84.271  1.00 20.14 ? 867  ALA A O     1 
ATOM   6215  C CB    . ALA A  1 869  ? -32.200 78.142  82.566  1.00 19.42 ? 867  ALA A CB    1 
ATOM   6216  N N     . LEU A  1 870  ? -32.465 81.257  83.209  1.00 21.78 ? 868  LEU A N     1 
ATOM   6217  C CA    . LEU A  1 870  ? -32.461 82.351  84.176  1.00 24.05 ? 868  LEU A CA    1 
ATOM   6218  C C     . LEU A  1 870  ? -33.849 82.970  84.301  1.00 21.51 ? 868  LEU A C     1 
ATOM   6219  O O     . LEU A  1 870  ? -34.310 83.271  85.402  1.00 20.14 ? 868  LEU A O     1 
ATOM   6220  C CB    . LEU A  1 870  ? -31.429 83.410  83.748  1.00 21.76 ? 868  LEU A CB    1 
ATOM   6221  C CG    . LEU A  1 870  ? -31.201 84.623  84.653  1.00 22.59 ? 868  LEU A CG    1 
ATOM   6222  C CD1   . LEU A  1 870  ? -30.149 84.306  85.704  1.00 23.11 ? 868  LEU A CD1   1 
ATOM   6223  C CD2   . LEU A  1 870  ? -30.799 85.860  83.865  1.00 23.08 ? 868  LEU A CD2   1 
ATOM   6224  N N     . HIS A  1 871  ? -34.542 83.145  83.178  1.00 20.54 ? 869  HIS A N     1 
ATOM   6225  C CA    . HIS A  1 871  ? -35.811 83.855  83.208  1.00 22.54 ? 869  HIS A CA    1 
ATOM   6226  C C     . HIS A  1 871  ? -36.974 83.000  83.703  1.00 24.36 ? 869  HIS A C     1 
ATOM   6227  O O     . HIS A  1 871  ? -38.073 83.529  83.871  1.00 21.73 ? 869  HIS A O     1 
ATOM   6228  C CB    . HIS A  1 871  ? -36.091 84.446  81.823  1.00 19.61 ? 869  HIS A CB    1 
ATOM   6229  C CG    . HIS A  1 871  ? -35.203 85.604  81.488  1.00 21.53 ? 869  HIS A CG    1 
ATOM   6230  N ND1   . HIS A  1 871  ? -35.363 86.852  82.055  1.00 25.54 ? 869  HIS A ND1   1 
ATOM   6231  C CD2   . HIS A  1 871  ? -34.126 85.698  80.672  1.00 21.41 ? 869  HIS A CD2   1 
ATOM   6232  C CE1   . HIS A  1 871  ? -34.428 87.667  81.594  1.00 29.88 ? 869  HIS A CE1   1 
ATOM   6233  N NE2   . HIS A  1 871  ? -33.664 86.992  80.752  1.00 25.46 ? 869  HIS A NE2   1 
ATOM   6234  N N     . GLU A  1 872  ? -36.753 81.719  84.000  1.00 24.13 ? 870  GLU A N     1 
ATOM   6235  C CA    . GLU A  1 872  ? -37.783 80.877  84.591  1.00 23.56 ? 870  GLU A CA    1 
ATOM   6236  C C     . GLU A  1 872  ? -37.747 80.874  86.114  1.00 23.35 ? 870  GLU A C     1 
ATOM   6237  O O     . GLU A  1 872  ? -38.579 80.203  86.738  1.00 24.64 ? 870  GLU A O     1 
ATOM   6238  C CB    . GLU A  1 872  ? -37.654 79.443  84.062  1.00 21.40 ? 870  GLU A CB    1 
ATOM   6239  C CG    . GLU A  1 872  ? -37.817 79.362  82.545  1.00 22.23 ? 870  GLU A CG    1 
ATOM   6240  C CD    . GLU A  1 872  ? -39.203 79.799  82.098  1.00 27.15 ? 870  GLU A CD    1 
ATOM   6241  O OE1   . GLU A  1 872  ? -40.144 79.721  82.918  1.00 27.69 ? 870  GLU A OE1   1 
ATOM   6242  O OE2   . GLU A  1 872  ? -39.349 80.220  80.930  1.00 27.08 ? 870  GLU A OE2   1 
ATOM   6243  N N     . LEU A  1 873  ? -36.822 81.616  86.726  1.00 23.25 ? 871  LEU A N     1 
ATOM   6244  C CA    . LEU A  1 873  ? -36.699 81.617  88.180  1.00 22.63 ? 871  LEU A CA    1 
ATOM   6245  C C     . LEU A  1 873  ? -37.713 82.563  88.804  1.00 22.88 ? 871  LEU A C     1 
ATOM   6246  O O     . LEU A  1 873  ? -37.958 83.659  88.290  1.00 23.96 ? 871  LEU A O     1 
ATOM   6247  C CB    . LEU A  1 873  ? -35.289 82.038  88.600  1.00 21.00 ? 871  LEU A CB    1 
ATOM   6248  C CG    . LEU A  1 873  ? -34.160 81.159  88.059  1.00 23.76 ? 871  LEU A CG    1 
ATOM   6249  C CD1   . LEU A  1 873  ? -32.795 81.742  88.408  1.00 24.27 ? 871  LEU A CD1   1 
ATOM   6250  C CD2   . LEU A  1 873  ? -34.317 79.766  88.626  1.00 27.52 ? 871  LEU A CD2   1 
ATOM   6251  N N     . HIS A  1 874  ? -38.280 82.146  89.939  1.00 21.41 ? 872  HIS A N     1 
ATOM   6252  C CA    . HIS A  1 874  ? -39.233 82.949  90.698  1.00 21.89 ? 872  HIS A CA    1 
ATOM   6253  C C     . HIS A  1 874  ? -38.502 83.552  91.892  1.00 20.22 ? 872  HIS A C     1 
ATOM   6254  O O     . HIS A  1 874  ? -38.006 82.820  92.744  1.00 18.85 ? 872  HIS A O     1 
ATOM   6255  C CB    . HIS A  1 874  ? -40.412 82.092  91.168  1.00 23.39 ? 872  HIS A CB    1 
ATOM   6256  C CG    . HIS A  1 874  ? -41.457 82.848  91.937  1.00 23.95 ? 872  HIS A CG    1 
ATOM   6257  N ND1   . HIS A  1 874  ? -42.620 82.257  92.383  1.00 29.09 ? 872  HIS A ND1   1 
ATOM   6258  C CD2   . HIS A  1 874  ? -41.523 84.145  92.326  1.00 30.13 ? 872  HIS A CD2   1 
ATOM   6259  C CE1   . HIS A  1 874  ? -43.348 83.150  93.029  1.00 30.46 ? 872  HIS A CE1   1 
ATOM   6260  N NE2   . HIS A  1 874  ? -42.706 84.305  93.007  1.00 34.13 ? 872  HIS A NE2   1 
ATOM   6261  N N     . ILE A  1 875  ? -38.437 84.876  91.943  1.00 22.52 ? 873  ILE A N     1 
ATOM   6262  C CA    . ILE A  1 875  ? -37.739 85.601  93.000  1.00 22.66 ? 873  ILE A CA    1 
ATOM   6263  C C     . ILE A  1 875  ? -38.800 86.289  93.846  1.00 25.68 ? 873  ILE A C     1 
ATOM   6264  O O     . ILE A  1 875  ? -39.676 86.975  93.306  1.00 24.83 ? 873  ILE A O     1 
ATOM   6265  C CB    . ILE A  1 875  ? -36.740 86.624  92.421  1.00 23.24 ? 873  ILE A CB    1 
ATOM   6266  C CG1   . ILE A  1 875  ? -35.426 85.965  91.967  1.00 25.60 ? 873  ILE A CG1   1 
ATOM   6267  C CG2   . ILE A  1 875  ? -36.380 87.680  93.462  1.00 26.17 ? 873  ILE A CG2   1 
ATOM   6268  C CD1   . ILE A  1 875  ? -35.531 84.927  90.886  1.00 26.64 ? 873  ILE A CD1   1 
ATOM   6269  N N     . GLY A  1 876  ? -38.736 86.103  95.161  1.00 22.11 ? 874  GLY A N     1 
ATOM   6270  C CA    . GLY A  1 876  ? -39.714 86.734  96.030  1.00 21.93 ? 874  GLY A CA    1 
ATOM   6271  C C     . GLY A  1 876  ? -39.476 86.350  97.476  1.00 21.38 ? 874  GLY A C     1 
ATOM   6272  O O     . GLY A  1 876  ? -38.500 85.671  97.816  1.00 21.74 ? 874  GLY A O     1 
ATOM   6273  N N     . ARG A  1 877  ? -40.388 86.813  98.332  1.00 24.48 ? 875  ARG A N     1 
ATOM   6274  C CA    . ARG A  1 877  ? -40.338 86.449  99.742  1.00 25.92 ? 875  ARG A CA    1 
ATOM   6275  C C     . ARG A  1 877  ? -40.457 84.937  99.867  1.00 22.94 ? 875  ARG A C     1 
ATOM   6276  O O     . ARG A  1 877  ? -41.274 84.312  99.187  1.00 22.88 ? 875  ARG A O     1 
ATOM   6277  C CB    . ARG A  1 877  ? -41.462 87.150  100.509 1.00 24.96 ? 875  ARG A CB    1 
ATOM   6278  C CG    . ARG A  1 877  ? -41.212 87.250  102.007 1.00 28.58 ? 875  ARG A CG    1 
ATOM   6279  C CD    . ARG A  1 877  ? -42.340 88.000  102.723 1.00 29.45 ? 875  ARG A CD    1 
ATOM   6280  N NE    . ARG A  1 877  ? -43.545 87.199  102.892 1.00 32.81 ? 875  ARG A NE    1 
ATOM   6281  C CZ    . ARG A  1 877  ? -44.646 87.611  103.507 1.00 37.43 ? 875  ARG A CZ    1 
ATOM   6282  N NH1   . ARG A  1 877  ? -44.777 88.858  103.937 1.00 32.33 ? 875  ARG A NH1   1 
ATOM   6283  N NH2   . ARG A  1 877  ? -45.639 86.746  103.706 1.00 34.98 ? 875  ARG A NH2   1 
ATOM   6284  N N     . THR A  1 878  ? -39.635 84.342  100.734 1.00 21.08 ? 876  THR A N     1 
ATOM   6285  C CA    . THR A  1 878  ? -39.397 82.900  100.666 1.00 20.61 ? 876  THR A CA    1 
ATOM   6286  C C     . THR A  1 878  ? -40.408 82.060  101.446 1.00 22.12 ? 876  THR A C     1 
ATOM   6287  O O     . THR A  1 878  ? -40.219 80.844  101.546 1.00 23.09 ? 876  THR A O     1 
ATOM   6288  C CB    . THR A  1 878  ? -37.965 82.567  101.134 1.00 23.66 ? 876  THR A CB    1 
ATOM   6289  O OG1   . THR A  1 878  ? -37.708 83.183  102.398 1.00 23.26 ? 876  THR A OG1   1 
ATOM   6290  C CG2   . THR A  1 878  ? -36.961 83.074  100.138 1.00 25.17 ? 876  THR A CG2   1 
ATOM   6291  N N     . ASP A  1 879  ? -41.479 82.653  101.980 1.00 22.56 ? 877  ASP A N     1 
ATOM   6292  C CA    . ASP A  1 879  ? -42.503 81.854  102.652 1.00 22.95 ? 877  ASP A CA    1 
ATOM   6293  C C     . ASP A  1 879  ? -43.500 81.267  101.651 1.00 23.16 ? 877  ASP A C     1 
ATOM   6294  O O     . ASP A  1 879  ? -44.661 81.007  101.995 1.00 23.68 ? 877  ASP A O     1 
ATOM   6295  C CB    . ASP A  1 879  ? -43.223 82.682  103.733 1.00 25.09 ? 877  ASP A CB    1 
ATOM   6296  C CG    . ASP A  1 879  ? -44.009 83.868  103.166 1.00 29.68 ? 877  ASP A CG    1 
ATOM   6297  O OD1   . ASP A  1 879  ? -43.573 84.479  102.168 1.00 32.71 ? 877  ASP A OD1   1 
ATOM   6298  O OD2   . ASP A  1 879  ? -45.063 84.201  103.738 1.00 29.58 ? 877  ASP A OD2   1 
ATOM   6299  N N     . ARG A  1 880  ? -43.045 81.048  100.414 1.00 20.88 ? 878  ARG A N     1 
ATOM   6300  C CA    . ARG A  1 880  ? -43.822 80.388  99.369  1.00 24.20 ? 878  ARG A CA    1 
ATOM   6301  C C     . ARG A  1 880  ? -42.967 79.316  98.716  1.00 22.63 ? 878  ARG A C     1 
ATOM   6302  O O     . ARG A  1 880  ? -41.829 79.586  98.305  1.00 22.11 ? 878  ARG A O     1 
ATOM   6303  C CB    . ARG A  1 880  ? -44.290 81.383  98.301  1.00 28.09 ? 878  ARG A CB    1 
ATOM   6304  C CG    . ARG A  1 880  ? -45.685 81.949  98.477  1.00 32.11 ? 878  ARG A CG    1 
ATOM   6305  C CD    . ARG A  1 880  ? -45.848 83.143  97.537  1.00 37.77 ? 878  ARG A CD    1 
ATOM   6306  N NE    . ARG A  1 880  ? -47.230 83.471  97.209  1.00 46.68 ? 878  ARG A NE    1 
ATOM   6307  C CZ    . ARG A  1 880  ? -48.004 84.275  97.928  1.00 51.74 ? 878  ARG A CZ    1 
ATOM   6308  N NH1   . ARG A  1 880  ? -47.595 84.777  99.085  1.00 51.81 ? 878  ARG A NH1   1 
ATOM   6309  N NH2   . ARG A  1 880  ? -49.217 84.584  97.474  1.00 53.56 ? 878  ARG A NH2   1 
ATOM   6310  N N     . LEU A  1 881  ? -43.527 78.112  98.588  1.00 22.19 ? 879  LEU A N     1 
ATOM   6311  C CA    . LEU A  1 881  ? -42.770 77.013  98.001  1.00 19.25 ? 879  LEU A CA    1 
ATOM   6312  C C     . LEU A  1 881  ? -42.360 77.319  96.566  1.00 22.29 ? 879  LEU A C     1 
ATOM   6313  O O     . LEU A  1 881  ? -41.314 76.853  96.108  1.00 19.30 ? 879  LEU A O     1 
ATOM   6314  C CB    . LEU A  1 881  ? -43.582 75.727  98.081  1.00 18.76 ? 879  LEU A CB    1 
ATOM   6315  C CG    . LEU A  1 881  ? -42.948 74.472  97.488  1.00 22.09 ? 879  LEU A CG    1 
ATOM   6316  C CD1   . LEU A  1 881  ? -41.760 73.985  98.343  1.00 23.18 ? 879  LEU A CD1   1 
ATOM   6317  C CD2   . LEU A  1 881  ? -44.016 73.386  97.312  1.00 23.10 ? 879  LEU A CD2   1 
ATOM   6318  N N     . SER A  1 882  ? -43.132 78.147  95.859  1.00 24.36 ? 880  SER A N     1 
ATOM   6319  C CA    . SER A  1 882  ? -42.829 78.437  94.466  1.00 25.37 ? 880  SER A CA    1 
ATOM   6320  C C     . SER A  1 882  ? -41.611 79.339  94.284  1.00 23.94 ? 880  SER A C     1 
ATOM   6321  O O     . SER A  1 882  ? -41.154 79.505  93.150  1.00 23.69 ? 880  SER A O     1 
ATOM   6322  C CB    . SER A  1 882  ? -44.048 79.085  93.799  1.00 23.97 ? 880  SER A CB    1 
ATOM   6323  O OG    . SER A  1 882  ? -44.379 80.297  94.450  1.00 21.09 ? 880  SER A OG    1 
ATOM   6324  N N     . VAL A  1 883  ? -41.066 79.915  95.349  1.00 22.69 ? 881  VAL A N     1 
ATOM   6325  C CA    . VAL A  1 883  ? -39.961 80.859  95.201  1.00 21.95 ? 881  VAL A CA    1 
ATOM   6326  C C     . VAL A  1 883  ? -38.645 80.104  95.073  1.00 22.15 ? 881  VAL A C     1 
ATOM   6327  O O     . VAL A  1 883  ? -38.316 79.261  95.914  1.00 24.99 ? 881  VAL A O     1 
ATOM   6328  C CB    . VAL A  1 883  ? -39.918 81.831  96.387  1.00 25.11 ? 881  VAL A CB    1 
ATOM   6329  C CG1   . VAL A  1 883  ? -38.586 82.567  96.387  1.00 22.99 ? 881  VAL A CG1   1 
ATOM   6330  C CG2   . VAL A  1 883  ? -41.094 82.796  96.311  1.00 24.36 ? 881  VAL A CG2   1 
ATOM   6331  N N     . ASP A  1 884  ? -37.876 80.420  94.032  1.00 18.51 ? 882  ASP A N     1 
ATOM   6332  C CA    . ASP A  1 884  ? -36.596 79.756  93.811  1.00 20.75 ? 882  ASP A CA    1 
ATOM   6333  C C     . ASP A  1 884  ? -35.454 80.506  94.471  1.00 20.92 ? 882  ASP A C     1 
ATOM   6334  O O     . ASP A  1 884  ? -34.563 79.894  95.072  1.00 24.53 ? 882  ASP A O     1 
ATOM   6335  C CB    . ASP A  1 884  ? -36.333 79.634  92.315  1.00 18.31 ? 882  ASP A CB    1 
ATOM   6336  C CG    . ASP A  1 884  ? -37.453 78.900  91.616  1.00 23.78 ? 882  ASP A CG    1 
ATOM   6337  O OD1   . ASP A  1 884  ? -37.703 77.731  91.996  1.00 23.28 ? 882  ASP A OD1   1 
ATOM   6338  O OD2   . ASP A  1 884  ? -38.123 79.507  90.755  1.00 21.63 ? 882  ASP A OD2   1 
ATOM   6339  N N     . VAL A  1 885  ? -35.476 81.827  94.368  1.00 22.85 ? 883  VAL A N     1 
ATOM   6340  C CA    . VAL A  1 885  ? -34.399 82.665  94.861  1.00 21.56 ? 883  VAL A CA    1 
ATOM   6341  C C     . VAL A  1 885  ? -35.005 83.731  95.759  1.00 23.57 ? 883  VAL A C     1 
ATOM   6342  O O     . VAL A  1 885  ? -35.927 84.442  95.350  1.00 20.99 ? 883  VAL A O     1 
ATOM   6343  C CB    . VAL A  1 885  ? -33.609 83.300  93.700  1.00 24.86 ? 883  VAL A CB    1 
ATOM   6344  C CG1   . VAL A  1 885  ? -32.528 84.224  94.235  1.00 21.32 ? 883  VAL A CG1   1 
ATOM   6345  C CG2   . VAL A  1 885  ? -32.994 82.203  92.806  1.00 24.04 ? 883  VAL A CG2   1 
ATOM   6346  N N     . GLY A  1 886  ? -34.496 83.837  96.980  1.00 19.23 ? 884  GLY A N     1 
ATOM   6347  C CA    . GLY A  1 886  ? -34.965 84.845  97.899  1.00 20.05 ? 884  GLY A CA    1 
ATOM   6348  C C     . GLY A  1 886  ? -34.140 86.113  97.844  1.00 20.87 ? 884  GLY A C     1 
ATOM   6349  O O     . GLY A  1 886  ? -33.416 86.387  96.877  1.00 20.40 ? 884  GLY A O     1 
ATOM   6350  N N     . PRO A  1 887  ? -34.227 86.905  98.902  1.00 22.40 ? 885  PRO A N     1 
ATOM   6351  C CA    . PRO A  1 887  ? -33.530 88.193  98.944  1.00 22.10 ? 885  PRO A CA    1 
ATOM   6352  C C     . PRO A  1 887  ? -32.068 88.018  99.337  1.00 24.63 ? 885  PRO A C     1 
ATOM   6353  O O     . PRO A  1 887  ? -31.641 86.960  99.802  1.00 21.30 ? 885  PRO A O     1 
ATOM   6354  C CB    . PRO A  1 887  ? -34.289 88.946  100.038 1.00 24.08 ? 885  PRO A CB    1 
ATOM   6355  C CG    . PRO A  1 887  ? -34.681 87.856  101.001 1.00 22.57 ? 885  PRO A CG    1 
ATOM   6356  C CD    . PRO A  1 887  ? -34.977 86.634  100.139 1.00 22.08 ? 885  PRO A CD    1 
ATOM   6357  N N     . VAL A  1 888  ? -31.297 89.089  99.151  1.00 20.60 ? 886  VAL A N     1 
ATOM   6358  C CA    . VAL A  1 888  ? -29.974 89.124  99.766  1.00 21.89 ? 886  VAL A CA    1 
ATOM   6359  C C     . VAL A  1 888  ? -30.190 89.641  101.187 1.00 20.97 ? 886  VAL A C     1 
ATOM   6360  O O     . VAL A  1 888  ? -31.288 90.094  101.531 1.00 21.16 ? 886  VAL A O     1 
ATOM   6361  C CB    . VAL A  1 888  ? -28.956 89.953  98.949  1.00 24.73 ? 886  VAL A CB    1 
ATOM   6362  C CG1   . VAL A  1 888  ? -28.674 89.251  97.595  1.00 21.53 ? 886  VAL A CG1   1 
ATOM   6363  C CG2   . VAL A  1 888  ? -29.431 91.364  98.712  1.00 22.44 ? 886  VAL A CG2   1 
ATOM   6364  N N     . ILE A  1 889  ? -29.164 89.547  102.036 1.00 21.53 ? 887  ILE A N     1 
ATOM   6365  C CA    . ILE A  1 889  ? -29.420 89.618  103.470 1.00 22.53 ? 887  ILE A CA    1 
ATOM   6366  C C     . ILE A  1 889  ? -29.737 91.042  103.946 1.00 23.25 ? 887  ILE A C     1 
ATOM   6367  O O     . ILE A  1 889  ? -30.527 91.214  104.886 1.00 23.36 ? 887  ILE A O     1 
ATOM   6368  C CB    . ILE A  1 889  ? -28.228 89.003  104.239 1.00 21.78 ? 887  ILE A CB    1 
ATOM   6369  C CG1   . ILE A  1 889  ? -28.520 88.965  105.745 1.00 23.90 ? 887  ILE A CG1   1 
ATOM   6370  C CG2   . ILE A  1 889  ? -26.932 89.747  103.942 1.00 22.50 ? 887  ILE A CG2   1 
ATOM   6371  C CD1   . ILE A  1 889  ? -29.623 88.005  106.122 1.00 25.12 ? 887  ILE A CD1   1 
ATOM   6372  N N     . THR A  1 890  ? -29.151 92.074  103.329 1.00 21.94 ? 888  THR A N     1 
ATOM   6373  C CA    . THR A  1 890  ? -29.310 93.451  103.800 1.00 22.44 ? 888  THR A CA    1 
ATOM   6374  C C     . THR A  1 890  ? -29.327 94.425  102.631 1.00 22.59 ? 888  THR A C     1 
ATOM   6375  O O     . THR A  1 890  ? -28.903 94.106  101.519 1.00 23.38 ? 888  THR A O     1 
ATOM   6376  C CB    . THR A  1 890  ? -28.172 93.909  104.738 1.00 24.12 ? 888  THR A CB    1 
ATOM   6377  O OG1   . THR A  1 890  ? -26.916 93.750  104.063 1.00 24.06 ? 888  THR A OG1   1 
ATOM   6378  C CG2   . THR A  1 890  ? -28.150 93.123  106.045 1.00 24.19 ? 888  THR A CG2   1 
ATOM   6379  N N     . SER A  1 891  ? -29.771 95.652  102.925 1.00 23.84 ? 889  SER A N     1 
ATOM   6380  C CA    . SER A  1 891  ? -29.668 96.736  101.951 1.00 27.39 ? 889  SER A CA    1 
ATOM   6381  C C     . SER A  1 891  ? -28.216 97.007  101.576 1.00 26.67 ? 889  SER A C     1 
ATOM   6382  O O     . SER A  1 891  ? -27.919 97.307  100.419 1.00 25.61 ? 889  SER A O     1 
ATOM   6383  C CB    . SER A  1 891  ? -30.314 98.011  102.495 1.00 28.76 ? 889  SER A CB    1 
ATOM   6384  O OG    . SER A  1 891  ? -31.706 97.840  102.675 1.00 38.69 ? 889  SER A OG    1 
ATOM   6385  N N     . GLU A  1 892  ? -27.300 96.935  102.549 1.00 27.16 ? 890  GLU A N     1 
ATOM   6386  C CA    . GLU A  1 892  ? -25.886 97.140  102.251 1.00 28.27 ? 890  GLU A CA    1 
ATOM   6387  C C     . GLU A  1 892  ? -25.370 96.078  101.283 1.00 28.15 ? 890  GLU A C     1 
ATOM   6388  O O     . GLU A  1 892  ? -24.627 96.389  100.344 1.00 26.56 ? 890  GLU A O     1 
ATOM   6389  C CB    . GLU A  1 892  ? -25.065 97.123  103.549 1.00 30.27 ? 890  GLU A CB    1 
ATOM   6390  C CG    . GLU A  1 892  ? -25.685 97.932  104.685 1.00 38.56 ? 890  GLU A CG    1 
ATOM   6391  C CD    . GLU A  1 892  ? -26.741 97.152  105.474 1.00 35.61 ? 890  GLU A CD    1 
ATOM   6392  O OE1   . GLU A  1 892  ? -26.377 96.150  106.139 1.00 49.47 ? 890  GLU A OE1   1 
ATOM   6393  O OE2   . GLU A  1 892  ? -27.929 97.537  105.420 1.00 36.11 ? 890  GLU A OE2   1 
ATOM   6394  N N     . ALA A  1 893  ? -25.732 94.815  101.512 1.00 25.54 ? 891  ALA A N     1 
ATOM   6395  C CA    . ALA A  1 893  ? -25.375 93.757  100.569 1.00 25.00 ? 891  ALA A CA    1 
ATOM   6396  C C     . ALA A  1 893  ? -25.928 94.068  99.184  1.00 30.23 ? 891  ALA A C     1 
ATOM   6397  O O     . ALA A  1 893  ? -25.222 93.959  98.172  1.00 27.76 ? 891  ALA A O     1 
ATOM   6398  C CB    . ALA A  1 893  ? -25.906 92.412  101.069 1.00 21.76 ? 891  ALA A CB    1 
ATOM   6399  N N     . LYS A  1 894  ? -27.186 94.494  99.129  1.00 24.56 ? 892  LYS A N     1 
ATOM   6400  C CA    . LYS A  1 894  ? -27.823 94.742  97.838  1.00 26.68 ? 892  LYS A CA    1 
ATOM   6401  C C     . LYS A  1 894  ? -27.091 95.835  97.076  1.00 29.29 ? 892  LYS A C     1 
ATOM   6402  O O     . LYS A  1 894  ? -26.746 95.663  95.903  1.00 27.78 ? 892  LYS A O     1 
ATOM   6403  C CB    . LYS A  1 894  ? -29.287 95.111  98.034  1.00 23.92 ? 892  LYS A CB    1 
ATOM   6404  C CG    . LYS A  1 894  ? -29.969 95.615  96.768  1.00 26.78 ? 892  LYS A CG    1 
ATOM   6405  C CD    . LYS A  1 894  ? -31.382 96.062  97.051  1.00 28.34 ? 892  LYS A CD    1 
ATOM   6406  C CE    . LYS A  1 894  ? -32.050 96.601  95.787  1.00 30.96 ? 892  LYS A CE    1 
ATOM   6407  N NZ    . LYS A  1 894  ? -33.414 97.068  96.116  1.00 37.99 ? 892  LYS A NZ    1 
ATOM   6408  N N     . ASP A  1 895  ? -26.808 96.956  97.749  1.00 28.93 ? 893  ASP A N     1 
ATOM   6409  C CA    . ASP A  1 895  ? -26.131 98.073  97.097  1.00 29.50 ? 893  ASP A CA    1 
ATOM   6410  C C     . ASP A  1 895  ? -24.739 97.686  96.620  1.00 28.41 ? 893  ASP A C     1 
ATOM   6411  O O     . ASP A  1 895  ? -24.326 98.072  95.521  1.00 32.00 ? 893  ASP A O     1 
ATOM   6412  C CB    . ASP A  1 895  ? -26.043 99.262  98.052  1.00 31.27 ? 893  ASP A CB    1 
ATOM   6413  C CG    . ASP A  1 895  ? -27.400 99.843  98.380  1.00 42.70 ? 893  ASP A CG    1 
ATOM   6414  O OD1   . ASP A  1 895  ? -28.356 99.623  97.591  1.00 43.40 ? 893  ASP A OD1   1 
ATOM   6415  O OD2   . ASP A  1 895  ? -27.509 100.522 99.426  1.00 45.83 ? 893  ASP A OD2   1 
ATOM   6416  N N     . ASN A  1 896  ? -23.987 96.960  97.449  1.00 25.99 ? 894  ASN A N     1 
ATOM   6417  C CA    . ASN A  1 896  ? -22.659 96.506  97.049  1.00 29.14 ? 894  ASN A CA    1 
ATOM   6418  C C     . ASN A  1 896  ? -22.726 95.671  95.777  1.00 27.88 ? 894  ASN A C     1 
ATOM   6419  O O     . ASN A  1 896  ? -21.946 95.879  94.840  1.00 26.62 ? 894  ASN A O     1 
ATOM   6420  C CB    . ASN A  1 896  ? -22.024 95.706  98.189  1.00 33.18 ? 894  ASN A CB    1 
ATOM   6421  C CG    . ASN A  1 896  ? -20.616 95.214  97.857  1.00 40.55 ? 894  ASN A CG    1 
ATOM   6422  O OD1   . ASN A  1 896  ? -20.433 94.133  97.285  1.00 45.73 ? 894  ASN A OD1   1 
ATOM   6423  N ND2   . ASN A  1 896  ? -19.616 95.994  98.241  1.00 38.16 ? 894  ASN A ND2   1 
ATOM   6424  N N     . ILE A  1 897  ? -23.657 94.716  95.727  1.00 27.52 ? 895  ILE A N     1 
ATOM   6425  C CA    . ILE A  1 897  ? -23.773 93.858  94.549  1.00 24.94 ? 895  ILE A CA    1 
ATOM   6426  C C     . ILE A  1 897  ? -24.195 94.676  93.331  1.00 27.79 ? 895  ILE A C     1 
ATOM   6427  O O     . ILE A  1 897  ? -23.631 94.537  92.236  1.00 26.37 ? 895  ILE A O     1 
ATOM   6428  C CB    . ILE A  1 897  ? -24.757 92.709  94.823  1.00 25.97 ? 895  ILE A CB    1 
ATOM   6429  C CG1   . ILE A  1 897  ? -24.246 91.798  95.935  1.00 23.30 ? 895  ILE A CG1   1 
ATOM   6430  C CG2   . ILE A  1 897  ? -24.987 91.891  93.563  1.00 26.44 ? 895  ILE A CG2   1 
ATOM   6431  C CD1   . ILE A  1 897  ? -25.337 91.008  96.598  1.00 24.13 ? 895  ILE A CD1   1 
ATOM   6432  N N     . GLU A  1 898  ? -25.171 95.560  93.508  1.00 26.71 ? 896  GLU A N     1 
ATOM   6433  C CA    . GLU A  1 898  ? -25.691 96.307  92.365  1.00 30.29 ? 896  GLU A CA    1 
ATOM   6434  C C     . GLU A  1 898  ? -24.676 97.310  91.832  1.00 27.91 ? 896  GLU A C     1 
ATOM   6435  O O     . GLU A  1 898  ? -24.664 97.595  90.629  1.00 28.83 ? 896  GLU A O     1 
ATOM   6436  C CB    . GLU A  1 898  ? -27.005 96.983  92.747  1.00 30.14 ? 896  GLU A CB    1 
ATOM   6437  C CG    . GLU A  1 898  ? -28.054 95.943  93.139  1.00 31.25 ? 896  GLU A CG    1 
ATOM   6438  C CD    . GLU A  1 898  ? -29.477 96.461  93.140  1.00 37.58 ? 896  GLU A CD    1 
ATOM   6439  O OE1   . GLU A  1 898  ? -29.730 97.534  93.719  1.00 39.09 ? 896  GLU A OE1   1 
ATOM   6440  O OE2   . GLU A  1 898  ? -30.347 95.766  92.569  1.00 40.27 ? 896  GLU A OE2   1 
ATOM   6441  N N     . LYS A  1 899  ? -23.810 97.838  92.697  1.00 26.66 ? 897  LYS A N     1 
ATOM   6442  C CA    . LYS A  1 899  ? -22.729 98.695  92.228  1.00 25.89 ? 897  LYS A CA    1 
ATOM   6443  C C     . LYS A  1 899  ? -21.790 97.926  91.306  1.00 26.75 ? 897  LYS A C     1 
ATOM   6444  O O     . LYS A  1 899  ? -21.349 98.451  90.279  1.00 28.12 ? 897  LYS A O     1 
ATOM   6445  C CB    . LYS A  1 899  ? -21.958 99.273  93.417  1.00 28.56 ? 897  LYS A CB    1 
ATOM   6446  N N     . HIS A  1 900  ? -21.483 96.673  91.649  1.00 26.67 ? 898  HIS A N     1 
ATOM   6447  C CA    . HIS A  1 900  ? -20.657 95.863  90.766  1.00 26.32 ? 898  HIS A CA    1 
ATOM   6448  C C     . HIS A  1 900  ? -21.330 95.676  89.414  1.00 25.79 ? 898  HIS A C     1 
ATOM   6449  O O     . HIS A  1 900  ? -20.697 95.837  88.364  1.00 28.63 ? 898  HIS A O     1 
ATOM   6450  C CB    . HIS A  1 900  ? -20.357 94.508  91.404  1.00 25.69 ? 898  HIS A CB    1 
ATOM   6451  C CG    . HIS A  1 900  ? -19.727 93.535  90.458  1.00 30.89 ? 898  HIS A CG    1 
ATOM   6452  N ND1   . HIS A  1 900  ? -18.393 93.587  90.118  1.00 30.19 ? 898  HIS A ND1   1 
ATOM   6453  C CD2   . HIS A  1 900  ? -20.255 92.501  89.760  1.00 27.68 ? 898  HIS A CD2   1 
ATOM   6454  C CE1   . HIS A  1 900  ? -18.121 92.615  89.262  1.00 31.90 ? 898  HIS A CE1   1 
ATOM   6455  N NE2   . HIS A  1 900  ? -19.232 91.937  89.034  1.00 27.77 ? 898  HIS A NE2   1 
ATOM   6456  N N     . ILE A  1 901  ? -22.620 95.344  89.424  1.00 25.67 ? 899  ILE A N     1 
ATOM   6457  C CA    . ILE A  1 901  ? -23.323 95.087  88.167  1.00 26.43 ? 899  ILE A CA    1 
ATOM   6458  C C     . ILE A  1 901  ? -23.303 96.324  87.285  1.00 29.85 ? 899  ILE A C     1 
ATOM   6459  O O     . ILE A  1 901  ? -23.025 96.245  86.080  1.00 29.33 ? 899  ILE A O     1 
ATOM   6460  C CB    . ILE A  1 901  ? -24.758 94.615  88.441  1.00 26.24 ? 899  ILE A CB    1 
ATOM   6461  C CG1   . ILE A  1 901  ? -24.722 93.266  89.179  1.00 25.20 ? 899  ILE A CG1   1 
ATOM   6462  C CG2   . ILE A  1 901  ? -25.545 94.535  87.115  1.00 24.51 ? 899  ILE A CG2   1 
ATOM   6463  C CD1   . ILE A  1 901  ? -26.039 92.904  89.833  1.00 21.92 ? 899  ILE A CD1   1 
ATOM   6464  N N     . GLU A  1 902  ? -23.580 97.487  87.870  1.00 26.69 ? 900  GLU A N     1 
ATOM   6465  C CA    . GLU A  1 902  ? -23.601 98.707  87.074  1.00 30.62 ? 900  GLU A CA    1 
ATOM   6466  C C     . GLU A  1 902  ? -22.219 99.051  86.527  1.00 26.98 ? 900  GLU A C     1 
ATOM   6467  O O     . GLU A  1 902  ? -22.105 99.574  85.415  1.00 31.57 ? 900  GLU A O     1 
ATOM   6468  C CB    . GLU A  1 902  ? -24.172 99.860  87.900  1.00 29.72 ? 900  GLU A CB    1 
ATOM   6469  C CG    . GLU A  1 902  ? -25.653 99.700  88.193  1.00 36.75 ? 900  GLU A CG    1 
ATOM   6470  C CD    . GLU A  1 902  ? -26.455 99.308  86.958  1.00 38.00 ? 900  GLU A CD    1 
ATOM   6471  O OE1   . GLU A  1 902  ? -26.270 99.951  85.904  1.00 42.04 ? 900  GLU A OE1   1 
ATOM   6472  O OE2   . GLU A  1 902  ? -27.256 98.347  87.036  1.00 36.46 ? 900  GLU A OE2   1 
ATOM   6473  N N     . ARG A  1 903  ? -21.157 98.792  87.291  1.00 28.99 ? 901  ARG A N     1 
ATOM   6474  C CA    . ARG A  1 903  ? -19.817 99.040  86.772  1.00 28.06 ? 901  ARG A CA    1 
ATOM   6475  C C     . ARG A  1 903  ? -19.521 98.152  85.568  1.00 33.96 ? 901  ARG A C     1 
ATOM   6476  O O     . ARG A  1 903  ? -18.949 98.613  84.570  1.00 33.51 ? 901  ARG A O     1 
ATOM   6477  C CB    . ARG A  1 903  ? -18.772 98.821  87.865  1.00 34.13 ? 901  ARG A CB    1 
ATOM   6478  N N     . MET A  1 904  ? -19.905 96.874  85.642  1.00 32.35 ? 902  MET A N     1 
ATOM   6479  C CA    . MET A  1 904  ? -19.738 95.978  84.502  1.00 29.17 ? 902  MET A CA    1 
ATOM   6480  C C     . MET A  1 904  ? -20.541 96.469  83.305  1.00 34.63 ? 902  MET A C     1 
ATOM   6481  O O     . MET A  1 904  ? -20.027 96.533  82.179  1.00 36.82 ? 902  MET A O     1 
ATOM   6482  C CB    . MET A  1 904  ? -20.148 94.553  84.885  1.00 28.51 ? 902  MET A CB    1 
ATOM   6483  C CG    . MET A  1 904  ? -19.243 93.896  85.905  1.00 28.19 ? 902  MET A CG    1 
ATOM   6484  S SD    . MET A  1 904  ? -17.539 93.745  85.333  1.00 37.81 ? 902  MET A SD    1 
ATOM   6485  C CE    . MET A  1 904  ? -16.726 95.032  86.286  1.00 36.51 ? 902  MET A CE    1 
ATOM   6486  N N     . ARG A  1 905  ? -21.804 96.839  83.533  1.00 31.54 ? 903  ARG A N     1 
ATOM   6487  C CA    . ARG A  1 905  ? -22.609 97.378  82.444  1.00 33.26 ? 903  ARG A CA    1 
ATOM   6488  C C     . ARG A  1 905  ? -21.992 98.661  81.908  1.00 34.67 ? 903  ARG A C     1 
ATOM   6489  O O     . ARG A  1 905  ? -22.003 98.908  80.696  1.00 34.72 ? 903  ARG A O     1 
ATOM   6490  C CB    . ARG A  1 905  ? -24.044 97.626  82.909  1.00 29.93 ? 903  ARG A CB    1 
ATOM   6491  C CG    . ARG A  1 905  ? -25.027 97.811  81.763  1.00 35.57 ? 903  ARG A CG    1 
ATOM   6492  C CD    . ARG A  1 905  ? -26.362 98.365  82.237  1.00 35.93 ? 903  ARG A CD    1 
ATOM   6493  N NE    . ARG A  1 905  ? -26.805 97.789  83.502  1.00 35.29 ? 903  ARG A NE    1 
ATOM   6494  C CZ    . ARG A  1 905  ? -27.557 96.703  83.615  1.00 31.79 ? 903  ARG A CZ    1 
ATOM   6495  N NH1   . ARG A  1 905  ? -27.896 95.981  82.559  1.00 33.24 ? 903  ARG A NH1   1 
ATOM   6496  N NH2   . ARG A  1 905  ? -27.984 96.333  84.819  1.00 37.34 ? 903  ARG A NH2   1 
ATOM   6497  N N     . GLY A  1 906  ? -21.432 99.481  82.803  1.00 31.25 ? 904  GLY A N     1 
ATOM   6498  C CA    . GLY A  1 906  ? -20.796 100.713 82.377  1.00 35.79 ? 904  GLY A CA    1 
ATOM   6499  C C     . GLY A  1 906  ? -19.593 100.478 81.491  1.00 35.71 ? 904  GLY A C     1 
ATOM   6500  O O     . GLY A  1 906  ? -19.280 101.309 80.632  1.00 38.33 ? 904  GLY A O     1 
ATOM   6501  N N     . LEU A  1 907  ? -18.912 99.346  81.672  1.00 32.98 ? 905  LEU A N     1 
ATOM   6502  C CA    . LEU A  1 907  ? -17.772 98.983  80.838  1.00 34.85 ? 905  LEU A CA    1 
ATOM   6503  C C     . LEU A  1 907  ? -18.186 98.336  79.524  1.00 33.19 ? 905  LEU A C     1 
ATOM   6504  O O     . LEU A  1 907  ? -17.318 97.892  78.765  1.00 40.83 ? 905  LEU A O     1 
ATOM   6505  C CB    . LEU A  1 907  ? -16.841 98.041  81.598  1.00 37.91 ? 905  LEU A CB    1 
ATOM   6506  C CG    . LEU A  1 907  ? -16.216 98.657  82.844  1.00 39.04 ? 905  LEU A CG    1 
ATOM   6507  C CD1   . LEU A  1 907  ? -15.515 97.594  83.663  1.00 40.03 ? 905  LEU A CD1   1 
ATOM   6508  C CD2   . LEU A  1 907  ? -15.263 99.748  82.440  1.00 35.99 ? 905  LEU A CD2   1 
ATOM   6509  N N     . GLY A  1 908  ? -19.477 98.263  79.242  1.00 33.60 ? 906  GLY A N     1 
ATOM   6510  C CA    . GLY A  1 908  ? -19.934 97.675  78.004  1.00 38.07 ? 906  GLY A CA    1 
ATOM   6511  C C     . GLY A  1 908  ? -20.075 96.171  78.013  1.00 34.84 ? 906  GLY A C     1 
ATOM   6512  O O     . GLY A  1 908  ? -20.327 95.593  76.954  1.00 35.30 ? 906  GLY A O     1 
ATOM   6513  N N     . ARG A  1 909  ? -19.922 95.514  79.159  1.00 33.85 ? 907  ARG A N     1 
ATOM   6514  C CA    . ARG A  1 909  ? -20.159 94.077  79.214  1.00 31.68 ? 907  ARG A CA    1 
ATOM   6515  C C     . ARG A  1 909  ? -21.641 93.765  79.041  1.00 33.90 ? 907  ARG A C     1 
ATOM   6516  O O     . ARG A  1 909  ? -22.518 94.498  79.510  1.00 35.00 ? 907  ARG A O     1 
ATOM   6517  C CB    . ARG A  1 909  ? -19.687 93.487  80.539  1.00 32.07 ? 907  ARG A CB    1 
ATOM   6518  C CG    . ARG A  1 909  ? -18.263 93.776  80.885  1.00 33.64 ? 907  ARG A CG    1 
ATOM   6519  C CD    . ARG A  1 909  ? -17.314 93.164  79.888  1.00 39.28 ? 907  ARG A CD    1 
ATOM   6520  N NE    . ARG A  1 909  ? -15.938 93.315  80.348  1.00 45.81 ? 907  ARG A NE    1 
ATOM   6521  C CZ    . ARG A  1 909  ? -15.153 94.331  80.023  1.00 48.52 ? 907  ARG A CZ    1 
ATOM   6522  N NH1   . ARG A  1 909  ? -15.563 95.285  79.202  1.00 45.07 ? 907  ARG A NH1   1 
ATOM   6523  N NH2   . ARG A  1 909  ? -13.929 94.396  80.540  1.00 54.76 ? 907  ARG A NH2   1 
ATOM   6524  N N     . LYS A  1 910  ? -21.915 92.648  78.375  1.00 30.78 ? 908  LYS A N     1 
ATOM   6525  C CA    . LYS A  1 910  ? -23.284 92.176  78.248  1.00 31.05 ? 908  LYS A CA    1 
ATOM   6526  C C     . LYS A  1 910  ? -23.791 91.671  79.593  1.00 29.56 ? 908  LYS A C     1 
ATOM   6527  O O     . LYS A  1 910  ? -23.178 90.799  80.218  1.00 28.28 ? 908  LYS A O     1 
ATOM   6528  C CB    . LYS A  1 910  ? -23.373 91.071  77.195  1.00 33.74 ? 908  LYS A CB    1 
ATOM   6529  C CG    . LYS A  1 910  ? -23.050 91.543  75.779  1.00 38.88 ? 908  LYS A CG    1 
ATOM   6530  C CD    . LYS A  1 910  ? -23.406 90.478  74.746  1.00 44.02 ? 908  LYS A CD    1 
ATOM   6531  C CE    . LYS A  1 910  ? -24.843 90.017  74.906  1.00 44.10 ? 908  LYS A CE    1 
ATOM   6532  N NZ    . LYS A  1 910  ? -25.268 89.111  73.796  1.00 55.43 ? 908  LYS A NZ    1 
ATOM   6533  N N     . VAL A  1 911  ? -24.924 92.211  80.025  1.00 28.00 ? 909  VAL A N     1 
ATOM   6534  C CA    . VAL A  1 911  ? -25.517 91.919  81.322  1.00 24.48 ? 909  VAL A CA    1 
ATOM   6535  C C     . VAL A  1 911  ? -26.939 91.439  81.077  1.00 28.30 ? 909  VAL A C     1 
ATOM   6536  O O     . VAL A  1 911  ? -27.739 92.146  80.448  1.00 27.71 ? 909  VAL A O     1 
ATOM   6537  C CB    . VAL A  1 911  ? -25.500 93.152  82.241  1.00 24.57 ? 909  VAL A CB    1 
ATOM   6538  C CG1   . VAL A  1 911  ? -26.317 92.896  83.507  1.00 25.23 ? 909  VAL A CG1   1 
ATOM   6539  C CG2   . VAL A  1 911  ? -24.043 93.566  82.584  1.00 25.60 ? 909  VAL A CG2   1 
ATOM   6540  N N     . GLU A  1 912  ? -27.244 90.233  81.548  1.00 23.20 ? 910  GLU A N     1 
ATOM   6541  C CA    . GLU A  1 912  ? -28.585 89.669  81.486  1.00 26.18 ? 910  GLU A CA    1 
ATOM   6542  C C     . GLU A  1 912  ? -29.162 89.615  82.893  1.00 26.99 ? 910  GLU A C     1 
ATOM   6543  O O     . GLU A  1 912  ? -28.528 89.071  83.805  1.00 25.19 ? 910  GLU A O     1 
ATOM   6544  C CB    . GLU A  1 912  ? -28.563 88.266  80.876  1.00 25.56 ? 910  GLU A CB    1 
ATOM   6545  C CG    . GLU A  1 912  ? -29.938 87.667  80.645  1.00 24.97 ? 910  GLU A CG    1 
ATOM   6546  C CD    . GLU A  1 912  ? -30.576 88.180  79.373  1.00 30.64 ? 910  GLU A CD    1 
ATOM   6547  O OE1   . GLU A  1 912  ? -29.843 88.749  78.534  1.00 30.56 ? 910  GLU A OE1   1 
ATOM   6548  O OE2   . GLU A  1 912  ? -31.805 88.017  79.216  1.00 33.35 ? 910  GLU A OE2   1 
ATOM   6549  N N     . GLN A  1 913  ? -30.355 90.175  83.072  1.00 22.48 ? 911  GLN A N     1 
ATOM   6550  C CA    . GLN A  1 913  ? -31.016 90.171  84.374  1.00 24.86 ? 911  GLN A CA    1 
ATOM   6551  C C     . GLN A  1 913  ? -32.480 89.807  84.222  1.00 25.40 ? 911  GLN A C     1 
ATOM   6552  O O     . GLN A  1 913  ? -33.127 90.180  83.242  1.00 24.97 ? 911  GLN A O     1 
ATOM   6553  C CB    . GLN A  1 913  ? -30.953 91.536  85.077  1.00 22.95 ? 911  GLN A CB    1 
ATOM   6554  C CG    . GLN A  1 913  ? -29.576 92.030  85.395  1.00 31.21 ? 911  GLN A CG    1 
ATOM   6555  C CD    . GLN A  1 913  ? -29.625 93.171  86.379  1.00 30.06 ? 911  GLN A CD    1 
ATOM   6556  O OE1   . GLN A  1 913  ? -30.233 94.205  86.110  1.00 36.67 ? 911  GLN A OE1   1 
ATOM   6557  N NE2   . GLN A  1 913  ? -29.015 92.981  87.536  1.00 26.73 ? 911  GLN A NE2   1 
ATOM   6558  N N     . ILE A  1 914  ? -33.016 89.117  85.222  1.00 28.20 ? 912  ILE A N     1 
ATOM   6559  C CA    . ILE A  1 914  ? -34.452 88.865  85.234  1.00 27.06 ? 912  ILE A CA    1 
ATOM   6560  C C     . ILE A  1 914  ? -35.167 90.069  85.826  1.00 29.36 ? 912  ILE A C     1 
ATOM   6561  O O     . ILE A  1 914  ? -34.642 90.776  86.694  1.00 28.47 ? 912  ILE A O     1 
ATOM   6562  C CB    . ILE A  1 914  ? -34.794 87.571  85.994  1.00 30.84 ? 912  ILE A CB    1 
ATOM   6563  C CG1   . ILE A  1 914  ? -34.181 87.583  87.385  1.00 30.37 ? 912  ILE A CG1   1 
ATOM   6564  C CG2   . ILE A  1 914  ? -34.270 86.395  85.236  1.00 32.54 ? 912  ILE A CG2   1 
ATOM   6565  C CD1   . ILE A  1 914  ? -35.197 87.428  88.467  1.00 33.84 ? 912  ILE A CD1   1 
ATOM   6566  N N     . GLY A  1 915  ? -36.362 90.342  85.313  1.00 29.49 ? 913  GLY A N     1 
ATOM   6567  C CA    . GLY A  1 915  ? -37.170 91.405  85.880  1.00 31.00 ? 913  GLY A CA    1 
ATOM   6568  C C     . GLY A  1 915  ? -37.780 90.942  87.190  1.00 29.75 ? 913  GLY A C     1 
ATOM   6569  O O     . GLY A  1 915  ? -38.259 89.818  87.310  1.00 31.74 ? 913  GLY A O     1 
ATOM   6570  N N     . LEU A  1 916  ? -37.737 91.814  88.190  1.00 26.91 ? 914  LEU A N     1 
ATOM   6571  C CA    . LEU A  1 916  ? -38.304 91.502  89.494  1.00 31.68 ? 914  LEU A CA    1 
ATOM   6572  C C     . LEU A  1 916  ? -39.727 92.034  89.621  1.00 32.12 ? 914  LEU A C     1 
ATOM   6573  O O     . LEU A  1 916  ? -40.078 93.073  89.056  1.00 33.63 ? 914  LEU A O     1 
ATOM   6574  C CB    . LEU A  1 916  ? -37.442 92.081  90.616  1.00 31.96 ? 914  LEU A CB    1 
ATOM   6575  C CG    . LEU A  1 916  ? -36.052 91.473  90.753  1.00 30.17 ? 914  LEU A CG    1 
ATOM   6576  C CD1   . LEU A  1 916  ? -35.395 91.990  92.017  1.00 30.70 ? 914  LEU A CD1   1 
ATOM   6577  C CD2   . LEU A  1 916  ? -36.152 89.955  90.754  1.00 29.51 ? 914  LEU A CD2   1 
ATOM   6578  N N     . ALA A  1 917  ? -40.540 91.320  90.392  1.00 32.42 ? 915  ALA A N     1 
ATOM   6579  C CA    . ALA A  1 917  ? -41.897 91.769  90.663  1.00 35.53 ? 915  ALA A CA    1 
ATOM   6580  C C     . ALA A  1 917  ? -41.884 92.983  91.588  1.00 35.39 ? 915  ALA A C     1 
ATOM   6581  O O     . ALA A  1 917  ? -40.938 93.213  92.347  1.00 32.24 ? 915  ALA A O     1 
ATOM   6582  C CB    . ALA A  1 917  ? -42.722 90.642  91.285  1.00 35.09 ? 915  ALA A CB    1 
ATOM   6583  N N     . SER A  1 918  ? -42.961 93.769  91.516  1.00 34.13 ? 916  SER A N     1 
ATOM   6584  C CA    . SER A  1 918  ? -43.066 94.958  92.359  1.00 35.48 ? 916  SER A CA    1 
ATOM   6585  C C     . SER A  1 918  ? -43.058 94.595  93.839  1.00 32.60 ? 916  SER A C     1 
ATOM   6586  O O     . SER A  1 918  ? -42.561 95.368  94.663  1.00 32.50 ? 916  SER A O     1 
ATOM   6587  C CB    . SER A  1 918  ? -44.333 95.744  92.008  1.00 37.91 ? 916  SER A CB    1 
ATOM   6588  O OG    . SER A  1 918  ? -45.496 94.974  92.273  1.00 44.74 ? 916  SER A OG    1 
ATOM   6589  N N     . GLU A  1 919  ? -43.568 93.412  94.190  1.00 31.68 ? 917  GLU A N     1 
ATOM   6590  C CA    . GLU A  1 919  ? -43.622 92.997  95.585  1.00 34.07 ? 917  GLU A CA    1 
ATOM   6591  C C     . GLU A  1 919  ? -42.244 92.904  96.221  1.00 32.34 ? 917  GLU A C     1 
ATOM   6592  O O     . GLU A  1 919  ? -42.152 92.850  97.451  1.00 31.89 ? 917  GLU A O     1 
ATOM   6593  C CB    . GLU A  1 919  ? -44.328 91.642  95.718  1.00 35.65 ? 917  GLU A CB    1 
ATOM   6594  C CG    . GLU A  1 919  ? -45.850 91.705  95.660  1.00 40.69 ? 917  GLU A CG    1 
ATOM   6595  C CD    . GLU A  1 919  ? -46.410 91.604  94.245  1.00 47.65 ? 917  GLU A CD    1 
ATOM   6596  O OE1   . GLU A  1 919  ? -45.646 91.758  93.263  1.00 43.63 ? 917  GLU A OE1   1 
ATOM   6597  O OE2   . GLU A  1 919  ? -47.631 91.365  94.119  1.00 54.95 ? 917  GLU A OE2   1 
ATOM   6598  N N     . THR A  1 920  ? -41.177 92.861  95.420  1.00 29.82 ? 918  THR A N     1 
ATOM   6599  C CA    . THR A  1 920  ? -39.837 92.760  95.995  1.00 29.22 ? 918  THR A CA    1 
ATOM   6600  C C     . THR A  1 920  ? -39.382 94.071  96.621  1.00 29.34 ? 918  THR A C     1 
ATOM   6601  O O     . THR A  1 920  ? -38.449 94.065  97.426  1.00 27.62 ? 918  THR A O     1 
ATOM   6602  C CB    . THR A  1 920  ? -38.816 92.311  94.938  1.00 29.96 ? 918  THR A CB    1 
ATOM   6603  O OG1   . THR A  1 920  ? -38.776 93.256  93.860  1.00 31.18 ? 918  THR A OG1   1 
ATOM   6604  C CG2   . THR A  1 920  ? -39.164 90.929  94.397  1.00 25.64 ? 918  THR A CG2   1 
ATOM   6605  N N     . GLY A  1 921  ? -40.031 95.187  96.285  1.00 26.99 ? 919  GLY A N     1 
ATOM   6606  C CA    . GLY A  1 921  ? -39.647 96.477  96.833  1.00 30.33 ? 919  GLY A CA    1 
ATOM   6607  C C     . GLY A  1 921  ? -39.655 96.555  98.349  1.00 29.81 ? 919  GLY A C     1 
ATOM   6608  O O     . GLY A  1 921  ? -38.957 97.403  98.917  1.00 32.19 ? 919  GLY A O     1 
ATOM   6609  N N     . VAL A  1 922  ? -40.426 95.692  99.023  1.00 30.56 ? 920  VAL A N     1 
ATOM   6610  C CA    . VAL A  1 922  ? -40.478 95.724  100.487 1.00 29.62 ? 920  VAL A CA    1 
ATOM   6611  C C     . VAL A  1 922  ? -39.306 95.002  101.136 1.00 29.31 ? 920  VAL A C     1 
ATOM   6612  O O     . VAL A  1 922  ? -39.154 95.066  102.361 1.00 29.55 ? 920  VAL A O     1 
ATOM   6613  C CB    . VAL A  1 922  ? -41.798 95.134  101.018 1.00 28.43 ? 920  VAL A CB    1 
ATOM   6614  C CG1   . VAL A  1 922  ? -42.984 96.017  100.617 1.00 30.10 ? 920  VAL A CG1   1 
ATOM   6615  C CG2   . VAL A  1 922  ? -41.994 93.721  100.519 1.00 26.14 ? 920  VAL A CG2   1 
ATOM   6616  N N     . GLY A  1 923  ? -38.472 94.322  100.353 1.00 27.98 ? 921  GLY A N     1 
ATOM   6617  C CA    . GLY A  1 923  ? -37.293 93.673  100.882 1.00 27.59 ? 921  GLY A CA    1 
ATOM   6618  C C     . GLY A  1 923  ? -36.055 94.074  100.106 1.00 25.99 ? 921  GLY A C     1 
ATOM   6619  O O     . GLY A  1 923  ? -36.066 95.072  99.378  1.00 28.71 ? 921  GLY A O     1 
ATOM   6620  N N     . THR A  1 924  ? -34.984 93.300  100.227 1.00 23.10 ? 922  THR A N     1 
ATOM   6621  C CA    . THR A  1 924  ? -33.714 93.646  99.587  1.00 25.25 ? 922  THR A CA    1 
ATOM   6622  C C     . THR A  1 924  ? -33.341 92.517  98.626  1.00 25.18 ? 922  THR A C     1 
ATOM   6623  O O     . THR A  1 924  ? -32.713 91.531  99.009  1.00 22.40 ? 922  THR A O     1 
ATOM   6624  C CB    . THR A  1 924  ? -32.634 93.891  100.636 1.00 25.70 ? 922  THR A CB    1 
ATOM   6625  O OG1   . THR A  1 924  ? -32.554 92.745  101.487 1.00 22.27 ? 922  THR A OG1   1 
ATOM   6626  C CG2   . THR A  1 924  ? -32.981 95.114  101.464 1.00 24.88 ? 922  THR A CG2   1 
ATOM   6627  N N     . PHE A  1 925  ? -33.730 92.667  97.366  1.00 23.60 ? 923  PHE A N     1 
ATOM   6628  C CA    . PHE A  1 925  ? -33.516 91.645  96.357  1.00 23.60 ? 923  PHE A CA    1 
ATOM   6629  C C     . PHE A  1 925  ? -32.550 92.147  95.292  1.00 24.49 ? 923  PHE A C     1 
ATOM   6630  O O     . PHE A  1 925  ? -32.564 93.329  94.917  1.00 25.23 ? 923  PHE A O     1 
ATOM   6631  C CB    . PHE A  1 925  ? -34.834 91.239  95.684  1.00 21.74 ? 923  PHE A CB    1 
ATOM   6632  C CG    . PHE A  1 925  ? -35.802 90.555  96.602  1.00 21.03 ? 923  PHE A CG    1 
ATOM   6633  C CD1   . PHE A  1 925  ? -36.634 91.294  97.424  1.00 21.20 ? 923  PHE A CD1   1 
ATOM   6634  C CD2   . PHE A  1 925  ? -35.894 89.175  96.630  1.00 21.02 ? 923  PHE A CD2   1 
ATOM   6635  C CE1   . PHE A  1 925  ? -37.543 90.662  98.268  1.00 22.63 ? 923  PHE A CE1   1 
ATOM   6636  C CE2   . PHE A  1 925  ? -36.807 88.542  97.458  1.00 20.46 ? 923  PHE A CE2   1 
ATOM   6637  C CZ    . PHE A  1 925  ? -37.630 89.279  98.271  1.00 20.78 ? 923  PHE A CZ    1 
ATOM   6638  N N     . VAL A  1 926  ? -31.723 91.234  94.804  1.00 20.84 ? 924  VAL A N     1 
ATOM   6639  C CA    . VAL A  1 926  ? -30.906 91.445  93.615  1.00 24.49 ? 924  VAL A CA    1 
ATOM   6640  C C     . VAL A  1 926  ? -31.360 90.435  92.583  1.00 24.58 ? 924  VAL A C     1 
ATOM   6641  O O     . VAL A  1 926  ? -31.412 89.236  92.878  1.00 21.09 ? 924  VAL A O     1 
ATOM   6642  C CB    . VAL A  1 926  ? -29.400 91.276  93.901  1.00 23.53 ? 924  VAL A CB    1 
ATOM   6643  C CG1   . VAL A  1 926  ? -28.587 91.375  92.617  1.00 24.36 ? 924  VAL A CG1   1 
ATOM   6644  C CG2   . VAL A  1 926  ? -28.939 92.326  94.912  1.00 25.58 ? 924  VAL A CG2   1 
ATOM   6645  N N     . PRO A  1 927  ? -31.741 90.848  91.384  1.00 25.14 ? 925  PRO A N     1 
ATOM   6646  C CA    . PRO A  1 927  ? -32.136 89.873  90.385  1.00 23.97 ? 925  PRO A CA    1 
ATOM   6647  C C     . PRO A  1 927  ? -30.945 89.031  89.970  1.00 25.28 ? 925  PRO A C     1 
ATOM   6648  O O     . PRO A  1 927  ? -29.838 89.558  89.794  1.00 21.66 ? 925  PRO A O     1 
ATOM   6649  C CB    . PRO A  1 927  ? -32.653 90.734  89.225  1.00 25.06 ? 925  PRO A CB    1 
ATOM   6650  C CG    . PRO A  1 927  ? -32.049 92.053  89.406  1.00 27.79 ? 925  PRO A CG    1 
ATOM   6651  C CD    . PRO A  1 927  ? -31.773 92.231  90.876  1.00 23.90 ? 925  PRO A CD    1 
ATOM   6652  N N     . PRO A  1 928  ? -31.121 87.716  89.866  1.00 22.31 ? 926  PRO A N     1 
ATOM   6653  C CA    . PRO A  1 928  ? -30.089 86.874  89.261  1.00 21.21 ? 926  PRO A CA    1 
ATOM   6654  C C     . PRO A  1 928  ? -29.596 87.456  87.947  1.00 22.05 ? 926  PRO A C     1 
ATOM   6655  O O     . PRO A  1 928  ? -30.382 87.862  87.089  1.00 20.71 ? 926  PRO A O     1 
ATOM   6656  C CB    . PRO A  1 928  ? -30.812 85.540  89.068  1.00 22.72 ? 926  PRO A CB    1 
ATOM   6657  C CG    . PRO A  1 928  ? -31.709 85.487  90.267  1.00 26.42 ? 926  PRO A CG    1 
ATOM   6658  C CD    . PRO A  1 928  ? -32.192 86.912  90.476  1.00 21.47 ? 926  PRO A CD    1 
ATOM   6659  N N     . THR A  1 929  ? -28.273 87.491  87.801  1.00 22.26 ? 927  THR A N     1 
ATOM   6660  C CA    . THR A  1 929  ? -27.608 88.270  86.767  1.00 23.81 ? 927  THR A CA    1 
ATOM   6661  C C     . THR A  1 929  ? -26.533 87.428  86.105  1.00 24.69 ? 927  THR A C     1 
ATOM   6662  O O     . THR A  1 929  ? -25.829 86.680  86.784  1.00 23.85 ? 927  THR A O     1 
ATOM   6663  C CB    . THR A  1 929  ? -26.978 89.536  87.375  1.00 23.52 ? 927  THR A CB    1 
ATOM   6664  O OG1   . THR A  1 929  ? -28.010 90.336  87.948  1.00 24.72 ? 927  THR A OG1   1 
ATOM   6665  C CG2   . THR A  1 929  ? -26.218 90.358  86.335  1.00 24.81 ? 927  THR A CG2   1 
ATOM   6666  N N     . ILE A  1 930  ? -26.399 87.557  84.782  1.00 21.42 ? 928  ILE A N     1 
ATOM   6667  C CA    . ILE A  1 930  ? -25.312 86.931  84.035  1.00 21.73 ? 928  ILE A CA    1 
ATOM   6668  C C     . ILE A  1 930  ? -24.522 88.043  83.370  1.00 25.41 ? 928  ILE A C     1 
ATOM   6669  O O     . ILE A  1 930  ? -25.098 88.872  82.652  1.00 25.94 ? 928  ILE A O     1 
ATOM   6670  C CB    . ILE A  1 930  ? -25.816 85.925  82.983  1.00 22.18 ? 928  ILE A CB    1 
ATOM   6671  C CG1   . ILE A  1 930  ? -26.535 84.745  83.630  1.00 24.85 ? 928  ILE A CG1   1 
ATOM   6672  C CG2   . ILE A  1 930  ? -24.637 85.430  82.134  1.00 22.14 ? 928  ILE A CG2   1 
ATOM   6673  C CD1   . ILE A  1 930  ? -27.340 83.904  82.614  1.00 23.27 ? 928  ILE A CD1   1 
ATOM   6674  N N     . ILE A  1 931  ? -23.213 88.072  83.614  1.00 22.09 ? 929  ILE A N     1 
ATOM   6675  C CA    . ILE A  1 931  ? -22.321 89.081  83.051  1.00 24.60 ? 929  ILE A CA    1 
ATOM   6676  C C     . ILE A  1 931  ? -21.262 88.368  82.219  1.00 26.34 ? 929  ILE A C     1 
ATOM   6677  O O     . ILE A  1 931  ? -20.541 87.506  82.733  1.00 22.46 ? 929  ILE A O     1 
ATOM   6678  C CB    . ILE A  1 931  ? -21.670 89.938  84.150  1.00 24.26 ? 929  ILE A CB    1 
ATOM   6679  C CG1   . ILE A  1 931  ? -22.743 90.595  85.030  1.00 23.98 ? 929  ILE A CG1   1 
ATOM   6680  C CG2   . ILE A  1 931  ? -20.715 90.969  83.544  1.00 26.99 ? 929  ILE A CG2   1 
ATOM   6681  C CD1   . ILE A  1 931  ? -22.151 91.336  86.246  1.00 24.75 ? 929  ILE A CD1   1 
ATOM   6682  N N     . GLU A  1 932  ? -21.161 88.724  80.940  1.00 25.85 ? 930  GLU A N     1 
ATOM   6683  C CA    . GLU A  1 932  ? -20.193 88.097  80.042  1.00 26.53 ? 930  GLU A CA    1 
ATOM   6684  C C     . GLU A  1 932  ? -18.904 88.913  80.038  1.00 28.67 ? 930  GLU A C     1 
ATOM   6685  O O     . GLU A  1 932  ? -18.914 90.102  79.697  1.00 30.30 ? 930  GLU A O     1 
ATOM   6686  C CB    . GLU A  1 932  ? -20.772 87.970  78.633  1.00 24.83 ? 930  GLU A CB    1 
ATOM   6687  C CG    . GLU A  1 932  ? -21.999 87.066  78.586  1.00 28.09 ? 930  GLU A CG    1 
ATOM   6688  C CD    . GLU A  1 932  ? -22.730 87.131  77.263  1.00 33.05 ? 930  GLU A CD    1 
ATOM   6689  O OE1   . GLU A  1 932  ? -22.068 87.003  76.210  1.00 33.45 ? 930  GLU A OE1   1 
ATOM   6690  O OE2   . GLU A  1 932  ? -23.964 87.325  77.278  1.00 32.19 ? 930  GLU A OE2   1 
ATOM   6691  N N     . LEU A  1 933  ? -17.806 88.289  80.442  1.00 24.79 ? 931  LEU A N     1 
ATOM   6692  C CA    . LEU A  1 933  ? -16.539 88.992  80.568  1.00 31.72 ? 931  LEU A CA    1 
ATOM   6693  C C     . LEU A  1 933  ? -15.618 88.660  79.403  1.00 35.63 ? 931  LEU A C     1 
ATOM   6694  O O     . LEU A  1 933  ? -15.716 87.600  78.783  1.00 34.05 ? 931  LEU A O     1 
ATOM   6695  C CB    . LEU A  1 933  ? -15.843 88.640  81.886  1.00 32.96 ? 931  LEU A CB    1 
ATOM   6696  C CG    . LEU A  1 933  ? -16.580 89.031  83.174  1.00 31.83 ? 931  LEU A CG    1 
ATOM   6697  C CD1   . LEU A  1 933  ? -15.813 88.529  84.383  1.00 29.28 ? 931  LEU A CD1   1 
ATOM   6698  C CD2   . LEU A  1 933  ? -16.783 90.536  83.251  1.00 33.17 ? 931  LEU A CD2   1 
ATOM   6699  N N     . GLU A  1 934  ? -14.699 89.584  79.121  1.00 36.83 ? 932  GLU A N     1 
ATOM   6700  C CA    . GLU A  1 934  ? -13.668 89.324  78.122  1.00 36.95 ? 932  GLU A CA    1 
ATOM   6701  C C     . GLU A  1 934  ? -12.589 88.400  78.677  1.00 46.21 ? 932  GLU A C     1 
ATOM   6702  O O     . GLU A  1 934  ? -12.227 87.404  78.041  1.00 42.91 ? 932  GLU A O     1 
ATOM   6703  C CB    . GLU A  1 934  ? -13.058 90.642  77.640  1.00 41.26 ? 932  GLU A CB    1 
ATOM   6704  N N     . LYS A  1 935  ? -12.080 88.704  79.872  1.00 42.64 ? 933  LYS A N     1 
ATOM   6705  C CA    . LYS A  1 935  ? -11.034 87.917  80.510  1.00 46.39 ? 933  LYS A CA    1 
ATOM   6706  C C     . LYS A  1 935  ? -11.392 87.675  81.969  1.00 41.32 ? 933  LYS A C     1 
ATOM   6707  O O     . LYS A  1 935  ? -12.097 88.475  82.591  1.00 40.12 ? 933  LYS A O     1 
ATOM   6708  C CB    . LYS A  1 935  ? -9.669  88.619  80.425  1.00 44.86 ? 933  LYS A CB    1 
ATOM   6709  N N     . LEU A  1 936  ? -10.899 86.558  82.512  1.00 40.13 ? 934  LEU A N     1 
ATOM   6710  C CA    . LEU A  1 936  ? -11.081 86.290  83.933  1.00 44.55 ? 934  LEU A CA    1 
ATOM   6711  C C     . LEU A  1 936  ? -10.511 87.407  84.792  1.00 43.86 ? 934  LEU A C     1 
ATOM   6712  O O     . LEU A  1 936  ? -10.945 87.577  85.935  1.00 41.64 ? 934  LEU A O     1 
ATOM   6713  C CB    . LEU A  1 936  ? -10.438 84.957  84.321  1.00 43.19 ? 934  LEU A CB    1 
ATOM   6714  N N     . SER A  1 937  ? -9.570  88.184  84.260  1.00 44.32 ? 935  SER A N     1 
ATOM   6715  C CA    . SER A  1 937  ? -8.984  89.303  84.983  1.00 43.97 ? 935  SER A CA    1 
ATOM   6716  C C     . SER A  1 937  ? -9.910  90.510  85.072  1.00 43.08 ? 935  SER A C     1 
ATOM   6717  O O     . SER A  1 937  ? -9.641  91.415  85.870  1.00 44.86 ? 935  SER A O     1 
ATOM   6718  C CB    . SER A  1 937  ? -7.657  89.706  84.327  1.00 44.97 ? 935  SER A CB    1 
ATOM   6719  O OG    . SER A  1 937  ? -7.768  89.681  82.914  1.00 47.75 ? 935  SER A OG    1 
ATOM   6720  N N     . ASP A  1 938  ? -10.988 90.554  84.285  1.00 43.36 ? 936  ASP A N     1 
ATOM   6721  C CA    . ASP A  1 938  ? -11.973 91.618  84.450  1.00 41.98 ? 936  ASP A CA    1 
ATOM   6722  C C     . ASP A  1 938  ? -12.629 91.573  85.819  1.00 40.14 ? 936  ASP A C     1 
ATOM   6723  O O     . ASP A  1 938  ? -13.135 92.600  86.291  1.00 41.18 ? 936  ASP A O     1 
ATOM   6724  C CB    . ASP A  1 938  ? -13.051 91.525  83.374  1.00 40.95 ? 936  ASP A CB    1 
ATOM   6725  C CG    . ASP A  1 938  ? -12.477 91.506  81.977  1.00 47.84 ? 936  ASP A CG    1 
ATOM   6726  O OD1   . ASP A  1 938  ? -11.255 91.731  81.833  1.00 49.69 ? 936  ASP A OD1   1 
ATOM   6727  O OD2   . ASP A  1 938  ? -13.247 91.255  81.021  1.00 48.58 ? 936  ASP A OD2   1 
ATOM   6728  N N     . LEU A  1 939  ? -12.635 90.408  86.460  1.00 37.36 ? 937  LEU A N     1 
ATOM   6729  C CA    A LEU A  1 939  ? -13.252 90.233  87.767  0.63 39.05 ? 937  LEU A CA    1 
ATOM   6730  C CA    B LEU A  1 939  ? -13.253 90.230  87.768  0.37 39.04 ? 937  LEU A CA    1 
ATOM   6731  C C     . LEU A  1 939  ? -12.178 90.412  88.833  1.00 39.66 ? 937  LEU A C     1 
ATOM   6732  O O     . LEU A  1 939  ? -11.301 89.555  88.992  1.00 40.14 ? 937  LEU A O     1 
ATOM   6733  C CB    A LEU A  1 939  ? -13.909 88.859  87.868  0.63 36.18 ? 937  LEU A CB    1 
ATOM   6734  C CB    B LEU A  1 939  ? -13.905 88.854  87.874  0.37 36.21 ? 937  LEU A CB    1 
ATOM   6735  C CG    A LEU A  1 939  ? -14.783 88.630  89.097  0.63 35.61 ? 937  LEU A CG    1 
ATOM   6736  C CG    B LEU A  1 939  ? -15.329 88.777  88.431  0.37 34.64 ? 937  LEU A CG    1 
ATOM   6737  C CD1   A LEU A  1 939  ? -15.933 89.625  89.114  0.63 33.95 ? 937  LEU A CD1   1 
ATOM   6738  C CD1   B LEU A  1 939  ? -15.672 87.342  88.802  0.37 33.29 ? 937  LEU A CD1   1 
ATOM   6739  C CD2   A LEU A  1 939  ? -15.307 87.204  89.108  0.63 33.37 ? 937  LEU A CD2   1 
ATOM   6740  C CD2   B LEU A  1 939  ? -15.509 89.701  89.624  0.37 34.63 ? 937  LEU A CD2   1 
ATOM   6741  N N     . GLN A  1 940  ? -12.250 91.519  89.568  1.00 38.03 ? 938  GLN A N     1 
ATOM   6742  C CA    . GLN A  1 940  ? -11.213 91.868  90.532  1.00 42.63 ? 938  GLN A CA    1 
ATOM   6743  C C     . GLN A  1 940  ? -11.692 91.883  91.981  1.00 47.16 ? 938  GLN A C     1 
ATOM   6744  O O     . GLN A  1 940  ? -10.946 92.335  92.859  1.00 47.48 ? 938  GLN A O     1 
ATOM   6745  C CB    . GLN A  1 940  ? -10.611 93.228  90.166  1.00 43.49 ? 938  GLN A CB    1 
ATOM   6746  N N     . ARG A  1 941  ? -12.899 91.397  92.265  1.00 44.92 ? 939  ARG A N     1 
ATOM   6747  C CA    . ARG A  1 941  ? -13.417 91.400  93.627  1.00 43.87 ? 939  ARG A CA    1 
ATOM   6748  C C     . ARG A  1 941  ? -14.431 90.276  93.780  1.00 39.11 ? 939  ARG A C     1 
ATOM   6749  O O     . ARG A  1 941  ? -15.116 89.909  92.823  1.00 37.23 ? 939  ARG A O     1 
ATOM   6750  C CB    . ARG A  1 941  ? -14.065 92.748  93.973  1.00 44.51 ? 939  ARG A CB    1 
ATOM   6751  N N     . GLU A  1 942  ? -14.517 89.719  94.984  1.00 42.20 ? 940  GLU A N     1 
ATOM   6752  C CA    . GLU A  1 942  ? -15.582 88.764  95.264  1.00 40.60 ? 940  GLU A CA    1 
ATOM   6753  C C     . GLU A  1 942  ? -16.910 89.503  95.334  1.00 39.06 ? 940  GLU A C     1 
ATOM   6754  O O     . GLU A  1 942  ? -17.031 90.522  96.020  1.00 40.70 ? 940  GLU A O     1 
ATOM   6755  C CB    . GLU A  1 942  ? -15.335 88.011  96.570  1.00 44.62 ? 940  GLU A CB    1 
ATOM   6756  C CG    . GLU A  1 942  ? -16.187 86.735  96.669  1.00 45.12 ? 940  GLU A CG    1 
ATOM   6757  C CD    . GLU A  1 942  ? -16.222 86.118  98.062  1.00 50.24 ? 940  GLU A CD    1 
ATOM   6758  O OE1   . GLU A  1 942  ? -15.947 86.835  99.051  1.00 51.63 ? 940  GLU A OE1   1 
ATOM   6759  O OE2   . GLU A  1 942  ? -16.532 84.906  98.161  1.00 45.52 ? 940  GLU A OE2   1 
ATOM   6760  N N     . VAL A  1 943  ? -17.900 89.008  94.601  1.00 33.14 ? 941  VAL A N     1 
ATOM   6761  C CA    . VAL A  1 943  ? -19.231 89.607  94.569  1.00 30.87 ? 941  VAL A CA    1 
ATOM   6762  C C     . VAL A  1 943  ? -20.173 88.573  95.164  1.00 30.00 ? 941  VAL A C     1 
ATOM   6763  O O     . VAL A  1 943  ? -20.501 87.571  94.517  1.00 25.81 ? 941  VAL A O     1 
ATOM   6764  C CB    . VAL A  1 943  ? -19.651 90.012  93.155  1.00 27.23 ? 941  VAL A CB    1 
ATOM   6765  C CG1   . VAL A  1 943  ? -21.083 90.548  93.151  1.00 28.47 ? 941  VAL A CG1   1 
ATOM   6766  C CG2   . VAL A  1 943  ? -18.688 91.054  92.620  1.00 35.60 ? 941  VAL A CG2   1 
ATOM   6767  N N     . PHE A  1 944  ? -20.595 88.800  96.407  1.00 27.28 ? 942  PHE A N     1 
ATOM   6768  C CA    . PHE A  1 944  ? -21.292 87.776  97.181  1.00 25.67 ? 942  PHE A CA    1 
ATOM   6769  C C     . PHE A  1 944  ? -22.799 87.905  96.969  1.00 24.80 ? 942  PHE A C     1 
ATOM   6770  O O     . PHE A  1 944  ? -23.560 88.307  97.846  1.00 25.54 ? 942  PHE A O     1 
ATOM   6771  C CB    . PHE A  1 944  ? -20.921 87.886  98.656  1.00 24.70 ? 942  PHE A CB    1 
ATOM   6772  C CG    . PHE A  1 944  ? -21.017 86.580  99.394  1.00 25.58 ? 942  PHE A CG    1 
ATOM   6773  C CD1   . PHE A  1 944  ? -20.072 85.585  99.183  1.00 25.35 ? 942  PHE A CD1   1 
ATOM   6774  C CD2   . PHE A  1 944  ? -22.039 86.350  100.299 1.00 24.93 ? 942  PHE A CD2   1 
ATOM   6775  C CE1   . PHE A  1 944  ? -20.153 84.386  99.853  1.00 26.91 ? 942  PHE A CE1   1 
ATOM   6776  C CE2   . PHE A  1 944  ? -22.129 85.148  100.974 1.00 24.57 ? 942  PHE A CE2   1 
ATOM   6777  C CZ    . PHE A  1 944  ? -21.181 84.164  100.749 1.00 23.74 ? 942  PHE A CZ    1 
ATOM   6778  N N     . GLY A  1 945  ? -23.230 87.524  95.771  1.00 20.20 ? 943  GLY A N     1 
ATOM   6779  C CA    . GLY A  1 945  ? -24.602 87.704  95.377  1.00 21.66 ? 943  GLY A CA    1 
ATOM   6780  C C     . GLY A  1 945  ? -24.905 86.876  94.152  1.00 21.40 ? 943  GLY A C     1 
ATOM   6781  O O     . GLY A  1 945  ? -24.041 86.158  93.638  1.00 22.20 ? 943  GLY A O     1 
ATOM   6782  N N     . PRO A  1 946  ? -26.145 86.983  93.635  1.00 20.49 ? 944  PRO A N     1 
ATOM   6783  C CA    . PRO A  1 946  ? -26.565 86.118  92.516  1.00 20.51 ? 944  PRO A CA    1 
ATOM   6784  C C     . PRO A  1 946  ? -26.058 86.662  91.187  1.00 22.11 ? 944  PRO A C     1 
ATOM   6785  O O     . PRO A  1 946  ? -26.811 87.141  90.334  1.00 21.00 ? 944  PRO A O     1 
ATOM   6786  C CB    . PRO A  1 946  ? -28.091 86.160  92.627  1.00 19.40 ? 944  PRO A CB    1 
ATOM   6787  C CG    . PRO A  1 946  ? -28.370 87.552  93.100  1.00 20.30 ? 944  PRO A CG    1 
ATOM   6788  C CD    . PRO A  1 946  ? -27.183 87.966  93.990  1.00 21.26 ? 944  PRO A CD    1 
ATOM   6789  N N     . VAL A  1 947  ? -24.743 86.617  90.995  1.00 21.76 ? 945  VAL A N     1 
ATOM   6790  C CA    . VAL A  1 947  ? -24.125 87.248  89.833  1.00 21.10 ? 945  VAL A CA    1 
ATOM   6791  C C     . VAL A  1 947  ? -23.113 86.284  89.237  1.00 23.12 ? 945  VAL A C     1 
ATOM   6792  O O     . VAL A  1 947  ? -22.052 86.048  89.825  1.00 24.55 ? 945  VAL A O     1 
ATOM   6793  C CB    . VAL A  1 947  ? -23.460 88.584  90.184  1.00 22.65 ? 945  VAL A CB    1 
ATOM   6794  C CG1   . VAL A  1 947  ? -22.758 89.156  88.968  1.00 21.68 ? 945  VAL A CG1   1 
ATOM   6795  C CG2   . VAL A  1 947  ? -24.487 89.554  90.748  1.00 20.43 ? 945  VAL A CG2   1 
ATOM   6796  N N     . LEU A  1 948  ? -23.432 85.740  88.067  1.00 22.11 ? 946  LEU A N     1 
ATOM   6797  C CA    . LEU A  1 948  ? -22.596 84.772  87.373  1.00 22.23 ? 946  LEU A CA    1 
ATOM   6798  C C     . LEU A  1 948  ? -21.801 85.471  86.276  1.00 21.56 ? 946  LEU A C     1 
ATOM   6799  O O     . LEU A  1 948  ? -22.375 86.153  85.428  1.00 22.50 ? 946  LEU A O     1 
ATOM   6800  C CB    . LEU A  1 948  ? -23.449 83.662  86.752  1.00 22.00 ? 946  LEU A CB    1 
ATOM   6801  C CG    . LEU A  1 948  ? -22.616 82.675  85.939  1.00 20.84 ? 946  LEU A CG    1 
ATOM   6802  C CD1   . LEU A  1 948  ? -21.543 81.954  86.814  1.00 18.78 ? 946  LEU A CD1   1 
ATOM   6803  C CD2   . LEU A  1 948  ? -23.533 81.674  85.261  1.00 21.49 ? 946  LEU A CD2   1 
ATOM   6804  N N     . HIS A  1 949  ? -20.487 85.289  86.284  1.00 23.11 ? 947  HIS A N     1 
ATOM   6805  C CA    . HIS A  1 949  ? -19.646 85.811  85.218  1.00 21.90 ? 947  HIS A CA    1 
ATOM   6806  C C     . HIS A  1 949  ? -19.298 84.682  84.259  1.00 21.79 ? 947  HIS A C     1 
ATOM   6807  O O     . HIS A  1 949  ? -19.072 83.545  84.678  1.00 23.73 ? 947  HIS A O     1 
ATOM   6808  C CB    . HIS A  1 949  ? -18.392 86.454  85.797  1.00 21.89 ? 947  HIS A CB    1 
ATOM   6809  C CG    . HIS A  1 949  ? -18.696 87.510  86.812  1.00 24.02 ? 947  HIS A CG    1 
ATOM   6810  N ND1   . HIS A  1 949  ? -18.915 87.219  88.141  1.00 24.35 ? 947  HIS A ND1   1 
ATOM   6811  C CD2   . HIS A  1 949  ? -18.892 88.844  86.680  1.00 23.49 ? 947  HIS A CD2   1 
ATOM   6812  C CE1   . HIS A  1 949  ? -19.191 88.335  88.793  1.00 25.37 ? 947  HIS A CE1   1 
ATOM   6813  N NE2   . HIS A  1 949  ? -19.190 89.334  87.928  1.00 25.77 ? 947  HIS A NE2   1 
ATOM   6814  N N     . VAL A  1 950  ? -19.305 84.985  82.963  1.00 21.78 ? 948  VAL A N     1 
ATOM   6815  C CA    . VAL A  1 950  ? -19.076 83.987  81.927  1.00 22.84 ? 948  VAL A CA    1 
ATOM   6816  C C     . VAL A  1 950  ? -17.907 84.434  81.062  1.00 24.55 ? 948  VAL A C     1 
ATOM   6817  O O     . VAL A  1 950  ? -17.882 85.575  80.579  1.00 24.20 ? 948  VAL A O     1 
ATOM   6818  C CB    . VAL A  1 950  ? -20.328 83.760  81.060  1.00 23.67 ? 948  VAL A CB    1 
ATOM   6819  C CG1   . VAL A  1 950  ? -20.059 82.663  80.028  1.00 23.61 ? 948  VAL A CG1   1 
ATOM   6820  C CG2   . VAL A  1 950  ? -21.541 83.403  81.915  1.00 21.26 ? 948  VAL A CG2   1 
ATOM   6821  N N     . ILE A  1 951  ? -16.957 83.524  80.843  1.00 23.01 ? 949  ILE A N     1 
ATOM   6822  C CA    . ILE A  1 951  ? -15.865 83.728  79.901  1.00 25.33 ? 949  ILE A CA    1 
ATOM   6823  C C     . ILE A  1 951  ? -15.810 82.523  78.972  1.00 26.40 ? 949  ILE A C     1 
ATOM   6824  O O     . ILE A  1 951  ? -16.275 81.432  79.307  1.00 24.13 ? 949  ILE A O     1 
ATOM   6825  C CB    . ILE A  1 951  ? -14.506 83.937  80.603  1.00 29.73 ? 949  ILE A CB    1 
ATOM   6826  C CG1   . ILE A  1 951  ? -14.085 82.669  81.337  1.00 27.98 ? 949  ILE A CG1   1 
ATOM   6827  C CG2   . ILE A  1 951  ? -14.583 85.098  81.586  1.00 31.26 ? 949  ILE A CG2   1 
ATOM   6828  C CD1   . ILE A  1 951  ? -12.798 82.833  82.108  1.00 32.42 ? 949  ILE A CD1   1 
ATOM   6829  N N     . ARG A  1 952  ? -15.236 82.735  77.788  1.00 24.18 ? 950  ARG A N     1 
ATOM   6830  C CA    . ARG A  1 952  ? -15.078 81.693  76.783  1.00 26.50 ? 950  ARG A CA    1 
ATOM   6831  C C     . ARG A  1 952  ? -13.599 81.372  76.603  1.00 27.86 ? 950  ARG A C     1 
ATOM   6832  O O     . ARG A  1 952  ? -12.744 82.245  76.763  1.00 25.93 ? 950  ARG A O     1 
ATOM   6833  C CB    . ARG A  1 952  ? -15.685 82.138  75.449  1.00 30.11 ? 950  ARG A CB    1 
ATOM   6834  C CG    . ARG A  1 952  ? -17.058 82.766  75.602  1.00 35.11 ? 950  ARG A CG    1 
ATOM   6835  C CD    . ARG A  1 952  ? -17.334 83.754  74.478  1.00 35.44 ? 950  ARG A CD    1 
ATOM   6836  N NE    . ARG A  1 952  ? -17.758 83.069  73.265  1.00 38.75 ? 950  ARG A NE    1 
ATOM   6837  C CZ    . ARG A  1 952  ? -19.018 82.980  72.857  1.00 35.58 ? 950  ARG A CZ    1 
ATOM   6838  N NH1   . ARG A  1 952  ? -20.006 83.546  73.533  1.00 35.68 ? 950  ARG A NH1   1 
ATOM   6839  N NH2   . ARG A  1 952  ? -19.294 82.301  71.750  1.00 33.31 ? 950  ARG A NH2   1 
ATOM   6840  N N     . TYR A  1 953  ? -13.289 80.118  76.255  1.00 27.12 ? 951  TYR A N     1 
ATOM   6841  C CA    . TYR A  1 953  ? -11.892 79.734  76.076  1.00 26.77 ? 951  TYR A CA    1 
ATOM   6842  C C     . TYR A  1 953  ? -11.737 78.788  74.892  1.00 27.54 ? 951  TYR A C     1 
ATOM   6843  O O     . TYR A  1 953  ? -12.634 78.004  74.573  1.00 28.86 ? 951  TYR A O     1 
ATOM   6844  C CB    . TYR A  1 953  ? -11.306 79.068  77.349  1.00 27.02 ? 951  TYR A CB    1 
ATOM   6845  C CG    . TYR A  1 953  ? -11.806 77.657  77.610  1.00 26.50 ? 951  TYR A CG    1 
ATOM   6846  C CD1   . TYR A  1 953  ? -13.001 77.438  78.283  1.00 21.29 ? 951  TYR A CD1   1 
ATOM   6847  C CD2   . TYR A  1 953  ? -11.078 76.547  77.190  1.00 24.16 ? 951  TYR A CD2   1 
ATOM   6848  C CE1   . TYR A  1 953  ? -13.452 76.157  78.534  1.00 21.74 ? 951  TYR A CE1   1 
ATOM   6849  C CE2   . TYR A  1 953  ? -11.537 75.256  77.430  1.00 21.98 ? 951  TYR A CE2   1 
ATOM   6850  C CZ    . TYR A  1 953  ? -12.720 75.070  78.103  1.00 19.40 ? 951  TYR A CZ    1 
ATOM   6851  O OH    . TYR A  1 953  ? -13.201 73.796  78.334  1.00 22.15 ? 951  TYR A OH    1 
ATOM   6852  N N     . ARG A  1 954  ? -10.572 78.853  74.256  1.00 29.99 ? 952  ARG A N     1 
ATOM   6853  C CA    . ARG A  1 954  ? -10.227 77.889  73.222  1.00 32.22 ? 952  ARG A CA    1 
ATOM   6854  C C     . ARG A  1 954  ? -9.661  76.616  73.842  1.00 29.02 ? 952  ARG A C     1 
ATOM   6855  O O     . ARG A  1 954  ? -8.947  76.662  74.845  1.00 31.18 ? 952  ARG A O     1 
ATOM   6856  C CB    . ARG A  1 954  ? -9.215  78.497  72.253  1.00 35.67 ? 952  ARG A CB    1 
ATOM   6857  C CG    . ARG A  1 954  ? -9.664  79.824  71.677  1.00 41.44 ? 952  ARG A CG    1 
ATOM   6858  C CD    . ARG A  1 954  ? -9.227  79.942  70.239  1.00 50.02 ? 952  ARG A CD    1 
ATOM   6859  N NE    . ARG A  1 954  ? -10.124 80.776  69.448  1.00 54.45 ? 952  ARG A NE    1 
ATOM   6860  C CZ    . ARG A  1 954  ? -11.353 80.429  69.092  1.00 53.68 ? 952  ARG A CZ    1 
ATOM   6861  N NH1   . ARG A  1 954  ? -11.908 79.303  69.521  1.00 48.63 ? 952  ARG A NH1   1 
ATOM   6862  N NH2   . ARG A  1 954  ? -12.046 81.235  68.291  1.00 52.42 ? 952  ARG A NH2   1 
ATOM   6863  N N     . ARG A  1 955  ? -9.969  75.470  73.218  1.00 30.65 ? 953  ARG A N     1 
ATOM   6864  C CA    . ARG A  1 955  ? -9.585  74.184  73.805  1.00 29.42 ? 953  ARG A CA    1 
ATOM   6865  C C     . ARG A  1 955  ? -8.080  74.102  74.058  1.00 30.88 ? 953  ARG A C     1 
ATOM   6866  O O     . ARG A  1 955  ? -7.652  73.614  75.110  1.00 36.78 ? 953  ARG A O     1 
ATOM   6867  C CB    . ARG A  1 955  ? -10.041 73.024  72.912  1.00 34.54 ? 953  ARG A CB    1 
ATOM   6868  C CG    . ARG A  1 955  ? -9.572  71.615  73.370  1.00 38.42 ? 953  ARG A CG    1 
ATOM   6869  C CD    . ARG A  1 955  ? -9.750  71.421  74.877  1.00 37.10 ? 953  ARG A CD    1 
ATOM   6870  N NE    . ARG A  1 955  ? -9.365  70.116  75.412  1.00 44.58 ? 953  ARG A NE    1 
ATOM   6871  C CZ    . ARG A  1 955  ? -8.256  69.871  76.103  1.00 44.78 ? 953  ARG A CZ    1 
ATOM   6872  N NH1   . ARG A  1 955  ? -7.324  70.797  76.274  1.00 39.42 ? 953  ARG A NH1   1 
ATOM   6873  N NH2   . ARG A  1 955  ? -8.078  68.663  76.640  1.00 41.07 ? 953  ARG A NH2   1 
ATOM   6874  N N     . ASP A  1 956  ? -7.257  74.576  73.112  1.00 29.69 ? 954  ASP A N     1 
ATOM   6875  C CA    . ASP A  1 956  ? -5.810  74.498  73.316  1.00 32.36 ? 954  ASP A CA    1 
ATOM   6876  C C     . ASP A  1 956  ? -5.341  75.373  74.468  1.00 32.98 ? 954  ASP A C     1 
ATOM   6877  O O     . ASP A  1 956  ? -4.227  75.175  74.970  1.00 35.68 ? 954  ASP A O     1 
ATOM   6878  C CB    . ASP A  1 956  ? -5.062  74.884  72.037  1.00 33.92 ? 954  ASP A CB    1 
ATOM   6879  C CG    . ASP A  1 956  ? -5.148  73.816  70.964  1.00 35.43 ? 954  ASP A CG    1 
ATOM   6880  O OD1   . ASP A  1 956  ? -5.561  72.680  71.282  1.00 36.42 ? 954  ASP A OD1   1 
ATOM   6881  O OD2   . ASP A  1 956  ? -4.809  74.124  69.801  1.00 43.44 ? 954  ASP A OD2   1 
ATOM   6882  N N     . ASP A  1 957  ? -6.163  76.328  74.902  1.00 30.83 ? 955  ASP A N     1 
ATOM   6883  C CA    . ASP A  1 957  ? -5.825  77.220  76.002  1.00 29.52 ? 955  ASP A CA    1 
ATOM   6884  C C     . ASP A  1 957  ? -6.310  76.714  77.357  1.00 27.32 ? 955  ASP A C     1 
ATOM   6885  O O     . ASP A  1 957  ? -6.223  77.456  78.338  1.00 27.89 ? 955  ASP A O     1 
ATOM   6886  C CB    . ASP A  1 957  ? -6.400  78.614  75.746  1.00 31.60 ? 955  ASP A CB    1 
ATOM   6887  C CG    . ASP A  1 957  ? -5.658  79.356  74.663  1.00 37.53 ? 955  ASP A CG    1 
ATOM   6888  O OD1   . ASP A  1 957  ? -4.438  79.139  74.531  1.00 39.56 ? 955  ASP A OD1   1 
ATOM   6889  O OD2   . ASP A  1 957  ? -6.294  80.157  73.938  1.00 39.99 ? 955  ASP A OD2   1 
ATOM   6890  N N     . LEU A  1 958  ? -6.787  75.470  77.439  1.00 26.01 ? 956  LEU A N     1 
ATOM   6891  C CA    . LEU A  1 958  ? -7.311  74.947  78.703  1.00 25.58 ? 956  LEU A CA    1 
ATOM   6892  C C     . LEU A  1 958  ? -6.279  75.041  79.822  1.00 26.79 ? 956  LEU A C     1 
ATOM   6893  O O     . LEU A  1 958  ? -6.591  75.474  80.938  1.00 23.61 ? 956  LEU A O     1 
ATOM   6894  C CB    . LEU A  1 958  ? -7.769  73.501  78.522  1.00 28.52 ? 956  LEU A CB    1 
ATOM   6895  C CG    . LEU A  1 958  ? -8.321  72.793  79.767  1.00 28.89 ? 956  LEU A CG    1 
ATOM   6896  C CD1   . LEU A  1 958  ? -9.496  73.563  80.383  1.00 22.26 ? 956  LEU A CD1   1 
ATOM   6897  C CD2   . LEU A  1 958  ? -8.724  71.369  79.422  1.00 26.51 ? 956  LEU A CD2   1 
ATOM   6898  N N     . ASP A  1 959  ? -5.039  74.638  79.545  1.00 26.67 ? 957  ASP A N     1 
ATOM   6899  C CA    . ASP A  1 959  ? -4.039  74.632  80.607  1.00 26.80 ? 957  ASP A CA    1 
ATOM   6900  C C     . ASP A  1 959  ? -3.739  76.047  81.083  1.00 23.39 ? 957  ASP A C     1 
ATOM   6901  O O     . ASP A  1 959  ? -3.562  76.282  82.281  1.00 26.18 ? 957  ASP A O     1 
ATOM   6902  C CB    . ASP A  1 959  ? -2.760  73.946  80.136  1.00 30.30 ? 957  ASP A CB    1 
ATOM   6903  C CG    . ASP A  1 959  ? -1.816  73.660  81.281  1.00 29.64 ? 957  ASP A CG    1 
ATOM   6904  O OD1   . ASP A  1 959  ? -2.255  73.022  82.256  1.00 30.14 ? 957  ASP A OD1   1 
ATOM   6905  O OD2   . ASP A  1 959  ? -0.651  74.095  81.226  1.00 38.36 ? 957  ASP A OD2   1 
ATOM   6906  N N     . ARG A  1 960  ? -3.685  77.003  80.162  1.00 25.01 ? 958  ARG A N     1 
ATOM   6907  C CA    . ARG A  1 960  ? -3.504  78.384  80.574  1.00 26.58 ? 958  ARG A CA    1 
ATOM   6908  C C     . ARG A  1 960  ? -4.711  78.882  81.366  1.00 29.76 ? 958  ARG A C     1 
ATOM   6909  O O     . ARG A  1 960  ? -4.555  79.628  82.345  1.00 29.19 ? 958  ARG A O     1 
ATOM   6910  C CB    . ARG A  1 960  ? -3.261  79.257  79.347  1.00 30.71 ? 958  ARG A CB    1 
ATOM   6911  C CG    . ARG A  1 960  ? -2.874  80.670  79.674  1.00 35.60 ? 958  ARG A CG    1 
ATOM   6912  C CD    . ARG A  1 960  ? -2.721  81.483  78.408  1.00 43.05 ? 958  ARG A CD    1 
ATOM   6913  N NE    . ARG A  1 960  ? -1.800  80.861  77.462  1.00 49.10 ? 958  ARG A NE    1 
ATOM   6914  C CZ    . ARG A  1 960  ? -0.478  80.951  77.533  1.00 48.71 ? 958  ARG A CZ    1 
ATOM   6915  N NH1   . ARG A  1 960  ? 0.121   81.580  78.535  1.00 50.72 ? 958  ARG A NH1   1 
ATOM   6916  N NH2   . ARG A  1 960  ? 0.263   80.398  76.575  1.00 50.15 ? 958  ARG A NH2   1 
ATOM   6917  N N     . LEU A  1 961  ? -5.923  78.489  80.955  1.00 26.59 ? 959  LEU A N     1 
ATOM   6918  C CA    . LEU A  1 961  ? -7.114  78.895  81.701  1.00 27.10 ? 959  LEU A CA    1 
ATOM   6919  C C     . LEU A  1 961  ? -7.051  78.412  83.143  1.00 27.05 ? 959  LEU A C     1 
ATOM   6920  O O     . LEU A  1 961  ? -7.353  79.171  84.072  1.00 27.66 ? 959  LEU A O     1 
ATOM   6921  C CB    . LEU A  1 961  ? -8.381  78.375  81.017  1.00 25.88 ? 959  LEU A CB    1 
ATOM   6922  C CG    . LEU A  1 961  ? -9.688  78.480  81.825  1.00 26.80 ? 959  LEU A CG    1 
ATOM   6923  C CD1   . LEU A  1 961  ? -10.056 79.930  82.123  1.00 29.48 ? 959  LEU A CD1   1 
ATOM   6924  C CD2   . LEU A  1 961  ? -10.833 77.787  81.104  1.00 25.93 ? 959  LEU A CD2   1 
ATOM   6925  N N     . VAL A  1 962  ? -6.650  77.154  83.353  1.00 24.24 ? 960  VAL A N     1 
ATOM   6926  C CA    . VAL A  1 962  ? -6.495  76.648  84.717  1.00 26.50 ? 960  VAL A CA    1 
ATOM   6927  C C     . VAL A  1 962  ? -5.519  77.515  85.500  1.00 27.55 ? 960  VAL A C     1 
ATOM   6928  O O     . VAL A  1 962  ? -5.744  77.808  86.680  1.00 24.44 ? 960  VAL A O     1 
ATOM   6929  C CB    . VAL A  1 962  ? -6.055  75.172  84.702  1.00 26.72 ? 960  VAL A CB    1 
ATOM   6930  C CG1   . VAL A  1 962  ? -5.701  74.696  86.136  1.00 22.97 ? 960  VAL A CG1   1 
ATOM   6931  C CG2   . VAL A  1 962  ? -7.153  74.308  84.086  1.00 27.30 ? 960  VAL A CG2   1 
ATOM   6932  N N     . ASP A  1 963  ? -4.423  77.941  84.854  1.00 27.77 ? 961  ASP A N     1 
ATOM   6933  C CA    . ASP A  1 963  ? -3.497  78.883  85.486  1.00 27.65 ? 961  ASP A CA    1 
ATOM   6934  C C     . ASP A  1 963  ? -4.203  80.173  85.888  1.00 29.15 ? 961  ASP A C     1 
ATOM   6935  O O     . ASP A  1 963  ? -3.952  80.713  86.974  1.00 30.84 ? 961  ASP A O     1 
ATOM   6936  C CB    . ASP A  1 963  ? -2.339  79.224  84.544  1.00 26.73 ? 961  ASP A CB    1 
ATOM   6937  C CG    . ASP A  1 963  ? -1.360  78.108  84.391  1.00 32.32 ? 961  ASP A CG    1 
ATOM   6938  O OD1   . ASP A  1 963  ? -1.404  77.158  85.201  1.00 36.53 ? 961  ASP A OD1   1 
ATOM   6939  O OD2   . ASP A  1 963  ? -0.523  78.192  83.457  1.00 39.73 ? 961  ASP A OD2   1 
ATOM   6940  N N     . ASP A  1 964  ? -5.050  80.706  85.001  1.00 27.56 ? 962  ASP A N     1 
ATOM   6941  C CA    . ASP A  1 964  ? -5.772  81.942  85.301  1.00 33.26 ? 962  ASP A CA    1 
ATOM   6942  C C     . ASP A  1 964  ? -6.704  81.759  86.492  1.00 32.15 ? 962  ASP A C     1 
ATOM   6943  O O     . ASP A  1 964  ? -6.794  82.637  87.357  1.00 36.11 ? 962  ASP A O     1 
ATOM   6944  C CB    . ASP A  1 964  ? -6.579  82.411  84.087  1.00 33.20 ? 962  ASP A CB    1 
ATOM   6945  C CG    . ASP A  1 964  ? -5.706  82.790  82.902  1.00 37.62 ? 962  ASP A CG    1 
ATOM   6946  O OD1   . ASP A  1 964  ? -4.466  82.852  83.058  1.00 39.39 ? 962  ASP A OD1   1 
ATOM   6947  O OD2   . ASP A  1 964  ? -6.273  83.016  81.806  1.00 44.51 ? 962  ASP A OD2   1 
ATOM   6948  N N     . VAL A  1 965  ? -7.411  80.627  86.548  1.00 26.93 ? 963  VAL A N     1 
ATOM   6949  C CA    . VAL A  1 965  ? -8.247  80.334  87.710  1.00 29.49 ? 963  VAL A CA    1 
ATOM   6950  C C     . VAL A  1 965  ? -7.399  80.303  88.975  1.00 29.28 ? 963  VAL A C     1 
ATOM   6951  O O     . VAL A  1 965  ? -7.730  80.943  89.983  1.00 29.20 ? 963  VAL A O     1 
ATOM   6952  C CB    . VAL A  1 965  ? -9.007  79.012  87.506  1.00 26.60 ? 963  VAL A CB    1 
ATOM   6953  C CG1   . VAL A  1 965  ? -9.796  78.645  88.748  1.00 26.89 ? 963  VAL A CG1   1 
ATOM   6954  C CG2   . VAL A  1 965  ? -9.941  79.113  86.306  1.00 25.85 ? 963  VAL A CG2   1 
ATOM   6955  N N     . ASN A  1 966  ? -6.294  79.546  88.940  1.00 28.56 ? 964  ASN A N     1 
ATOM   6956  C CA    . ASN A  1 966  ? -5.414  79.442  90.101  1.00 30.39 ? 964  ASN A CA    1 
ATOM   6957  C C     . ASN A  1 966  ? -4.856  80.797  90.508  1.00 31.72 ? 964  ASN A C     1 
ATOM   6958  O O     . ASN A  1 966  ? -4.643  81.043  91.702  1.00 30.44 ? 964  ASN A O     1 
ATOM   6959  C CB    . ASN A  1 966  ? -4.248  78.482  89.819  1.00 28.37 ? 964  ASN A CB    1 
ATOM   6960  C CG    . ASN A  1 966  ? -4.674  77.017  89.800  1.00 26.76 ? 964  ASN A CG    1 
ATOM   6961  O OD1   . ASN A  1 966  ? -5.683  76.635  90.406  1.00 26.52 ? 964  ASN A OD1   1 
ATOM   6962  N ND2   . ASN A  1 966  ? -3.895  76.187  89.110  1.00 25.77 ? 964  ASN A ND2   1 
ATOM   6963  N N     . ALA A  1 967  ? -4.602  81.682  89.539  1.00 28.30 ? 965  ALA A N     1 
ATOM   6964  C CA    . ALA A  1 967  ? -3.904  82.932  89.828  1.00 34.88 ? 965  ALA A CA    1 
ATOM   6965  C C     . ALA A  1 967  ? -4.727  83.908  90.659  1.00 32.24 ? 965  ALA A C     1 
ATOM   6966  O O     . ALA A  1 967  ? -4.155  84.880  91.163  1.00 33.11 ? 965  ALA A O     1 
ATOM   6967  C CB    . ALA A  1 967  ? -3.461  83.615  88.533  1.00 32.22 ? 965  ALA A CB    1 
ATOM   6968  N N     . THR A  1 968  ? -6.033  83.674  90.828  1.00 33.82 ? 966  THR A N     1 
ATOM   6969  C CA    . THR A  1 968  ? -6.832  84.507  91.726  1.00 33.35 ? 966  THR A CA    1 
ATOM   6970  C C     . THR A  1 968  ? -6.356  84.432  93.168  1.00 33.81 ? 966  THR A C     1 
ATOM   6971  O O     . THR A  1 968  ? -6.667  85.333  93.956  1.00 35.61 ? 966  THR A O     1 
ATOM   6972  C CB    . THR A  1 968  ? -8.302  84.097  91.712  1.00 35.63 ? 966  THR A CB    1 
ATOM   6973  O OG1   . THR A  1 968  ? -8.441  82.840  92.393  1.00 35.97 ? 966  THR A OG1   1 
ATOM   6974  C CG2   . THR A  1 968  ? -8.844  83.990  90.280  1.00 30.31 ? 966  THR A CG2   1 
ATOM   6975  N N     . GLY A  1 969  ? -5.641  83.367  93.539  1.00 33.81 ? 967  GLY A N     1 
ATOM   6976  C CA    . GLY A  1 969  ? -5.240  83.135  94.912  1.00 31.40 ? 967  GLY A CA    1 
ATOM   6977  C C     . GLY A  1 969  ? -6.273  82.417  95.763  1.00 31.95 ? 967  GLY A C     1 
ATOM   6978  O O     . GLY A  1 969  ? -5.927  81.904  96.838  1.00 29.04 ? 967  GLY A O     1 
ATOM   6979  N N     . TYR A  1 970  ? -7.526  82.367  95.313  1.00 28.49 ? 968  TYR A N     1 
ATOM   6980  C CA    . TYR A  1 970  ? -8.583  81.614  95.966  1.00 29.41 ? 968  TYR A CA    1 
ATOM   6981  C C     . TYR A  1 970  ? -8.482  80.131  95.604  1.00 30.15 ? 968  TYR A C     1 
ATOM   6982  O O     . TYR A  1 970  ? -7.704  79.725  94.741  1.00 29.10 ? 968  TYR A O     1 
ATOM   6983  C CB    . TYR A  1 970  ? -9.950  82.161  95.559  1.00 31.73 ? 968  TYR A CB    1 
ATOM   6984  C CG    . TYR A  1 970  ? -10.268 83.535  96.114  1.00 32.77 ? 968  TYR A CG    1 
ATOM   6985  C CD1   . TYR A  1 970  ? -10.670 83.692  97.434  1.00 33.07 ? 968  TYR A CD1   1 
ATOM   6986  C CD2   . TYR A  1 970  ? -10.191 84.670  95.312  1.00 34.65 ? 968  TYR A CD2   1 
ATOM   6987  C CE1   . TYR A  1 970  ? -10.982 84.939  97.948  1.00 37.90 ? 968  TYR A CE1   1 
ATOM   6988  C CE2   . TYR A  1 970  ? -10.497 85.928  95.817  1.00 34.11 ? 968  TYR A CE2   1 
ATOM   6989  C CZ    . TYR A  1 970  ? -10.892 86.056  97.138  1.00 43.25 ? 968  TYR A CZ    1 
ATOM   6990  O OH    . TYR A  1 970  ? -11.202 87.299  97.656  1.00 45.44 ? 968  TYR A OH    1 
ATOM   6991  N N     . GLY A  1 971  ? -9.281  79.312  96.277  1.00 28.99 ? 969  GLY A N     1 
ATOM   6992  C CA    . GLY A  1 971  ? -9.241  77.890  96.008  1.00 27.50 ? 969  GLY A CA    1 
ATOM   6993  C C     . GLY A  1 971  ? -10.213 77.118  96.867  1.00 27.07 ? 969  GLY A C     1 
ATOM   6994  O O     . GLY A  1 971  ? -9.816  76.221  97.619  1.00 24.77 ? 969  GLY A O     1 
ATOM   6995  N N     . LEU A  1 972  ? -11.498 77.455  96.760  1.00 27.12 ? 970  LEU A N     1 
ATOM   6996  C CA    . LEU A  1 972  ? -12.520 76.787  97.561  1.00 21.98 ? 970  LEU A CA    1 
ATOM   6997  C C     . LEU A  1 972  ? -13.156 75.654  96.771  1.00 27.68 ? 970  LEU A C     1 
ATOM   6998  O O     . LEU A  1 972  ? -12.765 74.493  96.916  1.00 24.82 ? 970  LEU A O     1 
ATOM   6999  C CB    . LEU A  1 972  ? -13.586 77.780  98.016  1.00 24.19 ? 970  LEU A CB    1 
ATOM   7000  C CG    . LEU A  1 972  ? -14.542 77.321  99.110  1.00 26.85 ? 970  LEU A CG    1 
ATOM   7001  C CD1   . LEU A  1 972  ? -13.798 76.625  100.270 1.00 22.71 ? 970  LEU A CD1   1 
ATOM   7002  C CD2   . LEU A  1 972  ? -15.287 78.546  99.617  1.00 25.27 ? 970  LEU A CD2   1 
ATOM   7003  N N     . THR A  1 973  ? -14.139 75.978  95.932  1.00 24.11 ? 971  THR A N     1 
ATOM   7004  C CA    . THR A  1 973  ? -14.822 74.969  95.141  1.00 22.52 ? 971  THR A CA    1 
ATOM   7005  C C     . THR A  1 973  ? -14.506 75.168  93.666  1.00 22.88 ? 971  THR A C     1 
ATOM   7006  O O     . THR A  1 973  ? -14.273 76.289  93.206  1.00 22.33 ? 971  THR A O     1 
ATOM   7007  C CB    . THR A  1 973  ? -16.339 75.006  95.353  1.00 22.47 ? 971  THR A CB    1 
ATOM   7008  O OG1   . THR A  1 973  ? -16.840 76.297  94.998  1.00 23.71 ? 971  THR A OG1   1 
ATOM   7009  C CG2   . THR A  1 973  ? -16.679 74.720  96.807  1.00 23.46 ? 971  THR A CG2   1 
ATOM   7010  N N     . PHE A  1 974  ? -14.513 74.061  92.931  1.00 20.40 ? 972  PHE A N     1 
ATOM   7011  C CA    . PHE A  1 974  ? -14.200 74.069  91.515  1.00 18.11 ? 972  PHE A CA    1 
ATOM   7012  C C     . PHE A  1 974  ? -15.045 72.999  90.853  1.00 17.93 ? 972  PHE A C     1 
ATOM   7013  O O     . PHE A  1 974  ? -15.192 71.904  91.393  1.00 17.82 ? 972  PHE A O     1 
ATOM   7014  C CB    . PHE A  1 974  ? -12.713 73.798  91.249  1.00 19.53 ? 972  PHE A CB    1 
ATOM   7015  C CG    . PHE A  1 974  ? -12.398 73.647  89.785  1.00 18.27 ? 972  PHE A CG    1 
ATOM   7016  C CD1   . PHE A  1 974  ? -12.282 74.763  88.969  1.00 18.43 ? 972  PHE A CD1   1 
ATOM   7017  C CD2   . PHE A  1 974  ? -12.262 72.395  89.223  1.00 18.53 ? 972  PHE A CD2   1 
ATOM   7018  C CE1   . PHE A  1 974  ? -12.020 74.633  87.608  1.00 18.96 ? 972  PHE A CE1   1 
ATOM   7019  C CE2   . PHE A  1 974  ? -11.995 72.234  87.853  1.00 18.26 ? 972  PHE A CE2   1 
ATOM   7020  C CZ    . PHE A  1 974  ? -11.865 73.352  87.048  1.00 20.32 ? 972  PHE A CZ    1 
ATOM   7021  N N     . GLY A  1 975  ? -15.602 73.305  89.687  1.00 18.25 ? 973  GLY A N     1 
ATOM   7022  C CA    . GLY A  1 975  ? -16.397 72.344  88.950  1.00 18.86 ? 973  GLY A CA    1 
ATOM   7023  C C     . GLY A  1 975  ? -15.835 72.066  87.570  1.00 18.08 ? 973  GLY A C     1 
ATOM   7024  O O     . GLY A  1 975  ? -15.275 72.947  86.913  1.00 18.01 ? 973  GLY A O     1 
ATOM   7025  N N     . LEU A  1 976  ? -16.026 70.832  87.115  1.00 18.96 ? 974  LEU A N     1 
ATOM   7026  C CA    . LEU A  1 976  ? -15.586 70.452  85.782  1.00 17.85 ? 974  LEU A CA    1 
ATOM   7027  C C     . LEU A  1 976  ? -16.672 69.603  85.144  1.00 17.74 ? 974  LEU A C     1 
ATOM   7028  O O     . LEU A  1 976  ? -17.084 68.587  85.708  1.00 17.63 ? 974  LEU A O     1 
ATOM   7029  C CB    . LEU A  1 976  ? -14.258 69.695  85.850  1.00 17.94 ? 974  LEU A CB    1 
ATOM   7030  C CG    . LEU A  1 976  ? -13.802 69.072  84.541  1.00 19.90 ? 974  LEU A CG    1 
ATOM   7031  C CD1   . LEU A  1 976  ? -13.498 70.161  83.508  1.00 20.05 ? 974  LEU A CD1   1 
ATOM   7032  C CD2   . LEU A  1 976  ? -12.573 68.234  84.826  1.00 20.01 ? 974  LEU A CD2   1 
ATOM   7033  N N     . HIS A  1 977  ? -17.164 70.034  83.979  1.00 17.85 ? 975  HIS A N     1 
ATOM   7034  C CA    . HIS A  1 977  ? -18.103 69.231  83.207  1.00 20.20 ? 975  HIS A CA    1 
ATOM   7035  C C     . HIS A  1 977  ? -17.394 68.747  81.947  1.00 18.45 ? 975  HIS A C     1 
ATOM   7036  O O     . HIS A  1 977  ? -17.066 69.550  81.065  1.00 19.21 ? 975  HIS A O     1 
ATOM   7037  C CB    . HIS A  1 977  ? -19.370 70.013  82.849  1.00 17.69 ? 975  HIS A CB    1 
ATOM   7038  C CG    . HIS A  1 977  ? -20.466 69.909  83.870  1.00 20.53 ? 975  HIS A CG    1 
ATOM   7039  N ND1   . HIS A  1 977  ? -20.369 70.469  85.127  1.00 28.34 ? 975  HIS A ND1   1 
ATOM   7040  C CD2   . HIS A  1 977  ? -21.681 69.318  83.817  1.00 22.70 ? 975  HIS A CD2   1 
ATOM   7041  C CE1   . HIS A  1 977  ? -21.487 70.245  85.796  1.00 21.49 ? 975  HIS A CE1   1 
ATOM   7042  N NE2   . HIS A  1 977  ? -22.299 69.551  85.022  1.00 24.07 ? 975  HIS A NE2   1 
ATOM   7043  N N     . THR A  1 978  ? -17.195 67.436  81.858  1.00 17.87 ? 976  THR A N     1 
ATOM   7044  C CA    . THR A  1 978  ? -16.580 66.787  80.709  1.00 19.25 ? 976  THR A CA    1 
ATOM   7045  C C     . THR A  1 978  ? -16.880 65.304  80.817  1.00 19.88 ? 976  THR A C     1 
ATOM   7046  O O     . THR A  1 978  ? -17.065 64.781  81.913  1.00 20.05 ? 976  THR A O     1 
ATOM   7047  C CB    . THR A  1 978  ? -15.052 67.022  80.638  1.00 19.27 ? 976  THR A CB    1 
ATOM   7048  O OG1   . THR A  1 978  ? -14.499 66.333  79.506  1.00 22.34 ? 976  THR A OG1   1 
ATOM   7049  C CG2   . THR A  1 978  ? -14.347 66.491  81.875  1.00 20.04 ? 976  THR A CG2   1 
ATOM   7050  N N     . ARG A  1 979  ? -16.921 64.632  79.671  1.00 23.46 ? 977  ARG A N     1 
ATOM   7051  C CA    . ARG A  1 979  ? -16.966 63.176  79.630  1.00 24.01 ? 977  ARG A CA    1 
ATOM   7052  C C     . ARG A  1 979  ? -15.602 62.550  79.349  1.00 25.02 ? 977  ARG A C     1 
ATOM   7053  O O     . ARG A  1 979  ? -15.501 61.320  79.265  1.00 22.44 ? 977  ARG A O     1 
ATOM   7054  C CB    . ARG A  1 979  ? -17.955 62.710  78.560  1.00 26.99 ? 977  ARG A CB    1 
ATOM   7055  C CG    . ARG A  1 979  ? -19.361 63.245  78.723  1.00 27.63 ? 977  ARG A CG    1 
ATOM   7056  C CD    . ARG A  1 979  ? -20.215 62.813  77.550  1.00 38.17 ? 977  ARG A CD    1 
ATOM   7057  N NE    . ARG A  1 979  ? -21.608 63.216  77.705  1.00 47.43 ? 977  ARG A NE    1 
ATOM   7058  C CZ    . ARG A  1 979  ? -22.577 62.907  76.853  1.00 45.20 ? 977  ARG A CZ    1 
ATOM   7059  N NH1   . ARG A  1 979  ? -22.341 62.196  75.760  1.00 40.22 ? 977  ARG A NH1   1 
ATOM   7060  N NH2   . ARG A  1 979  ? -23.818 63.314  77.109  1.00 45.24 ? 977  ARG A NH2   1 
ATOM   7061  N N     . LEU A  1 980  ? -14.559 63.357  79.202  1.00 21.12 ? 978  LEU A N     1 
ATOM   7062  C CA    . LEU A  1 980  ? -13.275 62.881  78.711  1.00 19.90 ? 978  LEU A CA    1 
ATOM   7063  C C     . LEU A  1 980  ? -12.322 62.687  79.884  1.00 19.14 ? 978  LEU A C     1 
ATOM   7064  O O     . LEU A  1 980  ? -11.994 63.655  80.575  1.00 19.72 ? 978  LEU A O     1 
ATOM   7065  C CB    . LEU A  1 980  ? -12.693 63.870  77.698  1.00 20.39 ? 978  LEU A CB    1 
ATOM   7066  C CG    . LEU A  1 980  ? -13.649 64.201  76.547  1.00 22.47 ? 978  LEU A CG    1 
ATOM   7067  C CD1   . LEU A  1 980  ? -13.046 65.286  75.658  1.00 29.41 ? 978  LEU A CD1   1 
ATOM   7068  C CD2   . LEU A  1 980  ? -13.955 62.944  75.720  1.00 26.19 ? 978  LEU A CD2   1 
ATOM   7069  N N     . ASP A  1 981  ? -11.870 61.440  80.092  1.00 21.54 ? 979  ASP A N     1 
ATOM   7070  C CA    . ASP A  1 981  ? -10.954 61.153  81.202  1.00 21.67 ? 979  ASP A CA    1 
ATOM   7071  C C     . ASP A  1 981  ? -9.657  61.935  81.087  1.00 18.98 ? 979  ASP A C     1 
ATOM   7072  O O     . ASP A  1 981  ? -9.070  62.320  82.107  1.00 22.30 ? 979  ASP A O     1 
ATOM   7073  C CB    . ASP A  1 981  ? -10.628 59.662  81.278  1.00 21.46 ? 979  ASP A CB    1 
ATOM   7074  C CG    . ASP A  1 981  ? -11.773 58.839  81.786  1.00 24.98 ? 979  ASP A CG    1 
ATOM   7075  O OD1   . ASP A  1 981  ? -12.695 59.415  82.390  1.00 25.25 ? 979  ASP A OD1   1 
ATOM   7076  O OD2   . ASP A  1 981  ? -11.752 57.603  81.575  1.00 28.90 ? 979  ASP A OD2   1 
ATOM   7077  N N     . GLU A  1 982  ? -9.158  62.139  79.863  1.00 20.60 ? 980  GLU A N     1 
ATOM   7078  C CA    . GLU A  1 982  ? -7.907  62.877  79.721  1.00 21.54 ? 980  GLU A CA    1 
ATOM   7079  C C     . GLU A  1 982  ? -8.066  64.303  80.224  1.00 24.91 ? 980  GLU A C     1 
ATOM   7080  O O     . GLU A  1 982  ? -7.166  64.843  80.876  1.00 21.82 ? 980  GLU A O     1 
ATOM   7081  C CB    . GLU A  1 982  ? -7.424  62.888  78.274  1.00 24.70 ? 980  GLU A CB    1 
ATOM   7082  C CG    . GLU A  1 982  ? -6.110  63.655  78.120  1.00 27.80 ? 980  GLU A CG    1 
ATOM   7083  C CD    . GLU A  1 982  ? -5.763  64.016  76.685  1.00 32.03 ? 980  GLU A CD    1 
ATOM   7084  O OE1   . GLU A  1 982  ? -6.642  64.516  75.955  1.00 35.27 ? 980  GLU A OE1   1 
ATOM   7085  O OE2   . GLU A  1 982  ? -4.598  63.802  76.283  1.00 31.92 ? 980  GLU A OE2   1 
ATOM   7086  N N     . THR A  1 983  ? -9.215  64.923  79.937  1.00 22.36 ? 981  THR A N     1 
ATOM   7087  C CA    . THR A  1 983  ? -9.485  66.265  80.451  1.00 22.24 ? 981  THR A CA    1 
ATOM   7088  C C     . THR A  1 983  ? -9.651  66.250  81.966  1.00 24.54 ? 981  THR A C     1 
ATOM   7089  O O     . THR A  1 983  ? -9.157  67.152  82.657  1.00 22.92 ? 981  THR A O     1 
ATOM   7090  C CB    . THR A  1 983  ? -10.736 66.851  79.778  1.00 27.77 ? 981  THR A CB    1 
ATOM   7091  O OG1   . THR A  1 983  ? -10.532 66.931  78.362  1.00 26.75 ? 981  THR A OG1   1 
ATOM   7092  C CG2   . THR A  1 983  ? -11.029 68.257  80.315  1.00 23.92 ? 981  THR A CG2   1 
ATOM   7093  N N     . ILE A  1 984  ? -10.335 65.230  82.505  1.00 21.15 ? 982  ILE A N     1 
ATOM   7094  C CA    . ILE A  1 984  ? -10.482 65.138  83.958  1.00 23.05 ? 982  ILE A CA    1 
ATOM   7095  C C     . ILE A  1 984  ? -9.116  65.052  84.616  1.00 24.50 ? 982  ILE A C     1 
ATOM   7096  O O     . ILE A  1 984  ? -8.812  65.801  85.555  1.00 20.59 ? 982  ILE A O     1 
ATOM   7097  C CB    . ILE A  1 984  ? -11.363 63.939  84.359  1.00 21.22 ? 982  ILE A CB    1 
ATOM   7098  C CG1   . ILE A  1 984  ? -12.817 64.194  83.969  1.00 21.95 ? 982  ILE A CG1   1 
ATOM   7099  C CG2   . ILE A  1 984  ? -11.246 63.679  85.856  1.00 21.55 ? 982  ILE A CG2   1 
ATOM   7100  C CD1   . ILE A  1 984  ? -13.717 62.973  84.027  1.00 25.86 ? 982  ILE A CD1   1 
ATOM   7101  N N     . ALA A  1 985  ? -8.274  64.137  84.127  1.00 19.95 ? 983  ALA A N     1 
ATOM   7102  C CA    . ALA A  1 985  ? -6.964  63.929  84.744  1.00 25.60 ? 983  ALA A CA    1 
ATOM   7103  C C     . ALA A  1 985  ? -6.140  65.210  84.702  1.00 23.63 ? 983  ALA A C     1 
ATOM   7104  O O     . ALA A  1 985  ? -5.580  65.645  85.715  1.00 24.19 ? 983  ALA A O     1 
ATOM   7105  C CB    . ALA A  1 985  ? -6.235  62.780  84.039  1.00 21.08 ? 983  ALA A CB    1 
ATOM   7106  N N     . HIS A  1 986  ? -6.107  65.855  83.541  1.00 22.81 ? 984  HIS A N     1 
ATOM   7107  C CA    . HIS A  1 986  ? -5.346  67.087  83.368  1.00 24.88 ? 984  HIS A CA    1 
ATOM   7108  C C     . HIS A  1 986  ? -5.850  68.181  84.301  1.00 26.55 ? 984  HIS A C     1 
ATOM   7109  O O     . HIS A  1 986  ? -5.089  68.734  85.104  1.00 26.58 ? 984  HIS A O     1 
ATOM   7110  C CB    . HIS A  1 986  ? -5.431  67.517  81.902  1.00 25.45 ? 984  HIS A CB    1 
ATOM   7111  C CG    . HIS A  1 986  ? -4.965  68.914  81.637  1.00 25.90 ? 984  HIS A CG    1 
ATOM   7112  N ND1   . HIS A  1 986  ? -5.328  69.604  80.504  1.00 30.04 ? 984  HIS A ND1   1 
ATOM   7113  C CD2   . HIS A  1 986  ? -4.150  69.740  82.337  1.00 28.54 ? 984  HIS A CD2   1 
ATOM   7114  C CE1   . HIS A  1 986  ? -4.769  70.803  80.522  1.00 33.91 ? 984  HIS A CE1   1 
ATOM   7115  N NE2   . HIS A  1 986  ? -4.058  70.914  81.630  1.00 30.99 ? 984  HIS A NE2   1 
ATOM   7116  N N     . VAL A  1 987  ? -7.140  68.505  84.214  1.00 23.93 ? 985  VAL A N     1 
ATOM   7117  C CA    . VAL A  1 987  ? -7.663  69.651  84.956  1.00 24.97 ? 985  VAL A CA    1 
ATOM   7118  C C     . VAL A  1 987  ? -7.575  69.410  86.458  1.00 22.89 ? 985  VAL A C     1 
ATOM   7119  O O     . VAL A  1 987  ? -7.130  70.286  87.210  1.00 23.63 ? 985  VAL A O     1 
ATOM   7120  C CB    . VAL A  1 987  ? -9.097  69.977  84.512  1.00 23.41 ? 985  VAL A CB    1 
ATOM   7121  C CG1   . VAL A  1 987  ? -9.732  70.979  85.476  1.00 23.69 ? 985  VAL A CG1   1 
ATOM   7122  C CG2   . VAL A  1 987  ? -9.078  70.546  83.098  1.00 22.01 ? 985  VAL A CG2   1 
ATOM   7123  N N     . THR A  1 988  ? -7.977  68.219  86.923  1.00 22.16 ? 986  THR A N     1 
ATOM   7124  C CA    . THR A  1 988  ? -7.958  67.990  88.363  1.00 24.24 ? 986  THR A CA    1 
ATOM   7125  C C     . THR A  1 988  ? -6.538  67.898  88.902  1.00 27.26 ? 986  THR A C     1 
ATOM   7126  O O     . THR A  1 988  ? -6.324  68.143  90.097  1.00 27.31 ? 986  THR A O     1 
ATOM   7127  C CB    . THR A  1 988  ? -8.739  66.727  88.748  1.00 25.35 ? 986  THR A CB    1 
ATOM   7128  O OG1   . THR A  1 988  ? -8.139  65.590  88.136  1.00 25.20 ? 986  THR A OG1   1 
ATOM   7129  C CG2   . THR A  1 988  ? -10.195 66.823  88.300  1.00 23.62 ? 986  THR A CG2   1 
ATOM   7130  N N     . SER A  1 989  ? -5.558  67.569  88.060  1.00 22.91 ? 987  SER A N     1 
ATOM   7131  C CA    . SER A  1 989  ? -4.191  67.562  88.567  1.00 25.92 ? 987  SER A CA    1 
ATOM   7132  C C     . SER A  1 989  ? -3.591  68.963  88.621  1.00 29.64 ? 987  SER A C     1 
ATOM   7133  O O     . SER A  1 989  ? -2.651  69.186  89.392  1.00 29.89 ? 987  SER A O     1 
ATOM   7134  C CB    . SER A  1 989  ? -3.310  66.625  87.729  1.00 27.26 ? 987  SER A CB    1 
ATOM   7135  O OG    . SER A  1 989  ? -3.056  67.153  86.443  1.00 34.14 ? 987  SER A OG    1 
ATOM   7136  N N     . ARG A  1 990  ? -4.134  69.919  87.858  1.00 24.91 ? 988  ARG A N     1 
ATOM   7137  C CA    . ARG A  1 990  ? -3.574  71.266  87.790  1.00 27.40 ? 988  ARG A CA    1 
ATOM   7138  C C     . ARG A  1 990  ? -4.322  72.291  88.633  1.00 29.30 ? 988  ARG A C     1 
ATOM   7139  O O     . ARG A  1 990  ? -3.697  73.251  89.101  1.00 28.43 ? 988  ARG A O     1 
ATOM   7140  C CB    . ARG A  1 990  ? -3.543  71.747  86.339  1.00 25.59 ? 988  ARG A CB    1 
ATOM   7141  C CG    . ARG A  1 990  ? -2.709  70.867  85.445  1.00 33.68 ? 988  ARG A CG    1 
ATOM   7142  C CD    . ARG A  1 990  ? -1.241  71.172  85.627  1.00 35.67 ? 988  ARG A CD    1 
ATOM   7143  N NE    . ARG A  1 990  ? -0.750  72.032  84.559  1.00 33.92 ? 988  ARG A NE    1 
ATOM   7144  C CZ    . ARG A  1 990  ? 0.514   72.416  84.428  1.00 35.87 ? 988  ARG A CZ    1 
ATOM   7145  N NH1   . ARG A  1 990  ? 1.434   72.091  85.326  1.00 33.85 ? 988  ARG A NH1   1 
ATOM   7146  N NH2   . ARG A  1 990  ? 0.862   73.148  83.375  1.00 31.52 ? 988  ARG A NH2   1 
ATOM   7147  N N     . ILE A  1 991  ? -5.636  72.113  88.842  1.00 23.01 ? 989  ILE A N     1 
ATOM   7148  C CA    . ILE A  1 991  ? -6.424  73.049  89.635  1.00 23.68 ? 989  ILE A CA    1 
ATOM   7149  C C     . ILE A  1 991  ? -6.006  72.975  91.101  1.00 26.08 ? 989  ILE A C     1 
ATOM   7150  O O     . ILE A  1 991  ? -5.731  71.893  91.639  1.00 27.07 ? 989  ILE A O     1 
ATOM   7151  C CB    . ILE A  1 991  ? -7.929  72.759  89.463  1.00 26.22 ? 989  ILE A CB    1 
ATOM   7152  C CG1   . ILE A  1 991  ? -8.768  73.941  89.952  1.00 24.70 ? 989  ILE A CG1   1 
ATOM   7153  C CG2   . ILE A  1 991  ? -8.337  71.458  90.187  1.00 25.69 ? 989  ILE A CG2   1 
ATOM   7154  C CD1   . ILE A  1 991  ? -8.659  75.177  89.055  1.00 24.31 ? 989  ILE A CD1   1 
ATOM   7155  N N     . LYS A  1 992  ? -5.926  74.133  91.755  1.00 21.27 ? 990  LYS A N     1 
ATOM   7156  C CA    . LYS A  1 992  ? -5.600  74.206  93.181  1.00 26.11 ? 990  LYS A CA    1 
ATOM   7157  C C     . LYS A  1 992  ? -6.841  74.643  93.964  1.00 28.66 ? 990  LYS A C     1 
ATOM   7158  O O     . LYS A  1 992  ? -7.040  75.829  94.246  1.00 35.25 ? 990  LYS A O     1 
ATOM   7159  C CB    . LYS A  1 992  ? -4.412  75.158  93.403  1.00 27.99 ? 990  LYS A CB    1 
ATOM   7160  N N     . ALA A  1 993  ? -7.679  73.667  94.328  1.00 23.78 ? 991  ALA A N     1 
ATOM   7161  C CA    . ALA A  1 993  ? -8.930  73.935  95.038  1.00 20.44 ? 991  ALA A CA    1 
ATOM   7162  C C     . ALA A  1 993  ? -9.225  72.808  96.022  1.00 22.00 ? 991  ALA A C     1 
ATOM   7163  O O     . ALA A  1 993  ? -8.888  71.643  95.777  1.00 21.58 ? 991  ALA A O     1 
ATOM   7164  C CB    . ALA A  1 993  ? -10.093 74.106  94.063  1.00 25.11 ? 991  ALA A CB    1 
ATOM   7165  N N     . GLY A  1 994  ? -9.874  73.166  97.140  1.00 21.04 ? 992  GLY A N     1 
ATOM   7166  C CA    . GLY A  1 994  ? -10.136 72.196  98.194  1.00 24.18 ? 992  GLY A CA    1 
ATOM   7167  C C     . GLY A  1 994  ? -11.311 71.267  97.948  1.00 21.60 ? 992  GLY A C     1 
ATOM   7168  O O     . GLY A  1 994  ? -11.336 70.160  98.499  1.00 18.29 ? 992  GLY A O     1 
ATOM   7169  N N     . ASN A  1 995  ? -12.288 71.687  97.141  1.00 18.22 ? 993  ASN A N     1 
ATOM   7170  C CA    . ASN A  1 995  ? -13.491 70.896  96.877  1.00 21.35 ? 993  ASN A CA    1 
ATOM   7171  C C     . ASN A  1 995  ? -13.712 70.866  95.371  1.00 19.21 ? 993  ASN A C     1 
ATOM   7172  O O     . ASN A  1 995  ? -14.003 71.902  94.770  1.00 21.51 ? 993  ASN A O     1 
ATOM   7173  C CB    . ASN A  1 995  ? -14.714 71.468  97.604  1.00 18.71 ? 993  ASN A CB    1 
ATOM   7174  C CG    . ASN A  1 995  ? -14.748 71.084  99.074  1.00 22.46 ? 993  ASN A CG    1 
ATOM   7175  O OD1   . ASN A  1 995  ? -14.105 71.713  99.902  1.00 20.14 ? 993  ASN A OD1   1 
ATOM   7176  N ND2   . ASN A  1 995  ? -15.490 70.036  99.396  1.00 22.50 ? 993  ASN A ND2   1 
ATOM   7177  N N     . LEU A  1 996  ? -13.499 69.704  94.758  1.00 19.27 ? 994  LEU A N     1 
ATOM   7178  C CA    . LEU A  1 996  ? -13.694 69.531  93.328  1.00 20.16 ? 994  LEU A CA    1 
ATOM   7179  C C     . LEU A  1 996  ? -14.987 68.773  93.087  1.00 17.68 ? 994  LEU A C     1 
ATOM   7180  O O     . LEU A  1 996  ? -15.364 67.890  93.858  1.00 17.64 ? 994  LEU A O     1 
ATOM   7181  C CB    . LEU A  1 996  ? -12.537 68.772  92.680  1.00 18.18 ? 994  LEU A CB    1 
ATOM   7182  C CG    . LEU A  1 996  ? -11.132 69.245  93.064  1.00 29.50 ? 994  LEU A CG    1 
ATOM   7183  C CD1   . LEU A  1 996  ? -10.097 68.368  92.380  1.00 25.98 ? 994  LEU A CD1   1 
ATOM   7184  C CD2   . LEU A  1 996  ? -10.940 70.714  92.700  1.00 24.93 ? 994  LEU A CD2   1 
ATOM   7185  N N     . TYR A  1 997  ? -15.667 69.123  91.999  1.00 18.05 ? 995  TYR A N     1 
ATOM   7186  C CA    . TYR A  1 997  ? -16.931 68.500  91.643  1.00 20.15 ? 995  TYR A CA    1 
ATOM   7187  C C     . TYR A  1 997  ? -16.890 68.194  90.157  1.00 17.49 ? 995  TYR A C     1 
ATOM   7188  O O     . TYR A  1 997  ? -16.560 69.076  89.360  1.00 18.67 ? 995  TYR A O     1 
ATOM   7189  C CB    . TYR A  1 997  ? -18.110 69.417  91.957  1.00 18.20 ? 995  TYR A CB    1 
ATOM   7190  C CG    . TYR A  1 997  ? -18.228 69.731  93.422  1.00 18.54 ? 995  TYR A CG    1 
ATOM   7191  C CD1   . TYR A  1 997  ? -18.921 68.874  94.278  1.00 19.27 ? 995  TYR A CD1   1 
ATOM   7192  C CD2   . TYR A  1 997  ? -17.646 70.869  93.956  1.00 18.83 ? 995  TYR A CD2   1 
ATOM   7193  C CE1   . TYR A  1 997  ? -19.032 69.150  95.622  1.00 21.22 ? 995  TYR A CE1   1 
ATOM   7194  C CE2   . TYR A  1 997  ? -17.757 71.152  95.301  1.00 22.13 ? 995  TYR A CE2   1 
ATOM   7195  C CZ    . TYR A  1 997  ? -18.458 70.292  96.124  1.00 21.70 ? 995  TYR A CZ    1 
ATOM   7196  O OH    . TYR A  1 997  ? -18.584 70.562  97.467  1.00 24.59 ? 995  TYR A OH    1 
ATOM   7197  N N     . ILE A  1 998  ? -17.149 66.945  89.785  1.00 17.45 ? 996  ILE A N     1 
ATOM   7198  C CA    A ILE A  1 998  ? -17.099 66.524  88.388  0.51 18.01 ? 996  ILE A CA    1 
ATOM   7199  C CA    B ILE A  1 998  ? -17.103 66.543  88.386  0.49 17.85 ? 996  ILE A CA    1 
ATOM   7200  C C     . ILE A  1 998  ? -18.508 66.160  87.942  1.00 17.37 ? 996  ILE A C     1 
ATOM   7201  O O     . ILE A  1 998  ? -19.141 65.275  88.525  1.00 17.32 ? 996  ILE A O     1 
ATOM   7202  C CB    A ILE A  1 998  ? -16.140 65.344  88.178  0.51 17.76 ? 996  ILE A CB    1 
ATOM   7203  C CB    B ILE A  1 998  ? -16.102 65.405  88.155  0.49 18.04 ? 996  ILE A CB    1 
ATOM   7204  C CG1   A ILE A  1 998  ? -14.771 65.633  88.804  0.51 18.39 ? 996  ILE A CG1   1 
ATOM   7205  C CG1   B ILE A  1 998  ? -14.691 65.888  88.510  0.49 18.63 ? 996  ILE A CG1   1 
ATOM   7206  C CG2   A ILE A  1 998  ? -16.017 65.034  86.702  0.51 18.26 ? 996  ILE A CG2   1 
ATOM   7207  C CG2   B ILE A  1 998  ? -16.183 64.914  86.725  0.49 18.20 ? 996  ILE A CG2   1 
ATOM   7208  C CD1   A ILE A  1 998  ? -14.046 66.798  88.178  0.51 18.53 ? 996  ILE A CD1   1 
ATOM   7209  C CD1   B ILE A  1 998  ? -13.618 64.863  88.316  0.49 21.08 ? 996  ILE A CD1   1 
ATOM   7210  N N     . ASN A  1 999  ? -18.992 66.849  86.912  1.00 18.32 ? 997  ASN A N     1 
ATOM   7211  C CA    . ASN A  1 999  ? -20.269 66.554  86.277  1.00 19.18 ? 997  ASN A CA    1 
ATOM   7212  C C     . ASN A  1 999  ? -21.453 66.694  87.234  1.00 19.01 ? 997  ASN A C     1 
ATOM   7213  O O     . ASN A  1 999  ? -22.422 65.945  87.148  1.00 17.46 ? 997  ASN A O     1 
ATOM   7214  C CB    . ASN A  1 999  ? -20.218 65.172  85.634  1.00 17.56 ? 997  ASN A CB    1 
ATOM   7215  C CG    . ASN A  1 999  ? -19.277 65.139  84.449  1.00 19.86 ? 997  ASN A CG    1 
ATOM   7216  O OD1   . ASN A  1 999  ? -19.095 66.159  83.762  1.00 19.62 ? 997  ASN A OD1   1 
ATOM   7217  N ND2   . ASN A  1 999  ? -18.693 63.979  84.185  1.00 20.40 ? 997  ASN A ND2   1 
ATOM   7218  N N     . ARG A  1 1000 ? -21.394 67.693  88.123  1.00 17.63 ? 998  ARG A N     1 
ATOM   7219  C CA    . ARG A  1 1000 ? -22.481 67.995  89.050  1.00 17.15 ? 998  ARG A CA    1 
ATOM   7220  C C     . ARG A  1 1000 ? -22.361 69.460  89.473  1.00 17.20 ? 998  ARG A C     1 
ATOM   7221  O O     . ARG A  1 1000 ? -21.452 70.174  89.045  1.00 19.57 ? 998  ARG A O     1 
ATOM   7222  C CB    . ARG A  1 1000 ? -22.447 67.042  90.252  1.00 17.13 ? 998  ARG A CB    1 
ATOM   7223  C CG    . ARG A  1 1000 ? -21.058 66.953  90.924  1.00 18.58 ? 998  ARG A CG    1 
ATOM   7224  C CD    . ARG A  1 1000 ? -21.215 66.611  92.397  1.00 19.26 ? 998  ARG A CD    1 
ATOM   7225  N NE    . ARG A  1 1000 ? -21.808 67.712  93.155  1.00 19.32 ? 998  ARG A NE    1 
ATOM   7226  C CZ    . ARG A  1 1000 ? -22.066 67.661  94.456  1.00 22.29 ? 998  ARG A CZ    1 
ATOM   7227  N NH1   . ARG A  1 1000 ? -21.815 66.574  95.161  1.00 18.73 ? 998  ARG A NH1   1 
ATOM   7228  N NH2   . ARG A  1 1000 ? -22.577 68.733  95.065  1.00 21.84 ? 998  ARG A NH2   1 
ATOM   7229  N N     . ASN A  1 1001 ? -23.295 69.922  90.299  1.00 17.18 ? 999  ASN A N     1 
ATOM   7230  C CA    . ASN A  1 1001 ? -23.144 71.279  90.824  1.00 17.27 ? 999  ASN A CA    1 
ATOM   7231  C C     . ASN A  1 1001 ? -21.979 71.319  91.826  1.00 17.75 ? 999  ASN A C     1 
ATOM   7232  O O     . ASN A  1 1001 ? -21.427 70.286  92.211  1.00 17.31 ? 999  ASN A O     1 
ATOM   7233  C CB    . ASN A  1 1001 ? -24.448 71.788  91.462  1.00 17.40 ? 999  ASN A CB    1 
ATOM   7234  C CG    . ASN A  1 1001 ? -24.848 71.049  92.741  1.00 24.32 ? 999  ASN A CG    1 
ATOM   7235  O OD1   . ASN A  1 1001 ? -24.039 70.827  93.641  1.00 23.11 ? 999  ASN A OD1   1 
ATOM   7236  N ND2   . ASN A  1 1001 ? -26.138 70.699  92.835  1.00 24.95 ? 999  ASN A ND2   1 
ATOM   7237  N N     . ILE A  1 1002 ? -21.626 72.526  92.262  1.00 17.45 ? 1000 ILE A N     1 
ATOM   7238  C CA    . ILE A  1 1002 ? -20.483 72.705  93.158  1.00 17.56 ? 1000 ILE A CA    1 
ATOM   7239  C C     . ILE A  1 1002 ? -20.904 73.182  94.549  1.00 19.78 ? 1000 ILE A C     1 
ATOM   7240  O O     . ILE A  1 1002 ? -20.055 73.666  95.323  1.00 17.73 ? 1000 ILE A O     1 
ATOM   7241  C CB    . ILE A  1 1002 ? -19.432 73.649  92.547  1.00 20.01 ? 1000 ILE A CB    1 
ATOM   7242  C CG1   . ILE A  1 1002 ? -19.974 75.074  92.391  1.00 17.77 ? 1000 ILE A CG1   1 
ATOM   7243  C CG2   . ILE A  1 1002 ? -18.980 73.119  91.213  1.00 17.63 ? 1000 ILE A CG2   1 
ATOM   7244  C CD1   . ILE A  1 1002 ? -18.911 76.085  92.022  1.00 17.95 ? 1000 ILE A CD1   1 
ATOM   7245  N N     . ILE A  1 1003 ? -22.168 73.010  94.922  1.00 17.77 ? 1001 ILE A N     1 
ATOM   7246  C CA    . ILE A  1 1003 ? -22.659 73.502  96.206  1.00 19.00 ? 1001 ILE A CA    1 
ATOM   7247  C C     . ILE A  1 1003 ? -23.181 72.347  97.063  1.00 23.18 ? 1001 ILE A C     1 
ATOM   7248  O O     . ILE A  1 1003 ? -23.326 71.210  96.610  1.00 26.42 ? 1001 ILE A O     1 
ATOM   7249  C CB    . ILE A  1 1003 ? -23.746 74.573  96.037  1.00 20.24 ? 1001 ILE A CB    1 
ATOM   7250  C CG1   . ILE A  1 1003 ? -24.996 73.989  95.354  1.00 22.27 ? 1001 ILE A CG1   1 
ATOM   7251  C CG2   . ILE A  1 1003 ? -23.191 75.784  95.277  1.00 17.81 ? 1001 ILE A CG2   1 
ATOM   7252  C CD1   . ILE A  1 1003 ? -26.228 74.926  95.463  1.00 24.99 ? 1001 ILE A CD1   1 
ATOM   7253  N N     . GLY A  1 1004 ? -23.473 72.665  98.320  1.00 22.26 ? 1002 GLY A N     1 
ATOM   7254  C CA    . GLY A  1 1004 ? -24.107 71.702  99.204  1.00 28.03 ? 1002 GLY A CA    1 
ATOM   7255  C C     . GLY A  1 1004 ? -23.199 70.577  99.656  1.00 28.07 ? 1002 GLY A C     1 
ATOM   7256  O O     . GLY A  1 1004 ? -23.647 69.427  99.749  1.00 26.18 ? 1002 GLY A O     1 
ATOM   7257  N N     . ALA A  1 1005 ? -21.926 70.877  99.925  1.00 26.97 ? 1003 ALA A N     1 
ATOM   7258  C CA    . ALA A  1 1005 ? -21.004 69.861  100.408 1.00 23.54 ? 1003 ALA A CA    1 
ATOM   7259  C C     . ALA A  1 1005 ? -21.570 69.212  101.664 1.00 25.91 ? 1003 ALA A C     1 
ATOM   7260  O O     . ALA A  1 1005 ? -22.125 69.895  102.531 1.00 26.94 ? 1003 ALA A O     1 
ATOM   7261  C CB    . ALA A  1 1005 ? -19.639 70.491  100.689 1.00 24.93 ? 1003 ALA A CB    1 
ATOM   7262  N N     . VAL A  1 1006 ? -21.465 67.876  101.738 1.00 21.00 ? 1004 VAL A N     1 
ATOM   7263  C CA    . VAL A  1 1006 ? -22.107 67.078  102.778 1.00 18.04 ? 1004 VAL A CA    1 
ATOM   7264  C C     . VAL A  1 1006 ? -21.069 66.691  103.823 1.00 19.09 ? 1004 VAL A C     1 
ATOM   7265  O O     . VAL A  1 1006 ? -19.971 66.232  103.489 1.00 21.71 ? 1004 VAL A O     1 
ATOM   7266  C CB    . VAL A  1 1006 ? -22.776 65.818  102.199 1.00 18.50 ? 1004 VAL A CB    1 
ATOM   7267  C CG1   . VAL A  1 1006 ? -23.380 64.966  103.298 1.00 20.41 ? 1004 VAL A CG1   1 
ATOM   7268  C CG2   . VAL A  1 1006 ? -23.898 66.212  101.211 1.00 22.61 ? 1004 VAL A CG2   1 
ATOM   7269  N N     . VAL A  1 1007 ? -21.444 66.842  105.091 1.00 19.99 ? 1005 VAL A N     1 
ATOM   7270  C CA    . VAL A  1 1007 ? -20.544 66.518  106.196 1.00 18.59 ? 1005 VAL A CA    1 
ATOM   7271  C C     . VAL A  1 1007 ? -20.097 65.061  106.109 1.00 19.12 ? 1005 VAL A C     1 
ATOM   7272  O O     . VAL A  1 1007 ? -20.906 64.156  105.873 1.00 20.29 ? 1005 VAL A O     1 
ATOM   7273  C CB    . VAL A  1 1007 ? -21.251 66.816  107.525 1.00 19.52 ? 1005 VAL A CB    1 
ATOM   7274  C CG1   . VAL A  1 1007 ? -20.408 66.342  108.680 1.00 19.04 ? 1005 VAL A CG1   1 
ATOM   7275  C CG2   . VAL A  1 1007 ? -21.522 68.308  107.663 1.00 18.85 ? 1005 VAL A CG2   1 
ATOM   7276  N N     . GLY A  1 1008 ? -18.788 64.824  106.310 1.00 19.09 ? 1006 GLY A N     1 
ATOM   7277  C CA    . GLY A  1 1008 ? -18.235 63.484  106.232 1.00 18.71 ? 1006 GLY A CA    1 
ATOM   7278  C C     . GLY A  1 1008 ? -18.239 62.849  104.858 1.00 21.31 ? 1006 GLY A C     1 
ATOM   7279  O O     . GLY A  1 1008 ? -17.835 61.687  104.728 1.00 21.33 ? 1006 GLY A O     1 
ATOM   7280  N N     . VAL A  1 1009 ? -18.706 63.564  103.834 1.00 20.61 ? 1007 VAL A N     1 
ATOM   7281  C CA    . VAL A  1 1009 ? -18.801 63.048  102.474 1.00 19.86 ? 1007 VAL A CA    1 
ATOM   7282  C C     . VAL A  1 1009 ? -18.000 63.910  101.512 1.00 18.04 ? 1007 VAL A C     1 
ATOM   7283  O O     . VAL A  1 1009 ? -17.154 63.407  100.763 1.00 18.50 ? 1007 VAL A O     1 
ATOM   7284  C CB    . VAL A  1 1009 ? -20.275 62.933  102.016 1.00 21.00 ? 1007 VAL A CB    1 
ATOM   7285  C CG1   . VAL A  1 1009 ? -20.352 62.282  100.618 1.00 20.59 ? 1007 VAL A CG1   1 
ATOM   7286  C CG2   . VAL A  1 1009 ? -21.097 62.111  103.037 1.00 19.56 ? 1007 VAL A CG2   1 
ATOM   7287  N N     . GLN A  1 1010 ? -18.243 65.222  101.529 1.00 20.02 ? 1008 GLN A N     1 
ATOM   7288  C CA    . GLN A  1 1010 ? -17.368 66.217  100.916 1.00 19.32 ? 1008 GLN A CA    1 
ATOM   7289  C C     . GLN A  1 1010 ? -16.933 67.145  102.041 1.00 18.20 ? 1008 GLN A C     1 
ATOM   7290  O O     . GLN A  1 1010 ? -17.458 68.257  102.176 1.00 21.64 ? 1008 GLN A O     1 
ATOM   7291  C CB    . GLN A  1 1010 ? -18.050 67.014  99.805  1.00 20.47 ? 1008 GLN A CB    1 
ATOM   7292  C CG    . GLN A  1 1010 ? -18.588 66.183  98.630  1.00 19.97 ? 1008 GLN A CG    1 
ATOM   7293  C CD    . GLN A  1 1010 ? -20.080 65.891  98.765  1.00 23.27 ? 1008 GLN A CD    1 
ATOM   7294  O OE1   . GLN A  1 1010 ? -20.836 66.688  99.342  1.00 20.64 ? 1008 GLN A OE1   1 
ATOM   7295  N NE2   . GLN A  1 1010 ? -20.513 64.737  98.232  1.00 19.96 ? 1008 GLN A NE2   1 
ATOM   7296  N N     . PRO A  1 1011 ? -15.993 66.716  102.880 1.00 19.44 ? 1009 PRO A N     1 
ATOM   7297  C CA    . PRO A  1 1011 ? -15.441 67.628  103.889 1.00 19.70 ? 1009 PRO A CA    1 
ATOM   7298  C C     . PRO A  1 1011 ? -15.078 68.950  103.231 1.00 19.90 ? 1009 PRO A C     1 
ATOM   7299  O O     . PRO A  1 1011 ? -14.506 68.974  102.149 1.00 20.05 ? 1009 PRO A O     1 
ATOM   7300  C CB    . PRO A  1 1011 ? -14.201 66.887  104.391 1.00 18.57 ? 1009 PRO A CB    1 
ATOM   7301  C CG    . PRO A  1 1011 ? -14.507 65.436  104.148 1.00 20.16 ? 1009 PRO A CG    1 
ATOM   7302  C CD    . PRO A  1 1011 ? -15.316 65.410  102.859 1.00 20.24 ? 1009 PRO A CD    1 
ATOM   7303  N N     . PHE A  1 1012 ? -15.421 70.057  103.880 1.00 21.56 ? 1010 PHE A N     1 
ATOM   7304  C CA    . PHE A  1 1012 ? -15.482 71.336  103.191 1.00 22.28 ? 1010 PHE A CA    1 
ATOM   7305  C C     . PHE A  1 1012 ? -14.452 72.324  103.727 1.00 23.49 ? 1010 PHE A C     1 
ATOM   7306  O O     . PHE A  1 1012 ? -14.302 72.497  104.942 1.00 22.47 ? 1010 PHE A O     1 
ATOM   7307  C CB    . PHE A  1 1012 ? -16.885 71.947  103.298 1.00 22.31 ? 1010 PHE A CB    1 
ATOM   7308  C CG    . PHE A  1 1012 ? -17.050 73.199  102.479 1.00 26.02 ? 1010 PHE A CG    1 
ATOM   7309  C CD1   . PHE A  1 1012 ? -17.368 73.119  101.139 1.00 24.38 ? 1010 PHE A CD1   1 
ATOM   7310  C CD2   . PHE A  1 1012 ? -16.871 74.456  103.049 1.00 26.89 ? 1010 PHE A CD2   1 
ATOM   7311  C CE1   . PHE A  1 1012 ? -17.507 74.272  100.370 1.00 28.16 ? 1010 PHE A CE1   1 
ATOM   7312  C CE2   . PHE A  1 1012 ? -17.001 75.611  102.289 1.00 27.60 ? 1010 PHE A CE2   1 
ATOM   7313  C CZ    . PHE A  1 1012 ? -17.336 75.515  100.946 1.00 24.35 ? 1010 PHE A CZ    1 
ATOM   7314  N N     . GLY A  1 1013 ? -13.781 73.002  102.806 1.00 25.14 ? 1011 GLY A N     1 
ATOM   7315  C CA    . GLY A  1 1013 ? -12.727 73.931  103.161 1.00 26.97 ? 1011 GLY A CA    1 
ATOM   7316  C C     . GLY A  1 1013 ? -11.679 74.027  102.074 1.00 24.52 ? 1011 GLY A C     1 
ATOM   7317  O O     . GLY A  1 1013 ? -11.318 73.023  101.448 1.00 27.92 ? 1011 GLY A O     1 
ATOM   7318  N N     . GLY A  1 1014 ? -11.186 75.237  101.832 1.00 25.40 ? 1012 GLY A N     1 
ATOM   7319  C CA    . GLY A  1 1014 ? -10.273 75.501  100.748 1.00 28.89 ? 1012 GLY A CA    1 
ATOM   7320  C C     . GLY A  1 1014 ? -8.885  75.888  101.226 1.00 31.54 ? 1012 GLY A C     1 
ATOM   7321  O O     . GLY A  1 1014 ? -8.541  75.782  102.407 1.00 32.31 ? 1012 GLY A O     1 
ATOM   7322  N N     . ARG A  1 1015 ? -8.085  76.355  100.273 1.00 30.35 ? 1013 ARG A N     1 
ATOM   7323  C CA    . ARG A  1 1015 ? -6.703  76.759  100.509 1.00 29.04 ? 1013 ARG A CA    1 
ATOM   7324  C C     . ARG A  1 1015 ? -6.513  78.193  100.031 1.00 30.21 ? 1013 ARG A C     1 
ATOM   7325  O O     . ARG A  1 1015 ? -7.428  78.813  99.482  1.00 25.38 ? 1013 ARG A O     1 
ATOM   7326  C CB    . ARG A  1 1015 ? -5.724  75.816  99.798  1.00 32.15 ? 1013 ARG A CB    1 
ATOM   7327  C CG    . ARG A  1 1015 ? -6.038  75.621  98.309  1.00 34.69 ? 1013 ARG A CG    1 
ATOM   7328  C CD    . ARG A  1 1015 ? -4.751  75.510  97.467  1.00 35.41 ? 1013 ARG A CD    1 
ATOM   7329  N NE    . ARG A  1 1015 ? -3.991  76.758  97.434  1.00 36.96 ? 1013 ARG A NE    1 
ATOM   7330  C CZ    . ARG A  1 1015 ? -4.266  77.783  96.634  1.00 38.42 ? 1013 ARG A CZ    1 
ATOM   7331  N NH1   . ARG A  1 1015 ? -5.292  77.754  95.793  1.00 38.32 ? 1013 ARG A NH1   1 
ATOM   7332  N NH2   . ARG A  1 1015 ? -3.487  78.863  96.668  1.00 40.99 ? 1013 ARG A NH2   1 
ATOM   7333  N N     . GLY A  1 1016 ? -5.304  78.711  100.227 1.00 27.35 ? 1014 GLY A N     1 
ATOM   7334  C CA    . GLY A  1 1016 ? -5.004  80.048  99.738  1.00 29.91 ? 1014 GLY A CA    1 
ATOM   7335  C C     . GLY A  1 1016 ? -5.857  81.079  100.454 1.00 30.57 ? 1014 GLY A C     1 
ATOM   7336  O O     . GLY A  1 1016 ? -5.991  81.055  101.681 1.00 30.94 ? 1014 GLY A O     1 
ATOM   7337  N N     . LEU A  1 1017 ? -6.461  81.992  99.682  1.00 28.26 ? 1015 LEU A N     1 
ATOM   7338  C CA    . LEU A  1 1017 ? -7.338  83.018  100.248 1.00 29.20 ? 1015 LEU A CA    1 
ATOM   7339  C C     . LEU A  1 1017 ? -8.665  82.459  100.756 1.00 29.18 ? 1015 LEU A C     1 
ATOM   7340  O O     . LEU A  1 1017 ? -9.467  83.224  101.302 1.00 31.66 ? 1015 LEU A O     1 
ATOM   7341  C CB    . LEU A  1 1017 ? -7.625  84.113  99.209  1.00 30.85 ? 1015 LEU A CB    1 
ATOM   7342  C CG    . LEU A  1 1017 ? -6.465  84.929  98.636  1.00 33.30 ? 1015 LEU A CG    1 
ATOM   7343  C CD1   . LEU A  1 1017 ? -6.951  85.829  97.494  1.00 31.76 ? 1015 LEU A CD1   1 
ATOM   7344  C CD2   . LEU A  1 1017 ? -5.787  85.762  99.727  1.00 30.12 ? 1015 LEU A CD2   1 
ATOM   7345  N N     . SER A  1 1018 ? -8.933  81.168  100.577 1.00 25.98 ? 1016 SER A N     1 
ATOM   7346  C CA    . SER A  1 1018 ? -10.235 80.620  100.937 1.00 28.33 ? 1016 SER A CA    1 
ATOM   7347  C C     . SER A  1 1018 ? -10.280 80.034  102.336 1.00 28.14 ? 1016 SER A C     1 
ATOM   7348  O O     . SER A  1 1018 ? -11.376 79.782  102.850 1.00 27.49 ? 1016 SER A O     1 
ATOM   7349  C CB    . SER A  1 1018 ? -10.656 79.545  99.936  1.00 28.30 ? 1016 SER A CB    1 
ATOM   7350  O OG    . SER A  1 1018 ? -10.837 80.122  98.651  1.00 28.59 ? 1016 SER A OG    1 
ATOM   7351  N N     . GLY A  1 1019 ? -9.138  79.812  102.968 1.00 27.12 ? 1017 GLY A N     1 
ATOM   7352  C CA    . GLY A  1 1019 ? -9.177  79.339  104.332 1.00 27.64 ? 1017 GLY A CA    1 
ATOM   7353  C C     . GLY A  1 1019 ? -7.817  78.889  104.800 1.00 27.02 ? 1017 GLY A C     1 
ATOM   7354  O O     . GLY A  1 1019 ? -6.861  78.787  104.031 1.00 26.75 ? 1017 GLY A O     1 
ATOM   7355  N N     . THR A  1 1020 ? -7.762  78.618  106.102 1.00 23.93 ? 1018 THR A N     1 
ATOM   7356  C CA    . THR A  1 1020 ? -6.626  77.988  106.742 1.00 26.65 ? 1018 THR A CA    1 
ATOM   7357  C C     . THR A  1 1020 ? -6.727  76.476  106.775 1.00 28.55 ? 1018 THR A C     1 
ATOM   7358  O O     . THR A  1 1020 ? -5.700  75.801  106.910 1.00 28.46 ? 1018 THR A O     1 
ATOM   7359  C CB    . THR A  1 1020 ? -6.526  78.469  108.187 1.00 25.32 ? 1018 THR A CB    1 
ATOM   7360  O OG1   . THR A  1 1020 ? -7.720  78.068  108.884 1.00 22.93 ? 1018 THR A OG1   1 
ATOM   7361  C CG2   . THR A  1 1020 ? -6.401  79.987  108.241 1.00 27.37 ? 1018 THR A CG2   1 
ATOM   7362  N N     . GLY A  1 1021 ? -7.940  75.932  106.720 1.00 23.82 ? 1019 GLY A N     1 
ATOM   7363  C CA    . GLY A  1 1021 ? -8.152  74.565  107.113 1.00 23.85 ? 1019 GLY A CA    1 
ATOM   7364  C C     . GLY A  1 1021 ? -7.989  74.444  108.619 1.00 23.97 ? 1019 GLY A C     1 
ATOM   7365  O O     . GLY A  1 1021 ? -7.691  75.427  109.315 1.00 24.14 ? 1019 GLY A O     1 
ATOM   7366  N N     . PRO A  1 1022 ? -8.211  73.233  109.157 1.00 22.19 ? 1020 PRO A N     1 
ATOM   7367  C CA    . PRO A  1 1022 ? -8.614  72.009  108.439 1.00 23.52 ? 1020 PRO A CA    1 
ATOM   7368  C C     . PRO A  1 1022 ? -10.077 72.058  107.970 1.00 24.41 ? 1020 PRO A C     1 
ATOM   7369  O O     . PRO A  1 1022 ? -10.835 72.957  108.338 1.00 25.27 ? 1020 PRO A O     1 
ATOM   7370  C CB    . PRO A  1 1022 ? -8.384  70.904  109.475 1.00 22.37 ? 1020 PRO A CB    1 
ATOM   7371  C CG    . PRO A  1 1022 ? -8.520  71.590  110.813 1.00 25.24 ? 1020 PRO A CG    1 
ATOM   7372  C CD    . PRO A  1 1022 ? -8.021  72.999  110.602 1.00 20.29 ? 1020 PRO A CD    1 
ATOM   7373  N N     . LYS A  1 1023 ? -10.488 71.089  107.161 1.00 20.85 ? 1021 LYS A N     1 
ATOM   7374  C CA    . LYS A  1 1023 ? -11.834 71.077  106.600 1.00 22.53 ? 1021 LYS A CA    1 
ATOM   7375  C C     . LYS A  1 1023 ? -12.897 70.840  107.668 1.00 21.75 ? 1021 LYS A C     1 
ATOM   7376  O O     . LYS A  1 1023 ? -12.767 69.924  108.483 1.00 20.17 ? 1021 LYS A O     1 
ATOM   7377  C CB    . LYS A  1 1023 ? -11.944 69.982  105.537 1.00 20.21 ? 1021 LYS A CB    1 
ATOM   7378  C CG    . LYS A  1 1023 ? -11.218 70.266  104.219 1.00 20.20 ? 1021 LYS A CG    1 
ATOM   7379  C CD    . LYS A  1 1023 ? -11.401 69.081  103.287 1.00 20.07 ? 1021 LYS A CD    1 
ATOM   7380  C CE    . LYS A  1 1023 ? -10.885 69.389  101.885 1.00 21.39 ? 1021 LYS A CE    1 
ATOM   7381  N NZ    . LYS A  1 1023 ? -11.899 70.199  101.133 1.00 21.81 ? 1021 LYS A NZ    1 
ATOM   7382  N N     . ALA A  1 1024 ? -13.968 71.640  107.632 1.00 21.40 ? 1022 ALA A N     1 
ATOM   7383  C CA    . ALA A  1 1024 ? -15.152 71.351  108.431 1.00 21.67 ? 1022 ALA A CA    1 
ATOM   7384  C C     . ALA A  1 1024 ? -15.798 70.075  107.927 1.00 21.81 ? 1022 ALA A C     1 
ATOM   7385  O O     . ALA A  1 1024 ? -15.786 69.793  106.727 1.00 21.86 ? 1022 ALA A O     1 
ATOM   7386  C CB    . ALA A  1 1024 ? -16.152 72.510  108.371 1.00 22.81 ? 1022 ALA A CB    1 
ATOM   7387  N N     . GLY A  1 1025 ? -16.345 69.290  108.850 1.00 21.67 ? 1023 GLY A N     1 
ATOM   7388  C CA    . GLY A  1 1025 ? -16.922 68.020  108.461 1.00 19.10 ? 1023 GLY A CA    1 
ATOM   7389  C C     . GLY A  1 1025 ? -15.904 67.032  107.953 1.00 19.03 ? 1023 GLY A C     1 
ATOM   7390  O O     . GLY A  1 1025 ? -16.242 66.162  107.154 1.00 18.88 ? 1023 GLY A O     1 
ATOM   7391  N N     . GLY A  1 1026 ? -14.661 67.138  108.413 1.00 19.17 ? 1024 GLY A N     1 
ATOM   7392  C CA    . GLY A  1 1026 ? -13.612 66.221  108.054 1.00 19.16 ? 1024 GLY A CA    1 
ATOM   7393  C C     . GLY A  1 1026 ? -12.848 65.779  109.282 1.00 19.43 ? 1024 GLY A C     1 
ATOM   7394  O O     . GLY A  1 1026 ? -13.039 66.305  110.378 1.00 19.62 ? 1024 GLY A O     1 
ATOM   7395  N N     . PRO A  1 1027 ? -11.953 64.806  109.107 1.00 19.46 ? 1025 PRO A N     1 
ATOM   7396  C CA    . PRO A  1 1027 ? -11.397 64.105  110.262 1.00 20.94 ? 1025 PRO A CA    1 
ATOM   7397  C C     . PRO A  1 1027 ? -10.224 64.816  110.902 1.00 19.91 ? 1025 PRO A C     1 
ATOM   7398  O O     . PRO A  1 1027 ? -9.762  64.365  111.961 1.00 20.17 ? 1025 PRO A O     1 
ATOM   7399  C CB    . PRO A  1 1027 ? -10.982 62.756  109.666 1.00 20.77 ? 1025 PRO A CB    1 
ATOM   7400  C CG    . PRO A  1 1027 ? -10.596 63.094  108.235 1.00 21.49 ? 1025 PRO A CG    1 
ATOM   7401  C CD    . PRO A  1 1027 ? -11.575 64.170  107.826 1.00 19.28 ? 1025 PRO A CD    1 
ATOM   7402  N N     . LEU A  1 1028 ? -9.718  65.904  110.307 1.00 19.82 ? 1026 LEU A N     1 
ATOM   7403  C CA    . LEU A  1 1028 ? -8.654  66.676  110.945 1.00 20.11 ? 1026 LEU A CA    1 
ATOM   7404  C C     . LEU A  1 1028 ? -9.180  67.817  111.799 1.00 22.65 ? 1026 LEU A C     1 
ATOM   7405  O O     . LEU A  1 1028 ? -8.387  68.461  112.496 1.00 20.79 ? 1026 LEU A O     1 
ATOM   7406  C CB    . LEU A  1 1028 ? -7.699  67.272  109.908 1.00 19.92 ? 1026 LEU A CB    1 
ATOM   7407  C CG    . LEU A  1 1028 ? -6.975  66.292  108.986 1.00 22.84 ? 1026 LEU A CG    1 
ATOM   7408  C CD1   . LEU A  1 1028 ? -5.928  67.047  108.168 1.00 20.18 ? 1026 LEU A CD1   1 
ATOM   7409  C CD2   . LEU A  1 1028 ? -6.350  65.154  109.758 1.00 23.78 ? 1026 LEU A CD2   1 
ATOM   7410  N N     . TYR A  1 1029 ? -10.490 68.060  111.776 1.00 20.07 ? 1027 TYR A N     1 
ATOM   7411  C CA    . TYR A  1 1029 ? -11.055 69.261  112.389 1.00 20.60 ? 1027 TYR A CA    1 
ATOM   7412  C C     . TYR A  1 1029 ? -10.856 69.284  113.902 1.00 21.35 ? 1027 TYR A C     1 
ATOM   7413  O O     . TYR A  1 1029 ? -10.405 70.292  114.461 1.00 20.73 ? 1027 TYR A O     1 
ATOM   7414  C CB    . TYR A  1 1029 ? -12.540 69.343  112.053 1.00 25.94 ? 1027 TYR A CB    1 
ATOM   7415  C CG    . TYR A  1 1029 ? -13.173 70.715  112.097 1.00 22.16 ? 1027 TYR A CG    1 
ATOM   7416  C CD1   . TYR A  1 1029 ? -12.786 71.711  111.212 1.00 24.43 ? 1027 TYR A CD1   1 
ATOM   7417  C CD2   . TYR A  1 1029 ? -14.206 70.985  112.981 1.00 24.02 ? 1027 TYR A CD2   1 
ATOM   7418  C CE1   . TYR A  1 1029 ? -13.401 72.949  111.214 1.00 20.85 ? 1027 TYR A CE1   1 
ATOM   7419  C CE2   . TYR A  1 1029 ? -14.838 72.226  112.995 1.00 22.03 ? 1027 TYR A CE2   1 
ATOM   7420  C CZ    . TYR A  1 1029 ? -14.437 73.195  112.102 1.00 23.54 ? 1027 TYR A CZ    1 
ATOM   7421  O OH    . TYR A  1 1029 ? -15.054 74.421  112.107 1.00 24.80 ? 1027 TYR A OH    1 
ATOM   7422  N N     . LEU A  1 1030 ? -11.249 68.208  114.594 1.00 20.64 ? 1028 LEU A N     1 
ATOM   7423  C CA    . LEU A  1 1030 ? -11.185 68.252  116.056 1.00 21.00 ? 1028 LEU A CA    1 
ATOM   7424  C C     . LEU A  1 1030 ? -9.752  68.373  116.544 1.00 21.21 ? 1028 LEU A C     1 
ATOM   7425  O O     . LEU A  1 1030 ? -9.511  68.951  117.613 1.00 21.51 ? 1028 LEU A O     1 
ATOM   7426  C CB    . LEU A  1 1030 ? -11.830 67.010  116.674 1.00 21.11 ? 1028 LEU A CB    1 
ATOM   7427  C CG    . LEU A  1 1030 ? -13.301 66.768  116.326 1.00 24.06 ? 1028 LEU A CG    1 
ATOM   7428  C CD1   . LEU A  1 1030 ? -13.808 65.567  117.086 1.00 23.21 ? 1028 LEU A CD1   1 
ATOM   7429  C CD2   . LEU A  1 1030 ? -14.101 67.987  116.694 1.00 24.52 ? 1028 LEU A CD2   1 
ATOM   7430  N N     . GLY A  1 1031 ? -8.793  67.825  115.797 1.00 21.08 ? 1029 GLY A N     1 
ATOM   7431  C CA    . GLY A  1 1031 ? -7.407  67.865  116.259 1.00 21.29 ? 1029 GLY A CA    1 
ATOM   7432  C C     . GLY A  1 1031 ? -6.832  69.263  116.373 1.00 21.40 ? 1029 GLY A C     1 
ATOM   7433  O O     . GLY A  1 1031 ? -5.837  69.469  117.084 1.00 21.66 ? 1029 GLY A O     1 
ATOM   7434  N N     . ARG A  1 1032 ? -7.414  70.225  115.671 1.00 21.22 ? 1030 ARG A N     1 
ATOM   7435  C CA    . ARG A  1 1032 ? -7.002  71.610  115.792 1.00 21.57 ? 1030 ARG A CA    1 
ATOM   7436  C C     . ARG A  1 1032 ? -7.512  72.255  117.071 1.00 21.67 ? 1030 ARG A C     1 
ATOM   7437  O O     . ARG A  1 1032 ? -7.064  73.348  117.415 1.00 21.92 ? 1030 ARG A O     1 
ATOM   7438  C CB    . ARG A  1 1032 ? -7.503  72.400  114.575 1.00 21.10 ? 1030 ARG A CB    1 
ATOM   7439  C CG    . ARG A  1 1032 ? -6.883  73.774  114.403 1.00 24.65 ? 1030 ARG A CG    1 
ATOM   7440  C CD    . ARG A  1 1032 ? -5.431  73.709  113.939 1.00 25.60 ? 1030 ARG A CD    1 
ATOM   7441  N NE    . ARG A  1 1032 ? -4.972  75.034  113.536 1.00 28.25 ? 1030 ARG A NE    1 
ATOM   7442  C CZ    . ARG A  1 1032 ? -3.966  75.697  114.090 1.00 28.12 ? 1030 ARG A CZ    1 
ATOM   7443  N NH1   . ARG A  1 1032 ? -3.248  75.175  115.074 1.00 27.66 ? 1030 ARG A NH1   1 
ATOM   7444  N NH2   . ARG A  1 1032 ? -3.667  76.913  113.640 1.00 28.34 ? 1030 ARG A NH2   1 
ATOM   7445  N N     . LEU A  1 1033 ? -8.438  71.614  117.783 1.00 21.75 ? 1031 LEU A N     1 
ATOM   7446  C CA    . LEU A  1 1033 ? -9.102  72.244  118.916 1.00 22.04 ? 1031 LEU A CA    1 
ATOM   7447  C C     . LEU A  1 1033 ? -8.619  71.680  120.241 1.00 23.61 ? 1031 LEU A C     1 
ATOM   7448  O O     . LEU A  1 1033 ? -9.261  71.904  121.274 1.00 23.07 ? 1031 LEU A O     1 
ATOM   7449  C CB    . LEU A  1 1033 ? -10.613 72.089  118.795 1.00 21.91 ? 1031 LEU A CB    1 
ATOM   7450  C CG    . LEU A  1 1033 ? -11.185 72.639  117.486 1.00 22.94 ? 1031 LEU A CG    1 
ATOM   7451  C CD1   . LEU A  1 1033 ? -12.667 72.395  117.430 1.00 21.47 ? 1031 LEU A CD1   1 
ATOM   7452  C CD2   . LEU A  1 1033 ? -10.907 74.140  117.364 1.00 22.91 ? 1031 LEU A CD2   1 
ATOM   7453  N N     . VAL A  1 1034 ? -7.521  70.924  120.216 1.00 22.43 ? 1032 VAL A N     1 
ATOM   7454  C CA    . VAL A  1 1034 ? -6.884  70.395  121.412 1.00 23.05 ? 1032 VAL A CA    1 
ATOM   7455  C C     . VAL A  1 1034 ? -5.393  70.696  121.335 1.00 24.99 ? 1032 VAL A C     1 
ATOM   7456  O O     . VAL A  1 1034 ? -4.856  71.051  120.285 1.00 24.31 ? 1032 VAL A O     1 
ATOM   7457  C CB    . VAL A  1 1034 ? -7.142  68.881  121.583 1.00 25.51 ? 1032 VAL A CB    1 
ATOM   7458  C CG1   . VAL A  1 1034 ? -8.630  68.618  121.860 1.00 24.64 ? 1032 VAL A CG1   1 
ATOM   7459  C CG2   . VAL A  1 1034 ? -6.667  68.104  120.371 1.00 22.80 ? 1032 VAL A CG2   1 
ATOM   7460  N N     . THR A  1 1035 ? -4.720  70.565  122.480 1.00 24.98 ? 1033 THR A N     1 
ATOM   7461  C CA    . THR A  1 1035 ? -3.310  70.910  122.529 1.00 27.18 ? 1033 THR A CA    1 
ATOM   7462  C C     . THR A  1 1035 ? -2.424  69.809  121.956 1.00 26.81 ? 1033 THR A C     1 
ATOM   7463  O O     . THR A  1 1035 ? -1.344  70.102  121.442 1.00 32.52 ? 1033 THR A O     1 
ATOM   7464  C CB    . THR A  1 1035 ? -2.927  71.232  123.970 1.00 27.54 ? 1033 THR A CB    1 
ATOM   7465  O OG1   . THR A  1 1035 ? -3.375  70.171  124.818 1.00 33.32 ? 1033 THR A OG1   1 
ATOM   7466  C CG2   . THR A  1 1035 ? -3.620  72.514  124.406 1.00 26.40 ? 1033 THR A CG2   1 
ATOM   7467  N N     . THR A  1 1036 ? -2.869  68.553  122.019 1.00 26.99 ? 1034 THR A N     1 
ATOM   7468  C CA    . THR A  1 1036 ? -2.177  67.406  121.435 1.00 26.21 ? 1034 THR A CA    1 
ATOM   7469  C C     . THR A  1 1036 ? -3.153  66.724  120.483 1.00 25.69 ? 1034 THR A C     1 
ATOM   7470  O O     . THR A  1 1036 ? -4.140  66.137  120.929 1.00 25.97 ? 1034 THR A O     1 
ATOM   7471  C CB    . THR A  1 1036 ? -1.723  66.428  122.521 1.00 32.11 ? 1034 THR A CB    1 
ATOM   7472  O OG1   . THR A  1 1036 ? -0.905  67.119  123.470 1.00 37.85 ? 1034 THR A OG1   1 
ATOM   7473  C CG2   . THR A  1 1036 ? -0.935  65.269  121.920 1.00 35.07 ? 1034 THR A CG2   1 
ATOM   7474  N N     . ALA A  1 1037 ? -2.871  66.780  119.190 1.00 22.41 ? 1035 ALA A N     1 
ATOM   7475  C CA    . ALA A  1 1037 ? -3.818  66.245  118.214 1.00 24.63 ? 1035 ALA A CA    1 
ATOM   7476  C C     . ALA A  1 1037 ? -3.837  64.718  118.280 1.00 25.48 ? 1035 ALA A C     1 
ATOM   7477  O O     . ALA A  1 1037 ? -2.782  64.090  118.399 1.00 27.48 ? 1035 ALA A O     1 
ATOM   7478  C CB    . ALA A  1 1037 ? -3.457  66.708  116.801 1.00 26.00 ? 1035 ALA A CB    1 
ATOM   7479  N N     . PRO A  1 1038 ? -5.015  64.098  118.225 1.00 26.69 ? 1036 PRO A N     1 
ATOM   7480  C CA    . PRO A  1 1038 ? -5.088  62.638  118.124 1.00 25.20 ? 1036 PRO A CA    1 
ATOM   7481  C C     . PRO A  1 1038 ? -4.809  62.187  116.696 1.00 26.37 ? 1036 PRO A C     1 
ATOM   7482  O O     . PRO A  1 1038 ? -4.701  62.989  115.770 1.00 26.53 ? 1036 PRO A O     1 
ATOM   7483  C CB    . PRO A  1 1038 ? -6.529  62.337  118.520 1.00 24.35 ? 1036 PRO A CB    1 
ATOM   7484  C CG    . PRO A  1 1038 ? -7.283  63.530  117.936 1.00 26.39 ? 1036 PRO A CG    1 
ATOM   7485  C CD    . PRO A  1 1038 ? -6.356  64.718  118.208 1.00 23.28 ? 1036 PRO A CD    1 
ATOM   7486  N N     . VAL A  1 1039 ? -4.681  60.874  116.534 1.00 23.36 ? 1037 VAL A N     1 
ATOM   7487  C CA    . VAL A  1 1039 ? -4.584  60.267  115.208 1.00 26.07 ? 1037 VAL A CA    1 
ATOM   7488  C C     . VAL A  1 1039 ? -5.995  60.099  114.657 1.00 22.21 ? 1037 VAL A C     1 
ATOM   7489  O O     . VAL A  1 1039 ? -6.786  59.349  115.243 1.00 21.38 ? 1037 VAL A O     1 
ATOM   7490  C CB    . VAL A  1 1039 ? -3.856  58.917  115.268 1.00 25.20 ? 1037 VAL A CB    1 
ATOM   7491  C CG1   . VAL A  1 1039 ? -3.644  58.366  113.876 1.00 26.55 ? 1037 VAL A CG1   1 
ATOM   7492  C CG2   . VAL A  1 1039 ? -2.534  59.056  116.007 1.00 23.77 ? 1037 VAL A CG2   1 
ATOM   7493  N N     . PRO A  1 1040 ? -6.368  60.756  113.558 1.00 23.12 ? 1038 PRO A N     1 
ATOM   7494  C CA    . PRO A  1 1040 ? -7.734  60.625  113.060 1.00 23.31 ? 1038 PRO A CA    1 
ATOM   7495  C C     . PRO A  1 1040 ? -8.014  59.216  112.571 1.00 24.40 ? 1038 PRO A C     1 
ATOM   7496  O O     . PRO A  1 1040 ? -7.082  58.467  112.235 1.00 25.43 ? 1038 PRO A O     1 
ATOM   7497  C CB    . PRO A  1 1040 ? -7.798  61.634  111.897 1.00 20.79 ? 1038 PRO A CB    1 
ATOM   7498  C CG    . PRO A  1 1040 ? -6.687  62.575  112.143 1.00 21.80 ? 1038 PRO A CG    1 
ATOM   7499  C CD    . PRO A  1 1040 ? -5.606  61.781  112.823 1.00 21.48 ? 1038 PRO A CD    1 
ATOM   7500  N N     . PRO A  1 1041 ? -9.288  58.823  112.513 1.00 22.17 ? 1039 PRO A N     1 
ATOM   7501  C CA    . PRO A  1 1041 ? -9.649  57.574  111.832 1.00 25.13 ? 1039 PRO A CA    1 
ATOM   7502  C C     . PRO A  1 1041 ? -9.074  57.541  110.421 1.00 23.21 ? 1039 PRO A C     1 
ATOM   7503  O O     . PRO A  1 1041 ? -9.045  58.555  109.717 1.00 22.12 ? 1039 PRO A O     1 
ATOM   7504  C CB    . PRO A  1 1041 ? -11.185 57.610  111.808 1.00 25.34 ? 1039 PRO A CB    1 
ATOM   7505  C CG    . PRO A  1 1041 ? -11.565 58.554  112.922 1.00 24.70 ? 1039 PRO A CG    1 
ATOM   7506  C CD    . PRO A  1 1041 ? -10.474 59.576  112.965 1.00 25.17 ? 1039 PRO A CD    1 
ATOM   7507  N N     . GLN A  1 1042 ? -8.618  56.358  110.024 1.00 21.47 ? 1040 GLN A N     1 
ATOM   7508  C CA    . GLN A  1 1042 ? -8.128  56.051  108.683 1.00 20.27 ? 1040 GLN A CA    1 
ATOM   7509  C C     . GLN A  1 1042 ? -7.004  56.970  108.212 1.00 22.18 ? 1040 GLN A C     1 
ATOM   7510  O O     . GLN A  1 1042 ? -6.774  57.088  107.010 1.00 23.39 ? 1040 GLN A O     1 
ATOM   7511  C CB    . GLN A  1 1042 ? -9.275  56.078  107.664 1.00 24.41 ? 1040 GLN A CB    1 
ATOM   7512  C CG    . GLN A  1 1042 ? -10.427 55.156  108.002 1.00 24.68 ? 1040 GLN A CG    1 
ATOM   7513  C CD    . GLN A  1 1042 ? -11.457 55.118  106.897 1.00 31.25 ? 1040 GLN A CD    1 
ATOM   7514  O OE1   . GLN A  1 1042 ? -12.558 55.625  107.047 1.00 35.33 ? 1040 GLN A OE1   1 
ATOM   7515  N NE2   . GLN A  1 1042 ? -11.094 54.523  105.779 1.00 32.80 ? 1040 GLN A NE2   1 
ATOM   7516  N N     . HIS A  1 1043 ? -6.284  57.628  109.122 1.00 20.33 ? 1041 HIS A N     1 
ATOM   7517  C CA    . HIS A  1 1043 ? -5.321  58.666  108.774 1.00 22.10 ? 1041 HIS A CA    1 
ATOM   7518  C C     . HIS A  1 1043 ? -3.915  58.074  108.835 1.00 23.31 ? 1041 HIS A C     1 
ATOM   7519  O O     . HIS A  1 1043 ? -3.308  57.996  109.910 1.00 22.21 ? 1041 HIS A O     1 
ATOM   7520  C CB    . HIS A  1 1043 ? -5.467  59.854  109.718 1.00 23.24 ? 1041 HIS A CB    1 
ATOM   7521  C CG    . HIS A  1 1043 ? -4.505  60.969  109.453 1.00 23.31 ? 1041 HIS A CG    1 
ATOM   7522  N ND1   . HIS A  1 1043 ? -4.769  61.977  108.550 1.00 20.37 ? 1041 HIS A ND1   1 
ATOM   7523  C CD2   . HIS A  1 1043 ? -3.305  61.265  110.010 1.00 23.39 ? 1041 HIS A CD2   1 
ATOM   7524  C CE1   . HIS A  1 1043 ? -3.761  62.831  108.540 1.00 22.16 ? 1041 HIS A CE1   1 
ATOM   7525  N NE2   . HIS A  1 1043 ? -2.857  62.421  109.416 1.00 22.11 ? 1041 HIS A NE2   1 
ATOM   7526  N N     . SER A  1 1044 ? -3.404  57.660  107.679 1.00 21.30 ? 1042 SER A N     1 
ATOM   7527  C CA    . SER A  1 1044 ? -2.077  57.071  107.521 1.00 22.39 ? 1042 SER A CA    1 
ATOM   7528  C C     . SER A  1 1044 ? -1.795  56.956  106.032 1.00 24.15 ? 1042 SER A C     1 
ATOM   7529  O O     . SER A  1 1044 ? -2.711  57.033  105.207 1.00 24.04 ? 1042 SER A O     1 
ATOM   7530  C CB    . SER A  1 1044 ? -1.960  55.689  108.181 1.00 22.91 ? 1042 SER A CB    1 
ATOM   7531  O OG    . SER A  1 1044 ? -2.669  54.730  107.421 1.00 25.26 ? 1042 SER A OG    1 
ATOM   7532  N N     . SER A  1 1045 ? -0.516  56.766  105.701 1.00 24.68 ? 1043 SER A N     1 
ATOM   7533  C CA    . SER A  1 1045 ? -0.123  56.563  104.314 1.00 24.87 ? 1043 SER A CA    1 
ATOM   7534  C C     . SER A  1 1045 ? 1.089   55.650  104.264 1.00 21.86 ? 1043 SER A C     1 
ATOM   7535  O O     . SER A  1 1045 ? 1.989   55.759  105.100 1.00 21.72 ? 1043 SER A O     1 
ATOM   7536  C CB    . SER A  1 1045 ? 0.196   57.891  103.615 1.00 22.20 ? 1043 SER A CB    1 
ATOM   7537  O OG    . SER A  1 1045 ? 0.732   57.656  102.323 1.00 22.83 ? 1043 SER A OG    1 
ATOM   7538  N N     . VAL A  1 1046 ? 1.111   54.737  103.286 1.00 20.78 ? 1044 VAL A N     1 
ATOM   7539  C CA    . VAL A  1 1046 ? 2.296   53.907  103.094 1.00 24.60 ? 1044 VAL A CA    1 
ATOM   7540  C C     . VAL A  1 1046 ? 3.312   54.568  102.179 1.00 22.95 ? 1044 VAL A C     1 
ATOM   7541  O O     . VAL A  1 1046 ? 4.378   53.990  101.942 1.00 23.77 ? 1044 VAL A O     1 
ATOM   7542  C CB    . VAL A  1 1046 ? 1.934   52.509  102.543 1.00 23.50 ? 1044 VAL A CB    1 
ATOM   7543  C CG1   . VAL A  1 1046 ? 0.980   51.810  103.499 1.00 27.43 ? 1044 VAL A CG1   1 
ATOM   7544  C CG2   . VAL A  1 1046 ? 1.349   52.617  101.134 1.00 21.19 ? 1044 VAL A CG2   1 
ATOM   7545  N N     . HIS A  1 1047 ? 3.009   55.759  101.650 1.00 21.67 ? 1045 HIS A N     1 
ATOM   7546  C CA    . HIS A  1 1047 ? 3.917   56.479  100.769 1.00 23.84 ? 1045 HIS A CA    1 
ATOM   7547  C C     . HIS A  1 1047 ? 4.892   57.296  101.601 1.00 27.12 ? 1045 HIS A C     1 
ATOM   7548  O O     . HIS A  1 1047 ? 4.508   57.920  102.593 1.00 26.65 ? 1045 HIS A O     1 
ATOM   7549  C CB    . HIS A  1 1047 ? 3.139   57.393  99.814  1.00 25.88 ? 1045 HIS A CB    1 
ATOM   7550  C CG    . HIS A  1 1047 ? 3.962   58.491  99.208  1.00 28.21 ? 1045 HIS A CG    1 
ATOM   7551  N ND1   . HIS A  1 1047 ? 4.766   58.300  98.102  1.00 27.25 ? 1045 HIS A ND1   1 
ATOM   7552  C CD2   . HIS A  1 1047 ? 4.092   59.800  99.543  1.00 29.74 ? 1045 HIS A CD2   1 
ATOM   7553  C CE1   . HIS A  1 1047 ? 5.360   59.440  97.787  1.00 30.83 ? 1045 HIS A CE1   1 
ATOM   7554  N NE2   . HIS A  1 1047 ? 4.960   60.370  98.640  1.00 22.53 ? 1045 HIS A NE2   1 
ATOM   7555  N N     . THR A  1 1048 ? 6.157   57.271  101.197 1.00 26.07 ? 1046 THR A N     1 
ATOM   7556  C CA    . THR A  1 1048 ? 7.198   58.093  101.791 1.00 23.43 ? 1046 THR A CA    1 
ATOM   7557  C C     . THR A  1 1048 ? 7.693   59.073  100.740 1.00 25.31 ? 1046 THR A C     1 
ATOM   7558  O O     . THR A  1 1048 ? 8.036   58.670  99.623  1.00 25.98 ? 1046 THR A O     1 
ATOM   7559  C CB    . THR A  1 1048 ? 8.355   57.242  102.297 1.00 25.63 ? 1046 THR A CB    1 
ATOM   7560  O OG1   . THR A  1 1048 ? 7.841   56.174  103.094 1.00 24.81 ? 1046 THR A OG1   1 
ATOM   7561  C CG2   . THR A  1 1048 ? 9.297   58.106  103.149 1.00 24.81 ? 1046 THR A CG2   1 
ATOM   7562  N N     . ASP A  1 1049 ? 7.709   60.349  101.083 1.00 22.37 ? 1047 ASP A N     1 
ATOM   7563  C CA    . ASP A  1 1049 ? 8.220   61.337  100.146 1.00 22.43 ? 1047 ASP A CA    1 
ATOM   7564  C C     . ASP A  1 1049 ? 9.673   61.006  99.791  1.00 21.58 ? 1047 ASP A C     1 
ATOM   7565  O O     . ASP A  1 1049 ? 10.498  60.806  100.691 1.00 21.80 ? 1047 ASP A O     1 
ATOM   7566  C CB    . ASP A  1 1049 ? 8.104   62.740  100.753 1.00 21.23 ? 1047 ASP A CB    1 
ATOM   7567  C CG    . ASP A  1 1049 ? 8.559   63.827  99.789  1.00 23.04 ? 1047 ASP A CG    1 
ATOM   7568  O OD1   . ASP A  1 1049 ? 9.779   64.079  99.713  1.00 22.99 ? 1047 ASP A OD1   1 
ATOM   7569  O OD2   . ASP A  1 1049 ? 7.699   64.396  99.066  1.00 25.94 ? 1047 ASP A OD2   1 
ATOM   7570  N N     . PRO A  1 1050 ? 10.023  60.925  98.508  1.00 21.79 ? 1048 PRO A N     1 
ATOM   7571  C CA    . PRO A  1 1050 ? 11.409  60.577  98.155  1.00 21.94 ? 1048 PRO A CA    1 
ATOM   7572  C C     . PRO A  1 1050 ? 12.418  61.686  98.436  1.00 23.52 ? 1048 PRO A C     1 
ATOM   7573  O O     . PRO A  1 1050 ? 13.608  61.399  98.626  1.00 24.18 ? 1048 PRO A O     1 
ATOM   7574  C CB    . PRO A  1 1050 ? 11.318  60.271  96.654  1.00 26.31 ? 1048 PRO A CB    1 
ATOM   7575  C CG    . PRO A  1 1050 ? 10.101  61.013  96.191  1.00 24.13 ? 1048 PRO A CG    1 
ATOM   7576  C CD    . PRO A  1 1050 ? 9.139   60.989  97.326  1.00 22.81 ? 1048 PRO A CD    1 
ATOM   7577  N N     . VAL A  1 1051 ? 11.999  62.949  98.426  1.00 22.00 ? 1049 VAL A N     1 
ATOM   7578  C CA    . VAL A  1 1051 ? 12.947  64.009  98.743  1.00 22.22 ? 1049 VAL A CA    1 
ATOM   7579  C C     . VAL A  1 1051 ? 13.250  64.001  100.234 1.00 22.33 ? 1049 VAL A C     1 
ATOM   7580  O O     . VAL A  1 1051 ? 14.400  64.183  100.645 1.00 22.61 ? 1049 VAL A O     1 
ATOM   7581  C CB    . VAL A  1 1051 ? 12.416  65.363  98.255  1.00 22.09 ? 1049 VAL A CB    1 
ATOM   7582  C CG1   . VAL A  1 1051 ? 13.393  66.467  98.567  1.00 25.26 ? 1049 VAL A CG1   1 
ATOM   7583  C CG2   . VAL A  1 1051 ? 12.144  65.280  96.736  1.00 22.02 ? 1049 VAL A CG2   1 
ATOM   7584  N N     . LEU A  1 1052 ? 12.235  63.748  101.065 1.00 22.12 ? 1050 LEU A N     1 
ATOM   7585  C CA    . LEU A  1 1052 ? 12.490  63.478  102.474 1.00 22.25 ? 1050 LEU A CA    1 
ATOM   7586  C C     . LEU A  1 1052 ? 13.544  62.388  102.634 1.00 22.52 ? 1050 LEU A C     1 
ATOM   7587  O O     . LEU A  1 1052 ? 14.466  62.517  103.439 1.00 22.78 ? 1050 LEU A O     1 
ATOM   7588  C CB    . LEU A  1 1052 ? 11.185  63.094  103.190 1.00 22.01 ? 1050 LEU A CB    1 
ATOM   7589  C CG    . LEU A  1 1052 ? 11.250  62.694  104.677 1.00 24.19 ? 1050 LEU A CG    1 
ATOM   7590  C CD1   . LEU A  1 1052 ? 11.740  61.275  104.934 1.00 22.32 ? 1050 LEU A CD1   1 
ATOM   7591  C CD2   . LEU A  1 1052 ? 12.125  63.689  105.451 1.00 22.38 ? 1050 LEU A CD2   1 
ATOM   7592  N N     . LEU A  1 1053 ? 13.404  61.292  101.883 1.00 22.49 ? 1051 LEU A N     1 
ATOM   7593  C CA    . LEU A  1 1053 ? 14.356  60.188  101.991 1.00 24.13 ? 1051 LEU A CA    1 
ATOM   7594  C C     . LEU A  1 1053 ? 15.757  60.620  101.568 1.00 23.07 ? 1051 LEU A C     1 
ATOM   7595  O O     . LEU A  1 1053 ? 16.746  60.253  102.210 1.00 23.36 ? 1051 LEU A O     1 
ATOM   7596  C CB    . LEU A  1 1053 ? 13.872  59.005  101.140 1.00 24.49 ? 1051 LEU A CB    1 
ATOM   7597  C CG    . LEU A  1 1053 ? 12.688  58.195  101.672 1.00 26.24 ? 1051 LEU A CG    1 
ATOM   7598  C CD1   . LEU A  1 1053 ? 12.267  57.114  100.665 1.00 22.96 ? 1051 LEU A CD1   1 
ATOM   7599  C CD2   . LEU A  1 1053 ? 13.000  57.574  103.029 1.00 24.73 ? 1051 LEU A CD2   1 
ATOM   7600  N N     . ASP A  1 1054 ? 15.861  61.403  100.490 1.00 23.03 ? 1052 ASP A N     1 
ATOM   7601  C CA    . ASP A  1 1054 ? 17.160  61.946  100.099 1.00 23.33 ? 1052 ASP A CA    1 
ATOM   7602  C C     . ASP A  1 1054 ? 17.726  62.837  101.195 1.00 23.49 ? 1052 ASP A C     1 
ATOM   7603  O O     . ASP A  1 1054 ? 18.936  62.821  101.455 1.00 24.38 ? 1052 ASP A O     1 
ATOM   7604  C CB    . ASP A  1 1054 ? 17.050  62.742  98.803  1.00 25.44 ? 1052 ASP A CB    1 
ATOM   7605  C CG    . ASP A  1 1054 ? 16.704  61.875  97.611  1.00 26.84 ? 1052 ASP A CG    1 
ATOM   7606  O OD1   . ASP A  1 1054 ? 16.767  60.635  97.750  1.00 26.22 ? 1052 ASP A OD1   1 
ATOM   7607  O OD2   . ASP A  1 1054 ? 16.353  62.435  96.552  1.00 26.70 ? 1052 ASP A OD2   1 
ATOM   7608  N N     . PHE A  1 1055 ? 16.861  63.613  101.850 1.00 23.28 ? 1053 PHE A N     1 
ATOM   7609  C CA    . PHE A  1 1055 ? 17.320  64.515  102.907 1.00 23.81 ? 1053 PHE A CA    1 
ATOM   7610  C C     . PHE A  1 1055 ? 17.820  63.741  104.120 1.00 23.63 ? 1053 PHE A C     1 
ATOM   7611  O O     . PHE A  1 1055 ? 18.841  64.103  104.717 1.00 23.93 ? 1053 PHE A O     1 
ATOM   7612  C CB    . PHE A  1 1055 ? 16.194  65.478  103.291 1.00 23.18 ? 1053 PHE A CB    1 
ATOM   7613  C CG    . PHE A  1 1055 ? 16.548  66.435  104.413 1.00 23.35 ? 1053 PHE A CG    1 
ATOM   7614  C CD1   . PHE A  1 1055 ? 17.612  67.317  104.289 1.00 27.04 ? 1053 PHE A CD1   1 
ATOM   7615  C CD2   . PHE A  1 1055 ? 15.774  66.488  105.561 1.00 23.24 ? 1053 PHE A CD2   1 
ATOM   7616  C CE1   . PHE A  1 1055 ? 17.925  68.223  105.329 1.00 23.82 ? 1053 PHE A CE1   1 
ATOM   7617  C CE2   . PHE A  1 1055 ? 16.072  67.389  106.592 1.00 23.43 ? 1053 PHE A CE2   1 
ATOM   7618  C CZ    . PHE A  1 1055 ? 17.150  68.247  106.471 1.00 23.72 ? 1053 PHE A CZ    1 
ATOM   7619  N N     . ALA A  1 1056 ? 17.135  62.658  104.495 1.00 26.70 ? 1054 ALA A N     1 
ATOM   7620  C CA    . ALA A  1 1056 ? 17.598  61.879  105.645 1.00 23.72 ? 1054 ALA A CA    1 
ATOM   7621  C C     . ALA A  1 1056 ? 18.965  61.251  105.386 1.00 24.07 ? 1054 ALA A C     1 
ATOM   7622  O O     . ALA A  1 1056 ? 19.825  61.229  106.281 1.00 24.37 ? 1054 ALA A O     1 
ATOM   7623  C CB    . ALA A  1 1056 ? 16.564  60.811  106.010 1.00 23.54 ? 1054 ALA A CB    1 
ATOM   7624  N N     . LYS A  1 1057 ? 19.186  60.720  104.175 1.00 29.15 ? 1055 LYS A N     1 
ATOM   7625  C CA    . LYS A  1 1057 ? 20.505  60.189  103.838 1.00 28.84 ? 1055 LYS A CA    1 
ATOM   7626  C C     . LYS A  1 1057 ? 21.561  61.286  103.863 1.00 28.88 ? 1055 LYS A C     1 
ATOM   7627  O O     . LYS A  1 1057 ? 22.688  61.066  104.327 1.00 32.12 ? 1055 LYS A O     1 
ATOM   7628  C CB    . LYS A  1 1057 ? 20.476  59.508  102.464 1.00 28.66 ? 1055 LYS A CB    1 
ATOM   7629  C CG    . LYS A  1 1057 ? 19.765  58.157  102.457 1.00 28.44 ? 1055 LYS A CG    1 
ATOM   7630  C CD    . LYS A  1 1057 ? 19.916  57.450  101.112 1.00 29.92 ? 1055 LYS A CD    1 
ATOM   7631  C CE    . LYS A  1 1057 ? 19.396  58.322  99.984  1.00 27.69 ? 1055 LYS A CE    1 
ATOM   7632  N NZ    . LYS A  1 1057 ? 19.177  57.548  98.734  1.00 31.82 ? 1055 LYS A NZ    1 
ATOM   7633  N N     . TRP A  1 1058 ? 21.215  62.474  103.358 1.00 28.15 ? 1056 TRP A N     1 
ATOM   7634  C CA    . TRP A  1 1058 ? 22.129  63.604  103.434 1.00 28.25 ? 1056 TRP A CA    1 
ATOM   7635  C C     . TRP A  1 1058 ? 22.468  63.935  104.882 1.00 27.89 ? 1056 TRP A C     1 
ATOM   7636  O O     . TRP A  1 1058 ? 23.636  64.167  105.210 1.00 31.84 ? 1056 TRP A O     1 
ATOM   7637  C CB    . TRP A  1 1058 ? 21.528  64.821  102.728 1.00 26.98 ? 1056 TRP A CB    1 
ATOM   7638  C CG    . TRP A  1 1058 ? 22.401  66.054  102.808 1.00 33.07 ? 1056 TRP A CG    1 
ATOM   7639  C CD1   . TRP A  1 1058 ? 23.440  66.380  101.982 1.00 28.80 ? 1056 TRP A CD1   1 
ATOM   7640  C CD2   . TRP A  1 1058 ? 22.304  67.126  103.771 1.00 31.70 ? 1056 TRP A CD2   1 
ATOM   7641  N NE1   . TRP A  1 1058 ? 23.998  67.581  102.375 1.00 32.89 ? 1056 TRP A NE1   1 
ATOM   7642  C CE2   . TRP A  1 1058 ? 23.315  68.062  103.461 1.00 31.27 ? 1056 TRP A CE2   1 
ATOM   7643  C CE3   . TRP A  1 1058 ? 21.457  67.385  104.855 1.00 28.18 ? 1056 TRP A CE3   1 
ATOM   7644  C CZ2   . TRP A  1 1058 ? 23.506  69.234  104.201 1.00 31.84 ? 1056 TRP A CZ2   1 
ATOM   7645  C CZ3   . TRP A  1 1058 ? 21.650  68.555  105.592 1.00 26.58 ? 1056 TRP A CZ3   1 
ATOM   7646  C CH2   . TRP A  1 1058 ? 22.668  69.459  105.260 1.00 29.38 ? 1056 TRP A CH2   1 
ATOM   7647  N N     . LEU A  1 1059 ? 21.462  63.938  105.767 1.00 26.03 ? 1057 LEU A N     1 
ATOM   7648  C CA    . LEU A  1 1059 ? 21.712  64.212  107.182 1.00 25.06 ? 1057 LEU A CA    1 
ATOM   7649  C C     . LEU A  1 1059 ? 22.685  63.201  107.763 1.00 30.18 ? 1057 LEU A C     1 
ATOM   7650  O O     . LEU A  1 1059 ? 23.636  63.564  108.471 1.00 28.57 ? 1057 LEU A O     1 
ATOM   7651  C CB    . LEU A  1 1059 ? 20.393  64.197  107.962 1.00 27.42 ? 1057 LEU A CB    1 
ATOM   7652  C CG    . LEU A  1 1059 ? 19.430  65.370  107.756 1.00 24.33 ? 1057 LEU A CG    1 
ATOM   7653  C CD1   . LEU A  1 1059 ? 18.093  65.093  108.412 1.00 24.05 ? 1057 LEU A CD1   1 
ATOM   7654  C CD2   . LEU A  1 1059 ? 20.047  66.645  108.339 1.00 24.57 ? 1057 LEU A CD2   1 
ATOM   7655  N N     . ASP A  1 1060 ? 22.463  61.917  107.476 1.00 30.67 ? 1058 ASP A N     1 
ATOM   7656  C CA    . ASP A  1 1060 ? 23.390  60.895  107.952 1.00 34.15 ? 1058 ASP A CA    1 
ATOM   7657  C C     . ASP A  1 1060 ? 24.793  61.127  107.403 1.00 33.56 ? 1058 ASP A C     1 
ATOM   7658  O O     . ASP A  1 1060 ? 25.785  60.981  108.129 1.00 36.79 ? 1058 ASP A O     1 
ATOM   7659  C CB    . ASP A  1 1060 ? 22.881  59.510  107.563 1.00 32.04 ? 1058 ASP A CB    1 
ATOM   7660  C CG    . ASP A  1 1060 ? 22.079  58.860  108.665 1.00 37.01 ? 1058 ASP A CG    1 
ATOM   7661  O OD1   . ASP A  1 1060 ? 22.365  59.140  109.857 1.00 35.19 ? 1058 ASP A OD1   1 
ATOM   7662  O OD2   . ASP A  1 1060 ? 21.170  58.069  108.340 1.00 35.63 ? 1058 ASP A OD2   1 
ATOM   7663  N N     . GLY A  1 1061 ? 24.892  61.527  106.132 1.00 31.49 ? 1059 GLY A N     1 
ATOM   7664  C CA    . GLY A  1 1061 ? 26.193  61.825  105.554 1.00 32.76 ? 1059 GLY A CA    1 
ATOM   7665  C C     . GLY A  1 1061 ? 26.922  62.939  106.285 1.00 35.02 ? 1059 GLY A C     1 
ATOM   7666  O O     . GLY A  1 1061 ? 28.142  62.883  106.456 1.00 35.64 ? 1059 GLY A O     1 
ATOM   7667  N N     . LYS A  1 1062 ? 26.187  63.960  106.734 1.00 32.20 ? 1060 LYS A N     1 
ATOM   7668  C CA    . LYS A  1 1062 ? 26.788  65.070  107.467 1.00 34.49 ? 1060 LYS A CA    1 
ATOM   7669  C C     . LYS A  1 1062 ? 27.043  64.754  108.936 1.00 33.94 ? 1060 LYS A C     1 
ATOM   7670  O O     . LYS A  1 1062 ? 27.613  65.593  109.643 1.00 38.75 ? 1060 LYS A O     1 
ATOM   7671  C CB    . LYS A  1 1062 ? 25.904  66.318  107.358 1.00 33.85 ? 1060 LYS A CB    1 
ATOM   7672  C CG    . LYS A  1 1062 ? 25.814  66.919  105.956 1.00 35.90 ? 1060 LYS A CG    1 
ATOM   7673  C CD    . LYS A  1 1062 ? 27.160  67.463  105.496 1.00 39.36 ? 1060 LYS A CD    1 
ATOM   7674  C CE    . LYS A  1 1062 ? 27.042  68.225  104.182 1.00 38.62 ? 1060 LYS A CE    1 
ATOM   7675  N NZ    . LYS A  1 1062 ? 28.361  68.732  103.699 1.00 41.98 ? 1060 LYS A NZ    1 
ATOM   7676  N N     . GLY A  1 1063 ? 26.652  63.578  109.417 1.00 32.96 ? 1061 GLY A N     1 
ATOM   7677  C CA    . GLY A  1 1063 ? 26.806  63.235  110.815 1.00 34.36 ? 1061 GLY A CA    1 
ATOM   7678  C C     . GLY A  1 1063 ? 25.643  63.625  111.701 1.00 33.35 ? 1061 GLY A C     1 
ATOM   7679  O O     . GLY A  1 1063 ? 25.692  63.364  112.914 1.00 29.79 ? 1061 GLY A O     1 
ATOM   7680  N N     . ALA A  1 1064 ? 24.598  64.241  111.136 1.00 31.85 ? 1062 ALA A N     1 
ATOM   7681  C CA    . ALA A  1 1064 ? 23.408  64.652  111.886 1.00 27.33 ? 1062 ALA A CA    1 
ATOM   7682  C C     . ALA A  1 1064 ? 22.500  63.437  112.074 1.00 27.35 ? 1062 ALA A C     1 
ATOM   7683  O O     . ALA A  1 1064 ? 21.418  63.316  111.492 1.00 25.27 ? 1062 ALA A O     1 
ATOM   7684  C CB    . ALA A  1 1064 ? 22.691  65.790  111.170 1.00 26.03 ? 1062 ALA A CB    1 
ATOM   7685  N N     . ARG A  1 1065 ? 22.968  62.526  112.926 1.00 27.27 ? 1063 ARG A N     1 
ATOM   7686  C CA    . ARG A  1 1065 ? 22.379  61.196  113.001 1.00 27.60 ? 1063 ARG A CA    1 
ATOM   7687  C C     . ARG A  1 1065 ? 21.004  61.223  113.658 1.00 29.29 ? 1063 ARG A C     1 
ATOM   7688  O O     . ARG A  1 1065 ? 20.074  60.563  113.183 1.00 30.38 ? 1063 ARG A O     1 
ATOM   7689  C CB    . ARG A  1 1065 ? 23.332  60.264  113.757 1.00 29.09 ? 1063 ARG A CB    1 
ATOM   7690  N N     . ALA A  1 1066 ? 20.845  61.968  114.758 1.00 27.58 ? 1064 ALA A N     1 
ATOM   7691  C CA    . ALA A  1 1066 ? 19.537  62.029  115.400 1.00 25.43 ? 1064 ALA A CA    1 
ATOM   7692  C C     . ALA A  1 1066 ? 18.523  62.712  114.495 1.00 26.92 ? 1064 ALA A C     1 
ATOM   7693  O O     . ALA A  1 1066 ? 17.360  62.302  114.436 1.00 26.45 ? 1064 ALA A O     1 
ATOM   7694  C CB    . ALA A  1 1066 ? 19.622  62.763  116.740 1.00 28.99 ? 1064 ALA A CB    1 
ATOM   7695  N N     . GLU A  1 1067 ? 18.955  63.751  113.778 1.00 28.03 ? 1065 GLU A N     1 
ATOM   7696  C CA    . GLU A  1 1067 ? 18.059  64.454  112.869 1.00 24.61 ? 1065 GLU A CA    1 
ATOM   7697  C C     . GLU A  1 1067 ? 17.654  63.565  111.703 1.00 24.36 ? 1065 GLU A C     1 
ATOM   7698  O O     . GLU A  1 1067 ? 16.502  63.611  111.253 1.00 26.18 ? 1065 GLU A O     1 
ATOM   7699  C CB    . GLU A  1 1067 ? 18.728  65.724  112.355 1.00 27.96 ? 1065 GLU A CB    1 
ATOM   7700  C CG    . GLU A  1 1067 ? 18.828  66.837  113.378 1.00 26.25 ? 1065 GLU A CG    1 
ATOM   7701  C CD    . GLU A  1 1067 ? 19.997  66.678  114.331 1.00 34.10 ? 1065 GLU A CD    1 
ATOM   7702  O OE1   . GLU A  1 1067 ? 20.787  65.707  114.195 1.00 31.18 ? 1065 GLU A OE1   1 
ATOM   7703  O OE2   . GLU A  1 1067 ? 20.127  67.543  115.226 1.00 32.15 ? 1065 GLU A OE2   1 
ATOM   7704  N N     . ALA A  1 1068 ? 18.590  62.758  111.194 1.00 24.53 ? 1066 ALA A N     1 
ATOM   7705  C CA    . ALA A  1 1068 ? 18.243  61.824  110.123 1.00 24.33 ? 1066 ALA A CA    1 
ATOM   7706  C C     . ALA A  1 1068 ? 17.173  60.838  110.577 1.00 25.00 ? 1066 ALA A C     1 
ATOM   7707  O O     . ALA A  1 1068 ? 16.236  60.538  109.830 1.00 24.52 ? 1066 ALA A O     1 
ATOM   7708  C CB    . ALA A  1 1068 ? 19.493  61.085  109.647 1.00 26.90 ? 1066 ALA A CB    1 
ATOM   7709  N N     . GLU A  1 1069 ? 17.293  60.328  111.804 1.00 24.40 ? 1067 GLU A N     1 
ATOM   7710  C CA    . GLU A  1 1069 ? 16.276  59.425  112.338 1.00 26.30 ? 1067 GLU A CA    1 
ATOM   7711  C C     . GLU A  1 1069 ? 14.931  60.129  112.509 1.00 27.97 ? 1067 GLU A C     1 
ATOM   7712  O O     . GLU A  1 1069 ? 13.882  59.559  112.187 1.00 26.62 ? 1067 GLU A O     1 
ATOM   7713  C CB    . GLU A  1 1069 ? 16.749  58.836  113.672 1.00 29.28 ? 1067 GLU A CB    1 
ATOM   7714  C CG    . GLU A  1 1069 ? 15.672  58.085  114.441 1.00 29.15 ? 1067 GLU A CG    1 
ATOM   7715  C CD    . GLU A  1 1069 ? 15.490  56.657  113.953 1.00 41.87 ? 1067 GLU A CD    1 
ATOM   7716  O OE1   . GLU A  1 1069 ? 16.223  56.236  113.023 1.00 46.54 ? 1067 GLU A OE1   1 
ATOM   7717  O OE2   . GLU A  1 1069 ? 14.606  55.957  114.502 1.00 47.93 ? 1067 GLU A OE2   1 
ATOM   7718  N N     . ALA A  1 1070 ? 14.938  61.367  113.015 1.00 24.52 ? 1068 ALA A N     1 
ATOM   7719  C CA    . ALA A  1 1070 ? 13.697  62.125  113.114 1.00 24.09 ? 1068 ALA A CA    1 
ATOM   7720  C C     . ALA A  1 1070 ? 13.085  62.329  111.739 1.00 23.37 ? 1068 ALA A C     1 
ATOM   7721  O O     . ALA A  1 1070 ? 11.860  62.298  111.583 1.00 24.89 ? 1068 ALA A O     1 
ATOM   7722  C CB    . ALA A  1 1070 ? 13.944  63.480  113.784 1.00 23.85 ? 1068 ALA A CB    1 
ATOM   7723  N N     . ALA A  1 1071 ? 13.932  62.542  110.732 1.00 23.39 ? 1069 ALA A N     1 
ATOM   7724  C CA    . ALA A  1 1071 ? 13.446  62.716  109.368 1.00 23.10 ? 1069 ALA A CA    1 
ATOM   7725  C C     . ALA A  1 1071 ? 12.798  61.434  108.855 1.00 22.94 ? 1069 ALA A C     1 
ATOM   7726  O O     . ALA A  1 1071 ? 11.704  61.464  108.273 1.00 22.64 ? 1069 ALA A O     1 
ATOM   7727  C CB    . ALA A  1 1071 ? 14.602  63.157  108.465 1.00 23.24 ? 1069 ALA A CB    1 
ATOM   7728  N N     . ARG A  1 1072 ? 13.456  60.290  109.058 1.00 23.92 ? 1070 ARG A N     1 
ATOM   7729  C CA    . ARG A  1 1072 ? 12.827  59.023  108.682 1.00 25.71 ? 1070 ARG A CA    1 
ATOM   7730  C C     . ARG A  1 1072 ? 11.505  58.830  109.419 1.00 23.90 ? 1070 ARG A C     1 
ATOM   7731  O O     . ARG A  1 1072 ? 10.515  58.397  108.823 1.00 23.29 ? 1070 ARG A O     1 
ATOM   7732  C CB    . ARG A  1 1072 ? 13.781  57.851  108.941 1.00 25.67 ? 1070 ARG A CB    1 
ATOM   7733  C CG    . ARG A  1 1072 ? 14.942  57.789  107.944 1.00 26.97 ? 1070 ARG A CG    1 
ATOM   7734  C CD    . ARG A  1 1072 ? 15.775  56.522  108.098 1.00 30.28 ? 1070 ARG A CD    1 
ATOM   7735  N NE    . ARG A  1 1072 ? 16.486  56.504  109.368 1.00 33.51 ? 1070 ARG A NE    1 
ATOM   7736  C CZ    . ARG A  1 1072 ? 17.714  56.964  109.546 1.00 32.48 ? 1070 ARG A CZ    1 
ATOM   7737  N NH1   . ARG A  1 1072 ? 18.418  57.468  108.541 1.00 34.42 ? 1070 ARG A NH1   1 
ATOM   7738  N NH2   . ARG A  1 1072 ? 18.254  56.914  110.760 1.00 31.62 ? 1070 ARG A NH2   1 
ATOM   7739  N N     . ASN A  1 1073 ? 11.457  59.185  110.706 1.00 23.86 ? 1071 ASN A N     1 
ATOM   7740  C CA    . ASN A  1 1073 ? 10.209  59.073  111.455 1.00 24.10 ? 1071 ASN A CA    1 
ATOM   7741  C C     . ASN A  1 1073 ? 9.132   59.996  110.887 1.00 25.98 ? 1071 ASN A C     1 
ATOM   7742  O O     . ASN A  1 1073 ? 7.960   59.616  110.806 1.00 27.52 ? 1071 ASN A O     1 
ATOM   7743  C CB    . ASN A  1 1073 ? 10.454  59.386  112.928 1.00 30.28 ? 1071 ASN A CB    1 
ATOM   7744  C CG    . ASN A  1 1073 ? 11.194  58.278  113.632 1.00 29.26 ? 1071 ASN A CG    1 
ATOM   7745  O OD1   . ASN A  1 1073 ? 11.287  57.158  113.120 1.00 36.39 ? 1071 ASN A OD1   1 
ATOM   7746  N ND2   . ASN A  1 1073 ? 11.720  58.573  114.813 1.00 33.15 ? 1071 ASN A ND2   1 
ATOM   7747  N N     . ALA A  1 1074 ? 9.509   61.220  110.504 1.00 22.77 ? 1072 ALA A N     1 
ATOM   7748  C CA    . ALA A  1 1074 ? 8.537   62.114  109.887 1.00 23.67 ? 1072 ALA A CA    1 
ATOM   7749  C C     . ALA A  1 1074 ? 8.028   61.535  108.578 1.00 23.16 ? 1072 ALA A C     1 
ATOM   7750  O O     . ALA A  1 1074 ? 6.829   61.620  108.281 1.00 24.67 ? 1072 ALA A O     1 
ATOM   7751  C CB    . ALA A  1 1074 ? 9.152   63.494  109.659 1.00 25.72 ? 1072 ALA A CB    1 
ATOM   7752  N N     . GLY A  1 1075 ? 8.923   60.950  107.775 1.00 24.69 ? 1073 GLY A N     1 
ATOM   7753  C CA    . GLY A  1 1075 ? 8.489   60.339  106.523 1.00 21.85 ? 1073 GLY A CA    1 
ATOM   7754  C C     . GLY A  1 1075 ? 7.456   59.249  106.735 1.00 24.80 ? 1073 GLY A C     1 
ATOM   7755  O O     . GLY A  1 1075 ? 6.500   59.118  105.961 1.00 23.82 ? 1073 GLY A O     1 
ATOM   7756  N N     . SER A  1 1076 ? 7.629   58.456  107.798 1.00 24.09 ? 1074 SER A N     1 
ATOM   7757  C CA    . SER A  1 1076 ? 6.674   57.400  108.118 1.00 24.83 ? 1074 SER A CA    1 
ATOM   7758  C C     . SER A  1 1076 ? 5.383   57.961  108.683 1.00 26.29 ? 1074 SER A C     1 
ATOM   7759  O O     . SER A  1 1076 ? 4.295   57.517  108.301 1.00 28.10 ? 1074 SER A O     1 
ATOM   7760  C CB    . SER A  1 1076 ? 7.281   56.408  109.115 1.00 25.56 ? 1074 SER A CB    1 
ATOM   7761  O OG    . SER A  1 1076 ? 8.210   55.576  108.463 1.00 31.61 ? 1074 SER A OG    1 
ATOM   7762  N N     . SER A  1 1077 ? 5.474   58.929  109.595 1.00 23.60 ? 1075 SER A N     1 
ATOM   7763  C CA    . SER A  1 1077 ? 4.265   59.453  110.223 1.00 25.54 ? 1075 SER A CA    1 
ATOM   7764  C C     . SER A  1 1077 ? 3.431   60.312  109.279 1.00 26.21 ? 1075 SER A C     1 
ATOM   7765  O O     . SER A  1 1077 ? 2.223   60.453  109.499 1.00 24.71 ? 1075 SER A O     1 
ATOM   7766  C CB    . SER A  1 1077 ? 4.617   60.268  111.465 1.00 24.86 ? 1075 SER A CB    1 
ATOM   7767  O OG    . SER A  1 1077 ? 5.296   59.450  112.404 1.00 31.31 ? 1075 SER A OG    1 
ATOM   7768  N N     . SER A  1 1078 ? 4.044   60.895  108.252 1.00 22.73 ? 1076 SER A N     1 
ATOM   7769  C CA    . SER A  1 1078 ? 3.286   61.705  107.305 1.00 20.97 ? 1076 SER A CA    1 
ATOM   7770  C C     . SER A  1 1078 ? 2.139   60.903  106.705 1.00 22.78 ? 1076 SER A C     1 
ATOM   7771  O O     . SER A  1 1078 ? 2.275   59.711  106.410 1.00 21.85 ? 1076 SER A O     1 
ATOM   7772  C CB    . SER A  1 1078 ? 4.200   62.210  106.192 1.00 24.54 ? 1076 SER A CB    1 
ATOM   7773  O OG    . SER A  1 1078 ? 3.428   62.903  105.208 1.00 20.70 ? 1076 SER A OG    1 
ATOM   7774  N N     . ALA A  1 1079 ? 0.996   61.563  106.525 1.00 20.52 ? 1077 ALA A N     1 
ATOM   7775  C CA    . ALA A  1 1079 ? -0.128  60.948  105.838 1.00 20.31 ? 1077 ALA A CA    1 
ATOM   7776  C C     . ALA A  1 1079 ? -0.266  61.454  104.408 1.00 20.68 ? 1077 ALA A C     1 
ATOM   7777  O O     . ALA A  1 1079 ? -1.297  61.213  103.766 1.00 19.90 ? 1077 ALA A O     1 
ATOM   7778  C CB    . ALA A  1 1079 ? -1.410  61.173  106.633 1.00 21.78 ? 1077 ALA A CB    1 
ATOM   7779  N N     . LEU A  1 1080 ? 0.764   62.126  103.891 1.00 20.75 ? 1078 LEU A N     1 
ATOM   7780  C CA    . LEU A  1 1080 ? 0.813   62.485  102.476 1.00 20.27 ? 1078 LEU A CA    1 
ATOM   7781  C C     . LEU A  1 1080 ? 0.586   61.252  101.616 1.00 21.76 ? 1078 LEU A C     1 
ATOM   7782  O O     . LEU A  1 1080 ? 1.225   60.218  101.811 1.00 20.82 ? 1078 LEU A O     1 
ATOM   7783  C CB    . LEU A  1 1080 ? 2.172   63.109  102.139 1.00 22.44 ? 1078 LEU A CB    1 
ATOM   7784  C CG    . LEU A  1 1080 ? 2.433   63.372  100.647 1.00 26.10 ? 1078 LEU A CG    1 
ATOM   7785  C CD1   . LEU A  1 1080 ? 1.564   64.508  100.123 1.00 21.85 ? 1078 LEU A CD1   1 
ATOM   7786  C CD2   . LEU A  1 1080 ? 3.909   63.647  100.370 1.00 20.91 ? 1078 LEU A CD2   1 
ATOM   7787  N N     . GLY A  1 1081 ? -0.320  61.369  100.648 1.00 19.80 ? 1079 GLY A N     1 
ATOM   7788  C CA    . GLY A  1 1081 ? -0.651  60.245  99.800  1.00 23.38 ? 1079 GLY A CA    1 
ATOM   7789  C C     . GLY A  1 1081 ? -1.884  59.477  100.222 1.00 22.58 ? 1079 GLY A C     1 
ATOM   7790  O O     . GLY A  1 1081 ? -2.311  58.572  99.484  1.00 19.59 ? 1079 GLY A O     1 
ATOM   7791  N N     . LEU A  1 1082 ? -2.456  59.787  101.390 1.00 19.61 ? 1080 LEU A N     1 
ATOM   7792  C CA    A LEU A  1 1082 ? -3.725  59.184  101.776 0.49 19.65 ? 1080 LEU A CA    1 
ATOM   7793  C CA    B LEU A  1 1082 ? -3.726  59.183  101.776 0.51 19.65 ? 1080 LEU A CA    1 
ATOM   7794  C C     . LEU A  1 1082 ? -4.736  59.367  100.653 1.00 20.35 ? 1080 LEU A C     1 
ATOM   7795  O O     . LEU A  1 1082 ? -4.830  60.441  100.061 1.00 21.10 ? 1080 LEU A O     1 
ATOM   7796  C CB    A LEU A  1 1082 ? -4.242  59.814  103.073 0.49 19.53 ? 1080 LEU A CB    1 
ATOM   7797  C CB    B LEU A  1 1082 ? -4.253  59.805  103.076 0.51 19.53 ? 1080 LEU A CB    1 
ATOM   7798  C CG    A LEU A  1 1082 ? -5.583  59.331  103.626 0.49 19.88 ? 1080 LEU A CG    1 
ATOM   7799  C CG    B LEU A  1 1082 ? -5.625  59.359  103.602 0.51 19.87 ? 1080 LEU A CG    1 
ATOM   7800  C CD1   A LEU A  1 1082 ? -5.541  57.842  103.915 0.49 21.36 ? 1080 LEU A CD1   1 
ATOM   7801  C CD1   B LEU A  1 1082 ? -5.671  59.485  105.121 0.51 19.63 ? 1080 LEU A CD1   1 
ATOM   7802  C CD2   A LEU A  1 1082 ? -5.930  60.110  104.897 0.49 19.53 ? 1080 LEU A CD2   1 
ATOM   7803  C CD2   B LEU A  1 1082 ? -6.760  60.171  103.003 0.51 19.22 ? 1080 LEU A CD2   1 
ATOM   7804  N N     . ASP A  1 1083 ? -5.476  58.301  100.352 1.00 19.31 ? 1081 ASP A N     1 
ATOM   7805  C CA    . ASP A  1 1083 ? -6.417  58.332  99.223  1.00 20.02 ? 1081 ASP A CA    1 
ATOM   7806  C C     . ASP A  1 1083 ? -7.620  57.457  99.580  1.00 25.15 ? 1081 ASP A C     1 
ATOM   7807  O O     . ASP A  1 1083 ? -7.564  56.235  99.428  1.00 25.90 ? 1081 ASP A O     1 
ATOM   7808  C CB    . ASP A  1 1083 ? -5.709  57.847  97.964  1.00 24.55 ? 1081 ASP A CB    1 
ATOM   7809  C CG    . ASP A  1 1083 ? -6.524  58.061  96.699  1.00 29.31 ? 1081 ASP A CG    1 
ATOM   7810  O OD1   . ASP A  1 1083 ? -7.609  58.670  96.766  1.00 31.01 ? 1081 ASP A OD1   1 
ATOM   7811  O OD2   . ASP A  1 1083 ? -6.052  57.620  95.628  1.00 38.60 ? 1081 ASP A OD2   1 
ATOM   7812  N N     . LEU A  1 1084 ? -8.701  58.080  100.043 1.00 21.36 ? 1082 LEU A N     1 
ATOM   7813  C CA    . LEU A  1 1084 ? -9.845  57.351  100.576 1.00 19.53 ? 1082 LEU A CA    1 
ATOM   7814  C C     . LEU A  1 1084 ? -11.094 57.621  99.758  1.00 20.55 ? 1082 LEU A C     1 
ATOM   7815  O O     . LEU A  1 1084 ? -11.295 58.729  99.255  1.00 20.08 ? 1082 LEU A O     1 
ATOM   7816  C CB    . LEU A  1 1084 ? -10.156 57.747  102.016 1.00 22.99 ? 1082 LEU A CB    1 
ATOM   7817  C CG    . LEU A  1 1084 ? -9.050  57.384  102.992 1.00 23.54 ? 1082 LEU A CG    1 
ATOM   7818  C CD1   . LEU A  1 1084 ? -9.520  57.787  104.370 1.00 24.26 ? 1082 LEU A CD1   1 
ATOM   7819  C CD2   . LEU A  1 1084 ? -8.726  55.885  102.899 1.00 26.34 ? 1082 LEU A CD2   1 
ATOM   7820  N N     . GLU A  1 1085 ? -11.942 56.610  99.651  1.00 22.04 ? 1083 GLU A N     1 
ATOM   7821  C CA    . GLU A  1 1085 ? -13.299 56.815  99.158  1.00 23.41 ? 1083 GLU A CA    1 
ATOM   7822  C C     . GLU A  1 1085 ? -14.235 56.827  100.360 1.00 24.85 ? 1083 GLU A C     1 
ATOM   7823  O O     . GLU A  1 1085 ? -14.187 55.920  101.197 1.00 27.18 ? 1083 GLU A O     1 
ATOM   7824  C CB    . GLU A  1 1085 ? -13.710 55.744  98.148  1.00 26.06 ? 1083 GLU A CB    1 
ATOM   7825  C CG    . GLU A  1 1085 ? -15.147 55.936  97.710  1.00 29.39 ? 1083 GLU A CG    1 
ATOM   7826  C CD    . GLU A  1 1085 ? -15.499 55.212  96.440  1.00 31.13 ? 1083 GLU A CD    1 
ATOM   7827  O OE1   . GLU A  1 1085 ? -14.606 54.585  95.831  1.00 37.09 ? 1083 GLU A OE1   1 
ATOM   7828  O OE2   . GLU A  1 1085 ? -16.684 55.286  96.046  1.00 36.96 ? 1083 GLU A OE2   1 
ATOM   7829  N N     . LEU A  1 1086 ? -15.025 57.887  100.484 1.00 21.03 ? 1084 LEU A N     1 
ATOM   7830  C CA    . LEU A  1 1086 ? -15.962 58.099  101.574 1.00 21.73 ? 1084 LEU A CA    1 
ATOM   7831  C C     . LEU A  1 1086 ? -17.338 57.561  101.198 1.00 26.87 ? 1084 LEU A C     1 
ATOM   7832  O O     . LEU A  1 1086 ? -17.790 57.759  100.062 1.00 24.08 ? 1084 LEU A O     1 
ATOM   7833  C CB    . LEU A  1 1086 ? -16.070 59.586  101.919 1.00 21.03 ? 1084 LEU A CB    1 
ATOM   7834  C CG    . LEU A  1 1086 ? -14.727 60.242  102.261 1.00 22.93 ? 1084 LEU A CG    1 
ATOM   7835  C CD1   . LEU A  1 1086 ? -14.875 61.703  102.701 1.00 22.06 ? 1084 LEU A CD1   1 
ATOM   7836  C CD2   . LEU A  1 1086 ? -14.010 59.430  103.341 1.00 25.76 ? 1084 LEU A CD2   1 
ATOM   7837  N N     . PRO A  1 1087 ? -17.992 56.861  102.127 1.00 24.89 ? 1085 PRO A N     1 
ATOM   7838  C CA    . PRO A  1 1087 ? -19.354 56.372  101.861 1.00 24.15 ? 1085 PRO A CA    1 
ATOM   7839  C C     . PRO A  1 1087 ? -20.329 57.516  101.633 1.00 28.22 ? 1085 PRO A C     1 
ATOM   7840  O O     . PRO A  1 1087 ? -20.298 58.537  102.319 1.00 27.35 ? 1085 PRO A O     1 
ATOM   7841  C CB    . PRO A  1 1087 ? -19.710 55.568  103.119 1.00 30.64 ? 1085 PRO A CB    1 
ATOM   7842  C CG    . PRO A  1 1087 ? -18.661 55.927  104.152 1.00 33.20 ? 1085 PRO A CG    1 
ATOM   7843  C CD    . PRO A  1 1087 ? -17.436 56.340  103.391 1.00 27.21 ? 1085 PRO A CD    1 
ATOM   7844  N N     . GLY A  1 1088 ? -21.198 57.325  100.647 1.00 25.06 ? 1086 GLY A N     1 
ATOM   7845  C CA    . GLY A  1 1088 ? -22.216 58.280  100.287 1.00 25.43 ? 1086 GLY A CA    1 
ATOM   7846  C C     . GLY A  1 1088 ? -23.295 57.588  99.482  1.00 22.14 ? 1086 GLY A C     1 
ATOM   7847  O O     . GLY A  1 1088 ? -23.456 56.368  99.550  1.00 21.72 ? 1086 GLY A O     1 
ATOM   7848  N N     . PRO A  1 1089 ? -24.036 58.347  98.681  1.00 23.79 ? 1087 PRO A N     1 
ATOM   7849  C CA    . PRO A  1 1089 ? -25.113 57.749  97.889  1.00 22.39 ? 1087 PRO A CA    1 
ATOM   7850  C C     . PRO A  1 1089 ? -24.579 56.964  96.699  1.00 24.72 ? 1087 PRO A C     1 
ATOM   7851  O O     . PRO A  1 1089 ? -23.449 57.155  96.236  1.00 24.83 ? 1087 PRO A O     1 
ATOM   7852  C CB    . PRO A  1 1089 ? -25.909 58.965  97.412  1.00 23.26 ? 1087 PRO A CB    1 
ATOM   7853  C CG    . PRO A  1 1089 ? -24.848 60.025  97.264  1.00 23.91 ? 1087 PRO A CG    1 
ATOM   7854  C CD    . PRO A  1 1089 ? -23.879 59.787  98.411  1.00 26.17 ? 1087 PRO A CD    1 
ATOM   7855  N N     . VAL A  1 1090 ? -25.440 56.088  96.178  1.00 22.41 ? 1088 VAL A N     1 
ATOM   7856  C CA    . VAL A  1 1090 ? -25.161 55.476  94.884  1.00 22.09 ? 1088 VAL A CA    1 
ATOM   7857  C C     . VAL A  1 1090 ? -25.068 56.570  93.820  1.00 20.64 ? 1088 VAL A C     1 
ATOM   7858  O O     . VAL A  1 1090 ? -25.588 57.682  93.981  1.00 18.79 ? 1088 VAL A O     1 
ATOM   7859  C CB    . VAL A  1 1090 ? -26.236 54.445  94.501  1.00 25.49 ? 1088 VAL A CB    1 
ATOM   7860  C CG1   . VAL A  1 1090 ? -26.356 53.356  95.556  1.00 22.76 ? 1088 VAL A CG1   1 
ATOM   7861  C CG2   . VAL A  1 1090 ? -27.584 55.135  94.258  1.00 22.27 ? 1088 VAL A CG2   1 
ATOM   7862  N N     . GLY A  1 1091 ? -24.402 56.240  92.715  1.00 20.14 ? 1089 GLY A N     1 
ATOM   7863  C CA    . GLY A  1 1091 ? -24.303 57.169  91.603  1.00 21.88 ? 1089 GLY A CA    1 
ATOM   7864  C C     . GLY A  1 1091 ? -23.386 58.337  91.854  1.00 20.97 ? 1089 GLY A C     1 
ATOM   7865  O O     . GLY A  1 1091 ? -23.452 59.348  91.143  1.00 22.55 ? 1089 GLY A O     1 
ATOM   7866  N N     . GLU A  1 1092 ? -22.509 58.221  92.847  1.00 19.82 ? 1090 GLU A N     1 
ATOM   7867  C CA    . GLU A  1 1092 ? -21.548 59.262  93.151  1.00 22.38 ? 1090 GLU A CA    1 
ATOM   7868  C C     . GLU A  1 1092 ? -20.318 58.588  93.743  1.00 20.59 ? 1090 GLU A C     1 
ATOM   7869  O O     . GLU A  1 1092 ? -20.456 57.597  94.459  1.00 22.96 ? 1090 GLU A O     1 
ATOM   7870  C CB    . GLU A  1 1092 ? -22.157 60.265  94.145  1.00 19.78 ? 1090 GLU A CB    1 
ATOM   7871  C CG    . GLU A  1 1092 ? -21.476 61.602  94.185  1.00 23.20 ? 1090 GLU A CG    1 
ATOM   7872  C CD    . GLU A  1 1092 ? -22.199 62.561  95.105  1.00 23.86 ? 1090 GLU A CD    1 
ATOM   7873  O OE1   . GLU A  1 1092 ? -22.134 62.365  96.339  1.00 23.55 ? 1090 GLU A OE1   1 
ATOM   7874  O OE2   . GLU A  1 1092 ? -22.852 63.495  94.582  1.00 30.88 ? 1090 GLU A OE2   1 
ATOM   7875  N N     . ARG A  1 1093 ? -19.128 59.106  93.424  1.00 18.99 ? 1091 ARG A N     1 
ATOM   7876  C CA    . ARG A  1 1093 ? -17.882 58.702  94.085  1.00 21.24 ? 1091 ARG A CA    1 
ATOM   7877  C C     . ARG A  1 1093 ? -17.316 59.903  94.824  1.00 19.08 ? 1091 ARG A C     1 
ATOM   7878  O O     . ARG A  1 1093 ? -17.080 60.955  94.225  1.00 18.54 ? 1091 ARG A O     1 
ATOM   7879  C CB    . ARG A  1 1093 ? -16.848 58.166  93.090  1.00 27.57 ? 1091 ARG A CB    1 
ATOM   7880  C CG    . ARG A  1 1093 ? -17.108 56.735  92.631  1.00 38.15 ? 1091 ARG A CG    1 
ATOM   7881  C CD    . ARG A  1 1093 ? -15.805 56.047  92.205  1.00 44.79 ? 1091 ARG A CD    1 
ATOM   7882  N NE    . ARG A  1 1093 ? -15.188 56.712  91.061  1.00 52.19 ? 1091 ARG A NE    1 
ATOM   7883  C CZ    . ARG A  1 1093 ? -15.470 56.437  89.793  1.00 50.42 ? 1091 ARG A CZ    1 
ATOM   7884  N NH1   . ARG A  1 1093 ? -16.351 55.504  89.467  1.00 52.60 ? 1091 ARG A NH1   1 
ATOM   7885  N NH2   . ARG A  1 1093 ? -14.846 57.108  88.827  1.00 44.17 ? 1091 ARG A NH2   1 
ATOM   7886  N N     . ASN A  1 1094 ? -17.080 59.740  96.119  1.00 20.22 ? 1092 ASN A N     1 
ATOM   7887  C CA    . ASN A  1 1094 ? -16.589 60.819  96.955  1.00 19.51 ? 1092 ASN A CA    1 
ATOM   7888  C C     . ASN A  1 1094 ? -15.218 60.439  97.486  1.00 18.32 ? 1092 ASN A C     1 
ATOM   7889  O O     . ASN A  1 1094 ? -15.085 59.449  98.213  1.00 22.23 ? 1092 ASN A O     1 
ATOM   7890  C CB    . ASN A  1 1094 ? -17.584 61.098  98.075  1.00 17.85 ? 1092 ASN A CB    1 
ATOM   7891  C CG    . ASN A  1 1094 ? -18.861 61.680  97.516  1.00 20.21 ? 1092 ASN A CG    1 
ATOM   7892  O OD1   . ASN A  1 1094 ? -18.866 62.828  97.074  1.00 22.29 ? 1092 ASN A OD1   1 
ATOM   7893  N ND2   . ASN A  1 1094 ? -19.918 60.880  97.464  1.00 19.86 ? 1092 ASN A ND2   1 
ATOM   7894  N N     . LEU A  1 1095 ? -14.209 61.214  97.101  1.00 19.10 ? 1093 LEU A N     1 
ATOM   7895  C CA    . LEU A  1 1095 ? -12.811 60.899  97.363  1.00 19.67 ? 1093 LEU A CA    1 
ATOM   7896  C C     . LEU A  1 1095 ? -12.195 61.961  98.254  1.00 20.62 ? 1093 LEU A C     1 
ATOM   7897  O O     . LEU A  1 1095 ? -12.513 63.150  98.154  1.00 19.43 ? 1093 LEU A O     1 
ATOM   7898  C CB    . LEU A  1 1095 ? -12.018 60.800  96.061  1.00 18.90 ? 1093 LEU A CB    1 
ATOM   7899  C CG    . LEU A  1 1095 ? -12.686 59.872  95.037  1.00 26.83 ? 1093 LEU A CG    1 
ATOM   7900  C CD1   . LEU A  1 1095 ? -12.064 60.054  93.653  1.00 28.36 ? 1093 LEU A CD1   1 
ATOM   7901  C CD2   . LEU A  1 1095 ? -12.580 58.435  95.495  1.00 27.16 ? 1093 LEU A CD2   1 
ATOM   7902  N N     . TYR A  1 1096 ? -11.284 61.516  99.117  1.00 18.34 ? 1094 TYR A N     1 
ATOM   7903  C CA    . TYR A  1 1096 ? -10.654 62.385  100.103 1.00 20.23 ? 1094 TYR A CA    1 
ATOM   7904  C C     . TYR A  1 1096 ? -9.174  62.043  100.076 1.00 20.41 ? 1094 TYR A C     1 
ATOM   7905  O O     . TYR A  1 1096 ? -8.812  60.871  100.228 1.00 18.98 ? 1094 TYR A O     1 
ATOM   7906  C CB    . TYR A  1 1096 ? -11.267 62.152  101.490 1.00 18.52 ? 1094 TYR A CB    1 
ATOM   7907  C CG    . TYR A  1 1096 ? -10.583 62.863  102.637 1.00 18.96 ? 1094 TYR A CG    1 
ATOM   7908  C CD1   . TYR A  1 1096 ? -10.954 64.151  102.999 1.00 18.64 ? 1094 TYR A CD1   1 
ATOM   7909  C CD2   . TYR A  1 1096 ? -9.591  62.228  103.373 1.00 21.11 ? 1094 TYR A CD2   1 
ATOM   7910  C CE1   . TYR A  1 1096 ? -10.330 64.805  104.055 1.00 20.36 ? 1094 TYR A CE1   1 
ATOM   7911  C CE2   . TYR A  1 1096 ? -8.957  62.874  104.433 1.00 19.35 ? 1094 TYR A CE2   1 
ATOM   7912  C CZ    . TYR A  1 1096 ? -9.347  64.156  104.773 1.00 19.00 ? 1094 TYR A CZ    1 
ATOM   7913  O OH    . TYR A  1 1096 ? -8.743  64.811  105.830 1.00 19.18 ? 1094 TYR A OH    1 
ATOM   7914  N N     . THR A  1 1097 ? -8.334  63.039  99.816  1.00 18.62 ? 1095 THR A N     1 
ATOM   7915  C CA    . THR A  1 1097 ? -6.912  62.813  99.572  1.00 21.39 ? 1095 THR A CA    1 
ATOM   7916  C C     . THR A  1 1097 ? -6.090  63.884  100.266 1.00 18.88 ? 1095 THR A C     1 
ATOM   7917  O O     . THR A  1 1097 ? -6.541  65.020  100.422 1.00 18.98 ? 1095 THR A O     1 
ATOM   7918  C CB    . THR A  1 1097 ? -6.568  62.821  98.082  1.00 21.43 ? 1095 THR A CB    1 
ATOM   7919  O OG1   . THR A  1 1097 ? -7.037  64.043  97.497  1.00 26.14 ? 1095 THR A OG1   1 
ATOM   7920  C CG2   . THR A  1 1097 ? -7.246  61.666  97.380  1.00 25.68 ? 1095 THR A CG2   1 
ATOM   7921  N N     . LEU A  1 1098 ? -4.869  63.521  100.667 1.00 19.22 ? 1096 LEU A N     1 
ATOM   7922  C CA    . LEU A  1 1098 ? -3.951  64.447  101.328 1.00 19.22 ? 1096 LEU A CA    1 
ATOM   7923  C C     . LEU A  1 1098 ? -2.764  64.710  100.410 1.00 19.31 ? 1096 LEU A C     1 
ATOM   7924  O O     . LEU A  1 1098 ? -2.078  63.777  99.985  1.00 19.39 ? 1096 LEU A O     1 
ATOM   7925  C CB    . LEU A  1 1098 ? -3.480  63.907  102.688 1.00 19.41 ? 1096 LEU A CB    1 
ATOM   7926  C CG    . LEU A  1 1098 ? -4.561  63.676  103.758 1.00 19.39 ? 1096 LEU A CG    1 
ATOM   7927  C CD1   . LEU A  1 1098 ? -3.940  63.133  105.086 1.00 19.63 ? 1096 LEU A CD1   1 
ATOM   7928  C CD2   . LEU A  1 1098 ? -5.409  64.930  104.034 1.00 19.30 ? 1096 LEU A CD2   1 
ATOM   7929  N N     . HIS A  1 1099 ? -2.551  65.975  100.084 1.00 19.31 ? 1097 HIS A N     1 
ATOM   7930  C CA    . HIS A  1 1099 ? -1.504  66.415  99.181  1.00 19.42 ? 1097 HIS A CA    1 
ATOM   7931  C C     . HIS A  1 1099 ? -0.541  67.332  99.920  1.00 19.62 ? 1097 HIS A C     1 
ATOM   7932  O O     . HIS A  1 1099 ? -0.802  67.767  101.043 1.00 22.32 ? 1097 HIS A O     1 
ATOM   7933  C CB    . HIS A  1 1099 ? -2.104  67.174  97.992  1.00 21.60 ? 1097 HIS A CB    1 
ATOM   7934  C CG    . HIS A  1 1099 ? -3.063  66.370  97.175  1.00 24.83 ? 1097 HIS A CG    1 
ATOM   7935  N ND1   . HIS A  1 1099 ? -2.709  65.786  95.979  1.00 26.04 ? 1097 HIS A ND1   1 
ATOM   7936  C CD2   . HIS A  1 1099 ? -4.368  66.064  97.374  1.00 23.26 ? 1097 HIS A CD2   1 
ATOM   7937  C CE1   . HIS A  1 1099 ? -3.751  65.144  95.479  1.00 25.96 ? 1097 HIS A CE1   1 
ATOM   7938  N NE2   . HIS A  1 1099 ? -4.769  65.293  96.308  1.00 24.69 ? 1097 HIS A NE2   1 
ATOM   7939  N N     . ALA A  1 1100 ? 0.571   67.652  99.267  1.00 19.78 ? 1098 ALA A N     1 
ATOM   7940  C CA    . ALA A  1 1100 ? 1.431   68.717  99.779  1.00 22.45 ? 1098 ALA A CA    1 
ATOM   7941  C C     . ALA A  1 1100 ? 0.657   70.032  99.816  1.00 26.18 ? 1098 ALA A C     1 
ATOM   7942  O O     . ALA A  1 1100 ? -0.253  70.261  99.021  1.00 22.57 ? 1098 ALA A O     1 
ATOM   7943  C CB    . ALA A  1 1100 ? 2.685   68.862  98.909  1.00 21.04 ? 1098 ALA A CB    1 
ATOM   7944  N N     . ARG A  1 1101 ? 1.006   70.894  100.769 1.00 22.23 ? 1099 ARG A N     1 
ATOM   7945  C CA    . ARG A  1 1101 ? 0.366   72.202  100.845 1.00 23.55 ? 1099 ARG A CA    1 
ATOM   7946  C C     . ARG A  1 1101 ? 0.943   73.179  99.830  1.00 23.99 ? 1099 ARG A C     1 
ATOM   7947  O O     . ARG A  1 1101 ? 0.201   73.981  99.257  1.00 23.79 ? 1099 ARG A O     1 
ATOM   7948  C CB    . ARG A  1 1101 ? 0.509   72.780  102.252 1.00 22.97 ? 1099 ARG A CB    1 
ATOM   7949  C CG    . ARG A  1 1101 ? -0.620  72.424  103.162 1.00 25.44 ? 1099 ARG A CG    1 
ATOM   7950  C CD    . ARG A  1 1101 ? -0.402  72.973  104.533 1.00 30.62 ? 1099 ARG A CD    1 
ATOM   7951  N NE    . ARG A  1 1101 ? -1.226  74.141  104.817 1.00 32.25 ? 1099 ARG A NE    1 
ATOM   7952  C CZ    . ARG A  1 1101 ? -2.410  74.101  105.420 1.00 37.64 ? 1099 ARG A CZ    1 
ATOM   7953  N NH1   . ARG A  1 1101 ? -2.993  72.950  105.726 1.00 31.39 ? 1099 ARG A NH1   1 
ATOM   7954  N NH2   . ARG A  1 1101 ? -3.018  75.244  105.735 1.00 31.64 ? 1099 ARG A NH2   1 
ATOM   7955  N N     . GLY A  1 1102 ? 2.251   73.130  99.598  1.00 20.43 ? 1100 GLY A N     1 
ATOM   7956  C CA    . GLY A  1 1102 ? 2.906   74.088  98.723  1.00 21.01 ? 1100 GLY A CA    1 
ATOM   7957  C C     . GLY A  1 1102 ? 4.282   74.439  99.240  1.00 26.91 ? 1100 GLY A C     1 
ATOM   7958  O O     . GLY A  1 1102 ? 5.095   73.543  99.476  1.00 22.36 ? 1100 GLY A O     1 
ATOM   7959  N N     . ARG A  1 1103 ? 4.566   75.726  99.432  1.00 21.14 ? 1101 ARG A N     1 
ATOM   7960  C CA    . ARG A  1 1103 ? 5.866   76.156  99.932  1.00 23.05 ? 1101 ARG A CA    1 
ATOM   7961  C C     . ARG A  1 1103 ? 5.679   76.650  101.353 1.00 21.57 ? 1101 ARG A C     1 
ATOM   7962  O O     . ARG A  1 1103 ? 4.897   77.576  101.587 1.00 22.11 ? 1101 ARG A O     1 
ATOM   7963  C CB    . ARG A  1 1103 ? 6.487   77.250  99.059  1.00 29.18 ? 1101 ARG A CB    1 
ATOM   7964  C CG    . ARG A  1 1103 ? 7.939   77.579  99.473  1.00 27.33 ? 1101 ARG A CG    1 
ATOM   7965  C CD    . ARG A  1 1103 ? 8.623   78.514  98.481  1.00 27.60 ? 1101 ARG A CD    1 
ATOM   7966  N NE    . ARG A  1 1103 ? 8.681   77.949  97.137  1.00 35.10 ? 1101 ARG A NE    1 
ATOM   7967  C CZ    . ARG A  1 1103 ? 9.694   77.241  96.645  1.00 36.84 ? 1101 ARG A CZ    1 
ATOM   7968  N NH1   . ARG A  1 1103 ? 10.779  76.965  97.369  1.00 32.68 ? 1101 ARG A NH1   1 
ATOM   7969  N NH2   . ARG A  1 1103 ? 9.626   76.805  95.387  1.00 39.31 ? 1101 ARG A NH2   1 
ATOM   7970  N N     . ILE A  1 1104 ? 6.392   76.028  102.295 1.00 22.44 ? 1102 ILE A N     1 
ATOM   7971  C CA    . ILE A  1 1104 ? 6.302   76.357  103.717 1.00 24.25 ? 1102 ILE A CA    1 
ATOM   7972  C C     . ILE A  1 1104 ? 7.423   77.331  104.066 1.00 22.19 ? 1102 ILE A C     1 
ATOM   7973  O O     . ILE A  1 1104 ? 8.588   77.109  103.710 1.00 22.37 ? 1102 ILE A O     1 
ATOM   7974  C CB    . ILE A  1 1104 ? 6.395   75.096  104.600 1.00 21.73 ? 1102 ILE A CB    1 
ATOM   7975  C CG1   . ILE A  1 1104 ? 5.424   74.005  104.136 1.00 21.38 ? 1102 ILE A CG1   1 
ATOM   7976  C CG2   . ILE A  1 1104 ? 6.156   75.461  106.066 1.00 22.23 ? 1102 ILE A CG2   1 
ATOM   7977  C CD1   . ILE A  1 1104 ? 3.948   74.388  104.216 1.00 21.16 ? 1102 ILE A CD1   1 
ATOM   7978  N N     . LEU A  1 1105 ? 7.062   78.424  104.736 1.00 22.34 ? 1103 LEU A N     1 
ATOM   7979  C CA    . LEU A  1 1105 ? 8.041   79.374  105.246 1.00 22.74 ? 1103 LEU A CA    1 
ATOM   7980  C C     . LEU A  1 1105 ? 8.676   78.767  106.483 1.00 22.88 ? 1103 LEU A C     1 
ATOM   7981  O O     . LEU A  1 1105 ? 7.965   78.405  107.430 1.00 22.78 ? 1103 LEU A O     1 
ATOM   7982  C CB    . LEU A  1 1105 ? 7.366   80.707  105.571 1.00 22.87 ? 1103 LEU A CB    1 
ATOM   7983  C CG    . LEU A  1 1105 ? 8.212   81.763  106.280 1.00 23.32 ? 1103 LEU A CG    1 
ATOM   7984  C CD1   . LEU A  1 1105 ? 9.380   82.227  105.379 1.00 23.58 ? 1103 LEU A CD1   1 
ATOM   7985  C CD2   . LEU A  1 1105 ? 7.318   82.909  106.651 1.00 23.41 ? 1103 LEU A CD2   1 
ATOM   7986  N N     . LEU A  1 1106 ? 9.996   78.618  106.465 1.00 23.13 ? 1104 LEU A N     1 
ATOM   7987  C CA    . LEU A  1 1106 ? 10.733  78.117  107.616 1.00 23.33 ? 1104 LEU A CA    1 
ATOM   7988  C C     . LEU A  1 1106 ? 11.430  79.281  108.296 1.00 23.74 ? 1104 LEU A C     1 
ATOM   7989  O O     . LEU A  1 1106 ? 12.125  80.064  107.644 1.00 25.36 ? 1104 LEU A O     1 
ATOM   7990  C CB    . LEU A  1 1106 ? 11.762  77.054  107.232 1.00 23.35 ? 1104 LEU A CB    1 
ATOM   7991  C CG    . LEU A  1 1106 ? 11.238  75.792  106.547 1.00 23.23 ? 1104 LEU A CG    1 
ATOM   7992  C CD1   . LEU A  1 1106 ? 12.302  74.693  106.621 1.00 23.10 ? 1104 LEU A CD1   1 
ATOM   7993  C CD2   . LEU A  1 1106 ? 9.940   75.335  107.171 1.00 22.72 ? 1104 LEU A CD2   1 
ATOM   7994  N N     . VAL A  1 1107 ? 11.247  79.390  109.604 1.00 24.58 ? 1105 VAL A N     1 
ATOM   7995  C CA    . VAL A  1 1107 ? 11.927  80.437  110.352 1.00 24.30 ? 1105 VAL A CA    1 
ATOM   7996  C C     . VAL A  1 1107 ? 12.707  79.748  111.464 1.00 24.50 ? 1105 VAL A C     1 
ATOM   7997  O O     . VAL A  1 1107 ? 12.250  79.709  112.611 1.00 25.18 ? 1105 VAL A O     1 
ATOM   7998  C CB    . VAL A  1 1107 ? 10.937  81.489  110.877 1.00 24.36 ? 1105 VAL A CB    1 
ATOM   7999  C CG1   . VAL A  1 1107 ? 11.690  82.660  111.489 1.00 24.85 ? 1105 VAL A CG1   1 
ATOM   8000  C CG2   . VAL A  1 1107 ? 10.052  81.982  109.729 1.00 24.12 ? 1105 VAL A CG2   1 
ATOM   8001  N N     . PRO A  1 1108 ? 13.868  79.181  111.166 1.00 24.82 ? 1106 PRO A N     1 
ATOM   8002  C CA    . PRO A  1 1108 ? 14.631  78.464  112.190 1.00 24.82 ? 1106 PRO A CA    1 
ATOM   8003  C C     . PRO A  1 1108 ? 15.465  79.408  113.043 1.00 27.33 ? 1106 PRO A C     1 
ATOM   8004  O O     . PRO A  1 1108 ? 15.724  80.557  112.685 1.00 27.12 ? 1106 PRO A O     1 
ATOM   8005  C CB    . PRO A  1 1108 ? 15.539  77.548  111.359 1.00 26.43 ? 1106 PRO A CB    1 
ATOM   8006  C CG    . PRO A  1 1108 ? 15.862  78.412  110.160 1.00 24.83 ? 1106 PRO A CG    1 
ATOM   8007  C CD    . PRO A  1 1108 ? 14.548  79.151  109.856 1.00 25.68 ? 1106 PRO A CD    1 
ATOM   8008  N N     . ALA A  1 1109 ? 15.891  78.884  114.185 1.00 25.48 ? 1107 ALA A N     1 
ATOM   8009  C CA    . ALA A  1 1109 ? 16.848  79.556  115.059 1.00 26.21 ? 1107 ALA A CA    1 
ATOM   8010  C C     . ALA A  1 1109 ? 18.180  78.826  115.157 1.00 27.54 ? 1107 ALA A C     1 
ATOM   8011  O O     . ALA A  1 1109 ? 19.224  79.468  115.274 1.00 29.97 ? 1107 ALA A O     1 
ATOM   8012  C CB    . ALA A  1 1109 ? 16.257  79.720  116.468 1.00 26.10 ? 1107 ALA A CB    1 
ATOM   8013  N N     . THR A  1 1110 ? 18.174  77.494  115.120 1.00 25.96 ? 1108 THR A N     1 
ATOM   8014  C CA    . THR A  1 1110 ? 19.373  76.686  115.276 1.00 26.16 ? 1108 THR A CA    1 
ATOM   8015  C C     . THR A  1 1110 ? 19.470  75.731  114.096 1.00 27.06 ? 1108 THR A C     1 
ATOM   8016  O O     . THR A  1 1110 ? 18.488  75.486  113.398 1.00 25.48 ? 1108 THR A O     1 
ATOM   8017  C CB    . THR A  1 1110 ? 19.347  75.872  116.568 1.00 27.22 ? 1108 THR A CB    1 
ATOM   8018  O OG1   . THR A  1 1110 ? 18.268  74.933  116.497 1.00 25.94 ? 1108 THR A OG1   1 
ATOM   8019  C CG2   . THR A  1 1110 ? 19.167  76.778  117.807 1.00 28.06 ? 1108 THR A CG2   1 
ATOM   8020  N N     . GLU A  1 1111 ? 20.658  75.161  113.898 1.00 27.86 ? 1109 GLU A N     1 
ATOM   8021  C CA    . GLU A  1 1111 ? 20.841  74.222  112.791 1.00 28.93 ? 1109 GLU A CA    1 
ATOM   8022  C C     . GLU A  1 1111 ? 19.955  72.987  112.953 1.00 26.07 ? 1109 GLU A C     1 
ATOM   8023  O O     . GLU A  1 1111 ? 19.281  72.559  112.004 1.00 26.33 ? 1109 GLU A O     1 
ATOM   8024  C CB    . GLU A  1 1111 ? 22.312  73.827  112.684 1.00 33.56 ? 1109 GLU A CB    1 
ATOM   8025  C CG    . GLU A  1 1111 ? 22.558  72.617  111.800 1.00 31.68 ? 1109 GLU A CG    1 
ATOM   8026  C CD    . GLU A  1 1111 ? 24.043  72.336  111.622 1.00 35.78 ? 1109 GLU A CD    1 
ATOM   8027  O OE1   . GLU A  1 1111 ? 24.699  73.089  110.873 1.00 35.89 ? 1109 GLU A OE1   1 
ATOM   8028  O OE2   . GLU A  1 1111 ? 24.551  71.380  112.243 1.00 33.03 ? 1109 GLU A OE2   1 
ATOM   8029  N N     . SER A  1 1112 ? 19.952  72.394  114.149 1.00 27.69 ? 1110 SER A N     1 
ATOM   8030  C CA    . SER A  1 1112 ? 19.098  71.239  114.396 1.00 29.81 ? 1110 SER A CA    1 
ATOM   8031  C C     . SER A  1 1112 ? 17.631  71.592  114.199 1.00 27.13 ? 1110 SER A C     1 
ATOM   8032  O O     . SER A  1 1112 ? 16.861  70.800  113.648 1.00 25.65 ? 1110 SER A O     1 
ATOM   8033  C CB    . SER A  1 1112 ? 19.326  70.709  115.806 1.00 30.23 ? 1110 SER A CB    1 
ATOM   8034  O OG    . SER A  1 1112 ? 18.524  69.568  116.039 1.00 32.62 ? 1110 SER A OG    1 
ATOM   8035  N N     . GLY A  1 1113 ? 17.225  72.780  114.643 1.00 25.34 ? 1111 GLY A N     1 
ATOM   8036  C CA    . GLY A  1 1113 ? 15.849  73.191  114.434 1.00 24.76 ? 1111 GLY A CA    1 
ATOM   8037  C C     . GLY A  1 1113 ? 15.500  73.295  112.966 1.00 24.45 ? 1111 GLY A C     1 
ATOM   8038  O O     . GLY A  1 1113 ? 14.421  72.869  112.548 1.00 24.10 ? 1111 GLY A O     1 
ATOM   8039  N N     . LEU A  1 1114 ? 16.423  73.834  112.159 1.00 24.60 ? 1112 LEU A N     1 
ATOM   8040  C CA    . LEU A  1 1114 ? 16.209  73.890  110.716 1.00 24.37 ? 1112 LEU A CA    1 
ATOM   8041  C C     . LEU A  1 1114 ? 16.088  72.493  110.131 1.00 24.12 ? 1112 LEU A C     1 
ATOM   8042  O O     . LEU A  1 1114 ? 15.194  72.229  109.316 1.00 23.79 ? 1112 LEU A O     1 
ATOM   8043  C CB    . LEU A  1 1114 ? 17.343  74.656  110.032 1.00 26.71 ? 1112 LEU A CB    1 
ATOM   8044  C CG    . LEU A  1 1114 ? 17.412  74.592  108.502 1.00 25.38 ? 1112 LEU A CG    1 
ATOM   8045  C CD1   . LEU A  1 1114 ? 16.119  75.097  107.861 1.00 25.34 ? 1112 LEU A CD1   1 
ATOM   8046  C CD2   . LEU A  1 1114 ? 18.593  75.393  107.989 1.00 27.29 ? 1112 LEU A CD2   1 
ATOM   8047  N N     . TYR A  1 1115 ? 16.960  71.581  110.547 1.00 24.30 ? 1113 TYR A N     1 
ATOM   8048  C CA    . TYR A  1 1115 ? 16.899  70.217  110.017 1.00 24.12 ? 1113 TYR A CA    1 
ATOM   8049  C C     . TYR A  1 1115 ? 15.569  69.553  110.354 1.00 23.81 ? 1113 TYR A C     1 
ATOM   8050  O O     . TYR A  1 1115 ? 14.991  68.855  109.515 1.00 23.53 ? 1113 TYR A O     1 
ATOM   8051  C CB    . TYR A  1 1115 ? 18.064  69.380  110.556 1.00 24.42 ? 1113 TYR A CB    1 
ATOM   8052  C CG    . TYR A  1 1115 ? 19.440  69.780  110.048 1.00 24.73 ? 1113 TYR A CG    1 
ATOM   8053  C CD1   . TYR A  1 1115 ? 19.589  70.638  108.968 1.00 25.45 ? 1113 TYR A CD1   1 
ATOM   8054  C CD2   . TYR A  1 1115 ? 20.598  69.300  110.666 1.00 26.33 ? 1113 TYR A CD2   1 
ATOM   8055  C CE1   . TYR A  1 1115 ? 20.856  71.006  108.503 1.00 25.03 ? 1113 TYR A CE1   1 
ATOM   8056  C CE2   . TYR A  1 1115 ? 21.852  69.644  110.206 1.00 25.38 ? 1113 TYR A CE2   1 
ATOM   8057  C CZ    . TYR A  1 1115 ? 21.978  70.506  109.134 1.00 26.82 ? 1113 TYR A CZ    1 
ATOM   8058  O OH    . TYR A  1 1115 ? 23.231  70.861  108.689 1.00 31.47 ? 1113 TYR A OH    1 
ATOM   8059  N N     . HIS A  1 1116 ? 15.080  69.741  111.588 1.00 23.87 ? 1114 HIS A N     1 
ATOM   8060  C CA    . HIS A  1 1116 ? 13.784  69.197  111.979 1.00 23.61 ? 1114 HIS A CA    1 
ATOM   8061  C C     . HIS A  1 1116 ? 12.647  69.846  111.190 1.00 23.29 ? 1114 HIS A C     1 
ATOM   8062  O O     . HIS A  1 1116 ? 11.730  69.151  110.740 1.00 22.99 ? 1114 HIS A O     1 
ATOM   8063  C CB    . HIS A  1 1116 ? 13.557  69.382  113.481 1.00 23.81 ? 1114 HIS A CB    1 
ATOM   8064  C CG    . HIS A  1 1116 ? 14.218  68.336  114.327 1.00 24.05 ? 1114 HIS A CG    1 
ATOM   8065  N ND1   . HIS A  1 1116 ? 15.495  68.472  114.833 1.00 31.33 ? 1114 HIS A ND1   1 
ATOM   8066  C CD2   . HIS A  1 1116 ? 13.766  67.138  114.770 1.00 25.01 ? 1114 HIS A CD2   1 
ATOM   8067  C CE1   . HIS A  1 1116 ? 15.803  67.399  115.540 1.00 24.57 ? 1114 HIS A CE1   1 
ATOM   8068  N NE2   . HIS A  1 1116 ? 14.770  66.576  115.520 1.00 28.24 ? 1114 HIS A NE2   1 
ATOM   8069  N N     . GLN A  1 1117 ? 12.686  71.174  111.017 1.00 23.36 ? 1115 GLN A N     1 
ATOM   8070  C CA    . GLN A  1 1117 ? 11.645  71.846  110.239 1.00 23.08 ? 1115 GLN A CA    1 
ATOM   8071  C C     . GLN A  1 1117 ? 11.655  71.374  108.795 1.00 22.86 ? 1115 GLN A C     1 
ATOM   8072  O O     . GLN A  1 1117 ? 10.592  71.130  108.207 1.00 22.55 ? 1115 GLN A O     1 
ATOM   8073  C CB    . GLN A  1 1117 ? 11.824  73.361  110.284 1.00 23.26 ? 1115 GLN A CB    1 
ATOM   8074  C CG    . GLN A  1 1117 ? 11.592  74.011  111.635 1.00 23.47 ? 1115 GLN A CG    1 
ATOM   8075  C CD    . GLN A  1 1117 ? 11.859  75.505  111.583 1.00 24.80 ? 1115 GLN A CD    1 
ATOM   8076  O OE1   . GLN A  1 1117 ? 12.448  75.997  110.623 1.00 24.89 ? 1115 GLN A OE1   1 
ATOM   8077  N NE2   . GLN A  1 1117 ? 11.428  76.237  112.619 1.00 23.95 ? 1115 GLN A NE2   1 
ATOM   8078  N N     . LEU A  1 1118 ? 12.843  71.280  108.192 1.00 23.05 ? 1116 LEU A N     1 
ATOM   8079  C CA    A LEU A  1 1118 ? 12.920  70.819  106.813 0.57 22.89 ? 1116 LEU A CA    1 
ATOM   8080  C CA    B LEU A  1 1118 ? 12.946  70.804  106.816 0.43 22.89 ? 1116 LEU A CA    1 
ATOM   8081  C C     . LEU A  1 1118 ? 12.398  69.391  106.691 1.00 22.67 ? 1116 LEU A C     1 
ATOM   8082  O O     . LEU A  1 1118 ? 11.638  69.079  105.766 1.00 22.40 ? 1116 LEU A O     1 
ATOM   8083  C CB    A LEU A  1 1118 ? 14.362  70.942  106.312 0.57 23.18 ? 1116 LEU A CB    1 
ATOM   8084  C CB    B LEU A  1 1118 ? 14.405  70.852  106.356 0.43 23.19 ? 1116 LEU A CB    1 
ATOM   8085  C CG    A LEU A  1 1118 ? 14.699  70.682  104.842 0.57 23.13 ? 1116 LEU A CG    1 
ATOM   8086  C CG    B LEU A  1 1118 ? 14.999  72.195  105.947 0.43 23.41 ? 1116 LEU A CG    1 
ATOM   8087  C CD1   A LEU A  1 1118 ? 13.716  71.373  103.895 0.57 22.88 ? 1116 LEU A CD1   1 
ATOM   8088  C CD1   B LEU A  1 1118 ? 16.510  72.081  105.832 0.43 23.76 ? 1116 LEU A CD1   1 
ATOM   8089  C CD2   A LEU A  1 1118 ? 16.121  71.152  104.573 0.57 23.50 ? 1116 LEU A CD2   1 
ATOM   8090  C CD2   B LEU A  1 1118 ? 14.396  72.640  104.637 0.43 23.21 ? 1116 LEU A CD2   1 
ATOM   8091  N N     . ALA A  1 1119 ? 12.773  68.517  107.625 1.00 22.80 ? 1117 ALA A N     1 
ATOM   8092  C CA    . ALA A  1 1119 ? 12.233  67.161  107.618 1.00 25.00 ? 1117 ALA A CA    1 
ATOM   8093  C C     . ALA A  1 1119 ? 10.702  67.164  107.660 1.00 22.32 ? 1117 ALA A C     1 
ATOM   8094  O O     . ALA A  1 1119 ? 10.054  66.445  106.889 1.00 22.98 ? 1117 ALA A O     1 
ATOM   8095  C CB    . ALA A  1 1119 ? 12.807  66.363  108.793 1.00 22.88 ? 1117 ALA A CB    1 
ATOM   8096  N N     . ALA A  1 1120 ? 10.104  67.971  108.546 1.00 22.32 ? 1118 ALA A N     1 
ATOM   8097  C CA    . ALA A  1 1120 ? 8.647   67.997  108.642 1.00 22.05 ? 1118 ALA A CA    1 
ATOM   8098  C C     . ALA A  1 1120 ? 8.035   68.435  107.325 1.00 21.79 ? 1118 ALA A C     1 
ATOM   8099  O O     . ALA A  1 1120 ? 7.071   67.822  106.836 1.00 21.77 ? 1118 ALA A O     1 
ATOM   8100  C CB    . ALA A  1 1120 ? 8.190   68.930  109.768 1.00 22.15 ? 1118 ALA A CB    1 
ATOM   8101  N N     . ALA A  1 1121 ? 8.615   69.467  106.708 1.00 21.88 ? 1119 ALA A N     1 
ATOM   8102  C CA    . ALA A  1 1121 ? 8.043   69.992  105.469 1.00 21.67 ? 1119 ALA A CA    1 
ATOM   8103  C C     . ALA A  1 1121 ? 8.236   69.033  104.299 1.00 21.56 ? 1119 ALA A C     1 
ATOM   8104  O O     . ALA A  1 1121 ? 7.318   68.857  103.476 1.00 21.30 ? 1119 ALA A O     1 
ATOM   8105  C CB    . ALA A  1 1121 ? 8.656   71.355  105.145 1.00 21.86 ? 1119 ALA A CB    1 
ATOM   8106  N N     . LEU A  1 1122 ? 9.426   68.434  104.181 1.00 21.76 ? 1120 LEU A N     1 
ATOM   8107  C CA    . LEU A  1 1122 ? 9.701   67.541  103.054 1.00 21.71 ? 1120 LEU A CA    1 
ATOM   8108  C C     . LEU A  1 1122 ? 8.888   66.258  103.157 1.00 22.74 ? 1120 LEU A C     1 
ATOM   8109  O O     . LEU A  1 1122 ? 8.387   65.756  102.148 1.00 23.21 ? 1120 LEU A O     1 
ATOM   8110  C CB    . LEU A  1 1122 ? 11.193  67.209  102.972 1.00 24.41 ? 1120 LEU A CB    1 
ATOM   8111  C CG    . LEU A  1 1122 ? 12.193  68.330  102.662 1.00 22.26 ? 1120 LEU A CG    1 
ATOM   8112  C CD1   . LEU A  1 1122 ? 13.623  67.812  102.689 1.00 22.93 ? 1120 LEU A CD1   1 
ATOM   8113  C CD2   . LEU A  1 1122 ? 11.859  68.907  101.310 1.00 22.36 ? 1120 LEU A CD2   1 
ATOM   8114  N N     . ALA A  1 1123 ? 8.723   65.730  104.373 1.00 21.57 ? 1121 ALA A N     1 
ATOM   8115  C CA    . ALA A  1 1123 ? 7.939   64.512  104.571 1.00 21.43 ? 1121 ALA A CA    1 
ATOM   8116  C C     . ALA A  1 1123 ? 6.477   64.690  104.192 1.00 24.96 ? 1121 ALA A C     1 
ATOM   8117  O O     . ALA A  1 1123 ? 5.799   63.691  103.938 1.00 20.97 ? 1121 ALA A O     1 
ATOM   8118  C CB    . ALA A  1 1123 ? 8.025   64.056  106.028 1.00 22.81 ? 1121 ALA A CB    1 
ATOM   8119  N N     . THR A  1 1124 ? 5.977   65.929  104.165 1.00 21.02 ? 1122 THR A N     1 
ATOM   8120  C CA    . THR A  1 1124 ? 4.604   66.199  103.773 1.00 20.74 ? 1122 THR A CA    1 
ATOM   8121  C C     . THR A  1 1124 ? 4.521   66.718  102.340 1.00 20.88 ? 1122 THR A C     1 
ATOM   8122  O O     . THR A  1 1124 ? 3.478   67.248  101.937 1.00 21.37 ? 1122 THR A O     1 
ATOM   8123  C CB    . THR A  1 1124 ? 3.951   67.161  104.778 1.00 20.73 ? 1122 THR A CB    1 
ATOM   8124  O OG1   . THR A  1 1124 ? 4.848   68.236  105.086 1.00 20.95 ? 1122 THR A OG1   1 
ATOM   8125  C CG2   . THR A  1 1124 ? 3.642   66.429  106.092 1.00 21.44 ? 1122 THR A CG2   1 
ATOM   8126  N N     . GLY A  1 1125 ? 5.594   66.536  101.554 1.00 20.76 ? 1123 GLY A N     1 
ATOM   8127  C CA    . GLY A  1 1125 ? 5.592   66.809  100.129 1.00 20.69 ? 1123 GLY A CA    1 
ATOM   8128  C C     . GLY A  1 1125 ? 5.869   68.240  99.739  1.00 20.87 ? 1123 GLY A C     1 
ATOM   8129  O O     . GLY A  1 1125 ? 5.824   68.556  98.539  1.00 20.74 ? 1123 GLY A O     1 
ATOM   8130  N N     . ASN A  1 1126 ? 6.158   69.110  100.702 1.00 20.91 ? 1124 ASN A N     1 
ATOM   8131  C CA    . ASN A  1 1126 ? 6.266   70.543  100.481 1.00 21.01 ? 1124 ASN A CA    1 
ATOM   8132  C C     . ASN A  1 1126 ? 7.673   70.938  100.036 1.00 22.19 ? 1124 ASN A C     1 
ATOM   8133  O O     . ASN A  1 1126 ? 8.650   70.218  100.244 1.00 22.29 ? 1124 ASN A O     1 
ATOM   8134  C CB    . ASN A  1 1126 ? 5.906   71.299  101.766 1.00 21.06 ? 1124 ASN A CB    1 
ATOM   8135  C CG    . ASN A  1 1126 ? 4.493   71.016  102.218 1.00 21.64 ? 1124 ASN A CG    1 
ATOM   8136  O OD1   . ASN A  1 1126 ? 3.540   71.429  101.561 1.00 21.12 ? 1124 ASN A OD1   1 
ATOM   8137  N ND2   . ASN A  1 1126 ? 4.345   70.296  103.325 1.00 20.81 ? 1124 ASN A ND2   1 
ATOM   8138  N N     . SER A  1 1127 ? 7.751   72.097  99.398  1.00 23.11 ? 1125 SER A N     1 
ATOM   8139  C CA    . SER A  1 1127 ? 8.983   72.842  99.246  1.00 23.80 ? 1125 SER A CA    1 
ATOM   8140  C C     . SER A  1 1127 ? 9.044   73.852  100.378 1.00 21.88 ? 1125 SER A C     1 
ATOM   8141  O O     . SER A  1 1127 ? 8.090   74.000  101.142 1.00 22.77 ? 1125 SER A O     1 
ATOM   8142  C CB    . SER A  1 1127 ? 9.022   73.534  97.886  1.00 28.94 ? 1125 SER A CB    1 
ATOM   8143  O OG    . SER A  1 1127 ? 7.950   74.452  97.803  1.00 27.08 ? 1125 SER A OG    1 
ATOM   8144  N N     . VAL A  1 1128 ? 10.181  74.532  100.516 1.00 23.09 ? 1126 VAL A N     1 
ATOM   8145  C CA    . VAL A  1 1128 ? 10.358  75.467  101.623 1.00 23.16 ? 1126 VAL A CA    1 
ATOM   8146  C C     . VAL A  1 1128 ? 10.993  76.758  101.133 1.00 25.30 ? 1126 VAL A C     1 
ATOM   8147  O O     . VAL A  1 1128 ? 11.722  76.783  100.138 1.00 25.60 ? 1126 VAL A O     1 
ATOM   8148  C CB    . VAL A  1 1128 ? 11.223  74.881  102.761 1.00 22.59 ? 1126 VAL A CB    1 
ATOM   8149  C CG1   . VAL A  1 1128 ? 10.621  73.578  103.276 1.00 22.34 ? 1126 VAL A CG1   1 
ATOM   8150  C CG2   . VAL A  1 1128 ? 12.681  74.683  102.290 1.00 22.88 ? 1126 VAL A CG2   1 
ATOM   8151  N N     . ALA A  1 1129 ? 10.729  77.830  101.873 1.00 24.63 ? 1127 ALA A N     1 
ATOM   8152  C CA    . ALA A  1 1129 ? 11.507  79.061  101.815 1.00 26.15 ? 1127 ALA A CA    1 
ATOM   8153  C C     . ALA A  1 1129 ? 12.066  79.279  103.211 1.00 23.47 ? 1127 ALA A C     1 
ATOM   8154  O O     . ALA A  1 1129 ? 11.296  79.333  104.174 1.00 23.36 ? 1127 ALA A O     1 
ATOM   8155  C CB    . ALA A  1 1129 ? 10.646  80.249  101.375 1.00 23.89 ? 1127 ALA A CB    1 
ATOM   8156  N N     . ILE A  1 1130 ? 13.391  79.354  103.325 1.00 23.80 ? 1128 ILE A N     1 
ATOM   8157  C CA    . ILE A  1 1130 ? 14.063  79.459  104.619 1.00 24.06 ? 1128 ILE A CA    1 
ATOM   8158  C C     . ILE A  1 1130 ? 14.451  80.912  104.853 1.00 30.02 ? 1128 ILE A C     1 
ATOM   8159  O O     . ILE A  1 1130 ? 15.071  81.547  103.988 1.00 28.05 ? 1128 ILE A O     1 
ATOM   8160  C CB    . ILE A  1 1130 ? 15.311  78.559  104.694 1.00 24.22 ? 1128 ILE A CB    1 
ATOM   8161  C CG1   . ILE A  1 1130 ? 14.980  77.107  104.348 1.00 24.37 ? 1128 ILE A CG1   1 
ATOM   8162  C CG2   . ILE A  1 1130 ? 15.906  78.607  106.096 1.00 24.47 ? 1128 ILE A CG2   1 
ATOM   8163  C CD1   . ILE A  1 1130 ? 16.219  76.249  104.222 1.00 25.08 ? 1128 ILE A CD1   1 
ATOM   8164  N N     . ASP A  1 1131 ? 14.119  81.427  106.038 1.00 24.55 ? 1129 ASP A N     1 
ATOM   8165  C CA    . ASP A  1 1131 ? 14.481  82.791  106.396 1.00 28.38 ? 1129 ASP A CA    1 
ATOM   8166  C C     . ASP A  1 1131 ? 15.985  82.998  106.282 1.00 29.24 ? 1129 ASP A C     1 
ATOM   8167  O O     . ASP A  1 1131 ? 16.762  82.390  107.026 1.00 28.03 ? 1129 ASP A O     1 
ATOM   8168  C CB    . ASP A  1 1131 ? 14.006  83.105  107.814 1.00 28.27 ? 1129 ASP A CB    1 
ATOM   8169  C CG    . ASP A  1 1131 ? 14.380  84.503  108.252 1.00 31.98 ? 1129 ASP A CG    1 
ATOM   8170  O OD1   . ASP A  1 1131 ? 14.463  85.396  107.384 1.00 30.06 ? 1129 ASP A OD1   1 
ATOM   8171  O OD2   . ASP A  1 1131 ? 14.595  84.699  109.465 1.00 33.30 ? 1129 ASP A OD2   1 
ATOM   8172  N N     . ALA A  1 1132 ? 16.410  83.845  105.343 1.00 30.39 ? 1130 ALA A N     1 
ATOM   8173  C CA    . ALA A  1 1132 ? 17.835  84.126  105.191 1.00 34.19 ? 1130 ALA A CA    1 
ATOM   8174  C C     . ALA A  1 1132 ? 18.408  84.882  106.386 1.00 32.57 ? 1130 ALA A C     1 
ATOM   8175  O O     . ALA A  1 1132 ? 19.627  84.853  106.600 1.00 40.57 ? 1130 ALA A O     1 
ATOM   8176  C CB    . ALA A  1 1132 ? 18.080  84.917  103.906 1.00 32.38 ? 1130 ALA A CB    1 
ATOM   8177  N N     . ALA A  1 1133 ? 17.563  85.552  107.174 1.00 35.52 ? 1131 ALA A N     1 
ATOM   8178  C CA    . ALA A  1 1133 ? 18.059  86.283  108.335 1.00 36.53 ? 1131 ALA A CA    1 
ATOM   8179  C C     . ALA A  1 1133 ? 18.450  85.359  109.477 1.00 35.43 ? 1131 ALA A C     1 
ATOM   8180  O O     . ALA A  1 1133 ? 19.037  85.827  110.456 1.00 38.26 ? 1131 ALA A O     1 
ATOM   8181  C CB    . ALA A  1 1133 ? 17.015  87.293  108.818 1.00 33.10 ? 1131 ALA A CB    1 
ATOM   8182  N N     . SER A  1 1134 ? 18.144  84.067  109.378 1.00 33.92 ? 1132 SER A N     1 
ATOM   8183  C CA    . SER A  1 1134 ? 18.607  83.104  110.367 1.00 32.45 ? 1132 SER A CA    1 
ATOM   8184  C C     . SER A  1 1134 ? 20.117  82.903  110.340 1.00 34.42 ? 1132 SER A C     1 
ATOM   8185  O O     . SER A  1 1134 ? 20.671  82.406  111.324 1.00 30.85 ? 1132 SER A O     1 
ATOM   8186  C CB    . SER A  1 1134 ? 17.933  81.755  110.134 1.00 36.08 ? 1132 SER A CB    1 
ATOM   8187  O OG    . SER A  1 1134 ? 18.342  81.215  108.884 1.00 33.33 ? 1132 SER A OG    1 
ATOM   8188  N N     . GLY A  1 1135 ? 20.786  83.243  109.238 1.00 30.95 ? 1133 GLY A N     1 
ATOM   8189  C CA    . GLY A  1 1135 ? 22.209  82.993  109.110 1.00 35.88 ? 1133 GLY A CA    1 
ATOM   8190  C C     . GLY A  1 1135 ? 22.615  81.534  109.061 1.00 34.98 ? 1133 GLY A C     1 
ATOM   8191  O O     . GLY A  1 1135 ? 23.769  81.212  109.352 1.00 35.82 ? 1133 GLY A O     1 
ATOM   8192  N N     . LEU A  1 1136 ? 21.710  80.628  108.692 1.00 30.12 ? 1134 LEU A N     1 
ATOM   8193  C CA    . LEU A  1 1136 ? 22.024  79.203  108.733 1.00 35.67 ? 1134 LEU A CA    1 
ATOM   8194  C C     . LEU A  1 1136 ? 22.351  78.633  107.354 1.00 34.64 ? 1134 LEU A C     1 
ATOM   8195  O O     . LEU A  1 1136 ? 22.245  77.417  107.153 1.00 33.93 ? 1134 LEU A O     1 
ATOM   8196  C CB    . LEU A  1 1136 ? 20.872  78.422  109.377 1.00 32.57 ? 1134 LEU A CB    1 
ATOM   8197  C CG    . LEU A  1 1136 ? 20.650  78.649  110.881 1.00 29.48 ? 1134 LEU A CG    1 
ATOM   8198  C CD1   . LEU A  1 1136 ? 19.291  78.088  111.313 1.00 28.68 ? 1134 LEU A CD1   1 
ATOM   8199  C CD2   . LEU A  1 1136 ? 21.793  78.043  111.720 1.00 33.31 ? 1134 LEU A CD2   1 
ATOM   8200  N N     . GLN A  1 1137 ? 22.747  79.486  106.405 1.00 34.19 ? 1135 GLN A N     1 
ATOM   8201  C CA    . GLN A  1 1137 ? 23.035  79.018  105.051 1.00 33.11 ? 1135 GLN A CA    1 
ATOM   8202  C C     . GLN A  1 1137 ? 24.136  77.961  105.037 1.00 33.64 ? 1135 GLN A C     1 
ATOM   8203  O O     . GLN A  1 1137 ? 24.057  76.984  104.282 1.00 34.51 ? 1135 GLN A O     1 
ATOM   8204  C CB    . GLN A  1 1137 ? 23.413  80.200  104.161 1.00 35.17 ? 1135 GLN A CB    1 
ATOM   8205  C CG    . GLN A  1 1137 ? 22.218  81.070  103.767 1.00 35.83 ? 1135 GLN A CG    1 
ATOM   8206  C CD    . GLN A  1 1137 ? 21.923  82.178  104.777 1.00 32.77 ? 1135 GLN A CD    1 
ATOM   8207  O OE1   . GLN A  1 1137 ? 22.378  82.141  105.926 1.00 38.64 ? 1135 GLN A OE1   1 
ATOM   8208  N NE2   . GLN A  1 1137 ? 21.180  83.183  104.338 1.00 40.41 ? 1135 GLN A NE2   1 
ATOM   8209  N N     . ALA A  1 1138 ? 25.163  78.116  105.872 1.00 30.79 ? 1136 ALA A N     1 
ATOM   8210  C CA    . ALA A  1 1138 ? 26.234  77.125  105.824 1.00 32.41 ? 1136 ALA A CA    1 
ATOM   8211  C C     . ALA A  1 1138 ? 25.800  75.751  106.325 1.00 33.24 ? 1136 ALA A C     1 
ATOM   8212  O O     . ALA A  1 1138 ? 26.557  74.787  106.173 1.00 33.21 ? 1136 ALA A O     1 
ATOM   8213  C CB    . ALA A  1 1138 ? 27.450  77.608  106.626 1.00 31.80 ? 1136 ALA A CB    1 
ATOM   8214  N N     . SER A  1 1139 ? 24.613  75.634  106.919 1.00 36.19 ? 1137 SER A N     1 
ATOM   8215  C CA    . SER A  1 1139 ? 24.160  74.355  107.442 1.00 34.00 ? 1137 SER A CA    1 
ATOM   8216  C C     . SER A  1 1139 ? 23.620  73.432  106.355 1.00 27.22 ? 1137 SER A C     1 
ATOM   8217  O O     . SER A  1 1139 ? 23.417  72.245  106.622 1.00 29.18 ? 1137 SER A O     1 
ATOM   8218  C CB    . SER A  1 1139 ? 23.093  74.577  108.524 1.00 32.61 ? 1137 SER A CB    1 
ATOM   8219  O OG    . SER A  1 1139 ? 23.693  74.965  109.755 1.00 36.13 ? 1137 SER A OG    1 
ATOM   8220  N N     . LEU A  1 1140 ? 23.420  73.937  105.140 1.00 29.16 ? 1138 LEU A N     1 
ATOM   8221  C CA    . LEU A  1 1140 ? 22.872  73.131  104.056 1.00 32.22 ? 1138 LEU A CA    1 
ATOM   8222  C C     . LEU A  1 1140 ? 23.808  73.104  102.852 1.00 35.86 ? 1138 LEU A C     1 
ATOM   8223  O O     . LEU A  1 1140 ? 23.361  73.284  101.715 1.00 37.45 ? 1138 LEU A O     1 
ATOM   8224  C CB    . LEU A  1 1140 ? 21.494  73.664  103.639 1.00 31.14 ? 1138 LEU A CB    1 
ATOM   8225  C CG    . LEU A  1 1140 ? 20.344  73.499  104.641 1.00 29.38 ? 1138 LEU A CG    1 
ATOM   8226  C CD1   . LEU A  1 1140 ? 19.099  74.174  104.111 1.00 33.11 ? 1138 LEU A CD1   1 
ATOM   8227  C CD2   . LEU A  1 1140 ? 20.052  72.030  104.927 1.00 31.49 ? 1138 LEU A CD2   1 
ATOM   8228  N N     . LYS A  1 1141 ? 25.100  72.883  103.082 1.00 33.28 ? 1139 LYS A N     1 
ATOM   8229  C CA    . LYS A  1 1141 ? 26.043  72.705  101.982 1.00 40.31 ? 1139 LYS A CA    1 
ATOM   8230  C C     . LYS A  1 1141 ? 25.897  71.321  101.351 1.00 37.89 ? 1139 LYS A C     1 
ATOM   8231  O O     . LYS A  1 1141 ? 25.663  70.324  102.043 1.00 38.11 ? 1139 LYS A O     1 
ATOM   8232  C CB    . LYS A  1 1141 ? 27.481  72.900  102.471 1.00 40.73 ? 1139 LYS A CB    1 
ATOM   8233  N N     . ASN A  1 1142 ? 26.037  71.268  100.024 1.00 37.39 ? 1140 ASN A N     1 
ATOM   8234  C CA    . ASN A  1 1142 ? 26.146  70.003  99.291  1.00 34.78 ? 1140 ASN A CA    1 
ATOM   8235  C C     . ASN A  1 1142 ? 24.877  69.162  99.400  1.00 37.30 ? 1140 ASN A C     1 
ATOM   8236  O O     . ASN A  1 1142 ? 24.943  67.948  99.600  1.00 37.17 ? 1140 ASN A O     1 
ATOM   8237  C CB    . ASN A  1 1142 ? 27.352  69.188  99.767  1.00 42.50 ? 1140 ASN A CB    1 
ATOM   8238  C CG    . ASN A  1 1142 ? 28.636  69.987  99.766  1.00 46.36 ? 1140 ASN A CG    1 
ATOM   8239  O OD1   . ASN A  1 1142 ? 29.320  70.087  100.789 1.00 45.94 ? 1140 ASN A OD1   1 
ATOM   8240  N ND2   . ASN A  1 1142 ? 28.972  70.565  98.617  1.00 45.48 ? 1140 ASN A ND2   1 
ATOM   8241  N N     . LEU A  1 1143 ? 23.714  69.800  99.268  1.00 39.29 ? 1141 LEU A N     1 
ATOM   8242  C CA    . LEU A  1 1143 ? 22.468  69.052  99.263  1.00 35.91 ? 1141 LEU A CA    1 
ATOM   8243  C C     . LEU A  1 1143 ? 22.333  68.256  97.966  1.00 34.92 ? 1141 LEU A C     1 
ATOM   8244  O O     . LEU A  1 1143 ? 22.765  68.708  96.901  1.00 33.11 ? 1141 LEU A O     1 
ATOM   8245  C CB    . LEU A  1 1143 ? 21.268  69.986  99.396  1.00 31.54 ? 1141 LEU A CB    1 
ATOM   8246  C CG    . LEU A  1 1143 ? 20.899  70.620  100.737 1.00 34.16 ? 1141 LEU A CG    1 
ATOM   8247  C CD1   . LEU A  1 1143 ? 19.848  71.692  100.486 1.00 33.19 ? 1141 LEU A CD1   1 
ATOM   8248  C CD2   . LEU A  1 1143 ? 20.396  69.582  101.750 1.00 31.27 ? 1141 LEU A CD2   1 
ATOM   8249  N N     . PRO A  1 1144 ? 21.719  67.076  98.021  1.00 33.63 ? 1142 PRO A N     1 
ATOM   8250  C CA    . PRO A  1 1144 ? 21.326  66.412  96.773  1.00 33.77 ? 1142 PRO A CA    1 
ATOM   8251  C C     . PRO A  1 1144 ? 20.421  67.343  95.976  1.00 34.03 ? 1142 PRO A C     1 
ATOM   8252  O O     . PRO A  1 1144 ? 19.660  68.133  96.544  1.00 32.77 ? 1142 PRO A O     1 
ATOM   8253  C CB    . PRO A  1 1144 ? 20.575  65.159  97.246  1.00 32.82 ? 1142 PRO A CB    1 
ATOM   8254  C CG    . PRO A  1 1144 ? 20.901  65.018  98.702  1.00 31.25 ? 1142 PRO A CG    1 
ATOM   8255  C CD    . PRO A  1 1144 ? 21.215  66.378  99.214  1.00 34.08 ? 1142 PRO A CD    1 
ATOM   8256  N N     . GLN A  1 1145 ? 20.538  67.271  94.647  1.00 31.67 ? 1143 GLN A N     1 
ATOM   8257  C CA    . GLN A  1 1145 ? 19.794  68.191  93.790  1.00 33.30 ? 1143 GLN A CA    1 
ATOM   8258  C C     . GLN A  1 1145 ? 18.292  68.088  94.031  1.00 34.12 ? 1143 GLN A C     1 
ATOM   8259  O O     . GLN A  1 1145 ? 17.579  69.094  93.960  1.00 30.22 ? 1143 GLN A O     1 
ATOM   8260  C CB    . GLN A  1 1145 ? 20.119  67.923  92.318  1.00 36.97 ? 1143 GLN A CB    1 
ATOM   8261  N N     . THR A  1 1146 ? 17.796  66.875  94.301  1.00 32.18 ? 1144 THR A N     1 
ATOM   8262  C CA    . THR A  1 1146 ? 16.377  66.679  94.592  1.00 31.65 ? 1144 THR A CA    1 
ATOM   8263  C C     . THR A  1 1146 ? 15.917  67.558  95.745  1.00 30.12 ? 1144 THR A C     1 
ATOM   8264  O O     . THR A  1 1146 ? 14.831  68.151  95.694  1.00 29.17 ? 1144 THR A O     1 
ATOM   8265  C CB    . THR A  1 1146 ? 16.111  65.216  94.931  1.00 28.70 ? 1144 THR A CB    1 
ATOM   8266  O OG1   . THR A  1 1146 ? 17.001  64.815  95.971  1.00 31.26 ? 1144 THR A OG1   1 
ATOM   8267  C CG2   . THR A  1 1146 ? 16.348  64.334  93.721  1.00 34.51 ? 1144 THR A CG2   1 
ATOM   8268  N N     . VAL A  1 1147 ? 16.727  67.635  96.800  1.00 25.18 ? 1145 VAL A N     1 
ATOM   8269  C CA    . VAL A  1 1147 ? 16.402  68.480  97.940  1.00 27.02 ? 1145 VAL A CA    1 
ATOM   8270  C C     . VAL A  1 1147 ? 16.620  69.949  97.594  1.00 27.96 ? 1145 VAL A C     1 
ATOM   8271  O O     . VAL A  1 1147 ? 15.775  70.798  97.892  1.00 27.21 ? 1145 VAL A O     1 
ATOM   8272  C CB    . VAL A  1 1147 ? 17.232  68.060  99.167  1.00 23.64 ? 1145 VAL A CB    1 
ATOM   8273  C CG1   . VAL A  1 1147 ? 16.765  68.813  100.388 1.00 23.63 ? 1145 VAL A CG1   1 
ATOM   8274  C CG2   . VAL A  1 1147 ? 17.155  66.544  99.380  1.00 23.32 ? 1145 VAL A CG2   1 
ATOM   8275  N N     . GLY A  1 1148 ? 17.764  70.269  96.977  1.00 29.23 ? 1146 GLY A N     1 
ATOM   8276  C CA    . GLY A  1 1148 ? 18.030  71.646  96.595  1.00 29.72 ? 1146 GLY A CA    1 
ATOM   8277  C C     . GLY A  1 1148 ? 16.941  72.246  95.728  1.00 27.69 ? 1146 GLY A C     1 
ATOM   8278  O O     . GLY A  1 1148 ? 16.636  73.437  95.846  1.00 28.42 ? 1146 GLY A O     1 
ATOM   8279  N N     . LEU A  1 1149 ? 16.335  71.438  94.852  1.00 26.88 ? 1147 LEU A N     1 
ATOM   8280  C CA    . LEU A  1 1149 ? 15.211  71.916  94.058  1.00 30.44 ? 1147 LEU A CA    1 
ATOM   8281  C C     . LEU A  1 1149 ? 14.046  72.347  94.932  1.00 27.01 ? 1147 LEU A C     1 
ATOM   8282  O O     . LEU A  1 1149 ? 13.232  73.162  94.503  1.00 29.18 ? 1147 LEU A O     1 
ATOM   8283  C CB    . LEU A  1 1149 ? 14.731  70.839  93.077  1.00 33.05 ? 1147 LEU A CB    1 
ATOM   8284  C CG    . LEU A  1 1149 ? 15.664  70.346  91.961  1.00 39.04 ? 1147 LEU A CG    1 
ATOM   8285  C CD1   . LEU A  1 1149 ? 15.016  69.181  91.215  1.00 40.37 ? 1147 LEU A CD1   1 
ATOM   8286  C CD2   . LEU A  1 1149 ? 16.051  71.448  90.989  1.00 39.18 ? 1147 LEU A CD2   1 
ATOM   8287  N N     . ARG A  1 1150 ? 13.953  71.828  96.155  1.00 27.71 ? 1148 ARG A N     1 
ATOM   8288  C CA    . ARG A  1 1150 ? 12.835  72.164  97.020  1.00 28.22 ? 1148 ARG A CA    1 
ATOM   8289  C C     . ARG A  1 1150 ? 13.134  73.326  97.954  1.00 26.52 ? 1148 ARG A C     1 
ATOM   8290  O O     . ARG A  1 1150 ? 12.223  73.806  98.632  1.00 25.95 ? 1148 ARG A O     1 
ATOM   8291  C CB    . ARG A  1 1150 ? 12.432  70.936  97.840  1.00 22.40 ? 1148 ARG A CB    1 
ATOM   8292  C CG    . ARG A  1 1150 ? 11.660  69.902  97.020  1.00 25.76 ? 1148 ARG A CG    1 
ATOM   8293  C CD    . ARG A  1 1150 ? 10.472  69.400  97.822  1.00 27.10 ? 1148 ARG A CD    1 
ATOM   8294  N NE    . ARG A  1 1150 ? 9.860   68.219  97.227  1.00 26.81 ? 1148 ARG A NE    1 
ATOM   8295  C CZ    . ARG A  1 1150 ? 9.278   67.261  97.931  1.00 28.48 ? 1148 ARG A CZ    1 
ATOM   8296  N NH1   . ARG A  1 1150 ? 9.180   67.337  99.253  1.00 22.50 ? 1148 ARG A NH1   1 
ATOM   8297  N NH2   . ARG A  1 1150 ? 8.787   66.200  97.296  1.00 24.55 ? 1148 ARG A NH2   1 
ATOM   8298  N N     . VAL A  1 1151 ? 14.382  73.771  98.020  1.00 26.62 ? 1149 VAL A N     1 
ATOM   8299  C CA    . VAL A  1 1151 ? 14.821  74.729  99.024  1.00 23.33 ? 1149 VAL A CA    1 
ATOM   8300  C C     . VAL A  1 1151 ? 15.109  76.058  98.344  1.00 31.31 ? 1149 VAL A C     1 
ATOM   8301  O O     . VAL A  1 1151 ? 15.833  76.109  97.343  1.00 34.60 ? 1149 VAL A O     1 
ATOM   8302  C CB    . VAL A  1 1151 ? 16.055  74.208  99.776  1.00 28.13 ? 1149 VAL A CB    1 
ATOM   8303  C CG1   . VAL A  1 1151 ? 16.617  75.281  100.684 1.00 32.32 ? 1149 VAL A CG1   1 
ATOM   8304  C CG2   . VAL A  1 1151 ? 15.676  72.991  100.570 1.00 27.91 ? 1149 VAL A CG2   1 
ATOM   8305  N N     . SER A  1 1152 ? 14.529  77.129  98.875  1.00 26.81 ? 1150 SER A N     1 
ATOM   8306  C CA    . SER A  1 1152 ? 14.959  78.470  98.526  1.00 34.07 ? 1150 SER A CA    1 
ATOM   8307  C C     . SER A  1 1152 ? 15.200  79.246  99.808  1.00 30.42 ? 1150 SER A C     1 
ATOM   8308  O O     . SER A  1 1152 ? 14.774  78.840  100.894 1.00 30.08 ? 1150 SER A O     1 
ATOM   8309  C CB    . SER A  1 1152 ? 13.936  79.199  97.646  1.00 28.43 ? 1150 SER A CB    1 
ATOM   8310  O OG    . SER A  1 1152 ? 12.722  79.385  98.346  1.00 40.45 ? 1150 SER A OG    1 
ATOM   8311  N N     . TRP A  1 1153 ? 15.879  80.375  99.670  1.00 31.24 ? 1151 TRP A N     1 
ATOM   8312  C CA    . TRP A  1 1153 ? 16.172  81.253  100.794 1.00 29.91 ? 1151 TRP A CA    1 
ATOM   8313  C C     . TRP A  1 1153 ? 15.499  82.594  100.558 1.00 32.95 ? 1151 TRP A C     1 
ATOM   8314  O O     . TRP A  1 1153 ? 15.500  83.109  99.438  1.00 35.27 ? 1151 TRP A O     1 
ATOM   8315  C CB    . TRP A  1 1153 ? 17.673  81.436  100.984 1.00 32.95 ? 1151 TRP A CB    1 
ATOM   8316  C CG    . TRP A  1 1153 ? 18.377  80.197  101.474 1.00 33.29 ? 1151 TRP A CG    1 
ATOM   8317  C CD1   . TRP A  1 1153 ? 18.861  79.173  100.710 1.00 32.93 ? 1151 TRP A CD1   1 
ATOM   8318  C CD2   . TRP A  1 1153 ? 18.685  79.860  102.837 1.00 29.46 ? 1151 TRP A CD2   1 
ATOM   8319  N NE1   . TRP A  1 1153 ? 19.443  78.222  101.512 1.00 34.49 ? 1151 TRP A NE1   1 
ATOM   8320  C CE2   . TRP A  1 1153 ? 19.346  78.617  102.820 1.00 31.03 ? 1151 TRP A CE2   1 
ATOM   8321  C CE3   . TRP A  1 1153 ? 18.457  80.485  104.064 1.00 27.18 ? 1151 TRP A CE3   1 
ATOM   8322  C CZ2   . TRP A  1 1153 ? 19.794  77.992  103.983 1.00 32.79 ? 1151 TRP A CZ2   1 
ATOM   8323  C CZ3   . TRP A  1 1153 ? 18.915  79.865  105.224 1.00 31.32 ? 1151 TRP A CZ3   1 
ATOM   8324  C CH2   . TRP A  1 1153 ? 19.564  78.630  105.173 1.00 32.72 ? 1151 TRP A CH2   1 
ATOM   8325  N N     . SER A  1 1154 ? 14.926  83.159  101.616 1.00 29.49 ? 1152 SER A N     1 
ATOM   8326  C CA    . SER A  1 1154 ? 14.080  84.337  101.496 1.00 32.52 ? 1152 SER A CA    1 
ATOM   8327  C C     . SER A  1 1154 ? 14.576  85.399  102.465 1.00 33.84 ? 1152 SER A C     1 
ATOM   8328  O O     . SER A  1 1154 ? 14.584  85.179  103.682 1.00 32.37 ? 1152 SER A O     1 
ATOM   8329  C CB    . SER A  1 1154 ? 12.614  83.981  101.770 1.00 30.47 ? 1152 SER A CB    1 
ATOM   8330  O OG    . SER A  1 1154 ? 11.763  85.105  101.600 1.00 31.81 ? 1152 SER A OG    1 
ATOM   8331  N N     . LYS A  1 1155 ? 15.021  86.532  101.926 1.00 31.89 ? 1153 LYS A N     1 
ATOM   8332  C CA    . LYS A  1 1155 ? 15.266  87.706  102.758 1.00 32.56 ? 1153 LYS A CA    1 
ATOM   8333  C C     . LYS A  1 1155 ? 14.004  88.541  102.912 1.00 31.95 ? 1153 LYS A C     1 
ATOM   8334  O O     . LYS A  1 1155 ? 13.719  89.058  104.000 1.00 38.24 ? 1153 LYS A O     1 
ATOM   8335  C CB    . LYS A  1 1155 ? 16.391  88.556  102.157 1.00 33.63 ? 1153 LYS A CB    1 
ATOM   8336  N N     . ASP A  1 1156 ? 13.230  88.651  101.843 1.00 32.58 ? 1154 ASP A N     1 
ATOM   8337  C CA    . ASP A  1 1156 ? 12.002  89.437  101.791 1.00 35.61 ? 1154 ASP A CA    1 
ATOM   8338  C C     . ASP A  1 1156 ? 10.856  88.433  101.673 1.00 34.48 ? 1154 ASP A C     1 
ATOM   8339  O O     . ASP A  1 1156 ? 10.486  88.025  100.572 1.00 33.38 ? 1154 ASP A O     1 
ATOM   8340  C CB    . ASP A  1 1156 ? 12.056  90.416  100.600 1.00 34.71 ? 1154 ASP A CB    1 
ATOM   8341  C CG    . ASP A  1 1156 ? 10.874  91.371  100.547 1.00 42.15 ? 1154 ASP A CG    1 
ATOM   8342  O OD1   . ASP A  1 1156 ? 9.817   91.079  101.149 1.00 42.47 ? 1154 ASP A OD1   1 
ATOM   8343  O OD2   . ASP A  1 1156 ? 11.002  92.422  99.872  1.00 42.36 ? 1154 ASP A OD2   1 
ATOM   8344  N N     . TRP A  1 1157 ? 10.300  88.032  102.822 1.00 33.50 ? 1155 TRP A N     1 
ATOM   8345  C CA    . TRP A  1 1157 ? 9.259   87.003  102.826 1.00 31.52 ? 1155 TRP A CA    1 
ATOM   8346  C C     . TRP A  1 1157 ? 8.085   87.380  101.930 1.00 34.44 ? 1155 TRP A C     1 
ATOM   8347  O O     . TRP A  1 1157 ? 7.546   86.528  101.210 1.00 32.04 ? 1155 TRP A O     1 
ATOM   8348  C CB    . TRP A  1 1157 ? 8.756   86.752  104.247 1.00 31.73 ? 1155 TRP A CB    1 
ATOM   8349  C CG    . TRP A  1 1157 ? 9.796   86.312  105.233 1.00 31.51 ? 1155 TRP A CG    1 
ATOM   8350  C CD1   . TRP A  1 1157 ? 11.082  85.946  104.970 1.00 30.97 ? 1155 TRP A CD1   1 
ATOM   8351  C CD2   . TRP A  1 1157 ? 9.628   86.206  106.654 1.00 30.90 ? 1155 TRP A CD2   1 
ATOM   8352  N NE1   . TRP A  1 1157 ? 11.726  85.619  106.145 1.00 32.15 ? 1155 TRP A NE1   1 
ATOM   8353  C CE2   . TRP A  1 1157 ? 10.852  85.771  107.190 1.00 30.14 ? 1155 TRP A CE2   1 
ATOM   8354  C CE3   . TRP A  1 1157 ? 8.557   86.448  107.524 1.00 30.18 ? 1155 TRP A CE3   1 
ATOM   8355  C CZ2   . TRP A  1 1157 ? 11.037  85.567  108.558 1.00 29.90 ? 1155 TRP A CZ2   1 
ATOM   8356  C CZ3   . TRP A  1 1157 ? 8.741   86.246  108.877 1.00 28.45 ? 1155 TRP A CZ3   1 
ATOM   8357  C CH2   . TRP A  1 1157 ? 9.969   85.811  109.382 1.00 29.13 ? 1155 TRP A CH2   1 
ATOM   8358  N N     . ALA A  1 1158 ? 7.665   88.649  101.961 1.00 32.12 ? 1156 ALA A N     1 
ATOM   8359  C CA    . ALA A  1 1158 ? 6.467   89.035  101.215 1.00 33.36 ? 1156 ALA A CA    1 
ATOM   8360  C C     . ALA A  1 1158 ? 6.688   89.024  99.710  1.00 37.63 ? 1156 ALA A C     1 
ATOM   8361  O O     . ALA A  1 1158 ? 5.714   89.067  98.948  1.00 41.11 ? 1156 ALA A O     1 
ATOM   8362  C CB    . ALA A  1 1158 ? 5.989   90.419  101.652 1.00 36.64 ? 1156 ALA A CB    1 
ATOM   8363  N N     . ALA A  1 1159 ? 7.939   88.992  99.260  1.00 36.15 ? 1157 ALA A N     1 
ATOM   8364  C CA    . ALA A  1 1159 ? 8.224   88.934  97.836  1.00 39.46 ? 1157 ALA A CA    1 
ATOM   8365  C C     . ALA A  1 1159 ? 8.294   87.512  97.317  1.00 36.30 ? 1157 ALA A C     1 
ATOM   8366  O O     . ALA A  1 1159 ? 8.127   87.294  96.112  1.00 41.34 ? 1157 ALA A O     1 
ATOM   8367  C CB    . ALA A  1 1159 ? 9.541   89.655  97.524  1.00 32.62 ? 1157 ALA A CB    1 
ATOM   8368  N N     . ASP A  1 1160 ? 8.508   86.544  98.200  1.00 37.44 ? 1158 ASP A N     1 
ATOM   8369  C CA    . ASP A  1 1160 ? 8.736   85.164  97.813  1.00 32.60 ? 1158 ASP A CA    1 
ATOM   8370  C C     . ASP A  1 1160 ? 7.519   84.283  98.036  1.00 34.66 ? 1158 ASP A C     1 
ATOM   8371  O O     . ASP A  1 1160 ? 7.605   83.066  97.856  1.00 36.51 ? 1158 ASP A O     1 
ATOM   8372  C CB    . ASP A  1 1160 ? 9.950   84.627  98.570  1.00 38.12 ? 1158 ASP A CB    1 
ATOM   8373  C CG    . ASP A  1 1160 ? 11.211  85.393  98.226  1.00 38.51 ? 1158 ASP A CG    1 
ATOM   8374  O OD1   . ASP A  1 1160 ? 11.321  85.838  97.061  1.00 40.62 ? 1158 ASP A OD1   1 
ATOM   8375  O OD2   . ASP A  1 1160 ? 12.080  85.573  99.106  1.00 37.02 ? 1158 ASP A OD2   1 
ATOM   8376  N N     . GLY A  1 1161 ? 6.390   84.870  98.409  1.00 33.84 ? 1159 GLY A N     1 
ATOM   8377  C CA    . GLY A  1 1161 ? 5.188   84.122  98.643  1.00 30.32 ? 1159 GLY A CA    1 
ATOM   8378  C C     . GLY A  1 1161 ? 4.402   83.930  97.365  1.00 38.06 ? 1159 GLY A C     1 
ATOM   8379  O O     . GLY A  1 1161 ? 4.876   84.243  96.270  1.00 38.62 ? 1159 GLY A O     1 
ATOM   8380  N N     . PRO A  1 1162 ? 3.174   83.414  97.481  1.00 34.28 ? 1160 PRO A N     1 
ATOM   8381  C CA    . PRO A  1 1162 ? 2.490   83.038  98.718  1.00 34.87 ? 1160 PRO A CA    1 
ATOM   8382  C C     . PRO A  1 1162 ? 3.038   81.746  99.303  1.00 34.49 ? 1160 PRO A C     1 
ATOM   8383  O O     . PRO A  1 1162 ? 3.454   80.824  98.594  1.00 28.37 ? 1160 PRO A O     1 
ATOM   8384  C CB    . PRO A  1 1162 ? 1.030   82.887  98.265  1.00 32.91 ? 1160 PRO A CB    1 
ATOM   8385  C CG    . PRO A  1 1162 ? 1.153   82.374  96.868  1.00 37.75 ? 1160 PRO A CG    1 
ATOM   8386  C CD    . PRO A  1 1162 ? 2.366   83.081  96.294  1.00 39.92 ? 1160 PRO A CD    1 
ATOM   8387  N N     . PHE A  1 1163 ? 3.059   81.677  100.626 1.00 25.22 ? 1161 PHE A N     1 
ATOM   8388  C CA    . PHE A  1 1163 ? 3.352   80.441  101.326 1.00 24.74 ? 1161 PHE A CA    1 
ATOM   8389  C C     . PHE A  1 1163 ? 2.056   79.732  101.702 1.00 24.74 ? 1161 PHE A C     1 
ATOM   8390  O O     . PHE A  1 1163 ? 0.953   80.272  101.578 1.00 28.02 ? 1161 PHE A O     1 
ATOM   8391  C CB    . PHE A  1 1163 ? 4.225   80.742  102.546 1.00 25.63 ? 1161 PHE A CB    1 
ATOM   8392  C CG    . PHE A  1 1163 ? 5.447   81.541  102.201 1.00 24.51 ? 1161 PHE A CG    1 
ATOM   8393  C CD1   . PHE A  1 1163 ? 6.393   81.027  101.329 1.00 25.76 ? 1161 PHE A CD1   1 
ATOM   8394  C CD2   . PHE A  1 1163 ? 5.634   82.816  102.714 1.00 24.61 ? 1161 PHE A CD2   1 
ATOM   8395  C CE1   . PHE A  1 1163 ? 7.507   81.759  100.988 1.00 28.49 ? 1161 PHE A CE1   1 
ATOM   8396  C CE2   . PHE A  1 1163 ? 6.748   83.562  102.374 1.00 25.90 ? 1161 PHE A CE2   1 
ATOM   8397  C CZ    . PHE A  1 1163 ? 7.687   83.037  101.516 1.00 29.56 ? 1161 PHE A CZ    1 
ATOM   8398  N N     . ALA A  1 1164 ? 2.194   78.476  102.114 1.00 26.10 ? 1162 ALA A N     1 
ATOM   8399  C CA    . ALA A  1 1164 ? 1.052   77.657  102.498 1.00 26.55 ? 1162 ALA A CA    1 
ATOM   8400  C C     . ALA A  1 1164 ? 1.112   77.258  103.964 1.00 26.41 ? 1162 ALA A C     1 
ATOM   8401  O O     . ALA A  1 1164 ? 0.339   76.399  104.398 1.00 28.71 ? 1162 ALA A O     1 
ATOM   8402  C CB    . ALA A  1 1164 ? 0.968   76.406  101.615 1.00 28.15 ? 1162 ALA A CB    1 
ATOM   8403  N N     . GLY A  1 1165 ? 2.015   77.857  104.725 1.00 23.40 ? 1163 GLY A N     1 
ATOM   8404  C CA    . GLY A  1 1165 ? 2.208   77.506  106.115 1.00 25.28 ? 1163 GLY A CA    1 
ATOM   8405  C C     . GLY A  1 1165 ? 3.560   77.997  106.571 1.00 25.07 ? 1163 GLY A C     1 
ATOM   8406  O O     . GLY A  1 1165 ? 4.389   78.450  105.776 1.00 21.94 ? 1163 GLY A O     1 
ATOM   8407  N N     . ALA A  1 1166 ? 3.783   77.896  107.878 1.00 23.52 ? 1164 ALA A N     1 
ATOM   8408  C CA    . ALA A  1 1166 ? 5.038   78.374  108.432 1.00 22.34 ? 1164 ALA A CA    1 
ATOM   8409  C C     . ALA A  1 1166 ? 5.430   77.505  109.620 1.00 22.55 ? 1164 ALA A C     1 
ATOM   8410  O O     . ALA A  1 1166 ? 4.572   77.029  110.367 1.00 24.45 ? 1164 ALA A O     1 
ATOM   8411  C CB    . ALA A  1 1166 ? 4.947   79.839  108.859 1.00 22.62 ? 1164 ALA A CB    1 
ATOM   8412  N N     . LEU A  1 1167 ? 6.731   77.276  109.759 1.00 22.66 ? 1165 LEU A N     1 
ATOM   8413  C CA    . LEU A  1 1167 ? 7.309   76.611  110.923 1.00 22.84 ? 1165 LEU A CA    1 
ATOM   8414  C C     . LEU A  1 1167 ? 8.307   77.565  111.553 1.00 23.26 ? 1165 LEU A C     1 
ATOM   8415  O O     . LEU A  1 1167 ? 9.199   78.073  110.867 1.00 26.22 ? 1165 LEU A O     1 
ATOM   8416  C CB    . LEU A  1 1167 ? 8.005   75.292  110.561 1.00 22.75 ? 1165 LEU A CB    1 
ATOM   8417  C CG    . LEU A  1 1167 ? 7.111   74.262  109.835 1.00 22.36 ? 1165 LEU A CG    1 
ATOM   8418  C CD1   . LEU A  1 1167 ? 7.939   73.037  109.510 1.00 22.35 ? 1165 LEU A CD1   1 
ATOM   8419  C CD2   . LEU A  1 1167 ? 5.903   73.885  110.686 1.00 22.23 ? 1165 LEU A CD2   1 
ATOM   8420  N N     . VAL A  1 1168 ? 8.156   77.806  112.853 1.00 23.47 ? 1166 VAL A N     1 
ATOM   8421  C CA    . VAL A  1 1168 ? 8.930   78.816  113.563 1.00 23.89 ? 1166 VAL A CA    1 
ATOM   8422  C C     . VAL A  1 1168 ? 9.612   78.160  114.751 1.00 24.13 ? 1166 VAL A C     1 
ATOM   8423  O O     . VAL A  1 1168 ? 9.003   77.340  115.444 1.00 24.02 ? 1166 VAL A O     1 
ATOM   8424  C CB    . VAL A  1 1168 ? 8.033   79.974  114.040 1.00 24.00 ? 1166 VAL A CB    1 
ATOM   8425  C CG1   . VAL A  1 1168 ? 8.872   81.043  114.743 1.00 25.23 ? 1166 VAL A CG1   1 
ATOM   8426  C CG2   . VAL A  1 1168 ? 7.229   80.551  112.875 1.00 23.76 ? 1166 VAL A CG2   1 
ATOM   8427  N N     . GLU A  1 1169 ? 10.870  78.517  114.984 1.00 24.48 ? 1167 GLU A N     1 
ATOM   8428  C CA    . GLU A  1 1169 ? 11.600  78.093  116.173 1.00 24.78 ? 1167 GLU A CA    1 
ATOM   8429  C C     . GLU A  1 1169 ? 12.041  79.322  116.960 1.00 25.38 ? 1167 GLU A C     1 
ATOM   8430  O O     . GLU A  1 1169 ? 12.492  80.311  116.378 1.00 25.37 ? 1167 GLU A O     1 
ATOM   8431  C CB    . GLU A  1 1169 ? 12.806  77.238  115.781 1.00 24.82 ? 1167 GLU A CB    1 
ATOM   8432  C CG    . GLU A  1 1169 ? 13.645  76.701  116.940 1.00 25.14 ? 1167 GLU A CG    1 
ATOM   8433  C CD    . GLU A  1 1169 ? 15.041  76.272  116.489 1.00 27.02 ? 1167 GLU A CD    1 
ATOM   8434  O OE1   . GLU A  1 1169 ? 15.367  76.413  115.285 1.00 26.01 ? 1167 GLU A OE1   1 
ATOM   8435  O OE2   . GLU A  1 1169 ? 15.814  75.795  117.346 1.00 27.61 ? 1167 GLU A OE2   1 
ATOM   8436  N N     . GLY A  1 1170 ? 11.879  79.284  118.272 1.00 25.45 ? 1168 GLY A N     1 
ATOM   8437  C CA    . GLY A  1 1170 ? 12.378  80.375  119.086 1.00 28.25 ? 1168 GLY A CA    1 
ATOM   8438  C C     . GLY A  1 1170 ? 11.751  80.384  120.462 1.00 27.41 ? 1168 GLY A C     1 
ATOM   8439  O O     . GLY A  1 1170 ? 10.877  79.578  120.780 1.00 28.49 ? 1168 GLY A O     1 
ATOM   8440  N N     . ASP A  1 1171 ? 12.234  81.323  121.287 1.00 27.88 ? 1169 ASP A N     1 
ATOM   8441  C CA    . ASP A  1 1171 ? 11.567  81.578  122.552 1.00 29.29 ? 1169 ASP A CA    1 
ATOM   8442  C C     . ASP A  1 1171 ? 10.292  82.379  122.306 1.00 30.58 ? 1169 ASP A C     1 
ATOM   8443  O O     . ASP A  1 1171 ? 9.948   82.723  121.167 1.00 29.29 ? 1169 ASP A O     1 
ATOM   8444  C CB    . ASP A  1 1171 ? 12.506  82.270  123.549 1.00 30.38 ? 1169 ASP A CB    1 
ATOM   8445  C CG    . ASP A  1 1171 ? 13.076  83.598  123.042 1.00 34.70 ? 1169 ASP A CG    1 
ATOM   8446  O OD1   . ASP A  1 1171 ? 12.475  84.272  122.179 1.00 32.06 ? 1169 ASP A OD1   1 
ATOM   8447  O OD2   . ASP A  1 1171 ? 14.161  83.980  123.531 1.00 39.25 ? 1169 ASP A OD2   1 
ATOM   8448  N N     . ALA A  1 1172 ? 9.574   82.667  123.394 1.00 29.48 ? 1170 ALA A N     1 
ATOM   8449  C CA    . ALA A  1 1172 ? 8.250   83.267  123.277 1.00 28.90 ? 1170 ALA A CA    1 
ATOM   8450  C C     . ALA A  1 1172 ? 8.310   84.627  122.588 1.00 30.63 ? 1170 ALA A C     1 
ATOM   8451  O O     . ALA A  1 1172 ? 7.465   84.938  121.739 1.00 27.84 ? 1170 ALA A O     1 
ATOM   8452  C CB    . ALA A  1 1172 ? 7.611   83.384  124.661 1.00 29.59 ? 1170 ALA A CB    1 
ATOM   8453  N N     . GLU A  1 1173 ? 9.317   85.440  122.918 1.00 30.54 ? 1171 GLU A N     1 
ATOM   8454  C CA    . GLU A  1 1173 ? 9.434   86.757  122.295 1.00 29.66 ? 1171 GLU A CA    1 
ATOM   8455  C C     . GLU A  1 1173 ? 9.739   86.642  120.805 1.00 29.81 ? 1171 GLU A C     1 
ATOM   8456  O O     . GLU A  1 1173 ? 9.187   87.396  119.993 1.00 32.79 ? 1171 GLU A O     1 
ATOM   8457  C CB    . GLU A  1 1173 ? 10.513  87.582  123.008 1.00 32.30 ? 1171 GLU A CB    1 
ATOM   8458  N N     . ARG A  1 1174 ? 10.613  85.705  120.424 1.00 30.48 ? 1172 ARG A N     1 
ATOM   8459  C CA    . ARG A  1 1174 ? 10.897  85.507  119.006 1.00 29.49 ? 1172 ARG A CA    1 
ATOM   8460  C C     . ARG A  1 1174 ? 9.671   84.987  118.268 1.00 28.67 ? 1172 ARG A C     1 
ATOM   8461  O O     . ARG A  1 1174 ? 9.374   85.434  117.150 1.00 30.47 ? 1172 ARG A O     1 
ATOM   8462  C CB    . ARG A  1 1174 ? 12.068  84.546  118.824 1.00 28.53 ? 1172 ARG A CB    1 
ATOM   8463  C CG    . ARG A  1 1174 ? 12.326  84.141  117.370 1.00 28.46 ? 1172 ARG A CG    1 
ATOM   8464  C CD    . ARG A  1 1174 ? 12.781  85.334  116.538 1.00 33.61 ? 1172 ARG A CD    1 
ATOM   8465  N NE    . ARG A  1 1174 ? 13.193  84.944  115.195 1.00 32.80 ? 1172 ARG A NE    1 
ATOM   8466  C CZ    . ARG A  1 1174 ? 13.315  85.785  114.178 1.00 36.02 ? 1172 ARG A CZ    1 
ATOM   8467  N NH1   . ARG A  1 1174 ? 13.077  87.081  114.319 1.00 35.39 ? 1172 ARG A NH1   1 
ATOM   8468  N NH2   . ARG A  1 1174 ? 13.670  85.315  112.987 1.00 32.36 ? 1172 ARG A NH2   1 
ATOM   8469  N N     . ILE A  1 1175 ? 8.959   84.031  118.866 1.00 26.98 ? 1173 ILE A N     1 
ATOM   8470  C CA    . ILE A  1 1175 ? 7.758   83.487  118.226 1.00 27.96 ? 1173 ILE A CA    1 
ATOM   8471  C C     . ILE A  1 1175 ? 6.733   84.589  117.996 1.00 26.68 ? 1173 ILE A C     1 
ATOM   8472  O O     . ILE A  1 1175 ? 6.152   84.697  116.913 1.00 25.18 ? 1173 ILE A O     1 
ATOM   8473  C CB    . ILE A  1 1175 ? 7.173   82.332  119.060 1.00 25.82 ? 1173 ILE A CB    1 
ATOM   8474  C CG1   . ILE A  1 1175 ? 8.105   81.116  119.000 1.00 28.33 ? 1173 ILE A CG1   1 
ATOM   8475  C CG2   . ILE A  1 1175 ? 5.760   81.975  118.569 1.00 24.90 ? 1173 ILE A CG2   1 
ATOM   8476  C CD1   . ILE A  1 1175 ? 7.752   79.988  119.958 1.00 26.80 ? 1173 ILE A CD1   1 
ATOM   8477  N N     . ARG A  1 1176 ? 6.505   85.435  119.008 1.00 27.49 ? 1174 ARG A N     1 
ATOM   8478  C CA    A ARG A  1 1176 ? 5.534   86.516  118.864 0.50 27.16 ? 1174 ARG A CA    1 
ATOM   8479  C CA    B ARG A  1 1176 ? 5.528   86.509  118.854 0.50 27.16 ? 1174 ARG A CA    1 
ATOM   8480  C C     . ARG A  1 1176 ? 5.937   87.470  117.746 1.00 26.05 ? 1174 ARG A C     1 
ATOM   8481  O O     . ARG A  1 1176 ? 5.101   87.878  116.933 1.00 29.65 ? 1174 ARG A O     1 
ATOM   8482  C CB    A ARG A  1 1176 ? 5.393   87.270  120.191 0.50 26.66 ? 1174 ARG A CB    1 
ATOM   8483  C CB    B ARG A  1 1176 ? 5.349   87.261  120.174 0.50 26.67 ? 1174 ARG A CB    1 
ATOM   8484  C CG    A ARG A  1 1176 ? 4.164   88.169  120.282 0.50 28.59 ? 1174 ARG A CG    1 
ATOM   8485  C CG    B ARG A  1 1176 ? 4.391   88.442  120.065 0.50 28.84 ? 1174 ARG A CG    1 
ATOM   8486  C CD    A ARG A  1 1176 ? 4.237   89.110  121.491 0.50 29.08 ? 1174 ARG A CD    1 
ATOM   8487  C CD    B ARG A  1 1176 ? 4.248   89.177  121.390 0.50 29.05 ? 1174 ARG A CD    1 
ATOM   8488  N NE    A ARG A  1 1176 ? 4.606   88.411  122.719 0.50 28.31 ? 1174 ARG A NE    1 
ATOM   8489  N NE    B ARG A  1 1176 ? 3.513   90.428  121.257 0.50 28.88 ? 1174 ARG A NE    1 
ATOM   8490  C CZ    A ARG A  1 1176 ? 3.737   87.873  123.566 0.50 31.83 ? 1174 ARG A CZ    1 
ATOM   8491  C CZ    B ARG A  1 1176 ? 4.077   91.611  121.046 0.50 33.16 ? 1174 ARG A CZ    1 
ATOM   8492  N NH1   A ARG A  1 1176 ? 2.431   87.955  123.365 0.50 30.79 ? 1174 ARG A NH1   1 
ATOM   8493  N NH1   B ARG A  1 1176 ? 5.386   91.739  120.913 0.50 31.95 ? 1174 ARG A NH1   1 
ATOM   8494  N NH2   A ARG A  1 1176 ? 4.188   87.241  124.646 0.50 27.43 ? 1174 ARG A NH2   1 
ATOM   8495  N NH2   B ARG A  1 1176 ? 3.307   92.692  120.972 0.50 34.38 ? 1174 ARG A NH2   1 
ATOM   8496  N N     . ALA A  1 1177 ? 7.218   87.830  117.690 1.00 26.31 ? 1175 ALA A N     1 
ATOM   8497  C CA    . ALA A  1 1177 ? 7.701   88.743  116.658 1.00 26.43 ? 1175 ALA A CA    1 
ATOM   8498  C C     . ALA A  1 1177 ? 7.543   88.135  115.268 1.00 25.96 ? 1175 ALA A C     1 
ATOM   8499  O O     . ALA A  1 1177 ? 7.143   88.822  114.321 1.00 27.72 ? 1175 ALA A O     1 
ATOM   8500  C CB    . ALA A  1 1177 ? 9.167   89.092  116.916 1.00 26.85 ? 1175 ALA A CB    1 
ATOM   8501  N N     . VAL A  1 1178 ? 7.879   86.849  115.126 1.00 26.74 ? 1176 VAL A N     1 
ATOM   8502  C CA    . VAL A  1 1178 ? 7.711   86.176  113.837 1.00 25.23 ? 1176 VAL A CA    1 
ATOM   8503  C C     . VAL A  1 1178 ? 6.232   86.059  113.481 1.00 25.55 ? 1176 VAL A C     1 
ATOM   8504  O O     . VAL A  1 1178 ? 5.839   86.304  112.336 1.00 26.90 ? 1176 VAL A O     1 
ATOM   8505  C CB    . VAL A  1 1178 ? 8.396   84.797  113.854 1.00 25.29 ? 1176 VAL A CB    1 
ATOM   8506  C CG1   . VAL A  1 1178 ? 8.114   84.035  112.562 1.00 24.58 ? 1176 VAL A CG1   1 
ATOM   8507  C CG2   . VAL A  1 1178 ? 9.899   84.938  114.056 1.00 25.39 ? 1176 VAL A CG2   1 
ATOM   8508  N N     . ASN A  1 1179 ? 5.395   85.667  114.446 1.00 26.87 ? 1177 ASN A N     1 
ATOM   8509  C CA    . ASN A  1 1179 ? 3.954   85.558  114.205 1.00 26.91 ? 1177 ASN A CA    1 
ATOM   8510  C C     . ASN A  1 1179 ? 3.379   86.874  113.700 1.00 28.21 ? 1177 ASN A C     1 
ATOM   8511  O O     . ASN A  1 1179 ? 2.560   86.896  112.772 1.00 27.38 ? 1177 ASN A O     1 
ATOM   8512  C CB    . ASN A  1 1179 ? 3.260   85.125  115.496 1.00 30.13 ? 1177 ASN A CB    1 
ATOM   8513  C CG    . ASN A  1 1179 ? 1.978   84.362  115.258 1.00 35.97 ? 1177 ASN A CG    1 
ATOM   8514  O OD1   . ASN A  1 1179 ? 1.754   83.795  114.184 1.00 35.35 ? 1177 ASN A OD1   1 
ATOM   8515  N ND2   . ASN A  1 1179 ? 1.121   84.335  116.277 1.00 36.70 ? 1177 ASN A ND2   1 
ATOM   8516  N N     . LYS A  1 1180 ? 3.817   87.988  114.284 1.00 27.06 ? 1178 LYS A N     1 
ATOM   8517  C CA    . LYS A  1 1180 ? 3.340   89.289  113.840 1.00 28.45 ? 1178 LYS A CA    1 
ATOM   8518  C C     . LYS A  1 1180 ? 3.848   89.618  112.442 1.00 28.07 ? 1178 LYS A C     1 
ATOM   8519  O O     . LYS A  1 1180 ? 3.096   90.143  111.617 1.00 30.48 ? 1178 LYS A O     1 
ATOM   8520  C CB    . LYS A  1 1180 ? 3.752   90.362  114.860 1.00 30.44 ? 1178 LYS A CB    1 
ATOM   8521  C CG    . LYS A  1 1180 ? 2.937   90.267  116.144 1.00 29.97 ? 1178 LYS A CG    1 
ATOM   8522  C CD    . LYS A  1 1180 ? 3.477   91.178  117.256 1.00 35.83 ? 1178 LYS A CD    1 
ATOM   8523  C CE    . LYS A  1 1180 ? 2.986   92.614  117.098 1.00 40.84 ? 1178 LYS A CE    1 
ATOM   8524  N NZ    . LYS A  1 1180 ? 1.489   92.725  117.154 1.00 43.28 ? 1178 LYS A NZ    1 
ATOM   8525  N N     . ALA A  1 1181 ? 5.110   89.294  112.143 1.00 27.33 ? 1179 ALA A N     1 
ATOM   8526  C CA    . ALA A  1 1181 ? 5.619   89.524  110.795 1.00 28.39 ? 1179 ALA A CA    1 
ATOM   8527  C C     . ALA A  1 1181 ? 4.887   88.660  109.770 1.00 28.56 ? 1179 ALA A C     1 
ATOM   8528  O O     . ALA A  1 1181 ? 4.602   89.116  108.656 1.00 29.20 ? 1179 ALA A O     1 
ATOM   8529  C CB    . ALA A  1 1181 ? 7.126   89.259  110.742 1.00 27.64 ? 1179 ALA A CB    1 
ATOM   8530  N N     . ILE A  1 1182 ? 4.572   87.411  110.122 1.00 28.06 ? 1180 ILE A N     1 
ATOM   8531  C CA    . ILE A  1 1182 ? 3.869   86.543  109.176 1.00 26.70 ? 1180 ILE A CA    1 
ATOM   8532  C C     . ILE A  1 1182 ? 2.451   87.045  108.931 1.00 27.01 ? 1180 ILE A C     1 
ATOM   8533  O O     . ILE A  1 1182 ? 1.935   86.964  107.807 1.00 28.54 ? 1180 ILE A O     1 
ATOM   8534  C CB    . ILE A  1 1182 ? 3.880   85.087  109.678 1.00 28.29 ? 1180 ILE A CB    1 
ATOM   8535  C CG1   . ILE A  1 1182 ? 5.286   84.510  109.559 1.00 25.36 ? 1180 ILE A CG1   1 
ATOM   8536  C CG2   . ILE A  1 1182 ? 2.861   84.230  108.914 1.00 26.93 ? 1180 ILE A CG2   1 
ATOM   8537  C CD1   . ILE A  1 1182 ? 5.462   83.179  110.305 1.00 27.02 ? 1180 ILE A CD1   1 
ATOM   8538  N N     . ALA A  1 1183 ? 1.797   87.575  109.968 1.00 26.38 ? 1181 ALA A N     1 
ATOM   8539  C CA    . ALA A  1 1183 ? 0.447   88.103  109.800 1.00 31.45 ? 1181 ALA A CA    1 
ATOM   8540  C C     . ALA A  1 1183 ? 0.413   89.275  108.831 1.00 33.31 ? 1181 ALA A C     1 
ATOM   8541  O O     . ALA A  1 1183 ? -0.627  89.525  108.203 1.00 33.15 ? 1181 ALA A O     1 
ATOM   8542  C CB    . ALA A  1 1183 ? -0.130  88.523  111.153 1.00 28.71 ? 1181 ALA A CB    1 
ATOM   8543  N N     . ALA A  1 1184 ? 1.532   89.980  108.673 1.00 30.76 ? 1182 ALA A N     1 
ATOM   8544  C CA    . ALA A  1 1184 ? 1.605   91.098  107.744 1.00 31.06 ? 1182 ALA A CA    1 
ATOM   8545  C C     . ALA A  1 1184 ? 1.865   90.670  106.306 1.00 34.72 ? 1182 ALA A C     1 
ATOM   8546  O O     . ALA A  1 1184 ? 1.847   91.527  105.417 1.00 36.01 ? 1182 ALA A O     1 
ATOM   8547  C CB    . ALA A  1 1184 ? 2.697   92.083  108.180 1.00 36.30 ? 1182 ALA A CB    1 
ATOM   8548  N N     . LEU A  1 1185 ? 2.113   89.389  106.049 1.00 29.15 ? 1183 LEU A N     1 
ATOM   8549  C CA    . LEU A  1 1185 ? 2.378   88.962  104.684 1.00 32.13 ? 1183 LEU A CA    1 
ATOM   8550  C C     . LEU A  1 1185 ? 1.086   89.034  103.880 1.00 33.25 ? 1183 LEU A C     1 
ATOM   8551  O O     . LEU A  1 1185 ? 0.043   88.563  104.350 1.00 33.68 ? 1183 LEU A O     1 
ATOM   8552  C CB    . LEU A  1 1185 ? 2.943   87.546  104.650 1.00 28.49 ? 1183 LEU A CB    1 
ATOM   8553  C CG    . LEU A  1 1185 ? 4.305   87.355  105.314 1.00 30.50 ? 1183 LEU A CG    1 
ATOM   8554  C CD1   . LEU A  1 1185 ? 4.642   85.871  105.406 1.00 29.21 ? 1183 LEU A CD1   1 
ATOM   8555  C CD2   . LEU A  1 1185 ? 5.395   88.116  104.559 1.00 32.79 ? 1183 LEU A CD2   1 
ATOM   8556  N N     . PRO A  1 1186 ? 1.104   89.623  102.685 1.00 34.77 ? 1184 PRO A N     1 
ATOM   8557  C CA    . PRO A  1 1186 ? -0.119  89.667  101.879 1.00 34.21 ? 1184 PRO A CA    1 
ATOM   8558  C C     . PRO A  1 1186 ? -0.508  88.283  101.391 1.00 30.72 ? 1184 PRO A C     1 
ATOM   8559  O O     . PRO A  1 1186 ? 0.323   87.386  101.250 1.00 31.50 ? 1184 PRO A O     1 
ATOM   8560  C CB    . PRO A  1 1186 ? 0.257   90.583  100.707 1.00 38.17 ? 1184 PRO A CB    1 
ATOM   8561  C CG    . PRO A  1 1186 ? 1.743   90.455  100.598 1.00 41.72 ? 1184 PRO A CG    1 
ATOM   8562  C CD    . PRO A  1 1186 ? 2.243   90.270  102.010 1.00 33.26 ? 1184 PRO A CD    1 
ATOM   8563  N N     . GLY A  1 1187 ? -1.795  88.122  101.119 1.00 31.49 ? 1185 GLY A N     1 
ATOM   8564  C CA    . GLY A  1 1187 ? -2.286  86.876  100.588 1.00 32.97 ? 1185 GLY A CA    1 
ATOM   8565  C C     . GLY A  1 1187 ? -2.896  86.004  101.659 1.00 28.61 ? 1185 GLY A C     1 
ATOM   8566  O O     . GLY A  1 1187 ? -3.603  86.486  102.552 1.00 33.44 ? 1185 GLY A O     1 
ATOM   8567  N N     . PRO A  1 1188 ? -2.627  84.701  101.594 1.00 24.51 ? 1186 PRO A N     1 
ATOM   8568  C CA    . PRO A  1 1188 ? -3.338  83.750  102.460 1.00 29.05 ? 1186 PRO A CA    1 
ATOM   8569  C C     . PRO A  1 1188 ? -2.953  83.875  103.926 1.00 28.82 ? 1186 PRO A C     1 
ATOM   8570  O O     . PRO A  1 1188 ? -1.820  84.212  104.272 1.00 28.20 ? 1186 PRO A O     1 
ATOM   8571  C CB    . PRO A  1 1188 ? -2.916  82.385  101.905 1.00 31.24 ? 1186 PRO A CB    1 
ATOM   8572  C CG    . PRO A  1 1188 ? -1.587  82.633  101.274 1.00 35.99 ? 1186 PRO A CG    1 
ATOM   8573  C CD    . PRO A  1 1188 ? -1.674  84.031  100.696 1.00 31.11 ? 1186 PRO A CD    1 
ATOM   8574  N N     . LEU A  1 1189 ? -3.914  83.564  104.794 1.00 27.96 ? 1187 LEU A N     1 
ATOM   8575  C CA    . LEU A  1 1189 ? -3.637  83.444  106.225 1.00 29.17 ? 1187 LEU A CA    1 
ATOM   8576  C C     . LEU A  1 1189 ? -2.844  82.168  106.468 1.00 32.68 ? 1187 LEU A C     1 
ATOM   8577  O O     . LEU A  1 1189 ? -3.367  81.067  106.277 1.00 36.11 ? 1187 LEU A O     1 
ATOM   8578  C CB    . LEU A  1 1189 ? -4.941  83.425  107.018 1.00 30.49 ? 1187 LEU A CB    1 
ATOM   8579  C CG    . LEU A  1 1189 ? -5.634  84.750  107.341 1.00 31.37 ? 1187 LEU A CG    1 
ATOM   8580  C CD1   . LEU A  1 1189 ? -6.093  85.474  106.088 1.00 31.32 ? 1187 LEU A CD1   1 
ATOM   8581  C CD2   . LEU A  1 1189 ? -6.813  84.496  108.257 1.00 32.93 ? 1187 LEU A CD2   1 
ATOM   8582  N N     . LEU A  1 1190 ? -1.587  82.299  106.888 1.00 29.93 ? 1188 LEU A N     1 
ATOM   8583  C CA    . LEU A  1 1190 ? -0.731  81.130  107.039 1.00 30.50 ? 1188 LEU A CA    1 
ATOM   8584  C C     . LEU A  1 1190 ? -1.031  80.420  108.351 1.00 30.87 ? 1188 LEU A C     1 
ATOM   8585  O O     . LEU A  1 1190 ? -1.131  81.056  109.405 1.00 28.98 ? 1188 LEU A O     1 
ATOM   8586  C CB    . LEU A  1 1190 ? 0.745   81.517  106.994 1.00 26.33 ? 1188 LEU A CB    1 
ATOM   8587  C CG    . LEU A  1 1190 ? 1.272   82.214  105.741 1.00 29.37 ? 1188 LEU A CG    1 
ATOM   8588  C CD1   . LEU A  1 1190 ? 2.798   82.176  105.738 1.00 31.13 ? 1188 LEU A CD1   1 
ATOM   8589  C CD2   . LEU A  1 1190 ? 0.704   81.573  104.477 1.00 28.88 ? 1188 LEU A CD2   1 
ATOM   8590  N N     . LEU A  1 1191 ? -1.177  79.103  108.285 1.00 25.81 ? 1189 LEU A N     1 
ATOM   8591  C CA    . LEU A  1 1191 ? -1.215  78.282  109.489 1.00 28.60 ? 1189 LEU A CA    1 
ATOM   8592  C C     . LEU A  1 1191 ? 0.215   78.158  110.008 1.00 28.80 ? 1189 LEU A C     1 
ATOM   8593  O O     . LEU A  1 1191 ? 1.066   77.532  109.361 1.00 28.51 ? 1189 LEU A O     1 
ATOM   8594  C CB    . LEU A  1 1191 ? -1.840  76.924  109.180 1.00 26.02 ? 1189 LEU A CB    1 
ATOM   8595  C CG    . LEU A  1 1191 ? -2.420  76.086  110.324 1.00 27.69 ? 1189 LEU A CG    1 
ATOM   8596  C CD1   . LEU A  1 1191 ? -3.237  74.929  109.756 1.00 28.12 ? 1189 LEU A CD1   1 
ATOM   8597  C CD2   . LEU A  1 1191 ? -1.309  75.550  111.241 1.00 25.60 ? 1189 LEU A CD2   1 
ATOM   8598  N N     . VAL A  1 1192 ? 0.475   78.769  111.178 1.00 28.30 ? 1190 VAL A N     1 
ATOM   8599  C CA    . VAL A  1 1192 ? 1.803   78.877  111.773 1.00 26.20 ? 1190 VAL A CA    1 
ATOM   8600  C C     . VAL A  1 1192 ? 1.927   77.875  112.917 1.00 26.79 ? 1190 VAL A C     1 
ATOM   8601  O O     . VAL A  1 1192 ? 1.021   77.746  113.751 1.00 26.40 ? 1190 VAL A O     1 
ATOM   8602  C CB    . VAL A  1 1192 ? 2.063   80.316  112.278 1.00 23.13 ? 1190 VAL A CB    1 
ATOM   8603  C CG1   . VAL A  1 1192 ? 3.459   80.429  112.897 1.00 25.98 ? 1190 VAL A CG1   1 
ATOM   8604  C CG2   . VAL A  1 1192 ? 1.924   81.330  111.137 1.00 27.99 ? 1190 VAL A CG2   1 
ATOM   8605  N N     . GLN A  1 1193 ? 3.050   77.166  112.964 1.00 23.33 ? 1191 GLN A N     1 
ATOM   8606  C CA    . GLN A  1 1193 ? 3.381   76.308  114.089 1.00 23.69 ? 1191 GLN A CA    1 
ATOM   8607  C C     . GLN A  1 1193 ? 4.700   76.764  114.685 1.00 23.05 ? 1191 GLN A C     1 
ATOM   8608  O O     . GLN A  1 1193 ? 5.657   77.056  113.960 1.00 23.11 ? 1191 GLN A O     1 
ATOM   8609  C CB    . GLN A  1 1193 ? 3.492   74.852  113.679 1.00 24.00 ? 1191 GLN A CB    1 
ATOM   8610  C CG    . GLN A  1 1193 ? 2.188   74.233  113.246 1.00 22.69 ? 1191 GLN A CG    1 
ATOM   8611  C CD    . GLN A  1 1193 ? 2.348   72.750  113.005 1.00 25.92 ? 1191 GLN A CD    1 
ATOM   8612  O OE1   . GLN A  1 1193 ? 2.428   71.965  113.950 1.00 26.29 ? 1191 GLN A OE1   1 
ATOM   8613  N NE2   . GLN A  1 1193 ? 2.436   72.362  111.744 1.00 23.22 ? 1191 GLN A NE2   1 
ATOM   8614  N N     . ALA A  1 1194 ? 4.766   76.796  116.005 1.00 23.33 ? 1192 ALA A N     1 
ATOM   8615  C CA    . ALA A  1 1194 ? 5.947   77.302  116.669 1.00 23.73 ? 1192 ALA A CA    1 
ATOM   8616  C C     . ALA A  1 1194 ? 6.389   76.325  117.743 1.00 25.78 ? 1192 ALA A C     1 
ATOM   8617  O O     . ALA A  1 1194 ? 5.569   75.624  118.347 1.00 23.99 ? 1192 ALA A O     1 
ATOM   8618  C CB    . ALA A  1 1194 ? 5.683   78.668  117.291 1.00 24.18 ? 1192 ALA A CB    1 
ATOM   8619  N N     . ALA A  1 1195 ? 7.698   76.288  117.964 1.00 24.17 ? 1193 ALA A N     1 
ATOM   8620  C CA    . ALA A  1 1195 ? 8.267   75.461  119.010 1.00 24.67 ? 1193 ALA A CA    1 
ATOM   8621  C C     . ALA A  1 1195 ? 9.560   76.100  119.489 1.00 28.70 ? 1193 ALA A C     1 
ATOM   8622  O O     . ALA A  1 1195 ? 10.261  76.767  118.722 1.00 26.63 ? 1193 ALA A O     1 
ATOM   8623  C CB    . ALA A  1 1195 ? 8.525   74.036  118.516 1.00 25.89 ? 1193 ALA A CB    1 
ATOM   8624  N N     . SER A  1 1196 ? 9.873   75.884  120.761 1.00 25.15 ? 1194 SER A N     1 
ATOM   8625  C CA    . SER A  1 1196 ? 11.181  76.271  121.256 1.00 28.26 ? 1194 SER A CA    1 
ATOM   8626  C C     . SER A  1 1196 ? 12.233  75.281  120.768 1.00 27.52 ? 1194 SER A C     1 
ATOM   8627  O O     . SER A  1 1196 ? 11.919  74.172  120.324 1.00 25.86 ? 1194 SER A O     1 
ATOM   8628  C CB    . SER A  1 1196 ? 11.183  76.323  122.783 1.00 31.91 ? 1194 SER A CB    1 
ATOM   8629  O OG    . SER A  1 1196 ? 10.966  75.028  123.325 1.00 30.57 ? 1194 SER A OG    1 
ATOM   8630  N N     . SER A  1 1197 ? 13.497  75.694  120.854 1.00 30.30 ? 1195 SER A N     1 
ATOM   8631  C CA    . SER A  1 1197 ? 14.574  74.757  120.560 1.00 30.17 ? 1195 SER A CA    1 
ATOM   8632  C C     . SER A  1 1197 ? 14.485  73.540  121.469 1.00 30.11 ? 1195 SER A C     1 
ATOM   8633  O O     . SER A  1 1197 ? 14.720  72.409  121.031 1.00 25.78 ? 1195 SER A O     1 
ATOM   8634  C CB    . SER A  1 1197 ? 15.930  75.440  120.717 1.00 31.17 ? 1195 SER A CB    1 
ATOM   8635  O OG    . SER A  1 1197 ? 16.065  76.500  119.790 1.00 31.82 ? 1195 SER A OG    1 
ATOM   8636  N N     . GLY A  1 1198 ? 14.130  73.754  122.737 1.00 29.89 ? 1196 GLY A N     1 
ATOM   8637  C CA    . GLY A  1 1198 ? 14.062  72.642  123.671 1.00 28.94 ? 1196 GLY A CA    1 
ATOM   8638  C C     . GLY A  1 1198 ? 12.906  71.709  123.375 1.00 30.14 ? 1196 GLY A C     1 
ATOM   8639  O O     . GLY A  1 1198 ? 13.030  70.491  123.523 1.00 26.74 ? 1196 GLY A O     1 
ATOM   8640  N N     . GLU A  1 1199 ? 11.769  72.266  122.945 1.00 26.00 ? 1197 GLU A N     1 
ATOM   8641  C CA    . GLU A  1 1199 ? 10.638  71.431  122.550 1.00 26.81 ? 1197 GLU A CA    1 
ATOM   8642  C C     . GLU A  1 1199 ? 10.972  70.587  121.329 1.00 30.98 ? 1197 GLU A C     1 
ATOM   8643  O O     . GLU A  1 1199 ? 10.517  69.440  121.214 1.00 26.04 ? 1197 GLU A O     1 
ATOM   8644  C CB    . GLU A  1 1199 ? 9.414   72.299  122.272 1.00 27.81 ? 1197 GLU A CB    1 
ATOM   8645  C CG    . GLU A  1 1199 ? 8.123   71.504  122.059 1.00 33.91 ? 1197 GLU A CG    1 
ATOM   8646  C CD    . GLU A  1 1199 ? 7.506   71.002  123.363 1.00 38.76 ? 1197 GLU A CD    1 
ATOM   8647  O OE1   . GLU A  1 1199 ? 8.121   71.189  124.433 1.00 37.69 ? 1197 GLU A OE1   1 
ATOM   8648  O OE2   . GLU A  1 1199 ? 6.392   70.431  123.315 1.00 47.37 ? 1197 GLU A OE2   1 
ATOM   8649  N N     . ILE A  1 1200 ? 11.741  71.145  120.387 1.00 26.32 ? 1198 ILE A N     1 
ATOM   8650  C CA    . ILE A  1 1200 ? 12.161  70.350  119.237 1.00 25.94 ? 1198 ILE A CA    1 
ATOM   8651  C C     . ILE A  1 1200 ? 13.008  69.172  119.696 1.00 25.40 ? 1198 ILE A C     1 
ATOM   8652  O O     . ILE A  1 1200 ? 12.918  68.073  119.138 1.00 27.95 ? 1198 ILE A O     1 
ATOM   8653  C CB    . ILE A  1 1200 ? 12.902  71.231  118.209 1.00 27.05 ? 1198 ILE A CB    1 
ATOM   8654  C CG1   . ILE A  1 1200 ? 11.931  72.231  117.562 1.00 24.43 ? 1198 ILE A CG1   1 
ATOM   8655  C CG2   . ILE A  1 1200 ? 13.573  70.374  117.122 1.00 25.27 ? 1198 ILE A CG2   1 
ATOM   8656  C CD1   . ILE A  1 1200 ? 12.596  73.185  116.603 1.00 24.48 ? 1198 ILE A CD1   1 
ATOM   8657  N N     . ALA A  1 1201 ? 13.838  69.377  120.725 1.00 26.07 ? 1199 ALA A N     1 
ATOM   8658  C CA    . ALA A  1 1201 ? 14.689  68.296  121.209 1.00 27.81 ? 1199 ALA A CA    1 
ATOM   8659  C C     . ALA A  1 1201 ? 13.886  67.256  121.985 1.00 27.00 ? 1199 ALA A C     1 
ATOM   8660  O O     . ALA A  1 1201 ? 14.176  66.055  121.902 1.00 26.39 ? 1199 ALA A O     1 
ATOM   8661  C CB    . ALA A  1 1201 ? 15.814  68.863  122.081 1.00 27.10 ? 1199 ALA A CB    1 
ATOM   8662  N N     . ARG A  1 1202 ? 12.875  67.692  122.740 1.00 25.59 ? 1200 ARG A N     1 
ATOM   8663  C CA    . ARG A  1 1202 ? 12.146  66.799  123.634 1.00 28.31 ? 1200 ARG A CA    1 
ATOM   8664  C C     . ARG A  1 1202 ? 10.980  66.092  122.958 1.00 29.52 ? 1200 ARG A C     1 
ATOM   8665  O O     . ARG A  1 1202 ? 10.758  64.901  123.201 1.00 29.98 ? 1200 ARG A O     1 
ATOM   8666  C CB    . ARG A  1 1202 ? 11.623  67.574  124.843 1.00 25.95 ? 1200 ARG A CB    1 
ATOM   8667  C CG    . ARG A  1 1202 ? 12.709  68.007  125.819 1.00 29.42 ? 1200 ARG A CG    1 
ATOM   8668  C CD    . ARG A  1 1202 ? 12.061  68.614  127.057 1.00 29.59 ? 1200 ARG A CD    1 
ATOM   8669  N NE    . ARG A  1 1202 ? 11.211  69.734  126.692 1.00 27.16 ? 1200 ARG A NE    1 
ATOM   8670  C CZ    . ARG A  1 1202 ? 11.606  71.000  126.646 1.00 29.63 ? 1200 ARG A CZ    1 
ATOM   8671  N NH1   . ARG A  1 1202 ? 12.805  71.375  127.083 1.00 27.19 ? 1200 ARG A NH1   1 
ATOM   8672  N NH2   . ARG A  1 1202 ? 10.780  71.914  126.145 1.00 29.99 ? 1200 ARG A NH2   1 
ATOM   8673  N N     . ASN A  1 1203 ? 10.233  66.800  122.114 1.00 28.05 ? 1201 ASN A N     1 
ATOM   8674  C CA    . ASN A  1 1203 ? 8.951   66.311  121.630 1.00 28.40 ? 1201 ASN A CA    1 
ATOM   8675  C C     . ASN A  1 1203 ? 9.021   65.961  120.147 1.00 33.18 ? 1201 ASN A C     1 
ATOM   8676  O O     . ASN A  1 1203 ? 9.198   66.860  119.304 1.00 29.40 ? 1201 ASN A O     1 
ATOM   8677  C CB    . ASN A  1 1203 ? 7.877   67.368  121.889 1.00 28.05 ? 1201 ASN A CB    1 
ATOM   8678  C CG    . ASN A  1 1203 ? 6.497   66.924  121.452 1.00 33.51 ? 1201 ASN A CG    1 
ATOM   8679  O OD1   . ASN A  1 1203 ? 6.304   65.786  121.037 1.00 30.70 ? 1201 ASN A OD1   1 
ATOM   8680  N ND2   . ASN A  1 1203 ? 5.526   67.828  121.550 1.00 36.28 ? 1201 ASN A ND2   1 
ATOM   8681  N N     . PRO A  1 1204 ? 8.874   64.686  119.779 1.00 31.12 ? 1202 PRO A N     1 
ATOM   8682  C CA    . PRO A  1 1204 ? 8.867   64.333  118.348 1.00 29.92 ? 1202 PRO A CA    1 
ATOM   8683  C C     . PRO A  1 1204 ? 7.721   64.959  117.586 1.00 31.16 ? 1202 PRO A C     1 
ATOM   8684  O O     . PRO A  1 1204 ? 7.809   65.094  116.357 1.00 30.79 ? 1202 PRO A O     1 
ATOM   8685  C CB    . PRO A  1 1204 ? 8.764   62.800  118.359 1.00 32.17 ? 1202 PRO A CB    1 
ATOM   8686  C CG    . PRO A  1 1204 ? 8.282   62.440  119.740 1.00 36.96 ? 1202 PRO A CG    1 
ATOM   8687  C CD    . PRO A  1 1204 ? 8.783   63.505  120.657 1.00 29.40 ? 1202 PRO A CD    1 
ATOM   8688  N N     . ASP A  1 1205 ? 6.644   65.336  118.273 1.00 29.78 ? 1203 ASP A N     1 
ATOM   8689  C CA    . ASP A  1 1205 ? 5.511   66.008  117.657 1.00 30.99 ? 1203 ASP A CA    1 
ATOM   8690  C C     . ASP A  1 1205 ? 5.527   67.515  117.906 1.00 30.85 ? 1203 ASP A C     1 
ATOM   8691  O O     . ASP A  1 1205 ? 4.462   68.146  117.902 1.00 30.01 ? 1203 ASP A O     1 
ATOM   8692  C CB    . ASP A  1 1205 ? 4.208   65.390  118.168 1.00 31.77 ? 1203 ASP A CB    1 
ATOM   8693  C CG    . ASP A  1 1205 ? 4.184   63.878  118.015 1.00 34.70 ? 1203 ASP A CG    1 
ATOM   8694  O OD1   . ASP A  1 1205 ? 4.507   63.380  116.913 1.00 35.91 ? 1203 ASP A OD1   1 
ATOM   8695  O OD2   . ASP A  1 1205 ? 3.870   63.186  119.010 1.00 41.58 ? 1203 ASP A OD2   1 
ATOM   8696  N N     . ALA A  1 1206 ? 6.710   68.097  118.158 1.00 25.69 ? 1204 ALA A N     1 
ATOM   8697  C CA    . ALA A  1 1206 ? 6.814   69.550  118.300 1.00 25.94 ? 1204 ALA A CA    1 
ATOM   8698  C C     . ALA A  1 1206 ? 6.074   70.261  117.177 1.00 29.90 ? 1204 ALA A C     1 
ATOM   8699  O O     . ALA A  1 1206 ? 5.321   71.212  117.416 1.00 25.46 ? 1204 ALA A O     1 
ATOM   8700  C CB    . ALA A  1 1206 ? 8.282   69.980  118.318 1.00 24.37 ? 1204 ALA A CB    1 
ATOM   8701  N N     . TYR A  1 1207 ? 6.275   69.809  115.944 1.00 26.98 ? 1205 TYR A N     1 
ATOM   8702  C CA    . TYR A  1 1207 ? 5.477   70.244  114.810 1.00 22.59 ? 1205 TYR A CA    1 
ATOM   8703  C C     . TYR A  1 1207 ? 4.524   69.119  114.454 1.00 29.22 ? 1205 TYR A C     1 
ATOM   8704  O O     . TYR A  1 1207 ? 4.881   67.940  114.536 1.00 31.54 ? 1205 TYR A O     1 
ATOM   8705  C CB    . TYR A  1 1207 ? 6.357   70.610  113.613 1.00 25.71 ? 1205 TYR A CB    1 
ATOM   8706  C CG    . TYR A  1 1207 ? 7.304   71.730  113.940 1.00 24.97 ? 1205 TYR A CG    1 
ATOM   8707  C CD1   . TYR A  1 1207 ? 6.811   72.998  114.261 1.00 26.12 ? 1205 TYR A CD1   1 
ATOM   8708  C CD2   . TYR A  1 1207 ? 8.680   71.519  113.991 1.00 26.91 ? 1205 TYR A CD2   1 
ATOM   8709  C CE1   . TYR A  1 1207 ? 7.657   74.038  114.583 1.00 23.21 ? 1205 TYR A CE1   1 
ATOM   8710  C CE2   . TYR A  1 1207 ? 9.552   72.563  114.320 1.00 25.52 ? 1205 TYR A CE2   1 
ATOM   8711  C CZ    . TYR A  1 1207 ? 9.021   73.819  114.617 1.00 23.72 ? 1205 TYR A CZ    1 
ATOM   8712  O OH    . TYR A  1 1207 ? 9.853   74.858  114.948 1.00 23.77 ? 1205 TYR A OH    1 
ATOM   8713  N N     . CYS A  1 1208 ? 3.299   69.473  114.112 1.00 23.11 ? 1206 CYS A N     1 
ATOM   8714  C CA    . CYS A  1 1208 ? 2.299   68.466  113.822 1.00 25.78 ? 1206 CYS A CA    1 
ATOM   8715  C C     . CYS A  1 1208 ? 2.152   68.362  112.311 1.00 24.46 ? 1206 CYS A C     1 
ATOM   8716  O O     . CYS A  1 1208 ? 1.978   69.378  111.621 1.00 23.56 ? 1206 CYS A O     1 
ATOM   8717  C CB    . CYS A  1 1208 ? 0.971   68.802  114.497 1.00 29.06 ? 1206 CYS A CB    1 
ATOM   8718  S SG    . CYS A  1 1208 ? -0.351  67.654  114.075 1.00 31.19 ? 1206 CYS A SG    1 
ATOM   8719  N N     . LEU A  1 1209 ? 2.278   67.142  111.797 1.00 21.42 ? 1207 LEU A N     1 
ATOM   8720  C CA    . LEU A  1 1209 ? 2.232   66.952  110.355 1.00 21.17 ? 1207 LEU A CA    1 
ATOM   8721  C C     . LEU A  1 1209 ? 0.817   67.034  109.793 1.00 21.66 ? 1207 LEU A C     1 
ATOM   8722  O O     . LEU A  1 1209 ? 0.672   67.149  108.566 1.00 21.31 ? 1207 LEU A O     1 
ATOM   8723  C CB    . LEU A  1 1209 ? 2.870   65.610  109.988 1.00 21.20 ? 1207 LEU A CB    1 
ATOM   8724  C CG    . LEU A  1 1209 ? 4.347   65.381  110.390 1.00 21.49 ? 1207 LEU A CG    1 
ATOM   8725  C CD1   . LEU A  1 1209 ? 4.858   64.081  109.801 1.00 22.36 ? 1207 LEU A CD1   1 
ATOM   8726  C CD2   . LEU A  1 1209 ? 5.231   66.531  109.942 1.00 21.57 ? 1207 LEU A CD2   1 
ATOM   8727  N N     . ASN A  1 1210 ? -0.229  66.987  110.637 1.00 21.53 ? 1208 ASN A N     1 
ATOM   8728  C CA    . ASN A  1 1210 ? -1.590  67.178  110.124 1.00 22.29 ? 1208 ASN A CA    1 
ATOM   8729  C C     . ASN A  1 1210 ? -1.709  68.507  109.395 1.00 23.05 ? 1208 ASN A C     1 
ATOM   8730  O O     . ASN A  1 1210 ? -2.438  68.621  108.408 1.00 21.72 ? 1208 ASN A O     1 
ATOM   8731  C CB    . ASN A  1 1210 ? -2.643  67.163  111.247 1.00 24.37 ? 1208 ASN A CB    1 
ATOM   8732  C CG    . ASN A  1 1210 ? -2.712  65.858  112.006 1.00 32.96 ? 1208 ASN A CG    1 
ATOM   8733  O OD1   . ASN A  1 1210 ? -1.977  64.907  111.736 1.00 37.91 ? 1208 ASN A OD1   1 
ATOM   8734  N ND2   . ASN A  1 1210 ? -3.597  65.822  113.001 1.00 38.09 ? 1208 ASN A ND2   1 
ATOM   8735  N N     . TRP A  1 1211 ? -1.047  69.544  109.902 1.00 21.06 ? 1209 TRP A N     1 
ATOM   8736  C CA    . TRP A  1 1211 ? -1.242  70.886  109.362 1.00 23.68 ? 1209 TRP A CA    1 
ATOM   8737  C C     . TRP A  1 1211 ? -0.257  71.232  108.250 1.00 23.51 ? 1209 TRP A C     1 
ATOM   8738  O O     . TRP A  1 1211 ? -0.227  72.384  107.813 1.00 27.88 ? 1209 TRP A O     1 
ATOM   8739  C CB    . TRP A  1 1211 ? -1.168  71.925  110.496 1.00 23.41 ? 1209 TRP A CB    1 
ATOM   8740  C CG    . TRP A  1 1211 ? -1.786  71.423  111.779 1.00 23.52 ? 1209 TRP A CG    1 
ATOM   8741  C CD1   . TRP A  1 1211 ? -1.186  71.360  113.013 1.00 27.15 ? 1209 TRP A CD1   1 
ATOM   8742  C CD2   . TRP A  1 1211 ? -3.096  70.861  111.947 1.00 24.96 ? 1209 TRP A CD2   1 
ATOM   8743  N NE1   . TRP A  1 1211 ? -2.056  70.823  113.936 1.00 26.89 ? 1209 TRP A NE1   1 
ATOM   8744  C CE2   . TRP A  1 1211 ? -3.228  70.497  113.303 1.00 23.97 ? 1209 TRP A CE2   1 
ATOM   8745  C CE3   . TRP A  1 1211 ? -4.178  70.637  111.080 1.00 25.30 ? 1209 TRP A CE3   1 
ATOM   8746  C CZ2   . TRP A  1 1211 ? -4.392  69.927  113.813 1.00 25.33 ? 1209 TRP A CZ2   1 
ATOM   8747  C CZ3   . TRP A  1 1211 ? -5.334  70.062  111.593 1.00 24.42 ? 1209 TRP A CZ3   1 
ATOM   8748  C CH2   . TRP A  1 1211 ? -5.431  69.713  112.938 1.00 22.12 ? 1209 TRP A CH2   1 
ATOM   8749  N N     . LEU A  1 1212 ? 0.535   70.266  107.777 1.00 20.66 ? 1210 LEU A N     1 
ATOM   8750  C CA    . LEU A  1 1212 ? 1.483   70.478  106.688 1.00 20.68 ? 1210 LEU A CA    1 
ATOM   8751  C C     . LEU A  1 1212 ? 1.069   69.784  105.398 1.00 20.42 ? 1210 LEU A C     1 
ATOM   8752  O O     . LEU A  1 1212 ? 1.835   69.803  104.424 1.00 20.45 ? 1210 LEU A O     1 
ATOM   8753  C CB    . LEU A  1 1212 ? 2.884   70.011  107.101 1.00 21.13 ? 1210 LEU A CB    1 
ATOM   8754  C CG    . LEU A  1 1212 ? 3.549   70.937  108.120 1.00 21.22 ? 1210 LEU A CG    1 
ATOM   8755  C CD1   . LEU A  1 1212 ? 4.776   70.280  108.764 1.00 23.83 ? 1210 LEU A CD1   1 
ATOM   8756  C CD2   . LEU A  1 1212 ? 3.924   72.261  107.446 1.00 21.29 ? 1210 LEU A CD2   1 
ATOM   8757  N N     . VAL A  1 1213 ? -0.096  69.144  105.383 1.00 20.22 ? 1211 VAL A N     1 
ATOM   8758  C CA    . VAL A  1 1213 ? -0.669  68.588  104.168 1.00 21.45 ? 1211 VAL A CA    1 
ATOM   8759  C C     . VAL A  1 1213 ? -1.943  69.361  103.870 1.00 21.73 ? 1211 VAL A C     1 
ATOM   8760  O O     . VAL A  1 1213 ? -2.495  70.060  104.723 1.00 20.09 ? 1211 VAL A O     1 
ATOM   8761  C CB    . VAL A  1 1213 ? -0.963  67.072  104.277 1.00 22.42 ? 1211 VAL A CB    1 
ATOM   8762  C CG1   . VAL A  1 1213 ? 0.324   66.278  104.450 1.00 24.65 ? 1211 VAL A CG1   1 
ATOM   8763  C CG2   . VAL A  1 1213 ? -1.942  66.782  105.426 1.00 19.89 ? 1211 VAL A CG2   1 
ATOM   8764  N N     . GLU A  1 1214 ? -2.434  69.193  102.647 1.00 21.21 ? 1212 GLU A N     1 
ATOM   8765  C CA    . GLU A  1 1214 ? -3.630  69.858  102.162 1.00 24.69 ? 1212 GLU A CA    1 
ATOM   8766  C C     . GLU A  1 1214 ? -4.676  68.794  101.883 1.00 19.23 ? 1212 GLU A C     1 
ATOM   8767  O O     . GLU A  1 1214 ? -4.384  67.819  101.182 1.00 19.17 ? 1212 GLU A O     1 
ATOM   8768  C CB    . GLU A  1 1214 ? -3.344  70.646  100.876 1.00 22.10 ? 1212 GLU A CB    1 
ATOM   8769  N N     . GLU A  1 1215 ? -5.869  68.967  102.456 1.00 20.13 ? 1213 GLU A N     1 
ATOM   8770  C CA    . GLU A  1 1215 ? -6.989  68.071  102.203 1.00 20.17 ? 1213 GLU A CA    1 
ATOM   8771  C C     . GLU A  1 1215 ? -7.676  68.467  100.914 1.00 19.65 ? 1213 GLU A C     1 
ATOM   8772  O O     . GLU A  1 1215 ? -7.952  69.650  100.692 1.00 20.68 ? 1213 GLU A O     1 
ATOM   8773  C CB    . GLU A  1 1215 ? -8.013  68.143  103.325 1.00 19.07 ? 1213 GLU A CB    1 
ATOM   8774  C CG    . GLU A  1 1215 ? -7.505  67.747  104.682 1.00 19.19 ? 1213 GLU A CG    1 
ATOM   8775  C CD    . GLU A  1 1215 ? -8.489  68.116  105.759 1.00 19.21 ? 1213 GLU A CD    1 
ATOM   8776  O OE1   . GLU A  1 1215 ? -8.560  69.312  106.103 1.00 21.25 ? 1213 GLU A OE1   1 
ATOM   8777  O OE2   . GLU A  1 1215 ? -9.189  67.214  106.249 1.00 19.47 ? 1213 GLU A OE2   1 
ATOM   8778  N N     . VAL A  1 1216 ? -7.979  67.479  100.080 1.00 18.65 ? 1214 VAL A N     1 
ATOM   8779  C CA    . VAL A  1 1216 ? -8.746  67.705  98.861  1.00 18.49 ? 1214 VAL A CA    1 
ATOM   8780  C C     . VAL A  1 1216 ? -9.924  66.739  98.852  1.00 18.55 ? 1214 VAL A C     1 
ATOM   8781  O O     . VAL A  1 1216 ? -9.764  65.541  99.100  1.00 18.37 ? 1214 VAL A O     1 
ATOM   8782  C CB    . VAL A  1 1216 ? -7.872  67.540  97.603  1.00 20.00 ? 1214 VAL A CB    1 
ATOM   8783  C CG1   . VAL A  1 1216 ? -8.691  67.736  96.326  1.00 22.05 ? 1214 VAL A CG1   1 
ATOM   8784  C CG2   . VAL A  1 1216 ? -6.719  68.541  97.610  1.00 22.37 ? 1214 VAL A CG2   1 
ATOM   8785  N N     . SER A  1 1217 ? -11.107 67.261  98.556  1.00 18.93 ? 1215 SER A N     1 
ATOM   8786  C CA    . SER A  1 1217 ? -12.306 66.455  98.414  1.00 19.45 ? 1215 SER A CA    1 
ATOM   8787  C C     . SER A  1 1217 ? -12.706 66.543  96.958  1.00 19.80 ? 1215 SER A C     1 
ATOM   8788  O O     . SER A  1 1217 ? -12.641 67.629  96.379  1.00 18.42 ? 1215 SER A O     1 
ATOM   8789  C CB    . SER A  1 1217 ? -13.425 66.972  99.319  1.00 19.85 ? 1215 SER A CB    1 
ATOM   8790  O OG    . SER A  1 1217 ? -14.688 66.505  98.886  1.00 24.24 ? 1215 SER A OG    1 
ATOM   8791  N N     . ALA A  1 1218 ? -13.002 65.399  96.348  1.00 18.26 ? 1216 ALA A N     1 
ATOM   8792  C CA    . ALA A  1 1218 ? -13.494 65.345  94.973  1.00 19.24 ? 1216 ALA A CA    1 
ATOM   8793  C C     . ALA A  1 1218 ? -14.779 64.535  94.944  1.00 17.71 ? 1216 ALA A C     1 
ATOM   8794  O O     . ALA A  1 1218 ? -14.814 63.405  95.437  1.00 18.62 ? 1216 ALA A O     1 
ATOM   8795  C CB    . ALA A  1 1218 ? -12.462 64.722  94.030  1.00 18.01 ? 1216 ALA A CB    1 
ATOM   8796  N N     . SER A  1 1219 ? -15.831 65.093  94.336  1.00 18.51 ? 1217 SER A N     1 
ATOM   8797  C CA    . SER A  1 1219 ? -17.126 64.435  94.267  1.00 18.18 ? 1217 SER A CA    1 
ATOM   8798  C C     . SER A  1 1219 ? -17.471 64.276  92.798  1.00 18.24 ? 1217 SER A C     1 
ATOM   8799  O O     . SER A  1 1219 ? -17.617 65.278  92.094  1.00 20.05 ? 1217 SER A O     1 
ATOM   8800  C CB    . SER A  1 1219 ? -18.203 65.247  94.992  1.00 19.65 ? 1217 SER A CB    1 
ATOM   8801  O OG    . SER A  1 1219 ? -19.459 64.608  94.912  1.00 20.00 ? 1217 SER A OG    1 
ATOM   8802  N N     . ILE A  1 1220 ? -17.578 63.030  92.341  1.00 17.90 ? 1218 ILE A N     1 
ATOM   8803  C CA    . ILE A  1 1220 ? -17.803 62.728  90.931  1.00 19.27 ? 1218 ILE A CA    1 
ATOM   8804  C C     . ILE A  1 1220 ? -19.185 62.116  90.765  1.00 17.92 ? 1218 ILE A C     1 
ATOM   8805  O O     . ILE A  1 1220 ? -19.513 61.102  91.393  1.00 20.76 ? 1218 ILE A O     1 
ATOM   8806  C CB    . ILE A  1 1220 ? -16.729 61.785  90.362  1.00 19.15 ? 1218 ILE A CB    1 
ATOM   8807  C CG1   . ILE A  1 1220 ? -15.324 62.377  90.544  1.00 25.80 ? 1218 ILE A CG1   1 
ATOM   8808  C CG2   . ILE A  1 1220 ? -17.022 61.502  88.893  1.00 22.24 ? 1218 ILE A CG2   1 
ATOM   8809  C CD1   . ILE A  1 1220 ? -14.531 61.758  91.657  1.00 27.53 ? 1218 ILE A CD1   1 
ATOM   8810  N N     . ASN A  1 1221 ? -19.982 62.716  89.889  1.00 20.71 ? 1219 ASN A N     1 
ATOM   8811  C CA    . ASN A  1 1221 ? -21.299 62.199  89.558  1.00 21.36 ? 1219 ASN A CA    1 
ATOM   8812  C C     . ASN A  1 1221 ? -21.111 61.085  88.538  1.00 22.88 ? 1219 ASN A C     1 
ATOM   8813  O O     . ASN A  1 1221 ? -20.791 61.349  87.381  1.00 24.73 ? 1219 ASN A O     1 
ATOM   8814  C CB    . ASN A  1 1221 ? -22.172 63.327  89.018  1.00 22.05 ? 1219 ASN A CB    1 
ATOM   8815  C CG    . ASN A  1 1221 ? -23.536 62.850  88.540  1.00 24.40 ? 1219 ASN A CG    1 
ATOM   8816  O OD1   . ASN A  1 1221 ? -23.943 61.707  88.773  1.00 22.31 ? 1219 ASN A OD1   1 
ATOM   8817  N ND2   . ASN A  1 1221 ? -24.252 63.742  87.867  1.00 24.64 ? 1219 ASN A ND2   1 
ATOM   8818  N N     . THR A  1 1222 ? -21.278 59.840  88.975  1.00 22.28 ? 1220 THR A N     1 
ATOM   8819  C CA    . THR A  1 1222 ? -21.117 58.678  88.116  1.00 25.57 ? 1220 THR A CA    1 
ATOM   8820  C C     . THR A  1 1222 ? -22.442 58.184  87.552  1.00 31.31 ? 1220 THR A C     1 
ATOM   8821  O O     . THR A  1 1222 ? -22.479 57.130  86.906  1.00 28.86 ? 1220 THR A O     1 
ATOM   8822  C CB    . THR A  1 1222 ? -20.422 57.549  88.874  1.00 28.05 ? 1220 THR A CB    1 
ATOM   8823  O OG1   . THR A  1 1222 ? -21.208 57.201  90.019  1.00 23.94 ? 1220 THR A OG1   1 
ATOM   8824  C CG2   . THR A  1 1222 ? -19.033 57.986  89.323  1.00 25.58 ? 1220 THR A CG2   1 
ATOM   8825  N N     . ALA A  1 1223 ? -23.526 58.913  87.779  1.00 23.13 ? 1221 ALA A N     1 
ATOM   8826  C CA    . ALA A  1 1223 ? -24.766 58.630  87.070  1.00 28.82 ? 1221 ALA A CA    1 
ATOM   8827  C C     . ALA A  1 1223 ? -24.906 59.465  85.808  1.00 39.24 ? 1221 ALA A C     1 
ATOM   8828  O O     . ALA A  1 1223 ? -25.891 59.304  85.082  1.00 47.17 ? 1221 ALA A O     1 
ATOM   8829  C CB    . ALA A  1 1223 ? -25.968 58.869  87.985  1.00 26.44 ? 1221 ALA A CB    1 
ATOM   8830  N N     . ALA A  1 1224 ? -23.930 60.344  85.532  1.00 54.41 ? 1222 ALA A N     1 
ATOM   8831  C CA    . ALA A  1 1224 ? -23.889 61.382  84.501  1.00 54.52 ? 1222 ALA A CA    1 
ATOM   8832  C C     . ALA A  1 1224 ? -23.843 60.837  83.065  1.00 64.18 ? 1222 ALA A C     1 
ATOM   8833  O O     . ALA A  1 1224 ? -23.663 61.658  82.156  1.00 67.57 ? 1222 ALA A O     1 
ATOM   8834  C CB    . ALA A  1 1224 ? -22.691 62.299  84.752  1.00 48.56 ? 1222 ALA A CB    1 
ATOM   8835  N N     . ALA A  1 1225 ? -23.973 59.535  82.818  1.00 55.62 ? 1223 ALA A N     1 
ATOM   8836  C CA    . ALA A  1 1225 ? -24.114 59.020  81.457  1.00 55.64 ? 1223 ALA A CA    1 
ATOM   8837  C C     . ALA A  1 1225 ? -25.191 57.940  81.408  1.00 59.17 ? 1223 ALA A C     1 
ATOM   8838  O O     . ALA A  1 1225 ? -26.373 58.237  81.236  1.00 64.19 ? 1223 ALA A O     1 
ATOM   8839  C CB    . ALA A  1 1225 ? -22.787 58.475  80.940  1.00 46.15 ? 1223 ALA A CB    1 
ATOM   8840  N N     . ALA B  1 16   ? 30.220  4.332   81.146  1.00 50.45 ? 14   ALA B N     1 
ATOM   8841  C CA    . ALA B  1 16   ? 29.257  5.422   81.286  1.00 55.68 ? 14   ALA B CA    1 
ATOM   8842  C C     . ALA B  1 16   ? 27.828  4.897   81.244  1.00 58.31 ? 14   ALA B C     1 
ATOM   8843  O O     . ALA B  1 16   ? 27.478  4.125   80.349  1.00 60.62 ? 14   ALA B O     1 
ATOM   8844  C CB    . ALA B  1 16   ? 29.466  6.467   80.192  1.00 51.14 ? 14   ALA B CB    1 
ATOM   8845  N N     . PRO B  1 17   ? 27.002  5.319   82.203  1.00 52.73 ? 15   PRO B N     1 
ATOM   8846  C CA    . PRO B  1 17   ? 25.599  4.883   82.206  1.00 49.77 ? 15   PRO B CA    1 
ATOM   8847  C C     . PRO B  1 17   ? 24.881  5.339   80.944  1.00 49.30 ? 15   PRO B C     1 
ATOM   8848  O O     . PRO B  1 17   ? 25.118  6.437   80.434  1.00 49.33 ? 15   PRO B O     1 
ATOM   8849  C CB    . PRO B  1 17   ? 25.017  5.554   83.456  1.00 50.18 ? 15   PRO B CB    1 
ATOM   8850  C CG    . PRO B  1 17   ? 26.193  5.942   84.284  1.00 49.81 ? 15   PRO B CG    1 
ATOM   8851  C CD    . PRO B  1 17   ? 27.304  6.222   83.325  1.00 49.36 ? 15   PRO B CD    1 
ATOM   8852  N N     . ALA B  1 18   ? 24.005  4.476   80.438  1.00 41.86 ? 16   ALA B N     1 
ATOM   8853  C CA    . ALA B  1 18   ? 23.200  4.828   79.280  1.00 40.37 ? 16   ALA B CA    1 
ATOM   8854  C C     . ALA B  1 18   ? 22.245  5.965   79.637  1.00 39.26 ? 16   ALA B C     1 
ATOM   8855  O O     . ALA B  1 18   ? 21.660  5.960   80.722  1.00 37.68 ? 16   ALA B O     1 
ATOM   8856  C CB    . ALA B  1 18   ? 22.411  3.614   78.789  1.00 41.03 ? 16   ALA B CB    1 
ATOM   8857  N N     . PRO B  1 19   ? 22.065  6.943   78.747  1.00 37.00 ? 17   PRO B N     1 
ATOM   8858  C CA    . PRO B  1 19   ? 21.204  8.093   79.066  1.00 34.92 ? 17   PRO B CA    1 
ATOM   8859  C C     . PRO B  1 19   ? 19.776  7.672   79.390  1.00 31.90 ? 17   PRO B C     1 
ATOM   8860  O O     . PRO B  1 19   ? 19.153  6.897   78.657  1.00 31.54 ? 17   PRO B O     1 
ATOM   8861  C CB    . PRO B  1 19   ? 21.257  8.945   77.789  1.00 32.83 ? 17   PRO B CB    1 
ATOM   8862  C CG    . PRO B  1 19   ? 22.478  8.477   77.049  1.00 37.87 ? 17   PRO B CG    1 
ATOM   8863  C CD    . PRO B  1 19   ? 22.623  7.020   77.387  1.00 34.85 ? 17   PRO B CD    1 
ATOM   8864  N N     . PHE B  1 20   ? 19.260  8.207   80.498  1.00 28.73 ? 18   PHE B N     1 
ATOM   8865  C CA    . PHE B  1 20   ? 17.880  8.067   80.958  1.00 29.55 ? 18   PHE B CA    1 
ATOM   8866  C C     . PHE B  1 20   ? 17.537  6.643   81.381  1.00 34.96 ? 18   PHE B C     1 
ATOM   8867  O O     . PHE B  1 20   ? 16.364  6.347   81.628  1.00 31.66 ? 18   PHE B O     1 
ATOM   8868  C CB    . PHE B  1 20   ? 16.883  8.555   79.898  1.00 25.87 ? 18   PHE B CB    1 
ATOM   8869  C CG    . PHE B  1 20   ? 17.085  9.995   79.499  1.00 26.57 ? 18   PHE B CG    1 
ATOM   8870  C CD1   . PHE B  1 20   ? 16.693  11.017  80.348  1.00 22.47 ? 18   PHE B CD1   1 
ATOM   8871  C CD2   . PHE B  1 20   ? 17.654  10.325  78.271  1.00 25.94 ? 18   PHE B CD2   1 
ATOM   8872  C CE1   . PHE B  1 20   ? 16.882  12.350  79.999  1.00 26.83 ? 18   PHE B CE1   1 
ATOM   8873  C CE2   . PHE B  1 20   ? 17.835  11.658  77.904  1.00 23.66 ? 18   PHE B CE2   1 
ATOM   8874  C CZ    . PHE B  1 20   ? 17.449  12.671  78.766  1.00 26.05 ? 18   PHE B CZ    1 
ATOM   8875  N N     . ALA B  1 21   ? 18.537  5.762   81.498  1.00 35.72 ? 19   ALA B N     1 
ATOM   8876  C CA    . ALA B  1 21   ? 18.293  4.381   81.908  1.00 39.49 ? 19   ALA B CA    1 
ATOM   8877  C C     . ALA B  1 21   ? 17.667  4.297   83.298  1.00 38.55 ? 19   ALA B C     1 
ATOM   8878  O O     . ALA B  1 21   ? 16.944  3.339   83.598  1.00 39.91 ? 19   ALA B O     1 
ATOM   8879  C CB    . ALA B  1 21   ? 19.606  3.596   81.871  1.00 36.58 ? 19   ALA B CB    1 
ATOM   8880  N N     . ASP B  1 22   ? 17.935  5.275   84.159  1.00 35.44 ? 20   ASP B N     1 
ATOM   8881  C CA    . ASP B  1 22   ? 17.375  5.310   85.508  1.00 35.14 ? 20   ASP B CA    1 
ATOM   8882  C C     . ASP B  1 22   ? 16.716  6.652   85.761  1.00 29.81 ? 20   ASP B C     1 
ATOM   8883  O O     . ASP B  1 22   ? 16.934  7.293   86.786  1.00 30.60 ? 20   ASP B O     1 
ATOM   8884  C CB    . ASP B  1 22   ? 18.444  5.033   86.562  1.00 38.86 ? 20   ASP B CB    1 
ATOM   8885  N N     . PHE B  1 23   ? 15.882  7.102   84.821  1.00 26.93 ? 21   PHE B N     1 
ATOM   8886  C CA    . PHE B  1 23   ? 15.353  8.461   84.913  1.00 26.82 ? 21   PHE B CA    1 
ATOM   8887  C C     . PHE B  1 23   ? 14.451  8.628   86.129  1.00 25.05 ? 21   PHE B C     1 
ATOM   8888  O O     . PHE B  1 23   ? 14.686  9.493   86.985  1.00 26.09 ? 21   PHE B O     1 
ATOM   8889  C CB    . PHE B  1 23   ? 14.576  8.833   83.644  1.00 22.46 ? 21   PHE B CB    1 
ATOM   8890  C CG    . PHE B  1 23   ? 13.975  10.205  83.720  1.00 26.73 ? 21   PHE B CG    1 
ATOM   8891  C CD1   . PHE B  1 23   ? 14.797  11.312  83.865  1.00 24.97 ? 21   PHE B CD1   1 
ATOM   8892  C CD2   . PHE B  1 23   ? 12.597  10.389  83.681  1.00 26.15 ? 21   PHE B CD2   1 
ATOM   8893  C CE1   . PHE B  1 23   ? 14.262  12.573  83.968  1.00 23.90 ? 21   PHE B CE1   1 
ATOM   8894  C CE2   . PHE B  1 23   ? 12.061  11.652  83.782  1.00 30.07 ? 21   PHE B CE2   1 
ATOM   8895  C CZ    . PHE B  1 23   ? 12.896  12.744  83.929  1.00 27.20 ? 21   PHE B CZ    1 
ATOM   8896  N N     . ALA B  1 24   ? 13.389  7.841   86.197  1.00 23.45 ? 22   ALA B N     1 
ATOM   8897  C CA    . ALA B  1 24   ? 12.444  7.929   87.299  1.00 28.74 ? 22   ALA B CA    1 
ATOM   8898  C C     . ALA B  1 24   ? 11.743  6.590   87.500  1.00 26.96 ? 22   ALA B C     1 
ATOM   8899  O O     . ALA B  1 24   ? 10.519  6.503   87.326  1.00 28.11 ? 22   ALA B O     1 
ATOM   8900  C CB    . ALA B  1 24   ? 11.423  9.039   87.037  1.00 26.72 ? 22   ALA B CB    1 
ATOM   8901  N N     . PRO B  1 25   ? 12.470  5.532   87.860  1.00 30.02 ? 23   PRO B N     1 
ATOM   8902  C CA    . PRO B  1 25   ? 11.827  4.245   88.084  1.00 32.69 ? 23   PRO B CA    1 
ATOM   8903  C C     . PRO B  1 25   ? 10.872  4.336   89.259  1.00 30.18 ? 23   PRO B C     1 
ATOM   8904  O O     . PRO B  1 25   ? 11.216  4.921   90.298  1.00 30.11 ? 23   PRO B O     1 
ATOM   8905  C CB    . PRO B  1 25   ? 13.006  3.305   88.392  1.00 30.77 ? 23   PRO B CB    1 
ATOM   8906  C CG    . PRO B  1 25   ? 14.051  4.186   88.953  1.00 31.80 ? 23   PRO B CG    1 
ATOM   8907  C CD    . PRO B  1 25   ? 13.905  5.491   88.198  1.00 29.42 ? 23   PRO B CD    1 
ATOM   8908  N N     . PRO B  1 26   ? 9.668   3.787   89.129  1.00 30.64 ? 24   PRO B N     1 
ATOM   8909  C CA    . PRO B  1 26   ? 8.713   3.827   90.240  1.00 29.35 ? 24   PRO B CA    1 
ATOM   8910  C C     . PRO B  1 26   ? 9.181   2.997   91.426  1.00 30.72 ? 24   PRO B C     1 
ATOM   8911  O O     . PRO B  1 26   ? 10.037  2.115   91.311  1.00 30.59 ? 24   PRO B O     1 
ATOM   8912  C CB    . PRO B  1 26   ? 7.436   3.239   89.633  1.00 30.13 ? 24   PRO B CB    1 
ATOM   8913  C CG    . PRO B  1 26   ? 7.930   2.348   88.521  1.00 33.21 ? 24   PRO B CG    1 
ATOM   8914  C CD    . PRO B  1 26   ? 9.132   3.068   87.958  1.00 30.54 ? 24   PRO B CD    1 
ATOM   8915  N N     . VAL B  1 27   ? 8.591   3.293   92.587  1.00 29.46 ? 25   VAL B N     1 
ATOM   8916  C CA    . VAL B  1 27   ? 8.920   2.549   93.797  1.00 31.85 ? 25   VAL B CA    1 
ATOM   8917  C C     . VAL B  1 27   ? 8.593   1.073   93.606  1.00 28.55 ? 25   VAL B C     1 
ATOM   8918  O O     . VAL B  1 27   ? 9.331   0.194   94.059  1.00 31.86 ? 25   VAL B O     1 
ATOM   8919  C CB    . VAL B  1 27   ? 8.185   3.153   95.010  1.00 31.26 ? 25   VAL B CB    1 
ATOM   8920  C CG1   . VAL B  1 27   ? 8.346   2.276   96.234  1.00 30.04 ? 25   VAL B CG1   1 
ATOM   8921  C CG2   . VAL B  1 27   ? 8.715   4.547   95.302  1.00 26.58 ? 25   VAL B CG2   1 
ATOM   8922  N N     . ARG B  1 28   ? 7.520   0.779   92.879  1.00 29.21 ? 26   ARG B N     1 
ATOM   8923  C CA    . ARG B  1 28   ? 7.036   -0.583  92.728  1.00 30.77 ? 26   ARG B CA    1 
ATOM   8924  C C     . ARG B  1 28   ? 6.259   -0.668  91.427  1.00 32.10 ? 26   ARG B C     1 
ATOM   8925  O O     . ARG B  1 28   ? 5.796   0.356   90.912  1.00 32.19 ? 26   ARG B O     1 
ATOM   8926  C CB    . ARG B  1 28   ? 6.141   -0.988  93.907  1.00 34.10 ? 26   ARG B CB    1 
ATOM   8927  C CG    . ARG B  1 28   ? 4.801   -0.260  93.951  1.00 33.90 ? 26   ARG B CG    1 
ATOM   8928  C CD    . ARG B  1 28   ? 4.035   -0.604  95.231  1.00 36.67 ? 26   ARG B CD    1 
ATOM   8929  N NE    . ARG B  1 28   ? 4.693   -0.095  96.434  1.00 37.79 ? 26   ARG B NE    1 
ATOM   8930  C CZ    . ARG B  1 28   ? 5.374   -0.840  97.294  1.00 43.45 ? 26   ARG B CZ    1 
ATOM   8931  N NH1   . ARG B  1 28   ? 5.520   -2.145  97.117  1.00 44.30 ? 26   ARG B NH1   1 
ATOM   8932  N NH2   . ARG B  1 28   ? 5.915   -0.264  98.365  1.00 38.73 ? 26   ARG B NH2   1 
ATOM   8933  N N     . PRO B  1 29   ? 6.118   -1.866  90.858  1.00 35.70 ? 27   PRO B N     1 
ATOM   8934  C CA    . PRO B  1 29   ? 5.235   -2.025  89.699  1.00 35.70 ? 27   PRO B CA    1 
ATOM   8935  C C     . PRO B  1 29   ? 3.816   -1.599  90.049  1.00 35.65 ? 27   PRO B C     1 
ATOM   8936  O O     . PRO B  1 29   ? 3.294   -1.921  91.118  1.00 34.96 ? 27   PRO B O     1 
ATOM   8937  C CB    . PRO B  1 29   ? 5.320   -3.526  89.385  1.00 33.93 ? 27   PRO B CB    1 
ATOM   8938  C CG    . PRO B  1 29   ? 6.630   -3.956  89.973  1.00 38.46 ? 27   PRO B CG    1 
ATOM   8939  C CD    . PRO B  1 29   ? 6.810   -3.120  91.204  1.00 34.97 ? 27   PRO B CD    1 
ATOM   8940  N N     . GLN B  1 30   ? 3.196   -0.855  89.142  1.00 37.65 ? 28   GLN B N     1 
ATOM   8941  C CA    . GLN B  1 30   ? 1.905   -0.248  89.430  1.00 37.60 ? 28   GLN B CA    1 
ATOM   8942  C C     . GLN B  1 30   ? 0.801   -1.277  89.225  1.00 38.00 ? 28   GLN B C     1 
ATOM   8943  O O     . GLN B  1 30   ? 0.583   -1.752  88.104  1.00 35.21 ? 28   GLN B O     1 
ATOM   8944  C CB    . GLN B  1 30   ? 1.696   0.985   88.550  1.00 37.78 ? 28   GLN B CB    1 
ATOM   8945  C CG    . GLN B  1 30   ? 2.802   2.040   88.722  1.00 31.46 ? 28   GLN B CG    1 
ATOM   8946  C CD    . GLN B  1 30   ? 2.750   2.730   90.069  1.00 31.12 ? 28   GLN B CD    1 
ATOM   8947  O OE1   . GLN B  1 30   ? 1.834   3.497   90.339  1.00 28.89 ? 28   GLN B OE1   1 
ATOM   8948  N NE2   . GLN B  1 30   ? 3.740   2.461   90.927  1.00 32.22 ? 28   GLN B NE2   1 
ATOM   8949  N N     . SER B  1 31   ? 0.100   -1.612  90.306  1.00 35.19 ? 29   SER B N     1 
ATOM   8950  C CA    . SER B  1 31   ? -1.016  -2.544  90.237  1.00 38.40 ? 29   SER B CA    1 
ATOM   8951  C C     . SER B  1 31   ? -2.167  -1.958  89.418  1.00 36.77 ? 29   SER B C     1 
ATOM   8952  O O     . SER B  1 31   ? -2.160  -0.789  89.022  1.00 32.96 ? 29   SER B O     1 
ATOM   8953  C CB    . SER B  1 31   ? -1.519  -2.873  91.638  1.00 38.69 ? 29   SER B CB    1 
ATOM   8954  O OG    . SER B  1 31   ? -2.348  -1.823  92.114  1.00 33.22 ? 29   SER B OG    1 
ATOM   8955  N N     . THR B  1 32   ? -3.188  -2.789  89.194  1.00 36.56 ? 30   THR B N     1 
ATOM   8956  C CA    . THR B  1 32   ? -4.393  -2.312  88.519  1.00 36.10 ? 30   THR B CA    1 
ATOM   8957  C C     . THR B  1 32   ? -5.070  -1.204  89.322  1.00 36.15 ? 30   THR B C     1 
ATOM   8958  O O     . THR B  1 32   ? -5.478  -0.180  88.758  1.00 36.29 ? 30   THR B O     1 
ATOM   8959  C CB    . THR B  1 32   ? -5.360  -3.475  88.267  1.00 43.21 ? 30   THR B CB    1 
ATOM   8960  O OG1   . THR B  1 32   ? -4.871  -4.268  87.179  1.00 41.65 ? 30   THR B OG1   1 
ATOM   8961  C CG2   . THR B  1 32   ? -6.754  -2.966  87.909  1.00 41.70 ? 30   THR B CG2   1 
ATOM   8962  N N     . LEU B  1 33   ? -5.167  -1.372  90.644  1.00 31.83 ? 31   LEU B N     1 
ATOM   8963  C CA    . LEU B  1 33   ? -5.805  -0.347  91.462  1.00 35.58 ? 31   LEU B CA    1 
ATOM   8964  C C     . LEU B  1 33   ? -4.967  0.925   91.518  1.00 34.17 ? 31   LEU B C     1 
ATOM   8965  O O     . LEU B  1 33   ? -5.515  2.034   91.517  1.00 33.90 ? 31   LEU B O     1 
ATOM   8966  C CB    . LEU B  1 33   ? -6.072  -0.889  92.862  1.00 36.28 ? 31   LEU B CB    1 
ATOM   8967  C CG    . LEU B  1 33   ? -7.108  -2.011  92.829  1.00 38.86 ? 31   LEU B CG    1 
ATOM   8968  C CD1   . LEU B  1 33   ? -7.054  -2.832  94.096  1.00 32.81 ? 31   LEU B CD1   1 
ATOM   8969  C CD2   . LEU B  1 33   ? -8.505  -1.448  92.603  1.00 39.17 ? 31   LEU B CD2   1 
ATOM   8970  N N     . ARG B  1 34   ? -3.637  0.792   91.548  1.00 33.72 ? 32   ARG B N     1 
ATOM   8971  C CA    . ARG B  1 34   ? -2.790  1.981   91.518  1.00 31.93 ? 32   ARG B CA    1 
ATOM   8972  C C     . ARG B  1 34   ? -2.926  2.722   90.191  1.00 31.90 ? 32   ARG B C     1 
ATOM   8973  O O     . ARG B  1 34   ? -2.926  3.957   90.159  1.00 30.37 ? 32   ARG B O     1 
ATOM   8974  C CB    . ARG B  1 34   ? -1.332  1.604   91.783  1.00 32.55 ? 32   ARG B CB    1 
ATOM   8975  C CG    . ARG B  1 34   ? -1.054  1.216   93.217  1.00 27.09 ? 32   ARG B CG    1 
ATOM   8976  C CD    . ARG B  1 34   ? -1.066  2.458   94.154  1.00 28.33 ? 32   ARG B CD    1 
ATOM   8977  N NE    . ARG B  1 34   ? -0.004  3.417   93.848  1.00 32.75 ? 32   ARG B NE    1 
ATOM   8978  C CZ    . ARG B  1 34   ? 1.190   3.431   94.428  1.00 32.16 ? 32   ARG B CZ    1 
ATOM   8979  N NH1   . ARG B  1 34   ? 1.518   2.544   95.351  1.00 30.31 ? 32   ARG B NH1   1 
ATOM   8980  N NH2   . ARG B  1 34   ? 2.074   4.362   94.076  1.00 30.70 ? 32   ARG B NH2   1 
ATOM   8981  N N     . ARG B  1 35   ? -3.063  1.986   89.086  1.00 30.15 ? 33   ARG B N     1 
ATOM   8982  C CA    . ARG B  1 35   ? -3.234  2.635   87.789  1.00 32.28 ? 33   ARG B CA    1 
ATOM   8983  C C     . ARG B  1 35   ? -4.548  3.404   87.696  1.00 31.82 ? 33   ARG B C     1 
ATOM   8984  O O     . ARG B  1 35   ? -4.600  4.453   87.040  1.00 30.07 ? 33   ARG B O     1 
ATOM   8985  C CB    . ARG B  1 35   ? -3.158  1.605   86.666  1.00 33.24 ? 33   ARG B CB    1 
ATOM   8986  C CG    . ARG B  1 35   ? -1.776  1.052   86.467  1.00 38.15 ? 33   ARG B CG    1 
ATOM   8987  C CD    . ARG B  1 35   ? -1.762  -0.011  85.394  1.00 46.17 ? 33   ARG B CD    1 
ATOM   8988  N NE    . ARG B  1 35   ? -0.443  -0.623  85.325  1.00 52.02 ? 33   ARG B NE    1 
ATOM   8989  C CZ    . ARG B  1 35   ? 0.600   -0.065  84.729  1.00 55.70 ? 33   ARG B CZ    1 
ATOM   8990  N NH1   . ARG B  1 35   ? 0.494   1.097   84.099  1.00 52.64 ? 33   ARG B NH1   1 
ATOM   8991  N NH2   . ARG B  1 35   ? 1.779   -0.680  84.773  1.00 55.02 ? 33   ARG B NH2   1 
ATOM   8992  N N     . ALA B  1 36   ? -5.611  2.907   88.329  1.00 29.85 ? 34   ALA B N     1 
ATOM   8993  C CA    . ALA B  1 36   ? -6.898  3.594   88.252  1.00 30.01 ? 34   ALA B CA    1 
ATOM   8994  C C     . ALA B  1 36   ? -6.857  4.912   89.006  1.00 29.05 ? 34   ALA B C     1 
ATOM   8995  O O     . ALA B  1 36   ? -7.481  5.898   88.599  1.00 27.23 ? 34   ALA B O     1 
ATOM   8996  C CB    . ALA B  1 36   ? -8.006  2.698   88.803  1.00 33.20 ? 34   ALA B CB    1 
ATOM   8997  N N     . ILE B  1 37   ? -6.129  4.944   90.119  1.00 29.99 ? 35   ILE B N     1 
ATOM   8998  C CA    . ILE B  1 37   ? -5.853  6.211   90.785  1.00 25.80 ? 35   ILE B CA    1 
ATOM   8999  C C     . ILE B  1 37   ? -5.186  7.175   89.822  1.00 24.44 ? 35   ILE B C     1 
ATOM   9000  O O     . ILE B  1 37   ? -5.633  8.316   89.641  1.00 25.57 ? 35   ILE B O     1 
ATOM   9001  C CB    . ILE B  1 37   ? -4.971  5.969   92.025  1.00 24.75 ? 35   ILE B CB    1 
ATOM   9002  C CG1   . ILE B  1 37   ? -5.725  5.149   93.069  1.00 25.53 ? 35   ILE B CG1   1 
ATOM   9003  C CG2   . ILE B  1 37   ? -4.471  7.291   92.578  1.00 25.38 ? 35   ILE B CG2   1 
ATOM   9004  C CD1   . ILE B  1 37   ? -4.797  4.579   94.175  1.00 25.73 ? 35   ILE B CD1   1 
ATOM   9005  N N     . THR B  1 38   ? -4.088  6.735   89.198  1.00 23.84 ? 36   THR B N     1 
ATOM   9006  C CA    . THR B  1 38   ? -3.292  7.639   88.381  1.00 23.41 ? 36   THR B CA    1 
ATOM   9007  C C     . THR B  1 38   ? -4.101  8.138   87.189  1.00 24.62 ? 36   THR B C     1 
ATOM   9008  O O     . THR B  1 38   ? -3.994  9.305   86.795  1.00 23.85 ? 36   THR B O     1 
ATOM   9009  C CB    . THR B  1 38   ? -2.005  6.937   87.932  1.00 25.16 ? 36   THR B CB    1 
ATOM   9010  O OG1   . THR B  1 38   ? -1.260  6.517   89.090  1.00 27.96 ? 36   THR B OG1   1 
ATOM   9011  C CG2   . THR B  1 38   ? -1.148  7.875   87.098  1.00 26.73 ? 36   THR B CG2   1 
ATOM   9012  N N     . ALA B  1 39   ? -4.959  7.275   86.655  1.00 28.97 ? 37   ALA B N     1 
ATOM   9013  C CA    . ALA B  1 39   ? -5.805  7.632   85.518  1.00 26.78 ? 37   ALA B CA    1 
ATOM   9014  C C     . ALA B  1 39   ? -6.788  8.752   85.851  1.00 27.14 ? 37   ALA B C     1 
ATOM   9015  O O     . ALA B  1 39   ? -7.238  9.471   84.952  1.00 30.50 ? 37   ALA B O     1 
ATOM   9016  C CB    . ALA B  1 39   ? -6.557  6.388   85.055  1.00 24.48 ? 37   ALA B CB    1 
ATOM   9017  N N     . ALA B  1 40   ? -7.164  8.893   87.115  1.00 27.73 ? 38   ALA B N     1 
ATOM   9018  C CA    . ALA B  1 40   ? -8.153  9.878   87.527  1.00 26.92 ? 38   ALA B CA    1 
ATOM   9019  C C     . ALA B  1 40   ? -7.540  11.219  87.923  1.00 26.56 ? 38   ALA B C     1 
ATOM   9020  O O     . ALA B  1 40   ? -8.293  12.143  88.248  1.00 26.47 ? 38   ALA B O     1 
ATOM   9021  C CB    . ALA B  1 40   ? -8.983  9.322   88.692  1.00 26.44 ? 38   ALA B CB    1 
ATOM   9022  N N     . TYR B  1 41   ? -6.205  11.344  87.847  1.00 27.95 ? 39   TYR B N     1 
ATOM   9023  C CA    . TYR B  1 41   ? -5.468  12.464  88.446  1.00 24.28 ? 39   TYR B CA    1 
ATOM   9024  C C     . TYR B  1 41   ? -6.034  13.813  88.009  1.00 26.59 ? 39   TYR B C     1 
ATOM   9025  O O     . TYR B  1 41   ? -6.314  14.681  88.844  1.00 23.76 ? 39   TYR B O     1 
ATOM   9026  C CB    . TYR B  1 41   ? -3.983  12.344  88.068  1.00 23.52 ? 39   TYR B CB    1 
ATOM   9027  C CG    . TYR B  1 41   ? -2.960  13.048  88.952  1.00 22.15 ? 39   TYR B CG    1 
ATOM   9028  C CD1   . TYR B  1 41   ? -3.267  14.222  89.626  1.00 22.88 ? 39   TYR B CD1   1 
ATOM   9029  C CD2   . TYR B  1 41   ? -1.666  12.546  89.068  1.00 26.02 ? 39   TYR B CD2   1 
ATOM   9030  C CE1   . TYR B  1 41   ? -2.314  14.871  90.421  1.00 23.01 ? 39   TYR B CE1   1 
ATOM   9031  C CE2   . TYR B  1 41   ? -0.703  13.185  89.861  1.00 22.68 ? 39   TYR B CE2   1 
ATOM   9032  C CZ    . TYR B  1 41   ? -1.031  14.354  90.519  1.00 23.51 ? 39   TYR B CZ    1 
ATOM   9033  O OH    . TYR B  1 41   ? -0.085  14.987  91.310  1.00 22.86 ? 39   TYR B OH    1 
ATOM   9034  N N     . ARG B  1 42   ? -6.246  13.997  86.702  1.00 21.81 ? 40   ARG B N     1 
ATOM   9035  C CA    . ARG B  1 42   ? -6.754  15.268  86.191  1.00 21.76 ? 40   ARG B CA    1 
ATOM   9036  C C     . ARG B  1 42   ? -7.958  15.039  85.284  1.00 22.06 ? 40   ARG B C     1 
ATOM   9037  O O     . ARG B  1 42   ? -8.150  15.738  84.287  1.00 29.07 ? 40   ARG B O     1 
ATOM   9038  C CB    . ARG B  1 42   ? -5.649  16.047  85.482  1.00 22.15 ? 40   ARG B CB    1 
ATOM   9039  C CG    . ARG B  1 42   ? -4.650  16.645  86.489  1.00 24.55 ? 40   ARG B CG    1 
ATOM   9040  C CD    . ARG B  1 42   ? -3.306  16.992  85.901  1.00 22.54 ? 40   ARG B CD    1 
ATOM   9041  N NE    . ARG B  1 42   ? -2.275  16.910  86.937  1.00 21.86 ? 40   ARG B NE    1 
ATOM   9042  C CZ    . ARG B  1 42   ? -2.067  17.819  87.882  1.00 22.04 ? 40   ARG B CZ    1 
ATOM   9043  N NH1   . ARG B  1 42   ? -2.773  18.937  87.943  1.00 23.28 ? 40   ARG B NH1   1 
ATOM   9044  N NH2   . ARG B  1 42   ? -1.115  17.607  88.785  1.00 21.74 ? 40   ARG B NH2   1 
ATOM   9045  N N     . ARG B  1 43   ? -8.802  14.082  85.651  1.00 21.39 ? 41   ARG B N     1 
ATOM   9046  C CA    . ARG B  1 43   ? -9.956  13.742  84.822  1.00 25.80 ? 41   ARG B CA    1 
ATOM   9047  C C     . ARG B  1 43   ? -10.898 14.939  84.735  1.00 27.49 ? 41   ARG B C     1 
ATOM   9048  O O     . ARG B  1 43   ? -11.057 15.672  85.715  1.00 26.86 ? 41   ARG B O     1 
ATOM   9049  C CB    . ARG B  1 43   ? -10.678 12.532  85.418  1.00 29.35 ? 41   ARG B CB    1 
ATOM   9050  C CG    . ARG B  1 43   ? -11.991 12.137  84.765  1.00 28.13 ? 41   ARG B CG    1 
ATOM   9051  C CD    . ARG B  1 43   ? -12.378 10.738  85.244  1.00 28.63 ? 41   ARG B CD    1 
ATOM   9052  N NE    . ARG B  1 43   ? -11.360 9.773   84.847  1.00 29.27 ? 41   ARG B NE    1 
ATOM   9053  C CZ    . ARG B  1 43   ? -11.097 8.648   85.498  1.00 30.15 ? 41   ARG B CZ    1 
ATOM   9054  N NH1   . ARG B  1 43   ? -11.737 8.328   86.608  1.00 28.90 ? 41   ARG B NH1   1 
ATOM   9055  N NH2   . ARG B  1 43   ? -10.177 7.818   85.012  1.00 30.10 ? 41   ARG B NH2   1 
ATOM   9056  N N     . PRO B  1 44   ? -11.509 15.193  83.579  1.00 28.41 ? 42   PRO B N     1 
ATOM   9057  C CA    . PRO B  1 44   ? -12.431 16.331  83.473  1.00 27.33 ? 42   PRO B CA    1 
ATOM   9058  C C     . PRO B  1 44   ? -13.522 16.275  84.532  1.00 22.96 ? 42   PRO B C     1 
ATOM   9059  O O     . PRO B  1 44   ? -14.035 15.210  84.861  1.00 24.59 ? 42   PRO B O     1 
ATOM   9060  C CB    . PRO B  1 44   ? -13.010 16.179  82.062  1.00 28.01 ? 42   PRO B CB    1 
ATOM   9061  C CG    . PRO B  1 44   ? -11.884 15.553  81.286  1.00 30.88 ? 42   PRO B CG    1 
ATOM   9062  C CD    . PRO B  1 44   ? -11.220 14.588  82.263  1.00 29.25 ? 42   PRO B CD    1 
ATOM   9063  N N     . GLU B  1 45   ? -13.892 17.448  85.049  1.00 26.14 ? 43   GLU B N     1 
ATOM   9064  C CA    . GLU B  1 45   ? -14.903 17.502  86.099  1.00 27.93 ? 43   GLU B CA    1 
ATOM   9065  C C     . GLU B  1 45   ? -16.242 16.959  85.619  1.00 29.63 ? 43   GLU B C     1 
ATOM   9066  O O     . GLU B  1 45   ? -16.967 16.317  86.384  1.00 28.37 ? 43   GLU B O     1 
ATOM   9067  C CB    . GLU B  1 45   ? -15.038 18.934  86.618  1.00 29.25 ? 43   GLU B CB    1 
ATOM   9068  C CG    . GLU B  1 45   ? -14.685 19.058  88.089  1.00 31.91 ? 43   GLU B CG    1 
ATOM   9069  C CD    . GLU B  1 45   ? -14.626 20.496  88.582  1.00 24.43 ? 43   GLU B CD    1 
ATOM   9070  O OE1   . GLU B  1 45   ? -13.988 21.330  87.903  1.00 26.98 ? 43   GLU B OE1   1 
ATOM   9071  O OE2   . GLU B  1 45   ? -15.221 20.782  89.647  1.00 28.20 ? 43   GLU B OE2   1 
ATOM   9072  N N     . THR B  1 46   ? -16.582 17.176  84.343  1.00 31.71 ? 44   THR B N     1 
ATOM   9073  C CA    . THR B  1 46   ? -17.820 16.607  83.830  1.00 29.62 ? 44   THR B CA    1 
ATOM   9074  C C     . THR B  1 46   ? -17.784 15.082  83.764  1.00 32.84 ? 44   THR B C     1 
ATOM   9075  O O     . THR B  1 46   ? -18.845 14.458  83.669  1.00 31.35 ? 44   THR B O     1 
ATOM   9076  C CB    . THR B  1 46   ? -18.128 17.177  82.447  1.00 28.46 ? 44   THR B CB    1 
ATOM   9077  O OG1   . THR B  1 46   ? -16.948 17.105  81.634  1.00 31.14 ? 44   THR B OG1   1 
ATOM   9078  C CG2   . THR B  1 46   ? -18.577 18.632  82.558  1.00 30.56 ? 44   THR B CG2   1 
ATOM   9079  N N     . GLU B  1 47   ? -16.601 14.462  83.789  1.00 28.70 ? 45   GLU B N     1 
ATOM   9080  C CA    . GLU B  1 47   ? -16.551 13.005  83.836  1.00 29.62 ? 45   GLU B CA    1 
ATOM   9081  C C     . GLU B  1 47   ? -16.520 12.467  85.262  1.00 27.30 ? 45   GLU B C     1 
ATOM   9082  O O     . GLU B  1 47   ? -16.968 11.340  85.505  1.00 30.55 ? 45   GLU B O     1 
ATOM   9083  C CB    . GLU B  1 47   ? -15.330 12.486  83.069  1.00 32.16 ? 45   GLU B CB    1 
ATOM   9084  C CG    . GLU B  1 47   ? -15.317 12.841  81.587  1.00 36.36 ? 45   GLU B CG    1 
ATOM   9085  C CD    . GLU B  1 47   ? -14.049 12.361  80.899  1.00 43.25 ? 45   GLU B CD    1 
ATOM   9086  O OE1   . GLU B  1 47   ? -13.322 11.538  81.503  1.00 42.04 ? 45   GLU B OE1   1 
ATOM   9087  O OE2   . GLU B  1 47   ? -13.776 12.806  79.762  1.00 50.13 ? 45   GLU B OE2   1 
ATOM   9088  N N     . CYS B  1 48   ? -16.027 13.262  86.213  1.00 29.43 ? 46   CYS B N     1 
ATOM   9089  C CA    . CYS B  1 48   ? -15.925 12.803  87.595  1.00 29.20 ? 46   CYS B CA    1 
ATOM   9090  C C     . CYS B  1 48   ? -17.282 12.790  88.280  1.00 30.13 ? 46   CYS B C     1 
ATOM   9091  O O     . CYS B  1 48   ? -17.578 11.893  89.078  1.00 29.29 ? 46   CYS B O     1 
ATOM   9092  C CB    . CYS B  1 48   ? -14.978 13.711  88.383  1.00 24.72 ? 46   CYS B CB    1 
ATOM   9093  S SG    . CYS B  1 48   ? -13.239 13.670  87.934  1.00 27.54 ? 46   CYS B SG    1 
ATOM   9094  N N     . LEU B  1 49   ? -18.111 13.779  87.996  1.00 27.42 ? 47   LEU B N     1 
ATOM   9095  C CA    . LEU B  1 49   ? -19.273 14.006  88.846  1.00 31.44 ? 47   LEU B CA    1 
ATOM   9096  C C     . LEU B  1 49   ? -20.401 12.992  88.685  1.00 29.71 ? 47   LEU B C     1 
ATOM   9097  O O     . LEU B  1 49   ? -20.948 12.560  89.706  1.00 31.46 ? 47   LEU B O     1 
ATOM   9098  C CB    . LEU B  1 49   ? -19.805 15.425  88.641  1.00 28.69 ? 47   LEU B CB    1 
ATOM   9099  C CG    . LEU B  1 49   ? -19.338 16.362  89.758  1.00 30.88 ? 47   LEU B CG    1 
ATOM   9100  C CD1   . LEU B  1 49   ? -19.855 15.854  91.111  1.00 30.10 ? 47   LEU B CD1   1 
ATOM   9101  C CD2   . LEU B  1 49   ? -17.808 16.482  89.801  1.00 30.23 ? 47   LEU B CD2   1 
ATOM   9102  N N     . PRO B  1 50   ? -20.787 12.576  87.472  1.00 30.50 ? 48   PRO B N     1 
ATOM   9103  C CA    . PRO B  1 50   ? -21.957 11.682  87.337  1.00 33.49 ? 48   PRO B CA    1 
ATOM   9104  C C     . PRO B  1 50   ? -21.824 10.402  88.153  1.00 35.15 ? 48   PRO B C     1 
ATOM   9105  O O     . PRO B  1 50   ? -22.786 10.021  88.837  1.00 35.22 ? 48   PRO B O     1 
ATOM   9106  C CB    . PRO B  1 50   ? -22.023 11.401  85.824  1.00 27.91 ? 48   PRO B CB    1 
ATOM   9107  C CG    . PRO B  1 50   ? -21.460 12.638  85.212  1.00 27.42 ? 48   PRO B CG    1 
ATOM   9108  C CD    . PRO B  1 50   ? -20.301 13.018  86.148  1.00 29.88 ? 48   PRO B CD    1 
ATOM   9109  N N     . PRO B  1 51   ? -20.679 9.700   88.138  1.00 32.16 ? 49   PRO B N     1 
ATOM   9110  C CA    . PRO B  1 51   ? -20.583 8.516   89.014  1.00 34.11 ? 49   PRO B CA    1 
ATOM   9111  C C     . PRO B  1 51   ? -20.615 8.858   90.495  1.00 35.89 ? 49   PRO B C     1 
ATOM   9112  O O     . PRO B  1 51   ? -21.053 8.028   91.302  1.00 37.13 ? 49   PRO B O     1 
ATOM   9113  C CB    . PRO B  1 51   ? -19.246 7.874   88.612  1.00 38.91 ? 49   PRO B CB    1 
ATOM   9114  C CG    . PRO B  1 51   ? -18.473 8.964   87.980  1.00 37.70 ? 49   PRO B CG    1 
ATOM   9115  C CD    . PRO B  1 51   ? -19.490 9.802   87.268  1.00 33.59 ? 49   PRO B CD    1 
ATOM   9116  N N     . LEU B  1 52   ? -20.167 10.054  90.881  1.00 33.00 ? 50   LEU B N     1 
ATOM   9117  C CA    . LEU B  1 52   ? -20.247 10.443  92.287  1.00 35.75 ? 50   LEU B CA    1 
ATOM   9118  C C     . LEU B  1 52   ? -21.685 10.742  92.683  1.00 35.69 ? 50   LEU B C     1 
ATOM   9119  O O     . LEU B  1 52   ? -22.138 10.330  93.756  1.00 34.29 ? 50   LEU B O     1 
ATOM   9120  C CB    . LEU B  1 52   ? -19.360 11.661  92.549  1.00 33.26 ? 50   LEU B CB    1 
ATOM   9121  C CG    . LEU B  1 52   ? -17.860 11.482  92.345  1.00 32.71 ? 50   LEU B CG    1 
ATOM   9122  C CD1   . LEU B  1 52   ? -17.150 12.832  92.424  1.00 31.15 ? 50   LEU B CD1   1 
ATOM   9123  C CD2   . LEU B  1 52   ? -17.322 10.524  93.392  1.00 32.11 ? 50   LEU B CD2   1 
ATOM   9124  N N     . VAL B  1 53   ? -22.418 11.454  91.818  1.00 35.38 ? 51   VAL B N     1 
ATOM   9125  C CA    . VAL B  1 53   ? -23.834 11.723  92.060  1.00 32.99 ? 51   VAL B CA    1 
ATOM   9126  C C     . VAL B  1 53   ? -24.596 10.420  92.256  1.00 36.79 ? 51   VAL B C     1 
ATOM   9127  O O     . VAL B  1 53   ? -25.451 10.312  93.142  1.00 36.55 ? 51   VAL B O     1 
ATOM   9128  C CB    . VAL B  1 53   ? -24.426 12.553  90.904  1.00 34.17 ? 51   VAL B CB    1 
ATOM   9129  C CG1   . VAL B  1 53   ? -25.961 12.576  90.983  1.00 38.99 ? 51   VAL B CG1   1 
ATOM   9130  C CG2   . VAL B  1 53   ? -23.881 13.960  90.934  1.00 31.28 ? 51   VAL B CG2   1 
ATOM   9131  N N     . GLU B  1 54   ? -24.288 9.407   91.441  1.00 36.96 ? 52   GLU B N     1 
ATOM   9132  C CA    . GLU B  1 54   ? -25.000 8.136   91.531  1.00 40.77 ? 52   GLU B CA    1 
ATOM   9133  C C     . GLU B  1 54   ? -24.712 7.434   92.851  1.00 37.70 ? 52   GLU B C     1 
ATOM   9134  O O     . GLU B  1 54   ? -25.618 6.866   93.466  1.00 45.95 ? 52   GLU B O     1 
ATOM   9135  C CB    . GLU B  1 54   ? -24.621 7.237   90.354  1.00 39.42 ? 52   GLU B CB    1 
ATOM   9136  N N     . ALA B  1 55   ? -23.456 7.466   93.301  1.00 40.02 ? 53   ALA B N     1 
ATOM   9137  C CA    . ALA B  1 55   ? -23.078 6.799   94.545  1.00 40.21 ? 53   ALA B CA    1 
ATOM   9138  C C     . ALA B  1 55   ? -23.599 7.534   95.776  1.00 38.53 ? 53   ALA B C     1 
ATOM   9139  O O     . ALA B  1 55   ? -23.859 6.904   96.808  1.00 41.16 ? 53   ALA B O     1 
ATOM   9140  C CB    . ALA B  1 55   ? -21.554 6.667   94.618  1.00 39.70 ? 53   ALA B CB    1 
ATOM   9141  N N     . ALA B  1 56   ? -23.751 8.855   95.690  1.00 39.32 ? 54   ALA B N     1 
ATOM   9142  C CA    . ALA B  1 56   ? -24.216 9.688   96.792  1.00 38.24 ? 54   ALA B CA    1 
ATOM   9143  C C     . ALA B  1 56   ? -25.730 9.894   96.805  1.00 43.52 ? 54   ALA B C     1 
ATOM   9144  O O     . ALA B  1 56   ? -26.225 10.668  97.633  1.00 42.13 ? 54   ALA B O     1 
ATOM   9145  C CB    . ALA B  1 56   ? -23.524 11.049  96.744  1.00 39.00 ? 54   ALA B CB    1 
ATOM   9146  N N     . THR B  1 57   ? -26.472 9.238   95.907  1.00 42.08 ? 55   THR B N     1 
ATOM   9147  C CA    . THR B  1 57   ? -27.924 9.378   95.861  1.00 44.23 ? 55   THR B CA    1 
ATOM   9148  C C     . THR B  1 57   ? -28.583 8.606   96.994  1.00 47.01 ? 55   THR B C     1 
ATOM   9149  O O     . THR B  1 57   ? -28.304 7.419   97.192  1.00 49.20 ? 55   THR B O     1 
ATOM   9150  C CB    . THR B  1 57   ? -28.469 8.883   94.521  1.00 44.57 ? 55   THR B CB    1 
ATOM   9151  O OG1   . THR B  1 57   ? -28.148 9.834   93.504  1.00 39.64 ? 55   THR B OG1   1 
ATOM   9152  C CG2   . THR B  1 57   ? -29.982 8.699   94.581  1.00 52.09 ? 55   THR B CG2   1 
ATOM   9153  N N     . GLN B  1 58   ? -29.468 9.275   97.730  1.00 47.83 ? 56   GLN B N     1 
ATOM   9154  C CA    . GLN B  1 58   ? -30.227 8.640   98.796  1.00 48.58 ? 56   GLN B CA    1 
ATOM   9155  C C     . GLN B  1 58   ? -31.724 8.751   98.527  1.00 49.59 ? 56   GLN B C     1 
ATOM   9156  O O     . GLN B  1 58   ? -32.188 9.636   97.801  1.00 53.40 ? 56   GLN B O     1 
ATOM   9157  C CB    . GLN B  1 58   ? -29.892 9.251   100.162 1.00 50.53 ? 56   GLN B CB    1 
ATOM   9158  C CG    . GLN B  1 58   ? -28.394 9.394   100.413 1.00 43.04 ? 56   GLN B CG    1 
ATOM   9159  C CD    . GLN B  1 58   ? -28.008 9.097   101.844 1.00 53.03 ? 56   GLN B CD    1 
ATOM   9160  O OE1   . GLN B  1 58   ? -28.274 8.008   102.361 1.00 59.07 ? 56   GLN B OE1   1 
ATOM   9161  N NE2   . GLN B  1 58   ? -27.375 10.065  102.498 1.00 55.62 ? 56   GLN B NE2   1 
ATOM   9162  N N     . SER B  1 59   ? -32.477 7.838   99.135  1.00 51.94 ? 57   SER B N     1 
ATOM   9163  C CA    . SER B  1 59   ? -33.924 7.812   98.978  1.00 54.00 ? 57   SER B CA    1 
ATOM   9164  C C     . SER B  1 59   ? -34.549 9.088   99.535  1.00 56.19 ? 57   SER B C     1 
ATOM   9165  O O     . SER B  1 59   ? -33.934 9.832   100.305 1.00 53.13 ? 57   SER B O     1 
ATOM   9166  C CB    . SER B  1 59   ? -34.520 6.590   99.680  1.00 55.23 ? 57   SER B CB    1 
ATOM   9167  O OG    . SER B  1 59   ? -34.235 6.597   101.073 1.00 58.57 ? 57   SER B OG    1 
ATOM   9168  N N     . LYS B  1 60   ? -35.795 9.337   99.126  1.00 57.41 ? 58   LYS B N     1 
ATOM   9169  C CA    . LYS B  1 60   ? -36.527 10.500  99.618  1.00 58.33 ? 58   LYS B CA    1 
ATOM   9170  C C     . LYS B  1 60   ? -36.762 10.419  101.122 1.00 59.15 ? 58   LYS B C     1 
ATOM   9171  O O     . LYS B  1 60   ? -36.803 11.451  101.801 1.00 61.04 ? 58   LYS B O     1 
ATOM   9172  C CB    . LYS B  1 60   ? -37.860 10.626  98.875  1.00 63.82 ? 58   LYS B CB    1 
ATOM   9173  C CG    . LYS B  1 60   ? -38.771 11.751  99.364  1.00 69.59 ? 58   LYS B CG    1 
ATOM   9174  C CD    . LYS B  1 60   ? -38.229 13.126  98.989  1.00 68.07 ? 58   LYS B CD    1 
ATOM   9175  C CE    . LYS B  1 60   ? -39.246 14.220  99.290  1.00 68.28 ? 58   LYS B CE    1 
ATOM   9176  N NZ    . LYS B  1 60   ? -38.730 15.573  98.939  1.00 71.22 ? 58   LYS B NZ    1 
ATOM   9177  N N     . GLU B  1 61   ? -36.924 9.211   101.660 1.00 56.96 ? 59   GLU B N     1 
ATOM   9178  C CA    . GLU B  1 61   ? -37.076 9.068   103.102 1.00 52.75 ? 59   GLU B CA    1 
ATOM   9179  C C     . GLU B  1 61   ? -35.811 9.519   103.814 1.00 57.08 ? 59   GLU B C     1 
ATOM   9180  O O     . GLU B  1 61   ? -35.854 10.366  104.715 1.00 57.77 ? 59   GLU B O     1 
ATOM   9181  C CB    . GLU B  1 61   ? -37.411 7.616   103.457 1.00 58.01 ? 59   GLU B CB    1 
ATOM   9182  N N     . ILE B  1 62   ? -34.667 8.977   103.399 1.00 56.55 ? 60   ILE B N     1 
ATOM   9183  C CA    . ILE B  1 62   ? -33.398 9.349   104.014 1.00 53.29 ? 60   ILE B CA    1 
ATOM   9184  C C     . ILE B  1 62   ? -33.102 10.826  103.782 1.00 52.06 ? 60   ILE B C     1 
ATOM   9185  O O     . ILE B  1 62   ? -32.639 11.528  104.687 1.00 52.39 ? 60   ILE B O     1 
ATOM   9186  C CB    . ILE B  1 62   ? -32.277 8.438   103.480 1.00 53.09 ? 60   ILE B CB    1 
ATOM   9187  C CG1   . ILE B  1 62   ? -32.533 6.995   103.919 1.00 53.03 ? 60   ILE B CG1   1 
ATOM   9188  C CG2   . ILE B  1 62   ? -30.912 8.926   103.933 1.00 54.69 ? 60   ILE B CG2   1 
ATOM   9189  C CD1   . ILE B  1 62   ? -31.482 6.011   103.464 1.00 54.86 ? 60   ILE B CD1   1 
ATOM   9190  N N     . ARG B  1 63   ? -33.391 11.331  102.581 1.00 47.55 ? 61   ARG B N     1 
ATOM   9191  C CA    . ARG B  1 63   ? -33.099 12.732  102.288 1.00 50.37 ? 61   ARG B CA    1 
ATOM   9192  C C     . ARG B  1 63   ? -33.924 13.669  103.161 1.00 53.07 ? 61   ARG B C     1 
ATOM   9193  O O     . ARG B  1 63   ? -33.410 14.683  103.649 1.00 52.81 ? 61   ARG B O     1 
ATOM   9194  C CB    . ARG B  1 63   ? -33.338 13.025  100.805 1.00 51.43 ? 61   ARG B CB    1 
ATOM   9195  C CG    . ARG B  1 63   ? -32.235 12.499  99.906  1.00 54.19 ? 61   ARG B CG    1 
ATOM   9196  C CD    . ARG B  1 63   ? -32.376 12.998  98.477  1.00 57.73 ? 61   ARG B CD    1 
ATOM   9197  N NE    . ARG B  1 63   ? -33.464 12.343  97.761  1.00 54.37 ? 61   ARG B NE    1 
ATOM   9198  C CZ    . ARG B  1 63   ? -34.497 12.974  97.218  1.00 56.60 ? 61   ARG B CZ    1 
ATOM   9199  N NH1   . ARG B  1 63   ? -34.633 14.288  97.306  1.00 55.88 ? 61   ARG B NH1   1 
ATOM   9200  N NH2   . ARG B  1 63   ? -35.415 12.270  96.566  1.00 55.43 ? 61   ARG B NH2   1 
ATOM   9201  N N     . ASP B  1 64   ? -35.207 13.348  103.369 1.00 52.69 ? 62   ASP B N     1 
ATOM   9202  C CA    . ASP B  1 64   ? -36.055 14.174  104.227 1.00 54.01 ? 62   ASP B CA    1 
ATOM   9203  C C     . ASP B  1 64   ? -35.577 14.142  105.675 1.00 48.09 ? 62   ASP B C     1 
ATOM   9204  O O     . ASP B  1 64   ? -35.499 15.186  106.330 1.00 49.77 ? 62   ASP B O     1 
ATOM   9205  C CB    . ASP B  1 64   ? -37.515 13.715  104.137 1.00 55.15 ? 62   ASP B CB    1 
ATOM   9206  C CG    . ASP B  1 64   ? -38.167 14.082  102.806 1.00 58.38 ? 62   ASP B CG    1 
ATOM   9207  O OD1   . ASP B  1 64   ? -37.450 14.521  101.886 1.00 57.10 ? 62   ASP B OD1   1 
ATOM   9208  O OD2   . ASP B  1 64   ? -39.403 13.934  102.683 1.00 65.31 ? 62   ASP B OD2   1 
ATOM   9209  N N     . ALA B  1 65   ? -35.275 12.950  106.196 1.00 48.83 ? 63   ALA B N     1 
ATOM   9210  C CA    . ALA B  1 65   ? -34.776 12.844  107.563 1.00 49.64 ? 63   ALA B CA    1 
ATOM   9211  C C     . ALA B  1 65   ? -33.404 13.497  107.722 1.00 52.81 ? 63   ALA B C     1 
ATOM   9212  O O     . ALA B  1 65   ? -33.047 13.924  108.826 1.00 52.04 ? 63   ALA B O     1 
ATOM   9213  C CB    . ALA B  1 65   ? -34.716 11.377  107.985 1.00 52.43 ? 63   ALA B CB    1 
ATOM   9214  N N     . ALA B  1 66   ? -32.625 13.589  106.637 1.00 49.75 ? 64   ALA B N     1 
ATOM   9215  C CA    . ALA B  1 66   ? -31.300 14.194  106.734 1.00 50.83 ? 64   ALA B CA    1 
ATOM   9216  C C     . ALA B  1 66   ? -31.392 15.709  106.844 1.00 51.37 ? 64   ALA B C     1 
ATOM   9217  O O     . ALA B  1 66   ? -30.687 16.321  107.654 1.00 47.42 ? 64   ALA B O     1 
ATOM   9218  C CB    . ALA B  1 66   ? -30.441 13.793  105.534 1.00 50.11 ? 64   ALA B CB    1 
ATOM   9219  N N     . ALA B  1 67   ? -32.256 16.331  106.039 1.00 48.50 ? 65   ALA B N     1 
ATOM   9220  C CA    . ALA B  1 67   ? -32.417 17.779  106.104 1.00 45.46 ? 65   ALA B CA    1 
ATOM   9221  C C     . ALA B  1 67   ? -33.033 18.210  107.425 1.00 51.69 ? 65   ALA B C     1 
ATOM   9222  O O     . ALA B  1 67   ? -32.851 19.357  107.846 1.00 55.16 ? 65   ALA B O     1 
ATOM   9223  C CB    . ALA B  1 67   ? -33.282 18.267  104.942 1.00 49.48 ? 65   ALA B CB    1 
ATOM   9224  N N     . SER B  1 68   ? -33.773 17.312  108.079 1.00 51.81 ? 66   SER B N     1 
ATOM   9225  C CA    . SER B  1 68   ? -34.381 17.629  109.365 1.00 53.29 ? 66   SER B CA    1 
ATOM   9226  C C     . SER B  1 68   ? -33.348 17.549  110.479 1.00 51.89 ? 66   SER B C     1 
ATOM   9227  O O     . SER B  1 68   ? -33.236 18.466  111.299 1.00 54.18 ? 66   SER B O     1 
ATOM   9228  C CB    . SER B  1 68   ? -35.554 16.686  109.640 1.00 49.53 ? 66   SER B CB    1 
ATOM   9229  N N     . THR B  1 69   ? -32.590 16.450  110.522 1.00 53.84 ? 67   THR B N     1 
ATOM   9230  C CA    . THR B  1 69   ? -31.414 16.380  111.383 1.00 49.38 ? 67   THR B CA    1 
ATOM   9231  C C     . THR B  1 69   ? -30.493 17.573  111.148 1.00 51.07 ? 67   THR B C     1 
ATOM   9232  O O     . THR B  1 69   ? -30.037 18.217  112.098 1.00 50.63 ? 67   THR B O     1 
ATOM   9233  C CB    . THR B  1 69   ? -30.666 15.069  111.135 1.00 54.51 ? 67   THR B CB    1 
ATOM   9234  O OG1   . THR B  1 69   ? -31.505 13.959  111.479 1.00 49.61 ? 67   THR B OG1   1 
ATOM   9235  C CG2   . THR B  1 69   ? -29.364 15.011  111.947 1.00 48.46 ? 67   THR B CG2   1 
ATOM   9236  N N     . ALA B  1 70   ? -30.216 17.891  109.877 1.00 47.05 ? 68   ALA B N     1 
ATOM   9237  C CA    . ALA B  1 70   ? -29.381 19.049  109.576 1.00 50.18 ? 68   ALA B CA    1 
ATOM   9238  C C     . ALA B  1 70   ? -30.038 20.347  110.027 1.00 53.60 ? 68   ALA B C     1 
ATOM   9239  O O     . ALA B  1 70   ? -29.337 21.299  110.400 1.00 54.05 ? 68   ALA B O     1 
ATOM   9240  C CB    . ALA B  1 70   ? -29.067 19.109  108.077 1.00 48.24 ? 68   ALA B CB    1 
ATOM   9241  N N     . ARG B  1 71   ? -31.374 20.403  109.997 1.00 48.30 ? 69   ARG B N     1 
ATOM   9242  C CA    . ARG B  1 71   ? -32.096 21.585  110.464 1.00 55.58 ? 69   ARG B CA    1 
ATOM   9243  C C     . ARG B  1 71   ? -31.863 21.830  111.953 1.00 52.63 ? 69   ARG B C     1 
ATOM   9244  O O     . ARG B  1 71   ? -31.533 22.948  112.367 1.00 50.42 ? 69   ARG B O     1 
ATOM   9245  C CB    . ARG B  1 71   ? -33.594 21.430  110.178 1.00 54.85 ? 69   ARG B CB    1 
ATOM   9246  N N     . LYS B  1 72   ? -32.046 20.795  112.775 1.00 52.81 ? 70   LYS B N     1 
ATOM   9247  C CA    . LYS B  1 72   ? -31.891 20.959  114.217 1.00 52.38 ? 70   LYS B CA    1 
ATOM   9248  C C     . LYS B  1 72   ? -30.472 21.374  114.587 1.00 53.95 ? 70   LYS B C     1 
ATOM   9249  O O     . LYS B  1 72   ? -30.269 22.065  115.592 1.00 55.78 ? 70   LYS B O     1 
ATOM   9250  C CB    . LYS B  1 72   ? -32.274 19.664  114.934 1.00 54.47 ? 70   LYS B CB    1 
ATOM   9251  N N     . LEU B  1 73   ? -29.482 20.983  113.779 1.00 56.39 ? 71   LEU B N     1 
ATOM   9252  C CA    . LEU B  1 73   ? -28.096 21.328  114.081 1.00 51.88 ? 71   LEU B CA    1 
ATOM   9253  C C     . LEU B  1 73   ? -27.829 22.808  113.833 1.00 51.33 ? 71   LEU B C     1 
ATOM   9254  O O     . LEU B  1 73   ? -27.259 23.494  114.688 1.00 48.97 ? 71   LEU B O     1 
ATOM   9255  C CB    . LEU B  1 73   ? -27.152 20.454  113.256 1.00 51.20 ? 71   LEU B CB    1 
ATOM   9256  C CG    . LEU B  1 73   ? -27.218 18.972  113.624 1.00 48.29 ? 71   LEU B CG    1 
ATOM   9257  C CD1   . LEU B  1 73   ? -26.362 18.128  112.697 1.00 49.13 ? 71   LEU B CD1   1 
ATOM   9258  C CD2   . LEU B  1 73   ? -26.799 18.780  115.077 1.00 49.92 ? 71   LEU B CD2   1 
ATOM   9259  N N     . ILE B  1 74   ? -28.246 23.323  112.672 1.00 51.25 ? 72   ILE B N     1 
ATOM   9260  C CA    . ILE B  1 74   ? -27.994 24.724  112.343 1.00 53.47 ? 72   ILE B CA    1 
ATOM   9261  C C     . ILE B  1 74   ? -28.740 25.648  113.295 1.00 53.31 ? 72   ILE B C     1 
ATOM   9262  O O     . ILE B  1 74   ? -28.254 26.739  113.625 1.00 54.17 ? 72   ILE B O     1 
ATOM   9263  C CB    . ILE B  1 74   ? -28.368 25.011  110.874 1.00 45.28 ? 72   ILE B CB    1 
ATOM   9264  N N     . GLU B  1 75   ? -29.928 25.239  113.746 1.00 54.27 ? 73   GLU B N     1 
ATOM   9265  C CA    . GLU B  1 75   ? -30.677 26.062  114.689 1.00 55.26 ? 73   GLU B CA    1 
ATOM   9266  C C     . GLU B  1 75   ? -30.032 26.033  116.069 1.00 51.97 ? 73   GLU B C     1 
ATOM   9267  O O     . GLU B  1 75   ? -29.857 27.082  116.703 1.00 51.09 ? 73   GLU B O     1 
ATOM   9268  C CB    . GLU B  1 75   ? -32.133 25.597  114.752 1.00 52.89 ? 73   GLU B CB    1 
ATOM   9269  N N     . ALA B  1 76   ? -29.656 24.841  116.541 1.00 51.03 ? 74   ALA B N     1 
ATOM   9270  C CA    . ALA B  1 76   ? -28.913 24.743  117.793 1.00 53.15 ? 74   ALA B CA    1 
ATOM   9271  C C     . ALA B  1 76   ? -27.608 25.528  117.727 1.00 53.58 ? 74   ALA B C     1 
ATOM   9272  O O     . ALA B  1 76   ? -27.262 26.250  118.670 1.00 55.34 ? 74   ALA B O     1 
ATOM   9273  C CB    . ALA B  1 76   ? -28.641 23.278  118.130 1.00 52.61 ? 74   ALA B CB    1 
ATOM   9274  N N     . LEU B  1 77   ? -26.873 25.414  116.614 1.00 54.86 ? 75   LEU B N     1 
ATOM   9275  C CA    . LEU B  1 77   ? -25.606 26.129  116.493 1.00 52.76 ? 75   LEU B CA    1 
ATOM   9276  C C     . LEU B  1 77   ? -25.822 27.638  116.484 1.00 51.41 ? 75   LEU B C     1 
ATOM   9277  O O     . LEU B  1 77   ? -25.049 28.385  117.091 1.00 53.97 ? 75   LEU B O     1 
ATOM   9278  C CB    . LEU B  1 77   ? -24.857 25.687  115.229 1.00 46.72 ? 75   LEU B CB    1 
ATOM   9279  N N     . ARG B  1 78   ? -26.861 28.107  115.796 1.00 51.28 ? 76   ARG B N     1 
ATOM   9280  C CA    . ARG B  1 78   ? -27.133 29.538  115.742 1.00 52.59 ? 76   ARG B CA    1 
ATOM   9281  C C     . ARG B  1 78   ? -27.800 30.058  117.008 1.00 55.97 ? 76   ARG B C     1 
ATOM   9282  O O     . ARG B  1 78   ? -27.901 31.279  117.175 1.00 54.64 ? 76   ARG B O     1 
ATOM   9283  C CB    . ARG B  1 78   ? -28.001 29.869  114.526 1.00 52.48 ? 76   ARG B CB    1 
ATOM   9284  C CG    . ARG B  1 78   ? -27.205 29.996  113.241 1.00 53.59 ? 76   ARG B CG    1 
ATOM   9285  C CD    . ARG B  1 78   ? -28.045 30.528  112.089 1.00 55.90 ? 76   ARG B CD    1 
ATOM   9286  N NE    . ARG B  1 78   ? -27.198 31.024  111.009 1.00 56.52 ? 76   ARG B NE    1 
ATOM   9287  C CZ    . ARG B  1 78   ? -27.647 31.611  109.907 1.00 60.18 ? 76   ARG B CZ    1 
ATOM   9288  N NH1   . ARG B  1 78   ? -28.942 31.779  109.692 1.00 56.09 ? 76   ARG B NH1   1 
ATOM   9289  N NH2   . ARG B  1 78   ? -26.774 32.042  108.999 1.00 58.21 ? 76   ARG B NH2   1 
ATOM   9290  N N     . GLY B  1 79   ? -28.248 29.169  117.892 1.00 51.62 ? 77   GLY B N     1 
ATOM   9291  C CA    . GLY B  1 79   ? -28.825 29.566  119.160 1.00 53.71 ? 77   GLY B CA    1 
ATOM   9292  C C     . GLY B  1 79   ? -27.832 29.480  120.301 1.00 52.93 ? 77   GLY B C     1 
ATOM   9293  O O     . GLY B  1 79   ? -28.221 29.258  121.449 1.00 52.39 ? 77   GLY B O     1 
ATOM   9294  N N     . LYS B  1 80   ? -26.547 29.649  119.988 1.00 57.50 ? 78   LYS B N     1 
ATOM   9295  C CA    . LYS B  1 80   ? -25.466 29.651  120.967 1.00 54.91 ? 78   LYS B CA    1 
ATOM   9296  C C     . LYS B  1 80   ? -24.529 30.824  120.701 1.00 57.50 ? 78   LYS B C     1 
ATOM   9297  O O     . LYS B  1 80   ? -24.483 31.374  119.598 1.00 57.69 ? 78   LYS B O     1 
ATOM   9298  C CB    . LYS B  1 80   ? -24.644 28.357  120.925 1.00 53.81 ? 78   LYS B CB    1 
ATOM   9299  C CG    . LYS B  1 80   ? -25.393 27.069  121.196 1.00 54.14 ? 78   LYS B CG    1 
ATOM   9300  C CD    . LYS B  1 80   ? -24.497 25.903  120.791 1.00 57.58 ? 78   LYS B CD    1 
ATOM   9301  C CE    . LYS B  1 80   ? -25.090 24.554  121.147 1.00 62.28 ? 78   LYS B CE    1 
ATOM   9302  N NZ    . LYS B  1 80   ? -24.216 23.457  120.638 1.00 58.07 ? 78   LYS B NZ    1 
ATOM   9303  N N     . HIS B  1 81   ? -23.755 31.181  121.719 1.00 59.30 ? 79   HIS B N     1 
ATOM   9304  C CA    . HIS B  1 81   ? -22.757 32.241  121.591 1.00 61.57 ? 79   HIS B CA    1 
ATOM   9305  C C     . HIS B  1 81   ? -21.664 31.881  120.576 1.00 65.09 ? 79   HIS B C     1 
ATOM   9306  O O     . HIS B  1 81   ? -20.783 31.059  120.840 1.00 61.69 ? 79   HIS B O     1 
ATOM   9307  C CB    . HIS B  1 81   ? -22.132 32.546  122.954 1.00 60.33 ? 79   HIS B CB    1 
ATOM   9308  N N     . GLY B  1 85   ? -15.115 35.753  121.523 1.00 50.42 ? 83   GLY B N     1 
ATOM   9309  C CA    . GLY B  1 85   ? -14.854 36.740  122.552 1.00 51.25 ? 83   GLY B CA    1 
ATOM   9310  C C     . GLY B  1 85   ? -14.233 38.015  122.010 1.00 53.50 ? 83   GLY B C     1 
ATOM   9311  O O     . GLY B  1 85   ? -14.275 39.062  122.661 1.00 51.55 ? 83   GLY B O     1 
ATOM   9312  N N     . VAL B  1 86   ? -13.644 37.926  120.815 1.00 53.73 ? 84   VAL B N     1 
ATOM   9313  C CA    . VAL B  1 86   ? -13.064 39.112  120.193 1.00 52.93 ? 84   VAL B CA    1 
ATOM   9314  C C     . VAL B  1 86   ? -14.157 40.094  119.791 1.00 51.47 ? 84   VAL B C     1 
ATOM   9315  O O     . VAL B  1 86   ? -13.967 41.314  119.883 1.00 50.59 ? 84   VAL B O     1 
ATOM   9316  C CB    . VAL B  1 86   ? -12.175 38.708  119.002 1.00 51.13 ? 84   VAL B CB    1 
ATOM   9317  C CG1   . VAL B  1 86   ? -12.236 39.742  117.884 1.00 51.47 ? 84   VAL B CG1   1 
ATOM   9318  C CG2   . VAL B  1 86   ? -10.739 38.531  119.466 1.00 50.26 ? 84   VAL B CG2   1 
ATOM   9319  N N     . GLU B  1 87   ? -15.325 39.587  119.383 1.00 55.01 ? 85   GLU B N     1 
ATOM   9320  C CA    . GLU B  1 87   ? -16.445 40.462  119.047 1.00 52.63 ? 85   GLU B CA    1 
ATOM   9321  C C     . GLU B  1 87   ? -16.862 41.316  120.238 1.00 49.97 ? 85   GLU B C     1 
ATOM   9322  O O     . GLU B  1 87   ? -17.203 42.495  120.079 1.00 49.03 ? 85   GLU B O     1 
ATOM   9323  C CB    . GLU B  1 87   ? -17.626 39.630  118.547 1.00 55.12 ? 85   GLU B CB    1 
ATOM   9324  N N     . GLY B  1 88   ? -16.835 40.744  121.444 1.00 51.98 ? 86   GLY B N     1 
ATOM   9325  C CA    . GLY B  1 88   ? -17.220 41.504  122.623 1.00 50.43 ? 86   GLY B CA    1 
ATOM   9326  C C     . GLY B  1 88   ? -16.174 42.510  123.058 1.00 49.23 ? 86   GLY B C     1 
ATOM   9327  O O     . GLY B  1 88   ? -16.510 43.559  123.617 1.00 46.75 ? 86   GLY B O     1 
ATOM   9328  N N     . LEU B  1 89   ? -14.897 42.206  122.821 1.00 48.07 ? 87   LEU B N     1 
ATOM   9329  C CA    . LEU B  1 89   ? -13.837 43.173  123.090 1.00 49.29 ? 87   LEU B CA    1 
ATOM   9330  C C     . LEU B  1 89   ? -13.954 44.373  122.157 1.00 42.51 ? 87   LEU B C     1 
ATOM   9331  O O     . LEU B  1 89   ? -13.926 45.528  122.600 1.00 40.47 ? 87   LEU B O     1 
ATOM   9332  C CB    . LEU B  1 89   ? -12.474 42.497  122.935 1.00 47.05 ? 87   LEU B CB    1 
ATOM   9333  C CG    . LEU B  1 89   ? -11.277 42.965  123.765 1.00 50.00 ? 87   LEU B CG    1 
ATOM   9334  C CD1   . LEU B  1 89   ? -10.088 42.057  123.476 1.00 49.60 ? 87   LEU B CD1   1 
ATOM   9335  C CD2   . LEU B  1 89   ? -10.913 44.417  123.498 1.00 46.58 ? 87   LEU B CD2   1 
ATOM   9336  N N     . VAL B  1 90   ? -14.087 44.113  120.856 1.00 44.77 ? 88   VAL B N     1 
ATOM   9337  C CA    . VAL B  1 90   ? -14.244 45.188  119.880 1.00 42.85 ? 88   VAL B CA    1 
ATOM   9338  C C     . VAL B  1 90   ? -15.465 46.038  120.212 1.00 46.75 ? 88   VAL B C     1 
ATOM   9339  O O     . VAL B  1 90   ? -15.417 47.273  120.137 1.00 45.47 ? 88   VAL B O     1 
ATOM   9340  C CB    . VAL B  1 90   ? -14.323 44.602  118.459 1.00 40.59 ? 88   VAL B CB    1 
ATOM   9341  C CG1   . VAL B  1 90   ? -14.708 45.673  117.460 1.00 39.32 ? 88   VAL B CG1   1 
ATOM   9342  C CG2   . VAL B  1 90   ? -12.994 43.984  118.068 1.00 42.89 ? 88   VAL B CG2   1 
ATOM   9343  N N     . GLN B  1 91   ? -16.566 45.396  120.619 1.00 45.75 ? 89   GLN B N     1 
ATOM   9344  C CA    . GLN B  1 91   ? -17.770 46.145  120.970 1.00 44.27 ? 89   GLN B CA    1 
ATOM   9345  C C     . GLN B  1 91   ? -17.587 46.931  122.263 1.00 44.51 ? 89   GLN B C     1 
ATOM   9346  O O     . GLN B  1 91   ? -17.987 48.098  122.346 1.00 44.72 ? 89   GLN B O     1 
ATOM   9347  C CB    . GLN B  1 91   ? -18.963 45.195  121.079 1.00 48.38 ? 89   GLN B CB    1 
ATOM   9348  N N     . GLU B  1 92   ? -16.976 46.318  123.280 1.00 44.00 ? 90   GLU B N     1 
ATOM   9349  C CA    . GLU B  1 92   ? -16.835 46.988  124.570 1.00 46.77 ? 90   GLU B CA    1 
ATOM   9350  C C     . GLU B  1 92   ? -16.030 48.277  124.454 1.00 42.82 ? 90   GLU B C     1 
ATOM   9351  O O     . GLU B  1 92   ? -16.354 49.279  125.101 1.00 38.97 ? 90   GLU B O     1 
ATOM   9352  C CB    . GLU B  1 92   ? -16.180 46.053  125.591 1.00 43.02 ? 90   GLU B CB    1 
ATOM   9353  C CG    . GLU B  1 92   ? -16.038 46.668  126.976 1.00 52.10 ? 90   GLU B CG    1 
ATOM   9354  C CD    . GLU B  1 92   ? -15.258 45.789  127.944 1.00 50.63 ? 90   GLU B CD    1 
ATOM   9355  O OE1   . GLU B  1 92   ? -14.864 44.668  127.550 1.00 57.83 ? 90   GLU B OE1   1 
ATOM   9356  O OE2   . GLU B  1 92   ? -15.035 46.224  129.094 1.00 52.36 ? 90   GLU B OE2   1 
ATOM   9357  N N     . TYR B  1 93   ? -14.962 48.272  123.661 1.00 41.54 ? 91   TYR B N     1 
ATOM   9358  C CA    . TYR B  1 93   ? -14.116 49.450  123.558 1.00 39.04 ? 91   TYR B CA    1 
ATOM   9359  C C     . TYR B  1 93   ? -14.339 50.218  122.267 1.00 40.44 ? 91   TYR B C     1 
ATOM   9360  O O     . TYR B  1 93   ? -13.545 51.112  121.951 1.00 41.09 ? 91   TYR B O     1 
ATOM   9361  C CB    . TYR B  1 93   ? -12.647 49.060  123.719 1.00 38.55 ? 91   TYR B CB    1 
ATOM   9362  C CG    . TYR B  1 93   ? -12.319 48.728  125.157 1.00 37.40 ? 91   TYR B CG    1 
ATOM   9363  C CD1   . TYR B  1 93   ? -11.905 49.716  126.043 1.00 38.22 ? 91   TYR B CD1   1 
ATOM   9364  C CD2   . TYR B  1 93   ? -12.467 47.440  125.640 1.00 40.93 ? 91   TYR B CD2   1 
ATOM   9365  C CE1   . TYR B  1 93   ? -11.625 49.421  127.370 1.00 41.80 ? 91   TYR B CE1   1 
ATOM   9366  C CE2   . TYR B  1 93   ? -12.188 47.136  126.959 1.00 40.66 ? 91   TYR B CE2   1 
ATOM   9367  C CZ    . TYR B  1 93   ? -11.767 48.130  127.817 1.00 41.44 ? 91   TYR B CZ    1 
ATOM   9368  O OH    . TYR B  1 93   ? -11.494 47.822  129.126 1.00 46.98 ? 91   TYR B OH    1 
ATOM   9369  N N     . SER B  1 94   ? -15.415 49.907  121.539 1.00 37.14 ? 92   SER B N     1 
ATOM   9370  C CA    . SER B  1 94   ? -15.753 50.551  120.270 1.00 36.39 ? 92   SER B CA    1 
ATOM   9371  C C     . SER B  1 94   ? -14.530 50.631  119.356 1.00 39.87 ? 92   SER B C     1 
ATOM   9372  O O     . SER B  1 94   ? -14.141 51.702  118.882 1.00 38.81 ? 92   SER B O     1 
ATOM   9373  C CB    . SER B  1 94   ? -16.358 51.937  120.497 1.00 38.09 ? 92   SER B CB    1 
ATOM   9374  O OG    . SER B  1 94   ? -17.352 51.921  121.513 1.00 42.52 ? 92   SER B OG    1 
ATOM   9375  N N     . LEU B  1 95   ? -13.911 49.476  119.119 1.00 34.05 ? 93   LEU B N     1 
ATOM   9376  C CA    . LEU B  1 95   ? -12.718 49.416  118.294 1.00 34.77 ? 93   LEU B CA    1 
ATOM   9377  C C     . LEU B  1 95   ? -13.099 49.302  116.829 1.00 36.03 ? 93   LEU B C     1 
ATOM   9378  O O     . LEU B  1 95   ? -14.040 48.590  116.468 1.00 37.79 ? 93   LEU B O     1 
ATOM   9379  C CB    . LEU B  1 95   ? -11.828 48.230  118.686 1.00 35.58 ? 93   LEU B CB    1 
ATOM   9380  C CG    . LEU B  1 95   ? -11.356 48.187  120.142 1.00 36.11 ? 93   LEU B CG    1 
ATOM   9381  C CD1   . LEU B  1 95   ? -10.471 46.976  120.398 1.00 33.34 ? 93   LEU B CD1   1 
ATOM   9382  C CD2   . LEU B  1 95   ? -10.638 49.472  120.500 1.00 33.80 ? 93   LEU B CD2   1 
ATOM   9383  N N     . SER B  1 96   ? -12.359 50.012  115.989 1.00 31.04 ? 94   SER B N     1 
ATOM   9384  C CA    . SER B  1 96   ? -12.394 49.712  114.577 1.00 30.73 ? 94   SER B CA    1 
ATOM   9385  C C     . SER B  1 96   ? -11.775 48.336  114.346 1.00 28.40 ? 94   SER B C     1 
ATOM   9386  O O     . SER B  1 96   ? -11.131 47.762  115.230 1.00 29.34 ? 94   SER B O     1 
ATOM   9387  C CB    . SER B  1 96   ? -11.648 50.784  113.788 1.00 30.82 ? 94   SER B CB    1 
ATOM   9388  O OG    . SER B  1 96   ? -10.246 50.678  113.982 1.00 27.67 ? 94   SER B OG    1 
ATOM   9389  N N     . SER B  1 97   ? -11.971 47.804  113.141 1.00 26.13 ? 95   SER B N     1 
ATOM   9390  C CA    . SER B  1 97   ? -11.306 46.555  112.770 1.00 29.69 ? 95   SER B CA    1 
ATOM   9391  C C     . SER B  1 97   ? -9.785  46.682  112.833 1.00 29.68 ? 95   SER B C     1 
ATOM   9392  O O     . SER B  1 97   ? -9.105  45.818  113.401 1.00 27.70 ? 95   SER B O     1 
ATOM   9393  C CB    . SER B  1 97   ? -11.755 46.125  111.374 1.00 28.76 ? 95   SER B CB    1 
ATOM   9394  O OG    . SER B  1 97   ? -13.145 45.872  111.412 1.00 37.54 ? 95   SER B OG    1 
ATOM   9395  N N     . GLN B  1 98   ? -9.228  47.747  112.241 1.00 25.94 ? 96   GLN B N     1 
ATOM   9396  C CA    . GLN B  1 98   ? -7.780  47.933  112.282 1.00 26.94 ? 96   GLN B CA    1 
ATOM   9397  C C     . GLN B  1 98   ? -7.292  48.073  113.717 1.00 27.60 ? 96   GLN B C     1 
ATOM   9398  O O     . GLN B  1 98   ? -6.201  47.603  114.060 1.00 26.04 ? 96   GLN B O     1 
ATOM   9399  C CB    . GLN B  1 98   ? -7.360  49.154  111.458 1.00 26.58 ? 96   GLN B CB    1 
ATOM   9400  C CG    . GLN B  1 98   ? -7.344  48.935  109.939 1.00 26.09 ? 96   GLN B CG    1 
ATOM   9401  C CD    . GLN B  1 98   ? -6.345  47.879  109.504 1.00 25.82 ? 96   GLN B CD    1 
ATOM   9402  O OE1   . GLN B  1 98   ? -6.624  46.681  109.579 1.00 31.60 ? 96   GLN B OE1   1 
ATOM   9403  N NE2   . GLN B  1 98   ? -5.176  48.314  109.036 1.00 24.88 ? 96   GLN B NE2   1 
ATOM   9404  N N     . GLU B  1 99   ? -8.085  48.713  114.573 1.00 27.23 ? 97   GLU B N     1 
ATOM   9405  C CA    . GLU B  1 99   ? -7.688  48.810  115.975 1.00 27.90 ? 97   GLU B CA    1 
ATOM   9406  C C     . GLU B  1 99   ? -7.731  47.444  116.649 1.00 28.30 ? 97   GLU B C     1 
ATOM   9407  O O     . GLU B  1 99   ? -6.865  47.125  117.474 1.00 26.78 ? 97   GLU B O     1 
ATOM   9408  C CB    . GLU B  1 99   ? -8.576  49.814  116.712 1.00 26.65 ? 97   GLU B CB    1 
ATOM   9409  C CG    . GLU B  1 99   ? -8.224  51.267  116.412 1.00 25.08 ? 97   GLU B CG    1 
ATOM   9410  C CD    . GLU B  1 99   ? -9.287  52.249  116.896 1.00 28.89 ? 97   GLU B CD    1 
ATOM   9411  O OE1   . GLU B  1 99   ? -10.348 51.805  117.375 1.00 28.82 ? 97   GLU B OE1   1 
ATOM   9412  O OE2   . GLU B  1 99   ? -9.057  53.474  116.800 1.00 30.43 ? 97   GLU B OE2   1 
ATOM   9413  N N     . GLY B  1 100  ? -8.722  46.618  116.303 1.00 28.97 ? 98   GLY B N     1 
ATOM   9414  C CA    . GLY B  1 100  ? -8.785  45.281  116.877 1.00 32.11 ? 98   GLY B CA    1 
ATOM   9415  C C     . GLY B  1 100  ? -7.592  44.428  116.482 1.00 28.44 ? 98   GLY B C     1 
ATOM   9416  O O     . GLY B  1 100  ? -6.992  43.756  117.325 1.00 27.96 ? 98   GLY B O     1 
ATOM   9417  N N     . VAL B  1 101  ? -7.219  44.465  115.202 1.00 26.79 ? 99   VAL B N     1 
ATOM   9418  C CA    . VAL B  1 101  ? -6.055  43.719  114.727 1.00 29.90 ? 99   VAL B CA    1 
ATOM   9419  C C     . VAL B  1 101  ? -4.782  44.241  115.380 1.00 28.41 ? 99   VAL B C     1 
ATOM   9420  O O     . VAL B  1 101  ? -3.932  43.461  115.831 1.00 25.16 ? 99   VAL B O     1 
ATOM   9421  C CB    . VAL B  1 101  ? -5.964  43.793  113.194 1.00 25.95 ? 99   VAL B CB    1 
ATOM   9422  C CG1   . VAL B  1 101  ? -4.677  43.141  112.700 1.00 24.74 ? 99   VAL B CG1   1 
ATOM   9423  C CG2   . VAL B  1 101  ? -7.196  43.139  112.560 1.00 27.55 ? 99   VAL B CG2   1 
ATOM   9424  N N     . ALA B  1 102  ? -4.636  45.567  115.452 1.00 26.33 ? 100  ALA B N     1 
ATOM   9425  C CA    . ALA B  1 102  ? -3.446  46.146  116.064 1.00 25.49 ? 100  ALA B CA    1 
ATOM   9426  C C     . ALA B  1 102  ? -3.331  45.767  117.532 1.00 27.10 ? 100  ALA B C     1 
ATOM   9427  O O     . ALA B  1 102  ? -2.228  45.503  118.023 1.00 28.47 ? 100  ALA B O     1 
ATOM   9428  C CB    . ALA B  1 102  ? -3.458  47.664  115.917 1.00 25.33 ? 100  ALA B CB    1 
ATOM   9429  N N     . LEU B  1 103  ? -4.453  45.759  118.255 1.00 24.87 ? 101  LEU B N     1 
ATOM   9430  C CA    . LEU B  1 103  ? -4.421  45.418  119.670 1.00 30.30 ? 101  LEU B CA    1 
ATOM   9431  C C     . LEU B  1 103  ? -3.995  43.972  119.875 1.00 27.72 ? 101  LEU B C     1 
ATOM   9432  O O     . LEU B  1 103  ? -3.180  43.674  120.757 1.00 26.56 ? 101  LEU B O     1 
ATOM   9433  C CB    . LEU B  1 103  ? -5.792  45.662  120.287 1.00 29.89 ? 101  LEU B CB    1 
ATOM   9434  C CG    . LEU B  1 103  ? -5.971  45.238  121.740 1.00 27.78 ? 101  LEU B CG    1 
ATOM   9435  C CD1   . LEU B  1 103  ? -5.139  46.118  122.658 1.00 26.89 ? 101  LEU B CD1   1 
ATOM   9436  C CD2   . LEU B  1 103  ? -7.437  45.337  122.094 1.00 30.63 ? 101  LEU B CD2   1 
ATOM   9437  N N     . MET B  1 104  ? -4.535  43.060  119.070 1.00 25.98 ? 102  MET B N     1 
ATOM   9438  C CA    . MET B  1 104  ? -4.143  41.661  119.190 1.00 29.97 ? 102  MET B CA    1 
ATOM   9439  C C     . MET B  1 104  ? -2.671  41.458  118.865 1.00 28.17 ? 102  MET B C     1 
ATOM   9440  O O     . MET B  1 104  ? -2.023  40.606  119.482 1.00 30.62 ? 102  MET B O     1 
ATOM   9441  C CB    . MET B  1 104  ? -5.031  40.791  118.301 1.00 28.23 ? 102  MET B CB    1 
ATOM   9442  C CG    . MET B  1 104  ? -6.511  40.892  118.680 1.00 28.57 ? 102  MET B CG    1 
ATOM   9443  S SD    . MET B  1 104  ? -6.812  40.524  120.424 1.00 39.06 ? 102  MET B SD    1 
ATOM   9444  C CE    . MET B  1 104  ? -6.467  38.768  120.435 1.00 43.47 ? 102  MET B CE    1 
ATOM   9445  N N     . CYS B  1 105  ? -2.122  42.227  117.911 1.00 22.41 ? 103  CYS B N     1 
ATOM   9446  C CA    . CYS B  1 105  ? -0.686  42.162  117.632 1.00 27.15 ? 103  CYS B CA    1 
ATOM   9447  C C     . CYS B  1 105  ? 0.112   42.603  118.842 1.00 29.77 ? 103  CYS B C     1 
ATOM   9448  O O     . CYS B  1 105  ? 1.101   41.960  119.222 1.00 29.80 ? 103  CYS B O     1 
ATOM   9449  C CB    . CYS B  1 105  ? -0.319  43.033  116.427 1.00 22.40 ? 103  CYS B CB    1 
ATOM   9450  S SG    . CYS B  1 105  ? -0.948  42.404  114.876 1.00 26.70 ? 103  CYS B SG    1 
ATOM   9451  N N     . LEU B  1 106  ? -0.308  43.711  119.459 1.00 25.18 ? 104  LEU B N     1 
ATOM   9452  C CA    . LEU B  1 106  ? 0.332   44.155  120.689 1.00 26.48 ? 104  LEU B CA    1 
ATOM   9453  C C     . LEU B  1 106  ? 0.192   43.112  121.792 1.00 29.92 ? 104  LEU B C     1 
ATOM   9454  O O     . LEU B  1 106  ? 1.144   42.864  122.545 1.00 27.90 ? 104  LEU B O     1 
ATOM   9455  C CB    . LEU B  1 106  ? -0.263  45.489  121.140 1.00 27.46 ? 104  LEU B CB    1 
ATOM   9456  C CG    . LEU B  1 106  ? 0.280   45.955  122.494 1.00 28.05 ? 104  LEU B CG    1 
ATOM   9457  C CD1   . LEU B  1 106  ? 1.724   46.363  122.329 1.00 32.45 ? 104  LEU B CD1   1 
ATOM   9458  C CD2   . LEU B  1 106  ? -0.568  47.087  123.084 1.00 28.72 ? 104  LEU B CD2   1 
ATOM   9459  N N     . ALA B  1 107  ? -0.992  42.504  121.919 1.00 26.39 ? 105  ALA B N     1 
ATOM   9460  C CA    . ALA B  1 107  ? -1.186  41.506  122.971 1.00 30.91 ? 105  ALA B CA    1 
ATOM   9461  C C     . ALA B  1 107  ? -0.304  40.284  122.735 1.00 30.29 ? 105  ALA B C     1 
ATOM   9462  O O     . ALA B  1 107  ? 0.219   39.694  123.690 1.00 32.37 ? 105  ALA B O     1 
ATOM   9463  C CB    . ALA B  1 107  ? -2.656  41.102  123.052 1.00 30.64 ? 105  ALA B CB    1 
ATOM   9464  N N     . GLU B  1 108  ? -0.125  39.901  121.471 1.00 31.21 ? 106  GLU B N     1 
ATOM   9465  C CA    . GLU B  1 108  ? 0.766   38.797  121.126 1.00 35.79 ? 106  GLU B CA    1 
ATOM   9466  C C     . GLU B  1 108  ? 2.206   39.120  121.507 1.00 36.70 ? 106  GLU B C     1 
ATOM   9467  O O     . GLU B  1 108  ? 2.894   38.302  122.132 1.00 35.86 ? 106  GLU B O     1 
ATOM   9468  C CB    . GLU B  1 108  ? 0.652   38.487  119.630 1.00 30.11 ? 106  GLU B CB    1 
ATOM   9469  C CG    . GLU B  1 108  ? 1.761   37.587  119.080 1.00 38.00 ? 106  GLU B CG    1 
ATOM   9470  C CD    . GLU B  1 108  ? 1.827   37.571  117.557 1.00 39.09 ? 106  GLU B CD    1 
ATOM   9471  O OE1   . GLU B  1 108  ? 0.846   37.979  116.895 1.00 37.00 ? 106  GLU B OE1   1 
ATOM   9472  O OE2   . GLU B  1 108  ? 2.878   37.160  117.011 1.00 46.41 ? 106  GLU B OE2   1 
ATOM   9473  N N     . ALA B  1 109  ? 2.673   40.322  121.154 1.00 34.43 ? 107  ALA B N     1 
ATOM   9474  C CA    . ALA B  1 109  ? 4.018   40.740  121.536 1.00 35.79 ? 107  ALA B CA    1 
ATOM   9475  C C     . ALA B  1 109  ? 4.186   40.745  123.048 1.00 35.50 ? 107  ALA B C     1 
ATOM   9476  O O     . ALA B  1 109  ? 5.224   40.311  123.564 1.00 35.43 ? 107  ALA B O     1 
ATOM   9477  C CB    . ALA B  1 109  ? 4.328   42.120  120.966 1.00 36.98 ? 107  ALA B CB    1 
ATOM   9478  N N     . LEU B  1 110  ? 3.176   41.226  123.777 1.00 29.35 ? 108  LEU B N     1 
ATOM   9479  C CA    . LEU B  1 110  ? 3.289   41.285  125.235 1.00 35.40 ? 108  LEU B CA    1 
ATOM   9480  C C     . LEU B  1 110  ? 3.326   39.893  125.855 1.00 36.81 ? 108  LEU B C     1 
ATOM   9481  O O     . LEU B  1 110  ? 3.958   39.697  126.900 1.00 35.90 ? 108  LEU B O     1 
ATOM   9482  C CB    . LEU B  1 110  ? 2.139   42.101  125.835 1.00 35.28 ? 108  LEU B CB    1 
ATOM   9483  C CG    . LEU B  1 110  ? 2.152   43.616  125.569 1.00 37.24 ? 108  LEU B CG    1 
ATOM   9484  C CD1   . LEU B  1 110  ? 0.835   44.250  126.010 1.00 30.10 ? 108  LEU B CD1   1 
ATOM   9485  C CD2   . LEU B  1 110  ? 3.334   44.287  126.272 1.00 36.62 ? 108  LEU B CD2   1 
ATOM   9486  N N     . LEU B  1 111  ? 2.663   38.921  125.238 1.00 35.33 ? 109  LEU B N     1 
ATOM   9487  C CA    . LEU B  1 111  ? 2.728   37.548  125.719 1.00 40.91 ? 109  LEU B CA    1 
ATOM   9488  C C     . LEU B  1 111  ? 4.049   36.858  125.393 1.00 42.06 ? 109  LEU B C     1 
ATOM   9489  O O     . LEU B  1 111  ? 4.294   35.760  125.904 1.00 42.08 ? 109  LEU B O     1 
ATOM   9490  C CB    . LEU B  1 111  ? 1.565   36.749  125.144 1.00 38.71 ? 109  LEU B CB    1 
ATOM   9491  C CG    . LEU B  1 111  ? 0.221   37.242  125.673 1.00 36.07 ? 109  LEU B CG    1 
ATOM   9492  C CD1   . LEU B  1 111  ? -0.898  36.698  124.821 1.00 39.80 ? 109  LEU B CD1   1 
ATOM   9493  C CD2   . LEU B  1 111  ? 0.040   36.854  127.131 1.00 39.86 ? 109  LEU B CD2   1 
ATOM   9494  N N     . ARG B  1 112  ? 4.904   37.460  124.564 1.00 42.63 ? 110  ARG B N     1 
ATOM   9495  C CA    . ARG B  1 112  ? 6.265   36.947  124.436 1.00 43.83 ? 110  ARG B CA    1 
ATOM   9496  C C     . ARG B  1 112  ? 7.111   37.273  125.665 1.00 44.03 ? 110  ARG B C     1 
ATOM   9497  O O     . ARG B  1 112  ? 8.267   36.843  125.745 1.00 46.97 ? 110  ARG B O     1 
ATOM   9498  C CB    . ARG B  1 112  ? 6.918   37.480  123.149 1.00 40.34 ? 110  ARG B CB    1 
ATOM   9499  C CG    . ARG B  1 112  ? 6.170   37.070  121.872 1.00 43.47 ? 110  ARG B CG    1 
ATOM   9500  C CD    . ARG B  1 112  ? 6.974   37.258  120.567 1.00 52.82 ? 110  ARG B CD    1 
ATOM   9501  N NE    . ARG B  1 112  ? 6.997   38.635  120.079 1.00 52.08 ? 110  ARG B NE    1 
ATOM   9502  C CZ    . ARG B  1 112  ? 6.263   39.105  119.076 1.00 54.68 ? 110  ARG B CZ    1 
ATOM   9503  N NH1   . ARG B  1 112  ? 5.424   38.331  118.405 1.00 53.20 ? 110  ARG B NH1   1 
ATOM   9504  N NH2   . ARG B  1 112  ? 6.375   40.387  118.734 1.00 58.33 ? 110  ARG B NH2   1 
ATOM   9505  N N     . ILE B  1 113  ? 6.546   38.001  126.623 1.00 42.76 ? 111  ILE B N     1 
ATOM   9506  C CA    . ILE B  1 113  ? 7.165   38.249  127.920 1.00 40.90 ? 111  ILE B CA    1 
ATOM   9507  C C     . ILE B  1 113  ? 6.555   37.260  128.917 1.00 48.56 ? 111  ILE B C     1 
ATOM   9508  O O     . ILE B  1 113  ? 5.397   37.449  129.327 1.00 45.89 ? 111  ILE B O     1 
ATOM   9509  C CB    . ILE B  1 113  ? 6.951   39.697  128.373 1.00 39.93 ? 111  ILE B CB    1 
ATOM   9510  C CG1   . ILE B  1 113  ? 7.418   40.665  127.285 1.00 42.96 ? 111  ILE B CG1   1 
ATOM   9511  C CG2   . ILE B  1 113  ? 7.668   39.952  129.683 1.00 39.96 ? 111  ILE B CG2   1 
ATOM   9512  C CD1   . ILE B  1 113  ? 7.156   42.119  127.615 1.00 44.38 ? 111  ILE B CD1   1 
ATOM   9513  N N     . PRO B  1 114  ? 7.288   36.222  129.338 1.00 52.77 ? 112  PRO B N     1 
ATOM   9514  C CA    . PRO B  1 114  ? 6.646   35.111  130.066 1.00 46.28 ? 112  PRO B CA    1 
ATOM   9515  C C     . PRO B  1 114  ? 6.295   35.388  131.521 1.00 44.03 ? 112  PRO B C     1 
ATOM   9516  O O     . PRO B  1 114  ? 5.391   34.725  132.047 1.00 44.87 ? 112  PRO B O     1 
ATOM   9517  C CB    . PRO B  1 114  ? 7.684   33.980  129.959 1.00 48.23 ? 112  PRO B CB    1 
ATOM   9518  C CG    . PRO B  1 114  ? 8.985   34.684  129.766 1.00 47.68 ? 112  PRO B CG    1 
ATOM   9519  C CD    . PRO B  1 114  ? 8.678   35.916  128.959 1.00 47.63 ? 112  PRO B CD    1 
ATOM   9520  N N     . ASP B  1 115  ? 6.956   36.319  132.200 1.00 43.49 ? 113  ASP B N     1 
ATOM   9521  C CA    . ASP B  1 115  ? 6.627   36.599  133.591 1.00 48.14 ? 113  ASP B CA    1 
ATOM   9522  C C     . ASP B  1 115  ? 5.488   37.606  133.665 1.00 48.42 ? 113  ASP B C     1 
ATOM   9523  O O     . ASP B  1 115  ? 5.582   38.697  133.096 1.00 45.69 ? 113  ASP B O     1 
ATOM   9524  C CB    . ASP B  1 115  ? 7.834   37.130  134.361 1.00 45.39 ? 113  ASP B CB    1 
ATOM   9525  C CG    . ASP B  1 115  ? 7.490   37.476  135.789 1.00 51.13 ? 113  ASP B CG    1 
ATOM   9526  O OD1   . ASP B  1 115  ? 7.029   36.575  136.523 1.00 58.70 ? 113  ASP B OD1   1 
ATOM   9527  O OD2   . ASP B  1 115  ? 7.664   38.649  136.182 1.00 53.41 ? 113  ASP B OD2   1 
ATOM   9528  N N     . THR B  1 116  ? 4.428   37.240  134.393 1.00 47.34 ? 114  THR B N     1 
ATOM   9529  C CA    . THR B  1 116  ? 3.247   38.095  134.488 1.00 49.72 ? 114  THR B CA    1 
ATOM   9530  C C     . THR B  1 116  ? 3.593   39.457  135.079 1.00 49.24 ? 114  THR B C     1 
ATOM   9531  O O     . THR B  1 116  ? 3.150   40.493  134.571 1.00 47.43 ? 114  THR B O     1 
ATOM   9532  C CB    . THR B  1 116  ? 2.162   37.404  135.322 1.00 51.74 ? 114  THR B CB    1 
ATOM   9533  O OG1   . THR B  1 116  ? 1.721   36.215  134.654 1.00 54.35 ? 114  THR B OG1   1 
ATOM   9534  C CG2   . THR B  1 116  ? 0.967   38.324  135.534 1.00 54.49 ? 114  THR B CG2   1 
ATOM   9535  N N     . ALA B  1 117  ? 4.403   39.477  136.141 1.00 51.30 ? 115  ALA B N     1 
ATOM   9536  C CA    . ALA B  1 117  ? 4.734   40.739  136.794 1.00 47.47 ? 115  ALA B CA    1 
ATOM   9537  C C     . ALA B  1 117  ? 5.562   41.644  135.886 1.00 46.72 ? 115  ALA B C     1 
ATOM   9538  O O     . ALA B  1 117  ? 5.371   42.866  135.880 1.00 48.00 ? 115  ALA B O     1 
ATOM   9539  C CB    . ALA B  1 117  ? 5.471   40.470  138.109 1.00 51.69 ? 115  ALA B CB    1 
ATOM   9540  N N     . THR B  1 118  ? 6.493   41.068  135.120 1.00 46.38 ? 116  THR B N     1 
ATOM   9541  C CA    . THR B  1 118  ? 7.287   41.868  134.190 1.00 47.41 ? 116  THR B CA    1 
ATOM   9542  C C     . THR B  1 118  ? 6.411   42.437  133.083 1.00 42.76 ? 116  THR B C     1 
ATOM   9543  O O     . THR B  1 118  ? 6.514   43.620  132.737 1.00 43.03 ? 116  THR B O     1 
ATOM   9544  C CB    . THR B  1 118  ? 8.415   41.028  133.585 1.00 42.64 ? 116  THR B CB    1 
ATOM   9545  O OG1   . THR B  1 118  ? 9.216   40.463  134.633 1.00 48.99 ? 116  THR B OG1   1 
ATOM   9546  C CG2   . THR B  1 118  ? 9.294   41.891  132.695 1.00 44.32 ? 116  THR B CG2   1 
ATOM   9547  N N     . ARG B  1 119  ? 5.553   41.597  132.510 1.00 44.43 ? 117  ARG B N     1 
ATOM   9548  C CA    . ARG B  1 119  ? 4.653   42.055  131.457 1.00 41.52 ? 117  ARG B CA    1 
ATOM   9549  C C     . ARG B  1 119  ? 3.701   43.127  131.978 1.00 41.48 ? 117  ARG B C     1 
ATOM   9550  O O     . ARG B  1 119  ? 3.515   44.170  131.342 1.00 39.95 ? 117  ARG B O     1 
ATOM   9551  C CB    . ARG B  1 119  ? 3.877   40.872  130.893 1.00 42.58 ? 117  ARG B CB    1 
ATOM   9552  C CG    . ARG B  1 119  ? 2.942   41.241  129.774 1.00 35.49 ? 117  ARG B CG    1 
ATOM   9553  C CD    . ARG B  1 119  ? 2.018   40.090  129.446 1.00 42.78 ? 117  ARG B CD    1 
ATOM   9554  N NE    . ARG B  1 119  ? 2.646   38.786  129.640 1.00 45.11 ? 117  ARG B NE    1 
ATOM   9555  C CZ    . ARG B  1 119  ? 2.170   37.838  130.438 1.00 49.62 ? 117  ARG B CZ    1 
ATOM   9556  N NH1   . ARG B  1 119  ? 1.051   38.008  131.127 1.00 43.45 ? 117  ARG B NH1   1 
ATOM   9557  N NH2   . ARG B  1 119  ? 2.825   36.684  130.539 1.00 50.04 ? 117  ARG B NH2   1 
ATOM   9558  N N     . ASP B  1 120  ? 3.098   42.890  133.148 1.00 44.56 ? 118  ASP B N     1 
ATOM   9559  C CA    . ASP B  1 120  ? 2.150   43.847  133.712 1.00 46.37 ? 118  ASP B CA    1 
ATOM   9560  C C     . ASP B  1 120  ? 2.816   45.167  134.071 1.00 44.60 ? 118  ASP B C     1 
ATOM   9561  O O     . ASP B  1 120  ? 2.168   46.221  134.021 1.00 43.12 ? 118  ASP B O     1 
ATOM   9562  C CB    . ASP B  1 120  ? 1.465   43.256  134.946 1.00 47.93 ? 118  ASP B CB    1 
ATOM   9563  C CG    . ASP B  1 120  ? 0.463   42.173  134.596 1.00 50.21 ? 118  ASP B CG    1 
ATOM   9564  O OD1   . ASP B  1 120  ? 0.365   41.802  133.403 1.00 52.13 ? 118  ASP B OD1   1 
ATOM   9565  O OD2   . ASP B  1 120  ? -0.228  41.693  135.520 1.00 53.80 ? 118  ASP B OD2   1 
ATOM   9566  N N     . ALA B  1 121  ? 4.097   45.135  134.449 1.00 47.22 ? 119  ALA B N     1 
ATOM   9567  C CA    . ALA B  1 121  ? 4.804   46.371  134.760 1.00 44.35 ? 119  ALA B CA    1 
ATOM   9568  C C     . ALA B  1 121  ? 5.143   47.148  133.493 1.00 46.02 ? 119  ALA B C     1 
ATOM   9569  O O     . ALA B  1 121  ? 5.070   48.381  133.484 1.00 46.78 ? 119  ALA B O     1 
ATOM   9570  C CB    . ALA B  1 121  ? 6.071   46.074  135.566 1.00 47.24 ? 119  ALA B CB    1 
ATOM   9571  N N     . LEU B  1 122  ? 5.514   46.450  132.417 1.00 42.00 ? 120  LEU B N     1 
ATOM   9572  C CA    . LEU B  1 122  ? 5.737   47.136  131.149 1.00 43.10 ? 120  LEU B CA    1 
ATOM   9573  C C     . LEU B  1 122  ? 4.455   47.795  130.654 1.00 42.39 ? 120  LEU B C     1 
ATOM   9574  O O     . LEU B  1 122  ? 4.489   48.905  130.109 1.00 41.60 ? 120  LEU B O     1 
ATOM   9575  C CB    . LEU B  1 122  ? 6.275   46.164  130.099 1.00 42.34 ? 120  LEU B CB    1 
ATOM   9576  C CG    . LEU B  1 122  ? 6.520   46.797  128.724 1.00 43.98 ? 120  LEU B CG    1 
ATOM   9577  C CD1   . LEU B  1 122  ? 7.725   47.730  128.764 1.00 43.94 ? 120  LEU B CD1   1 
ATOM   9578  C CD2   . LEU B  1 122  ? 6.660   45.748  127.613 1.00 41.35 ? 120  LEU B CD2   1 
ATOM   9579  N N     . ILE B  1 123  ? 3.314   47.129  130.852 1.00 39.16 ? 121  ILE B N     1 
ATOM   9580  C CA    . ILE B  1 123  ? 2.029   47.674  130.416 1.00 42.66 ? 121  ILE B CA    1 
ATOM   9581  C C     . ILE B  1 123  ? 1.694   48.936  131.202 1.00 47.27 ? 121  ILE B C     1 
ATOM   9582  O O     . ILE B  1 123  ? 1.358   49.978  130.625 1.00 47.76 ? 121  ILE B O     1 
ATOM   9583  C CB    . ILE B  1 123  ? 0.920   46.615  130.566 1.00 38.33 ? 121  ILE B CB    1 
ATOM   9584  C CG1   . ILE B  1 123  ? 1.125   45.461  129.582 1.00 34.62 ? 121  ILE B CG1   1 
ATOM   9585  C CG2   . ILE B  1 123  ? -0.453  47.244  130.390 1.00 40.71 ? 121  ILE B CG2   1 
ATOM   9586  C CD1   . ILE B  1 123  ? 0.207   44.292  129.838 1.00 35.70 ? 121  ILE B CD1   1 
ATOM   9587  N N     . ARG B  1 124  ? 1.774   48.858  132.532 1.00 42.51 ? 122  ARG B N     1 
ATOM   9588  C CA    . ARG B  1 124  ? 1.361   49.981  133.368 1.00 49.91 ? 122  ARG B CA    1 
ATOM   9589  C C     . ARG B  1 124  ? 2.318   51.163  133.255 1.00 52.64 ? 122  ARG B C     1 
ATOM   9590  O O     . ARG B  1 124  ? 1.898   52.314  133.416 1.00 59.23 ? 122  ARG B O     1 
ATOM   9591  C CB    . ARG B  1 124  ? 1.242   49.536  134.828 1.00 46.99 ? 122  ARG B CB    1 
ATOM   9592  N N     . ASP B  1 125  ? 3.593   50.912  132.965 1.00 50.09 ? 123  ASP B N     1 
ATOM   9593  C CA    . ASP B  1 125  ? 4.614   51.942  133.062 1.00 52.30 ? 123  ASP B CA    1 
ATOM   9594  C C     . ASP B  1 125  ? 5.181   52.395  131.722 1.00 50.00 ? 123  ASP B C     1 
ATOM   9595  O O     . ASP B  1 125  ? 5.923   53.383  131.690 1.00 55.42 ? 123  ASP B O     1 
ATOM   9596  C CB    . ASP B  1 125  ? 5.764   51.455  133.961 1.00 50.10 ? 123  ASP B CB    1 
ATOM   9597  C CG    . ASP B  1 125  ? 5.285   51.002  135.336 1.00 55.10 ? 123  ASP B CG    1 
ATOM   9598  O OD1   . ASP B  1 125  ? 4.356   51.629  135.885 1.00 56.90 ? 123  ASP B OD1   1 
ATOM   9599  O OD2   . ASP B  1 125  ? 5.840   50.017  135.873 1.00 57.32 ? 123  ASP B OD2   1 
ATOM   9600  N N     . LYS B  1 126  ? 4.859   51.724  130.617 1.00 47.87 ? 124  LYS B N     1 
ATOM   9601  C CA    . LYS B  1 126  ? 5.477   52.103  129.354 1.00 46.44 ? 124  LYS B CA    1 
ATOM   9602  C C     . LYS B  1 126  ? 4.483   52.086  128.198 1.00 49.79 ? 124  LYS B C     1 
ATOM   9603  O O     . LYS B  1 126  ? 4.388   53.057  127.438 1.00 52.22 ? 124  LYS B O     1 
ATOM   9604  C CB    . LYS B  1 126  ? 6.660   51.180  129.053 1.00 49.80 ? 124  LYS B CB    1 
ATOM   9605  N N     . ILE B  1 127  ? 3.734   50.993  128.057 1.00 46.79 ? 125  ILE B N     1 
ATOM   9606  C CA    . ILE B  1 127  ? 2.858   50.833  126.898 1.00 44.28 ? 125  ILE B CA    1 
ATOM   9607  C C     . ILE B  1 127  ? 1.597   51.678  127.044 1.00 47.58 ? 125  ILE B C     1 
ATOM   9608  O O     . ILE B  1 127  ? 1.171   52.351  126.098 1.00 44.51 ? 125  ILE B O     1 
ATOM   9609  C CB    . ILE B  1 127  ? 2.512   49.347  126.693 1.00 43.15 ? 125  ILE B CB    1 
ATOM   9610  C CG1   . ILE B  1 127  ? 3.789   48.506  126.622 1.00 42.31 ? 125  ILE B CG1   1 
ATOM   9611  C CG2   . ILE B  1 127  ? 1.653   49.168  125.443 1.00 41.80 ? 125  ILE B CG2   1 
ATOM   9612  C CD1   . ILE B  1 127  ? 4.761   48.957  125.567 1.00 47.18 ? 125  ILE B CD1   1 
ATOM   9613  N N     . ALA B  1 128  ? 0.970   51.652  128.222 1.00 43.03 ? 126  ALA B N     1 
ATOM   9614  C CA    . ALA B  1 128  ? -0.275  52.389  128.407 1.00 47.10 ? 126  ALA B CA    1 
ATOM   9615  C C     . ALA B  1 128  ? -0.089  53.897  128.324 1.00 51.81 ? 126  ALA B C     1 
ATOM   9616  O O     . ALA B  1 128  ? -1.084  54.629  128.368 1.00 48.70 ? 126  ALA B O     1 
ATOM   9617  C CB    . ALA B  1 128  ? -0.919  52.020  129.739 1.00 42.96 ? 126  ALA B CB    1 
ATOM   9618  N N     . ASP B  1 129  ? 1.150   54.373  128.205 1.00 55.22 ? 127  ASP B N     1 
ATOM   9619  C CA    . ASP B  1 129  ? 1.446   55.779  127.972 1.00 57.21 ? 127  ASP B CA    1 
ATOM   9620  C C     . ASP B  1 129  ? 1.841   56.047  126.525 1.00 56.23 ? 127  ASP B C     1 
ATOM   9621  O O     . ASP B  1 129  ? 2.588   56.990  126.249 1.00 63.24 ? 127  ASP B O     1 
ATOM   9622  C CB    . ASP B  1 129  ? 2.545   56.252  128.925 1.00 59.80 ? 127  ASP B CB    1 
ATOM   9623  C CG    . ASP B  1 129  ? 2.087   56.283  130.373 1.00 64.27 ? 127  ASP B CG    1 
ATOM   9624  O OD1   . ASP B  1 129  ? 0.913   56.633  130.625 1.00 66.82 ? 127  ASP B OD1   1 
ATOM   9625  O OD2   . ASP B  1 129  ? 2.899   55.952  131.261 1.00 70.58 ? 127  ASP B OD2   1 
ATOM   9626  N N     . GLY B  1 130  ? 1.361   55.222  125.593 1.00 54.20 ? 128  GLY B N     1 
ATOM   9627  C CA    . GLY B  1 130  ? 1.634   55.401  124.182 1.00 53.51 ? 128  GLY B CA    1 
ATOM   9628  C C     . GLY B  1 130  ? 3.038   55.060  123.740 1.00 58.09 ? 128  GLY B C     1 
ATOM   9629  O O     . GLY B  1 130  ? 3.284   54.978  122.531 1.00 52.58 ? 128  GLY B O     1 
ATOM   9630  N N     . ASN B  1 131  ? 3.973   54.864  124.670 1.00 66.50 ? 129  ASN B N     1 
ATOM   9631  C CA    . ASN B  1 131  ? 5.348   54.503  124.330 1.00 65.08 ? 129  ASN B CA    1 
ATOM   9632  C C     . ASN B  1 131  ? 5.389   52.998  124.084 1.00 66.20 ? 129  ASN B C     1 
ATOM   9633  O O     . ASN B  1 131  ? 5.829   52.204  124.920 1.00 70.28 ? 129  ASN B O     1 
ATOM   9634  C CB    . ASN B  1 131  ? 6.308   54.925  125.437 1.00 60.78 ? 129  ASN B CB    1 
ATOM   9635  N N     . TRP B  1 132  ? 4.900   52.599  122.910 1.00 57.88 ? 130  TRP B N     1 
ATOM   9636  C CA    . TRP B  1 132  ? 4.898   51.196  122.520 1.00 55.45 ? 130  TRP B CA    1 
ATOM   9637  C C     . TRP B  1 132  ? 5.911   50.863  121.439 1.00 59.42 ? 130  TRP B C     1 
ATOM   9638  O O     . TRP B  1 132  ? 6.388   49.727  121.392 1.00 60.70 ? 130  TRP B O     1 
ATOM   9639  C CB    . TRP B  1 132  ? 3.497   50.766  122.050 1.00 50.76 ? 130  TRP B CB    1 
ATOM   9640  C CG    . TRP B  1 132  ? 2.974   51.460  120.813 1.00 45.54 ? 130  TRP B CG    1 
ATOM   9641  C CD1   . TRP B  1 132  ? 2.139   52.542  120.768 1.00 45.25 ? 130  TRP B CD1   1 
ATOM   9642  C CD2   . TRP B  1 132  ? 3.233   51.099  119.450 1.00 43.51 ? 130  TRP B CD2   1 
ATOM   9643  N NE1   . TRP B  1 132  ? 1.866   52.878  119.462 1.00 41.24 ? 130  TRP B NE1   1 
ATOM   9644  C CE2   . TRP B  1 132  ? 2.529   52.012  118.634 1.00 43.21 ? 130  TRP B CE2   1 
ATOM   9645  C CE3   . TRP B  1 132  ? 3.991   50.096  118.840 1.00 43.42 ? 130  TRP B CE3   1 
ATOM   9646  C CZ2   . TRP B  1 132  ? 2.569   51.952  117.244 1.00 36.38 ? 130  TRP B CZ2   1 
ATOM   9647  C CZ3   . TRP B  1 132  ? 4.026   50.037  117.466 1.00 42.74 ? 130  TRP B CZ3   1 
ATOM   9648  C CH2   . TRP B  1 132  ? 3.318   50.959  116.678 1.00 35.52 ? 130  TRP B CH2   1 
ATOM   9649  N N     . LYS B  1 133  ? 6.262   51.824  120.581 1.00 63.35 ? 131  LYS B N     1 
ATOM   9650  C CA    . LYS B  1 133  ? 7.206   51.538  119.505 1.00 67.89 ? 131  LYS B CA    1 
ATOM   9651  C C     . LYS B  1 133  ? 8.584   51.189  120.054 1.00 70.81 ? 131  LYS B C     1 
ATOM   9652  O O     . LYS B  1 133  ? 9.222   50.236  119.590 1.00 73.55 ? 131  LYS B O     1 
ATOM   9653  C CB    . LYS B  1 133  ? 7.291   52.733  118.555 1.00 67.14 ? 131  LYS B CB    1 
ATOM   9654  N N     . SER B  1 134  ? 9.057   51.944  121.048 1.00 73.51 ? 132  SER B N     1 
ATOM   9655  C CA    . SER B  1 134  ? 10.393  51.716  121.589 1.00 74.16 ? 132  SER B CA    1 
ATOM   9656  C C     . SER B  1 134  ? 10.473  50.386  122.331 1.00 74.46 ? 132  SER B C     1 
ATOM   9657  O O     . SER B  1 134  ? 11.356  49.564  122.059 1.00 72.73 ? 132  SER B O     1 
ATOM   9658  C CB    . SER B  1 134  ? 10.787  52.872  122.509 1.00 68.89 ? 132  SER B CB    1 
ATOM   9659  N N     . HIS B  1 135  ? 9.549   50.153  123.268 1.00 72.58 ? 133  HIS B N     1 
ATOM   9660  C CA    . HIS B  1 135  ? 9.618   48.968  124.118 1.00 73.31 ? 133  HIS B CA    1 
ATOM   9661  C C     . HIS B  1 135  ? 9.325   47.674  123.364 1.00 72.68 ? 133  HIS B C     1 
ATOM   9662  O O     . HIS B  1 135  ? 9.690   46.597  123.848 1.00 70.46 ? 133  HIS B O     1 
ATOM   9663  C CB    . HIS B  1 135  ? 8.651   49.113  125.295 1.00 67.55 ? 133  HIS B CB    1 
ATOM   9664  N N     . LEU B  1 136  ? 8.670   47.747  122.207 1.00 71.48 ? 134  LEU B N     1 
ATOM   9665  C CA    . LEU B  1 136  ? 8.381   46.556  121.406 1.00 69.78 ? 134  LEU B CA    1 
ATOM   9666  C C     . LEU B  1 136  ? 8.531   46.858  119.914 1.00 71.52 ? 134  LEU B C     1 
ATOM   9667  O O     . LEU B  1 136  ? 9.514   46.470  119.281 1.00 73.87 ? 134  LEU B O     1 
ATOM   9668  C CB    . LEU B  1 136  ? 6.969   46.034  121.696 1.00 62.79 ? 134  LEU B CB    1 
ATOM   9669  C CG    . LEU B  1 136  ? 6.578   45.763  123.151 1.00 57.87 ? 134  LEU B CG    1 
ATOM   9670  C CD1   . LEU B  1 136  ? 5.077   45.659  123.272 1.00 48.67 ? 134  LEU B CD1   1 
ATOM   9671  C CD2   . LEU B  1 136  ? 7.250   44.503  123.680 1.00 55.33 ? 134  LEU B CD2   1 
ATOM   9672  N N     . ARG B  1 140  ? 11.904  43.853  114.895 1.00 45.09 ? 138  ARG B N     1 
ATOM   9673  C CA    . ARG B  1 140  ? 10.799  43.322  114.106 1.00 51.23 ? 138  ARG B CA    1 
ATOM   9674  C C     . ARG B  1 140  ? 9.510   44.102  114.372 1.00 47.18 ? 138  ARG B C     1 
ATOM   9675  O O     . ARG B  1 140  ? 9.215   44.490  115.508 1.00 38.10 ? 138  ARG B O     1 
ATOM   9676  C CB    . ARG B  1 140  ? 10.590  41.829  114.398 1.00 44.26 ? 138  ARG B CB    1 
ATOM   9677  N N     . SER B  1 141  ? 8.755   44.336  113.302 1.00 37.92 ? 139  SER B N     1 
ATOM   9678  C CA    . SER B  1 141  ? 7.496   45.050  113.415 1.00 35.55 ? 139  SER B CA    1 
ATOM   9679  C C     . SER B  1 141  ? 6.571   44.356  114.410 1.00 35.34 ? 139  SER B C     1 
ATOM   9680  O O     . SER B  1 141  ? 6.545   43.126  114.519 1.00 34.93 ? 139  SER B O     1 
ATOM   9681  C CB    . SER B  1 141  ? 6.826   45.144  112.043 1.00 32.87 ? 139  SER B CB    1 
ATOM   9682  O OG    . SER B  1 141  ? 5.497   45.640  112.144 1.00 34.60 ? 139  SER B OG    1 
ATOM   9683  N N     . LEU B  1 142  ? 5.809   45.161  115.147 1.00 31.40 ? 140  LEU B N     1 
ATOM   9684  C CA    . LEU B  1 142  ? 4.751   44.608  115.977 1.00 30.95 ? 140  LEU B CA    1 
ATOM   9685  C C     . LEU B  1 142  ? 3.731   43.838  115.157 1.00 30.93 ? 140  LEU B C     1 
ATOM   9686  O O     . LEU B  1 142  ? 3.007   43.002  115.708 1.00 24.11 ? 140  LEU B O     1 
ATOM   9687  C CB    . LEU B  1 142  ? 4.038   45.728  116.728 1.00 29.30 ? 140  LEU B CB    1 
ATOM   9688  C CG    . LEU B  1 142  ? 3.457   45.286  118.058 1.00 32.28 ? 140  LEU B CG    1 
ATOM   9689  C CD1   . LEU B  1 142  ? 4.565   45.148  119.067 1.00 37.42 ? 140  LEU B CD1   1 
ATOM   9690  C CD2   . LEU B  1 142  ? 2.444   46.265  118.521 1.00 35.08 ? 140  LEU B CD2   1 
ATOM   9691  N N     . PHE B  1 143  ? 3.653   44.112  113.854 1.00 26.97 ? 141  PHE B N     1 
ATOM   9692  C CA    . PHE B  1 143  ? 2.535   43.679  113.031 1.00 27.19 ? 141  PHE B CA    1 
ATOM   9693  C C     . PHE B  1 143  ? 2.896   42.531  112.090 1.00 26.45 ? 141  PHE B C     1 
ATOM   9694  O O     . PHE B  1 143  ? 2.155   42.260  111.143 1.00 25.41 ? 141  PHE B O     1 
ATOM   9695  C CB    . PHE B  1 143  ? 1.996   44.891  112.275 1.00 24.76 ? 141  PHE B CB    1 
ATOM   9696  C CG    . PHE B  1 143  ? 1.672   46.042  113.188 1.00 20.78 ? 141  PHE B CG    1 
ATOM   9697  C CD1   . PHE B  1 143  ? 0.767   45.876  114.226 1.00 20.48 ? 141  PHE B CD1   1 
ATOM   9698  C CD2   . PHE B  1 143  ? 2.291   47.263  113.039 1.00 21.52 ? 141  PHE B CD2   1 
ATOM   9699  C CE1   . PHE B  1 143  ? 0.476   46.906  115.089 1.00 23.42 ? 141  PHE B CE1   1 
ATOM   9700  C CE2   . PHE B  1 143  ? 1.989   48.312  113.893 1.00 22.69 ? 141  PHE B CE2   1 
ATOM   9701  C CZ    . PHE B  1 143  ? 1.093   48.134  114.922 1.00 22.60 ? 141  PHE B CZ    1 
ATOM   9702  N N     . VAL B  1 144  ? 3.980   41.806  112.380 1.00 29.07 ? 142  VAL B N     1 
ATOM   9703  C CA    . VAL B  1 144  ? 4.438   40.734  111.491 1.00 32.74 ? 142  VAL B CA    1 
ATOM   9704  C C     . VAL B  1 144  ? 3.349   39.682  111.285 1.00 29.41 ? 142  VAL B C     1 
ATOM   9705  O O     . VAL B  1 144  ? 3.204   39.125  110.189 1.00 30.66 ? 142  VAL B O     1 
ATOM   9706  C CB    . VAL B  1 144  ? 5.737   40.110  112.039 1.00 31.85 ? 142  VAL B CB    1 
ATOM   9707  C CG1   . VAL B  1 144  ? 6.083   38.836  111.295 1.00 37.76 ? 142  VAL B CG1   1 
ATOM   9708  C CG2   . VAL B  1 144  ? 6.880   41.103  111.925 1.00 38.59 ? 142  VAL B CG2   1 
ATOM   9709  N N     . ASN B  1 145  ? 2.560   39.396  112.322 1.00 32.83 ? 143  ASN B N     1 
ATOM   9710  C CA    . ASN B  1 145  ? 1.506   38.392  112.225 1.00 32.07 ? 143  ASN B CA    1 
ATOM   9711  C C     . ASN B  1 145  ? 0.119   38.993  112.047 1.00 31.19 ? 143  ASN B C     1 
ATOM   9712  O O     . ASN B  1 145  ? -0.878  38.321  112.328 1.00 30.00 ? 143  ASN B O     1 
ATOM   9713  C CB    . ASN B  1 145  ? 1.517   37.490  113.457 1.00 35.31 ? 143  ASN B CB    1 
ATOM   9714  C CG    . ASN B  1 145  ? 2.684   36.539  113.453 1.00 37.82 ? 143  ASN B CG    1 
ATOM   9715  O OD1   . ASN B  1 145  ? 3.029   35.979  112.411 1.00 44.04 ? 143  ASN B OD1   1 
ATOM   9716  N ND2   . ASN B  1 145  ? 3.312   36.359  114.612 1.00 40.65 ? 143  ASN B ND2   1 
ATOM   9717  N N     . ALA B  1 146  ? 0.028   40.242  111.592 1.00 27.42 ? 144  ALA B N     1 
ATOM   9718  C CA    . ALA B  1 146  ? -1.270  40.897  111.596 1.00 26.89 ? 144  ALA B CA    1 
ATOM   9719  C C     . ALA B  1 146  ? -2.217  40.304  110.561 1.00 27.01 ? 144  ALA B C     1 
ATOM   9720  O O     . ALA B  1 146  ? -3.434  40.423  110.722 1.00 29.71 ? 144  ALA B O     1 
ATOM   9721  C CB    . ALA B  1 146  ? -1.112  42.403  111.370 1.00 29.13 ? 144  ALA B CB    1 
ATOM   9722  N N     . ALA B  1 147  ? -1.698  39.669  109.506 1.00 28.99 ? 145  ALA B N     1 
ATOM   9723  C CA    . ALA B  1 147  ? -2.600  38.999  108.569 1.00 28.24 ? 145  ALA B CA    1 
ATOM   9724  C C     . ALA B  1 147  ? -3.394  37.912  109.279 1.00 30.58 ? 145  ALA B C     1 
ATOM   9725  O O     . ALA B  1 147  ? -4.590  37.731  109.021 1.00 31.35 ? 145  ALA B O     1 
ATOM   9726  C CB    . ALA B  1 147  ? -1.817  38.424  107.387 1.00 25.73 ? 145  ALA B CB    1 
ATOM   9727  N N     . THR B  1 148  ? -2.754  37.211  110.219 1.00 28.10 ? 146  THR B N     1 
ATOM   9728  C CA    . THR B  1 148  ? -3.448  36.189  110.995 1.00 28.17 ? 146  THR B CA    1 
ATOM   9729  C C     . THR B  1 148  ? -4.541  36.806  111.857 1.00 34.23 ? 146  THR B C     1 
ATOM   9730  O O     . THR B  1 148  ? -5.693  36.359  111.834 1.00 34.33 ? 146  THR B O     1 
ATOM   9731  C CB    . THR B  1 148  ? -2.443  35.432  111.873 1.00 35.41 ? 146  THR B CB    1 
ATOM   9732  O OG1   . THR B  1 148  ? -1.515  34.725  111.044 1.00 41.33 ? 146  THR B OG1   1 
ATOM   9733  C CG2   . THR B  1 148  ? -3.159  34.454  112.794 1.00 37.18 ? 146  THR B CG2   1 
ATOM   9734  N N     . TRP B  1 149  ? -4.195  37.830  112.640 1.00 27.95 ? 147  TRP B N     1 
ATOM   9735  C CA    . TRP B  1 149  ? -5.204  38.488  113.454 1.00 29.55 ? 147  TRP B CA    1 
ATOM   9736  C C     . TRP B  1 149  ? -6.260  39.165  112.597 1.00 27.10 ? 147  TRP B C     1 
ATOM   9737  O O     . TRP B  1 149  ? -7.424  39.246  113.001 1.00 30.02 ? 147  TRP B O     1 
ATOM   9738  C CB    . TRP B  1 149  ? -4.553  39.504  114.376 1.00 26.52 ? 147  TRP B CB    1 
ATOM   9739  C CG    . TRP B  1 149  ? -3.700  38.841  115.388 1.00 27.50 ? 147  TRP B CG    1 
ATOM   9740  C CD1   . TRP B  1 149  ? -2.343  38.916  115.493 1.00 26.54 ? 147  TRP B CD1   1 
ATOM   9741  C CD2   . TRP B  1 149  ? -4.143  37.963  116.426 1.00 29.81 ? 147  TRP B CD2   1 
ATOM   9742  N NE1   . TRP B  1 149  ? -1.915  38.161  116.557 1.00 26.73 ? 147  TRP B NE1   1 
ATOM   9743  C CE2   . TRP B  1 149  ? -3.001  37.563  117.144 1.00 30.97 ? 147  TRP B CE2   1 
ATOM   9744  C CE3   . TRP B  1 149  ? -5.396  37.490  116.830 1.00 34.08 ? 147  TRP B CE3   1 
ATOM   9745  C CZ2   . TRP B  1 149  ? -3.072  36.705  118.245 1.00 34.13 ? 147  TRP B CZ2   1 
ATOM   9746  C CZ3   . TRP B  1 149  ? -5.466  36.632  117.926 1.00 36.74 ? 147  TRP B CZ3   1 
ATOM   9747  C CH2   . TRP B  1 149  ? -4.308  36.253  118.618 1.00 36.14 ? 147  TRP B CH2   1 
ATOM   9748  N N     . GLY B  1 150  ? -5.867  39.686  111.440 1.00 27.71 ? 148  GLY B N     1 
ATOM   9749  C CA    . GLY B  1 150  ? -6.860  40.228  110.525 1.00 30.50 ? 148  GLY B CA    1 
ATOM   9750  C C     . GLY B  1 150  ? -7.914  39.200  110.164 1.00 34.72 ? 148  GLY B C     1 
ATOM   9751  O O     . GLY B  1 150  ? -9.111  39.502  110.129 1.00 34.60 ? 148  GLY B O     1 
ATOM   9752  N N     . LEU B  1 151  ? -7.481  37.965  109.913 1.00 34.92 ? 149  LEU B N     1 
ATOM   9753  C CA    . LEU B  1 151  ? -8.419  36.879  109.667 1.00 35.24 ? 149  LEU B CA    1 
ATOM   9754  C C     . LEU B  1 151  ? -9.280  36.620  110.895 1.00 34.89 ? 149  LEU B C     1 
ATOM   9755  O O     . LEU B  1 151  ? -10.486 36.389  110.783 1.00 35.58 ? 149  LEU B O     1 
ATOM   9756  C CB    . LEU B  1 151  ? -7.639  35.629  109.257 1.00 36.66 ? 149  LEU B CB    1 
ATOM   9757  C CG    . LEU B  1 151  ? -8.399  34.444  108.679 1.00 43.80 ? 149  LEU B CG    1 
ATOM   9758  C CD1   . LEU B  1 151  ? -9.462  34.934  107.722 1.00 39.70 ? 149  LEU B CD1   1 
ATOM   9759  C CD2   . LEU B  1 151  ? -7.429  33.522  107.967 1.00 43.36 ? 149  LEU B CD2   1 
ATOM   9760  N N     . VAL B  1 152  ? -8.680  36.688  112.083 1.00 36.89 ? 150  VAL B N     1 
ATOM   9761  C CA    . VAL B  1 152  ? -9.416  36.445  113.317 1.00 35.55 ? 150  VAL B CA    1 
ATOM   9762  C C     . VAL B  1 152  ? -10.450 37.538  113.568 1.00 37.94 ? 150  VAL B C     1 
ATOM   9763  O O     . VAL B  1 152  ? -11.564 37.260  114.025 1.00 40.51 ? 150  VAL B O     1 
ATOM   9764  C CB    . VAL B  1 152  ? -8.430  36.325  114.492 1.00 33.86 ? 150  VAL B CB    1 
ATOM   9765  C CG1   . VAL B  1 152  ? -9.175  36.267  115.809 1.00 39.19 ? 150  VAL B CG1   1 
ATOM   9766  C CG2   . VAL B  1 152  ? -7.560  35.100  114.312 1.00 37.60 ? 150  VAL B CG2   1 
ATOM   9767  N N     . VAL B  1 153  ? -10.100 38.793  113.283 1.00 33.67 ? 151  VAL B N     1 
ATOM   9768  C CA    . VAL B  1 153  ? -10.947 39.921  113.662 1.00 36.08 ? 151  VAL B CA    1 
ATOM   9769  C C     . VAL B  1 153  ? -12.024 40.195  112.617 1.00 34.61 ? 151  VAL B C     1 
ATOM   9770  O O     . VAL B  1 153  ? -13.168 40.514  112.961 1.00 32.33 ? 151  VAL B O     1 
ATOM   9771  C CB    . VAL B  1 153  ? -10.077 41.167  113.900 1.00 35.17 ? 151  VAL B CB    1 
ATOM   9772  C CG1   . VAL B  1 153  ? -10.950 42.412  114.057 1.00 35.19 ? 151  VAL B CG1   1 
ATOM   9773  C CG2   . VAL B  1 153  ? -9.200  40.967  115.119 1.00 32.78 ? 151  VAL B CG2   1 
ATOM   9774  N N     . THR B  1 154  ? -11.673 40.118  111.334 1.00 34.26 ? 152  THR B N     1 
ATOM   9775  C CA    . THR B  1 154  ? -12.576 40.501  110.260 1.00 34.80 ? 152  THR B CA    1 
ATOM   9776  C C     . THR B  1 154  ? -13.016 39.332  109.398 1.00 35.67 ? 152  THR B C     1 
ATOM   9777  O O     . THR B  1 154  ? -13.926 39.499  108.579 1.00 40.48 ? 152  THR B O     1 
ATOM   9778  C CB    . THR B  1 154  ? -11.919 41.550  109.348 1.00 33.14 ? 152  THR B CB    1 
ATOM   9779  O OG1   . THR B  1 154  ? -10.877 40.931  108.586 1.00 37.25 ? 152  THR B OG1   1 
ATOM   9780  C CG2   . THR B  1 154  ? -11.328 42.686  110.161 1.00 41.04 ? 152  THR B CG2   1 
ATOM   9781  N N     . GLY B  1 155  ? -12.391 38.167  109.537 1.00 35.24 ? 153  GLY B N     1 
ATOM   9782  C CA    . GLY B  1 155  ? -12.695 37.077  108.633 1.00 36.29 ? 153  GLY B CA    1 
ATOM   9783  C C     . GLY B  1 155  ? -12.131 37.225  107.240 1.00 38.80 ? 153  GLY B C     1 
ATOM   9784  O O     . GLY B  1 155  ? -12.496 36.448  106.355 1.00 44.15 ? 153  GLY B O     1 
ATOM   9785  N N     . LYS B  1 156  ? -11.252 38.196  107.010 1.00 35.26 ? 154  LYS B N     1 
ATOM   9786  C CA    . LYS B  1 156  ? -10.672 38.434  105.698 1.00 37.64 ? 154  LYS B CA    1 
ATOM   9787  C C     . LYS B  1 156  ? -9.159  38.292  105.779 1.00 37.28 ? 154  LYS B C     1 
ATOM   9788  O O     . LYS B  1 156  ? -8.531  38.730  106.751 1.00 33.67 ? 154  LYS B O     1 
ATOM   9789  C CB    . LYS B  1 156  ? -11.053 39.821  105.169 1.00 42.33 ? 154  LYS B CB    1 
ATOM   9790  N N     . LEU B  1 157  ? -8.576  37.660  104.769 1.00 32.31 ? 155  LEU B N     1 
ATOM   9791  C CA    . LEU B  1 157  ? -7.143  37.414  104.730 1.00 38.83 ? 155  LEU B CA    1 
ATOM   9792  C C     . LEU B  1 157  ? -6.511  38.286  103.655 1.00 39.50 ? 155  LEU B C     1 
ATOM   9793  O O     . LEU B  1 157  ? -7.033  38.372  102.541 1.00 40.60 ? 155  LEU B O     1 
ATOM   9794  C CB    . LEU B  1 157  ? -6.851  35.939  104.456 1.00 40.32 ? 155  LEU B CB    1 
ATOM   9795  N N     . THR B  1 158  ? -5.402  38.943  103.993 1.00 38.02 ? 156  THR B N     1 
ATOM   9796  C CA    . THR B  1 158  ? -4.542  39.571  102.999 1.00 38.63 ? 156  THR B CA    1 
ATOM   9797  C C     . THR B  1 158  ? -3.144  38.986  103.118 1.00 35.77 ? 156  THR B C     1 
ATOM   9798  O O     . THR B  1 158  ? -2.768  38.446  104.163 1.00 39.41 ? 156  THR B O     1 
ATOM   9799  C CB    . THR B  1 158  ? -4.487  41.091  103.164 1.00 38.39 ? 156  THR B CB    1 
ATOM   9800  O OG1   . THR B  1 158  ? -3.801  41.405  104.378 1.00 35.12 ? 156  THR B OG1   1 
ATOM   9801  C CG2   . THR B  1 158  ? -5.888  41.662  103.218 1.00 38.75 ? 156  THR B CG2   1 
ATOM   9802  N N     . SER B  1 159  ? -2.371  39.080  102.033 1.00 34.15 ? 157  SER B N     1 
ATOM   9803  C CA    . SER B  1 159  ? -1.020  38.531  102.078 1.00 34.82 ? 157  SER B CA    1 
ATOM   9804  C C     . SER B  1 159  ? -0.049  39.485  102.759 1.00 30.38 ? 157  SER B C     1 
ATOM   9805  O O     . SER B  1 159  ? 0.937   39.040  103.359 1.00 33.47 ? 157  SER B O     1 
ATOM   9806  C CB    . SER B  1 159  ? -0.521  38.185  100.668 1.00 33.89 ? 157  SER B CB    1 
ATOM   9807  O OG    . SER B  1 159  ? -0.462  39.327  99.823  1.00 40.09 ? 157  SER B OG    1 
ATOM   9808  N N     . THR B  1 160  ? -0.308  40.786  102.694 1.00 33.09 ? 158  THR B N     1 
ATOM   9809  C CA    . THR B  1 160  ? 0.542   41.746  103.370 1.00 29.15 ? 158  THR B CA    1 
ATOM   9810  C C     . THR B  1 160  ? -0.311  42.680  104.224 1.00 27.82 ? 158  THR B C     1 
ATOM   9811  O O     . THR B  1 160  ? -1.537  42.728  104.128 1.00 28.53 ? 158  THR B O     1 
ATOM   9812  C CB    . THR B  1 160  ? 1.403   42.547  102.379 1.00 26.94 ? 158  THR B CB    1 
ATOM   9813  O OG1   . THR B  1 160  ? 0.556   43.263  101.477 1.00 26.47 ? 158  THR B OG1   1 
ATOM   9814  C CG2   . THR B  1 160  ? 2.336   41.619  101.574 1.00 30.62 ? 158  THR B CG2   1 
ATOM   9815  N N     . VAL B  1 161  ? 0.388   43.463  105.032 1.00 23.21 ? 159  VAL B N     1 
ATOM   9816  C CA    . VAL B  1 161  ? -0.168  44.163  106.171 1.00 26.56 ? 159  VAL B CA    1 
ATOM   9817  C C     . VAL B  1 161  ? 0.072   45.650  105.953 1.00 25.62 ? 159  VAL B C     1 
ATOM   9818  O O     . VAL B  1 161  ? 1.174   46.041  105.557 1.00 24.43 ? 159  VAL B O     1 
ATOM   9819  C CB    . VAL B  1 161  ? 0.513   43.649  107.458 1.00 26.89 ? 159  VAL B CB    1 
ATOM   9820  C CG1   . VAL B  1 161  ? 0.578   44.690  108.529 1.00 30.39 ? 159  VAL B CG1   1 
ATOM   9821  C CG2   . VAL B  1 161  ? -0.186  42.384  107.935 1.00 36.35 ? 159  VAL B CG2   1 
ATOM   9822  N N     . ASN B  1 162  ? -0.956  46.478  106.181 1.00 22.32 ? 160  ASN B N     1 
ATOM   9823  C CA    . ASN B  1 162  ? -0.751  47.928  106.109 1.00 22.93 ? 160  ASN B CA    1 
ATOM   9824  C C     . ASN B  1 162  ? -0.285  48.361  107.489 1.00 22.13 ? 160  ASN B C     1 
ATOM   9825  O O     . ASN B  1 162  ? -1.087  48.679  108.375 1.00 20.72 ? 160  ASN B O     1 
ATOM   9826  C CB    . ASN B  1 162  ? -2.001  48.679  105.664 1.00 26.60 ? 160  ASN B CB    1 
ATOM   9827  C CG    . ASN B  1 162  ? -1.738  50.181  105.465 1.00 29.68 ? 160  ASN B CG    1 
ATOM   9828  O OD1   . ASN B  1 162  ? -0.769  50.726  105.999 1.00 25.16 ? 160  ASN B OD1   1 
ATOM   9829  N ND2   . ASN B  1 162  ? -2.603  50.848  104.707 1.00 23.65 ? 160  ASN B ND2   1 
ATOM   9830  N N     . ASP B  1 163  ? 1.038   48.361  107.668 1.00 21.11 ? 161  ASP B N     1 
ATOM   9831  C CA    . ASP B  1 163  ? 1.593   48.613  108.993 1.00 18.85 ? 161  ASP B CA    1 
ATOM   9832  C C     . ASP B  1 163  ? 1.509   50.082  109.394 1.00 20.29 ? 161  ASP B C     1 
ATOM   9833  O O     . ASP B  1 163  ? 1.591   50.386  110.587 1.00 21.73 ? 161  ASP B O     1 
ATOM   9834  C CB    . ASP B  1 163  ? 3.039   48.109  109.075 1.00 22.04 ? 161  ASP B CB    1 
ATOM   9835  C CG    . ASP B  1 163  ? 3.931   48.610  107.927 1.00 25.93 ? 161  ASP B CG    1 
ATOM   9836  O OD1   . ASP B  1 163  ? 3.487   48.645  106.758 1.00 22.45 ? 161  ASP B OD1   1 
ATOM   9837  O OD2   . ASP B  1 163  ? 5.105   48.935  108.202 1.00 28.06 ? 161  ASP B OD2   1 
ATOM   9838  N N     . ARG B  1 164  ? 1.358   51.003  108.437 1.00 22.39 ? 162  ARG B N     1 
ATOM   9839  C CA    . ARG B  1 164  ? 1.117   52.391  108.828 1.00 22.87 ? 162  ARG B CA    1 
ATOM   9840  C C     . ARG B  1 164  ? -0.291  52.571  109.386 1.00 22.95 ? 162  ARG B C     1 
ATOM   9841  O O     . ARG B  1 164  ? -0.491  53.313  110.354 1.00 20.66 ? 162  ARG B O     1 
ATOM   9842  C CB    . ARG B  1 164  ? 1.338   53.329  107.635 1.00 19.85 ? 162  ARG B CB    1 
ATOM   9843  C CG    . ARG B  1 164  ? 2.764   53.396  107.102 1.00 23.83 ? 162  ARG B CG    1 
ATOM   9844  C CD    . ARG B  1 164  ? 3.799   53.537  108.227 1.00 27.24 ? 162  ARG B CD    1 
ATOM   9845  N NE    . ARG B  1 164  ? 3.444   54.564  109.197 1.00 32.95 ? 162  ARG B NE    1 
ATOM   9846  C CZ    . ARG B  1 164  ? 3.890   54.584  110.445 1.00 34.30 ? 162  ARG B CZ    1 
ATOM   9847  N NH1   . ARG B  1 164  ? 4.703   53.644  110.902 1.00 39.48 ? 162  ARG B NH1   1 
ATOM   9848  N NH2   . ARG B  1 164  ? 3.507   55.566  111.258 1.00 34.79 ? 162  ARG B NH2   1 
ATOM   9849  N N     . SER B  1 165  ? -1.288  51.959  108.742 1.00 21.95 ? 163  SER B N     1 
ATOM   9850  C CA    . SER B  1 165  ? -2.646  51.978  109.267 1.00 22.76 ? 163  SER B CA    1 
ATOM   9851  C C     . SER B  1 165  ? -2.705  51.322  110.637 1.00 21.00 ? 163  SER B C     1 
ATOM   9852  O O     . SER B  1 165  ? -3.370  51.821  111.548 1.00 21.58 ? 163  SER B O     1 
ATOM   9853  C CB    . SER B  1 165  ? -3.590  51.271  108.275 1.00 21.20 ? 163  SER B CB    1 
ATOM   9854  O OG    . SER B  1 165  ? -4.864  51.045  108.866 1.00 22.20 ? 163  SER B OG    1 
ATOM   9855  N N     . LEU B  1 166  ? -1.976  50.218  110.815 1.00 21.15 ? 164  LEU B N     1 
ATOM   9856  C CA    . LEU B  1 166  ? -2.019  49.525  112.097 1.00 21.47 ? 164  LEU B CA    1 
ATOM   9857  C C     . LEU B  1 166  ? -1.312  50.323  113.185 1.00 21.82 ? 164  LEU B C     1 
ATOM   9858  O O     . LEU B  1 166  ? -1.774  50.362  114.334 1.00 21.95 ? 164  LEU B O     1 
ATOM   9859  C CB    . LEU B  1 166  ? -1.407  48.136  111.947 1.00 20.52 ? 164  LEU B CB    1 
ATOM   9860  C CG    . LEU B  1 166  ? -2.320  47.170  111.191 1.00 22.09 ? 164  LEU B CG    1 
ATOM   9861  C CD1   . LEU B  1 166  ? -1.579  45.895  110.895 1.00 23.96 ? 164  LEU B CD1   1 
ATOM   9862  C CD2   . LEU B  1 166  ? -3.591  46.884  111.999 1.00 21.94 ? 164  LEU B CD2   1 
ATOM   9863  N N     . ALA B  1 167  ? -0.175  50.945  112.851 1.00 22.10 ? 165  ALA B N     1 
ATOM   9864  C CA    . ALA B  1 167  ? 0.513   51.761  113.851 1.00 22.75 ? 165  ALA B CA    1 
ATOM   9865  C C     . ALA B  1 167  ? -0.345  52.959  114.242 1.00 21.94 ? 165  ALA B C     1 
ATOM   9866  O O     . ALA B  1 167  ? -0.397  53.340  115.408 1.00 22.59 ? 165  ALA B O     1 
ATOM   9867  C CB    . ALA B  1 167  ? 1.886   52.197  113.321 1.00 21.94 ? 165  ALA B CB    1 
ATOM   9868  N N     . ALA B  1 168  ? -1.062  53.544  113.278 1.00 21.91 ? 166  ALA B N     1 
ATOM   9869  C CA    . ALA B  1 168  ? -1.978  54.638  113.601 1.00 22.54 ? 166  ALA B CA    1 
ATOM   9870  C C     . ALA B  1 168  ? -3.128  54.163  114.487 1.00 23.12 ? 166  ALA B C     1 
ATOM   9871  O O     . ALA B  1 168  ? -3.530  54.860  115.418 1.00 23.78 ? 166  ALA B O     1 
ATOM   9872  C CB    . ALA B  1 168  ? -2.528  55.267  112.308 1.00 22.38 ? 166  ALA B CB    1 
ATOM   9873  N N     . ALA B  1 169  ? -3.677  52.982  114.197 1.00 22.91 ? 167  ALA B N     1 
ATOM   9874  C CA    . ALA B  1 169  ? -4.772  52.438  114.992 1.00 23.47 ? 167  ALA B CA    1 
ATOM   9875  C C     . ALA B  1 169  ? -4.319  52.139  116.408 1.00 24.08 ? 167  ALA B C     1 
ATOM   9876  O O     . ALA B  1 169  ? -5.047  52.393  117.372 1.00 24.53 ? 167  ALA B O     1 
ATOM   9877  C CB    . ALA B  1 169  ? -5.297  51.158  114.339 1.00 23.75 ? 167  ALA B CB    1 
ATOM   9878  N N     . LEU B  1 170  ? -3.122  51.590  116.546 1.00 23.38 ? 168  LEU B N     1 
ATOM   9879  C CA    . LEU B  1 170  ? -2.651  51.217  117.875 1.00 23.70 ? 168  LEU B CA    1 
ATOM   9880  C C     . LEU B  1 170  ? -2.419  52.452  118.732 1.00 24.24 ? 168  LEU B C     1 
ATOM   9881  O O     . LEU B  1 170  ? -2.811  52.487  119.907 1.00 26.49 ? 168  LEU B O     1 
ATOM   9882  C CB    . LEU B  1 170  ? -1.382  50.388  117.756 1.00 26.68 ? 168  LEU B CB    1 
ATOM   9883  C CG    . LEU B  1 170  ? -0.826  49.882  119.090 1.00 27.40 ? 168  LEU B CG    1 
ATOM   9884  C CD1   . LEU B  1 170  ? -1.904  49.183  119.888 1.00 26.74 ? 168  LEU B CD1   1 
ATOM   9885  C CD2   . LEU B  1 170  ? 0.287   48.926  118.778 1.00 28.83 ? 168  LEU B CD2   1 
ATOM   9886  N N     . THR B  1 171  ? -1.784  53.476  118.161 1.00 25.42 ? 169  THR B N     1 
ATOM   9887  C CA    . THR B  1 171  ? -1.640  54.741  118.879 1.00 25.43 ? 169  THR B CA    1 
ATOM   9888  C C     . THR B  1 171  ? -2.996  55.313  119.255 1.00 25.33 ? 169  THR B C     1 
ATOM   9889  O O     . THR B  1 171  ? -3.188  55.792  120.376 1.00 27.15 ? 169  THR B O     1 
ATOM   9890  C CB    . THR B  1 171  ? -0.868  55.747  118.025 1.00 27.81 ? 169  THR B CB    1 
ATOM   9891  O OG1   . THR B  1 171  ? 0.439   55.232  117.750 1.00 30.74 ? 169  THR B OG1   1 
ATOM   9892  C CG2   . THR B  1 171  ? -0.767  57.098  118.743 1.00 28.66 ? 169  THR B CG2   1 
ATOM   9893  N N     . ARG B  1 172  ? -3.949  55.283  118.321 1.00 25.29 ? 170  ARG B N     1 
ATOM   9894  C CA    . ARG B  1 172  ? -5.257  55.855  118.591 1.00 25.96 ? 170  ARG B CA    1 
ATOM   9895  C C     . ARG B  1 172  ? -5.948  55.129  119.736 1.00 26.53 ? 170  ARG B C     1 
ATOM   9896  O O     . ARG B  1 172  ? -6.492  55.758  120.645 1.00 27.31 ? 170  ARG B O     1 
ATOM   9897  C CB    . ARG B  1 172  ? -6.120  55.801  117.326 1.00 25.70 ? 170  ARG B CB    1 
ATOM   9898  C CG    . ARG B  1 172  ? -7.336  56.690  117.400 1.00 26.43 ? 170  ARG B CG    1 
ATOM   9899  C CD    . ARG B  1 172  ? -8.243  56.510  116.174 1.00 26.21 ? 170  ARG B CD    1 
ATOM   9900  N NE    . ARG B  1 172  ? -7.514  56.615  114.919 1.00 25.43 ? 170  ARG B NE    1 
ATOM   9901  C CZ    . ARG B  1 172  ? -7.245  55.589  114.123 1.00 24.73 ? 170  ARG B CZ    1 
ATOM   9902  N NH1   . ARG B  1 172  ? -7.587  54.356  114.451 1.00 24.69 ? 170  ARG B NH1   1 
ATOM   9903  N NH2   . ARG B  1 172  ? -6.603  55.804  112.975 1.00 24.10 ? 170  ARG B NH2   1 
ATOM   9904  N N     . LEU B  1 173  ? -5.920  53.798  119.720 1.00 26.19 ? 171  LEU B N     1 
ATOM   9905  C CA    . LEU B  1 173  ? -6.687  53.055  120.712 1.00 26.76 ? 171  LEU B CA    1 
ATOM   9906  C C     . LEU B  1 173  ? -6.056  53.166  122.092 1.00 27.64 ? 171  LEU B C     1 
ATOM   9907  O O     . LEU B  1 173  ? -6.770  53.243  123.096 1.00 27.96 ? 171  LEU B O     1 
ATOM   9908  C CB    . LEU B  1 173  ? -6.834  51.592  120.281 1.00 29.73 ? 171  LEU B CB    1 
ATOM   9909  C CG    . LEU B  1 173  ? -5.687  50.595  120.410 1.00 26.84 ? 171  LEU B CG    1 
ATOM   9910  C CD1   . LEU B  1 173  ? -5.773  49.836  121.730 1.00 30.22 ? 171  LEU B CD1   1 
ATOM   9911  C CD2   . LEU B  1 173  ? -5.729  49.625  119.246 1.00 25.17 ? 171  LEU B CD2   1 
ATOM   9912  N N     . ILE B  1 174  ? -4.725  53.204  122.161 1.00 26.73 ? 172  ILE B N     1 
ATOM   9913  C CA    . ILE B  1 174  ? -4.067  53.355  123.463 1.00 27.16 ? 172  ILE B CA    1 
ATOM   9914  C C     . ILE B  1 174  ? -4.336  54.740  124.038 1.00 27.86 ? 172  ILE B C     1 
ATOM   9915  O O     . ILE B  1 174  ? -4.636  54.892  125.230 1.00 28.60 ? 172  ILE B O     1 
ATOM   9916  C CB    . ILE B  1 174  ? -2.558  53.084  123.341 1.00 26.50 ? 172  ILE B CB    1 
ATOM   9917  C CG1   . ILE B  1 174  ? -2.305  51.618  122.969 1.00 25.92 ? 172  ILE B CG1   1 
ATOM   9918  C CG2   . ILE B  1 174  ? -1.838  53.482  124.639 1.00 29.48 ? 172  ILE B CG2   1 
ATOM   9919  C CD1   . ILE B  1 174  ? -0.871  51.321  122.635 1.00 31.96 ? 172  ILE B CD1   1 
ATOM   9920  N N     . SER B  1 175  ? -4.201  55.778  123.204 1.00 29.01 ? 173  SER B N     1 
ATOM   9921  C CA    . SER B  1 175  ? -4.457  57.135  123.684 1.00 28.54 ? 173  SER B CA    1 
ATOM   9922  C C     . SER B  1 175  ? -5.913  57.327  124.087 1.00 29.18 ? 173  SER B C     1 
ATOM   9923  O O     . SER B  1 175  ? -6.212  58.140  124.967 1.00 29.98 ? 173  SER B O     1 
ATOM   9924  C CB    . SER B  1 175  ? -4.074  58.165  122.619 1.00 30.99 ? 173  SER B CB    1 
ATOM   9925  O OG    . SER B  1 175  ? -2.690  58.149  122.358 1.00 34.30 ? 173  SER B OG    1 
ATOM   9926  N N     . ARG B  1 176  ? -6.832  56.600  123.451 1.00 29.58 ? 174  ARG B N     1 
ATOM   9927  C CA    . ARG B  1 176  ? -8.248  56.733  123.771 1.00 29.79 ? 174  ARG B CA    1 
ATOM   9928  C C     . ARG B  1 176  ? -8.615  55.923  125.014 1.00 30.40 ? 174  ARG B C     1 
ATOM   9929  O O     . ARG B  1 176  ? -9.325  56.418  125.902 1.00 32.34 ? 174  ARG B O     1 
ATOM   9930  C CB    . ARG B  1 176  ? -9.088  56.290  122.563 1.00 29.42 ? 174  ARG B CB    1 
ATOM   9931  C CG    . ARG B  1 176  ? -10.577 56.635  122.650 1.00 31.50 ? 174  ARG B CG    1 
ATOM   9932  C CD    . ARG B  1 176  ? -11.307 56.304  121.343 1.00 30.17 ? 174  ARG B CD    1 
ATOM   9933  N NE    . ARG B  1 176  ? -11.416 54.864  121.126 1.00 29.52 ? 174  ARG B NE    1 
ATOM   9934  C CZ    . ARG B  1 176  ? -10.822 54.179  120.158 1.00 32.11 ? 174  ARG B CZ    1 
ATOM   9935  N NH1   . ARG B  1 176  ? -10.103 54.779  119.214 1.00 29.93 ? 174  ARG B NH1   1 
ATOM   9936  N NH2   . ARG B  1 176  ? -10.966 52.855  120.120 1.00 35.45 ? 174  ARG B NH2   1 
ATOM   9937  N N     . CYS B  1 177  ? -8.098  54.694  125.116 1.00 30.91 ? 175  CYS B N     1 
ATOM   9938  C CA    . CYS B  1 177  ? -8.585  53.730  126.091 1.00 30.99 ? 175  CYS B CA    1 
ATOM   9939  C C     . CYS B  1 177  ? -7.571  53.328  127.154 1.00 30.99 ? 175  CYS B C     1 
ATOM   9940  O O     . CYS B  1 177  ? -7.982  52.783  128.179 1.00 36.37 ? 175  CYS B O     1 
ATOM   9941  C CB    . CYS B  1 177  ? -9.071  52.458  125.383 1.00 30.88 ? 175  CYS B CB    1 
ATOM   9942  S SG    . CYS B  1 177  ? -10.408 52.752  124.180 1.00 39.67 ? 175  CYS B SG    1 
ATOM   9943  N N     . GLY B  1 178  ? -6.278  53.543  126.933 1.00 30.97 ? 176  GLY B N     1 
ATOM   9944  C CA    . GLY B  1 178  ? -5.350  53.386  128.053 1.00 34.65 ? 176  GLY B CA    1 
ATOM   9945  C C     . GLY B  1 178  ? -5.071  51.939  128.444 1.00 34.61 ? 176  GLY B C     1 
ATOM   9946  O O     . GLY B  1 178  ? -5.302  50.995  127.696 1.00 32.62 ? 176  GLY B O     1 
ATOM   9947  N N     . GLU B  1 179  ? -4.548  51.785  129.660 1.00 36.08 ? 177  GLU B N     1 
ATOM   9948  C CA    . GLU B  1 179  ? -4.216  50.457  130.168 1.00 37.00 ? 177  GLU B CA    1 
ATOM   9949  C C     . GLU B  1 179  ? -5.362  49.446  130.127 1.00 35.53 ? 177  GLU B C     1 
ATOM   9950  O O     . GLU B  1 179  ? -5.092  48.278  129.796 1.00 34.73 ? 177  GLU B O     1 
ATOM   9951  C CB    . GLU B  1 179  ? -3.678  50.564  131.605 1.00 37.11 ? 177  GLU B CB    1 
ATOM   9952  C CG    . GLU B  1 179  ? -3.157  49.241  132.130 1.00 41.42 ? 177  GLU B CG    1 
ATOM   9953  C CD    . GLU B  1 179  ? -2.584  49.325  133.531 1.00 48.57 ? 177  GLU B CD    1 
ATOM   9954  O OE1   . GLU B  1 179  ? -2.751  50.367  134.202 1.00 48.94 ? 177  GLU B OE1   1 
ATOM   9955  O OE2   . GLU B  1 179  ? -1.961  48.334  133.959 1.00 52.41 ? 177  GLU B OE2   1 
ATOM   9956  N N     . PRO B  1 180  ? -6.619  49.786  130.453 1.00 33.53 ? 178  PRO B N     1 
ATOM   9957  C CA    . PRO B  1 180  ? -7.644  48.729  130.514 1.00 34.58 ? 178  PRO B CA    1 
ATOM   9958  C C     . PRO B  1 180  ? -7.877  48.008  129.201 1.00 39.28 ? 178  PRO B C     1 
ATOM   9959  O O     . PRO B  1 180  ? -8.201  46.813  129.222 1.00 36.63 ? 178  PRO B O     1 
ATOM   9960  C CB    . PRO B  1 180  ? -8.897  49.478  130.983 1.00 39.26 ? 178  PRO B CB    1 
ATOM   9961  C CG    . PRO B  1 180  ? -8.377  50.631  131.745 1.00 36.68 ? 178  PRO B CG    1 
ATOM   9962  C CD    . PRO B  1 180  ? -7.131  51.054  131.007 1.00 36.19 ? 178  PRO B CD    1 
ATOM   9963  N N     . VAL B  1 181  ? -7.720  48.676  128.054 1.00 31.39 ? 179  VAL B N     1 
ATOM   9964  C CA    . VAL B  1 181  ? -7.932  47.946  126.814 1.00 33.73 ? 179  VAL B CA    1 
ATOM   9965  C C     . VAL B  1 181  ? -6.736  47.050  126.522 1.00 34.71 ? 179  VAL B C     1 
ATOM   9966  O O     . VAL B  1 181  ? -6.899  45.968  125.946 1.00 30.36 ? 179  VAL B O     1 
ATOM   9967  C CB    . VAL B  1 181  ? -8.231  48.893  125.633 1.00 36.74 ? 179  VAL B CB    1 
ATOM   9968  C CG1   . VAL B  1 181  ? -6.979  49.636  125.166 1.00 31.61 ? 179  VAL B CG1   1 
ATOM   9969  C CG2   . VAL B  1 181  ? -8.813  48.104  124.471 1.00 37.22 ? 179  VAL B CG2   1 
ATOM   9970  N N     . ILE B  1 182  ? -5.532  47.470  126.918 1.00 33.10 ? 180  ILE B N     1 
ATOM   9971  C CA    . ILE B  1 182  ? -4.363  46.615  126.753 1.00 36.41 ? 180  ILE B CA    1 
ATOM   9972  C C     . ILE B  1 182  ? -4.520  45.348  127.584 1.00 35.45 ? 180  ILE B C     1 
ATOM   9973  O O     . ILE B  1 182  ? -4.256  44.238  127.100 1.00 36.80 ? 180  ILE B O     1 
ATOM   9974  C CB    . ILE B  1 182  ? -3.075  47.380  127.115 1.00 33.73 ? 180  ILE B CB    1 
ATOM   9975  C CG1   . ILE B  1 182  ? -2.867  48.563  126.170 1.00 31.40 ? 180  ILE B CG1   1 
ATOM   9976  C CG2   . ILE B  1 182  ? -1.862  46.466  126.991 1.00 33.51 ? 180  ILE B CG2   1 
ATOM   9977  C CD1   . ILE B  1 182  ? -2.002  49.644  126.762 1.00 30.88 ? 180  ILE B CD1   1 
ATOM   9978  N N     . ARG B  1 183  ? -4.971  45.490  128.840 1.00 35.43 ? 181  ARG B N     1 
ATOM   9979  C CA    . ARG B  1 183  ? -5.139  44.322  129.701 1.00 32.55 ? 181  ARG B CA    1 
ATOM   9980  C C     . ARG B  1 183  ? -6.168  43.359  129.128 1.00 38.60 ? 181  ARG B C     1 
ATOM   9981  O O     . ARG B  1 183  ? -5.974  42.137  129.170 1.00 38.69 ? 181  ARG B O     1 
ATOM   9982  C CB    . ARG B  1 183  ? -5.548  44.738  131.117 1.00 35.38 ? 181  ARG B CB    1 
ATOM   9983  C CG    . ARG B  1 183  ? -4.671  45.791  131.790 1.00 44.27 ? 181  ARG B CG    1 
ATOM   9984  C CD    . ARG B  1 183  ? -5.075  45.972  133.262 1.00 45.84 ? 181  ARG B CD    1 
ATOM   9985  N NE    . ARG B  1 183  ? -5.229  47.370  133.665 1.00 57.08 ? 181  ARG B NE    1 
ATOM   9986  C CZ    . ARG B  1 183  ? -6.386  47.963  133.950 1.00 49.91 ? 181  ARG B CZ    1 
ATOM   9987  N NH1   . ARG B  1 183  ? -7.536  47.313  133.870 1.00 48.54 ? 181  ARG B NH1   1 
ATOM   9988  N NH2   . ARG B  1 183  ? -6.387  49.237  134.337 1.00 47.88 ? 181  ARG B NH2   1 
ATOM   9989  N N     . ARG B  1 184  ? -7.273  43.892  128.586 1.00 37.05 ? 182  ARG B N     1 
ATOM   9990  C CA    . ARG B  1 184  ? -8.302  43.038  127.997 1.00 39.34 ? 182  ARG B CA    1 
ATOM   9991  C C     . ARG B  1 184  ? -7.785  42.306  126.766 1.00 38.78 ? 182  ARG B C     1 
ATOM   9992  O O     . ARG B  1 184  ? -8.083  41.122  126.576 1.00 41.29 ? 182  ARG B O     1 
ATOM   9993  C CB    . ARG B  1 184  ? -9.543  43.864  127.651 1.00 41.25 ? 182  ARG B CB    1 
ATOM   9994  C CG    . ARG B  1 184  ? -10.403 44.212  128.866 1.00 48.18 ? 182  ARG B CG    1 
ATOM   9995  C CD    . ARG B  1 184  ? -11.379 43.085  129.228 1.00 50.27 ? 182  ARG B CD    1 
ATOM   9996  N NE    . ARG B  1 184  ? -12.596 43.123  128.419 1.00 51.03 ? 182  ARG B NE    1 
ATOM   9997  C CZ    . ARG B  1 184  ? -12.914 42.242  127.477 1.00 55.91 ? 182  ARG B CZ    1 
ATOM   9998  N NH1   . ARG B  1 184  ? -12.137 41.205  127.205 1.00 56.44 ? 182  ARG B NH1   1 
ATOM   9999  N NH2   . ARG B  1 184  ? -14.044 42.403  126.792 1.00 52.62 ? 182  ARG B NH2   1 
ATOM   10000 N N     . GLY B  1 185  ? -7.021  42.994  125.915 1.00 36.27 ? 183  GLY B N     1 
ATOM   10001 C CA    . GLY B  1 185  ? -6.471  42.346  124.732 1.00 36.52 ? 183  GLY B CA    1 
ATOM   10002 C C     . GLY B  1 185  ? -5.501  41.230  125.071 1.00 38.94 ? 183  GLY B C     1 
ATOM   10003 O O     . GLY B  1 185  ? -5.511  40.174  124.433 1.00 34.55 ? 183  GLY B O     1 
ATOM   10004 N N     . VAL B  1 186  ? -4.646  41.450  126.076 1.00 33.79 ? 184  VAL B N     1 
ATOM   10005 C CA    . VAL B  1 186  ? -3.731  40.403  126.537 1.00 38.27 ? 184  VAL B CA    1 
ATOM   10006 C C     . VAL B  1 186  ? -4.514  39.193  127.037 1.00 39.34 ? 184  VAL B C     1 
ATOM   10007 O O     . VAL B  1 186  ? -4.210  38.047  126.685 1.00 39.51 ? 184  VAL B O     1 
ATOM   10008 C CB    . VAL B  1 186  ? -2.794  40.946  127.629 1.00 37.51 ? 184  VAL B CB    1 
ATOM   10009 C CG1   . VAL B  1 186  ? -2.058  39.798  128.321 1.00 36.31 ? 184  VAL B CG1   1 
ATOM   10010 C CG2   . VAL B  1 186  ? -1.811  41.931  127.041 1.00 35.05 ? 184  VAL B CG2   1 
ATOM   10011 N N     . ASP B  1 187  ? -5.533  39.432  127.868 1.00 39.50 ? 185  ASP B N     1 
ATOM   10012 C CA    . ASP B  1 187  ? -6.347  38.330  128.375 1.00 40.94 ? 185  ASP B CA    1 
ATOM   10013 C C     . ASP B  1 187  ? -7.014  37.577  127.234 1.00 44.69 ? 185  ASP B C     1 
ATOM   10014 O O     . ASP B  1 187  ? -7.133  36.347  127.275 1.00 45.04 ? 185  ASP B O     1 
ATOM   10015 C CB    . ASP B  1 187  ? -7.397  38.852  129.358 1.00 41.98 ? 185  ASP B CB    1 
ATOM   10016 C CG    . ASP B  1 187  ? -6.791  39.296  130.681 1.00 50.71 ? 185  ASP B CG    1 
ATOM   10017 O OD1   . ASP B  1 187  ? -5.570  39.097  130.878 1.00 53.74 ? 185  ASP B OD1   1 
ATOM   10018 O OD2   . ASP B  1 187  ? -7.537  39.844  131.527 1.00 49.68 ? 185  ASP B OD2   1 
ATOM   10019 N N     . MET B  1 188  ? -7.434  38.302  126.195 1.00 44.22 ? 186  MET B N     1 
ATOM   10020 C CA    . MET B  1 188  ? -8.101  37.671  125.064 1.00 41.14 ? 186  MET B CA    1 
ATOM   10021 C C     . MET B  1 188  ? -7.125  36.834  124.250 1.00 41.37 ? 186  MET B C     1 
ATOM   10022 O O     . MET B  1 188  ? -7.389  35.662  123.962 1.00 47.14 ? 186  MET B O     1 
ATOM   10023 C CB    . MET B  1 188  ? -8.758  38.740  124.193 1.00 45.48 ? 186  MET B CB    1 
ATOM   10024 C CG    . MET B  1 188  ? -9.490  38.202  122.984 1.00 49.39 ? 186  MET B CG    1 
ATOM   10025 S SD    . MET B  1 188  ? -10.839 37.105  123.453 1.00 54.63 ? 186  MET B SD    1 
ATOM   10026 C CE    . MET B  1 188  ? -11.634 38.073  124.733 1.00 53.03 ? 186  MET B CE    1 
ATOM   10027 N N     . ALA B  1 189  ? -5.993  37.423  123.860 1.00 42.12 ? 187  ALA B N     1 
ATOM   10028 C CA    . ALA B  1 189  ? -4.996  36.672  123.104 1.00 43.25 ? 187  ALA B CA    1 
ATOM   10029 C C     . ALA B  1 189  ? -4.537  35.438  123.873 1.00 45.55 ? 187  ALA B C     1 
ATOM   10030 O O     . ALA B  1 189  ? -4.343  34.368  123.285 1.00 44.03 ? 187  ALA B O     1 
ATOM   10031 C CB    . ALA B  1 189  ? -3.809  37.573  122.759 1.00 39.40 ? 187  ALA B CB    1 
ATOM   10032 N N     . MET B  1 190  ? -4.380  35.563  125.193 1.00 43.44 ? 188  MET B N     1 
ATOM   10033 C CA    . MET B  1 190  ? -3.942  34.426  126.001 1.00 47.95 ? 188  MET B CA    1 
ATOM   10034 C C     . MET B  1 190  ? -4.952  33.283  125.936 1.00 47.79 ? 188  MET B C     1 
ATOM   10035 O O     . MET B  1 190  ? -4.579  32.119  125.750 1.00 50.16 ? 188  MET B O     1 
ATOM   10036 C CB    . MET B  1 190  ? -3.716  34.865  127.449 1.00 44.52 ? 188  MET B CB    1 
ATOM   10037 C CG    . MET B  1 190  ? -2.397  34.389  128.046 1.00 52.71 ? 188  MET B CG    1 
ATOM   10038 S SD    . MET B  1 190  ? -2.336  34.489  129.852 1.00 68.27 ? 188  MET B SD    1 
ATOM   10039 C CE    . MET B  1 190  ? -2.692  36.220  130.150 1.00 47.44 ? 188  MET B CE    1 
ATOM   10040 N N     . ARG B  1 191  ? -6.240  33.599  126.078 1.00 44.91 ? 189  ARG B N     1 
ATOM   10041 C CA    . ARG B  1 191  ? -7.266  32.564  125.983 1.00 49.54 ? 189  ARG B CA    1 
ATOM   10042 C C     . ARG B  1 191  ? -7.264  31.917  124.601 1.00 51.67 ? 189  ARG B C     1 
ATOM   10043 O O     . ARG B  1 191  ? -7.248  30.686  124.479 1.00 52.51 ? 189  ARG B O     1 
ATOM   10044 C CB    . ARG B  1 191  ? -8.640  33.150  126.310 1.00 47.08 ? 189  ARG B CB    1 
ATOM   10045 N N     . MET B  1 192  ? -7.259  32.732  123.545 1.00 47.23 ? 190  MET B N     1 
ATOM   10046 C CA    . MET B  1 192  ? -7.268  32.186  122.193 1.00 44.91 ? 190  MET B CA    1 
ATOM   10047 C C     . MET B  1 192  ? -6.013  31.368  121.918 1.00 48.91 ? 190  MET B C     1 
ATOM   10048 O O     . MET B  1 192  ? -6.090  30.176  121.594 1.00 50.65 ? 190  MET B O     1 
ATOM   10049 C CB    . MET B  1 192  ? -7.401  33.312  121.166 1.00 49.02 ? 190  MET B CB    1 
ATOM   10050 C CG    . MET B  1 192  ? -8.633  34.179  121.325 1.00 47.56 ? 190  MET B CG    1 
ATOM   10051 S SD    . MET B  1 192  ? -8.752  35.351  119.965 1.00 54.11 ? 190  MET B SD    1 
ATOM   10052 C CE    . MET B  1 192  ? -9.352  34.264  118.685 1.00 41.59 ? 190  MET B CE    1 
ATOM   10053 N N     . MET B  1 193  ? -4.839  31.998  122.034 1.00 43.40 ? 191  MET B N     1 
ATOM   10054 C CA    . MET B  1 193  ? -3.599  31.345  121.625 1.00 48.54 ? 191  MET B CA    1 
ATOM   10055 C C     . MET B  1 193  ? -3.266  30.128  122.474 1.00 47.59 ? 191  MET B C     1 
ATOM   10056 O O     . MET B  1 193  ? -2.521  29.256  122.016 1.00 48.97 ? 191  MET B O     1 
ATOM   10057 C CB    . MET B  1 193  ? -2.426  32.323  121.685 1.00 49.48 ? 191  MET B CB    1 
ATOM   10058 C CG    . MET B  1 193  ? -2.428  33.370  120.599 1.00 47.93 ? 191  MET B CG    1 
ATOM   10059 S SD    . MET B  1 193  ? -0.771  34.021  120.320 1.00 56.57 ? 191  MET B SD    1 
ATOM   10060 C CE    . MET B  1 193  ? -0.519  34.995  121.784 1.00 43.16 ? 191  MET B CE    1 
ATOM   10061 N N     . GLY B  1 194  ? -3.792  30.046  123.689 1.00 47.44 ? 192  GLY B N     1 
ATOM   10062 C CA    . GLY B  1 194  ? -3.411  28.967  124.578 1.00 49.57 ? 192  GLY B CA    1 
ATOM   10063 C C     . GLY B  1 194  ? -4.472  27.906  124.780 1.00 50.41 ? 192  GLY B C     1 
ATOM   10064 O O     . GLY B  1 194  ? -4.167  26.814  125.269 1.00 51.16 ? 192  GLY B O     1 
ATOM   10065 N N     . GLU B  1 195  ? -5.721  28.209  124.416 1.00 47.06 ? 193  GLU B N     1 
ATOM   10066 C CA    . GLU B  1 195  ? -6.836  27.308  124.680 1.00 49.22 ? 193  GLU B CA    1 
ATOM   10067 C C     . GLU B  1 195  ? -7.781  27.115  123.506 1.00 48.40 ? 193  GLU B C     1 
ATOM   10068 O O     . GLU B  1 195  ? -8.465  26.084  123.468 1.00 44.94 ? 193  GLU B O     1 
ATOM   10069 C CB    . GLU B  1 195  ? -7.653  27.798  125.885 1.00 51.12 ? 193  GLU B CB    1 
ATOM   10070 C CG    . GLU B  1 195  ? -6.824  28.018  127.139 1.00 58.75 ? 193  GLU B CG    1 
ATOM   10071 C CD    . GLU B  1 195  ? -7.645  28.526  128.308 1.00 61.35 ? 193  GLU B CD    1 
ATOM   10072 O OE1   . GLU B  1 195  ? -8.889  28.415  128.255 1.00 55.82 ? 193  GLU B OE1   1 
ATOM   10073 O OE2   . GLU B  1 195  ? -7.042  29.035  129.278 1.00 66.39 ? 193  GLU B OE2   1 
ATOM   10074 N N     . GLN B  1 196  ? -7.849  28.055  122.559 1.00 46.47 ? 194  GLN B N     1 
ATOM   10075 C CA    . GLN B  1 196  ? -8.705  27.946  121.383 1.00 43.04 ? 194  GLN B CA    1 
ATOM   10076 C C     . GLN B  1 196  ? -7.952  27.441  120.155 1.00 43.00 ? 194  GLN B C     1 
ATOM   10077 O O     . GLN B  1 196  ? -8.419  26.520  119.479 1.00 46.55 ? 194  GLN B O     1 
ATOM   10078 C CB    . GLN B  1 196  ? -9.352  29.301  121.074 1.00 48.23 ? 194  GLN B CB    1 
ATOM   10079 N N     . PHE B  1 197  ? -6.793  28.028  119.848 1.00 41.10 ? 195  PHE B N     1 
ATOM   10080 C CA    . PHE B  1 197  ? -6.015  27.575  118.695 1.00 44.72 ? 195  PHE B CA    1 
ATOM   10081 C C     . PHE B  1 197  ? -5.346  26.235  118.969 1.00 41.52 ? 195  PHE B C     1 
ATOM   10082 O O     . PHE B  1 197  ? -5.232  25.394  118.070 1.00 42.53 ? 195  PHE B O     1 
ATOM   10083 C CB    . PHE B  1 197  ? -4.961  28.618  118.318 1.00 45.43 ? 195  PHE B CB    1 
ATOM   10084 C CG    . PHE B  1 197  ? -5.538  29.948  117.921 1.00 48.02 ? 195  PHE B CG    1 
ATOM   10085 C CD1   . PHE B  1 197  ? -6.813  30.032  117.383 1.00 47.76 ? 195  PHE B CD1   1 
ATOM   10086 C CD2   . PHE B  1 197  ? -4.809  31.115  118.097 1.00 48.88 ? 195  PHE B CD2   1 
ATOM   10087 C CE1   . PHE B  1 197  ? -7.349  31.257  117.017 1.00 48.88 ? 195  PHE B CE1   1 
ATOM   10088 C CE2   . PHE B  1 197  ? -5.338  32.345  117.739 1.00 47.07 ? 195  PHE B CE2   1 
ATOM   10089 C CZ    . PHE B  1 197  ? -6.610  32.416  117.198 1.00 47.97 ? 195  PHE B CZ    1 
ATOM   10090 N N     . VAL B  1 198  ? -4.878  26.024  120.190 1.00 37.61 ? 196  VAL B N     1 
ATOM   10091 C CA    . VAL B  1 198  ? -4.271  24.755  120.553 1.00 36.09 ? 196  VAL B CA    1 
ATOM   10092 C C     . VAL B  1 198  ? -5.011  24.195  121.752 1.00 40.47 ? 196  VAL B C     1 
ATOM   10093 O O     . VAL B  1 198  ? -5.614  24.925  122.547 1.00 40.23 ? 196  VAL B O     1 
ATOM   10094 C CB    . VAL B  1 198  ? -2.760  24.879  120.857 1.00 34.55 ? 196  VAL B CB    1 
ATOM   10095 C CG1   . VAL B  1 198  ? -2.005  25.377  119.630 1.00 37.65 ? 196  VAL B CG1   1 
ATOM   10096 C CG2   . VAL B  1 198  ? -2.529  25.789  122.044 1.00 39.45 ? 196  VAL B CG2   1 
ATOM   10097 N N     . THR B  1 199  ? -4.964  22.876  121.879 1.00 40.16 ? 197  THR B N     1 
ATOM   10098 C CA    . THR B  1 199  ? -5.481  22.272  123.090 1.00 32.29 ? 197  THR B CA    1 
ATOM   10099 C C     . THR B  1 199  ? -4.503  22.453  124.245 1.00 40.55 ? 197  THR B C     1 
ATOM   10100 O O     . THR B  1 199  ? -4.922  22.556  125.402 1.00 41.07 ? 197  THR B O     1 
ATOM   10101 C CB    . THR B  1 199  ? -5.781  20.798  122.837 1.00 34.93 ? 197  THR B CB    1 
ATOM   10102 O OG1   . THR B  1 199  ? -6.390  20.664  121.541 1.00 38.19 ? 197  THR B OG1   1 
ATOM   10103 C CG2   . THR B  1 199  ? -6.749  20.269  123.891 1.00 37.02 ? 197  THR B CG2   1 
ATOM   10104 N N     . GLY B  1 200  ? -3.210  22.521  123.944 1.00 35.18 ? 198  GLY B N     1 
ATOM   10105 C CA    . GLY B  1 200  ? -2.202  22.775  124.952 1.00 38.51 ? 198  GLY B CA    1 
ATOM   10106 C C     . GLY B  1 200  ? -0.895  23.157  124.302 1.00 39.38 ? 198  GLY B C     1 
ATOM   10107 O O     . GLY B  1 200  ? -0.655  22.875  123.124 1.00 34.07 ? 198  GLY B O     1 
ATOM   10108 N N     . GLU B  1 201  ? -0.048  23.819  125.084 1.00 42.01 ? 199  GLU B N     1 
ATOM   10109 C CA    . GLU B  1 201  ? 1.273   24.194  124.600 1.00 41.85 ? 199  GLU B CA    1 
ATOM   10110 C C     . GLU B  1 201  ? 2.271   23.046  124.689 1.00 38.91 ? 199  GLU B C     1 
ATOM   10111 O O     . GLU B  1 201  ? 3.298   23.078  124.005 1.00 42.28 ? 199  GLU B O     1 
ATOM   10112 C CB    . GLU B  1 201  ? 1.771   25.418  125.377 1.00 44.53 ? 199  GLU B CB    1 
ATOM   10113 C CG    . GLU B  1 201  ? 0.876   26.638  125.175 1.00 52.06 ? 199  GLU B CG    1 
ATOM   10114 C CD    . GLU B  1 201  ? 1.431   27.912  125.795 1.00 61.49 ? 199  GLU B CD    1 
ATOM   10115 O OE1   . GLU B  1 201  ? 2.049   27.835  126.880 1.00 59.63 ? 199  GLU B OE1   1 
ATOM   10116 O OE2   . GLU B  1 201  ? 1.246   28.992  125.189 1.00 65.49 ? 199  GLU B OE2   1 
ATOM   10117 N N     . THR B  1 202  ? 1.989   22.044  125.517 1.00 37.43 ? 200  THR B N     1 
ATOM   10118 C CA    . THR B  1 202  ? 2.757   20.813  125.600 1.00 36.78 ? 200  THR B CA    1 
ATOM   10119 C C     . THR B  1 202  ? 1.784   19.647  125.539 1.00 37.65 ? 200  THR B C     1 
ATOM   10120 O O     . THR B  1 202  ? 0.608   19.793  125.869 1.00 35.59 ? 200  THR B O     1 
ATOM   10121 C CB    . THR B  1 202  ? 3.548   20.715  126.902 1.00 37.85 ? 200  THR B CB    1 
ATOM   10122 O OG1   . THR B  1 202  ? 2.625   20.656  128.001 1.00 37.37 ? 200  THR B OG1   1 
ATOM   10123 C CG2   . THR B  1 202  ? 4.473   21.916  127.064 1.00 39.20 ? 200  THR B CG2   1 
ATOM   10124 N N     . ILE B  1 203  ? 2.282   18.479  125.122 1.00 34.70 ? 201  ILE B N     1 
ATOM   10125 C CA    . ILE B  1 203  ? 1.415   17.306  125.078 1.00 34.66 ? 201  ILE B CA    1 
ATOM   10126 C C     . ILE B  1 203  ? 0.909   16.985  126.474 1.00 34.79 ? 201  ILE B C     1 
ATOM   10127 O O     . ILE B  1 203  ? -0.231  16.537  126.643 1.00 33.83 ? 201  ILE B O     1 
ATOM   10128 C CB    . ILE B  1 203  ? 2.140   16.104  124.430 1.00 32.35 ? 201  ILE B CB    1 
ATOM   10129 C CG1   . ILE B  1 203  ? 1.179   14.929  124.239 1.00 28.14 ? 201  ILE B CG1   1 
ATOM   10130 C CG2   . ILE B  1 203  ? 3.334   15.656  125.260 1.00 30.94 ? 201  ILE B CG2   1 
ATOM   10131 C CD1   . ILE B  1 203  ? 0.124   15.190  123.192 1.00 27.80 ? 201  ILE B CD1   1 
ATOM   10132 N N     . ARG B  1 204  ? 1.731   17.246  127.495 1.00 33.97 ? 202  ARG B N     1 
ATOM   10133 C CA    . ARG B  1 204  ? 1.315   17.053  128.879 1.00 34.50 ? 202  ARG B CA    1 
ATOM   10134 C C     . ARG B  1 204  ? 0.068   17.870  129.194 1.00 35.76 ? 202  ARG B C     1 
ATOM   10135 O O     . ARG B  1 204  ? -0.906  17.352  129.752 1.00 35.55 ? 202  ARG B O     1 
ATOM   10136 C CB    . ARG B  1 204  ? 2.475   17.438  129.803 1.00 39.46 ? 202  ARG B CB    1 
ATOM   10137 C CG    . ARG B  1 204  ? 2.255   17.155  131.247 1.00 41.45 ? 202  ARG B CG    1 
ATOM   10138 C CD    . ARG B  1 204  ? 3.512   17.488  132.062 1.00 40.03 ? 202  ARG B CD    1 
ATOM   10139 N NE    . ARG B  1 204  ? 3.652   18.916  132.318 1.00 38.25 ? 202  ARG B NE    1 
ATOM   10140 C CZ    . ARG B  1 204  ? 3.097   19.539  133.349 1.00 40.66 ? 202  ARG B CZ    1 
ATOM   10141 N NH1   . ARG B  1 204  ? 2.302   18.901  134.194 1.00 43.42 ? 202  ARG B NH1   1 
ATOM   10142 N NH2   . ARG B  1 204  ? 3.350   20.831  133.544 1.00 42.38 ? 202  ARG B NH2   1 
ATOM   10143 N N     . GLU B  1 205  ? 0.076   19.151  128.823 1.00 34.40 ? 203  GLU B N     1 
ATOM   10144 C CA    . GLU B  1 205  ? -1.066  20.021  129.082 1.00 36.13 ? 203  GLU B CA    1 
ATOM   10145 C C     . GLU B  1 205  ? -2.267  19.649  128.214 1.00 37.23 ? 203  GLU B C     1 
ATOM   10146 O O     . GLU B  1 205  ? -3.409  19.653  128.686 1.00 32.77 ? 203  GLU B O     1 
ATOM   10147 C CB    . GLU B  1 205  ? -0.665  21.475  128.838 1.00 40.67 ? 203  GLU B CB    1 
ATOM   10148 C CG    . GLU B  1 205  ? -1.790  22.467  129.015 1.00 44.58 ? 203  GLU B CG    1 
ATOM   10149 C CD    . GLU B  1 205  ? -1.319  23.898  128.872 1.00 51.59 ? 203  GLU B CD    1 
ATOM   10150 O OE1   . GLU B  1 205  ? -0.437  24.156  128.025 1.00 51.51 ? 203  GLU B OE1   1 
ATOM   10151 O OE2   . GLU B  1 205  ? -1.825  24.765  129.615 1.00 60.51 ? 203  GLU B OE2   1 
ATOM   10152 N N     . ALA B  1 206  ? -2.034  19.352  126.938 1.00 32.24 ? 204  ALA B N     1 
ATOM   10153 C CA    . ALA B  1 206  ? -3.134  18.939  126.075 1.00 35.21 ? 204  ALA B CA    1 
ATOM   10154 C C     . ALA B  1 206  ? -3.847  17.713  126.640 1.00 35.38 ? 204  ALA B C     1 
ATOM   10155 O O     . ALA B  1 206  ? -5.082  17.647  126.632 1.00 36.54 ? 204  ALA B O     1 
ATOM   10156 C CB    . ALA B  1 206  ? -2.613  18.670  124.663 1.00 31.80 ? 204  ALA B CB    1 
ATOM   10157 N N     . LEU B  1 207  ? -3.085  16.742  127.153 1.00 31.01 ? 205  LEU B N     1 
ATOM   10158 C CA    . LEU B  1 207  ? -3.694  15.517  127.665 1.00 36.63 ? 205  LEU B CA    1 
ATOM   10159 C C     . LEU B  1 207  ? -4.529  15.798  128.907 1.00 40.02 ? 205  LEU B C     1 
ATOM   10160 O O     . LEU B  1 207  ? -5.672  15.333  129.012 1.00 40.12 ? 205  LEU B O     1 
ATOM   10161 C CB    . LEU B  1 207  ? -2.621  14.464  127.954 1.00 36.18 ? 205  LEU B CB    1 
ATOM   10162 C CG    . LEU B  1 207  ? -1.875  13.849  126.753 1.00 33.37 ? 205  LEU B CG    1 
ATOM   10163 C CD1   . LEU B  1 207  ? -0.610  13.123  127.237 1.00 30.56 ? 205  LEU B CD1   1 
ATOM   10164 C CD2   . LEU B  1 207  ? -2.773  12.896  125.966 1.00 30.81 ? 205  LEU B CD2   1 
ATOM   10165 N N     . LYS B  1 208  ? -3.979  16.560  129.863 1.00 34.44 ? 206  LYS B N     1 
ATOM   10166 C CA    . LYS B  1 208  ? -4.772  16.961  131.022 1.00 37.83 ? 206  LYS B CA    1 
ATOM   10167 C C     . LYS B  1 208  ? -6.042  17.697  130.602 1.00 39.75 ? 206  LYS B C     1 
ATOM   10168 O O     . LYS B  1 208  ? -7.106  17.497  131.197 1.00 42.69 ? 206  LYS B O     1 
ATOM   10169 C CB    . LYS B  1 208  ? -3.935  17.825  131.969 1.00 40.48 ? 206  LYS B CB    1 
ATOM   10170 N N     . ARG B  1 209  ? -5.958  18.551  129.584 1.00 38.71 ? 207  ARG B N     1 
ATOM   10171 C CA    . ARG B  1 209  ? -7.140  19.290  129.165 1.00 40.58 ? 207  ARG B CA    1 
ATOM   10172 C C     . ARG B  1 209  ? -8.122  18.437  128.378 1.00 45.67 ? 207  ARG B C     1 
ATOM   10173 O O     . ARG B  1 209  ? -9.255  18.877  128.149 1.00 46.06 ? 207  ARG B O     1 
ATOM   10174 C CB    . ARG B  1 209  ? -6.743  20.516  128.339 1.00 42.48 ? 207  ARG B CB    1 
ATOM   10175 C CG    . ARG B  1 209  ? -6.156  21.637  129.184 1.00 44.53 ? 207  ARG B CG    1 
ATOM   10176 C CD    . ARG B  1 209  ? -5.934  22.890  128.365 1.00 47.69 ? 207  ARG B CD    1 
ATOM   10177 N NE    . ARG B  1 209  ? -5.382  23.971  129.173 1.00 55.37 ? 207  ARG B NE    1 
ATOM   10178 C CZ    . ARG B  1 209  ? -4.811  25.061  128.678 1.00 58.36 ? 207  ARG B CZ    1 
ATOM   10179 N NH1   . ARG B  1 209  ? -4.669  25.237  127.372 1.00 52.10 ? 207  ARG B NH1   1 
ATOM   10180 N NH2   . ARG B  1 209  ? -4.369  25.997  129.514 1.00 59.37 ? 207  ARG B NH2   1 
ATOM   10181 N N     . SER B  1 210  ? -7.729  17.231  127.973 1.00 42.77 ? 208  SER B N     1 
ATOM   10182 C CA    . SER B  1 210  ? -8.623  16.391  127.187 1.00 40.48 ? 208  SER B CA    1 
ATOM   10183 C C     . SER B  1 210  ? -9.613  15.617  128.047 1.00 39.49 ? 208  SER B C     1 
ATOM   10184 O O     . SER B  1 210  ? -10.601 15.101  127.516 1.00 39.60 ? 208  SER B O     1 
ATOM   10185 C CB    . SER B  1 210  ? -7.806  15.418  126.339 1.00 34.31 ? 208  SER B CB    1 
ATOM   10186 O OG    . SER B  1 210  ? -6.983  16.121  125.419 1.00 35.72 ? 208  SER B OG    1 
ATOM   10187 N N     . LYS B  1 211  ? -9.369  15.532  129.355 1.00 43.42 ? 209  LYS B N     1 
ATOM   10188 C CA    . LYS B  1 211  ? -10.207 14.716  130.228 1.00 39.72 ? 209  LYS B CA    1 
ATOM   10189 C C     . LYS B  1 211  ? -11.660 15.180  130.226 1.00 45.47 ? 209  LYS B C     1 
ATOM   10190 O O     . LYS B  1 211  ? -12.575 14.353  130.339 1.00 44.32 ? 209  LYS B O     1 
ATOM   10191 C CB    . LYS B  1 211  ? -9.642  14.746  131.643 1.00 41.68 ? 209  LYS B CB    1 
ATOM   10192 C CG    . LYS B  1 211  ? -8.207  14.267  131.738 1.00 51.44 ? 209  LYS B CG    1 
ATOM   10193 C CD    . LYS B  1 211  ? -8.096  12.780  131.416 1.00 55.34 ? 209  LYS B CD    1 
ATOM   10194 C CE    . LYS B  1 211  ? -6.788  12.197  131.933 1.00 57.14 ? 209  LYS B CE    1 
ATOM   10195 N NZ    . LYS B  1 211  ? -5.613  12.813  131.255 1.00 56.94 ? 209  LYS B NZ    1 
ATOM   10196 N N     . GLU B  1 212  ? -11.888 16.489  130.087 1.00 44.14 ? 210  GLU B N     1 
ATOM   10197 C CA    . GLU B  1 212  ? -13.238 17.032  130.168 1.00 43.19 ? 210  GLU B CA    1 
ATOM   10198 C C     . GLU B  1 212  ? -14.124 16.463  129.066 1.00 43.90 ? 210  GLU B C     1 
ATOM   10199 O O     . GLU B  1 212  ? -15.161 15.851  129.336 1.00 45.03 ? 210  GLU B O     1 
ATOM   10200 C CB    . GLU B  1 212  ? -13.188 18.560  130.095 1.00 43.04 ? 210  GLU B CB    1 
ATOM   10201 N N     . LEU B  1 213  ? -13.720 16.639  127.810 1.00 41.46 ? 211  LEU B N     1 
ATOM   10202 C CA    . LEU B  1 213  ? -14.559 16.165  126.715 1.00 45.16 ? 211  LEU B CA    1 
ATOM   10203 C C     . LEU B  1 213  ? -14.502 14.648  126.573 1.00 45.55 ? 211  LEU B C     1 
ATOM   10204 O O     . LEU B  1 213  ? -15.454 14.043  126.065 1.00 44.56 ? 211  LEU B O     1 
ATOM   10205 C CB    . LEU B  1 213  ? -14.166 16.855  125.408 1.00 42.42 ? 211  LEU B CB    1 
ATOM   10206 C CG    . LEU B  1 213  ? -14.293 18.381  125.455 1.00 45.05 ? 211  LEU B CG    1 
ATOM   10207 C CD1   . LEU B  1 213  ? -14.245 18.984  124.078 1.00 45.29 ? 211  LEU B CD1   1 
ATOM   10208 C CD2   . LEU B  1 213  ? -15.570 18.809  126.168 1.00 50.95 ? 211  LEU B CD2   1 
ATOM   10209 N N     . GLU B  1 214  ? -13.413 14.011  127.019 1.00 42.79 ? 212  GLU B N     1 
ATOM   10210 C CA    . GLU B  1 214  ? -13.374 12.551  126.983 1.00 42.93 ? 212  GLU B CA    1 
ATOM   10211 C C     . GLU B  1 214  ? -14.443 11.950  127.891 1.00 44.92 ? 212  GLU B C     1 
ATOM   10212 O O     . GLU B  1 214  ? -15.077 10.950  127.534 1.00 45.72 ? 212  GLU B O     1 
ATOM   10213 C CB    . GLU B  1 214  ? -11.984 12.036  127.359 1.00 44.23 ? 212  GLU B CB    1 
ATOM   10214 C CG    . GLU B  1 214  ? -10.961 12.126  126.213 1.00 41.34 ? 212  GLU B CG    1 
ATOM   10215 C CD    . GLU B  1 214  ? -9.623  11.489  126.565 1.00 39.87 ? 212  GLU B CD    1 
ATOM   10216 O OE1   . GLU B  1 214  ? -9.407  11.183  127.753 1.00 46.53 ? 212  GLU B OE1   1 
ATOM   10217 O OE2   . GLU B  1 214  ? -8.782  11.301  125.656 1.00 41.59 ? 212  GLU B OE2   1 
ATOM   10218 N N     . GLU B  1 215  ? -14.674 12.556  129.058 1.00 43.71 ? 213  GLU B N     1 
ATOM   10219 C CA    . GLU B  1 215  ? -15.738 12.076  129.929 1.00 43.12 ? 213  GLU B CA    1 
ATOM   10220 C C     . GLU B  1 215  ? -17.113 12.270  129.302 1.00 49.28 ? 213  GLU B C     1 
ATOM   10221 O O     . GLU B  1 215  ? -18.043 11.535  129.643 1.00 51.13 ? 213  GLU B O     1 
ATOM   10222 C CB    . GLU B  1 215  ? -15.672 12.772  131.294 1.00 47.50 ? 213  GLU B CB    1 
ATOM   10223 N N     . LYS B  1 216  ? -17.258 13.224  128.379 1.00 47.70 ? 214  LYS B N     1 
ATOM   10224 C CA    . LYS B  1 216  ? -18.509 13.389  127.648 1.00 50.09 ? 214  LYS B CA    1 
ATOM   10225 C C     . LYS B  1 216  ? -18.612 12.483  126.426 1.00 47.23 ? 214  LYS B C     1 
ATOM   10226 O O     . LYS B  1 216  ? -19.663 12.472  125.779 1.00 50.10 ? 214  LYS B O     1 
ATOM   10227 C CB    . LYS B  1 216  ? -18.690 14.843  127.202 1.00 47.04 ? 214  LYS B CB    1 
ATOM   10228 C CG    . LYS B  1 216  ? -18.789 15.861  128.326 1.00 53.69 ? 214  LYS B CG    1 
ATOM   10229 C CD    . LYS B  1 216  ? -19.539 17.095  127.839 1.00 55.38 ? 214  LYS B CD    1 
ATOM   10230 C CE    . LYS B  1 216  ? -19.293 18.304  128.723 1.00 59.38 ? 214  LYS B CE    1 
ATOM   10231 N NZ    . LYS B  1 216  ? -18.063 19.042  128.311 1.00 60.79 ? 214  LYS B NZ    1 
ATOM   10232 N N     . GLY B  1 217  ? -17.557 11.739  126.088 1.00 44.84 ? 215  GLY B N     1 
ATOM   10233 C CA    . GLY B  1 217  ? -17.595 10.772  125.006 1.00 45.17 ? 215  GLY B CA    1 
ATOM   10234 C C     . GLY B  1 217  ? -16.770 11.121  123.784 1.00 46.41 ? 215  GLY B C     1 
ATOM   10235 O O     . GLY B  1 217  ? -16.763 10.338  122.824 1.00 47.30 ? 215  GLY B O     1 
ATOM   10236 N N     . PHE B  1 218  ? -16.100 12.269  123.763 1.00 41.81 ? 216  PHE B N     1 
ATOM   10237 C CA    . PHE B  1 218  ? -15.162 12.562  122.693 1.00 42.59 ? 216  PHE B CA    1 
ATOM   10238 C C     . PHE B  1 218  ? -13.875 11.764  122.877 1.00 42.20 ? 216  PHE B C     1 
ATOM   10239 O O     . PHE B  1 218  ? -13.553 11.291  123.971 1.00 40.23 ? 216  PHE B O     1 
ATOM   10240 C CB    . PHE B  1 218  ? -14.815 14.053  122.650 1.00 43.36 ? 216  PHE B CB    1 
ATOM   10241 C CG    . PHE B  1 218  ? -15.967 14.939  122.286 1.00 45.10 ? 216  PHE B CG    1 
ATOM   10242 C CD1   . PHE B  1 218  ? -16.897 15.318  123.242 1.00 46.19 ? 216  PHE B CD1   1 
ATOM   10243 C CD2   . PHE B  1 218  ? -16.114 15.406  120.992 1.00 43.07 ? 216  PHE B CD2   1 
ATOM   10244 C CE1   . PHE B  1 218  ? -17.955 16.139  122.911 1.00 46.77 ? 216  PHE B CE1   1 
ATOM   10245 C CE2   . PHE B  1 218  ? -17.171 16.228  120.655 1.00 45.54 ? 216  PHE B CE2   1 
ATOM   10246 C CZ    . PHE B  1 218  ? -18.095 16.591  121.617 1.00 44.21 ? 216  PHE B CZ    1 
ATOM   10247 N N     . SER B  1 219  ? -13.132 11.621  121.783 1.00 39.62 ? 217  SER B N     1 
ATOM   10248 C CA    . SER B  1 219  ? -11.764 11.126  121.819 1.00 36.13 ? 217  SER B CA    1 
ATOM   10249 C C     . SER B  1 219  ? -10.879 12.156  121.134 1.00 36.42 ? 217  SER B C     1 
ATOM   10250 O O     . SER B  1 219  ? -11.355 13.189  120.655 1.00 38.03 ? 217  SER B O     1 
ATOM   10251 C CB    . SER B  1 219  ? -11.639 9.742   121.168 1.00 38.40 ? 217  SER B CB    1 
ATOM   10252 O OG    . SER B  1 219  ? -11.909 9.801   119.773 1.00 40.26 ? 217  SER B OG    1 
ATOM   10253 N N     . TYR B  1 220  ? -9.576  11.879  121.083 1.00 34.93 ? 218  TYR B N     1 
ATOM   10254 C CA    . TYR B  1 220  ? -8.620  12.874  120.631 1.00 33.01 ? 218  TYR B CA    1 
ATOM   10255 C C     . TYR B  1 220  ? -7.596  12.264  119.685 1.00 31.01 ? 218  TYR B C     1 
ATOM   10256 O O     . TYR B  1 220  ? -7.279  11.075  119.755 1.00 34.94 ? 218  TYR B O     1 
ATOM   10257 C CB    . TYR B  1 220  ? -7.906  13.529  121.821 1.00 30.73 ? 218  TYR B CB    1 
ATOM   10258 C CG    . TYR B  1 220  ? -8.710  14.637  122.467 1.00 32.72 ? 218  TYR B CG    1 
ATOM   10259 C CD1   . TYR B  1 220  ? -9.648  14.371  123.470 1.00 34.39 ? 218  TYR B CD1   1 
ATOM   10260 C CD2   . TYR B  1 220  ? -8.529  15.951  122.078 1.00 32.00 ? 218  TYR B CD2   1 
ATOM   10261 C CE1   . TYR B  1 220  ? -10.382 15.400  124.046 1.00 33.53 ? 218  TYR B CE1   1 
ATOM   10262 C CE2   . TYR B  1 220  ? -9.255  16.974  122.647 1.00 33.13 ? 218  TYR B CE2   1 
ATOM   10263 C CZ    . TYR B  1 220  ? -10.177 16.698  123.624 1.00 34.01 ? 218  TYR B CZ    1 
ATOM   10264 O OH    . TYR B  1 220  ? -10.877 17.750  124.166 1.00 36.46 ? 218  TYR B OH    1 
ATOM   10265 N N     . SER B  1 221  ? -7.094  13.102  118.788 1.00 31.69 ? 219  SER B N     1 
ATOM   10266 C CA    . SER B  1 221  ? -5.930  12.802  117.964 1.00 28.64 ? 219  SER B CA    1 
ATOM   10267 C C     . SER B  1 221  ? -5.056  14.044  118.002 1.00 30.37 ? 219  SER B C     1 
ATOM   10268 O O     . SER B  1 221  ? -5.488  15.117  117.571 1.00 29.54 ? 219  SER B O     1 
ATOM   10269 C CB    . SER B  1 221  ? -6.327  12.452  116.522 1.00 28.37 ? 219  SER B CB    1 
ATOM   10270 O OG    . SER B  1 221  ? -5.179  12.363  115.691 1.00 29.14 ? 219  SER B OG    1 
ATOM   10271 N N     . TYR B  1 222  ? -3.847  13.918  118.538 1.00 28.78 ? 220  TYR B N     1 
ATOM   10272 C CA    . TYR B  1 222  ? -3.025  15.089  118.792 1.00 28.36 ? 220  TYR B CA    1 
ATOM   10273 C C     . TYR B  1 222  ? -2.107  15.371  117.623 1.00 26.58 ? 220  TYR B C     1 
ATOM   10274 O O     . TYR B  1 222  ? -1.510  14.457  117.046 1.00 27.64 ? 220  TYR B O     1 
ATOM   10275 C CB    . TYR B  1 222  ? -2.211  14.907  120.072 1.00 27.36 ? 220  TYR B CB    1 
ATOM   10276 C CG    . TYR B  1 222  ? -3.111  14.725  121.258 1.00 28.21 ? 220  TYR B CG    1 
ATOM   10277 C CD1   . TYR B  1 222  ? -3.680  15.818  121.885 1.00 28.30 ? 220  TYR B CD1   1 
ATOM   10278 C CD2   . TYR B  1 222  ? -3.421  13.456  121.733 1.00 28.98 ? 220  TYR B CD2   1 
ATOM   10279 C CE1   . TYR B  1 222  ? -4.516  15.666  122.945 1.00 29.11 ? 220  TYR B CE1   1 
ATOM   10280 C CE2   . TYR B  1 222  ? -4.268  13.290  122.808 1.00 30.61 ? 220  TYR B CE2   1 
ATOM   10281 C CZ    . TYR B  1 222  ? -4.811  14.405  123.407 1.00 29.86 ? 220  TYR B CZ    1 
ATOM   10282 O OH    . TYR B  1 222  ? -5.650  14.269  124.474 1.00 31.92 ? 220  TYR B OH    1 
ATOM   10283 N N     . ASP B  1 223  ? -2.004  16.654  117.293 1.00 27.19 ? 221  ASP B N     1 
ATOM   10284 C CA    . ASP B  1 223  ? -1.195  17.164  116.192 1.00 30.46 ? 221  ASP B CA    1 
ATOM   10285 C C     . ASP B  1 223  ? -0.077  18.014  116.791 1.00 35.87 ? 221  ASP B C     1 
ATOM   10286 O O     . ASP B  1 223  ? -0.295  19.173  117.160 1.00 36.07 ? 221  ASP B O     1 
ATOM   10287 C CB    . ASP B  1 223  ? -2.049  17.976  115.228 1.00 32.11 ? 221  ASP B CB    1 
ATOM   10288 C CG    . ASP B  1 223  ? -1.209  18.793  114.257 1.00 38.27 ? 221  ASP B CG    1 
ATOM   10289 O OD1   . ASP B  1 223  ? -0.174  18.281  113.785 1.00 38.22 ? 221  ASP B OD1   1 
ATOM   10290 O OD2   . ASP B  1 223  ? -1.578  19.946  113.968 1.00 40.86 ? 221  ASP B OD2   1 
ATOM   10291 N N     . MET B  1 224  ? 1.109   17.424  116.909 1.00 32.55 ? 222  MET B N     1 
ATOM   10292 C CA    . MET B  1 224  ? 2.298   18.188  117.243 1.00 36.97 ? 222  MET B CA    1 
ATOM   10293 C C     . MET B  1 224  ? 2.566   19.128  116.079 1.00 37.04 ? 222  MET B C     1 
ATOM   10294 O O     . MET B  1 224  ? 2.876   18.678  114.973 1.00 42.10 ? 222  MET B O     1 
ATOM   10295 C CB    . MET B  1 224  ? 3.470   17.248  117.506 1.00 33.25 ? 222  MET B CB    1 
ATOM   10296 C CG    . MET B  1 224  ? 3.178   16.216  118.580 1.00 30.50 ? 222  MET B CG    1 
ATOM   10297 S SD    . MET B  1 224  ? 2.687   16.926  120.173 1.00 38.22 ? 222  MET B SD    1 
ATOM   10298 C CE    . MET B  1 224  ? 4.282   17.474  120.778 1.00 30.47 ? 222  MET B CE    1 
ATOM   10299 N N     . LEU B  1 225  ? 2.354   20.420  116.299 1.00 37.29 ? 223  LEU B N     1 
ATOM   10300 C CA    . LEU B  1 225  ? 2.468   21.403  115.227 1.00 40.65 ? 223  LEU B CA    1 
ATOM   10301 C C     . LEU B  1 225  ? 3.806   21.262  114.521 1.00 47.05 ? 223  LEU B C     1 
ATOM   10302 O O     . LEU B  1 225  ? 4.864   21.440  115.132 1.00 44.70 ? 223  LEU B O     1 
ATOM   10303 C CB    . LEU B  1 225  ? 2.308   22.804  115.808 1.00 44.10 ? 223  LEU B CB    1 
ATOM   10304 C CG    . LEU B  1 225  ? 0.896   23.078  116.313 1.00 45.61 ? 223  LEU B CG    1 
ATOM   10305 C CD1   . LEU B  1 225  ? 0.862   24.383  117.088 1.00 46.52 ? 223  LEU B CD1   1 
ATOM   10306 C CD2   . LEU B  1 225  ? -0.082  23.094  115.136 1.00 42.38 ? 223  LEU B CD2   1 
ATOM   10307 N N     . GLY B  1 226  ? 3.755   20.912  113.238 1.00 40.57 ? 224  GLY B N     1 
ATOM   10308 C CA    . GLY B  1 226  ? 4.958   20.576  112.507 1.00 43.07 ? 224  GLY B CA    1 
ATOM   10309 C C     . GLY B  1 226  ? 4.691   20.044  111.113 1.00 37.89 ? 224  GLY B C     1 
ATOM   10310 O O     . GLY B  1 226  ? 3.832   19.175  110.918 1.00 36.50 ? 224  GLY B O     1 
ATOM   10311 N N     . GLU B  1 227  ? 5.425   20.568  110.136 1.00 38.38 ? 225  GLU B N     1 
ATOM   10312 C CA    . GLU B  1 227  ? 5.262   20.193  108.738 1.00 33.12 ? 225  GLU B CA    1 
ATOM   10313 C C     . GLU B  1 227  ? 6.333   20.885  107.915 1.00 30.76 ? 225  GLU B C     1 
ATOM   10314 O O     . GLU B  1 227  ? 6.943   21.865  108.353 1.00 32.61 ? 225  GLU B O     1 
ATOM   10315 C CB    . GLU B  1 227  ? 3.877   20.559  108.198 1.00 37.23 ? 225  GLU B CB    1 
ATOM   10316 C CG    . GLU B  1 227  ? 3.497   22.014  108.370 1.00 39.12 ? 225  GLU B CG    1 
ATOM   10317 C CD    . GLU B  1 227  ? 2.150   22.320  107.747 1.00 43.42 ? 225  GLU B CD    1 
ATOM   10318 O OE1   . GLU B  1 227  ? 2.073   22.400  106.500 1.00 44.10 ? 225  GLU B OE1   1 
ATOM   10319 O OE2   . GLU B  1 227  ? 1.166   22.459  108.501 1.00 45.41 ? 225  GLU B OE2   1 
ATOM   10320 N N     . ALA B  1 228  ? 6.531   20.368  106.704 1.00 28.23 ? 226  ALA B N     1 
ATOM   10321 C CA    . ALA B  1 228  ? 7.452   20.932  105.721 1.00 29.56 ? 226  ALA B CA    1 
ATOM   10322 C C     . ALA B  1 228  ? 8.810   21.236  106.351 1.00 27.92 ? 226  ALA B C     1 
ATOM   10323 O O     . ALA B  1 228  ? 9.259   22.384  106.418 1.00 28.10 ? 226  ALA B O     1 
ATOM   10324 C CB    . ALA B  1 228  ? 6.849   22.183  105.069 1.00 30.43 ? 226  ALA B CB    1 
ATOM   10325 N N     . ALA B  1 229  ? 9.446   20.182  106.860 1.00 23.36 ? 227  ALA B N     1 
ATOM   10326 C CA    . ALA B  1 229  ? 10.823  20.312  107.318 1.00 25.49 ? 227  ALA B CA    1 
ATOM   10327 C C     . ALA B  1 229  ? 11.693  20.869  106.194 1.00 24.47 ? 227  ALA B C     1 
ATOM   10328 O O     . ALA B  1 229  ? 11.583  20.441  105.039 1.00 26.71 ? 227  ALA B O     1 
ATOM   10329 C CB    . ALA B  1 229  ? 11.351  18.958  107.779 1.00 20.79 ? 227  ALA B CB    1 
ATOM   10330 N N     . THR B  1 230  ? 12.516  21.858  106.528 1.00 25.25 ? 228  THR B N     1 
ATOM   10331 C CA    . THR B  1 230  ? 13.424  22.495  105.585 1.00 26.58 ? 228  THR B CA    1 
ATOM   10332 C C     . THR B  1 230  ? 14.831  21.920  105.637 1.00 25.89 ? 228  THR B C     1 
ATOM   10333 O O     . THR B  1 230  ? 15.518  21.900  104.611 1.00 22.83 ? 228  THR B O     1 
ATOM   10334 C CB    . THR B  1 230  ? 13.497  24.008  105.857 1.00 31.22 ? 228  THR B CB    1 
ATOM   10335 O OG1   . THR B  1 230  ? 12.181  24.569  105.830 1.00 34.15 ? 228  THR B OG1   1 
ATOM   10336 C CG2   . THR B  1 230  ? 14.347  24.713  104.807 1.00 28.88 ? 228  THR B CG2   1 
ATOM   10337 N N     . THR B  1 231  ? 15.274  21.464  106.808 1.00 26.23 ? 229  THR B N     1 
ATOM   10338 C CA    . THR B  1 231  ? 16.612  20.928  107.005 1.00 25.59 ? 229  THR B CA    1 
ATOM   10339 C C     . THR B  1 231  ? 16.515  19.558  107.664 1.00 26.00 ? 229  THR B C     1 
ATOM   10340 O O     . THR B  1 231  ? 15.473  19.183  108.217 1.00 25.46 ? 229  THR B O     1 
ATOM   10341 C CB    . THR B  1 231  ? 17.466  21.824  107.904 1.00 24.22 ? 229  THR B CB    1 
ATOM   10342 O OG1   . THR B  1 231  ? 16.962  21.728  109.244 1.00 28.05 ? 229  THR B OG1   1 
ATOM   10343 C CG2   . THR B  1 231  ? 17.427  23.286  107.440 1.00 23.14 ? 229  THR B CG2   1 
ATOM   10344 N N     . ALA B  1 232  ? 17.635  18.826  107.619 1.00 22.94 ? 230  ALA B N     1 
ATOM   10345 C CA    . ALA B  1 232  ? 17.705  17.546  108.318 1.00 27.17 ? 230  ALA B CA    1 
ATOM   10346 C C     . ALA B  1 232  ? 17.424  17.711  109.805 1.00 28.25 ? 230  ALA B C     1 
ATOM   10347 O O     . ALA B  1 232  ? 16.788  16.846  110.426 1.00 24.14 ? 230  ALA B O     1 
ATOM   10348 C CB    . ALA B  1 232  ? 19.075  16.904  108.103 1.00 29.31 ? 230  ALA B CB    1 
ATOM   10349 N N     . ALA B  1 233  ? 17.910  18.806  110.400 1.00 27.51 ? 231  ALA B N     1 
ATOM   10350 C CA    . ALA B  1 233  ? 17.723  19.022  111.830 1.00 26.71 ? 231  ALA B CA    1 
ATOM   10351 C C     . ALA B  1 233  ? 16.266  19.311  112.157 1.00 27.38 ? 231  ALA B C     1 
ATOM   10352 O O     . ALA B  1 233  ? 15.794  18.938  113.234 1.00 24.50 ? 231  ALA B O     1 
ATOM   10353 C CB    . ALA B  1 233  ? 18.616  20.169  112.322 1.00 24.18 ? 231  ALA B CB    1 
ATOM   10354 N N     . ASP B  1 234  ? 15.544  19.980  111.250 1.00 19.63 ? 232  ASP B N     1 
ATOM   10355 C CA    . ASP B  1 234  ? 14.109  20.167  111.433 1.00 26.29 ? 232  ASP B CA    1 
ATOM   10356 C C     . ASP B  1 234  ? 13.399  18.830  111.519 1.00 24.99 ? 232  ASP B C     1 
ATOM   10357 O O     . ASP B  1 234  ? 12.560  18.614  112.397 1.00 21.67 ? 232  ASP B O     1 
ATOM   10358 C CB    . ASP B  1 234  ? 13.513  20.957  110.266 1.00 23.86 ? 232  ASP B CB    1 
ATOM   10359 C CG    . ASP B  1 234  ? 13.848  22.422  110.305 1.00 30.84 ? 232  ASP B CG    1 
ATOM   10360 O OD1   . ASP B  1 234  ? 14.276  22.917  111.364 1.00 32.03 ? 232  ASP B OD1   1 
ATOM   10361 O OD2   . ASP B  1 234  ? 13.655  23.078  109.252 1.00 31.82 ? 232  ASP B OD2   1 
ATOM   10362 N N     . ALA B  1 235  ? 13.671  17.953  110.548 1.00 22.44 ? 233  ALA B N     1 
ATOM   10363 C CA    . ALA B  1 235  ? 12.992  16.670  110.463 1.00 23.60 ? 233  ALA B CA    1 
ATOM   10364 C C     . ALA B  1 235  ? 13.320  15.798  111.658 1.00 23.49 ? 233  ALA B C     1 
ATOM   10365 O O     . ALA B  1 235  ? 12.437  15.121  112.193 1.00 23.70 ? 233  ALA B O     1 
ATOM   10366 C CB    . ALA B  1 235  ? 13.381  15.962  109.164 1.00 26.19 ? 233  ALA B CB    1 
ATOM   10367 N N     . GLU B  1 236  ? 14.584  15.809  112.096 1.00 23.04 ? 234  GLU B N     1 
ATOM   10368 C CA    . GLU B  1 236  ? 14.961  15.018  113.258 1.00 22.25 ? 234  GLU B CA    1 
ATOM   10369 C C     . GLU B  1 236  ? 14.256  15.528  114.509 1.00 25.93 ? 234  GLU B C     1 
ATOM   10370 O O     . GLU B  1 236  ? 13.819  14.736  115.356 1.00 25.83 ? 234  GLU B O     1 
ATOM   10371 C CB    . GLU B  1 236  ? 16.486  15.054  113.424 1.00 24.54 ? 234  GLU B CB    1 
ATOM   10372 C CG    . GLU B  1 236  ? 17.032  14.115  114.468 1.00 30.25 ? 234  GLU B CG    1 
ATOM   10373 C CD    . GLU B  1 236  ? 18.553  14.178  114.575 1.00 37.14 ? 234  GLU B CD    1 
ATOM   10374 O OE1   . GLU B  1 236  ? 19.206  14.793  113.701 1.00 40.67 ? 234  GLU B OE1   1 
ATOM   10375 O OE2   . GLU B  1 236  ? 19.094  13.609  115.545 1.00 39.63 ? 234  GLU B OE2   1 
ATOM   10376 N N     . ARG B  1 237  ? 14.126  16.850  114.638 1.00 22.67 ? 235  ARG B N     1 
ATOM   10377 C CA    . ARG B  1 237  ? 13.392  17.410  115.767 1.00 23.49 ? 235  ARG B CA    1 
ATOM   10378 C C     . ARG B  1 237  ? 11.920  17.015  115.718 1.00 23.81 ? 235  ARG B C     1 
ATOM   10379 O O     . ARG B  1 237  ? 11.349  16.588  116.726 1.00 24.42 ? 235  ARG B O     1 
ATOM   10380 C CB    . ARG B  1 237  ? 13.530  18.928  115.788 1.00 26.54 ? 235  ARG B CB    1 
ATOM   10381 C CG    . ARG B  1 237  ? 12.848  19.542  116.973 1.00 30.43 ? 235  ARG B CG    1 
ATOM   10382 C CD    . ARG B  1 237  ? 12.315  20.932  116.694 1.00 39.39 ? 235  ARG B CD    1 
ATOM   10383 N NE    . ARG B  1 237  ? 11.722  21.485  117.906 1.00 47.47 ? 235  ARG B NE    1 
ATOM   10384 C CZ    . ARG B  1 237  ? 12.117  22.601  118.500 1.00 43.76 ? 235  ARG B CZ    1 
ATOM   10385 N NH1   . ARG B  1 237  ? 13.056  23.371  117.971 1.00 44.63 ? 235  ARG B NH1   1 
ATOM   10386 N NH2   . ARG B  1 237  ? 11.548  22.961  119.648 1.00 41.10 ? 235  ARG B NH2   1 
ATOM   10387 N N     . TYR B  1 238  ? 11.284  17.146  114.548 1.00 22.59 ? 236  TYR B N     1 
ATOM   10388 C CA    . TYR B  1 238  ? 9.879   16.748  114.442 1.00 23.31 ? 236  TYR B CA    1 
ATOM   10389 C C     . TYR B  1 238  ? 9.707   15.271  114.774 1.00 22.87 ? 236  TYR B C     1 
ATOM   10390 O O     . TYR B  1 238  ? 8.728   14.879  115.416 1.00 23.08 ? 236  TYR B O     1 
ATOM   10391 C CB    . TYR B  1 238  ? 9.331   17.041  113.038 1.00 21.74 ? 236  TYR B CB    1 
ATOM   10392 C CG    . TYR B  1 238  ? 9.136   18.514  112.725 1.00 25.51 ? 236  TYR B CG    1 
ATOM   10393 C CD1   . TYR B  1 238  ? 8.736   19.414  113.711 1.00 34.65 ? 236  TYR B CD1   1 
ATOM   10394 C CD2   . TYR B  1 238  ? 9.378   19.010  111.449 1.00 26.25 ? 236  TYR B CD2   1 
ATOM   10395 C CE1   . TYR B  1 238  ? 8.566   20.766  113.426 1.00 35.93 ? 236  TYR B CE1   1 
ATOM   10396 C CE2   . TYR B  1 238  ? 9.218   20.353  111.159 1.00 30.79 ? 236  TYR B CE2   1 
ATOM   10397 C CZ    . TYR B  1 238  ? 8.809   21.225  112.149 1.00 37.44 ? 236  TYR B CZ    1 
ATOM   10398 O OH    . TYR B  1 238  ? 8.647   22.563  111.850 1.00 40.48 ? 236  TYR B OH    1 
ATOM   10399 N N     . TYR B  1 239  ? 10.648  14.432  114.344 1.00 22.65 ? 237  TYR B N     1 
ATOM   10400 C CA    . TYR B  1 239  ? 10.577  13.026  114.724 1.00 23.30 ? 237  TYR B CA    1 
ATOM   10401 C C     . TYR B  1 239  ? 10.617  12.870  116.241 1.00 25.49 ? 237  TYR B C     1 
ATOM   10402 O O     . TYR B  1 239  ? 9.813   12.136  116.830 1.00 25.31 ? 237  TYR B O     1 
ATOM   10403 C CB    . TYR B  1 239  ? 11.719  12.247  114.080 1.00 23.37 ? 237  TYR B CB    1 
ATOM   10404 C CG    . TYR B  1 239  ? 11.798  10.817  114.549 1.00 25.84 ? 237  TYR B CG    1 
ATOM   10405 C CD1   . TYR B  1 239  ? 11.047  9.823   113.943 1.00 26.77 ? 237  TYR B CD1   1 
ATOM   10406 C CD2   . TYR B  1 239  ? 12.622  10.455  115.608 1.00 24.38 ? 237  TYR B CD2   1 
ATOM   10407 C CE1   . TYR B  1 239  ? 11.106  8.514   114.375 1.00 27.85 ? 237  TYR B CE1   1 
ATOM   10408 C CE2   . TYR B  1 239  ? 12.678  9.145   116.050 1.00 31.61 ? 237  TYR B CE2   1 
ATOM   10409 C CZ    . TYR B  1 239  ? 11.925  8.176   115.416 1.00 27.87 ? 237  TYR B CZ    1 
ATOM   10410 O OH    . TYR B  1 239  ? 11.982  6.870   115.844 1.00 35.35 ? 237  TYR B OH    1 
ATOM   10411 N N     . ARG B  1 240  ? 11.555  13.553  116.894 1.00 24.95 ? 238  ARG B N     1 
ATOM   10412 C CA    . ARG B  1 240  ? 11.654  13.397  118.337 1.00 26.47 ? 238  ARG B CA    1 
ATOM   10413 C C     . ARG B  1 240  ? 10.418  13.928  119.050 1.00 24.85 ? 238  ARG B C     1 
ATOM   10414 O O     . ARG B  1 240  ? 10.023  13.367  120.080 1.00 26.06 ? 238  ARG B O     1 
ATOM   10415 C CB    . ARG B  1 240  ? 12.919  14.077  118.869 1.00 27.08 ? 238  ARG B CB    1 
ATOM   10416 C CG    . ARG B  1 240  ? 14.198  13.432  118.364 1.00 28.09 ? 238  ARG B CG    1 
ATOM   10417 C CD    . ARG B  1 240  ? 14.310  11.977  118.815 1.00 25.54 ? 238  ARG B CD    1 
ATOM   10418 N NE    . ARG B  1 240  ? 15.505  11.359  118.260 1.00 34.52 ? 238  ARG B NE    1 
ATOM   10419 C CZ    . ARG B  1 240  ? 15.821  10.078  118.390 1.00 40.43 ? 238  ARG B CZ    1 
ATOM   10420 N NH1   . ARG B  1 240  ? 15.064  9.246   119.084 1.00 33.54 ? 238  ARG B NH1   1 
ATOM   10421 N NH2   . ARG B  1 240  ? 16.930  9.621   117.810 1.00 41.93 ? 238  ARG B NH2   1 
ATOM   10422 N N     . ASP B  1 241  ? 9.808   14.999  118.527 1.00 25.19 ? 239  ASP B N     1 
ATOM   10423 C CA    . ASP B  1 241  ? 8.550   15.501  119.077 1.00 26.18 ? 239  ASP B CA    1 
ATOM   10424 C C     . ASP B  1 241  ? 7.436   14.462  118.938 1.00 24.95 ? 239  ASP B C     1 
ATOM   10425 O O     . ASP B  1 241  ? 6.665   14.236  119.874 1.00 25.18 ? 239  ASP B O     1 
ATOM   10426 C CB    . ASP B  1 241  ? 8.136   16.801  118.376 1.00 26.62 ? 239  ASP B CB    1 
ATOM   10427 C CG    . ASP B  1 241  ? 9.042   17.992  118.712 1.00 34.58 ? 239  ASP B CG    1 
ATOM   10428 O OD1   . ASP B  1 241  ? 9.802   17.951  119.706 1.00 37.72 ? 239  ASP B OD1   1 
ATOM   10429 O OD2   . ASP B  1 241  ? 8.969   18.992  117.965 1.00 37.87 ? 239  ASP B OD2   1 
ATOM   10430 N N     . TYR B  1 242  ? 7.321   13.841  117.760 1.00 25.70 ? 240  TYR B N     1 
ATOM   10431 C CA    . TYR B  1 242  ? 6.329   12.781  117.583 1.00 25.04 ? 240  TYR B CA    1 
ATOM   10432 C C     . TYR B  1 242  ? 6.569   11.634  118.554 1.00 25.73 ? 240  TYR B C     1 
ATOM   10433 O O     . TYR B  1 242  ? 5.627   11.133  119.182 1.00 26.35 ? 240  TYR B O     1 
ATOM   10434 C CB    . TYR B  1 242  ? 6.360   12.252  116.153 1.00 24.71 ? 240  TYR B CB    1 
ATOM   10435 C CG    . TYR B  1 242  ? 5.768   13.170  115.103 1.00 24.13 ? 240  TYR B CG    1 
ATOM   10436 C CD1   . TYR B  1 242  ? 4.751   14.061  115.406 1.00 25.75 ? 240  TYR B CD1   1 
ATOM   10437 C CD2   . TYR B  1 242  ? 6.226   13.119  113.805 1.00 25.88 ? 240  TYR B CD2   1 
ATOM   10438 C CE1   . TYR B  1 242  ? 4.196   14.892  114.413 1.00 26.83 ? 240  TYR B CE1   1 
ATOM   10439 C CE2   . TYR B  1 242  ? 5.693   13.935  112.814 1.00 28.59 ? 240  TYR B CE2   1 
ATOM   10440 C CZ    . TYR B  1 242  ? 4.685   14.820  113.126 1.00 25.63 ? 240  TYR B CZ    1 
ATOM   10441 O OH    . TYR B  1 242  ? 4.171   15.614  112.120 1.00 25.42 ? 240  TYR B OH    1 
ATOM   10442 N N     . GLU B  1 243  ? 7.833   11.225  118.706 1.00 26.04 ? 241  GLU B N     1 
ATOM   10443 C CA    . GLU B  1 243  ? 8.185   10.097  119.564 1.00 26.42 ? 241  GLU B CA    1 
ATOM   10444 C C     . GLU B  1 243  ? 7.845   10.381  121.020 1.00 27.51 ? 241  GLU B C     1 
ATOM   10445 O O     . GLU B  1 243  ? 7.265   9.536   121.716 1.00 27.61 ? 241  GLU B O     1 
ATOM   10446 C CB    . GLU B  1 243  ? 9.672   9.797   119.415 1.00 26.93 ? 241  GLU B CB    1 
ATOM   10447 C CG    . GLU B  1 243  ? 10.209  8.724   120.334 1.00 30.65 ? 241  GLU B CG    1 
ATOM   10448 C CD    . GLU B  1 243  ? 11.721  8.654   120.252 1.00 34.39 ? 241  GLU B CD    1 
ATOM   10449 O OE1   . GLU B  1 243  ? 12.354  9.730   120.262 1.00 30.76 ? 241  GLU B OE1   1 
ATOM   10450 O OE2   . GLU B  1 243  ? 12.271  7.536   120.164 1.00 37.17 ? 241  GLU B OE2   1 
ATOM   10451 N N     . SER B  1 244  ? 8.237   11.561  121.509 1.00 26.51 ? 242  SER B N     1 
ATOM   10452 C CA    A SER B  1 244  ? 7.885   11.950  122.869 0.26 27.39 ? 242  SER B CA    1 
ATOM   10453 C CA    B SER B  1 244  ? 7.885   11.943  122.871 0.37 27.39 ? 242  SER B CA    1 
ATOM   10454 C CA    C SER B  1 244  ? 7.885   11.949  122.870 0.37 27.39 ? 242  SER B CA    1 
ATOM   10455 C C     . SER B  1 244  ? 6.373   11.988  123.058 1.00 27.30 ? 242  SER B C     1 
ATOM   10456 O O     . SER B  1 244  ? 5.855   11.548  124.090 1.00 28.00 ? 242  SER B O     1 
ATOM   10457 C CB    A SER B  1 244  ? 8.503   13.311  123.191 0.26 27.98 ? 242  SER B CB    1 
ATOM   10458 C CB    B SER B  1 244  ? 8.511   13.295  123.209 0.37 27.47 ? 242  SER B CB    1 
ATOM   10459 C CB    C SER B  1 244  ? 8.500   13.311  123.197 0.37 27.47 ? 242  SER B CB    1 
ATOM   10460 O OG    A SER B  1 244  ? 7.991   13.825  124.404 0.26 28.15 ? 242  SER B OG    1 
ATOM   10461 O OG    B SER B  1 244  ? 9.908   13.262  122.984 0.37 28.33 ? 242  SER B OG    1 
ATOM   10462 O OG    C SER B  1 244  ? 8.021   14.304  122.306 0.37 28.62 ? 242  SER B OG    1 
ATOM   10463 N N     . ALA B  1 245  ? 5.650   12.508  122.068 1.00 26.87 ? 243  ALA B N     1 
ATOM   10464 C CA    . ALA B  1 245  ? 4.198   12.586  122.179 1.00 29.17 ? 243  ALA B CA    1 
ATOM   10465 C C     . ALA B  1 245  ? 3.557   11.199  122.231 1.00 27.95 ? 243  ALA B C     1 
ATOM   10466 O O     . ALA B  1 245  ? 2.625   10.972  123.008 1.00 28.60 ? 243  ALA B O     1 
ATOM   10467 C CB    . ALA B  1 245  ? 3.629   13.396  121.013 1.00 29.74 ? 243  ALA B CB    1 
ATOM   10468 N N     . ILE B  1 246  ? 4.034   10.264  121.405 1.00 27.90 ? 244  ILE B N     1 
ATOM   10469 C CA    . ILE B  1 246  ? 3.484   8.909   121.424 1.00 28.63 ? 244  ILE B CA    1 
ATOM   10470 C C     . ILE B  1 246  ? 3.643   8.279   122.803 1.00 29.41 ? 244  ILE B C     1 
ATOM   10471 O O     . ILE B  1 246  ? 2.718   7.643   123.326 1.00 31.01 ? 244  ILE B O     1 
ATOM   10472 C CB    . ILE B  1 246  ? 4.136   8.045   120.329 1.00 28.45 ? 244  ILE B CB    1 
ATOM   10473 C CG1   . ILE B  1 246  ? 3.708   8.531   118.946 1.00 27.82 ? 244  ILE B CG1   1 
ATOM   10474 C CG2   . ILE B  1 246  ? 3.730   6.567   120.511 1.00 29.30 ? 244  ILE B CG2   1 
ATOM   10475 C CD1   . ILE B  1 246  ? 4.408   7.808   117.803 1.00 27.59 ? 244  ILE B CD1   1 
ATOM   10476 N N     . HIS B  1 247  ? 4.809   8.454   123.429 1.00 30.03 ? 245  HIS B N     1 
ATOM   10477 C CA    . HIS B  1 247  ? 4.979   7.909   124.771 1.00 30.04 ? 245  HIS B CA    1 
ATOM   10478 C C     . HIS B  1 247  ? 3.952   8.495   125.730 1.00 30.43 ? 245  HIS B C     1 
ATOM   10479 O O     . HIS B  1 247  ? 3.327   7.762   126.498 1.00 31.26 ? 245  HIS B O     1 
ATOM   10480 C CB    . HIS B  1 247  ? 6.403   8.151   125.283 1.00 31.33 ? 245  HIS B CB    1 
ATOM   10481 C CG    . HIS B  1 247  ? 7.416   7.243   124.665 1.00 31.00 ? 245  HIS B CG    1 
ATOM   10482 N ND1   . HIS B  1 247  ? 7.420   5.881   124.877 1.00 30.71 ? 245  HIS B ND1   1 
ATOM   10483 C CD2   . HIS B  1 247  ? 8.440   7.496   123.817 1.00 31.63 ? 245  HIS B CD2   1 
ATOM   10484 C CE1   . HIS B  1 247  ? 8.412   5.336   124.196 1.00 34.72 ? 245  HIS B CE1   1 
ATOM   10485 N NE2   . HIS B  1 247  ? 9.050   6.295   123.549 1.00 34.76 ? 245  HIS B NE2   1 
ATOM   10486 N N     . ALA B  1 248  ? 3.764   9.815   125.691 1.00 29.89 ? 246  ALA B N     1 
ATOM   10487 C CA    . ALA B  1 248  ? 2.815   10.463  126.590 1.00 30.27 ? 246  ALA B CA    1 
ATOM   10488 C C     . ALA B  1 248  ? 1.387   10.016  126.302 1.00 30.74 ? 246  ALA B C     1 
ATOM   10489 O O     . ALA B  1 248  ? 0.642   9.650   127.217 1.00 31.53 ? 246  ALA B O     1 
ATOM   10490 C CB    . ALA B  1 248  ? 2.928   11.986  126.470 1.00 29.57 ? 246  ALA B CB    1 
ATOM   10491 N N     . ILE B  1 249  ? 0.977   10.078  125.032 1.00 30.29 ? 247  ILE B N     1 
ATOM   10492 C CA    . ILE B  1 249  ? -0.376  9.668   124.673 1.00 32.30 ? 247  ILE B CA    1 
ATOM   10493 C C     . ILE B  1 249  ? -0.572  8.194   124.984 1.00 31.69 ? 247  ILE B C     1 
ATOM   10494 O O     . ILE B  1 249  ? -1.577  7.795   125.584 1.00 32.35 ? 247  ILE B O     1 
ATOM   10495 C CB    . ILE B  1 249  ? -0.647  9.985   123.191 1.00 30.05 ? 247  ILE B CB    1 
ATOM   10496 C CG1   . ILE B  1 249  ? -0.490  11.487  122.951 1.00 29.28 ? 247  ILE B CG1   1 
ATOM   10497 C CG2   . ILE B  1 249  ? -2.038  9.497   122.769 1.00 30.54 ? 247  ILE B CG2   1 
ATOM   10498 C CD1   . ILE B  1 249  ? -0.157  11.841  121.525 1.00 28.45 ? 247  ILE B CD1   1 
ATOM   10499 N N     . GLY B  1 250  ? 0.410   7.369   124.612 1.00 33.00 ? 248  GLY B N     1 
ATOM   10500 C CA    . GLY B  1 250  ? 0.328   5.945   124.895 1.00 32.30 ? 248  GLY B CA    1 
ATOM   10501 C C     . GLY B  1 250  ? 0.130   5.646   126.365 1.00 35.23 ? 248  GLY B C     1 
ATOM   10502 O O     . GLY B  1 250  ? -0.723  4.835   126.738 1.00 36.58 ? 248  GLY B O     1 
ATOM   10503 N N     . LYS B  1 251  ? 0.917   6.298   127.230 1.00 34.32 ? 249  LYS B N     1 
ATOM   10504 C CA    . LYS B  1 251  ? 0.740   6.071   128.661 1.00 33.78 ? 249  LYS B CA    1 
ATOM   10505 C C     . LYS B  1 251  ? -0.618  6.584   129.132 1.00 34.20 ? 249  LYS B C     1 
ATOM   10506 O O     . LYS B  1 251  ? -1.287  5.929   129.937 1.00 35.13 ? 249  LYS B O     1 
ATOM   10507 C CB    . LYS B  1 251  ? 1.883   6.721   129.455 1.00 33.48 ? 249  LYS B CB    1 
ATOM   10508 N N     . ALA B  1 252  ? -1.055  7.737   128.620 1.00 33.58 ? 250  ALA B N     1 
ATOM   10509 C CA    . ALA B  1 252  ? -2.360  8.280   128.991 1.00 35.25 ? 250  ALA B CA    1 
ATOM   10510 C C     . ALA B  1 252  ? -3.501  7.418   128.460 1.00 38.95 ? 250  ALA B C     1 
ATOM   10511 O O     . ALA B  1 252  ? -4.549  7.302   129.103 1.00 38.96 ? 250  ALA B O     1 
ATOM   10512 C CB    . ALA B  1 252  ? -2.508  9.704   128.460 1.00 35.02 ? 250  ALA B CB    1 
ATOM   10513 N N     . SER B  1 253  ? -3.329  6.836   127.271 1.00 37.66 ? 251  SER B N     1 
ATOM   10514 C CA    . SER B  1 253  ? -4.345  5.943   126.724 1.00 35.23 ? 251  SER B CA    1 
ATOM   10515 C C     . SER B  1 253  ? -4.673  4.825   127.705 1.00 39.74 ? 251  SER B C     1 
ATOM   10516 O O     . SER B  1 253  ? -5.837  4.439   127.852 1.00 41.90 ? 251  SER B O     1 
ATOM   10517 C CB    . SER B  1 253  ? -3.870  5.365   125.394 1.00 36.47 ? 251  SER B CB    1 
ATOM   10518 O OG    . SER B  1 253  ? -4.850  4.504   124.840 1.00 39.18 ? 251  SER B OG    1 
ATOM   10519 N N     . ALA B  1 254  ? -3.653  4.298   128.384 1.00 39.20 ? 252  ALA B N     1 
ATOM   10520 C CA    . ALA B  1 254  ? -3.813  3.308   129.453 1.00 39.37 ? 252  ALA B CA    1 
ATOM   10521 C C     . ALA B  1 254  ? -4.616  2.097   128.986 1.00 43.32 ? 252  ALA B C     1 
ATOM   10522 O O     . ALA B  1 254  ? -5.423  1.534   129.731 1.00 41.00 ? 252  ALA B O     1 
ATOM   10523 C CB    . ALA B  1 254  ? -4.446  3.933   130.699 1.00 39.90 ? 252  ALA B CB    1 
ATOM   10524 N N     . GLY B  1 255  ? -4.388  1.691   127.737 1.00 41.22 ? 253  GLY B N     1 
ATOM   10525 C CA    . GLY B  1 255  ? -4.997  0.479   127.226 1.00 42.39 ? 253  GLY B CA    1 
ATOM   10526 C C     . GLY B  1 255  ? -6.424  0.615   126.751 1.00 45.06 ? 253  GLY B C     1 
ATOM   10527 O O     . GLY B  1 255  ? -7.109  -0.401  126.597 1.00 48.32 ? 253  GLY B O     1 
ATOM   10528 N N     . ARG B  1 256  ? -6.900  1.837   126.507 1.00 41.62 ? 254  ARG B N     1 
ATOM   10529 C CA    . ARG B  1 256  ? -8.268  2.013   126.035 1.00 44.03 ? 254  ARG B CA    1 
ATOM   10530 C C     . ARG B  1 256  ? -8.444  1.585   124.585 1.00 45.30 ? 254  ARG B C     1 
ATOM   10531 O O     . ARG B  1 256  ? -9.584  1.503   124.117 1.00 42.89 ? 254  ARG B O     1 
ATOM   10532 C CB    . ARG B  1 256  ? -8.712  3.471   126.218 1.00 42.20 ? 254  ARG B CB    1 
ATOM   10533 C CG    . ARG B  1 256  ? -9.184  3.798   127.642 1.00 46.00 ? 254  ARG B CG    1 
ATOM   10534 C CD    . ARG B  1 256  ? -9.486  5.282   127.802 1.00 45.54 ? 254  ARG B CD    1 
ATOM   10535 N NE    . ARG B  1 256  ? -8.257  6.062   127.873 1.00 46.53 ? 254  ARG B NE    1 
ATOM   10536 C CZ    . ARG B  1 256  ? -8.167  7.367   127.646 1.00 44.32 ? 254  ARG B CZ    1 
ATOM   10537 N NH1   . ARG B  1 256  ? -9.224  8.087   127.315 1.00 40.30 ? 254  ARG B NH1   1 
ATOM   10538 N NH2   . ARG B  1 256  ? -6.981  7.962   127.745 1.00 45.91 ? 254  ARG B NH2   1 
ATOM   10539 N N     . GLY B  1 257  ? -7.354  1.294   123.874 1.00 43.17 ? 255  GLY B N     1 
ATOM   10540 C CA    . GLY B  1 257  ? -7.438  0.834   122.505 1.00 37.68 ? 255  GLY B CA    1 
ATOM   10541 C C     . GLY B  1 257  ? -7.546  1.975   121.519 1.00 38.88 ? 255  GLY B C     1 
ATOM   10542 O O     . GLY B  1 257  ? -7.623  3.156   121.867 1.00 39.59 ? 255  GLY B O     1 
ATOM   10543 N N     . ILE B  1 258  ? -7.580  1.601   120.240 1.00 37.30 ? 256  ILE B N     1 
ATOM   10544 C CA    . ILE B  1 258  ? -7.470  2.598   119.183 1.00 39.95 ? 256  ILE B CA    1 
ATOM   10545 C C     . ILE B  1 258  ? -8.767  3.357   118.918 1.00 38.16 ? 256  ILE B C     1 
ATOM   10546 O O     . ILE B  1 258  ? -8.723  4.405   118.261 1.00 33.69 ? 256  ILE B O     1 
ATOM   10547 C CB    . ILE B  1 258  ? -6.992  1.938   117.879 1.00 38.04 ? 256  ILE B CB    1 
ATOM   10548 C CG1   . ILE B  1 258  ? -7.944  0.822   117.468 1.00 40.84 ? 256  ILE B CG1   1 
ATOM   10549 C CG2   . ILE B  1 258  ? -5.579  1.397   118.023 1.00 38.02 ? 256  ILE B CG2   1 
ATOM   10550 C CD1   . ILE B  1 258  ? -7.517  0.101   116.224 1.00 42.15 ? 256  ILE B CD1   1 
ATOM   10551 N N     . TYR B  1 259  ? -9.920  2.870   119.399 1.00 39.50 ? 257  TYR B N     1 
ATOM   10552 C CA    . TYR B  1 259  ? -11.197 3.534   119.119 1.00 42.80 ? 257  TYR B CA    1 
ATOM   10553 C C     . TYR B  1 259  ? -11.672 4.424   120.259 1.00 39.46 ? 257  TYR B C     1 
ATOM   10554 O O     . TYR B  1 259  ? -12.152 5.533   120.012 1.00 46.80 ? 257  TYR B O     1 
ATOM   10555 C CB    . TYR B  1 259  ? -12.288 2.503   118.777 1.00 39.54 ? 257  TYR B CB    1 
ATOM   10556 C CG    . TYR B  1 259  ? -11.863 1.568   117.666 1.00 41.94 ? 257  TYR B CG    1 
ATOM   10557 C CD1   . TYR B  1 259  ? -11.630 2.046   116.383 1.00 39.47 ? 257  TYR B CD1   1 
ATOM   10558 C CD2   . TYR B  1 259  ? -11.667 0.217   117.906 1.00 43.95 ? 257  TYR B CD2   1 
ATOM   10559 C CE1   . TYR B  1 259  ? -11.211 1.201   115.366 1.00 41.36 ? 257  TYR B CE1   1 
ATOM   10560 C CE2   . TYR B  1 259  ? -11.256 -0.638  116.893 1.00 40.65 ? 257  TYR B CE2   1 
ATOM   10561 C CZ    . TYR B  1 259  ? -11.027 -0.138  115.629 1.00 41.93 ? 257  TYR B CZ    1 
ATOM   10562 O OH    . TYR B  1 259  ? -10.605 -0.985  114.632 1.00 42.36 ? 257  TYR B OH    1 
ATOM   10563 N N     . GLU B  1 260  ? -11.562 3.970   121.502 1.00 40.33 ? 258  GLU B N     1 
ATOM   10564 C CA    . GLU B  1 260  ? -11.930 4.805   122.635 1.00 42.33 ? 258  GLU B CA    1 
ATOM   10565 C C     . GLU B  1 260  ? -10.775 5.678   123.112 1.00 46.10 ? 258  GLU B C     1 
ATOM   10566 O O     . GLU B  1 260  ? -11.011 6.780   123.623 1.00 46.99 ? 258  GLU B O     1 
ATOM   10567 C CB    . GLU B  1 260  ? -12.434 3.930   123.790 1.00 44.02 ? 258  GLU B CB    1 
ATOM   10568 N N     . GLY B  1 261  ? -9.534  5.227   122.935 1.00 41.44 ? 259  GLY B N     1 
ATOM   10569 C CA    . GLY B  1 261  ? -8.388  5.954   123.433 1.00 41.86 ? 259  GLY B CA    1 
ATOM   10570 C C     . GLY B  1 261  ? -7.845  6.958   122.437 1.00 39.40 ? 259  GLY B C     1 
ATOM   10571 O O     . GLY B  1 261  ? -8.185  6.934   121.251 1.00 35.78 ? 259  GLY B O     1 
ATOM   10572 N N     . PRO B  1 262  ? -6.966  7.843   122.905 1.00 35.13 ? 260  PRO B N     1 
ATOM   10573 C CA    . PRO B  1 262  ? -6.415  8.888   122.038 1.00 33.16 ? 260  PRO B CA    1 
ATOM   10574 C C     . PRO B  1 262  ? -5.420  8.334   121.032 1.00 32.35 ? 260  PRO B C     1 
ATOM   10575 O O     . PRO B  1 262  ? -4.860  7.249   121.193 1.00 35.41 ? 260  PRO B O     1 
ATOM   10576 C CB    . PRO B  1 262  ? -5.718  9.827   123.028 1.00 34.03 ? 260  PRO B CB    1 
ATOM   10577 C CG    . PRO B  1 262  ? -5.312  8.925   124.153 1.00 33.01 ? 260  PRO B CG    1 
ATOM   10578 C CD    . PRO B  1 262  ? -6.413  7.905   124.275 1.00 35.49 ? 260  PRO B CD    1 
ATOM   10579 N N     . GLY B  1 263  ? -5.198  9.117   119.979 1.00 30.69 ? 261  GLY B N     1 
ATOM   10580 C CA    . GLY B  1 263  ? -4.162  8.831   119.001 1.00 30.06 ? 261  GLY B CA    1 
ATOM   10581 C C     . GLY B  1 263  ? -3.312  10.030  118.616 1.00 29.08 ? 261  GLY B C     1 
ATOM   10582 O O     . GLY B  1 263  ? -3.432  11.108  119.207 1.00 29.32 ? 261  GLY B O     1 
ATOM   10583 N N     . ILE B  1 264  ? -2.447  9.859   117.620 1.00 28.56 ? 262  ILE B N     1 
ATOM   10584 C CA    . ILE B  1 264  ? -1.588  10.929  117.135 1.00 27.59 ? 262  ILE B CA    1 
ATOM   10585 C C     . ILE B  1 264  ? -1.758  11.059  115.630 1.00 27.83 ? 262  ILE B C     1 
ATOM   10586 O O     . ILE B  1 264  ? -2.059  10.081  114.939 1.00 27.32 ? 262  ILE B O     1 
ATOM   10587 C CB    . ILE B  1 264  ? -0.110  10.668  117.494 1.00 32.44 ? 262  ILE B CB    1 
ATOM   10588 C CG1   . ILE B  1 264  ? 0.743   11.917  117.258 1.00 29.90 ? 262  ILE B CG1   1 
ATOM   10589 C CG2   . ILE B  1 264  ? 0.438   9.479   116.701 1.00 27.85 ? 262  ILE B CG2   1 
ATOM   10590 C CD1   . ILE B  1 264  ? 2.112   11.817  117.916 1.00 28.71 ? 262  ILE B CD1   1 
ATOM   10591 N N     . SER B  1 265  ? -1.590  12.284  115.126 1.00 27.73 ? 263  SER B N     1 
ATOM   10592 C CA    . SER B  1 265  ? -1.549  12.564  113.697 1.00 26.14 ? 263  SER B CA    1 
ATOM   10593 C C     . SER B  1 265  ? -0.174  13.106  113.331 1.00 28.40 ? 263  SER B C     1 
ATOM   10594 O O     . SER B  1 265  ? 0.416   13.888  114.084 1.00 29.66 ? 263  SER B O     1 
ATOM   10595 C CB    . SER B  1 265  ? -2.626  13.575  113.284 1.00 30.80 ? 263  SER B CB    1 
ATOM   10596 O OG    . SER B  1 265  ? -3.917  13.002  113.329 1.00 31.08 ? 263  SER B OG    1 
ATOM   10597 N N     . ILE B  1 266  ? 0.348   12.676  112.186 1.00 24.65 ? 264  ILE B N     1 
ATOM   10598 C CA    . ILE B  1 266  ? 1.644   13.142  111.712 1.00 26.76 ? 264  ILE B CA    1 
ATOM   10599 C C     . ILE B  1 266  ? 1.529   13.571  110.259 1.00 26.11 ? 264  ILE B C     1 
ATOM   10600 O O     . ILE B  1 266  ? 0.622   13.166  109.526 1.00 27.94 ? 264  ILE B O     1 
ATOM   10601 C CB    . ILE B  1 266  ? 2.750   12.075  111.843 1.00 25.53 ? 264  ILE B CB    1 
ATOM   10602 C CG1   . ILE B  1 266  ? 2.474   10.908  110.900 1.00 30.04 ? 264  ILE B CG1   1 
ATOM   10603 C CG2   . ILE B  1 266  ? 2.876   11.591  113.281 1.00 24.80 ? 264  ILE B CG2   1 
ATOM   10604 C CD1   . ILE B  1 266  ? 3.584   9.879   110.869 1.00 35.65 ? 264  ILE B CD1   1 
ATOM   10605 N N     . LYS B  1 267  ? 2.490   14.383  109.842 1.00 24.40 ? 265  LYS B N     1 
ATOM   10606 C CA    . LYS B  1 267  ? 2.647   14.779  108.455 1.00 24.14 ? 265  LYS B CA    1 
ATOM   10607 C C     . LYS B  1 267  ? 3.966   14.223  107.944 1.00 22.89 ? 265  LYS B C     1 
ATOM   10608 O O     . LYS B  1 267  ? 5.014   14.422  108.573 1.00 22.97 ? 265  LYS B O     1 
ATOM   10609 C CB    . LYS B  1 267  ? 2.617   16.302  108.306 1.00 25.10 ? 265  LYS B CB    1 
ATOM   10610 C CG    . LYS B  1 267  ? 1.285   16.918  108.700 1.00 28.97 ? 265  LYS B CG    1 
ATOM   10611 C CD    . LYS B  1 267  ? 1.140   18.353  108.174 1.00 35.05 ? 265  LYS B CD    1 
ATOM   10612 C CE    . LYS B  1 267  ? -0.268  18.881  108.434 1.00 40.21 ? 265  LYS B CE    1 
ATOM   10613 N NZ    . LYS B  1 267  ? -0.754  18.456  109.791 1.00 40.07 ? 265  LYS B NZ    1 
ATOM   10614 N N     . LEU B  1 268  ? 3.917   13.538  106.801 1.00 22.10 ? 266  LEU B N     1 
ATOM   10615 C CA    . LEU B  1 268  ? 5.147   12.995  106.238 1.00 23.76 ? 266  LEU B CA    1 
ATOM   10616 C C     . LEU B  1 268  ? 6.157   14.091  105.897 1.00 23.21 ? 266  LEU B C     1 
ATOM   10617 O O     . LEU B  1 268  ? 7.367   13.872  106.024 1.00 23.26 ? 266  LEU B O     1 
ATOM   10618 C CB    . LEU B  1 268  ? 4.819   12.149  105.012 1.00 21.96 ? 266  LEU B CB    1 
ATOM   10619 C CG    . LEU B  1 268  ? 4.013   10.899  105.381 1.00 22.71 ? 266  LEU B CG    1 
ATOM   10620 C CD1   . LEU B  1 268  ? 3.784   9.995   104.183 1.00 23.44 ? 266  LEU B CD1   1 
ATOM   10621 C CD2   . LEU B  1 268  ? 4.688   10.133  106.510 1.00 23.68 ? 266  LEU B CD2   1 
ATOM   10622 N N     . SER B  1 269  ? 5.690   15.279  105.490 1.00 20.71 ? 267  SER B N     1 
ATOM   10623 C CA    . SER B  1 269  ? 6.609   16.351  105.139 1.00 20.10 ? 267  SER B CA    1 
ATOM   10624 C C     . SER B  1 269  ? 7.387   16.846  106.351 1.00 20.72 ? 267  SER B C     1 
ATOM   10625 O O     . SER B  1 269  ? 8.416   17.505  106.183 1.00 21.97 ? 267  SER B O     1 
ATOM   10626 C CB    . SER B  1 269  ? 5.856   17.517  104.486 1.00 24.39 ? 267  SER B CB    1 
ATOM   10627 O OG    . SER B  1 269  ? 4.981   18.158  105.401 1.00 21.63 ? 267  SER B OG    1 
ATOM   10628 N N     . ALA B  1 270  ? 6.924   16.523  107.557 1.00 20.57 ? 268  ALA B N     1 
ATOM   10629 C CA    . ALA B  1 270  ? 7.649   16.893  108.771 1.00 21.13 ? 268  ALA B CA    1 
ATOM   10630 C C     . ALA B  1 270  ? 8.861   16.008  109.028 1.00 22.68 ? 268  ALA B C     1 
ATOM   10631 O O     . ALA B  1 270  ? 9.772   16.428  109.753 1.00 22.17 ? 268  ALA B O     1 
ATOM   10632 C CB    . ALA B  1 270  ? 6.709   16.827  109.982 1.00 23.38 ? 268  ALA B CB    1 
ATOM   10633 N N     . LEU B  1 271  ? 8.892   14.803  108.451 1.00 22.01 ? 269  LEU B N     1 
ATOM   10634 C CA    . LEU B  1 271  ? 9.875   13.777  108.782 1.00 21.95 ? 269  LEU B CA    1 
ATOM   10635 C C     . LEU B  1 271  ? 11.032  13.697  107.797 1.00 24.85 ? 269  LEU B C     1 
ATOM   10636 O O     . LEU B  1 271  ? 11.965  12.921  108.029 1.00 24.98 ? 269  LEU B O     1 
ATOM   10637 C CB    . LEU B  1 271  ? 9.194   12.401  108.871 1.00 22.11 ? 269  LEU B CB    1 
ATOM   10638 C CG    . LEU B  1 271  ? 8.110   12.352  109.943 1.00 23.06 ? 269  LEU B CG    1 
ATOM   10639 C CD1   . LEU B  1 271  ? 7.409   11.007  109.962 1.00 28.13 ? 269  LEU B CD1   1 
ATOM   10640 C CD2   . LEU B  1 271  ? 8.769   12.642  111.310 1.00 25.09 ? 269  LEU B CD2   1 
ATOM   10641 N N     . HIS B  1 272  ? 10.998  14.466  106.707 1.00 20.61 ? 270  HIS B N     1 
ATOM   10642 C CA    . HIS B  1 272  ? 12.108  14.484  105.768 1.00 22.64 ? 270  HIS B CA    1 
ATOM   10643 C C     . HIS B  1 272  ? 12.098  15.811  105.032 1.00 23.11 ? 270  HIS B C     1 
ATOM   10644 O O     . HIS B  1 272  ? 11.012  16.300  104.690 1.00 23.89 ? 270  HIS B O     1 
ATOM   10645 C CB    . HIS B  1 272  ? 12.010  13.326  104.768 1.00 25.35 ? 270  HIS B CB    1 
ATOM   10646 C CG    . HIS B  1 272  ? 13.303  13.020  104.094 1.00 27.65 ? 270  HIS B CG    1 
ATOM   10647 N ND1   . HIS B  1 272  ? 13.794  13.779  103.055 1.00 25.15 ? 270  HIS B ND1   1 
ATOM   10648 C CD2   . HIS B  1 272  ? 14.229  12.062  104.335 1.00 27.19 ? 270  HIS B CD2   1 
ATOM   10649 C CE1   . HIS B  1 272  ? 14.961  13.291  102.673 1.00 29.91 ? 270  HIS B CE1   1 
ATOM   10650 N NE2   . HIS B  1 272  ? 15.245  12.246  103.431 1.00 32.76 ? 270  HIS B NE2   1 
ATOM   10651 N N     . PRO B  1 273  ? 13.259  16.427  104.782 1.00 21.47 ? 271  PRO B N     1 
ATOM   10652 C CA    . PRO B  1 273  ? 13.275  17.712  104.065 1.00 23.18 ? 271  PRO B CA    1 
ATOM   10653 C C     . PRO B  1 273  ? 13.034  17.604  102.566 1.00 24.75 ? 271  PRO B C     1 
ATOM   10654 O O     . PRO B  1 273  ? 12.824  18.645  101.930 1.00 23.52 ? 271  PRO B O     1 
ATOM   10655 C CB    . PRO B  1 273  ? 14.680  18.259  104.355 1.00 26.21 ? 271  PRO B CB    1 
ATOM   10656 C CG    . PRO B  1 273  ? 15.496  17.078  104.755 1.00 27.09 ? 271  PRO B CG    1 
ATOM   10657 C CD    . PRO B  1 273  ? 14.552  16.116  105.418 1.00 24.41 ? 271  PRO B CD    1 
ATOM   10658 N N     . ARG B  1 274  ? 13.074  16.399  101.982 1.00 23.37 ? 272  ARG B N     1 
ATOM   10659 C CA    . ARG B  1 274  ? 12.882  16.206  100.542 1.00 21.74 ? 272  ARG B CA    1 
ATOM   10660 C C     . ARG B  1 274  ? 11.777  15.173  100.306 1.00 24.93 ? 272  ARG B C     1 
ATOM   10661 O O     . ARG B  1 274  ? 11.941  14.174  99.605  1.00 25.87 ? 272  ARG B O     1 
ATOM   10662 C CB    . ARG B  1 274  ? 14.184  15.782  99.848  1.00 23.29 ? 272  ARG B CB    1 
ATOM   10663 C CG    . ARG B  1 274  ? 15.329  16.808  99.950  1.00 24.13 ? 272  ARG B CG    1 
ATOM   10664 C CD    . ARG B  1 274  ? 14.933  18.204  99.422  1.00 24.10 ? 272  ARG B CD    1 
ATOM   10665 N NE    . ARG B  1 274  ? 14.434  18.151  98.053  1.00 21.50 ? 272  ARG B NE    1 
ATOM   10666 C CZ    . ARG B  1 274  ? 15.198  17.985  96.978  1.00 24.23 ? 272  ARG B CZ    1 
ATOM   10667 N NH1   . ARG B  1 274  ? 16.515  17.867  97.071  1.00 23.62 ? 272  ARG B NH1   1 
ATOM   10668 N NH2   . ARG B  1 274  ? 14.628  17.942  95.780  1.00 21.75 ? 272  ARG B NH2   1 
ATOM   10669 N N     . TYR B  1 275  ? 10.619  15.430  100.891 1.00 21.57 ? 273  TYR B N     1 
ATOM   10670 C CA    . TYR B  1 275  ? 9.467   14.557  100.705 1.00 23.63 ? 273  TYR B CA    1 
ATOM   10671 C C     . TYR B  1 275  ? 8.793   14.887  99.373  1.00 23.62 ? 273  TYR B C     1 
ATOM   10672 O O     . TYR B  1 275  ? 7.980   15.809  99.292  1.00 21.92 ? 273  TYR B O     1 
ATOM   10673 C CB    . TYR B  1 275  ? 8.506   14.719  101.872 1.00 24.36 ? 273  TYR B CB    1 
ATOM   10674 C CG    . TYR B  1 275  ? 7.254   13.917  101.701 1.00 21.25 ? 273  TYR B CG    1 
ATOM   10675 C CD1   . TYR B  1 275  ? 7.310   12.595  101.268 1.00 27.58 ? 273  TYR B CD1   1 
ATOM   10676 C CD2   . TYR B  1 275  ? 6.015   14.470  101.984 1.00 20.95 ? 273  TYR B CD2   1 
ATOM   10677 C CE1   . TYR B  1 275  ? 6.158   11.851  101.105 1.00 27.37 ? 273  TYR B CE1   1 
ATOM   10678 C CE2   . TYR B  1 275  ? 4.857   13.738  101.829 1.00 24.07 ? 273  TYR B CE2   1 
ATOM   10679 C CZ    . TYR B  1 275  ? 4.935   12.427  101.382 1.00 26.92 ? 273  TYR B CZ    1 
ATOM   10680 O OH    . TYR B  1 275  ? 3.795   11.691  101.230 1.00 23.58 ? 273  TYR B OH    1 
ATOM   10681 N N     . SER B  1 276  ? 9.129   14.134  98.324  1.00 20.30 ? 274  SER B N     1 
ATOM   10682 C CA    . SER B  1 276  ? 8.569   14.400  96.995  1.00 22.96 ? 274  SER B CA    1 
ATOM   10683 C C     . SER B  1 276  ? 8.832   13.208  96.083  1.00 22.32 ? 274  SER B C     1 
ATOM   10684 O O     . SER B  1 276  ? 9.756   12.427  96.307  1.00 21.18 ? 274  SER B O     1 
ATOM   10685 C CB    . SER B  1 276  ? 9.161   15.668  96.366  1.00 30.44 ? 274  SER B CB    1 
ATOM   10686 O OG    . SER B  1 276  ? 10.509  15.454  95.971  1.00 27.26 ? 274  SER B OG    1 
ATOM   10687 N N     . ARG B  1 277  ? 8.005   13.085  95.042  1.00 19.43 ? 275  ARG B N     1 
ATOM   10688 C CA    . ARG B  1 277  ? 8.185   12.003  94.075  1.00 22.70 ? 275  ARG B CA    1 
ATOM   10689 C C     . ARG B  1 277  ? 9.569   12.036  93.440  1.00 21.58 ? 275  ARG B C     1 
ATOM   10690 O O     . ARG B  1 277  ? 10.153  10.985  93.155  1.00 21.50 ? 275  ARG B O     1 
ATOM   10691 C CB    . ARG B  1 277  ? 7.113   12.083  92.987  1.00 21.31 ? 275  ARG B CB    1 
ATOM   10692 C CG    . ARG B  1 277  ? 7.310   11.091  91.845  1.00 23.55 ? 275  ARG B CG    1 
ATOM   10693 C CD    . ARG B  1 277  ? 7.210   9.654   92.313  1.00 22.23 ? 275  ARG B CD    1 
ATOM   10694 N NE    . ARG B  1 277  ? 7.406   8.733   91.200  1.00 22.61 ? 275  ARG B NE    1 
ATOM   10695 C CZ    . ARG B  1 277  ? 8.593   8.374   90.728  1.00 23.03 ? 275  ARG B CZ    1 
ATOM   10696 N NH1   . ARG B  1 277  ? 9.720   8.822   91.270  1.00 25.28 ? 275  ARG B NH1   1 
ATOM   10697 N NH2   . ARG B  1 277  ? 8.652   7.545   89.689  1.00 27.66 ? 275  ARG B NH2   1 
ATOM   10698 N N     . ALA B  1 278  ? 10.091  13.229  93.157  1.00 22.45 ? 276  ALA B N     1 
ATOM   10699 C CA    . ALA B  1 278  ? 11.402  13.298  92.520  1.00 23.89 ? 276  ALA B CA    1 
ATOM   10700 C C     . ALA B  1 278  ? 12.474  12.674  93.408  1.00 23.75 ? 276  ALA B C     1 
ATOM   10701 O O     . ALA B  1 278  ? 13.464  12.142  92.904  1.00 25.00 ? 276  ALA B O     1 
ATOM   10702 C CB    . ALA B  1 278  ? 11.766  14.744  92.176  1.00 24.10 ? 276  ALA B CB    1 
ATOM   10703 N N     . GLN B  1 279  ? 12.269  12.690  94.720  1.00 22.29 ? 277  GLN B N     1 
ATOM   10704 C CA    . GLN B  1 279  ? 13.220  12.129  95.678  1.00 20.74 ? 277  GLN B CA    1 
ATOM   10705 C C     . GLN B  1 279  ? 12.719  10.814  96.277  1.00 22.27 ? 277  GLN B C     1 
ATOM   10706 O O     . GLN B  1 279  ? 13.054  10.478  97.414  1.00 25.28 ? 277  GLN B O     1 
ATOM   10707 C CB    . GLN B  1 279  ? 13.515  13.154  96.774  1.00 24.84 ? 277  GLN B CB    1 
ATOM   10708 C CG    . GLN B  1 279  ? 14.097  14.466  96.244  1.00 27.11 ? 277  GLN B CG    1 
ATOM   10709 C CD    . GLN B  1 279  ? 15.452  14.268  95.573  1.00 29.99 ? 277  GLN B CD    1 
ATOM   10710 O OE1   . GLN B  1 279  ? 16.256  13.445  96.009  1.00 34.43 ? 277  GLN B OE1   1 
ATOM   10711 N NE2   . GLN B  1 279  ? 15.702  15.017  94.505  1.00 24.71 ? 277  GLN B NE2   1 
ATOM   10712 N N     . ALA B  1 280  ? 11.942  10.046  95.505  1.00 22.41 ? 278  ALA B N     1 
ATOM   10713 C CA    . ALA B  1 280  ? 11.287  8.850   96.039  1.00 23.62 ? 278  ALA B CA    1 
ATOM   10714 C C     . ALA B  1 280  ? 12.282  7.889   96.683  1.00 26.48 ? 278  ALA B C     1 
ATOM   10715 O O     . ALA B  1 280  ? 11.976  7.272   97.711  1.00 25.22 ? 278  ALA B O     1 
ATOM   10716 C CB    . ALA B  1 280  ? 10.514  8.132   94.927  1.00 23.30 ? 278  ALA B CB    1 
ATOM   10717 N N     . ALA B  1 281  ? 13.464  7.719   96.083  1.00 25.52 ? 279  ALA B N     1 
ATOM   10718 C CA    . ALA B  1 281  ? 14.430  6.778   96.653  1.00 29.45 ? 279  ALA B CA    1 
ATOM   10719 C C     . ALA B  1 281  ? 14.859  7.216   98.045  1.00 28.63 ? 279  ALA B C     1 
ATOM   10720 O O     . ALA B  1 281  ? 15.013  6.384   98.950  1.00 28.95 ? 279  ALA B O     1 
ATOM   10721 C CB    . ALA B  1 281  ? 15.649  6.629   95.739  1.00 32.02 ? 279  ALA B CB    1 
ATOM   10722 N N     . ARG B  1 282  ? 15.045  8.518   98.242  1.00 24.16 ? 280  ARG B N     1 
ATOM   10723 C CA    . ARG B  1 282  ? 15.358  8.999   99.584  1.00 26.73 ? 280  ARG B CA    1 
ATOM   10724 C C     . ARG B  1 282  ? 14.155  8.861   100.509 1.00 24.57 ? 280  ARG B C     1 
ATOM   10725 O O     . ARG B  1 282  ? 14.308  8.574   101.700 1.00 29.84 ? 280  ARG B O     1 
ATOM   10726 C CB    . ARG B  1 282  ? 15.835  10.450  99.527  1.00 28.65 ? 280  ARG B CB    1 
ATOM   10727 C CG    . ARG B  1 282  ? 17.195  10.644  98.865  1.00 28.08 ? 280  ARG B CG    1 
ATOM   10728 C CD    . ARG B  1 282  ? 17.734  12.029  99.179  1.00 27.88 ? 280  ARG B CD    1 
ATOM   10729 N NE    . ARG B  1 282  ? 18.043  12.167  100.599 1.00 27.86 ? 280  ARG B NE    1 
ATOM   10730 C CZ    . ARG B  1 282  ? 18.190  13.329  101.219 1.00 30.66 ? 280  ARG B CZ    1 
ATOM   10731 N NH1   . ARG B  1 282  ? 18.084  14.476  100.564 1.00 28.08 ? 280  ARG B NH1   1 
ATOM   10732 N NH2   . ARG B  1 282  ? 18.453  13.340  102.526 1.00 30.36 ? 280  ARG B NH2   1 
ATOM   10733 N N     . VAL B  1 283  ? 12.950  9.067   99.980  1.00 24.89 ? 281  VAL B N     1 
ATOM   10734 C CA    . VAL B  1 283  ? 11.746  8.932   100.794 1.00 21.75 ? 281  VAL B CA    1 
ATOM   10735 C C     . VAL B  1 283  ? 11.624  7.506   101.311 1.00 23.37 ? 281  VAL B C     1 
ATOM   10736 O O     . VAL B  1 283  ? 11.473  7.273   102.512 1.00 27.52 ? 281  VAL B O     1 
ATOM   10737 C CB    . VAL B  1 283  ? 10.500  9.343   99.985  1.00 22.58 ? 281  VAL B CB    1 
ATOM   10738 C CG1   . VAL B  1 283  ? 9.232   9.018   100.781 1.00 21.90 ? 281  VAL B CG1   1 
ATOM   10739 C CG2   . VAL B  1 283  ? 10.559  10.837  99.647  1.00 25.16 ? 281  VAL B CG2   1 
ATOM   10740 N N     . MET B  1 284  ? 11.733  6.529   100.408 1.00 22.85 ? 282  MET B N     1 
ATOM   10741 C CA    . MET B  1 284  ? 11.617  5.130   100.817 1.00 23.63 ? 282  MET B CA    1 
ATOM   10742 C C     . MET B  1 284  ? 12.753  4.710   101.752 1.00 28.43 ? 282  MET B C     1 
ATOM   10743 O O     . MET B  1 284  ? 12.535  3.937   102.695 1.00 27.93 ? 282  MET B O     1 
ATOM   10744 C CB    . MET B  1 284  ? 11.587  4.242   99.584  1.00 24.98 ? 282  MET B CB    1 
ATOM   10745 C CG    . MET B  1 284  ? 10.396  4.525   98.673  1.00 25.09 ? 282  MET B CG    1 
ATOM   10746 S SD    . MET B  1 284  ? 8.847   4.449   99.592  1.00 31.28 ? 282  MET B SD    1 
ATOM   10747 C CE    . MET B  1 284  ? 8.706   2.688   99.844  1.00 29.15 ? 282  MET B CE    1 
ATOM   10748 N N     . GLY B  1 285  ? 13.976  5.196   101.500 1.00 26.52 ? 283  GLY B N     1 
ATOM   10749 C CA    . GLY B  1 285  ? 15.131  4.740   102.264 1.00 26.31 ? 283  GLY B CA    1 
ATOM   10750 C C     . GLY B  1 285  ? 15.356  5.468   103.569 1.00 31.71 ? 283  GLY B C     1 
ATOM   10751 O O     . GLY B  1 285  ? 15.977  4.908   104.481 1.00 31.75 ? 283  GLY B O     1 
ATOM   10752 N N     . GLU B  1 286  ? 14.856  6.696   103.693 1.00 27.97 ? 284  GLU B N     1 
ATOM   10753 C CA    . GLU B  1 286  ? 15.144  7.513   104.871 1.00 28.45 ? 284  GLU B CA    1 
ATOM   10754 C C     . GLU B  1 286  ? 13.901  7.936   105.634 1.00 28.26 ? 284  GLU B C     1 
ATOM   10755 O O     . GLU B  1 286  ? 13.898  7.910   106.867 1.00 29.23 ? 284  GLU B O     1 
ATOM   10756 C CB    . GLU B  1 286  ? 15.935  8.769   104.463 1.00 30.99 ? 284  GLU B CB    1 
ATOM   10757 C CG    . GLU B  1 286  ? 17.287  8.484   103.797 1.00 31.42 ? 284  GLU B CG    1 
ATOM   10758 C CD    . GLU B  1 286  ? 17.856  9.706   103.090 1.00 34.01 ? 284  GLU B CD    1 
ATOM   10759 O OE1   . GLU B  1 286  ? 17.597  10.838  103.552 1.00 31.79 ? 284  GLU B OE1   1 
ATOM   10760 O OE2   . GLU B  1 286  ? 18.553  9.537   102.064 1.00 35.43 ? 284  GLU B OE2   1 
ATOM   10761 N N     . LEU B  1 287  ? 12.850  8.350   104.930 1.00 29.85 ? 285  LEU B N     1 
ATOM   10762 C CA    . LEU B  1 287  ? 11.619  8.769   105.590 1.00 25.88 ? 285  LEU B CA    1 
ATOM   10763 C C     . LEU B  1 287  ? 10.838  7.568   106.109 1.00 27.63 ? 285  LEU B C     1 
ATOM   10764 O O     . LEU B  1 287  ? 10.409  7.558   107.266 1.00 27.08 ? 285  LEU B O     1 
ATOM   10765 C CB    . LEU B  1 287  ? 10.764  9.592   104.617 1.00 23.72 ? 285  LEU B CB    1 
ATOM   10766 C CG    . LEU B  1 287  ? 9.675   10.526  105.166 1.00 27.79 ? 285  LEU B CG    1 
ATOM   10767 C CD1   . LEU B  1 287  ? 9.105   11.403  104.046 1.00 22.78 ? 285  LEU B CD1   1 
ATOM   10768 C CD2   . LEU B  1 287  ? 8.534   9.775   105.838 1.00 25.85 ? 285  LEU B CD2   1 
ATOM   10769 N N     . LEU B  1 288  ? 10.631  6.549   105.263 1.00 27.75 ? 286  LEU B N     1 
ATOM   10770 C CA    . LEU B  1 288  ? 9.863   5.374   105.675 1.00 26.93 ? 286  LEU B CA    1 
ATOM   10771 C C     . LEU B  1 288  ? 10.355  4.738   106.973 1.00 28.23 ? 286  LEU B C     1 
ATOM   10772 O O     . LEU B  1 288  ? 9.515   4.446   107.840 1.00 26.87 ? 286  LEU B O     1 
ATOM   10773 C CB    . LEU B  1 288  ? 9.845   4.343   104.535 1.00 30.44 ? 286  LEU B CB    1 
ATOM   10774 C CG    . LEU B  1 288  ? 9.226   2.992   104.896 1.00 37.11 ? 286  LEU B CG    1 
ATOM   10775 C CD1   . LEU B  1 288  ? 7.769   3.153   105.340 1.00 30.23 ? 286  LEU B CD1   1 
ATOM   10776 C CD2   . LEU B  1 288  ? 9.350   2.022   103.731 1.00 38.86 ? 286  LEU B CD2   1 
ATOM   10777 N N     . PRO B  1 289  ? 11.656  4.495   107.184 1.00 31.34 ? 287  PRO B N     1 
ATOM   10778 C CA    . PRO B  1 289  ? 12.070  3.895   108.468 1.00 27.58 ? 287  PRO B CA    1 
ATOM   10779 C C     . PRO B  1 289  ? 11.707  4.738   109.676 1.00 28.85 ? 287  PRO B C     1 
ATOM   10780 O O     . PRO B  1 289  ? 11.513  4.192   110.770 1.00 30.07 ? 287  PRO B O     1 
ATOM   10781 C CB    . PRO B  1 289  ? 13.590  3.757   108.315 1.00 31.65 ? 287  PRO B CB    1 
ATOM   10782 C CG    . PRO B  1 289  ? 13.799  3.642   106.849 1.00 32.84 ? 287  PRO B CG    1 
ATOM   10783 C CD    . PRO B  1 289  ? 12.792  4.587   106.250 1.00 31.83 ? 287  PRO B CD    1 
ATOM   10784 N N     . ARG B  1 290  ? 11.620  6.059   109.520 1.00 27.58 ? 288  ARG B N     1 
ATOM   10785 C CA    . ARG B  1 290  ? 11.166  6.892   110.627 1.00 27.67 ? 288  ARG B CA    1 
ATOM   10786 C C     . ARG B  1 290  ? 9.683   6.690   110.915 1.00 27.46 ? 288  ARG B C     1 
ATOM   10787 O O     . ARG B  1 290  ? 9.294   6.576   112.080 1.00 28.62 ? 288  ARG B O     1 
ATOM   10788 C CB    . ARG B  1 290  ? 11.479  8.360   110.342 1.00 26.80 ? 288  ARG B CB    1 
ATOM   10789 C CG    . ARG B  1 290  ? 12.963  8.638   110.458 1.00 33.63 ? 288  ARG B CG    1 
ATOM   10790 C CD    . ARG B  1 290  ? 13.340  9.877   109.694 1.00 34.11 ? 288  ARG B CD    1 
ATOM   10791 N NE    . ARG B  1 290  ? 14.459  10.563  110.325 1.00 38.00 ? 288  ARG B NE    1 
ATOM   10792 C CZ    . ARG B  1 290  ? 14.934  11.737  109.933 1.00 35.06 ? 288  ARG B CZ    1 
ATOM   10793 N NH1   . ARG B  1 290  ? 14.423  12.377  108.890 1.00 37.05 ? 288  ARG B NH1   1 
ATOM   10794 N NH2   . ARG B  1 290  ? 15.933  12.288  110.612 1.00 34.51 ? 288  ARG B NH2   1 
ATOM   10795 N N     . VAL B  1 291  ? 8.833   6.637   109.879 1.00 25.21 ? 289  VAL B N     1 
ATOM   10796 C CA    . VAL B  1 291  ? 7.417   6.365   110.126 1.00 25.38 ? 289  VAL B CA    1 
ATOM   10797 C C     . VAL B  1 291  ? 7.248   4.984   110.748 1.00 27.77 ? 289  VAL B C     1 
ATOM   10798 O O     . VAL B  1 291  ? 6.415   4.783   111.642 1.00 28.10 ? 289  VAL B O     1 
ATOM   10799 C CB    . VAL B  1 291  ? 6.595   6.484   108.826 1.00 25.12 ? 289  VAL B CB    1 
ATOM   10800 C CG1   . VAL B  1 291  ? 5.108   6.348   109.134 1.00 26.06 ? 289  VAL B CG1   1 
ATOM   10801 C CG2   . VAL B  1 291  ? 6.865   7.787   108.149 1.00 30.03 ? 289  VAL B CG2   1 
ATOM   10802 N N     . LYS B  1 292  ? 8.020   4.008   110.271 1.00 29.00 ? 290  LYS B N     1 
ATOM   10803 C CA    . LYS B  1 292  ? 7.917   2.654   110.810 1.00 27.42 ? 290  LYS B CA    1 
ATOM   10804 C C     . LYS B  1 292  ? 8.241   2.640   112.298 1.00 29.43 ? 290  LYS B C     1 
ATOM   10805 O O     . LYS B  1 292  ? 7.542   1.995   113.092 1.00 30.58 ? 290  LYS B O     1 
ATOM   10806 C CB    . LYS B  1 292  ? 8.844   1.728   110.018 1.00 33.71 ? 290  LYS B CB    1 
ATOM   10807 C CG    . LYS B  1 292  ? 9.327   0.486   110.737 1.00 37.81 ? 290  LYS B CG    1 
ATOM   10808 C CD    . LYS B  1 292  ? 8.223   -0.514  110.926 1.00 36.71 ? 290  LYS B CD    1 
ATOM   10809 C CE    . LYS B  1 292  ? 8.758   -1.775  111.626 1.00 42.74 ? 290  LYS B CE    1 
ATOM   10810 N NZ    . LYS B  1 292  ? 9.751   -2.519  110.779 1.00 41.93 ? 290  LYS B NZ    1 
ATOM   10811 N N     . ALA B  1 293  ? 9.281   3.370   112.694 1.00 30.46 ? 291  ALA B N     1 
ATOM   10812 C CA    . ALA B  1 293  ? 9.668   3.403   114.099 1.00 34.52 ? 291  ALA B CA    1 
ATOM   10813 C C     . ALA B  1 293  ? 8.580   4.046   114.947 1.00 30.03 ? 291  ALA B C     1 
ATOM   10814 O O     . ALA B  1 293  ? 8.289   3.580   116.055 1.00 32.85 ? 291  ALA B O     1 
ATOM   10815 C CB    . ALA B  1 293  ? 10.991  4.148   114.254 1.00 29.52 ? 291  ALA B CB    1 
ATOM   10816 N N     . LEU B  1 294  ? 7.951   5.101   114.431 1.00 31.59 ? 292  LEU B N     1 
ATOM   10817 C CA    . LEU B  1 294  ? 6.861   5.749   115.155 1.00 28.16 ? 292  LEU B CA    1 
ATOM   10818 C C     . LEU B  1 294  ? 5.642   4.845   115.233 1.00 29.80 ? 292  LEU B C     1 
ATOM   10819 O O     . LEU B  1 294  ? 4.959   4.808   116.259 1.00 28.41 ? 292  LEU B O     1 
ATOM   10820 C CB    . LEU B  1 294  ? 6.488   7.079   114.482 1.00 26.42 ? 292  LEU B CB    1 
ATOM   10821 C CG    . LEU B  1 294  ? 7.533   8.205   114.488 1.00 25.71 ? 292  LEU B CG    1 
ATOM   10822 C CD1   . LEU B  1 294  ? 7.060   9.420   113.685 1.00 25.00 ? 292  LEU B CD1   1 
ATOM   10823 C CD2   . LEU B  1 294  ? 7.896   8.614   115.906 1.00 25.90 ? 292  LEU B CD2   1 
ATOM   10824 N N     . ALA B  1 295  ? 5.331   4.135   114.141 1.00 28.02 ? 293  ALA B N     1 
ATOM   10825 C CA    . ALA B  1 295  ? 4.198   3.219   114.155 1.00 30.70 ? 293  ALA B CA    1 
ATOM   10826 C C     . ALA B  1 295  ? 4.452   2.040   115.083 1.00 30.31 ? 293  ALA B C     1 
ATOM   10827 O O     . ALA B  1 295  ? 3.519   1.552   115.736 1.00 31.73 ? 293  ALA B O     1 
ATOM   10828 C CB    . ALA B  1 295  ? 3.889   2.749   112.726 1.00 28.64 ? 293  ALA B CB    1 
ATOM   10829 N N     . LEU B  1 296  ? 5.711   1.602   115.194 1.00 32.00 ? 294  LEU B N     1 
ATOM   10830 C CA    . LEU B  1 296  ? 6.051   0.554   116.156 1.00 30.46 ? 294  LEU B CA    1 
ATOM   10831 C C     . LEU B  1 296  ? 5.761   0.993   117.587 1.00 34.89 ? 294  LEU B C     1 
ATOM   10832 O O     . LEU B  1 296  ? 5.270   0.198   118.400 1.00 36.08 ? 294  LEU B O     1 
ATOM   10833 C CB    . LEU B  1 296  ? 7.520   0.161   116.010 1.00 36.21 ? 294  LEU B CB    1 
ATOM   10834 C CG    . LEU B  1 296  ? 7.896   -1.200  116.603 1.00 41.23 ? 294  LEU B CG    1 
ATOM   10835 C CD1   . LEU B  1 296  ? 7.210   -2.309  115.813 1.00 45.89 ? 294  LEU B CD1   1 
ATOM   10836 C CD2   . LEU B  1 296  ? 9.402   -1.397  116.606 1.00 45.86 ? 294  LEU B CD2   1 
ATOM   10837 N N     . LEU B  1 297  ? 6.072   2.249   117.925 1.00 30.49 ? 295  LEU B N     1 
ATOM   10838 C CA    . LEU B  1 297  ? 5.722   2.750   119.256 1.00 30.56 ? 295  LEU B CA    1 
ATOM   10839 C C     . LEU B  1 297  ? 4.211   2.843   119.426 1.00 32.51 ? 295  LEU B C     1 
ATOM   10840 O O     . LEU B  1 297  ? 3.675   2.501   120.484 1.00 31.79 ? 295  LEU B O     1 
ATOM   10841 C CB    . LEU B  1 297  ? 6.359   4.116   119.499 1.00 29.57 ? 295  LEU B CB    1 
ATOM   10842 C CG    . LEU B  1 297  ? 7.875   4.178   119.641 1.00 35.38 ? 295  LEU B CG    1 
ATOM   10843 C CD1   . LEU B  1 297  ? 8.313   5.625   119.812 1.00 37.58 ? 295  LEU B CD1   1 
ATOM   10844 C CD2   . LEU B  1 297  ? 8.328   3.353   120.828 1.00 35.44 ? 295  LEU B CD2   1 
ATOM   10845 N N     . ALA B  1 298  ? 3.503   3.308   118.396 1.00 30.80 ? 296  ALA B N     1 
ATOM   10846 C CA    . ALA B  1 298  ? 2.049   3.397   118.494 1.00 30.60 ? 296  ALA B CA    1 
ATOM   10847 C C     . ALA B  1 298  ? 1.430   2.023   118.700 1.00 31.59 ? 296  ALA B C     1 
ATOM   10848 O O     . ALA B  1 298  ? 0.480   1.874   119.474 1.00 32.58 ? 296  ALA B O     1 
ATOM   10849 C CB    . ALA B  1 298  ? 1.475   4.060   117.239 1.00 29.97 ? 296  ALA B CB    1 
ATOM   10850 N N     . LYS B  1 299  ? 1.957   1.010   118.010 1.00 32.68 ? 297  LYS B N     1 
ATOM   10851 C CA    . LYS B  1 299  ? 1.471   -0.355  118.199 1.00 35.44 ? 297  LYS B CA    1 
ATOM   10852 C C     . LYS B  1 299  ? 1.727   -0.844  119.621 1.00 33.48 ? 297  LYS B C     1 
ATOM   10853 O O     . LYS B  1 299  ? 0.873   -1.504  120.225 1.00 35.69 ? 297  LYS B O     1 
ATOM   10854 C CB    . LYS B  1 299  ? 2.137   -1.289  117.185 1.00 34.56 ? 297  LYS B CB    1 
ATOM   10855 C CG    . LYS B  1 299  ? 1.984   -2.756  117.542 1.00 40.64 ? 297  LYS B CG    1 
ATOM   10856 C CD    . LYS B  1 299  ? 2.959   -3.639  116.793 1.00 44.34 ? 297  LYS B CD    1 
ATOM   10857 C CE    . LYS B  1 299  ? 2.839   -5.082  117.286 1.00 51.97 ? 297  LYS B CE    1 
ATOM   10858 N NZ    . LYS B  1 299  ? 3.852   -5.988  116.666 1.00 55.04 ? 297  LYS B NZ    1 
ATOM   10859 N N     . ASN B  1 300  ? 2.900   -0.540  120.172 1.00 34.93 ? 298  ASN B N     1 
ATOM   10860 C CA    . ASN B  1 300  ? 3.216   -1.047  121.504 1.00 33.90 ? 298  ASN B CA    1 
ATOM   10861 C C     . ASN B  1 300  ? 2.274   -0.479  122.553 1.00 34.22 ? 298  ASN B C     1 
ATOM   10862 O O     . ASN B  1 300  ? 1.978   -1.147  123.548 1.00 37.84 ? 298  ASN B O     1 
ATOM   10863 C CB    . ASN B  1 300  ? 4.667   -0.731  121.852 1.00 41.99 ? 298  ASN B CB    1 
ATOM   10864 C CG    . ASN B  1 300  ? 5.640   -1.479  120.971 1.00 46.05 ? 298  ASN B CG    1 
ATOM   10865 O OD1   . ASN B  1 300  ? 5.315   -2.546  120.440 1.00 48.34 ? 298  ASN B OD1   1 
ATOM   10866 N ND2   . ASN B  1 300  ? 6.838   -0.926  120.803 1.00 45.31 ? 298  ASN B ND2   1 
ATOM   10867 N N     . TYR B  1 301  ? 1.803   0.749   122.356 1.00 33.56 ? 299  TYR B N     1 
ATOM   10868 C CA    . TYR B  1 301  ? 0.808   1.352   123.230 1.00 33.86 ? 299  TYR B CA    1 
ATOM   10869 C C     . TYR B  1 301  ? -0.620  1.107   122.757 1.00 34.25 ? 299  TYR B C     1 
ATOM   10870 O O     . TYR B  1 301  ? -1.569  1.441   123.479 1.00 34.92 ? 299  TYR B O     1 
ATOM   10871 C CB    . TYR B  1 301  ? 1.059   2.859   123.340 1.00 33.01 ? 299  TYR B CB    1 
ATOM   10872 C CG    . TYR B  1 301  ? 2.324   3.219   124.117 1.00 32.77 ? 299  TYR B CG    1 
ATOM   10873 C CD1   . TYR B  1 301  ? 2.384   3.055   125.488 1.00 37.29 ? 299  TYR B CD1   1 
ATOM   10874 C CD2   . TYR B  1 301  ? 3.441   3.742   123.470 1.00 31.93 ? 299  TYR B CD2   1 
ATOM   10875 C CE1   . TYR B  1 301  ? 3.532   3.388   126.204 1.00 36.86 ? 299  TYR B CE1   1 
ATOM   10876 C CE2   . TYR B  1 301  ? 4.590   4.084   124.172 1.00 32.20 ? 299  TYR B CE2   1 
ATOM   10877 C CZ    . TYR B  1 301  ? 4.630   3.906   125.536 1.00 32.38 ? 299  TYR B CZ    1 
ATOM   10878 O OH    . TYR B  1 301  ? 5.768   4.241   126.235 1.00 33.00 ? 299  TYR B OH    1 
ATOM   10879 N N     . ASP B  1 302  ? -0.783  0.531   121.573 1.00 34.16 ? 300  ASP B N     1 
ATOM   10880 C CA    . ASP B  1 302  ? -2.089  0.312   120.961 1.00 34.84 ? 300  ASP B CA    1 
ATOM   10881 C C     . ASP B  1 302  ? -2.886  1.609   120.872 1.00 33.97 ? 300  ASP B C     1 
ATOM   10882 O O     . ASP B  1 302  ? -4.019  1.717   121.347 1.00 34.51 ? 300  ASP B O     1 
ATOM   10883 C CB    . ASP B  1 302  ? -2.893  -0.761  121.691 1.00 35.66 ? 300  ASP B CB    1 
ATOM   10884 C CG    . ASP B  1 302  ? -3.966  -1.334  120.797 1.00 41.63 ? 300  ASP B CG    1 
ATOM   10885 O OD1   . ASP B  1 302  ? -3.647  -1.505  119.595 1.00 35.56 ? 300  ASP B OD1   1 
ATOM   10886 O OD2   . ASP B  1 302  ? -5.103  -1.577  121.263 1.00 39.42 ? 300  ASP B OD2   1 
ATOM   10887 N N     . ILE B  1 303  ? -2.265  2.612   120.267 1.00 33.01 ? 301  ILE B N     1 
ATOM   10888 C CA    . ILE B  1 303  ? -2.948  3.850   119.933 1.00 35.39 ? 301  ILE B CA    1 
ATOM   10889 C C     . ILE B  1 303  ? -2.968  3.975   118.418 1.00 31.78 ? 301  ILE B C     1 
ATOM   10890 O O     . ILE B  1 303  ? -2.220  3.306   117.705 1.00 31.63 ? 301  ILE B O     1 
ATOM   10891 C CB    . ILE B  1 303  ? -2.281  5.080   120.575 1.00 31.81 ? 301  ILE B CB    1 
ATOM   10892 C CG1   . ILE B  1 303  ? -0.904  5.333   119.957 1.00 31.00 ? 301  ILE B CG1   1 
ATOM   10893 C CG2   . ILE B  1 303  ? -2.127  4.868   122.066 1.00 32.46 ? 301  ILE B CG2   1 
ATOM   10894 C CD1   . ILE B  1 303  ? -0.327  6.691   120.303 1.00 30.29 ? 301  ILE B CD1   1 
ATOM   10895 N N     . GLY B  1 304  ? -3.829  4.859   117.931 1.00 33.69 ? 302  GLY B N     1 
ATOM   10896 C CA    . GLY B  1 304  ? -3.860  5.145   116.510 1.00 30.79 ? 302  GLY B CA    1 
ATOM   10897 C C     . GLY B  1 304  ? -2.769  6.118   116.103 1.00 30.97 ? 302  GLY B C     1 
ATOM   10898 O O     . GLY B  1 304  ? -2.379  7.015   116.853 1.00 31.94 ? 302  GLY B O     1 
ATOM   10899 N N     . LEU B  1 305  ? -2.256  5.924   114.889 1.00 30.70 ? 303  LEU B N     1 
ATOM   10900 C CA    . LEU B  1 305  ? -1.286  6.838   114.288 1.00 29.52 ? 303  LEU B CA    1 
ATOM   10901 C C     . LEU B  1 305  ? -1.797  7.155   112.896 1.00 28.73 ? 303  LEU B C     1 
ATOM   10902 O O     . LEU B  1 305  ? -1.863  6.260   112.048 1.00 30.65 ? 303  LEU B O     1 
ATOM   10903 C CB    . LEU B  1 305  ? 0.114   6.222   114.222 1.00 30.93 ? 303  LEU B CB    1 
ATOM   10904 C CG    . LEU B  1 305  ? 1.220   7.078   113.588 1.00 29.24 ? 303  LEU B CG    1 
ATOM   10905 C CD1   . LEU B  1 305  ? 2.515   6.919   114.360 1.00 27.67 ? 303  LEU B CD1   1 
ATOM   10906 C CD2   . LEU B  1 305  ? 1.447   6.735   112.129 1.00 34.14 ? 303  LEU B CD2   1 
ATOM   10907 N N     . ASN B  1 306  ? -2.151  8.415   112.661 1.00 27.34 ? 304  ASN B N     1 
ATOM   10908 C CA    . ASN B  1 306  ? -2.779  8.833   111.410 1.00 28.80 ? 304  ASN B CA    1 
ATOM   10909 C C     . ASN B  1 306  ? -1.803  9.637   110.563 1.00 26.09 ? 304  ASN B C     1 
ATOM   10910 O O     . ASN B  1 306  ? -1.145  10.547  111.066 1.00 27.43 ? 304  ASN B O     1 
ATOM   10911 C CB    . ASN B  1 306  ? -4.031  9.673   111.676 1.00 27.05 ? 304  ASN B CB    1 
ATOM   10912 C CG    . ASN B  1 306  ? -4.573  10.297  110.416 1.00 30.62 ? 304  ASN B CG    1 
ATOM   10913 O OD1   . ASN B  1 306  ? -4.239  11.433  110.058 1.00 32.41 ? 304  ASN B OD1   1 
ATOM   10914 N ND2   . ASN B  1 306  ? -5.384  9.548   109.719 1.00 29.57 ? 304  ASN B ND2   1 
ATOM   10915 N N     . ILE B  1 307  ? -1.745  9.323   109.272 1.00 25.98 ? 305  ILE B N     1 
ATOM   10916 C CA    . ILE B  1 307  ? -0.944  10.060  108.299 1.00 25.81 ? 305  ILE B CA    1 
ATOM   10917 C C     . ILE B  1 307  ? -1.836  11.095  107.621 1.00 26.39 ? 305  ILE B C     1 
ATOM   10918 O O     . ILE B  1 307  ? -2.689  10.751  106.791 1.00 24.86 ? 305  ILE B O     1 
ATOM   10919 C CB    . ILE B  1 307  ? -0.310  9.122   107.264 1.00 26.56 ? 305  ILE B CB    1 
ATOM   10920 C CG1   . ILE B  1 307  ? 0.706   8.185   107.933 1.00 28.87 ? 305  ILE B CG1   1 
ATOM   10921 C CG2   . ILE B  1 307  ? 0.337   9.913   106.155 1.00 25.43 ? 305  ILE B CG2   1 
ATOM   10922 C CD1   . ILE B  1 307  ? 1.226   7.096   106.998 1.00 32.32 ? 305  ILE B CD1   1 
ATOM   10923 N N     . ASP B  1 308  ? -1.613  12.370  107.949 1.00 24.80 ? 306  ASP B N     1 
ATOM   10924 C CA    . ASP B  1 308  ? -2.348  13.460  107.325 1.00 23.66 ? 306  ASP B CA    1 
ATOM   10925 C C     . ASP B  1 308  ? -2.064  13.512  105.831 1.00 26.11 ? 306  ASP B C     1 
ATOM   10926 O O     . ASP B  1 308  ? -0.991  13.121  105.364 1.00 25.80 ? 306  ASP B O     1 
ATOM   10927 C CB    . ASP B  1 308  ? -1.962  14.812  107.949 1.00 24.55 ? 306  ASP B CB    1 
ATOM   10928 C CG    . ASP B  1 308  ? -2.459  14.971  109.369 1.00 30.56 ? 306  ASP B CG    1 
ATOM   10929 O OD1   . ASP B  1 308  ? -3.197  14.080  109.851 1.00 26.05 ? 306  ASP B OD1   1 
ATOM   10930 O OD2   . ASP B  1 308  ? -2.101  15.994  110.011 1.00 30.30 ? 306  ASP B OD2   1 
ATOM   10931 N N     . ALA B  1 309  ? -3.032  14.025  105.078 1.00 25.01 ? 307  ALA B N     1 
ATOM   10932 C CA    . ALA B  1 309  ? -2.876  14.191  103.646 1.00 22.58 ? 307  ALA B CA    1 
ATOM   10933 C C     . ALA B  1 309  ? -2.483  15.630  103.337 1.00 23.37 ? 307  ALA B C     1 
ATOM   10934 O O     . ALA B  1 309  ? -2.973  16.572  103.966 1.00 23.90 ? 307  ALA B O     1 
ATOM   10935 C CB    . ALA B  1 309  ? -4.161  13.808  102.900 1.00 22.92 ? 307  ALA B CB    1 
ATOM   10936 N N     . GLU B  1 310  ? -1.569  15.787  102.383 1.00 21.34 ? 308  GLU B N     1 
ATOM   10937 C CA    . GLU B  1 310  ? -1.009  17.093  102.075 1.00 23.65 ? 308  GLU B CA    1 
ATOM   10938 C C     . GLU B  1 310  ? -1.290  17.458  100.619 1.00 22.81 ? 308  GLU B C     1 
ATOM   10939 O O     . GLU B  1 310  ? -2.420  17.271  100.145 1.00 23.29 ? 308  GLU B O     1 
ATOM   10940 C CB    . GLU B  1 310  ? 0.488   17.098  102.419 1.00 23.97 ? 308  GLU B CB    1 
ATOM   10941 C CG    . GLU B  1 310  ? 0.723   16.707  103.877 1.00 25.53 ? 308  GLU B CG    1 
ATOM   10942 C CD    . GLU B  1 310  ? 2.164   16.881  104.364 1.00 24.36 ? 308  GLU B CD    1 
ATOM   10943 O OE1   . GLU B  1 310  ? 2.626   18.027  104.529 1.00 27.58 ? 308  GLU B OE1   1 
ATOM   10944 O OE2   . GLU B  1 310  ? 2.829   15.868  104.615 1.00 22.71 ? 308  GLU B OE2   1 
ATOM   10945 N N     . GLU B  1 311  ? -0.284  17.953  99.895  1.00 21.57 ? 309  GLU B N     1 
ATOM   10946 C CA    . GLU B  1 311  ? -0.510  18.420  98.536  1.00 23.60 ? 309  GLU B CA    1 
ATOM   10947 C C     . GLU B  1 311  ? -0.839  17.248  97.607  1.00 23.75 ? 309  GLU B C     1 
ATOM   10948 O O     . GLU B  1 311  ? -0.502  16.088  97.870  1.00 21.31 ? 309  GLU B O     1 
ATOM   10949 C CB    . GLU B  1 311  ? 0.713   19.193  98.013  1.00 23.27 ? 309  GLU B CB    1 
ATOM   10950 C CG    . GLU B  1 311  ? 1.045   20.507  98.767  1.00 24.21 ? 309  GLU B CG    1 
ATOM   10951 C CD    . GLU B  1 311  ? 1.933   20.313  99.982  1.00 26.96 ? 309  GLU B CD    1 
ATOM   10952 O OE1   . GLU B  1 311  ? 2.196   19.154  100.370 1.00 23.57 ? 309  GLU B OE1   1 
ATOM   10953 O OE2   . GLU B  1 311  ? 2.352   21.335  100.566 1.00 27.83 ? 309  GLU B OE2   1 
ATOM   10954 N N     . ALA B  1 312  ? -1.510  17.569  96.497  1.00 19.85 ? 310  ALA B N     1 
ATOM   10955 C CA    . ALA B  1 312  ? -1.914  16.535  95.561  1.00 19.83 ? 310  ALA B CA    1 
ATOM   10956 C C     . ALA B  1 312  ? -0.729  15.753  95.004  1.00 22.04 ? 310  ALA B C     1 
ATOM   10957 O O     . ALA B  1 312  ? -0.861  14.548  94.754  1.00 23.03 ? 310  ALA B O     1 
ATOM   10958 C CB    . ALA B  1 312  ? -2.724  17.137  94.402  1.00 20.49 ? 310  ALA B CB    1 
ATOM   10959 N N     . ASP B  1 313  ? 0.428   16.400  94.783  1.00 23.09 ? 311  ASP B N     1 
ATOM   10960 C CA    . ASP B  1 313  ? 1.544   15.669  94.182  1.00 20.31 ? 311  ASP B CA    1 
ATOM   10961 C C     . ASP B  1 313  ? 2.265   14.761  95.184  1.00 21.52 ? 311  ASP B C     1 
ATOM   10962 O O     . ASP B  1 313  ? 3.250   14.119  94.821  1.00 23.72 ? 311  ASP B O     1 
ATOM   10963 C CB    . ASP B  1 313  ? 2.543   16.631  93.493  1.00 20.77 ? 311  ASP B CB    1 
ATOM   10964 C CG    . ASP B  1 313  ? 3.210   17.634  94.440  1.00 28.48 ? 311  ASP B CG    1 
ATOM   10965 O OD1   . ASP B  1 313  ? 3.118   17.512  95.665  1.00 22.59 ? 311  ASP B OD1   1 
ATOM   10966 O OD2   . ASP B  1 313  ? 3.853   18.570  93.927  1.00 27.62 ? 311  ASP B OD2   1 
ATOM   10967 N N     . ARG B  1 314  ? 1.791   14.680  96.420  1.00 22.34 ? 312  ARG B N     1 
ATOM   10968 C CA    . ARG B  1 314  ? 2.306   13.725  97.391  1.00 20.56 ? 312  ARG B CA    1 
ATOM   10969 C C     . ARG B  1 314  ? 1.360   12.561  97.656  1.00 22.82 ? 312  ARG B C     1 
ATOM   10970 O O     . ARG B  1 314  ? 1.727   11.628  98.383  1.00 21.43 ? 312  ARG B O     1 
ATOM   10971 C CB    . ARG B  1 314  ? 2.616   14.452  98.702  1.00 20.72 ? 312  ARG B CB    1 
ATOM   10972 C CG    . ARG B  1 314  ? 3.901   15.266  98.621  1.00 24.60 ? 312  ARG B CG    1 
ATOM   10973 C CD    . ARG B  1 314  ? 3.950   16.385  99.650  1.00 23.51 ? 312  ARG B CD    1 
ATOM   10974 N NE    . ARG B  1 314  ? 5.315   16.883  99.799  1.00 22.95 ? 312  ARG B NE    1 
ATOM   10975 C CZ    . ARG B  1 314  ? 5.673   17.908  100.561 1.00 23.98 ? 312  ARG B CZ    1 
ATOM   10976 N NH1   . ARG B  1 314  ? 4.776   18.640  101.208 1.00 20.00 ? 312  ARG B NH1   1 
ATOM   10977 N NH2   . ARG B  1 314  ? 6.966   18.190  100.699 1.00 21.75 ? 312  ARG B NH2   1 
ATOM   10978 N N     . LEU B  1 315  ? 0.158   12.575  97.083  1.00 25.27 ? 313  LEU B N     1 
ATOM   10979 C CA    . LEU B  1 315  ? -0.833  11.561  97.426  1.00 22.30 ? 313  LEU B CA    1 
ATOM   10980 C C     . LEU B  1 315  ? -0.337  10.164  97.066  1.00 24.96 ? 313  LEU B C     1 
ATOM   10981 O O     . LEU B  1 315  ? -0.276  9.273   97.920  1.00 25.15 ? 313  LEU B O     1 
ATOM   10982 C CB    . LEU B  1 315  ? -2.157  11.865  96.716  1.00 23.39 ? 313  LEU B CB    1 
ATOM   10983 C CG    . LEU B  1 315  ? -3.467  11.268  97.236  1.00 23.75 ? 313  LEU B CG    1 
ATOM   10984 C CD1   . LEU B  1 315  ? -4.629  11.739  96.356  1.00 22.56 ? 313  LEU B CD1   1 
ATOM   10985 C CD2   . LEU B  1 315  ? -3.466  9.743   97.294  1.00 25.26 ? 313  LEU B CD2   1 
ATOM   10986 N N     . GLU B  1 316  ? -0.012  9.940   95.792  1.00 22.42 ? 314  GLU B N     1 
ATOM   10987 C CA    . GLU B  1 316  ? 0.331   8.583   95.385  1.00 24.13 ? 314  GLU B CA    1 
ATOM   10988 C C     . GLU B  1 316  ? 1.645   8.127   96.009  1.00 27.67 ? 314  GLU B C     1 
ATOM   10989 O O     . GLU B  1 316  ? 1.796   6.941   96.321  1.00 29.67 ? 314  GLU B O     1 
ATOM   10990 C CB    . GLU B  1 316  ? 0.356   8.498   93.864  1.00 27.82 ? 314  GLU B CB    1 
ATOM   10991 C CG    . GLU B  1 316  ? -1.040  8.685   93.321  1.00 24.41 ? 314  GLU B CG    1 
ATOM   10992 C CD    . GLU B  1 316  ? -1.131  8.544   91.813  1.00 28.48 ? 314  GLU B CD    1 
ATOM   10993 O OE1   . GLU B  1 316  ? -0.518  7.602   91.268  1.00 29.60 ? 314  GLU B OE1   1 
ATOM   10994 O OE2   . GLU B  1 316  ? -1.801  9.389   91.173  1.00 28.75 ? 314  GLU B OE2   1 
ATOM   10995 N N     . LEU B  1 317  ? 2.577   9.055   96.238  1.00 26.22 ? 315  LEU B N     1 
ATOM   10996 C CA    . LEU B  1 317  ? 3.817   8.716   96.939  1.00 27.82 ? 315  LEU B CA    1 
ATOM   10997 C C     . LEU B  1 317  ? 3.534   8.178   98.332  1.00 27.52 ? 315  LEU B C     1 
ATOM   10998 O O     . LEU B  1 317  ? 4.161   7.202   98.768  1.00 28.49 ? 315  LEU B O     1 
ATOM   10999 C CB    . LEU B  1 317  ? 4.732   9.938   97.017  1.00 23.80 ? 315  LEU B CB    1 
ATOM   11000 C CG    . LEU B  1 317  ? 6.021   9.801   97.841  1.00 24.84 ? 315  LEU B CG    1 
ATOM   11001 C CD1   . LEU B  1 317  ? 6.832   8.609   97.360  1.00 28.81 ? 315  LEU B CD1   1 
ATOM   11002 C CD2   . LEU B  1 317  ? 6.838   11.092  97.774  1.00 26.80 ? 315  LEU B CD2   1 
ATOM   11003 N N     . SER B  1 318  ? 2.592   8.797   99.047  1.00 24.58 ? 316  SER B N     1 
ATOM   11004 C CA    . SER B  1 318  ? 2.290   8.346   100.403 1.00 25.04 ? 316  SER B CA    1 
ATOM   11005 C C     . SER B  1 318  ? 1.672   6.951   100.412 1.00 27.37 ? 316  SER B C     1 
ATOM   11006 O O     . SER B  1 318  ? 1.800   6.230   101.404 1.00 28.64 ? 316  SER B O     1 
ATOM   11007 C CB    . SER B  1 318  ? 1.354   9.335   101.098 1.00 23.03 ? 316  SER B CB    1 
ATOM   11008 O OG    . SER B  1 318  ? 0.064   9.316   100.499 1.00 27.14 ? 316  SER B OG    1 
ATOM   11009 N N     . LEU B  1 319  ? 0.982   6.562   99.335  1.00 26.12 ? 317  LEU B N     1 
ATOM   11010 C CA    . LEU B  1 319  ? 0.426   5.216   99.261  1.00 25.36 ? 317  LEU B CA    1 
ATOM   11011 C C     . LEU B  1 319  ? 1.511   4.149   99.234  1.00 25.57 ? 317  LEU B C     1 
ATOM   11012 O O     . LEU B  1 319  ? 1.281   3.023   99.686  1.00 26.80 ? 317  LEU B O     1 
ATOM   11013 C CB    . LEU B  1 319  ? -0.460  5.082   98.014  1.00 25.31 ? 317  LEU B CB    1 
ATOM   11014 C CG    . LEU B  1 319  ? -1.659  6.029   97.941  1.00 26.97 ? 317  LEU B CG    1 
ATOM   11015 C CD1   . LEU B  1 319  ? -2.401  5.874   96.594  1.00 25.01 ? 317  LEU B CD1   1 
ATOM   11016 C CD2   . LEU B  1 319  ? -2.618  5.772   99.103  1.00 29.12 ? 317  LEU B CD2   1 
ATOM   11017 N N     . ASP B  1 320  ? 2.683   4.466   98.683  1.00 28.47 ? 318  ASP B N     1 
ATOM   11018 C CA    . ASP B  1 320  ? 3.786   3.512   98.703  1.00 29.44 ? 318  ASP B CA    1 
ATOM   11019 C C     . ASP B  1 320  ? 4.300   3.289   100.120 1.00 30.89 ? 318  ASP B C     1 
ATOM   11020 O O     . ASP B  1 320  ? 4.700   2.173   100.470 1.00 29.91 ? 318  ASP B O     1 
ATOM   11021 C CB    . ASP B  1 320  ? 4.906   3.996   97.786  1.00 26.75 ? 318  ASP B CB    1 
ATOM   11022 C CG    . ASP B  1 320  ? 4.593   3.755   96.326  1.00 30.40 ? 318  ASP B CG    1 
ATOM   11023 O OD1   . ASP B  1 320  ? 4.307   2.593   95.971  1.00 32.30 ? 318  ASP B OD1   1 
ATOM   11024 O OD2   . ASP B  1 320  ? 4.620   4.720   95.536  1.00 27.04 ? 318  ASP B OD2   1 
ATOM   11025 N N     . LEU B  1 321  ? 4.296   4.331   100.954 1.00 26.45 ? 319  LEU B N     1 
ATOM   11026 C CA    . LEU B  1 321  ? 4.669   4.128   102.353 1.00 28.05 ? 319  LEU B CA    1 
ATOM   11027 C C     . LEU B  1 321  ? 3.591   3.351   103.090 1.00 28.74 ? 319  LEU B C     1 
ATOM   11028 O O     . LEU B  1 321  ? 3.896   2.441   103.871 1.00 28.90 ? 319  LEU B O     1 
ATOM   11029 C CB    . LEU B  1 321  ? 4.931   5.470   103.048 1.00 27.10 ? 319  LEU B CB    1 
ATOM   11030 C CG    . LEU B  1 321  ? 6.297   6.092   102.782 1.00 27.45 ? 319  LEU B CG    1 
ATOM   11031 C CD1   . LEU B  1 321  ? 6.227   6.985   101.582 1.00 29.33 ? 319  LEU B CD1   1 
ATOM   11032 C CD2   . LEU B  1 321  ? 6.761   6.863   104.006 1.00 27.60 ? 319  LEU B CD2   1 
ATOM   11033 N N     . LEU B  1 322  ? 2.322   3.701   102.853 1.00 26.32 ? 320  LEU B N     1 
ATOM   11034 C CA    . LEU B  1 322  ? 1.221   2.981   103.481 1.00 27.33 ? 320  LEU B CA    1 
ATOM   11035 C C     . LEU B  1 322  ? 1.281   1.501   103.136 1.00 28.91 ? 320  LEU B C     1 
ATOM   11036 O O     . LEU B  1 322  ? 1.065   0.642   104.000 1.00 30.50 ? 320  LEU B O     1 
ATOM   11037 C CB    . LEU B  1 322  ? -0.114  3.574   103.024 1.00 27.10 ? 320  LEU B CB    1 
ATOM   11038 C CG    . LEU B  1 322  ? -1.346  2.934   103.666 1.00 28.66 ? 320  LEU B CG    1 
ATOM   11039 C CD1   . LEU B  1 322  ? -1.396  3.290   105.153 1.00 29.76 ? 320  LEU B CD1   1 
ATOM   11040 C CD2   . LEU B  1 322  ? -2.628  3.341   102.955 1.00 28.92 ? 320  LEU B CD2   1 
ATOM   11041 N N     . GLU B  1 323  ? 1.594   1.193   101.874 1.00 27.52 ? 321  GLU B N     1 
ATOM   11042 C CA    . GLU B  1 323  ? 1.696   -0.195  101.429 1.00 31.48 ? 321  GLU B CA    1 
ATOM   11043 C C     . GLU B  1 323  ? 2.727   -0.967  102.246 1.00 31.42 ? 321  GLU B C     1 
ATOM   11044 O O     . GLU B  1 323  ? 2.447   -2.069  102.731 1.00 35.69 ? 321  GLU B O     1 
ATOM   11045 C CB    . GLU B  1 323  ? 2.046   -0.235  99.937  1.00 35.13 ? 321  GLU B CB    1 
ATOM   11046 C CG    . GLU B  1 323  ? 2.373   -1.634  99.417  1.00 34.38 ? 321  GLU B CG    1 
ATOM   11047 C CD    . GLU B  1 323  ? 1.220   -2.299  98.662  1.00 39.99 ? 321  GLU B CD    1 
ATOM   11048 O OE1   . GLU B  1 323  ? 0.309   -1.595  98.168  1.00 38.82 ? 321  GLU B OE1   1 
ATOM   11049 O OE2   . GLU B  1 323  ? 1.235   -3.542  98.561  1.00 39.08 ? 321  GLU B OE2   1 
ATOM   11050 N N     . VAL B  1 324  ? 3.926   -0.399  102.415 1.00 29.16 ? 322  VAL B N     1 
ATOM   11051 C CA    . VAL B  1 324  ? 4.974   -1.091  103.158 1.00 29.93 ? 322  VAL B CA    1 
ATOM   11052 C C     . VAL B  1 324  ? 4.580   -1.236  104.621 1.00 34.07 ? 322  VAL B C     1 
ATOM   11053 O O     . VAL B  1 324  ? 4.796   -2.290  105.231 1.00 35.30 ? 322  VAL B O     1 
ATOM   11054 C CB    . VAL B  1 324  ? 6.326   -0.359  103.012 1.00 32.86 ? 322  VAL B CB    1 
ATOM   11055 C CG1   . VAL B  1 324  ? 7.368   -0.970  103.955 1.00 35.34 ? 322  VAL B CG1   1 
ATOM   11056 C CG2   . VAL B  1 324  ? 6.810   -0.411  101.571 1.00 33.93 ? 322  VAL B CG2   1 
ATOM   11057 N N     . LEU B  1 325  ? 3.986   -0.195  105.207 1.00 31.92 ? 323  LEU B N     1 
ATOM   11058 C CA    . LEU B  1 325  ? 3.612   -0.271  106.616 1.00 32.66 ? 323  LEU B CA    1 
ATOM   11059 C C     . LEU B  1 325  ? 2.560   -1.347  106.850 1.00 34.12 ? 323  LEU B C     1 
ATOM   11060 O O     . LEU B  1 325  ? 2.675   -2.138  107.788 1.00 30.45 ? 323  LEU B O     1 
ATOM   11061 C CB    . LEU B  1 325  ? 3.122   1.093   107.111 1.00 28.46 ? 323  LEU B CB    1 
ATOM   11062 C CG    . LEU B  1 325  ? 4.182   2.202   107.084 1.00 33.80 ? 323  LEU B CG    1 
ATOM   11063 C CD1   . LEU B  1 325  ? 3.536   3.574   107.150 1.00 31.25 ? 323  LEU B CD1   1 
ATOM   11064 C CD2   . LEU B  1 325  ? 5.192   2.018   108.235 1.00 27.79 ? 323  LEU B CD2   1 
ATOM   11065 N N     . CYS B  1 326  ? 1.537   -1.415  105.995 1.00 31.62 ? 324  CYS B N     1 
ATOM   11066 C CA    . CYS B  1 326  ? 0.479   -2.391  106.228 1.00 31.68 ? 324  CYS B CA    1 
ATOM   11067 C C     . CYS B  1 326  ? 0.953   -3.828  106.046 1.00 33.18 ? 324  CYS B C     1 
ATOM   11068 O O     . CYS B  1 326  ? 0.368   -4.737  106.646 1.00 34.56 ? 324  CYS B O     1 
ATOM   11069 C CB    . CYS B  1 326  ? -0.710  -2.102  105.311 1.00 32.87 ? 324  CYS B CB    1 
ATOM   11070 S SG    . CYS B  1 326  ? -1.529  -0.568  105.764 1.00 34.75 ? 324  CYS B SG    1 
ATOM   11071 N N     . LEU B  1 327  ? 2.013   -4.049  105.267 1.00 32.41 ? 325  LEU B N     1 
ATOM   11072 C CA    . LEU B  1 327  ? 2.585   -5.376  105.053 1.00 34.32 ? 325  LEU B CA    1 
ATOM   11073 C C     . LEU B  1 327  ? 3.793   -5.655  105.940 1.00 38.41 ? 325  LEU B C     1 
ATOM   11074 O O     . LEU B  1 327  ? 4.384   -6.741  105.847 1.00 38.69 ? 325  LEU B O     1 
ATOM   11075 C CB    . LEU B  1 327  ? 2.973   -5.539  103.587 1.00 34.15 ? 325  LEU B CB    1 
ATOM   11076 C CG    . LEU B  1 327  ? 1.788   -5.485  102.619 1.00 37.47 ? 325  LEU B CG    1 
ATOM   11077 C CD1   . LEU B  1 327  ? 2.282   -5.341  101.196 1.00 40.87 ? 325  LEU B CD1   1 
ATOM   11078 C CD2   . LEU B  1 327  ? 0.950   -6.746  102.775 1.00 38.12 ? 325  LEU B CD2   1 
ATOM   11079 N N     . ASP B  1 328  ? 4.170   -4.713  106.799 1.00 34.97 ? 326  ASP B N     1 
ATOM   11080 C CA    . ASP B  1 328  ? 5.302   -4.923  107.694 1.00 31.70 ? 326  ASP B CA    1 
ATOM   11081 C C     . ASP B  1 328  ? 4.904   -5.866  108.818 1.00 38.36 ? 326  ASP B C     1 
ATOM   11082 O O     . ASP B  1 328  ? 4.027   -5.544  109.628 1.00 40.97 ? 326  ASP B O     1 
ATOM   11083 C CB    . ASP B  1 328  ? 5.779   -3.582  108.251 1.00 36.11 ? 326  ASP B CB    1 
ATOM   11084 C CG    . ASP B  1 328  ? 7.134   -3.680  108.941 1.00 41.44 ? 326  ASP B CG    1 
ATOM   11085 O OD1   . ASP B  1 328  ? 7.381   -4.681  109.641 1.00 40.68 ? 326  ASP B OD1   1 
ATOM   11086 O OD2   . ASP B  1 328  ? 7.959   -2.756  108.773 1.00 45.55 ? 326  ASP B OD2   1 
ATOM   11087 N N     . GLY B  1 329  ? 5.554   -7.033  108.872 1.00 39.00 ? 327  GLY B N     1 
ATOM   11088 C CA    . GLY B  1 329  ? 5.253   -8.012  109.903 1.00 37.26 ? 327  GLY B CA    1 
ATOM   11089 C C     . GLY B  1 329  ? 5.534   -7.539  111.317 1.00 39.89 ? 327  GLY B C     1 
ATOM   11090 O O     . GLY B  1 329  ? 4.951   -8.074  112.265 1.00 44.74 ? 327  GLY B O     1 
ATOM   11091 N N     . ASP B  1 330  ? 6.416   -6.553  111.487 1.00 38.32 ? 328  ASP B N     1 
ATOM   11092 C CA    . ASP B  1 330  ? 6.668   -6.024  112.826 1.00 42.62 ? 328  ASP B CA    1 
ATOM   11093 C C     . ASP B  1 330  ? 5.453   -5.305  113.391 1.00 40.53 ? 328  ASP B C     1 
ATOM   11094 O O     . ASP B  1 330  ? 5.320   -5.204  114.608 1.00 39.78 ? 328  ASP B O     1 
ATOM   11095 C CB    . ASP B  1 330  ? 7.872   -5.073  112.828 1.00 43.74 ? 328  ASP B CB    1 
ATOM   11096 C CG    . ASP B  1 330  ? 9.175   -5.770  112.452 1.00 52.73 ? 328  ASP B CG    1 
ATOM   11097 O OD1   . ASP B  1 330  ? 9.262   -7.011  112.614 1.00 52.30 ? 328  ASP B OD1   1 
ATOM   11098 O OD2   . ASP B  1 330  ? 10.117  -5.077  111.999 1.00 45.07 ? 328  ASP B OD2   1 
ATOM   11099 N N     . LEU B  1 331  ? 4.558   -4.813  112.538 1.00 41.30 ? 329  LEU B N     1 
ATOM   11100 C CA    . LEU B  1 331  ? 3.338   -4.160  112.988 1.00 37.35 ? 329  LEU B CA    1 
ATOM   11101 C C     . LEU B  1 331  ? 2.150   -5.114  113.048 1.00 40.84 ? 329  LEU B C     1 
ATOM   11102 O O     . LEU B  1 331  ? 1.016   -4.660  113.251 1.00 40.58 ? 329  LEU B O     1 
ATOM   11103 C CB    . LEU B  1 331  ? 3.025   -2.969  112.074 1.00 36.01 ? 329  LEU B CB    1 
ATOM   11104 C CG    . LEU B  1 331  ? 4.073   -1.856  112.127 1.00 37.69 ? 329  LEU B CG    1 
ATOM   11105 C CD1   . LEU B  1 331  ? 3.944   -0.879  110.967 1.00 30.22 ? 329  LEU B CD1   1 
ATOM   11106 C CD2   . LEU B  1 331  ? 3.989   -1.122  113.454 1.00 35.55 ? 329  LEU B CD2   1 
ATOM   11107 N N     . SER B  1 332  ? 2.392   -6.417  112.875 1.00 38.22 ? 330  SER B N     1 
ATOM   11108 C CA    . SER B  1 332  ? 1.319   -7.400  112.789 1.00 42.09 ? 330  SER B CA    1 
ATOM   11109 C C     . SER B  1 332  ? 0.437   -7.350  114.030 1.00 41.61 ? 330  SER B C     1 
ATOM   11110 O O     . SER B  1 332  ? 0.932   -7.382  115.161 1.00 46.59 ? 330  SER B O     1 
ATOM   11111 C CB    . SER B  1 332  ? 1.913   -8.801  112.620 1.00 42.79 ? 330  SER B CB    1 
ATOM   11112 O OG    . SER B  1 332  ? 0.932   -9.758  112.246 1.00 47.05 ? 330  SER B OG    1 
ATOM   11113 N N     . GLY B  1 333  ? -0.875  -7.271  113.814 1.00 41.63 ? 331  GLY B N     1 
ATOM   11114 C CA    . GLY B  1 333  ? -1.833  -7.239  114.899 1.00 44.26 ? 331  GLY B CA    1 
ATOM   11115 C C     . GLY B  1 333  ? -2.339  -5.859  115.261 1.00 49.70 ? 331  GLY B C     1 
ATOM   11116 O O     . GLY B  1 333  ? -3.340  -5.756  115.981 1.00 53.78 ? 331  GLY B O     1 
ATOM   11117 N N     . TRP B  1 334  ? -1.693  -4.804  114.773 1.00 40.34 ? 332  TRP B N     1 
ATOM   11118 C CA    . TRP B  1 334  ? -2.058  -3.435  115.107 1.00 40.04 ? 332  TRP B CA    1 
ATOM   11119 C C     . TRP B  1 334  ? -2.991  -2.870  114.047 1.00 43.16 ? 332  TRP B C     1 
ATOM   11120 O O     . TRP B  1 334  ? -2.654  -2.873  112.860 1.00 42.71 ? 332  TRP B O     1 
ATOM   11121 C CB    . TRP B  1 334  ? -0.798  -2.583  115.210 1.00 38.74 ? 332  TRP B CB    1 
ATOM   11122 C CG    . TRP B  1 334  ? -1.018  -1.127  115.475 1.00 37.92 ? 332  TRP B CG    1 
ATOM   11123 C CD1   . TRP B  1 334  ? -1.686  -0.569  116.528 1.00 39.02 ? 332  TRP B CD1   1 
ATOM   11124 C CD2   . TRP B  1 334  ? -0.524  -0.037  114.691 1.00 37.84 ? 332  TRP B CD2   1 
ATOM   11125 N NE1   . TRP B  1 334  ? -1.653  0.805   116.433 1.00 36.79 ? 332  TRP B NE1   1 
ATOM   11126 C CE2   . TRP B  1 334  ? -0.941  1.155   115.317 1.00 32.38 ? 332  TRP B CE2   1 
ATOM   11127 C CE3   . TRP B  1 334  ? 0.233   0.046   113.522 1.00 34.69 ? 332  TRP B CE3   1 
ATOM   11128 C CZ2   . TRP B  1 334  ? -0.625  2.411   114.811 1.00 30.81 ? 332  TRP B CZ2   1 
ATOM   11129 C CZ3   . TRP B  1 334  ? 0.545   1.291   113.025 1.00 34.26 ? 332  TRP B CZ3   1 
ATOM   11130 C CH2   . TRP B  1 334  ? 0.120   2.458   113.670 1.00 32.18 ? 332  TRP B CH2   1 
ATOM   11131 N N     . ASN B  1 335  ? -4.154  -2.381  114.478 1.00 35.37 ? 333  ASN B N     1 
ATOM   11132 C CA    . ASN B  1 335  ? -5.121  -1.757  113.589 1.00 39.94 ? 333  ASN B CA    1 
ATOM   11133 C C     . ASN B  1 335  ? -5.141  -0.235  113.719 1.00 36.40 ? 333  ASN B C     1 
ATOM   11134 O O     . ASN B  1 335  ? -6.090  0.407   113.264 1.00 35.42 ? 333  ASN B O     1 
ATOM   11135 C CB    . ASN B  1 335  ? -6.519  -2.327  113.848 1.00 38.09 ? 333  ASN B CB    1 
ATOM   11136 C CG    . ASN B  1 335  ? -6.610  -3.817  113.551 1.00 43.93 ? 333  ASN B CG    1 
ATOM   11137 O OD1   . ASN B  1 335  ? -6.181  -4.280  112.494 1.00 43.90 ? 333  ASN B OD1   1 
ATOM   11138 N ND2   . ASN B  1 335  ? -7.158  -4.576  114.494 1.00 47.29 ? 333  ASN B ND2   1 
ATOM   11139 N N     . GLY B  1 336  ? -4.127  0.361   114.330 1.00 36.91 ? 334  GLY B N     1 
ATOM   11140 C CA    . GLY B  1 336  ? -4.187  1.793   114.528 1.00 32.83 ? 334  GLY B CA    1 
ATOM   11141 C C     . GLY B  1 336  ? -3.644  2.644   113.411 1.00 34.17 ? 334  GLY B C     1 
ATOM   11142 O O     . GLY B  1 336  ? -3.653  3.876   113.529 1.00 30.35 ? 334  GLY B O     1 
ATOM   11143 N N     . MET B  1 337  ? -3.170  2.036   112.324 1.00 32.64 ? 335  MET B N     1 
ATOM   11144 C CA    . MET B  1 337  ? -2.617  2.810   111.222 1.00 33.28 ? 335  MET B CA    1 
ATOM   11145 C C     . MET B  1 337  ? -3.742  3.563   110.531 1.00 36.66 ? 335  MET B C     1 
ATOM   11146 O O     . MET B  1 337  ? -4.738  2.954   110.119 1.00 31.86 ? 335  MET B O     1 
ATOM   11147 C CB    . MET B  1 337  ? -1.898  1.894   110.238 1.00 37.60 ? 335  MET B CB    1 
ATOM   11148 C CG    . MET B  1 337  ? -1.233  2.635   109.088 1.00 32.66 ? 335  MET B CG    1 
ATOM   11149 S SD    . MET B  1 337  ? 0.047   3.773   109.636 1.00 50.96 ? 335  MET B SD    1 
ATOM   11150 C CE    . MET B  1 337  ? 1.393   2.661   110.004 1.00 34.04 ? 335  MET B CE    1 
ATOM   11151 N N     . GLY B  1 338  ? -3.590  4.884   110.418 1.00 34.77 ? 336  GLY B N     1 
ATOM   11152 C CA    . GLY B  1 338  ? -4.615  5.733   109.839 1.00 31.97 ? 336  GLY B CA    1 
ATOM   11153 C C     . GLY B  1 338  ? -4.105  6.547   108.665 1.00 28.39 ? 336  GLY B C     1 
ATOM   11154 O O     . GLY B  1 338  ? -2.920  6.879   108.582 1.00 28.52 ? 336  GLY B O     1 
ATOM   11155 N N     . PHE B  1 339  ? -5.023  6.878   107.757 1.00 27.52 ? 337  PHE B N     1 
ATOM   11156 C CA    . PHE B  1 339  ? -4.675  7.517   106.502 1.00 28.61 ? 337  PHE B CA    1 
ATOM   11157 C C     . PHE B  1 339  ? -5.806  8.460   106.117 1.00 28.92 ? 337  PHE B C     1 
ATOM   11158 O O     . PHE B  1 339  ? -6.977  8.069   106.154 1.00 30.09 ? 337  PHE B O     1 
ATOM   11159 C CB    . PHE B  1 339  ? -4.455  6.457   105.413 1.00 26.91 ? 337  PHE B CB    1 
ATOM   11160 C CG    . PHE B  1 339  ? -3.676  6.942   104.236 1.00 29.45 ? 337  PHE B CG    1 
ATOM   11161 C CD1   . PHE B  1 339  ? -2.293  6.995   104.274 1.00 31.28 ? 337  PHE B CD1   1 
ATOM   11162 C CD2   . PHE B  1 339  ? -4.327  7.316   103.073 1.00 29.60 ? 337  PHE B CD2   1 
ATOM   11163 C CE1   . PHE B  1 339  ? -1.574  7.443   103.167 1.00 30.19 ? 337  PHE B CE1   1 
ATOM   11164 C CE2   . PHE B  1 339  ? -3.614  7.752   101.968 1.00 31.10 ? 337  PHE B CE2   1 
ATOM   11165 C CZ    . PHE B  1 339  ? -2.237  7.815   102.018 1.00 30.54 ? 337  PHE B CZ    1 
ATOM   11166 N N     . VAL B  1 340  ? -5.457  9.690   105.765 1.00 27.35 ? 338  VAL B N     1 
ATOM   11167 C CA    . VAL B  1 340  ? -6.418  10.694  105.329 1.00 27.33 ? 338  VAL B CA    1 
ATOM   11168 C C     . VAL B  1 340  ? -6.602  10.590  103.822 1.00 25.81 ? 338  VAL B C     1 
ATOM   11169 O O     . VAL B  1 340  ? -5.629  10.404  103.082 1.00 26.14 ? 338  VAL B O     1 
ATOM   11170 C CB    . VAL B  1 340  ? -5.943  12.107  105.716 1.00 26.65 ? 338  VAL B CB    1 
ATOM   11171 C CG1   . VAL B  1 340  ? -6.900  13.152  105.157 1.00 26.00 ? 338  VAL B CG1   1 
ATOM   11172 C CG2   . VAL B  1 340  ? -5.812  12.231  107.222 1.00 25.35 ? 338  VAL B CG2   1 
ATOM   11173 N N     . VAL B  1 341  ? -7.850  10.714  103.365 1.00 25.53 ? 339  VAL B N     1 
ATOM   11174 C CA    . VAL B  1 341  ? -8.172  10.831  101.945 1.00 25.24 ? 339  VAL B CA    1 
ATOM   11175 C C     . VAL B  1 341  ? -9.000  12.100  101.763 1.00 24.95 ? 339  VAL B C     1 
ATOM   11176 O O     . VAL B  1 341  ? -9.925  12.353  102.542 1.00 25.56 ? 339  VAL B O     1 
ATOM   11177 C CB    . VAL B  1 341  ? -8.922  9.588   101.425 1.00 29.91 ? 339  VAL B CB    1 
ATOM   11178 C CG1   . VAL B  1 341  ? -8.036  8.348   101.556 1.00 31.19 ? 339  VAL B CG1   1 
ATOM   11179 C CG2   . VAL B  1 341  ? -10.235 9.365   102.193 1.00 33.03 ? 339  VAL B CG2   1 
ATOM   11180 N N     . GLN B  1 342  ? -8.651  12.908  100.759 1.00 24.25 ? 340  GLN B N     1 
ATOM   11181 C CA    . GLN B  1 342  ? -9.253  14.223  100.556 1.00 23.90 ? 340  GLN B CA    1 
ATOM   11182 C C     . GLN B  1 342  ? -10.336 14.137  99.482  1.00 26.65 ? 340  GLN B C     1 
ATOM   11183 O O     . GLN B  1 342  ? -10.037 13.838  98.323  1.00 23.84 ? 340  GLN B O     1 
ATOM   11184 C CB    . GLN B  1 342  ? -8.197  15.257  100.161 1.00 23.56 ? 340  GLN B CB    1 
ATOM   11185 C CG    . GLN B  1 342  ? -7.104  15.439  101.222 1.00 22.84 ? 340  GLN B CG    1 
ATOM   11186 C CD    . GLN B  1 342  ? -5.755  15.783  100.615 1.00 24.53 ? 340  GLN B CD    1 
ATOM   11187 O OE1   . GLN B  1 342  ? -5.286  15.104  99.704  1.00 23.04 ? 340  GLN B OE1   1 
ATOM   11188 N NE2   . GLN B  1 342  ? -5.117  16.843  101.123 1.00 22.23 ? 340  GLN B NE2   1 
ATOM   11189 N N     . ALA B  1 343  ? -11.582 14.409  99.878  1.00 24.55 ? 341  ALA B N     1 
ATOM   11190 C CA    . ALA B  1 343  ? -12.728 14.265  98.984  1.00 25.03 ? 341  ALA B CA    1 
ATOM   11191 C C     . ALA B  1 343  ? -12.764 15.343  97.916  1.00 26.40 ? 341  ALA B C     1 
ATOM   11192 O O     . ALA B  1 343  ? -13.432 15.152  96.888  1.00 24.36 ? 341  ALA B O     1 
ATOM   11193 C CB    . ALA B  1 343  ? -14.038 14.301  99.772  1.00 27.22 ? 341  ALA B CB    1 
ATOM   11194 N N     . TYR B  1 344  ? -12.079 16.473  98.134  1.00 25.71 ? 342  TYR B N     1 
ATOM   11195 C CA    . TYR B  1 344  ? -12.006 17.437  97.044  1.00 25.22 ? 342  TYR B CA    1 
ATOM   11196 C C     . TYR B  1 344  ? -11.110 16.967  95.916  1.00 25.30 ? 342  TYR B C     1 
ATOM   11197 O O     . TYR B  1 344  ? -11.043 17.653  94.899  1.00 25.82 ? 342  TYR B O     1 
ATOM   11198 C CB    . TYR B  1 344  ? -11.563 18.833  97.533  1.00 22.70 ? 342  TYR B CB    1 
ATOM   11199 C CG    . TYR B  1 344  ? -10.110 19.110  97.935  1.00 23.45 ? 342  TYR B CG    1 
ATOM   11200 C CD1   . TYR B  1 344  ? -9.140  18.116  98.010  1.00 25.01 ? 342  TYR B CD1   1 
ATOM   11201 C CD2   . TYR B  1 344  ? -9.729  20.413  98.267  1.00 23.89 ? 342  TYR B CD2   1 
ATOM   11202 C CE1   . TYR B  1 344  ? -7.822  18.427  98.407  1.00 22.98 ? 342  TYR B CE1   1 
ATOM   11203 C CE2   . TYR B  1 344  ? -8.440  20.725  98.655  1.00 23.45 ? 342  TYR B CE2   1 
ATOM   11204 C CZ    . TYR B  1 344  ? -7.494  19.740  98.724  1.00 22.74 ? 342  TYR B CZ    1 
ATOM   11205 O OH    . TYR B  1 344  ? -6.222  20.087  99.131  1.00 21.49 ? 342  TYR B OH    1 
ATOM   11206 N N     . GLY B  1 345  ? -10.454 15.818  96.059  1.00 24.67 ? 343  GLY B N     1 
ATOM   11207 C CA    . GLY B  1 345  ? -9.562  15.317  95.031  1.00 22.77 ? 343  GLY B CA    1 
ATOM   11208 C C     . GLY B  1 345  ? -10.280 14.353  94.097  1.00 22.89 ? 343  GLY B C     1 
ATOM   11209 O O     . GLY B  1 345  ? -11.083 13.533  94.525  1.00 23.87 ? 343  GLY B O     1 
ATOM   11210 N N     . LYS B  1 346  ? -9.935  14.447  92.817  1.00 22.52 ? 344  LYS B N     1 
ATOM   11211 C CA    . LYS B  1 346  ? -10.576 13.633  91.794  1.00 22.91 ? 344  LYS B CA    1 
ATOM   11212 C C     . LYS B  1 346  ? -10.222 12.161  91.924  1.00 25.82 ? 344  LYS B C     1 
ATOM   11213 O O     . LYS B  1 346  ? -10.939 11.307  91.390  1.00 25.95 ? 344  LYS B O     1 
ATOM   11214 C CB    . LYS B  1 346  ? -10.164 14.147  90.425  1.00 23.64 ? 344  LYS B CB    1 
ATOM   11215 C CG    . LYS B  1 346  ? -10.628 15.568  90.169  1.00 24.60 ? 344  LYS B CG    1 
ATOM   11216 C CD    . LYS B  1 346  ? -10.119 16.075  88.845  1.00 22.10 ? 344  LYS B CD    1 
ATOM   11217 C CE    . LYS B  1 346  ? -10.844 17.349  88.453  1.00 27.98 ? 344  LYS B CE    1 
ATOM   11218 N NZ    . LYS B  1 346  ? -10.223 18.016  87.274  1.00 25.49 ? 344  LYS B NZ    1 
ATOM   11219 N N     . ARG B  1 347  ? -9.144  11.845  92.625  1.00 24.64 ? 345  ARG B N     1 
ATOM   11220 C CA    . ARG B  1 347  ? -8.725  10.460  92.741  1.00 25.12 ? 345  ARG B CA    1 
ATOM   11221 C C     . ARG B  1 347  ? -9.338  9.746   93.937  1.00 26.82 ? 345  ARG B C     1 
ATOM   11222 O O     . ARG B  1 347  ? -9.189  8.527   94.034  1.00 25.06 ? 345  ARG B O     1 
ATOM   11223 C CB    . ARG B  1 347  ? -7.194  10.377  92.819  1.00 26.72 ? 345  ARG B CB    1 
ATOM   11224 C CG    . ARG B  1 347  ? -6.503  10.771  91.492  1.00 22.77 ? 345  ARG B CG    1 
ATOM   11225 C CD    . ARG B  1 347  ? -5.033  11.001  91.684  1.00 24.43 ? 345  ARG B CD    1 
ATOM   11226 N NE    . ARG B  1 347  ? -4.763  12.225  92.441  1.00 21.77 ? 345  ARG B NE    1 
ATOM   11227 C CZ    . ARG B  1 347  ? -3.581  12.566  92.933  1.00 24.31 ? 345  ARG B CZ    1 
ATOM   11228 N NH1   . ARG B  1 347  ? -2.520  11.789  92.783  1.00 23.40 ? 345  ARG B NH1   1 
ATOM   11229 N NH2   . ARG B  1 347  ? -3.456  13.730  93.572  1.00 20.97 ? 345  ARG B NH2   1 
ATOM   11230 N N     . CYS B  1 348  ? -10.045 10.464  94.822  1.00 24.59 ? 346  CYS B N     1 
ATOM   11231 C CA    . CYS B  1 348  ? -10.508 9.968   96.114  1.00 27.04 ? 346  CYS B CA    1 
ATOM   11232 C C     . CYS B  1 348  ? -11.182 8.597   96.047  1.00 29.93 ? 346  CYS B C     1 
ATOM   11233 O O     . CYS B  1 348  ? -10.750 7.684   96.753  1.00 28.40 ? 346  CYS B O     1 
ATOM   11234 C CB    . CYS B  1 348  ? -11.449 10.997  96.755  1.00 28.15 ? 346  CYS B CB    1 
ATOM   11235 S SG    . CYS B  1 348  ? -11.679 10.752  98.549  1.00 36.23 ? 346  CYS B SG    1 
ATOM   11236 N N     . PRO B  1 349  ? -12.229 8.384   95.243  1.00 26.46 ? 347  PRO B N     1 
ATOM   11237 C CA    . PRO B  1 349  ? -12.861 7.058   95.274  1.00 27.37 ? 347  PRO B CA    1 
ATOM   11238 C C     . PRO B  1 349  ? -11.920 5.944   94.858  1.00 28.12 ? 347  PRO B C     1 
ATOM   11239 O O     . PRO B  1 349  ? -12.035 4.824   95.379  1.00 29.29 ? 347  PRO B O     1 
ATOM   11240 C CB    . PRO B  1 349  ? -14.042 7.200   94.305  1.00 28.27 ? 347  PRO B CB    1 
ATOM   11241 C CG    . PRO B  1 349  ? -13.698 8.373   93.455  1.00 27.64 ? 347  PRO B CG    1 
ATOM   11242 C CD    . PRO B  1 349  ? -12.878 9.286   94.275  1.00 27.94 ? 347  PRO B CD    1 
ATOM   11243 N N     . PHE B  1 350  ? -10.996 6.213   93.930  1.00 26.84 ? 348  PHE B N     1 
ATOM   11244 C CA    . PHE B  1 350  ? -10.062 5.178   93.502  1.00 28.37 ? 348  PHE B CA    1 
ATOM   11245 C C     . PHE B  1 350  ? -8.982  4.946   94.550  1.00 28.05 ? 348  PHE B C     1 
ATOM   11246 O O     . PHE B  1 350  ? -8.528  3.807   94.733  1.00 27.39 ? 348  PHE B O     1 
ATOM   11247 C CB    . PHE B  1 350  ? -9.461  5.548   92.147  1.00 26.37 ? 348  PHE B CB    1 
ATOM   11248 C CG    . PHE B  1 350  ? -10.507 5.958   91.142  1.00 29.07 ? 348  PHE B CG    1 
ATOM   11249 C CD1   . PHE B  1 350  ? -11.251 5.004   90.478  1.00 33.28 ? 348  PHE B CD1   1 
ATOM   11250 C CD2   . PHE B  1 350  ? -10.785 7.303   90.921  1.00 29.47 ? 348  PHE B CD2   1 
ATOM   11251 C CE1   . PHE B  1 350  ? -12.250 5.373   89.570  1.00 29.67 ? 348  PHE B CE1   1 
ATOM   11252 C CE2   . PHE B  1 350  ? -11.775 7.680   90.015  1.00 30.99 ? 348  PHE B CE2   1 
ATOM   11253 C CZ    . PHE B  1 350  ? -12.505 6.714   89.344  1.00 31.57 ? 348  PHE B CZ    1 
ATOM   11254 N N     . VAL B  1 351  ? -8.605  5.993   95.284  1.00 28.78 ? 349  VAL B N     1 
ATOM   11255 C CA    . VAL B  1 351  ? -7.688  5.801   96.409  1.00 26.33 ? 349  VAL B CA    1 
ATOM   11256 C C     . VAL B  1 351  ? -8.338  4.933   97.487  1.00 30.28 ? 349  VAL B C     1 
ATOM   11257 O O     . VAL B  1 351  ? -7.701  4.032   98.046  1.00 28.82 ? 349  VAL B O     1 
ATOM   11258 C CB    . VAL B  1 351  ? -7.234  7.161   96.970  1.00 28.83 ? 349  VAL B CB    1 
ATOM   11259 C CG1   . VAL B  1 351  ? -6.340  6.955   98.199  1.00 25.85 ? 349  VAL B CG1   1 
ATOM   11260 C CG2   . VAL B  1 351  ? -6.502  7.968   95.905  1.00 26.15 ? 349  VAL B CG2   1 
ATOM   11261 N N     . LEU B  1 352  ? -9.609  5.195   97.801  1.00 27.58 ? 350  LEU B N     1 
ATOM   11262 C CA    . LEU B  1 352  ? -10.337 4.352   98.742  1.00 28.49 ? 350  LEU B CA    1 
ATOM   11263 C C     . LEU B  1 352  ? -10.417 2.903   98.262  1.00 31.23 ? 350  LEU B C     1 
ATOM   11264 O O     . LEU B  1 352  ? -10.275 1.976   99.063  1.00 33.41 ? 350  LEU B O     1 
ATOM   11265 C CB    . LEU B  1 352  ? -11.740 4.916   98.977  1.00 30.94 ? 350  LEU B CB    1 
ATOM   11266 C CG    . LEU B  1 352  ? -11.763 6.255   99.709  1.00 32.82 ? 350  LEU B CG    1 
ATOM   11267 C CD1   . LEU B  1 352  ? -13.160 6.774   99.800  1.00 32.21 ? 350  LEU B CD1   1 
ATOM   11268 C CD2   . LEU B  1 352  ? -11.200 6.050   101.108 1.00 29.52 ? 350  LEU B CD2   1 
ATOM   11269 N N     . ASP B  1 353  ? -10.680 2.686   96.970  1.00 30.50 ? 351  ASP B N     1 
ATOM   11270 C CA    . ASP B  1 353  ? -10.624 1.331   96.420  1.00 36.31 ? 351  ASP B CA    1 
ATOM   11271 C C     . ASP B  1 353  ? -9.284  0.676   96.728  1.00 33.91 ? 351  ASP B C     1 
ATOM   11272 O O     . ASP B  1 353  ? -9.225  -0.484  97.159  1.00 34.38 ? 351  ASP B O     1 
ATOM   11273 C CB    . ASP B  1 353  ? -10.842 1.348   94.903  1.00 31.41 ? 351  ASP B CB    1 
ATOM   11274 C CG    . ASP B  1 353  ? -12.279 1.600   94.508  1.00 37.72 ? 351  ASP B CG    1 
ATOM   11275 O OD1   . ASP B  1 353  ? -13.183 1.429   95.358  1.00 36.98 ? 351  ASP B OD1   1 
ATOM   11276 O OD2   . ASP B  1 353  ? -12.489 1.965   93.326  1.00 36.19 ? 351  ASP B OD2   1 
ATOM   11277 N N     . PHE B  1 354  ? -8.192  1.409   96.490  1.00 31.40 ? 352  PHE B N     1 
ATOM   11278 C CA    . PHE B  1 354  ? -6.865  0.862   96.740  1.00 33.84 ? 352  PHE B CA    1 
ATOM   11279 C C     . PHE B  1 354  ? -6.668  0.558   98.222  1.00 33.97 ? 352  PHE B C     1 
ATOM   11280 O O     . PHE B  1 354  ? -6.157  -0.512  98.580  1.00 33.91 ? 352  PHE B O     1 
ATOM   11281 C CB    . PHE B  1 354  ? -5.784  1.825   96.235  1.00 30.69 ? 352  PHE B CB    1 
ATOM   11282 C CG    . PHE B  1 354  ? -4.424  1.526   96.789  1.00 28.93 ? 352  PHE B CG    1 
ATOM   11283 C CD1   . PHE B  1 354  ? -3.649  0.528   96.231  1.00 34.45 ? 352  PHE B CD1   1 
ATOM   11284 C CD2   . PHE B  1 354  ? -3.939  2.206   97.895  1.00 31.07 ? 352  PHE B CD2   1 
ATOM   11285 C CE1   . PHE B  1 354  ? -2.409  0.215   96.758  1.00 35.36 ? 352  PHE B CE1   1 
ATOM   11286 C CE2   . PHE B  1 354  ? -2.702  1.901   98.425  1.00 34.93 ? 352  PHE B CE2   1 
ATOM   11287 C CZ    . PHE B  1 354  ? -1.934  0.905   97.852  1.00 33.94 ? 352  PHE B CZ    1 
ATOM   11288 N N     . ILE B  1 355  ? -7.094  1.475   99.100  1.00 31.80 ? 353  ILE B N     1 
ATOM   11289 C CA    . ILE B  1 355  ? -6.896  1.283   100.540 1.00 32.51 ? 353  ILE B CA    1 
ATOM   11290 C C     . ILE B  1 355  ? -7.763  0.145   101.074 1.00 35.20 ? 353  ILE B C     1 
ATOM   11291 O O     . ILE B  1 355  ? -7.328  -0.633  101.938 1.00 31.68 ? 353  ILE B O     1 
ATOM   11292 C CB    . ILE B  1 355  ? -7.167  2.596   101.297 1.00 28.93 ? 353  ILE B CB    1 
ATOM   11293 C CG1   . ILE B  1 355  ? -6.156  3.666   100.877 1.00 27.85 ? 353  ILE B CG1   1 
ATOM   11294 C CG2   . ILE B  1 355  ? -7.115  2.361   102.809 1.00 32.08 ? 353  ILE B CG2   1 
ATOM   11295 C CD1   . ILE B  1 355  ? -6.406  5.012   101.498 1.00 27.77 ? 353  ILE B CD1   1 
ATOM   11296 N N     . ILE B  1 356  ? -9.008  0.029   100.589 1.00 31.37 ? 354  ILE B N     1 
ATOM   11297 C CA    . ILE B  1 356  ? -9.859  -1.070  101.047 1.00 34.89 ? 354  ILE B CA    1 
ATOM   11298 C C     . ILE B  1 356  ? -9.264  -2.406  100.622 1.00 33.79 ? 354  ILE B C     1 
ATOM   11299 O O     . ILE B  1 356  ? -9.239  -3.371  101.397 1.00 36.51 ? 354  ILE B O     1 
ATOM   11300 C CB    . ILE B  1 356  ? -11.298 -0.895  100.523 1.00 37.59 ? 354  ILE B CB    1 
ATOM   11301 C CG1   . ILE B  1 356  ? -12.009 0.230   101.276 1.00 35.43 ? 354  ILE B CG1   1 
ATOM   11302 C CG2   . ILE B  1 356  ? -12.076 -2.196  100.646 1.00 38.72 ? 354  ILE B CG2   1 
ATOM   11303 C CD1   . ILE B  1 356  ? -13.182 0.822   100.519 1.00 39.38 ? 354  ILE B CD1   1 
ATOM   11304 N N     . ASP B  1 357  ? -8.760  -2.481  99.389  1.00 33.92 ? 355  ASP B N     1 
ATOM   11305 C CA    . ASP B  1 357  ? -8.087  -3.697  98.946  1.00 36.94 ? 355  ASP B CA    1 
ATOM   11306 C C     . ASP B  1 357  ? -6.837  -3.971  99.777  1.00 37.26 ? 355  ASP B C     1 
ATOM   11307 O O     . ASP B  1 357  ? -6.559  -5.122  100.129 1.00 34.81 ? 355  ASP B O     1 
ATOM   11308 C CB    . ASP B  1 357  ? -7.732  -3.585  97.467  1.00 38.16 ? 355  ASP B CB    1 
ATOM   11309 C CG    . ASP B  1 357  ? -6.910  -4.756  96.974  1.00 38.02 ? 355  ASP B CG    1 
ATOM   11310 O OD1   . ASP B  1 357  ? -7.455  -5.877  96.907  1.00 42.22 ? 355  ASP B OD1   1 
ATOM   11311 O OD2   . ASP B  1 357  ? -5.720  -4.554  96.641  1.00 40.80 ? 355  ASP B OD2   1 
ATOM   11312 N N     . LEU B  1 358  ? -6.065  -2.926  100.089 1.00 34.08 ? 356  LEU B N     1 
ATOM   11313 C CA    . LEU B  1 358  ? -4.852  -3.114  100.882 1.00 34.86 ? 356  LEU B CA    1 
ATOM   11314 C C     . LEU B  1 358  ? -5.184  -3.646  102.267 1.00 35.52 ? 356  LEU B C     1 
ATOM   11315 O O     . LEU B  1 358  ? -4.483  -4.516  102.794 1.00 39.92 ? 356  LEU B O     1 
ATOM   11316 C CB    . LEU B  1 358  ? -4.085  -1.799  100.973 1.00 30.61 ? 356  LEU B CB    1 
ATOM   11317 C CG    . LEU B  1 358  ? -2.908  -1.712  101.960 1.00 32.43 ? 356  LEU B CG    1 
ATOM   11318 C CD1   . LEU B  1 358  ? -1.889  -2.785  101.680 1.00 31.35 ? 356  LEU B CD1   1 
ATOM   11319 C CD2   . LEU B  1 358  ? -2.247  -0.330  101.845 1.00 29.90 ? 356  LEU B CD2   1 
ATOM   11320 N N     . ALA B  1 359  ? -6.260  -3.138  102.868 1.00 32.41 ? 357  ALA B N     1 
ATOM   11321 C CA    . ALA B  1 359  ? -6.677  -3.619  104.174 1.00 37.32 ? 357  ALA B CA    1 
ATOM   11322 C C     . ALA B  1 359  ? -7.109  -5.074  104.100 1.00 40.95 ? 357  ALA B C     1 
ATOM   11323 O O     . ALA B  1 359  ? -6.874  -5.852  105.031 1.00 39.88 ? 357  ALA B O     1 
ATOM   11324 C CB    . ALA B  1 359  ? -7.811  -2.743  104.701 1.00 36.29 ? 357  ALA B CB    1 
ATOM   11325 N N     . ARG B  1 360  ? -7.732  -5.465  102.986 1.00 35.62 ? 358  ARG B N     1 
ATOM   11326 C CA    . ARG B  1 360  ? -8.188  -6.842  102.854 1.00 40.59 ? 358  ARG B CA    1 
ATOM   11327 C C     . ARG B  1 360  ? -7.020  -7.807  102.763 1.00 36.17 ? 358  ARG B C     1 
ATOM   11328 O O     . ARG B  1 360  ? -7.034  -8.858  103.409 1.00 41.70 ? 358  ARG B O     1 
ATOM   11329 C CB    . ARG B  1 360  ? -9.096  -6.982  101.632 1.00 38.36 ? 358  ARG B CB    1 
ATOM   11330 C CG    . ARG B  1 360  ? -10.484 -6.443  101.853 1.00 40.72 ? 358  ARG B CG    1 
ATOM   11331 C CD    . ARG B  1 360  ? -11.375 -6.776  100.671 1.00 47.33 ? 358  ARG B CD    1 
ATOM   11332 N NE    . ARG B  1 360  ? -12.726 -6.259  100.851 1.00 50.20 ? 358  ARG B NE    1 
ATOM   11333 C CZ    . ARG B  1 360  ? -13.314 -5.400  100.030 1.00 50.25 ? 358  ARG B CZ    1 
ATOM   11334 N NH1   . ARG B  1 360  ? -12.702 -4.951  98.945  1.00 52.55 ? 358  ARG B NH1   1 
ATOM   11335 N NH2   . ARG B  1 360  ? -14.553 -4.994  100.294 1.00 54.16 ? 358  ARG B NH2   1 
ATOM   11336 N N     . ARG B  1 361  ? -5.993  -7.472  101.983 1.00 37.11 ? 359  ARG B N     1 
ATOM   11337 C CA    . ARG B  1 361  ? -4.905  -8.421  101.786 1.00 45.26 ? 359  ARG B CA    1 
ATOM   11338 C C     . ARG B  1 361  ? -3.838  -8.344  102.865 1.00 43.97 ? 359  ARG B C     1 
ATOM   11339 O O     . ARG B  1 361  ? -3.060  -9.295  103.008 1.00 41.16 ? 359  ARG B O     1 
ATOM   11340 C CB    . ARG B  1 361  ? -4.258  -8.228  100.411 1.00 45.85 ? 359  ARG B CB    1 
ATOM   11341 C CG    . ARG B  1 361  ? -3.900  -6.813  100.063 1.00 43.42 ? 359  ARG B CG    1 
ATOM   11342 C CD    . ARG B  1 361  ? -3.644  -6.679  98.555  1.00 40.51 ? 359  ARG B CD    1 
ATOM   11343 N NE    . ARG B  1 361  ? -3.408  -5.286  98.189  1.00 37.85 ? 359  ARG B NE    1 
ATOM   11344 C CZ    . ARG B  1 361  ? -2.239  -4.664  98.273  1.00 36.51 ? 359  ARG B CZ    1 
ATOM   11345 N NH1   . ARG B  1 361  ? -1.146  -5.295  98.666  1.00 33.92 ? 359  ARG B NH1   1 
ATOM   11346 N NH2   . ARG B  1 361  ? -2.168  -3.372  97.965  1.00 32.81 ? 359  ARG B NH2   1 
ATOM   11347 N N     . SER B  1 362  ? -3.782  -7.247  103.619 1.00 37.15 ? 360  SER B N     1 
ATOM   11348 C CA    . SER B  1 362  ? -2.840  -7.129  104.722 1.00 37.46 ? 360  SER B CA    1 
ATOM   11349 C C     . SER B  1 362  ? -3.401  -7.616  106.045 1.00 40.61 ? 360  SER B C     1 
ATOM   11350 O O     . SER B  1 362  ? -2.622  -7.839  106.979 1.00 42.14 ? 360  SER B O     1 
ATOM   11351 C CB    . SER B  1 362  ? -2.404  -5.672  104.895 1.00 37.57 ? 360  SER B CB    1 
ATOM   11352 O OG    . SER B  1 362  ? -3.520  -4.877  105.255 1.00 35.96 ? 360  SER B OG    1 
ATOM   11353 N N     . GLY B  1 363  ? -4.719  -7.757  106.164 1.00 35.84 ? 361  GLY B N     1 
ATOM   11354 C CA    . GLY B  1 363  ? -5.313  -8.069  107.450 1.00 37.14 ? 361  GLY B CA    1 
ATOM   11355 C C     . GLY B  1 363  ? -5.202  -6.960  108.472 1.00 36.92 ? 361  GLY B C     1 
ATOM   11356 O O     . GLY B  1 363  ? -5.149  -7.234  109.676 1.00 41.85 ? 361  GLY B O     1 
ATOM   11357 N N     . ARG B  1 364  ? -5.128  -5.713  108.019 1.00 40.62 ? 362  ARG B N     1 
ATOM   11358 C CA    . ARG B  1 364  ? -5.152  -4.529  108.872 1.00 42.97 ? 362  ARG B CA    1 
ATOM   11359 C C     . ARG B  1 364  ? -6.481  -3.822  108.660 1.00 40.80 ? 362  ARG B C     1 
ATOM   11360 O O     . ARG B  1 364  ? -6.851  -3.546  107.518 1.00 41.04 ? 362  ARG B O     1 
ATOM   11361 C CB    . ARG B  1 364  ? -4.018  -3.557  108.520 1.00 38.87 ? 362  ARG B CB    1 
ATOM   11362 C CG    . ARG B  1 364  ? -2.613  -4.121  108.565 1.00 40.12 ? 362  ARG B CG    1 
ATOM   11363 C CD    . ARG B  1 364  ? -2.095  -4.244  109.996 1.00 39.31 ? 362  ARG B CD    1 
ATOM   11364 N NE    . ARG B  1 364  ? -0.912  -5.094  110.038 1.00 38.21 ? 362  ARG B NE    1 
ATOM   11365 C CZ    . ARG B  1 364  ? 0.315   -4.673  109.764 1.00 36.75 ? 362  ARG B CZ    1 
ATOM   11366 N NH1   . ARG B  1 364  ? 0.561   -3.407  109.464 1.00 35.87 ? 362  ARG B NH1   1 
ATOM   11367 N NH2   . ARG B  1 364  ? 1.320   -5.545  109.784 1.00 41.13 ? 362  ARG B NH2   1 
ATOM   11368 N N     . ARG B  1 365  ? -7.193  -3.522  109.738 1.00 36.59 ? 363  ARG B N     1 
ATOM   11369 C CA    . ARG B  1 365  ? -8.362  -2.657  109.608 1.00 34.63 ? 363  ARG B CA    1 
ATOM   11370 C C     . ARG B  1 365  ? -7.870  -1.215  109.597 1.00 34.64 ? 363  ARG B C     1 
ATOM   11371 O O     . ARG B  1 365  ? -7.612  -0.630  110.648 1.00 39.57 ? 363  ARG B O     1 
ATOM   11372 C CB    . ARG B  1 365  ? -9.361  -2.898  110.728 1.00 40.31 ? 363  ARG B CB    1 
ATOM   11373 C CG    . ARG B  1 365  ? -10.584 -2.006  110.627 1.00 38.72 ? 363  ARG B CG    1 
ATOM   11374 C CD    . ARG B  1 365  ? -11.817 -2.705  111.183 1.00 46.79 ? 363  ARG B CD    1 
ATOM   11375 N NE    . ARG B  1 365  ? -13.022 -1.902  111.017 1.00 45.68 ? 363  ARG B NE    1 
ATOM   11376 C CZ    . ARG B  1 365  ? -13.509 -1.090  111.944 1.00 45.72 ? 363  ARG B CZ    1 
ATOM   11377 N NH1   . ARG B  1 365  ? -12.932 -0.970  113.130 1.00 42.06 ? 363  ARG B NH1   1 
ATOM   11378 N NH2   . ARG B  1 365  ? -14.602 -0.383  111.678 1.00 43.51 ? 363  ARG B NH2   1 
ATOM   11379 N N     . ILE B  1 366  ? -7.738  -0.638  108.405 1.00 35.04 ? 364  ILE B N     1 
ATOM   11380 C CA    . ILE B  1 366  ? -7.109  0.671   108.253 1.00 34.30 ? 364  ILE B CA    1 
ATOM   11381 C C     . ILE B  1 366  ? -8.093  1.756   108.664 1.00 36.21 ? 364  ILE B C     1 
ATOM   11382 O O     . ILE B  1 366  ? -9.255  1.751   108.246 1.00 34.77 ? 364  ILE B O     1 
ATOM   11383 C CB    . ILE B  1 366  ? -6.623  0.873   106.809 1.00 31.03 ? 364  ILE B CB    1 
ATOM   11384 C CG1   . ILE B  1 366  ? -5.581  -0.190  106.469 1.00 35.05 ? 364  ILE B CG1   1 
ATOM   11385 C CG2   . ILE B  1 366  ? -6.089  2.296   106.593 1.00 29.97 ? 364  ILE B CG2   1 
ATOM   11386 C CD1   . ILE B  1 366  ? -5.108  -0.167  105.044 1.00 33.52 ? 364  ILE B CD1   1 
ATOM   11387 N N     . MET B  1 367  ? -7.634  2.686   109.499 1.00 31.14 ? 365  MET B N     1 
ATOM   11388 C CA    . MET B  1 367  ? -8.431  3.851   109.864 1.00 30.92 ? 365  MET B CA    1 
ATOM   11389 C C     . MET B  1 367  ? -8.358  4.875   108.737 1.00 31.48 ? 365  MET B C     1 
ATOM   11390 O O     . MET B  1 367  ? -7.268  5.316   108.365 1.00 30.30 ? 365  MET B O     1 
ATOM   11391 C CB    . MET B  1 367  ? -7.927  4.438   111.179 1.00 32.83 ? 365  MET B CB    1 
ATOM   11392 C CG    . MET B  1 367  ? -7.835  3.396   112.268 1.00 32.35 ? 365  MET B CG    1 
ATOM   11393 S SD    . MET B  1 367  ? -7.073  4.003   113.791 1.00 42.19 ? 365  MET B SD    1 
ATOM   11394 C CE    . MET B  1 367  ? -8.428  4.936   114.504 1.00 38.62 ? 365  MET B CE    1 
ATOM   11395 N N     . VAL B  1 368  ? -9.504  5.232   108.163 1.00 30.47 ? 366  VAL B N     1 
ATOM   11396 C CA    . VAL B  1 368  ? -9.541  6.134   107.014 1.00 29.31 ? 366  VAL B CA    1 
ATOM   11397 C C     . VAL B  1 368  ? -10.264 7.403   107.432 1.00 30.89 ? 366  VAL B C     1 
ATOM   11398 O O     . VAL B  1 368  ? -11.478 7.378   107.683 1.00 32.82 ? 366  VAL B O     1 
ATOM   11399 C CB    . VAL B  1 368  ? -10.228 5.506   105.792 1.00 29.56 ? 366  VAL B CB    1 
ATOM   11400 C CG1   . VAL B  1 368  ? -10.084 6.445   104.613 1.00 29.09 ? 366  VAL B CG1   1 
ATOM   11401 C CG2   . VAL B  1 368  ? -9.626  4.164   105.467 1.00 34.09 ? 366  VAL B CG2   1 
ATOM   11402 N N     . ARG B  1 369  ? -9.540  8.521   107.477 1.00 28.29 ? 367  ARG B N     1 
ATOM   11403 C CA    . ARG B  1 369  ? -10.163 9.804   107.774 1.00 28.04 ? 367  ARG B CA    1 
ATOM   11404 C C     . ARG B  1 369  ? -10.515 10.448  106.445 1.00 27.50 ? 367  ARG B C     1 
ATOM   11405 O O     . ARG B  1 369  ? -9.626  10.785  105.664 1.00 28.14 ? 367  ARG B O     1 
ATOM   11406 C CB    . ARG B  1 369  ? -9.254  10.720  108.593 1.00 29.23 ? 367  ARG B CB    1 
ATOM   11407 C CG    . ARG B  1 369  ? -9.901  12.093  108.867 1.00 27.28 ? 367  ARG B CG    1 
ATOM   11408 C CD    . ARG B  1 369  ? -8.879  13.163  109.226 1.00 28.39 ? 367  ARG B CD    1 
ATOM   11409 N NE    . ARG B  1 369  ? -8.206  12.857  110.486 1.00 28.19 ? 367  ARG B NE    1 
ATOM   11410 C CZ    . ARG B  1 369  ? -6.995  13.291  110.801 1.00 29.41 ? 367  ARG B CZ    1 
ATOM   11411 N NH1   . ARG B  1 369  ? -6.286  14.026  109.959 1.00 27.72 ? 367  ARG B NH1   1 
ATOM   11412 N NH2   . ARG B  1 369  ? -6.482  12.980  111.992 1.00 27.04 ? 367  ARG B NH2   1 
ATOM   11413 N N     . LEU B  1 370  ? -11.809 10.600  106.186 1.00 27.89 ? 368  LEU B N     1 
ATOM   11414 C CA    . LEU B  1 370  ? -12.280 11.274  104.987 1.00 27.91 ? 368  LEU B CA    1 
ATOM   11415 C C     . LEU B  1 370  ? -12.441 12.750  105.305 1.00 26.99 ? 368  LEU B C     1 
ATOM   11416 O O     . LEU B  1 370  ? -13.186 13.111  106.216 1.00 28.64 ? 368  LEU B O     1 
ATOM   11417 C CB    . LEU B  1 370  ? -13.606 10.679  104.528 1.00 28.16 ? 368  LEU B CB    1 
ATOM   11418 C CG    . LEU B  1 370  ? -14.256 11.263  103.271 1.00 31.08 ? 368  LEU B CG    1 
ATOM   11419 C CD1   . LEU B  1 370  ? -13.503 10.888  102.003 1.00 28.98 ? 368  LEU B CD1   1 
ATOM   11420 C CD2   . LEU B  1 370  ? -15.672 10.750  103.220 1.00 31.39 ? 368  LEU B CD2   1 
ATOM   11421 N N     . VAL B  1 371  ? -11.745 13.602  104.561 1.00 26.15 ? 369  VAL B N     1 
ATOM   11422 C CA    . VAL B  1 371  ? -11.847 15.042  104.726 1.00 25.68 ? 369  VAL B CA    1 
ATOM   11423 C C     . VAL B  1 371  ? -12.240 15.633  103.392 1.00 26.88 ? 369  VAL B C     1 
ATOM   11424 O O     . VAL B  1 371  ? -12.311 14.940  102.380 1.00 28.72 ? 369  VAL B O     1 
ATOM   11425 C CB    . VAL B  1 371  ? -10.528 15.674  105.208 1.00 25.05 ? 369  VAL B CB    1 
ATOM   11426 C CG1   . VAL B  1 371  ? -10.027 14.961  106.451 1.00 25.47 ? 369  VAL B CG1   1 
ATOM   11427 C CG2   . VAL B  1 371  ? -9.475  15.659  104.081 1.00 24.33 ? 369  VAL B CG2   1 
ATOM   11428 N N     . LYS B  1 372  ? -12.474 16.939  103.390 1.00 24.89 ? 370  LYS B N     1 
ATOM   11429 C CA    . LYS B  1 372  ? -12.636 17.587  102.097 1.00 26.45 ? 370  LYS B CA    1 
ATOM   11430 C C     . LYS B  1 372  ? -11.275 18.010  101.551 1.00 23.55 ? 370  LYS B C     1 
ATOM   11431 O O     . LYS B  1 372  ? -10.823 17.456  100.549 1.00 25.25 ? 370  LYS B O     1 
ATOM   11432 C CB    . LYS B  1 372  ? -13.660 18.722  102.205 1.00 25.87 ? 370  LYS B CB    1 
ATOM   11433 C CG    . LYS B  1 372  ? -15.042 18.155  102.565 1.00 28.76 ? 370  LYS B CG    1 
ATOM   11434 C CD    . LYS B  1 372  ? -16.186 19.143  102.424 1.00 29.87 ? 370  LYS B CD    1 
ATOM   11435 C CE    . LYS B  1 372  ? -17.476 18.524  102.984 1.00 35.97 ? 370  LYS B CE    1 
ATOM   11436 N NZ    . LYS B  1 372  ? -18.495 19.552  103.332 1.00 27.69 ? 370  LYS B NZ    1 
ATOM   11437 N N     . GLY B  1 373  ? -10.559 18.908  102.239 1.00 25.61 ? 371  GLY B N     1 
ATOM   11438 C CA    . GLY B  1 373  ? -9.199  19.203  101.808 1.00 24.55 ? 371  GLY B CA    1 
ATOM   11439 C C     . GLY B  1 373  ? -8.724  20.610  102.116 1.00 25.65 ? 371  GLY B C     1 
ATOM   11440 O O     . GLY B  1 373  ? -9.482  21.568  101.948 1.00 27.50 ? 371  GLY B O     1 
ATOM   11441 N N     . ALA B  1 374  ? -7.466  20.748  102.561 1.00 22.80 ? 372  ALA B N     1 
ATOM   11442 C CA    . ALA B  1 374  ? -6.981  21.987  103.149 1.00 22.59 ? 372  ALA B CA    1 
ATOM   11443 C C     . ALA B  1 374  ? -6.142  22.839  102.201 1.00 25.07 ? 372  ALA B C     1 
ATOM   11444 O O     . ALA B  1 374  ? -5.670  23.909  102.610 1.00 24.45 ? 372  ALA B O     1 
ATOM   11445 C CB    . ALA B  1 374  ? -6.153  21.680  104.410 1.00 26.17 ? 372  ALA B CB    1 
ATOM   11446 N N     . TYR B  1 375  ? -5.923  22.404  100.956 1.00 21.81 ? 373  TYR B N     1 
ATOM   11447 C CA    . TYR B  1 375  ? -4.936  23.055  100.104 1.00 21.96 ? 373  TYR B CA    1 
ATOM   11448 C C     . TYR B  1 375  ? -5.559  23.583  98.821  1.00 19.98 ? 373  TYR B C     1 
ATOM   11449 O O     . TYR B  1 375  ? -4.857  23.745  97.828  1.00 21.18 ? 373  TYR B O     1 
ATOM   11450 C CB    . TYR B  1 375  ? -3.787  22.107  99.758  1.00 19.36 ? 373  TYR B CB    1 
ATOM   11451 C CG    . TYR B  1 375  ? -3.052  21.524  100.945 1.00 21.95 ? 373  TYR B CG    1 
ATOM   11452 C CD1   . TYR B  1 375  ? -3.587  20.449  101.653 1.00 21.21 ? 373  TYR B CD1   1 
ATOM   11453 C CD2   . TYR B  1 375  ? -1.829  22.038  101.350 1.00 25.35 ? 373  TYR B CD2   1 
ATOM   11454 C CE1   . TYR B  1 375  ? -2.916  19.909  102.740 1.00 23.44 ? 373  TYR B CE1   1 
ATOM   11455 C CE2   . TYR B  1 375  ? -1.153  21.496  102.429 1.00 26.86 ? 373  TYR B CE2   1 
ATOM   11456 C CZ    . TYR B  1 375  ? -1.704  20.436  103.117 1.00 26.72 ? 373  TYR B CZ    1 
ATOM   11457 O OH    . TYR B  1 375  ? -1.044  19.892  104.198 1.00 25.56 ? 373  TYR B OH    1 
ATOM   11458 N N     . TRP B  1 376  ? -6.862  23.873  98.837  1.00 19.64 ? 374  TRP B N     1 
ATOM   11459 C CA    . TRP B  1 376  ? -7.571  24.094  97.573  1.00 20.17 ? 374  TRP B CA    1 
ATOM   11460 C C     . TRP B  1 376  ? -6.985  25.267  96.790  1.00 19.46 ? 374  TRP B C     1 
ATOM   11461 O O     . TRP B  1 376  ? -6.679  25.137  95.606  1.00 21.14 ? 374  TRP B O     1 
ATOM   11462 C CB    . TRP B  1 376  ? -9.068  24.294  97.832  1.00 20.05 ? 374  TRP B CB    1 
ATOM   11463 C CG    . TRP B  1 376  ? -9.852  24.462  96.550  1.00 22.46 ? 374  TRP B CG    1 
ATOM   11464 C CD1   . TRP B  1 376  ? -10.338 23.476  95.755  1.00 21.88 ? 374  TRP B CD1   1 
ATOM   11465 C CD2   . TRP B  1 376  ? -10.198 25.698  95.917  1.00 24.83 ? 374  TRP B CD2   1 
ATOM   11466 N NE1   . TRP B  1 376  ? -10.985 24.016  94.665  1.00 21.36 ? 374  TRP B NE1   1 
ATOM   11467 C CE2   . TRP B  1 376  ? -10.911 25.380  94.740  1.00 23.44 ? 374  TRP B CE2   1 
ATOM   11468 C CE3   . TRP B  1 376  ? -9.990  27.042  96.240  1.00 25.28 ? 374  TRP B CE3   1 
ATOM   11469 C CZ2   . TRP B  1 376  ? -11.413 26.357  93.879  1.00 22.90 ? 374  TRP B CZ2   1 
ATOM   11470 C CZ3   . TRP B  1 376  ? -10.482 28.017  95.379  1.00 27.08 ? 374  TRP B CZ3   1 
ATOM   11471 C CH2   . TRP B  1 376  ? -11.196 27.667  94.214  1.00 24.99 ? 374  TRP B CH2   1 
ATOM   11472 N N     . ASP B  1 377  ? -6.820  26.423  97.430  1.00 21.35 ? 375  ASP B N     1 
ATOM   11473 C CA    . ASP B  1 377  ? -6.287  27.584  96.716  1.00 23.17 ? 375  ASP B CA    1 
ATOM   11474 C C     . ASP B  1 377  ? -4.914  27.300  96.118  1.00 26.48 ? 375  ASP B C     1 
ATOM   11475 O O     . ASP B  1 377  ? -4.610  27.738  95.004  1.00 21.34 ? 375  ASP B O     1 
ATOM   11476 C CB    . ASP B  1 377  ? -6.199  28.784  97.658  1.00 32.84 ? 375  ASP B CB    1 
ATOM   11477 C CG    . ASP B  1 377  ? -7.552  29.385  97.957  1.00 33.18 ? 375  ASP B CG    1 
ATOM   11478 O OD1   . ASP B  1 377  ? -8.231  29.814  97.001  1.00 39.71 ? 375  ASP B OD1   1 
ATOM   11479 O OD2   . ASP B  1 377  ? -7.946  29.418  99.140  1.00 40.48 ? 375  ASP B OD2   1 
ATOM   11480 N N     . ALA B  1 378  ? -4.055  26.610  96.865  1.00 23.90 ? 376  ALA B N     1 
ATOM   11481 C CA    . ALA B  1 378  ? -2.712  26.329  96.380  1.00 23.92 ? 376  ALA B CA    1 
ATOM   11482 C C     . ALA B  1 378  ? -2.736  25.351  95.215  1.00 22.11 ? 376  ALA B C     1 
ATOM   11483 O O     . ALA B  1 378  ? -1.886  25.445  94.323  1.00 20.33 ? 376  ALA B O     1 
ATOM   11484 C CB    . ALA B  1 378  ? -1.845  25.786  97.520  1.00 23.93 ? 376  ALA B CB    1 
ATOM   11485 N N     . GLU B  1 379  ? -3.697  24.416  95.202  1.00 20.75 ? 377  GLU B N     1 
ATOM   11486 C CA    . GLU B  1 379  ? -3.770  23.449  94.103  1.00 20.58 ? 377  GLU B CA    1 
ATOM   11487 C C     . GLU B  1 379  ? -4.215  24.123  92.810  1.00 20.90 ? 377  GLU B C     1 
ATOM   11488 O O     . GLU B  1 379  ? -3.720  23.788  91.729  1.00 20.70 ? 377  GLU B O     1 
ATOM   11489 C CB    . GLU B  1 379  ? -4.724  22.298  94.438  1.00 19.32 ? 377  GLU B CB    1 
ATOM   11490 C CG    . GLU B  1 379  ? -4.348  21.479  95.672  1.00 20.14 ? 377  GLU B CG    1 
ATOM   11491 C CD    . GLU B  1 379  ? -3.066  20.658  95.497  1.00 25.72 ? 377  GLU B CD    1 
ATOM   11492 O OE1   . GLU B  1 379  ? -2.459  20.669  94.399  1.00 22.48 ? 377  GLU B OE1   1 
ATOM   11493 O OE2   . GLU B  1 379  ? -2.666  19.985  96.474  1.00 24.34 ? 377  GLU B OE2   1 
ATOM   11494 N N     . ILE B  1 380  ? -5.150  25.066  92.906  1.00 20.02 ? 378  ILE B N     1 
ATOM   11495 C CA    . ILE B  1 380  ? -5.572  25.806  91.716  1.00 18.87 ? 378  ILE B CA    1 
ATOM   11496 C C     . ILE B  1 380  ? -4.397  26.590  91.150  1.00 19.12 ? 378  ILE B C     1 
ATOM   11497 O O     . ILE B  1 380  ? -4.075  26.486  89.966  1.00 20.36 ? 378  ILE B O     1 
ATOM   11498 C CB    . ILE B  1 380  ? -6.764  26.726  92.045  1.00 19.49 ? 378  ILE B CB    1 
ATOM   11499 C CG1   . ILE B  1 380  ? -7.953  25.928  92.599  1.00 23.42 ? 378  ILE B CG1   1 
ATOM   11500 C CG2   . ILE B  1 380  ? -7.159  27.566  90.809  1.00 19.56 ? 378  ILE B CG2   1 
ATOM   11501 C CD1   . ILE B  1 380  ? -8.565  24.893  91.634  1.00 20.72 ? 378  ILE B CD1   1 
ATOM   11502 N N     . LYS B  1 381  ? -3.732  27.378  91.995  1.00 19.50 ? 379  LYS B N     1 
ATOM   11503 C CA    . LYS B  1 381  ? -2.582  28.155  91.529  1.00 20.10 ? 379  LYS B CA    1 
ATOM   11504 C C     . LYS B  1 381  ? -1.510  27.265  90.905  1.00 17.75 ? 379  LYS B C     1 
ATOM   11505 O O     . LYS B  1 381  ? -0.956  27.596  89.851  1.00 17.82 ? 379  LYS B O     1 
ATOM   11506 C CB    . LYS B  1 381  ? -1.995  28.958  92.690  1.00 19.06 ? 379  LYS B CB    1 
ATOM   11507 C CG    . LYS B  1 381  ? -0.813  29.797  92.282  1.00 23.29 ? 379  LYS B CG    1 
ATOM   11508 C CD    . LYS B  1 381  ? -0.342  30.685  93.432  1.00 21.12 ? 379  LYS B CD    1 
ATOM   11509 C CE    . LYS B  1 381  ? 0.769   31.639  92.991  1.00 23.07 ? 379  LYS B CE    1 
ATOM   11510 N NZ    . LYS B  1 381  ? 1.237   32.489  94.145  1.00 19.72 ? 379  LYS B NZ    1 
ATOM   11511 N N     . ARG B  1 382  ? -1.206  26.129  91.538  1.00 18.08 ? 380  ARG B N     1 
ATOM   11512 C CA    . ARG B  1 382  ? -0.117  25.271  91.078  1.00 21.64 ? 380  ARG B CA    1 
ATOM   11513 C C     . ARG B  1 382  ? -0.415  24.675  89.706  1.00 19.38 ? 380  ARG B C     1 
ATOM   11514 O O     . ARG B  1 382  ? 0.457   24.635  88.831  1.00 18.57 ? 380  ARG B O     1 
ATOM   11515 C CB    . ARG B  1 382  ? 0.128   24.150  92.098  1.00 24.44 ? 380  ARG B CB    1 
ATOM   11516 C CG    . ARG B  1 382  ? 1.367   23.293  91.822  1.00 29.42 ? 380  ARG B CG    1 
ATOM   11517 C CD    . ARG B  1 382  ? 2.673   24.033  92.120  1.00 30.94 ? 380  ARG B CD    1 
ATOM   11518 N NE    . ARG B  1 382  ? 3.284   24.583  90.915  1.00 34.54 ? 380  ARG B NE    1 
ATOM   11519 C CZ    . ARG B  1 382  ? 4.283   25.458  90.904  1.00 38.47 ? 380  ARG B CZ    1 
ATOM   11520 N NH1   . ARG B  1 382  ? 4.781   25.950  92.027  1.00 41.89 ? 380  ARG B NH1   1 
ATOM   11521 N NH2   . ARG B  1 382  ? 4.788   25.857  89.734  1.00 32.46 ? 380  ARG B NH2   1 
ATOM   11522 N N     . ALA B  1 383  ? -1.624  24.165  89.519  1.00 16.96 ? 381  ALA B N     1 
ATOM   11523 C CA    . ALA B  1 383  ? -1.974  23.592  88.217  1.00 19.97 ? 381  ALA B CA    1 
ATOM   11524 C C     . ALA B  1 383  ? -1.912  24.647  87.114  1.00 19.16 ? 381  ALA B C     1 
ATOM   11525 O O     . ALA B  1 383  ? -1.526  24.354  85.965  1.00 18.20 ? 381  ALA B O     1 
ATOM   11526 C CB    . ALA B  1 383  ? -3.363  22.973  88.284  1.00 20.88 ? 381  ALA B CB    1 
ATOM   11527 N N     . GLN B  1 384  ? -2.291  25.880  87.445  1.00 18.28 ? 382  GLN B N     1 
ATOM   11528 C CA    . GLN B  1 384  ? -2.244  26.957  86.459  1.00 18.91 ? 382  GLN B CA    1 
ATOM   11529 C C     . GLN B  1 384  ? -0.809  27.327  86.123  1.00 19.80 ? 382  GLN B C     1 
ATOM   11530 O O     . GLN B  1 384  ? -0.464  27.450  84.952  1.00 20.23 ? 382  GLN B O     1 
ATOM   11531 C CB    . GLN B  1 384  ? -3.011  28.169  86.964  1.00 18.60 ? 382  GLN B CB    1 
ATOM   11532 C CG    . GLN B  1 384  ? -4.524  27.933  87.112  1.00 16.19 ? 382  GLN B CG    1 
ATOM   11533 C CD    . GLN B  1 384  ? -5.236  29.220  87.494  1.00 20.19 ? 382  GLN B CD    1 
ATOM   11534 O OE1   . GLN B  1 384  ? -4.660  30.078  88.155  1.00 21.42 ? 382  GLN B OE1   1 
ATOM   11535 N NE2   . GLN B  1 384  ? -6.493  29.358  87.078  1.00 19.76 ? 382  GLN B NE2   1 
ATOM   11536 N N     . LEU B  1 385  ? 0.056   27.466  87.143  1.00 17.03 ? 383  LEU B N     1 
ATOM   11537 C CA    . LEU B  1 385  ? 1.467   27.751  86.896  1.00 18.55 ? 383  LEU B CA    1 
ATOM   11538 C C     . LEU B  1 385  ? 2.132   26.679  86.039  1.00 18.53 ? 383  LEU B C     1 
ATOM   11539 O O     . LEU B  1 385  ? 2.985   26.990  85.199  1.00 20.12 ? 383  LEU B O     1 
ATOM   11540 C CB    . LEU B  1 385  ? 2.220   27.883  88.223  1.00 17.92 ? 383  LEU B CB    1 
ATOM   11541 C CG    . LEU B  1 385  ? 1.913   29.169  88.986  1.00 23.70 ? 383  LEU B CG    1 
ATOM   11542 C CD1   . LEU B  1 385  ? 2.678   29.187  90.301  1.00 21.69 ? 383  LEU B CD1   1 
ATOM   11543 C CD2   . LEU B  1 385  ? 2.295   30.352  88.122  1.00 24.66 ? 383  LEU B CD2   1 
ATOM   11544 N N     . ASP B  1 386  ? 1.793   25.412  86.269  1.00 19.44 ? 384  ASP B N     1 
ATOM   11545 C CA    . ASP B  1 386  ? 2.463   24.303  85.607  1.00 20.61 ? 384  ASP B CA    1 
ATOM   11546 C C     . ASP B  1 386  ? 1.819   23.946  84.273  1.00 20.24 ? 384  ASP B C     1 
ATOM   11547 O O     . ASP B  1 386  ? 2.276   23.008  83.605  1.00 22.66 ? 384  ASP B O     1 
ATOM   11548 C CB    . ASP B  1 386  ? 2.495   23.078  86.543  1.00 19.97 ? 384  ASP B CB    1 
ATOM   11549 C CG    . ASP B  1 386  ? 3.377   23.305  87.784  1.00 26.03 ? 384  ASP B CG    1 
ATOM   11550 O OD1   . ASP B  1 386  ? 4.062   24.343  87.864  1.00 28.00 ? 384  ASP B OD1   1 
ATOM   11551 O OD2   . ASP B  1 386  ? 3.377   22.446  88.691  1.00 26.02 ? 384  ASP B OD2   1 
ATOM   11552 N N     . GLY B  1 387  ? 0.806   24.698  83.853  1.00 19.11 ? 385  GLY B N     1 
ATOM   11553 C CA    . GLY B  1 387  ? 0.144   24.410  82.585  1.00 18.89 ? 385  GLY B CA    1 
ATOM   11554 C C     . GLY B  1 387  ? -0.345  22.984  82.447  1.00 24.02 ? 385  GLY B C     1 
ATOM   11555 O O     . GLY B  1 387  ? -0.237  22.398  81.363  1.00 22.86 ? 385  GLY B O     1 
ATOM   11556 N N     . LEU B  1 388  ? -0.893  22.404  83.511  1.00 19.62 ? 386  LEU B N     1 
ATOM   11557 C CA    . LEU B  1 388  ? -1.294  21.004  83.405  1.00 22.12 ? 386  LEU B CA    1 
ATOM   11558 C C     . LEU B  1 388  ? -2.706  20.879  82.824  1.00 23.82 ? 386  LEU B C     1 
ATOM   11559 O O     . LEU B  1 388  ? -3.432  21.859  82.668  1.00 22.62 ? 386  LEU B O     1 
ATOM   11560 C CB    . LEU B  1 388  ? -1.174  20.316  84.761  1.00 25.74 ? 386  LEU B CB    1 
ATOM   11561 C CG    . LEU B  1 388  ? 0.284   20.359  85.225  1.00 23.70 ? 386  LEU B CG    1 
ATOM   11562 C CD1   . LEU B  1 388  ? 0.471   19.604  86.527  1.00 22.58 ? 386  LEU B CD1   1 
ATOM   11563 C CD2   . LEU B  1 388  ? 1.255   19.825  84.149  1.00 25.78 ? 386  LEU B CD2   1 
ATOM   11564 N N     . ALA B  1 389  ? -3.089  19.643  82.487  1.00 25.42 ? 387  ALA B N     1 
ATOM   11565 C CA    . ALA B  1 389  ? -4.295  19.431  81.689  1.00 25.51 ? 387  ALA B CA    1 
ATOM   11566 C C     . ALA B  1 389  ? -5.546  19.921  82.406  1.00 24.09 ? 387  ALA B C     1 
ATOM   11567 O O     . ALA B  1 389  ? -6.463  20.471  81.784  1.00 24.66 ? 387  ALA B O     1 
ATOM   11568 C CB    . ALA B  1 389  ? -4.437  17.946  81.346  1.00 30.39 ? 387  ALA B CB    1 
ATOM   11569 N N     . ASP B  1 390  ? -5.612  19.711  83.710  1.00 22.94 ? 388  ASP B N     1 
ATOM   11570 C CA    . ASP B  1 390  ? -6.795  20.038  84.485  1.00 19.15 ? 388  ASP B CA    1 
ATOM   11571 C C     . ASP B  1 390  ? -6.333  20.130  85.927  1.00 19.87 ? 388  ASP B C     1 
ATOM   11572 O O     . ASP B  1 390  ? -5.143  19.994  86.213  1.00 22.83 ? 388  ASP B O     1 
ATOM   11573 C CB    . ASP B  1 390  ? -7.889  18.988  84.285  1.00 24.59 ? 388  ASP B CB    1 
ATOM   11574 C CG    . ASP B  1 390  ? -9.286  19.539  84.492  1.00 29.07 ? 388  ASP B CG    1 
ATOM   11575 O OD1   . ASP B  1 390  ? -9.515  20.280  85.470  1.00 26.13 ? 388  ASP B OD1   1 
ATOM   11576 O OD2   . ASP B  1 390  ? -10.166 19.230  83.658  1.00 26.17 ? 388  ASP B OD2   1 
ATOM   11577 N N     . PHE B  1 391  ? -7.253  20.373  86.801  1.00 20.21 ? 389  PHE B N     1 
ATOM   11578 C CA    . PHE B  1 391  ? -6.918  20.452  88.215  1.00 21.15 ? 389  PHE B CA    1 
ATOM   11579 C C     . PHE B  1 391  ? -6.985  19.064  88.831  1.00 19.78 ? 389  PHE B C     1 
ATOM   11580 O O     . PHE B  1 391  ? -7.703  18.193  88.336  1.00 21.15 ? 389  PHE B O     1 
ATOM   11581 C CB    . PHE B  1 391  ? -7.890  21.396  88.932  1.00 23.23 ? 389  PHE B CB    1 
ATOM   11582 C CG    . PHE B  1 391  ? -7.827  22.806  88.413  1.00 20.71 ? 389  PHE B CG    1 
ATOM   11583 C CD1   . PHE B  1 391  ? -6.763  23.623  88.759  1.00 18.66 ? 389  PHE B CD1   1 
ATOM   11584 C CD2   . PHE B  1 391  ? -8.797  23.298  87.558  1.00 19.03 ? 389  PHE B CD2   1 
ATOM   11585 C CE1   . PHE B  1 391  ? -6.664  24.907  88.271  1.00 19.29 ? 389  PHE B CE1   1 
ATOM   11586 C CE2   . PHE B  1 391  ? -8.707  24.605  87.070  1.00 21.01 ? 389  PHE B CE2   1 
ATOM   11587 C CZ    . PHE B  1 391  ? -7.635  25.406  87.433  1.00 18.99 ? 389  PHE B CZ    1 
ATOM   11588 N N     . PRO B  1 392  ? -6.222  18.810  89.890  1.00 19.44 ? 390  PRO B N     1 
ATOM   11589 C CA    . PRO B  1 392  ? -6.361  17.548  90.621  1.00 21.43 ? 390  PRO B CA    1 
ATOM   11590 C C     . PRO B  1 392  ? -7.432  17.593  91.697  1.00 20.36 ? 390  PRO B C     1 
ATOM   11591 O O     . PRO B  1 392  ? -7.568  16.627  92.454  1.00 23.35 ? 390  PRO B O     1 
ATOM   11592 C CB    . PRO B  1 392  ? -4.975  17.406  91.253  1.00 19.66 ? 390  PRO B CB    1 
ATOM   11593 C CG    . PRO B  1 392  ? -4.626  18.823  91.605  1.00 19.13 ? 390  PRO B CG    1 
ATOM   11594 C CD    . PRO B  1 392  ? -5.165  19.666  90.466  1.00 18.85 ? 390  PRO B CD    1 
ATOM   11595 N N     . VAL B  1 393  ? -8.131  18.719  91.810  1.00 21.77 ? 391  VAL B N     1 
ATOM   11596 C CA    . VAL B  1 393  ? -9.228  18.918  92.747  1.00 23.48 ? 391  VAL B CA    1 
ATOM   11597 C C     . VAL B  1 393  ? -10.407 19.490  91.971  1.00 22.76 ? 391  VAL B C     1 
ATOM   11598 O O     . VAL B  1 393  ? -10.258 20.015  90.866  1.00 23.93 ? 391  VAL B O     1 
ATOM   11599 C CB    . VAL B  1 393  ? -8.847  19.872  93.902  1.00 20.42 ? 391  VAL B CB    1 
ATOM   11600 C CG1   . VAL B  1 393  ? -7.714  19.295  94.738  1.00 22.37 ? 391  VAL B CG1   1 
ATOM   11601 C CG2   . VAL B  1 393  ? -8.450  21.245  93.349  1.00 19.94 ? 391  VAL B CG2   1 
ATOM   11602 N N     . PHE B  1 394  ? -11.584 19.411  92.577  1.00 24.34 ? 392  PHE B N     1 
ATOM   11603 C CA    . PHE B  1 394  ? -12.748 20.058  91.987  1.00 21.43 ? 392  PHE B CA    1 
ATOM   11604 C C     . PHE B  1 394  ? -12.629 21.580  92.081  1.00 22.72 ? 392  PHE B C     1 
ATOM   11605 O O     . PHE B  1 394  ? -11.830 22.128  92.852  1.00 22.83 ? 392  PHE B O     1 
ATOM   11606 C CB    . PHE B  1 394  ? -14.020 19.557  92.663  1.00 24.64 ? 392  PHE B CB    1 
ATOM   11607 C CG    . PHE B  1 394  ? -14.183 18.073  92.574  1.00 27.72 ? 392  PHE B CG    1 
ATOM   11608 C CD1   . PHE B  1 394  ? -14.408 17.459  91.350  1.00 24.69 ? 392  PHE B CD1   1 
ATOM   11609 C CD2   . PHE B  1 394  ? -14.083 17.287  93.701  1.00 24.66 ? 392  PHE B CD2   1 
ATOM   11610 C CE1   . PHE B  1 394  ? -14.533 16.088  91.257  1.00 26.67 ? 392  PHE B CE1   1 
ATOM   11611 C CE2   . PHE B  1 394  ? -14.205 15.922  93.620  1.00 24.40 ? 392  PHE B CE2   1 
ATOM   11612 C CZ    . PHE B  1 394  ? -14.431 15.315  92.393  1.00 26.37 ? 392  PHE B CZ    1 
ATOM   11613 N N     . THR B  1 395  ? -13.418 22.269  91.256  1.00 21.71 ? 393  THR B N     1 
ATOM   11614 C CA    . THR B  1 395  ? -13.417 23.726  91.211  1.00 24.96 ? 393  THR B CA    1 
ATOM   11615 C C     . THR B  1 395  ? -14.711 24.361  91.712  1.00 26.55 ? 393  THR B C     1 
ATOM   11616 O O     . THR B  1 395  ? -14.735 25.580  91.917  1.00 25.93 ? 393  THR B O     1 
ATOM   11617 C CB    . THR B  1 395  ? -13.148 24.230  89.782  1.00 25.30 ? 393  THR B CB    1 
ATOM   11618 O OG1   . THR B  1 395  ? -14.239 23.859  88.927  1.00 27.32 ? 393  THR B OG1   1 
ATOM   11619 C CG2   . THR B  1 395  ? -11.838 23.655  89.240  1.00 27.37 ? 393  THR B CG2   1 
ATOM   11620 N N     . ARG B  1 396  ? -15.786 23.591  91.878  1.00 27.70 ? 394  ARG B N     1 
ATOM   11621 C CA    . ARG B  1 396  ? -16.989 24.059  92.562  1.00 24.15 ? 394  ARG B CA    1 
ATOM   11622 C C     . ARG B  1 396  ? -17.095 23.381  93.915  1.00 27.20 ? 394  ARG B C     1 
ATOM   11623 O O     . ARG B  1 396  ? -16.928 22.160  94.018  1.00 24.74 ? 394  ARG B O     1 
ATOM   11624 C CB    . ARG B  1 396  ? -18.246 23.783  91.740  1.00 26.88 ? 394  ARG B CB    1 
ATOM   11625 C CG    . ARG B  1 396  ? -18.281 24.543  90.435  1.00 26.18 ? 394  ARG B CG    1 
ATOM   11626 C CD    . ARG B  1 396  ? -19.634 24.342  89.741  1.00 28.30 ? 394  ARG B CD    1 
ATOM   11627 N NE    . ARG B  1 396  ? -19.624 24.922  88.402  1.00 40.61 ? 394  ARG B NE    1 
ATOM   11628 C CZ    . ARG B  1 396  ? -20.534 25.769  87.935  1.00 43.92 ? 394  ARG B CZ    1 
ATOM   11629 N NH1   . ARG B  1 396  ? -21.583 26.130  88.660  1.00 48.78 ? 394  ARG B NH1   1 
ATOM   11630 N NH2   . ARG B  1 396  ? -20.391 26.263  86.705  1.00 37.91 ? 394  ARG B NH2   1 
ATOM   11631 N N     . LYS B  1 397  ? -17.386 24.170  94.951  1.00 29.38 ? 395  LYS B N     1 
ATOM   11632 C CA    . LYS B  1 397  ? -17.445 23.612  96.298  1.00 30.25 ? 395  LYS B CA    1 
ATOM   11633 C C     . LYS B  1 397  ? -18.539 22.556  96.419  1.00 31.19 ? 395  LYS B C     1 
ATOM   11634 O O     . LYS B  1 397  ? -18.398 21.593  97.182  1.00 30.35 ? 395  LYS B O     1 
ATOM   11635 C CB    . LYS B  1 397  ? -17.661 24.733  97.310  1.00 31.90 ? 395  LYS B CB    1 
ATOM   11636 C CG    . LYS B  1 397  ? -17.360 24.348  98.745  1.00 34.29 ? 395  LYS B CG    1 
ATOM   11637 C CD    . LYS B  1 397  ? -18.605 23.858  99.446  1.00 36.89 ? 395  LYS B CD    1 
ATOM   11638 C CE    . LYS B  1 397  ? -18.336 23.534  100.905 1.00 35.14 ? 395  LYS B CE    1 
ATOM   11639 N NZ    . LYS B  1 397  ? -19.603 23.064  101.549 1.00 37.49 ? 395  LYS B NZ    1 
ATOM   11640 N N     . ILE B  1 398  ? -19.628 22.703  95.666  1.00 27.98 ? 396  ILE B N     1 
ATOM   11641 C CA    . ILE B  1 398  ? -20.678 21.705  95.762  1.00 29.41 ? 396  ILE B CA    1 
ATOM   11642 C C     . ILE B  1 398  ? -20.202 20.362  95.218  1.00 25.88 ? 396  ILE B C     1 
ATOM   11643 O O     . ILE B  1 398  ? -20.684 19.310  95.643  1.00 28.61 ? 396  ILE B O     1 
ATOM   11644 C CB    . ILE B  1 398  ? -21.941 22.219  95.047  1.00 30.33 ? 396  ILE B CB    1 
ATOM   11645 C CG1   . ILE B  1 398  ? -23.134 21.349  95.394  1.00 36.93 ? 396  ILE B CG1   1 
ATOM   11646 C CG2   . ILE B  1 398  ? -21.713 22.304  93.532  1.00 32.98 ? 396  ILE B CG2   1 
ATOM   11647 C CD1   . ILE B  1 398  ? -24.445 21.987  95.020  1.00 41.68 ? 396  ILE B CD1   1 
ATOM   11648 N N     . HIS B  1 399  ? -19.235 20.363  94.300  1.00 24.62 ? 397  HIS B N     1 
ATOM   11649 C CA    . HIS B  1 399  ? -18.712 19.094  93.795  1.00 29.13 ? 397  HIS B CA    1 
ATOM   11650 C C     . HIS B  1 399  ? -17.950 18.341  94.869  1.00 27.57 ? 397  HIS B C     1 
ATOM   11651 O O     . HIS B  1 399  ? -18.054 17.112  94.971  1.00 27.31 ? 397  HIS B O     1 
ATOM   11652 C CB    . HIS B  1 399  ? -17.817 19.340  92.586  1.00 29.24 ? 397  HIS B CB    1 
ATOM   11653 C CG    . HIS B  1 399  ? -18.575 19.823  91.393  1.00 26.66 ? 397  HIS B CG    1 
ATOM   11654 N ND1   . HIS B  1 399  ? -17.962 20.367  90.285  1.00 26.16 ? 397  HIS B ND1   1 
ATOM   11655 C CD2   . HIS B  1 399  ? -19.907 19.860  91.148  1.00 28.69 ? 397  HIS B CD2   1 
ATOM   11656 C CE1   . HIS B  1 399  ? -18.889 20.708  89.401  1.00 28.08 ? 397  HIS B CE1   1 
ATOM   11657 N NE2   . HIS B  1 399  ? -20.074 20.412  89.902  1.00 27.85 ? 397  HIS B NE2   1 
ATOM   11658 N N     . THR B  1 400  ? -17.166 19.063  95.665  1.00 29.69 ? 398  THR B N     1 
ATOM   11659 C CA    . THR B  1 400  ? -16.480 18.428  96.782  1.00 27.05 ? 398  THR B CA    1 
ATOM   11660 C C     . THR B  1 400  ? -17.480 17.796  97.740  1.00 27.60 ? 398  THR B C     1 
ATOM   11661 O O     . THR B  1 400  ? -17.282 16.663  98.198  1.00 30.35 ? 398  THR B O     1 
ATOM   11662 C CB    . THR B  1 400  ? -15.599 19.458  97.493  1.00 25.56 ? 398  THR B CB    1 
ATOM   11663 O OG1   . THR B  1 400  ? -14.537 19.878  96.620  1.00 23.93 ? 398  THR B OG1   1 
ATOM   11664 C CG2   . THR B  1 400  ? -14.991 18.879  98.757  1.00 25.12 ? 398  THR B CG2   1 
ATOM   11665 N N     . ASP B  1 401  ? -18.577 18.499  98.039  1.00 28.99 ? 399  ASP B N     1 
ATOM   11666 C CA    . ASP B  1 401  ? -19.580 17.945  98.949  1.00 31.95 ? 399  ASP B CA    1 
ATOM   11667 C C     . ASP B  1 401  ? -20.177 16.657  98.399  1.00 27.51 ? 399  ASP B C     1 
ATOM   11668 O O     . ASP B  1 401  ? -20.371 15.690  99.140  1.00 30.30 ? 399  ASP B O     1 
ATOM   11669 C CB    . ASP B  1 401  ? -20.694 18.959  99.218  1.00 32.67 ? 399  ASP B CB    1 
ATOM   11670 C CG    . ASP B  1 401  ? -20.211 20.164  100.010 1.00 38.08 ? 399  ASP B CG    1 
ATOM   11671 O OD1   . ASP B  1 401  ? -19.178 20.052  100.710 1.00 34.33 ? 399  ASP B OD1   1 
ATOM   11672 O OD2   . ASP B  1 401  ? -20.871 21.222  99.941  1.00 36.93 ? 399  ASP B OD2   1 
ATOM   11673 N N     . VAL B  1 402  ? -20.477 16.626  97.098  1.00 31.23 ? 400  VAL B N     1 
ATOM   11674 C CA    . VAL B  1 402  ? -20.999 15.404  96.501  1.00 27.93 ? 400  VAL B CA    1 
ATOM   11675 C C     . VAL B  1 402  ? -19.959 14.294  96.565  1.00 29.08 ? 400  VAL B C     1 
ATOM   11676 O O     . VAL B  1 402  ? -20.264 13.157  96.949  1.00 30.39 ? 400  VAL B O     1 
ATOM   11677 C CB    . VAL B  1 402  ? -21.465 15.678  95.059  1.00 31.05 ? 400  VAL B CB    1 
ATOM   11678 C CG1   . VAL B  1 402  ? -21.879 14.386  94.386  1.00 33.06 ? 400  VAL B CG1   1 
ATOM   11679 C CG2   . VAL B  1 402  ? -22.617 16.663  95.089  1.00 33.53 ? 400  VAL B CG2   1 
ATOM   11680 N N     . SER B  1 403  ? -18.717 14.610  96.184  1.00 29.28 ? 401  SER B N     1 
ATOM   11681 C CA    . SER B  1 403  ? -17.618 13.657  96.285  1.00 30.40 ? 401  SER B CA    1 
ATOM   11682 C C     . SER B  1 403  ? -17.539 13.066  97.686  1.00 32.90 ? 401  SER B C     1 
ATOM   11683 O O     . SER B  1 403  ? -17.480 11.843  97.864  1.00 31.38 ? 401  SER B O     1 
ATOM   11684 C CB    . SER B  1 403  ? -16.304 14.356  95.913  1.00 28.93 ? 401  SER B CB    1 
ATOM   11685 O OG    . SER B  1 403  ? -15.185 13.494  96.056  1.00 32.46 ? 401  SER B OG    1 
ATOM   11686 N N     . TYR B  1 404  ? -17.582 13.930  98.698  1.00 31.51 ? 402  TYR B N     1 
ATOM   11687 C CA    . TYR B  1 404  ? -17.458 13.476  100.080 1.00 33.31 ? 402  TYR B CA    1 
ATOM   11688 C C     . TYR B  1 404  ? -18.567 12.489  100.436 1.00 34.94 ? 402  TYR B C     1 
ATOM   11689 O O     . TYR B  1 404  ? -18.306 11.398  100.962 1.00 33.72 ? 402  TYR B O     1 
ATOM   11690 C CB    . TYR B  1 404  ? -17.464 14.696  101.004 1.00 29.62 ? 402  TYR B CB    1 
ATOM   11691 C CG    . TYR B  1 404  ? -17.107 14.398  102.445 1.00 32.04 ? 402  TYR B CG    1 
ATOM   11692 C CD1   . TYR B  1 404  ? -18.023 13.804  103.293 1.00 33.39 ? 402  TYR B CD1   1 
ATOM   11693 C CD2   . TYR B  1 404  ? -15.867 14.738  102.958 1.00 32.57 ? 402  TYR B CD2   1 
ATOM   11694 C CE1   . TYR B  1 404  ? -17.706 13.529  104.616 1.00 32.33 ? 402  TYR B CE1   1 
ATOM   11695 C CE2   . TYR B  1 404  ? -15.540 14.469  104.282 1.00 28.31 ? 402  TYR B CE2   1 
ATOM   11696 C CZ    . TYR B  1 404  ? -16.462 13.865  105.098 1.00 33.47 ? 402  TYR B CZ    1 
ATOM   11697 O OH    . TYR B  1 404  ? -16.155 13.594  106.414 1.00 34.07 ? 402  TYR B OH    1 
ATOM   11698 N N     . ILE B  1 405  ? -19.815 12.832  100.106 1.00 35.38 ? 403  ILE B N     1 
ATOM   11699 C CA    . ILE B  1 405  ? -20.937 11.956  100.436 1.00 36.49 ? 403  ILE B CA    1 
ATOM   11700 C C     . ILE B  1 405  ? -20.817 10.628  99.693  1.00 31.83 ? 403  ILE B C     1 
ATOM   11701 O O     . ILE B  1 405  ? -21.127 9.561   100.239 1.00 33.78 ? 403  ILE B O     1 
ATOM   11702 C CB    . ILE B  1 405  ? -22.261 12.688  100.139 1.00 37.42 ? 403  ILE B CB    1 
ATOM   11703 C CG1   . ILE B  1 405  ? -22.381 13.927  101.036 1.00 38.95 ? 403  ILE B CG1   1 
ATOM   11704 C CG2   . ILE B  1 405  ? -23.474 11.782  100.330 1.00 36.95 ? 403  ILE B CG2   1 
ATOM   11705 C CD1   . ILE B  1 405  ? -23.594 14.796  100.731 1.00 44.48 ? 403  ILE B CD1   1 
ATOM   11706 N N     . ALA B  1 406  ? -20.337 10.665  98.445  1.00 36.62 ? 404  ALA B N     1 
ATOM   11707 C CA    . ALA B  1 406  ? -20.191 9.433   97.673  1.00 36.07 ? 404  ALA B CA    1 
ATOM   11708 C C     . ALA B  1 406  ? -19.109 8.539   98.258  1.00 36.51 ? 404  ALA B C     1 
ATOM   11709 O O     . ALA B  1 406  ? -19.285 7.318   98.349  1.00 36.16 ? 404  ALA B O     1 
ATOM   11710 C CB    . ALA B  1 406  ? -19.883 9.755   96.208  1.00 35.27 ? 404  ALA B CB    1 
ATOM   11711 N N     . CYS B  1 407  ? -17.983 9.127   98.664  1.00 33.38 ? 405  CYS B N     1 
ATOM   11712 C CA    . CYS B  1 407  ? -16.912 8.335   99.251  1.00 36.97 ? 405  CYS B CA    1 
ATOM   11713 C C     . CYS B  1 407  ? -17.306 7.797   100.622 1.00 37.35 ? 405  CYS B C     1 
ATOM   11714 O O     . CYS B  1 407  ? -16.895 6.691   100.997 1.00 34.94 ? 405  CYS B O     1 
ATOM   11715 C CB    . CYS B  1 407  ? -15.638 9.179   99.320  1.00 35.76 ? 405  CYS B CB    1 
ATOM   11716 S SG    . CYS B  1 407  ? -14.969 9.599   97.655  1.00 37.39 ? 405  CYS B SG    1 
ATOM   11717 N N     . ALA B  1 408  ? -18.115 8.552   101.371 1.00 33.86 ? 406  ALA B N     1 
ATOM   11718 C CA    . ALA B  1 408  ? -18.681 8.029   102.612 1.00 38.25 ? 406  ALA B CA    1 
ATOM   11719 C C     . ALA B  1 408  ? -19.512 6.771   102.368 1.00 36.13 ? 406  ALA B C     1 
ATOM   11720 O O     . ALA B  1 408  ? -19.452 5.818   103.150 1.00 36.70 ? 406  ALA B O     1 
ATOM   11721 C CB    . ALA B  1 408  ? -19.527 9.104   103.287 1.00 39.43 ? 406  ALA B CB    1 
ATOM   11722 N N     . ALA B  1 409  ? -20.299 6.740   101.288 1.00 35.72 ? 407  ALA B N     1 
ATOM   11723 C CA    . ALA B  1 409  ? -21.051 5.528   100.978 1.00 38.12 ? 407  ALA B CA    1 
ATOM   11724 C C     . ALA B  1 409  ? -20.120 4.355   100.689 1.00 34.01 ? 407  ALA B C     1 
ATOM   11725 O O     . ALA B  1 409  ? -20.410 3.216   101.066 1.00 38.87 ? 407  ALA B O     1 
ATOM   11726 C CB    . ALA B  1 409  ? -21.985 5.776   99.786  1.00 38.00 ? 407  ALA B CB    1 
ATOM   11727 N N     . LYS B  1 410  ? -19.003 4.617   100.002 1.00 37.48 ? 408  LYS B N     1 
ATOM   11728 C CA    . LYS B  1 410  ? -18.024 3.572   99.718  1.00 34.13 ? 408  LYS B CA    1 
ATOM   11729 C C     . LYS B  1 410  ? -17.372 3.075   101.003 1.00 38.89 ? 408  LYS B C     1 
ATOM   11730 O O     . LYS B  1 410  ? -17.191 1.864   101.195 1.00 38.82 ? 408  LYS B O     1 
ATOM   11731 C CB    . LYS B  1 410  ? -16.974 4.113   98.740  1.00 34.44 ? 408  LYS B CB    1 
ATOM   11732 C CG    . LYS B  1 410  ? -15.863 3.137   98.394  1.00 36.11 ? 408  LYS B CG    1 
ATOM   11733 C CD    . LYS B  1 410  ? -14.848 3.750   97.420  1.00 37.47 ? 408  LYS B CD    1 
ATOM   11734 C CE    . LYS B  1 410  ? -15.414 3.937   96.013  1.00 38.65 ? 408  LYS B CE    1 
ATOM   11735 N NZ    . LYS B  1 410  ? -15.492 2.669   95.209  1.00 37.41 ? 408  LYS B NZ    1 
ATOM   11736 N N     . LEU B  1 411  ? -17.054 3.997   101.910 1.00 35.40 ? 409  LEU B N     1 
ATOM   11737 C CA    . LEU B  1 411  ? -16.426 3.629   103.177 1.00 34.35 ? 409  LEU B CA    1 
ATOM   11738 C C     . LEU B  1 411  ? -17.379 2.839   104.064 1.00 36.53 ? 409  LEU B C     1 
ATOM   11739 O O     . LEU B  1 411  ? -17.004 1.801   104.628 1.00 35.74 ? 409  LEU B O     1 
ATOM   11740 C CB    . LEU B  1 411  ? -15.942 4.890   103.889 1.00 34.37 ? 409  LEU B CB    1 
ATOM   11741 C CG    . LEU B  1 411  ? -14.583 5.392   103.405 1.00 39.90 ? 409  LEU B CG    1 
ATOM   11742 C CD1   . LEU B  1 411  ? -14.321 6.811   103.885 1.00 36.61 ? 409  LEU B CD1   1 
ATOM   11743 C CD2   . LEU B  1 411  ? -13.506 4.440   103.893 1.00 35.97 ? 409  LEU B CD2   1 
ATOM   11744 N N     . LEU B  1 412  ? -18.627 3.304   104.185 1.00 41.09 ? 410  LEU B N     1 
ATOM   11745 C CA    . LEU B  1 412  ? -19.613 2.630   105.028 1.00 42.41 ? 410  LEU B CA    1 
ATOM   11746 C C     . LEU B  1 412  ? -19.915 1.204   104.581 1.00 43.25 ? 410  LEU B C     1 
ATOM   11747 O O     . LEU B  1 412  ? -20.433 0.417   105.380 1.00 44.50 ? 410  LEU B O     1 
ATOM   11748 C CB    . LEU B  1 412  ? -20.908 3.442   105.073 1.00 38.93 ? 410  LEU B CB    1 
ATOM   11749 C CG    . LEU B  1 412  ? -20.793 4.742   105.874 1.00 43.42 ? 410  LEU B CG    1 
ATOM   11750 C CD1   . LEU B  1 412  ? -22.049 5.579   105.762 1.00 40.17 ? 410  LEU B CD1   1 
ATOM   11751 C CD2   . LEU B  1 412  ? -20.496 4.431   107.322 1.00 42.29 ? 410  LEU B CD2   1 
ATOM   11752 N N     . ALA B  1 413  ? -19.615 0.848   103.334 1.00 41.84 ? 411  ALA B N     1 
ATOM   11753 C CA    . ALA B  1 413  ? -19.843 -0.516  102.872 1.00 38.06 ? 411  ALA B CA    1 
ATOM   11754 C C     . ALA B  1 413  ? -18.693 -1.467  103.186 1.00 45.78 ? 411  ALA B C     1 
ATOM   11755 O O     . ALA B  1 413  ? -18.849 -2.679  102.992 1.00 43.51 ? 411  ALA B O     1 
ATOM   11756 C CB    . ALA B  1 413  ? -20.112 -0.528  101.360 1.00 44.05 ? 411  ALA B CB    1 
ATOM   11757 N N     . ALA B  1 414  ? -17.557 -0.963  103.687 1.00 41.33 ? 412  ALA B N     1 
ATOM   11758 C CA    . ALA B  1 414  ? -16.372 -1.782  103.921 1.00 39.69 ? 412  ALA B CA    1 
ATOM   11759 C C     . ALA B  1 414  ? -15.895 -1.721  105.373 1.00 42.80 ? 412  ALA B C     1 
ATOM   11760 O O     . ALA B  1 414  ? -14.709 -1.925  105.647 1.00 41.82 ? 412  ALA B O     1 
ATOM   11761 C CB    . ALA B  1 414  ? -15.241 -1.365  102.980 1.00 38.04 ? 412  ALA B CB    1 
ATOM   11762 N N     . THR B  1 415  ? -16.809 -1.466  106.315 1.00 40.24 ? 413  THR B N     1 
ATOM   11763 C CA    . THR B  1 415  ? -16.419 -1.258  107.708 1.00 40.62 ? 413  THR B CA    1 
ATOM   11764 C C     . THR B  1 415  ? -15.794 -2.485  108.352 1.00 44.27 ? 413  THR B C     1 
ATOM   11765 O O     . THR B  1 415  ? -15.214 -2.362  109.438 1.00 42.45 ? 413  THR B O     1 
ATOM   11766 C CB    . THR B  1 415  ? -17.621 -0.815  108.535 1.00 40.84 ? 413  THR B CB    1 
ATOM   11767 O OG1   . THR B  1 415  ? -18.683 -1.763  108.372 1.00 47.58 ? 413  THR B OG1   1 
ATOM   11768 C CG2   . THR B  1 415  ? -18.090 0.557   108.078 1.00 36.88 ? 413  THR B CG2   1 
ATOM   11769 N N     . ASP B  1 416  ? -15.899 -3.660  107.734 1.00 43.53 ? 414  ASP B N     1 
ATOM   11770 C CA    . ASP B  1 416  ? -15.204 -4.824  108.274 1.00 41.59 ? 414  ASP B CA    1 
ATOM   11771 C C     . ASP B  1 416  ? -13.697 -4.668  108.139 1.00 43.59 ? 414  ASP B C     1 
ATOM   11772 O O     . ASP B  1 416  ? -12.941 -5.099  109.020 1.00 51.10 ? 414  ASP B O     1 
ATOM   11773 C CB    . ASP B  1 416  ? -15.666 -6.105  107.571 1.00 48.47 ? 414  ASP B CB    1 
ATOM   11774 C CG    . ASP B  1 416  ? -16.997 -6.625  108.097 1.00 56.49 ? 414  ASP B CG    1 
ATOM   11775 O OD1   . ASP B  1 416  ? -17.567 -6.010  109.023 1.00 53.99 ? 414  ASP B OD1   1 
ATOM   11776 O OD2   . ASP B  1 416  ? -17.471 -7.661  107.581 1.00 63.84 ? 414  ASP B OD2   1 
ATOM   11777 N N     . VAL B  1 417  ? -13.235 -4.044  107.056 1.00 39.47 ? 415  VAL B N     1 
ATOM   11778 C CA    . VAL B  1 417  ? -11.803 -3.944  106.805 1.00 41.87 ? 415  VAL B CA    1 
ATOM   11779 C C     . VAL B  1 417  ? -11.266 -2.524  106.900 1.00 40.02 ? 415  VAL B C     1 
ATOM   11780 O O     . VAL B  1 417  ? -10.044 -2.341  106.809 1.00 44.08 ? 415  VAL B O     1 
ATOM   11781 C CB    . VAL B  1 417  ? -11.429 -4.566  105.443 1.00 41.13 ? 415  VAL B CB    1 
ATOM   11782 C CG1   . VAL B  1 417  ? -11.799 -6.053  105.433 1.00 41.34 ? 415  VAL B CG1   1 
ATOM   11783 C CG2   . VAL B  1 417  ? -12.113 -3.821  104.312 1.00 44.13 ? 415  VAL B CG2   1 
ATOM   11784 N N     . VAL B  1 418  ? -12.118 -1.515  107.076 1.00 39.36 ? 416  VAL B N     1 
ATOM   11785 C CA    . VAL B  1 418  ? -11.662 -0.145  107.283 1.00 38.54 ? 416  VAL B CA    1 
ATOM   11786 C C     . VAL B  1 418  ? -12.552 0.518   108.321 1.00 42.08 ? 416  VAL B C     1 
ATOM   11787 O O     . VAL B  1 418  ? -13.757 0.255   108.395 1.00 39.06 ? 416  VAL B O     1 
ATOM   11788 C CB    . VAL B  1 418  ? -11.647 0.708   105.992 1.00 36.79 ? 416  VAL B CB    1 
ATOM   11789 C CG1   . VAL B  1 418  ? -10.667 0.151   104.964 1.00 36.90 ? 416  VAL B CG1   1 
ATOM   11790 C CG2   . VAL B  1 418  ? -13.044 0.842   105.408 1.00 35.77 ? 416  VAL B CG2   1 
ATOM   11791 N N     . PHE B  1 419  ? -11.941 1.385   109.135 1.00 36.62 ? 417  PHE B N     1 
ATOM   11792 C CA    . PHE B  1 419  ? -12.645 2.156   110.149 1.00 38.53 ? 417  PHE B CA    1 
ATOM   11793 C C     . PHE B  1 419  ? -12.843 3.575   109.627 1.00 39.43 ? 417  PHE B C     1 
ATOM   11794 O O     . PHE B  1 419  ? -11.892 4.375   109.647 1.00 36.14 ? 417  PHE B O     1 
ATOM   11795 C CB    . PHE B  1 419  ? -11.854 2.162   111.467 1.00 36.91 ? 417  PHE B CB    1 
ATOM   11796 C CG    . PHE B  1 419  ? -12.450 3.032   112.533 1.00 34.96 ? 417  PHE B CG    1 
ATOM   11797 C CD1   . PHE B  1 419  ? -13.728 2.789   113.013 1.00 38.77 ? 417  PHE B CD1   1 
ATOM   11798 C CD2   . PHE B  1 419  ? -11.720 4.074   113.085 1.00 38.66 ? 417  PHE B CD2   1 
ATOM   11799 C CE1   . PHE B  1 419  ? -14.278 3.580   114.007 1.00 39.51 ? 417  PHE B CE1   1 
ATOM   11800 C CE2   . PHE B  1 419  ? -12.265 4.869   114.083 1.00 37.22 ? 417  PHE B CE2   1 
ATOM   11801 C CZ    . PHE B  1 419  ? -13.545 4.621   114.546 1.00 40.26 ? 417  PHE B CZ    1 
ATOM   11802 N N     . PRO B  1 420  ? -14.032 3.931   109.128 1.00 36.19 ? 418  PRO B N     1 
ATOM   11803 C CA    . PRO B  1 420  ? -14.223 5.268   108.548 1.00 37.00 ? 418  PRO B CA    1 
ATOM   11804 C C     . PRO B  1 420  ? -14.285 6.342   109.622 1.00 38.32 ? 418  PRO B C     1 
ATOM   11805 O O     . PRO B  1 420  ? -14.917 6.163   110.665 1.00 36.95 ? 418  PRO B O     1 
ATOM   11806 C CB    . PRO B  1 420  ? -15.564 5.152   107.806 1.00 34.43 ? 418  PRO B CB    1 
ATOM   11807 C CG    . PRO B  1 420  ? -15.808 3.692   107.653 1.00 34.00 ? 418  PRO B CG    1 
ATOM   11808 C CD    . PRO B  1 420  ? -15.187 3.058   108.870 1.00 37.41 ? 418  PRO B CD    1 
ATOM   11809 N N     . GLN B  1 421  ? -13.647 7.479   109.338 1.00 36.31 ? 419  GLN B N     1 
ATOM   11810 C CA    . GLN B  1 421  ? -13.599 8.619   110.250 1.00 33.60 ? 419  GLN B CA    1 
ATOM   11811 C C     . GLN B  1 421  ? -13.992 9.861   109.462 1.00 32.37 ? 419  GLN B C     1 
ATOM   11812 O O     . GLN B  1 421  ? -13.200 10.366  108.658 1.00 29.36 ? 419  GLN B O     1 
ATOM   11813 C CB    . GLN B  1 421  ? -12.206 8.771   110.866 1.00 33.24 ? 419  GLN B CB    1 
ATOM   11814 C CG    . GLN B  1 421  ? -11.711 7.516   111.567 1.00 31.38 ? 419  GLN B CG    1 
ATOM   11815 C CD    . GLN B  1 421  ? -10.218 7.537   111.875 1.00 33.25 ? 419  GLN B CD    1 
ATOM   11816 O OE1   . GLN B  1 421  ? -9.800  7.453   113.041 1.00 34.10 ? 419  GLN B OE1   1 
ATOM   11817 N NE2   . GLN B  1 421  ? -9.408  7.611   110.836 1.00 29.71 ? 419  GLN B NE2   1 
ATOM   11818 N N     . PHE B  1 422  ? -15.194 10.374  109.707 1.00 32.67 ? 420  PHE B N     1 
ATOM   11819 C CA    . PHE B  1 422  ? -15.771 11.424  108.868 1.00 35.14 ? 420  PHE B CA    1 
ATOM   11820 C C     . PHE B  1 422  ? -15.501 12.789  109.490 1.00 31.55 ? 420  PHE B C     1 
ATOM   11821 O O     . PHE B  1 422  ? -16.206 13.222  110.404 1.00 35.97 ? 420  PHE B O     1 
ATOM   11822 C CB    . PHE B  1 422  ? -17.258 11.172  108.652 1.00 35.46 ? 420  PHE B CB    1 
ATOM   11823 C CG    . PHE B  1 422  ? -17.543 9.859   107.994 1.00 37.12 ? 420  PHE B CG    1 
ATOM   11824 C CD1   . PHE B  1 422  ? -17.233 9.659   106.654 1.00 34.64 ? 420  PHE B CD1   1 
ATOM   11825 C CD2   . PHE B  1 422  ? -18.114 8.823   108.706 1.00 36.96 ? 420  PHE B CD2   1 
ATOM   11826 C CE1   . PHE B  1 422  ? -17.486 8.445   106.043 1.00 37.69 ? 420  PHE B CE1   1 
ATOM   11827 C CE2   . PHE B  1 422  ? -18.374 7.602   108.096 1.00 42.55 ? 420  PHE B CE2   1 
ATOM   11828 C CZ    . PHE B  1 422  ? -18.057 7.420   106.754 1.00 36.65 ? 420  PHE B CZ    1 
ATOM   11829 N N     . ALA B  1 423  ? -14.487 13.478  108.961 1.00 32.65 ? 421  ALA B N     1 
ATOM   11830 C CA    . ALA B  1 423  ? -14.056 14.772  109.474 1.00 31.92 ? 421  ALA B CA    1 
ATOM   11831 C C     . ALA B  1 423  ? -14.767 15.879  108.708 1.00 34.36 ? 421  ALA B C     1 
ATOM   11832 O O     . ALA B  1 423  ? -14.484 16.103  107.529 1.00 34.81 ? 421  ALA B O     1 
ATOM   11833 C CB    . ALA B  1 423  ? -12.539 14.916  109.350 1.00 30.15 ? 421  ALA B CB    1 
ATOM   11834 N N     . THR B  1 424  ? -15.660 16.597  109.384 1.00 37.90 ? 422  THR B N     1 
ATOM   11835 C CA    . THR B  1 424  ? -16.318 17.739  108.765 1.00 31.79 ? 422  THR B CA    1 
ATOM   11836 C C     . THR B  1 424  ? -16.946 18.605  109.846 1.00 34.49 ? 422  THR B C     1 
ATOM   11837 O O     . THR B  1 424  ? -17.362 18.107  110.895 1.00 37.73 ? 422  THR B O     1 
ATOM   11838 C CB    . THR B  1 424  ? -17.394 17.301  107.746 1.00 35.80 ? 422  THR B CB    1 
ATOM   11839 O OG1   . THR B  1 424  ? -18.053 18.455  107.212 1.00 30.70 ? 422  THR B OG1   1 
ATOM   11840 C CG2   . THR B  1 424  ? -18.419 16.383  108.393 1.00 34.20 ? 422  THR B CG2   1 
ATOM   11841 N N     . HIS B  1 425  ? -16.999 19.906  109.575 1.00 32.25 ? 423  HIS B N     1 
ATOM   11842 C CA    . HIS B  1 425  ? -17.734 20.865  110.389 1.00 34.06 ? 423  HIS B CA    1 
ATOM   11843 C C     . HIS B  1 425  ? -19.067 21.265  109.762 1.00 42.88 ? 423  HIS B C     1 
ATOM   11844 O O     . HIS B  1 425  ? -19.697 22.223  110.221 1.00 43.43 ? 423  HIS B O     1 
ATOM   11845 C CB    . HIS B  1 425  ? -16.890 22.112  110.610 1.00 32.98 ? 423  HIS B CB    1 
ATOM   11846 C CG    . HIS B  1 425  ? -15.626 21.855  111.375 1.00 38.23 ? 423  HIS B CG    1 
ATOM   11847 N ND1   . HIS B  1 425  ? -14.489 22.619  111.216 1.00 41.85 ? 423  HIS B ND1   1 
ATOM   11848 C CD2   . HIS B  1 425  ? -15.322 20.917  112.301 1.00 38.28 ? 423  HIS B CD2   1 
ATOM   11849 C CE1   . HIS B  1 425  ? -13.540 22.167  112.018 1.00 40.47 ? 423  HIS B CE1   1 
ATOM   11850 N NE2   . HIS B  1 425  ? -14.021 21.135  112.688 1.00 35.41 ? 423  HIS B NE2   1 
ATOM   11851 N N     . ASN B  1 426  ? -19.495 20.572  108.716 1.00 39.27 ? 424  ASN B N     1 
ATOM   11852 C CA    . ASN B  1 426  ? -20.652 20.979  107.929 1.00 40.76 ? 424  ASN B CA    1 
ATOM   11853 C C     . ASN B  1 426  ? -21.861 20.168  108.380 1.00 37.34 ? 424  ASN B C     1 
ATOM   11854 O O     . ASN B  1 426  ? -21.882 18.942  108.234 1.00 43.66 ? 424  ASN B O     1 
ATOM   11855 C CB    . ASN B  1 426  ? -20.369 20.794  106.438 1.00 37.09 ? 424  ASN B CB    1 
ATOM   11856 C CG    . ASN B  1 426  ? -21.485 21.326  105.555 1.00 37.29 ? 424  ASN B CG    1 
ATOM   11857 O OD1   . ASN B  1 426  ? -22.668 21.146  105.849 1.00 40.21 ? 424  ASN B OD1   1 
ATOM   11858 N ND2   . ASN B  1 426  ? -21.111 21.986  104.466 1.00 36.41 ? 424  ASN B ND2   1 
ATOM   11859 N N     . ALA B  1 427  ? -22.860 20.860  108.938 1.00 42.87 ? 425  ALA B N     1 
ATOM   11860 C CA    . ALA B  1 427  ? -24.015 20.183  109.522 1.00 44.95 ? 425  ALA B CA    1 
ATOM   11861 C C     . ALA B  1 427  ? -24.772 19.367  108.483 1.00 42.97 ? 425  ALA B C     1 
ATOM   11862 O O     . ALA B  1 427  ? -25.301 18.288  108.790 1.00 37.07 ? 425  ALA B O     1 
ATOM   11863 C CB    . ALA B  1 427  ? -24.942 21.208  110.175 1.00 42.82 ? 425  ALA B CB    1 
ATOM   11864 N N     . GLN B  1 428  ? -24.841 19.867  107.249 1.00 41.77 ? 426  GLN B N     1 
ATOM   11865 C CA    . GLN B  1 428  ? -25.531 19.133  106.193 1.00 40.42 ? 426  GLN B CA    1 
ATOM   11866 C C     . GLN B  1 428  ? -24.772 17.863  105.822 1.00 43.07 ? 426  GLN B C     1 
ATOM   11867 O O     . GLN B  1 428  ? -25.374 16.789  105.684 1.00 42.69 ? 426  GLN B O     1 
ATOM   11868 C CB    . GLN B  1 428  ? -25.725 20.037  104.973 1.00 42.27 ? 426  GLN B CB    1 
ATOM   11869 C CG    . GLN B  1 428  ? -26.775 19.551  103.985 1.00 43.10 ? 426  GLN B CG    1 
ATOM   11870 C CD    . GLN B  1 428  ? -26.303 18.374  103.152 1.00 45.40 ? 426  GLN B CD    1 
ATOM   11871 O OE1   . GLN B  1 428  ? -25.142 18.319  102.741 1.00 44.92 ? 426  GLN B OE1   1 
ATOM   11872 N NE2   . GLN B  1 428  ? -27.199 17.423  102.903 1.00 41.65 ? 426  GLN B NE2   1 
ATOM   11873 N N     . THR B  1 429  ? -23.448 17.969  105.644 1.00 41.73 ? 427  THR B N     1 
ATOM   11874 C CA    . THR B  1 429  ? -22.631 16.785  105.386 1.00 41.83 ? 427  THR B CA    1 
ATOM   11875 C C     . THR B  1 429  ? -22.813 15.742  106.485 1.00 41.26 ? 427  THR B C     1 
ATOM   11876 O O     . THR B  1 429  ? -23.019 14.553  106.206 1.00 40.42 ? 427  THR B O     1 
ATOM   11877 C CB    . THR B  1 429  ? -21.153 17.176  105.268 1.00 39.34 ? 427  THR B CB    1 
ATOM   11878 O OG1   . THR B  1 429  ? -20.993 18.202  104.281 1.00 41.54 ? 427  THR B OG1   1 
ATOM   11879 C CG2   . THR B  1 429  ? -20.320 15.967  104.883 1.00 35.66 ? 427  THR B CG2   1 
ATOM   11880 N N     . LEU B  1 430  ? -22.729 16.173  107.747 1.00 41.76 ? 428  LEU B N     1 
ATOM   11881 C CA    . LEU B  1 430  ? -22.852 15.251  108.876 1.00 42.69 ? 428  LEU B CA    1 
ATOM   11882 C C     . LEU B  1 430  ? -24.204 14.540  108.876 1.00 43.33 ? 428  LEU B C     1 
ATOM   11883 O O     . LEU B  1 430  ? -24.278 13.311  109.024 1.00 40.51 ? 428  LEU B O     1 
ATOM   11884 C CB    . LEU B  1 430  ? -22.646 16.022  110.182 1.00 43.54 ? 428  LEU B CB    1 
ATOM   11885 C CG    . LEU B  1 430  ? -22.430 15.328  111.530 1.00 41.03 ? 428  LEU B CG    1 
ATOM   11886 C CD1   . LEU B  1 430  ? -22.100 16.382  112.578 1.00 40.82 ? 428  LEU B CD1   1 
ATOM   11887 C CD2   . LEU B  1 430  ? -23.616 14.486  112.003 1.00 46.28 ? 428  LEU B CD2   1 
ATOM   11888 N N     . ALA B  1 431  ? -25.289 15.304  108.747 1.00 44.25 ? 429  ALA B N     1 
ATOM   11889 C CA    . ALA B  1 431  ? -26.619 14.697  108.782 1.00 46.47 ? 429  ALA B CA    1 
ATOM   11890 C C     . ALA B  1 431  ? -26.800 13.694  107.649 1.00 46.36 ? 429  ALA B C     1 
ATOM   11891 O O     . ALA B  1 431  ? -27.400 12.628  107.844 1.00 43.40 ? 429  ALA B O     1 
ATOM   11892 C CB    . ALA B  1 431  ? -27.695 15.780  108.718 1.00 42.48 ? 429  ALA B CB    1 
ATOM   11893 N N     . ALA B  1 432  ? -26.271 14.013  106.459 1.00 45.14 ? 430  ALA B N     1 
ATOM   11894 C CA    . ALA B  1 432  ? -26.355 13.089  105.332 1.00 43.38 ? 430  ALA B CA    1 
ATOM   11895 C C     . ALA B  1 432  ? -25.682 11.762  105.655 1.00 46.99 ? 430  ALA B C     1 
ATOM   11896 O O     . ALA B  1 432  ? -26.223 10.692  105.358 1.00 43.68 ? 430  ALA B O     1 
ATOM   11897 C CB    . ALA B  1 432  ? -25.722 13.717  104.088 1.00 45.28 ? 430  ALA B CB    1 
ATOM   11898 N N     . ILE B  1 433  ? -24.497 11.809  106.267 1.00 42.56 ? 431  ILE B N     1 
ATOM   11899 C CA    . ILE B  1 433  ? -23.783 10.576  106.573 1.00 45.23 ? 431  ILE B CA    1 
ATOM   11900 C C     . ILE B  1 433  ? -24.449 9.851   107.732 1.00 44.45 ? 431  ILE B C     1 
ATOM   11901 O O     . ILE B  1 433  ? -24.571 8.619   107.728 1.00 43.20 ? 431  ILE B O     1 
ATOM   11902 C CB    . ILE B  1 433  ? -22.306 10.875  106.876 1.00 40.23 ? 431  ILE B CB    1 
ATOM   11903 C CG1   . ILE B  1 433  ? -21.623 11.442  105.632 1.00 46.13 ? 431  ILE B CG1   1 
ATOM   11904 C CG2   . ILE B  1 433  ? -21.604 9.613   107.370 1.00 39.30 ? 431  ILE B CG2   1 
ATOM   11905 C CD1   . ILE B  1 433  ? -20.158 11.494  105.764 1.00 41.65 ? 431  ILE B CD1   1 
ATOM   11906 N N     . TYR B  1 434  ? -24.877 10.603  108.742 1.00 46.39 ? 432  TYR B N     1 
ATOM   11907 C CA    . TYR B  1 434  ? -25.544 10.009  109.894 1.00 45.22 ? 432  TYR B CA    1 
ATOM   11908 C C     . TYR B  1 434  ? -26.699 9.111   109.459 1.00 49.96 ? 432  TYR B C     1 
ATOM   11909 O O     . TYR B  1 434  ? -26.827 7.969   109.917 1.00 50.41 ? 432  TYR B O     1 
ATOM   11910 C CB    . TYR B  1 434  ? -26.020 11.129  110.818 1.00 46.07 ? 432  TYR B CB    1 
ATOM   11911 C CG    . TYR B  1 434  ? -26.910 10.682  111.946 1.00 47.45 ? 432  TYR B CG    1 
ATOM   11912 C CD1   . TYR B  1 434  ? -26.413 9.897   112.984 1.00 47.94 ? 432  TYR B CD1   1 
ATOM   11913 C CD2   . TYR B  1 434  ? -28.247 11.062  111.989 1.00 48.56 ? 432  TYR B CD2   1 
ATOM   11914 C CE1   . TYR B  1 434  ? -27.232 9.495   114.028 1.00 53.65 ? 432  TYR B CE1   1 
ATOM   11915 C CE2   . TYR B  1 434  ? -29.074 10.663  113.031 1.00 47.48 ? 432  TYR B CE2   1 
ATOM   11916 C CZ    . TYR B  1 434  ? -28.562 9.881   114.044 1.00 49.38 ? 432  TYR B CZ    1 
ATOM   11917 O OH    . TYR B  1 434  ? -29.376 9.483   115.078 1.00 57.54 ? 432  TYR B OH    1 
ATOM   11918 N N     . HIS B  1 435  ? -27.524 9.593   108.536 1.00 48.39 ? 433  HIS B N     1 
ATOM   11919 C CA    . HIS B  1 435  ? -28.665 8.796   108.104 1.00 52.77 ? 433  HIS B CA    1 
ATOM   11920 C C     . HIS B  1 435  ? -28.270 7.719   107.103 1.00 53.81 ? 433  HIS B C     1 
ATOM   11921 O O     . HIS B  1 435  ? -28.853 6.629   107.113 1.00 50.65 ? 433  HIS B O     1 
ATOM   11922 C CB    . HIS B  1 435  ? -29.739 9.712   107.532 1.00 47.89 ? 433  HIS B CB    1 
ATOM   11923 C CG    . HIS B  1 435  ? -30.413 10.548  108.572 1.00 52.33 ? 433  HIS B CG    1 
ATOM   11924 N ND1   . HIS B  1 435  ? -31.340 10.030  109.451 1.00 52.59 ? 433  HIS B ND1   1 
ATOM   11925 C CD2   . HIS B  1 435  ? -30.273 11.855  108.898 1.00 50.27 ? 433  HIS B CD2   1 
ATOM   11926 C CE1   . HIS B  1 435  ? -31.756 10.986  110.262 1.00 49.69 ? 433  HIS B CE1   1 
ATOM   11927 N NE2   . HIS B  1 435  ? -31.128 12.103  109.946 1.00 51.04 ? 433  HIS B NE2   1 
ATOM   11928 N N     . MET B  1 436  ? -27.277 7.990   106.255 1.00 51.57 ? 434  MET B N     1 
ATOM   11929 C CA    . MET B  1 436  ? -26.787 6.966   105.337 1.00 48.95 ? 434  MET B CA    1 
ATOM   11930 C C     . MET B  1 436  ? -26.252 5.759   106.097 1.00 52.49 ? 434  MET B C     1 
ATOM   11931 O O     . MET B  1 436  ? -26.436 4.613   105.668 1.00 50.42 ? 434  MET B O     1 
ATOM   11932 C CB    . MET B  1 436  ? -25.707 7.565   104.433 1.00 50.18 ? 434  MET B CB    1 
ATOM   11933 C CG    . MET B  1 436  ? -24.955 6.571   103.560 1.00 51.33 ? 434  MET B CG    1 
ATOM   11934 S SD    . MET B  1 436  ? -23.567 7.354   102.698 1.00 53.42 ? 434  MET B SD    1 
ATOM   11935 C CE    . MET B  1 436  ? -24.354 8.833   102.076 1.00 46.07 ? 434  MET B CE    1 
ATOM   11936 N N     . ALA B  1 437  ? -25.611 5.998   107.248 1.00 49.69 ? 435  ALA B N     1 
ATOM   11937 C CA    . ALA B  1 437  ? -24.983 4.921   108.004 1.00 52.93 ? 435  ALA B CA    1 
ATOM   11938 C C     . ALA B  1 437  ? -26.005 3.944   108.568 1.00 58.05 ? 435  ALA B C     1 
ATOM   11939 O O     . ALA B  1 437  ? -25.676 2.773   108.794 1.00 57.58 ? 435  ALA B O     1 
ATOM   11940 C CB    . ALA B  1 437  ? -24.128 5.503   109.132 1.00 50.71 ? 435  ALA B CB    1 
ATOM   11941 N N     . GLY B  1 438  ? -27.235 4.394   108.810 1.00 62.28 ? 436  GLY B N     1 
ATOM   11942 C CA    . GLY B  1 438  ? -28.276 3.496   109.271 1.00 61.18 ? 436  GLY B CA    1 
ATOM   11943 C C     . GLY B  1 438  ? -28.483 3.511   110.771 1.00 65.94 ? 436  GLY B C     1 
ATOM   11944 O O     . GLY B  1 438  ? -28.257 4.536   111.424 1.00 70.15 ? 436  GLY B O     1 
ATOM   11945 N N     . LYS B  1 439  ? -28.901 2.374   111.330 1.00 62.05 ? 437  LYS B N     1 
ATOM   11946 C CA    . LYS B  1 439  ? -29.271 2.285   112.738 1.00 61.54 ? 437  LYS B CA    1 
ATOM   11947 C C     . LYS B  1 439  ? -28.390 1.359   113.566 1.00 63.11 ? 437  LYS B C     1 
ATOM   11948 O O     . LYS B  1 439  ? -28.211 1.617   114.759 1.00 63.60 ? 437  LYS B O     1 
ATOM   11949 C CB    . LYS B  1 439  ? -30.736 1.824   112.872 1.00 63.40 ? 437  LYS B CB    1 
ATOM   11950 N N     . ASP B  1 440  ? -27.847 0.291   112.983 1.00 62.83 ? 438  ASP B N     1 
ATOM   11951 C CA    . ASP B  1 440  ? -27.074 -0.690  113.742 1.00 62.04 ? 438  ASP B CA    1 
ATOM   11952 C C     . ASP B  1 440  ? -25.665 -0.154  113.951 1.00 66.23 ? 438  ASP B C     1 
ATOM   11953 O O     . ASP B  1 440  ? -24.857 -0.136  113.016 1.00 68.80 ? 438  ASP B O     1 
ATOM   11954 C CB    . ASP B  1 440  ? -27.046 -2.030  113.014 1.00 66.41 ? 438  ASP B CB    1 
ATOM   11955 N N     . PHE B  1 441  ? -25.363 0.286   115.173 1.00 57.80 ? 439  PHE B N     1 
ATOM   11956 C CA    . PHE B  1 441  ? -24.086 0.919   115.458 1.00 59.79 ? 439  PHE B CA    1 
ATOM   11957 C C     . PHE B  1 441  ? -23.419 0.289   116.672 1.00 62.42 ? 439  PHE B C     1 
ATOM   11958 O O     . PHE B  1 441  ? -24.080 -0.124  117.630 1.00 60.08 ? 439  PHE B O     1 
ATOM   11959 C CB    . PHE B  1 441  ? -24.233 2.431   115.700 1.00 55.18 ? 439  PHE B CB    1 
ATOM   11960 C CG    . PHE B  1 441  ? -22.914 3.149   115.840 1.00 58.81 ? 439  PHE B CG    1 
ATOM   11961 C CD1   . PHE B  1 441  ? -22.270 3.666   114.725 1.00 52.21 ? 439  PHE B CD1   1 
ATOM   11962 C CD2   . PHE B  1 441  ? -22.313 3.298   117.083 1.00 56.07 ? 439  PHE B CD2   1 
ATOM   11963 C CE1   . PHE B  1 441  ? -21.057 4.322   114.843 1.00 47.55 ? 439  PHE B CE1   1 
ATOM   11964 C CE2   . PHE B  1 441  ? -21.093 3.950   117.212 1.00 53.34 ? 439  PHE B CE2   1 
ATOM   11965 C CZ    . PHE B  1 441  ? -20.464 4.464   116.091 1.00 54.33 ? 439  PHE B CZ    1 
ATOM   11966 N N     . HIS B  1 442  ? -22.089 0.235   116.610 1.00 58.96 ? 440  HIS B N     1 
ATOM   11967 C CA    . HIS B  1 442  ? -21.236 -0.062  117.750 1.00 55.85 ? 440  HIS B CA    1 
ATOM   11968 C C     . HIS B  1 442  ? -19.979 0.787   117.632 1.00 53.21 ? 440  HIS B C     1 
ATOM   11969 O O     . HIS B  1 442  ? -19.528 1.097   116.525 1.00 50.13 ? 440  HIS B O     1 
ATOM   11970 C CB    . HIS B  1 442  ? -20.875 -1.555  117.824 1.00 58.32 ? 440  HIS B CB    1 
ATOM   11971 C CG    . HIS B  1 442  ? -20.180 -2.074  116.601 1.00 58.99 ? 440  HIS B CG    1 
ATOM   11972 N ND1   . HIS B  1 442  ? -18.810 -2.043  116.452 1.00 56.33 ? 440  HIS B ND1   1 
ATOM   11973 C CD2   . HIS B  1 442  ? -20.669 -2.635  115.468 1.00 56.53 ? 440  HIS B CD2   1 
ATOM   11974 C CE1   . HIS B  1 442  ? -18.484 -2.563  115.282 1.00 56.66 ? 440  HIS B CE1   1 
ATOM   11975 N NE2   . HIS B  1 442  ? -19.594 -2.933  114.667 1.00 61.67 ? 440  HIS B NE2   1 
ATOM   11976 N N     . VAL B  1 443  ? -19.427 1.193   118.778 1.00 53.23 ? 441  VAL B N     1 
ATOM   11977 C CA    . VAL B  1 443  ? -18.170 1.930   118.754 1.00 47.91 ? 441  VAL B CA    1 
ATOM   11978 C C     . VAL B  1 443  ? -17.113 1.056   118.092 1.00 49.79 ? 441  VAL B C     1 
ATOM   11979 O O     . VAL B  1 443  ? -17.019 -0.148  118.358 1.00 49.43 ? 441  VAL B O     1 
ATOM   11980 C CB    . VAL B  1 443  ? -17.773 2.373   120.171 1.00 54.46 ? 441  VAL B CB    1 
ATOM   11981 C CG1   . VAL B  1 443  ? -16.358 2.942   120.182 1.00 46.47 ? 441  VAL B CG1   1 
ATOM   11982 C CG2   . VAL B  1 443  ? -18.756 3.419   120.687 1.00 53.65 ? 441  VAL B CG2   1 
ATOM   11983 N N     . GLY B  1 444  ? -16.349 1.647   117.176 1.00 47.36 ? 442  GLY B N     1 
ATOM   11984 C CA    . GLY B  1 444  ? -15.434 0.897   116.347 1.00 44.01 ? 442  GLY B CA    1 
ATOM   11985 C C     . GLY B  1 444  ? -15.944 0.639   114.944 1.00 47.04 ? 442  GLY B C     1 
ATOM   11986 O O     . GLY B  1 444  ? -15.154 0.236   114.080 1.00 44.16 ? 442  GLY B O     1 
ATOM   11987 N N     . LYS B  1 445  ? -17.237 0.862   114.698 1.00 45.83 ? 443  LYS B N     1 
ATOM   11988 C CA    . LYS B  1 445  ? -17.779 0.760   113.346 1.00 46.95 ? 443  LYS B CA    1 
ATOM   11989 C C     . LYS B  1 445  ? -17.312 1.930   112.489 1.00 46.02 ? 443  LYS B C     1 
ATOM   11990 O O     . LYS B  1 445  ? -16.628 1.741   111.476 1.00 45.03 ? 443  LYS B O     1 
ATOM   11991 C CB    . LYS B  1 445  ? -19.308 0.696   113.401 1.00 45.28 ? 443  LYS B CB    1 
ATOM   11992 N N     . TYR B  1 446  ? -17.682 3.149   112.878 1.00 44.22 ? 444  TYR B N     1 
ATOM   11993 C CA    . TYR B  1 446  ? -17.126 4.368   112.308 1.00 42.62 ? 444  TYR B CA    1 
ATOM   11994 C C     . TYR B  1 446  ? -17.137 5.445   113.391 1.00 45.57 ? 444  TYR B C     1 
ATOM   11995 O O     . TYR B  1 446  ? -17.579 5.212   114.521 1.00 41.59 ? 444  TYR B O     1 
ATOM   11996 C CB    . TYR B  1 446  ? -17.900 4.808   111.060 1.00 38.06 ? 444  TYR B CB    1 
ATOM   11997 C CG    . TYR B  1 446  ? -19.296 5.308   111.343 1.00 43.53 ? 444  TYR B CG    1 
ATOM   11998 C CD1   . TYR B  1 446  ? -20.378 4.438   111.339 1.00 44.66 ? 444  TYR B CD1   1 
ATOM   11999 C CD2   . TYR B  1 446  ? -19.536 6.652   111.599 1.00 41.54 ? 444  TYR B CD2   1 
ATOM   12000 C CE1   . TYR B  1 446  ? -21.660 4.892   111.589 1.00 46.68 ? 444  TYR B CE1   1 
ATOM   12001 C CE2   . TYR B  1 446  ? -20.813 7.113   111.860 1.00 43.47 ? 444  TYR B CE2   1 
ATOM   12002 C CZ    . TYR B  1 446  ? -21.871 6.230   111.850 1.00 48.11 ? 444  TYR B CZ    1 
ATOM   12003 O OH    . TYR B  1 446  ? -23.146 6.686   112.101 1.00 49.73 ? 444  TYR B OH    1 
ATOM   12004 N N     . GLU B  1 447  ? -16.644 6.634   113.039 1.00 39.78 ? 445  GLU B N     1 
ATOM   12005 C CA    . GLU B  1 447  ? -16.660 7.761   113.959 1.00 35.82 ? 445  GLU B CA    1 
ATOM   12006 C C     . GLU B  1 447  ? -16.658 9.053   113.162 1.00 35.59 ? 445  GLU B C     1 
ATOM   12007 O O     . GLU B  1 447  ? -16.361 9.068   111.969 1.00 37.59 ? 445  GLU B O     1 
ATOM   12008 C CB    . GLU B  1 447  ? -15.455 7.730   114.908 1.00 37.66 ? 445  GLU B CB    1 
ATOM   12009 C CG    . GLU B  1 447  ? -14.173 8.199   114.235 1.00 35.01 ? 445  GLU B CG    1 
ATOM   12010 C CD    . GLU B  1 447  ? -12.972 8.201   115.170 1.00 38.13 ? 445  GLU B CD    1 
ATOM   12011 O OE1   . GLU B  1 447  ? -13.083 7.693   116.311 1.00 35.14 ? 445  GLU B OE1   1 
ATOM   12012 O OE2   . GLU B  1 447  ? -11.916 8.703   114.749 1.00 33.61 ? 445  GLU B OE2   1 
ATOM   12013 N N     . PHE B  1 448  ? -16.990 10.143  113.838 1.00 38.51 ? 446  PHE B N     1 
ATOM   12014 C CA    . PHE B  1 448  ? -16.852 11.484  113.291 1.00 35.90 ? 446  PHE B CA    1 
ATOM   12015 C C     . PHE B  1 448  ? -15.573 12.142  113.805 1.00 33.06 ? 446  PHE B C     1 
ATOM   12016 O O     . PHE B  1 448  ? -14.982 11.706  114.792 1.00 35.11 ? 446  PHE B O     1 
ATOM   12017 C CB    . PHE B  1 448  ? -18.059 12.343  113.663 1.00 38.75 ? 446  PHE B CB    1 
ATOM   12018 C CG    . PHE B  1 448  ? -19.318 11.960  112.947 1.00 36.08 ? 446  PHE B CG    1 
ATOM   12019 C CD1   . PHE B  1 448  ? -19.518 12.336  111.632 1.00 38.00 ? 446  PHE B CD1   1 
ATOM   12020 C CD2   . PHE B  1 448  ? -20.303 11.224  113.592 1.00 40.87 ? 446  PHE B CD2   1 
ATOM   12021 C CE1   . PHE B  1 448  ? -20.679 11.985  110.961 1.00 40.72 ? 446  PHE B CE1   1 
ATOM   12022 C CE2   . PHE B  1 448  ? -21.465 10.870  112.932 1.00 50.16 ? 446  PHE B CE2   1 
ATOM   12023 C CZ    . PHE B  1 448  ? -21.651 11.254  111.610 1.00 43.76 ? 446  PHE B CZ    1 
ATOM   12024 N N     . GLN B  1 449  ? -15.149 13.215  113.132 1.00 35.50 ? 447  GLN B N     1 
ATOM   12025 C CA    . GLN B  1 449  ? -13.994 13.966  113.613 1.00 33.62 ? 447  GLN B CA    1 
ATOM   12026 C C     . GLN B  1 449  ? -14.213 15.458  113.410 1.00 36.12 ? 447  GLN B C     1 
ATOM   12027 O O     . GLN B  1 449  ? -14.959 15.877  112.525 1.00 36.71 ? 447  GLN B O     1 
ATOM   12028 C CB    . GLN B  1 449  ? -12.689 13.535  112.927 1.00 29.28 ? 447  GLN B CB    1 
ATOM   12029 C CG    . GLN B  1 449  ? -12.300 12.086  113.156 1.00 33.80 ? 447  GLN B CG    1 
ATOM   12030 C CD    . GLN B  1 449  ? -10.836 11.823  112.870 1.00 33.83 ? 447  GLN B CD    1 
ATOM   12031 O OE1   . GLN B  1 449  ? -10.151 12.662  112.289 1.00 30.47 ? 447  GLN B OE1   1 
ATOM   12032 N NE2   . GLN B  1 449  ? -10.347 10.653  113.282 1.00 32.51 ? 447  GLN B NE2   1 
ATOM   12033 N N     . CYS B  1 450  ? -13.551 16.257  114.247 1.00 32.86 ? 448  CYS B N     1 
ATOM   12034 C CA    . CYS B  1 450  ? -13.627 17.709  114.154 1.00 32.57 ? 448  CYS B CA    1 
ATOM   12035 C C     . CYS B  1 450  ? -12.332 18.308  114.694 1.00 34.49 ? 448  CYS B C     1 
ATOM   12036 O O     . CYS B  1 450  ? -11.509 17.617  115.300 1.00 29.48 ? 448  CYS B O     1 
ATOM   12037 C CB    . CYS B  1 450  ? -14.836 18.259  114.922 1.00 35.68 ? 448  CYS B CB    1 
ATOM   12038 S SG    . CYS B  1 450  ? -14.619 18.319  116.742 1.00 39.95 ? 448  CYS B SG    1 
ATOM   12039 N N     . LEU B  1 451  ? -12.163 19.610  114.474 1.00 33.63 ? 449  LEU B N     1 
ATOM   12040 C CA    . LEU B  1 451  ? -10.980 20.319  114.944 1.00 32.53 ? 449  LEU B CA    1 
ATOM   12041 C C     . LEU B  1 451  ? -11.231 20.927  116.315 1.00 35.33 ? 449  LEU B C     1 
ATOM   12042 O O     . LEU B  1 451  ? -12.340 21.376  116.616 1.00 36.18 ? 449  LEU B O     1 
ATOM   12043 C CB    . LEU B  1 451  ? -10.573 21.417  113.959 1.00 36.38 ? 449  LEU B CB    1 
ATOM   12044 N N     . HIS B  1 452  ? -10.182 20.938  117.144 1.00 34.16 ? 450  HIS B N     1 
ATOM   12045 C CA    . HIS B  1 452  ? -10.261 21.562  118.457 1.00 41.19 ? 450  HIS B CA    1 
ATOM   12046 C C     . HIS B  1 452  ? -10.714 23.010  118.344 1.00 35.02 ? 450  HIS B C     1 
ATOM   12047 O O     . HIS B  1 452  ? -10.290 23.744  117.450 1.00 35.86 ? 450  HIS B O     1 
ATOM   12048 C CB    . HIS B  1 452  ? -8.903  21.506  119.158 1.00 35.96 ? 450  HIS B CB    1 
ATOM   12049 C CG    . HIS B  1 452  ? -8.827  22.381  120.371 1.00 37.01 ? 450  HIS B CG    1 
ATOM   12050 N ND1   . HIS B  1 452  ? -9.385  22.027  121.580 1.00 41.54 ? 450  HIS B ND1   1 
ATOM   12051 C CD2   . HIS B  1 452  ? -8.291  23.611  120.550 1.00 41.72 ? 450  HIS B CD2   1 
ATOM   12052 C CE1   . HIS B  1 452  ? -9.178  22.993  122.459 1.00 42.10 ? 450  HIS B CE1   1 
ATOM   12053 N NE2   . HIS B  1 452  ? -8.522  23.969  121.857 1.00 38.21 ? 450  HIS B NE2   1 
ATOM   12054 N N     . GLY B  1 453  ? -11.576 23.416  119.265 1.00 39.52 ? 451  GLY B N     1 
ATOM   12055 C CA    . GLY B  1 453  ? -12.076 24.789  119.305 1.00 40.03 ? 451  GLY B CA    1 
ATOM   12056 C C     . GLY B  1 453  ? -13.210 25.067  118.348 1.00 45.30 ? 451  GLY B C     1 
ATOM   12057 O O     . GLY B  1 453  ? -14.273 25.540  118.760 1.00 51.96 ? 451  GLY B O     1 
ATOM   12058 N N     . MET B  1 454  ? -13.021 24.745  117.072 1.00 41.44 ? 452  MET B N     1 
ATOM   12059 C CA    . MET B  1 454  ? -14.014 25.065  116.055 1.00 44.68 ? 452  MET B CA    1 
ATOM   12060 C C     . MET B  1 454  ? -15.168 24.072  116.056 1.00 43.35 ? 452  MET B C     1 
ATOM   12061 O O     . MET B  1 454  ? -16.330 24.473  115.953 1.00 48.17 ? 452  MET B O     1 
ATOM   12062 C CB    . MET B  1 454  ? -13.346 25.098  114.679 1.00 45.89 ? 452  MET B CB    1 
ATOM   12063 C CG    . MET B  1 454  ? -14.220 25.645  113.552 1.00 47.62 ? 452  MET B CG    1 
ATOM   12064 S SD    . MET B  1 454  ? -14.380 27.436  113.670 1.00 66.48 ? 452  MET B SD    1 
ATOM   12065 C CE    . MET B  1 454  ? -12.663 27.908  113.889 1.00 60.08 ? 452  MET B CE    1 
ATOM   12066 N N     . GLY B  1 455  ? -14.868 22.781  116.175 1.00 42.58 ? 453  GLY B N     1 
ATOM   12067 C CA    . GLY B  1 455  ? -15.838 21.733  115.935 1.00 42.98 ? 453  GLY B CA    1 
ATOM   12068 C C     . GLY B  1 455  ? -16.726 21.352  117.086 1.00 48.75 ? 453  GLY B C     1 
ATOM   12069 O O     . GLY B  1 455  ? -17.734 20.676  116.864 1.00 46.19 ? 453  GLY B O     1 
ATOM   12070 N N     . GLU B  1 456  ? -16.383 21.756  118.312 1.00 49.20 ? 454  GLU B N     1 
ATOM   12071 C CA    . GLU B  1 456  ? -17.141 21.348  119.488 1.00 51.70 ? 454  GLU B CA    1 
ATOM   12072 C C     . GLU B  1 456  ? -18.575 21.876  119.516 1.00 50.75 ? 454  GLU B C     1 
ATOM   12073 O O     . GLU B  1 456  ? -19.473 21.128  119.921 1.00 51.56 ? 454  GLU B O     1 
ATOM   12074 C CB    . GLU B  1 456  ? -16.421 21.777  120.769 1.00 54.31 ? 454  GLU B CB    1 
ATOM   12075 C CG    . GLU B  1 456  ? -15.151 21.008  121.062 1.00 55.97 ? 454  GLU B CG    1 
ATOM   12076 C CD    . GLU B  1 456  ? -13.937 21.671  120.461 1.00 53.05 ? 454  GLU B CD    1 
ATOM   12077 O OE1   . GLU B  1 456  ? -14.077 22.272  119.375 1.00 53.94 ? 454  GLU B OE1   1 
ATOM   12078 O OE2   . GLU B  1 456  ? -12.852 21.606  121.081 1.00 49.11 ? 454  GLU B OE2   1 
ATOM   12079 N N     . PRO B  1 457  ? -18.842 23.140  119.148 1.00 46.99 ? 455  PRO B N     1 
ATOM   12080 C CA    . PRO B  1 457  ? -20.242 23.599  119.132 1.00 53.21 ? 455  PRO B CA    1 
ATOM   12081 C C     . PRO B  1 457  ? -21.174 22.693  118.343 1.00 53.10 ? 455  PRO B C     1 
ATOM   12082 O O     . PRO B  1 457  ? -22.361 22.592  118.677 1.00 53.21 ? 455  PRO B O     1 
ATOM   12083 C CB    . PRO B  1 457  ? -20.142 24.991  118.496 1.00 52.98 ? 455  PRO B CB    1 
ATOM   12084 C CG    . PRO B  1 457  ? -18.793 25.462  118.861 1.00 49.29 ? 455  PRO B CG    1 
ATOM   12085 C CD    . PRO B  1 457  ? -17.920 24.243  118.807 1.00 50.53 ? 455  PRO B CD    1 
ATOM   12086 N N     . LEU B  1 458  ? -20.669 22.017  117.312 1.00 50.65 ? 456  LEU B N     1 
ATOM   12087 C CA    . LEU B  1 458  ? -21.501 21.132  116.510 1.00 47.95 ? 456  LEU B CA    1 
ATOM   12088 C C     . LEU B  1 458  ? -21.586 19.735  117.109 1.00 47.80 ? 456  LEU B C     1 
ATOM   12089 O O     . LEU B  1 458  ? -22.676 19.168  117.224 1.00 44.91 ? 456  LEU B O     1 
ATOM   12090 C CB    . LEU B  1 458  ? -20.964 21.054  115.072 1.00 46.66 ? 456  LEU B CB    1 
ATOM   12091 C CG    . LEU B  1 458  ? -21.657 20.034  114.164 1.00 45.30 ? 456  LEU B CG    1 
ATOM   12092 C CD1   . LEU B  1 458  ? -23.120 20.385  113.996 1.00 43.37 ? 456  LEU B CD1   1 
ATOM   12093 C CD2   . LEU B  1 458  ? -20.971 19.932  112.807 1.00 45.04 ? 456  LEU B CD2   1 
ATOM   12094 N N     . TYR B  1 459  ? -20.453 19.169  117.507 1.00 47.22 ? 457  TYR B N     1 
ATOM   12095 C CA    . TYR B  1 459  ? -20.447 17.755  117.847 1.00 47.27 ? 457  TYR B CA    1 
ATOM   12096 C C     . TYR B  1 459  ? -20.921 17.467  119.266 1.00 48.42 ? 457  TYR B C     1 
ATOM   12097 O O     . TYR B  1 459  ? -21.063 16.294  119.630 1.00 47.70 ? 457  TYR B O     1 
ATOM   12098 C CB    . TYR B  1 459  ? -19.056 17.182  117.590 1.00 42.41 ? 457  TYR B CB    1 
ATOM   12099 C CG    . TYR B  1 459  ? -18.884 16.897  116.118 1.00 42.32 ? 457  TYR B CG    1 
ATOM   12100 C CD1   . TYR B  1 459  ? -19.280 15.679  115.590 1.00 41.36 ? 457  TYR B CD1   1 
ATOM   12101 C CD2   . TYR B  1 459  ? -18.386 17.863  115.249 1.00 43.74 ? 457  TYR B CD2   1 
ATOM   12102 C CE1   . TYR B  1 459  ? -19.163 15.413  114.247 1.00 42.44 ? 457  TYR B CE1   1 
ATOM   12103 C CE2   . TYR B  1 459  ? -18.254 17.601  113.888 1.00 39.39 ? 457  TYR B CE2   1 
ATOM   12104 C CZ    . TYR B  1 459  ? -18.645 16.366  113.399 1.00 39.29 ? 457  TYR B CZ    1 
ATOM   12105 O OH    . TYR B  1 459  ? -18.536 16.069  112.058 1.00 41.36 ? 457  TYR B OH    1 
ATOM   12106 N N     . GLU B  1 460  ? -21.199 18.491  120.068 1.00 44.33 ? 458  GLU B N     1 
ATOM   12107 C CA    . GLU B  1 460  ? -21.883 18.209  121.321 1.00 56.79 ? 458  GLU B CA    1 
ATOM   12108 C C     . GLU B  1 460  ? -23.331 17.791  121.097 1.00 56.59 ? 458  GLU B C     1 
ATOM   12109 O O     . GLU B  1 460  ? -23.966 17.288  122.033 1.00 57.05 ? 458  GLU B O     1 
ATOM   12110 C CB    . GLU B  1 460  ? -21.805 19.419  122.252 1.00 59.06 ? 458  GLU B CB    1 
ATOM   12111 C CG    . GLU B  1 460  ? -22.174 20.740  121.608 1.00 58.50 ? 458  GLU B CG    1 
ATOM   12112 C CD    . GLU B  1 460  ? -21.758 21.925  122.462 1.00 63.75 ? 458  GLU B CD    1 
ATOM   12113 O OE1   . GLU B  1 460  ? -21.008 21.719  123.441 1.00 63.10 ? 458  GLU B OE1   1 
ATOM   12114 O OE2   . GLU B  1 460  ? -22.176 23.062  122.154 1.00 67.99 ? 458  GLU B OE2   1 
ATOM   12115 N N     . GLU B  1 461  ? -23.853 17.970  119.882 1.00 54.55 ? 459  GLU B N     1 
ATOM   12116 C CA    . GLU B  1 461  ? -25.177 17.504  119.497 1.00 59.35 ? 459  GLU B CA    1 
ATOM   12117 C C     . GLU B  1 461  ? -25.157 16.096  118.912 1.00 59.57 ? 459  GLU B C     1 
ATOM   12118 O O     . GLU B  1 461  ? -26.202 15.607  118.467 1.00 57.55 ? 459  GLU B O     1 
ATOM   12119 C CB    . GLU B  1 461  ? -25.801 18.475  118.491 1.00 53.19 ? 459  GLU B CB    1 
ATOM   12120 C CG    . GLU B  1 461  ? -25.533 19.950  118.795 1.00 51.97 ? 459  GLU B CG    1 
ATOM   12121 C CD    . GLU B  1 461  ? -26.236 20.434  120.057 1.00 65.67 ? 459  GLU B CD    1 
ATOM   12122 O OE1   . GLU B  1 461  ? -27.114 19.710  120.575 1.00 61.45 ? 459  GLU B OE1   1 
ATOM   12123 O OE2   . GLU B  1 461  ? -25.911 21.543  120.533 1.00 67.46 ? 459  GLU B OE2   1 
ATOM   12124 N N     . VAL B  1 462  ? -24.001 15.428  118.927 1.00 56.21 ? 460  VAL B N     1 
ATOM   12125 C CA    . VAL B  1 462  ? -23.804 14.145  118.263 1.00 54.91 ? 460  VAL B CA    1 
ATOM   12126 C C     . VAL B  1 462  ? -23.385 13.064  119.252 1.00 54.88 ? 460  VAL B C     1 
ATOM   12127 O O     . VAL B  1 462  ? -23.933 11.954  119.253 1.00 47.65 ? 460  VAL B O     1 
ATOM   12128 C CB    . VAL B  1 462  ? -22.766 14.260  117.123 1.00 48.70 ? 460  VAL B CB    1 
ATOM   12129 C CG1   . VAL B  1 462  ? -22.605 12.926  116.410 1.00 45.99 ? 460  VAL B CG1   1 
ATOM   12130 C CG2   . VAL B  1 462  ? -23.151 15.371  116.158 1.00 47.17 ? 460  VAL B CG2   1 
ATOM   12131 N N     . VAL B  1 463  ? -22.399 13.364  120.089 1.00 49.30 ? 461  VAL B N     1 
ATOM   12132 C CA    . VAL B  1 463  ? -21.831 12.377  120.995 1.00 51.00 ? 461  VAL B CA    1 
ATOM   12133 C C     . VAL B  1 463  ? -22.791 12.139  122.151 1.00 53.28 ? 461  VAL B C     1 
ATOM   12134 O O     . VAL B  1 463  ? -23.328 13.090  122.733 1.00 55.29 ? 461  VAL B O     1 
ATOM   12135 C CB    . VAL B  1 463  ? -20.459 12.841  121.506 1.00 42.16 ? 461  VAL B CB    1 
ATOM   12136 C CG1   . VAL B  1 463  ? -19.843 11.773  122.384 1.00 52.71 ? 461  VAL B CG1   1 
ATOM   12137 C CG2   . VAL B  1 463  ? -19.540 13.186  120.333 1.00 47.25 ? 461  VAL B CG2   1 
ATOM   12138 N N     . GLY B  1 464  ? -23.005 10.876  122.483 1.00 51.76 ? 462  GLY B N     1 
ATOM   12139 C CA    . GLY B  1 464  ? -23.694 10.507  123.702 1.00 57.49 ? 462  GLY B CA    1 
ATOM   12140 C C     . GLY B  1 464  ? -25.049 9.875   123.434 1.00 64.02 ? 462  GLY B C     1 
ATOM   12141 O O     . GLY B  1 464  ? -25.705 10.143  122.420 1.00 62.21 ? 462  GLY B O     1 
ATOM   12142 N N     . ARG B  1 465  ? -25.485 9.028   124.374 1.00 64.81 ? 463  ARG B N     1 
ATOM   12143 C CA    . ARG B  1 465  ? -26.806 8.420   124.270 1.00 69.21 ? 463  ARG B CA    1 
ATOM   12144 C C     . ARG B  1 465  ? -27.917 9.463   124.238 1.00 72.28 ? 463  ARG B C     1 
ATOM   12145 O O     . ARG B  1 465  ? -29.009 9.172   123.738 1.00 71.15 ? 463  ARG B O     1 
ATOM   12146 C CB    . ARG B  1 465  ? -27.034 7.442   125.426 1.00 68.28 ? 463  ARG B CB    1 
ATOM   12147 N N     . GLY B  1 466  ? -27.660 10.673  124.744 1.00 70.32 ? 464  GLY B N     1 
ATOM   12148 C CA    . GLY B  1 466  ? -28.639 11.744  124.690 1.00 67.83 ? 464  GLY B CA    1 
ATOM   12149 C C     . GLY B  1 466  ? -28.716 12.491  123.374 1.00 76.31 ? 464  GLY B C     1 
ATOM   12150 O O     . GLY B  1 466  ? -29.675 13.240  123.158 1.00 73.94 ? 464  GLY B O     1 
ATOM   12151 N N     . LYS B  1 467  ? -27.733 12.309  122.492 1.00 73.24 ? 465  LYS B N     1 
ATOM   12152 C CA    . LYS B  1 467  ? -27.712 13.006  121.212 1.00 70.79 ? 465  LYS B CA    1 
ATOM   12153 C C     . LYS B  1 467  ? -27.947 12.042  120.056 1.00 73.35 ? 465  LYS B C     1 
ATOM   12154 O O     . LYS B  1 467  ? -28.991 11.382  119.994 1.00 74.51 ? 465  LYS B O     1 
ATOM   12155 C CB    . LYS B  1 467  ? -26.381 13.739  121.035 1.00 69.07 ? 465  LYS B CB    1 
ATOM   12156 C CG    . LYS B  1 467  ? -26.190 14.893  122.000 1.00 70.30 ? 465  LYS B CG    1 
ATOM   12157 C CD    . LYS B  1 467  ? -27.331 15.898  121.883 1.00 71.62 ? 465  LYS B CD    1 
ATOM   12158 C CE    . LYS B  1 467  ? -27.098 17.101  122.786 1.00 71.01 ? 465  LYS B CE    1 
ATOM   12159 N NZ    . LYS B  1 467  ? -27.961 18.261  122.425 1.00 65.72 ? 465  LYS B NZ    1 
ATOM   12160 N N     . LEU B  1 468  ? -26.993 11.963  119.130 1.00 55.36 ? 466  LEU B N     1 
ATOM   12161 C CA    . LEU B  1 468  ? -27.053 10.984  118.056 1.00 50.27 ? 466  LEU B CA    1 
ATOM   12162 C C     . LEU B  1 468  ? -26.339 9.688   118.408 1.00 56.13 ? 466  LEU B C     1 
ATOM   12163 O O     . LEU B  1 468  ? -26.385 8.738   117.620 1.00 55.02 ? 466  LEU B O     1 
ATOM   12164 C CB    . LEU B  1 468  ? -26.461 11.570  116.772 1.00 55.28 ? 466  LEU B CB    1 
ATOM   12165 N N     . ASP B  1 469  ? -25.685 9.631   119.572 1.00 54.35 ? 467  ASP B N     1 
ATOM   12166 C CA    . ASP B  1 469  ? -24.951 8.444   120.016 1.00 56.50 ? 467  ASP B CA    1 
ATOM   12167 C C     . ASP B  1 469  ? -23.869 8.061   119.012 1.00 48.50 ? 467  ASP B C     1 
ATOM   12168 O O     . ASP B  1 469  ? -23.689 6.889   118.674 1.00 55.54 ? 467  ASP B O     1 
ATOM   12169 C CB    . ASP B  1 469  ? -25.898 7.266   120.290 1.00 53.07 ? 467  ASP B CB    1 
ATOM   12170 N N     . ARG B  1 470  ? -23.139 9.060   118.529 1.00 50.77 ? 468  ARG B N     1 
ATOM   12171 C CA    . ARG B  1 470  ? -22.044 8.824   117.606 1.00 51.67 ? 468  ARG B CA    1 
ATOM   12172 C C     . ARG B  1 470  ? -20.805 9.536   118.137 1.00 43.05 ? 468  ARG B C     1 
ATOM   12173 O O     . ARG B  1 470  ? -20.883 10.714  118.520 1.00 45.21 ? 468  ARG B O     1 
ATOM   12174 C CB    . ARG B  1 470  ? -22.401 9.303   116.189 1.00 51.00 ? 468  ARG B CB    1 
ATOM   12175 C CG    . ARG B  1 470  ? -23.603 8.573   115.569 1.00 45.92 ? 468  ARG B CG    1 
ATOM   12176 C CD    . ARG B  1 470  ? -23.365 7.061   115.473 1.00 48.31 ? 468  ARG B CD    1 
ATOM   12177 N NE    . ARG B  1 470  ? -24.470 6.340   114.840 1.00 51.96 ? 468  ARG B NE    1 
ATOM   12178 C CZ    . ARG B  1 470  ? -25.476 5.770   115.492 1.00 53.58 ? 468  ARG B CZ    1 
ATOM   12179 N NH1   . ARG B  1 470  ? -25.567 5.826   116.810 1.00 53.42 ? 468  ARG B NH1   1 
ATOM   12180 N NH2   . ARG B  1 470  ? -26.415 5.126   114.805 1.00 49.88 ? 468  ARG B NH2   1 
ATOM   12181 N N     . PRO B  1 471  ? -19.660 8.868   118.194 1.00 46.55 ? 469  PRO B N     1 
ATOM   12182 C CA    . PRO B  1 471  ? -18.466 9.489   118.776 1.00 43.78 ? 469  PRO B CA    1 
ATOM   12183 C C     . PRO B  1 471  ? -17.789 10.458  117.815 1.00 45.41 ? 469  PRO B C     1 
ATOM   12184 O O     . PRO B  1 471  ? -17.930 10.380  116.591 1.00 43.90 ? 469  PRO B O     1 
ATOM   12185 C CB    . PRO B  1 471  ? -17.563 8.291   119.084 1.00 45.34 ? 469  PRO B CB    1 
ATOM   12186 C CG    . PRO B  1 471  ? -17.968 7.260   118.095 1.00 46.69 ? 469  PRO B CG    1 
ATOM   12187 C CD    . PRO B  1 471  ? -19.443 7.451   117.852 1.00 45.51 ? 469  PRO B CD    1 
ATOM   12188 N N     . CYS B  1 472  ? -17.059 11.405  118.402 1.00 41.61 ? 470  CYS B N     1 
ATOM   12189 C CA    . CYS B  1 472  ? -16.288 12.384  117.650 1.00 43.61 ? 470  CYS B CA    1 
ATOM   12190 C C     . CYS B  1 472  ? -14.870 12.429  118.195 1.00 42.26 ? 470  CYS B C     1 
ATOM   12191 O O     . CYS B  1 472  ? -14.673 12.562  119.408 1.00 40.15 ? 470  CYS B O     1 
ATOM   12192 C CB    . CYS B  1 472  ? -16.911 13.779  117.722 1.00 38.35 ? 470  CYS B CB    1 
ATOM   12193 S SG    . CYS B  1 472  ? -16.075 14.965  116.641 1.00 41.99 ? 470  CYS B SG    1 
ATOM   12194 N N     . ARG B  1 473  ? -13.890 12.309  117.303 1.00 36.87 ? 471  ARG B N     1 
ATOM   12195 C CA    . ARG B  1 473  ? -12.483 12.438  117.661 1.00 37.26 ? 471  ARG B CA    1 
ATOM   12196 C C     . ARG B  1 473  ? -12.016 13.841  117.315 1.00 37.76 ? 471  ARG B C     1 
ATOM   12197 O O     . ARG B  1 473  ? -12.175 14.291  116.174 1.00 31.94 ? 471  ARG B O     1 
ATOM   12198 C CB    . ARG B  1 473  ? -11.617 11.404  116.941 1.00 36.63 ? 471  ARG B CB    1 
ATOM   12199 C CG    . ARG B  1 473  ? -10.144 11.443  117.361 1.00 32.89 ? 471  ARG B CG    1 
ATOM   12200 C CD    . ARG B  1 473  ? -9.381  10.328  116.694 1.00 32.48 ? 471  ARG B CD    1 
ATOM   12201 N NE    . ARG B  1 473  ? -10.071 9.057   116.865 1.00 34.19 ? 471  ARG B NE    1 
ATOM   12202 C CZ    . ARG B  1 473  ? -9.892  8.249   117.897 1.00 36.05 ? 471  ARG B CZ    1 
ATOM   12203 N NH1   . ARG B  1 473  ? -9.020  8.535   118.850 1.00 34.68 ? 471  ARG B NH1   1 
ATOM   12204 N NH2   . ARG B  1 473  ? -10.597 7.124   117.971 1.00 35.62 ? 471  ARG B NH2   1 
ATOM   12205 N N     . ILE B  1 474  ? -11.440 14.522  118.298 1.00 35.06 ? 472  ILE B N     1 
ATOM   12206 C CA    . ILE B  1 474  ? -11.048 15.921  118.168 1.00 34.88 ? 472  ILE B CA    1 
ATOM   12207 C C     . ILE B  1 474  ? -9.584  15.992  117.746 1.00 34.33 ? 472  ILE B C     1 
ATOM   12208 O O     . ILE B  1 474  ? -8.696  15.487  118.443 1.00 30.40 ? 472  ILE B O     1 
ATOM   12209 C CB    . ILE B  1 474  ? -11.273 16.681  119.486 1.00 33.21 ? 472  ILE B CB    1 
ATOM   12210 C CG1   . ILE B  1 474  ? -12.762 16.702  119.844 1.00 37.63 ? 472  ILE B CG1   1 
ATOM   12211 C CG2   . ILE B  1 474  ? -10.715 18.088  119.394 1.00 36.18 ? 472  ILE B CG2   1 
ATOM   12212 C CD1   . ILE B  1 474  ? -13.093 17.598  121.004 1.00 38.79 ? 472  ILE B CD1   1 
ATOM   12213 N N     . TYR B  1 475  ? -9.336  16.628  116.611 1.00 33.69 ? 473  TYR B N     1 
ATOM   12214 C CA    . TYR B  1 475  ? -7.985  16.898  116.132 1.00 30.14 ? 473  TYR B CA    1 
ATOM   12215 C C     . TYR B  1 475  ? -7.412  18.048  116.947 1.00 33.33 ? 473  TYR B C     1 
ATOM   12216 O O     . TYR B  1 475  ? -7.876  19.189  116.846 1.00 33.86 ? 473  TYR B O     1 
ATOM   12217 C CB    . TYR B  1 475  ? -8.028  17.232  114.647 1.00 29.18 ? 473  TYR B CB    1 
ATOM   12218 C CG    . TYR B  1 475  ? -6.691  17.346  113.953 1.00 31.87 ? 473  TYR B CG    1 
ATOM   12219 C CD1   . TYR B  1 475  ? -6.023  18.559  113.897 1.00 34.57 ? 473  TYR B CD1   1 
ATOM   12220 C CD2   . TYR B  1 475  ? -6.119  16.249  113.322 1.00 25.73 ? 473  TYR B CD2   1 
ATOM   12221 C CE1   . TYR B  1 475  ? -4.807  18.675  113.242 1.00 37.06 ? 473  TYR B CE1   1 
ATOM   12222 C CE2   . TYR B  1 475  ? -4.902  16.353  112.671 1.00 29.80 ? 473  TYR B CE2   1 
ATOM   12223 C CZ    . TYR B  1 475  ? -4.254  17.566  112.629 1.00 34.36 ? 473  TYR B CZ    1 
ATOM   12224 O OH    . TYR B  1 475  ? -3.046  17.677  111.978 1.00 36.77 ? 473  TYR B OH    1 
ATOM   12225 N N     . ALA B  1 476  ? -6.402  17.749  117.755 1.00 29.59 ? 474  ALA B N     1 
ATOM   12226 C CA    . ALA B  1 476  ? -5.957  18.649  118.819 1.00 33.76 ? 474  ALA B CA    1 
ATOM   12227 C C     . ALA B  1 476  ? -4.547  19.157  118.555 1.00 34.30 ? 474  ALA B C     1 
ATOM   12228 O O     . ALA B  1 476  ? -3.569  18.427  118.797 1.00 28.13 ? 474  ALA B O     1 
ATOM   12229 C CB    . ALA B  1 476  ? -6.023  17.926  120.160 1.00 29.93 ? 474  ALA B CB    1 
ATOM   12230 N N     . PRO B  1 477  ? -4.390  20.392  118.076 1.00 30.83 ? 475  PRO B N     1 
ATOM   12231 C CA    . PRO B  1 477  ? -3.048  20.945  117.876 1.00 29.69 ? 475  PRO B CA    1 
ATOM   12232 C C     . PRO B  1 477  ? -2.349  21.164  119.202 1.00 31.25 ? 475  PRO B C     1 
ATOM   12233 O O     . PRO B  1 477  ? -2.967  21.517  120.211 1.00 32.17 ? 475  PRO B O     1 
ATOM   12234 C CB    . PRO B  1 477  ? -3.312  22.280  117.169 1.00 32.06 ? 475  PRO B CB    1 
ATOM   12235 C CG    . PRO B  1 477  ? -4.737  22.167  116.639 1.00 32.56 ? 475  PRO B CG    1 
ATOM   12236 C CD    . PRO B  1 477  ? -5.440  21.328  117.640 1.00 33.45 ? 475  PRO B CD    1 
ATOM   12237 N N     . VAL B  1 478  ? -1.039  20.940  119.191 1.00 26.81 ? 476  VAL B N     1 
ATOM   12238 C CA    . VAL B  1 478  ? -0.222  21.033  120.392 1.00 29.15 ? 476  VAL B CA    1 
ATOM   12239 C C     . VAL B  1 478  ? 1.086   21.709  120.013 1.00 33.93 ? 476  VAL B C     1 
ATOM   12240 O O     . VAL B  1 478  ? 1.816   21.209  119.150 1.00 32.88 ? 476  VAL B O     1 
ATOM   12241 C CB    . VAL B  1 478  ? 0.054   19.655  121.019 1.00 27.44 ? 476  VAL B CB    1 
ATOM   12242 C CG1   . VAL B  1 478  ? 0.913   19.807  122.249 1.00 32.04 ? 476  VAL B CG1   1 
ATOM   12243 C CG2   . VAL B  1 478  ? -1.241  18.956  121.382 1.00 30.80 ? 476  VAL B CG2   1 
ATOM   12244 N N     . GLY B  1 479  ? 1.378   22.837  120.644 1.00 37.06 ? 477  GLY B N     1 
ATOM   12245 C CA    . GLY B  1 479  ? 2.624   23.531  120.396 1.00 41.71 ? 477  GLY B CA    1 
ATOM   12246 C C     . GLY B  1 479  ? 2.528   25.009  120.732 1.00 47.20 ? 477  GLY B C     1 
ATOM   12247 O O     . GLY B  1 479  ? 1.539   25.482  121.295 1.00 38.50 ? 477  GLY B O     1 
ATOM   12248 N N     . THR B  1 480  ? 3.600   25.724  120.367 1.00 47.87 ? 478  THR B N     1 
ATOM   12249 C CA    . THR B  1 480  ? 3.705   27.169  120.559 1.00 52.39 ? 478  THR B CA    1 
ATOM   12250 C C     . THR B  1 480  ? 4.311   27.922  119.381 1.00 56.83 ? 478  THR B C     1 
ATOM   12251 O O     . THR B  1 480  ? 4.291   29.158  119.404 1.00 57.42 ? 478  THR B O     1 
ATOM   12252 C CB    . THR B  1 480  ? 4.556   27.479  121.798 1.00 54.10 ? 478  THR B CB    1 
ATOM   12253 O OG1   . THR B  1 480  ? 5.808   26.788  121.692 1.00 48.39 ? 478  THR B OG1   1 
ATOM   12254 C CG2   . THR B  1 480  ? 3.848   27.053  123.067 1.00 52.83 ? 478  THR B CG2   1 
ATOM   12255 N N     . HIS B  1 481  ? 4.852   27.241  118.368 1.00 56.30 ? 479  HIS B N     1 
ATOM   12256 C CA    . HIS B  1 481  ? 5.646   27.903  117.337 1.00 53.37 ? 479  HIS B CA    1 
ATOM   12257 C C     . HIS B  1 481  ? 4.805   28.909  116.561 1.00 56.13 ? 479  HIS B C     1 
ATOM   12258 O O     . HIS B  1 481  ? 3.816   28.541  115.917 1.00 55.89 ? 479  HIS B O     1 
ATOM   12259 C CB    . HIS B  1 481  ? 6.247   26.864  116.392 1.00 54.48 ? 479  HIS B CB    1 
ATOM   12260 N N     . GLU B  1 482  ? 5.219   30.178  116.616 1.00 52.64 ? 480  GLU B N     1 
ATOM   12261 C CA    . GLU B  1 482  ? 4.456   31.256  115.991 1.00 54.87 ? 480  GLU B CA    1 
ATOM   12262 C C     . GLU B  1 482  ? 4.185   30.985  114.515 1.00 56.19 ? 480  GLU B C     1 
ATOM   12263 O O     . GLU B  1 482  ? 3.071   31.219  114.029 1.00 58.41 ? 480  GLU B O     1 
ATOM   12264 C CB    . GLU B  1 482  ? 5.196   32.585  116.166 1.00 53.30 ? 480  GLU B CB    1 
ATOM   12265 N N     . THR B  1 483  ? 5.186   30.488  113.784 1.00 54.69 ? 481  THR B N     1 
ATOM   12266 C CA    . THR B  1 483  ? 4.997   30.203  112.362 1.00 57.52 ? 481  THR B CA    1 
ATOM   12267 C C     . THR B  1 483  ? 3.912   29.153  112.149 1.00 55.87 ? 481  THR B C     1 
ATOM   12268 O O     . THR B  1 483  ? 2.964   29.359  111.379 1.00 53.44 ? 481  THR B O     1 
ATOM   12269 C CB    . THR B  1 483  ? 6.313   29.734  111.744 1.00 51.37 ? 481  THR B CB    1 
ATOM   12270 O OG1   . THR B  1 483  ? 7.231   30.832  111.686 1.00 56.05 ? 481  THR B OG1   1 
ATOM   12271 C CG2   . THR B  1 483  ? 6.079   29.183  110.342 1.00 52.30 ? 481  THR B CG2   1 
ATOM   12272 N N     . LEU B  1 484  ? 4.049   28.012  112.822 1.00 61.06 ? 482  LEU B N     1 
ATOM   12273 C CA    . LEU B  1 484  ? 3.078   26.935  112.705 1.00 62.96 ? 482  LEU B CA    1 
ATOM   12274 C C     . LEU B  1 484  ? 1.722   27.321  113.287 1.00 61.88 ? 482  LEU B C     1 
ATOM   12275 O O     . LEU B  1 484  ? 0.699   26.765  112.868 1.00 59.37 ? 482  LEU B O     1 
ATOM   12276 C CB    . LEU B  1 484  ? 3.636   25.681  113.382 1.00 56.62 ? 482  LEU B CB    1 
ATOM   12277 C CG    . LEU B  1 484  ? 5.059   25.328  112.926 1.00 54.69 ? 482  LEU B CG    1 
ATOM   12278 C CD1   . LEU B  1 484  ? 5.640   24.177  113.726 1.00 49.19 ? 482  LEU B CD1   1 
ATOM   12279 C CD2   . LEU B  1 484  ? 5.104   25.019  111.424 1.00 54.08 ? 482  LEU B CD2   1 
ATOM   12280 N N     . LEU B  1 485  ? 1.690   28.275  114.221 1.00 57.53 ? 483  LEU B N     1 
ATOM   12281 C CA    . LEU B  1 485  ? 0.415   28.748  114.750 1.00 54.24 ? 483  LEU B CA    1 
ATOM   12282 C C     . LEU B  1 485  ? -0.311  29.633  113.744 1.00 55.67 ? 483  LEU B C     1 
ATOM   12283 O O     . LEU B  1 485  ? -1.542  29.559  113.617 1.00 56.06 ? 483  LEU B O     1 
ATOM   12284 C CB    . LEU B  1 485  ? 0.635   29.488  116.066 1.00 56.21 ? 483  LEU B CB    1 
ATOM   12285 C CG    . LEU B  1 485  ? 0.745   28.520  117.243 1.00 57.86 ? 483  LEU B CG    1 
ATOM   12286 C CD1   . LEU B  1 485  ? 1.060   29.248  118.540 1.00 54.11 ? 483  LEU B CD1   1 
ATOM   12287 C CD2   . LEU B  1 485  ? -0.549  27.741  117.360 1.00 52.62 ? 483  LEU B CD2   1 
ATOM   12288 N N     . ALA B  1 486  ? 0.426   30.479  113.020 1.00 55.07 ? 484  ALA B N     1 
ATOM   12289 C CA    . ALA B  1 486  ? -0.197  31.231  111.937 1.00 53.62 ? 484  ALA B CA    1 
ATOM   12290 C C     . ALA B  1 486  ? -0.807  30.287  110.908 1.00 51.21 ? 484  ALA B C     1 
ATOM   12291 O O     . ALA B  1 486  ? -1.915  30.526  110.410 1.00 50.61 ? 484  ALA B O     1 
ATOM   12292 C CB    . ALA B  1 486  ? 0.823   32.164  111.285 1.00 51.54 ? 484  ALA B CB    1 
ATOM   12293 N N     . TYR B  1 487  ? -0.106  29.194  110.597 1.00 52.68 ? 485  TYR B N     1 
ATOM   12294 C CA    . TYR B  1 487  ? -0.646  28.205  109.670 1.00 48.35 ? 485  TYR B CA    1 
ATOM   12295 C C     . TYR B  1 487  ? -1.930  27.581  110.211 1.00 54.93 ? 485  TYR B C     1 
ATOM   12296 O O     . TYR B  1 487  ? -2.901  27.396  109.467 1.00 49.21 ? 485  TYR B O     1 
ATOM   12297 C CB    . TYR B  1 487  ? 0.404   27.128  109.393 1.00 54.57 ? 485  TYR B CB    1 
ATOM   12298 N N     . LEU B  1 488  ? -1.956  27.267  111.512 1.00 50.50 ? 486  LEU B N     1 
ATOM   12299 C CA    . LEU B  1 488  ? -3.126  26.620  112.101 1.00 55.02 ? 486  LEU B CA    1 
ATOM   12300 C C     . LEU B  1 488  ? -4.354  27.523  112.041 1.00 54.66 ? 486  LEU B C     1 
ATOM   12301 O O     . LEU B  1 488  ? -5.456  27.065  111.714 1.00 55.77 ? 486  LEU B O     1 
ATOM   12302 C CB    . LEU B  1 488  ? -2.833  26.212  113.548 1.00 49.87 ? 486  LEU B CB    1 
ATOM   12303 N N     . VAL B  1 489  ? -4.182  28.811  112.350 1.00 51.14 ? 487  VAL B N     1 
ATOM   12304 C CA    . VAL B  1 489  ? -5.316  29.730  112.359 1.00 53.84 ? 487  VAL B CA    1 
ATOM   12305 C C     . VAL B  1 489  ? -5.888  29.894  110.956 1.00 53.51 ? 487  VAL B C     1 
ATOM   12306 O O     . VAL B  1 489  ? -7.111  29.982  110.776 1.00 50.88 ? 487  VAL B O     1 
ATOM   12307 C CB    . VAL B  1 489  ? -4.901  31.083  112.964 1.00 54.13 ? 487  VAL B CB    1 
ATOM   12308 C CG1   . VAL B  1 489  ? -6.046  32.091  112.850 1.00 52.57 ? 487  VAL B CG1   1 
ATOM   12309 C CG2   . VAL B  1 489  ? -4.480  30.902  114.415 1.00 51.28 ? 487  VAL B CG2   1 
ATOM   12310 N N     . ARG B  1 490  ? -5.017  29.938  109.942 1.00 47.94 ? 488  ARG B N     1 
ATOM   12311 C CA    . ARG B  1 490  ? -5.490  30.049  108.566 1.00 52.04 ? 488  ARG B CA    1 
ATOM   12312 C C     . ARG B  1 490  ? -6.295  28.821  108.156 1.00 59.73 ? 488  ARG B C     1 
ATOM   12313 O O     . ARG B  1 490  ? -7.221  28.927  107.342 1.00 58.57 ? 488  ARG B O     1 
ATOM   12314 C CB    . ARG B  1 490  ? -4.307  30.262  107.621 1.00 46.82 ? 488  ARG B CB    1 
ATOM   12315 N N     . ARG B  1 491  ? -5.967  27.653  108.718 1.00 49.68 ? 489  ARG B N     1 
ATOM   12316 C CA    . ARG B  1 491  ? -6.757  26.458  108.460 1.00 52.93 ? 489  ARG B CA    1 
ATOM   12317 C C     . ARG B  1 491  ? -8.006  26.418  109.332 1.00 55.65 ? 489  ARG B C     1 
ATOM   12318 O O     . ARG B  1 491  ? -9.068  25.978  108.875 1.00 55.89 ? 489  ARG B O     1 
ATOM   12319 C CB    . ARG B  1 491  ? -5.909  25.204  108.680 1.00 53.27 ? 489  ARG B CB    1 
ATOM   12320 C CG    . ARG B  1 491  ? -4.821  25.000  107.639 1.00 53.03 ? 489  ARG B CG    1 
ATOM   12321 C CD    . ARG B  1 491  ? -4.249  23.583  107.692 1.00 50.69 ? 489  ARG B CD    1 
ATOM   12322 N NE    . ARG B  1 491  ? -3.208  23.389  106.689 1.00 50.23 ? 489  ARG B NE    1 
ATOM   12323 C CZ    . ARG B  1 491  ? -1.912  23.298  106.962 1.00 50.47 ? 489  ARG B CZ    1 
ATOM   12324 N NH1   . ARG B  1 491  ? -1.465  23.316  108.207 1.00 47.65 ? 489  ARG B NH1   1 
ATOM   12325 N NH2   . ARG B  1 491  ? -1.044  23.184  105.960 1.00 42.39 ? 489  ARG B NH2   1 
ATOM   12326 N N     . LEU B  1 492  ? -7.894  26.865  110.590 1.00 59.56 ? 490  LEU B N     1 
ATOM   12327 C CA    . LEU B  1 492  ? -9.060  26.940  111.469 1.00 59.50 ? 490  LEU B CA    1 
ATOM   12328 C C     . LEU B  1 492  ? -10.174 27.765  110.836 1.00 60.48 ? 490  LEU B C     1 
ATOM   12329 O O     . LEU B  1 492  ? -11.351 27.391  110.895 1.00 58.29 ? 490  LEU B O     1 
ATOM   12330 C CB    . LEU B  1 492  ? -8.670  27.543  112.825 1.00 58.40 ? 490  LEU B CB    1 
ATOM   12331 C CG    . LEU B  1 492  ? -8.637  26.720  114.124 1.00 58.02 ? 490  LEU B CG    1 
ATOM   12332 C CD1   . LEU B  1 492  ? -9.631  25.560  114.114 1.00 57.06 ? 490  LEU B CD1   1 
ATOM   12333 C CD2   . LEU B  1 492  ? -7.229  26.236  114.448 1.00 56.88 ? 490  LEU B CD2   1 
ATOM   12334 N N     . LEU B  1 493  ? -9.819  28.888  110.214 1.00 58.72 ? 491  LEU B N     1 
ATOM   12335 C CA    . LEU B  1 493  ? -10.795 29.819  109.672 1.00 57.42 ? 491  LEU B CA    1 
ATOM   12336 C C     . LEU B  1 493  ? -10.998 29.650  108.173 1.00 56.75 ? 491  LEU B C     1 
ATOM   12337 O O     . LEU B  1 493  ? -11.598 30.523  107.537 1.00 57.61 ? 491  LEU B O     1 
ATOM   12338 C CB    . LEU B  1 493  ? -10.380 31.252  110.006 1.00 51.44 ? 491  LEU B CB    1 
ATOM   12339 C CG    . LEU B  1 493  ? -10.279 31.472  111.517 1.00 51.40 ? 491  LEU B CG    1 
ATOM   12340 C CD1   . LEU B  1 493  ? -9.882  32.900  111.862 1.00 46.34 ? 491  LEU B CD1   1 
ATOM   12341 C CD2   . LEU B  1 493  ? -11.596 31.094  112.188 1.00 57.92 ? 491  LEU B CD2   1 
ATOM   12342 N N     . GLU B  1 494  ? -10.514 28.544  107.602 1.00 61.40 ? 492  GLU B N     1 
ATOM   12343 C CA    . GLU B  1 494  ? -10.761 28.192  106.202 1.00 58.46 ? 492  GLU B CA    1 
ATOM   12344 C C     . GLU B  1 494  ? -10.318 29.307  105.259 1.00 55.84 ? 492  GLU B C     1 
ATOM   12345 O O     . GLU B  1 494  ? -10.974 29.585  104.253 1.00 58.05 ? 492  GLU B O     1 
ATOM   12346 C CB    . GLU B  1 494  ? -12.235 27.844  105.977 1.00 58.98 ? 492  GLU B CB    1 
ATOM   12347 C CG    . GLU B  1 494  ? -12.808 26.879  107.005 1.00 59.61 ? 492  GLU B CG    1 
ATOM   12348 C CD    . GLU B  1 494  ? -12.188 25.497  106.907 1.00 61.65 ? 492  GLU B CD    1 
ATOM   12349 O OE1   . GLU B  1 494  ? -11.852 25.083  105.778 1.00 60.18 ? 492  GLU B OE1   1 
ATOM   12350 O OE2   . GLU B  1 494  ? -12.029 24.830  107.954 1.00 60.62 ? 492  GLU B OE2   1 
ATOM   12351 N N     . ASN B  1 495  ? -9.204  29.960  105.596 1.00 53.50 ? 493  ASN B N     1 
ATOM   12352 C CA    . ASN B  1 495  ? -8.668  31.089  104.833 1.00 56.27 ? 493  ASN B CA    1 
ATOM   12353 C C     . ASN B  1 495  ? -9.673  32.228  104.678 1.00 56.05 ? 493  ASN B C     1 
ATOM   12354 O O     . ASN B  1 495  ? -9.571  33.022  103.736 1.00 57.11 ? 493  ASN B O     1 
ATOM   12355 C CB    . ASN B  1 495  ? -8.176  30.648  103.450 1.00 54.51 ? 493  ASN B CB    1 
ATOM   12356 C CG    . ASN B  1 495  ? -6.707  30.320  103.434 1.00 55.00 ? 493  ASN B CG    1 
ATOM   12357 O OD1   . ASN B  1 495  ? -6.072  30.229  104.482 1.00 58.84 ? 493  ASN B OD1   1 
ATOM   12358 N ND2   . ASN B  1 495  ? -6.154  30.133  102.241 1.00 54.82 ? 493  ASN B ND2   1 
ATOM   12359 N N     . GLY B  1 496  ? -10.643 32.330  105.581 1.00 57.76 ? 494  GLY B N     1 
ATOM   12360 C CA    . GLY B  1 496  ? -11.678 33.342  105.436 1.00 62.30 ? 494  GLY B CA    1 
ATOM   12361 C C     . GLY B  1 496  ? -12.484 33.213  104.163 1.00 67.69 ? 494  GLY B C     1 
ATOM   12362 O O     . GLY B  1 496  ? -12.835 34.227  103.547 1.00 73.94 ? 494  GLY B O     1 
ATOM   12363 N N     . ALA B  1 497  ? -12.779 31.984  103.749 1.00 63.50 ? 495  ALA B N     1 
ATOM   12364 C CA    . ALA B  1 497  ? -13.550 31.753  102.537 1.00 58.04 ? 495  ALA B CA    1 
ATOM   12365 C C     . ALA B  1 497  ? -15.035 31.921  102.828 1.00 54.63 ? 495  ALA B C     1 
ATOM   12366 O O     . ALA B  1 497  ? -15.572 31.290  103.744 1.00 54.66 ? 495  ALA B O     1 
ATOM   12367 C CB    . ALA B  1 497  ? -13.267 30.357  101.984 1.00 56.92 ? 495  ALA B CB    1 
ATOM   12368 N N     . ASN B  1 498  ? -15.696 32.781  102.047 1.00 55.64 ? 496  ASN B N     1 
ATOM   12369 C CA    . ASN B  1 498  ? -17.128 33.002  102.222 1.00 56.11 ? 496  ASN B CA    1 
ATOM   12370 C C     . ASN B  1 498  ? -17.937 31.750  101.908 1.00 51.09 ? 496  ASN B C     1 
ATOM   12371 O O     . ASN B  1 498  ? -19.055 31.597  102.408 1.00 53.70 ? 496  ASN B O     1 
ATOM   12372 C CB    . ASN B  1 498  ? -17.591 34.166  101.342 1.00 57.21 ? 496  ASN B CB    1 
ATOM   12373 N N     . SER B  1 499  ? -17.401 30.851  101.085 1.00 50.92 ? 497  SER B N     1 
ATOM   12374 C CA    . SER B  1 499  ? -18.107 29.617  100.763 1.00 50.09 ? 497  SER B CA    1 
ATOM   12375 C C     . SER B  1 499  ? -18.054 28.594  101.889 1.00 48.11 ? 497  SER B C     1 
ATOM   12376 O O     . SER B  1 499  ? -18.756 27.582  101.816 1.00 45.02 ? 497  SER B O     1 
ATOM   12377 C CB    . SER B  1 499  ? -17.521 28.993  99.500  1.00 48.61 ? 497  SER B CB    1 
ATOM   12378 O OG    . SER B  1 499  ? -16.146 28.701  99.691  1.00 39.35 ? 497  SER B OG    1 
ATOM   12379 N N     . SER B  1 500  ? -17.230 28.815  102.908 1.00 44.59 ? 498  SER B N     1 
ATOM   12380 C CA    . SER B  1 500  ? -17.066 27.832  103.963 1.00 45.72 ? 498  SER B CA    1 
ATOM   12381 C C     . SER B  1 500  ? -18.267 27.855  104.899 1.00 49.51 ? 498  SER B C     1 
ATOM   12382 O O     . SER B  1 500  ? -18.855 28.909  105.157 1.00 48.92 ? 498  SER B O     1 
ATOM   12383 C CB    . SER B  1 500  ? -15.778 28.099  104.745 1.00 48.66 ? 498  SER B CB    1 
ATOM   12384 O OG    . SER B  1 500  ? -15.759 29.424  105.249 1.00 54.62 ? 498  SER B OG    1 
ATOM   12385 N N     . PHE B  1 501  ? -18.639 26.671  105.386 1.00 43.20 ? 499  PHE B N     1 
ATOM   12386 C CA    . PHE B  1 501  ? -19.675 26.570  106.407 1.00 47.85 ? 499  PHE B CA    1 
ATOM   12387 C C     . PHE B  1 501  ? -19.341 27.441  107.615 1.00 50.19 ? 499  PHE B C     1 
ATOM   12388 O O     . PHE B  1 501  ? -20.223 28.105  108.172 1.00 49.94 ? 499  PHE B O     1 
ATOM   12389 C CB    . PHE B  1 501  ? -19.840 25.106  106.818 1.00 43.15 ? 499  PHE B CB    1 
ATOM   12390 C CG    . PHE B  1 501  ? -21.025 24.845  107.701 1.00 45.20 ? 499  PHE B CG    1 
ATOM   12391 C CD1   . PHE B  1 501  ? -21.002 25.188  109.045 1.00 49.39 ? 499  PHE B CD1   1 
ATOM   12392 C CD2   . PHE B  1 501  ? -22.157 24.235  107.191 1.00 44.84 ? 499  PHE B CD2   1 
ATOM   12393 C CE1   . PHE B  1 501  ? -22.091 24.948  109.855 1.00 49.63 ? 499  PHE B CE1   1 
ATOM   12394 C CE2   . PHE B  1 501  ? -23.250 23.983  108.001 1.00 49.16 ? 499  PHE B CE2   1 
ATOM   12395 C CZ    . PHE B  1 501  ? -23.216 24.339  109.334 1.00 47.24 ? 499  PHE B CZ    1 
ATOM   12396 N N     . VAL B  1 502  ? -18.068 27.456  108.022 1.00 53.15 ? 500  VAL B N     1 
ATOM   12397 C CA    . VAL B  1 502  ? -17.645 28.240  109.183 1.00 56.19 ? 500  VAL B CA    1 
ATOM   12398 C C     . VAL B  1 502  ? -18.101 29.688  109.045 1.00 56.82 ? 500  VAL B C     1 
ATOM   12399 O O     . VAL B  1 502  ? -18.662 30.275  109.978 1.00 59.49 ? 500  VAL B O     1 
ATOM   12400 C CB    . VAL B  1 502  ? -16.118 28.143  109.365 1.00 51.36 ? 500  VAL B CB    1 
ATOM   12401 N N     . HIS B  1 503  ? -17.883 30.281  107.872 1.00 49.83 ? 501  HIS B N     1 
ATOM   12402 C CA    . HIS B  1 503  ? -18.283 31.668  107.660 1.00 52.36 ? 501  HIS B CA    1 
ATOM   12403 C C     . HIS B  1 503  ? -19.786 31.816  107.432 1.00 56.40 ? 501  HIS B C     1 
ATOM   12404 O O     . HIS B  1 503  ? -20.369 32.832  107.829 1.00 56.47 ? 501  HIS B O     1 
ATOM   12405 C CB    . HIS B  1 503  ? -17.506 32.260  106.481 1.00 53.99 ? 501  HIS B CB    1 
ATOM   12406 C CG    . HIS B  1 503  ? -18.116 33.507  105.920 1.00 60.28 ? 501  HIS B CG    1 
ATOM   12407 N ND1   . HIS B  1 503  ? -19.131 33.484  104.985 1.00 59.86 ? 501  HIS B ND1   1 
ATOM   12408 C CD2   . HIS B  1 503  ? -17.852 34.814  106.155 1.00 61.55 ? 501  HIS B CD2   1 
ATOM   12409 C CE1   . HIS B  1 503  ? -19.470 34.723  104.675 1.00 60.64 ? 501  HIS B CE1   1 
ATOM   12410 N NE2   . HIS B  1 503  ? -18.709 35.549  105.371 1.00 66.82 ? 501  HIS B NE2   1 
ATOM   12411 N N     . ARG B  1 504  ? -20.429 30.823  106.811 1.00 55.14 ? 502  ARG B N     1 
ATOM   12412 C CA    . ARG B  1 504  ? -21.819 30.977  106.389 1.00 50.77 ? 502  ARG B CA    1 
ATOM   12413 C C     . ARG B  1 504  ? -22.793 30.826  107.552 1.00 53.97 ? 502  ARG B C     1 
ATOM   12414 O O     . ARG B  1 504  ? -23.828 31.501  107.587 1.00 53.76 ? 502  ARG B O     1 
ATOM   12415 C CB    . ARG B  1 504  ? -22.140 29.972  105.281 1.00 46.66 ? 502  ARG B CB    1 
ATOM   12416 C CG    . ARG B  1 504  ? -21.578 30.376  103.920 1.00 49.52 ? 502  ARG B CG    1 
ATOM   12417 C CD    . ARG B  1 504  ? -21.547 29.221  102.926 1.00 48.57 ? 502  ARG B CD    1 
ATOM   12418 N NE    . ARG B  1 504  ? -22.827 28.536  102.789 1.00 46.66 ? 502  ARG B NE    1 
ATOM   12419 C CZ    . ARG B  1 504  ? -23.825 28.951  102.021 1.00 50.15 ? 502  ARG B CZ    1 
ATOM   12420 N NH1   . ARG B  1 504  ? -23.766 30.106  101.376 1.00 53.89 ? 502  ARG B NH1   1 
ATOM   12421 N NH2   . ARG B  1 504  ? -24.906 28.185  101.890 1.00 45.72 ? 502  ARG B NH2   1 
ATOM   12422 N N     . ILE B  1 505  ? -22.490 29.944  108.508 1.00 53.08 ? 503  ILE B N     1 
ATOM   12423 C CA    . ILE B  1 505  ? -23.336 29.802  109.687 1.00 54.64 ? 503  ILE B CA    1 
ATOM   12424 C C     . ILE B  1 505  ? -23.407 31.100  110.479 1.00 56.84 ? 503  ILE B C     1 
ATOM   12425 O O     . ILE B  1 505  ? -24.348 31.301  111.252 1.00 54.86 ? 503  ILE B O     1 
ATOM   12426 C CB    . ILE B  1 505  ? -22.834 28.644  110.574 1.00 51.72 ? 503  ILE B CB    1 
ATOM   12427 N N     . ASN B  1 506  ? -22.440 31.999  110.289 1.00 53.39 ? 504  ASN B N     1 
ATOM   12428 C CA    . ASN B  1 506  ? -22.379 33.270  111.000 1.00 60.17 ? 504  ASN B CA    1 
ATOM   12429 C C     . ASN B  1 506  ? -22.832 34.456  110.155 1.00 60.67 ? 504  ASN B C     1 
ATOM   12430 O O     . ASN B  1 506  ? -22.884 35.578  110.669 1.00 59.27 ? 504  ASN B O     1 
ATOM   12431 C CB    . ASN B  1 506  ? -20.953 33.521  111.508 1.00 59.57 ? 504  ASN B CB    1 
ATOM   12432 N N     . ASP B  1 507  ? -23.144 34.247  108.877 1.00 56.14 ? 505  ASP B N     1 
ATOM   12433 C CA    . ASP B  1 507  ? -23.658 35.322  108.043 1.00 61.07 ? 505  ASP B CA    1 
ATOM   12434 C C     . ASP B  1 507  ? -25.166 35.418  108.226 1.00 65.44 ? 505  ASP B C     1 
ATOM   12435 O O     . ASP B  1 507  ? -25.871 34.429  107.981 1.00 62.55 ? 505  ASP B O     1 
ATOM   12436 C CB    . ASP B  1 507  ? -23.325 35.081  106.580 1.00 60.86 ? 505  ASP B CB    1 
ATOM   12437 C CG    . ASP B  1 507  ? -23.434 36.343  105.741 1.00 65.55 ? 505  ASP B CG    1 
ATOM   12438 O OD1   . ASP B  1 507  ? -24.411 37.096  105.920 1.00 70.16 ? 505  ASP B OD1   1 
ATOM   12439 O OD2   . ASP B  1 507  ? -22.540 36.589  104.905 1.00 68.98 ? 505  ASP B OD2   1 
ATOM   12440 N N     . PRO B  1 508  ? -25.696 36.561  108.672 1.00 67.99 ? 506  PRO B N     1 
ATOM   12441 C CA    . PRO B  1 508  ? -27.156 36.690  108.808 1.00 66.39 ? 506  PRO B CA    1 
ATOM   12442 C C     . PRO B  1 508  ? -27.905 36.636  107.484 1.00 66.60 ? 506  PRO B C     1 
ATOM   12443 O O     . PRO B  1 508  ? -29.118 36.389  107.493 1.00 64.58 ? 506  PRO B O     1 
ATOM   12444 C CB    . PRO B  1 508  ? -27.327 38.058  109.488 1.00 66.50 ? 506  PRO B CB    1 
ATOM   12445 C CG    . PRO B  1 508  ? -26.010 38.330  110.143 1.00 66.39 ? 506  PRO B CG    1 
ATOM   12446 C CD    . PRO B  1 508  ? -24.981 37.715  109.242 1.00 65.69 ? 506  PRO B CD    1 
ATOM   12447 N N     . LYS B  1 509  ? -27.229 36.859  106.353 1.00 66.59 ? 507  LYS B N     1 
ATOM   12448 C CA    . LYS B  1 509  ? -27.899 36.777  105.059 1.00 63.92 ? 507  LYS B CA    1 
ATOM   12449 C C     . LYS B  1 509  ? -28.298 35.340  104.735 1.00 68.33 ? 507  LYS B C     1 
ATOM   12450 O O     . LYS B  1 509  ? -29.435 35.078  104.324 1.00 71.11 ? 507  LYS B O     1 
ATOM   12451 C CB    . LYS B  1 509  ? -26.998 37.351  103.966 1.00 65.74 ? 507  LYS B CB    1 
ATOM   12452 N N     . VAL B  1 510  ? -27.379 34.392  104.928 1.00 67.88 ? 508  VAL B N     1 
ATOM   12453 C CA    . VAL B  1 510  ? -27.651 32.998  104.589 1.00 64.42 ? 508  VAL B CA    1 
ATOM   12454 C C     . VAL B  1 510  ? -28.686 32.425  105.548 1.00 61.02 ? 508  VAL B C     1 
ATOM   12455 O O     . VAL B  1 510  ? -28.540 32.512  106.773 1.00 60.62 ? 508  VAL B O     1 
ATOM   12456 C CB    . VAL B  1 510  ? -26.354 32.175  104.609 1.00 58.01 ? 508  VAL B CB    1 
ATOM   12457 C CG1   . VAL B  1 510  ? -26.662 30.692  104.468 1.00 56.84 ? 508  VAL B CG1   1 
ATOM   12458 C CG2   . VAL B  1 510  ? -25.429 32.628  103.497 1.00 59.44 ? 508  VAL B CG2   1 
ATOM   12459 N N     . SER B  1 511  ? -29.735 31.829  104.988 1.00 61.80 ? 509  SER B N     1 
ATOM   12460 C CA    . SER B  1 511  ? -30.820 31.211  105.735 1.00 57.02 ? 509  SER B CA    1 
ATOM   12461 C C     . SER B  1 511  ? -30.551 29.726  105.948 1.00 57.20 ? 509  SER B C     1 
ATOM   12462 O O     . SER B  1 511  ? -29.702 29.119  105.289 1.00 58.95 ? 509  SER B O     1 
ATOM   12463 C CB    . SER B  1 511  ? -32.142 31.389  104.993 1.00 58.01 ? 509  SER B CB    1 
ATOM   12464 O OG    . SER B  1 511  ? -32.052 30.818  103.699 1.00 57.81 ? 509  SER B OG    1 
ATOM   12465 N N     . ILE B  1 512  ? -31.309 29.135  106.875 1.00 51.33 ? 510  ILE B N     1 
ATOM   12466 C CA    . ILE B  1 512  ? -31.137 27.717  107.177 1.00 57.94 ? 510  ILE B CA    1 
ATOM   12467 C C     . ILE B  1 512  ? -31.501 26.861  105.972 1.00 58.03 ? 510  ILE B C     1 
ATOM   12468 O O     . ILE B  1 512  ? -30.946 25.768  105.787 1.00 55.22 ? 510  ILE B O     1 
ATOM   12469 C CB    . ILE B  1 512  ? -31.960 27.325  108.421 1.00 49.75 ? 510  ILE B CB    1 
ATOM   12470 N N     . ASP B  1 513  ? -32.433 27.335  105.139 1.00 55.73 ? 511  ASP B N     1 
ATOM   12471 C CA    . ASP B  1 513  ? -32.756 26.633  103.901 1.00 55.07 ? 511  ASP B CA    1 
ATOM   12472 C C     . ASP B  1 513  ? -31.531 26.526  103.000 1.00 52.53 ? 511  ASP B C     1 
ATOM   12473 O O     . ASP B  1 513  ? -31.234 25.455  102.462 1.00 52.80 ? 511  ASP B O     1 
ATOM   12474 C CB    . ASP B  1 513  ? -33.892 27.349  103.169 1.00 53.81 ? 511  ASP B CB    1 
ATOM   12475 C CG    . ASP B  1 513  ? -35.248 27.107  103.803 1.00 63.13 ? 511  ASP B CG    1 
ATOM   12476 O OD1   . ASP B  1 513  ? -35.573 25.939  104.113 1.00 64.81 ? 511  ASP B OD1   1 
ATOM   12477 O OD2   . ASP B  1 513  ? -35.991 28.094  103.984 1.00 65.36 ? 511  ASP B OD2   1 
ATOM   12478 N N     . GLU B  1 514  ? -30.814 27.637  102.819 1.00 49.77 ? 512  GLU B N     1 
ATOM   12479 C CA    . GLU B  1 514  ? -29.589 27.618  102.024 1.00 53.62 ? 512  GLU B CA    1 
ATOM   12480 C C     . GLU B  1 514  ? -28.576 26.632  102.596 1.00 53.78 ? 512  GLU B C     1 
ATOM   12481 O O     . GLU B  1 514  ? -28.002 25.817  101.864 1.00 48.05 ? 512  GLU B O     1 
ATOM   12482 C CB    . GLU B  1 514  ? -28.984 29.021  101.953 1.00 55.54 ? 512  GLU B CB    1 
ATOM   12483 C CG    . GLU B  1 514  ? -29.932 30.099  101.456 1.00 60.12 ? 512  GLU B CG    1 
ATOM   12484 C CD    . GLU B  1 514  ? -29.250 31.448  101.302 1.00 64.06 ? 512  GLU B CD    1 
ATOM   12485 O OE1   . GLU B  1 514  ? -28.145 31.493  100.710 1.00 63.03 ? 512  GLU B OE1   1 
ATOM   12486 O OE2   . GLU B  1 514  ? -29.817 32.460  101.779 1.00 62.12 ? 512  GLU B OE2   1 
ATOM   12487 N N     . LEU B  1 515  ? -28.345 26.690  103.910 1.00 50.04 ? 513  LEU B N     1 
ATOM   12488 C CA    . LEU B  1 515  ? -27.364 25.808  104.523 1.00 50.06 ? 513  LEU B CA    1 
ATOM   12489 C C     . LEU B  1 515  ? -27.779 24.341  104.468 1.00 50.09 ? 513  LEU B C     1 
ATOM   12490 O O     . LEU B  1 515  ? -26.906 23.467  104.514 1.00 45.98 ? 513  LEU B O     1 
ATOM   12491 C CB    . LEU B  1 515  ? -27.111 26.235  105.973 1.00 42.76 ? 513  LEU B CB    1 
ATOM   12492 N N     . ILE B  1 516  ? -29.078 24.044  104.340 1.00 47.23 ? 514  ILE B N     1 
ATOM   12493 C CA    . ILE B  1 516  ? -29.561 22.664  104.394 1.00 46.55 ? 514  ILE B CA    1 
ATOM   12494 C C     . ILE B  1 516  ? -29.753 22.046  103.012 1.00 49.21 ? 514  ILE B C     1 
ATOM   12495 O O     . ILE B  1 516  ? -30.100 20.859  102.918 1.00 47.99 ? 514  ILE B O     1 
ATOM   12496 C CB    . ILE B  1 516  ? -30.874 22.567  105.200 1.00 52.78 ? 514  ILE B CB    1 
ATOM   12497 N N     . ALA B  1 517  ? -29.530 22.809  101.941 1.00 44.01 ? 515  ALA B N     1 
ATOM   12498 C CA    . ALA B  1 517  ? -29.723 22.297  100.587 1.00 49.29 ? 515  ALA B CA    1 
ATOM   12499 C C     . ALA B  1 517  ? -28.860 21.066  100.327 1.00 49.07 ? 515  ALA B C     1 
ATOM   12500 O O     . ALA B  1 517  ? -27.691 21.008  100.729 1.00 45.85 ? 515  ALA B O     1 
ATOM   12501 C CB    . ALA B  1 517  ? -29.399 23.384  99.564  1.00 42.17 ? 515  ALA B CB    1 
ATOM   12502 N N     . ASP B  1 518  ? -29.449 20.071  99.645  1.00 43.05 ? 516  ASP B N     1 
ATOM   12503 C CA    . ASP B  1 518  ? -28.768 18.813  99.357  1.00 43.78 ? 516  ASP B CA    1 
ATOM   12504 C C     . ASP B  1 518  ? -27.840 18.998  98.163  1.00 41.60 ? 516  ASP B C     1 
ATOM   12505 O O     . ASP B  1 518  ? -28.315 19.208  97.040  1.00 44.05 ? 516  ASP B O     1 
ATOM   12506 C CB    . ASP B  1 518  ? -29.778 17.697  99.079  1.00 44.07 ? 516  ASP B CB    1 
ATOM   12507 C CG    . ASP B  1 518  ? -29.136 16.314  99.042  1.00 47.69 ? 516  ASP B CG    1 
ATOM   12508 O OD1   . ASP B  1 518  ? -27.927 16.207  98.734  1.00 47.12 ? 516  ASP B OD1   1 
ATOM   12509 O OD2   . ASP B  1 518  ? -29.842 15.321  99.323  1.00 51.01 ? 516  ASP B OD2   1 
ATOM   12510 N N     . PRO B  1 519  ? -26.521 18.916  98.352  1.00 36.60 ? 517  PRO B N     1 
ATOM   12511 C CA    . PRO B  1 519  ? -25.613 19.121  97.210  1.00 38.27 ? 517  PRO B CA    1 
ATOM   12512 C C     . PRO B  1 519  ? -25.806 18.098  96.102  1.00 38.63 ? 517  PRO B C     1 
ATOM   12513 O O     . PRO B  1 519  ? -25.644 18.434  94.923  1.00 39.66 ? 517  PRO B O     1 
ATOM   12514 C CB    . PRO B  1 519  ? -24.215 19.018  97.847  1.00 39.00 ? 517  PRO B CB    1 
ATOM   12515 C CG    . PRO B  1 519  ? -24.418 18.224  99.088  1.00 44.44 ? 517  PRO B CG    1 
ATOM   12516 C CD    . PRO B  1 519  ? -25.787 18.594  99.592  1.00 39.82 ? 517  PRO B CD    1 
ATOM   12517 N N     . VAL B  1 520  ? -26.169 16.864  96.448  1.00 40.34 ? 518  VAL B N     1 
ATOM   12518 C CA    . VAL B  1 520  ? -26.353 15.827  95.439  1.00 38.89 ? 518  VAL B CA    1 
ATOM   12519 C C     . VAL B  1 520  ? -27.482 16.199  94.482  1.00 43.30 ? 518  VAL B C     1 
ATOM   12520 O O     . VAL B  1 520  ? -27.358 16.034  93.262  1.00 40.82 ? 518  VAL B O     1 
ATOM   12521 C CB    . VAL B  1 520  ? -26.617 14.470  96.113  1.00 40.62 ? 518  VAL B CB    1 
ATOM   12522 C CG1   . VAL B  1 520  ? -26.707 13.376  95.059  1.00 43.88 ? 518  VAL B CG1   1 
ATOM   12523 C CG2   . VAL B  1 520  ? -25.531 14.163  97.144  1.00 35.10 ? 518  VAL B CG2   1 
ATOM   12524 N N     . GLU B  1 521  ? -28.593 16.713  95.016  1.00 39.19 ? 519  GLU B N     1 
ATOM   12525 C CA    . GLU B  1 521  ? -29.728 17.060  94.163  1.00 43.67 ? 519  GLU B CA    1 
ATOM   12526 C C     . GLU B  1 521  ? -29.533 18.393  93.457  1.00 43.93 ? 519  GLU B C     1 
ATOM   12527 O O     . GLU B  1 521  ? -30.049 18.581  92.346  1.00 43.01 ? 519  GLU B O     1 
ATOM   12528 C CB    . GLU B  1 521  ? -31.029 17.088  94.973  1.00 42.19 ? 519  GLU B CB    1 
ATOM   12529 C CG    . GLU B  1 521  ? -31.389 15.771  95.628  1.00 43.67 ? 519  GLU B CG    1 
ATOM   12530 C CD    . GLU B  1 521  ? -31.452 14.613  94.641  1.00 49.99 ? 519  GLU B CD    1 
ATOM   12531 O OE1   . GLU B  1 521  ? -31.773 14.843  93.450  1.00 44.51 ? 519  GLU B OE1   1 
ATOM   12532 O OE2   . GLU B  1 521  ? -31.176 13.468  95.057  1.00 51.37 ? 519  GLU B OE2   1 
ATOM   12533 N N     . VAL B  1 522  ? -28.815 19.333  94.074  1.00 39.54 ? 520  VAL B N     1 
ATOM   12534 C CA    . VAL B  1 522  ? -28.511 20.580  93.375  1.00 40.37 ? 520  VAL B CA    1 
ATOM   12535 C C     . VAL B  1 522  ? -27.619 20.303  92.173  1.00 44.29 ? 520  VAL B C     1 
ATOM   12536 O O     . VAL B  1 522  ? -27.810 20.878  91.094  1.00 46.07 ? 520  VAL B O     1 
ATOM   12537 C CB    . VAL B  1 522  ? -27.866 21.603  94.329  1.00 39.81 ? 520  VAL B CB    1 
ATOM   12538 C CG1   . VAL B  1 522  ? -27.532 22.875  93.580  1.00 44.65 ? 520  VAL B CG1   1 
ATOM   12539 C CG2   . VAL B  1 522  ? -28.782 21.902  95.508  1.00 44.55 ? 520  VAL B CG2   1 
ATOM   12540 N N     . VAL B  1 523  ? -26.633 19.416  92.332  1.00 38.99 ? 521  VAL B N     1 
ATOM   12541 C CA    . VAL B  1 523  ? -25.770 19.078  91.204  1.00 41.48 ? 521  VAL B CA    1 
ATOM   12542 C C     . VAL B  1 523  ? -26.557 18.324  90.140  1.00 41.55 ? 521  VAL B C     1 
ATOM   12543 O O     . VAL B  1 523  ? -26.391 18.564  88.938  1.00 39.94 ? 521  VAL B O     1 
ATOM   12544 C CB    . VAL B  1 523  ? -24.546 18.276  91.679  1.00 41.91 ? 521  VAL B CB    1 
ATOM   12545 C CG1   . VAL B  1 523  ? -23.831 17.643  90.496  1.00 36.15 ? 521  VAL B CG1   1 
ATOM   12546 C CG2   . VAL B  1 523  ? -23.592 19.192  92.428  1.00 31.88 ? 521  VAL B CG2   1 
ATOM   12547 N N     . ARG B  1 524  ? -27.415 17.401  90.563  1.00 42.20 ? 522  ARG B N     1 
ATOM   12548 C CA    . ARG B  1 524  ? -28.171 16.599  89.609  1.00 40.54 ? 522  ARG B CA    1 
ATOM   12549 C C     . ARG B  1 524  ? -29.035 17.467  88.705  1.00 46.44 ? 522  ARG B C     1 
ATOM   12550 O O     . ARG B  1 524  ? -29.260 17.117  87.539  1.00 45.71 ? 522  ARG B O     1 
ATOM   12551 C CB    . ARG B  1 524  ? -29.036 15.582  90.352  1.00 42.83 ? 522  ARG B CB    1 
ATOM   12552 C CG    . ARG B  1 524  ? -29.716 14.587  89.431  1.00 44.57 ? 522  ARG B CG    1 
ATOM   12553 C CD    . ARG B  1 524  ? -30.888 13.897  90.102  1.00 49.04 ? 522  ARG B CD    1 
ATOM   12554 N NE    . ARG B  1 524  ? -30.519 13.271  91.365  1.00 42.48 ? 522  ARG B NE    1 
ATOM   12555 C CZ    . ARG B  1 524  ? -29.794 12.166  91.473  1.00 50.32 ? 522  ARG B CZ    1 
ATOM   12556 N NH1   . ARG B  1 524  ? -29.301 11.553  90.407  1.00 54.28 ? 522  ARG B NH1   1 
ATOM   12557 N NH2   . ARG B  1 524  ? -29.548 11.669  92.681  1.00 52.46 ? 522  ARG B NH2   1 
ATOM   12558 N N     . ALA B  1 525  ? -29.511 18.603  89.213  1.00 44.66 ? 523  ALA B N     1 
ATOM   12559 C CA    . ALA B  1 525  ? -30.417 19.465  88.465  1.00 44.89 ? 523  ALA B CA    1 
ATOM   12560 C C     . ALA B  1 525  ? -29.698 20.450  87.557  1.00 45.91 ? 523  ALA B C     1 
ATOM   12561 O O     . ALA B  1 525  ? -30.356 21.133  86.768  1.00 43.97 ? 523  ALA B O     1 
ATOM   12562 C CB    . ALA B  1 525  ? -31.332 20.237  89.423  1.00 42.67 ? 523  ALA B CB    1 
ATOM   12563 N N     . MET B  1 526  ? -28.380 20.542  87.637  1.00 42.88 ? 524  MET B N     1 
ATOM   12564 C CA    . MET B  1 526  ? -27.679 21.529  86.843  1.00 42.37 ? 524  MET B CA    1 
ATOM   12565 C C     . MET B  1 526  ? -27.713 21.141  85.364  1.00 42.52 ? 524  MET B C     1 
ATOM   12566 O O     . MET B  1 526  ? -27.858 19.964  85.028  1.00 41.41 ? 524  MET B O     1 
ATOM   12567 C CB    . MET B  1 526  ? -26.251 21.676  87.345  1.00 44.16 ? 524  MET B CB    1 
ATOM   12568 C CG    . MET B  1 526  ? -26.213 22.346  88.695  1.00 43.05 ? 524  MET B CG    1 
ATOM   12569 S SD    . MET B  1 526  ? -24.552 22.584  89.341  1.00 54.53 ? 524  MET B SD    1 
ATOM   12570 C CE    . MET B  1 526  ? -23.868 23.748  88.162  1.00 49.37 ? 524  MET B CE    1 
ATOM   12571 N N     . PRO B  1 527  ? -27.608 22.124  84.457  1.00 45.82 ? 525  PRO B N     1 
ATOM   12572 C CA    . PRO B  1 527  ? -27.734 21.802  83.024  1.00 44.16 ? 525  PRO B CA    1 
ATOM   12573 C C     . PRO B  1 527  ? -26.620 20.905  82.520  1.00 41.90 ? 525  PRO B C     1 
ATOM   12574 O O     . PRO B  1 527  ? -26.871 20.004  81.712  1.00 36.95 ? 525  PRO B O     1 
ATOM   12575 C CB    . PRO B  1 527  ? -27.706 23.183  82.357  1.00 40.72 ? 525  PRO B CB    1 
ATOM   12576 C CG    . PRO B  1 527  ? -26.909 24.026  83.286  1.00 44.86 ? 525  PRO B CG    1 
ATOM   12577 C CD    . PRO B  1 527  ? -27.260 23.542  84.672  1.00 45.94 ? 525  PRO B CD    1 
ATOM   12578 N N     . VAL B  1 528  ? -25.392 21.123  82.989  1.00 40.15 ? 526  VAL B N     1 
ATOM   12579 C CA    . VAL B  1 528  ? -24.254 20.271  82.675  1.00 36.24 ? 526  VAL B CA    1 
ATOM   12580 C C     . VAL B  1 528  ? -23.713 19.771  84.006  1.00 35.07 ? 526  VAL B C     1 
ATOM   12581 O O     . VAL B  1 528  ? -23.105 20.539  84.761  1.00 38.66 ? 526  VAL B O     1 
ATOM   12582 C CB    . VAL B  1 528  ? -23.172 21.019  81.882  1.00 35.20 ? 526  VAL B CB    1 
ATOM   12583 C CG1   . VAL B  1 528  ? -21.899 20.202  81.812  1.00 36.08 ? 526  VAL B CG1   1 
ATOM   12584 C CG2   . VAL B  1 528  ? -23.657 21.338  80.473  1.00 36.18 ? 526  VAL B CG2   1 
ATOM   12585 N N     . VAL B  1 529  ? -23.934 18.492  84.300  1.00 36.03 ? 527  VAL B N     1 
ATOM   12586 C CA    . VAL B  1 529  ? -23.462 17.941  85.564  1.00 32.50 ? 527  VAL B CA    1 
ATOM   12587 C C     . VAL B  1 529  ? -21.938 17.964  85.580  1.00 33.33 ? 527  VAL B C     1 
ATOM   12588 O O     . VAL B  1 529  ? -21.278 17.473  84.652  1.00 34.35 ? 527  VAL B O     1 
ATOM   12589 C CB    . VAL B  1 529  ? -24.015 16.525  85.783  1.00 32.02 ? 527  VAL B CB    1 
ATOM   12590 C CG1   . VAL B  1 529  ? -23.334 15.865  86.987  1.00 34.50 ? 527  VAL B CG1   1 
ATOM   12591 C CG2   . VAL B  1 529  ? -25.545 16.562  85.978  1.00 39.11 ? 527  VAL B CG2   1 
ATOM   12592 N N     . GLY B  1 530  ? -21.370 18.564  86.624  1.00 33.31 ? 528  GLY B N     1 
ATOM   12593 C CA    . GLY B  1 530  ? -19.933 18.595  86.769  1.00 29.85 ? 528  GLY B CA    1 
ATOM   12594 C C     . GLY B  1 530  ? -19.217 19.709  86.040  1.00 32.60 ? 528  GLY B C     1 
ATOM   12595 O O     . GLY B  1 530  ? -17.983 19.685  85.975  1.00 30.69 ? 528  GLY B O     1 
ATOM   12596 N N     . ALA B  1 531  ? -19.945 20.684  85.496  1.00 29.44 ? 529  ALA B N     1 
ATOM   12597 C CA    . ALA B  1 531  ? -19.312 21.824  84.850  1.00 30.77 ? 529  ALA B CA    1 
ATOM   12598 C C     . ALA B  1 531  ? -18.335 22.531  85.782  1.00 29.98 ? 529  ALA B C     1 
ATOM   12599 O O     . ALA B  1 531  ? -18.642 22.792  86.950  1.00 31.40 ? 529  ALA B O     1 
ATOM   12600 C CB    . ALA B  1 531  ? -20.373 22.812  84.369  1.00 33.61 ? 529  ALA B CB    1 
ATOM   12601 N N     . LYS B  1 532  ? -17.160 22.850  85.237  1.00 26.58 ? 530  LYS B N     1 
ATOM   12602 C CA    . LYS B  1 532  ? -16.128 23.619  85.932  1.00 29.47 ? 530  LYS B CA    1 
ATOM   12603 C C     . LYS B  1 532  ? -16.701 24.940  86.427  1.00 32.23 ? 530  LYS B C     1 
ATOM   12604 O O     . LYS B  1 532  ? -17.650 25.477  85.854  1.00 29.07 ? 530  LYS B O     1 
ATOM   12605 C CB    . LYS B  1 532  ? -14.945 23.893  84.982  1.00 29.19 ? 530  LYS B CB    1 
ATOM   12606 C CG    . LYS B  1 532  ? -13.825 24.764  85.557  1.00 33.04 ? 530  LYS B CG    1 
ATOM   12607 C CD    . LYS B  1 532  ? -12.712 25.040  84.540  1.00 31.02 ? 530  LYS B CD    1 
ATOM   12608 C CE    . LYS B  1 532  ? -13.221 25.820  83.334  1.00 29.77 ? 530  LYS B CE    1 
ATOM   12609 N NZ    . LYS B  1 532  ? -13.600 27.230  83.646  1.00 30.51 ? 530  LYS B NZ    1 
ATOM   12610 N N     . HIS B  1 533  ? -16.120 25.468  87.502  1.00 27.62 ? 531  HIS B N     1 
ATOM   12611 C CA    . HIS B  1 533  ? -16.488 26.802  87.960  1.00 26.70 ? 531  HIS B CA    1 
ATOM   12612 C C     . HIS B  1 533  ? -16.264 27.821  86.849  1.00 33.25 ? 531  HIS B C     1 
ATOM   12613 O O     . HIS B  1 533  ? -15.209 27.831  86.204  1.00 28.31 ? 531  HIS B O     1 
ATOM   12614 C CB    . HIS B  1 533  ? -15.667 27.192  89.189  1.00 27.99 ? 531  HIS B CB    1 
ATOM   12615 C CG    . HIS B  1 533  ? -16.224 28.363  89.929  1.00 34.50 ? 531  HIS B CG    1 
ATOM   12616 N ND1   . HIS B  1 533  ? -16.145 29.651  89.449  1.00 35.67 ? 531  HIS B ND1   1 
ATOM   12617 C CD2   . HIS B  1 533  ? -16.885 28.440  91.110  1.00 36.37 ? 531  HIS B CD2   1 
ATOM   12618 C CE1   . HIS B  1 533  ? -16.726 30.474  90.304  1.00 39.97 ? 531  HIS B CE1   1 
ATOM   12619 N NE2   . HIS B  1 533  ? -17.183 29.765  91.320  1.00 39.24 ? 531  HIS B NE2   1 
ATOM   12620 N N     . ASP B  1 534  ? -17.258 28.692  86.644  1.00 33.71 ? 532  ASP B N     1 
ATOM   12621 C CA    . ASP B  1 534  ? -17.214 29.657  85.548  1.00 37.28 ? 532  ASP B CA    1 
ATOM   12622 C C     . ASP B  1 534  ? -16.106 30.688  85.699  1.00 33.01 ? 532  ASP B C     1 
ATOM   12623 O O     . ASP B  1 534  ? -15.687 31.277  84.699  1.00 33.23 ? 532  ASP B O     1 
ATOM   12624 C CB    . ASP B  1 534  ? -18.552 30.389  85.439  1.00 37.44 ? 532  ASP B CB    1 
ATOM   12625 C CG    . ASP B  1 534  ? -19.655 29.504  84.919  1.00 50.10 ? 532  ASP B CG    1 
ATOM   12626 O OD1   . ASP B  1 534  ? -19.382 28.694  84.003  1.00 51.72 ? 532  ASP B OD1   1 
ATOM   12627 O OD2   . ASP B  1 534  ? -20.791 29.617  85.431  1.00 58.14 ? 532  ASP B OD2   1 
ATOM   12628 N N     . ARG B  1 535  ? -15.643 30.942  86.916  1.00 29.44 ? 533  ARG B N     1 
ATOM   12629 C CA    . ARG B  1 535  ? -14.666 31.985  87.161  1.00 30.00 ? 533  ARG B CA    1 
ATOM   12630 C C     . ARG B  1 535  ? -13.252 31.442  87.347  1.00 31.57 ? 533  ARG B C     1 
ATOM   12631 O O     . ARG B  1 535  ? -12.348 32.213  87.678  1.00 31.74 ? 533  ARG B O     1 
ATOM   12632 C CB    . ARG B  1 535  ? -15.074 32.806  88.385  1.00 36.05 ? 533  ARG B CB    1 
ATOM   12633 N N     . ILE B  1 536  ? -13.031 30.142  87.157  1.00 25.04 ? 534  ILE B N     1 
ATOM   12634 C CA    . ILE B  1 536  ? -11.696 29.566  87.305  1.00 28.55 ? 534  ILE B CA    1 
ATOM   12635 C C     . ILE B  1 536  ? -11.229 29.081  85.943  1.00 26.26 ? 534  ILE B C     1 
ATOM   12636 O O     . ILE B  1 536  ? -11.872 28.217  85.331  1.00 26.58 ? 534  ILE B O     1 
ATOM   12637 C CB    . ILE B  1 536  ? -11.671 28.427  88.331  1.00 25.84 ? 534  ILE B CB    1 
ATOM   12638 C CG1   . ILE B  1 536  ? -12.230 28.917  89.664  1.00 31.46 ? 534  ILE B CG1   1 
ATOM   12639 C CG2   . ILE B  1 536  ? -10.248 27.921  88.512  1.00 28.36 ? 534  ILE B CG2   1 
ATOM   12640 C CD1   . ILE B  1 536  ? -12.063 27.937  90.771  1.00 29.74 ? 534  ILE B CD1   1 
ATOM   12641 N N     . ALA B  1 537  ? -10.114 29.639  85.472  1.00 25.70 ? 535  ALA B N     1 
ATOM   12642 C CA    . ALA B  1 537  ? -9.581  29.271  84.166  1.00 25.45 ? 535  ALA B CA    1 
ATOM   12643 C C     . ALA B  1 537  ? -8.819  27.956  84.244  1.00 23.04 ? 535  ALA B C     1 
ATOM   12644 O O     . ALA B  1 537  ? -7.963  27.779  85.114  1.00 21.17 ? 535  ALA B O     1 
ATOM   12645 C CB    . ALA B  1 537  ? -8.669  30.371  83.634  1.00 25.76 ? 535  ALA B CB    1 
ATOM   12646 N N     . LEU B  1 538  ? -9.158  27.017  83.353  1.00 23.85 ? 536  LEU B N     1 
ATOM   12647 C CA    . LEU B  1 538  ? -8.274  25.891  83.079  1.00 23.67 ? 536  LEU B CA    1 
ATOM   12648 C C     . LEU B  1 538  ? -6.889  26.423  82.741  1.00 23.92 ? 536  LEU B C     1 
ATOM   12649 O O     . LEU B  1 538  ? -6.776  27.504  82.153  1.00 21.85 ? 536  LEU B O     1 
ATOM   12650 C CB    . LEU B  1 538  ? -8.801  25.045  81.916  1.00 26.26 ? 536  LEU B CB    1 
ATOM   12651 C CG    . LEU B  1 538  ? -9.960  24.129  82.252  1.00 29.23 ? 536  LEU B CG    1 
ATOM   12652 C CD1   . LEU B  1 538  ? -10.496 23.538  80.964  1.00 27.94 ? 536  LEU B CD1   1 
ATOM   12653 C CD2   . LEU B  1 538  ? -9.479  23.037  83.177  1.00 27.10 ? 536  LEU B CD2   1 
ATOM   12654 N N     . PRO B  1 539  ? -5.815  25.724  83.123  1.00 21.73 ? 537  PRO B N     1 
ATOM   12655 C CA    . PRO B  1 539  ? -4.471  26.247  82.828  1.00 21.44 ? 537  PRO B CA    1 
ATOM   12656 C C     . PRO B  1 539  ? -4.295  26.616  81.360  1.00 19.82 ? 537  PRO B C     1 
ATOM   12657 O O     . PRO B  1 539  ? -3.705  27.661  81.060  1.00 21.95 ? 537  PRO B O     1 
ATOM   12658 C CB    . PRO B  1 539  ? -3.548  25.104  83.285  1.00 18.46 ? 537  PRO B CB    1 
ATOM   12659 C CG    . PRO B  1 539  ? -4.343  24.431  84.384  1.00 19.91 ? 537  PRO B CG    1 
ATOM   12660 C CD    . PRO B  1 539  ? -5.775  24.483  83.915  1.00 20.69 ? 537  PRO B CD    1 
ATOM   12661 N N     . ALA B  1 540  ? -4.865  25.834  80.438  1.00 19.65 ? 538  ALA B N     1 
ATOM   12662 C CA    . ALA B  1 540  ? -4.750  26.161  79.019  1.00 23.73 ? 538  ALA B CA    1 
ATOM   12663 C C     . ALA B  1 540  ? -5.442  27.476  78.662  1.00 26.65 ? 538  ALA B C     1 
ATOM   12664 O O     . ALA B  1 540  ? -5.069  28.117  77.667  1.00 22.89 ? 538  ALA B O     1 
ATOM   12665 C CB    . ALA B  1 540  ? -5.331  25.020  78.171  1.00 20.70 ? 538  ALA B CB    1 
ATOM   12666 N N     . GLU B  1 541  ? -6.427  27.894  79.457  1.00 25.72 ? 539  GLU B N     1 
ATOM   12667 C CA    . GLU B  1 541  ? -7.279  29.033  79.145  1.00 26.37 ? 539  GLU B CA    1 
ATOM   12668 C C     . GLU B  1 541  ? -6.930  30.272  79.976  1.00 25.21 ? 539  GLU B C     1 
ATOM   12669 O O     . GLU B  1 541  ? -7.710  31.229  80.024  1.00 25.44 ? 539  GLU B O     1 
ATOM   12670 C CB    . GLU B  1 541  ? -8.743  28.613  79.317  1.00 24.31 ? 539  GLU B CB    1 
ATOM   12671 C CG    . GLU B  1 541  ? -9.113  27.509  78.300  1.00 29.56 ? 539  GLU B CG    1 
ATOM   12672 C CD    . GLU B  1 541  ? -10.468 26.849  78.528  1.00 42.46 ? 539  GLU B CD    1 
ATOM   12673 O OE1   . GLU B  1 541  ? -11.235 27.291  79.409  1.00 42.08 ? 539  GLU B OE1   1 
ATOM   12674 O OE2   . GLU B  1 541  ? -10.767 25.869  77.810  1.00 44.95 ? 539  GLU B OE2   1 
ATOM   12675 N N     . LEU B  1 542  ? -5.746  30.288  80.586  1.00 21.73 ? 540  LEU B N     1 
ATOM   12676 C CA    . LEU B  1 542  ? -5.341  31.403  81.441  1.00 20.02 ? 540  LEU B CA    1 
ATOM   12677 C C     . LEU B  1 542  ? -5.362  32.748  80.721  1.00 24.22 ? 540  LEU B C     1 
ATOM   12678 O O     . LEU B  1 542  ? -5.505  33.793  81.367  1.00 22.53 ? 540  LEU B O     1 
ATOM   12679 C CB    . LEU B  1 542  ? -3.927  31.170  81.961  1.00 23.74 ? 540  LEU B CB    1 
ATOM   12680 C CG    . LEU B  1 542  ? -3.583  30.594  83.323  1.00 28.63 ? 540  LEU B CG    1 
ATOM   12681 C CD1   . LEU B  1 542  ? -2.151  31.018  83.596  1.00 24.42 ? 540  LEU B CD1   1 
ATOM   12682 C CD2   . LEU B  1 542  ? -4.543  31.018  84.434  1.00 21.98 ? 540  LEU B CD2   1 
ATOM   12683 N N     . PHE B  1 543  ? -5.176  32.757  79.401  1.00 22.21 ? 541  PHE B N     1 
ATOM   12684 C CA    . PHE B  1 543  ? -5.110  34.011  78.657  1.00 22.28 ? 541  PHE B CA    1 
ATOM   12685 C C     . PHE B  1 543  ? -6.364  34.277  77.840  1.00 26.05 ? 541  PHE B C     1 
ATOM   12686 O O     . PHE B  1 543  ? -6.369  35.201  77.021  1.00 25.47 ? 541  PHE B O     1 
ATOM   12687 C CB    . PHE B  1 543  ? -3.870  34.014  77.769  1.00 18.65 ? 541  PHE B CB    1 
ATOM   12688 C CG    . PHE B  1 543  ? -2.628  33.717  78.535  1.00 20.90 ? 541  PHE B CG    1 
ATOM   12689 C CD1   . PHE B  1 543  ? -2.338  34.438  79.678  1.00 25.60 ? 541  PHE B CD1   1 
ATOM   12690 C CD2   . PHE B  1 543  ? -1.806  32.660  78.185  1.00 17.45 ? 541  PHE B CD2   1 
ATOM   12691 C CE1   . PHE B  1 543  ? -1.207  34.149  80.439  1.00 22.96 ? 541  PHE B CE1   1 
ATOM   12692 C CE2   . PHE B  1 543  ? -0.671  32.363  78.941  1.00 21.81 ? 541  PHE B CE2   1 
ATOM   12693 C CZ    . PHE B  1 543  ? -0.374  33.116  80.060  1.00 24.92 ? 541  PHE B CZ    1 
ATOM   12694 N N     . GLY B  1 544  ? -7.427  33.511  78.065  1.00 25.25 ? 542  GLY B N     1 
ATOM   12695 C CA    . GLY B  1 544  ? -8.690  33.765  77.386  1.00 25.80 ? 542  GLY B CA    1 
ATOM   12696 C C     . GLY B  1 544  ? -8.569  33.567  75.887  1.00 31.86 ? 542  GLY B C     1 
ATOM   12697 O O     . GLY B  1 544  ? -7.856  32.680  75.404  1.00 25.32 ? 542  GLY B O     1 
ATOM   12698 N N     . ASP B  1 545  ? -9.274  34.412  75.130  1.00 27.56 ? 543  ASP B N     1 
ATOM   12699 C CA    . ASP B  1 545  ? -9.260  34.315  73.679  1.00 34.86 ? 543  ASP B CA    1 
ATOM   12700 C C     . ASP B  1 545  ? -7.972  34.835  73.048  1.00 31.22 ? 543  ASP B C     1 
ATOM   12701 O O     . ASP B  1 545  ? -7.774  34.640  71.846  1.00 31.64 ? 543  ASP B O     1 
ATOM   12702 C CB    . ASP B  1 545  ? -10.467 35.067  73.115  1.00 36.75 ? 543  ASP B CB    1 
ATOM   12703 C CG    . ASP B  1 545  ? -11.760 34.626  73.760  1.00 44.95 ? 543  ASP B CG    1 
ATOM   12704 O OD1   . ASP B  1 545  ? -11.926 33.403  73.966  1.00 44.47 ? 543  ASP B OD1   1 
ATOM   12705 O OD2   . ASP B  1 545  ? -12.597 35.496  74.082  1.00 56.73 ? 543  ASP B OD2   1 
ATOM   12706 N N     . ALA B  1 546  ? -7.091  35.475  73.821  1.00 27.66 ? 544  ALA B N     1 
ATOM   12707 C CA    . ALA B  1 546  ? -5.857  36.017  73.255  1.00 29.06 ? 544  ALA B CA    1 
ATOM   12708 C C     . ALA B  1 546  ? -4.990  34.920  72.643  1.00 29.32 ? 544  ALA B C     1 
ATOM   12709 O O     . ALA B  1 546  ? -4.506  35.057  71.513  1.00 27.25 ? 544  ALA B O     1 
ATOM   12710 C CB    . ALA B  1 546  ? -5.079  36.779  74.327  1.00 27.67 ? 544  ALA B CB    1 
ATOM   12711 N N     . ARG B  1 547  ? -4.790  33.821  73.371  1.00 25.50 ? 545  ARG B N     1 
ATOM   12712 C CA    . ARG B  1 547  ? -3.911  32.743  72.933  1.00 25.36 ? 545  ARG B CA    1 
ATOM   12713 C C     . ARG B  1 547  ? -4.044  31.583  73.906  1.00 24.24 ? 545  ARG B C     1 
ATOM   12714 O O     . ARG B  1 547  ? -4.519  31.744  75.032  1.00 22.45 ? 545  ARG B O     1 
ATOM   12715 C CB    . ARG B  1 547  ? -2.453  33.197  72.854  1.00 28.46 ? 545  ARG B CB    1 
ATOM   12716 C CG    . ARG B  1 547  ? -1.924  33.649  74.184  1.00 23.77 ? 545  ARG B CG    1 
ATOM   12717 C CD    . ARG B  1 547  ? -0.486  34.107  74.088  1.00 26.86 ? 545  ARG B CD    1 
ATOM   12718 N NE    . ARG B  1 547  ? -0.169  34.935  75.238  1.00 25.84 ? 545  ARG B NE    1 
ATOM   12719 C CZ    . ARG B  1 547  ? 0.578   34.556  76.269  1.00 25.78 ? 545  ARG B CZ    1 
ATOM   12720 N NH1   . ARG B  1 547  ? 1.166   33.368  76.304  1.00 22.38 ? 545  ARG B NH1   1 
ATOM   12721 N NH2   . ARG B  1 547  ? 0.737   35.390  77.290  1.00 24.77 ? 545  ARG B NH2   1 
ATOM   12722 N N     . THR B  1 548  ? -3.615  30.414  73.453  1.00 20.99 ? 546  THR B N     1 
ATOM   12723 C CA    . THR B  1 548  ? -3.608  29.206  74.260  1.00 18.97 ? 546  THR B CA    1 
ATOM   12724 C C     . THR B  1 548  ? -2.312  29.124  75.062  1.00 20.93 ? 546  THR B C     1 
ATOM   12725 O O     . THR B  1 548  ? -1.225  29.213  74.494  1.00 18.01 ? 546  THR B O     1 
ATOM   12726 C CB    . THR B  1 548  ? -3.752  27.992  73.353  1.00 20.97 ? 546  THR B CB    1 
ATOM   12727 O OG1   . THR B  1 548  ? -4.924  28.175  72.542  1.00 24.12 ? 546  THR B OG1   1 
ATOM   12728 C CG2   . THR B  1 548  ? -3.896  26.730  74.177  1.00 20.97 ? 546  THR B CG2   1 
ATOM   12729 N N     . ASN B  1 549  ? -2.439  28.960  76.379  1.00 18.39 ? 547  ASN B N     1 
ATOM   12730 C CA    . ASN B  1 549  ? -1.273  28.800  77.238  1.00 20.99 ? 547  ASN B CA    1 
ATOM   12731 C C     . ASN B  1 549  ? -0.529  27.520  76.879  1.00 19.94 ? 547  ASN B C     1 
ATOM   12732 O O     . ASN B  1 549  ? -1.152  26.519  76.514  1.00 22.89 ? 547  ASN B O     1 
ATOM   12733 C CB    . ASN B  1 549  ? -1.726  28.770  78.700  1.00 20.12 ? 547  ASN B CB    1 
ATOM   12734 C CG    . ASN B  1 549  ? -0.558  28.845  79.690  1.00 17.10 ? 547  ASN B CG    1 
ATOM   12735 O OD1   . ASN B  1 549  ? 0.556   29.237  79.336  1.00 19.61 ? 547  ASN B OD1   1 
ATOM   12736 N ND2   . ASN B  1 549  ? -0.825  28.456  80.939  1.00 21.14 ? 547  ASN B ND2   1 
ATOM   12737 N N     . SER B  1 550  ? 0.809   27.550  76.991  1.00 20.73 ? 548  SER B N     1 
ATOM   12738 C CA    . SER B  1 550  ? 1.590   26.334  76.791  1.00 19.09 ? 548  SER B CA    1 
ATOM   12739 C C     . SER B  1 550  ? 1.242   25.312  77.869  1.00 18.55 ? 548  SER B C     1 
ATOM   12740 O O     . SER B  1 550  ? 0.816   25.661  78.975  1.00 22.55 ? 548  SER B O     1 
ATOM   12741 C CB    . SER B  1 550  ? 3.089   26.635  76.814  1.00 19.82 ? 548  SER B CB    1 
ATOM   12742 O OG    . SER B  1 550  ? 3.451   27.280  78.026  1.00 19.82 ? 548  SER B OG    1 
ATOM   12743 N N     . ALA B  1 551  ? 1.412   24.037  77.538  1.00 18.45 ? 549  ALA B N     1 
ATOM   12744 C CA    . ALA B  1 551  ? 1.131   22.948  78.462  1.00 19.81 ? 549  ALA B CA    1 
ATOM   12745 C C     . ALA B  1 551  ? 2.432   22.326  78.942  1.00 20.81 ? 549  ALA B C     1 
ATOM   12746 O O     . ALA B  1 551  ? 3.378   22.151  78.160  1.00 18.65 ? 549  ALA B O     1 
ATOM   12747 C CB    . ALA B  1 551  ? 0.264   21.866  77.815  1.00 21.94 ? 549  ALA B CB    1 
ATOM   12748 N N     . GLY B  1 552  ? 2.474   21.988  80.225  1.00 21.93 ? 550  GLY B N     1 
ATOM   12749 C CA    . GLY B  1 552  ? 3.601   21.298  80.810  1.00 23.23 ? 550  GLY B CA    1 
ATOM   12750 C C     . GLY B  1 552  ? 3.375   19.801  80.897  1.00 21.76 ? 550  GLY B C     1 
ATOM   12751 O O     . GLY B  1 552  ? 2.493   19.231  80.246  1.00 23.33 ? 550  GLY B O     1 
ATOM   12752 N N     . LEU B  1 553  ? 4.191   19.148  81.721  1.00 23.14 ? 551  LEU B N     1 
ATOM   12753 C CA    . LEU B  1 553  ? 4.046   17.722  81.962  1.00 26.07 ? 551  LEU B CA    1 
ATOM   12754 C C     . LEU B  1 553  ? 4.118   17.491  83.463  1.00 21.96 ? 551  LEU B C     1 
ATOM   12755 O O     . LEU B  1 553  ? 4.862   18.177  84.158  1.00 24.25 ? 551  LEU B O     1 
ATOM   12756 C CB    . LEU B  1 553  ? 5.129   16.916  81.232  1.00 27.22 ? 551  LEU B CB    1 
ATOM   12757 C CG    . LEU B  1 553  ? 5.105   16.932  79.701  1.00 28.24 ? 551  LEU B CG    1 
ATOM   12758 C CD1   . LEU B  1 553  ? 6.433   16.392  79.147  1.00 28.30 ? 551  LEU B CD1   1 
ATOM   12759 C CD2   . LEU B  1 553  ? 3.900   16.154  79.131  1.00 26.48 ? 551  LEU B CD2   1 
ATOM   12760 N N     . ASP B  1 554  ? 3.317   16.560  83.963  1.00 25.87 ? 552  ASP B N     1 
ATOM   12761 C CA    . ASP B  1 554  ? 3.196   16.351  85.406  1.00 27.11 ? 552  ASP B CA    1 
ATOM   12762 C C     . ASP B  1 554  ? 4.227   15.307  85.818  1.00 25.68 ? 552  ASP B C     1 
ATOM   12763 O O     . ASP B  1 554  ? 4.023   14.107  85.630  1.00 23.74 ? 552  ASP B O     1 
ATOM   12764 C CB    . ASP B  1 554  ? 1.781   15.916  85.772  1.00 25.86 ? 552  ASP B CB    1 
ATOM   12765 C CG    . ASP B  1 554  ? 1.588   15.755  87.268  1.00 27.43 ? 552  ASP B CG    1 
ATOM   12766 O OD1   . ASP B  1 554  ? 2.574   15.918  88.026  1.00 25.51 ? 552  ASP B OD1   1 
ATOM   12767 O OD2   . ASP B  1 554  ? 0.441   15.467  87.673  1.00 28.64 ? 552  ASP B OD2   1 
ATOM   12768 N N     . LEU B  1 555  ? 5.325   15.758  86.409  1.00 23.98 ? 553  LEU B N     1 
ATOM   12769 C CA    . LEU B  1 555  ? 6.382   14.838  86.798  1.00 26.38 ? 553  LEU B CA    1 
ATOM   12770 C C     . LEU B  1 555  ? 6.063   14.076  88.081  1.00 27.33 ? 553  LEU B C     1 
ATOM   12771 O O     . LEU B  1 555  ? 6.947   13.388  88.603  1.00 26.25 ? 553  LEU B O     1 
ATOM   12772 C CB    . LEU B  1 555  ? 7.712   15.593  86.936  1.00 25.97 ? 553  LEU B CB    1 
ATOM   12773 C CG    . LEU B  1 555  ? 8.287   16.231  85.654  1.00 28.15 ? 553  LEU B CG    1 
ATOM   12774 C CD1   . LEU B  1 555  ? 9.684   16.804  85.881  1.00 28.02 ? 553  LEU B CD1   1 
ATOM   12775 C CD2   . LEU B  1 555  ? 8.306   15.232  84.499  1.00 30.20 ? 553  LEU B CD2   1 
ATOM   12776 N N     . SER B  1 556  ? 4.837   14.177  88.600  1.00 24.01 ? 554  SER B N     1 
ATOM   12777 C CA    . SER B  1 556  ? 4.386   13.340  89.707  1.00 23.15 ? 554  SER B CA    1 
ATOM   12778 C C     . SER B  1 556  ? 3.469   12.224  89.232  1.00 25.35 ? 554  SER B C     1 
ATOM   12779 O O     . SER B  1 556  ? 3.087   11.357  90.026  1.00 27.07 ? 554  SER B O     1 
ATOM   12780 C CB    . SER B  1 556  ? 3.651   14.186  90.761  1.00 24.85 ? 554  SER B CB    1 
ATOM   12781 O OG    . SER B  1 556  ? 2.401   14.640  90.239  1.00 27.05 ? 554  SER B OG    1 
ATOM   12782 N N     . ASN B  1 557  ? 3.128   12.228  87.948  1.00 24.74 ? 555  ASN B N     1 
ATOM   12783 C CA    . ASN B  1 557  ? 2.215   11.276  87.341  1.00 26.69 ? 555  ASN B CA    1 
ATOM   12784 C C     . ASN B  1 557  ? 3.016   10.093  86.795  1.00 24.40 ? 555  ASN B C     1 
ATOM   12785 O O     . ASN B  1 557  ? 3.886   10.272  85.933  1.00 25.11 ? 555  ASN B O     1 
ATOM   12786 C CB    . ASN B  1 557  ? 1.428   11.984  86.238  1.00 25.05 ? 555  ASN B CB    1 
ATOM   12787 C CG    . ASN B  1 557  ? 0.382   11.096  85.595  1.00 27.18 ? 555  ASN B CG    1 
ATOM   12788 O OD1   . ASN B  1 557  ? 0.673   9.975   85.179  1.00 26.70 ? 555  ASN B OD1   1 
ATOM   12789 N ND2   . ASN B  1 557  ? -0.860  11.589  85.530  1.00 24.10 ? 555  ASN B ND2   1 
ATOM   12790 N N     . GLU B  1 558  ? 2.747   8.892   87.320  1.00 28.78 ? 556  GLU B N     1 
ATOM   12791 C CA    . GLU B  1 558  ? 3.548   7.727   86.937  1.00 28.81 ? 556  GLU B CA    1 
ATOM   12792 C C     . GLU B  1 558  ? 3.346   7.344   85.478  1.00 28.98 ? 556  GLU B C     1 
ATOM   12793 O O     . GLU B  1 558  ? 4.283   6.846   84.846  1.00 31.94 ? 556  GLU B O     1 
ATOM   12794 C CB    . GLU B  1 558  ? 3.233   6.524   87.823  1.00 28.36 ? 556  GLU B CB    1 
ATOM   12795 C CG    . GLU B  1 558  ? 3.615   6.727   89.264  1.00 26.70 ? 556  GLU B CG    1 
ATOM   12796 C CD    . GLU B  1 558  ? 5.113   6.699   89.514  1.00 29.77 ? 556  GLU B CD    1 
ATOM   12797 O OE1   . GLU B  1 558  ? 5.916   6.435   88.588  1.00 31.35 ? 556  GLU B OE1   1 
ATOM   12798 O OE2   . GLU B  1 558  ? 5.489   6.936   90.669  1.00 29.98 ? 556  GLU B OE2   1 
ATOM   12799 N N     . GLU B  1 559  ? 2.137   7.522   84.940  1.00 28.97 ? 557  GLU B N     1 
ATOM   12800 C CA    . GLU B  1 559  ? 1.944   7.338   83.502  1.00 29.60 ? 557  GLU B CA    1 
ATOM   12801 C C     . GLU B  1 559  ? 2.890   8.237   82.718  1.00 26.96 ? 557  GLU B C     1 
ATOM   12802 O O     . GLU B  1 559  ? 3.558   7.794   81.776  1.00 25.57 ? 557  GLU B O     1 
ATOM   12803 C CB    . GLU B  1 559  ? 0.504   7.655   83.086  1.00 33.27 ? 557  GLU B CB    1 
ATOM   12804 C CG    . GLU B  1 559  ? -0.595  6.708   83.523  1.00 37.77 ? 557  GLU B CG    1 
ATOM   12805 C CD    . GLU B  1 559  ? -1.960  7.128   82.950  1.00 44.01 ? 557  GLU B CD    1 
ATOM   12806 O OE1   . GLU B  1 559  ? -1.992  7.836   81.915  1.00 47.78 ? 557  GLU B OE1   1 
ATOM   12807 O OE2   . GLU B  1 559  ? -3.001  6.762   83.539  1.00 42.65 ? 557  GLU B OE2   1 
ATOM   12808 N N     . THR B  1 560  ? 2.932   9.521   83.087  1.00 24.82 ? 558  THR B N     1 
ATOM   12809 C CA    . THR B  1 560  ? 3.790   10.484  82.410  1.00 26.42 ? 558  THR B CA    1 
ATOM   12810 C C     . THR B  1 560  ? 5.263   10.115  82.558  1.00 26.67 ? 558  THR B C     1 
ATOM   12811 O O     . THR B  1 560  ? 6.020   10.152  81.583  1.00 25.62 ? 558  THR B O     1 
ATOM   12812 C CB    . THR B  1 560  ? 3.533   11.899  82.960  1.00 27.31 ? 558  THR B CB    1 
ATOM   12813 O OG1   . THR B  1 560  ? 2.149   12.255  82.797  1.00 27.59 ? 558  THR B OG1   1 
ATOM   12814 C CG2   . THR B  1 560  ? 4.394   12.919  82.227  1.00 24.08 ? 558  THR B CG2   1 
ATOM   12815 N N     . LEU B  1 561  ? 5.695   9.766   83.775  1.00 24.48 ? 559  LEU B N     1 
ATOM   12816 C CA    . LEU B  1 561  ? 7.097   9.407   83.966  1.00 25.69 ? 559  LEU B CA    1 
ATOM   12817 C C     . LEU B  1 561  ? 7.478   8.191   83.133  1.00 25.91 ? 559  LEU B C     1 
ATOM   12818 O O     . LEU B  1 561  ? 8.570   8.151   82.556  1.00 28.92 ? 559  LEU B O     1 
ATOM   12819 C CB    . LEU B  1 561  ? 7.397   9.152   85.443  1.00 24.70 ? 559  LEU B CB    1 
ATOM   12820 C CG    . LEU B  1 561  ? 7.296   10.405  86.312  1.00 25.70 ? 559  LEU B CG    1 
ATOM   12821 C CD1   . LEU B  1 561  ? 7.447   10.027  87.780  1.00 23.34 ? 559  LEU B CD1   1 
ATOM   12822 C CD2   . LEU B  1 561  ? 8.352   11.400  85.903  1.00 21.27 ? 559  LEU B CD2   1 
ATOM   12823 N N     . ALA B  1 562  ? 6.592   7.197   83.043  1.00 27.98 ? 560  ALA B N     1 
ATOM   12824 C CA    . ALA B  1 562  ? 6.919   6.003   82.267  1.00 26.19 ? 560  ALA B CA    1 
ATOM   12825 C C     . ALA B  1 562  ? 7.009   6.319   80.776  1.00 30.15 ? 560  ALA B C     1 
ATOM   12826 O O     . ALA B  1 562  ? 7.974   5.936   80.107  1.00 27.21 ? 560  ALA B O     1 
ATOM   12827 C CB    . ALA B  1 562  ? 5.896   4.901   82.529  1.00 27.62 ? 560  ALA B CB    1 
ATOM   12828 N N     . SER B  1 563  ? 6.022   7.031   80.232  1.00 25.66 ? 561  SER B N     1 
ATOM   12829 C CA    . SER B  1 563  ? 6.093   7.337   78.807  1.00 26.27 ? 561  SER B CA    1 
ATOM   12830 C C     . SER B  1 563  ? 7.200   8.344   78.505  1.00 27.77 ? 561  SER B C     1 
ATOM   12831 O O     . SER B  1 563  ? 7.815   8.287   77.434  1.00 29.18 ? 561  SER B O     1 
ATOM   12832 C CB    . SER B  1 563  ? 4.741   7.843   78.300  1.00 31.97 ? 561  SER B CB    1 
ATOM   12833 O OG    . SER B  1 563  ? 4.527   9.178   78.709  1.00 36.60 ? 561  SER B OG    1 
ATOM   12834 N N     . LEU B  1 564  ? 7.476   9.263   79.437  1.00 27.00 ? 562  LEU B N     1 
ATOM   12835 C CA    . LEU B  1 564  ? 8.575   10.203  79.251  1.00 26.90 ? 562  LEU B CA    1 
ATOM   12836 C C     . LEU B  1 564  ? 9.927   9.496   79.289  1.00 28.39 ? 562  LEU B C     1 
ATOM   12837 O O     . LEU B  1 564  ? 10.829  9.833   78.515  1.00 26.98 ? 562  LEU B O     1 
ATOM   12838 C CB    . LEU B  1 564  ? 8.509   11.292  80.321  1.00 26.33 ? 562  LEU B CB    1 
ATOM   12839 C CG    . LEU B  1 564  ? 9.495   12.434  80.215  1.00 26.91 ? 562  LEU B CG    1 
ATOM   12840 C CD1   . LEU B  1 564  ? 9.246   13.196  78.924  1.00 26.84 ? 562  LEU B CD1   1 
ATOM   12841 C CD2   . LEU B  1 564  ? 9.341   13.346  81.438  1.00 29.75 ? 562  LEU B CD2   1 
ATOM   12842 N N     . THR B  1 565  ? 10.095  8.530   80.196  1.00 25.96 ? 563  THR B N     1 
ATOM   12843 C CA    . THR B  1 565  ? 11.331  7.757   80.228  1.00 29.15 ? 563  THR B CA    1 
ATOM   12844 C C     . THR B  1 565  ? 11.617  7.149   78.857  1.00 29.00 ? 563  THR B C     1 
ATOM   12845 O O     . THR B  1 565  ? 12.748  7.209   78.363  1.00 28.51 ? 563  THR B O     1 
ATOM   12846 C CB    . THR B  1 565  ? 11.250  6.661   81.297  1.00 30.11 ? 563  THR B CB    1 
ATOM   12847 O OG1   . THR B  1 565  ? 11.149  7.249   82.609  1.00 28.26 ? 563  THR B OG1   1 
ATOM   12848 C CG2   . THR B  1 565  ? 12.491  5.778   81.243  1.00 29.92 ? 563  THR B CG2   1 
ATOM   12849 N N     . GLU B  1 566  ? 10.595  6.603   78.206  1.00 29.64 ? 564  GLU B N     1 
ATOM   12850 C CA    . GLU B  1 566  ? 10.822  5.986   76.903  1.00 30.91 ? 564  GLU B CA    1 
ATOM   12851 C C     . GLU B  1 566  ? 11.132  7.032   75.835  1.00 29.21 ? 564  GLU B C     1 
ATOM   12852 O O     . GLU B  1 566  ? 11.996  6.808   74.978  1.00 28.76 ? 564  GLU B O     1 
ATOM   12853 C CB    . GLU B  1 566  ? 9.619   5.128   76.504  1.00 35.13 ? 564  GLU B CB    1 
ATOM   12854 C CG    . GLU B  1 566  ? 9.473   3.867   77.349  1.00 40.07 ? 564  GLU B CG    1 
ATOM   12855 C CD    . GLU B  1 566  ? 10.809  3.181   77.642  1.00 46.56 ? 564  GLU B CD    1 
ATOM   12856 O OE1   . GLU B  1 566  ? 11.551  2.862   76.681  1.00 51.09 ? 564  GLU B OE1   1 
ATOM   12857 O OE2   . GLU B  1 566  ? 11.116  2.963   78.842  1.00 44.31 ? 564  GLU B OE2   1 
ATOM   12858 N N     . ALA B  1 567  ? 10.452  8.186   75.879  1.00 27.34 ? 565  ALA B N     1 
ATOM   12859 C CA    . ALA B  1 567  ? 10.712  9.252   74.909  1.00 25.65 ? 565  ALA B CA    1 
ATOM   12860 C C     . ALA B  1 567  ? 12.115  9.823   75.070  1.00 26.75 ? 565  ALA B C     1 
ATOM   12861 O O     . ALA B  1 567  ? 12.779  10.159  74.077  1.00 24.32 ? 565  ALA B O     1 
ATOM   12862 C CB    . ALA B  1 567  ? 9.673   10.366  75.056  1.00 25.17 ? 565  ALA B CB    1 
ATOM   12863 N N     . LEU B  1 568  ? 12.575  9.945   76.313  1.00 23.84 ? 566  LEU B N     1 
ATOM   12864 C CA    . LEU B  1 568  ? 13.917  10.449  76.579  1.00 25.11 ? 566  LEU B CA    1 
ATOM   12865 C C     . LEU B  1 568  ? 14.983  9.455   76.119  1.00 26.36 ? 566  LEU B C     1 
ATOM   12866 O O     . LEU B  1 568  ? 15.963  9.838   75.470  1.00 27.01 ? 566  LEU B O     1 
ATOM   12867 C CB    . LEU B  1 568  ? 14.055  10.762  78.073  1.00 26.77 ? 566  LEU B CB    1 
ATOM   12868 C CG    . LEU B  1 568  ? 13.153  11.874  78.645  1.00 25.40 ? 566  LEU B CG    1 
ATOM   12869 C CD1   . LEU B  1 568  ? 13.290  11.970  80.164  1.00 25.29 ? 566  LEU B CD1   1 
ATOM   12870 C CD2   . LEU B  1 568  ? 13.426  13.243  77.999  1.00 22.40 ? 566  LEU B CD2   1 
ATOM   12871 N N     . ARG B  1 569  ? 14.816  8.175   76.461  1.00 25.43 ? 567  ARG B N     1 
ATOM   12872 C CA    . ARG B  1 569  ? 15.702  7.133   75.947  1.00 27.86 ? 567  ARG B CA    1 
ATOM   12873 C C     . ARG B  1 569  ? 15.766  7.152   74.425  1.00 28.02 ? 567  ARG B C     1 
ATOM   12874 O O     . ARG B  1 569  ? 16.855  7.105   73.840  1.00 29.94 ? 567  ARG B O     1 
ATOM   12875 C CB    . ARG B  1 569  ? 15.242  5.758   76.437  1.00 29.67 ? 567  ARG B CB    1 
ATOM   12876 C CG    . ARG B  1 569  ? 15.543  5.471   77.898  1.00 30.83 ? 567  ARG B CG    1 
ATOM   12877 C CD    . ARG B  1 569  ? 15.127  4.050   78.269  1.00 35.79 ? 567  ARG B CD    1 
ATOM   12878 N NE    . ARG B  1 569  ? 15.305  3.764   79.688  1.00 45.29 ? 567  ARG B NE    1 
ATOM   12879 C CZ    . ARG B  1 569  ? 14.615  2.851   80.361  1.00 49.00 ? 567  ARG B CZ    1 
ATOM   12880 N NH1   . ARG B  1 569  ? 13.648  2.153   79.788  1.00 45.39 ? 567  ARG B NH1   1 
ATOM   12881 N NH2   . ARG B  1 569  ? 14.895  2.637   81.644  1.00 49.77 ? 567  ARG B NH2   1 
ATOM   12882 N N     . GLU B  1 570  ? 14.604  7.211   73.763  1.00 28.19 ? 568  GLU B N     1 
ATOM   12883 C CA    . GLU B  1 570  ? 14.590  7.249   72.302  1.00 25.84 ? 568  GLU B CA    1 
ATOM   12884 C C     . GLU B  1 570  ? 15.297  8.491   71.774  1.00 24.63 ? 568  GLU B C     1 
ATOM   12885 O O     . GLU B  1 570  ? 15.993  8.427   70.757  1.00 27.07 ? 568  GLU B O     1 
ATOM   12886 C CB    . GLU B  1 570  ? 13.153  7.188   71.782  1.00 28.16 ? 568  GLU B CB    1 
ATOM   12887 N N     . SER B  1 571  ? 15.165  9.626   72.475  1.00 24.79 ? 569  SER B N     1 
ATOM   12888 C CA    . SER B  1 571  ? 15.796  10.855  72.010  1.00 24.71 ? 569  SER B CA    1 
ATOM   12889 C C     . SER B  1 571  ? 17.308  10.738  72.033  1.00 31.05 ? 569  SER B C     1 
ATOM   12890 O O     . SER B  1 571  ? 17.988  11.322  71.183  1.00 26.61 ? 569  SER B O     1 
ATOM   12891 C CB    . SER B  1 571  ? 15.365  12.040  72.867  1.00 22.71 ? 569  SER B CB    1 
ATOM   12892 O OG    . SER B  1 571  ? 16.114  12.047  74.089  1.00 27.59 ? 569  SER B OG    1 
ATOM   12893 N N     . ALA B  1 572  ? 17.852  10.011  73.008  1.00 29.33 ? 570  ALA B N     1 
ATOM   12894 C CA    . ALA B  1 572  ? 19.292  9.844   73.065  1.00 28.80 ? 570  ALA B CA    1 
ATOM   12895 C C     . ALA B  1 572  ? 19.818  8.891   72.000  1.00 31.22 ? 570  ALA B C     1 
ATOM   12896 O O     . ALA B  1 572  ? 21.037  8.846   71.788  1.00 31.19 ? 570  ALA B O     1 
ATOM   12897 C CB    . ALA B  1 572  ? 19.701  9.357   74.451  1.00 26.50 ? 570  ALA B CB    1 
ATOM   12898 N N     . ALA B  1 573  ? 18.945  8.141   71.331  1.00 29.53 ? 571  ALA B N     1 
ATOM   12899 C CA    . ALA B  1 573  ? 19.384  7.242   70.273  1.00 31.07 ? 571  ALA B CA    1 
ATOM   12900 C C     . ALA B  1 573  ? 19.310  7.874   68.884  1.00 27.37 ? 571  ALA B C     1 
ATOM   12901 O O     . ALA B  1 573  ? 19.777  7.259   67.921  1.00 27.14 ? 571  ALA B O     1 
ATOM   12902 C CB    . ALA B  1 573  ? 18.566  5.945   70.293  1.00 28.87 ? 571  ALA B CB    1 
ATOM   12903 N N     . MET B  1 574  ? 18.773  9.086   68.767  1.00 27.00 ? 572  MET B N     1 
ATOM   12904 C CA    . MET B  1 574  ? 18.703  9.764   67.481  1.00 29.30 ? 572  MET B CA    1 
ATOM   12905 C C     . MET B  1 574  ? 20.034  10.422  67.135  1.00 27.01 ? 572  MET B C     1 
ATOM   12906 O O     . MET B  1 574  ? 20.810  10.811  68.011  1.00 26.01 ? 572  MET B O     1 
ATOM   12907 C CB    . MET B  1 574  ? 17.597  10.816  67.486  1.00 27.29 ? 572  MET B CB    1 
ATOM   12908 C CG    . MET B  1 574  ? 16.196  10.241  67.714  1.00 29.46 ? 572  MET B CG    1 
ATOM   12909 S SD    . MET B  1 574  ? 15.034  11.523  68.224  1.00 34.04 ? 572  MET B SD    1 
ATOM   12910 C CE    . MET B  1 574  ? 13.562  10.528  68.512  1.00 34.49 ? 572  MET B CE    1 
ATOM   12911 N N     . LYS B  1 575  ? 20.272  10.574  65.840  1.00 23.18 ? 573  LYS B N     1 
ATOM   12912 C CA    . LYS B  1 575  ? 21.434  11.294  65.322  1.00 27.36 ? 573  LYS B CA    1 
ATOM   12913 C C     . LYS B  1 575  ? 21.095  12.783  65.251  1.00 25.06 ? 573  LYS B C     1 
ATOM   12914 O O     . LYS B  1 575  ? 20.429  13.242  64.323  1.00 25.78 ? 573  LYS B O     1 
ATOM   12915 C CB    . LYS B  1 575  ? 21.838  10.744  63.958  1.00 23.57 ? 573  LYS B CB    1 
ATOM   12916 C CG    . LYS B  1 575  ? 22.949  11.531  63.294  1.00 29.74 ? 573  LYS B CG    1 
ATOM   12917 C CD    . LYS B  1 575  ? 23.495  10.797  62.076  1.00 34.88 ? 573  LYS B CD    1 
ATOM   12918 C CE    . LYS B  1 575  ? 24.631  11.572  61.425  1.00 42.53 ? 573  LYS B CE    1 
ATOM   12919 N NZ    . LYS B  1 575  ? 25.713  11.880  62.408  1.00 46.16 ? 573  LYS B NZ    1 
ATOM   12920 N N     . TRP B  1 576  ? 21.565  13.543  66.231  1.00 23.07 ? 574  TRP B N     1 
ATOM   12921 C CA    . TRP B  1 576  ? 21.331  14.981  66.280  1.00 27.52 ? 574  TRP B CA    1 
ATOM   12922 C C     . TRP B  1 576  ? 22.473  15.727  65.597  1.00 28.96 ? 574  TRP B C     1 
ATOM   12923 O O     . TRP B  1 576  ? 23.648  15.527  65.933  1.00 25.82 ? 574  TRP B O     1 
ATOM   12924 C CB    . TRP B  1 576  ? 21.201  15.459  67.722  1.00 26.23 ? 574  TRP B CB    1 
ATOM   12925 C CG    . TRP B  1 576  ? 20.048  14.882  68.472  1.00 28.02 ? 574  TRP B CG    1 
ATOM   12926 C CD1   . TRP B  1 576  ? 20.089  13.901  69.422  1.00 27.91 ? 574  TRP B CD1   1 
ATOM   12927 C CD2   . TRP B  1 576  ? 18.677  15.269  68.351  1.00 25.76 ? 574  TRP B CD2   1 
ATOM   12928 N NE1   . TRP B  1 576  ? 18.823  13.655  69.903  1.00 24.81 ? 574  TRP B NE1   1 
ATOM   12929 C CE2   . TRP B  1 576  ? 17.936  14.476  69.254  1.00 26.68 ? 574  TRP B CE2   1 
ATOM   12930 C CE3   . TRP B  1 576  ? 18.003  16.210  67.564  1.00 25.50 ? 574  TRP B CE3   1 
ATOM   12931 C CZ2   . TRP B  1 576  ? 16.550  14.596  69.396  1.00 26.91 ? 574  TRP B CZ2   1 
ATOM   12932 C CZ3   . TRP B  1 576  ? 16.632  16.330  67.706  1.00 24.99 ? 574  TRP B CZ3   1 
ATOM   12933 C CH2   . TRP B  1 576  ? 15.917  15.525  68.611  1.00 25.37 ? 574  TRP B CH2   1 
ATOM   12934 N N     . THR B  1 577  ? 22.123  16.600  64.654  1.00 26.21 ? 575  THR B N     1 
ATOM   12935 C CA    . THR B  1 577  ? 23.112  17.392  63.940  1.00 25.37 ? 575  THR B CA    1 
ATOM   12936 C C     . THR B  1 577  ? 22.671  18.849  63.884  1.00 24.04 ? 575  THR B C     1 
ATOM   12937 O O     . THR B  1 577  ? 21.498  19.183  64.078  1.00 24.24 ? 575  THR B O     1 
ATOM   12938 C CB    . THR B  1 577  ? 23.341  16.870  62.513  1.00 26.96 ? 575  THR B CB    1 
ATOM   12939 O OG1   . THR B  1 577  ? 22.111  16.944  61.777  1.00 27.64 ? 575  THR B OG1   1 
ATOM   12940 C CG2   . THR B  1 577  ? 23.824  15.436  62.526  1.00 29.99 ? 575  THR B CG2   1 
ATOM   12941 N N     . ALA B  1 578  ? 23.646  19.715  63.627  1.00 23.87 ? 576  ALA B N     1 
ATOM   12942 C CA    . ALA B  1 578  ? 23.405  21.116  63.314  1.00 20.89 ? 576  ALA B CA    1 
ATOM   12943 C C     . ALA B  1 578  ? 24.380  21.507  62.220  1.00 20.98 ? 576  ALA B C     1 
ATOM   12944 O O     . ALA B  1 578  ? 25.577  21.218  62.313  1.00 25.55 ? 576  ALA B O     1 
ATOM   12945 C CB    . ALA B  1 578  ? 23.581  22.037  64.528  1.00 18.97 ? 576  ALA B CB    1 
ATOM   12946 N N     . LEU B  1 579  ? 23.875  22.131  61.176  1.00 23.22 ? 577  LEU B N     1 
ATOM   12947 C CA    . LEU B  1 579  ? 24.717  22.500  60.053  1.00 24.36 ? 577  LEU B CA    1 
ATOM   12948 C C     . LEU B  1 579  ? 24.399  23.932  59.658  1.00 22.37 ? 577  LEU B C     1 
ATOM   12949 O O     . LEU B  1 579  ? 23.363  24.469  60.053  1.00 22.48 ? 577  LEU B O     1 
ATOM   12950 C CB    . LEU B  1 579  ? 24.499  21.558  58.865  1.00 27.42 ? 577  LEU B CB    1 
ATOM   12951 C CG    . LEU B  1 579  ? 25.169  20.209  59.118  1.00 30.53 ? 577  LEU B CG    1 
ATOM   12952 C CD1   . LEU B  1 579  ? 24.134  19.153  59.413  1.00 33.25 ? 577  LEU B CD1   1 
ATOM   12953 C CD2   . LEU B  1 579  ? 26.011  19.840  57.930  1.00 32.53 ? 577  LEU B CD2   1 
ATOM   12954 N N     . PRO B  1 580  ? 25.283  24.576  58.897  1.00 21.33 ? 578  PRO B N     1 
ATOM   12955 C CA    . PRO B  1 580  ? 24.911  25.859  58.287  1.00 22.26 ? 578  PRO B CA    1 
ATOM   12956 C C     . PRO B  1 580  ? 23.789  25.630  57.295  1.00 22.02 ? 578  PRO B C     1 
ATOM   12957 O O     . PRO B  1 580  ? 24.031  25.090  56.214  1.00 24.94 ? 578  PRO B O     1 
ATOM   12958 C CB    . PRO B  1 580  ? 26.195  26.312  57.574  1.00 24.44 ? 578  PRO B CB    1 
ATOM   12959 C CG    . PRO B  1 580  ? 27.287  25.442  58.119  1.00 27.79 ? 578  PRO B CG    1 
ATOM   12960 C CD    . PRO B  1 580  ? 26.645  24.161  58.528  1.00 23.75 ? 578  PRO B CD    1 
ATOM   12961 N N     . GLN B  1 581  ? 22.574  26.008  57.660  1.00 24.66 ? 579  GLN B N     1 
ATOM   12962 C CA    . GLN B  1 581  ? 21.394  25.814  56.813  1.00 21.74 ? 579  GLN B CA    1 
ATOM   12963 C C     . GLN B  1 581  ? 21.125  27.121  56.079  1.00 21.74 ? 579  GLN B C     1 
ATOM   12964 O O     . GLN B  1 581  ? 20.458  28.013  56.593  1.00 22.45 ? 579  GLN B O     1 
ATOM   12965 C CB    . GLN B  1 581  ? 20.195  25.396  57.651  1.00 23.31 ? 579  GLN B CB    1 
ATOM   12966 C CG    . GLN B  1 581  ? 20.369  24.055  58.336  1.00 23.68 ? 579  GLN B CG    1 
ATOM   12967 C CD    . GLN B  1 581  ? 20.471  22.894  57.366  1.00 26.31 ? 579  GLN B CD    1 
ATOM   12968 O OE1   . GLN B  1 581  ? 20.178  23.027  56.172  1.00 27.39 ? 579  GLN B OE1   1 
ATOM   12969 N NE2   . GLN B  1 581  ? 20.901  21.740  57.875  1.00 27.72 ? 579  GLN B NE2   1 
ATOM   12970 N N     . LEU B  1 582  ? 21.668  27.233  54.872  1.00 22.42 ? 580  LEU B N     1 
ATOM   12971 C CA    . LEU B  1 582  ? 21.438  28.394  54.029  1.00 23.75 ? 580  LEU B CA    1 
ATOM   12972 C C     . LEU B  1 582  ? 20.133  28.211  53.256  1.00 25.89 ? 580  LEU B C     1 
ATOM   12973 O O     . LEU B  1 582  ? 19.549  27.126  53.225  1.00 23.88 ? 580  LEU B O     1 
ATOM   12974 C CB    . LEU B  1 582  ? 22.624  28.605  53.077  1.00 22.77 ? 580  LEU B CB    1 
ATOM   12975 C CG    . LEU B  1 582  ? 23.790  29.456  53.623  1.00 31.29 ? 580  LEU B CG    1 
ATOM   12976 C CD1   . LEU B  1 582  ? 24.292  28.936  54.974  1.00 28.22 ? 580  LEU B CD1   1 
ATOM   12977 C CD2   . LEU B  1 582  ? 24.945  29.543  52.629  1.00 33.10 ? 580  LEU B CD2   1 
ATOM   12978 N N     . ALA B  1 583  ? 19.675  29.300  52.628  1.00 22.07 ? 581  ALA B N     1 
ATOM   12979 C CA    . ALA B  1 583  ? 18.449  29.233  51.835  1.00 26.70 ? 581  ALA B CA    1 
ATOM   12980 C C     . ALA B  1 583  ? 18.540  28.194  50.721  1.00 32.65 ? 581  ALA B C     1 
ATOM   12981 O O     . ALA B  1 583  ? 17.516  27.611  50.336  1.00 34.24 ? 581  ALA B O     1 
ATOM   12982 C CB    . ALA B  1 583  ? 18.131  30.607  51.245  1.00 23.16 ? 581  ALA B CB    1 
ATOM   12983 N N     . THR B  1 584  ? 19.739  27.956  50.188  1.00 24.02 ? 582  THR B N     1 
ATOM   12984 C CA    . THR B  1 584  ? 19.949  27.019  49.091  1.00 27.16 ? 582  THR B CA    1 
ATOM   12985 C C     . THR B  1 584  ? 20.244  25.601  49.557  1.00 27.79 ? 582  THR B C     1 
ATOM   12986 O O     . THR B  1 584  ? 20.417  24.713  48.721  1.00 24.72 ? 582  THR B O     1 
ATOM   12987 C CB    . THR B  1 584  ? 21.100  27.493  48.195  1.00 29.42 ? 582  THR B CB    1 
ATOM   12988 O OG1   . THR B  1 584  ? 22.279  27.670  48.997  1.00 31.61 ? 582  THR B OG1   1 
ATOM   12989 C CG2   . THR B  1 584  ? 20.737  28.810  47.528  1.00 33.13 ? 582  THR B CG2   1 
ATOM   12990 N N     . GLY B  1 585  ? 20.329  25.367  50.859  1.00 26.92 ? 583  GLY B N     1 
ATOM   12991 C CA    . GLY B  1 585  ? 20.618  24.054  51.365  1.00 23.29 ? 583  GLY B CA    1 
ATOM   12992 C C     . GLY B  1 585  ? 21.740  24.153  52.366  1.00 25.29 ? 583  GLY B C     1 
ATOM   12993 O O     . GLY B  1 585  ? 22.257  25.244  52.635  1.00 24.64 ? 583  GLY B O     1 
ATOM   12994 N N     . PRO B  1 586  ? 22.121  23.029  52.959  1.00 23.71 ? 584  PRO B N     1 
ATOM   12995 C CA    . PRO B  1 586  ? 23.183  23.056  53.967  1.00 26.16 ? 584  PRO B CA    1 
ATOM   12996 C C     . PRO B  1 586  ? 24.545  23.236  53.317  1.00 28.48 ? 584  PRO B C     1 
ATOM   12997 O O     . PRO B  1 586  ? 24.799  22.767  52.205  1.00 27.18 ? 584  PRO B O     1 
ATOM   12998 C CB    . PRO B  1 586  ? 23.067  21.683  54.636  1.00 26.25 ? 584  PRO B CB    1 
ATOM   12999 C CG    . PRO B  1 586  ? 22.514  20.811  53.552  1.00 26.68 ? 584  PRO B CG    1 
ATOM   13000 C CD    . PRO B  1 586  ? 21.582  21.677  52.759  1.00 25.70 ? 584  PRO B CD    1 
ATOM   13001 N N     . ALA B  1 587  ? 25.425  23.930  54.031  1.00 30.36 ? 585  ALA B N     1 
ATOM   13002 C CA    . ALA B  1 587  ? 26.789  24.168  53.577  1.00 30.97 ? 585  ALA B CA    1 
ATOM   13003 C C     . ALA B  1 587  ? 27.758  23.270  54.324  1.00 27.62 ? 585  ALA B C     1 
ATOM   13004 O O     . ALA B  1 587  ? 27.456  22.742  55.397  1.00 28.00 ? 585  ALA B O     1 
ATOM   13005 C CB    . ALA B  1 587  ? 27.195  25.632  53.774  1.00 33.08 ? 585  ALA B CB    1 
ATOM   13006 N N     . ALA B  1 588  ? 28.938  23.104  53.735  1.00 32.13 ? 586  ALA B N     1 
ATOM   13007 C CA    . ALA B  1 588  ? 30.001  22.346  54.365  1.00 31.45 ? 586  ALA B CA    1 
ATOM   13008 C C     . ALA B  1 588  ? 30.779  23.234  55.331  1.00 31.95 ? 586  ALA B C     1 
ATOM   13009 O O     . ALA B  1 588  ? 30.679  24.465  55.309  1.00 34.24 ? 586  ALA B O     1 
ATOM   13010 C CB    . ALA B  1 588  ? 30.935  21.743  53.313  1.00 37.20 ? 586  ALA B CB    1 
ATOM   13011 N N     . GLY B  1 589  ? 31.540  22.593  56.206  1.00 39.01 ? 587  GLY B N     1 
ATOM   13012 C CA    . GLY B  1 589  ? 32.324  23.337  57.173  1.00 35.52 ? 587  GLY B CA    1 
ATOM   13013 C C     . GLY B  1 589  ? 33.061  22.386  58.084  1.00 33.69 ? 587  GLY B C     1 
ATOM   13014 O O     . GLY B  1 589  ? 33.036  21.173  57.887  1.00 33.41 ? 587  GLY B O     1 
ATOM   13015 N N     . GLU B  1 590  ? 33.719  22.960  59.092  1.00 35.46 ? 588  GLU B N     1 
ATOM   13016 C CA    . GLU B  1 590  ? 34.408  22.167  60.097  1.00 34.89 ? 588  GLU B CA    1 
ATOM   13017 C C     . GLU B  1 590  ? 33.402  21.562  61.070  1.00 35.11 ? 588  GLU B C     1 
ATOM   13018 O O     . GLU B  1 590  ? 32.543  22.265  61.606  1.00 34.43 ? 588  GLU B O     1 
ATOM   13019 C CB    . GLU B  1 590  ? 35.420  23.026  60.858  1.00 35.66 ? 588  GLU B CB    1 
ATOM   13020 N N     . THR B  1 591  ? 33.536  20.263  61.319  1.00 36.33 ? 589  THR B N     1 
ATOM   13021 C CA    . THR B  1 591  ? 32.628  19.518  62.178  1.00 36.77 ? 589  THR B CA    1 
ATOM   13022 C C     . THR B  1 591  ? 33.296  19.176  63.505  1.00 35.59 ? 589  THR B C     1 
ATOM   13023 O O     . THR B  1 591  ? 34.468  18.783  63.535  1.00 34.90 ? 589  THR B O     1 
ATOM   13024 C CB    . THR B  1 591  ? 32.174  18.232  61.483  1.00 38.00 ? 589  THR B CB    1 
ATOM   13025 O OG1   . THR B  1 591  ? 31.619  18.563  60.203  1.00 37.74 ? 589  THR B OG1   1 
ATOM   13026 C CG2   . THR B  1 591  ? 31.107  17.516  62.321  1.00 37.20 ? 589  THR B CG2   1 
ATOM   13027 N N     . ARG B  1 592  ? 32.546  19.323  64.600  1.00 33.71 ? 590  ARG B N     1 
ATOM   13028 C CA    . ARG B  1 592  ? 33.003  18.881  65.910  1.00 33.69 ? 590  ARG B CA    1 
ATOM   13029 C C     . ARG B  1 592  ? 31.846  18.259  66.679  1.00 33.14 ? 590  ARG B C     1 
ATOM   13030 O O     . ARG B  1 592  ? 30.671  18.454  66.354  1.00 30.43 ? 590  ARG B O     1 
ATOM   13031 C CB    . ARG B  1 592  ? 33.626  20.026  66.718  1.00 40.13 ? 590  ARG B CB    1 
ATOM   13032 C CG    . ARG B  1 592  ? 32.843  21.305  66.705  1.00 39.25 ? 590  ARG B CG    1 
ATOM   13033 C CD    . ARG B  1 592  ? 33.782  22.513  66.775  1.00 46.12 ? 590  ARG B CD    1 
ATOM   13034 N NE    . ARG B  1 592  ? 34.310  22.749  68.115  1.00 47.99 ? 590  ARG B NE    1 
ATOM   13035 C CZ    . ARG B  1 592  ? 33.827  23.650  68.962  1.00 49.82 ? 590  ARG B CZ    1 
ATOM   13036 N NH1   . ARG B  1 592  ? 32.796  24.415  68.641  1.00 43.80 ? 590  ARG B NH1   1 
ATOM   13037 N NH2   . ARG B  1 592  ? 34.395  23.790  70.157  1.00 48.71 ? 590  ARG B NH2   1 
ATOM   13038 N N     . THR B  1 593  ? 32.191  17.510  67.721  1.00 32.03 ? 591  THR B N     1 
ATOM   13039 C CA    A THR B  1 593  ? 31.193  16.794  68.500  0.74 32.78 ? 591  THR B CA    1 
ATOM   13040 C CA    B THR B  1 593  ? 31.199  16.792  68.507  0.26 32.72 ? 591  THR B CA    1 
ATOM   13041 C C     . THR B  1 593  ? 30.665  17.670  69.634  1.00 31.94 ? 591  THR B C     1 
ATOM   13042 O O     . THR B  1 593  ? 31.398  18.473  70.221  1.00 32.06 ? 591  THR B O     1 
ATOM   13043 C CB    A THR B  1 593  ? 31.773  15.487  69.048  0.74 31.25 ? 591  THR B CB    1 
ATOM   13044 C CB    B THR B  1 593  ? 31.794  15.499  69.073  0.26 31.27 ? 591  THR B CB    1 
ATOM   13045 O OG1   A THR B  1 593  ? 32.833  15.776  69.967  0.74 33.99 ? 591  THR B OG1   1 
ATOM   13046 O OG1   B THR B  1 593  ? 30.903  14.941  70.046  0.26 30.05 ? 591  THR B OG1   1 
ATOM   13047 C CG2   A THR B  1 593  ? 32.321  14.639  67.908  0.74 28.66 ? 591  THR B CG2   1 
ATOM   13048 C CG2   B THR B  1 593  ? 33.147  15.766  69.713  0.26 33.19 ? 591  THR B CG2   1 
ATOM   13049 N N     . VAL B  1 594  ? 29.374  17.528  69.910  1.00 30.27 ? 592  VAL B N     1 
ATOM   13050 C CA    . VAL B  1 594  ? 28.684  18.254  70.971  1.00 26.19 ? 592  VAL B CA    1 
ATOM   13051 C C     . VAL B  1 594  ? 28.569  17.310  72.155  1.00 27.49 ? 592  VAL B C     1 
ATOM   13052 O O     . VAL B  1 594  ? 28.043  16.201  72.022  1.00 25.08 ? 592  VAL B O     1 
ATOM   13053 C CB    . VAL B  1 594  ? 27.300  18.734  70.506  1.00 29.88 ? 592  VAL B CB    1 
ATOM   13054 C CG1   . VAL B  1 594  ? 26.541  19.446  71.650  1.00 20.19 ? 592  VAL B CG1   1 
ATOM   13055 C CG2   . VAL B  1 594  ? 27.433  19.620  69.266  1.00 29.10 ? 592  VAL B CG2   1 
ATOM   13056 N N     . LEU B  1 595  ? 29.069  17.733  73.309  1.00 28.75 ? 593  LEU B N     1 
ATOM   13057 C CA    . LEU B  1 595  ? 29.182  16.859  74.464  1.00 28.94 ? 593  LEU B CA    1 
ATOM   13058 C C     . LEU B  1 595  ? 28.205  17.270  75.556  1.00 25.70 ? 593  LEU B C     1 
ATOM   13059 O O     . LEU B  1 595  ? 27.800  18.428  75.654  1.00 28.10 ? 593  LEU B O     1 
ATOM   13060 C CB    . LEU B  1 595  ? 30.618  16.870  75.022  1.00 24.30 ? 593  LEU B CB    1 
ATOM   13061 C CG    . LEU B  1 595  ? 31.703  16.401  74.042  1.00 28.67 ? 593  LEU B CG    1 
ATOM   13062 C CD1   . LEU B  1 595  ? 33.076  16.503  74.697  1.00 33.00 ? 593  LEU B CD1   1 
ATOM   13063 C CD2   . LEU B  1 595  ? 31.449  14.981  73.539  1.00 31.68 ? 593  LEU B CD2   1 
ATOM   13064 N N     . ASN B  1 596  ? 27.833  16.298  76.369  1.00 25.74 ? 594  ASN B N     1 
ATOM   13065 C CA    . ASN B  1 596  ? 27.011  16.545  77.547  1.00 24.60 ? 594  ASN B CA    1 
ATOM   13066 C C     . ASN B  1 596  ? 27.864  17.224  78.609  1.00 25.26 ? 594  ASN B C     1 
ATOM   13067 O O     . ASN B  1 596  ? 28.847  16.625  79.060  1.00 22.94 ? 594  ASN B O     1 
ATOM   13068 C CB    . ASN B  1 596  ? 26.470  15.211  78.057  1.00 23.54 ? 594  ASN B CB    1 
ATOM   13069 C CG    . ASN B  1 596  ? 25.444  15.360  79.154  1.00 26.23 ? 594  ASN B CG    1 
ATOM   13070 O OD1   . ASN B  1 596  ? 25.427  16.348  79.891  1.00 23.48 ? 594  ASN B OD1   1 
ATOM   13071 N ND2   . ASN B  1 596  ? 24.567  14.360  79.267  1.00 24.02 ? 594  ASN B ND2   1 
ATOM   13072 N N     . PRO B  1 597  ? 27.550  18.458  79.029  1.00 24.74 ? 595  PRO B N     1 
ATOM   13073 C CA    . PRO B  1 597  ? 28.381  19.096  80.065  1.00 25.47 ? 595  PRO B CA    1 
ATOM   13074 C C     . PRO B  1 597  ? 28.380  18.346  81.388  1.00 25.83 ? 595  PRO B C     1 
ATOM   13075 O O     . PRO B  1 597  ? 29.315  18.521  82.180  1.00 26.75 ? 595  PRO B O     1 
ATOM   13076 C CB    . PRO B  1 597  ? 27.772  20.504  80.208  1.00 20.90 ? 595  PRO B CB    1 
ATOM   13077 C CG    . PRO B  1 597  ? 26.391  20.410  79.587  1.00 27.59 ? 595  PRO B CG    1 
ATOM   13078 C CD    . PRO B  1 597  ? 26.491  19.350  78.529  1.00 24.59 ? 595  PRO B CD    1 
ATOM   13079 N N     . GLY B  1 598  ? 27.373  17.511  81.655  1.00 26.07 ? 596  GLY B N     1 
ATOM   13080 C CA    . GLY B  1 598  ? 27.395  16.691  82.854  1.00 26.60 ? 596  GLY B CA    1 
ATOM   13081 C C     . GLY B  1 598  ? 28.247  15.444  82.759  1.00 28.32 ? 596  GLY B C     1 
ATOM   13082 O O     . GLY B  1 598  ? 28.477  14.777  83.777  1.00 28.24 ? 596  GLY B O     1 
ATOM   13083 N N     . ASP B  1 599  ? 28.745  15.130  81.565  1.00 25.03 ? 597  ASP B N     1 
ATOM   13084 C CA    . ASP B  1 599  ? 29.489  13.901  81.337  1.00 27.86 ? 597  ASP B CA    1 
ATOM   13085 C C     . ASP B  1 599  ? 30.056  13.961  79.927  1.00 28.90 ? 597  ASP B C     1 
ATOM   13086 O O     . ASP B  1 599  ? 29.333  13.715  78.960  1.00 29.38 ? 597  ASP B O     1 
ATOM   13087 C CB    . ASP B  1 599  ? 28.568  12.693  81.536  1.00 28.64 ? 597  ASP B CB    1 
ATOM   13088 C CG    . ASP B  1 599  ? 29.307  11.358  81.513  1.00 36.00 ? 597  ASP B CG    1 
ATOM   13089 O OD1   . ASP B  1 599  ? 30.459  11.286  81.020  1.00 33.08 ? 597  ASP B OD1   1 
ATOM   13090 O OD2   . ASP B  1 599  ? 28.703  10.366  81.981  1.00 30.20 ? 597  ASP B OD2   1 
ATOM   13091 N N     . HIS B  1 600  ? 31.337  14.305  79.796  1.00 27.40 ? 598  HIS B N     1 
ATOM   13092 C CA    . HIS B  1 600  ? 31.914  14.498  78.474  1.00 28.92 ? 598  HIS B CA    1 
ATOM   13093 C C     . HIS B  1 600  ? 32.075  13.194  77.708  1.00 26.87 ? 598  HIS B C     1 
ATOM   13094 O O     . HIS B  1 600  ? 32.397  13.235  76.517  1.00 29.23 ? 598  HIS B O     1 
ATOM   13095 C CB    . HIS B  1 600  ? 33.252  15.242  78.591  1.00 30.00 ? 598  HIS B CB    1 
ATOM   13096 C CG    . HIS B  1 600  ? 33.095  16.700  78.907  1.00 29.24 ? 598  HIS B CG    1 
ATOM   13097 N ND1   . HIS B  1 600  ? 34.162  17.571  78.974  1.00 31.34 ? 598  HIS B ND1   1 
ATOM   13098 C CD2   . HIS B  1 600  ? 31.991  17.438  79.174  1.00 26.17 ? 598  HIS B CD2   1 
ATOM   13099 C CE1   . HIS B  1 600  ? 33.721  18.782  79.272  1.00 30.21 ? 598  HIS B CE1   1 
ATOM   13100 N NE2   . HIS B  1 600  ? 32.408  18.727  79.400  1.00 29.45 ? 598  HIS B NE2   1 
ATOM   13101 N N     . ARG B  1 601  ? 31.840  12.049  78.349  1.00 27.58 ? 599  ARG B N     1 
ATOM   13102 C CA    . ARG B  1 601  ? 31.806  10.777  77.644  1.00 27.97 ? 599  ARG B CA    1 
ATOM   13103 C C     . ARG B  1 601  ? 30.510  10.590  76.871  1.00 29.93 ? 599  ARG B C     1 
ATOM   13104 O O     . ARG B  1 601  ? 30.445  9.718   76.000  1.00 30.41 ? 599  ARG B O     1 
ATOM   13105 C CB    . ARG B  1 601  ? 31.967  9.620   78.624  1.00 35.95 ? 599  ARG B CB    1 
ATOM   13106 C CG    . ARG B  1 601  ? 33.175  9.744   79.534  1.00 32.63 ? 599  ARG B CG    1 
ATOM   13107 C CD    . ARG B  1 601  ? 33.093  8.716   80.648  1.00 39.61 ? 599  ARG B CD    1 
ATOM   13108 N NE    . ARG B  1 601  ? 31.882  8.890   81.444  1.00 38.36 ? 599  ARG B NE    1 
ATOM   13109 C CZ    . ARG B  1 601  ? 31.529  8.109   82.456  1.00 42.53 ? 599  ARG B CZ    1 
ATOM   13110 N NH1   . ARG B  1 601  ? 32.275  7.081   82.829  1.00 37.37 ? 599  ARG B NH1   1 
ATOM   13111 N NH2   . ARG B  1 601  ? 30.397  8.364   83.107  1.00 40.95 ? 599  ARG B NH2   1 
ATOM   13112 N N     . ASP B  1 602  ? 29.476  11.355  77.211  1.00 28.00 ? 600  ASP B N     1 
ATOM   13113 C CA    . ASP B  1 602  ? 28.152  11.249  76.596  1.00 28.68 ? 600  ASP B CA    1 
ATOM   13114 C C     . ASP B  1 602  ? 28.130  12.194  75.406  1.00 29.73 ? 600  ASP B C     1 
ATOM   13115 O O     . ASP B  1 602  ? 28.013  13.414  75.562  1.00 29.65 ? 600  ASP B O     1 
ATOM   13116 C CB    . ASP B  1 602  ? 27.060  11.585  77.608  1.00 31.32 ? 600  ASP B CB    1 
ATOM   13117 C CG    . ASP B  1 602  ? 25.663  11.537  77.003  1.00 30.26 ? 600  ASP B CG    1 
ATOM   13118 O OD1   . ASP B  1 602  ? 25.466  10.748  76.065  1.00 32.63 ? 600  ASP B OD1   1 
ATOM   13119 O OD2   . ASP B  1 602  ? 24.774  12.286  77.464  1.00 32.84 ? 600  ASP B OD2   1 
ATOM   13120 N N     . VAL B  1 603  ? 28.250  11.628  74.212  1.00 30.06 ? 601  VAL B N     1 
ATOM   13121 C CA    . VAL B  1 603  ? 28.254  12.402  72.984  1.00 30.41 ? 601  VAL B CA    1 
ATOM   13122 C C     . VAL B  1 603  ? 26.808  12.620  72.562  1.00 30.03 ? 601  VAL B C     1 
ATOM   13123 O O     . VAL B  1 603  ? 26.021  11.672  72.482  1.00 29.34 ? 601  VAL B O     1 
ATOM   13124 C CB    . VAL B  1 603  ? 29.066  11.689  71.890  1.00 31.89 ? 601  VAL B CB    1 
ATOM   13125 C CG1   . VAL B  1 603  ? 28.920  12.409  70.572  1.00 30.71 ? 601  VAL B CG1   1 
ATOM   13126 C CG2   . VAL B  1 603  ? 30.533  11.602  72.304  1.00 32.97 ? 601  VAL B CG2   1 
ATOM   13127 N N     . VAL B  1 604  ? 26.446  13.875  72.344  1.00 25.29 ? 602  VAL B N     1 
ATOM   13128 C CA    . VAL B  1 604  ? 25.062  14.242  72.088  1.00 26.68 ? 602  VAL B CA    1 
ATOM   13129 C C     . VAL B  1 604  ? 24.786  14.346  70.602  1.00 25.12 ? 602  VAL B C     1 
ATOM   13130 O O     . VAL B  1 604  ? 23.706  13.965  70.143  1.00 25.10 ? 602  VAL B O     1 
ATOM   13131 C CB    . VAL B  1 604  ? 24.714  15.562  72.802  1.00 25.75 ? 602  VAL B CB    1 
ATOM   13132 C CG1   . VAL B  1 604  ? 23.231  15.888  72.618  1.00 24.32 ? 602  VAL B CG1   1 
ATOM   13133 C CG2   . VAL B  1 604  ? 25.050  15.453  74.272  1.00 26.03 ? 602  VAL B CG2   1 
ATOM   13134 N N     . GLY B  1 605  ? 25.760  14.850  69.856  1.00 23.26 ? 603  GLY B N     1 
ATOM   13135 C CA    . GLY B  1 605  ? 25.581  15.022  68.426  1.00 27.01 ? 603  GLY B CA    1 
ATOM   13136 C C     . GLY B  1 605  ? 26.806  15.681  67.838  1.00 29.83 ? 603  GLY B C     1 
ATOM   13137 O O     . GLY B  1 605  ? 27.878  15.677  68.445  1.00 28.33 ? 603  GLY B O     1 
ATOM   13138 N N     . SER B  1 606  ? 26.652  16.246  66.649  1.00 23.35 ? 604  SER B N     1 
ATOM   13139 C CA    . SER B  1 606  ? 27.769  16.926  66.016  1.00 28.48 ? 604  SER B CA    1 
ATOM   13140 C C     . SER B  1 606  ? 27.284  18.195  65.334  1.00 28.58 ? 604  SER B C     1 
ATOM   13141 O O     . SER B  1 606  ? 26.143  18.283  64.868  1.00 27.45 ? 604  SER B O     1 
ATOM   13142 C CB    . SER B  1 606  ? 28.491  16.020  65.012  1.00 33.80 ? 604  SER B CB    1 
ATOM   13143 O OG    . SER B  1 606  ? 27.755  15.886  63.823  1.00 39.12 ? 604  SER B OG    1 
ATOM   13144 N N     . VAL B  1 607  ? 28.161  19.187  65.296  1.00 25.78 ? 605  VAL B N     1 
ATOM   13145 C CA    . VAL B  1 607  ? 27.851  20.470  64.687  1.00 24.68 ? 605  VAL B CA    1 
ATOM   13146 C C     . VAL B  1 607  ? 28.855  20.745  63.576  1.00 30.88 ? 605  VAL B C     1 
ATOM   13147 O O     . VAL B  1 607  ? 30.054  20.486  63.718  1.00 27.76 ? 605  VAL B O     1 
ATOM   13148 C CB    . VAL B  1 607  ? 27.851  21.614  65.721  1.00 27.11 ? 605  VAL B CB    1 
ATOM   13149 C CG1   . VAL B  1 607  ? 29.181  21.670  66.495  1.00 27.57 ? 605  VAL B CG1   1 
ATOM   13150 C CG2   . VAL B  1 607  ? 27.556  22.950  65.031  1.00 26.84 ? 605  VAL B CG2   1 
ATOM   13151 N N     . THR B  1 608  ? 28.352  21.248  62.460  1.00 28.31 ? 606  THR B N     1 
ATOM   13152 C CA    . THR B  1 608  ? 29.181  21.763  61.384  1.00 25.76 ? 606  THR B CA    1 
ATOM   13153 C C     . THR B  1 608  ? 29.076  23.281  61.421  1.00 25.59 ? 606  THR B C     1 
ATOM   13154 O O     . THR B  1 608  ? 27.975  23.836  61.355  1.00 25.36 ? 606  THR B O     1 
ATOM   13155 C CB    . THR B  1 608  ? 28.733  21.197  60.038  1.00 26.74 ? 606  THR B CB    1 
ATOM   13156 O OG1   . THR B  1 608  ? 28.891  19.775  60.063  1.00 27.69 ? 606  THR B OG1   1 
ATOM   13157 C CG2   . THR B  1 608  ? 29.575  21.766  58.907  1.00 24.42 ? 606  THR B CG2   1 
ATOM   13158 N N     . GLU B  1 609  ? 30.211  23.950  61.571  1.00 26.51 ? 607  GLU B N     1 
ATOM   13159 C CA    . GLU B  1 609  ? 30.196  25.378  61.813  1.00 28.12 ? 607  GLU B CA    1 
ATOM   13160 C C     . GLU B  1 609  ? 30.380  26.146  60.511  1.00 28.26 ? 607  GLU B C     1 
ATOM   13161 O O     . GLU B  1 609  ? 30.862  25.614  59.506  1.00 27.07 ? 607  GLU B O     1 
ATOM   13162 C CB    . GLU B  1 609  ? 31.239  25.749  62.873  1.00 30.71 ? 607  GLU B CB    1 
ATOM   13163 C CG    . GLU B  1 609  ? 30.733  25.311  64.245  1.00 28.83 ? 607  GLU B CG    1 
ATOM   13164 C CD    . GLU B  1 609  ? 31.711  25.505  65.402  1.00 37.70 ? 607  GLU B CD    1 
ATOM   13165 O OE1   . GLU B  1 609  ? 32.929  25.687  65.168  1.00 35.09 ? 607  GLU B OE1   1 
ATOM   13166 O OE2   . GLU B  1 609  ? 31.237  25.463  66.564  1.00 33.65 ? 607  GLU B OE2   1 
ATOM   13167 N N     . THR B  1 610  ? 29.933  27.398  60.535  1.00 27.79 ? 608  THR B N     1 
ATOM   13168 C CA    . THR B  1 610  ? 29.783  28.214  59.336  1.00 28.42 ? 608  THR B CA    1 
ATOM   13169 C C     . THR B  1 610  ? 31.089  28.932  59.023  1.00 29.75 ? 608  THR B C     1 
ATOM   13170 O O     . THR B  1 610  ? 31.726  29.495  59.920  1.00 30.70 ? 608  THR B O     1 
ATOM   13171 C CB    . THR B  1 610  ? 28.670  29.247  59.522  1.00 26.98 ? 608  THR B CB    1 
ATOM   13172 O OG1   . THR B  1 610  ? 27.531  28.627  60.126  1.00 26.17 ? 608  THR B OG1   1 
ATOM   13173 C CG2   . THR B  1 610  ? 28.262  29.867  58.188  1.00 28.66 ? 608  THR B CG2   1 
ATOM   13174 N N     . SER B  1 611  ? 31.479  28.925  57.753  1.00 29.24 ? 609  SER B N     1 
ATOM   13175 C CA    . SER B  1 611  ? 32.578  29.783  57.338  1.00 34.48 ? 609  SER B CA    1 
ATOM   13176 C C     . SER B  1 611  ? 32.098  31.228  57.280  1.00 35.70 ? 609  SER B C     1 
ATOM   13177 O O     . SER B  1 611  ? 30.908  31.505  57.095  1.00 30.97 ? 609  SER B O     1 
ATOM   13178 C CB    . SER B  1 611  ? 33.130  29.350  55.980  1.00 34.48 ? 609  SER B CB    1 
ATOM   13179 O OG    . SER B  1 611  ? 32.232  29.685  54.939  1.00 35.90 ? 609  SER B OG    1 
ATOM   13180 N N     . GLU B  1 612  ? 33.036  32.160  57.463  1.00 34.13 ? 610  GLU B N     1 
ATOM   13181 C CA    . GLU B  1 612  ? 32.671  33.570  57.411  1.00 36.88 ? 610  GLU B CA    1 
ATOM   13182 C C     . GLU B  1 612  ? 32.151  33.956  56.029  1.00 35.01 ? 610  GLU B C     1 
ATOM   13183 O O     . GLU B  1 612  ? 31.245  34.788  55.911  1.00 36.38 ? 610  GLU B O     1 
ATOM   13184 C CB    . GLU B  1 612  ? 33.865  34.433  57.817  1.00 37.20 ? 610  GLU B CB    1 
ATOM   13185 C CG    . GLU B  1 612  ? 34.154  34.368  59.314  1.00 39.91 ? 610  GLU B CG    1 
ATOM   13186 C CD    . GLU B  1 612  ? 35.473  35.024  59.698  1.00 45.73 ? 610  GLU B CD    1 
ATOM   13187 O OE1   . GLU B  1 612  ? 35.716  36.181  59.286  1.00 49.23 ? 610  GLU B OE1   1 
ATOM   13188 O OE2   . GLU B  1 612  ? 36.266  34.374  60.411  1.00 47.01 ? 610  GLU B OE2   1 
ATOM   13189 N N     . GLU B  1 613  ? 32.703  33.354  54.972  1.00 32.58 ? 611  GLU B N     1 
ATOM   13190 C CA    . GLU B  1 613  ? 32.190  33.617  53.633  1.00 33.08 ? 611  GLU B CA    1 
ATOM   13191 C C     . GLU B  1 613  ? 30.750  33.132  53.494  1.00 33.84 ? 611  GLU B C     1 
ATOM   13192 O O     . GLU B  1 613  ? 29.929  33.793  52.849  1.00 31.86 ? 611  GLU B O     1 
ATOM   13193 C CB    . GLU B  1 613  ? 33.086  32.961  52.584  1.00 34.75 ? 611  GLU B CB    1 
ATOM   13194 N N     . ASP B  1 614  ? 30.428  31.976  54.086  1.00 32.71 ? 612  ASP B N     1 
ATOM   13195 C CA    . ASP B  1 614  ? 29.049  31.489  54.055  1.00 34.13 ? 612  ASP B CA    1 
ATOM   13196 C C     . ASP B  1 614  ? 28.139  32.346  54.922  1.00 29.46 ? 612  ASP B C     1 
ATOM   13197 O O     . ASP B  1 614  ? 26.962  32.529  54.595  1.00 28.69 ? 612  ASP B O     1 
ATOM   13198 C CB    . ASP B  1 614  ? 28.981  30.027  54.500  1.00 30.77 ? 612  ASP B CB    1 
ATOM   13199 C CG    . ASP B  1 614  ? 29.381  29.065  53.399  1.00 34.39 ? 612  ASP B CG    1 
ATOM   13200 O OD1   . ASP B  1 614  ? 29.209  29.415  52.215  1.00 39.79 ? 612  ASP B OD1   1 
ATOM   13201 O OD2   . ASP B  1 614  ? 29.863  27.959  53.712  1.00 39.97 ? 612  ASP B OD2   1 
ATOM   13202 N N     . ALA B  1 615  ? 28.661  32.874  56.031  1.00 29.55 ? 613  ALA B N     1 
ATOM   13203 C CA    . ALA B  1 615  ? 27.890  33.824  56.822  1.00 27.98 ? 613  ALA B CA    1 
ATOM   13204 C C     . ALA B  1 615  ? 27.486  35.019  55.976  1.00 29.28 ? 613  ALA B C     1 
ATOM   13205 O O     . ALA B  1 615  ? 26.319  35.419  55.960  1.00 25.52 ? 613  ALA B O     1 
ATOM   13206 C CB    . ALA B  1 615  ? 28.699  34.277  58.037  1.00 31.14 ? 613  ALA B CB    1 
ATOM   13207 N N     . ARG B  1 616  ? 28.440  35.584  55.230  1.00 31.45 ? 614  ARG B N     1 
ATOM   13208 C CA    . ARG B  1 616  ? 28.113  36.711  54.362  1.00 27.65 ? 614  ARG B CA    1 
ATOM   13209 C C     . ARG B  1 616  ? 27.142  36.300  53.268  1.00 29.44 ? 614  ARG B C     1 
ATOM   13210 O O     . ARG B  1 616  ? 26.224  37.060  52.939  1.00 32.35 ? 614  ARG B O     1 
ATOM   13211 C CB    . ARG B  1 616  ? 29.382  37.311  53.759  1.00 36.95 ? 614  ARG B CB    1 
ATOM   13212 C CG    . ARG B  1 616  ? 30.158  38.195  54.738  1.00 38.36 ? 614  ARG B CG    1 
ATOM   13213 C CD    . ARG B  1 616  ? 31.305  38.915  54.048  1.00 41.32 ? 614  ARG B CD    1 
ATOM   13214 N NE    . ARG B  1 616  ? 32.426  38.019  53.804  1.00 45.01 ? 614  ARG B NE    1 
ATOM   13215 C CZ    . ARG B  1 616  ? 33.259  37.610  54.750  1.00 45.93 ? 614  ARG B CZ    1 
ATOM   13216 N NH1   . ARG B  1 616  ? 33.116  37.997  56.010  1.00 42.20 ? 614  ARG B NH1   1 
ATOM   13217 N NH2   . ARG B  1 616  ? 34.251  36.783  54.429  1.00 44.19 ? 614  ARG B NH2   1 
ATOM   13218 N N     . ARG B  1 617  ? 27.313  35.099  52.709  1.00 29.55 ? 615  ARG B N     1 
ATOM   13219 C CA    . ARG B  1 617  ? 26.417  34.658  51.644  1.00 31.50 ? 615  ARG B CA    1 
ATOM   13220 C C     . ARG B  1 617  ? 24.991  34.496  52.159  1.00 28.50 ? 615  ARG B C     1 
ATOM   13221 O O     . ARG B  1 617  ? 24.031  34.851  51.467  1.00 26.41 ? 615  ARG B O     1 
ATOM   13222 C CB    . ARG B  1 617  ? 26.928  33.358  51.015  1.00 30.73 ? 615  ARG B CB    1 
ATOM   13223 C CG    . ARG B  1 617  ? 25.937  32.714  50.045  1.00 34.38 ? 615  ARG B CG    1 
ATOM   13224 C CD    . ARG B  1 617  ? 26.607  31.769  49.052  1.00 41.08 ? 615  ARG B CD    1 
ATOM   13225 N NE    . ARG B  1 617  ? 27.098  30.536  49.661  1.00 49.79 ? 615  ARG B NE    1 
ATOM   13226 C CZ    . ARG B  1 617  ? 26.473  29.365  49.598  1.00 52.90 ? 615  ARG B CZ    1 
ATOM   13227 N NH1   . ARG B  1 617  ? 25.301  29.236  48.991  1.00 50.79 ? 615  ARG B NH1   1 
ATOM   13228 N NH2   . ARG B  1 617  ? 27.037  28.296  50.157  1.00 46.32 ? 615  ARG B NH2   1 
ATOM   13229 N N     . ALA B  1 618  ? 24.831  33.994  53.385  1.00 25.00 ? 616  ALA B N     1 
ATOM   13230 C CA    . ALA B  1 618  ? 23.498  33.877  53.969  1.00 26.86 ? 616  ALA B CA    1 
ATOM   13231 C C     . ALA B  1 618  ? 22.820  35.237  54.074  1.00 23.12 ? 616  ALA B C     1 
ATOM   13232 O O     . ALA B  1 618  ? 21.627  35.363  53.790  1.00 26.34 ? 616  ALA B O     1 
ATOM   13233 C CB    . ALA B  1 618  ? 23.581  33.217  55.348  1.00 24.65 ? 616  ALA B CB    1 
ATOM   13234 N N     . VAL B  1 619  ? 23.565  36.270  54.480  1.00 25.43 ? 617  VAL B N     1 
ATOM   13235 C CA    . VAL B  1 619  ? 22.970  37.601  54.581  1.00 24.37 ? 617  VAL B CA    1 
ATOM   13236 C C     . VAL B  1 619  ? 22.514  38.082  53.208  1.00 28.80 ? 617  VAL B C     1 
ATOM   13237 O O     . VAL B  1 619  ? 21.443  38.683  53.075  1.00 28.17 ? 617  VAL B O     1 
ATOM   13238 C CB    . VAL B  1 619  ? 23.949  38.593  55.236  1.00 24.83 ? 617  VAL B CB    1 
ATOM   13239 C CG1   . VAL B  1 619  ? 23.309  39.957  55.361  1.00 24.44 ? 617  VAL B CG1   1 
ATOM   13240 C CG2   . VAL B  1 619  ? 24.338  38.109  56.628  1.00 25.62 ? 617  VAL B CG2   1 
ATOM   13241 N N     . ARG B  1 620  ? 23.302  37.810  52.162  1.00 27.33 ? 618  ARG B N     1 
ATOM   13242 C CA    . ARG B  1 620  ? 22.878  38.225  50.826  1.00 31.00 ? 618  ARG B CA    1 
ATOM   13243 C C     . ARG B  1 620  ? 21.649  37.448  50.367  1.00 26.51 ? 618  ARG B C     1 
ATOM   13244 O O     . ARG B  1 620  ? 20.770  38.006  49.703  1.00 26.82 ? 618  ARG B O     1 
ATOM   13245 C CB    . ARG B  1 620  ? 24.026  38.066  49.829  1.00 31.20 ? 618  ARG B CB    1 
ATOM   13246 C CG    . ARG B  1 620  ? 25.223  38.948  50.141  1.00 34.22 ? 618  ARG B CG    1 
ATOM   13247 C CD    . ARG B  1 620  ? 26.173  39.052  48.938  1.00 39.80 ? 618  ARG B CD    1 
ATOM   13248 N NE    . ARG B  1 620  ? 26.579  37.733  48.467  1.00 40.47 ? 618  ARG B NE    1 
ATOM   13249 C CZ    . ARG B  1 620  ? 27.629  37.063  48.918  1.00 39.95 ? 618  ARG B CZ    1 
ATOM   13250 N NH1   . ARG B  1 620  ? 28.455  37.587  49.811  1.00 37.55 ? 618  ARG B NH1   1 
ATOM   13251 N NH2   . ARG B  1 620  ? 27.857  35.833  48.462  1.00 45.31 ? 618  ARG B NH2   1 
ATOM   13252 N N     . LEU B  1 621  ? 21.582  36.153  50.692  1.00 24.51 ? 619  LEU B N     1 
ATOM   13253 C CA    . LEU B  1 621  ? 20.389  35.361  50.398  1.00 27.14 ? 619  LEU B CA    1 
ATOM   13254 C C     . LEU B  1 621  ? 19.171  35.861  51.180  1.00 28.68 ? 619  LEU B C     1 
ATOM   13255 O O     . LEU B  1 621  ? 18.049  35.888  50.653  1.00 26.52 ? 619  LEU B O     1 
ATOM   13256 C CB    . LEU B  1 621  ? 20.666  33.887  50.707  1.00 26.09 ? 619  LEU B CB    1 
ATOM   13257 C CG    . LEU B  1 621  ? 21.662  33.117  49.832  1.00 28.39 ? 619  LEU B CG    1 
ATOM   13258 C CD1   . LEU B  1 621  ? 22.006  31.778  50.464  1.00 28.83 ? 619  LEU B CD1   1 
ATOM   13259 C CD2   . LEU B  1 621  ? 21.107  32.919  48.417  1.00 31.84 ? 619  LEU B CD2   1 
ATOM   13260 N N     . ALA B  1 622  ? 19.367  36.267  52.438  1.00 24.35 ? 620  ALA B N     1 
ATOM   13261 C CA    . ALA B  1 622  ? 18.264  36.847  53.195  1.00 28.83 ? 620  ALA B CA    1 
ATOM   13262 C C     . ALA B  1 622  ? 17.804  38.155  52.560  1.00 26.16 ? 620  ALA B C     1 
ATOM   13263 O O     . ALA B  1 622  ? 16.597  38.424  52.473  1.00 23.61 ? 620  ALA B O     1 
ATOM   13264 C CB    . ALA B  1 622  ? 18.670  37.061  54.665  1.00 23.18 ? 620  ALA B CB    1 
ATOM   13265 N N     . ALA B  1 623  ? 18.754  38.965  52.076  1.00 25.62 ? 621  ALA B N     1 
ATOM   13266 C CA    . ALA B  1 623  ? 18.381  40.238  51.466  1.00 29.29 ? 621  ALA B CA    1 
ATOM   13267 C C     . ALA B  1 623  ? 17.590  40.016  50.184  1.00 28.01 ? 621  ALA B C     1 
ATOM   13268 O O     . ALA B  1 623  ? 16.594  40.709  49.929  1.00 27.38 ? 621  ALA B O     1 
ATOM   13269 C CB    . ALA B  1 623  ? 19.626  41.078  51.188  1.00 25.75 ? 621  ALA B CB    1 
ATOM   13270 N N     . ASP B  1 624  ? 18.010  39.045  49.375  1.00 25.47 ? 622  ASP B N     1 
ATOM   13271 C CA    . ASP B  1 624  ? 17.297  38.767  48.130  1.00 26.90 ? 622  ASP B CA    1 
ATOM   13272 C C     . ASP B  1 624  ? 15.874  38.294  48.388  1.00 30.13 ? 622  ASP B C     1 
ATOM   13273 O O     . ASP B  1 624  ? 14.967  38.603  47.610  1.00 32.53 ? 622  ASP B O     1 
ATOM   13274 C CB    . ASP B  1 624  ? 18.063  37.728  47.311  1.00 32.29 ? 622  ASP B CB    1 
ATOM   13275 N N     . ALA B  1 625  ? 15.652  37.558  49.467  1.00 29.44 ? 623  ALA B N     1 
ATOM   13276 C CA    . ALA B  1 625  ? 14.328  37.039  49.762  1.00 30.17 ? 623  ALA B CA    1 
ATOM   13277 C C     . ALA B  1 625  ? 13.516  37.941  50.680  1.00 29.43 ? 623  ALA B C     1 
ATOM   13278 O O     . ALA B  1 625  ? 12.344  37.643  50.932  1.00 26.77 ? 623  ALA B O     1 
ATOM   13279 C CB    . ALA B  1 625  ? 14.444  35.653  50.388  1.00 35.80 ? 623  ALA B CB    1 
ATOM   13280 N N     . ALA B  1 626  ? 14.100  39.030  51.179  1.00 27.20 ? 624  ALA B N     1 
ATOM   13281 C CA    . ALA B  1 626  ? 13.382  39.899  52.113  1.00 26.28 ? 624  ALA B CA    1 
ATOM   13282 C C     . ALA B  1 626  ? 12.051  40.413  51.573  1.00 27.63 ? 624  ALA B C     1 
ATOM   13283 O O     . ALA B  1 626  ? 11.057  40.369  52.317  1.00 29.12 ? 624  ALA B O     1 
ATOM   13284 C CB    . ALA B  1 626  ? 14.290  41.059  52.540  1.00 25.22 ? 624  ALA B CB    1 
ATOM   13285 N N     . PRO B  1 627  ? 11.951  40.926  50.340  1.00 27.75 ? 625  PRO B N     1 
ATOM   13286 C CA    . PRO B  1 627  ? 10.644  41.419  49.877  1.00 27.33 ? 625  PRO B CA    1 
ATOM   13287 C C     . PRO B  1 627  ? 9.563   40.350  49.835  1.00 25.67 ? 625  PRO B C     1 
ATOM   13288 O O     . PRO B  1 627  ? 8.406   40.634  50.176  1.00 30.53 ? 625  PRO B O     1 
ATOM   13289 C CB    . PRO B  1 627  ? 10.962  41.971  48.476  1.00 29.33 ? 625  PRO B CB    1 
ATOM   13290 C CG    . PRO B  1 627  ? 12.433  42.297  48.521  1.00 30.79 ? 625  PRO B CG    1 
ATOM   13291 C CD    . PRO B  1 627  ? 13.025  41.221  49.367  1.00 30.06 ? 625  PRO B CD    1 
ATOM   13292 N N     . ASP B  1 628  ? 9.902   39.126  49.423  1.00 25.35 ? 626  ASP B N     1 
ATOM   13293 C CA    . ASP B  1 628  ? 8.906   38.059  49.368  1.00 27.70 ? 626  ASP B CA    1 
ATOM   13294 C C     . ASP B  1 628  ? 8.323   37.777  50.746  1.00 29.12 ? 626  ASP B C     1 
ATOM   13295 O O     . ASP B  1 628  ? 7.112   37.584  50.890  1.00 24.33 ? 626  ASP B O     1 
ATOM   13296 C CB    . ASP B  1 628  ? 9.518   36.778  48.792  1.00 28.66 ? 626  ASP B CB    1 
ATOM   13297 C CG    . ASP B  1 628  ? 9.870   36.893  47.310  1.00 36.01 ? 626  ASP B CG    1 
ATOM   13298 O OD1   . ASP B  1 628  ? 9.133   37.550  46.548  1.00 39.00 ? 626  ASP B OD1   1 
ATOM   13299 O OD2   . ASP B  1 628  ? 10.899  36.320  46.913  1.00 41.71 ? 626  ASP B OD2   1 
ATOM   13300 N N     . TRP B  1 629  ? 9.170   37.737  51.774  1.00 24.35 ? 627  TRP B N     1 
ATOM   13301 C CA    . TRP B  1 629  ? 8.675   37.423  53.108  1.00 23.24 ? 627  TRP B CA    1 
ATOM   13302 C C     . TRP B  1 629  ? 7.882   38.594  53.692  1.00 21.94 ? 627  TRP B C     1 
ATOM   13303 O O     . TRP B  1 629  ? 6.849   38.397  54.346  1.00 22.38 ? 627  TRP B O     1 
ATOM   13304 C CB    . TRP B  1 629  ? 9.853   37.026  54.011  1.00 20.26 ? 627  TRP B CB    1 
ATOM   13305 C CG    . TRP B  1 629  ? 9.423   36.716  55.406  1.00 23.48 ? 627  TRP B CG    1 
ATOM   13306 C CD1   . TRP B  1 629  ? 9.776   37.386  56.541  1.00 20.33 ? 627  TRP B CD1   1 
ATOM   13307 C CD2   . TRP B  1 629  ? 8.520   35.678  55.813  1.00 25.37 ? 627  TRP B CD2   1 
ATOM   13308 N NE1   . TRP B  1 629  ? 9.147   36.828  57.631  1.00 21.23 ? 627  TRP B NE1   1 
ATOM   13309 C CE2   . TRP B  1 629  ? 8.370   35.781  57.213  1.00 21.47 ? 627  TRP B CE2   1 
ATOM   13310 C CE3   . TRP B  1 629  ? 7.827   34.671  55.133  1.00 24.20 ? 627  TRP B CE3   1 
ATOM   13311 C CZ2   . TRP B  1 629  ? 7.557   34.912  57.946  1.00 20.16 ? 627  TRP B CZ2   1 
ATOM   13312 C CZ3   . TRP B  1 629  ? 7.013   33.809  55.864  1.00 22.30 ? 627  TRP B CZ3   1 
ATOM   13313 C CH2   . TRP B  1 629  ? 6.889   33.938  57.256  1.00 24.43 ? 627  TRP B CH2   1 
ATOM   13314 N N     . ALA B  1 630  ? 8.344   39.822  53.454  1.00 23.87 ? 628  ALA B N     1 
ATOM   13315 C CA    . ALA B  1 630  ? 7.587   40.988  53.883  1.00 24.54 ? 628  ALA B CA    1 
ATOM   13316 C C     . ALA B  1 630  ? 6.191   41.003  53.271  1.00 26.45 ? 628  ALA B C     1 
ATOM   13317 O O     . ALA B  1 630  ? 5.253   41.519  53.883  1.00 28.35 ? 628  ALA B O     1 
ATOM   13318 C CB    . ALA B  1 630  ? 8.342   42.265  53.511  1.00 27.02 ? 628  ALA B CB    1 
ATOM   13319 N N     . ALA B  1 631  ? 6.036   40.425  52.081  1.00 26.04 ? 629  ALA B N     1 
ATOM   13320 C CA    . ALA B  1 631  ? 4.759   40.401  51.381  1.00 25.55 ? 629  ALA B CA    1 
ATOM   13321 C C     . ALA B  1 631  ? 3.800   39.345  51.922  1.00 27.84 ? 629  ALA B C     1 
ATOM   13322 O O     . ALA B  1 631  ? 2.619   39.346  51.550  1.00 25.72 ? 629  ALA B O     1 
ATOM   13323 C CB    . ALA B  1 631  ? 4.998   40.179  49.886  1.00 26.12 ? 629  ALA B CB    1 
ATOM   13324 N N     . VAL B  1 632  ? 4.259   38.455  52.792  1.00 25.51 ? 630  VAL B N     1 
ATOM   13325 C CA    . VAL B  1 632  ? 3.331   37.499  53.400  1.00 23.10 ? 630  VAL B CA    1 
ATOM   13326 C C     . VAL B  1 632  ? 2.460   38.246  54.398  1.00 22.05 ? 630  VAL B C     1 
ATOM   13327 O O     . VAL B  1 632  ? 3.004   38.956  55.270  1.00 25.65 ? 630  VAL B O     1 
ATOM   13328 C CB    . VAL B  1 632  ? 4.101   36.369  54.082  1.00 23.21 ? 630  VAL B CB    1 
ATOM   13329 C CG1   . VAL B  1 632  ? 3.143   35.406  54.779  1.00 21.65 ? 630  VAL B CG1   1 
ATOM   13330 C CG2   . VAL B  1 632  ? 4.989   35.644  53.069  1.00 24.31 ? 630  VAL B CG2   1 
ATOM   13331 N N     . PRO B  1 633  ? 1.133   38.162  54.291  1.00 21.77 ? 631  PRO B N     1 
ATOM   13332 C CA    . PRO B  1 633  ? 0.259   38.889  55.215  1.00 22.14 ? 631  PRO B CA    1 
ATOM   13333 C C     . PRO B  1 633  ? 0.636   38.598  56.654  1.00 23.23 ? 631  PRO B C     1 
ATOM   13334 O O     . PRO B  1 633  ? 1.000   37.461  56.988  1.00 22.02 ? 631  PRO B O     1 
ATOM   13335 C CB    . PRO B  1 633  ? -1.137  38.345  54.886  1.00 23.56 ? 631  PRO B CB    1 
ATOM   13336 C CG    . PRO B  1 633  ? -1.037  38.026  53.418  1.00 22.70 ? 631  PRO B CG    1 
ATOM   13337 C CD    . PRO B  1 633  ? 0.365   37.514  53.206  1.00 21.04 ? 631  PRO B CD    1 
ATOM   13338 N N     . PRO B  1 634  ? 0.569   39.603  57.522  1.00 24.92 ? 632  PRO B N     1 
ATOM   13339 C CA    . PRO B  1 634  ? 0.949   39.383  58.929  1.00 25.49 ? 632  PRO B CA    1 
ATOM   13340 C C     . PRO B  1 634  ? 0.206   38.231  59.591  1.00 19.87 ? 632  PRO B C     1 
ATOM   13341 O O     . PRO B  1 634  ? 0.812   37.491  60.378  1.00 21.56 ? 632  PRO B O     1 
ATOM   13342 C CB    . PRO B  1 634  ? 0.618   40.726  59.592  1.00 23.99 ? 632  PRO B CB    1 
ATOM   13343 C CG    . PRO B  1 634  ? 0.665   41.721  58.478  1.00 27.89 ? 632  PRO B CG    1 
ATOM   13344 C CD    . PRO B  1 634  ? 0.232   41.009  57.236  1.00 21.77 ? 632  PRO B CD    1 
ATOM   13345 N N     . SER B  1 635  ? -1.079  38.049  59.300  1.00 21.63 ? 633  SER B N     1 
ATOM   13346 C CA    . SER B  1 635  ? -1.817  36.959  59.934  1.00 21.46 ? 633  SER B CA    1 
ATOM   13347 C C     . SER B  1 635  ? -1.322  35.600  59.453  1.00 20.65 ? 633  SER B C     1 
ATOM   13348 O O     . SER B  1 635  ? -1.405  34.612  60.191  1.00 20.64 ? 633  SER B O     1 
ATOM   13349 C CB    . SER B  1 635  ? -3.318  37.100  59.663  1.00 26.37 ? 633  SER B CB    1 
ATOM   13350 O OG    . SER B  1 635  ? -3.567  37.069  58.267  1.00 30.86 ? 633  SER B OG    1 
ATOM   13351 N N     . GLU B  1 636  ? -0.822  35.525  58.218  1.00 21.06 ? 634  GLU B N     1 
ATOM   13352 C CA    . GLU B  1 636  ? -0.250  34.275  57.733  1.00 20.91 ? 634  GLU B CA    1 
ATOM   13353 C C     . GLU B  1 636  ? 1.121   34.027  58.334  1.00 20.84 ? 634  GLU B C     1 
ATOM   13354 O O     . GLU B  1 636  ? 1.490   32.870  58.571  1.00 21.28 ? 634  GLU B O     1 
ATOM   13355 C CB    . GLU B  1 636  ? -0.162  34.286  56.212  1.00 25.31 ? 634  GLU B CB    1 
ATOM   13356 C CG    . GLU B  1 636  ? -1.535  34.185  55.591  1.00 28.61 ? 634  GLU B CG    1 
ATOM   13357 C CD    . GLU B  1 636  ? -2.287  32.962  56.091  1.00 40.40 ? 634  GLU B CD    1 
ATOM   13358 O OE1   . GLU B  1 636  ? -1.721  31.841  56.016  1.00 41.69 ? 634  GLU B OE1   1 
ATOM   13359 O OE2   . GLU B  1 636  ? -3.427  33.124  56.586  1.00 47.91 ? 634  GLU B OE2   1 
ATOM   13360 N N     . ARG B  1 637  ? 1.893   35.087  58.563  1.00 17.59 ? 635  ARG B N     1 
ATOM   13361 C CA    . ARG B  1 637  ? 3.155   34.908  59.277  1.00 18.10 ? 635  ARG B CA    1 
ATOM   13362 C C     . ARG B  1 637  ? 2.906   34.439  60.711  1.00 20.61 ? 635  ARG B C     1 
ATOM   13363 O O     . ARG B  1 637  ? 3.608   33.544  61.218  1.00 19.84 ? 635  ARG B O     1 
ATOM   13364 C CB    . ARG B  1 637  ? 3.963   36.203  59.260  1.00 21.14 ? 635  ARG B CB    1 
ATOM   13365 C CG    . ARG B  1 637  ? 4.200   36.786  57.860  1.00 22.57 ? 635  ARG B CG    1 
ATOM   13366 C CD    . ARG B  1 637  ? 5.292   37.869  57.850  1.00 22.70 ? 635  ARG B CD    1 
ATOM   13367 N NE    . ARG B  1 637  ? 5.005   39.011  58.717  1.00 22.53 ? 635  ARG B NE    1 
ATOM   13368 C CZ    . ARG B  1 637  ? 4.647   40.215  58.282  1.00 27.89 ? 635  ARG B CZ    1 
ATOM   13369 N NH1   . ARG B  1 637  ? 4.422   40.453  56.994  1.00 29.65 ? 635  ARG B NH1   1 
ATOM   13370 N NH2   . ARG B  1 637  ? 4.513   41.208  59.158  1.00 21.41 ? 635  ARG B NH2   1 
ATOM   13371 N N     . ALA B  1 638  ? 1.932   35.056  61.391  1.00 20.14 ? 636  ALA B N     1 
ATOM   13372 C CA    . ALA B  1 638  ? 1.554   34.621  62.735  1.00 18.62 ? 636  ALA B CA    1 
ATOM   13373 C C     . ALA B  1 638  ? 1.076   33.171  62.743  1.00 19.49 ? 636  ALA B C     1 
ATOM   13374 O O     . ALA B  1 638  ? 1.357   32.420  63.679  1.00 19.11 ? 636  ALA B O     1 
ATOM   13375 C CB    . ALA B  1 638  ? 0.475   35.544  63.296  1.00 19.35 ? 636  ALA B CB    1 
ATOM   13376 N N     . ALA B  1 639  ? 0.339   32.762  61.711  1.00 18.21 ? 637  ALA B N     1 
ATOM   13377 C CA    . ALA B  1 639  ? -0.083  31.367  61.614  1.00 21.10 ? 637  ALA B CA    1 
ATOM   13378 C C     . ALA B  1 639  ? 1.106   30.410  61.569  1.00 18.22 ? 637  ALA B C     1 
ATOM   13379 O O     . ALA B  1 639  ? 1.005   29.280  62.073  1.00 19.43 ? 637  ALA B O     1 
ATOM   13380 C CB    . ALA B  1 639  ? -0.970  31.175  60.376  1.00 17.06 ? 637  ALA B CB    1 
ATOM   13381 N N     . CYS B  1 640  ? 2.231   30.829  60.965  1.00 17.57 ? 638  CYS B N     1 
ATOM   13382 C CA    . CYS B  1 640  ? 3.427   29.983  60.963  1.00 18.02 ? 638  CYS B CA    1 
ATOM   13383 C C     . CYS B  1 640  ? 3.939   29.799  62.378  1.00 18.70 ? 638  CYS B C     1 
ATOM   13384 O O     . CYS B  1 640  ? 4.325   28.696  62.786  1.00 15.80 ? 638  CYS B O     1 
ATOM   13385 C CB    . CYS B  1 640  ? 4.551   30.599  60.123  1.00 16.41 ? 638  CYS B CB    1 
ATOM   13386 S SG    . CYS B  1 640  ? 4.262   30.582  58.360  1.00 21.77 ? 638  CYS B SG    1 
ATOM   13387 N N     . LEU B  1 641  ? 3.949   30.882  63.139  1.00 15.07 ? 639  LEU B N     1 
ATOM   13388 C CA    . LEU B  1 641  ? 4.402   30.781  64.523  1.00 16.06 ? 639  LEU B CA    1 
ATOM   13389 C C     . LEU B  1 641  ? 3.491   29.873  65.336  1.00 17.93 ? 639  LEU B C     1 
ATOM   13390 O O     . LEU B  1 641  ? 3.969   29.084  66.164  1.00 17.57 ? 639  LEU B O     1 
ATOM   13391 C CB    . LEU B  1 641  ? 4.463   32.172  65.170  1.00 17.83 ? 639  LEU B CB    1 
ATOM   13392 C CG    . LEU B  1 641  ? 5.737   32.996  65.101  1.00 19.71 ? 639  LEU B CG    1 
ATOM   13393 C CD1   . LEU B  1 641  ? 6.216   33.179  63.650  1.00 21.97 ? 639  LEU B CD1   1 
ATOM   13394 C CD2   . LEU B  1 641  ? 5.536   34.342  65.800  1.00 20.59 ? 639  LEU B CD2   1 
ATOM   13395 N N     . ASP B  1 642  ? 2.171   29.980  65.128  1.00 17.33 ? 640  ASP B N     1 
ATOM   13396 C CA    . ASP B  1 642  ? 1.235   29.143  65.877  1.00 18.86 ? 640  ASP B CA    1 
ATOM   13397 C C     . ASP B  1 642  ? 1.397   27.672  65.507  1.00 15.66 ? 640  ASP B C     1 
ATOM   13398 O O     . ASP B  1 642  ? 1.309   26.792  66.369  1.00 16.02 ? 640  ASP B O     1 
ATOM   13399 C CB    . ASP B  1 642  ? -0.211  29.601  65.640  1.00 19.27 ? 640  ASP B CB    1 
ATOM   13400 C CG    . ASP B  1 642  ? -0.590  30.848  66.452  1.00 22.59 ? 640  ASP B CG    1 
ATOM   13401 O OD1   . ASP B  1 642  ? 0.063   31.154  67.485  1.00 21.23 ? 640  ASP B OD1   1 
ATOM   13402 O OD2   . ASP B  1 642  ? -1.540  31.537  66.045  1.00 21.04 ? 640  ASP B OD2   1 
ATOM   13403 N N     . ARG B  1 643  ? 1.620   27.375  64.227  1.00 16.84 ? 641  ARG B N     1 
ATOM   13404 C CA    . ARG B  1 643  ? 1.844   25.985  63.853  1.00 18.35 ? 641  ARG B CA    1 
ATOM   13405 C C     . ARG B  1 643  ? 3.126   25.458  64.483  1.00 19.09 ? 641  ARG B C     1 
ATOM   13406 O O     . ARG B  1 643  ? 3.191   24.296  64.899  1.00 19.99 ? 641  ARG B O     1 
ATOM   13407 C CB    . ARG B  1 643  ? 1.881   25.851  62.331  1.00 19.26 ? 641  ARG B CB    1 
ATOM   13408 C CG    . ARG B  1 643  ? 0.489   25.943  61.707  1.00 24.21 ? 641  ARG B CG    1 
ATOM   13409 C CD    . ARG B  1 643  ? 0.508   25.534  60.223  1.00 25.14 ? 641  ARG B CD    1 
ATOM   13410 N NE    . ARG B  1 643  ? 1.299   26.459  59.417  1.00 27.60 ? 641  ARG B NE    1 
ATOM   13411 C CZ    . ARG B  1 643  ? 0.795   27.509  58.786  1.00 27.74 ? 641  ARG B CZ    1 
ATOM   13412 N NH1   . ARG B  1 643  ? -0.493  27.792  58.849  1.00 24.38 ? 641  ARG B NH1   1 
ATOM   13413 N NH2   . ARG B  1 643  ? 1.601   28.279  58.059  1.00 25.63 ? 641  ARG B NH2   1 
ATOM   13414 N N     . ALA B  1 644  ? 4.145   26.306  64.570  1.00 18.53 ? 642  ALA B N     1 
ATOM   13415 C CA    . ALA B  1 644  ? 5.399   25.898  65.192  1.00 17.50 ? 642  ALA B CA    1 
ATOM   13416 C C     . ALA B  1 644  ? 5.195   25.586  66.662  1.00 20.68 ? 642  ALA B C     1 
ATOM   13417 O O     . ALA B  1 644  ? 5.804   24.644  67.192  1.00 17.09 ? 642  ALA B O     1 
ATOM   13418 C CB    . ALA B  1 644  ? 6.448   27.000  65.028  1.00 16.86 ? 642  ALA B CB    1 
ATOM   13419 N N     . ALA B  1 645  ? 4.373   26.401  67.348  1.00 18.21 ? 643  ALA B N     1 
ATOM   13420 C CA    . ALA B  1 645  ? 4.090   26.143  68.757  1.00 16.48 ? 643  ALA B CA    1 
ATOM   13421 C C     . ALA B  1 645  ? 3.385   24.808  68.928  1.00 19.31 ? 643  ALA B C     1 
ATOM   13422 O O     . ALA B  1 645  ? 3.714   24.040  69.839  1.00 19.45 ? 643  ALA B O     1 
ATOM   13423 C CB    . ALA B  1 645  ? 3.265   27.286  69.352  1.00 18.05 ? 643  ALA B CB    1 
ATOM   13424 N N     . GLU B  1 646  ? 2.425   24.499  68.043  1.00 17.70 ? 644  GLU B N     1 
ATOM   13425 C CA    . GLU B  1 646  ? 1.768   23.193  68.102  1.00 24.84 ? 644  GLU B CA    1 
ATOM   13426 C C     . GLU B  1 646  ? 2.772   22.060  67.962  1.00 22.74 ? 644  GLU B C     1 
ATOM   13427 O O     . GLU B  1 646  ? 2.655   21.027  68.635  1.00 23.18 ? 644  GLU B O     1 
ATOM   13428 C CB    . GLU B  1 646  ? 0.712   23.059  66.999  1.00 20.92 ? 644  GLU B CB    1 
ATOM   13429 C CG    . GLU B  1 646  ? -0.511  23.898  67.210  1.00 25.42 ? 644  GLU B CG    1 
ATOM   13430 C CD    . GLU B  1 646  ? -1.239  23.518  68.480  1.00 34.54 ? 644  GLU B CD    1 
ATOM   13431 O OE1   . GLU B  1 646  ? -1.282  22.309  68.811  1.00 44.52 ? 644  GLU B OE1   1 
ATOM   13432 O OE2   . GLU B  1 646  ? -1.743  24.433  69.162  1.00 39.15 ? 644  GLU B OE2   1 
ATOM   13433 N N     . LEU B  1 647  ? 3.754   22.227  67.072  1.00 19.05 ? 645  LEU B N     1 
ATOM   13434 C CA    . LEU B  1 647  ? 4.738   21.171  66.842  1.00 20.14 ? 645  LEU B CA    1 
ATOM   13435 C C     . LEU B  1 647  ? 5.660   21.009  68.042  1.00 20.84 ? 645  LEU B C     1 
ATOM   13436 O O     . LEU B  1 647  ? 5.986   19.884  68.433  1.00 21.54 ? 645  LEU B O     1 
ATOM   13437 C CB    . LEU B  1 647  ? 5.561   21.485  65.589  1.00 21.30 ? 645  LEU B CB    1 
ATOM   13438 C CG    . LEU B  1 647  ? 4.849   21.470  64.236  1.00 21.51 ? 645  LEU B CG    1 
ATOM   13439 C CD1   . LEU B  1 647  ? 5.818   21.869  63.110  1.00 24.42 ? 645  LEU B CD1   1 
ATOM   13440 C CD2   . LEU B  1 647  ? 4.234   20.097  63.958  1.00 27.98 ? 645  LEU B CD2   1 
ATOM   13441 N N     . MET B  1 648  ? 6.088   22.117  68.632  1.00 19.25 ? 646  MET B N     1 
ATOM   13442 C CA    . MET B  1 648  ? 6.940   22.033  69.816  1.00 18.76 ? 646  MET B CA    1 
ATOM   13443 C C     . MET B  1 648  ? 6.187   21.430  70.993  1.00 21.08 ? 646  MET B C     1 
ATOM   13444 O O     . MET B  1 648  ? 6.772   20.704  71.807  1.00 23.06 ? 646  MET B O     1 
ATOM   13445 C CB    . MET B  1 648  ? 7.454   23.414  70.207  1.00 18.91 ? 646  MET B CB    1 
ATOM   13446 C CG    . MET B  1 648  ? 8.531   23.957  69.313  1.00 24.03 ? 646  MET B CG    1 
ATOM   13447 S SD    . MET B  1 648  ? 9.325   25.371  70.117  1.00 22.13 ? 646  MET B SD    1 
ATOM   13448 C CE    . MET B  1 648  ? 10.250  25.980  68.712  1.00 17.36 ? 646  MET B CE    1 
ATOM   13449 N N     . GLN B  1 649  ? 4.905   21.771  71.124  1.00 21.64 ? 647  GLN B N     1 
ATOM   13450 C CA    . GLN B  1 649  ? 4.081   21.189  72.177  1.00 19.39 ? 647  GLN B CA    1 
ATOM   13451 C C     . GLN B  1 649  ? 3.963   19.678  72.011  1.00 19.77 ? 647  GLN B C     1 
ATOM   13452 O O     . GLN B  1 649  ? 4.102   18.929  72.980  1.00 21.78 ? 647  GLN B O     1 
ATOM   13453 C CB    . GLN B  1 649  ? 2.696   21.827  72.168  1.00 22.13 ? 647  GLN B CB    1 
ATOM   13454 C CG    . GLN B  1 649  ? 1.819   21.294  73.279  1.00 20.49 ? 647  GLN B CG    1 
ATOM   13455 C CD    . GLN B  1 649  ? 2.236   21.878  74.601  1.00 22.72 ? 647  GLN B CD    1 
ATOM   13456 O OE1   . GLN B  1 649  ? 1.917   23.028  74.901  1.00 21.64 ? 647  GLN B OE1   1 
ATOM   13457 N NE2   . GLN B  1 649  ? 3.009   21.115  75.383  1.00 20.45 ? 647  GLN B NE2   1 
ATOM   13458 N N     . ALA B  1 650  ? 3.657   19.220  70.791  1.00 20.87 ? 648  ALA B N     1 
ATOM   13459 C CA    . ALA B  1 650  ? 3.515   17.789  70.520  1.00 22.70 ? 648  ALA B CA    1 
ATOM   13460 C C     . ALA B  1 650  ? 4.833   17.043  70.685  1.00 27.69 ? 648  ALA B C     1 
ATOM   13461 O O     . ALA B  1 650  ? 4.840   15.872  71.082  1.00 27.84 ? 648  ALA B O     1 
ATOM   13462 C CB    . ALA B  1 650  ? 2.978   17.566  69.103  1.00 21.69 ? 648  ALA B CB    1 
ATOM   13463 N N     . ARG B  1 651  ? 5.948   17.689  70.361  1.00 23.10 ? 649  ARG B N     1 
ATOM   13464 C CA    . ARG B  1 651  ? 7.256   17.061  70.385  1.00 21.47 ? 649  ARG B CA    1 
ATOM   13465 C C     . ARG B  1 651  ? 8.032   17.388  71.647  1.00 22.49 ? 649  ARG B C     1 
ATOM   13466 O O     . ARG B  1 651  ? 9.224   17.086  71.727  1.00 24.32 ? 649  ARG B O     1 
ATOM   13467 C CB    . ARG B  1 651  ? 8.029   17.474  69.144  1.00 23.72 ? 649  ARG B CB    1 
ATOM   13468 C CG    . ARG B  1 651  ? 7.246   17.014  67.892  1.00 23.24 ? 649  ARG B CG    1 
ATOM   13469 C CD    . ARG B  1 651  ? 7.919   17.400  66.623  1.00 25.17 ? 649  ARG B CD    1 
ATOM   13470 N NE    . ARG B  1 651  ? 7.045   17.101  65.499  1.00 24.81 ? 649  ARG B NE    1 
ATOM   13471 C CZ    . ARG B  1 651  ? 7.236   17.552  64.270  1.00 29.15 ? 649  ARG B CZ    1 
ATOM   13472 N NH1   . ARG B  1 651  ? 8.302   18.278  63.961  1.00 24.79 ? 649  ARG B NH1   1 
ATOM   13473 N NH2   . ARG B  1 651  ? 6.323   17.287  63.332  1.00 26.77 ? 649  ARG B NH2   1 
ATOM   13474 N N     . MET B  1 652  ? 7.371   17.972  72.642  1.00 23.77 ? 650  MET B N     1 
ATOM   13475 C CA    . MET B  1 652  ? 8.052   18.353  73.875  1.00 19.71 ? 650  MET B CA    1 
ATOM   13476 C C     . MET B  1 652  ? 8.883   17.227  74.484  1.00 23.27 ? 650  MET B C     1 
ATOM   13477 O O     . MET B  1 652  ? 10.033  17.492  74.863  1.00 24.31 ? 650  MET B O     1 
ATOM   13478 C CB    . MET B  1 652  ? 7.028   18.898  74.884  1.00 20.82 ? 650  MET B CB    1 
ATOM   13479 C CG    . MET B  1 652  ? 7.644   19.284  76.242  1.00 21.99 ? 650  MET B CG    1 
ATOM   13480 S SD    . MET B  1 652  ? 6.477   20.035  77.417  1.00 24.29 ? 650  MET B SD    1 
ATOM   13481 C CE    . MET B  1 652  ? 6.409   21.716  76.833  1.00 22.79 ? 650  MET B CE    1 
ATOM   13482 N N     . PRO B  1 653  ? 8.401   15.980  74.604  1.00 21.42 ? 651  PRO B N     1 
ATOM   13483 C CA    . PRO B  1 653  ? 9.241   14.971  75.278  1.00 22.68 ? 651  PRO B CA    1 
ATOM   13484 C C     . PRO B  1 653  ? 10.589  14.769  74.600  1.00 22.57 ? 651  PRO B C     1 
ATOM   13485 O O     . PRO B  1 653  ? 11.598  14.641  75.298  1.00 25.02 ? 651  PRO B O     1 
ATOM   13486 C CB    . PRO B  1 653  ? 8.373   13.705  75.239  1.00 25.72 ? 651  PRO B CB    1 
ATOM   13487 C CG    . PRO B  1 653  ? 6.975   14.214  75.156  1.00 29.03 ? 651  PRO B CG    1 
ATOM   13488 C CD    . PRO B  1 653  ? 7.070   15.431  74.279  1.00 23.81 ? 651  PRO B CD    1 
ATOM   13489 N N     . THR B  1 654  ? 10.636  14.769  73.264  1.00 24.34 ? 652  THR B N     1 
ATOM   13490 C CA    . THR B  1 654  ? 11.908  14.634  72.550  1.00 25.57 ? 652  THR B CA    1 
ATOM   13491 C C     . THR B  1 654  ? 12.768  15.880  72.708  1.00 27.20 ? 652  THR B C     1 
ATOM   13492 O O     . THR B  1 654  ? 13.989  15.776  72.894  1.00 29.09 ? 652  THR B O     1 
ATOM   13493 C CB    . THR B  1 654  ? 11.657  14.353  71.067  1.00 26.72 ? 652  THR B CB    1 
ATOM   13494 O OG1   . THR B  1 654  ? 10.845  13.185  70.941  1.00 26.09 ? 652  THR B OG1   1 
ATOM   13495 C CG2   . THR B  1 654  ? 12.982  14.128  70.314  1.00 23.04 ? 652  THR B CG2   1 
ATOM   13496 N N     . LEU B  1 655  ? 12.153  17.065  72.647  1.00 24.86 ? 653  LEU B N     1 
ATOM   13497 C CA    . LEU B  1 655  ? 12.909  18.293  72.875  1.00 20.85 ? 653  LEU B CA    1 
ATOM   13498 C C     . LEU B  1 655  ? 13.553  18.284  74.248  1.00 21.42 ? 653  LEU B C     1 
ATOM   13499 O O     . LEU B  1 655  ? 14.726  18.652  74.385  1.00 21.55 ? 653  LEU B O     1 
ATOM   13500 C CB    . LEU B  1 655  ? 12.014  19.518  72.733  1.00 24.07 ? 653  LEU B CB    1 
ATOM   13501 C CG    . LEU B  1 655  ? 11.366  19.606  71.357  1.00 25.05 ? 653  LEU B CG    1 
ATOM   13502 C CD1   . LEU B  1 655  ? 10.640  20.944  71.163  1.00 22.03 ? 653  LEU B CD1   1 
ATOM   13503 C CD2   . LEU B  1 655  ? 12.450  19.398  70.319  1.00 24.45 ? 653  LEU B CD2   1 
ATOM   13504 N N     . LEU B  1 656  ? 12.804  17.855  75.272  1.00 20.94 ? 654  LEU B N     1 
ATOM   13505 C CA    . LEU B  1 656  ? 13.355  17.771  76.627  1.00 21.59 ? 654  LEU B CA    1 
ATOM   13506 C C     . LEU B  1 656  ? 14.647  16.983  76.649  1.00 22.45 ? 654  LEU B C     1 
ATOM   13507 O O     . LEU B  1 656  ? 15.631  17.396  77.270  1.00 24.52 ? 654  LEU B O     1 
ATOM   13508 C CB    . LEU B  1 656  ? 12.359  17.106  77.578  1.00 22.74 ? 654  LEU B CB    1 
ATOM   13509 C CG    . LEU B  1 656  ? 10.996  17.743  77.718  1.00 25.53 ? 654  LEU B CG    1 
ATOM   13510 C CD1   . LEU B  1 656  ? 10.129  16.955  78.687  1.00 24.27 ? 654  LEU B CD1   1 
ATOM   13511 C CD2   . LEU B  1 656  ? 11.175  19.179  78.134  1.00 24.57 ? 654  LEU B CD2   1 
ATOM   13512 N N     . GLY B  1 657  ? 14.649  15.814  76.002  1.00 25.84 ? 655  GLY B N     1 
ATOM   13513 C CA    . GLY B  1 657  ? 15.815  14.952  76.072  1.00 26.12 ? 655  GLY B CA    1 
ATOM   13514 C C     . GLY B  1 657  ? 17.045  15.612  75.489  1.00 27.15 ? 655  GLY B C     1 
ATOM   13515 O O     . GLY B  1 657  ? 18.148  15.468  76.014  1.00 25.01 ? 655  GLY B O     1 
ATOM   13516 N N     . LEU B  1 658  ? 16.864  16.359  74.400  1.00 22.36 ? 656  LEU B N     1 
ATOM   13517 C CA    . LEU B  1 658  ? 17.976  17.098  73.820  1.00 25.74 ? 656  LEU B CA    1 
ATOM   13518 C C     . LEU B  1 658  ? 18.445  18.218  74.744  1.00 25.93 ? 656  LEU B C     1 
ATOM   13519 O O     . LEU B  1 658  ? 19.655  18.395  74.944  1.00 24.27 ? 656  LEU B O     1 
ATOM   13520 C CB    . LEU B  1 658  ? 17.565  17.648  72.451  1.00 25.49 ? 656  LEU B CB    1 
ATOM   13521 C CG    . LEU B  1 658  ? 18.708  18.260  71.641  1.00 26.86 ? 656  LEU B CG    1 
ATOM   13522 C CD1   . LEU B  1 658  ? 19.879  17.293  71.524  1.00 22.61 ? 656  LEU B CD1   1 
ATOM   13523 C CD2   . LEU B  1 658  ? 18.198  18.707  70.271  1.00 25.57 ? 656  LEU B CD2   1 
ATOM   13524 N N     . ILE B  1 659  ? 17.508  18.974  75.332  1.00 23.13 ? 657  ILE B N     1 
ATOM   13525 C CA    . ILE B  1 659  ? 17.890  20.102  76.185  1.00 19.95 ? 657  ILE B CA    1 
ATOM   13526 C C     . ILE B  1 659  ? 18.585  19.602  77.432  1.00 22.86 ? 657  ILE B C     1 
ATOM   13527 O O     . ILE B  1 659  ? 19.527  20.231  77.929  1.00 22.22 ? 657  ILE B O     1 
ATOM   13528 C CB    . ILE B  1 659  ? 16.664  20.963  76.550  1.00 21.31 ? 657  ILE B CB    1 
ATOM   13529 C CG1   . ILE B  1 659  ? 16.147  21.687  75.316  1.00 19.86 ? 657  ILE B CG1   1 
ATOM   13530 C CG2   . ILE B  1 659  ? 17.012  22.011  77.623  1.00 21.75 ? 657  ILE B CG2   1 
ATOM   13531 C CD1   . ILE B  1 659  ? 14.669  22.106  75.435  1.00 23.37 ? 657  ILE B CD1   1 
ATOM   13532 N N     . ILE B  1 660  ? 18.110  18.482  77.973  1.00 21.16 ? 658  ILE B N     1 
ATOM   13533 C CA    . ILE B  1 660  ? 18.720  17.924  79.178  1.00 19.78 ? 658  ILE B CA    1 
ATOM   13534 C C     . ILE B  1 660  ? 20.181  17.578  78.924  1.00 18.46 ? 658  ILE B C     1 
ATOM   13535 O O     . ILE B  1 660  ? 21.061  17.867  79.751  1.00 22.82 ? 658  ILE B O     1 
ATOM   13536 C CB    . ILE B  1 660  ? 17.912  16.701  79.653  1.00 21.47 ? 658  ILE B CB    1 
ATOM   13537 C CG1   . ILE B  1 660  ? 16.613  17.157  80.322  1.00 20.93 ? 658  ILE B CG1   1 
ATOM   13538 C CG2   . ILE B  1 660  ? 18.744  15.837  80.617  1.00 23.55 ? 658  ILE B CG2   1 
ATOM   13539 C CD1   . ILE B  1 660  ? 15.597  16.041  80.484  1.00 25.81 ? 658  ILE B CD1   1 
ATOM   13540 N N     . ARG B  1 661  ? 20.467  16.940  77.789  1.00 20.90 ? 659  ARG B N     1 
ATOM   13541 C CA    . ARG B  1 661  ? 21.807  16.402  77.565  1.00 24.49 ? 659  ARG B CA    1 
ATOM   13542 C C     . ARG B  1 661  ? 22.745  17.400  76.905  1.00 24.77 ? 659  ARG B C     1 
ATOM   13543 O O     . ARG B  1 661  ? 23.937  17.404  77.204  1.00 25.92 ? 659  ARG B O     1 
ATOM   13544 C CB    . ARG B  1 661  ? 21.752  15.128  76.712  1.00 23.03 ? 659  ARG B CB    1 
ATOM   13545 C CG    . ARG B  1 661  ? 21.233  13.909  77.466  1.00 25.15 ? 659  ARG B CG    1 
ATOM   13546 C CD    . ARG B  1 661  ? 21.087  12.675  76.572  1.00 28.94 ? 659  ARG B CD    1 
ATOM   13547 N NE    . ARG B  1 661  ? 22.325  12.239  75.931  1.00 29.22 ? 659  ARG B NE    1 
ATOM   13548 C CZ    . ARG B  1 661  ? 22.472  12.102  74.618  1.00 29.73 ? 659  ARG B CZ    1 
ATOM   13549 N NH1   . ARG B  1 661  ? 21.488  12.381  73.780  1.00 25.68 ? 659  ARG B NH1   1 
ATOM   13550 N NH2   . ARG B  1 661  ? 23.628  11.655  74.132  1.00 29.55 ? 659  ARG B NH2   1 
ATOM   13551 N N     . GLU B  1 662  ? 22.247  18.228  75.987  1.00 22.12 ? 660  GLU B N     1 
ATOM   13552 C CA    . GLU B  1 662  ? 23.122  19.206  75.349  1.00 21.57 ? 660  GLU B CA    1 
ATOM   13553 C C     . GLU B  1 662  ? 23.374  20.407  76.247  1.00 22.12 ? 660  GLU B C     1 
ATOM   13554 O O     . GLU B  1 662  ? 24.474  20.963  76.247  1.00 24.65 ? 660  GLU B O     1 
ATOM   13555 C CB    . GLU B  1 662  ? 22.532  19.685  74.020  1.00 24.66 ? 660  GLU B CB    1 
ATOM   13556 C CG    . GLU B  1 662  ? 23.382  20.793  73.391  1.00 24.72 ? 660  GLU B CG    1 
ATOM   13557 C CD    . GLU B  1 662  ? 22.794  21.354  72.112  1.00 23.47 ? 660  GLU B CD    1 
ATOM   13558 O OE1   . GLU B  1 662  ? 21.566  21.572  72.055  1.00 24.81 ? 660  GLU B OE1   1 
ATOM   13559 O OE2   . GLU B  1 662  ? 23.570  21.573  71.164  1.00 24.95 ? 660  GLU B OE2   1 
ATOM   13560 N N     . ALA B  1 663  ? 22.367  20.837  77.000  1.00 21.11 ? 661  ALA B N     1 
ATOM   13561 C CA    . ALA B  1 663  ? 22.506  22.044  77.801  1.00 23.78 ? 661  ALA B CA    1 
ATOM   13562 C C     . ALA B  1 663  ? 22.721  21.767  79.280  1.00 22.42 ? 661  ALA B C     1 
ATOM   13563 O O     . ALA B  1 663  ? 22.984  22.710  80.034  1.00 23.53 ? 661  ALA B O     1 
ATOM   13564 C CB    . ALA B  1 663  ? 21.281  22.943  77.625  1.00 24.31 ? 661  ALA B CB    1 
ATOM   13565 N N     . GLY B  1 664  ? 22.630  20.512  79.708  1.00 23.16 ? 662  GLY B N     1 
ATOM   13566 C CA    . GLY B  1 664  ? 22.796  20.198  81.119  1.00 25.24 ? 662  GLY B CA    1 
ATOM   13567 C C     . GLY B  1 664  ? 21.673  20.654  82.028  1.00 23.92 ? 662  GLY B C     1 
ATOM   13568 O O     . GLY B  1 664  ? 21.915  20.929  83.210  1.00 25.69 ? 662  GLY B O     1 
ATOM   13569 N N     . LYS B  1 665  ? 20.448  20.734  81.521  1.00 19.14 ? 663  LYS B N     1 
ATOM   13570 C CA    . LYS B  1 665  ? 19.300  21.170  82.308  1.00 21.56 ? 663  LYS B CA    1 
ATOM   13571 C C     . LYS B  1 665  ? 18.588  19.992  82.955  1.00 21.80 ? 663  LYS B C     1 
ATOM   13572 O O     . LYS B  1 665  ? 18.610  18.871  82.441  1.00 20.51 ? 663  LYS B O     1 
ATOM   13573 C CB    . LYS B  1 665  ? 18.298  21.938  81.442  1.00 21.43 ? 663  LYS B CB    1 
ATOM   13574 C CG    . LYS B  1 665  ? 18.821  23.272  81.030  1.00 30.17 ? 663  LYS B CG    1 
ATOM   13575 C CD    . LYS B  1 665  ? 17.752  24.185  80.511  1.00 27.81 ? 663  LYS B CD    1 
ATOM   13576 C CE    . LYS B  1 665  ? 18.358  25.551  80.246  1.00 28.88 ? 663  LYS B CE    1 
ATOM   13577 N NZ    . LYS B  1 665  ? 17.365  26.647  80.338  1.00 31.78 ? 663  LYS B NZ    1 
ATOM   13578 N N     . SER B  1 666  ? 17.941  20.260  84.088  1.00 21.86 ? 664  SER B N     1 
ATOM   13579 C CA    . SER B  1 666  ? 17.056  19.268  84.684  1.00 24.30 ? 664  SER B CA    1 
ATOM   13580 C C     . SER B  1 666  ? 15.778  19.157  83.865  1.00 23.52 ? 664  SER B C     1 
ATOM   13581 O O     . SER B  1 666  ? 15.437  20.053  83.088  1.00 24.77 ? 664  SER B O     1 
ATOM   13582 C CB    . SER B  1 666  ? 16.701  19.652  86.115  1.00 29.67 ? 664  SER B CB    1 
ATOM   13583 O OG    . SER B  1 666  ? 15.862  20.788  86.103  1.00 28.94 ? 664  SER B OG    1 
ATOM   13584 N N     . ALA B  1 667  ? 15.057  18.049  84.053  1.00 20.19 ? 665  ALA B N     1 
ATOM   13585 C CA    . ALA B  1 667  ? 13.808  17.852  83.311  1.00 24.92 ? 665  ALA B CA    1 
ATOM   13586 C C     . ALA B  1 667  ? 12.826  19.002  83.535  1.00 25.11 ? 665  ALA B C     1 
ATOM   13587 O O     . ALA B  1 667  ? 12.208  19.501  82.586  1.00 22.32 ? 665  ALA B O     1 
ATOM   13588 C CB    . ALA B  1 667  ? 13.176  16.517  83.701  1.00 27.57 ? 665  ALA B CB    1 
ATOM   13589 N N     . LEU B  1 668  ? 12.655  19.429  84.788  1.00 25.13 ? 666  LEU B N     1 
ATOM   13590 C CA    . LEU B  1 668  ? 11.708  20.503  85.078  1.00 26.13 ? 666  LEU B CA    1 
ATOM   13591 C C     . LEU B  1 668  ? 12.087  21.787  84.354  1.00 23.65 ? 666  LEU B C     1 
ATOM   13592 O O     . LEU B  1 668  ? 11.224  22.471  83.788  1.00 22.89 ? 666  LEU B O     1 
ATOM   13593 C CB    . LEU B  1 668  ? 11.642  20.753  86.585  1.00 30.32 ? 666  LEU B CB    1 
ATOM   13594 C CG    . LEU B  1 668  ? 10.431  21.545  87.055  1.00 34.54 ? 666  LEU B CG    1 
ATOM   13595 C CD1   . LEU B  1 668  ? 9.161   20.710  86.864  1.00 33.12 ? 666  LEU B CD1   1 
ATOM   13596 C CD2   . LEU B  1 668  ? 10.615  21.949  88.505  1.00 39.46 ? 666  LEU B CD2   1 
ATOM   13597 N N     . ASN B  1 669  ? 13.378  22.133  84.353  1.00 24.61 ? 667  ASN B N     1 
ATOM   13598 C CA    . ASN B  1 669  ? 13.802  23.342  83.656  1.00 21.39 ? 667  ASN B CA    1 
ATOM   13599 C C     . ASN B  1 669  ? 13.696  23.183  82.147  1.00 20.41 ? 667  ASN B C     1 
ATOM   13600 O O     . ASN B  1 669  ? 13.421  24.162  81.438  1.00 23.57 ? 667  ASN B O     1 
ATOM   13601 C CB    . ASN B  1 669  ? 15.230  23.711  84.053  1.00 23.84 ? 667  ASN B CB    1 
ATOM   13602 C CG    . ASN B  1 669  ? 15.325  24.170  85.492  1.00 29.44 ? 667  ASN B CG    1 
ATOM   13603 O OD1   . ASN B  1 669  ? 16.130  23.660  86.272  1.00 30.12 ? 667  ASN B OD1   1 
ATOM   13604 N ND2   . ASN B  1 669  ? 14.496  25.140  85.853  1.00 34.46 ? 667  ASN B ND2   1 
ATOM   13605 N N     . ALA B  1 670  ? 13.891  21.962  81.636  1.00 17.74 ? 668  ALA B N     1 
ATOM   13606 C CA    . ALA B  1 670  ? 13.720  21.744  80.203  1.00 19.34 ? 668  ALA B CA    1 
ATOM   13607 C C     . ALA B  1 670  ? 12.263  21.926  79.783  1.00 22.10 ? 668  ALA B C     1 
ATOM   13608 O O     . ALA B  1 670  ? 11.989  22.432  78.683  1.00 18.28 ? 668  ALA B O     1 
ATOM   13609 C CB    . ALA B  1 670  ? 14.222  20.357  79.815  1.00 18.97 ? 668  ALA B CB    1 
ATOM   13610 N N     . ILE B  1 671  ? 11.314  21.505  80.633  1.00 16.27 ? 669  ILE B N     1 
ATOM   13611 C CA    . ILE B  1 671  ? 9.892   21.741  80.337  1.00 21.44 ? 669  ILE B CA    1 
ATOM   13612 C C     . ILE B  1 671  ? 9.616   23.237  80.289  1.00 19.71 ? 669  ILE B C     1 
ATOM   13613 O O     . ILE B  1 671  ? 8.959   23.742  79.376  1.00 18.46 ? 669  ILE B O     1 
ATOM   13614 C CB    . ILE B  1 671  ? 8.994   21.029  81.371  1.00 19.25 ? 669  ILE B CB    1 
ATOM   13615 C CG1   . ILE B  1 671  ? 9.069   19.507  81.179  1.00 20.22 ? 669  ILE B CG1   1 
ATOM   13616 C CG2   . ILE B  1 671  ? 7.538   21.548  81.310  1.00 20.64 ? 669  ILE B CG2   1 
ATOM   13617 C CD1   . ILE B  1 671  ? 8.547   18.674  82.344  1.00 25.40 ? 669  ILE B CD1   1 
ATOM   13618 N N     . ALA B  1 672  ? 10.143  23.973  81.264  1.00 17.09 ? 670  ALA B N     1 
ATOM   13619 C CA    . ALA B  1 672  ? 9.968   25.421  81.288  1.00 21.45 ? 670  ALA B CA    1 
ATOM   13620 C C     . ALA B  1 672  ? 10.546  26.056  80.036  1.00 18.99 ? 670  ALA B C     1 
ATOM   13621 O O     . ALA B  1 672  ? 9.979   27.013  79.495  1.00 24.68 ? 670  ALA B O     1 
ATOM   13622 C CB    . ALA B  1 672  ? 10.635  26.011  82.538  1.00 20.44 ? 670  ALA B CB    1 
ATOM   13623 N N     . GLU B  1 673  ? 11.680  25.537  79.569  1.00 19.52 ? 671  GLU B N     1 
ATOM   13624 C CA    . GLU B  1 673  ? 12.303  26.060  78.361  1.00 21.38 ? 671  GLU B CA    1 
ATOM   13625 C C     . GLU B  1 673  ? 11.388  25.891  77.155  1.00 18.87 ? 671  GLU B C     1 
ATOM   13626 O O     . GLU B  1 673  ? 11.110  26.854  76.435  1.00 21.24 ? 671  GLU B O     1 
ATOM   13627 C CB    . GLU B  1 673  ? 13.624  25.351  78.115  1.00 20.73 ? 671  GLU B CB    1 
ATOM   13628 C CG    . GLU B  1 673  ? 14.292  25.770  76.832  1.00 27.05 ? 671  GLU B CG    1 
ATOM   13629 C CD    . GLU B  1 673  ? 15.506  26.629  77.074  1.00 24.33 ? 671  GLU B CD    1 
ATOM   13630 O OE1   . GLU B  1 673  ? 16.082  26.541  78.186  1.00 34.04 ? 671  GLU B OE1   1 
ATOM   13631 O OE2   . GLU B  1 673  ? 15.907  27.362  76.149  1.00 20.53 ? 671  GLU B OE2   1 
ATOM   13632 N N     . VAL B  1 674  ? 10.912  24.667  76.925  1.00 17.54 ? 672  VAL B N     1 
ATOM   13633 C CA    . VAL B  1 674  ? 10.037  24.415  75.779  1.00 18.11 ? 672  VAL B CA    1 
ATOM   13634 C C     . VAL B  1 674  ? 8.732   25.201  75.911  1.00 16.21 ? 672  VAL B C     1 
ATOM   13635 O O     . VAL B  1 674  ? 8.212   25.734  74.920  1.00 17.52 ? 672  VAL B O     1 
ATOM   13636 C CB    . VAL B  1 674  ? 9.776   22.901  75.619  1.00 18.87 ? 672  VAL B CB    1 
ATOM   13637 C CG1   . VAL B  1 674  ? 8.934   22.627  74.396  1.00 19.55 ? 672  VAL B CG1   1 
ATOM   13638 C CG2   . VAL B  1 674  ? 11.073  22.140  75.525  1.00 22.95 ? 672  VAL B CG2   1 
ATOM   13639 N N     . ARG B  1 675  ? 8.161   25.261  77.122  1.00 16.87 ? 673  ARG B N     1 
ATOM   13640 C CA    . ARG B  1 675  ? 6.928   26.028  77.304  1.00 20.93 ? 673  ARG B CA    1 
ATOM   13641 C C     . ARG B  1 675  ? 7.139   27.497  76.975  1.00 19.37 ? 673  ARG B C     1 
ATOM   13642 O O     . ARG B  1 675  ? 6.267   28.133  76.371  1.00 16.69 ? 673  ARG B O     1 
ATOM   13643 C CB    . ARG B  1 675  ? 6.405   25.900  78.738  1.00 18.63 ? 673  ARG B CB    1 
ATOM   13644 C CG    . ARG B  1 675  ? 5.768   24.574  79.110  1.00 19.76 ? 673  ARG B CG    1 
ATOM   13645 C CD    . ARG B  1 675  ? 5.052   24.693  80.474  1.00 19.42 ? 673  ARG B CD    1 
ATOM   13646 N NE    . ARG B  1 675  ? 3.912   25.605  80.410  1.00 21.30 ? 673  ARG B NE    1 
ATOM   13647 C CZ    . ARG B  1 675  ? 3.370   26.200  81.466  1.00 22.12 ? 673  ARG B CZ    1 
ATOM   13648 N NH1   . ARG B  1 675  ? 3.874   26.046  82.689  1.00 20.59 ? 673  ARG B NH1   1 
ATOM   13649 N NH2   . ARG B  1 675  ? 2.316   26.982  81.293  1.00 22.96 ? 673  ARG B NH2   1 
ATOM   13650 N N     . GLU B  1 676  ? 8.257   28.071  77.434  1.00 17.53 ? 674  GLU B N     1 
ATOM   13651 C CA    . GLU B  1 676  ? 8.554   29.468  77.121  1.00 20.06 ? 674  GLU B CA    1 
ATOM   13652 C C     . GLU B  1 676  ? 8.683   29.687  75.618  1.00 19.09 ? 674  GLU B C     1 
ATOM   13653 O O     . GLU B  1 676  ? 8.179   30.683  75.089  1.00 17.44 ? 674  GLU B O     1 
ATOM   13654 C CB    . GLU B  1 676  ? 9.835   29.926  77.831  1.00 19.61 ? 674  GLU B CB    1 
ATOM   13655 C CG    . GLU B  1 676  ? 10.097  31.418  77.628  1.00 23.44 ? 674  GLU B CG    1 
ATOM   13656 C CD    . GLU B  1 676  ? 11.174  31.998  78.551  1.00 35.43 ? 674  GLU B CD    1 
ATOM   13657 O OE1   . GLU B  1 676  ? 12.024  31.235  79.057  1.00 33.55 ? 674  GLU B OE1   1 
ATOM   13658 O OE2   . GLU B  1 676  ? 11.154  33.230  78.774  1.00 40.58 ? 674  GLU B OE2   1 
ATOM   13659 N N     . ALA B  1 677  ? 9.342   28.760  74.908  1.00 18.03 ? 675  ALA B N     1 
ATOM   13660 C CA    . ALA B  1 677  ? 9.420   28.878  73.455  1.00 20.05 ? 675  ALA B CA    1 
ATOM   13661 C C     . ALA B  1 677  ? 8.026   28.883  72.830  1.00 18.31 ? 675  ALA B C     1 
ATOM   13662 O O     . ALA B  1 677  ? 7.734   29.708  71.958  1.00 18.67 ? 675  ALA B O     1 
ATOM   13663 C CB    . ALA B  1 677  ? 10.268  27.746  72.877  1.00 17.23 ? 675  ALA B CB    1 
ATOM   13664 N N     . ILE B  1 678  ? 7.157   27.962  73.269  1.00 20.22 ? 676  ILE B N     1 
ATOM   13665 C CA    . ILE B  1 678  ? 5.762   27.920  72.797  1.00 15.66 ? 676  ILE B CA    1 
ATOM   13666 C C     . ILE B  1 678  ? 5.055   29.231  73.119  1.00 16.92 ? 676  ILE B C     1 
ATOM   13667 O O     . ILE B  1 678  ? 4.298   29.755  72.300  1.00 19.58 ? 676  ILE B O     1 
ATOM   13668 C CB    . ILE B  1 678  ? 5.018   26.731  73.434  1.00 16.71 ? 676  ILE B CB    1 
ATOM   13669 C CG1   . ILE B  1 678  ? 5.549   25.401  72.906  1.00 18.45 ? 676  ILE B CG1   1 
ATOM   13670 C CG2   . ILE B  1 678  ? 3.496   26.857  73.248  1.00 16.24 ? 676  ILE B CG2   1 
ATOM   13671 C CD1   . ILE B  1 678  ? 5.325   24.266  73.828  1.00 19.48 ? 676  ILE B CD1   1 
ATOM   13672 N N     . ASP B  1 679  ? 5.278   29.774  74.323  1.00 19.28 ? 677  ASP B N     1 
ATOM   13673 C CA    . ASP B  1 679  ? 4.605   31.018  74.697  1.00 19.23 ? 677  ASP B CA    1 
ATOM   13674 C C     . ASP B  1 679  ? 5.074   32.192  73.840  1.00 16.49 ? 677  ASP B C     1 
ATOM   13675 O O     . ASP B  1 679  ? 4.258   33.027  73.437  1.00 19.03 ? 677  ASP B O     1 
ATOM   13676 C CB    . ASP B  1 679  ? 4.832   31.346  76.179  1.00 17.56 ? 677  ASP B CB    1 
ATOM   13677 C CG    . ASP B  1 679  ? 4.107   30.384  77.128  1.00 22.61 ? 677  ASP B CG    1 
ATOM   13678 O OD1   . ASP B  1 679  ? 3.098   29.779  76.727  1.00 22.99 ? 677  ASP B OD1   1 
ATOM   13679 O OD2   . ASP B  1 679  ? 4.560   30.238  78.285  1.00 24.49 ? 677  ASP B OD2   1 
ATOM   13680 N N     . PHE B  1 680  ? 6.386   32.300  73.596  1.00 15.65 ? 678  PHE B N     1 
ATOM   13681 C CA    . PHE B  1 680  ? 6.903   33.333  72.700  1.00 17.58 ? 678  PHE B CA    1 
ATOM   13682 C C     . PHE B  1 680  ? 6.221   33.259  71.347  1.00 16.38 ? 678  PHE B C     1 
ATOM   13683 O O     . PHE B  1 680  ? 5.761   34.271  70.808  1.00 14.77 ? 678  PHE B O     1 
ATOM   13684 C CB    . PHE B  1 680  ? 8.410   33.168  72.503  1.00 15.81 ? 678  PHE B CB    1 
ATOM   13685 C CG    . PHE B  1 680  ? 9.247   33.834  73.565  1.00 16.02 ? 678  PHE B CG    1 
ATOM   13686 C CD1   . PHE B  1 680  ? 9.006   35.153  73.925  1.00 15.29 ? 678  PHE B CD1   1 
ATOM   13687 C CD2   . PHE B  1 680  ? 10.292  33.156  74.159  1.00 18.30 ? 678  PHE B CD2   1 
ATOM   13688 C CE1   . PHE B  1 680  ? 9.815   35.788  74.889  1.00 16.64 ? 678  PHE B CE1   1 
ATOM   13689 C CE2   . PHE B  1 680  ? 11.093  33.775  75.118  1.00 20.20 ? 678  PHE B CE2   1 
ATOM   13690 C CZ    . PHE B  1 680  ? 10.836  35.091  75.487  1.00 17.60 ? 678  PHE B CZ    1 
ATOM   13691 N N     . LEU B  1 681  ? 6.177   32.056  70.778  1.00 17.59 ? 679  LEU B N     1 
ATOM   13692 C CA    . LEU B  1 681  ? 5.584   31.874  69.459  1.00 14.66 ? 679  LEU B CA    1 
ATOM   13693 C C     . LEU B  1 681  ? 4.134   32.351  69.434  1.00 18.46 ? 679  LEU B C     1 
ATOM   13694 O O     . LEU B  1 681  ? 3.726   33.098  68.532  1.00 19.09 ? 679  LEU B O     1 
ATOM   13695 C CB    . LEU B  1 681  ? 5.672   30.397  69.057  1.00 19.56 ? 679  LEU B CB    1 
ATOM   13696 C CG    . LEU B  1 681  ? 7.061   29.875  68.722  1.00 20.03 ? 679  LEU B CG    1 
ATOM   13697 C CD1   . LEU B  1 681  ? 7.115   28.337  68.709  1.00 16.47 ? 679  LEU B CD1   1 
ATOM   13698 C CD2   . LEU B  1 681  ? 7.498   30.445  67.391  1.00 14.49 ? 679  LEU B CD2   1 
ATOM   13699 N N     . ARG B  1 682  ? 3.333   31.899  70.401  1.00 14.26 ? 680  ARG B N     1 
ATOM   13700 C CA    . ARG B  1 682  ? 1.918   32.247  70.429  1.00 18.74 ? 680  ARG B CA    1 
ATOM   13701 C C     . ARG B  1 682  ? 1.703   33.701  70.809  1.00 17.67 ? 680  ARG B C     1 
ATOM   13702 O O     . ARG B  1 682  ? 0.731   34.319  70.366  1.00 16.35 ? 680  ARG B O     1 
ATOM   13703 C CB    . ARG B  1 682  ? 1.168   31.335  71.400  1.00 15.08 ? 680  ARG B CB    1 
ATOM   13704 C CG    . ARG B  1 682  ? 1.048   29.920  70.878  1.00 18.48 ? 680  ARG B CG    1 
ATOM   13705 C CD    . ARG B  1 682  ? 0.421   29.019  71.879  1.00 17.46 ? 680  ARG B CD    1 
ATOM   13706 N NE    . ARG B  1 682  ? 0.227   27.680  71.347  1.00 19.39 ? 680  ARG B NE    1 
ATOM   13707 C CZ    . ARG B  1 682  ? -0.019  26.619  72.099  1.00 20.88 ? 680  ARG B CZ    1 
ATOM   13708 N NH1   . ARG B  1 682  ? -0.059  26.705  73.416  1.00 21.48 ? 680  ARG B NH1   1 
ATOM   13709 N NH2   . ARG B  1 682  ? -0.183  25.437  71.514  1.00 22.26 ? 680  ARG B NH2   1 
ATOM   13710 N N     . TYR B  1 683  ? 2.571   34.257  71.640  1.00 16.86 ? 681  TYR B N     1 
ATOM   13711 C CA    . TYR B  1 683  ? 2.373   35.637  72.066  1.00 18.39 ? 681  TYR B CA    1 
ATOM   13712 C C     . TYR B  1 683  ? 2.687   36.612  70.941  1.00 15.50 ? 681  TYR B C     1 
ATOM   13713 O O     . TYR B  1 683  ? 1.913   37.539  70.675  1.00 18.60 ? 681  TYR B O     1 
ATOM   13714 C CB    . TYR B  1 683  ? 3.251   35.926  73.278  1.00 15.44 ? 681  TYR B CB    1 
ATOM   13715 C CG    . TYR B  1 683  ? 3.218   37.378  73.717  1.00 17.88 ? 681  TYR B CG    1 
ATOM   13716 C CD1   . TYR B  1 683  ? 2.173   37.851  74.504  1.00 18.25 ? 681  TYR B CD1   1 
ATOM   13717 C CD2   . TYR B  1 683  ? 4.251   38.260  73.380  1.00 15.69 ? 681  TYR B CD2   1 
ATOM   13718 C CE1   . TYR B  1 683  ? 2.113   39.173  74.890  1.00 16.99 ? 681  TYR B CE1   1 
ATOM   13719 C CE2   . TYR B  1 683  ? 4.202   39.581  73.764  1.00 17.16 ? 681  TYR B CE2   1 
ATOM   13720 C CZ    . TYR B  1 683  ? 3.129   40.030  74.528  1.00 16.27 ? 681  TYR B CZ    1 
ATOM   13721 O OH    . TYR B  1 683  ? 3.045   41.352  74.934  1.00 18.83 ? 681  TYR B OH    1 
ATOM   13722 N N     . TYR B  1 684  ? 3.834   36.429  70.280  1.00 14.12 ? 682  TYR B N     1 
ATOM   13723 C CA    . TYR B  1 684  ? 4.192   37.311  69.176  1.00 17.98 ? 682  TYR B CA    1 
ATOM   13724 C C     . TYR B  1 684  ? 3.233   37.115  68.011  1.00 17.99 ? 682  TYR B C     1 
ATOM   13725 O O     . TYR B  1 684  ? 2.981   38.053  67.256  1.00 19.08 ? 682  TYR B O     1 
ATOM   13726 C CB    . TYR B  1 684  ? 5.637   37.083  68.727  1.00 16.48 ? 682  TYR B CB    1 
ATOM   13727 C CG    . TYR B  1 684  ? 6.681   37.450  69.779  1.00 14.44 ? 682  TYR B CG    1 
ATOM   13728 C CD1   . TYR B  1 684  ? 6.551   38.613  70.513  1.00 15.84 ? 682  TYR B CD1   1 
ATOM   13729 C CD2   . TYR B  1 684  ? 7.764   36.628  70.023  1.00 15.39 ? 682  TYR B CD2   1 
ATOM   13730 C CE1   . TYR B  1 684  ? 7.469   38.937  71.497  1.00 18.15 ? 682  TYR B CE1   1 
ATOM   13731 C CE2   . TYR B  1 684  ? 8.713   36.948  70.997  1.00 16.98 ? 682  TYR B CE2   1 
ATOM   13732 C CZ    . TYR B  1 684  ? 8.543   38.120  71.719  1.00 17.46 ? 682  TYR B CZ    1 
ATOM   13733 O OH    . TYR B  1 684  ? 9.434   38.483  72.717  1.00 17.18 ? 682  TYR B OH    1 
ATOM   13734 N N     . ALA B  1 685  ? 2.668   35.919  67.874  1.00 14.89 ? 683  ALA B N     1 
ATOM   13735 C CA    . ALA B  1 685  ? 1.618   35.711  66.877  1.00 18.58 ? 683  ALA B CA    1 
ATOM   13736 C C     . ALA B  1 685  ? 0.382   36.548  67.194  1.00 19.41 ? 683  ALA B C     1 
ATOM   13737 O O     . ALA B  1 685  ? -0.168  37.233  66.317  1.00 18.82 ? 683  ALA B O     1 
ATOM   13738 C CB    . ALA B  1 685  ? 1.263   34.223  66.797  1.00 18.07 ? 683  ALA B CB    1 
ATOM   13739 N N     . GLU B  1 686  ? -0.077  36.510  68.448  1.00 16.34 ? 684  GLU B N     1 
ATOM   13740 C CA    . GLU B  1 686  ? -1.252  37.294  68.817  1.00 20.15 ? 684  GLU B CA    1 
ATOM   13741 C C     . GLU B  1 686  ? -0.962  38.792  68.761  1.00 21.11 ? 684  GLU B C     1 
ATOM   13742 O O     . GLU B  1 686  ? -1.777  39.561  68.250  1.00 19.45 ? 684  GLU B O     1 
ATOM   13743 C CB    . GLU B  1 686  ? -1.746  36.890  70.202  1.00 21.18 ? 684  GLU B CB    1 
ATOM   13744 C CG    . GLU B  1 686  ? -2.879  37.787  70.749  1.00 23.27 ? 684  GLU B CG    1 
ATOM   13745 C CD    . GLU B  1 686  ? -4.155  37.741  69.901  1.00 29.95 ? 684  GLU B CD    1 
ATOM   13746 O OE1   . GLU B  1 686  ? -4.337  36.800  69.083  1.00 28.11 ? 684  GLU B OE1   1 
ATOM   13747 O OE2   . GLU B  1 686  ? -4.990  38.658  70.068  1.00 31.08 ? 684  GLU B OE2   1 
ATOM   13748 N N     . GLN B  1 687  ? 0.220   39.224  69.220  1.00 16.86 ? 685  GLN B N     1 
ATOM   13749 C CA    . GLN B  1 687  ? 0.537   40.654  69.153  1.00 17.90 ? 685  GLN B CA    1 
ATOM   13750 C C     . GLN B  1 687  ? 0.581   41.148  67.709  1.00 23.41 ? 685  GLN B C     1 
ATOM   13751 O O     . GLN B  1 687  ? 0.216   42.297  67.424  1.00 19.92 ? 685  GLN B O     1 
ATOM   13752 C CB    . GLN B  1 687  ? 1.863   40.939  69.850  1.00 19.88 ? 685  GLN B CB    1 
ATOM   13753 C CG    . GLN B  1 687  ? 1.776   40.723  71.345  1.00 18.58 ? 685  GLN B CG    1 
ATOM   13754 C CD    . GLN B  1 687  ? 0.744   41.606  71.993  1.00 20.92 ? 685  GLN B CD    1 
ATOM   13755 O OE1   . GLN B  1 687  ? 0.802   42.831  71.885  1.00 22.00 ? 685  GLN B OE1   1 
ATOM   13756 N NE2   . GLN B  1 687  ? -0.222  40.989  72.660  1.00 25.34 ? 685  GLN B NE2   1 
ATOM   13757 N N     . THR B  1 688  ? 1.034   40.293  66.790  1.00 18.78 ? 686  THR B N     1 
ATOM   13758 C CA    . THR B  1 688  ? 0.983   40.618  65.364  1.00 20.14 ? 686  THR B CA    1 
ATOM   13759 C C     . THR B  1 688  ? -0.457  40.762  64.879  1.00 20.25 ? 686  THR B C     1 
ATOM   13760 O O     . THR B  1 688  ? -0.799  41.738  64.197  1.00 21.41 ? 686  THR B O     1 
ATOM   13761 C CB    . THR B  1 688  ? 1.713   39.535  64.554  1.00 16.44 ? 686  THR B CB    1 
ATOM   13762 O OG1   . THR B  1 688  ? 3.109   39.560  64.856  1.00 20.35 ? 686  THR B OG1   1 
ATOM   13763 C CG2   . THR B  1 688  ? 1.510   39.744  63.035  1.00 17.50 ? 686  THR B CG2   1 
ATOM   13764 N N     . ARG B  1 689  ? -1.315  39.787  65.197  1.00 18.21 ? 687  ARG B N     1 
ATOM   13765 C CA    . ARG B  1 689  ? -2.721  39.876  64.784  1.00 21.62 ? 687  ARG B CA    1 
ATOM   13766 C C     . ARG B  1 689  ? -3.394  41.127  65.347  1.00 22.91 ? 687  ARG B C     1 
ATOM   13767 O O     . ARG B  1 689  ? -4.340  41.644  64.751  1.00 22.11 ? 687  ARG B O     1 
ATOM   13768 C CB    . ARG B  1 689  ? -3.497  38.631  65.229  1.00 20.88 ? 687  ARG B CB    1 
ATOM   13769 C CG    . ARG B  1 689  ? -3.245  37.384  64.387  1.00 22.30 ? 687  ARG B CG    1 
ATOM   13770 C CD    . ARG B  1 689  ? -4.159  36.254  64.827  1.00 24.88 ? 687  ARG B CD    1 
ATOM   13771 N NE    . ARG B  1 689  ? -3.935  35.867  66.215  1.00 24.75 ? 687  ARG B NE    1 
ATOM   13772 C CZ    . ARG B  1 689  ? -3.149  34.869  66.591  1.00 25.62 ? 687  ARG B CZ    1 
ATOM   13773 N NH1   . ARG B  1 689  ? -2.482  34.151  65.705  1.00 25.63 ? 687  ARG B NH1   1 
ATOM   13774 N NH2   . ARG B  1 689  ? -3.028  34.588  67.890  1.00 23.26 ? 687  ARG B NH2   1 
ATOM   13775 N N     . ARG B  1 690  ? -2.908  41.644  66.476  1.00 19.11 ? 688  ARG B N     1 
ATOM   13776 C CA    . ARG B  1 690  ? -3.496  42.850  67.048  1.00 19.92 ? 688  ARG B CA    1 
ATOM   13777 C C     . ARG B  1 690  ? -2.962  44.140  66.434  1.00 20.36 ? 688  ARG B C     1 
ATOM   13778 O O     . ARG B  1 690  ? -3.582  45.196  66.623  1.00 22.42 ? 688  ARG B O     1 
ATOM   13779 C CB    . ARG B  1 690  ? -3.237  42.908  68.554  1.00 19.49 ? 688  ARG B CB    1 
ATOM   13780 C CG    . ARG B  1 690  ? -3.889  41.800  69.360  1.00 23.44 ? 688  ARG B CG    1 
ATOM   13781 C CD    . ARG B  1 690  ? -5.389  42.048  69.517  1.00 25.43 ? 688  ARG B CD    1 
ATOM   13782 N NE    . ARG B  1 690  ? -5.648  43.298  70.228  1.00 27.91 ? 688  ARG B NE    1 
ATOM   13783 C CZ    . ARG B  1 690  ? -6.226  44.360  69.682  1.00 30.37 ? 688  ARG B CZ    1 
ATOM   13784 N NH1   . ARG B  1 690  ? -6.678  44.336  68.433  1.00 28.43 ? 688  ARG B NH1   1 
ATOM   13785 N NH2   . ARG B  1 690  ? -6.365  45.468  70.408  1.00 23.13 ? 688  ARG B NH2   1 
ATOM   13786 N N     . THR B  1 691  ? -1.819  44.103  65.748  1.00 21.45 ? 689  THR B N     1 
ATOM   13787 C CA    . THR B  1 691  ? -1.176  45.383  65.465  1.00 21.38 ? 689  THR B CA    1 
ATOM   13788 C C     . THR B  1 691  ? -0.729  45.586  64.023  1.00 25.87 ? 689  THR B C     1 
ATOM   13789 O O     . THR B  1 691  ? -0.851  46.704  63.520  1.00 26.80 ? 689  THR B O     1 
ATOM   13790 C CB    . THR B  1 691  ? 0.051   45.580  66.383  1.00 24.44 ? 689  THR B CB    1 
ATOM   13791 O OG1   . THR B  1 691  ? 0.964   44.485  66.212  1.00 21.90 ? 689  THR B OG1   1 
ATOM   13792 C CG2   . THR B  1 691  ? -0.391  45.668  67.846  1.00 22.07 ? 689  THR B CG2   1 
ATOM   13793 N N     . LEU B  1 692  ? -0.172  44.573  63.361  1.00 21.23 ? 690  LEU B N     1 
ATOM   13794 C CA    . LEU B  1 692  ? 0.659   44.859  62.193  1.00 21.86 ? 690  LEU B CA    1 
ATOM   13795 C C     . LEU B  1 692  ? -0.173  45.053  60.929  1.00 23.13 ? 690  LEU B C     1 
ATOM   13796 O O     . LEU B  1 692  ? -1.085  44.271  60.637  1.00 25.05 ? 690  LEU B O     1 
ATOM   13797 C CB    . LEU B  1 692  ? 1.709   43.766  61.982  1.00 21.98 ? 690  LEU B CB    1 
ATOM   13798 C CG    . LEU B  1 692  ? 2.851   43.774  63.016  1.00 22.21 ? 690  LEU B CG    1 
ATOM   13799 C CD1   . LEU B  1 692  ? 3.997   42.851  62.577  1.00 24.68 ? 690  LEU B CD1   1 
ATOM   13800 C CD2   . LEU B  1 692  ? 3.371   45.174  63.258  1.00 26.00 ? 690  LEU B CD2   1 
ATOM   13801 N N     . GLY B  1 693  ? 0.153   46.111  60.193  1.00 23.63 ? 691  GLY B N     1 
ATOM   13802 C CA    . GLY B  1 693  ? -0.527  46.460  58.967  1.00 24.01 ? 691  GLY B CA    1 
ATOM   13803 C C     . GLY B  1 693  ? 0.466   46.733  57.858  1.00 29.49 ? 691  GLY B C     1 
ATOM   13804 O O     . GLY B  1 693  ? 1.683   46.661  58.052  1.00 28.22 ? 691  GLY B O     1 
ATOM   13805 N N     . PRO B  1 694  ? -0.038  47.051  56.662  1.00 34.93 ? 692  PRO B N     1 
ATOM   13806 C CA    . PRO B  1 694  ? 0.870   47.311  55.534  1.00 32.37 ? 692  PRO B CA    1 
ATOM   13807 C C     . PRO B  1 694  ? 1.836   48.454  55.783  1.00 36.59 ? 692  PRO B C     1 
ATOM   13808 O O     . PRO B  1 694  ? 2.941   48.454  55.224  1.00 41.96 ? 692  PRO B O     1 
ATOM   13809 C CB    . PRO B  1 694  ? -0.092  47.629  54.379  1.00 34.79 ? 692  PRO B CB    1 
ATOM   13810 C CG    . PRO B  1 694  ? -1.401  47.023  54.788  1.00 36.04 ? 692  PRO B CG    1 
ATOM   13811 C CD    . PRO B  1 694  ? -1.454  47.147  56.276  1.00 34.90 ? 692  PRO B CD    1 
ATOM   13812 N N     . GLY B  1 695  ? 1.465   49.429  56.608  1.00 32.44 ? 693  GLY B N     1 
ATOM   13813 C CA    . GLY B  1 695  ? 2.351   50.541  56.857  1.00 30.32 ? 693  GLY B CA    1 
ATOM   13814 C C     . GLY B  1 695  ? 3.455   50.278  57.842  1.00 33.81 ? 693  GLY B C     1 
ATOM   13815 O O     . GLY B  1 695  ? 4.280   51.165  58.084  1.00 30.38 ? 693  GLY B O     1 
ATOM   13816 N N     . HIS B  1 696  ? 3.491   49.082  58.432  1.00 30.39 ? 694  HIS B N     1 
ATOM   13817 C CA    . HIS B  1 696  ? 4.512   48.732  59.412  1.00 29.94 ? 694  HIS B CA    1 
ATOM   13818 C C     . HIS B  1 696  ? 5.561   47.888  58.692  1.00 30.95 ? 694  HIS B C     1 
ATOM   13819 O O     . HIS B  1 696  ? 5.620   46.662  58.808  1.00 30.81 ? 694  HIS B O     1 
ATOM   13820 C CB    . HIS B  1 696  ? 3.879   48.034  60.608  1.00 25.96 ? 694  HIS B CB    1 
ATOM   13821 C CG    . HIS B  1 696  ? 2.769   48.825  61.232  1.00 26.52 ? 694  HIS B CG    1 
ATOM   13822 N ND1   . HIS B  1 696  ? 1.460   48.393  61.253  1.00 24.51 ? 694  HIS B ND1   1 
ATOM   13823 C CD2   . HIS B  1 696  ? 2.768   50.047  61.813  1.00 25.60 ? 694  HIS B CD2   1 
ATOM   13824 C CE1   . HIS B  1 696  ? 0.706   49.298  61.848  1.00 26.09 ? 694  HIS B CE1   1 
ATOM   13825 N NE2   . HIS B  1 696  ? 1.476   50.311  62.201  1.00 26.79 ? 694  HIS B NE2   1 
ATOM   13826 N N     . GLY B  1 697  ? 6.396   48.581  57.923  1.00 32.09 ? 695  GLY B N     1 
ATOM   13827 C CA    . GLY B  1 697  ? 7.353   47.945  57.049  1.00 30.69 ? 695  GLY B CA    1 
ATOM   13828 C C     . GLY B  1 697  ? 8.471   47.257  57.800  1.00 25.08 ? 695  GLY B C     1 
ATOM   13829 O O     . GLY B  1 697  ? 8.904   47.697  58.863  1.00 25.26 ? 695  GLY B O     1 
ATOM   13830 N N     . PRO B  1 698  ? 8.969   46.161  57.254  1.00 26.63 ? 696  PRO B N     1 
ATOM   13831 C CA    . PRO B  1 698  ? 10.049  45.430  57.925  1.00 25.85 ? 696  PRO B CA    1 
ATOM   13832 C C     . PRO B  1 698  ? 11.372  46.164  57.804  1.00 24.99 ? 696  PRO B C     1 
ATOM   13833 O O     . PRO B  1 698  ? 11.577  47.006  56.930  1.00 25.84 ? 696  PRO B O     1 
ATOM   13834 C CB    . PRO B  1 698  ? 10.096  44.088  57.185  1.00 28.05 ? 696  PRO B CB    1 
ATOM   13835 C CG    . PRO B  1 698  ? 8.842   44.052  56.353  1.00 33.85 ? 696  PRO B CG    1 
ATOM   13836 C CD    . PRO B  1 698  ? 8.496   45.473  56.046  1.00 28.28 ? 696  PRO B CD    1 
ATOM   13837 N N     . LEU B  1 699  ? 12.277  45.841  58.725  1.00 24.58 ? 697  LEU B N     1 
ATOM   13838 C CA    . LEU B  1 699  ? 13.631  46.382  58.651  1.00 25.81 ? 697  LEU B CA    1 
ATOM   13839 C C     . LEU B  1 699  ? 14.419  45.746  57.512  1.00 25.20 ? 697  LEU B C     1 
ATOM   13840 O O     . LEU B  1 699  ? 15.147  46.436  56.790  1.00 24.23 ? 697  LEU B O     1 
ATOM   13841 C CB    . LEU B  1 699  ? 14.354  46.150  59.972  1.00 24.85 ? 697  LEU B CB    1 
ATOM   13842 C CG    . LEU B  1 699  ? 13.734  46.772  61.227  1.00 24.89 ? 697  LEU B CG    1 
ATOM   13843 C CD1   . LEU B  1 699  ? 14.610  46.416  62.418  1.00 26.98 ? 697  LEU B CD1   1 
ATOM   13844 C CD2   . LEU B  1 699  ? 13.631  48.280  61.059  1.00 29.49 ? 697  LEU B CD2   1 
ATOM   13845 N N     . GLY B  1 700  ? 14.290  44.432  57.343  1.00 22.40 ? 698  GLY B N     1 
ATOM   13846 C CA    . GLY B  1 700  ? 15.145  43.679  56.458  1.00 23.52 ? 698  GLY B CA    1 
ATOM   13847 C C     . GLY B  1 700  ? 15.776  42.523  57.209  1.00 24.97 ? 698  GLY B C     1 
ATOM   13848 O O     . GLY B  1 700  ? 15.282  42.110  58.260  1.00 20.97 ? 698  GLY B O     1 
ATOM   13849 N N     . PRO B  1 701  ? 16.875  41.979  56.689  1.00 24.47 ? 699  PRO B N     1 
ATOM   13850 C CA    . PRO B  1 701  ? 17.511  40.821  57.339  1.00 24.07 ? 699  PRO B CA    1 
ATOM   13851 C C     . PRO B  1 701  ? 17.922  41.134  58.769  1.00 23.05 ? 699  PRO B C     1 
ATOM   13852 O O     . PRO B  1 701  ? 18.593  42.124  59.032  1.00 21.81 ? 699  PRO B O     1 
ATOM   13853 C CB    . PRO B  1 701  ? 18.732  40.549  56.455  1.00 24.76 ? 699  PRO B CB    1 
ATOM   13854 C CG    . PRO B  1 701  ? 18.352  41.124  55.119  1.00 23.68 ? 699  PRO B CG    1 
ATOM   13855 C CD    . PRO B  1 701  ? 17.573  42.361  55.445  1.00 25.60 ? 699  PRO B CD    1 
ATOM   13856 N N     . ILE B  1 702  ? 17.508  40.284  59.701  1.00 22.38 ? 700  ILE B N     1 
ATOM   13857 C CA    A ILE B  1 702  ? 17.822  40.466  61.113  0.44 19.83 ? 700  ILE B CA    1 
ATOM   13858 C CA    B ILE B  1 702  ? 17.813  40.463  61.119  0.56 19.85 ? 700  ILE B CA    1 
ATOM   13859 C C     . ILE B  1 702  ? 18.743  39.344  61.556  1.00 21.58 ? 700  ILE B C     1 
ATOM   13860 O O     . ILE B  1 702  ? 18.445  38.161  61.345  1.00 22.89 ? 700  ILE B O     1 
ATOM   13861 C CB    A ILE B  1 702  ? 16.555  40.516  61.980  0.44 20.16 ? 700  ILE B CB    1 
ATOM   13862 C CB    B ILE B  1 702  ? 16.545  40.479  61.994  0.56 20.15 ? 700  ILE B CB    1 
ATOM   13863 C CG1   A ILE B  1 702  ? 15.807  41.825  61.727  0.44 22.10 ? 700  ILE B CG1   1 
ATOM   13864 C CG1   B ILE B  1 702  ? 15.606  41.628  61.605  0.56 22.20 ? 700  ILE B CG1   1 
ATOM   13865 C CG2   A ILE B  1 702  ? 16.914  40.360  63.468  0.44 19.88 ? 700  ILE B CG2   1 
ATOM   13866 C CG2   B ILE B  1 702  ? 16.928  40.553  63.489  0.56 19.83 ? 700  ILE B CG2   1 
ATOM   13867 C CD1   A ILE B  1 702  ? 14.679  42.059  62.671  0.44 18.37 ? 700  ILE B CD1   1 
ATOM   13868 C CD1   B ILE B  1 702  ? 16.207  43.009  61.721  0.56 21.04 ? 700  ILE B CD1   1 
ATOM   13869 N N     . VAL B  1 703  ? 19.851  39.719  62.178  1.00 20.26 ? 701  VAL B N     1 
ATOM   13870 C CA    . VAL B  1 703  ? 20.788  38.775  62.768  1.00 19.26 ? 701  VAL B CA    1 
ATOM   13871 C C     . VAL B  1 703  ? 20.342  38.527  64.205  1.00 21.65 ? 701  VAL B C     1 
ATOM   13872 O O     . VAL B  1 703  ? 20.225  39.469  64.994  1.00 20.88 ? 701  VAL B O     1 
ATOM   13873 C CB    . VAL B  1 703  ? 22.220  39.321  62.716  1.00 25.43 ? 701  VAL B CB    1 
ATOM   13874 C CG1   . VAL B  1 703  ? 23.135  38.476  63.590  1.00 19.35 ? 701  VAL B CG1   1 
ATOM   13875 C CG2   . VAL B  1 703  ? 22.725  39.353  61.275  1.00 21.83 ? 701  VAL B CG2   1 
ATOM   13876 N N     . CYS B  1 704  ? 20.086  37.264  64.542  1.00 19.26 ? 702  CYS B N     1 
ATOM   13877 C CA    . CYS B  1 704  ? 19.604  36.874  65.864  1.00 19.37 ? 702  CYS B CA    1 
ATOM   13878 C C     . CYS B  1 704  ? 20.688  36.023  66.506  1.00 18.45 ? 702  CYS B C     1 
ATOM   13879 O O     . CYS B  1 704  ? 20.972  34.916  66.034  1.00 18.55 ? 702  CYS B O     1 
ATOM   13880 C CB    . CYS B  1 704  ? 18.288  36.101  65.778  1.00 18.46 ? 702  CYS B CB    1 
ATOM   13881 S SG    . CYS B  1 704  ? 16.846  37.031  65.202  1.00 21.52 ? 702  CYS B SG    1 
ATOM   13882 N N     . ILE B  1 705  ? 21.302  36.544  67.567  1.00 18.90 ? 703  ILE B N     1 
ATOM   13883 C CA    . ILE B  1 705  ? 22.416  35.886  68.254  1.00 19.41 ? 703  ILE B CA    1 
ATOM   13884 C C     . ILE B  1 705  ? 21.919  35.496  69.643  1.00 20.10 ? 703  ILE B C     1 
ATOM   13885 O O     . ILE B  1 705  ? 21.455  36.352  70.399  1.00 20.52 ? 703  ILE B O     1 
ATOM   13886 C CB    . ILE B  1 705  ? 23.649  36.799  68.338  1.00 19.52 ? 703  ILE B CB    1 
ATOM   13887 C CG1   . ILE B  1 705  ? 24.245  37.049  66.939  1.00 21.47 ? 703  ILE B CG1   1 
ATOM   13888 C CG2   . ILE B  1 705  ? 24.728  36.185  69.251  1.00 20.96 ? 703  ILE B CG2   1 
ATOM   13889 C CD1   . ILE B  1 705  ? 25.295  38.154  66.907  1.00 25.03 ? 703  ILE B CD1   1 
ATOM   13890 N N     . SER B  1 706  ? 21.971  34.207  69.964  1.00 20.27 ? 704  SER B N     1 
ATOM   13891 C CA    . SER B  1 706  ? 21.297  33.716  71.152  1.00 19.83 ? 704  SER B CA    1 
ATOM   13892 C C     . SER B  1 706  ? 22.283  33.027  72.089  1.00 21.02 ? 704  SER B C     1 
ATOM   13893 O O     . SER B  1 706  ? 23.366  32.594  71.669  1.00 21.44 ? 704  SER B O     1 
ATOM   13894 C CB    . SER B  1 706  ? 20.172  32.742  70.780  1.00 20.36 ? 704  SER B CB    1 
ATOM   13895 O OG    . SER B  1 706  ? 20.685  31.687  69.994  1.00 21.13 ? 704  SER B OG    1 
ATOM   13896 N N     . PRO B  1 707  ? 21.932  32.899  73.366  1.00 22.34 ? 705  PRO B N     1 
ATOM   13897 C CA    . PRO B  1 707  ? 22.877  32.345  74.339  1.00 20.86 ? 705  PRO B CA    1 
ATOM   13898 C C     . PRO B  1 707  ? 22.712  30.848  74.570  1.00 24.62 ? 705  PRO B C     1 
ATOM   13899 O O     . PRO B  1 707  ? 21.771  30.220  74.067  1.00 21.96 ? 705  PRO B O     1 
ATOM   13900 C CB    . PRO B  1 707  ? 22.546  33.142  75.606  1.00 21.42 ? 705  PRO B CB    1 
ATOM   13901 C CG    . PRO B  1 707  ? 21.087  33.327  75.545  1.00 20.23 ? 705  PRO B CG    1 
ATOM   13902 C CD    . PRO B  1 707  ? 20.737  33.445  74.040  1.00 23.10 ? 705  PRO B CD    1 
ATOM   13903 N N     . TRP B  1 708  ? 23.622  30.269  75.351  1.00 20.82 ? 706  TRP B N     1 
ATOM   13904 C CA    . TRP B  1 708  ? 23.607  28.835  75.622  1.00 22.91 ? 706  TRP B CA    1 
ATOM   13905 C C     . TRP B  1 708  ? 22.749  28.461  76.825  1.00 22.99 ? 706  TRP B C     1 
ATOM   13906 O O     . TRP B  1 708  ? 22.484  27.274  77.029  1.00 22.16 ? 706  TRP B O     1 
ATOM   13907 C CB    . TRP B  1 708  ? 25.044  28.318  75.835  1.00 21.31 ? 706  TRP B CB    1 
ATOM   13908 C CG    . TRP B  1 708  ? 25.801  29.173  76.828  1.00 24.35 ? 706  TRP B CG    1 
ATOM   13909 C CD1   . TRP B  1 708  ? 26.687  30.169  76.543  1.00 26.53 ? 706  TRP B CD1   1 
ATOM   13910 C CD2   . TRP B  1 708  ? 25.686  29.132  78.250  1.00 21.04 ? 706  TRP B CD2   1 
ATOM   13911 N NE1   . TRP B  1 708  ? 27.149  30.741  77.709  1.00 24.67 ? 706  TRP B NE1   1 
ATOM   13912 C CE2   . TRP B  1 708  ? 26.541  30.124  78.768  1.00 25.50 ? 706  TRP B CE2   1 
ATOM   13913 C CE3   . TRP B  1 708  ? 24.950  28.343  79.140  1.00 24.66 ? 706  TRP B CE3   1 
ATOM   13914 C CZ2   . TRP B  1 708  ? 26.676  30.352  80.142  1.00 25.64 ? 706  TRP B CZ2   1 
ATOM   13915 C CZ3   . TRP B  1 708  ? 25.085  28.564  80.495  1.00 24.38 ? 706  TRP B CZ3   1 
ATOM   13916 C CH2   . TRP B  1 708  ? 25.937  29.566  80.985  1.00 23.65 ? 706  TRP B CH2   1 
ATOM   13917 N N     . ASN B  1 709  ? 22.312  29.434  77.629  1.00 20.10 ? 707  ASN B N     1 
ATOM   13918 C CA    . ASN B  1 709  ? 21.602  29.139  78.869  1.00 23.24 ? 707  ASN B CA    1 
ATOM   13919 C C     . ASN B  1 709  ? 20.097  29.017  78.682  1.00 24.03 ? 707  ASN B C     1 
ATOM   13920 O O     . ASN B  1 709  ? 19.428  28.384  79.505  1.00 25.30 ? 707  ASN B O     1 
ATOM   13921 C CB    . ASN B  1 709  ? 21.923  30.209  79.923  1.00 22.28 ? 707  ASN B CB    1 
ATOM   13922 C CG    . ASN B  1 709  ? 21.426  31.590  79.528  1.00 27.26 ? 707  ASN B CG    1 
ATOM   13923 O OD1   . ASN B  1 709  ? 21.337  31.910  78.346  1.00 29.31 ? 707  ASN B OD1   1 
ATOM   13924 N ND2   . ASN B  1 709  ? 21.100  32.412  80.514  1.00 25.23 ? 707  ASN B ND2   1 
ATOM   13925 N N     . PHE B  1 710  ? 19.556  29.590  77.618  1.00 23.22 ? 708  PHE B N     1 
ATOM   13926 C CA    . PHE B  1 710  ? 18.180  29.349  77.192  1.00 24.42 ? 708  PHE B CA    1 
ATOM   13927 C C     . PHE B  1 710  ? 18.251  29.031  75.712  1.00 23.55 ? 708  PHE B C     1 
ATOM   13928 O O     . PHE B  1 710  ? 17.810  29.819  74.866  1.00 22.79 ? 708  PHE B O     1 
ATOM   13929 C CB    . PHE B  1 710  ? 17.277  30.547  77.485  1.00 26.43 ? 708  PHE B CB    1 
ATOM   13930 C CG    . PHE B  1 710  ? 17.046  30.761  78.946  1.00 28.71 ? 708  PHE B CG    1 
ATOM   13931 C CD1   . PHE B  1 710  ? 16.211  29.913  79.651  1.00 31.82 ? 708  PHE B CD1   1 
ATOM   13932 C CD2   . PHE B  1 710  ? 17.696  31.787  79.625  1.00 30.93 ? 708  PHE B CD2   1 
ATOM   13933 C CE1   . PHE B  1 710  ? 16.008  30.094  81.021  1.00 31.22 ? 708  PHE B CE1   1 
ATOM   13934 C CE2   . PHE B  1 710  ? 17.490  31.977  80.990  1.00 34.84 ? 708  PHE B CE2   1 
ATOM   13935 C CZ    . PHE B  1 710  ? 16.643  31.129  81.682  1.00 31.75 ? 708  PHE B CZ    1 
ATOM   13936 N N     . PRO B  1 711  ? 18.816  27.867  75.370  1.00 20.85 ? 709  PRO B N     1 
ATOM   13937 C CA    . PRO B  1 711  ? 19.183  27.596  73.981  1.00 20.42 ? 709  PRO B CA    1 
ATOM   13938 C C     . PRO B  1 711  ? 17.995  27.331  73.060  1.00 19.51 ? 709  PRO B C     1 
ATOM   13939 O O     . PRO B  1 711  ? 18.190  27.289  71.845  1.00 20.65 ? 709  PRO B O     1 
ATOM   13940 C CB    . PRO B  1 711  ? 20.080  26.357  74.103  1.00 18.83 ? 709  PRO B CB    1 
ATOM   13941 C CG    . PRO B  1 711  ? 19.531  25.627  75.283  1.00 21.76 ? 709  PRO B CG    1 
ATOM   13942 C CD    . PRO B  1 711  ? 19.186  26.746  76.263  1.00 20.89 ? 709  PRO B CD    1 
ATOM   13943 N N     . LEU B  1 712  ? 16.795  27.121  73.585  1.00 21.02 ? 710  LEU B N     1 
ATOM   13944 C CA    . LEU B  1 712  ? 15.604  27.097  72.739  1.00 20.16 ? 710  LEU B CA    1 
ATOM   13945 C C     . LEU B  1 712  ? 14.707  28.299  72.950  1.00 18.62 ? 710  LEU B C     1 
ATOM   13946 O O     . LEU B  1 712  ? 14.184  28.850  71.972  1.00 19.51 ? 710  LEU B O     1 
ATOM   13947 C CB    . LEU B  1 712  ? 14.775  25.829  72.983  1.00 17.89 ? 710  LEU B CB    1 
ATOM   13948 C CG    . LEU B  1 712  ? 13.551  25.679  72.058  1.00 19.29 ? 710  LEU B CG    1 
ATOM   13949 C CD1   . LEU B  1 712  ? 13.992  25.541  70.619  1.00 19.70 ? 710  LEU B CD1   1 
ATOM   13950 C CD2   . LEU B  1 712  ? 12.713  24.488  72.476  1.00 23.14 ? 710  LEU B CD2   1 
ATOM   13951 N N     . ALA B  1 713  ? 14.490  28.707  74.201  1.00 20.19 ? 711  ALA B N     1 
ATOM   13952 C CA    . ALA B  1 713  ? 13.469  29.714  74.465  1.00 20.75 ? 711  ALA B CA    1 
ATOM   13953 C C     . ALA B  1 713  ? 13.900  31.089  73.957  1.00 19.73 ? 711  ALA B C     1 
ATOM   13954 O O     . ALA B  1 713  ? 13.128  31.772  73.279  1.00 17.47 ? 711  ALA B O     1 
ATOM   13955 C CB    . ALA B  1 713  ? 13.132  29.763  75.957  1.00 20.78 ? 711  ALA B CB    1 
ATOM   13956 N N     . ILE B  1 714  ? 15.116  31.530  74.290  1.00 19.75 ? 712  ILE B N     1 
ATOM   13957 C CA    . ILE B  1 714  ? 15.528  32.851  73.812  1.00 18.03 ? 712  ILE B CA    1 
ATOM   13958 C C     . ILE B  1 714  ? 15.885  32.790  72.329  1.00 20.08 ? 712  ILE B C     1 
ATOM   13959 O O     . ILE B  1 714  ? 15.593  33.719  71.566  1.00 20.59 ? 712  ILE B O     1 
ATOM   13960 C CB    . ILE B  1 714  ? 16.683  33.391  74.675  1.00 22.44 ? 712  ILE B CB    1 
ATOM   13961 C CG1   . ILE B  1 714  ? 16.130  33.810  76.034  1.00 21.59 ? 712  ILE B CG1   1 
ATOM   13962 C CG2   . ILE B  1 714  ? 17.387  34.577  74.000  1.00 21.07 ? 712  ILE B CG2   1 
ATOM   13963 C CD1   . ILE B  1 714  ? 17.238  34.118  77.035  1.00 30.85 ? 712  ILE B CD1   1 
ATOM   13964 N N     . PHE B  1 715  ? 16.488  31.681  71.901  1.00 20.53 ? 713  PHE B N     1 
ATOM   13965 C CA    . PHE B  1 715  ? 16.653  31.408  70.481  1.00 19.09 ? 713  PHE B CA    1 
ATOM   13966 C C     . PHE B  1 715  ? 15.336  31.613  69.739  1.00 18.82 ? 713  PHE B C     1 
ATOM   13967 O O     . PHE B  1 715  ? 15.271  32.368  68.763  1.00 18.72 ? 713  PHE B O     1 
ATOM   13968 C CB    . PHE B  1 715  ? 17.167  29.976  70.305  1.00 20.17 ? 713  PHE B CB    1 
ATOM   13969 C CG    . PHE B  1 715  ? 17.360  29.566  68.880  1.00 19.15 ? 713  PHE B CG    1 
ATOM   13970 C CD1   . PHE B  1 715  ? 18.498  29.945  68.191  1.00 19.41 ? 713  PHE B CD1   1 
ATOM   13971 C CD2   . PHE B  1 715  ? 16.400  28.808  68.224  1.00 25.12 ? 713  PHE B CD2   1 
ATOM   13972 C CE1   . PHE B  1 715  ? 18.692  29.570  66.873  1.00 25.21 ? 713  PHE B CE1   1 
ATOM   13973 C CE2   . PHE B  1 715  ? 16.583  28.425  66.892  1.00 20.00 ? 713  PHE B CE2   1 
ATOM   13974 C CZ    . PHE B  1 715  ? 17.727  28.805  66.222  1.00 21.19 ? 713  PHE B CZ    1 
ATOM   13975 N N     . THR B  1 716  ? 14.265  30.968  70.221  1.00 18.71 ? 714  THR B N     1 
ATOM   13976 C CA    . THR B  1 716  ? 12.967  31.028  69.540  1.00 19.33 ? 714  THR B CA    1 
ATOM   13977 C C     . THR B  1 716  ? 12.338  32.406  69.649  1.00 19.55 ? 714  THR B C     1 
ATOM   13978 O O     . THR B  1 716  ? 11.790  32.922  68.665  1.00 19.79 ? 714  THR B O     1 
ATOM   13979 C CB    . THR B  1 716  ? 12.027  29.969  70.119  1.00 18.49 ? 714  THR B CB    1 
ATOM   13980 O OG1   . THR B  1 716  ? 12.599  28.678  69.921  1.00 19.30 ? 714  THR B OG1   1 
ATOM   13981 C CG2   . THR B  1 716  ? 10.661  29.988  69.419  1.00 19.60 ? 714  THR B CG2   1 
ATOM   13982 N N     . GLY B  1 717  ? 12.379  33.012  70.836  1.00 18.67 ? 715  GLY B N     1 
ATOM   13983 C CA    . GLY B  1 717  ? 11.704  34.289  71.011  1.00 18.05 ? 715  GLY B CA    1 
ATOM   13984 C C     . GLY B  1 717  ? 12.223  35.354  70.062  1.00 19.33 ? 715  GLY B C     1 
ATOM   13985 O O     . GLY B  1 717  ? 11.443  36.060  69.414  1.00 19.71 ? 715  GLY B O     1 
ATOM   13986 N N     . GLN B  1 718  ? 13.551  35.496  69.977  1.00 18.25 ? 716  GLN B N     1 
ATOM   13987 C CA    . GLN B  1 718  ? 14.132  36.522  69.103  1.00 20.60 ? 716  GLN B CA    1 
ATOM   13988 C C     . GLN B  1 718  ? 13.773  36.248  67.653  1.00 18.80 ? 716  GLN B C     1 
ATOM   13989 O O     . GLN B  1 718  ? 13.351  37.154  66.914  1.00 20.34 ? 716  GLN B O     1 
ATOM   13990 C CB    . GLN B  1 718  ? 15.660  36.587  69.267  1.00 17.94 ? 716  GLN B CB    1 
ATOM   13991 C CG    . GLN B  1 718  ? 16.144  37.014  70.689  1.00 18.73 ? 716  GLN B CG    1 
ATOM   13992 C CD    . GLN B  1 718  ? 17.662  37.139  70.824  1.00 21.72 ? 716  GLN B CD    1 
ATOM   13993 O OE1   . GLN B  1 718  ? 18.148  37.993  71.570  1.00 26.72 ? 716  GLN B OE1   1 
ATOM   13994 N NE2   . GLN B  1 718  ? 18.416  36.283  70.135  1.00 19.99 ? 716  GLN B NE2   1 
ATOM   13995 N N     . ILE B  1 719  ? 13.893  34.986  67.244  1.00 17.53 ? 717  ILE B N     1 
ATOM   13996 C CA    . ILE B  1 719  ? 13.683  34.636  65.845  1.00 14.98 ? 717  ILE B CA    1 
ATOM   13997 C C     . ILE B  1 719  ? 12.225  34.812  65.473  1.00 16.78 ? 717  ILE B C     1 
ATOM   13998 O O     . ILE B  1 719  ? 11.906  35.380  64.417  1.00 17.68 ? 717  ILE B O     1 
ATOM   13999 C CB    . ILE B  1 719  ? 14.173  33.194  65.602  1.00 18.34 ? 717  ILE B CB    1 
ATOM   14000 C CG1   . ILE B  1 719  ? 15.707  33.145  65.614  1.00 18.31 ? 717  ILE B CG1   1 
ATOM   14001 C CG2   . ILE B  1 719  ? 13.623  32.654  64.338  1.00 23.32 ? 717  ILE B CG2   1 
ATOM   14002 C CD1   . ILE B  1 719  ? 16.238  31.747  65.735  1.00 23.12 ? 717  ILE B CD1   1 
ATOM   14003 N N     . ALA B  1 720  ? 11.314  34.354  66.345  1.00 14.20 ? 718  ALA B N     1 
ATOM   14004 C CA    . ALA B  1 720  ? 9.877   34.460  66.063  1.00 16.52 ? 718  ALA B CA    1 
ATOM   14005 C C     . ALA B  1 720  ? 9.446   35.909  65.920  1.00 17.33 ? 718  ALA B C     1 
ATOM   14006 O O     . ALA B  1 720  ? 8.651   36.251  65.034  1.00 16.94 ? 718  ALA B O     1 
ATOM   14007 C CB    . ALA B  1 720  ? 9.062   33.787  67.184  1.00 17.19 ? 718  ALA B CB    1 
ATOM   14008 N N     . ALA B  1 721  ? 9.950   36.771  66.800  1.00 18.36 ? 719  ALA B N     1 
ATOM   14009 C CA    . ALA B  1 721  ? 9.592   38.179  66.741  1.00 20.64 ? 719  ALA B CA    1 
ATOM   14010 C C     . ALA B  1 721  ? 10.051  38.790  65.433  1.00 17.48 ? 719  ALA B C     1 
ATOM   14011 O O     . ALA B  1 721  ? 9.285   39.502  64.771  1.00 19.25 ? 719  ALA B O     1 
ATOM   14012 C CB    . ALA B  1 721  ? 10.207  38.934  67.920  1.00 19.16 ? 719  ALA B CB    1 
ATOM   14013 N N     . ALA B  1 722  ? 11.314  38.541  65.069  1.00 17.94 ? 720  ALA B N     1 
ATOM   14014 C CA    . ALA B  1 722  ? 11.867  39.107  63.845  1.00 19.71 ? 720  ALA B CA    1 
ATOM   14015 C C     . ALA B  1 722  ? 11.094  38.599  62.633  1.00 20.06 ? 720  ALA B C     1 
ATOM   14016 O O     . ALA B  1 722  ? 10.711  39.382  61.754  1.00 19.46 ? 720  ALA B O     1 
ATOM   14017 C CB    . ALA B  1 722  ? 13.356  38.770  63.735  1.00 17.08 ? 720  ALA B CB    1 
ATOM   14018 N N     . LEU B  1 723  ? 10.819  37.292  62.594  1.00 17.58 ? 721  LEU B N     1 
ATOM   14019 C CA    . LEU B  1 723  ? 10.067  36.715  61.477  1.00 17.82 ? 721  LEU B CA    1 
ATOM   14020 C C     . LEU B  1 723  ? 8.669   37.299  61.376  1.00 19.66 ? 721  LEU B C     1 
ATOM   14021 O O     . LEU B  1 723  ? 8.238   37.740  60.294  1.00 22.74 ? 721  LEU B O     1 
ATOM   14022 C CB    . LEU B  1 723  ? 9.972   35.194  61.626  1.00 18.26 ? 721  LEU B CB    1 
ATOM   14023 C CG    . LEU B  1 723  ? 11.238  34.380  61.391  1.00 21.20 ? 721  LEU B CG    1 
ATOM   14024 C CD1   . LEU B  1 723  ? 10.987  32.942  61.797  1.00 20.69 ? 721  LEU B CD1   1 
ATOM   14025 C CD2   . LEU B  1 723  ? 11.696  34.489  59.940  1.00 19.71 ? 721  LEU B CD2   1 
ATOM   14026 N N     . VAL B  1 724  ? 7.902   37.241  62.470  1.00 17.42 ? 722  VAL B N     1 
ATOM   14027 C CA    . VAL B  1 724  ? 6.509   37.647  62.368  1.00 17.20 ? 722  VAL B CA    1 
ATOM   14028 C C     . VAL B  1 724  ? 6.388   39.130  62.049  1.00 20.76 ? 722  VAL B C     1 
ATOM   14029 O O     . VAL B  1 724  ? 5.376   39.556  61.469  1.00 22.10 ? 722  VAL B O     1 
ATOM   14030 C CB    . VAL B  1 724  ? 5.738   37.294  63.649  1.00 18.52 ? 722  VAL B CB    1 
ATOM   14031 C CG1   . VAL B  1 724  ? 6.009   38.365  64.761  1.00 17.32 ? 722  VAL B CG1   1 
ATOM   14032 C CG2   . VAL B  1 724  ? 4.242   37.106  63.316  1.00 16.96 ? 722  VAL B CG2   1 
ATOM   14033 N N     . ALA B  1 725  ? 7.406   39.926  62.384  1.00 19.28 ? 723  ALA B N     1 
ATOM   14034 C CA    . ALA B  1 725  ? 7.447   41.328  61.980  1.00 20.84 ? 723  ALA B CA    1 
ATOM   14035 C C     . ALA B  1 725  ? 7.763   41.491  60.501  1.00 22.06 ? 723  ALA B C     1 
ATOM   14036 O O     . ALA B  1 725  ? 7.775   42.623  60.009  1.00 23.63 ? 723  ALA B O     1 
ATOM   14037 C CB    . ALA B  1 725  ? 8.466   42.095  62.826  1.00 22.43 ? 723  ALA B CB    1 
ATOM   14038 N N     . GLY B  1 726  ? 7.965   40.392  59.779  1.00 19.41 ? 724  GLY B N     1 
ATOM   14039 C CA    . GLY B  1 726  ? 8.200   40.444  58.349  1.00 23.97 ? 724  GLY B CA    1 
ATOM   14040 C C     . GLY B  1 726  ? 9.658   40.482  57.934  1.00 22.23 ? 724  GLY B C     1 
ATOM   14041 O O     . GLY B  1 726  ? 9.947   40.818  56.786  1.00 22.26 ? 724  GLY B O     1 
ATOM   14042 N N     . ASN B  1 727  ? 10.595  40.136  58.830  1.00 17.92 ? 725  ASN B N     1 
ATOM   14043 C CA    . ASN B  1 727  ? 12.020  40.146  58.522  1.00 20.07 ? 725  ASN B CA    1 
ATOM   14044 C C     . ASN B  1 727  ? 12.563  38.732  58.334  1.00 18.49 ? 725  ASN B C     1 
ATOM   14045 O O     . ASN B  1 727  ? 12.255  37.848  59.132  1.00 21.06 ? 725  ASN B O     1 
ATOM   14046 C CB    . ASN B  1 727  ? 12.809  40.802  59.651  1.00 15.96 ? 725  ASN B CB    1 
ATOM   14047 C CG    . ASN B  1 727  ? 12.281  42.175  60.004  1.00 22.40 ? 725  ASN B CG    1 
ATOM   14048 O OD1   . ASN B  1 727  ? 12.607  43.159  59.336  1.00 22.79 ? 725  ASN B OD1   1 
ATOM   14049 N ND2   . ASN B  1 727  ? 11.465  42.255  61.069  1.00 20.93 ? 725  ASN B ND2   1 
ATOM   14050 N N     . PRO B  1 728  ? 13.393  38.490  57.321  1.00 19.11 ? 726  PRO B N     1 
ATOM   14051 C CA    . PRO B  1 728  ? 14.115  37.219  57.259  1.00 20.17 ? 726  PRO B CA    1 
ATOM   14052 C C     . PRO B  1 728  ? 15.218  37.241  58.299  1.00 19.54 ? 726  PRO B C     1 
ATOM   14053 O O     . PRO B  1 728  ? 15.730  38.305  58.652  1.00 21.79 ? 726  PRO B O     1 
ATOM   14054 C CB    . PRO B  1 728  ? 14.679  37.196  55.836  1.00 22.99 ? 726  PRO B CB    1 
ATOM   14055 C CG    . PRO B  1 728  ? 14.867  38.653  55.512  1.00 24.22 ? 726  PRO B CG    1 
ATOM   14056 C CD    . PRO B  1 728  ? 13.819  39.420  56.260  1.00 24.89 ? 726  PRO B CD    1 
ATOM   14057 N N     . VAL B  1 729  ? 15.564  36.061  58.804  1.00 18.68 ? 727  VAL B N     1 
ATOM   14058 C CA    . VAL B  1 729  ? 16.439  35.940  59.971  1.00 21.66 ? 727  VAL B CA    1 
ATOM   14059 C C     . VAL B  1 729  ? 17.686  35.130  59.642  1.00 19.53 ? 727  VAL B C     1 
ATOM   14060 O O     . VAL B  1 729  ? 17.627  34.113  58.942  1.00 21.54 ? 727  VAL B O     1 
ATOM   14061 C CB    . VAL B  1 729  ? 15.681  35.315  61.161  1.00 16.56 ? 727  VAL B CB    1 
ATOM   14062 C CG1   . VAL B  1 729  ? 16.681  34.862  62.283  1.00 18.24 ? 727  VAL B CG1   1 
ATOM   14063 C CG2   . VAL B  1 729  ? 14.634  36.294  61.650  1.00 19.77 ? 727  VAL B CG2   1 
ATOM   14064 N N     . LEU B  1 730  ? 18.817  35.587  60.169  1.00 19.34 ? 728  LEU B N     1 
ATOM   14065 C CA    . LEU B  1 730  ? 20.044  34.813  60.261  1.00 22.43 ? 728  LEU B CA    1 
ATOM   14066 C C     . LEU B  1 730  ? 20.176  34.413  61.724  1.00 24.09 ? 728  LEU B C     1 
ATOM   14067 O O     . LEU B  1 730  ? 20.358  35.271  62.586  1.00 20.55 ? 728  LEU B O     1 
ATOM   14068 C CB    . LEU B  1 730  ? 21.255  35.620  59.794  1.00 20.10 ? 728  LEU B CB    1 
ATOM   14069 C CG    . LEU B  1 730  ? 21.295  36.163  58.360  1.00 20.01 ? 728  LEU B CG    1 
ATOM   14070 C CD1   . LEU B  1 730  ? 20.864  35.099  57.368  1.00 23.63 ? 728  LEU B CD1   1 
ATOM   14071 C CD2   . LEU B  1 730  ? 20.468  37.440  58.178  1.00 24.31 ? 728  LEU B CD2   1 
ATOM   14072 N N     . ALA B  1 731  ? 20.057  33.122  62.010  1.00 21.11 ? 729  ALA B N     1 
ATOM   14073 C CA    . ALA B  1 731  ? 20.045  32.635  63.383  1.00 20.86 ? 729  ALA B CA    1 
ATOM   14074 C C     . ALA B  1 731  ? 21.428  32.090  63.714  1.00 20.52 ? 729  ALA B C     1 
ATOM   14075 O O     . ALA B  1 731  ? 21.853  31.076  63.154  1.00 22.94 ? 729  ALA B O     1 
ATOM   14076 C CB    . ALA B  1 731  ? 18.964  31.572  63.580  1.00 17.76 ? 729  ALA B CB    1 
ATOM   14077 N N     . LYS B  1 732  ? 22.131  32.766  64.628  1.00 23.48 ? 730  LYS B N     1 
ATOM   14078 C CA    . LYS B  1 732  ? 23.455  32.342  65.061  1.00 25.12 ? 730  LYS B CA    1 
ATOM   14079 C C     . LYS B  1 732  ? 23.350  31.856  66.495  1.00 24.52 ? 730  LYS B C     1 
ATOM   14080 O O     . LYS B  1 732  ? 23.359  32.674  67.424  1.00 20.91 ? 730  LYS B O     1 
ATOM   14081 C CB    . LYS B  1 732  ? 24.467  33.485  64.959  1.00 22.55 ? 730  LYS B CB    1 
ATOM   14082 C CG    . LYS B  1 732  ? 25.869  33.032  64.540  1.00 26.55 ? 730  LYS B CG    1 
ATOM   14083 C CD    . LYS B  1 732  ? 26.515  32.124  65.569  1.00 27.56 ? 730  LYS B CD    1 
ATOM   14084 C CE    . LYS B  1 732  ? 26.774  32.865  66.850  1.00 24.06 ? 730  LYS B CE    1 
ATOM   14085 N NZ    . LYS B  1 732  ? 27.631  32.074  67.772  1.00 27.33 ? 730  LYS B NZ    1 
ATOM   14086 N N     . PRO B  1 733  ? 23.250  30.553  66.729  1.00 23.56 ? 731  PRO B N     1 
ATOM   14087 C CA    . PRO B  1 733  ? 23.120  30.056  68.097  1.00 21.89 ? 731  PRO B CA    1 
ATOM   14088 C C     . PRO B  1 733  ? 24.466  30.045  68.797  1.00 21.56 ? 731  PRO B C     1 
ATOM   14089 O O     . PRO B  1 733  ? 25.527  30.109  68.171  1.00 21.63 ? 731  PRO B O     1 
ATOM   14090 C CB    . PRO B  1 733  ? 22.612  28.631  67.898  1.00 24.24 ? 731  PRO B CB    1 
ATOM   14091 C CG    . PRO B  1 733  ? 23.351  28.198  66.682  1.00 22.00 ? 731  PRO B CG    1 
ATOM   14092 C CD    . PRO B  1 733  ? 23.391  29.444  65.772  1.00 25.55 ? 731  PRO B CD    1 
ATOM   14093 N N     . ALA B  1 734  ? 24.396  29.929  70.117  1.00 21.87 ? 732  ALA B N     1 
ATOM   14094 C CA    . ALA B  1 734  ? 25.602  29.790  70.919  1.00 20.87 ? 732  ALA B CA    1 
ATOM   14095 C C     . ALA B  1 734  ? 26.422  28.585  70.472  1.00 26.60 ? 732  ALA B C     1 
ATOM   14096 O O     . ALA B  1 734  ? 25.882  27.553  70.052  1.00 23.06 ? 732  ALA B O     1 
ATOM   14097 C CB    . ALA B  1 734  ? 25.233  29.658  72.398  1.00 20.35 ? 732  ALA B CB    1 
ATOM   14098 N N     . GLU B  1 735  ? 27.753  28.718  70.589  1.00 23.05 ? 733  GLU B N     1 
ATOM   14099 C CA    . GLU B  1 735  ? 28.638  27.651  70.152  1.00 23.20 ? 733  GLU B CA    1 
ATOM   14100 C C     . GLU B  1 735  ? 28.390  26.369  70.941  1.00 21.20 ? 733  GLU B C     1 
ATOM   14101 O O     . GLU B  1 735  ? 28.531  25.264  70.402  1.00 22.47 ? 733  GLU B O     1 
ATOM   14102 C CB    . GLU B  1 735  ? 30.103  28.096  70.291  1.00 29.76 ? 733  GLU B CB    1 
ATOM   14103 C CG    . GLU B  1 735  ? 31.109  27.107  69.727  1.00 37.50 ? 733  GLU B CG    1 
ATOM   14104 C CD    . GLU B  1 735  ? 32.568  27.476  70.032  1.00 43.07 ? 733  GLU B CD    1 
ATOM   14105 O OE1   . GLU B  1 735  ? 32.820  28.602  70.515  1.00 40.60 ? 733  GLU B OE1   1 
ATOM   14106 O OE2   . GLU B  1 735  ? 33.453  26.630  69.786  1.00 40.78 ? 733  GLU B OE2   1 
ATOM   14107 N N     . GLU B  1 736  ? 28.020  26.496  72.215  1.00 23.25 ? 734  GLU B N     1 
ATOM   14108 C CA    . GLU B  1 736  ? 27.856  25.336  73.083  1.00 23.52 ? 734  GLU B CA    1 
ATOM   14109 C C     . GLU B  1 736  ? 26.579  24.542  72.813  1.00 24.29 ? 734  GLU B C     1 
ATOM   14110 O O     . GLU B  1 736  ? 26.519  23.358  73.164  1.00 22.77 ? 734  GLU B O     1 
ATOM   14111 C CB    . GLU B  1 736  ? 27.863  25.785  74.544  1.00 24.44 ? 734  GLU B CB    1 
ATOM   14112 C CG    . GLU B  1 736  ? 29.146  26.458  74.959  1.00 27.97 ? 734  GLU B CG    1 
ATOM   14113 C CD    . GLU B  1 736  ? 29.170  27.962  74.723  1.00 28.14 ? 734  GLU B CD    1 
ATOM   14114 O OE1   . GLU B  1 736  ? 28.278  28.522  74.045  1.00 23.33 ? 734  GLU B OE1   1 
ATOM   14115 O OE2   . GLU B  1 736  ? 30.107  28.594  75.235  1.00 31.94 ? 734  GLU B OE2   1 
ATOM   14116 N N     . THR B  1 737  ? 25.550  25.151  72.222  1.00 21.24 ? 735  THR B N     1 
ATOM   14117 C CA    . THR B  1 737  ? 24.230  24.521  72.147  1.00 22.39 ? 735  THR B CA    1 
ATOM   14118 C C     . THR B  1 737  ? 23.631  24.624  70.751  1.00 21.20 ? 735  THR B C     1 
ATOM   14119 O O     . THR B  1 737  ? 22.497  25.070  70.594  1.00 21.43 ? 735  THR B O     1 
ATOM   14120 C CB    . THR B  1 737  ? 23.280  25.137  73.177  1.00 21.17 ? 735  THR B CB    1 
ATOM   14121 O OG1   . THR B  1 737  ? 23.190  26.547  72.971  1.00 21.18 ? 735  THR B OG1   1 
ATOM   14122 C CG2   . THR B  1 737  ? 23.783  24.876  74.608  1.00 22.45 ? 735  THR B CG2   1 
ATOM   14123 N N     . PRO B  1 738  ? 24.340  24.170  69.718  1.00 22.05 ? 736  PRO B N     1 
ATOM   14124 C CA    . PRO B  1 738  ? 23.777  24.295  68.362  1.00 23.13 ? 736  PRO B CA    1 
ATOM   14125 C C     . PRO B  1 738  ? 22.656  23.304  68.062  1.00 23.29 ? 736  PRO B C     1 
ATOM   14126 O O     . PRO B  1 738  ? 21.867  23.543  67.125  1.00 19.83 ? 736  PRO B O     1 
ATOM   14127 C CB    . PRO B  1 738  ? 24.996  24.049  67.473  1.00 19.83 ? 736  PRO B CB    1 
ATOM   14128 C CG    . PRO B  1 738  ? 25.757  23.019  68.231  1.00 23.39 ? 736  PRO B CG    1 
ATOM   14129 C CD    . PRO B  1 738  ? 25.637  23.462  69.690  1.00 21.36 ? 736  PRO B CD    1 
ATOM   14130 N N     . LEU B  1 739  ? 22.565  22.188  68.796  1.00 19.07 ? 737  LEU B N     1 
ATOM   14131 C CA    . LEU B  1 739  ? 21.676  21.110  68.361  1.00 23.16 ? 737  LEU B CA    1 
ATOM   14132 C C     . LEU B  1 739  ? 20.215  21.472  68.572  1.00 21.35 ? 737  LEU B C     1 
ATOM   14133 O O     . LEU B  1 739  ? 19.381  21.245  67.683  1.00 21.47 ? 737  LEU B O     1 
ATOM   14134 C CB    . LEU B  1 739  ? 22.012  19.803  69.090  1.00 21.98 ? 737  LEU B CB    1 
ATOM   14135 C CG    . LEU B  1 739  ? 23.450  19.312  68.956  1.00 23.47 ? 737  LEU B CG    1 
ATOM   14136 C CD1   . LEU B  1 739  ? 23.654  17.951  69.649  1.00 21.31 ? 737  LEU B CD1   1 
ATOM   14137 C CD2   . LEU B  1 739  ? 23.825  19.226  67.501  1.00 21.97 ? 737  LEU B CD2   1 
ATOM   14138 N N     . ILE B  1 740  ? 19.874  22.010  69.745  1.00 18.90 ? 738  ILE B N     1 
ATOM   14139 C CA    . ILE B  1 740  ? 18.483  22.390  69.975  1.00 19.64 ? 738  ILE B CA    1 
ATOM   14140 C C     . ILE B  1 740  ? 18.103  23.552  69.066  1.00 20.19 ? 738  ILE B C     1 
ATOM   14141 O O     . ILE B  1 740  ? 16.970  23.613  68.572  1.00 21.47 ? 738  ILE B O     1 
ATOM   14142 C CB    . ILE B  1 740  ? 18.239  22.696  71.466  1.00 25.33 ? 738  ILE B CB    1 
ATOM   14143 C CG1   . ILE B  1 740  ? 16.743  22.892  71.740  1.00 24.50 ? 738  ILE B CG1   1 
ATOM   14144 C CG2   . ILE B  1 740  ? 19.088  23.869  71.939  1.00 23.57 ? 738  ILE B CG2   1 
ATOM   14145 C CD1   . ILE B  1 740  ? 15.915  21.640  71.465  1.00 23.38 ? 738  ILE B CD1   1 
ATOM   14146 N N     . ALA B  1 741  ? 19.058  24.433  68.750  1.00 19.62 ? 739  ALA B N     1 
ATOM   14147 C CA    . ALA B  1 741  ? 18.792  25.506  67.794  1.00 20.49 ? 739  ALA B CA    1 
ATOM   14148 C C     . ALA B  1 741  ? 18.436  24.952  66.419  1.00 19.74 ? 739  ALA B C     1 
ATOM   14149 O O     . ALA B  1 741  ? 17.474  25.412  65.785  1.00 21.50 ? 739  ALA B O     1 
ATOM   14150 C CB    . ALA B  1 741  ? 19.996  26.435  67.691  1.00 20.21 ? 739  ALA B CB    1 
ATOM   14151 N N     . ALA B  1 742  ? 19.218  23.981  65.928  1.00 21.07 ? 740  ALA B N     1 
ATOM   14152 C CA    . ALA B  1 742  ? 18.886  23.327  64.661  1.00 21.70 ? 740  ALA B CA    1 
ATOM   14153 C C     . ALA B  1 742  ? 17.486  22.720  64.703  1.00 21.67 ? 740  ALA B C     1 
ATOM   14154 O O     . ALA B  1 742  ? 16.731  22.795  63.718  1.00 20.46 ? 740  ALA B O     1 
ATOM   14155 C CB    . ALA B  1 742  ? 19.930  22.250  64.340  1.00 19.72 ? 740  ALA B CB    1 
ATOM   14156 N N     . GLU B  1 743  ? 17.134  22.074  65.819  1.00 19.79 ? 741  GLU B N     1 
ATOM   14157 C CA    . GLU B  1 743  ? 15.788  21.520  65.942  1.00 20.46 ? 741  GLU B CA    1 
ATOM   14158 C C     . GLU B  1 743  ? 14.743  22.622  65.925  1.00 20.22 ? 741  GLU B C     1 
ATOM   14159 O O     . GLU B  1 743  ? 13.689  22.473  65.299  1.00 21.03 ? 741  GLU B O     1 
ATOM   14160 C CB    . GLU B  1 743  ? 15.672  20.674  67.209  1.00 25.08 ? 741  GLU B CB    1 
ATOM   14161 C CG    . GLU B  1 743  ? 14.294  20.094  67.421  1.00 26.60 ? 741  GLU B CG    1 
ATOM   14162 C CD    . GLU B  1 743  ? 13.947  18.984  66.445  1.00 25.75 ? 741  GLU B CD    1 
ATOM   14163 O OE1   . GLU B  1 743  ? 14.828  18.551  65.659  1.00 23.44 ? 741  GLU B OE1   1 
ATOM   14164 O OE2   . GLU B  1 743  ? 12.776  18.538  66.475  1.00 26.93 ? 741  GLU B OE2   1 
ATOM   14165 N N     . GLY B  1 744  ? 15.022  23.737  66.607  1.00 19.14 ? 742  GLY B N     1 
ATOM   14166 C CA    . GLY B  1 744  ? 14.161  24.901  66.510  1.00 19.75 ? 742  GLY B CA    1 
ATOM   14167 C C     . GLY B  1 744  ? 13.944  25.345  65.078  1.00 17.87 ? 742  GLY B C     1 
ATOM   14168 O O     . GLY B  1 744  ? 12.812  25.606  64.663  1.00 21.80 ? 742  GLY B O     1 
ATOM   14169 N N     . VAL B  1 745  ? 15.027  25.425  64.293  1.00 19.29 ? 743  VAL B N     1 
ATOM   14170 C CA    . VAL B  1 745  ? 14.891  25.830  62.894  1.00 17.66 ? 743  VAL B CA    1 
ATOM   14171 C C     . VAL B  1 745  ? 14.078  24.799  62.114  1.00 20.67 ? 743  VAL B C     1 
ATOM   14172 O O     . VAL B  1 745  ? 13.205  25.161  61.314  1.00 19.16 ? 743  VAL B O     1 
ATOM   14173 C CB    . VAL B  1 745  ? 16.276  26.082  62.253  1.00 21.94 ? 743  VAL B CB    1 
ATOM   14174 C CG1   . VAL B  1 745  ? 16.146  26.253  60.726  1.00 17.41 ? 743  VAL B CG1   1 
ATOM   14175 C CG2   . VAL B  1 745  ? 16.913  27.342  62.846  1.00 22.19 ? 743  VAL B CG2   1 
ATOM   14176 N N     . ARG B  1 746  ? 14.316  23.503  62.349  1.00 19.19 ? 744  ARG B N     1 
ATOM   14177 C CA    . ARG B  1 746  ? 13.511  22.492  61.649  1.00 22.24 ? 744  ARG B CA    1 
ATOM   14178 C C     . ARG B  1 746  ? 12.012  22.701  61.889  1.00 18.50 ? 744  ARG B C     1 
ATOM   14179 O O     . ARG B  1 746  ? 11.191  22.575  60.962  1.00 17.57 ? 744  ARG B O     1 
ATOM   14180 C CB    . ARG B  1 746  ? 13.901  21.078  62.092  1.00 23.65 ? 744  ARG B CB    1 
ATOM   14181 C CG    . ARG B  1 746  ? 15.305  20.628  61.760  1.00 25.55 ? 744  ARG B CG    1 
ATOM   14182 C CD    . ARG B  1 746  ? 15.547  19.214  62.301  1.00 25.83 ? 744  ARG B CD    1 
ATOM   14183 N NE    . ARG B  1 746  ? 16.944  18.854  62.112  1.00 27.44 ? 744  ARG B NE    1 
ATOM   14184 C CZ    . ARG B  1 746  ? 17.847  18.823  63.078  1.00 24.47 ? 744  ARG B CZ    1 
ATOM   14185 N NH1   . ARG B  1 746  ? 17.498  18.918  64.352  1.00 22.50 ? 744  ARG B NH1   1 
ATOM   14186 N NH2   . ARG B  1 746  ? 19.132  18.683  62.756  1.00 22.46 ? 744  ARG B NH2   1 
ATOM   14187 N N     . ILE B  1 747  ? 11.636  23.027  63.126  1.00 19.56 ? 745  ILE B N     1 
ATOM   14188 C CA    . ILE B  1 747  ? 10.220  23.117  63.456  1.00 21.45 ? 745  ILE B CA    1 
ATOM   14189 C C     . ILE B  1 747  ? 9.606   24.362  62.831  1.00 18.90 ? 745  ILE B C     1 
ATOM   14190 O O     . ILE B  1 747  ? 8.508   24.310  62.259  1.00 19.22 ? 745  ILE B O     1 
ATOM   14191 C CB    . ILE B  1 747  ? 10.049  23.073  64.983  1.00 21.26 ? 745  ILE B CB    1 
ATOM   14192 C CG1   . ILE B  1 747  ? 10.289  21.631  65.467  1.00 19.53 ? 745  ILE B CG1   1 
ATOM   14193 C CG2   . ILE B  1 747  ? 8.680   23.622  65.396  1.00 18.72 ? 745  ILE B CG2   1 
ATOM   14194 C CD1   . ILE B  1 747  ? 10.479  21.523  66.937  1.00 21.26 ? 745  ILE B CD1   1 
ATOM   14195 N N     . LEU B  1 748  ? 10.320  25.489  62.898  1.00 17.71 ? 746  LEU B N     1 
ATOM   14196 C CA    . LEU B  1 748  ? 9.841   26.711  62.260  1.00 17.57 ? 746  LEU B CA    1 
ATOM   14197 C C     . LEU B  1 748  ? 9.692   26.531  60.757  1.00 19.78 ? 746  LEU B C     1 
ATOM   14198 O O     . LEU B  1 748  ? 8.703   26.981  60.168  1.00 19.28 ? 746  LEU B O     1 
ATOM   14199 C CB    . LEU B  1 748  ? 10.789  27.869  62.573  1.00 18.04 ? 746  LEU B CB    1 
ATOM   14200 C CG    . LEU B  1 748  ? 10.570  28.472  63.960  1.00 25.40 ? 746  LEU B CG    1 
ATOM   14201 C CD1   . LEU B  1 748  ? 11.700  29.449  64.374  1.00 22.47 ? 746  LEU B CD1   1 
ATOM   14202 C CD2   . LEU B  1 748  ? 9.234   29.147  63.963  1.00 25.58 ? 746  LEU B CD2   1 
ATOM   14203 N N     . ARG B  1 749  ? 10.660  25.866  60.119  1.00 17.38 ? 747  ARG B N     1 
ATOM   14204 C CA    . ARG B  1 749  ? 10.542  25.611  58.683  1.00 18.74 ? 747  ARG B CA    1 
ATOM   14205 C C     . ARG B  1 749  ? 9.410   24.643  58.378  1.00 18.88 ? 747  ARG B C     1 
ATOM   14206 O O     . ARG B  1 749  ? 8.695   24.815  57.386  1.00 18.77 ? 747  ARG B O     1 
ATOM   14207 C CB    . ARG B  1 749  ? 11.859  25.074  58.136  1.00 18.83 ? 747  ARG B CB    1 
ATOM   14208 C CG    . ARG B  1 749  ? 12.943  26.135  57.992  1.00 18.73 ? 747  ARG B CG    1 
ATOM   14209 C CD    . ARG B  1 749  ? 14.118  25.541  57.247  1.00 18.95 ? 747  ARG B CD    1 
ATOM   14210 N NE    . ARG B  1 749  ? 15.191  26.502  57.034  1.00 21.32 ? 747  ARG B NE    1 
ATOM   14211 C CZ    . ARG B  1 749  ? 16.251  26.247  56.280  1.00 24.53 ? 747  ARG B CZ    1 
ATOM   14212 N NH1   . ARG B  1 749  ? 16.393  25.081  55.663  1.00 20.99 ? 747  ARG B NH1   1 
ATOM   14213 N NH2   . ARG B  1 749  ? 17.190  27.180  56.144  1.00 22.29 ? 747  ARG B NH2   1 
ATOM   14214 N N     . GLU B  1 750  ? 9.256   23.594  59.187  1.00 18.06 ? 748  GLU B N     1 
ATOM   14215 C CA    . GLU B  1 750  ? 8.135   22.683  58.976  1.00 22.56 ? 748  GLU B CA    1 
ATOM   14216 C C     . GLU B  1 750  ? 6.812   23.405  59.142  1.00 20.51 ? 748  GLU B C     1 
ATOM   14217 O O     . GLU B  1 750  ? 5.835   23.083  58.456  1.00 20.32 ? 748  GLU B O     1 
ATOM   14218 C CB    . GLU B  1 750  ? 8.216   21.504  59.950  1.00 19.77 ? 748  GLU B CB    1 
ATOM   14219 C CG    . GLU B  1 750  ? 7.171   20.418  59.701  1.00 19.07 ? 748  GLU B CG    1 
ATOM   14220 C CD    . GLU B  1 750  ? 7.317   19.255  60.657  1.00 24.76 ? 748  GLU B CD    1 
ATOM   14221 O OE1   . GLU B  1 750  ? 8.408   19.115  61.269  1.00 24.13 ? 748  GLU B OE1   1 
ATOM   14222 O OE2   . GLU B  1 750  ? 6.332   18.502  60.831  1.00 27.42 ? 748  GLU B OE2   1 
ATOM   14223 N N     . ALA B  1 751  ? 6.769   24.399  60.037  1.00 20.89 ? 749  ALA B N     1 
ATOM   14224 C CA    . ALA B  1 751  ? 5.567   25.187  60.276  1.00 23.26 ? 749  ALA B CA    1 
ATOM   14225 C C     . ALA B  1 751  ? 5.247   26.154  59.148  1.00 20.09 ? 749  ALA B C     1 
ATOM   14226 O O     . ALA B  1 751  ? 4.157   26.733  59.153  1.00 22.83 ? 749  ALA B O     1 
ATOM   14227 C CB    . ALA B  1 751  ? 5.713   25.987  61.568  1.00 20.34 ? 749  ALA B CB    1 
ATOM   14228 N N     . GLY B  1 752  ? 6.155   26.355  58.199  1.00 21.04 ? 750  GLY B N     1 
ATOM   14229 C CA    . GLY B  1 752  ? 5.886   27.215  57.057  1.00 19.58 ? 750  GLY B CA    1 
ATOM   14230 C C     . GLY B  1 752  ? 6.825   28.390  56.876  1.00 19.99 ? 750  GLY B C     1 
ATOM   14231 O O     . GLY B  1 752  ? 6.661   29.136  55.903  1.00 20.06 ? 750  GLY B O     1 
ATOM   14232 N N     . ILE B  1 753  ? 7.795   28.630  57.757  1.00 19.63 ? 751  ILE B N     1 
ATOM   14233 C CA    . ILE B  1 753  ? 8.797   29.667  57.499  1.00 19.99 ? 751  ILE B CA    1 
ATOM   14234 C C     . ILE B  1 753  ? 9.688   29.207  56.348  1.00 17.84 ? 751  ILE B C     1 
ATOM   14235 O O     . ILE B  1 753  ? 10.334  28.153  56.450  1.00 19.73 ? 751  ILE B O     1 
ATOM   14236 C CB    . ILE B  1 753  ? 9.659   29.956  58.742  1.00 16.91 ? 751  ILE B CB    1 
ATOM   14237 C CG1   . ILE B  1 753  ? 8.798   30.352  59.945  1.00 22.03 ? 751  ILE B CG1   1 
ATOM   14238 C CG2   . ILE B  1 753  ? 10.712  31.011  58.400  1.00 19.87 ? 751  ILE B CG2   1 
ATOM   14239 C CD1   . ILE B  1 753  ? 7.977   31.619  59.724  1.00 21.48 ? 751  ILE B CD1   1 
ATOM   14240 N N     . PRO B  1 754  ? 9.755   29.946  55.240  1.00 18.74 ? 752  PRO B N     1 
ATOM   14241 C CA    . PRO B  1 754  ? 10.576  29.502  54.108  1.00 22.37 ? 752  PRO B CA    1 
ATOM   14242 C C     . PRO B  1 754  ? 12.048  29.439  54.475  1.00 21.54 ? 752  PRO B C     1 
ATOM   14243 O O     . PRO B  1 754  ? 12.530  30.177  55.336  1.00 21.28 ? 752  PRO B O     1 
ATOM   14244 C CB    . PRO B  1 754  ? 10.322  30.571  53.035  1.00 23.82 ? 752  PRO B CB    1 
ATOM   14245 C CG    . PRO B  1 754  ? 9.162   31.362  53.509  1.00 25.72 ? 752  PRO B CG    1 
ATOM   14246 C CD    . PRO B  1 754  ? 9.151   31.264  54.997  1.00 19.79 ? 752  PRO B CD    1 
ATOM   14247 N N     . ALA B  1 755  ? 12.769  28.539  53.796  1.00 22.34 ? 753  ALA B N     1 
ATOM   14248 C CA    . ALA B  1 755  ? 14.205  28.398  54.043  1.00 22.63 ? 753  ALA B CA    1 
ATOM   14249 C C     . ALA B  1 755  ? 14.938  29.730  53.888  1.00 22.84 ? 753  ALA B C     1 
ATOM   14250 O O     . ALA B  1 755  ? 15.864  30.033  54.650  1.00 24.29 ? 753  ALA B O     1 
ATOM   14251 C CB    . ALA B  1 755  ? 14.786  27.339  53.108  1.00 26.42 ? 753  ALA B CB    1 
ATOM   14252 N N     . SER B  1 756  ? 14.523  30.560  52.929  1.00 24.34 ? 754  SER B N     1 
ATOM   14253 C CA    . SER B  1 756  ? 15.230  31.818  52.710  1.00 21.86 ? 754  SER B CA    1 
ATOM   14254 C C     . SER B  1 756  ? 14.932  32.843  53.793  1.00 23.29 ? 754  SER B C     1 
ATOM   14255 O O     . SER B  1 756  ? 15.682  33.815  53.934  1.00 28.41 ? 754  SER B O     1 
ATOM   14256 C CB    . SER B  1 756  ? 14.871  32.384  51.341  1.00 28.08 ? 754  SER B CB    1 
ATOM   14257 O OG    . SER B  1 756  ? 13.507  32.755  51.320  1.00 30.32 ? 754  SER B OG    1 
ATOM   14258 N N     . ALA B  1 757  ? 13.860  32.649  54.557  1.00 22.19 ? 755  ALA B N     1 
ATOM   14259 C CA    . ALA B  1 757  ? 13.515  33.530  55.655  1.00 19.22 ? 755  ALA B CA    1 
ATOM   14260 C C     . ALA B  1 757  ? 14.158  33.119  56.970  1.00 21.19 ? 755  ALA B C     1 
ATOM   14261 O O     . ALA B  1 757  ? 14.151  33.911  57.909  1.00 20.03 ? 755  ALA B O     1 
ATOM   14262 C CB    . ALA B  1 757  ? 12.000  33.580  55.862  1.00 20.99 ? 755  ALA B CB    1 
ATOM   14263 N N     . LEU B  1 758  ? 14.683  31.906  57.074  1.00 17.81 ? 756  LEU B N     1 
ATOM   14264 C CA    . LEU B  1 758  ? 15.270  31.458  58.340  1.00 20.50 ? 756  LEU B CA    1 
ATOM   14265 C C     . LEU B  1 758  ? 16.461  30.561  58.029  1.00 22.62 ? 756  LEU B C     1 
ATOM   14266 O O     . LEU B  1 758  ? 16.298  29.395  57.658  1.00 22.46 ? 756  LEU B O     1 
ATOM   14267 C CB    . LEU B  1 758  ? 14.236  30.749  59.206  1.00 18.00 ? 756  LEU B CB    1 
ATOM   14268 C CG    . LEU B  1 758  ? 14.795  30.107  60.470  1.00 18.27 ? 756  LEU B CG    1 
ATOM   14269 C CD1   . LEU B  1 758  ? 15.459  31.182  61.316  1.00 18.83 ? 756  LEU B CD1   1 
ATOM   14270 C CD2   . LEU B  1 758  ? 13.682  29.430  61.258  1.00 23.86 ? 756  LEU B CD2   1 
ATOM   14271 N N     . GLN B  1 759  ? 17.660  31.109  58.201  1.00 20.83 ? 757  GLN B N     1 
ATOM   14272 C CA    . GLN B  1 759  ? 18.894  30.389  57.972  1.00 17.47 ? 757  GLN B CA    1 
ATOM   14273 C C     . GLN B  1 759  ? 19.597  30.206  59.305  1.00 18.17 ? 757  GLN B C     1 
ATOM   14274 O O     . GLN B  1 759  ? 19.548  31.094  60.161  1.00 20.32 ? 757  GLN B O     1 
ATOM   14275 C CB    . GLN B  1 759  ? 19.791  31.128  56.969  1.00 21.05 ? 757  GLN B CB    1 
ATOM   14276 C CG    . GLN B  1 759  ? 19.122  31.261  55.573  1.00 19.09 ? 757  GLN B CG    1 
ATOM   14277 C CD    . GLN B  1 759  ? 19.933  32.092  54.613  1.00 21.32 ? 757  GLN B CD    1 
ATOM   14278 O OE1   . GLN B  1 759  ? 20.732  31.564  53.859  1.00 22.52 ? 757  GLN B OE1   1 
ATOM   14279 N NE2   . GLN B  1 759  ? 19.732  33.398  54.638  1.00 21.55 ? 757  GLN B NE2   1 
ATOM   14280 N N     . LEU B  1 760  ? 20.169  29.026  59.493  1.00 20.40 ? 758  LEU B N     1 
ATOM   14281 C CA    . LEU B  1 760  ? 20.919  28.691  60.697  1.00 19.75 ? 758  LEU B CA    1 
ATOM   14282 C C     . LEU B  1 760  ? 22.410  28.762  60.403  1.00 17.96 ? 758  LEU B C     1 
ATOM   14283 O O     . LEU B  1 760  ? 22.900  28.109  59.477  1.00 19.65 ? 758  LEU B O     1 
ATOM   14284 C CB    . LEU B  1 760  ? 20.550  27.296  61.197  1.00 18.23 ? 758  LEU B CB    1 
ATOM   14285 C CG    . LEU B  1 760  ? 21.252  26.902  62.491  1.00 20.99 ? 758  LEU B CG    1 
ATOM   14286 C CD1   . LEU B  1 760  ? 20.583  27.652  63.632  1.00 18.34 ? 758  LEU B CD1   1 
ATOM   14287 C CD2   . LEU B  1 760  ? 21.196  25.392  62.672  1.00 18.67 ? 758  LEU B CD2   1 
ATOM   14288 N N     . LEU B  1 761  ? 23.154  29.486  61.240  1.00 22.66 ? 759  LEU B N     1 
ATOM   14289 C CA    . LEU B  1 761  ? 24.605  29.613  61.074  1.00 20.98 ? 759  LEU B CA    1 
ATOM   14290 C C     . LEU B  1 761  ? 25.317  29.262  62.372  1.00 20.28 ? 759  LEU B C     1 
ATOM   14291 O O     . LEU B  1 761  ? 25.652  30.151  63.163  1.00 25.05 ? 759  LEU B O     1 
ATOM   14292 C CB    . LEU B  1 761  ? 24.997  31.025  60.632  1.00 21.39 ? 759  LEU B CB    1 
ATOM   14293 C CG    . LEU B  1 761  ? 24.401  31.629  59.353  1.00 23.75 ? 759  LEU B CG    1 
ATOM   14294 C CD1   . LEU B  1 761  ? 24.513  30.642  58.186  1.00 25.77 ? 759  LEU B CD1   1 
ATOM   14295 C CD2   . LEU B  1 761  ? 22.974  32.112  59.535  1.00 21.26 ? 759  LEU B CD2   1 
ATOM   14296 N N     . PRO B  1 762  ? 25.575  27.984  62.624  1.00 18.42 ? 760  PRO B N     1 
ATOM   14297 C CA    . PRO B  1 762  ? 26.322  27.619  63.834  1.00 18.57 ? 760  PRO B CA    1 
ATOM   14298 C C     . PRO B  1 762  ? 27.762  28.103  63.771  1.00 23.34 ? 760  PRO B C     1 
ATOM   14299 O O     . PRO B  1 762  ? 28.346  28.303  62.703  1.00 23.62 ? 760  PRO B O     1 
ATOM   14300 C CB    . PRO B  1 762  ? 26.265  26.083  63.856  1.00 23.01 ? 760  PRO B CB    1 
ATOM   14301 C CG    . PRO B  1 762  ? 25.236  25.694  62.832  1.00 21.92 ? 760  PRO B CG    1 
ATOM   14302 C CD    . PRO B  1 762  ? 25.235  26.806  61.810  1.00 22.18 ? 760  PRO B CD    1 
ATOM   14303 N N     . GLY B  1 763  ? 28.344  28.263  64.949  1.00 26.18 ? 761  GLY B N     1 
ATOM   14304 C CA    . GLY B  1 763  ? 29.747  28.606  65.056  1.00 22.36 ? 761  GLY B CA    1 
ATOM   14305 C C     . GLY B  1 763  ? 29.977  29.505  66.253  1.00 24.19 ? 761  GLY B C     1 
ATOM   14306 O O     . GLY B  1 763  ? 29.087  29.732  67.073  1.00 26.47 ? 761  GLY B O     1 
ATOM   14307 N N     . ASP B  1 764  ? 31.188  30.033  66.322  1.00 30.74 ? 762  ASP B N     1 
ATOM   14308 C CA    . ASP B  1 764  ? 31.595  30.828  67.465  1.00 33.31 ? 762  ASP B CA    1 
ATOM   14309 C C     . ASP B  1 764  ? 31.361  32.316  67.184  1.00 32.11 ? 762  ASP B C     1 
ATOM   14310 O O     . ASP B  1 764  ? 30.591  32.686  66.283  1.00 28.82 ? 762  ASP B O     1 
ATOM   14311 C CB    . ASP B  1 764  ? 33.050  30.498  67.822  1.00 32.20 ? 762  ASP B CB    1 
ATOM   14312 C CG    . ASP B  1 764  ? 34.030  30.788  66.685  1.00 36.94 ? 762  ASP B CG    1 
ATOM   14313 O OD1   . ASP B  1 764  ? 33.725  31.602  65.790  1.00 33.89 ? 762  ASP B OD1   1 
ATOM   14314 O OD2   . ASP B  1 764  ? 35.128  30.187  66.688  1.00 41.56 ? 762  ASP B OD2   1 
ATOM   14315 N N     . GLY B  1 765  ? 32.025  33.181  67.955  1.00 29.86 ? 763  GLY B N     1 
ATOM   14316 C CA    . GLY B  1 765  ? 31.833  34.607  67.801  1.00 29.97 ? 763  GLY B CA    1 
ATOM   14317 C C     . GLY B  1 765  ? 32.337  35.167  66.494  1.00 27.85 ? 763  GLY B C     1 
ATOM   14318 O O     . GLY B  1 765  ? 31.928  36.266  66.110  1.00 31.63 ? 763  GLY B O     1 
ATOM   14319 N N     . ARG B  1 766  ? 33.225  34.449  65.808  1.00 28.16 ? 764  ARG B N     1 
ATOM   14320 C CA    . ARG B  1 766  ? 33.667  34.906  64.499  1.00 27.58 ? 764  ARG B CA    1 
ATOM   14321 C C     . ARG B  1 766  ? 32.521  34.853  63.497  1.00 32.18 ? 764  ARG B C     1 
ATOM   14322 O O     . ARG B  1 766  ? 32.446  35.690  62.590  1.00 29.65 ? 764  ARG B O     1 
ATOM   14323 C CB    . ARG B  1 766  ? 34.838  34.066  64.009  1.00 38.44 ? 764  ARG B CB    1 
ATOM   14324 N N     . VAL B  1 767  ? 31.610  33.894  63.664  1.00 29.15 ? 765  VAL B N     1 
ATOM   14325 C CA    . VAL B  1 767  ? 30.433  33.826  62.803  1.00 26.01 ? 765  VAL B CA    1 
ATOM   14326 C C     . VAL B  1 767  ? 29.477  34.973  63.113  1.00 27.70 ? 765  VAL B C     1 
ATOM   14327 O O     . VAL B  1 767  ? 28.933  35.610  62.203  1.00 25.91 ? 765  VAL B O     1 
ATOM   14328 C CB    . VAL B  1 767  ? 29.739  32.465  62.954  1.00 25.61 ? 765  VAL B CB    1 
ATOM   14329 C CG1   . VAL B  1 767  ? 28.479  32.420  62.071  1.00 23.18 ? 765  VAL B CG1   1 
ATOM   14330 C CG2   . VAL B  1 767  ? 30.694  31.345  62.596  1.00 25.80 ? 765  VAL B CG2   1 
ATOM   14331 N N     . GLY B  1 768  ? 29.226  35.234  64.399  1.00 23.99 ? 766  GLY B N     1 
ATOM   14332 C CA    . GLY B  1 768  ? 28.359  36.348  64.741  1.00 27.45 ? 766  GLY B CA    1 
ATOM   14333 C C     . GLY B  1 768  ? 28.911  37.667  64.240  1.00 28.12 ? 766  GLY B C     1 
ATOM   14334 O O     . GLY B  1 768  ? 28.171  38.506  63.722  1.00 27.13 ? 766  GLY B O     1 
ATOM   14335 N N     . ALA B  1 769  ? 30.223  37.860  64.387  1.00 29.68 ? 767  ALA B N     1 
ATOM   14336 C CA    . ALA B  1 769  ? 30.865  39.084  63.924  1.00 30.46 ? 767  ALA B CA    1 
ATOM   14337 C C     . ALA B  1 769  ? 30.676  39.269  62.426  1.00 28.62 ? 767  ALA B C     1 
ATOM   14338 O O     . ALA B  1 769  ? 30.368  40.372  61.960  1.00 27.24 ? 767  ALA B O     1 
ATOM   14339 C CB    . ALA B  1 769  ? 32.356  39.059  64.279  1.00 29.18 ? 767  ALA B CB    1 
ATOM   14340 N N     . ALA B  1 770  ? 30.846  38.193  61.658  1.00 26.31 ? 768  ALA B N     1 
ATOM   14341 C CA    . ALA B  1 770  ? 30.682  38.286  60.215  1.00 28.03 ? 768  ALA B CA    1 
ATOM   14342 C C     . ALA B  1 770  ? 29.236  38.604  59.841  1.00 30.60 ? 768  ALA B C     1 
ATOM   14343 O O     . ALA B  1 770  ? 28.983  39.304  58.851  1.00 28.18 ? 768  ALA B O     1 
ATOM   14344 C CB    . ALA B  1 770  ? 31.136  36.985  59.553  1.00 26.07 ? 768  ALA B CB    1 
ATOM   14345 N N     . LEU B  1 771  ? 28.268  38.099  60.614  1.00 24.05 ? 769  LEU B N     1 
ATOM   14346 C CA    . LEU B  1 771  ? 26.876  38.397  60.293  1.00 26.75 ? 769  LEU B CA    1 
ATOM   14347 C C     . LEU B  1 771  ? 26.545  39.847  60.620  1.00 26.88 ? 769  LEU B C     1 
ATOM   14348 O O     . LEU B  1 771  ? 25.897  40.539  59.830  1.00 25.54 ? 769  LEU B O     1 
ATOM   14349 C CB    . LEU B  1 771  ? 25.941  37.453  61.047  1.00 26.87 ? 769  LEU B CB    1 
ATOM   14350 C CG    . LEU B  1 771  ? 25.963  35.981  60.639  1.00 22.86 ? 769  LEU B CG    1 
ATOM   14351 C CD1   . LEU B  1 771  ? 25.236  35.138  61.675  1.00 21.97 ? 769  LEU B CD1   1 
ATOM   14352 C CD2   . LEU B  1 771  ? 25.298  35.831  59.283  1.00 22.26 ? 769  LEU B CD2   1 
ATOM   14353 N N     . VAL B  1 772  ? 26.998  40.328  61.778  1.00 25.65 ? 770  VAL B N     1 
ATOM   14354 C CA    . VAL B  1 772  ? 26.688  41.697  62.181  1.00 27.88 ? 770  VAL B CA    1 
ATOM   14355 C C     . VAL B  1 772  ? 27.320  42.707  61.226  1.00 28.76 ? 770  VAL B C     1 
ATOM   14356 O O     . VAL B  1 772  ? 26.747  43.774  60.975  1.00 29.23 ? 770  VAL B O     1 
ATOM   14357 C CB    . VAL B  1 772  ? 27.152  41.922  63.632  1.00 27.01 ? 770  VAL B CB    1 
ATOM   14358 C CG1   . VAL B  1 772  ? 27.180  43.414  63.965  1.00 24.79 ? 770  VAL B CG1   1 
ATOM   14359 C CG2   . VAL B  1 772  ? 26.239  41.151  64.616  1.00 25.24 ? 770  VAL B CG2   1 
ATOM   14360 N N     . ALA B  1 773  ? 28.505  42.396  60.686  1.00 29.23 ? 771  ALA B N     1 
ATOM   14361 C CA    . ALA B  1 773  ? 29.241  43.308  59.815  1.00 30.04 ? 771  ALA B CA    1 
ATOM   14362 C C     . ALA B  1 773  ? 28.775  43.275  58.366  1.00 33.12 ? 771  ALA B C     1 
ATOM   14363 O O     . ALA B  1 773  ? 29.173  44.153  57.593  1.00 32.63 ? 771  ALA B O     1 
ATOM   14364 C CB    . ALA B  1 773  ? 30.736  42.987  59.851  1.00 30.51 ? 771  ALA B CB    1 
ATOM   14365 N N     . ALA B  1 774  ? 27.970  42.289  57.979  1.00 31.11 ? 772  ALA B N     1 
ATOM   14366 C CA    . ALA B  1 774  ? 27.509  42.188  56.599  1.00 30.35 ? 772  ALA B CA    1 
ATOM   14367 C C     . ALA B  1 774  ? 26.697  43.414  56.194  1.00 30.45 ? 772  ALA B C     1 
ATOM   14368 O O     . ALA B  1 774  ? 25.893  43.939  56.971  1.00 31.06 ? 772  ALA B O     1 
ATOM   14369 C CB    . ALA B  1 774  ? 26.676  40.923  56.410  1.00 31.24 ? 772  ALA B CB    1 
ATOM   14370 N N     . ALA B  1 775  ? 26.891  43.843  54.941  1.00 32.57 ? 773  ALA B N     1 
ATOM   14371 C CA    . ALA B  1 775  ? 26.318  45.099  54.463  1.00 33.23 ? 773  ALA B CA    1 
ATOM   14372 C C     . ALA B  1 775  ? 24.790  45.108  54.474  1.00 31.17 ? 773  ALA B C     1 
ATOM   14373 O O     . ALA B  1 775  ? 24.182  46.175  54.618  1.00 32.46 ? 773  ALA B O     1 
ATOM   14374 C CB    . ALA B  1 775  ? 26.824  45.390  53.051  1.00 35.07 ? 773  ALA B CB    1 
ATOM   14375 N N     . GLU B  1 776  ? 24.142  43.959  54.300  1.00 30.01 ? 774  GLU B N     1 
ATOM   14376 C CA    . GLU B  1 776  ? 22.684  43.953  54.205  1.00 27.02 ? 774  GLU B CA    1 
ATOM   14377 C C     . GLU B  1 776  ? 21.991  43.741  55.545  1.00 25.72 ? 774  GLU B C     1 
ATOM   14378 O O     . GLU B  1 776  ? 20.756  43.725  55.590  1.00 26.45 ? 774  GLU B O     1 
ATOM   14379 C CB    . GLU B  1 776  ? 22.217  42.879  53.218  1.00 28.96 ? 774  GLU B CB    1 
ATOM   14380 C CG    . GLU B  1 776  ? 22.756  43.035  51.799  1.00 31.15 ? 774  GLU B CG    1 
ATOM   14381 C CD    . GLU B  1 776  ? 24.093  42.339  51.597  1.00 36.89 ? 774  GLU B CD    1 
ATOM   14382 O OE1   . GLU B  1 776  ? 24.688  41.859  52.589  1.00 37.65 ? 774  GLU B OE1   1 
ATOM   14383 O OE2   . GLU B  1 776  ? 24.552  42.268  50.442  1.00 40.48 ? 774  GLU B OE2   1 
ATOM   14384 N N     . THR B  1 777  ? 22.748  43.575  56.629  1.00 25.81 ? 775  THR B N     1 
ATOM   14385 C CA    . THR B  1 777  ? 22.159  43.374  57.943  1.00 28.29 ? 775  THR B CA    1 
ATOM   14386 C C     . THR B  1 777  ? 21.400  44.624  58.374  1.00 26.68 ? 775  THR B C     1 
ATOM   14387 O O     . THR B  1 777  ? 21.953  45.727  58.378  1.00 27.44 ? 775  THR B O     1 
ATOM   14388 C CB    . THR B  1 777  ? 23.259  43.020  58.946  1.00 26.20 ? 775  THR B CB    1 
ATOM   14389 O OG1   . THR B  1 777  ? 23.781  41.720  58.631  1.00 27.72 ? 775  THR B OG1   1 
ATOM   14390 C CG2   . THR B  1 777  ? 22.728  43.029  60.385  1.00 25.83 ? 775  THR B CG2   1 
ATOM   14391 N N     . ALA B  1 778  ? 20.119  44.458  58.704  1.00 23.66 ? 776  ALA B N     1 
ATOM   14392 C CA    . ALA B  1 778  ? 19.240  45.593  58.969  1.00 24.00 ? 776  ALA B CA    1 
ATOM   14393 C C     . ALA B  1 778  ? 18.856  45.717  60.436  1.00 25.31 ? 776  ALA B C     1 
ATOM   14394 O O     . ALA B  1 778  ? 18.155  46.661  60.803  1.00 25.00 ? 776  ALA B O     1 
ATOM   14395 C CB    . ALA B  1 778  ? 17.964  45.495  58.130  1.00 24.85 ? 776  ALA B CB    1 
ATOM   14396 N N     . GLY B  1 779  ? 19.308  44.802  61.277  1.00 24.95 ? 777  GLY B N     1 
ATOM   14397 C CA    . GLY B  1 779  ? 19.041  44.867  62.694  1.00 23.42 ? 777  GLY B CA    1 
ATOM   14398 C C     . GLY B  1 779  ? 19.665  43.661  63.348  1.00 22.32 ? 777  GLY B C     1 
ATOM   14399 O O     . GLY B  1 779  ? 19.926  42.641  62.698  1.00 20.73 ? 777  GLY B O     1 
ATOM   14400 N N     . VAL B  1 780  ? 19.931  43.804  64.646  1.00 20.83 ? 778  VAL B N     1 
ATOM   14401 C CA    . VAL B  1 780  ? 20.558  42.734  65.411  1.00 22.98 ? 778  VAL B CA    1 
ATOM   14402 C C     . VAL B  1 780  ? 19.758  42.529  66.684  1.00 19.31 ? 778  VAL B C     1 
ATOM   14403 O O     . VAL B  1 780  ? 19.381  43.494  67.355  1.00 20.41 ? 778  VAL B O     1 
ATOM   14404 C CB    . VAL B  1 780  ? 22.045  43.017  65.741  1.00 20.67 ? 778  VAL B CB    1 
ATOM   14405 C CG1   . VAL B  1 780  ? 22.610  41.898  66.578  1.00 20.53 ? 778  VAL B CG1   1 
ATOM   14406 C CG2   . VAL B  1 780  ? 22.884  43.161  64.459  1.00 19.47 ? 778  VAL B CG2   1 
ATOM   14407 N N     . MET B  1 781  ? 19.501  41.271  67.015  1.00 19.31 ? 779  MET B N     1 
ATOM   14408 C CA    . MET B  1 781  ? 18.921  40.900  68.296  1.00 22.08 ? 779  MET B CA    1 
ATOM   14409 C C     . MET B  1 781  ? 19.948  40.041  69.011  1.00 22.90 ? 779  MET B C     1 
ATOM   14410 O O     . MET B  1 781  ? 20.396  39.023  68.472  1.00 21.21 ? 779  MET B O     1 
ATOM   14411 C CB    . MET B  1 781  ? 17.597  40.163  68.106  1.00 17.85 ? 779  MET B CB    1 
ATOM   14412 C CG    . MET B  1 781  ? 16.593  40.950  67.277  1.00 21.87 ? 779  MET B CG    1 
ATOM   14413 S SD    . MET B  1 781  ? 15.105  40.003  66.967  1.00 23.72 ? 779  MET B SD    1 
ATOM   14414 C CE    . MET B  1 781  ? 14.212  40.307  68.491  1.00 23.98 ? 779  MET B CE    1 
ATOM   14415 N N     . PHE B  1 782  ? 20.350  40.462  70.205  1.00 22.34 ? 780  PHE B N     1 
ATOM   14416 C CA    . PHE B  1 782  ? 21.462  39.803  70.868  1.00 22.91 ? 780  PHE B CA    1 
ATOM   14417 C C     . PHE B  1 782  ? 21.127  39.593  72.334  1.00 23.53 ? 780  PHE B C     1 
ATOM   14418 O O     . PHE B  1 782  ? 20.627  40.502  72.994  1.00 23.98 ? 780  PHE B O     1 
ATOM   14419 C CB    . PHE B  1 782  ? 22.753  40.629  70.731  1.00 22.42 ? 780  PHE B CB    1 
ATOM   14420 C CG    . PHE B  1 782  ? 23.868  40.159  71.611  1.00 23.36 ? 780  PHE B CG    1 
ATOM   14421 C CD1   . PHE B  1 782  ? 24.674  39.093  71.227  1.00 20.77 ? 780  PHE B CD1   1 
ATOM   14422 C CD2   . PHE B  1 782  ? 24.109  40.777  72.831  1.00 23.35 ? 780  PHE B CD2   1 
ATOM   14423 C CE1   . PHE B  1 782  ? 25.708  38.654  72.041  1.00 23.92 ? 780  PHE B CE1   1 
ATOM   14424 C CE2   . PHE B  1 782  ? 25.134  40.339  73.651  1.00 25.05 ? 780  PHE B CE2   1 
ATOM   14425 C CZ    . PHE B  1 782  ? 25.930  39.279  73.255  1.00 25.15 ? 780  PHE B CZ    1 
ATOM   14426 N N     . THR B  1 783  ? 21.398  38.397  72.837  1.00 22.23 ? 781  THR B N     1 
ATOM   14427 C CA    . THR B  1 783  ? 21.309  38.124  74.266  1.00 25.06 ? 781  THR B CA    1 
ATOM   14428 C C     . THR B  1 783  ? 22.617  37.469  74.673  1.00 26.24 ? 781  THR B C     1 
ATOM   14429 O O     . THR B  1 783  ? 23.011  36.452  74.091  1.00 25.83 ? 781  THR B O     1 
ATOM   14430 C CB    . THR B  1 783  ? 20.089  37.247  74.592  1.00 24.66 ? 781  THR B CB    1 
ATOM   14431 O OG1   . THR B  1 783  ? 18.905  37.882  74.091  1.00 20.92 ? 781  THR B OG1   1 
ATOM   14432 C CG2   . THR B  1 783  ? 19.924  37.069  76.088  1.00 27.84 ? 781  THR B CG2   1 
ATOM   14433 N N     . GLY B  1 784  ? 23.313  38.080  75.633  1.00 24.14 ? 782  GLY B N     1 
ATOM   14434 C CA    . GLY B  1 784  ? 24.620  37.587  76.037  1.00 24.28 ? 782  GLY B CA    1 
ATOM   14435 C C     . GLY B  1 784  ? 25.343  38.627  76.877  1.00 22.89 ? 782  GLY B C     1 
ATOM   14436 O O     . GLY B  1 784  ? 24.712  39.487  77.500  1.00 26.64 ? 782  GLY B O     1 
ATOM   14437 N N     . SER B  1 785  ? 26.670  38.555  76.855  1.00 25.56 ? 783  SER B N     1 
ATOM   14438 C CA    . SER B  1 785  ? 27.482  39.405  77.721  1.00 28.41 ? 783  SER B CA    1 
ATOM   14439 C C     . SER B  1 785  ? 27.370  40.877  77.330  1.00 30.86 ? 783  SER B C     1 
ATOM   14440 O O     . SER B  1 785  ? 27.151  41.222  76.169  1.00 24.44 ? 783  SER B O     1 
ATOM   14441 C CB    . SER B  1 785  ? 28.946  38.975  77.678  1.00 28.58 ? 783  SER B CB    1 
ATOM   14442 O OG    . SER B  1 785  ? 29.531  39.232  76.411  1.00 31.61 ? 783  SER B OG    1 
ATOM   14443 N N     . THR B  1 786  ? 27.515  41.752  78.330  1.00 28.86 ? 784  THR B N     1 
ATOM   14444 C CA    . THR B  1 786  ? 27.623  43.183  78.058  1.00 31.42 ? 784  THR B CA    1 
ATOM   14445 C C     . THR B  1 786  ? 28.766  43.476  77.094  1.00 31.13 ? 784  THR B C     1 
ATOM   14446 O O     . THR B  1 786  ? 28.628  44.314  76.193  1.00 31.00 ? 784  THR B O     1 
ATOM   14447 C CB    . THR B  1 786  ? 27.844  43.963  79.359  1.00 34.37 ? 784  THR B CB    1 
ATOM   14448 O OG1   . THR B  1 786  ? 26.728  43.782  80.238  1.00 35.12 ? 784  THR B OG1   1 
ATOM   14449 C CG2   . THR B  1 786  ? 28.009  45.441  79.064  1.00 36.60 ? 784  THR B CG2   1 
ATOM   14450 N N     . GLU B  1 787  ? 29.908  42.808  77.282  1.00 27.40 ? 785  GLU B N     1 
ATOM   14451 C CA    . GLU B  1 787  ? 31.093  43.105  76.485  1.00 29.63 ? 785  GLU B CA    1 
ATOM   14452 C C     . GLU B  1 787  ? 30.831  42.894  74.998  1.00 33.49 ? 785  GLU B C     1 
ATOM   14453 O O     . GLU B  1 787  ? 31.206  43.730  74.167  1.00 28.83 ? 785  GLU B O     1 
ATOM   14454 C CB    . GLU B  1 787  ? 32.271  42.241  76.944  1.00 38.07 ? 785  GLU B CB    1 
ATOM   14455 N N     . VAL B  1 788  ? 30.191  41.776  74.643  1.00 27.84 ? 786  VAL B N     1 
ATOM   14456 C CA    . VAL B  1 788  ? 29.926  41.502  73.231  1.00 28.72 ? 786  VAL B CA    1 
ATOM   14457 C C     . VAL B  1 788  ? 28.864  42.452  72.685  1.00 27.19 ? 786  VAL B C     1 
ATOM   14458 O O     . VAL B  1 788  ? 28.921  42.847  71.516  1.00 29.53 ? 786  VAL B O     1 
ATOM   14459 C CB    . VAL B  1 788  ? 29.520  40.026  73.036  1.00 30.48 ? 786  VAL B CB    1 
ATOM   14460 C CG1   . VAL B  1 788  ? 29.092  39.763  71.602  1.00 27.74 ? 786  VAL B CG1   1 
ATOM   14461 C CG2   . VAL B  1 788  ? 30.670  39.109  73.416  1.00 31.42 ? 786  VAL B CG2   1 
ATOM   14462 N N     . ALA B  1 789  ? 27.891  42.845  73.510  1.00 24.58 ? 787  ALA B N     1 
ATOM   14463 C CA    . ALA B  1 789  ? 26.882  43.791  73.043  1.00 26.28 ? 787  ALA B CA    1 
ATOM   14464 C C     . ALA B  1 789  ? 27.515  45.122  72.642  1.00 28.69 ? 787  ALA B C     1 
ATOM   14465 O O     . ALA B  1 789  ? 27.085  45.746  71.664  1.00 23.84 ? 787  ALA B O     1 
ATOM   14466 C CB    . ALA B  1 789  ? 25.810  44.007  74.111  1.00 26.22 ? 787  ALA B CB    1 
ATOM   14467 N N     . ARG B  1 790  ? 28.528  45.580  73.397  1.00 27.34 ? 788  ARG B N     1 
ATOM   14468 C CA    . ARG B  1 790  ? 29.198  46.831  73.049  1.00 28.35 ? 788  ARG B CA    1 
ATOM   14469 C C     . ARG B  1 790  ? 29.999  46.681  71.765  1.00 25.97 ? 788  ARG B C     1 
ATOM   14470 O O     . ARG B  1 790  ? 30.086  47.619  70.966  1.00 31.43 ? 788  ARG B O     1 
ATOM   14471 C CB    . ARG B  1 790  ? 30.113  47.300  74.194  1.00 28.91 ? 788  ARG B CB    1 
ATOM   14472 C CG    . ARG B  1 790  ? 29.422  47.499  75.533  1.00 31.99 ? 788  ARG B CG    1 
ATOM   14473 C CD    . ARG B  1 790  ? 28.183  48.397  75.447  1.00 38.33 ? 788  ARG B CD    1 
ATOM   14474 N NE    . ARG B  1 790  ? 28.477  49.705  74.866  1.00 42.03 ? 788  ARG B NE    1 
ATOM   14475 C CZ    . ARG B  1 790  ? 28.708  50.812  75.561  1.00 37.80 ? 788  ARG B CZ    1 
ATOM   14476 N NH1   . ARG B  1 790  ? 28.682  50.820  76.884  1.00 34.86 ? 788  ARG B NH1   1 
ATOM   14477 N NH2   . ARG B  1 790  ? 28.964  51.944  74.908  1.00 37.66 ? 788  ARG B NH2   1 
ATOM   14478 N N     . LEU B  1 791  ? 30.588  45.511  71.543  1.00 23.64 ? 789  LEU B N     1 
ATOM   14479 C CA    . LEU B  1 791  ? 31.300  45.278  70.293  1.00 26.00 ? 789  LEU B CA    1 
ATOM   14480 C C     . LEU B  1 791  ? 30.338  45.299  69.113  1.00 27.44 ? 789  LEU B C     1 
ATOM   14481 O O     . LEU B  1 791  ? 30.626  45.910  68.075  1.00 27.33 ? 789  LEU B O     1 
ATOM   14482 C CB    . LEU B  1 791  ? 32.044  43.949  70.344  1.00 30.17 ? 789  LEU B CB    1 
ATOM   14483 C CG    . LEU B  1 791  ? 33.229  43.799  71.298  1.00 32.10 ? 789  LEU B CG    1 
ATOM   14484 C CD1   . LEU B  1 791  ? 33.755  42.377  71.208  1.00 34.07 ? 789  LEU B CD1   1 
ATOM   14485 C CD2   . LEU B  1 791  ? 34.327  44.810  70.956  1.00 28.95 ? 789  LEU B CD2   1 
ATOM   14486 N N     . ILE B  1 792  ? 29.184  44.647  69.259  1.00 24.38 ? 790  ILE B N     1 
ATOM   14487 C CA    . ILE B  1 792  ? 28.167  44.689  68.204  1.00 24.49 ? 790  ILE B CA    1 
ATOM   14488 C C     . ILE B  1 792  ? 27.708  46.119  67.959  1.00 25.25 ? 790  ILE B C     1 
ATOM   14489 O O     . ILE B  1 792  ? 27.555  46.554  66.811  1.00 27.30 ? 790  ILE B O     1 
ATOM   14490 C CB    . ILE B  1 792  ? 26.983  43.774  68.565  1.00 20.66 ? 790  ILE B CB    1 
ATOM   14491 C CG1   . ILE B  1 792  ? 27.405  42.305  68.563  1.00 21.98 ? 790  ILE B CG1   1 
ATOM   14492 C CG2   . ILE B  1 792  ? 25.796  44.010  67.613  1.00 21.97 ? 790  ILE B CG2   1 
ATOM   14493 C CD1   . ILE B  1 792  ? 26.360  41.398  69.191  1.00 24.37 ? 790  ILE B CD1   1 
ATOM   14494 N N     . GLN B  1 793  ? 27.460  46.867  69.033  1.00 26.19 ? 791  GLN B N     1 
ATOM   14495 C CA    . GLN B  1 793  ? 27.003  48.243  68.892  1.00 27.78 ? 791  GLN B CA    1 
ATOM   14496 C C     . GLN B  1 793  ? 28.011  49.093  68.121  1.00 26.29 ? 791  GLN B C     1 
ATOM   14497 O O     . GLN B  1 793  ? 27.628  49.901  67.270  1.00 28.18 ? 791  GLN B O     1 
ATOM   14498 C CB    . GLN B  1 793  ? 26.742  48.833  70.279  1.00 29.65 ? 791  GLN B CB    1 
ATOM   14499 C CG    . GLN B  1 793  ? 26.439  50.313  70.279  1.00 27.95 ? 791  GLN B CG    1 
ATOM   14500 C CD    . GLN B  1 793  ? 26.726  50.950  71.617  1.00 32.18 ? 791  GLN B CD    1 
ATOM   14501 O OE1   . GLN B  1 793  ? 27.735  50.637  72.270  1.00 29.84 ? 791  GLN B OE1   1 
ATOM   14502 N NE2   . GLN B  1 793  ? 25.837  51.838  72.047  1.00 35.44 ? 791  GLN B NE2   1 
ATOM   14503 N N     . ALA B  1 794  ? 29.306  48.926  68.402  1.00 27.63 ? 792  ALA B N     1 
ATOM   14504 C CA    . ALA B  1 794  ? 30.320  49.697  67.688  1.00 31.73 ? 792  ALA B CA    1 
ATOM   14505 C C     . ALA B  1 794  ? 30.383  49.300  66.220  1.00 31.87 ? 792  ALA B C     1 
ATOM   14506 O O     . ALA B  1 794  ? 30.556  50.157  65.346  1.00 30.75 ? 792  ALA B O     1 
ATOM   14507 C CB    . ALA B  1 794  ? 31.690  49.514  68.346  1.00 28.49 ? 792  ALA B CB    1 
ATOM   14508 N N     . GLN B  1 795  ? 30.261  48.005  65.930  1.00 28.74 ? 793  GLN B N     1 
ATOM   14509 C CA    . GLN B  1 795  ? 30.259  47.570  64.538  1.00 30.54 ? 793  GLN B CA    1 
ATOM   14510 C C     . GLN B  1 795  ? 29.087  48.180  63.774  1.00 30.48 ? 793  GLN B C     1 
ATOM   14511 O O     . GLN B  1 795  ? 29.259  48.667  62.645  1.00 28.68 ? 793  GLN B O     1 
ATOM   14512 C CB    . GLN B  1 795  ? 30.225  46.043  64.476  1.00 32.05 ? 793  GLN B CB    1 
ATOM   14513 C CG    . GLN B  1 795  ? 30.183  45.482  63.064  1.00 36.36 ? 793  GLN B CG    1 
ATOM   14514 C CD    . GLN B  1 795  ? 31.516  45.625  62.344  1.00 39.87 ? 793  GLN B CD    1 
ATOM   14515 O OE1   . GLN B  1 795  ? 32.545  45.160  62.830  1.00 46.97 ? 793  GLN B OE1   1 
ATOM   14516 N NE2   . GLN B  1 795  ? 31.501  46.279  61.184  1.00 41.21 ? 793  GLN B NE2   1 
ATOM   14517 N N     . LEU B  1 796  ? 27.891  48.184  64.385  1.00 26.23 ? 794  LEU B N     1 
ATOM   14518 C CA    . LEU B  1 796  ? 26.699  48.714  63.724  1.00 27.25 ? 794  LEU B CA    1 
ATOM   14519 C C     . LEU B  1 796  ? 26.763  50.224  63.549  1.00 29.51 ? 794  LEU B C     1 
ATOM   14520 O O     . LEU B  1 796  ? 26.208  50.754  62.583  1.00 32.70 ? 794  LEU B O     1 
ATOM   14521 C CB    . LEU B  1 796  ? 25.441  48.358  64.517  1.00 27.30 ? 794  LEU B CB    1 
ATOM   14522 C CG    . LEU B  1 796  ? 25.055  46.883  64.589  1.00 26.26 ? 794  LEU B CG    1 
ATOM   14523 C CD1   . LEU B  1 796  ? 23.830  46.697  65.483  1.00 23.81 ? 794  LEU B CD1   1 
ATOM   14524 C CD2   . LEU B  1 796  ? 24.807  46.354  63.178  1.00 25.21 ? 794  LEU B CD2   1 
ATOM   14525 N N     . ALA B  1 797  ? 27.423  50.929  64.468  1.00 30.05 ? 795  ALA B N     1 
ATOM   14526 C CA    . ALA B  1 797  ? 27.440  52.389  64.423  1.00 32.99 ? 795  ALA B CA    1 
ATOM   14527 C C     . ALA B  1 797  ? 28.175  52.922  63.203  1.00 33.92 ? 795  ALA B C     1 
ATOM   14528 O O     . ALA B  1 797  ? 28.079  54.118  62.906  1.00 35.16 ? 795  ALA B O     1 
ATOM   14529 C CB    . ALA B  1 797  ? 28.085  52.953  65.690  1.00 31.87 ? 795  ALA B CB    1 
ATOM   14530 N N     . ASP B  1 798  ? 28.930  52.071  62.507  1.00 31.43 ? 796  ASP B N     1 
ATOM   14531 C CA    . ASP B  1 798  ? 29.591  52.494  61.284  1.00 35.80 ? 796  ASP B CA    1 
ATOM   14532 C C     . ASP B  1 798  ? 28.624  52.600  60.114  1.00 35.09 ? 796  ASP B C     1 
ATOM   14533 O O     . ASP B  1 798  ? 28.914  53.320  59.152  1.00 39.26 ? 796  ASP B O     1 
ATOM   14534 C CB    . ASP B  1 798  ? 30.708  51.514  60.941  1.00 38.56 ? 796  ASP B CB    1 
ATOM   14535 C CG    . ASP B  1 798  ? 31.833  52.164  60.167  1.00 39.78 ? 796  ASP B CG    1 
ATOM   14536 O OD1   . ASP B  1 798  ? 32.531  53.024  60.742  1.00 50.06 ? 796  ASP B OD1   1 
ATOM   14537 O OD2   . ASP B  1 798  ? 32.020  51.812  58.987  1.00 44.63 ? 796  ASP B OD2   1 
ATOM   14538 N N     . ARG B  1 799  ? 27.498  51.900  60.172  1.00 33.71 ? 797  ARG B N     1 
ATOM   14539 C CA    . ARG B  1 799  ? 26.567  51.796  59.059  1.00 32.94 ? 797  ARG B CA    1 
ATOM   14540 C C     . ARG B  1 799  ? 25.276  52.543  59.358  1.00 33.00 ? 797  ARG B C     1 
ATOM   14541 O O     . ARG B  1 799  ? 24.941  52.838  60.508  1.00 32.30 ? 797  ARG B O     1 
ATOM   14542 C CB    . ARG B  1 799  ? 26.240  50.325  58.745  1.00 36.45 ? 797  ARG B CB    1 
ATOM   14543 C CG    . ARG B  1 799  ? 27.456  49.454  58.425  1.00 39.63 ? 797  ARG B CG    1 
ATOM   14544 C CD    . ARG B  1 799  ? 27.090  48.159  57.689  1.00 41.51 ? 797  ARG B CD    1 
ATOM   14545 N NE    . ARG B  1 799  ? 26.696  47.067  58.577  1.00 43.23 ? 797  ARG B NE    1 
ATOM   14546 C CZ    . ARG B  1 799  ? 25.440  46.695  58.796  1.00 41.72 ? 797  ARG B CZ    1 
ATOM   14547 N NH1   . ARG B  1 799  ? 24.424  47.318  58.222  1.00 35.77 ? 797  ARG B NH1   1 
ATOM   14548 N NH2   . ARG B  1 799  ? 25.198  45.666  59.603  1.00 41.58 ? 797  ARG B NH2   1 
ATOM   14549 N N     . LEU B  1 800  ? 24.548  52.841  58.293  1.00 34.36 ? 798  LEU B N     1 
ATOM   14550 C CA    . LEU B  1 800  ? 23.184  53.326  58.365  1.00 30.88 ? 798  LEU B CA    1 
ATOM   14551 C C     . LEU B  1 800  ? 22.299  52.388  57.556  1.00 34.20 ? 798  LEU B C     1 
ATOM   14552 O O     . LEU B  1 800  ? 22.780  51.664  56.680  1.00 32.44 ? 798  LEU B O     1 
ATOM   14553 C CB    . LEU B  1 800  ? 23.060  54.764  57.836  1.00 32.81 ? 798  LEU B CB    1 
ATOM   14554 C CG    . LEU B  1 800  ? 23.685  55.874  58.686  1.00 29.68 ? 798  LEU B CG    1 
ATOM   14555 C CD1   . LEU B  1 800  ? 23.512  57.223  58.002  1.00 32.81 ? 798  LEU B CD1   1 
ATOM   14556 C CD2   . LEU B  1 800  ? 23.061  55.901  60.059  1.00 27.24 ? 798  LEU B CD2   1 
ATOM   14557 N N     . SER B  1 801  ? 21.000  52.405  57.876  1.00 32.42 ? 799  SER B N     1 
ATOM   14558 C CA    . SER B  1 801  ? 20.007  51.602  57.179  1.00 34.38 ? 799  SER B CA    1 
ATOM   14559 C C     . SER B  1 801  ? 19.835  52.109  55.756  1.00 38.38 ? 799  SER B C     1 
ATOM   14560 O O     . SER B  1 801  ? 20.308  53.194  55.414  1.00 35.79 ? 799  SER B O     1 
ATOM   14561 C CB    . SER B  1 801  ? 18.669  51.655  57.919  1.00 36.63 ? 799  SER B CB    1 
ATOM   14562 O OG    . SER B  1 801  ? 17.979  52.869  57.654  1.00 34.32 ? 799  SER B OG    1 
ATOM   14563 N N     . PRO B  1 802  ? 19.153  51.340  54.893  1.00 41.04 ? 800  PRO B N     1 
ATOM   14564 C CA    . PRO B  1 802  ? 18.783  51.888  53.576  1.00 44.07 ? 800  PRO B CA    1 
ATOM   14565 C C     . PRO B  1 802  ? 18.116  53.253  53.663  1.00 43.71 ? 800  PRO B C     1 
ATOM   14566 O O     . PRO B  1 802  ? 18.344  54.106  52.798  1.00 45.04 ? 800  PRO B O     1 
ATOM   14567 C CB    . PRO B  1 802  ? 17.831  50.820  53.016  1.00 41.95 ? 800  PRO B CB    1 
ATOM   14568 C CG    . PRO B  1 802  ? 18.308  49.539  53.640  1.00 43.00 ? 800  PRO B CG    1 
ATOM   14569 C CD    . PRO B  1 802  ? 18.827  49.904  55.011  1.00 39.25 ? 800  PRO B CD    1 
ATOM   14570 N N     . ALA B  1 803  ? 17.310  53.487  54.699  1.00 40.12 ? 801  ALA B N     1 
ATOM   14571 C CA    . ALA B  1 803  ? 16.617  54.757  54.872  1.00 38.71 ? 801  ALA B CA    1 
ATOM   14572 C C     . ALA B  1 803  ? 17.464  55.816  55.566  1.00 39.03 ? 801  ALA B C     1 
ATOM   14573 O O     . ALA B  1 803  ? 16.936  56.887  55.875  1.00 39.97 ? 801  ALA B O     1 
ATOM   14574 C CB    . ALA B  1 803  ? 15.321  54.545  55.665  1.00 37.66 ? 801  ALA B CB    1 
ATOM   14575 N N     . GLY B  1 804  ? 18.738  55.539  55.845  1.00 37.09 ? 802  GLY B N     1 
ATOM   14576 C CA    . GLY B  1 804  ? 19.596  56.513  56.499  1.00 36.15 ? 802  GLY B CA    1 
ATOM   14577 C C     . GLY B  1 804  ? 19.453  56.630  58.004  1.00 36.28 ? 802  GLY B C     1 
ATOM   14578 O O     . GLY B  1 804  ? 19.695  57.713  58.556  1.00 32.63 ? 802  GLY B O     1 
ATOM   14579 N N     . ARG B  1 805  ? 19.085  55.550  58.690  1.00 31.09 ? 803  ARG B N     1 
ATOM   14580 C CA    . ARG B  1 805  ? 18.871  55.563  60.128  1.00 32.52 ? 803  ARG B CA    1 
ATOM   14581 C C     . ARG B  1 805  ? 19.796  54.577  60.829  1.00 28.31 ? 803  ARG B C     1 
ATOM   14582 O O     . ARG B  1 805  ? 20.300  53.633  60.211  1.00 28.87 ? 803  ARG B O     1 
ATOM   14583 C CB    . ARG B  1 805  ? 17.417  55.213  60.482  1.00 30.31 ? 803  ARG B CB    1 
ATOM   14584 C CG    . ARG B  1 805  ? 16.403  56.186  59.965  1.00 33.87 ? 803  ARG B CG    1 
ATOM   14585 C CD    . ARG B  1 805  ? 15.033  55.879  60.551  1.00 39.38 ? 803  ARG B CD    1 
ATOM   14586 N NE    . ARG B  1 805  ? 13.972  56.436  59.720  1.00 45.22 ? 803  ARG B NE    1 
ATOM   14587 C CZ    . ARG B  1 805  ? 13.280  55.737  58.829  1.00 45.25 ? 803  ARG B CZ    1 
ATOM   14588 N NH1   . ARG B  1 805  ? 13.478  54.438  58.665  1.00 39.57 ? 803  ARG B NH1   1 
ATOM   14589 N NH2   . ARG B  1 805  ? 12.361  56.355  58.092  1.00 51.53 ? 803  ARG B NH2   1 
ATOM   14590 N N     . PRO B  1 806  ? 20.018  54.751  62.130  1.00 29.24 ? 804  PRO B N     1 
ATOM   14591 C CA    . PRO B  1 806  ? 20.770  53.742  62.880  1.00 30.92 ? 804  PRO B CA    1 
ATOM   14592 C C     . PRO B  1 806  ? 20.135  52.362  62.746  1.00 26.34 ? 804  PRO B C     1 
ATOM   14593 O O     . PRO B  1 806  ? 18.908  52.221  62.694  1.00 28.95 ? 804  PRO B O     1 
ATOM   14594 C CB    . PRO B  1 806  ? 20.708  54.259  64.323  1.00 29.94 ? 804  PRO B CB    1 
ATOM   14595 C CG    . PRO B  1 806  ? 20.574  55.748  64.176  1.00 26.67 ? 804  PRO B CG    1 
ATOM   14596 C CD    . PRO B  1 806  ? 19.636  55.893  62.982  1.00 29.66 ? 804  PRO B CD    1 
ATOM   14597 N N     . ILE B  1 807  ? 20.991  51.347  62.663  1.00 26.24 ? 805  ILE B N     1 
ATOM   14598 C CA    . ILE B  1 807  ? 20.582  49.944  62.657  1.00 26.60 ? 805  ILE B CA    1 
ATOM   14599 C C     . ILE B  1 807  ? 20.117  49.567  64.059  1.00 27.81 ? 805  ILE B C     1 
ATOM   14600 O O     . ILE B  1 807  ? 20.901  49.676  65.013  1.00 26.31 ? 805  ILE B O     1 
ATOM   14601 C CB    . ILE B  1 807  ? 21.729  49.024  62.210  1.00 29.22 ? 805  ILE B CB    1 
ATOM   14602 C CG1   . ILE B  1 807  ? 22.313  49.490  60.876  1.00 32.10 ? 805  ILE B CG1   1 
ATOM   14603 C CG2   . ILE B  1 807  ? 21.246  47.585  62.102  1.00 25.04 ? 805  ILE B CG2   1 
ATOM   14604 C CD1   . ILE B  1 807  ? 21.361  49.367  59.736  1.00 32.37 ? 805  ILE B CD1   1 
ATOM   14605 N N     . PRO B  1 808  ? 18.865  49.146  64.240  1.00 26.66 ? 806  PRO B N     1 
ATOM   14606 C CA    . PRO B  1 808  ? 18.406  48.770  65.584  1.00 26.94 ? 806  PRO B CA    1 
ATOM   14607 C C     . PRO B  1 808  ? 19.229  47.624  66.159  1.00 27.16 ? 806  PRO B C     1 
ATOM   14608 O O     . PRO B  1 808  ? 19.591  46.674  65.461  1.00 26.11 ? 806  PRO B O     1 
ATOM   14609 C CB    . PRO B  1 808  ? 16.946  48.360  65.353  1.00 29.12 ? 806  PRO B CB    1 
ATOM   14610 C CG    . PRO B  1 808  ? 16.529  49.113  64.157  1.00 29.91 ? 806  PRO B CG    1 
ATOM   14611 C CD    . PRO B  1 808  ? 17.753  49.188  63.271  1.00 27.36 ? 806  PRO B CD    1 
ATOM   14612 N N     . LEU B  1 809  ? 19.565  47.746  67.440  1.00 24.62 ? 807  LEU B N     1 
ATOM   14613 C CA    . LEU B  1 809  ? 20.143  46.659  68.215  1.00 22.64 ? 807  LEU B CA    1 
ATOM   14614 C C     . LEU B  1 809  ? 19.270  46.450  69.443  1.00 24.93 ? 807  LEU B C     1 
ATOM   14615 O O     . LEU B  1 809  ? 19.070  47.381  70.231  1.00 24.42 ? 807  LEU B O     1 
ATOM   14616 C CB    . LEU B  1 809  ? 21.587  46.972  68.617  1.00 25.19 ? 807  LEU B CB    1 
ATOM   14617 C CG    . LEU B  1 809  ? 22.260  46.089  69.667  1.00 26.47 ? 807  LEU B CG    1 
ATOM   14618 C CD1   . LEU B  1 809  ? 22.409  44.643  69.201  1.00 22.61 ? 807  LEU B CD1   1 
ATOM   14619 C CD2   . LEU B  1 809  ? 23.634  46.672  70.058  1.00 26.62 ? 807  LEU B CD2   1 
ATOM   14620 N N     . ILE B  1 810  ? 18.742  45.241  69.593  1.00 23.04 ? 808  ILE B N     1 
ATOM   14621 C CA    . ILE B  1 810  ? 18.025  44.827  70.791  1.00 22.89 ? 808  ILE B CA    1 
ATOM   14622 C C     . ILE B  1 810  ? 18.956  43.891  71.533  1.00 25.98 ? 808  ILE B C     1 
ATOM   14623 O O     . ILE B  1 810  ? 19.342  42.838  71.006  1.00 22.68 ? 808  ILE B O     1 
ATOM   14624 C CB    . ILE B  1 810  ? 16.686  44.144  70.465  1.00 24.80 ? 808  ILE B CB    1 
ATOM   14625 C CG1   . ILE B  1 810  ? 15.769  45.100  69.725  1.00 26.93 ? 808  ILE B CG1   1 
ATOM   14626 C CG2   . ILE B  1 810  ? 16.007  43.663  71.740  1.00 28.05 ? 808  ILE B CG2   1 
ATOM   14627 C CD1   . ILE B  1 810  ? 14.455  44.454  69.350  1.00 29.70 ? 808  ILE B CD1   1 
ATOM   14628 N N     . ALA B  1 811  ? 19.356  44.294  72.736  1.00 25.01 ? 809  ALA B N     1 
ATOM   14629 C CA    . ALA B  1 811  ? 20.339  43.547  73.503  1.00 27.81 ? 809  ALA B CA    1 
ATOM   14630 C C     . ALA B  1 811  ? 19.821  43.370  74.921  1.00 29.00 ? 809  ALA B C     1 
ATOM   14631 O O     . ALA B  1 811  ? 19.433  44.346  75.571  1.00 27.73 ? 809  ALA B O     1 
ATOM   14632 C CB    . ALA B  1 811  ? 21.703  44.253  73.494  1.00 28.45 ? 809  ALA B CB    1 
ATOM   14633 N N     . GLU B  1 812  ? 19.776  42.121  75.379  1.00 27.64 ? 810  GLU B N     1 
ATOM   14634 C CA    . GLU B  1 812  ? 19.514  41.794  76.775  1.00 30.27 ? 810  GLU B CA    1 
ATOM   14635 C C     . GLU B  1 812  ? 20.817  41.257  77.346  1.00 27.72 ? 810  GLU B C     1 
ATOM   14636 O O     . GLU B  1 812  ? 21.386  40.303  76.807  1.00 25.11 ? 810  GLU B O     1 
ATOM   14637 C CB    . GLU B  1 812  ? 18.376  40.776  76.918  1.00 30.55 ? 810  GLU B CB    1 
ATOM   14638 C CG    . GLU B  1 812  ? 17.820  40.646  78.366  1.00 36.04 ? 810  GLU B CG    1 
ATOM   14639 C CD    . GLU B  1 812  ? 18.315  39.401  79.114  1.00 41.32 ? 810  GLU B CD    1 
ATOM   14640 O OE1   . GLU B  1 812  ? 17.833  38.277  78.813  1.00 40.57 ? 810  GLU B OE1   1 
ATOM   14641 O OE2   . GLU B  1 812  ? 19.192  39.543  80.005  1.00 42.34 ? 810  GLU B OE2   1 
ATOM   14642 N N     . THR B  1 813  ? 21.314  41.893  78.406  1.00 28.66 ? 811  THR B N     1 
ATOM   14643 C CA    . THR B  1 813  ? 22.679  41.637  78.834  1.00 26.56 ? 811  THR B CA    1 
ATOM   14644 C C     . THR B  1 813  ? 22.801  41.372  80.330  1.00 33.03 ? 811  THR B C     1 
ATOM   14645 O O     . THR B  1 813  ? 23.829  41.696  80.929  1.00 33.21 ? 811  THR B O     1 
ATOM   14646 C CB    . THR B  1 813  ? 23.603  42.794  78.435  1.00 31.43 ? 811  THR B CB    1 
ATOM   14647 O OG1   . THR B  1 813  ? 23.086  44.032  78.949  1.00 29.21 ? 811  THR B OG1   1 
ATOM   14648 C CG2   . THR B  1 813  ? 23.721  42.885  76.911  1.00 31.49 ? 811  THR B CG2   1 
ATOM   14649 N N     . GLY B  1 814  ? 21.794  40.774  80.958  1.00 29.38 ? 812  GLY B N     1 
ATOM   14650 C CA    . GLY B  1 814  ? 22.044  40.201  82.279  1.00 36.54 ? 812  GLY B CA    1 
ATOM   14651 C C     . GLY B  1 814  ? 21.990  41.199  83.425  1.00 33.66 ? 812  GLY B C     1 
ATOM   14652 O O     . GLY B  1 814  ? 21.573  42.347  83.273  1.00 30.38 ? 812  GLY B O     1 
ATOM   14653 N N     . GLY B  1 815  ? 22.419  40.741  84.600  1.00 31.10 ? 813  GLY B N     1 
ATOM   14654 C CA    . GLY B  1 815  ? 22.209  41.559  85.784  1.00 28.82 ? 813  GLY B CA    1 
ATOM   14655 C C     . GLY B  1 815  ? 23.002  41.073  86.978  1.00 31.31 ? 813  GLY B C     1 
ATOM   14656 O O     . GLY B  1 815  ? 23.578  39.983  86.982  1.00 35.80 ? 813  GLY B O     1 
ATOM   14657 N N     . GLN B  1 816  ? 23.001  41.907  88.005  1.00 26.86 ? 814  GLN B N     1 
ATOM   14658 C CA    . GLN B  1 816  ? 23.605  41.603  89.300  1.00 26.23 ? 814  GLN B CA    1 
ATOM   14659 C C     . GLN B  1 816  ? 22.475  41.645  90.318  1.00 24.42 ? 814  GLN B C     1 
ATOM   14660 O O     . GLN B  1 816  ? 22.326  42.614  91.062  1.00 27.46 ? 814  GLN B O     1 
ATOM   14661 C CB    . GLN B  1 816  ? 24.714  42.612  89.630  1.00 31.46 ? 814  GLN B CB    1 
ATOM   14662 C CG    . GLN B  1 816  ? 25.544  42.244  90.825  1.00 33.45 ? 814  GLN B CG    1 
ATOM   14663 C CD    . GLN B  1 816  ? 26.443  41.057  90.560  1.00 35.87 ? 814  GLN B CD    1 
ATOM   14664 O OE1   . GLN B  1 816  ? 25.966  39.952  90.327  1.00 36.01 ? 814  GLN B OE1   1 
ATOM   14665 N NE2   . GLN B  1 816  ? 27.758  41.280  90.599  1.00 41.11 ? 814  GLN B NE2   1 
ATOM   14666 N N     . ASN B  1 817  ? 21.656  40.599  90.328  1.00 24.20 ? 815  ASN B N     1 
ATOM   14667 C CA    . ASN B  1 817  ? 20.309  40.693  90.877  1.00 22.28 ? 815  ASN B CA    1 
ATOM   14668 C C     . ASN B  1 817  ? 20.302  40.444  92.375  1.00 19.95 ? 815  ASN B C     1 
ATOM   14669 O O     . ASN B  1 817  ? 20.949  39.515  92.862  1.00 21.61 ? 815  ASN B O     1 
ATOM   14670 C CB    . ASN B  1 817  ? 19.386  39.702  90.179  1.00 21.00 ? 815  ASN B CB    1 
ATOM   14671 C CG    . ASN B  1 817  ? 19.523  39.768  88.690  1.00 22.58 ? 815  ASN B CG    1 
ATOM   14672 O OD1   . ASN B  1 817  ? 19.347  40.834  88.101  1.00 20.04 ? 815  ASN B OD1   1 
ATOM   14673 N ND2   . ASN B  1 817  ? 19.913  38.651  88.073  1.00 21.10 ? 815  ASN B ND2   1 
ATOM   14674 N N     . ALA B  1 818  ? 19.535  41.262  93.086  1.00 21.53 ? 816  ALA B N     1 
ATOM   14675 C CA    . ALA B  1 818  ? 19.459  41.231  94.538  1.00 24.11 ? 816  ALA B CA    1 
ATOM   14676 C C     . ALA B  1 818  ? 18.067  40.830  94.998  1.00 21.15 ? 816  ALA B C     1 
ATOM   14677 O O     . ALA B  1 818  ? 17.079  40.952  94.267  1.00 20.77 ? 816  ALA B O     1 
ATOM   14678 C CB    . ALA B  1 818  ? 19.821  42.598  95.141  1.00 21.21 ? 816  ALA B CB    1 
ATOM   14679 N N     . MET B  1 819  ? 18.007  40.319  96.227  1.00 16.47 ? 817  MET B N     1 
ATOM   14680 C CA    . MET B  1 819  ? 16.760  40.157  96.956  1.00 18.41 ? 817  MET B CA    1 
ATOM   14681 C C     . MET B  1 819  ? 16.972  40.720  98.350  1.00 20.93 ? 817  MET B C     1 
ATOM   14682 O O     . MET B  1 819  ? 17.981  40.415  98.992  1.00 18.74 ? 817  MET B O     1 
ATOM   14683 C CB    . MET B  1 819  ? 16.309  38.695  97.035  1.00 21.13 ? 817  MET B CB    1 
ATOM   14684 C CG    . MET B  1 819  ? 15.099  38.448  97.971  1.00 20.35 ? 817  MET B CG    1 
ATOM   14685 S SD    . MET B  1 819  ? 14.843  36.663  98.221  1.00 24.20 ? 817  MET B SD    1 
ATOM   14686 C CE    . MET B  1 819  ? 14.202  36.198  96.615  1.00 21.04 ? 817  MET B CE    1 
ATOM   14687 N N     . ILE B  1 820  ? 16.035  41.547  98.801  1.00 21.68 ? 818  ILE B N     1 
ATOM   14688 C CA    . ILE B  1 820  ? 16.065  42.140  100.133 1.00 17.80 ? 818  ILE B CA    1 
ATOM   14689 C C     . ILE B  1 820  ? 15.013  41.443  100.981 1.00 20.36 ? 818  ILE B C     1 
ATOM   14690 O O     . ILE B  1 820  ? 13.862  41.301  100.562 1.00 20.04 ? 818  ILE B O     1 
ATOM   14691 C CB    . ILE B  1 820  ? 15.827  43.658  100.087 1.00 18.30 ? 818  ILE B CB    1 
ATOM   14692 C CG1   . ILE B  1 820  ? 16.961  44.361  99.338  1.00 20.14 ? 818  ILE B CG1   1 
ATOM   14693 C CG2   . ILE B  1 820  ? 15.702  44.235  101.509 1.00 19.35 ? 818  ILE B CG2   1 
ATOM   14694 C CD1   . ILE B  1 820  ? 16.821  45.893  99.339  1.00 21.41 ? 818  ILE B CD1   1 
ATOM   14695 N N     . VAL B  1 821  ? 15.421  40.967  102.149 1.00 18.55 ? 819  VAL B N     1 
ATOM   14696 C CA    . VAL B  1 821  ? 14.555  40.260  103.089 1.00 17.87 ? 819  VAL B CA    1 
ATOM   14697 C C     . VAL B  1 821  ? 14.579  41.013  104.412 1.00 23.90 ? 819  VAL B C     1 
ATOM   14698 O O     . VAL B  1 821  ? 15.657  41.253  104.965 1.00 22.25 ? 819  VAL B O     1 
ATOM   14699 C CB    . VAL B  1 821  ? 15.037  38.813  103.309 1.00 20.43 ? 819  VAL B CB    1 
ATOM   14700 C CG1   . VAL B  1 821  ? 14.148  38.089  104.326 1.00 19.26 ? 819  VAL B CG1   1 
ATOM   14701 C CG2   . VAL B  1 821  ? 15.058  38.068  101.993 1.00 18.83 ? 819  VAL B CG2   1 
ATOM   14702 N N     . ASP B  1 822  ? 13.404  41.364  104.934 1.00 23.60 ? 820  ASP B N     1 
ATOM   14703 C CA    . ASP B  1 822  ? 13.367  42.005  106.242 1.00 22.41 ? 820  ASP B CA    1 
ATOM   14704 C C     . ASP B  1 822  ? 12.904  41.009  107.302 1.00 23.01 ? 820  ASP B C     1 
ATOM   14705 O O     . ASP B  1 822  ? 12.644  39.836  107.029 1.00 22.52 ? 820  ASP B O     1 
ATOM   14706 C CB    . ASP B  1 822  ? 12.530  43.294  106.213 1.00 23.62 ? 820  ASP B CB    1 
ATOM   14707 C CG    . ASP B  1 822  ? 11.022  43.055  106.128 1.00 24.68 ? 820  ASP B CG    1 
ATOM   14708 O OD1   . ASP B  1 822  ? 10.543  41.913  106.280 1.00 24.53 ? 820  ASP B OD1   1 
ATOM   14709 O OD2   . ASP B  1 822  ? 10.303  44.057  105.895 1.00 27.55 ? 820  ASP B OD2   1 
ATOM   14710 N N     . SER B  1 823  ? 12.829  41.483  108.547 1.00 24.27 ? 821  SER B N     1 
ATOM   14711 C CA    . SER B  1 823  ? 12.528  40.591  109.658 1.00 25.72 ? 821  SER B CA    1 
ATOM   14712 C C     . SER B  1 823  ? 11.062  40.182  109.724 1.00 28.38 ? 821  SER B C     1 
ATOM   14713 O O     . SER B  1 823  ? 10.688  39.449  110.642 1.00 28.47 ? 821  SER B O     1 
ATOM   14714 C CB    . SER B  1 823  ? 12.939  41.256  110.973 1.00 25.65 ? 821  SER B CB    1 
ATOM   14715 O OG    . SER B  1 823  ? 12.180  42.433  111.168 1.00 26.90 ? 821  SER B OG    1 
ATOM   14716 N N     . SER B  1 824  ? 10.207  40.623  108.800 1.00 27.03 ? 822  SER B N     1 
ATOM   14717 C CA    . SER B  1 824  ? 8.829   40.150  108.805 1.00 26.79 ? 822  SER B CA    1 
ATOM   14718 C C     . SER B  1 824  ? 8.583   39.005  107.831 1.00 28.08 ? 822  SER B C     1 
ATOM   14719 O O     . SER B  1 824  ? 7.491   38.439  107.843 1.00 27.57 ? 822  SER B O     1 
ATOM   14720 C CB    . SER B  1 824  ? 7.866   41.284  108.469 1.00 29.73 ? 822  SER B CB    1 
ATOM   14721 O OG    . SER B  1 824  ? 8.003   41.624  107.118 1.00 23.69 ? 822  SER B OG    1 
ATOM   14722 N N     . ALA B  1 825  ? 9.550   38.676  106.977 1.00 23.42 ? 823  ALA B N     1 
ATOM   14723 C CA    . ALA B  1 825  ? 9.363   37.621  105.987 1.00 24.72 ? 823  ALA B CA    1 
ATOM   14724 C C     . ALA B  1 825  ? 9.317   36.250  106.659 1.00 27.60 ? 823  ALA B C     1 
ATOM   14725 O O     . ALA B  1 825  ? 9.853   36.048  107.744 1.00 25.78 ? 823  ALA B O     1 
ATOM   14726 C CB    . ALA B  1 825  ? 10.496  37.656  104.957 1.00 21.62 ? 823  ALA B CB    1 
ATOM   14727 N N     . LEU B  1 826  ? 8.686   35.293  105.991 1.00 28.36 ? 824  LEU B N     1 
ATOM   14728 C CA    . LEU B  1 826  ? 8.615   33.929  106.510 1.00 28.17 ? 824  LEU B CA    1 
ATOM   14729 C C     . LEU B  1 826  ? 9.873   33.182  106.085 1.00 29.78 ? 824  LEU B C     1 
ATOM   14730 O O     . LEU B  1 826  ? 10.067  32.915  104.895 1.00 27.43 ? 824  LEU B O     1 
ATOM   14731 C CB    . LEU B  1 826  ? 7.363   33.216  106.009 1.00 32.93 ? 824  LEU B CB    1 
ATOM   14732 C CG    . LEU B  1 826  ? 7.219   31.786  106.541 1.00 29.72 ? 824  LEU B CG    1 
ATOM   14733 C CD1   . LEU B  1 826  ? 7.206   31.797  108.058 1.00 37.29 ? 824  LEU B CD1   1 
ATOM   14734 C CD2   . LEU B  1 826  ? 5.971   31.120  106.001 1.00 37.18 ? 824  LEU B CD2   1 
ATOM   14735 N N     . ALA B  1 827  ? 10.717  32.834  107.062 1.00 26.32 ? 825  ALA B N     1 
ATOM   14736 C CA    . ALA B  1 827  ? 12.023  32.247  106.768 1.00 26.56 ? 825  ALA B CA    1 
ATOM   14737 C C     . ALA B  1 827  ? 11.928  31.080  105.786 1.00 28.84 ? 825  ALA B C     1 
ATOM   14738 O O     . ALA B  1 827  ? 12.706  31.004  104.829 1.00 28.11 ? 825  ALA B O     1 
ATOM   14739 C CB    . ALA B  1 827  ? 12.701  31.800  108.068 1.00 28.99 ? 825  ALA B CB    1 
ATOM   14740 N N     . GLU B  1 828  ? 10.971  30.166  105.993 1.00 27.20 ? 826  GLU B N     1 
ATOM   14741 C CA    . GLU B  1 828  ? 10.905  28.975  105.142 1.00 26.73 ? 826  GLU B CA    1 
ATOM   14742 C C     . GLU B  1 828  ? 10.583  29.341  103.702 1.00 27.04 ? 826  GLU B C     1 
ATOM   14743 O O     . GLU B  1 828  ? 11.073  28.706  102.754 1.00 26.37 ? 826  GLU B O     1 
ATOM   14744 C CB    . GLU B  1 828  ? 9.864   27.993  105.676 1.00 29.23 ? 826  GLU B CB    1 
ATOM   14745 C CG    . GLU B  1 828  ? 10.301  27.236  106.927 1.00 34.31 ? 826  GLU B CG    1 
ATOM   14746 C CD    . GLU B  1 828  ? 10.170  28.053  108.207 1.00 36.75 ? 826  GLU B CD    1 
ATOM   14747 O OE1   . GLU B  1 828  ? 9.636   29.185  108.162 1.00 31.47 ? 826  GLU B OE1   1 
ATOM   14748 O OE2   . GLU B  1 828  ? 10.607  27.548  109.266 1.00 38.57 ? 826  GLU B OE2   1 
ATOM   14749 N N     . GLN B  1 829  ? 9.760   30.360  103.516 1.00 25.40 ? 827  GLN B N     1 
ATOM   14750 C CA    . GLN B  1 829  ? 9.450   30.789  102.162 1.00 25.41 ? 827  GLN B CA    1 
ATOM   14751 C C     . GLN B  1 829  ? 10.642  31.501  101.542 1.00 24.13 ? 827  GLN B C     1 
ATOM   14752 O O     . GLN B  1 829  ? 10.950  31.295  100.365 1.00 25.23 ? 827  GLN B O     1 
ATOM   14753 C CB    . GLN B  1 829  ? 8.221   31.683  102.180 1.00 28.58 ? 827  GLN B CB    1 
ATOM   14754 C CG    . GLN B  1 829  ? 7.787   32.149  100.816 1.00 32.06 ? 827  GLN B CG    1 
ATOM   14755 C CD    . GLN B  1 829  ? 6.549   33.013  100.894 1.00 37.39 ? 827  GLN B CD    1 
ATOM   14756 O OE1   . GLN B  1 829  ? 6.079   33.346  101.990 1.00 39.41 ? 827  GLN B OE1   1 
ATOM   14757 N NE2   . GLN B  1 829  ? 6.005   33.377  99.733  1.00 38.83 ? 827  GLN B NE2   1 
ATOM   14758 N N     . VAL B  1 830  ? 11.347  32.319  102.330 1.00 23.72 ? 828  VAL B N     1 
ATOM   14759 C CA    . VAL B  1 830  ? 12.567  32.950  101.840 1.00 21.19 ? 828  VAL B CA    1 
ATOM   14760 C C     . VAL B  1 830  ? 13.550  31.901  101.346 1.00 22.14 ? 828  VAL B C     1 
ATOM   14761 O O     . VAL B  1 830  ? 14.131  32.031  100.265 1.00 21.56 ? 828  VAL B O     1 
ATOM   14762 C CB    . VAL B  1 830  ? 13.207  33.817  102.940 1.00 23.11 ? 828  VAL B CB    1 
ATOM   14763 C CG1   . VAL B  1 830  ? 14.622  34.235  102.515 1.00 23.78 ? 828  VAL B CG1   1 
ATOM   14764 C CG2   . VAL B  1 830  ? 12.344  35.021  103.224 1.00 22.45 ? 828  VAL B CG2   1 
ATOM   14765 N N     . VAL B  1 831  ? 13.780  30.859  102.152 1.00 21.11 ? 829  VAL B N     1 
ATOM   14766 C CA    . VAL B  1 831  ? 14.841  29.913  101.831 1.00 21.02 ? 829  VAL B CA    1 
ATOM   14767 C C     . VAL B  1 831  ? 14.510  29.150  100.554 1.00 21.17 ? 829  VAL B C     1 
ATOM   14768 O O     . VAL B  1 831  ? 15.371  28.988  99.673  1.00 23.27 ? 829  VAL B O     1 
ATOM   14769 C CB    . VAL B  1 831  ? 15.101  28.976  103.028 1.00 23.76 ? 829  VAL B CB    1 
ATOM   14770 C CG1   . VAL B  1 831  ? 15.805  27.690  102.591 1.00 24.34 ? 829  VAL B CG1   1 
ATOM   14771 C CG2   . VAL B  1 831  ? 15.967  29.691  104.045 1.00 25.52 ? 829  VAL B CG2   1 
ATOM   14772 N N     . GLY B  1 832  ? 13.262  28.693  100.416 1.00 20.49 ? 830  GLY B N     1 
ATOM   14773 C CA    . GLY B  1 832  ? 12.863  28.033  99.181  1.00 22.57 ? 830  GLY B CA    1 
ATOM   14774 C C     . GLY B  1 832  ? 13.033  28.936  97.973  1.00 24.47 ? 830  GLY B C     1 
ATOM   14775 O O     . GLY B  1 832  ? 13.532  28.510  96.927  1.00 22.56 ? 830  GLY B O     1 
ATOM   14776 N N     . ASP B  1 833  ? 12.656  30.209  98.115  1.00 21.78 ? 831  ASP B N     1 
ATOM   14777 C CA    . ASP B  1 833  ? 12.761  31.133  96.988  1.00 18.65 ? 831  ASP B CA    1 
ATOM   14778 C C     . ASP B  1 833  ? 14.206  31.508  96.701  1.00 21.65 ? 831  ASP B C     1 
ATOM   14779 O O     . ASP B  1 833  ? 14.543  31.829  95.564  1.00 20.15 ? 831  ASP B O     1 
ATOM   14780 C CB    . ASP B  1 833  ? 11.911  32.371  97.264  1.00 17.29 ? 831  ASP B CB    1 
ATOM   14781 C CG    . ASP B  1 833  ? 10.423  32.057  97.205  1.00 24.35 ? 831  ASP B CG    1 
ATOM   14782 O OD1   . ASP B  1 833  ? 10.075  31.001  96.621  1.00 25.36 ? 831  ASP B OD1   1 
ATOM   14783 O OD2   . ASP B  1 833  ? 9.614   32.841  97.736  1.00 24.22 ? 831  ASP B OD2   1 
ATOM   14784 N N     . VAL B  1 834  ? 15.080  31.458  97.712  1.00 17.34 ? 832  VAL B N     1 
ATOM   14785 C CA    . VAL B  1 834  ? 16.493  31.742  97.493  1.00 16.58 ? 832  VAL B CA    1 
ATOM   14786 C C     . VAL B  1 834  ? 17.188  30.552  96.847  1.00 19.31 ? 832  VAL B C     1 
ATOM   14787 O O     . VAL B  1 834  ? 18.007  30.719  95.937  1.00 22.96 ? 832  VAL B O     1 
ATOM   14788 C CB    . VAL B  1 834  ? 17.173  32.135  98.826  1.00 16.16 ? 832  VAL B CB    1 
ATOM   14789 C CG1   . VAL B  1 834  ? 18.679  32.127  98.666  1.00 19.72 ? 832  VAL B CG1   1 
ATOM   14790 C CG2   . VAL B  1 834  ? 16.718  33.521  99.255  1.00 19.13 ? 832  VAL B CG2   1 
ATOM   14791 N N     . ILE B  1 835  ? 16.931  29.337  97.350  1.00 17.46 ? 833  ILE B N     1 
ATOM   14792 C CA    . ILE B  1 835  ? 17.556  28.148  96.772  1.00 19.52 ? 833  ILE B CA    1 
ATOM   14793 C C     . ILE B  1 835  ? 17.227  28.064  95.292  1.00 20.20 ? 833  ILE B C     1 
ATOM   14794 O O     . ILE B  1 835  ? 18.098  27.827  94.447  1.00 22.53 ? 833  ILE B O     1 
ATOM   14795 C CB    . ILE B  1 835  ? 17.103  26.884  97.530  1.00 21.80 ? 833  ILE B CB    1 
ATOM   14796 C CG1   . ILE B  1 835  ? 17.687  26.847  98.952  1.00 24.23 ? 833  ILE B CG1   1 
ATOM   14797 C CG2   . ILE B  1 835  ? 17.493  25.602  96.769  1.00 24.45 ? 833  ILE B CG2   1 
ATOM   14798 C CD1   . ILE B  1 835  ? 19.080  26.284  99.050  1.00 31.61 ? 833  ILE B CD1   1 
ATOM   14799 N N     . THR B  1 836  ? 15.972  28.316  94.952  1.00 22.46 ? 834  THR B N     1 
ATOM   14800 C CA    . THR B  1 836  ? 15.558  28.303  93.557  1.00 20.65 ? 834  THR B CA    1 
ATOM   14801 C C     . THR B  1 836  ? 16.198  29.442  92.767  1.00 20.80 ? 834  THR B C     1 
ATOM   14802 O O     . THR B  1 836  ? 16.793  29.213  91.712  1.00 21.98 ? 834  THR B O     1 
ATOM   14803 C CB    . THR B  1 836  ? 14.032  28.377  93.499  1.00 24.76 ? 834  THR B CB    1 
ATOM   14804 O OG1   . THR B  1 836  ? 13.495  27.172  94.064  1.00 27.85 ? 834  THR B OG1   1 
ATOM   14805 C CG2   . THR B  1 836  ? 13.556  28.522  92.081  1.00 26.26 ? 834  THR B CG2   1 
ATOM   14806 N N     . SER B  1 837  ? 16.093  30.680  93.258  1.00 18.64 ? 835  SER B N     1 
ATOM   14807 C CA    . SER B  1 837  ? 16.600  31.813  92.484  1.00 18.56 ? 835  SER B CA    1 
ATOM   14808 C C     . SER B  1 837  ? 18.112  31.745  92.261  1.00 20.19 ? 835  SER B C     1 
ATOM   14809 O O     . SER B  1 837  ? 18.603  32.116  91.190  1.00 18.89 ? 835  SER B O     1 
ATOM   14810 C CB    . SER B  1 837  ? 16.232  33.126  93.176  1.00 15.56 ? 835  SER B CB    1 
ATOM   14811 O OG    . SER B  1 837  ? 14.839  33.294  93.253  1.00 17.24 ? 835  SER B OG    1 
ATOM   14812 N N     . ALA B  1 838  ? 18.883  31.324  93.278  1.00 16.99 ? 836  ALA B N     1 
ATOM   14813 C CA    . ALA B  1 838  ? 20.332  31.342  93.141  1.00 18.24 ? 836  ALA B CA    1 
ATOM   14814 C C     . ALA B  1 838  ? 20.905  30.102  92.452  1.00 17.04 ? 836  ALA B C     1 
ATOM   14815 O O     . ALA B  1 838  ? 21.927  30.204  91.768  1.00 20.59 ? 836  ALA B O     1 
ATOM   14816 C CB    . ALA B  1 838  ? 20.992  31.476  94.521  1.00 16.95 ? 836  ALA B CB    1 
ATOM   14817 N N     . PHE B  1 839  ? 20.300  28.930  92.631  1.00 20.14 ? 837  PHE B N     1 
ATOM   14818 C CA    . PHE B  1 839  ? 20.947  27.692  92.233  1.00 21.38 ? 837  PHE B CA    1 
ATOM   14819 C C     . PHE B  1 839  ? 20.196  26.887  91.188  1.00 20.78 ? 837  PHE B C     1 
ATOM   14820 O O     . PHE B  1 839  ? 20.775  25.943  90.634  1.00 26.50 ? 837  PHE B O     1 
ATOM   14821 C CB    . PHE B  1 839  ? 21.194  26.819  93.466  1.00 22.03 ? 837  PHE B CB    1 
ATOM   14822 C CG    . PHE B  1 839  ? 21.941  27.546  94.563  1.00 23.69 ? 837  PHE B CG    1 
ATOM   14823 C CD1   . PHE B  1 839  ? 23.159  28.170  94.299  1.00 27.24 ? 837  PHE B CD1   1 
ATOM   14824 C CD2   . PHE B  1 839  ? 21.414  27.636  95.839  1.00 23.04 ? 837  PHE B CD2   1 
ATOM   14825 C CE1   . PHE B  1 839  ? 23.848  28.854  95.298  1.00 24.14 ? 837  PHE B CE1   1 
ATOM   14826 C CE2   . PHE B  1 839  ? 22.110  28.327  96.856  1.00 23.36 ? 837  PHE B CE2   1 
ATOM   14827 C CZ    . PHE B  1 839  ? 23.320  28.934  96.574  1.00 26.24 ? 837  PHE B CZ    1 
ATOM   14828 N N     . ASP B  1 840  ? 18.947  27.219  90.899  1.00 23.70 ? 838  ASP B N     1 
ATOM   14829 C CA    . ASP B  1 840  ? 18.273  26.600  89.770  1.00 23.24 ? 838  ASP B CA    1 
ATOM   14830 C C     . ASP B  1 840  ? 19.078  26.847  88.505  1.00 22.11 ? 838  ASP B C     1 
ATOM   14831 O O     . ASP B  1 840  ? 19.588  27.948  88.280  1.00 20.61 ? 838  ASP B O     1 
ATOM   14832 C CB    . ASP B  1 840  ? 16.855  27.157  89.623  1.00 26.92 ? 838  ASP B CB    1 
ATOM   14833 C CG    . ASP B  1 840  ? 16.123  26.587  88.445  1.00 28.00 ? 838  ASP B CG    1 
ATOM   14834 O OD1   . ASP B  1 840  ? 16.339  27.066  87.315  1.00 30.03 ? 838  ASP B OD1   1 
ATOM   14835 O OD2   . ASP B  1 840  ? 15.332  25.653  88.656  1.00 33.50 ? 838  ASP B OD2   1 
ATOM   14836 N N     . SER B  1 841  ? 19.188  25.810  87.680  1.00 22.09 ? 839  SER B N     1 
ATOM   14837 C CA    . SER B  1 841  ? 19.963  25.880  86.450  1.00 23.03 ? 839  SER B CA    1 
ATOM   14838 C C     . SER B  1 841  ? 21.409  26.256  86.737  1.00 21.62 ? 839  SER B C     1 
ATOM   14839 O O     . SER B  1 841  ? 22.049  26.947  85.942  1.00 22.94 ? 839  SER B O     1 
ATOM   14840 C CB    . SER B  1 841  ? 19.319  26.853  85.459  1.00 24.12 ? 839  SER B CB    1 
ATOM   14841 O OG    . SER B  1 841  ? 17.990  26.422  85.178  1.00 29.12 ? 839  SER B OG    1 
ATOM   14842 N N     . ALA B  1 842  ? 21.908  25.789  87.891  1.00 18.66 ? 840  ALA B N     1 
ATOM   14843 C CA    . ALA B  1 842  ? 23.268  26.070  88.363  1.00 18.89 ? 840  ALA B CA    1 
ATOM   14844 C C     . ALA B  1 842  ? 23.580  27.565  88.300  1.00 17.44 ? 840  ALA B C     1 
ATOM   14845 O O     . ALA B  1 842  ? 24.700  27.973  87.978  1.00 23.45 ? 840  ALA B O     1 
ATOM   14846 C CB    . ALA B  1 842  ? 24.299  25.259  87.575  1.00 20.45 ? 840  ALA B CB    1 
ATOM   14847 N N     . GLY B  1 843  ? 22.579  28.383  88.625  1.00 20.47 ? 841  GLY B N     1 
ATOM   14848 C CA    . GLY B  1 843  ? 22.722  29.828  88.614  1.00 21.00 ? 841  GLY B CA    1 
ATOM   14849 C C     . GLY B  1 843  ? 22.998  30.442  87.259  1.00 24.43 ? 841  GLY B C     1 
ATOM   14850 O O     . GLY B  1 843  ? 23.498  31.572  87.185  1.00 23.45 ? 841  GLY B O     1 
ATOM   14851 N N     . GLN B  1 844  ? 22.683  29.732  86.177  1.00 21.38 ? 842  GLN B N     1 
ATOM   14852 C CA    . GLN B  1 844  ? 22.986  30.193  84.827  1.00 21.54 ? 842  GLN B CA    1 
ATOM   14853 C C     . GLN B  1 844  ? 21.797  30.892  84.178  1.00 24.39 ? 842  GLN B C     1 
ATOM   14854 O O     . GLN B  1 844  ? 21.623  30.838  82.960  1.00 27.99 ? 842  GLN B O     1 
ATOM   14855 C CB    . GLN B  1 844  ? 23.481  29.023  83.980  1.00 19.30 ? 842  GLN B CB    1 
ATOM   14856 C CG    . GLN B  1 844  ? 24.820  28.432  84.530  1.00 19.08 ? 842  GLN B CG    1 
ATOM   14857 C CD    . GLN B  1 844  ? 25.317  27.263  83.711  1.00 20.26 ? 842  GLN B CD    1 
ATOM   14858 O OE1   . GLN B  1 844  ? 26.487  27.182  83.376  1.00 20.70 ? 842  GLN B OE1   1 
ATOM   14859 N NE2   . GLN B  1 844  ? 24.415  26.365  83.354  1.00 26.27 ? 842  GLN B NE2   1 
ATOM   14860 N N     . ARG B  1 845  ? 20.970  31.538  84.981  1.00 25.54 ? 843  ARG B N     1 
ATOM   14861 C CA    . ARG B  1 845  ? 19.935  32.425  84.491  1.00 23.12 ? 843  ARG B CA    1 
ATOM   14862 C C     . ARG B  1 845  ? 20.414  33.863  84.576  1.00 26.76 ? 843  ARG B C     1 
ATOM   14863 O O     . ARG B  1 845  ? 21.077  34.258  85.543  1.00 25.60 ? 843  ARG B O     1 
ATOM   14864 C CB    . ARG B  1 845  ? 18.656  32.274  85.302  1.00 21.74 ? 843  ARG B CB    1 
ATOM   14865 C CG    . ARG B  1 845  ? 18.067  30.914  85.254  1.00 25.68 ? 843  ARG B CG    1 
ATOM   14866 C CD    . ARG B  1 845  ? 16.785  30.920  86.049  1.00 29.60 ? 843  ARG B CD    1 
ATOM   14867 N NE    . ARG B  1 845  ? 16.130  29.625  86.014  1.00 27.07 ? 843  ARG B NE    1 
ATOM   14868 C CZ    . ARG B  1 845  ? 15.119  29.319  85.214  1.00 29.91 ? 843  ARG B CZ    1 
ATOM   14869 N NH1   . ARG B  1 845  ? 14.594  30.212  84.386  1.00 32.45 ? 843  ARG B NH1   1 
ATOM   14870 N NH2   . ARG B  1 845  ? 14.612  28.091  85.256  1.00 33.43 ? 843  ARG B NH2   1 
ATOM   14871 N N     . CYS B  1 846  ? 20.046  34.658  83.575  1.00 23.23 ? 844  CYS B N     1 
ATOM   14872 C CA    . CYS B  1 846  ? 20.310  36.089  83.676  1.00 25.88 ? 844  CYS B CA    1 
ATOM   14873 C C     . CYS B  1 846  ? 19.556  36.705  84.851  1.00 24.16 ? 844  CYS B C     1 
ATOM   14874 O O     . CYS B  1 846  ? 20.011  37.701  85.420  1.00 25.81 ? 844  CYS B O     1 
ATOM   14875 C CB    . CYS B  1 846  ? 19.939  36.781  82.362  1.00 32.01 ? 844  CYS B CB    1 
ATOM   14876 S SG    . CYS B  1 846  ? 20.915  36.145  80.954  1.00 48.84 ? 844  CYS B SG    1 
ATOM   14877 N N     . SER B  1 847  ? 18.429  36.113  85.240  1.00 22.05 ? 845  SER B N     1 
ATOM   14878 C CA    . SER B  1 847  ? 17.617  36.563  86.366  1.00 20.15 ? 845  SER B CA    1 
ATOM   14879 C C     . SER B  1 847  ? 18.084  36.030  87.719  1.00 24.46 ? 845  SER B C     1 
ATOM   14880 O O     . SER B  1 847  ? 17.466  36.365  88.739  1.00 21.30 ? 845  SER B O     1 
ATOM   14881 C CB    . SER B  1 847  ? 16.164  36.136  86.147  1.00 23.14 ? 845  SER B CB    1 
ATOM   14882 O OG    . SER B  1 847  ? 16.124  34.744  85.860  1.00 28.37 ? 845  SER B OG    1 
ATOM   14883 N N     . ALA B  1 848  ? 19.133  35.215  87.750  1.00 19.98 ? 846  ALA B N     1 
ATOM   14884 C CA    . ALA B  1 848  ? 19.485  34.466  88.956  1.00 23.54 ? 846  ALA B CA    1 
ATOM   14885 C C     . ALA B  1 848  ? 19.828  35.415  90.095  1.00 20.35 ? 846  ALA B C     1 
ATOM   14886 O O     . ALA B  1 848  ? 20.367  36.501  89.884  1.00 22.21 ? 846  ALA B O     1 
ATOM   14887 C CB    . ALA B  1 848  ? 20.674  33.533  88.689  1.00 20.23 ? 846  ALA B CB    1 
ATOM   14888 N N     . LEU B  1 849  ? 19.498  34.991  91.315  1.00 21.55 ? 847  LEU B N     1 
ATOM   14889 C CA    . LEU B  1 849  ? 19.818  35.778  92.499  1.00 21.27 ? 847  LEU B CA    1 
ATOM   14890 C C     . LEU B  1 849  ? 21.317  35.714  92.768  1.00 20.03 ? 847  LEU B C     1 
ATOM   14891 O O     . LEU B  1 849  ? 21.873  34.627  92.957  1.00 20.60 ? 847  LEU B O     1 
ATOM   14892 C CB    . LEU B  1 849  ? 19.026  35.258  93.696  1.00 20.27 ? 847  LEU B CB    1 
ATOM   14893 C CG    . LEU B  1 849  ? 19.377  35.846  95.059  1.00 19.59 ? 847  LEU B CG    1 
ATOM   14894 C CD1   . LEU B  1 849  ? 19.063  37.355  95.115  1.00 21.29 ? 847  LEU B CD1   1 
ATOM   14895 C CD2   . LEU B  1 849  ? 18.636  35.086  96.147  1.00 22.46 ? 847  LEU B CD2   1 
ATOM   14896 N N     . ARG B  1 850  ? 21.962  36.883  92.794  1.00 20.08 ? 848  ARG B N     1 
ATOM   14897 C CA    . ARG B  1 850  ? 23.394  36.992  93.049  1.00 18.92 ? 848  ARG B CA    1 
ATOM   14898 C C     . ARG B  1 850  ? 23.710  37.517  94.437  1.00 22.56 ? 848  ARG B C     1 
ATOM   14899 O O     . ARG B  1 850  ? 24.708  37.100  95.021  1.00 23.66 ? 848  ARG B O     1 
ATOM   14900 C CB    . ARG B  1 850  ? 24.060  37.912  92.014  1.00 21.72 ? 848  ARG B CB    1 
ATOM   14901 C CG    . ARG B  1 850  ? 23.739  37.555  90.551  1.00 19.65 ? 848  ARG B CG    1 
ATOM   14902 C CD    . ARG B  1 850  ? 24.075  36.102  90.270  1.00 21.17 ? 848  ARG B CD    1 
ATOM   14903 N NE    . ARG B  1 850  ? 23.933  35.778  88.853  1.00 22.67 ? 848  ARG B NE    1 
ATOM   14904 C CZ    . ARG B  1 850  ? 23.987  34.545  88.374  1.00 25.60 ? 848  ARG B CZ    1 
ATOM   14905 N NH1   . ARG B  1 850  ? 24.111  33.501  89.177  1.00 19.81 ? 848  ARG B NH1   1 
ATOM   14906 N NH2   . ARG B  1 850  ? 23.886  34.351  87.059  1.00 22.56 ? 848  ARG B NH2   1 
ATOM   14907 N N     . VAL B  1 851  ? 22.891  38.422  94.968  1.00 24.18 ? 849  VAL B N     1 
ATOM   14908 C CA    . VAL B  1 851  ? 23.150  39.061  96.256  1.00 22.74 ? 849  VAL B CA    1 
ATOM   14909 C C     . VAL B  1 851  ? 21.898  38.966  97.118  1.00 21.86 ? 849  VAL B C     1 
ATOM   14910 O O     . VAL B  1 851  ? 20.885  39.619  96.832  1.00 20.17 ? 849  VAL B O     1 
ATOM   14911 C CB    . VAL B  1 851  ? 23.583  40.523  96.112  1.00 24.14 ? 849  VAL B CB    1 
ATOM   14912 C CG1   . VAL B  1 851  ? 24.004  41.050  97.488  1.00 24.76 ? 849  VAL B CG1   1 
ATOM   14913 C CG2   . VAL B  1 851  ? 24.725  40.662  95.119  1.00 23.31 ? 849  VAL B CG2   1 
ATOM   14914 N N     . LEU B  1 852  ? 21.977  38.196  98.196  1.00 22.51 ? 850  LEU B N     1 
ATOM   14915 C CA    . LEU B  1 852  ? 20.900  38.112  99.173  1.00 21.57 ? 850  LEU B CA    1 
ATOM   14916 C C     . LEU B  1 852  ? 21.183  39.083  100.309 1.00 20.84 ? 850  LEU B C     1 
ATOM   14917 O O     . LEU B  1 852  ? 22.245  39.006  100.943 1.00 25.52 ? 850  LEU B O     1 
ATOM   14918 C CB    . LEU B  1 852  ? 20.762  36.693  99.713  1.00 19.34 ? 850  LEU B CB    1 
ATOM   14919 C CG    . LEU B  1 852  ? 19.671  36.528  100.770 1.00 15.91 ? 850  LEU B CG    1 
ATOM   14920 C CD1   . LEU B  1 852  ? 18.240  36.884  100.247 1.00 19.58 ? 850  LEU B CD1   1 
ATOM   14921 C CD2   . LEU B  1 852  ? 19.732  35.093  101.282 1.00 16.11 ? 850  LEU B CD2   1 
ATOM   14922 N N     . CYS B  1 853  ? 20.251  39.997  100.554 1.00 21.37 ? 851  CYS B N     1 
ATOM   14923 C CA    . CYS B  1 853  ? 20.391  41.030  101.580 1.00 20.71 ? 851  CYS B CA    1 
ATOM   14924 C C     . CYS B  1 853  ? 19.451  40.715  102.740 1.00 18.83 ? 851  CYS B C     1 
ATOM   14925 O O     . CYS B  1 853  ? 18.232  40.824  102.606 1.00 20.96 ? 851  CYS B O     1 
ATOM   14926 C CB    . CYS B  1 853  ? 20.095  42.412  100.997 1.00 20.30 ? 851  CYS B CB    1 
ATOM   14927 S SG    . CYS B  1 853  ? 21.103  42.833  99.560  1.00 26.54 ? 851  CYS B SG    1 
ATOM   14928 N N     . LEU B  1 854  ? 20.016  40.362  103.895 1.00 19.43 ? 852  LEU B N     1 
ATOM   14929 C CA    . LEU B  1 854  ? 19.236  39.925  105.045 1.00 21.92 ? 852  LEU B CA    1 
ATOM   14930 C C     . LEU B  1 854  ? 19.293  40.975  106.143 1.00 24.26 ? 852  LEU B C     1 
ATOM   14931 O O     . LEU B  1 854  ? 20.386  41.403  106.529 1.00 24.58 ? 852  LEU B O     1 
ATOM   14932 C CB    . LEU B  1 854  ? 19.761  38.597  105.602 1.00 22.48 ? 852  LEU B CB    1 
ATOM   14933 C CG    . LEU B  1 854  ? 19.781  37.393  104.650 1.00 20.30 ? 852  LEU B CG    1 
ATOM   14934 C CD1   . LEU B  1 854  ? 20.330  36.144  105.345 1.00 18.89 ? 852  LEU B CD1   1 
ATOM   14935 C CD2   . LEU B  1 854  ? 18.381  37.143  104.118 1.00 22.07 ? 852  LEU B CD2   1 
ATOM   14936 N N     . GLN B  1 855  ? 18.127  41.344  106.671 1.00 23.48 ? 853  GLN B N     1 
ATOM   14937 C CA    . GLN B  1 855  ? 18.096  42.213  107.839 1.00 24.99 ? 853  GLN B CA    1 
ATOM   14938 C C     . GLN B  1 855  ? 18.857  41.551  108.972 1.00 25.25 ? 853  GLN B C     1 
ATOM   14939 O O     . GLN B  1 855  ? 18.706  40.352  109.218 1.00 25.76 ? 853  GLN B O     1 
ATOM   14940 C CB    . GLN B  1 855  ? 16.659  42.517  108.277 1.00 21.43 ? 853  GLN B CB    1 
ATOM   14941 C CG    . GLN B  1 855  ? 16.608  43.604  109.364 1.00 25.00 ? 853  GLN B CG    1 
ATOM   14942 C CD    . GLN B  1 855  ? 15.198  44.003  109.737 1.00 28.62 ? 853  GLN B CD    1 
ATOM   14943 O OE1   . GLN B  1 855  ? 14.314  44.055  108.885 1.00 30.68 ? 853  GLN B OE1   1 
ATOM   14944 N NE2   . GLN B  1 855  ? 14.980  44.292  111.016 1.00 30.20 ? 853  GLN B NE2   1 
ATOM   14945 N N     . GLU B  1 856  ? 19.681  42.351  109.661 1.00 25.64 ? 854  GLU B N     1 
ATOM   14946 C CA    . GLU B  1 856  ? 20.629  41.832  110.648 1.00 26.59 ? 854  GLU B CA    1 
ATOM   14947 C C     . GLU B  1 856  ? 19.946  40.962  111.698 1.00 28.20 ? 854  GLU B C     1 
ATOM   14948 O O     . GLU B  1 856  ? 20.504  39.948  112.142 1.00 32.92 ? 854  GLU B O     1 
ATOM   14949 C CB    . GLU B  1 856  ? 21.350  43.013  111.311 1.00 28.62 ? 854  GLU B CB    1 
ATOM   14950 C CG    . GLU B  1 856  ? 22.533  42.626  112.169 1.00 43.37 ? 854  GLU B CG    1 
ATOM   14951 C CD    . GLU B  1 856  ? 23.716  42.154  111.343 1.00 48.59 ? 854  GLU B CD    1 
ATOM   14952 O OE1   . GLU B  1 856  ? 24.314  42.988  110.617 1.00 51.47 ? 854  GLU B OE1   1 
ATOM   14953 O OE2   . GLU B  1 856  ? 24.037  40.946  111.411 1.00 51.28 ? 854  GLU B OE2   1 
ATOM   14954 N N     . ASP B  1 857  ? 18.725  41.333  112.089 1.00 26.48 ? 855  ASP B N     1 
ATOM   14955 C CA    . ASP B  1 857  ? 18.020  40.628  113.153 1.00 28.99 ? 855  ASP B CA    1 
ATOM   14956 C C     . ASP B  1 857  ? 17.705  39.177  112.795 1.00 34.95 ? 855  ASP B C     1 
ATOM   14957 O O     . ASP B  1 857  ? 17.616  38.328  113.688 1.00 31.11 ? 855  ASP B O     1 
ATOM   14958 C CB    . ASP B  1 857  ? 16.727  41.376  113.491 1.00 34.40 ? 855  ASP B CB    1 
ATOM   14959 N N     . VAL B  1 858  ? 17.500  38.863  111.513 1.00 28.25 ? 856  VAL B N     1 
ATOM   14960 C CA    . VAL B  1 858  ? 17.112  37.509  111.131 1.00 26.33 ? 856  VAL B CA    1 
ATOM   14961 C C     . VAL B  1 858  ? 18.168  36.797  110.306 1.00 25.13 ? 856  VAL B C     1 
ATOM   14962 O O     . VAL B  1 858  ? 17.968  35.621  109.956 1.00 27.25 ? 856  VAL B O     1 
ATOM   14963 C CB    . VAL B  1 858  ? 15.763  37.502  110.390 1.00 27.37 ? 856  VAL B CB    1 
ATOM   14964 C CG1   . VAL B  1 858  ? 14.652  37.985  111.317 1.00 31.82 ? 856  VAL B CG1   1 
ATOM   14965 C CG2   . VAL B  1 858  ? 15.856  38.352  109.155 1.00 23.84 ? 856  VAL B CG2   1 
ATOM   14966 N N     . ALA B  1 859  ? 19.303  37.445  110.023 1.00 25.39 ? 857  ALA B N     1 
ATOM   14967 C CA    . ALA B  1 859  ? 20.281  36.904  109.079 1.00 26.32 ? 857  ALA B CA    1 
ATOM   14968 C C     . ALA B  1 859  ? 20.811  35.548  109.521 1.00 24.65 ? 857  ALA B C     1 
ATOM   14969 O O     . ALA B  1 859  ? 20.901  34.620  108.715 1.00 26.80 ? 857  ALA B O     1 
ATOM   14970 C CB    . ALA B  1 859  ? 21.429  37.892  108.889 1.00 23.57 ? 857  ALA B CB    1 
ATOM   14971 N N     . ASP B  1 860  ? 21.172  35.413  110.803 1.00 28.04 ? 858  ASP B N     1 
ATOM   14972 C CA    . ASP B  1 860  ? 21.755  34.158  111.280 1.00 29.64 ? 858  ASP B CA    1 
ATOM   14973 C C     . ASP B  1 860  ? 20.796  32.987  111.104 1.00 29.66 ? 858  ASP B C     1 
ATOM   14974 O O     . ASP B  1 860  ? 21.176  31.933  110.580 1.00 28.92 ? 858  ASP B O     1 
ATOM   14975 C CB    . ASP B  1 860  ? 22.172  34.292  112.748 1.00 30.56 ? 858  ASP B CB    1 
ATOM   14976 C CG    . ASP B  1 860  ? 23.332  35.242  112.929 1.00 40.82 ? 858  ASP B CG    1 
ATOM   14977 O OD1   . ASP B  1 860  ? 24.207  35.277  112.033 1.00 40.79 ? 858  ASP B OD1   1 
ATOM   14978 O OD2   . ASP B  1 860  ? 23.355  35.968  113.945 1.00 43.41 ? 858  ASP B OD2   1 
ATOM   14979 N N     . ARG B  1 861  ? 19.544  33.150  111.537 1.00 29.07 ? 859  ARG B N     1 
ATOM   14980 C CA    . ARG B  1 861  ? 18.599  32.044  111.458 1.00 27.01 ? 859  ARG B CA    1 
ATOM   14981 C C     . ARG B  1 861  ? 18.312  31.657  110.007 1.00 26.30 ? 859  ARG B C     1 
ATOM   14982 O O     . ARG B  1 861  ? 18.241  30.468  109.677 1.00 25.76 ? 859  ARG B O     1 
ATOM   14983 C CB    . ARG B  1 861  ? 17.307  32.398  112.196 1.00 32.11 ? 859  ARG B CB    1 
ATOM   14984 C CG    . ARG B  1 861  ? 16.292  31.263  112.176 1.00 36.42 ? 859  ARG B CG    1 
ATOM   14985 C CD    . ARG B  1 861  ? 15.077  31.518  113.059 1.00 47.34 ? 859  ARG B CD    1 
ATOM   14986 N NE    . ARG B  1 861  ? 14.059  30.493  112.846 1.00 49.73 ? 859  ARG B NE    1 
ATOM   14987 C CZ    . ARG B  1 861  ? 12.980  30.659  112.093 1.00 46.24 ? 859  ARG B CZ    1 
ATOM   14988 N NH1   . ARG B  1 861  ? 12.710  31.823  111.523 1.00 46.20 ? 859  ARG B NH1   1 
ATOM   14989 N NH2   . ARG B  1 861  ? 12.151  29.633  111.908 1.00 44.63 ? 859  ARG B NH2   1 
ATOM   14990 N N     . ILE B  1 862  ? 18.176  32.643  109.116 1.00 24.13 ? 860  ILE B N     1 
ATOM   14991 C CA    . ILE B  1 862  ? 17.900  32.328  107.714 1.00 22.04 ? 860  ILE B CA    1 
ATOM   14992 C C     . ILE B  1 862  ? 19.111  31.672  107.064 1.00 22.93 ? 860  ILE B C     1 
ATOM   14993 O O     . ILE B  1 862  ? 18.977  30.717  106.287 1.00 20.83 ? 860  ILE B O     1 
ATOM   14994 C CB    . ILE B  1 862  ? 17.452  33.602  106.973 1.00 23.41 ? 860  ILE B CB    1 
ATOM   14995 C CG1   . ILE B  1 862  ? 16.032  33.966  107.426 1.00 27.90 ? 860  ILE B CG1   1 
ATOM   14996 C CG2   . ILE B  1 862  ? 17.520  33.415  105.480 1.00 22.66 ? 860  ILE B CG2   1 
ATOM   14997 C CD1   . ILE B  1 862  ? 15.479  35.270  106.850 1.00 25.27 ? 860  ILE B CD1   1 
ATOM   14998 N N     . LEU B  1 863  ? 20.318  32.141  107.406 1.00 25.14 ? 861  LEU B N     1 
ATOM   14999 C CA    . LEU B  1 863  ? 21.530  31.524  106.876 1.00 26.38 ? 861  LEU B CA    1 
ATOM   15000 C C     . LEU B  1 863  ? 21.656  30.075  107.325 1.00 24.88 ? 861  LEU B C     1 
ATOM   15001 O O     . LEU B  1 863  ? 22.060  29.210  106.543 1.00 22.76 ? 861  LEU B O     1 
ATOM   15002 C CB    . LEU B  1 863  ? 22.764  32.315  107.314 1.00 23.79 ? 861  LEU B CB    1 
ATOM   15003 C CG    . LEU B  1 863  ? 23.124  33.568  106.517 1.00 29.83 ? 861  LEU B CG    1 
ATOM   15004 C CD1   . LEU B  1 863  ? 24.234  34.336  107.222 1.00 34.99 ? 861  LEU B CD1   1 
ATOM   15005 C CD2   . LEU B  1 863  ? 23.532  33.184  105.101 1.00 32.93 ? 861  LEU B CD2   1 
ATOM   15006 N N     . THR B  1 864  ? 21.352  29.792  108.594 1.00 25.56 ? 862  THR B N     1 
ATOM   15007 C CA    . THR B  1 864  ? 21.408  28.405  109.053 1.00 25.94 ? 862  THR B CA    1 
ATOM   15008 C C     . THR B  1 864  ? 20.410  27.535  108.298 1.00 27.77 ? 862  THR B C     1 
ATOM   15009 O O     . THR B  1 864  ? 20.729  26.403  107.904 1.00 26.50 ? 862  THR B O     1 
ATOM   15010 C CB    . THR B  1 864  ? 21.153  28.345  110.558 1.00 29.32 ? 862  THR B CB    1 
ATOM   15011 O OG1   . THR B  1 864  ? 22.123  29.160  111.206 1.00 23.26 ? 862  THR B OG1   1 
ATOM   15012 C CG2   . THR B  1 864  ? 21.278  26.926  111.078 1.00 33.85 ? 862  THR B CG2   1 
ATOM   15013 N N     . MET B  1 865  ? 19.195  28.051  108.083 1.00 22.71 ? 863  MET B N     1 
ATOM   15014 C CA    . MET B  1 865  ? 18.185  27.302  107.341 1.00 26.51 ? 863  MET B CA    1 
ATOM   15015 C C     . MET B  1 865  ? 18.619  27.103  105.897 1.00 24.70 ? 863  MET B C     1 
ATOM   15016 O O     . MET B  1 865  ? 18.481  26.010  105.336 1.00 22.42 ? 863  MET B O     1 
ATOM   15017 C CB    . MET B  1 865  ? 16.852  28.046  107.400 1.00 22.85 ? 863  MET B CB    1 
ATOM   15018 C CG    . MET B  1 865  ? 15.654  27.298  106.820 1.00 30.78 ? 863  MET B CG    1 
ATOM   15019 S SD    . MET B  1 865  ? 14.094  28.106  107.298 1.00 34.25 ? 863  MET B SD    1 
ATOM   15020 C CE    . MET B  1 865  ? 14.580  28.791  108.879 1.00 25.82 ? 863  MET B CE    1 
ATOM   15021 N N     . LEU B  1 866  ? 19.151  28.157  105.287 1.00 22.00 ? 864  LEU B N     1 
ATOM   15022 C CA    . LEU B  1 866  ? 19.602  28.079  103.900 1.00 23.87 ? 864  LEU B CA    1 
ATOM   15023 C C     . LEU B  1 866  ? 20.721  27.051  103.738 1.00 21.94 ? 864  LEU B C     1 
ATOM   15024 O O     . LEU B  1 866  ? 20.696  26.236  102.809 1.00 24.18 ? 864  LEU B O     1 
ATOM   15025 C CB    . LEU B  1 866  ? 20.055  29.467  103.444 1.00 19.92 ? 864  LEU B CB    1 
ATOM   15026 C CG    . LEU B  1 866  ? 20.580  29.614  102.026 1.00 27.15 ? 864  LEU B CG    1 
ATOM   15027 C CD1   . LEU B  1 866  ? 19.438  29.371  101.046 1.00 25.73 ? 864  LEU B CD1   1 
ATOM   15028 C CD2   . LEU B  1 866  ? 21.160  30.998  101.829 1.00 28.43 ? 864  LEU B CD2   1 
ATOM   15029 N N     . LYS B  1 867  ? 21.699  27.050  104.651 1.00 22.02 ? 865  LYS B N     1 
ATOM   15030 C CA    . LYS B  1 867  ? 22.780  26.074  104.560 1.00 22.74 ? 865  LYS B CA    1 
ATOM   15031 C C     . LYS B  1 867  ? 22.259  24.654  104.745 1.00 25.29 ? 865  LYS B C     1 
ATOM   15032 O O     . LYS B  1 867  ? 22.704  23.725  104.058 1.00 25.75 ? 865  LYS B O     1 
ATOM   15033 C CB    . LYS B  1 867  ? 23.862  26.398  105.597 1.00 25.74 ? 865  LYS B CB    1 
ATOM   15034 C CG    . LYS B  1 867  ? 24.609  27.683  105.273 1.00 24.78 ? 865  LYS B CG    1 
ATOM   15035 C CD    . LYS B  1 867  ? 25.497  28.115  106.412 1.00 31.83 ? 865  LYS B CD    1 
ATOM   15036 C CE    . LYS B  1 867  ? 26.280  29.357  106.022 1.00 34.38 ? 865  LYS B CE    1 
ATOM   15037 N NZ    . LYS B  1 867  ? 27.057  29.878  107.179 1.00 37.90 ? 865  LYS B NZ    1 
ATOM   15038 N N     . GLY B  1 868  ? 21.302  24.469  105.656 1.00 25.63 ? 866  GLY B N     1 
ATOM   15039 C CA    . GLY B  1 868  ? 20.735  23.146  105.844 1.00 23.50 ? 866  GLY B CA    1 
ATOM   15040 C C     . GLY B  1 868  ? 19.976  22.683  104.621 1.00 22.85 ? 866  GLY B C     1 
ATOM   15041 O O     . GLY B  1 868  ? 20.041  21.508  104.244 1.00 25.56 ? 866  GLY B O     1 
ATOM   15042 N N     . ALA B  1 869  ? 19.260  23.603  103.972 1.00 22.37 ? 867  ALA B N     1 
ATOM   15043 C CA    . ALA B  1 869  ? 18.532  23.253  102.754 1.00 21.45 ? 867  ALA B CA    1 
ATOM   15044 C C     . ALA B  1 869  ? 19.495  22.969  101.608 1.00 24.76 ? 867  ALA B C     1 
ATOM   15045 O O     . ALA B  1 869  ? 19.252  22.075  100.787 1.00 24.50 ? 867  ALA B O     1 
ATOM   15046 C CB    . ALA B  1 869  ? 17.578  24.385  102.387 1.00 23.29 ? 867  ALA B CB    1 
ATOM   15047 N N     . LEU B  1 870  ? 20.605  23.713  101.554 1.00 24.68 ? 868  LEU B N     1 
ATOM   15048 C CA    . LEU B  1 870  ? 21.616  23.504  100.521 1.00 26.00 ? 868  LEU B CA    1 
ATOM   15049 C C     . LEU B  1 870  ? 22.136  22.075  100.538 1.00 28.65 ? 868  LEU B C     1 
ATOM   15050 O O     . LEU B  1 870  ? 22.313  21.461  99.484  1.00 28.55 ? 868  LEU B O     1 
ATOM   15051 C CB    . LEU B  1 870  ? 22.765  24.498  100.714 1.00 27.60 ? 868  LEU B CB    1 
ATOM   15052 C CG    . LEU B  1 870  ? 23.880  24.621  99.677  1.00 32.33 ? 868  LEU B CG    1 
ATOM   15053 C CD1   . LEU B  1 870  ? 23.536  25.696  98.671  1.00 33.18 ? 868  LEU B CD1   1 
ATOM   15054 C CD2   . LEU B  1 870  ? 25.237  24.913  100.333 1.00 36.27 ? 868  LEU B CD2   1 
ATOM   15055 N N     . HIS B  1 871  ? 22.366  21.513  101.718 1.00 24.89 ? 869  HIS B N     1 
ATOM   15056 C CA    . HIS B  1 871  ? 22.990  20.200  101.772 1.00 26.12 ? 869  HIS B CA    1 
ATOM   15057 C C     . HIS B  1 871  ? 22.034  19.068  101.431 1.00 28.54 ? 869  HIS B C     1 
ATOM   15058 O O     . HIS B  1 871  ? 22.471  17.921  101.352 1.00 26.87 ? 869  HIS B O     1 
ATOM   15059 C CB    . HIS B  1 871  ? 23.634  19.993  103.143 1.00 32.70 ? 869  HIS B CB    1 
ATOM   15060 C CG    . HIS B  1 871  ? 24.864  20.829  103.347 1.00 36.09 ? 869  HIS B CG    1 
ATOM   15061 N ND1   . HIS B  1 871  ? 26.051  20.574  102.689 1.00 39.48 ? 869  HIS B ND1   1 
ATOM   15062 C CD2   . HIS B  1 871  ? 25.088  21.920  104.117 1.00 32.15 ? 869  HIS B CD2   1 
ATOM   15063 C CE1   . HIS B  1 871  ? 26.953  21.470  103.051 1.00 37.34 ? 869  HIS B CE1   1 
ATOM   15064 N NE2   . HIS B  1 871  ? 26.394  22.300  103.912 1.00 38.95 ? 869  HIS B NE2   1 
ATOM   15065 N N     . GLU B  1 872  ? 20.761  19.364  101.174 1.00 26.17 ? 870  GLU B N     1 
ATOM   15066 C CA    . GLU B  1 872  ? 19.815  18.370  100.696 1.00 25.34 ? 870  GLU B CA    1 
ATOM   15067 C C     . GLU B  1 872  ? 19.713  18.330  99.171  1.00 26.03 ? 870  GLU B C     1 
ATOM   15068 O O     . GLU B  1 872  ? 18.967  17.506  98.635  1.00 26.87 ? 870  GLU B O     1 
ATOM   15069 C CB    . GLU B  1 872  ? 18.432  18.635  101.309 1.00 24.65 ? 870  GLU B CB    1 
ATOM   15070 C CG    . GLU B  1 872  ? 18.419  18.607  102.833 1.00 24.28 ? 870  GLU B CG    1 
ATOM   15071 C CD    . GLU B  1 872  ? 18.746  17.236  103.403 1.00 27.41 ? 870  GLU B CD    1 
ATOM   15072 O OE1   . GLU B  1 872  ? 18.507  16.218  102.715 1.00 31.49 ? 870  GLU B OE1   1 
ATOM   15073 O OE2   . GLU B  1 872  ? 19.255  17.178  104.537 1.00 30.66 ? 870  GLU B OE2   1 
ATOM   15074 N N     . LEU B  1 873  ? 20.434  19.194  98.465  1.00 26.91 ? 871  LEU B N     1 
ATOM   15075 C CA    . LEU B  1 873  ? 20.356  19.228  97.007  1.00 26.73 ? 871  LEU B CA    1 
ATOM   15076 C C     . LEU B  1 873  ? 21.170  18.097  96.402  1.00 26.62 ? 871  LEU B C     1 
ATOM   15077 O O     . LEU B  1 873  ? 22.247  17.760  96.895  1.00 27.19 ? 871  LEU B O     1 
ATOM   15078 C CB    . LEU B  1 873  ? 20.865  20.564  96.476  1.00 24.23 ? 871  LEU B CB    1 
ATOM   15079 C CG    . LEU B  1 873  ? 20.092  21.809  96.904  1.00 28.88 ? 871  LEU B CG    1 
ATOM   15080 C CD1   . LEU B  1 873  ? 20.751  23.053  96.309  1.00 27.78 ? 871  LEU B CD1   1 
ATOM   15081 C CD2   . LEU B  1 873  ? 18.594  21.708  96.516  1.00 27.21 ? 871  LEU B CD2   1 
ATOM   15082 N N     . HIS B  1 874  ? 20.649  17.508  95.325  1.00 24.05 ? 872  HIS B N     1 
ATOM   15083 C CA    . HIS B  1 874  ? 21.360  16.478  94.575  1.00 26.93 ? 872  HIS B CA    1 
ATOM   15084 C C     . HIS B  1 874  ? 21.950  17.102  93.306  1.00 26.79 ? 872  HIS B C     1 
ATOM   15085 O O     . HIS B  1 874  ? 21.208  17.619  92.467  1.00 23.50 ? 872  HIS B O     1 
ATOM   15086 C CB    . HIS B  1 874  ? 20.420  15.323  94.227  1.00 25.52 ? 872  HIS B CB    1 
ATOM   15087 C CG    . HIS B  1 874  ? 21.081  14.209  93.478  1.00 27.03 ? 872  HIS B CG    1 
ATOM   15088 N ND1   . HIS B  1 874  ? 20.374  13.180  92.896  1.00 29.43 ? 872  HIS B ND1   1 
ATOM   15089 C CD2   . HIS B  1 874  ? 22.389  13.957  93.226  1.00 35.04 ? 872  HIS B CD2   1 
ATOM   15090 C CE1   . HIS B  1 874  ? 21.213  12.357  92.294  1.00 32.91 ? 872  HIS B CE1   1 
ATOM   15091 N NE2   . HIS B  1 874  ? 22.443  12.801  92.487  1.00 35.07 ? 872  HIS B NE2   1 
ATOM   15092 N N     . ILE B  1 875  ? 23.277  17.059  93.175  1.00 23.48 ? 873  ILE B N     1 
ATOM   15093 C CA    . ILE B  1 875  ? 23.992  17.613  92.025  1.00 26.16 ? 873  ILE B CA    1 
ATOM   15094 C C     . ILE B  1 875  ? 24.517  16.455  91.186  1.00 27.52 ? 873  ILE B C     1 
ATOM   15095 O O     . ILE B  1 875  ? 25.118  15.521  91.726  1.00 26.84 ? 873  ILE B O     1 
ATOM   15096 C CB    . ILE B  1 875  ? 25.151  18.531  92.455  1.00 26.62 ? 873  ILE B CB    1 
ATOM   15097 C CG1   . ILE B  1 875  ? 24.653  19.926  92.841  1.00 28.39 ? 873  ILE B CG1   1 
ATOM   15098 C CG2   . ILE B  1 875  ? 26.154  18.684  91.320  1.00 31.78 ? 873  ILE B CG2   1 
ATOM   15099 C CD1   . ILE B  1 875  ? 23.796  19.982  94.084  1.00 34.22 ? 873  ILE B CD1   1 
ATOM   15100 N N     . GLY B  1 876  ? 24.300  16.507  89.875  1.00 20.74 ? 874  GLY B N     1 
ATOM   15101 C CA    . GLY B  1 876  ? 24.782  15.423  89.046  1.00 26.03 ? 874  GLY B CA    1 
ATOM   15102 C C     . GLY B  1 876  ? 24.279  15.557  87.626  1.00 24.90 ? 874  GLY B C     1 
ATOM   15103 O O     . GLY B  1 876  ? 23.700  16.579  87.242  1.00 22.39 ? 874  GLY B O     1 
ATOM   15104 N N     . ARG B  1 877  ? 24.551  14.513  86.851  1.00 24.40 ? 875  ARG B N     1 
ATOM   15105 C CA    . ARG B  1 877  ? 24.102  14.475  85.466  1.00 24.70 ? 875  ARG B CA    1 
ATOM   15106 C C     . ARG B  1 877  ? 22.581  14.453  85.436  1.00 26.59 ? 875  ARG B C     1 
ATOM   15107 O O     . ARG B  1 877  ? 21.952  13.682  86.164  1.00 25.59 ? 875  ARG B O     1 
ATOM   15108 C CB    . ARG B  1 877  ? 24.682  13.245  84.772  1.00 29.04 ? 875  ARG B CB    1 
ATOM   15109 C CG    . ARG B  1 877  ? 24.643  13.304  83.265  1.00 28.53 ? 875  ARG B CG    1 
ATOM   15110 C CD    . ARG B  1 877  ? 25.333  12.077  82.688  1.00 31.88 ? 875  ARG B CD    1 
ATOM   15111 N NE    . ARG B  1 877  ? 24.435  10.937  82.591  1.00 27.50 ? 875  ARG B NE    1 
ATOM   15112 C CZ    . ARG B  1 877  ? 24.743  9.800   81.983  1.00 40.25 ? 875  ARG B CZ    1 
ATOM   15113 N NH1   . ARG B  1 877  ? 25.946  9.596   81.469  1.00 37.01 ? 875  ARG B NH1   1 
ATOM   15114 N NH2   . ARG B  1 877  ? 23.817  8.850   81.874  1.00 39.81 ? 875  ARG B NH2   1 
ATOM   15115 N N     . THR B  1 878  ? 21.993  15.291  84.577  1.00 23.70 ? 876  THR B N     1 
ATOM   15116 C CA    . THR B  1 878  ? 20.595  15.688  84.696  1.00 24.50 ? 876  THR B CA    1 
ATOM   15117 C C     . THR B  1 878  ? 19.615  14.719  84.038  1.00 25.34 ? 876  THR B C     1 
ATOM   15118 O O     . THR B  1 878  ? 18.421  15.025  83.971  1.00 24.75 ? 876  THR B O     1 
ATOM   15119 C CB    . THR B  1 878  ? 20.406  17.086  84.108  1.00 24.33 ? 876  THR B CB    1 
ATOM   15120 O OG1   . THR B  1 878  ? 21.018  17.137  82.810  1.00 24.74 ? 876  THR B OG1   1 
ATOM   15121 C CG2   . THR B  1 878  ? 21.040  18.124  85.010  1.00 23.56 ? 876  THR B CG2   1 
ATOM   15122 N N     . ASP B  1 879  ? 20.072  13.554  83.573  1.00 28.88 ? 877  ASP B N     1 
ATOM   15123 C CA    . ASP B  1 879  ? 19.157  12.545  83.050  1.00 27.41 ? 877  ASP B CA    1 
ATOM   15124 C C     . ASP B  1 879  ? 18.585  11.654  84.156  1.00 26.27 ? 877  ASP B C     1 
ATOM   15125 O O     . ASP B  1 879  ? 18.196  10.508  83.892  1.00 26.19 ? 877  ASP B O     1 
ATOM   15126 C CB    . ASP B  1 879  ? 19.837  11.715  81.952  1.00 26.39 ? 877  ASP B CB    1 
ATOM   15127 C CG    . ASP B  1 879  ? 21.004  10.885  82.459  1.00 29.83 ? 877  ASP B CG    1 
ATOM   15128 O OD1   . ASP B  1 879  ? 21.738  11.339  83.360  1.00 32.16 ? 877  ASP B OD1   1 
ATOM   15129 O OD2   . ASP B  1 879  ? 21.193  9.764   81.940  1.00 30.93 ? 877  ASP B OD2   1 
ATOM   15130 N N     . ARG B  1 880  ? 18.510  12.175  85.384  1.00 25.88 ? 878  ARG B N     1 
ATOM   15131 C CA    . ARG B  1 880  ? 17.823  11.554  86.511  1.00 25.86 ? 878  ARG B CA    1 
ATOM   15132 C C     . ARG B  1 880  ? 16.852  12.562  87.110  1.00 26.95 ? 878  ARG B C     1 
ATOM   15133 O O     . ARG B  1 880  ? 17.223  13.719  87.340  1.00 23.78 ? 878  ARG B O     1 
ATOM   15134 C CB    . ARG B  1 880  ? 18.818  11.095  87.592  1.00 25.41 ? 878  ARG B CB    1 
ATOM   15135 C CG    . ARG B  1 880  ? 19.677  9.913   87.196  1.00 34.88 ? 878  ARG B CG    1 
ATOM   15136 C CD    . ARG B  1 880  ? 20.571  9.466   88.353  1.00 43.75 ? 878  ARG B CD    1 
ATOM   15137 N NE    . ARG B  1 880  ? 21.611  8.548   87.900  1.00 53.50 ? 878  ARG B NE    1 
ATOM   15138 C CZ    . ARG B  1 880  ? 21.580  7.231   88.061  1.00 57.51 ? 878  ARG B CZ    1 
ATOM   15139 N NH1   . ARG B  1 880  ? 20.585  6.634   88.699  1.00 59.19 ? 878  ARG B NH1   1 
ATOM   15140 N NH2   . ARG B  1 880  ? 22.575  6.494   87.571  1.00 61.03 ? 878  ARG B NH2   1 
ATOM   15141 N N     . LEU B  1 881  ? 15.610  12.130  87.361  1.00 23.87 ? 879  LEU B N     1 
ATOM   15142 C CA    . LEU B  1 881  ? 14.624  13.028  87.964  1.00 22.63 ? 879  LEU B CA    1 
ATOM   15143 C C     . LEU B  1 881  ? 15.079  13.546  89.322  1.00 25.44 ? 879  LEU B C     1 
ATOM   15144 O O     . LEU B  1 881  ? 14.774  14.687  89.688  1.00 23.38 ? 879  LEU B O     1 
ATOM   15145 C CB    . LEU B  1 881  ? 13.280  12.315  88.095  1.00 26.29 ? 879  LEU B CB    1 
ATOM   15146 C CG    . LEU B  1 881  ? 12.098  13.105  88.659  1.00 25.12 ? 879  LEU B CG    1 
ATOM   15147 C CD1   . LEU B  1 881  ? 11.697  14.221  87.686  1.00 27.13 ? 879  LEU B CD1   1 
ATOM   15148 C CD2   . LEU B  1 881  ? 10.929  12.167  88.971  1.00 24.36 ? 879  LEU B CD2   1 
ATOM   15149 N N     . SER B  1 882  ? 15.836  12.747  90.069  1.00 23.45 ? 880  SER B N     1 
ATOM   15150 C CA    . SER B  1 882  ? 16.244  13.163  91.410  1.00 24.24 ? 880  SER B CA    1 
ATOM   15151 C C     . SER B  1 882  ? 17.302  14.262  91.433  1.00 27.31 ? 880  SER B C     1 
ATOM   15152 O O     . SER B  1 882  ? 17.628  14.750  92.525  1.00 25.70 ? 880  SER B O     1 
ATOM   15153 C CB    . SER B  1 882  ? 16.770  11.956  92.188  1.00 27.58 ? 880  SER B CB    1 
ATOM   15154 O OG    . SER B  1 882  ? 17.876  11.373  91.527  1.00 27.55 ? 880  SER B OG    1 
ATOM   15155 N N     . VAL B  1 883  ? 17.874  14.642  90.294  1.00 22.08 ? 881  VAL B N     1 
ATOM   15156 C CA    . VAL B  1 883  ? 18.921  15.664  90.283  1.00 22.72 ? 881  VAL B CA    1 
ATOM   15157 C C     . VAL B  1 883  ? 18.278  17.043  90.375  1.00 22.42 ? 881  VAL B C     1 
ATOM   15158 O O     . VAL B  1 883  ? 17.381  17.387  89.595  1.00 22.55 ? 881  VAL B O     1 
ATOM   15159 C CB    . VAL B  1 883  ? 19.811  15.543  89.030  1.00 22.11 ? 881  VAL B CB    1 
ATOM   15160 C CG1   . VAL B  1 883  ? 20.632  16.828  88.818  1.00 21.52 ? 881  VAL B CG1   1 
ATOM   15161 C CG2   . VAL B  1 883  ? 20.736  14.333  89.138  1.00 22.64 ? 881  VAL B CG2   1 
ATOM   15162 N N     . ASP B  1 884  ? 18.745  17.843  91.328  1.00 20.95 ? 882  ASP B N     1 
ATOM   15163 C CA    . ASP B  1 884  ? 18.254  19.200  91.518  1.00 24.25 ? 882  ASP B CA    1 
ATOM   15164 C C     . ASP B  1 884  ? 19.046  20.212  90.708  1.00 28.36 ? 882  ASP B C     1 
ATOM   15165 O O     . ASP B  1 884  ? 18.455  21.105  90.088  1.00 29.92 ? 882  ASP B O     1 
ATOM   15166 C CB    . ASP B  1 884  ? 18.322  19.566  93.005  1.00 23.80 ? 882  ASP B CB    1 
ATOM   15167 C CG    . ASP B  1 884  ? 17.479  18.638  93.858  1.00 26.64 ? 882  ASP B CG    1 
ATOM   15168 O OD1   . ASP B  1 884  ? 16.270  18.487  93.561  1.00 26.38 ? 882  ASP B OD1   1 
ATOM   15169 O OD2   . ASP B  1 884  ? 18.025  18.034  94.791  1.00 25.06 ? 882  ASP B OD2   1 
ATOM   15170 N N     . VAL B  1 885  ? 20.372  20.074  90.698  1.00 24.28 ? 883  VAL B N     1 
ATOM   15171 C CA    . VAL B  1 885  ? 21.278  21.034  90.082  1.00 26.07 ? 883  VAL B CA    1 
ATOM   15172 C C     . VAL B  1 885  ? 22.230  20.270  89.168  1.00 23.81 ? 883  VAL B C     1 
ATOM   15173 O O     . VAL B  1 885  ? 22.856  19.290  89.588  1.00 22.14 ? 883  VAL B O     1 
ATOM   15174 C CB    . VAL B  1 885  ? 22.041  21.842  91.153  1.00 27.20 ? 883  VAL B CB    1 
ATOM   15175 C CG1   . VAL B  1 885  ? 23.152  22.684  90.539  1.00 28.35 ? 883  VAL B CG1   1 
ATOM   15176 C CG2   . VAL B  1 885  ? 21.066  22.725  91.926  1.00 27.07 ? 883  VAL B CG2   1 
ATOM   15177 N N     . GLY B  1 886  ? 22.290  20.679  87.903  1.00 22.34 ? 884  GLY B N     1 
ATOM   15178 C CA    . GLY B  1 886  ? 23.199  20.074  86.967  1.00 20.30 ? 884  GLY B CA    1 
ATOM   15179 C C     . GLY B  1 886  ? 24.511  20.815  86.826  1.00 18.51 ? 884  GLY B C     1 
ATOM   15180 O O     . GLY B  1 886  ? 24.922  21.611  87.687  1.00 22.77 ? 884  GLY B O     1 
ATOM   15181 N N     . PRO B  1 887  ? 25.196  20.559  85.719  1.00 22.02 ? 885  PRO B N     1 
ATOM   15182 C CA    . PRO B  1 887  ? 26.538  21.103  85.511  1.00 20.69 ? 885  PRO B CA    1 
ATOM   15183 C C     . PRO B  1 887  ? 26.489  22.546  85.036  1.00 24.39 ? 885  PRO B C     1 
ATOM   15184 O O     . PRO B  1 887  ? 25.451  23.051  84.609  1.00 20.05 ? 885  PRO B O     1 
ATOM   15185 C CB    . PRO B  1 887  ? 27.110  20.191  84.418  1.00 20.91 ? 885  PRO B CB    1 
ATOM   15186 C CG    . PRO B  1 887  ? 25.908  19.769  83.643  1.00 24.84 ? 885  PRO B CG    1 
ATOM   15187 C CD    . PRO B  1 887  ? 24.770  19.671  84.621  1.00 20.31 ? 885  PRO B CD    1 
ATOM   15188 N N     . VAL B  1 888  ? 27.653  23.201  85.088  1.00 21.41 ? 886  VAL B N     1 
ATOM   15189 C CA    . VAL B  1 888  ? 27.797  24.460  84.361  1.00 23.49 ? 886  VAL B CA    1 
ATOM   15190 C C     . VAL B  1 888  ? 28.188  24.108  82.930  1.00 20.66 ? 886  VAL B C     1 
ATOM   15191 O O     . VAL B  1 888  ? 28.578  22.971  82.644  1.00 21.25 ? 886  VAL B O     1 
ATOM   15192 C CB    . VAL B  1 888  ? 28.801  25.427  85.013  1.00 26.19 ? 886  VAL B CB    1 
ATOM   15193 C CG1   . VAL B  1 888  ? 28.261  25.936  86.369  1.00 22.75 ? 886  VAL B CG1   1 
ATOM   15194 C CG2   . VAL B  1 888  ? 30.179  24.801  85.126  1.00 24.43 ? 886  VAL B CG2   1 
ATOM   15195 N N     . ILE B  1 889  ? 28.097  25.078  82.020  1.00 22.96 ? 887  ILE B N     1 
ATOM   15196 C CA    . ILE B  1 889  ? 28.028  24.719  80.597  1.00 22.70 ? 887  ILE B CA    1 
ATOM   15197 C C     . ILE B  1 889  ? 29.375  24.236  80.041  1.00 21.40 ? 887  ILE B C     1 
ATOM   15198 O O     . ILE B  1 889  ? 29.409  23.362  79.163  1.00 22.37 ? 887  ILE B O     1 
ATOM   15199 C CB    . ILE B  1 889  ? 27.451  25.914  79.806  1.00 21.63 ? 887  ILE B CB    1 
ATOM   15200 C CG1   . ILE B  1 889  ? 27.182  25.542  78.341  1.00 22.84 ? 887  ILE B CG1   1 
ATOM   15201 C CG2   . ILE B  1 889  ? 28.344  27.145  79.929  1.00 22.48 ? 887  ILE B CG2   1 
ATOM   15202 C CD1   . ILE B  1 889  ? 26.128  24.453  78.161  1.00 23.43 ? 887  ILE B CD1   1 
ATOM   15203 N N     . THR B  1 890  ? 30.504  24.743  80.548  1.00 23.12 ? 888  THR B N     1 
ATOM   15204 C CA    . THR B  1 890  ? 31.814  24.423  79.973  1.00 22.83 ? 888  THR B CA    1 
ATOM   15205 C C     . THR B  1 890  ? 32.876  24.417  81.063  1.00 20.97 ? 888  THR B C     1 
ATOM   15206 O O     . THR B  1 890  ? 32.664  24.934  82.157  1.00 22.35 ? 888  THR B O     1 
ATOM   15207 C CB    . THR B  1 890  ? 32.275  25.440  78.917  1.00 23.89 ? 888  THR B CB    1 
ATOM   15208 O OG1   . THR B  1 890  ? 32.372  26.731  79.532  1.00 26.80 ? 888  THR B OG1   1 
ATOM   15209 C CG2   . THR B  1 890  ? 31.310  25.521  77.726  1.00 20.91 ? 888  THR B CG2   1 
ATOM   15210 N N     . SER B  1 891  ? 34.047  23.871  80.716  1.00 28.57 ? 889  SER B N     1 
ATOM   15211 C CA    . SER B  1 891  ? 35.222  23.974  81.588  1.00 24.23 ? 889  SER B CA    1 
ATOM   15212 C C     . SER B  1 891  ? 35.576  25.426  81.862  1.00 27.93 ? 889  SER B C     1 
ATOM   15213 O O     . SER B  1 891  ? 35.916  25.786  82.995  1.00 29.22 ? 889  SER B O     1 
ATOM   15214 C CB    . SER B  1 891  ? 36.427  23.268  80.951  1.00 29.59 ? 889  SER B CB    1 
ATOM   15215 O OG    . SER B  1 891  ? 36.278  21.860  80.940  1.00 37.46 ? 889  SER B OG    1 
ATOM   15216 N N     . GLU B  1 892  ? 35.526  26.274  80.827  1.00 27.18 ? 890  GLU B N     1 
ATOM   15217 C CA    . GLU B  1 892  ? 35.924  27.668  80.991  1.00 28.64 ? 890  GLU B CA    1 
ATOM   15218 C C     . GLU B  1 892  ? 34.976  28.397  81.933  1.00 28.34 ? 890  GLU B C     1 
ATOM   15219 O O     . GLU B  1 892  ? 35.419  29.192  82.772  1.00 30.25 ? 890  GLU B O     1 
ATOM   15220 C CB    . GLU B  1 892  ? 35.993  28.368  79.629  1.00 31.59 ? 890  GLU B CB    1 
ATOM   15221 N N     . ALA B  1 893  ? 33.668  28.133  81.819  1.00 27.98 ? 891  ALA B N     1 
ATOM   15222 C CA    . ALA B  1 893  ? 32.724  28.653  82.802  1.00 27.31 ? 891  ALA B CA    1 
ATOM   15223 C C     . ALA B  1 893  ? 33.098  28.183  84.204  1.00 28.71 ? 891  ALA B C     1 
ATOM   15224 O O     . ALA B  1 893  ? 33.192  28.987  85.139  1.00 29.02 ? 891  ALA B O     1 
ATOM   15225 C CB    . ALA B  1 893  ? 31.297  28.225  82.446  1.00 25.24 ? 891  ALA B CB    1 
ATOM   15226 N N     . LYS B  1 894  ? 33.344  26.879  84.361  1.00 26.68 ? 892  LYS B N     1 
ATOM   15227 C CA    . LYS B  1 894  ? 33.690  26.343  85.673  1.00 24.61 ? 892  LYS B CA    1 
ATOM   15228 C C     . LYS B  1 894  ? 34.927  27.041  86.242  1.00 30.04 ? 892  LYS B C     1 
ATOM   15229 O O     . LYS B  1 894  ? 34.910  27.525  87.379  1.00 28.50 ? 892  LYS B O     1 
ATOM   15230 C CB    . LYS B  1 894  ? 33.895  24.831  85.576  1.00 26.99 ? 892  LYS B CB    1 
ATOM   15231 C CG    . LYS B  1 894  ? 34.530  24.182  86.812  1.00 27.47 ? 892  LYS B CG    1 
ATOM   15232 C CD    . LYS B  1 894  ? 34.585  22.665  86.637  1.00 25.00 ? 892  LYS B CD    1 
ATOM   15233 C CE    . LYS B  1 894  ? 35.540  21.991  87.613  1.00 33.45 ? 892  LYS B CE    1 
ATOM   15234 N NZ    . LYS B  1 894  ? 34.870  21.608  88.873  1.00 37.79 ? 892  LYS B NZ    1 
ATOM   15235 N N     . ASP B  1 895  ? 35.997  27.142  85.445  1.00 27.59 ? 893  ASP B N     1 
ATOM   15236 C CA    . ASP B  1 895  ? 37.220  27.786  85.927  1.00 31.10 ? 893  ASP B CA    1 
ATOM   15237 C C     . ASP B  1 895  ? 36.967  29.243  86.293  1.00 28.94 ? 893  ASP B C     1 
ATOM   15238 O O     . ASP B  1 895  ? 37.496  29.740  87.292  1.00 32.65 ? 893  ASP B O     1 
ATOM   15239 C CB    . ASP B  1 895  ? 38.318  27.712  84.862  1.00 30.99 ? 893  ASP B CB    1 
ATOM   15240 C CG    . ASP B  1 895  ? 38.675  26.298  84.488  1.00 34.44 ? 893  ASP B CG    1 
ATOM   15241 O OD1   . ASP B  1 895  ? 38.410  25.381  85.298  1.00 40.38 ? 893  ASP B OD1   1 
ATOM   15242 O OD2   . ASP B  1 895  ? 39.227  26.104  83.383  1.00 40.49 ? 893  ASP B OD2   1 
ATOM   15243 N N     . ASN B  1 896  ? 36.192  29.945  85.467  1.00 27.13 ? 894  ASN B N     1 
ATOM   15244 C CA    . ASN B  1 896  ? 35.865  31.344  85.720  1.00 30.89 ? 894  ASN B CA    1 
ATOM   15245 C C     . ASN B  1 896  ? 35.122  31.508  87.044  1.00 32.94 ? 894  ASN B C     1 
ATOM   15246 O O     . ASN B  1 896  ? 35.435  32.413  87.830  1.00 31.33 ? 894  ASN B O     1 
ATOM   15247 C CB    . ASN B  1 896  ? 35.038  31.880  84.545  1.00 32.82 ? 894  ASN B CB    1 
ATOM   15248 C CG    . ASN B  1 896  ? 34.772  33.381  84.625  1.00 44.78 ? 894  ASN B CG    1 
ATOM   15249 O OD1   . ASN B  1 896  ? 34.427  33.916  85.678  1.00 49.50 ? 894  ASN B OD1   1 
ATOM   15250 N ND2   . ASN B  1 896  ? 34.912  34.064  83.489  1.00 48.88 ? 894  ASN B ND2   1 
ATOM   15251 N N     . ILE B  1 897  ? 34.143  30.634  87.310  1.00 29.26 ? 895  ILE B N     1 
ATOM   15252 C CA    . ILE B  1 897  ? 33.389  30.693  88.563  1.00 29.43 ? 895  ILE B CA    1 
ATOM   15253 C C     . ILE B  1 897  ? 34.287  30.353  89.746  1.00 28.36 ? 895  ILE B C     1 
ATOM   15254 O O     . ILE B  1 897  ? 34.276  31.041  90.773  1.00 29.44 ? 895  ILE B O     1 
ATOM   15255 C CB    . ILE B  1 897  ? 32.176  29.747  88.515  1.00 28.97 ? 895  ILE B CB    1 
ATOM   15256 C CG1   . ILE B  1 897  ? 31.189  30.182  87.444  1.00 25.93 ? 895  ILE B CG1   1 
ATOM   15257 C CG2   . ILE B  1 897  ? 31.503  29.663  89.901  1.00 25.11 ? 895  ILE B CG2   1 
ATOM   15258 C CD1   . ILE B  1 897  ? 30.327  29.047  86.947  1.00 24.11 ? 895  ILE B CD1   1 
ATOM   15259 N N     . GLU B  1 898  ? 35.056  29.272  89.633  1.00 30.86 ? 896  GLU B N     1 
ATOM   15260 C CA    . GLU B  1 898  ? 35.893  28.859  90.756  1.00 32.76 ? 896  GLU B CA    1 
ATOM   15261 C C     . GLU B  1 898  ? 37.010  29.858  91.034  1.00 33.52 ? 896  GLU B C     1 
ATOM   15262 O O     . GLU B  1 898  ? 37.420  30.014  92.190  1.00 37.17 ? 896  GLU B O     1 
ATOM   15263 C CB    . GLU B  1 898  ? 36.462  27.464  90.503  1.00 32.27 ? 896  GLU B CB    1 
ATOM   15264 C CG    . GLU B  1 898  ? 35.379  26.400  90.421  1.00 33.77 ? 896  GLU B CG    1 
ATOM   15265 C CD    . GLU B  1 898  ? 35.934  24.993  90.221  1.00 39.23 ? 896  GLU B CD    1 
ATOM   15266 O OE1   . GLU B  1 898  ? 36.992  24.845  89.563  1.00 41.48 ? 896  GLU B OE1   1 
ATOM   15267 O OE2   . GLU B  1 898  ? 35.306  24.036  90.726  1.00 42.54 ? 896  GLU B OE2   1 
ATOM   15268 N N     . LYS B  1 899  ? 37.512  30.539  90.001  1.00 34.06 ? 897  LYS B N     1 
ATOM   15269 C CA    . LYS B  1 899  ? 38.496  31.599  90.214  1.00 32.51 ? 897  LYS B CA    1 
ATOM   15270 C C     . LYS B  1 899  ? 37.926  32.715  91.087  1.00 33.81 ? 897  LYS B C     1 
ATOM   15271 O O     . LYS B  1 899  ? 38.619  33.250  91.962  1.00 30.51 ? 897  LYS B O     1 
ATOM   15272 C CB    . LYS B  1 899  ? 38.955  32.152  88.868  1.00 37.94 ? 897  LYS B CB    1 
ATOM   15273 C CG    . LYS B  1 899  ? 39.849  33.388  88.954  1.00 39.59 ? 897  LYS B CG    1 
ATOM   15274 C CD    . LYS B  1 899  ? 39.844  34.123  87.616  1.00 44.28 ? 897  LYS B CD    1 
ATOM   15275 C CE    . LYS B  1 899  ? 40.854  35.254  87.572  1.00 47.45 ? 897  LYS B CE    1 
ATOM   15276 N NZ    . LYS B  1 899  ? 40.636  36.084  86.357  1.00 49.02 ? 897  LYS B NZ    1 
ATOM   15277 N N     . HIS B  1 900  ? 36.659  33.076  90.868  1.00 28.00 ? 898  HIS B N     1 
ATOM   15278 C CA    . HIS B  1 900  ? 35.999  34.031  91.752  1.00 29.47 ? 898  HIS B CA    1 
ATOM   15279 C C     . HIS B  1 900  ? 35.888  33.491  93.168  1.00 31.47 ? 898  HIS B C     1 
ATOM   15280 O O     . HIS B  1 900  ? 36.127  34.219  94.139  1.00 34.31 ? 898  HIS B O     1 
ATOM   15281 C CB    . HIS B  1 900  ? 34.608  34.371  91.229  1.00 36.06 ? 898  HIS B CB    1 
ATOM   15282 C CG    . HIS B  1 900  ? 33.809  35.210  92.174  1.00 35.53 ? 898  HIS B CG    1 
ATOM   15283 N ND1   . HIS B  1 900  ? 34.044  36.556  92.349  1.00 36.02 ? 898  HIS B ND1   1 
ATOM   15284 C CD2   . HIS B  1 900  ? 32.790  34.892  93.009  1.00 34.87 ? 898  HIS B CD2   1 
ATOM   15285 C CE1   . HIS B  1 900  ? 33.189  37.037  93.236  1.00 36.86 ? 898  HIS B CE1   1 
ATOM   15286 N NE2   . HIS B  1 900  ? 32.419  36.047  93.653  1.00 33.82 ? 898  HIS B NE2   1 
ATOM   15287 N N     . ILE B  1 901  ? 35.504  32.222  93.308  1.00 30.86 ? 899  ILE B N     1 
ATOM   15288 C CA    . ILE B  1 901  ? 35.289  31.646  94.631  1.00 28.79 ? 899  ILE B CA    1 
ATOM   15289 C C     . ILE B  1 901  ? 36.591  31.627  95.411  1.00 34.96 ? 899  ILE B C     1 
ATOM   15290 O O     . ILE B  1 901  ? 36.629  31.966  96.601  1.00 41.08 ? 899  ILE B O     1 
ATOM   15291 C CB    . ILE B  1 901  ? 34.678  30.240  94.507  1.00 32.03 ? 899  ILE B CB    1 
ATOM   15292 C CG1   . ILE B  1 901  ? 33.254  30.328  93.931  1.00 27.40 ? 899  ILE B CG1   1 
ATOM   15293 C CG2   . ILE B  1 901  ? 34.686  29.517  95.846  1.00 31.03 ? 899  ILE B CG2   1 
ATOM   15294 C CD1   . ILE B  1 901  ? 32.610  28.986  93.777  1.00 28.57 ? 899  ILE B CD1   1 
ATOM   15295 N N     . GLU B  1 902  ? 37.685  31.268  94.743  1.00 37.78 ? 900  GLU B N     1 
ATOM   15296 C CA    . GLU B  1 902  ? 38.989  31.231  95.402  1.00 35.17 ? 900  GLU B CA    1 
ATOM   15297 C C     . GLU B  1 902  ? 39.455  32.625  95.793  1.00 35.96 ? 900  GLU B C     1 
ATOM   15298 O O     . GLU B  1 902  ? 40.050  32.805  96.859  1.00 40.08 ? 900  GLU B O     1 
ATOM   15299 C CB    . GLU B  1 902  ? 40.014  30.561  94.491  1.00 37.61 ? 900  GLU B CB    1 
ATOM   15300 C CG    . GLU B  1 902  ? 39.779  29.078  94.349  1.00 40.19 ? 900  GLU B CG    1 
ATOM   15301 C CD    . GLU B  1 902  ? 39.557  28.401  95.691  1.00 43.26 ? 900  GLU B CD    1 
ATOM   15302 O OE1   . GLU B  1 902  ? 40.457  28.467  96.550  1.00 46.52 ? 900  GLU B OE1   1 
ATOM   15303 O OE2   . GLU B  1 902  ? 38.469  27.819  95.897  1.00 47.20 ? 900  GLU B OE2   1 
ATOM   15304 N N     . ARG B  1 903  ? 39.209  33.622  94.940  1.00 33.40 ? 901  ARG B N     1 
ATOM   15305 C CA    . ARG B  1 903  ? 39.518  34.997  95.313  1.00 37.56 ? 901  ARG B CA    1 
ATOM   15306 C C     . ARG B  1 903  ? 38.741  35.417  96.559  1.00 44.13 ? 901  ARG B C     1 
ATOM   15307 O O     . ARG B  1 903  ? 39.306  36.038  97.468  1.00 45.47 ? 901  ARG B O     1 
ATOM   15308 C CB    . ARG B  1 903  ? 39.224  35.936  94.146  1.00 37.31 ? 901  ARG B CB    1 
ATOM   15309 C CG    . ARG B  1 903  ? 39.488  37.396  94.452  1.00 43.50 ? 901  ARG B CG    1 
ATOM   15310 C CD    . ARG B  1 903  ? 38.815  38.311  93.437  1.00 50.34 ? 901  ARG B CD    1 
ATOM   15311 N NE    . ARG B  1 903  ? 38.991  39.720  93.775  1.00 58.46 ? 901  ARG B NE    1 
ATOM   15312 C CZ    . ARG B  1 903  ? 39.891  40.518  93.215  1.00 64.46 ? 901  ARG B CZ    1 
ATOM   15313 N NH1   . ARG B  1 903  ? 40.700  40.086  92.260  1.00 65.51 ? 901  ARG B NH1   1 
ATOM   15314 N NH2   . ARG B  1 903  ? 39.981  41.783  93.621  1.00 59.86 ? 901  ARG B NH2   1 
ATOM   15315 N N     . MET B  1 904  ? 37.447  35.076  96.630  1.00 40.31 ? 902  MET B N     1 
ATOM   15316 C CA    . MET B  1 904  ? 36.680  35.385  97.836  1.00 42.43 ? 902  MET B CA    1 
ATOM   15317 C C     . MET B  1 904  ? 37.230  34.639  99.048  1.00 41.76 ? 902  MET B C     1 
ATOM   15318 O O     . MET B  1 904  ? 37.380  35.220  100.130 1.00 42.03 ? 902  MET B O     1 
ATOM   15319 C CB    . MET B  1 904  ? 35.201  35.052  97.635  1.00 37.59 ? 902  MET B CB    1 
ATOM   15320 C CG    . MET B  1 904  ? 34.508  35.926  96.620  1.00 36.63 ? 902  MET B CG    1 
ATOM   15321 S SD    . MET B  1 904  ? 34.629  37.687  96.992  1.00 43.24 ? 902  MET B SD    1 
ATOM   15322 C CE    . MET B  1 904  ? 35.639  38.268  95.632  1.00 43.98 ? 902  MET B CE    1 
ATOM   15323 N N     . ARG B  1 905  ? 37.531  33.351  98.889  1.00 42.13 ? 903  ARG B N     1 
ATOM   15324 C CA    . ARG B  1 905  ? 38.087  32.584  99.999  1.00 43.61 ? 903  ARG B CA    1 
ATOM   15325 C C     . ARG B  1 905  ? 39.458  33.118  100.397 1.00 43.93 ? 903  ARG B C     1 
ATOM   15326 O O     . ARG B  1 905  ? 39.777  33.208  101.588 1.00 46.41 ? 903  ARG B O     1 
ATOM   15327 C CB    . ARG B  1 905  ? 38.175  31.104  99.623  1.00 46.11 ? 903  ARG B CB    1 
ATOM   15328 C CG    . ARG B  1 905  ? 37.747  30.164  100.733 1.00 48.44 ? 903  ARG B CG    1 
ATOM   15329 C CD    . ARG B  1 905  ? 38.158  28.737  100.432 1.00 52.53 ? 903  ARG B CD    1 
ATOM   15330 N NE    . ARG B  1 905  ? 37.530  28.200  99.228  1.00 46.78 ? 903  ARG B NE    1 
ATOM   15331 C CZ    . ARG B  1 905  ? 36.475  27.396  99.226  1.00 43.30 ? 903  ARG B CZ    1 
ATOM   15332 N NH1   . ARG B  1 905  ? 35.855  27.064  100.347 1.00 46.28 ? 903  ARG B NH1   1 
ATOM   15333 N NH2   . ARG B  1 905  ? 36.035  26.906  98.071  1.00 42.06 ? 903  ARG B NH2   1 
ATOM   15334 N N     . GLY B  1 906  ? 40.279  33.490  99.413  1.00 44.13 ? 904  GLY B N     1 
ATOM   15335 C CA    . GLY B  1 906  ? 41.583  34.051  99.722  1.00 47.13 ? 904  GLY B CA    1 
ATOM   15336 C C     . GLY B  1 906  ? 41.488  35.410  100.380 1.00 49.04 ? 904  GLY B C     1 
ATOM   15337 O O     . GLY B  1 906  ? 42.379  35.799  101.142 1.00 45.43 ? 904  GLY B O     1 
ATOM   15338 N N     . LEU B  1 907  ? 40.407  36.145  100.111 1.00 49.39 ? 905  LEU B N     1 
ATOM   15339 C CA    . LEU B  1 907  ? 40.180  37.427  100.762 1.00 48.52 ? 905  LEU B CA    1 
ATOM   15340 C C     . LEU B  1 907  ? 39.674  37.284  102.193 1.00 49.20 ? 905  LEU B C     1 
ATOM   15341 O O     . LEU B  1 907  ? 39.574  38.294  102.897 1.00 55.07 ? 905  LEU B O     1 
ATOM   15342 C CB    . LEU B  1 907  ? 39.194  38.266  99.946  1.00 46.26 ? 905  LEU B CB    1 
ATOM   15343 N N     . GLY B  1 908  ? 39.348  36.069  102.638 1.00 48.46 ? 906  GLY B N     1 
ATOM   15344 C CA    . GLY B  1 908  ? 38.946  35.812  104.009 1.00 43.59 ? 906  GLY B CA    1 
ATOM   15345 C C     . GLY B  1 908  ? 37.466  35.562  104.225 1.00 47.21 ? 906  GLY B C     1 
ATOM   15346 O O     . GLY B  1 908  ? 37.080  35.226  105.354 1.00 37.95 ? 906  GLY B O     1 
ATOM   15347 N N     . ARG B  1 909  ? 36.625  35.697  103.195 1.00 40.96 ? 907  ARG B N     1 
ATOM   15348 C CA    . ARG B  1 909  ? 35.179  35.603  103.381 1.00 35.67 ? 907  ARG B CA    1 
ATOM   15349 C C     . ARG B  1 909  ? 34.749  34.168  103.676 1.00 41.39 ? 907  ARG B C     1 
ATOM   15350 O O     . ARG B  1 909  ? 35.373  33.204  103.225 1.00 45.46 ? 907  ARG B O     1 
ATOM   15351 C CB    . ARG B  1 909  ? 34.458  36.126  102.140 1.00 39.38 ? 907  ARG B CB    1 
ATOM   15352 N N     . LYS B  1 910  ? 33.671  34.027  104.450 1.00 35.87 ? 908  LYS B N     1 
ATOM   15353 C CA    . LYS B  1 910  ? 33.120  32.702  104.726 1.00 35.18 ? 908  LYS B CA    1 
ATOM   15354 C C     . LYS B  1 910  ? 32.456  32.133  103.472 1.00 42.16 ? 908  LYS B C     1 
ATOM   15355 O O     . LYS B  1 910  ? 31.661  32.817  102.819 1.00 42.22 ? 908  LYS B O     1 
ATOM   15356 C CB    . LYS B  1 910  ? 32.107  32.767  105.869 1.00 33.64 ? 908  LYS B CB    1 
ATOM   15357 N N     . VAL B  1 911  ? 32.760  30.867  103.166 1.00 40.75 ? 909  VAL B N     1 
ATOM   15358 C CA    . VAL B  1 911  ? 32.354  30.188  101.933 1.00 35.56 ? 909  VAL B CA    1 
ATOM   15359 C C     . VAL B  1 911  ? 31.818  28.808  102.312 1.00 37.30 ? 909  VAL B C     1 
ATOM   15360 O O     . VAL B  1 911  ? 32.577  27.958  102.793 1.00 41.95 ? 909  VAL B O     1 
ATOM   15361 C CB    . VAL B  1 911  ? 33.525  30.056  100.944 1.00 39.69 ? 909  VAL B CB    1 
ATOM   15362 C CG1   . VAL B  1 911  ? 33.121  29.244  99.710  1.00 35.34 ? 909  VAL B CG1   1 
ATOM   15363 C CG2   . VAL B  1 911  ? 34.066  31.423  100.547 1.00 36.87 ? 909  VAL B CG2   1 
ATOM   15364 N N     . GLU B  1 912  ? 30.523  28.582  102.099 1.00 38.22 ? 910  GLU B N     1 
ATOM   15365 C CA    . GLU B  1 912  ? 29.892  27.283  102.312 1.00 33.89 ? 910  GLU B CA    1 
ATOM   15366 C C     . GLU B  1 912  ? 29.637  26.612  100.966 1.00 37.31 ? 910  GLU B C     1 
ATOM   15367 O O     . GLU B  1 912  ? 29.095  27.245  100.056 1.00 31.65 ? 910  GLU B O     1 
ATOM   15368 C CB    . GLU B  1 912  ? 28.573  27.441  103.068 1.00 36.80 ? 910  GLU B CB    1 
ATOM   15369 C CG    . GLU B  1 912  ? 27.853  26.129  103.380 1.00 34.53 ? 910  GLU B CG    1 
ATOM   15370 C CD    . GLU B  1 912  ? 28.269  25.549  104.719 1.00 41.06 ? 910  GLU B CD    1 
ATOM   15371 O OE1   . GLU B  1 912  ? 28.813  26.312  105.545 1.00 37.27 ? 910  GLU B OE1   1 
ATOM   15372 O OE2   . GLU B  1 912  ? 28.064  24.337  104.945 1.00 43.88 ? 910  GLU B OE2   1 
ATOM   15373 N N     . GLN B  1 913  ? 30.000  25.329  100.846 1.00 31.50 ? 911  GLN B N     1 
ATOM   15374 C CA    . GLN B  1 913  ? 29.798  24.596  99.602  1.00 35.13 ? 911  GLN B CA    1 
ATOM   15375 C C     . GLN B  1 913  ? 29.278  23.186  99.846  1.00 38.32 ? 911  GLN B C     1 
ATOM   15376 O O     . GLN B  1 913  ? 29.669  22.520  100.808 1.00 38.44 ? 911  GLN B O     1 
ATOM   15377 C CB    . GLN B  1 913  ? 31.088  24.510  98.783  1.00 31.55 ? 911  GLN B CB    1 
ATOM   15378 C CG    . GLN B  1 913  ? 31.461  25.801  98.082  1.00 35.60 ? 911  GLN B CG    1 
ATOM   15379 C CD    . GLN B  1 913  ? 32.661  25.632  97.173  1.00 33.70 ? 911  GLN B CD    1 
ATOM   15380 O OE1   . GLN B  1 913  ? 33.689  25.111  97.586  1.00 37.64 ? 911  GLN B OE1   1 
ATOM   15381 N NE2   . GLN B  1 913  ? 32.527  26.055  95.925  1.00 27.75 ? 911  GLN B NE2   1 
ATOM   15382 N N     . ILE B  1 914  ? 28.377  22.761  98.957  1.00 36.23 ? 912  ILE B N     1 
ATOM   15383 C CA    . ILE B  1 914  ? 27.964  21.368  98.846  1.00 35.43 ? 912  ILE B CA    1 
ATOM   15384 C C     . ILE B  1 914  ? 29.147  20.491  98.443  1.00 39.51 ? 912  ILE B C     1 
ATOM   15385 O O     . ILE B  1 914  ? 29.949  20.856  97.575  1.00 38.91 ? 912  ILE B O     1 
ATOM   15386 C CB    . ILE B  1 914  ? 26.842  21.270  97.796  1.00 36.45 ? 912  ILE B CB    1 
ATOM   15387 C CG1   . ILE B  1 914  ? 25.509  21.754  98.355  1.00 35.38 ? 912  ILE B CG1   1 
ATOM   15388 C CG2   . ILE B  1 914  ? 26.734  19.870  97.212  1.00 39.77 ? 912  ILE B CG2   1 
ATOM   15389 C CD1   . ILE B  1 914  ? 24.406  21.726  97.316  1.00 32.04 ? 912  ILE B CD1   1 
ATOM   15390 N N     . GLY B  1 915  ? 29.249  19.312  99.053  1.00 46.01 ? 913  GLY B N     1 
ATOM   15391 C CA    . GLY B  1 915  ? 30.211  18.323  98.587  1.00 46.31 ? 913  GLY B CA    1 
ATOM   15392 C C     . GLY B  1 915  ? 29.658  17.568  97.388  1.00 46.54 ? 913  GLY B C     1 
ATOM   15393 O O     . GLY B  1 915  ? 28.551  17.022  97.440  1.00 52.87 ? 913  GLY B O     1 
ATOM   15394 N N     . LEU B  1 916  ? 30.429  17.532  96.304  1.00 41.28 ? 914  LEU B N     1 
ATOM   15395 C CA    . LEU B  1 916  ? 29.990  16.878  95.075  1.00 37.00 ? 914  LEU B CA    1 
ATOM   15396 C C     . LEU B  1 916  ? 30.412  15.416  95.051  1.00 38.53 ? 914  LEU B C     1 
ATOM   15397 O O     . LEU B  1 916  ? 31.465  15.044  95.580  1.00 39.70 ? 914  LEU B O     1 
ATOM   15398 C CB    . LEU B  1 916  ? 30.554  17.589  93.846  1.00 35.09 ? 914  LEU B CB    1 
ATOM   15399 C CG    . LEU B  1 916  ? 30.163  19.052  93.654  1.00 37.76 ? 914  LEU B CG    1 
ATOM   15400 C CD1   . LEU B  1 916  ? 30.662  19.542  92.311  1.00 35.28 ? 914  LEU B CD1   1 
ATOM   15401 C CD2   . LEU B  1 916  ? 28.655  19.252  93.777  1.00 34.78 ? 914  LEU B CD2   1 
ATOM   15402 N N     . ALA B  1 917  ? 29.581  14.585  94.425  1.00 34.32 ? 915  ALA B N     1 
ATOM   15403 C CA    . ALA B  1 917  ? 29.898  13.170  94.300  1.00 38.60 ? 915  ALA B CA    1 
ATOM   15404 C C     . ALA B  1 917  ? 31.053  12.968  93.319  1.00 42.03 ? 915  ALA B C     1 
ATOM   15405 O O     . ALA B  1 917  ? 31.336  13.815  92.463  1.00 36.31 ? 915  ALA B O     1 
ATOM   15406 C CB    . ALA B  1 917  ? 28.670  12.379  93.846  1.00 39.00 ? 915  ALA B CB    1 
ATOM   15407 N N     . SER B  1 918  ? 31.733  11.826  93.454  1.00 38.26 ? 916  SER B N     1 
ATOM   15408 C CA    . SER B  1 918  ? 32.841  11.532  92.550  1.00 40.64 ? 916  SER B CA    1 
ATOM   15409 C C     . SER B  1 918  ? 32.377  11.463  91.098  1.00 39.95 ? 916  SER B C     1 
ATOM   15410 O O     . SER B  1 918  ? 33.117  11.863  90.192  1.00 36.77 ? 916  SER B O     1 
ATOM   15411 C CB    . SER B  1 918  ? 33.524  10.225  92.962  1.00 44.35 ? 916  SER B CB    1 
ATOM   15412 O OG    . SER B  1 918  ? 32.624  9.133   92.866  1.00 50.29 ? 916  SER B OG    1 
ATOM   15413 N N     . GLU B  1 919  ? 31.147  10.991  90.861  1.00 40.52 ? 917  GLU B N     1 
ATOM   15414 C CA    . GLU B  1 919  ? 30.631  10.855  89.501  1.00 40.35 ? 917  GLU B CA    1 
ATOM   15415 C C     . GLU B  1 919  ? 30.579  12.181  88.757  1.00 38.72 ? 917  GLU B C     1 
ATOM   15416 O O     . GLU B  1 919  ? 30.495  12.182  87.521  1.00 38.23 ? 917  GLU B O     1 
ATOM   15417 C CB    . GLU B  1 919  ? 29.231  10.235  89.520  1.00 40.51 ? 917  GLU B CB    1 
ATOM   15418 C CG    . GLU B  1 919  ? 29.185  8.752   89.864  1.00 49.92 ? 917  GLU B CG    1 
ATOM   15419 C CD    . GLU B  1 919  ? 29.323  8.476   91.357  1.00 57.57 ? 917  GLU B CD    1 
ATOM   15420 O OE1   . GLU B  1 919  ? 29.502  9.439   92.140  1.00 49.50 ? 917  GLU B OE1   1 
ATOM   15421 O OE2   . GLU B  1 919  ? 29.251  7.287   91.746  1.00 61.17 ? 917  GLU B OE2   1 
ATOM   15422 N N     . THR B  1 920  ? 30.600  13.309  89.472  1.00 33.99 ? 918  THR B N     1 
ATOM   15423 C CA    . THR B  1 920  ? 30.617  14.601  88.799  1.00 32.09 ? 918  THR B CA    1 
ATOM   15424 C C     . THR B  1 920  ? 31.934  14.869  88.076  1.00 34.91 ? 918  THR B C     1 
ATOM   15425 O O     . THR B  1 920  ? 31.975  15.754  87.214  1.00 32.14 ? 918  THR B O     1 
ATOM   15426 C CB    . THR B  1 920  ? 30.353  15.737  89.796  1.00 34.13 ? 918  THR B CB    1 
ATOM   15427 O OG1   . THR B  1 920  ? 31.403  15.785  90.775  1.00 32.75 ? 918  THR B OG1   1 
ATOM   15428 C CG2   . THR B  1 920  ? 29.002  15.566  90.486  1.00 31.59 ? 918  THR B CG2   1 
ATOM   15429 N N     . GLY B  1 921  ? 33.006  14.130  88.403  1.00 30.55 ? 919  GLY B N     1 
ATOM   15430 C CA    . GLY B  1 921  ? 34.314  14.363  87.802  1.00 34.69 ? 919  GLY B CA    1 
ATOM   15431 C C     . GLY B  1 921  ? 34.358  14.274  86.284  1.00 32.93 ? 919  GLY B C     1 
ATOM   15432 O O     . GLY B  1 921  ? 35.259  14.849  85.666  1.00 36.73 ? 919  GLY B O     1 
ATOM   15433 N N     . VAL B  1 922  ? 33.408  13.570  85.660  1.00 30.82 ? 920  VAL B N     1 
ATOM   15434 C CA    . VAL B  1 922  ? 33.409  13.440  84.201  1.00 32.67 ? 920  VAL B CA    1 
ATOM   15435 C C     . VAL B  1 922  ? 32.724  14.601  83.498  1.00 30.72 ? 920  VAL B C     1 
ATOM   15436 O O     . VAL B  1 922  ? 32.736  14.660  82.262  1.00 31.42 ? 920  VAL B O     1 
ATOM   15437 C CB    . VAL B  1 922  ? 32.747  12.116  83.775  1.00 31.91 ? 920  VAL B CB    1 
ATOM   15438 C CG1   . VAL B  1 922  ? 33.618  10.946  84.184  1.00 33.78 ? 920  VAL B CG1   1 
ATOM   15439 C CG2   . VAL B  1 922  ? 31.344  12.010  84.392  1.00 30.85 ? 920  VAL B CG2   1 
ATOM   15440 N N     . GLY B  1 923  ? 32.122  15.525  84.237  1.00 26.71 ? 921  GLY B N     1 
ATOM   15441 C CA    . GLY B  1 923  ? 31.537  16.704  83.638  1.00 25.94 ? 921  GLY B CA    1 
ATOM   15442 C C     . GLY B  1 923  ? 32.097  17.948  84.290  1.00 28.39 ? 921  GLY B C     1 
ATOM   15443 O O     . GLY B  1 923  ? 33.072  17.858  85.042  1.00 29.27 ? 921  GLY B O     1 
ATOM   15444 N N     . THR B  1 924  ? 31.499  19.102  84.018  1.00 23.98 ? 922  THR B N     1 
ATOM   15445 C CA    . THR B  1 924  ? 31.929  20.384  84.583  1.00 24.90 ? 922  THR B CA    1 
ATOM   15446 C C     . THR B  1 924  ? 30.879  20.864  85.578  1.00 23.21 ? 922  THR B C     1 
ATOM   15447 O O     . THR B  1 924  ? 29.905  21.515  85.197  1.00 25.01 ? 922  THR B O     1 
ATOM   15448 C CB    . THR B  1 924  ? 32.149  21.412  83.479  1.00 22.75 ? 922  THR B CB    1 
ATOM   15449 O OG1   . THR B  1 924  ? 31.013  21.413  82.600  1.00 24.20 ? 922  THR B OG1   1 
ATOM   15450 C CG2   . THR B  1 924  ? 33.371  21.058  82.665  1.00 27.66 ? 922  THR B CG2   1 
ATOM   15451 N N     . PHE B  1 925  ? 31.103  20.586  86.861  1.00 24.65 ? 923  PHE B N     1 
ATOM   15452 C CA    . PHE B  1 925  ? 30.179  20.977  87.917  1.00 22.67 ? 923  PHE B CA    1 
ATOM   15453 C C     . PHE B  1 925  ? 30.843  21.976  88.846  1.00 27.71 ? 923  PHE B C     1 
ATOM   15454 O O     . PHE B  1 925  ? 32.039  21.862  89.154  1.00 28.95 ? 923  PHE B O     1 
ATOM   15455 C CB    . PHE B  1 925  ? 29.710  19.772  88.740  1.00 23.99 ? 923  PHE B CB    1 
ATOM   15456 C CG    . PHE B  1 925  ? 28.882  18.792  87.966  1.00 23.11 ? 923  PHE B CG    1 
ATOM   15457 C CD1   . PHE B  1 925  ? 29.484  17.820  87.186  1.00 24.27 ? 923  PHE B CD1   1 
ATOM   15458 C CD2   . PHE B  1 925  ? 27.499  18.847  88.020  1.00 22.63 ? 923  PHE B CD2   1 
ATOM   15459 C CE1   . PHE B  1 925  ? 28.711  16.909  86.469  1.00 24.70 ? 923  PHE B CE1   1 
ATOM   15460 C CE2   . PHE B  1 925  ? 26.721  17.947  87.307  1.00 21.32 ? 923  PHE B CE2   1 
ATOM   15461 C CZ    . PHE B  1 925  ? 27.327  16.977  86.532  1.00 22.65 ? 923  PHE B CZ    1 
ATOM   15462 N N     . VAL B  1 926  ? 30.053  22.949  89.285  1.00 24.45 ? 924  VAL B N     1 
ATOM   15463 C CA    . VAL B  1 926  ? 30.409  23.841  90.383  1.00 22.89 ? 924  VAL B CA    1 
ATOM   15464 C C     . VAL B  1 926  ? 29.407  23.600  91.502  1.00 23.28 ? 924  VAL B C     1 
ATOM   15465 O O     . VAL B  1 926  ? 28.199  23.638  91.254  1.00 23.90 ? 924  VAL B O     1 
ATOM   15466 C CB    . VAL B  1 926  ? 30.393  25.324  89.967  1.00 20.06 ? 924  VAL B CB    1 
ATOM   15467 C CG1   . VAL B  1 926  ? 30.619  26.216  91.196  1.00 23.32 ? 924  VAL B CG1   1 
ATOM   15468 C CG2   . VAL B  1 926  ? 31.451  25.587  88.918  1.00 24.13 ? 924  VAL B CG2   1 
ATOM   15469 N N     . PRO B  1 927  ? 29.840  23.333  92.727  1.00 23.89 ? 925  PRO B N     1 
ATOM   15470 C CA    . PRO B  1 927  ? 28.879  23.100  93.801  1.00 25.34 ? 925  PRO B CA    1 
ATOM   15471 C C     . PRO B  1 927  ? 28.153  24.380  94.155  1.00 24.09 ? 925  PRO B C     1 
ATOM   15472 O O     . PRO B  1 927  ? 28.728  25.482  94.092  1.00 24.06 ? 925  PRO B O     1 
ATOM   15473 C CB    . PRO B  1 927  ? 29.754  22.615  94.967  1.00 30.44 ? 925  PRO B CB    1 
ATOM   15474 C CG    . PRO B  1 927  ? 31.098  23.181  94.687  1.00 28.52 ? 925  PRO B CG    1 
ATOM   15475 C CD    . PRO B  1 927  ? 31.236  23.203  93.193  1.00 24.53 ? 925  PRO B CD    1 
ATOM   15476 N N     . PRO B  1 928  ? 26.875  24.280  94.490  1.00 26.33 ? 926  PRO B N     1 
ATOM   15477 C CA    . PRO B  1 928  ? 26.172  25.435  95.040  1.00 26.21 ? 926  PRO B CA    1 
ATOM   15478 C C     . PRO B  1 928  ? 26.947  26.019  96.207  1.00 27.79 ? 926  PRO B C     1 
ATOM   15479 O O     . PRO B  1 928  ? 27.387  25.301  97.105  1.00 29.41 ? 926  PRO B O     1 
ATOM   15480 C CB    . PRO B  1 928  ? 24.829  24.843  95.462  1.00 29.46 ? 926  PRO B CB    1 
ATOM   15481 C CG    . PRO B  1 928  ? 24.591  23.796  94.410  1.00 31.27 ? 926  PRO B CG    1 
ATOM   15482 C CD    . PRO B  1 928  ? 25.951  23.178  94.168  1.00 30.80 ? 926  PRO B CD    1 
ATOM   15483 N N     . THR B  1 929  ? 27.127  27.338  96.172  1.00 24.96 ? 927  THR B N     1 
ATOM   15484 C CA    . THR B  1 929  ? 28.052  28.032  97.052  1.00 26.05 ? 927  THR B CA    1 
ATOM   15485 C C     . THR B  1 929  ? 27.390  29.265  97.642  1.00 26.60 ? 927  THR B C     1 
ATOM   15486 O O     . THR B  1 929  ? 26.676  29.995  96.950  1.00 25.82 ? 927  THR B O     1 
ATOM   15487 C CB    . THR B  1 929  ? 29.317  28.445  96.291  1.00 24.93 ? 927  THR B CB    1 
ATOM   15488 O OG1   . THR B  1 929  ? 29.892  27.287  95.680  1.00 26.33 ? 927  THR B OG1   1 
ATOM   15489 C CG2   . THR B  1 929  ? 30.341  29.085  97.228  1.00 27.41 ? 927  THR B CG2   1 
ATOM   15490 N N     . ILE B  1 930  ? 27.637  29.490  98.930  1.00 25.90 ? 928  ILE B N     1 
ATOM   15491 C CA    . ILE B  1 930  ? 27.168  30.674  99.630  1.00 31.18 ? 928  ILE B CA    1 
ATOM   15492 C C     . ILE B  1 930  ? 28.401  31.399  100.139 1.00 33.07 ? 928  ILE B C     1 
ATOM   15493 O O     . ILE B  1 930  ? 29.230  30.806  100.847 1.00 33.59 ? 928  ILE B O     1 
ATOM   15494 C CB    . ILE B  1 930  ? 26.210  30.325  100.782 1.00 27.49 ? 928  ILE B CB    1 
ATOM   15495 C CG1   . ILE B  1 930  ? 25.027  29.492  100.282 1.00 32.06 ? 928  ILE B CG1   1 
ATOM   15496 C CG2   . ILE B  1 930  ? 25.733  31.599  101.479 1.00 31.28 ? 928  ILE B CG2   1 
ATOM   15497 C CD1   . ILE B  1 930  ? 24.130  29.010  101.407 1.00 29.43 ? 928  ILE B CD1   1 
ATOM   15498 N N     . ILE B  1 931  ? 28.548  32.661  99.751  1.00 29.22 ? 929  ILE B N     1 
ATOM   15499 C CA    . ILE B  1 931  ? 29.676  33.485  100.167 1.00 30.11 ? 929  ILE B CA    1 
ATOM   15500 C C     . ILE B  1 931  ? 29.121  34.662  100.956 1.00 32.80 ? 929  ILE B C     1 
ATOM   15501 O O     . ILE B  1 931  ? 28.215  35.351  100.488 1.00 28.70 ? 929  ILE B O     1 
ATOM   15502 C CB    . ILE B  1 931  ? 30.495  33.973  98.957  1.00 30.14 ? 929  ILE B CB    1 
ATOM   15503 C CG1   . ILE B  1 931  ? 31.021  32.783  98.150  1.00 29.04 ? 929  ILE B CG1   1 
ATOM   15504 C CG2   . ILE B  1 931  ? 31.635  34.887  99.403  1.00 32.91 ? 929  ILE B CG2   1 
ATOM   15505 C CD1   . ILE B  1 931  ? 31.933  33.186  97.032  1.00 30.34 ? 929  ILE B CD1   1 
ATOM   15506 N N     . GLU B  1 932  ? 29.652  34.897  102.148 1.00 32.29 ? 930  GLU B N     1 
ATOM   15507 C CA    . GLU B  1 932  ? 29.191  36.013  102.968 1.00 34.60 ? 930  GLU B CA    1 
ATOM   15508 C C     . GLU B  1 932  ? 30.127  37.194  102.753 1.00 33.81 ? 930  GLU B C     1 
ATOM   15509 O O     . GLU B  1 932  ? 31.344  37.061  102.917 1.00 38.42 ? 930  GLU B O     1 
ATOM   15510 C CB    . GLU B  1 932  ? 29.104  35.605  104.437 1.00 35.94 ? 930  GLU B CB    1 
ATOM   15511 C CG    . GLU B  1 932  ? 27.931  34.656  104.667 1.00 38.39 ? 930  GLU B CG    1 
ATOM   15512 C CD    . GLU B  1 932  ? 27.950  33.983  106.020 1.00 45.97 ? 930  GLU B CD    1 
ATOM   15513 O OE1   . GLU B  1 932  ? 27.974  34.707  107.037 1.00 40.35 ? 930  GLU B OE1   1 
ATOM   15514 O OE2   . GLU B  1 932  ? 27.937  32.726  106.061 1.00 44.78 ? 930  GLU B OE2   1 
ATOM   15515 N N     . LEU B  1 933  ? 29.566  38.323  102.339 1.00 30.28 ? 931  LEU B N     1 
ATOM   15516 C CA    . LEU B  1 933  ? 30.334  39.512  102.005 1.00 38.77 ? 931  LEU B CA    1 
ATOM   15517 C C     . LEU B  1 933  ? 30.267  40.530  103.133 1.00 47.31 ? 931  LEU B C     1 
ATOM   15518 O O     . LEU B  1 933  ? 29.314  40.559  103.915 1.00 45.31 ? 931  LEU B O     1 
ATOM   15519 C CB    . LEU B  1 933  ? 29.823  40.171  100.727 1.00 41.50 ? 931  LEU B CB    1 
ATOM   15520 C CG    . LEU B  1 933  ? 29.786  39.367  99.432  1.00 38.32 ? 931  LEU B CG    1 
ATOM   15521 C CD1   . LEU B  1 933  ? 29.277  40.262  98.319  1.00 43.04 ? 931  LEU B CD1   1 
ATOM   15522 C CD2   . LEU B  1 933  ? 31.153  38.812  99.089  1.00 37.62 ? 931  LEU B CD2   1 
ATOM   15523 N N     . GLU B  1 934  ? 31.291  41.380  103.195 1.00 51.02 ? 932  GLU B N     1 
ATOM   15524 C CA    . GLU B  1 934  ? 31.263  42.528  104.093 1.00 52.84 ? 932  GLU B CA    1 
ATOM   15525 C C     . GLU B  1 934  ? 30.407  43.642  103.505 1.00 55.39 ? 932  GLU B C     1 
ATOM   15526 O O     . GLU B  1 934  ? 29.443  44.095  104.129 1.00 60.64 ? 932  GLU B O     1 
ATOM   15527 C CB    . GLU B  1 934  ? 32.689  43.021  104.364 1.00 55.50 ? 932  GLU B CB    1 
ATOM   15528 N N     . LYS B  1 935  ? 30.734  44.079  102.292 1.00 57.90 ? 933  LYS B N     1 
ATOM   15529 C CA    . LYS B  1 935  ? 29.985  45.117  101.602 1.00 58.61 ? 933  LYS B CA    1 
ATOM   15530 C C     . LYS B  1 935  ? 29.571  44.617  100.226 1.00 55.08 ? 933  LYS B C     1 
ATOM   15531 O O     . LYS B  1 935  ? 30.240  43.770  99.630  1.00 56.86 ? 933  LYS B O     1 
ATOM   15532 C CB    . LYS B  1 935  ? 30.811  46.410  101.465 1.00 61.66 ? 933  LYS B CB    1 
ATOM   15533 N N     . LEU B  1 936  ? 28.455  45.149  99.724  1.00 56.70 ? 934  LEU B N     1 
ATOM   15534 C CA    . LEU B  1 936  ? 28.025  44.808  98.373  1.00 54.73 ? 934  LEU B CA    1 
ATOM   15535 C C     . LEU B  1 936  ? 29.061  45.214  97.335  1.00 59.35 ? 934  LEU B C     1 
ATOM   15536 O O     . LEU B  1 936  ? 29.053  44.681  96.219  1.00 54.24 ? 934  LEU B O     1 
ATOM   15537 C CB    . LEU B  1 936  ? 26.676  45.465  98.063  1.00 53.73 ? 934  LEU B CB    1 
ATOM   15538 N N     . SER B  1 937  ? 29.960  46.137  97.684  1.00 59.16 ? 935  SER B N     1 
ATOM   15539 C CA    . SER B  1 937  ? 31.040  46.548  96.800  1.00 61.34 ? 935  SER B CA    1 
ATOM   15540 C C     . SER B  1 937  ? 32.175  45.533  96.741  1.00 55.37 ? 935  SER B C     1 
ATOM   15541 O O     . SER B  1 937  ? 33.078  45.695  95.915  1.00 59.15 ? 935  SER B O     1 
ATOM   15542 C CB    . SER B  1 937  ? 31.586  47.913  97.237  1.00 58.49 ? 935  SER B CB    1 
ATOM   15543 N N     . ASP B  1 938  ? 32.155  44.500  97.592  1.00 55.60 ? 936  ASP B N     1 
ATOM   15544 C CA    . ASP B  1 938  ? 33.117  43.406  97.475  1.00 55.48 ? 936  ASP B CA    1 
ATOM   15545 C C     . ASP B  1 938  ? 32.926  42.611  96.188  1.00 54.32 ? 936  ASP B C     1 
ATOM   15546 O O     . ASP B  1 938  ? 33.851  41.917  95.755  1.00 53.93 ? 936  ASP B O     1 
ATOM   15547 C CB    . ASP B  1 938  ? 33.003  42.452  98.668  1.00 53.14 ? 936  ASP B CB    1 
ATOM   15548 C CG    . ASP B  1 938  ? 33.256  43.137  100.000 1.00 62.15 ? 936  ASP B CG    1 
ATOM   15549 O OD1   . ASP B  1 938  ? 33.575  44.347  100.007 1.00 61.53 ? 936  ASP B OD1   1 
ATOM   15550 O OD2   . ASP B  1 938  ? 33.133  42.455  101.044 1.00 62.82 ? 936  ASP B OD2   1 
ATOM   15551 N N     . LEU B  1 939  ? 31.748  42.690  95.581  1.00 52.89 ? 937  LEU B N     1 
ATOM   15552 C CA    . LEU B  1 939  ? 31.424  41.954  94.368  1.00 49.58 ? 937  LEU B CA    1 
ATOM   15553 C C     . LEU B  1 939  ? 31.668  42.882  93.189  1.00 50.15 ? 937  LEU B C     1 
ATOM   15554 O O     . LEU B  1 939  ? 30.899  43.818  92.959  1.00 52.57 ? 937  LEU B O     1 
ATOM   15555 C CB    . LEU B  1 939  ? 29.976  41.474  94.413  1.00 43.20 ? 937  LEU B CB    1 
ATOM   15556 C CG    . LEU B  1 939  ? 29.512  40.443  93.393  1.00 45.22 ? 937  LEU B CG    1 
ATOM   15557 C CD1   . LEU B  1 939  ? 30.419  39.215  93.411  1.00 44.63 ? 937  LEU B CD1   1 
ATOM   15558 C CD2   . LEU B  1 939  ? 28.079  40.064  93.719  1.00 37.31 ? 937  LEU B CD2   1 
ATOM   15559 N N     . GLN B  1 940  ? 32.739  42.625  92.442  1.00 53.98 ? 938  GLN B N     1 
ATOM   15560 C CA    . GLN B  1 940  ? 33.174  43.527  91.386  1.00 52.58 ? 938  GLN B CA    1 
ATOM   15561 C C     . GLN B  1 940  ? 32.869  43.009  89.986  1.00 56.01 ? 938  GLN B C     1 
ATOM   15562 O O     . GLN B  1 940  ? 33.286  43.639  89.008  1.00 59.84 ? 938  GLN B O     1 
ATOM   15563 C CB    . GLN B  1 940  ? 34.672  43.814  91.525  1.00 53.38 ? 938  GLN B CB    1 
ATOM   15564 N N     . ARG B  1 941  ? 32.151  41.892  89.854  1.00 49.74 ? 939  ARG B N     1 
ATOM   15565 C CA    . ARG B  1 941  ? 31.799  41.397  88.527  1.00 50.58 ? 939  ARG B CA    1 
ATOM   15566 C C     . ARG B  1 941  ? 30.671  40.377  88.628  1.00 43.73 ? 939  ARG B C     1 
ATOM   15567 O O     . ARG B  1 941  ? 30.413  39.804  89.689  1.00 43.04 ? 939  ARG B O     1 
ATOM   15568 C CB    . ARG B  1 941  ? 33.012  40.783  87.811  1.00 48.96 ? 939  ARG B CB    1 
ATOM   15569 C CG    . ARG B  1 941  ? 33.609  39.546  88.471  1.00 49.88 ? 939  ARG B CG    1 
ATOM   15570 C CD    . ARG B  1 941  ? 34.780  39.013  87.643  1.00 50.35 ? 939  ARG B CD    1 
ATOM   15571 N NE    . ARG B  1 941  ? 35.293  37.727  88.108  1.00 50.13 ? 939  ARG B NE    1 
ATOM   15572 C CZ    . ARG B  1 941  ? 34.948  36.549  87.603  1.00 47.86 ? 939  ARG B CZ    1 
ATOM   15573 N NH1   . ARG B  1 941  ? 34.038  36.443  86.649  1.00 48.56 ? 939  ARG B NH1   1 
ATOM   15574 N NH2   . ARG B  1 941  ? 35.537  35.448  88.064  1.00 41.87 ? 939  ARG B NH2   1 
ATOM   15575 N N     . GLU B  1 942  ? 29.998  40.166  87.500  1.00 43.76 ? 940  GLU B N     1 
ATOM   15576 C CA    . GLU B  1 942  ? 28.967  39.143  87.421  1.00 42.79 ? 940  GLU B CA    1 
ATOM   15577 C C     . GLU B  1 942  ? 29.621  37.767  87.412  1.00 38.52 ? 940  GLU B C     1 
ATOM   15578 O O     . GLU B  1 942  ? 30.515  37.497  86.606  1.00 42.24 ? 940  GLU B O     1 
ATOM   15579 C CB    . GLU B  1 942  ? 28.115  39.345  86.164  1.00 46.59 ? 940  GLU B CB    1 
ATOM   15580 C CG    . GLU B  1 942  ? 26.810  38.535  86.119  1.00 45.16 ? 940  GLU B CG    1 
ATOM   15581 C CD    . GLU B  1 942  ? 26.135  38.600  84.754  1.00 52.04 ? 940  GLU B CD    1 
ATOM   15582 O OE1   . GLU B  1 942  ? 26.833  38.904  83.763  1.00 54.95 ? 940  GLU B OE1   1 
ATOM   15583 O OE2   . GLU B  1 942  ? 24.908  38.356  84.665  1.00 48.24 ? 940  GLU B OE2   1 
ATOM   15584 N N     . VAL B  1 943  ? 29.190  36.901  88.320  1.00 35.67 ? 941  VAL B N     1 
ATOM   15585 C CA    . VAL B  1 943  ? 29.668  35.526  88.389  1.00 34.84 ? 941  VAL B CA    1 
ATOM   15586 C C     . VAL B  1 943  ? 28.499  34.629  88.007  1.00 31.16 ? 941  VAL B C     1 
ATOM   15587 O O     . VAL B  1 943  ? 27.534  34.477  88.769  1.00 28.22 ? 941  VAL B O     1 
ATOM   15588 C CB    . VAL B  1 943  ? 30.229  35.184  89.772  1.00 35.91 ? 941  VAL B CB    1 
ATOM   15589 C CG1   . VAL B  1 943  ? 30.836  33.797  89.767  1.00 31.24 ? 941  VAL B CG1   1 
ATOM   15590 C CG2   . VAL B  1 943  ? 31.274  36.219  90.160  1.00 36.76 ? 941  VAL B CG2   1 
ATOM   15591 N N     . PHE B  1 944  ? 28.588  34.041  86.818  1.00 27.49 ? 942  PHE B N     1 
ATOM   15592 C CA    . PHE B  1 944  ? 27.451  33.390  86.173  1.00 27.50 ? 942  PHE B CA    1 
ATOM   15593 C C     . PHE B  1 944  ? 27.421  31.903  86.532  1.00 27.87 ? 942  PHE B C     1 
ATOM   15594 O O     . PHE B  1 944  ? 27.620  31.010  85.705  1.00 28.79 ? 942  PHE B O     1 
ATOM   15595 C CB    . PHE B  1 944  ? 27.524  33.603  84.672  1.00 27.05 ? 942  PHE B CB    1 
ATOM   15596 C CG    . PHE B  1 944  ? 26.189  33.675  84.022  1.00 28.73 ? 942  PHE B CG    1 
ATOM   15597 C CD1   . PHE B  1 944  ? 25.395  34.811  84.162  1.00 30.80 ? 942  PHE B CD1   1 
ATOM   15598 C CD2   . PHE B  1 944  ? 25.721  32.618  83.270  1.00 28.01 ? 942  PHE B CD2   1 
ATOM   15599 C CE1   . PHE B  1 944  ? 24.155  34.882  83.559  1.00 28.15 ? 942  PHE B CE1   1 
ATOM   15600 C CE2   . PHE B  1 944  ? 24.480  32.683  82.665  1.00 25.99 ? 942  PHE B CE2   1 
ATOM   15601 C CZ    . PHE B  1 944  ? 23.697  33.823  82.805  1.00 27.29 ? 942  PHE B CZ    1 
ATOM   15602 N N     . GLY B  1 945  ? 27.167  31.647  87.807  1.00 24.00 ? 943  GLY B N     1 
ATOM   15603 C CA    . GLY B  1 945  ? 27.224  30.304  88.326  1.00 25.41 ? 943  GLY B CA    1 
ATOM   15604 C C     . GLY B  1 945  ? 26.451  30.186  89.622  1.00 22.36 ? 943  GLY B C     1 
ATOM   15605 O O     . GLY B  1 945  ? 25.818  31.136  90.083  1.00 22.07 ? 943  GLY B O     1 
ATOM   15606 N N     . PRO B  1 946  ? 26.491  29.022  90.235  1.00 19.59 ? 944  PRO B N     1 
ATOM   15607 C CA    . PRO B  1 946  ? 25.649  28.793  91.419  1.00 19.97 ? 944  PRO B CA    1 
ATOM   15608 C C     . PRO B  1 946  ? 26.291  29.364  92.675  1.00 22.24 ? 944  PRO B C     1 
ATOM   15609 O O     . PRO B  1 946  ? 26.626  28.633  93.597  1.00 24.52 ? 944  PRO B O     1 
ATOM   15610 C CB    . PRO B  1 946  ? 25.543  27.264  91.453  1.00 17.83 ? 944  PRO B CB    1 
ATOM   15611 C CG    . PRO B  1 946  ? 26.851  26.799  90.849  1.00 24.88 ? 944  PRO B CG    1 
ATOM   15612 C CD    . PRO B  1 946  ? 27.191  27.810  89.782  1.00 20.72 ? 944  PRO B CD    1 
ATOM   15613 N N     . VAL B  1 947  ? 26.467  30.686  92.699  1.00 20.58 ? 945  VAL B N     1 
ATOM   15614 C CA    . VAL B  1 947  ? 27.222  31.358  93.759  1.00 22.84 ? 945  VAL B CA    1 
ATOM   15615 C C     . VAL B  1 947  ? 26.368  32.481  94.335  1.00 25.12 ? 945  VAL B C     1 
ATOM   15616 O O     . VAL B  1 947  ? 26.178  33.525  93.691  1.00 25.59 ? 945  VAL B O     1 
ATOM   15617 C CB    . VAL B  1 947  ? 28.571  31.894  93.259  1.00 22.58 ? 945  VAL B CB    1 
ATOM   15618 C CG1   . VAL B  1 947  ? 29.403  32.429  94.433  1.00 24.66 ? 945  VAL B CG1   1 
ATOM   15619 C CG2   . VAL B  1 947  ? 29.348  30.787  92.548  1.00 23.81 ? 945  VAL B CG2   1 
ATOM   15620 N N     . LEU B  1 948  ? 25.858  32.273  95.541  1.00 23.58 ? 946  LEU B N     1 
ATOM   15621 C CA    . LEU B  1 948  ? 25.049  33.262  96.229  1.00 22.58 ? 946  LEU B CA    1 
ATOM   15622 C C     . LEU B  1 948  ? 25.917  34.047  97.195  1.00 25.45 ? 946  LEU B C     1 
ATOM   15623 O O     . LEU B  1 948  ? 26.609  33.459  98.030  1.00 25.98 ? 946  LEU B O     1 
ATOM   15624 C CB    . LEU B  1 948  ? 23.907  32.598  96.997  1.00 22.73 ? 946  LEU B CB    1 
ATOM   15625 C CG    . LEU B  1 948  ? 23.005  33.564  97.781  1.00 23.69 ? 946  LEU B CG    1 
ATOM   15626 C CD1   . LEU B  1 948  ? 22.210  34.472  96.838  1.00 20.06 ? 946  LEU B CD1   1 
ATOM   15627 C CD2   . LEU B  1 948  ? 22.066  32.776  98.684  1.00 23.41 ? 946  LEU B CD2   1 
ATOM   15628 N N     . HIS B  1 949  ? 25.877  35.364  97.077  1.00 24.73 ? 947  HIS B N     1 
ATOM   15629 C CA    . HIS B  1 949  ? 26.530  36.258  98.023  1.00 28.26 ? 947  HIS B CA    1 
ATOM   15630 C C     . HIS B  1 949  ? 25.495  36.778  99.013  1.00 27.39 ? 947  HIS B C     1 
ATOM   15631 O O     . HIS B  1 949  ? 24.356  37.063  98.641  1.00 25.69 ? 947  HIS B O     1 
ATOM   15632 C CB    . HIS B  1 949  ? 27.210  37.409  97.285  1.00 25.33 ? 947  HIS B CB    1 
ATOM   15633 C CG    . HIS B  1 949  ? 28.153  36.950  96.218  1.00 31.01 ? 947  HIS B CG    1 
ATOM   15634 N ND1   . HIS B  1 949  ? 27.736  36.660  94.936  1.00 26.71 ? 947  HIS B ND1   1 
ATOM   15635 C CD2   . HIS B  1 949  ? 29.483  36.694  96.248  1.00 32.09 ? 947  HIS B CD2   1 
ATOM   15636 C CE1   . HIS B  1 949  ? 28.769  36.257  94.218  1.00 29.33 ? 947  HIS B CE1   1 
ATOM   15637 N NE2   . HIS B  1 949  ? 29.841  36.264  94.991  1.00 33.20 ? 947  HIS B NE2   1 
ATOM   15638 N N     . VAL B  1 950  ? 25.878  36.871  100.285 1.00 27.22 ? 948  VAL B N     1 
ATOM   15639 C CA    . VAL B  1 950  ? 24.960  37.300  101.335 1.00 26.20 ? 948  VAL B CA    1 
ATOM   15640 C C     . VAL B  1 950  ? 25.558  38.504  102.048 1.00 29.52 ? 948  VAL B C     1 
ATOM   15641 O O     . VAL B  1 950  ? 26.726  38.471  102.461 1.00 31.11 ? 948  VAL B O     1 
ATOM   15642 C CB    . VAL B  1 950  ? 24.659  36.167  102.337 1.00 29.33 ? 948  VAL B CB    1 
ATOM   15643 C CG1   . VAL B  1 950  ? 23.620  36.635  103.359 1.00 26.96 ? 948  VAL B CG1   1 
ATOM   15644 C CG2   . VAL B  1 950  ? 24.160  34.933  101.614 1.00 25.31 ? 948  VAL B CG2   1 
ATOM   15645 N N     . ILE B  1 951  ? 24.767  39.565  102.181 1.00 25.97 ? 949  ILE B N     1 
ATOM   15646 C CA    . ILE B  1 951  ? 25.142  40.711  103.002 1.00 26.58 ? 949  ILE B CA    1 
ATOM   15647 C C     . ILE B  1 951  ? 24.026  40.979  103.999 1.00 27.04 ? 949  ILE B C     1 
ATOM   15648 O O     . ILE B  1 951  ? 22.861  40.650  103.763 1.00 24.76 ? 949  ILE B O     1 
ATOM   15649 C CB    . ILE B  1 951  ? 25.430  41.973  102.172 1.00 31.28 ? 949  ILE B CB    1 
ATOM   15650 C CG1   . ILE B  1 951  ? 24.246  42.296  101.272 1.00 32.62 ? 949  ILE B CG1   1 
ATOM   15651 C CG2   . ILE B  1 951  ? 26.711  41.819  101.366 1.00 41.71 ? 949  ILE B CG2   1 
ATOM   15652 C CD1   . ILE B  1 951  ? 24.518  43.442  100.318 1.00 38.93 ? 949  ILE B CD1   1 
ATOM   15653 N N     . ARG B  1 952  ? 24.393  41.586  105.123 1.00 24.46 ? 950  ARG B N     1 
ATOM   15654 C CA    . ARG B  1 952  ? 23.469  41.885  106.204 1.00 23.82 ? 950  ARG B CA    1 
ATOM   15655 C C     . ARG B  1 952  ? 23.327  43.392  106.307 1.00 24.61 ? 950  ARG B C     1 
ATOM   15656 O O     . ARG B  1 952  ? 24.280  44.136  106.058 1.00 26.81 ? 950  ARG B O     1 
ATOM   15657 C CB    . ARG B  1 952  ? 23.968  41.308  107.536 1.00 30.86 ? 950  ARG B CB    1 
ATOM   15658 C CG    . ARG B  1 952  ? 24.384  39.854  107.437 1.00 32.67 ? 950  ARG B CG    1 
ATOM   15659 C CD    . ARG B  1 952  ? 25.464  39.520  108.443 1.00 38.28 ? 950  ARG B CD    1 
ATOM   15660 N NE    . ARG B  1 952  ? 24.897  39.171  109.737 1.00 43.83 ? 950  ARG B NE    1 
ATOM   15661 C CZ    . ARG B  1 952  ? 24.774  37.929  110.185 1.00 40.17 ? 950  ARG B CZ    1 
ATOM   15662 N NH1   . ARG B  1 952  ? 25.192  36.893  109.473 1.00 38.45 ? 950  ARG B NH1   1 
ATOM   15663 N NH2   . ARG B  1 952  ? 24.221  37.723  111.378 1.00 39.85 ? 950  ARG B NH2   1 
ATOM   15664 N N     . TYR B  1 953  ? 22.124  43.850  106.638 1.00 24.74 ? 951  TYR B N     1 
ATOM   15665 C CA    . TYR B  1 953  ? 21.902  45.281  106.718 1.00 23.82 ? 951  TYR B CA    1 
ATOM   15666 C C     . TYR B  1 953  ? 21.073  45.599  107.951 1.00 26.35 ? 951  TYR B C     1 
ATOM   15667 O O     . TYR B  1 953  ? 20.285  44.773  108.424 1.00 22.92 ? 951  TYR B O     1 
ATOM   15668 C CB    . TYR B  1 953  ? 21.206  45.810  105.446 1.00 24.39 ? 951  TYR B CB    1 
ATOM   15669 C CG    . TYR B  1 953  ? 19.757  45.399  105.333 1.00 25.31 ? 951  TYR B CG    1 
ATOM   15670 C CD1   . TYR B  1 953  ? 19.400  44.154  104.821 1.00 25.70 ? 951  TYR B CD1   1 
ATOM   15671 C CD2   . TYR B  1 953  ? 18.746  46.260  105.720 1.00 21.18 ? 951  TYR B CD2   1 
ATOM   15672 C CE1   . TYR B  1 953  ? 18.073  43.783  104.715 1.00 22.01 ? 951  TYR B CE1   1 
ATOM   15673 C CE2   . TYR B  1 953  ? 17.419  45.891  105.631 1.00 24.81 ? 951  TYR B CE2   1 
ATOM   15674 C CZ    . TYR B  1 953  ? 17.087  44.650  105.117 1.00 23.50 ? 951  TYR B CZ    1 
ATOM   15675 O OH    . TYR B  1 953  ? 15.754  44.290  105.016 1.00 24.17 ? 951  TYR B OH    1 
ATOM   15676 N N     . ARG B  1 954  ? 21.278  46.806  108.476 1.00 27.50 ? 952  ARG B N     1 
ATOM   15677 C CA    . ARG B  1 954  ? 20.439  47.326  109.544 1.00 28.59 ? 952  ARG B CA    1 
ATOM   15678 C C     . ARG B  1 954  ? 19.198  47.979  108.950 1.00 28.36 ? 952  ARG B C     1 
ATOM   15679 O O     . ARG B  1 954  ? 19.271  48.659  107.921 1.00 29.53 ? 952  ARG B O     1 
ATOM   15680 C CB    . ARG B  1 954  ? 21.220  48.334  110.396 1.00 32.49 ? 952  ARG B CB    1 
ATOM   15681 N N     . ARG B  1 955  ? 18.052  47.764  109.607 1.00 34.35 ? 953  ARG B N     1 
ATOM   15682 C CA    . ARG B  1 955  ? 16.774  48.236  109.077 1.00 35.43 ? 953  ARG B CA    1 
ATOM   15683 C C     . ARG B  1 955  ? 16.814  49.723  108.737 1.00 35.61 ? 953  ARG B C     1 
ATOM   15684 O O     . ARG B  1 955  ? 16.235  50.157  107.735 1.00 37.45 ? 953  ARG B O     1 
ATOM   15685 C CB    . ARG B  1 955  ? 15.662  47.942  110.087 1.00 40.31 ? 953  ARG B CB    1 
ATOM   15686 C CG    . ARG B  1 955  ? 14.398  48.771  109.912 1.00 44.78 ? 953  ARG B CG    1 
ATOM   15687 C CD    . ARG B  1 955  ? 13.500  48.201  108.835 1.00 49.20 ? 953  ARG B CD    1 
ATOM   15688 N NE    . ARG B  1 955  ? 12.237  48.920  108.716 1.00 51.41 ? 953  ARG B NE    1 
ATOM   15689 C CZ    . ARG B  1 955  ? 11.940  49.750  107.724 1.00 54.97 ? 953  ARG B CZ    1 
ATOM   15690 N NH1   . ARG B  1 955  ? 12.809  50.015  106.760 1.00 50.74 ? 953  ARG B NH1   1 
ATOM   15691 N NH2   . ARG B  1 955  ? 10.740  50.323  107.693 1.00 57.98 ? 953  ARG B NH2   1 
ATOM   15692 N N     . ASP B  1 956  ? 17.497  50.522  109.557 1.00 29.77 ? 954  ASP B N     1 
ATOM   15693 C CA    . ASP B  1 956  ? 17.610  51.951  109.281 1.00 34.43 ? 954  ASP B CA    1 
ATOM   15694 C C     . ASP B  1 956  ? 18.455  52.259  108.054 1.00 31.48 ? 954  ASP B C     1 
ATOM   15695 O O     . ASP B  1 956  ? 18.452  53.408  107.600 1.00 37.19 ? 954  ASP B O     1 
ATOM   15696 C CB    . ASP B  1 956  ? 18.204  52.679  110.490 1.00 36.68 ? 954  ASP B CB    1 
ATOM   15697 C CG    . ASP B  1 956  ? 17.293  52.647  111.688 1.00 40.16 ? 954  ASP B CG    1 
ATOM   15698 O OD1   . ASP B  1 956  ? 16.065  52.532  111.483 1.00 43.45 ? 954  ASP B OD1   1 
ATOM   15699 O OD2   . ASP B  1 956  ? 17.805  52.740  112.829 1.00 48.36 ? 954  ASP B OD2   1 
ATOM   15700 N N     . ASP B  1 957  ? 19.194  51.285  107.533 1.00 27.28 ? 955  ASP B N     1 
ATOM   15701 C CA    . ASP B  1 957  ? 20.029  51.484  106.356 1.00 31.39 ? 955  ASP B CA    1 
ATOM   15702 C C     . ASP B  1 957  ? 19.354  50.999  105.082 1.00 27.27 ? 955  ASP B C     1 
ATOM   15703 O O     . ASP B  1 957  ? 20.026  50.878  104.057 1.00 27.93 ? 955  ASP B O     1 
ATOM   15704 C CB    . ASP B  1 957  ? 21.374  50.764  106.511 1.00 29.83 ? 955  ASP B CB    1 
ATOM   15705 C CG    . ASP B  1 957  ? 22.340  51.488  107.437 1.00 38.52 ? 955  ASP B CG    1 
ATOM   15706 O OD1   . ASP B  1 957  ? 22.199  52.715  107.637 1.00 42.90 ? 955  ASP B OD1   1 
ATOM   15707 O OD2   . ASP B  1 957  ? 23.257  50.818  107.957 1.00 38.19 ? 955  ASP B OD2   1 
ATOM   15708 N N     . LEU B  1 958  ? 18.053  50.693  105.138 1.00 25.74 ? 956  LEU B N     1 
ATOM   15709 C CA    . LEU B  1 958  ? 17.359  50.138  103.977 1.00 23.19 ? 956  LEU B CA    1 
ATOM   15710 C C     . LEU B  1 958  ? 17.474  51.055  102.767 1.00 25.26 ? 956  LEU B C     1 
ATOM   15711 O O     . LEU B  1 958  ? 17.781  50.606  101.656 1.00 24.73 ? 956  LEU B O     1 
ATOM   15712 C CB    . LEU B  1 958  ? 15.891  49.894  104.315 1.00 29.61 ? 956  LEU B CB    1 
ATOM   15713 C CG    . LEU B  1 958  ? 15.089  49.246  103.186 1.00 24.05 ? 956  LEU B CG    1 
ATOM   15714 C CD1   . LEU B  1 958  ? 15.794  47.981  102.763 1.00 22.61 ? 956  LEU B CD1   1 
ATOM   15715 C CD2   . LEU B  1 958  ? 13.675  48.952  103.664 1.00 29.74 ? 956  LEU B CD2   1 
ATOM   15716 N N     . ASP B  1 959  ? 17.232  52.350  102.957 1.00 27.84 ? 957  ASP B N     1 
ATOM   15717 C CA    . ASP B  1 959  ? 17.237  53.234  101.799 1.00 26.32 ? 957  ASP B CA    1 
ATOM   15718 C C     . ASP B  1 959  ? 18.626  53.309  101.182 1.00 24.40 ? 957  ASP B C     1 
ATOM   15719 O O     . ASP B  1 959  ? 18.761  53.329  99.956  1.00 25.66 ? 957  ASP B O     1 
ATOM   15720 C CB    . ASP B  1 959  ? 16.738  54.622  102.181 1.00 25.19 ? 957  ASP B CB    1 
ATOM   15721 C CG    . ASP B  1 959  ? 16.341  55.428  100.978 1.00 30.73 ? 957  ASP B CG    1 
ATOM   15722 O OD1   . ASP B  1 959  ? 15.591  54.883  100.130 1.00 27.23 ? 957  ASP B OD1   1 
ATOM   15723 O OD2   . ASP B  1 959  ? 16.771  56.599  100.879 1.00 31.99 ? 957  ASP B OD2   1 
ATOM   15724 N N     . ARG B  1 960  ? 19.671  53.326  102.021 1.00 24.00 ? 958  ARG B N     1 
ATOM   15725 C CA    . ARG B  1 960  ? 21.035  53.299  101.511 1.00 24.74 ? 958  ARG B CA    1 
ATOM   15726 C C     . ARG B  1 960  ? 21.352  51.963  100.846 1.00 25.58 ? 958  ARG B C     1 
ATOM   15727 O O     . ARG B  1 960  ? 22.076  51.919  99.844  1.00 29.32 ? 958  ARG B O     1 
ATOM   15728 C CB    . ARG B  1 960  ? 22.022  53.581  102.646 1.00 21.90 ? 958  ARG B CB    1 
ATOM   15729 N N     . LEU B  1 961  ? 20.817  50.862  101.379 1.00 23.67 ? 959  LEU B N     1 
ATOM   15730 C CA    . LEU B  1 961  ? 21.060  49.568  100.746 1.00 23.04 ? 959  LEU B CA    1 
ATOM   15731 C C     . LEU B  1 961  ? 20.498  49.545  99.326  1.00 26.44 ? 959  LEU B C     1 
ATOM   15732 O O     . LEU B  1 961  ? 21.155  49.059  98.398  1.00 26.59 ? 959  LEU B O     1 
ATOM   15733 C CB    . LEU B  1 961  ? 20.460  48.444  101.596 1.00 24.45 ? 959  LEU B CB    1 
ATOM   15734 C CG    . LEU B  1 961  ? 20.467  47.026  100.995 1.00 24.92 ? 959  LEU B CG    1 
ATOM   15735 C CD1   . LEU B  1 961  ? 21.887  46.482  100.869 1.00 29.68 ? 959  LEU B CD1   1 
ATOM   15736 C CD2   . LEU B  1 961  ? 19.581  46.059  101.793 1.00 24.31 ? 959  LEU B CD2   1 
ATOM   15737 N N     . VAL B  1 962  ? 19.300  50.094  99.137  1.00 23.56 ? 960  VAL B N     1 
ATOM   15738 C CA    . VAL B  1 962  ? 18.728  50.217  97.799  1.00 24.09 ? 960  VAL B CA    1 
ATOM   15739 C C     . VAL B  1 962  ? 19.666  50.994  96.877  1.00 25.68 ? 960  VAL B C     1 
ATOM   15740 O O     . VAL B  1 962  ? 19.884  50.606  95.724  1.00 25.18 ? 960  VAL B O     1 
ATOM   15741 C CB    . VAL B  1 962  ? 17.340  50.870  97.881  1.00 26.02 ? 960  VAL B CB    1 
ATOM   15742 C CG1   . VAL B  1 962  ? 16.849  51.217  96.493  1.00 25.61 ? 960  VAL B CG1   1 
ATOM   15743 C CG2   . VAL B  1 962  ? 16.356  49.944  98.603  1.00 24.83 ? 960  VAL B CG2   1 
ATOM   15744 N N     . ASP B  1 963  ? 20.226  52.111  97.364  1.00 28.46 ? 961  ASP B N     1 
ATOM   15745 C CA    . ASP B  1 963  ? 21.246  52.839  96.605  1.00 31.72 ? 961  ASP B CA    1 
ATOM   15746 C C     . ASP B  1 963  ? 22.384  51.927  96.175  1.00 27.20 ? 961  ASP B C     1 
ATOM   15747 O O     . ASP B  1 963  ? 22.842  51.981  95.028  1.00 28.88 ? 961  ASP B O     1 
ATOM   15748 C CB    . ASP B  1 963  ? 21.828  53.986  97.432  1.00 31.01 ? 961  ASP B CB    1 
ATOM   15749 C CG    . ASP B  1 963  ? 20.916  55.166  97.503  1.00 35.81 ? 961  ASP B CG    1 
ATOM   15750 O OD1   . ASP B  1 963  ? 20.039  55.273  96.624  1.00 34.37 ? 961  ASP B OD1   1 
ATOM   15751 O OD2   . ASP B  1 963  ? 21.094  55.995  98.428  1.00 35.96 ? 961  ASP B OD2   1 
ATOM   15752 N N     . ASP B  1 964  ? 22.878  51.105  97.100  1.00 25.63 ? 962  ASP B N     1 
ATOM   15753 C CA    . ASP B  1 964  ? 23.994  50.225  96.783  1.00 30.07 ? 962  ASP B CA    1 
ATOM   15754 C C     . ASP B  1 964  ? 23.616  49.235  95.694  1.00 27.44 ? 962  ASP B C     1 
ATOM   15755 O O     . ASP B  1 964  ? 24.437  48.904  94.831  1.00 28.26 ? 962  ASP B O     1 
ATOM   15756 C CB    . ASP B  1 964  ? 24.449  49.482  98.035  1.00 30.59 ? 962  ASP B CB    1 
ATOM   15757 C CG    . ASP B  1 964  ? 25.105  50.387  99.035  1.00 34.39 ? 962  ASP B CG    1 
ATOM   15758 O OD1   . ASP B  1 964  ? 25.294  51.584  98.717  1.00 36.59 ? 962  ASP B OD1   1 
ATOM   15759 O OD2   . ASP B  1 964  ? 25.428  49.900  100.142 1.00 39.47 ? 962  ASP B OD2   1 
ATOM   15760 N N     . VAL B  1 965  ? 22.383  48.734  95.733  1.00 26.58 ? 963  VAL B N     1 
ATOM   15761 C CA    . VAL B  1 965  ? 21.923  47.813  94.694  1.00 23.92 ? 963  VAL B CA    1 
ATOM   15762 C C     . VAL B  1 965  ? 21.851  48.528  93.353  1.00 26.77 ? 963  VAL B C     1 
ATOM   15763 O O     . VAL B  1 965  ? 22.321  48.019  92.330  1.00 29.02 ? 963  VAL B O     1 
ATOM   15764 C CB    . VAL B  1 965  ? 20.566  47.203  95.094  1.00 28.18 ? 963  VAL B CB    1 
ATOM   15765 C CG1   . VAL B  1 965  ? 19.952  46.401  93.938  1.00 25.86 ? 963  VAL B CG1   1 
ATOM   15766 C CG2   . VAL B  1 965  ? 20.736  46.330  96.326  1.00 24.71 ? 963  VAL B CG2   1 
ATOM   15767 N N     . ASN B  1 966  ? 21.279  49.731  93.344  1.00 26.18 ? 964  ASN B N     1 
ATOM   15768 C CA    . ASN B  1 966  ? 21.173  50.511  92.118  1.00 27.04 ? 964  ASN B CA    1 
ATOM   15769 C C     . ASN B  1 966  ? 22.535  50.924  91.571  1.00 28.51 ? 964  ASN B C     1 
ATOM   15770 O O     . ASN B  1 966  ? 22.656  51.179  90.370  1.00 30.47 ? 964  ASN B O     1 
ATOM   15771 C CB    . ASN B  1 966  ? 20.342  51.774  92.363  1.00 27.48 ? 964  ASN B CB    1 
ATOM   15772 C CG    . ASN B  1 966  ? 18.848  51.491  92.566  1.00 29.13 ? 964  ASN B CG    1 
ATOM   15773 O OD1   . ASN B  1 966  ? 18.314  50.459  92.133  1.00 26.70 ? 964  ASN B OD1   1 
ATOM   15774 N ND2   . ASN B  1 966  ? 18.165  52.440  93.190  1.00 22.06 ? 964  ASN B ND2   1 
ATOM   15775 N N     . ALA B  1 967  ? 23.556  51.017  92.429  1.00 27.75 ? 965  ALA B N     1 
ATOM   15776 C CA    . ALA B  1 967  ? 24.833  51.588  92.027  1.00 28.41 ? 965  ALA B CA    1 
ATOM   15777 C C     . ALA B  1 967  ? 25.657  50.678  91.124  1.00 33.49 ? 965  ALA B C     1 
ATOM   15778 O O     . ALA B  1 967  ? 26.640  51.154  90.546  1.00 37.17 ? 965  ALA B O     1 
ATOM   15779 C CB    . ALA B  1 967  ? 25.655  51.958  93.267  1.00 23.08 ? 965  ALA B CB    1 
ATOM   15780 N N     . THR B  1 968  ? 25.312  49.393  90.998  1.00 27.77 ? 966  THR B N     1 
ATOM   15781 C CA    . THR B  1 968  ? 26.007  48.544  90.037  1.00 32.47 ? 966  THR B CA    1 
ATOM   15782 C C     . THR B  1 968  ? 25.741  48.966  88.592  1.00 35.37 ? 966  THR B C     1 
ATOM   15783 O O     . THR B  1 968  ? 26.501  48.582  87.695  1.00 37.43 ? 966  THR B O     1 
ATOM   15784 C CB    . THR B  1 968  ? 25.601  47.075  90.203  1.00 33.19 ? 966  THR B CB    1 
ATOM   15785 O OG1   . THR B  1 968  ? 24.338  46.854  89.563  1.00 34.53 ? 966  THR B OG1   1 
ATOM   15786 C CG2   . THR B  1 968  ? 25.484  46.704  91.671  1.00 32.43 ? 966  THR B CG2   1 
ATOM   15787 N N     . GLY B  1 969  ? 24.681  49.736  88.342  1.00 35.64 ? 967  GLY B N     1 
ATOM   15788 C CA    . GLY B  1 969  ? 24.295  50.082  86.991  1.00 32.47 ? 967  GLY B CA    1 
ATOM   15789 C C     . GLY B  1 969  ? 23.466  49.038  86.271  1.00 34.89 ? 967  GLY B C     1 
ATOM   15790 O O     . GLY B  1 969  ? 22.921  49.335  85.201  1.00 32.58 ? 967  GLY B O     1 
ATOM   15791 N N     . TYR B  1 970  ? 23.365  47.824  86.806  1.00 31.04 ? 968  TYR B N     1 
ATOM   15792 C CA    . TYR B  1 970  ? 22.423  46.843  86.287  1.00 31.98 ? 968  TYR B CA    1 
ATOM   15793 C C     . TYR B  1 970  ? 21.025  47.120  86.831  1.00 32.98 ? 968  TYR B C     1 
ATOM   15794 O O     . TYR B  1 970  ? 20.846  47.845  87.814  1.00 33.17 ? 968  TYR B O     1 
ATOM   15795 C CB    . TYR B  1 970  ? 22.842  45.424  86.674  1.00 33.64 ? 968  TYR B CB    1 
ATOM   15796 C CG    . TYR B  1 970  ? 24.105  44.927  86.011  1.00 34.12 ? 968  TYR B CG    1 
ATOM   15797 C CD1   . TYR B  1 970  ? 24.078  44.431  84.712  1.00 35.89 ? 968  TYR B CD1   1 
ATOM   15798 C CD2   . TYR B  1 970  ? 25.316  44.925  86.693  1.00 36.74 ? 968  TYR B CD2   1 
ATOM   15799 C CE1   . TYR B  1 970  ? 25.233  43.964  84.099  1.00 39.68 ? 968  TYR B CE1   1 
ATOM   15800 C CE2   . TYR B  1 970  ? 26.473  44.457  86.091  1.00 41.81 ? 968  TYR B CE2   1 
ATOM   15801 C CZ    . TYR B  1 970  ? 26.424  43.979  84.796  1.00 42.23 ? 968  TYR B CZ    1 
ATOM   15802 O OH    . TYR B  1 970  ? 27.575  43.516  84.201  1.00 56.61 ? 968  TYR B OH    1 
ATOM   15803 N N     . GLY B  1 971  ? 20.024  46.536  86.177  1.00 30.23 ? 969  GLY B N     1 
ATOM   15804 C CA    . GLY B  1 971  ? 18.672  46.641  86.678  1.00 26.86 ? 969  GLY B CA    1 
ATOM   15805 C C     . GLY B  1 971  ? 17.771  45.607  86.042  1.00 23.85 ? 969  GLY B C     1 
ATOM   15806 O O     . GLY B  1 971  ? 16.813  45.955  85.337  1.00 23.29 ? 969  GLY B O     1 
ATOM   15807 N N     . LEU B  1 972  ? 18.069  44.330  86.276  1.00 27.36 ? 970  LEU B N     1 
ATOM   15808 C CA    . LEU B  1 972  ? 17.300  43.266  85.632  1.00 22.91 ? 970  LEU B CA    1 
ATOM   15809 C C     . LEU B  1 972  ? 16.191  42.766  86.557  1.00 25.09 ? 970  LEU B C     1 
ATOM   15810 O O     . LEU B  1 972  ? 15.050  43.244  86.479  1.00 23.81 ? 970  LEU B O     1 
ATOM   15811 C CB    . LEU B  1 972  ? 18.218  42.117  85.198  1.00 26.22 ? 970  LEU B CB    1 
ATOM   15812 C CG    . LEU B  1 972  ? 17.547  41.091  84.274  1.00 27.04 ? 970  LEU B CG    1 
ATOM   15813 C CD1   . LEU B  1 972  ? 16.812  41.802  83.127  1.00 26.04 ? 970  LEU B CD1   1 
ATOM   15814 C CD2   . LEU B  1 972  ? 18.562  40.114  83.714  1.00 28.47 ? 970  LEU B CD2   1 
ATOM   15815 N N     . THR B  1 973  ? 16.493  41.810  87.437  1.00 21.77 ? 971  THR B N     1 
ATOM   15816 C CA    . THR B  1 973  ? 15.501  41.323  88.380  1.00 18.76 ? 971  THR B CA    1 
ATOM   15817 C C     . THR B  1 973  ? 15.833  41.753  89.806  1.00 21.47 ? 971  THR B C     1 
ATOM   15818 O O     . THR B  1 973  ? 16.992  41.998  90.156  1.00 21.95 ? 971  THR B O     1 
ATOM   15819 C CB    . THR B  1 973  ? 15.347  39.800  88.322  1.00 20.72 ? 971  THR B CB    1 
ATOM   15820 O OG1   . THR B  1 973  ? 16.573  39.177  88.706  1.00 21.28 ? 971  THR B OG1   1 
ATOM   15821 C CG2   . THR B  1 973  ? 14.976  39.358  86.916  1.00 22.56 ? 971  THR B CG2   1 
ATOM   15822 N N     . PHE B  1 974  ? 14.781  41.843  90.620  1.00 18.51 ? 972  PHE B N     1 
ATOM   15823 C CA    . PHE B  1 974  ? 14.907  42.269  92.005  1.00 22.25 ? 972  PHE B CA    1 
ATOM   15824 C C     . PHE B  1 974  ? 13.796  41.621  92.814  1.00 18.11 ? 972  PHE B C     1 
ATOM   15825 O O     . PHE B  1 974  ? 12.635  41.623  92.399  1.00 17.15 ? 972  PHE B O     1 
ATOM   15826 C CB    . PHE B  1 974  ? 14.826  43.795  92.151  1.00 16.96 ? 972  PHE B CB    1 
ATOM   15827 C CG    . PHE B  1 974  ? 14.751  44.250  93.591  1.00 19.28 ? 972  PHE B CG    1 
ATOM   15828 C CD1   . PHE B  1 974  ? 15.908  44.328  94.365  1.00 24.40 ? 972  PHE B CD1   1 
ATOM   15829 C CD2   . PHE B  1 974  ? 13.527  44.566  94.174  1.00 20.36 ? 972  PHE B CD2   1 
ATOM   15830 C CE1   . PHE B  1 974  ? 15.853  44.734  95.685  1.00 22.22 ? 972  PHE B CE1   1 
ATOM   15831 C CE2   . PHE B  1 974  ? 13.451  44.958  95.485  1.00 22.43 ? 972  PHE B CE2   1 
ATOM   15832 C CZ    . PHE B  1 974  ? 14.623  45.039  96.261  1.00 19.55 ? 972  PHE B CZ    1 
ATOM   15833 N N     . GLY B  1 975  ? 14.152  41.094  93.982  1.00 15.17 ? 973  GLY B N     1 
ATOM   15834 C CA    . GLY B  1 975  ? 13.199  40.440  94.849  1.00 19.14 ? 973  GLY B CA    1 
ATOM   15835 C C     . GLY B  1 975  ? 13.120  41.144  96.187  1.00 23.21 ? 973  GLY B C     1 
ATOM   15836 O O     . GLY B  1 975  ? 14.105  41.701  96.672  1.00 18.75 ? 973  GLY B O     1 
ATOM   15837 N N     . LEU B  1 976  ? 11.932  41.114  96.779  1.00 19.30 ? 974  LEU B N     1 
ATOM   15838 C CA    . LEU B  1 976  ? 11.715  41.700  98.094  1.00 19.89 ? 974  LEU B CA    1 
ATOM   15839 C C     . LEU B  1 976  ? 10.772  40.800  98.864  1.00 21.44 ? 974  LEU B C     1 
ATOM   15840 O O     . LEU B  1 976  ? 9.666   40.529  98.402  1.00 17.69 ? 974  LEU B O     1 
ATOM   15841 C CB    . LEU B  1 976  ? 11.135  43.112  97.979  1.00 19.09 ? 974  LEU B CB    1 
ATOM   15842 C CG    . LEU B  1 976  ? 10.670  43.765  99.292  1.00 21.80 ? 974  LEU B CG    1 
ATOM   15843 C CD1   . LEU B  1 976  ? 11.853  44.088  100.219 1.00 19.19 ? 974  LEU B CD1   1 
ATOM   15844 C CD2   . LEU B  1 976  ? 9.905   45.013  98.970  1.00 23.32 ? 974  LEU B CD2   1 
ATOM   15845 N N     . HIS B  1 977  ? 11.203  40.331  100.028 1.00 20.51 ? 975  HIS B N     1 
ATOM   15846 C CA    . HIS B  1 977  ? 10.353  39.529  100.896 1.00 19.25 ? 975  HIS B CA    1 
ATOM   15847 C C     . HIS B  1 977  ? 10.042  40.336  102.148 1.00 20.20 ? 975  HIS B C     1 
ATOM   15848 O O     . HIS B  1 977  ? 10.953  40.662  102.926 1.00 20.45 ? 975  HIS B O     1 
ATOM   15849 C CB    . HIS B  1 977  ? 11.022  38.212  101.284 1.00 18.57 ? 975  HIS B CB    1 
ATOM   15850 C CG    . HIS B  1 977  ? 10.720  37.077  100.355 1.00 20.45 ? 975  HIS B CG    1 
ATOM   15851 N ND1   . HIS B  1 977  ? 11.231  37.011  99.079  1.00 26.71 ? 975  HIS B ND1   1 
ATOM   15852 C CD2   . HIS B  1 977  ? 10.000  35.944  100.535 1.00 20.16 ? 975  HIS B CD2   1 
ATOM   15853 C CE1   . HIS B  1 977  ? 10.833  35.887  98.506  1.00 24.85 ? 975  HIS B CE1   1 
ATOM   15854 N NE2   . HIS B  1 977  ? 10.094  35.218  99.374  1.00 23.10 ? 975  HIS B NE2   1 
ATOM   15855 N N     . THR B  1 978  ? 8.765   40.621  102.348 1.00 20.02 ? 976  THR B N     1 
ATOM   15856 C CA    . THR B  1 978  ? 8.275   41.384  103.486 1.00 19.45 ? 976  THR B CA    1 
ATOM   15857 C C     . THR B  1 978  ? 6.771   41.230  103.521 1.00 23.78 ? 976  THR B C     1 
ATOM   15858 O O     . THR B  1 978  ? 6.138   40.999  102.489 1.00 25.04 ? 976  THR B O     1 
ATOM   15859 C CB    . THR B  1 978  ? 8.657   42.868  103.377 1.00 23.46 ? 976  THR B CB    1 
ATOM   15860 O OG1   . THR B  1 978  ? 8.167   43.596  104.511 1.00 23.28 ? 976  THR B OG1   1 
ATOM   15861 C CG2   . THR B  1 978  ? 8.065   43.454  102.128 1.00 22.14 ? 976  THR B CG2   1 
ATOM   15862 N N     . ARG B  1 979  ? 6.206   41.361  104.715 1.00 25.23 ? 977  ARG B N     1 
ATOM   15863 C CA    . ARG B  1 979  ? 4.763   41.421  104.861 1.00 26.11 ? 977  ARG B CA    1 
ATOM   15864 C C     . ARG B  1 979  ? 4.265   42.838  105.081 1.00 25.15 ? 977  ARG B C     1 
ATOM   15865 O O     . ARG B  1 979  ? 3.063   43.025  105.282 1.00 25.16 ? 977  ARG B O     1 
ATOM   15866 C CB    . ARG B  1 979  ? 4.303   40.551  106.029 1.00 29.83 ? 977  ARG B CB    1 
ATOM   15867 C CG    . ARG B  1 979  ? 4.562   39.073  105.861 1.00 36.27 ? 977  ARG B CG    1 
ATOM   15868 C CD    . ARG B  1 979  ? 4.319   38.377  107.190 1.00 41.23 ? 977  ARG B CD    1 
ATOM   15869 N NE    . ARG B  1 979  ? 4.888   37.037  107.236 1.00 47.80 ? 977  ARG B NE    1 
ATOM   15870 C CZ    . ARG B  1 979  ? 4.837   36.243  108.297 1.00 50.08 ? 977  ARG B CZ    1 
ATOM   15871 N NH1   . ARG B  1 979  ? 4.217   36.613  109.407 1.00 48.36 ? 977  ARG B NH1   1 
ATOM   15872 N NH2   . ARG B  1 979  ? 5.424   35.049  108.243 1.00 49.40 ? 977  ARG B NH2   1 
ATOM   15873 N N     . LEU B  1 980  ? 5.149   43.833  105.052 1.00 20.41 ? 978  LEU B N     1 
ATOM   15874 C CA    . LEU B  1 980  ? 4.793   45.194  105.440 1.00 21.17 ? 978  LEU B CA    1 
ATOM   15875 C C     . LEU B  1 980  ? 4.593   46.070  104.207 1.00 23.28 ? 978  LEU B C     1 
ATOM   15876 O O     . LEU B  1 980  ? 5.522   46.249  103.409 1.00 22.89 ? 978  LEU B O     1 
ATOM   15877 C CB    . LEU B  1 980  ? 5.874   45.783  106.345 1.00 19.47 ? 978  LEU B CB    1 
ATOM   15878 C CG    . LEU B  1 980  ? 6.222   44.890  107.540 1.00 26.30 ? 978  LEU B CG    1 
ATOM   15879 C CD1   . LEU B  1 980  ? 7.357   45.516  108.343 1.00 25.75 ? 978  LEU B CD1   1 
ATOM   15880 C CD2   . LEU B  1 980  ? 4.998   44.697  108.409 1.00 23.26 ? 978  LEU B CD2   1 
ATOM   15881 N N     . ASP B  1 981  ? 3.394   46.642  104.082 1.00 22.60 ? 979  ASP B N     1 
ATOM   15882 C CA    . ASP B  1 981  ? 3.077   47.486  102.929 1.00 22.00 ? 979  ASP B CA    1 
ATOM   15883 C C     . ASP B  1 981  ? 3.983   48.713  102.840 1.00 22.47 ? 979  ASP B C     1 
ATOM   15884 O O     . ASP B  1 981  ? 4.343   49.142  101.739 1.00 22.55 ? 979  ASP B O     1 
ATOM   15885 C CB    . ASP B  1 981  ? 1.615   47.925  102.988 1.00 23.41 ? 979  ASP B CB    1 
ATOM   15886 C CG    . ASP B  1 981  ? 0.641   46.825  102.557 1.00 28.73 ? 979  ASP B CG    1 
ATOM   15887 O OD1   . ASP B  1 981  ? 1.082   45.790  102.016 1.00 28.48 ? 979  ASP B OD1   1 
ATOM   15888 O OD2   . ASP B  1 981  ? -0.576  47.017  102.759 1.00 29.08 ? 979  ASP B OD2   1 
ATOM   15889 N N     . GLU B  1 982  ? 4.345   49.317  103.980 1.00 22.60 ? 980  GLU B N     1 
ATOM   15890 C CA    . GLU B  1 982  ? 5.208   50.494  103.906 1.00 22.19 ? 980  GLU B CA    1 
ATOM   15891 C C     . GLU B  1 982  ? 6.561   50.141  103.295 1.00 23.19 ? 980  GLU B C     1 
ATOM   15892 O O     . GLU B  1 982  ? 7.141   50.930  102.541 1.00 21.46 ? 980  GLU B O     1 
ATOM   15893 C CB    . GLU B  1 982  ? 5.406   51.122  105.289 1.00 25.58 ? 980  GLU B CB    1 
ATOM   15894 C CG    . GLU B  1 982  ? 6.266   52.379  105.207 1.00 26.77 ? 980  GLU B CG    1 
ATOM   15895 C CD    . GLU B  1 982  ? 6.707   52.895  106.556 1.00 36.01 ? 980  GLU B CD    1 
ATOM   15896 O OE1   . GLU B  1 982  ? 6.743   52.106  107.526 1.00 40.99 ? 980  GLU B OE1   1 
ATOM   15897 O OE2   . GLU B  1 982  ? 7.003   54.102  106.648 1.00 37.06 ? 980  GLU B OE2   1 
ATOM   15898 N N     . THR B  1 983  ? 7.074   48.949  103.606 1.00 21.28 ? 981  THR B N     1 
ATOM   15899 C CA    . THR B  1 983  ? 8.356   48.517  103.070 1.00 20.68 ? 981  THR B CA    1 
ATOM   15900 C C     . THR B  1 983  ? 8.258   48.206  101.585 1.00 21.76 ? 981  THR B C     1 
ATOM   15901 O O     . THR B  1 983  ? 9.173   48.525  100.812 1.00 23.26 ? 981  THR B O     1 
ATOM   15902 C CB    . THR B  1 983  ? 8.835   47.302  103.855 1.00 23.03 ? 981  THR B CB    1 
ATOM   15903 O OG1   . THR B  1 983  ? 9.073   47.712  105.205 1.00 23.24 ? 981  THR B OG1   1 
ATOM   15904 C CG2   . THR B  1 983  ? 10.102  46.710  103.232 1.00 22.91 ? 981  THR B CG2   1 
ATOM   15905 N N     . ILE B  1 984  ? 7.162   47.581  101.172 1.00 22.22 ? 982  ILE B N     1 
ATOM   15906 C CA    . ILE B  1 984  ? 6.947   47.354  99.748  1.00 20.08 ? 982  ILE B CA    1 
ATOM   15907 C C     . ILE B  1 984  ? 6.934   48.684  99.005  1.00 21.55 ? 982  ILE B C     1 
ATOM   15908 O O     . ILE B  1 984  ? 7.636   48.861  98.000  1.00 22.56 ? 982  ILE B O     1 
ATOM   15909 C CB    . ILE B  1 984  ? 5.648   46.564  99.521  1.00 23.24 ? 982  ILE B CB    1 
ATOM   15910 C CG1   . ILE B  1 984  ? 5.811   45.137  100.060 1.00 25.79 ? 982  ILE B CG1   1 
ATOM   15911 C CG2   . ILE B  1 984  ? 5.294   46.548  98.039  1.00 21.58 ? 982  ILE B CG2   1 
ATOM   15912 C CD1   . ILE B  1 984  ? 4.516   44.380  100.241 1.00 27.24 ? 982  ILE B CD1   1 
ATOM   15913 N N     . ALA B  1 985  ? 6.167   49.651  99.513  1.00 21.55 ? 983  ALA B N     1 
ATOM   15914 C CA    . ALA B  1 985  ? 6.041   50.930  98.816  1.00 23.46 ? 983  ALA B CA    1 
ATOM   15915 C C     . ALA B  1 985  ? 7.379   51.651  98.765  1.00 24.46 ? 983  ALA B C     1 
ATOM   15916 O O     . ALA B  1 985  ? 7.765   52.181  97.721  1.00 24.50 ? 983  ALA B O     1 
ATOM   15917 C CB    . ALA B  1 985  ? 4.978   51.809  99.480  1.00 21.54 ? 983  ALA B CB    1 
ATOM   15918 N N     . HIS B  1 986  ? 8.101   51.678  99.888  1.00 21.79 ? 984  HIS B N     1 
ATOM   15919 C CA    . HIS B  1 986  ? 9.408   52.327  99.922  1.00 23.51 ? 984  HIS B CA    1 
ATOM   15920 C C     . HIS B  1 986  ? 10.362  51.684  98.924  1.00 21.87 ? 984  HIS B C     1 
ATOM   15921 O O     . HIS B  1 986  ? 10.914  52.364  98.055  1.00 24.47 ? 984  HIS B O     1 
ATOM   15922 C CB    . HIS B  1 986  ? 9.966   52.276  101.351 1.00 21.23 ? 984  HIS B CB    1 
ATOM   15923 C CG    . HIS B  1 986  ? 11.384  52.756  101.495 1.00 26.91 ? 984  HIS B CG    1 
ATOM   15924 N ND1   . HIS B  1 986  ? 12.041  52.740  102.705 1.00 29.87 ? 984  HIS B ND1   1 
ATOM   15925 C CD2   . HIS B  1 986  ? 12.276  53.241  100.594 1.00 29.38 ? 984  HIS B CD2   1 
ATOM   15926 C CE1   . HIS B  1 986  ? 13.271  53.199  102.548 1.00 34.14 ? 984  HIS B CE1   1 
ATOM   15927 N NE2   . HIS B  1 986  ? 13.442  53.507  101.275 1.00 26.35 ? 984  HIS B NE2   1 
ATOM   15928 N N     . VAL B  1 987  ? 10.539  50.363  99.006  1.00 21.52 ? 985  VAL B N     1 
ATOM   15929 C CA    . VAL B  1 987  ? 11.574  49.695  98.214  1.00 22.81 ? 985  VAL B CA    1 
ATOM   15930 C C     . VAL B  1 987  ? 11.231  49.714  96.723  1.00 22.03 ? 985  VAL B C     1 
ATOM   15931 O O     . VAL B  1 987  ? 12.096  49.991  95.880  1.00 21.16 ? 985  VAL B O     1 
ATOM   15932 C CB    . VAL B  1 987  ? 11.792  48.263  98.733  1.00 21.65 ? 985  VAL B CB    1 
ATOM   15933 C CG1   . VAL B  1 987  ? 12.656  47.478  97.774  1.00 19.31 ? 985  VAL B CG1   1 
ATOM   15934 C CG2   . VAL B  1 987  ? 12.485  48.302  100.100 1.00 19.63 ? 985  VAL B CG2   1 
ATOM   15935 N N     . THR B  1 988  ? 9.978   49.423  96.367  1.00 21.50 ? 986  THR B N     1 
ATOM   15936 C CA    . THR B  1 988  ? 9.626   49.401  94.950  1.00 25.07 ? 986  THR B CA    1 
ATOM   15937 C C     . THR B  1 988  ? 9.601   50.796  94.332  1.00 24.11 ? 986  THR B C     1 
ATOM   15938 O O     . THR B  1 988  ? 9.715   50.912  93.109  1.00 28.15 ? 986  THR B O     1 
ATOM   15939 C CB    . THR B  1 988  ? 8.271   48.708  94.720  1.00 25.61 ? 986  THR B CB    1 
ATOM   15940 O OG1   . THR B  1 988  ? 7.209   49.447  95.344  1.00 26.43 ? 986  THR B OG1   1 
ATOM   15941 C CG2   . THR B  1 988  ? 8.299   47.270  95.261  1.00 26.91 ? 986  THR B CG2   1 
ATOM   15942 N N     . SER B  1 989  ? 9.456   51.851  95.136  1.00 27.67 ? 987  SER B N     1 
ATOM   15943 C CA    . SER B  1 989  ? 9.560   53.212  94.620  1.00 26.32 ? 987  SER B CA    1 
ATOM   15944 C C     . SER B  1 989  ? 11.009  53.655  94.408  1.00 29.84 ? 987  SER B C     1 
ATOM   15945 O O     . SER B  1 989  ? 11.252  54.565  93.612  1.00 29.74 ? 987  SER B O     1 
ATOM   15946 C CB    . SER B  1 989  ? 8.856   54.198  95.559  1.00 22.28 ? 987  SER B CB    1 
ATOM   15947 O OG    . SER B  1 989  ? 9.571   54.367  96.784  1.00 30.94 ? 987  SER B OG    1 
ATOM   15948 N N     . ARG B  1 990  ? 11.976  53.039  95.091  1.00 23.47 ? 988  ARG B N     1 
ATOM   15949 C CA    . ARG B  1 990  ? 13.363  53.471  95.004  1.00 25.64 ? 988  ARG B CA    1 
ATOM   15950 C C     . ARG B  1 990  ? 14.263  52.546  94.194  1.00 25.85 ? 988  ARG B C     1 
ATOM   15951 O O     . ARG B  1 990  ? 15.293  53.003  93.696  1.00 27.96 ? 988  ARG B O     1 
ATOM   15952 C CB    . ARG B  1 990  ? 13.951  53.628  96.412  1.00 22.62 ? 988  ARG B CB    1 
ATOM   15953 C CG    . ARG B  1 990  ? 13.131  54.559  97.299  1.00 29.49 ? 988  ARG B CG    1 
ATOM   15954 C CD    . ARG B  1 990  ? 13.409  56.015  96.986  1.00 31.67 ? 988  ARG B CD    1 
ATOM   15955 N NE    . ARG B  1 990  ? 14.557  56.510  97.740  1.00 28.73 ? 988  ARG B NE    1 
ATOM   15956 C CZ    . ARG B  1 990  ? 14.974  57.769  97.727  1.00 28.10 ? 988  ARG B CZ    1 
ATOM   15957 N NH1   . ARG B  1 990  ? 14.388  58.681  96.974  1.00 30.39 ? 988  ARG B NH1   1 
ATOM   15958 N NH2   . ARG B  1 990  ? 15.995  58.121  98.499  1.00 26.94 ? 988  ARG B NH2   1 
ATOM   15959 N N     . ILE B  1 991  ? 13.918  51.266  94.052  1.00 25.98 ? 989  ILE B N     1 
ATOM   15960 C CA    . ILE B  1 991  ? 14.772  50.370  93.284  1.00 25.46 ? 989  ILE B CA    1 
ATOM   15961 C C     . ILE B  1 991  ? 14.604  50.661  91.795  1.00 25.27 ? 989  ILE B C     1 
ATOM   15962 O O     . ILE B  1 991  ? 13.531  51.056  91.332  1.00 25.94 ? 989  ILE B O     1 
ATOM   15963 C CB    . ILE B  1 991  ? 14.448  48.901  93.612  1.00 25.29 ? 989  ILE B CB    1 
ATOM   15964 C CG1   . ILE B  1 991  ? 15.560  47.973  93.092  1.00 23.38 ? 989  ILE B CG1   1 
ATOM   15965 C CG2   . ILE B  1 991  ? 13.085  48.531  93.055  1.00 25.44 ? 989  ILE B CG2   1 
ATOM   15966 C CD1   . ILE B  1 991  ? 16.785  47.941  94.025  1.00 23.20 ? 989  ILE B CD1   1 
ATOM   15967 N N     . LYS B  1 992  ? 15.679  50.494  91.041  1.00 23.30 ? 990  LYS B N     1 
ATOM   15968 C CA    . LYS B  1 992  ? 15.662  50.720  89.598  1.00 25.60 ? 990  LYS B CA    1 
ATOM   15969 C C     . LYS B  1 992  ? 15.915  49.370  88.929  1.00 24.49 ? 990  LYS B C     1 
ATOM   15970 O O     . LYS B  1 992  ? 17.057  48.991  88.662  1.00 34.17 ? 990  LYS B O     1 
ATOM   15971 C CB    . LYS B  1 992  ? 16.700  51.767  89.188  1.00 30.25 ? 990  LYS B CB    1 
ATOM   15972 N N     . ALA B  1 993  ? 14.845  48.626  88.691  1.00 23.62 ? 991  ALA B N     1 
ATOM   15973 C CA    . ALA B  1 993  ? 14.978  47.323  88.054  1.00 19.77 ? 991  ALA B CA    1 
ATOM   15974 C C     . ALA B  1 993  ? 13.749  47.074  87.190  1.00 17.94 ? 991  ALA B C     1 
ATOM   15975 O O     . ALA B  1 993  ? 12.656  47.561  87.478  1.00 23.16 ? 991  ALA B O     1 
ATOM   15976 C CB    . ALA B  1 993  ? 15.161  46.201  89.084  1.00 22.05 ? 991  ALA B CB    1 
ATOM   15977 N N     . GLY B  1 994  ? 13.950  46.319  86.112  1.00 21.68 ? 992  GLY B N     1 
ATOM   15978 C CA    . GLY B  1 994  ? 12.872  46.117  85.161  1.00 20.65 ? 992  GLY B CA    1 
ATOM   15979 C C     . GLY B  1 994  ? 11.874  45.054  85.560  1.00 22.06 ? 992  GLY B C     1 
ATOM   15980 O O     . GLY B  1 994  ? 10.730  45.080  85.100  1.00 20.05 ? 992  GLY B O     1 
ATOM   15981 N N     . ASN B  1 995  ? 12.282  44.096  86.390  1.00 19.57 ? 993  ASN B N     1 
ATOM   15982 C CA    . ASN B  1 995  ? 11.433  42.980  86.792  1.00 16.71 ? 993  ASN B CA    1 
ATOM   15983 C C     . ASN B  1 995  ? 11.510  42.845  88.307  1.00 19.00 ? 993  ASN B C     1 
ATOM   15984 O O     . ASN B  1 995  ? 12.545  42.427  88.833  1.00 20.97 ? 993  ASN B O     1 
ATOM   15985 C CB    . ASN B  1 995  ? 11.867  41.678  86.120  1.00 15.54 ? 993  ASN B CB    1 
ATOM   15986 C CG    . ASN B  1 995  ? 11.364  41.565  84.688  1.00 18.71 ? 993  ASN B CG    1 
ATOM   15987 O OD1   . ASN B  1 995  ? 12.002  42.045  83.751  1.00 21.17 ? 993  ASN B OD1   1 
ATOM   15988 N ND2   . ASN B  1 995  ? 10.227  40.910  84.517  1.00 19.52 ? 993  ASN B ND2   1 
ATOM   15989 N N     . LEU B  1 996  ? 10.412  43.180  88.983  1.00 20.44 ? 994  LEU B N     1 
ATOM   15990 C CA    . LEU B  1 996  ? 10.282  43.146  90.434  1.00 18.58 ? 994  LEU B CA    1 
ATOM   15991 C C     . LEU B  1 996  ? 9.431   41.959  90.872  1.00 20.18 ? 994  LEU B C     1 
ATOM   15992 O O     . LEU B  1 996  ? 8.410   41.643  90.256  1.00 19.29 ? 994  LEU B O     1 
ATOM   15993 C CB    . LEU B  1 996  ? 9.636   44.432  90.955  1.00 20.52 ? 994  LEU B CB    1 
ATOM   15994 C CG    . LEU B  1 996  ? 10.176  45.760  90.407  1.00 24.06 ? 994  LEU B CG    1 
ATOM   15995 C CD1   . LEU B  1 996  ? 9.481   46.952  91.079  1.00 27.17 ? 994  LEU B CD1   1 
ATOM   15996 C CD2   . LEU B  1 996  ? 11.698  45.840  90.569  1.00 26.14 ? 994  LEU B CD2   1 
ATOM   15997 N N     . TYR B  1 997  ? 9.833   41.324  91.964  1.00 16.53 ? 995  TYR B N     1 
ATOM   15998 C CA    . TYR B  1 997  ? 9.125   40.165  92.481  1.00 20.50 ? 995  TYR B CA    1 
ATOM   15999 C C     . TYR B  1 997  ? 8.953   40.330  93.977  1.00 19.42 ? 995  TYR B C     1 
ATOM   16000 O O     . TYR B  1 997  ? 9.927   40.598  94.687  1.00 20.92 ? 995  TYR B O     1 
ATOM   16001 C CB    . TYR B  1 997  ? 9.883   38.877  92.173  1.00 19.10 ? 995  TYR B CB    1 
ATOM   16002 C CG    . TYR B  1 997  ? 10.062  38.640  90.697  1.00 21.53 ? 995  TYR B CG    1 
ATOM   16003 C CD1   . TYR B  1 997  ? 9.060   38.048  89.949  1.00 20.43 ? 995  TYR B CD1   1 
ATOM   16004 C CD2   . TYR B  1 997  ? 11.233  39.016  90.051  1.00 23.91 ? 995  TYR B CD2   1 
ATOM   16005 C CE1   . TYR B  1 997  ? 9.216   37.831  88.596  1.00 21.43 ? 995  TYR B CE1   1 
ATOM   16006 C CE2   . TYR B  1 997  ? 11.407  38.789  88.687  1.00 22.76 ? 995  TYR B CE2   1 
ATOM   16007 C CZ    . TYR B  1 997  ? 10.387  38.204  87.976  1.00 20.78 ? 995  TYR B CZ    1 
ATOM   16008 O OH    . TYR B  1 997  ? 10.535  37.985  86.641  1.00 27.62 ? 995  TYR B OH    1 
ATOM   16009 N N     . ILE B  1 998  ? 7.731   40.156  94.458  1.00 20.56 ? 996  ILE B N     1 
ATOM   16010 C CA    . ILE B  1 998  ? 7.416   40.387  95.861  1.00 19.96 ? 996  ILE B CA    1 
ATOM   16011 C C     . ILE B  1 998  ? 6.939   39.076  96.470  1.00 17.46 ? 996  ILE B C     1 
ATOM   16012 O O     . ILE B  1 998  ? 5.896   38.545  96.071  1.00 19.36 ? 996  ILE B O     1 
ATOM   16013 C CB    . ILE B  1 998  ? 6.364   41.489  96.039  1.00 21.68 ? 996  ILE B CB    1 
ATOM   16014 C CG1   . ILE B  1 998  ? 6.801   42.788  95.340  1.00 22.33 ? 996  ILE B CG1   1 
ATOM   16015 C CG2   . ILE B  1 998  ? 6.103   41.739  97.522  1.00 20.74 ? 996  ILE B CG2   1 
ATOM   16016 C CD1   . ILE B  1 998  ? 8.038   43.393  95.931  1.00 24.04 ? 996  ILE B CD1   1 
ATOM   16017 N N     . ASN B  1 999  ? 7.703   38.563  97.439  1.00 16.93 ? 997  ASN B N     1 
ATOM   16018 C CA    . ASN B  1 999  ? 7.306   37.395  98.225  1.00 19.47 ? 997  ASN B CA    1 
ATOM   16019 C C     . ASN B  1 999  ? 7.217   36.140  97.354  1.00 18.25 ? 997  ASN B C     1 
ATOM   16020 O O     . ASN B  1 999  ? 6.348   35.291  97.549  1.00 21.30 ? 997  ASN B O     1 
ATOM   16021 C CB    . ASN B  1 999  ? 5.993   37.657  98.982  1.00 20.20 ? 997  ASN B CB    1 
ATOM   16022 C CG    . ASN B  1 999  ? 6.167   38.697  100.095 1.00 17.36 ? 997  ASN B CG    1 
ATOM   16023 O OD1   . ASN B  1 999  ? 7.237   38.773  100.699 1.00 21.13 ? 997  ASN B OD1   1 
ATOM   16024 N ND2   . ASN B  1 999  ? 5.132   39.492  100.363 1.00 20.92 ? 997  ASN B ND2   1 
ATOM   16025 N N     . ARG B  1 1000 ? 8.131   36.034  96.386  1.00 16.62 ? 998  ARG B N     1 
ATOM   16026 C CA    . ARG B  1 1000 ? 8.278   34.850  95.545  1.00 18.66 ? 998  ARG B CA    1 
ATOM   16027 C C     . ARG B  1 1000 ? 9.705   34.830  95.003  1.00 18.36 ? 998  ARG B C     1 
ATOM   16028 O O     . ARG B  1 1000 ? 10.509  35.721  95.298  1.00 19.21 ? 998  ARG B O     1 
ATOM   16029 C CB    . ARG B  1 1000 ? 7.244   34.856  94.409  1.00 18.28 ? 998  ARG B CB    1 
ATOM   16030 C CG    . ARG B  1 1000 ? 7.211   36.178  93.672  1.00 18.28 ? 998  ARG B CG    1 
ATOM   16031 C CD    . ARG B  1 1000 ? 6.737   35.969  92.210  1.00 19.55 ? 998  ARG B CD    1 
ATOM   16032 N NE    . ARG B  1 1000 ? 7.730   35.227  91.446  1.00 17.56 ? 998  ARG B NE    1 
ATOM   16033 C CZ    . ARG B  1 1000 ? 7.581   34.879  90.176  1.00 21.15 ? 998  ARG B CZ    1 
ATOM   16034 N NH1   . ARG B  1 1000 ? 6.494   35.208  89.496  1.00 18.33 ? 998  ARG B NH1   1 
ATOM   16035 N NH2   . ARG B  1 1000 ? 8.545   34.190  89.573  1.00 22.46 ? 998  ARG B NH2   1 
ATOM   16036 N N     . ASN B  1 1001 ? 10.027  33.811  94.200  1.00 17.62 ? 999  ASN B N     1 
ATOM   16037 C CA    . ASN B  1 1001 ? 11.358  33.780  93.606  1.00 18.07 ? 999  ASN B CA    1 
ATOM   16038 C C     . ASN B  1 1001 ? 11.466  34.855  92.518  1.00 18.31 ? 999  ASN B C     1 
ATOM   16039 O O     . ASN B  1 1001 ? 10.493  35.522  92.179  1.00 18.99 ? 999  ASN B O     1 
ATOM   16040 C CB    . ASN B  1 1001 ? 11.696  32.371  93.096  1.00 16.21 ? 999  ASN B CB    1 
ATOM   16041 C CG    . ASN B  1 1001 ? 10.905  31.974  91.887  1.00 23.46 ? 999  ASN B CG    1 
ATOM   16042 O OD1   . ASN B  1 1001 ? 10.723  32.764  90.982  1.00 21.15 ? 999  ASN B OD1   1 
ATOM   16043 N ND2   . ASN B  1 1001 ? 10.426  30.731  91.869  1.00 24.67 ? 999  ASN B ND2   1 
ATOM   16044 N N     . ILE B  1 1002 ? 12.664  35.034  91.967  1.00 18.50 ? 1000 ILE B N     1 
ATOM   16045 C CA    . ILE B  1 1002 ? 12.857  36.126  91.021  1.00 18.51 ? 1000 ILE B CA    1 
ATOM   16046 C C     . ILE B  1 1002 ? 13.191  35.626  89.617  1.00 22.66 ? 1000 ILE B C     1 
ATOM   16047 O O     . ILE B  1 1002 ? 13.665  36.403  88.781  1.00 22.10 ? 1000 ILE B O     1 
ATOM   16048 C CB    . ILE B  1 1002 ? 13.919  37.118  91.528  1.00 20.26 ? 1000 ILE B CB    1 
ATOM   16049 C CG1   . ILE B  1 1002 ? 15.309  36.460  91.594  1.00 18.48 ? 1000 ILE B CG1   1 
ATOM   16050 C CG2   . ILE B  1 1002 ? 13.500  37.645  92.879  1.00 18.21 ? 1000 ILE B CG2   1 
ATOM   16051 C CD1   . ILE B  1 1002 ? 16.450  37.444  91.864  1.00 15.90 ? 1000 ILE B CD1   1 
ATOM   16052 N N     . ILE B  1 1003 ? 12.929  34.351  89.332  1.00 20.00 ? 1001 ILE B N     1 
ATOM   16053 C CA    . ILE B  1 1003 ? 13.305  33.749  88.058  1.00 21.41 ? 1001 ILE B CA    1 
ATOM   16054 C C     . ILE B  1 1003 ? 12.046  33.282  87.324  1.00 26.42 ? 1001 ILE B C     1 
ATOM   16055 O O     . ILE B  1 1003 ? 10.929  33.339  87.845  1.00 25.37 ? 1001 ILE B O     1 
ATOM   16056 C CB    . ILE B  1 1003 ? 14.294  32.577  88.217  1.00 22.55 ? 1001 ILE B CB    1 
ATOM   16057 C CG1   . ILE B  1 1003 ? 13.652  31.412  88.975  1.00 26.24 ? 1001 ILE B CG1   1 
ATOM   16058 C CG2   . ILE B  1 1003 ? 15.560  33.040  88.928  1.00 19.55 ? 1001 ILE B CG2   1 
ATOM   16059 C CD1   . ILE B  1 1003 ? 14.508  30.145  88.967  1.00 25.53 ? 1001 ILE B CD1   1 
ATOM   16060 N N     . GLY B  1 1004 ? 12.255  32.813  86.099  1.00 23.76 ? 1002 GLY B N     1 
ATOM   16061 C CA    . GLY B  1 1004 ? 11.191  32.181  85.338  1.00 26.80 ? 1002 GLY B CA    1 
ATOM   16062 C C     . GLY B  1 1004 ? 10.094  33.127  84.899  1.00 26.75 ? 1002 GLY B C     1 
ATOM   16063 O O     . GLY B  1 1004 ? 8.908   32.776  84.980  1.00 26.98 ? 1002 GLY B O     1 
ATOM   16064 N N     . ALA B  1 1005 ? 10.460  34.326  84.450  1.00 26.60 ? 1003 ALA B N     1 
ATOM   16065 C CA    . ALA B  1 1005 ? 9.477   35.288  83.981  1.00 19.59 ? 1003 ALA B CA    1 
ATOM   16066 C C     . ALA B  1 1005 ? 8.652   34.682  82.854  1.00 21.17 ? 1003 ALA B C     1 
ATOM   16067 O O     . ALA B  1 1005 ? 9.187   34.008  81.972  1.00 28.61 ? 1003 ALA B O     1 
ATOM   16068 C CB    . ALA B  1 1005 ? 10.166  36.562  83.495  1.00 23.10 ? 1003 ALA B CB    1 
ATOM   16069 N N     . VAL B  1 1006 ? 7.348   34.928  82.894  1.00 19.63 ? 1004 VAL B N     1 
ATOM   16070 C CA    . VAL B  1 1006 ? 6.373   34.278  82.018  1.00 19.08 ? 1004 VAL B CA    1 
ATOM   16071 C C     . VAL B  1 1006 ? 5.994   35.239  80.905  1.00 23.68 ? 1004 VAL B C     1 
ATOM   16072 O O     . VAL B  1 1006 ? 5.619   36.391  81.164  1.00 19.32 ? 1004 VAL B O     1 
ATOM   16073 C CB    . VAL B  1 1006 ? 5.135   33.823  82.814  1.00 20.23 ? 1004 VAL B CB    1 
ATOM   16074 C CG1   . VAL B  1 1006 ? 3.999   33.372  81.888  1.00 18.62 ? 1004 VAL B CG1   1 
ATOM   16075 C CG2   . VAL B  1 1006 ? 5.526   32.695  83.764  1.00 22.78 ? 1004 VAL B CG2   1 
ATOM   16076 N N     . VAL B  1 1007 ? 6.085   34.756  79.667  1.00 18.90 ? 1005 VAL B N     1 
ATOM   16077 C CA    . VAL B  1 1007 ? 5.748   35.573  78.505  1.00 20.19 ? 1005 VAL B CA    1 
ATOM   16078 C C     . VAL B  1 1007 ? 4.370   36.207  78.668  1.00 17.59 ? 1005 VAL B C     1 
ATOM   16079 O O     . VAL B  1 1007 ? 3.379   35.530  78.969  1.00 19.62 ? 1005 VAL B O     1 
ATOM   16080 C CB    . VAL B  1 1007 ? 5.828   34.715  77.232  1.00 19.12 ? 1005 VAL B CB    1 
ATOM   16081 C CG1   . VAL B  1 1007 ? 5.323   35.536  76.081  1.00 17.27 ? 1005 VAL B CG1   1 
ATOM   16082 C CG2   . VAL B  1 1007 ? 7.250   34.264  76.985  1.00 19.72 ? 1005 VAL B CG2   1 
ATOM   16083 N N     . GLY B  1 1008 ? 4.302   37.523  78.448  1.00 19.32 ? 1006 GLY B N     1 
ATOM   16084 C CA    . GLY B  1 1008 ? 3.037   38.228  78.495  1.00 17.71 ? 1006 GLY B CA    1 
ATOM   16085 C C     . GLY B  1 1008 ? 2.431   38.387  79.878  1.00 19.49 ? 1006 GLY B C     1 
ATOM   16086 O O     . GLY B  1 1008 ? 1.296   38.869  79.987  1.00 21.23 ? 1006 GLY B O     1 
ATOM   16087 N N     . VAL B  1 1009 ? 3.158   38.012  80.932  1.00 18.91 ? 1007 VAL B N     1 
ATOM   16088 C CA    . VAL B  1 1009 ? 2.662   38.092  82.306  1.00 21.40 ? 1007 VAL B CA    1 
ATOM   16089 C C     . VAL B  1 1009 ? 3.682   38.853  83.146  1.00 20.49 ? 1007 VAL B C     1 
ATOM   16090 O O     . VAL B  1 1009 ? 3.326   39.758  83.912  1.00 17.53 ? 1007 VAL B O     1 
ATOM   16091 C CB    . VAL B  1 1009 ? 2.395   36.697  82.898  1.00 21.59 ? 1007 VAL B CB    1 
ATOM   16092 C CG1   . VAL B  1 1009 ? 1.904   36.820  84.352  1.00 21.93 ? 1007 VAL B CG1   1 
ATOM   16093 C CG2   . VAL B  1 1009 ? 1.364   35.935  82.035  1.00 19.79 ? 1007 VAL B CG2   1 
ATOM   16094 N N     . GLN B  1 1010 ? 4.950   38.465  83.028  1.00 19.42 ? 1008 GLN B N     1 
ATOM   16095 C CA    . GLN B  1 1010 ? 6.086   39.274  83.470  1.00 18.47 ? 1008 GLN B CA    1 
ATOM   16096 C C     . GLN B  1 1010 ? 6.967   39.527  82.252  1.00 17.93 ? 1008 GLN B C     1 
ATOM   16097 O O     . GLN B  1 1010 ? 8.010   38.881  82.099  1.00 18.03 ? 1008 GLN B O     1 
ATOM   16098 C CB    . GLN B  1 1010 ? 6.897   38.600  84.575  1.00 20.57 ? 1008 GLN B CB    1 
ATOM   16099 C CG    . GLN B  1 1010 ? 6.117   38.269  85.819  1.00 20.26 ? 1008 GLN B CG    1 
ATOM   16100 C CD    . GLN B  1 1010 ? 5.735   36.818  85.884  1.00 20.09 ? 1008 GLN B CD    1 
ATOM   16101 O OE1   . GLN B  1 1010 ? 6.429   35.942  85.344  1.00 20.62 ? 1008 GLN B OE1   1 
ATOM   16102 N NE2   . GLN B  1 1010 ? 4.621   36.546  86.542  1.00 18.78 ? 1008 GLN B NE2   1 
ATOM   16103 N N     . PRO B  1 1011 ? 6.562   40.432  81.356  1.00 19.86 ? 1009 PRO B N     1 
ATOM   16104 C CA    . PRO B  1 1011 ? 7.464   40.862  80.278  1.00 18.50 ? 1009 PRO B CA    1 
ATOM   16105 C C     . PRO B  1 1011 ? 8.844   41.157  80.833  1.00 21.48 ? 1009 PRO B C     1 
ATOM   16106 O O     . PRO B  1 1011 ? 8.989   41.833  81.851  1.00 22.03 ? 1009 PRO B O     1 
ATOM   16107 C CB    . PRO B  1 1011 ? 6.787   42.120  79.732  1.00 19.55 ? 1009 PRO B CB    1 
ATOM   16108 C CG    . PRO B  1 1011 ? 5.339   41.930  80.041  1.00 23.76 ? 1009 PRO B CG    1 
ATOM   16109 C CD    . PRO B  1 1011 ? 5.307   41.197  81.374  1.00 19.62 ? 1009 PRO B CD    1 
ATOM   16110 N N     . PHE B  1 1012 ? 9.862   40.642  80.157  1.00 18.85 ? 1010 PHE B N     1 
ATOM   16111 C CA    . PHE B  1 1012 ? 11.177  40.482  80.753  1.00 22.15 ? 1010 PHE B CA    1 
ATOM   16112 C C     . PHE B  1 1012 ? 12.203  41.391  80.097  1.00 20.66 ? 1010 PHE B C     1 
ATOM   16113 O O     . PHE B  1 1012 ? 12.337  41.404  78.876  1.00 21.50 ? 1010 PHE B O     1 
ATOM   16114 C CB    . PHE B  1 1012 ? 11.644  39.038  80.646  1.00 16.61 ? 1010 PHE B CB    1 
ATOM   16115 C CG    . PHE B  1 1012 ? 12.936  38.794  81.364  1.00 19.88 ? 1010 PHE B CG    1 
ATOM   16116 C CD1   . PHE B  1 1012 ? 12.949  38.593  82.730  1.00 24.06 ? 1010 PHE B CD1   1 
ATOM   16117 C CD2   . PHE B  1 1012 ? 14.140  38.799  80.671  1.00 22.93 ? 1010 PHE B CD2   1 
ATOM   16118 C CE1   . PHE B  1 1012 ? 14.144  38.368  83.397  1.00 21.46 ? 1010 PHE B CE1   1 
ATOM   16119 C CE2   . PHE B  1 1012 ? 15.342  38.577  81.334  1.00 28.75 ? 1010 PHE B CE2   1 
ATOM   16120 C CZ    . PHE B  1 1012 ? 15.336  38.363  82.695  1.00 26.17 ? 1010 PHE B CZ    1 
ATOM   16121 N N     . GLY B  1 1013 ? 12.951  42.107  80.909  1.00 21.80 ? 1011 GLY B N     1 
ATOM   16122 C CA    . GLY B  1 1013 ? 14.049  42.920  80.424  1.00 23.34 ? 1011 GLY B CA    1 
ATOM   16123 C C     . GLY B  1 1013 ? 14.230  44.087  81.368  1.00 27.76 ? 1011 GLY B C     1 
ATOM   16124 O O     . GLY B  1 1013 ? 13.297  44.566  82.013  1.00 25.17 ? 1011 GLY B O     1 
ATOM   16125 N N     . GLY B  1 1014 ? 15.472  44.541  81.478  1.00 29.68 ? 1012 GLY B N     1 
ATOM   16126 C CA    . GLY B  1 1014 ? 15.766  45.622  82.392  1.00 27.13 ? 1012 GLY B CA    1 
ATOM   16127 C C     . GLY B  1 1014 ? 16.293  46.875  81.728  1.00 32.81 ? 1012 GLY B C     1 
ATOM   16128 O O     . GLY B  1 1014 ? 16.096  47.090  80.528  1.00 34.08 ? 1012 GLY B O     1 
ATOM   16129 N N     . ARG B  1 1015 ? 16.969  47.705  82.518  1.00 32.80 ? 1013 ARG B N     1 
ATOM   16130 C CA    . ARG B  1 1015 ? 17.528  48.988  82.114  1.00 36.79 ? 1013 ARG B CA    1 
ATOM   16131 C C     . ARG B  1 1015 ? 19.013  49.031  82.462  1.00 34.16 ? 1013 ARG B C     1 
ATOM   16132 O O     . ARG B  1 1015 ? 19.569  48.106  83.066  1.00 33.65 ? 1013 ARG B O     1 
ATOM   16133 C CB    . ARG B  1 1015 ? 16.795  50.138  82.810  1.00 35.38 ? 1013 ARG B CB    1 
ATOM   16134 C CG    . ARG B  1 1015 ? 16.650  49.913  84.313  1.00 35.03 ? 1013 ARG B CG    1 
ATOM   16135 C CD    . ARG B  1 1015 ? 16.703  51.209  85.091  1.00 43.31 ? 1013 ARG B CD    1 
ATOM   16136 N NE    . ARG B  1 1015 ? 18.024  51.826  84.997  1.00 47.50 ? 1013 ARG B NE    1 
ATOM   16137 C CZ    . ARG B  1 1015 ? 19.054  51.530  85.782  1.00 43.86 ? 1013 ARG B CZ    1 
ATOM   16138 N NH1   . ARG B  1 1015 ? 18.956  50.628  86.748  1.00 39.67 ? 1013 ARG B NH1   1 
ATOM   16139 N NH2   . ARG B  1 1015 ? 20.216  52.151  85.588  1.00 45.86 ? 1013 ARG B NH2   1 
ATOM   16140 N N     . GLY B  1 1016 ? 19.650  50.141  82.104  1.00 33.74 ? 1014 GLY B N     1 
ATOM   16141 C CA    . GLY B  1 1016 ? 21.053  50.306  82.443  1.00 33.13 ? 1014 GLY B CA    1 
ATOM   16142 C C     . GLY B  1 1016 ? 21.905  49.289  81.714  1.00 31.44 ? 1014 GLY B C     1 
ATOM   16143 O O     . GLY B  1 1016 ? 21.730  49.044  80.516  1.00 32.88 ? 1014 GLY B O     1 
ATOM   16144 N N     . LEU B  1 1017 ? 22.842  48.679  82.445  1.00 32.15 ? 1015 LEU B N     1 
ATOM   16145 C CA    . LEU B  1 1017 ? 23.738  47.676  81.878  1.00 32.13 ? 1015 LEU B CA    1 
ATOM   16146 C C     . LEU B  1 1017 ? 23.034  46.361  81.549  1.00 30.70 ? 1015 LEU B C     1 
ATOM   16147 O O     . LEU B  1 1017 ? 23.669  45.471  80.963  1.00 28.83 ? 1015 LEU B O     1 
ATOM   16148 C CB    . LEU B  1 1017 ? 24.896  47.426  82.845  1.00 31.99 ? 1015 LEU B CB    1 
ATOM   16149 C CG    . LEU B  1 1017 ? 25.782  48.653  83.103  1.00 33.58 ? 1015 LEU B CG    1 
ATOM   16150 C CD1   . LEU B  1 1017 ? 26.744  48.404  84.263  1.00 37.81 ? 1015 LEU B CD1   1 
ATOM   16151 C CD2   . LEU B  1 1017 ? 26.539  49.043  81.842  1.00 27.96 ? 1015 LEU B CD2   1 
ATOM   16152 N N     . SER B  1 1018 ? 21.747  46.237  81.902  1.00 27.19 ? 1016 SER B N     1 
ATOM   16153 C CA    . SER B  1 1018 ? 20.969  45.021  81.698  1.00 28.58 ? 1016 SER B CA    1 
ATOM   16154 C C     . SER B  1 1018 ? 20.366  44.918  80.303  1.00 29.02 ? 1016 SER B C     1 
ATOM   16155 O O     . SER B  1 1018 ? 19.982  43.820  79.889  1.00 30.02 ? 1016 SER B O     1 
ATOM   16156 C CB    . SER B  1 1018 ? 19.843  44.933  82.744  1.00 30.10 ? 1016 SER B CB    1 
ATOM   16157 O OG    . SER B  1 1018 ? 20.364  44.558  84.015  1.00 31.20 ? 1016 SER B OG    1 
ATOM   16158 N N     . GLY B  1 1019 ? 20.245  46.015  79.578  1.00 29.59 ? 1017 GLY B N     1 
ATOM   16159 C CA    . GLY B  1 1019 ? 19.776  45.907  78.213  1.00 27.29 ? 1017 GLY B CA    1 
ATOM   16160 C C     . GLY B  1 1019 ? 19.256  47.218  77.674  1.00 29.18 ? 1017 GLY B C     1 
ATOM   16161 O O     . GLY B  1 1019 ? 19.165  48.227  78.373  1.00 27.62 ? 1017 GLY B O     1 
ATOM   16162 N N     . THR B  1 1020 ? 18.889  47.159  76.397  1.00 23.37 ? 1018 THR B N     1 
ATOM   16163 C CA    . THR B  1 1020 ? 18.283  48.272  75.689  1.00 27.61 ? 1018 THR B CA    1 
ATOM   16164 C C     . THR B  1 1020 ? 16.771  48.304  75.816  1.00 26.56 ? 1018 THR B C     1 
ATOM   16165 O O     . THR B  1 1020 ? 16.168  49.371  75.649  1.00 27.71 ? 1018 THR B O     1 
ATOM   16166 C CB    . THR B  1 1020 ? 18.633  48.189  74.203  1.00 27.02 ? 1018 THR B CB    1 
ATOM   16167 O OG1   . THR B  1 1020 ? 18.090  46.970  73.672  1.00 25.77 ? 1018 THR B OG1   1 
ATOM   16168 C CG2   . THR B  1 1020 ? 20.154  48.209  74.009  1.00 27.41 ? 1018 THR B CG2   1 
ATOM   16169 N N     . GLY B  1 1021 ? 16.142  47.168  76.089  1.00 22.68 ? 1019 GLY B N     1 
ATOM   16170 C CA    . GLY B  1 1021 ? 14.723  47.052  75.887  1.00 24.69 ? 1019 GLY B CA    1 
ATOM   16171 C C     . GLY B  1 1021 ? 14.448  47.068  74.398  1.00 24.39 ? 1019 GLY B C     1 
ATOM   16172 O O     . GLY B  1 1021 ? 15.367  47.106  73.572  1.00 22.33 ? 1019 GLY B O     1 
ATOM   16173 N N     . PRO B  1 1022 ? 13.178  46.995  74.022  1.00 21.67 ? 1020 PRO B N     1 
ATOM   16174 C CA    . PRO B  1 1022 ? 12.007  46.788  74.878  1.00 20.35 ? 1020 PRO B CA    1 
ATOM   16175 C C     . PRO B  1 1022 ? 11.963  45.384  75.460  1.00 19.05 ? 1020 PRO B C     1 
ATOM   16176 O O     . PRO B  1 1022 ? 12.723  44.504  75.054  1.00 22.37 ? 1020 PRO B O     1 
ATOM   16177 C CB    . PRO B  1 1022 ? 10.831  47.020  73.922  1.00 20.39 ? 1020 PRO B CB    1 
ATOM   16178 C CG    . PRO B  1 1022 ? 11.381  46.612  72.558  1.00 23.22 ? 1020 PRO B CG    1 
ATOM   16179 C CD    . PRO B  1 1022 ? 12.844  46.984  72.587  1.00 24.73 ? 1020 PRO B CD    1 
ATOM   16180 N N     . LYS B  1 1023 ? 11.055  45.150  76.402  1.00 20.55 ? 1021 LYS B N     1 
ATOM   16181 C CA    . LYS B  1 1023 ? 11.016  43.868  77.084  1.00 20.40 ? 1021 LYS B CA    1 
ATOM   16182 C C     . LYS B  1 1023 ? 10.603  42.754  76.138  1.00 17.88 ? 1021 LYS B C     1 
ATOM   16183 O O     . LYS B  1 1023 ? 9.644   42.895  75.372  1.00 15.51 ? 1021 LYS B O     1 
ATOM   16184 C CB    . LYS B  1 1023 ? 10.035  43.924  78.250  1.00 21.63 ? 1021 LYS B CB    1 
ATOM   16185 C CG    . LYS B  1 1023 ? 10.505  44.741  79.441  1.00 18.83 ? 1021 LYS B CG    1 
ATOM   16186 C CD    . LYS B  1 1023 ? 9.362   44.808  80.437  1.00 21.46 ? 1021 LYS B CD    1 
ATOM   16187 C CE    . LYS B  1 1023 ? 9.832   45.295  81.791  1.00 23.92 ? 1021 LYS B CE    1 
ATOM   16188 N NZ    . LYS B  1 1023 ? 10.460  44.151  82.503  1.00 19.96 ? 1021 LYS B NZ    1 
ATOM   16189 N N     . ALA B  1 1024 ? 11.315  41.630  76.223  1.00 22.19 ? 1022 ALA B N     1 
ATOM   16190 C CA    . ALA B  1 1024 ? 10.882  40.406  75.563  1.00 21.52 ? 1022 ALA B CA    1 
ATOM   16191 C C     . ALA B  1 1024 ? 9.560   39.917  76.143  1.00 22.12 ? 1022 ALA B C     1 
ATOM   16192 O O     . ALA B  1 1024 ? 9.284   40.060  77.335  1.00 18.43 ? 1022 ALA B O     1 
ATOM   16193 C CB    . ALA B  1 1024 ? 11.954  39.325  75.707  1.00 18.91 ? 1022 ALA B CB    1 
ATOM   16194 N N     . GLY B  1 1025 ? 8.715   39.346  75.293  1.00 17.03 ? 1023 GLY B N     1 
ATOM   16195 C CA    . GLY B  1 1025 ? 7.451   38.877  75.821  1.00 14.16 ? 1023 GLY B CA    1 
ATOM   16196 C C     . GLY B  1 1025 ? 6.562   39.995  76.313  1.00 15.69 ? 1023 GLY B C     1 
ATOM   16197 O O     . GLY B  1 1025 ? 5.707   39.773  77.165  1.00 16.85 ? 1023 GLY B O     1 
ATOM   16198 N N     . GLY B  1 1026 ? 6.724   41.193  75.760  1.00 16.90 ? 1024 GLY B N     1 
ATOM   16199 C CA    . GLY B  1 1026 ? 5.897   42.316  76.105  1.00 15.78 ? 1024 GLY B CA    1 
ATOM   16200 C C     . GLY B  1 1026 ? 5.432   43.010  74.842  1.00 18.72 ? 1024 GLY B C     1 
ATOM   16201 O O     . GLY B  1 1026 ? 5.875   42.691  73.731  1.00 16.74 ? 1024 GLY B O     1 
ATOM   16202 N N     . PRO B  1 1027 ? 4.558   44.003  75.007  1.00 22.04 ? 1025 PRO B N     1 
ATOM   16203 C CA    . PRO B  1 1027 ? 3.807   44.544  73.866  1.00 17.64 ? 1025 PRO B CA    1 
ATOM   16204 C C     . PRO B  1 1027 ? 4.563   45.584  73.056  1.00 18.81 ? 1025 PRO B C     1 
ATOM   16205 O O     . PRO B  1 1027 ? 4.067   45.990  71.997  1.00 17.88 ? 1025 PRO B O     1 
ATOM   16206 C CB    . PRO B  1 1027 ? 2.588   45.163  74.544  1.00 18.53 ? 1025 PRO B CB    1 
ATOM   16207 C CG    . PRO B  1 1027 ? 3.141   45.644  75.869  1.00 22.39 ? 1025 PRO B CG    1 
ATOM   16208 C CD    . PRO B  1 1027 ? 4.089   44.560  76.293  1.00 21.38 ? 1025 PRO B CD    1 
ATOM   16209 N N     . LEU B  1 1028 ? 5.727   46.046  73.517  1.00 18.87 ? 1026 LEU B N     1 
ATOM   16210 C CA    . LEU B  1 1028 ? 6.535   46.976  72.735  1.00 20.66 ? 1026 LEU B CA    1 
ATOM   16211 C C     . LEU B  1 1028 ? 7.570   46.289  71.861  1.00 18.31 ? 1026 LEU B C     1 
ATOM   16212 O O     . LEU B  1 1028 ? 8.202   46.960  71.040  1.00 20.58 ? 1026 LEU B O     1 
ATOM   16213 C CB    . LEU B  1 1028 ? 7.252   47.974  73.648  1.00 16.42 ? 1026 LEU B CB    1 
ATOM   16214 C CG    . LEU B  1 1028 ? 6.374   48.938  74.453  1.00 24.56 ? 1026 LEU B CG    1 
ATOM   16215 C CD1   . LEU B  1 1028 ? 7.241   49.875  75.285  1.00 22.39 ? 1026 LEU B CD1   1 
ATOM   16216 C CD2   . LEU B  1 1028 ? 5.497   49.741  73.514  1.00 27.07 ? 1026 LEU B CD2   1 
ATOM   16217 N N     . TYR B  1 1029 ? 7.711   44.967  71.970  1.00 16.35 ? 1027 TYR B N     1 
ATOM   16218 C CA    . TYR B  1 1029 ? 8.824   44.257  71.343  1.00 19.66 ? 1027 TYR B CA    1 
ATOM   16219 C C     . TYR B  1 1029 ? 8.778   44.342  69.824  1.00 19.76 ? 1027 TYR B C     1 
ATOM   16220 O O     . TYR B  1 1029 ? 9.770   44.711  69.181  1.00 19.81 ? 1027 TYR B O     1 
ATOM   16221 C CB    . TYR B  1 1029 ? 8.798   42.796  71.784  1.00 19.17 ? 1027 TYR B CB    1 
ATOM   16222 C CG    . TYR B  1 1029 ? 10.108  42.049  71.709  1.00 19.45 ? 1027 TYR B CG    1 
ATOM   16223 C CD1   . TYR B  1 1029 ? 11.189  42.401  72.514  1.00 19.09 ? 1027 TYR B CD1   1 
ATOM   16224 C CD2   . TYR B  1 1029 ? 10.232  40.927  70.900  1.00 20.69 ? 1027 TYR B CD2   1 
ATOM   16225 C CE1   . TYR B  1 1029 ? 12.342  41.685  72.480  1.00 20.26 ? 1027 TYR B CE1   1 
ATOM   16226 C CE2   . TYR B  1 1029 ? 11.399  40.201  70.863  1.00 18.24 ? 1027 TYR B CE2   1 
ATOM   16227 C CZ    . TYR B  1 1029 ? 12.445  40.581  71.656  1.00 24.21 ? 1027 TYR B CZ    1 
ATOM   16228 O OH    . TYR B  1 1029 ? 13.592  39.844  71.616  1.00 23.97 ? 1027 TYR B OH    1 
ATOM   16229 N N     . LEU B  1 1030 ? 7.639   43.967  69.232  1.00 18.94 ? 1028 LEU B N     1 
ATOM   16230 C CA    . LEU B  1 1030 ? 7.546   43.905  67.775  1.00 21.74 ? 1028 LEU B CA    1 
ATOM   16231 C C     . LEU B  1 1030 ? 7.773   45.266  67.129  1.00 21.78 ? 1028 LEU B C     1 
ATOM   16232 O O     . LEU B  1 1030 ? 8.269   45.339  65.998  1.00 20.72 ? 1028 LEU B O     1 
ATOM   16233 C CB    . LEU B  1 1030 ? 6.186   43.345  67.355  1.00 20.51 ? 1028 LEU B CB    1 
ATOM   16234 C CG    . LEU B  1 1030 ? 5.918   41.887  67.761  1.00 20.32 ? 1028 LEU B CG    1 
ATOM   16235 C CD1   . LEU B  1 1030 ? 4.559   41.431  67.190  1.00 20.25 ? 1028 LEU B CD1   1 
ATOM   16236 C CD2   . LEU B  1 1030 ? 7.056   40.967  67.295  1.00 21.33 ? 1028 LEU B CD2   1 
ATOM   16237 N N     . GLY B  1 1031 ? 7.420   46.350  67.818  1.00 22.65 ? 1029 GLY B N     1 
ATOM   16238 C CA    . GLY B  1 1031 ? 7.567   47.671  67.218  1.00 21.21 ? 1029 GLY B CA    1 
ATOM   16239 C C     . GLY B  1 1031 ? 9.002   48.060  66.926  1.00 22.85 ? 1029 GLY B C     1 
ATOM   16240 O O     . GLY B  1 1031 ? 9.246   48.949  66.105  1.00 22.82 ? 1029 GLY B O     1 
ATOM   16241 N N     . ARG B  1 1032 ? 9.959   47.434  67.595  1.00 20.76 ? 1030 ARG B N     1 
ATOM   16242 C CA    . ARG B  1 1032 ? 11.353  47.732  67.341  1.00 22.24 ? 1030 ARG B CA    1 
ATOM   16243 C C     . ARG B  1 1032 ? 11.852  47.071  66.065  1.00 22.89 ? 1030 ARG B C     1 
ATOM   16244 O O     . ARG B  1 1032 ? 12.903  47.458  65.546  1.00 25.81 ? 1030 ARG B O     1 
ATOM   16245 C CB    . ARG B  1 1032 ? 12.192  47.290  68.543  1.00 23.71 ? 1030 ARG B CB    1 
ATOM   16246 C CG    . ARG B  1 1032 ? 13.605  47.768  68.502  1.00 27.16 ? 1030 ARG B CG    1 
ATOM   16247 C CD    . ARG B  1 1032 ? 13.701  49.226  68.897  1.00 30.79 ? 1030 ARG B CD    1 
ATOM   16248 N NE    . ARG B  1 1032 ? 15.093  49.568  69.145  1.00 31.52 ? 1030 ARG B NE    1 
ATOM   16249 C CZ    . ARG B  1 1032 ? 15.825  50.351  68.365  1.00 35.09 ? 1030 ARG B CZ    1 
ATOM   16250 N NH1   . ARG B  1 1032 ? 15.298  50.979  67.325  1.00 35.00 ? 1030 ARG B NH1   1 
ATOM   16251 N NH2   . ARG B  1 1032 ? 17.117  50.508  68.636  1.00 32.13 ? 1030 ARG B NH2   1 
ATOM   16252 N N     . LEU B  1 1033 ? 11.088  46.121  65.531  1.00 20.03 ? 1031 LEU B N     1 
ATOM   16253 C CA    . LEU B  1 1033 ? 11.480  45.300  64.395  1.00 23.15 ? 1031 LEU B CA    1 
ATOM   16254 C C     . LEU B  1 1033 ? 10.810  45.730  63.095  1.00 22.45 ? 1031 LEU B C     1 
ATOM   16255 O O     . LEU B  1 1033 ? 10.821  44.965  62.122  1.00 21.43 ? 1031 LEU B O     1 
ATOM   16256 C CB    . LEU B  1 1033 ? 11.150  43.836  64.696  1.00 20.37 ? 1031 LEU B CB    1 
ATOM   16257 C CG    . LEU B  1 1033 ? 11.876  43.392  65.970  1.00 21.85 ? 1031 LEU B CG    1 
ATOM   16258 C CD1   . LEU B  1 1033 ? 11.438  42.006  66.427  1.00 23.55 ? 1031 LEU B CD1   1 
ATOM   16259 C CD2   . LEU B  1 1033 ? 13.397  43.446  65.790  1.00 27.13 ? 1031 LEU B CD2   1 
ATOM   16260 N N     . VAL B  1 1034 ? 10.178  46.902  63.078  1.00 20.89 ? 1032 VAL B N     1 
ATOM   16261 C CA    . VAL B  1 1034 ? 9.571   47.464  61.877  1.00 23.09 ? 1032 VAL B CA    1 
ATOM   16262 C C     . VAL B  1 1034 ? 10.045  48.905  61.768  1.00 26.16 ? 1032 VAL B C     1 
ATOM   16263 O O     . VAL B  1 1034 ? 10.570  49.477  62.720  1.00 23.02 ? 1032 VAL B O     1 
ATOM   16264 C CB    . VAL B  1 1034 ? 8.027   47.399  61.893  1.00 22.25 ? 1032 VAL B CB    1 
ATOM   16265 C CG1   . VAL B  1 1034 ? 7.553   45.957  61.692  1.00 24.62 ? 1032 VAL B CG1   1 
ATOM   16266 C CG2   . VAL B  1 1034 ? 7.478   47.995  63.185  1.00 21.10 ? 1032 VAL B CG2   1 
ATOM   16267 N N     . THR B  1 1035 ? 9.888   49.492  60.581  1.00 25.31 ? 1033 THR B N     1 
ATOM   16268 C CA    . THR B  1 1035 ? 10.370  50.859  60.413  1.00 27.36 ? 1033 THR B CA    1 
ATOM   16269 C C     . THR B  1 1035 ? 9.392   51.886  60.978  1.00 30.26 ? 1033 THR B C     1 
ATOM   16270 O O     . THR B  1 1035 ? 9.814   52.983  61.360  1.00 34.44 ? 1033 THR B O     1 
ATOM   16271 C CB    . THR B  1 1035 ? 10.655  51.150  58.938  1.00 29.27 ? 1033 THR B CB    1 
ATOM   16272 O OG1   . THR B  1 1035 ? 9.616   50.592  58.130  1.00 30.96 ? 1033 THR B OG1   1 
ATOM   16273 C CG2   . THR B  1 1035 ? 11.999  50.553  58.523  1.00 32.79 ? 1033 THR B CG2   1 
ATOM   16274 N N     . THR B  1 1036 ? 8.102   51.553  61.039  1.00 26.76 ? 1034 THR B N     1 
ATOM   16275 C CA    . THR B  1 1036 ? 7.086   52.381  61.682  1.00 30.61 ? 1034 THR B CA    1 
ATOM   16276 C C     . THR B  1 1036 ? 6.395   51.543  62.743  1.00 26.43 ? 1034 THR B C     1 
ATOM   16277 O O     . THR B  1 1036 ? 5.711   50.570  62.416  1.00 24.47 ? 1034 THR B O     1 
ATOM   16278 C CB    . THR B  1 1036 ? 6.046   52.890  60.685  1.00 26.94 ? 1034 THR B CB    1 
ATOM   16279 O OG1   . THR B  1 1036 ? 6.702   53.518  59.582  1.00 35.84 ? 1034 THR B OG1   1 
ATOM   16280 C CG2   . THR B  1 1036 ? 5.121   53.887  61.363  1.00 31.95 ? 1034 THR B CG2   1 
ATOM   16281 N N     . ALA B  1 1037 ? 6.558   51.919  63.980  1.00 24.40 ? 1035 ALA B N     1 
ATOM   16282 C CA    . ALA B  1 1037 ? 6.026   51.081  65.038  1.00 25.19 ? 1035 ALA B CA    1 
ATOM   16283 C C     . ALA B  1 1037 ? 4.509   51.261  65.151  1.00 27.60 ? 1035 ALA B C     1 
ATOM   16284 O O     . ALA B  1 1037 ? 3.999   52.370  64.985  1.00 23.94 ? 1035 ALA B O     1 
ATOM   16285 C CB    . ALA B  1 1037 ? 6.706   51.415  66.367  1.00 23.37 ? 1035 ALA B CB    1 
ATOM   16286 N N     . PRO B  1 1038 ? 3.768   50.190  65.405  1.00 22.55 ? 1036 PRO B N     1 
ATOM   16287 C CA    . PRO B  1 1038 ? 2.326   50.318  65.641  1.00 24.80 ? 1036 PRO B CA    1 
ATOM   16288 C C     . PRO B  1 1038 ? 2.041   50.750  67.074  1.00 23.58 ? 1036 PRO B C     1 
ATOM   16289 O O     . PRO B  1 1038 ? 2.925   50.818  67.931  1.00 21.00 ? 1036 PRO B O     1 
ATOM   16290 C CB    . PRO B  1 1038 ? 1.793   48.904  65.382  1.00 22.83 ? 1036 PRO B CB    1 
ATOM   16291 C CG    . PRO B  1 1038 ? 2.930   48.015  65.807  1.00 22.32 ? 1036 PRO B CG    1 
ATOM   16292 C CD    . PRO B  1 1038 ? 4.208   48.779  65.402  1.00 24.65 ? 1036 PRO B CD    1 
ATOM   16293 N N     . VAL B  1 1039 ? 0.771   51.036  67.317  1.00 27.64 ? 1037 VAL B N     1 
ATOM   16294 C CA    . VAL B  1 1039 ? 0.262   51.275  68.664  1.00 23.51 ? 1037 VAL B CA    1 
ATOM   16295 C C     . VAL B  1 1039 ? -0.014  49.922  69.306  1.00 21.19 ? 1037 VAL B C     1 
ATOM   16296 O O     . VAL B  1 1039 ? -0.879  49.175  68.831  1.00 20.18 ? 1037 VAL B O     1 
ATOM   16297 C CB    . VAL B  1 1039 ? -0.996  52.150  68.622  1.00 25.83 ? 1037 VAL B CB    1 
ATOM   16298 C CG1   . VAL B  1 1039 ? -1.477  52.446  70.053  1.00 24.15 ? 1037 VAL B CG1   1 
ATOM   16299 C CG2   . VAL B  1 1039 ? -0.678  53.435  67.859  1.00 24.93 ? 1037 VAL B CG2   1 
ATOM   16300 N N     . PRO B  1 1040 ? 0.684   49.558  70.374  1.00 20.70 ? 1038 PRO B N     1 
ATOM   16301 C CA    . PRO B  1 1040 ? 0.445   48.251  71.007  1.00 22.72 ? 1038 PRO B CA    1 
ATOM   16302 C C     . PRO B  1 1040 ? -0.952  48.163  71.593  1.00 21.32 ? 1038 PRO B C     1 
ATOM   16303 O O     . PRO B  1 1040 ? -1.588  49.194  71.862  1.00 23.77 ? 1038 PRO B O     1 
ATOM   16304 C CB    . PRO B  1 1040 ? 1.509   48.192  72.121  1.00 19.40 ? 1038 PRO B CB    1 
ATOM   16305 C CG    . PRO B  1 1040 ? 2.510   49.199  71.752  1.00 20.86 ? 1038 PRO B CG    1 
ATOM   16306 C CD    . PRO B  1 1040 ? 1.802   50.283  70.989  1.00 21.55 ? 1038 PRO B CD    1 
ATOM   16307 N N     . PRO B  1 1041 ? -1.455  46.948  71.834  1.00 22.58 ? 1039 PRO B N     1 
ATOM   16308 C CA    . PRO B  1 1041 ? -2.710  46.806  72.578  1.00 21.30 ? 1039 PRO B CA    1 
ATOM   16309 C C     . PRO B  1 1041 ? -2.610  47.467  73.943  1.00 22.89 ? 1039 PRO B C     1 
ATOM   16310 O O     . PRO B  1 1041 ? -1.593  47.354  74.637  1.00 24.79 ? 1039 PRO B O     1 
ATOM   16311 C CB    . PRO B  1 1041 ? -2.886  45.288  72.702  1.00 26.21 ? 1039 PRO B CB    1 
ATOM   16312 C CG    . PRO B  1 1041 ? -1.995  44.706  71.661  1.00 22.98 ? 1039 PRO B CG    1 
ATOM   16313 C CD    . PRO B  1 1041 ? -0.845  45.646  71.523  1.00 22.54 ? 1039 PRO B CD    1 
ATOM   16314 N N     . GLN B  1 1042 ? -3.667  48.192  74.303  1.00 22.74 ? 1040 GLN B N     1 
ATOM   16315 C CA    . GLN B  1 1042 ? -3.815  48.789  75.628  1.00 26.28 ? 1040 GLN B CA    1 
ATOM   16316 C C     . GLN B  1 1042 ? -2.744  49.833  75.931  1.00 24.38 ? 1040 GLN B C     1 
ATOM   16317 O O     . GLN B  1 1042 ? -2.530  50.197  77.094  1.00 22.93 ? 1040 GLN B O     1 
ATOM   16318 C CB    . GLN B  1 1042 ? -3.808  47.704  76.716  1.00 28.62 ? 1040 GLN B CB    1 
ATOM   16319 C CG    . GLN B  1 1042 ? -5.018  46.788  76.688  1.00 25.80 ? 1040 GLN B CG    1 
ATOM   16320 C CD    . GLN B  1 1042 ? -4.945  45.730  77.762  1.00 37.11 ? 1040 GLN B CD    1 
ATOM   16321 O OE1   . GLN B  1 1042 ? -4.262  44.726  77.605  1.00 39.29 ? 1040 GLN B OE1   1 
ATOM   16322 N NE2   . GLN B  1 1042 ? -5.632  45.962  78.869  1.00 39.44 ? 1040 GLN B NE2   1 
ATOM   16323 N N     . HIS B  1 1043 ? -2.063  50.339  74.921  1.00 18.88 ? 1041 HIS B N     1 
ATOM   16324 C CA    . HIS B  1 1043 ? -0.917  51.224  75.117  1.00 21.64 ? 1041 HIS B CA    1 
ATOM   16325 C C     . HIS B  1 1043 ? -1.377  52.679  75.033  1.00 24.01 ? 1041 HIS B C     1 
ATOM   16326 O O     . HIS B  1 1043 ? -1.375  53.287  73.961  1.00 24.22 ? 1041 HIS B O     1 
ATOM   16327 C CB    . HIS B  1 1043 ? 0.149   50.917  74.074  1.00 21.29 ? 1041 HIS B CB    1 
ATOM   16328 C CG    . HIS B  1 1043 ? 1.360   51.783  74.176  1.00 20.54 ? 1041 HIS B CG    1 
ATOM   16329 N ND1   . HIS B  1 1043 ? 2.446   51.448  74.955  1.00 22.28 ? 1041 HIS B ND1   1 
ATOM   16330 C CD2   . HIS B  1 1043 ? 1.658   52.975  73.603  1.00 24.16 ? 1041 HIS B CD2   1 
ATOM   16331 C CE1   . HIS B  1 1043 ? 3.364   52.392  74.853  1.00 25.00 ? 1041 HIS B CE1   1 
ATOM   16332 N NE2   . HIS B  1 1043 ? 2.911   53.329  74.040  1.00 21.87 ? 1041 HIS B NE2   1 
ATOM   16333 N N     . SER B  1 1044 ? -1.763  53.242  76.175  1.00 21.88 ? 1042 SER B N     1 
ATOM   16334 C CA    . SER B  1 1044 ? -2.192  54.634  76.234  1.00 20.54 ? 1042 SER B CA    1 
ATOM   16335 C C     . SER B  1 1044 ? -2.164  55.071  77.687  1.00 23.28 ? 1042 SER B C     1 
ATOM   16336 O O     . SER B  1 1044 ? -2.011  54.253  78.593  1.00 21.89 ? 1042 SER B O     1 
ATOM   16337 C CB    . SER B  1 1044 ? -3.602  54.818  75.653  1.00 20.90 ? 1042 SER B CB    1 
ATOM   16338 O OG    . SER B  1 1044 ? -4.577  54.294  76.536  1.00 20.43 ? 1042 SER B OG    1 
ATOM   16339 N N     . SER B  1 1045 ? -2.343  56.371  77.902  1.00 21.16 ? 1043 SER B N     1 
ATOM   16340 C CA    . SER B  1 1045 ? -2.392  56.899  79.258  1.00 21.81 ? 1043 SER B CA    1 
ATOM   16341 C C     . SER B  1 1045 ? -3.201  58.186  79.274  1.00 21.52 ? 1043 SER B C     1 
ATOM   16342 O O     . SER B  1 1045 ? -3.128  58.976  78.329  1.00 22.81 ? 1043 SER B O     1 
ATOM   16343 C CB    . SER B  1 1045 ? -0.978  57.151  79.795  1.00 23.19 ? 1043 SER B CB    1 
ATOM   16344 O OG    . SER B  1 1045 ? -1.041  57.830  81.032  1.00 23.07 ? 1043 SER B OG    1 
ATOM   16345 N N     . VAL B  1 1046 ? -3.980  58.397  80.347  1.00 19.11 ? 1044 VAL B N     1 
ATOM   16346 C CA    . VAL B  1 1046 ? -4.731  59.647  80.481  1.00 22.66 ? 1044 VAL B CA    1 
ATOM   16347 C C     . VAL B  1 1046 ? -3.921  60.741  81.159  1.00 23.08 ? 1044 VAL B C     1 
ATOM   16348 O O     . VAL B  1 1046 ? -4.394  61.885  81.245  1.00 24.01 ? 1044 VAL B O     1 
ATOM   16349 C CB    . VAL B  1 1046 ? -6.060  59.454  81.251  1.00 25.06 ? 1044 VAL B CB    1 
ATOM   16350 C CG1   . VAL B  1 1046 ? -6.961  58.483  80.517  1.00 27.21 ? 1044 VAL B CG1   1 
ATOM   16351 C CG2   . VAL B  1 1046 ? -5.794  58.963  82.651  1.00 22.20 ? 1044 VAL B CG2   1 
ATOM   16352 N N     . HIS B  1 1047 ? -2.716  60.431  81.634  1.00 22.72 ? 1045 HIS B N     1 
ATOM   16353 C CA    . HIS B  1 1047 ? -1.843  61.410  82.274  1.00 24.95 ? 1045 HIS B CA    1 
ATOM   16354 C C     . HIS B  1 1047 ? -1.107  62.252  81.235  1.00 24.14 ? 1045 HIS B C     1 
ATOM   16355 O O     . HIS B  1 1047 ? -0.624  61.743  80.215  1.00 24.79 ? 1045 HIS B O     1 
ATOM   16356 C CB    . HIS B  1 1047 ? -0.836  60.683  83.178  1.00 24.61 ? 1045 HIS B CB    1 
ATOM   16357 C CG    . HIS B  1 1047 ? 0.358   61.503  83.591  1.00 30.13 ? 1045 HIS B CG    1 
ATOM   16358 N ND1   . HIS B  1 1047 ? 0.304   62.464  84.580  1.00 29.59 ? 1045 HIS B ND1   1 
ATOM   16359 C CD2   . HIS B  1 1047 ? 1.653   61.468  83.174  1.00 28.80 ? 1045 HIS B CD2   1 
ATOM   16360 C CE1   . HIS B  1 1047 ? 1.504   63.000  84.740  1.00 28.69 ? 1045 HIS B CE1   1 
ATOM   16361 N NE2   . HIS B  1 1047 ? 2.340   62.416  83.897  1.00 24.81 ? 1045 HIS B NE2   1 
ATOM   16362 N N     . THR B  1 1048 ? -1.010  63.546  81.509  1.00 20.27 ? 1046 THR B N     1 
ATOM   16363 C CA    . THR B  1 1048 ? -0.223  64.462  80.700  1.00 21.63 ? 1046 THR B CA    1 
ATOM   16364 C C     . THR B  1 1048 ? 0.901   65.015  81.564  1.00 21.68 ? 1046 THR B C     1 
ATOM   16365 O O     . THR B  1 1048 ? 0.642   65.547  82.643  1.00 23.95 ? 1046 THR B O     1 
ATOM   16366 C CB    . THR B  1 1048 ? -1.080  65.601  80.164  1.00 27.75 ? 1046 THR B CB    1 
ATOM   16367 O OG1   . THR B  1 1048 ? -2.234  65.060  79.508  1.00 25.39 ? 1046 THR B OG1   1 
ATOM   16368 C CG2   . THR B  1 1048 ? -0.275  66.447  79.173  1.00 26.59 ? 1046 THR B CG2   1 
ATOM   16369 N N     . ASP B  1 1049 ? 2.127   64.898  81.089  1.00 21.34 ? 1047 ASP B N     1 
ATOM   16370 C CA    . ASP B  1 1049 ? 3.257   65.373  81.870  1.00 18.42 ? 1047 ASP B CA    1 
ATOM   16371 C C     . ASP B  1 1049 ? 3.136   66.879  82.085  1.00 20.55 ? 1047 ASP B C     1 
ATOM   16372 O O     . ASP B  1 1049 ? 2.913   67.626  81.120  1.00 22.56 ? 1047 ASP B O     1 
ATOM   16373 C CB    . ASP B  1 1049 ? 4.573   65.029  81.182  1.00 22.42 ? 1047 ASP B CB    1 
ATOM   16374 C CG    . ASP B  1 1049 ? 5.771   65.502  81.983  1.00 23.32 ? 1047 ASP B CG    1 
ATOM   16375 O OD1   . ASP B  1 1049 ? 6.111   66.694  81.848  1.00 23.28 ? 1047 ASP B OD1   1 
ATOM   16376 O OD2   . ASP B  1 1049 ? 6.301   64.718  82.794  1.00 26.37 ? 1047 ASP B OD2   1 
ATOM   16377 N N     . PRO B  1 1050 ? 3.251   67.369  83.323  1.00 21.75 ? 1048 PRO B N     1 
ATOM   16378 C CA    . PRO B  1 1050 ? 2.981   68.800  83.546  1.00 26.71 ? 1048 PRO B CA    1 
ATOM   16379 C C     . PRO B  1 1050 ? 4.080   69.714  83.020  1.00 24.87 ? 1048 PRO B C     1 
ATOM   16380 O O     . PRO B  1 1050 ? 3.794   70.863  82.657  1.00 27.05 ? 1048 PRO B O     1 
ATOM   16381 C CB    . PRO B  1 1050 ? 2.833   68.897  85.071  1.00 27.06 ? 1048 PRO B CB    1 
ATOM   16382 C CG    . PRO B  1 1050 ? 3.598   67.723  85.607  1.00 24.85 ? 1048 PRO B CG    1 
ATOM   16383 C CD    . PRO B  1 1050 ? 3.406   66.625  84.583  1.00 23.65 ? 1048 PRO B CD    1 
ATOM   16384 N N     . VAL B  1 1051 ? 5.328   69.245  82.975  1.00 25.54 ? 1049 VAL B N     1 
ATOM   16385 C CA    . VAL B  1 1051 ? 6.399   70.055  82.403  1.00 25.73 ? 1049 VAL B CA    1 
ATOM   16386 C C     . VAL B  1 1051 ? 6.246   70.154  80.892  1.00 23.58 ? 1049 VAL B C     1 
ATOM   16387 O O     . VAL B  1 1051 ? 6.479   71.216  80.301  1.00 27.26 ? 1049 VAL B O     1 
ATOM   16388 C CB    . VAL B  1 1051 ? 7.768   69.492  82.811  1.00 27.34 ? 1049 VAL B CB    1 
ATOM   16389 C CG1   . VAL B  1 1051 ? 8.867   70.368  82.255  1.00 26.87 ? 1049 VAL B CG1   1 
ATOM   16390 C CG2   . VAL B  1 1051 ? 7.856   69.415  84.323  1.00 24.37 ? 1049 VAL B CG2   1 
ATOM   16391 N N     . LEU B  1 1052 ? 5.815   69.069  80.242  1.00 22.25 ? 1050 LEU B N     1 
ATOM   16392 C CA    . LEU B  1 1052 ? 5.415   69.166  78.835  1.00 21.46 ? 1050 LEU B CA    1 
ATOM   16393 C C     . LEU B  1 1052 ? 4.377   70.268  78.635  1.00 26.10 ? 1050 LEU B C     1 
ATOM   16394 O O     . LEU B  1 1052 ? 4.491   71.098  77.720  1.00 22.74 ? 1050 LEU B O     1 
ATOM   16395 C CB    . LEU B  1 1052 ? 4.885   67.805  78.353  1.00 23.14 ? 1050 LEU B CB    1 
ATOM   16396 C CG    . LEU B  1 1052 ? 4.392   67.589  76.902  1.00 22.09 ? 1050 LEU B CG    1 
ATOM   16397 C CD1   . LEU B  1 1052 ? 2.971   68.137  76.648  1.00 21.34 ? 1050 LEU B CD1   1 
ATOM   16398 C CD2   . LEU B  1 1052 ? 5.394   68.140  75.867  1.00 20.68 ? 1050 LEU B CD2   1 
ATOM   16399 N N     . LEU B  1 1053 ? 3.349   70.294  79.489  1.00 26.08 ? 1051 LEU B N     1 
ATOM   16400 C CA    . LEU B  1 1053 ? 2.320   71.319  79.368  1.00 28.44 ? 1051 LEU B CA    1 
ATOM   16401 C C     . LEU B  1 1053 ? 2.910   72.716  79.542  1.00 27.58 ? 1051 LEU B C     1 
ATOM   16402 O O     . LEU B  1 1053 ? 2.520   73.650  78.836  1.00 28.72 ? 1051 LEU B O     1 
ATOM   16403 C CB    . LEU B  1 1053 ? 1.199   71.064  80.386  1.00 29.36 ? 1051 LEU B CB    1 
ATOM   16404 C CG    . LEU B  1 1053 ? 0.258   69.879  80.087  1.00 30.24 ? 1051 LEU B CG    1 
ATOM   16405 C CD1   . LEU B  1 1053 ? -0.670  69.578  81.257  1.00 32.57 ? 1051 LEU B CD1   1 
ATOM   16406 C CD2   . LEU B  1 1053 ? -0.564  70.140  78.843  1.00 29.49 ? 1051 LEU B CD2   1 
ATOM   16407 N N     . ASP B  1 1054 ? 3.853   72.876  80.472  1.00 30.65 ? 1052 ASP B N     1 
ATOM   16408 C CA    . ASP B  1 1054 ? 4.480   74.183  80.660  1.00 33.40 ? 1052 ASP B CA    1 
ATOM   16409 C C     . ASP B  1 1054 ? 5.301   74.577  79.439  1.00 30.27 ? 1052 ASP B C     1 
ATOM   16410 O O     . ASP B  1 1054 ? 5.309   75.749  79.037  1.00 31.86 ? 1052 ASP B O     1 
ATOM   16411 C CB    . ASP B  1 1054 ? 5.354   74.172  81.911  1.00 29.05 ? 1052 ASP B CB    1 
ATOM   16412 C CG    . ASP B  1 1054 ? 4.542   74.172  83.194  1.00 33.31 ? 1052 ASP B CG    1 
ATOM   16413 O OD1   . ASP B  1 1054 ? 3.318   74.389  83.117  1.00 29.10 ? 1052 ASP B OD1   1 
ATOM   16414 O OD2   . ASP B  1 1054 ? 5.124   73.956  84.279  1.00 35.18 ? 1052 ASP B OD2   1 
ATOM   16415 N N     . PHE B  1 1055 ? 5.970   73.600  78.820  1.00 26.85 ? 1053 PHE B N     1 
ATOM   16416 C CA    . PHE B  1 1055 ? 6.746   73.856  77.611  1.00 27.79 ? 1053 PHE B CA    1 
ATOM   16417 C C     . PHE B  1 1055 ? 5.849   74.286  76.460  1.00 28.79 ? 1053 PHE B C     1 
ATOM   16418 O O     . PHE B  1 1055 ? 6.198   75.199  75.704  1.00 26.47 ? 1053 PHE B O     1 
ATOM   16419 C CB    . PHE B  1 1055 ? 7.539   72.603  77.241  1.00 23.77 ? 1053 PHE B CB    1 
ATOM   16420 C CG    . PHE B  1 1055 ? 8.448   72.762  76.047  1.00 25.65 ? 1053 PHE B CG    1 
ATOM   16421 C CD1   . PHE B  1 1055 ? 9.396   73.768  76.003  1.00 28.13 ? 1053 PHE B CD1   1 
ATOM   16422 C CD2   . PHE B  1 1055 ? 8.389   71.861  74.990  1.00 26.20 ? 1053 PHE B CD2   1 
ATOM   16423 C CE1   . PHE B  1 1055 ? 10.242  73.898  74.903  1.00 30.95 ? 1053 PHE B CE1   1 
ATOM   16424 C CE2   . PHE B  1 1055 ? 9.241   71.982  73.893  1.00 24.58 ? 1053 PHE B CE2   1 
ATOM   16425 C CZ    . PHE B  1 1055 ? 10.164  73.004  73.854  1.00 25.50 ? 1053 PHE B CZ    1 
ATOM   16426 N N     . ALA B  1 1056 ? 4.680   73.650  76.317  1.00 27.58 ? 1054 ALA B N     1 
ATOM   16427 C CA    . ALA B  1 1056 ? 3.761   74.031  75.242  1.00 28.41 ? 1054 ALA B CA    1 
ATOM   16428 C C     . ALA B  1 1056 ? 3.243   75.454  75.416  1.00 30.48 ? 1054 ALA B C     1 
ATOM   16429 O O     . ALA B  1 1056 ? 3.064   76.177  74.427  1.00 32.88 ? 1054 ALA B O     1 
ATOM   16430 C CB    . ALA B  1 1056 ? 2.591   73.051  75.159  1.00 28.21 ? 1054 ALA B CB    1 
ATOM   16431 N N     . LYS B  1 1057 ? 2.968   75.870  76.655  1.00 29.18 ? 1055 LYS B N     1 
ATOM   16432 C CA    . LYS B  1 1057 ? 2.519   77.245  76.861  1.00 33.83 ? 1055 LYS B CA    1 
ATOM   16433 C C     . LYS B  1 1057 ? 3.630   78.233  76.544  1.00 35.96 ? 1055 LYS B C     1 
ATOM   16434 O O     . LYS B  1 1057 ? 3.384   79.280  75.930  1.00 33.98 ? 1055 LYS B O     1 
ATOM   16435 C CB    . LYS B  1 1057 ? 2.030   77.448  78.291  1.00 36.05 ? 1055 LYS B CB    1 
ATOM   16436 C CG    . LYS B  1 1057 ? 0.624   76.957  78.538  1.00 35.48 ? 1055 LYS B CG    1 
ATOM   16437 C CD    . LYS B  1 1057 ? 0.225   77.210  79.971  1.00 35.35 ? 1055 LYS B CD    1 
ATOM   16438 C CE    . LYS B  1 1057 ? 1.212   76.558  80.910  1.00 34.55 ? 1055 LYS B CE    1 
ATOM   16439 N NZ    . LYS B  1 1057 ? 0.719   76.617  82.310  1.00 37.35 ? 1055 LYS B NZ    1 
ATOM   16440 N N     . TRP B  1 1058 ? 4.856   77.918  76.974  1.00 34.34 ? 1056 TRP B N     1 
ATOM   16441 C CA    . TRP B  1 1058 ? 6.011   78.741  76.630  1.00 35.29 ? 1056 TRP B CA    1 
ATOM   16442 C C     . TRP B  1 1058 ? 6.167   78.852  75.118  1.00 36.46 ? 1056 TRP B C     1 
ATOM   16443 O O     . TRP B  1 1058 ? 6.393   79.947  74.590  1.00 35.45 ? 1056 TRP B O     1 
ATOM   16444 C CB    . TRP B  1 1058 ? 7.265   78.146  77.277  1.00 37.23 ? 1056 TRP B CB    1 
ATOM   16445 C CG    . TRP B  1 1058 ? 8.546   78.865  76.982  1.00 39.59 ? 1056 TRP B CG    1 
ATOM   16446 C CD1   . TRP B  1 1058 ? 9.013   79.991  77.594  1.00 38.50 ? 1056 TRP B CD1   1 
ATOM   16447 C CD2   . TRP B  1 1058 ? 9.533   78.494  76.011  1.00 36.24 ? 1056 TRP B CD2   1 
ATOM   16448 N NE1   . TRP B  1 1058 ? 10.233  80.347  77.066  1.00 40.29 ? 1056 TRP B NE1   1 
ATOM   16449 C CE2   . TRP B  1 1058 ? 10.573  79.447  76.088  1.00 40.69 ? 1056 TRP B CE2   1 
ATOM   16450 C CE3   . TRP B  1 1058 ? 9.637   77.458  75.080  1.00 36.70 ? 1056 TRP B CE3   1 
ATOM   16451 C CZ2   . TRP B  1 1058 ? 11.703  79.391  75.272  1.00 35.97 ? 1056 TRP B CZ2   1 
ATOM   16452 C CZ3   . TRP B  1 1058 ? 10.772  77.402  74.269  1.00 39.97 ? 1056 TRP B CZ3   1 
ATOM   16453 C CH2   . TRP B  1 1058 ? 11.787  78.364  74.376  1.00 33.52 ? 1056 TRP B CH2   1 
ATOM   16454 N N     . LEU B  1 1059 ? 6.007   77.734  74.400  1.00 33.06 ? 1057 LEU B N     1 
ATOM   16455 C CA    . LEU B  1 1059 ? 6.108   77.775  72.944  1.00 34.65 ? 1057 LEU B CA    1 
ATOM   16456 C C     . LEU B  1 1059 ? 5.029   78.660  72.332  1.00 39.27 ? 1057 LEU B C     1 
ATOM   16457 O O     . LEU B  1 1059 ? 5.286   79.379  71.359  1.00 36.67 ? 1057 LEU B O     1 
ATOM   16458 C CB    . LEU B  1 1059 ? 6.019   76.366  72.363  1.00 32.98 ? 1057 LEU B CB    1 
ATOM   16459 C CG    . LEU B  1 1059 ? 7.237   75.474  72.608  1.00 32.66 ? 1057 LEU B CG    1 
ATOM   16460 C CD1   . LEU B  1 1059 ? 6.932   74.079  72.118  1.00 27.53 ? 1057 LEU B CD1   1 
ATOM   16461 C CD2   . LEU B  1 1059 ? 8.458   76.042  71.898  1.00 30.13 ? 1057 LEU B CD2   1 
ATOM   16462 N N     . ASP B  1 1060 ? 3.808   78.608  72.872  1.00 34.44 ? 1058 ASP B N     1 
ATOM   16463 C CA    . ASP B  1 1060 ? 2.752   79.475  72.352  1.00 39.26 ? 1058 ASP B CA    1 
ATOM   16464 C C     . ASP B  1 1060 ? 3.017   80.938  72.685  1.00 37.43 ? 1058 ASP B C     1 
ATOM   16465 O O     . ASP B  1 1060 ? 2.642   81.825  71.910  1.00 42.45 ? 1058 ASP B O     1 
ATOM   16466 C CB    . ASP B  1 1060 ? 1.389   79.055  72.897  1.00 40.59 ? 1058 ASP B CB    1 
ATOM   16467 C CG    . ASP B  1 1060 ? 0.675   78.071  71.991  1.00 41.39 ? 1058 ASP B CG    1 
ATOM   16468 O OD1   . ASP B  1 1060 ? 0.706   78.254  70.747  1.00 47.11 ? 1058 ASP B OD1   1 
ATOM   16469 O OD2   . ASP B  1 1060 ? 0.085   77.110  72.525  1.00 40.53 ? 1058 ASP B OD2   1 
ATOM   16470 N N     . GLY B  1 1061 ? 3.642   81.211  73.829  1.00 39.60 ? 1059 GLY B N     1 
ATOM   16471 C CA    . GLY B  1 1061 ? 4.055   82.574  74.123  1.00 38.28 ? 1059 GLY B CA    1 
ATOM   16472 C C     . GLY B  1 1061 ? 5.084   83.093  73.139  1.00 44.46 ? 1059 GLY B C     1 
ATOM   16473 O O     . GLY B  1 1061 ? 5.151   84.296  72.880  1.00 49.56 ? 1059 GLY B O     1 
ATOM   16474 N N     . LYS B  1 1062 ? 5.896   82.196  72.574  1.00 44.14 ? 1060 LYS B N     1 
ATOM   16475 C CA    . LYS B  1 1062 ? 6.869   82.570  71.559  1.00 45.24 ? 1060 LYS B CA    1 
ATOM   16476 C C     . LYS B  1 1062 ? 6.257   82.699  70.176  1.00 45.56 ? 1060 LYS B C     1 
ATOM   16477 O O     . LYS B  1 1062 ? 6.898   83.260  69.282  1.00 50.63 ? 1060 LYS B O     1 
ATOM   16478 C CB    . LYS B  1 1062 ? 7.984   81.533  71.481  1.00 45.82 ? 1060 LYS B CB    1 
ATOM   16479 C CG    . LYS B  1 1062 ? 8.962   81.548  72.610  1.00 45.06 ? 1060 LYS B CG    1 
ATOM   16480 C CD    . LYS B  1 1062 ? 9.972   80.448  72.370  1.00 45.34 ? 1060 LYS B CD    1 
ATOM   16481 C CE    . LYS B  1 1062 ? 10.582  80.559  70.981  1.00 44.17 ? 1060 LYS B CE    1 
ATOM   16482 N NZ    . LYS B  1 1062 ? 11.739  81.491  70.963  1.00 45.04 ? 1060 LYS B NZ    1 
ATOM   16483 N N     . GLY B  1 1063 ? 5.049   82.181  69.976  1.00 45.81 ? 1061 GLY B N     1 
ATOM   16484 C CA    . GLY B  1 1063 ? 4.513   82.064  68.640  1.00 39.82 ? 1061 GLY B CA    1 
ATOM   16485 C C     . GLY B  1 1063 ? 5.052   80.886  67.868  1.00 44.46 ? 1061 GLY B C     1 
ATOM   16486 O O     . GLY B  1 1063 ? 4.960   80.868  66.638  1.00 47.24 ? 1061 GLY B O     1 
ATOM   16487 N N     . ALA B  1 1064 ? 5.634   79.898  68.550  1.00 40.06 ? 1062 ALA B N     1 
ATOM   16488 C CA    . ALA B  1 1064 ? 6.055   78.668  67.887  1.00 37.79 ? 1062 ALA B CA    1 
ATOM   16489 C C     . ALA B  1 1064 ? 4.846   77.739  67.822  1.00 41.37 ? 1062 ALA B C     1 
ATOM   16490 O O     . ALA B  1 1064 ? 4.762   76.714  68.503  1.00 37.44 ? 1062 ALA B O     1 
ATOM   16491 C CB    . ALA B  1 1064 ? 7.231   78.026  68.613  1.00 37.33 ? 1062 ALA B CB    1 
ATOM   16492 N N     . ARG B  1 1065 ? 3.890   78.134  66.970  1.00 42.07 ? 1063 ARG B N     1 
ATOM   16493 C CA    . ARG B  1 1065 ? 2.580   77.487  66.952  1.00 33.41 ? 1063 ARG B CA    1 
ATOM   16494 C C     . ARG B  1 1065 ? 2.677   76.044  66.489  1.00 36.98 ? 1063 ARG B C     1 
ATOM   16495 O O     . ARG B  1 1065 ? 2.064   75.152  67.089  1.00 38.26 ? 1063 ARG B O     1 
ATOM   16496 C CB    . ARG B  1 1065 ? 1.615   78.272  66.058  1.00 41.70 ? 1063 ARG B CB    1 
ATOM   16497 N N     . ALA B  1 1066 ? 3.437   75.792  65.419  1.00 36.27 ? 1064 ALA B N     1 
ATOM   16498 C CA    . ALA B  1 1066 ? 3.601   74.423  64.941  1.00 35.98 ? 1064 ALA B CA    1 
ATOM   16499 C C     . ALA B  1 1066 ? 4.213   73.542  66.020  1.00 37.11 ? 1064 ALA B C     1 
ATOM   16500 O O     . ALA B  1 1066 ? 3.805   72.388  66.200  1.00 35.28 ? 1064 ALA B O     1 
ATOM   16501 C CB    . ALA B  1 1066 ? 4.468   74.400  63.684  1.00 34.65 ? 1064 ALA B CB    1 
ATOM   16502 N N     . GLU B  1 1067 ? 5.187   74.076  66.753  1.00 33.33 ? 1065 GLU B N     1 
ATOM   16503 C CA    . GLU B  1 1067 ? 5.859   73.285  67.772  1.00 34.12 ? 1065 GLU B CA    1 
ATOM   16504 C C     . GLU B  1 1067 ? 4.997   73.141  69.021  1.00 31.86 ? 1065 GLU B C     1 
ATOM   16505 O O     . GLU B  1 1067 ? 4.964   72.064  69.628  1.00 31.82 ? 1065 GLU B O     1 
ATOM   16506 C CB    . GLU B  1 1067 ? 7.216   73.912  68.107  1.00 35.31 ? 1065 GLU B CB    1 
ATOM   16507 C CG    . GLU B  1 1067 ? 8.254   73.779  66.998  1.00 28.86 ? 1065 GLU B CG    1 
ATOM   16508 C CD    . GLU B  1 1067 ? 8.129   74.854  65.938  1.00 37.66 ? 1065 GLU B CD    1 
ATOM   16509 O OE1   . GLU B  1 1067 ? 7.286   75.765  66.094  1.00 38.10 ? 1065 GLU B OE1   1 
ATOM   16510 O OE2   . GLU B  1 1067 ? 8.884   74.791  64.948  1.00 40.43 ? 1065 GLU B OE2   1 
ATOM   16511 N N     . ALA B  1 1068 ? 4.308   74.215  69.423  1.00 32.07 ? 1066 ALA B N     1 
ATOM   16512 C CA    . ALA B  1 1068 ? 3.352   74.112  70.521  1.00 35.53 ? 1066 ALA B CA    1 
ATOM   16513 C C     . ALA B  1 1068 ? 2.309   73.039  70.237  1.00 33.18 ? 1066 ALA B C     1 
ATOM   16514 O O     . ALA B  1 1068 ? 1.989   72.225  71.113  1.00 31.60 ? 1066 ALA B O     1 
ATOM   16515 C CB    . ALA B  1 1068 ? 2.677   75.459  70.767  1.00 30.81 ? 1066 ALA B CB    1 
ATOM   16516 N N     . GLU B  1 1069 ? 1.783   73.010  69.011  1.00 33.76 ? 1067 GLU B N     1 
ATOM   16517 C CA    . GLU B  1 1069 ? 0.837   71.966  68.633  1.00 34.85 ? 1067 GLU B CA    1 
ATOM   16518 C C     . GLU B  1 1069 ? 1.487   70.585  68.675  1.00 35.24 ? 1067 GLU B C     1 
ATOM   16519 O O     . GLU B  1 1069 ? 0.891   69.624  69.180  1.00 31.00 ? 1067 GLU B O     1 
ATOM   16520 C CB    . GLU B  1 1069 ? 0.269   72.253  67.243  1.00 36.07 ? 1067 GLU B CB    1 
ATOM   16521 C CG    . GLU B  1 1069 ? -0.647  71.159  66.698  1.00 37.67 ? 1067 GLU B CG    1 
ATOM   16522 C CD    . GLU B  1 1069 ? -2.047  71.191  67.301  1.00 42.93 ? 1067 GLU B CD    1 
ATOM   16523 O OE1   . GLU B  1 1069 ? -2.209  71.654  68.454  1.00 49.40 ? 1067 GLU B OE1   1 
ATOM   16524 O OE2   . GLU B  1 1069 ? -2.996  70.759  66.610  1.00 51.98 ? 1067 GLU B OE2   1 
ATOM   16525 N N     . ALA B  1 1070 ? 2.712   70.469  68.151  1.00 31.82 ? 1068 ALA B N     1 
ATOM   16526 C CA    . ALA B  1 1070 ? 3.433   69.204  68.229  1.00 34.94 ? 1068 ALA B CA    1 
ATOM   16527 C C     . ALA B  1 1070 ? 3.626   68.767  69.675  1.00 25.12 ? 1068 ALA B C     1 
ATOM   16528 O O     . ALA B  1 1070 ? 3.500   67.581  69.990  1.00 26.62 ? 1068 ALA B O     1 
ATOM   16529 C CB    . ALA B  1 1070 ? 4.784   69.316  67.518  1.00 31.82 ? 1068 ALA B CB    1 
ATOM   16530 N N     . ALA B  1 1071 ? 3.927   69.714  70.570  1.00 27.18 ? 1069 ALA B N     1 
ATOM   16531 C CA    . ALA B  1 1071 ? 4.152   69.362  71.968  1.00 25.57 ? 1069 ALA B CA    1 
ATOM   16532 C C     . ALA B  1 1071 ? 2.879   68.818  72.614  1.00 28.42 ? 1069 ALA B C     1 
ATOM   16533 O O     . ALA B  1 1071 ? 2.924   67.794  73.306  1.00 24.34 ? 1069 ALA B O     1 
ATOM   16534 C CB    . ALA B  1 1071 ? 4.676   70.569  72.744  1.00 22.97 ? 1069 ALA B CB    1 
ATOM   16535 N N     . ARG B  1 1072 ? 1.736   69.488  72.390  1.00 26.72 ? 1070 ARG B N     1 
ATOM   16536 C CA    A ARG B  1 1072 ? 0.463   69.012  72.932  0.53 28.80 ? 1070 ARG B CA    1 
ATOM   16537 C CA    B ARG B  1 1072 ? 0.481   69.002  72.953  0.47 28.80 ? 1070 ARG B CA    1 
ATOM   16538 C C     . ARG B  1 1072 ? 0.140   67.615  72.421  1.00 29.72 ? 1070 ARG B C     1 
ATOM   16539 O O     . ARG B  1 1072 ? -0.311  66.750  73.181  1.00 28.29 ? 1070 ARG B O     1 
ATOM   16540 C CB    A ARG B  1 1072 ? -0.670  69.976  72.561  0.53 30.61 ? 1070 ARG B CB    1 
ATOM   16541 C CB    B ARG B  1 1072 ? -0.644  69.999  72.669  0.47 30.64 ? 1070 ARG B CB    1 
ATOM   16542 C CG    A ARG B  1 1072 ? -0.640  71.318  73.285  0.53 32.91 ? 1070 ARG B CG    1 
ATOM   16543 C CG    B ARG B  1 1072 ? -0.392  71.348  73.333  0.47 32.82 ? 1070 ARG B CG    1 
ATOM   16544 C CD    A ARG B  1 1072 ? -1.853  72.167  72.920  0.53 32.61 ? 1070 ARG B CD    1 
ATOM   16545 C CD    B ARG B  1 1072 ? -1.617  72.238  73.392  0.47 33.61 ? 1070 ARG B CD    1 
ATOM   16546 N NE    A ARG B  1 1072 ? -1.776  72.687  71.561  0.53 36.19 ? 1070 ARG B NE    1 
ATOM   16547 N NE    B ARG B  1 1072 ? -1.403  73.309  74.357  0.47 34.18 ? 1070 ARG B NE    1 
ATOM   16548 C CZ    A ARG B  1 1072 ? -1.336  73.898  71.246  0.53 35.98 ? 1070 ARG B CZ    1 
ATOM   16549 C CZ    B ARG B  1 1072 ? -0.870  74.486  74.060  0.47 33.95 ? 1070 ARG B CZ    1 
ATOM   16550 N NH1   A ARG B  1 1072 ? -0.936  74.750  72.174  0.53 36.62 ? 1070 ARG B NH1   1 
ATOM   16551 N NH1   B ARG B  1 1072 ? -0.531  74.797  72.820  0.47 36.12 ? 1070 ARG B NH1   1 
ATOM   16552 N NH2   A ARG B  1 1072 ? -1.297  74.262  69.968  0.53 32.87 ? 1070 ARG B NH2   1 
ATOM   16553 N NH2   B ARG B  1 1072 ? -0.671  75.370  75.031  0.47 34.45 ? 1070 ARG B NH2   1 
ATOM   16554 N N     . ASN B  1 1073 ? 0.368   67.375  71.130  1.00 27.50 ? 1071 ASN B N     1 
ATOM   16555 C CA    . ASN B  1 1073 ? 0.109   66.054  70.567  1.00 28.31 ? 1071 ASN B CA    1 
ATOM   16556 C C     . ASN B  1 1073 ? 1.036   65.000  71.155  1.00 28.18 ? 1071 ASN B C     1 
ATOM   16557 O O     . ASN B  1 1073 ? 0.614   63.861  71.392  1.00 27.94 ? 1071 ASN B O     1 
ATOM   16558 C CB    . ASN B  1 1073 ? 0.229   66.110  69.051  1.00 28.40 ? 1071 ASN B CB    1 
ATOM   16559 C CG    . ASN B  1 1073 ? -0.924  66.870  68.422  1.00 33.08 ? 1071 ASN B CG    1 
ATOM   16560 O OD1   . ASN B  1 1073 ? -1.906  67.185  69.099  1.00 39.96 ? 1071 ASN B OD1   1 
ATOM   16561 N ND2   . ASN B  1 1073 ? -0.810  67.184  67.134  1.00 35.36 ? 1071 ASN B ND2   1 
ATOM   16562 N N     . ALA B  1 1074 ? 2.303   65.353  71.401  1.00 25.88 ? 1072 ALA B N     1 
ATOM   16563 C CA    . ALA B  1 1074 ? 3.191   64.429  72.095  1.00 23.76 ? 1072 ALA B CA    1 
ATOM   16564 C C     . ALA B  1 1074 ? 2.668   64.131  73.496  1.00 24.21 ? 1072 ALA B C     1 
ATOM   16565 O O     . ALA B  1 1074 ? 2.671   62.977  73.945  1.00 23.25 ? 1072 ALA B O     1 
ATOM   16566 C CB    . ALA B  1 1074 ? 4.608   65.006  72.144  1.00 21.90 ? 1072 ALA B CB    1 
ATOM   16567 N N     . GLY B  1 1075 ? 2.225   65.170  74.207  1.00 20.51 ? 1073 GLY B N     1 
ATOM   16568 C CA    . GLY B  1 1075 ? 1.706   64.975  75.555  1.00 27.63 ? 1073 GLY B CA    1 
ATOM   16569 C C     . GLY B  1 1075 ? 0.536   64.012  75.618  1.00 27.27 ? 1073 GLY B C     1 
ATOM   16570 O O     . GLY B  1 1075 ? 0.401   63.261  76.589  1.00 26.89 ? 1073 GLY B O     1 
ATOM   16571 N N     . SER B  1 1076 ? -0.315  64.007  74.581  1.00 23.53 ? 1074 SER B N     1 
ATOM   16572 C CA    . SER B  1 1076 ? -1.470  63.119  74.560  1.00 26.69 ? 1074 SER B CA    1 
ATOM   16573 C C     . SER B  1 1076 ? -1.083  61.701  74.160  1.00 26.60 ? 1074 SER B C     1 
ATOM   16574 O O     . SER B  1 1076 ? -1.541  60.728  74.774  1.00 29.14 ? 1074 SER B O     1 
ATOM   16575 C CB    . SER B  1 1076 ? -2.531  63.671  73.605  1.00 28.64 ? 1074 SER B CB    1 
ATOM   16576 O OG    . SER B  1 1076 ? -3.119  64.860  74.117  1.00 30.87 ? 1074 SER B OG    1 
ATOM   16577 N N     . SER B  1 1077 ? -0.233  61.550  73.150  1.00 24.15 ? 1075 SER B N     1 
ATOM   16578 C CA    . SER B  1 1077 ? 0.032   60.207  72.658  1.00 27.84 ? 1075 SER B CA    1 
ATOM   16579 C C     . SER B  1 1077 ? 1.013   59.462  73.547  1.00 22.90 ? 1075 SER B C     1 
ATOM   16580 O O     . SER B  1 1077 ? 1.067   58.230  73.490  1.00 26.08 ? 1075 SER B O     1 
ATOM   16581 C CB    . SER B  1 1077 ? 0.536   60.255  71.218  1.00 30.80 ? 1075 SER B CB    1 
ATOM   16582 O OG    . SER B  1 1077 ? 1.716   61.004  71.122  1.00 34.39 ? 1075 SER B OG    1 
ATOM   16583 N N     . SER B  1 1078 ? 1.756   60.181  74.380  1.00 21.89 ? 1076 SER B N     1 
ATOM   16584 C CA    . SER B  1 1078 ? 2.620   59.539  75.368  1.00 21.68 ? 1076 SER B CA    1 
ATOM   16585 C C     . SER B  1 1078 ? 1.826   58.538  76.198  1.00 23.17 ? 1076 SER B C     1 
ATOM   16586 O O     . SER B  1 1078 ? 0.702   58.813  76.626  1.00 22.73 ? 1076 SER B O     1 
ATOM   16587 C CB    . SER B  1 1078 ? 3.232   60.599  76.290  1.00 18.15 ? 1076 SER B CB    1 
ATOM   16588 O OG    . SER B  1 1078 ? 3.939   59.986  77.360  1.00 19.70 ? 1076 SER B OG    1 
ATOM   16589 N N     . ALA B  1 1079 ? 2.419   57.379  76.449  1.00 20.47 ? 1077 ALA B N     1 
ATOM   16590 C CA    . ALA B  1 1079 ? 1.792   56.408  77.325  1.00 19.96 ? 1077 ALA B CA    1 
ATOM   16591 C C     . ALA B  1 1079 ? 2.423   56.411  78.712  1.00 22.62 ? 1077 ALA B C     1 
ATOM   16592 O O     . ALA B  1 1079 ? 2.196   55.484  79.493  1.00 20.00 ? 1077 ALA B O     1 
ATOM   16593 C CB    . ALA B  1 1079 ? 1.854   55.015  76.700  1.00 21.97 ? 1077 ALA B CB    1 
ATOM   16594 N N     . LEU B  1 1080 ? 3.198   57.443  79.036  1.00 22.78 ? 1078 LEU B N     1 
ATOM   16595 C CA    . LEU B  1 1080 ? 3.703   57.608  80.389  1.00 19.89 ? 1078 LEU B CA    1 
ATOM   16596 C C     . LEU B  1 1080 ? 2.561   57.549  81.401  1.00 19.40 ? 1078 LEU B C     1 
ATOM   16597 O O     . LEU B  1 1080 ? 1.563   58.254  81.266  1.00 21.11 ? 1078 LEU B O     1 
ATOM   16598 C CB    . LEU B  1 1080 ? 4.419   58.949  80.488  1.00 19.04 ? 1078 LEU B CB    1 
ATOM   16599 C CG    . LEU B  1 1080 ? 4.819   59.352  81.899  1.00 19.92 ? 1078 LEU B CG    1 
ATOM   16600 C CD1   . LEU B  1 1080 ? 5.980   58.493  82.378  1.00 18.66 ? 1078 LEU B CD1   1 
ATOM   16601 C CD2   . LEU B  1 1080 ? 5.161   60.827  81.914  1.00 17.77 ? 1078 LEU B CD2   1 
ATOM   16602 N N     . GLY B  1 1081 ? 2.735   56.738  82.446  1.00 18.92 ? 1079 GLY B N     1 
ATOM   16603 C CA    . GLY B  1 1081 ? 1.718   56.557  83.456  1.00 22.18 ? 1079 GLY B CA    1 
ATOM   16604 C C     . GLY B  1 1081 ? 0.814   55.353  83.256  1.00 23.28 ? 1079 GLY B C     1 
ATOM   16605 O O     . GLY B  1 1081 ? -0.034  55.094  84.118  1.00 20.90 ? 1079 GLY B O     1 
ATOM   16606 N N     . LEU B  1 1082 ? 0.941   54.640  82.135  1.00 22.15 ? 1080 LEU B N     1 
ATOM   16607 C CA    A LEU B  1 1082 ? 0.204   53.395  81.949  0.55 22.09 ? 1080 LEU B CA    1 
ATOM   16608 C CA    B LEU B  1 1082 ? 0.206   53.395  81.948  0.45 21.82 ? 1080 LEU B CA    1 
ATOM   16609 C C     . LEU B  1 1082 ? 0.383   52.505  83.170  1.00 20.22 ? 1080 LEU B C     1 
ATOM   16610 O O     . LEU B  1 1082 ? 1.472   52.421  83.732  1.00 20.74 ? 1080 LEU B O     1 
ATOM   16611 C CB    A LEU B  1 1082 ? 0.697   52.672  80.691  0.55 20.66 ? 1080 LEU B CB    1 
ATOM   16612 C CB    B LEU B  1 1082 ? 0.708   52.685  80.686  0.45 20.58 ? 1080 LEU B CB    1 
ATOM   16613 C CG    A LEU B  1 1082 ? -0.006  51.359  80.312  0.55 22.04 ? 1080 LEU B CG    1 
ATOM   16614 C CG    B LEU B  1 1082 ? 0.110   51.335  80.271  0.45 22.06 ? 1080 LEU B CG    1 
ATOM   16615 C CD1   A LEU B  1 1082 ? -1.500  51.571  80.229  0.55 22.78 ? 1080 LEU B CD1   1 
ATOM   16616 C CD1   B LEU B  1 1082 ? 0.149   51.209  78.759  0.45 20.49 ? 1080 LEU B CD1   1 
ATOM   16617 C CD2   A LEU B  1 1082 ? 0.527   50.805  78.992  0.55 20.06 ? 1080 LEU B CD2   1 
ATOM   16618 C CD2   B LEU B  1 1082 ? 0.877   50.187  80.907  0.45 18.81 ? 1080 LEU B CD2   1 
ATOM   16619 N N     . ASP B  1 1083 ? -0.702  51.853  83.589  1.00 21.35 ? 1081 ASP B N     1 
ATOM   16620 C CA    . ASP B  1 1083 ? -0.685  51.051  84.814  1.00 24.81 ? 1081 ASP B CA    1 
ATOM   16621 C C     . ASP B  1 1083 ? -1.718  49.943  84.639  1.00 25.76 ? 1081 ASP B C     1 
ATOM   16622 O O     . ASP B  1 1083 ? -2.914  50.170  84.865  1.00 28.78 ? 1081 ASP B O     1 
ATOM   16623 C CB    . ASP B  1 1083 ? -0.994  51.924  86.025  1.00 25.37 ? 1081 ASP B CB    1 
ATOM   16624 C CG    . ASP B  1 1083 ? -0.878  51.179  87.349  1.00 32.83 ? 1081 ASP B CG    1 
ATOM   16625 O OD1   . ASP B  1 1083 ? -0.338  50.051  87.377  1.00 36.01 ? 1081 ASP B OD1   1 
ATOM   16626 O OD2   . ASP B  1 1083 ? -1.344  51.728  88.372  1.00 38.76 ? 1081 ASP B OD2   1 
ATOM   16627 N N     . LEU B  1 1084 ? -1.258  48.757  84.242  1.00 21.11 ? 1082 LEU B N     1 
ATOM   16628 C CA    . LEU B  1 1084 ? -2.139  47.666  83.851  1.00 24.05 ? 1082 LEU B CA    1 
ATOM   16629 C C     . LEU B  1 1084 ? -1.894  46.447  84.721  1.00 25.01 ? 1082 LEU B C     1 
ATOM   16630 O O     . LEU B  1 1084 ? -0.761  46.184  85.131  1.00 23.55 ? 1082 LEU B O     1 
ATOM   16631 C CB    . LEU B  1 1084 ? -1.905  47.256  82.395  1.00 24.47 ? 1082 LEU B CB    1 
ATOM   16632 C CG    . LEU B  1 1084 ? -2.210  48.276  81.304  1.00 28.34 ? 1082 LEU B CG    1 
ATOM   16633 C CD1   . LEU B  1 1084 ? -1.813  47.701  79.957  1.00 26.65 ? 1082 LEU B CD1   1 
ATOM   16634 C CD2   . LEU B  1 1084 ? -3.679  48.668  81.322  1.00 33.11 ? 1082 LEU B CD2   1 
ATOM   16635 N N     . GLU B  1 1085 ? -2.952  45.674  84.964  1.00 24.23 ? 1083 GLU B N     1 
ATOM   16636 C CA    . GLU B  1 1085 ? -2.788  44.336  85.513  1.00 23.21 ? 1083 GLU B CA    1 
ATOM   16637 C C     . GLU B  1 1085 ? -2.895  43.335  84.369  1.00 27.28 ? 1083 GLU B C     1 
ATOM   16638 O O     . GLU B  1 1085 ? -3.811  43.423  83.543  1.00 27.28 ? 1083 GLU B O     1 
ATOM   16639 C CB    . GLU B  1 1085 ? -3.808  44.024  86.611  1.00 24.19 ? 1083 GLU B CB    1 
ATOM   16640 C CG    . GLU B  1 1085 ? -3.604  42.610  87.159  1.00 29.73 ? 1083 GLU B CG    1 
ATOM   16641 C CD    . GLU B  1 1085 ? -4.260  42.343  88.497  1.00 37.84 ? 1083 GLU B CD    1 
ATOM   16642 O OE1   . GLU B  1 1085 ? -4.783  43.290  89.130  1.00 39.41 ? 1083 GLU B OE1   1 
ATOM   16643 O OE2   . GLU B  1 1085 ? -4.239  41.163  88.916  1.00 37.79 ? 1083 GLU B OE2   1 
ATOM   16644 N N     . LEU B  1 1086 ? -1.940  42.424  84.297  1.00 25.66 ? 1084 LEU B N     1 
ATOM   16645 C CA    . LEU B  1 1086 ? -1.902  41.417  83.244  1.00 22.33 ? 1084 LEU B CA    1 
ATOM   16646 C C     . LEU B  1 1086 ? -2.528  40.116  83.728  1.00 27.18 ? 1084 LEU B C     1 
ATOM   16647 O O     . LEU B  1 1086 ? -2.319  39.718  84.883  1.00 26.39 ? 1084 LEU B O     1 
ATOM   16648 C CB    . LEU B  1 1086 ? -0.462  41.155  82.793  1.00 25.46 ? 1084 LEU B CB    1 
ATOM   16649 C CG    . LEU B  1 1086 ? 0.329   42.350  82.259  1.00 24.97 ? 1084 LEU B CG    1 
ATOM   16650 C CD1   . LEU B  1 1086 ? 1.657   41.917  81.650  1.00 23.10 ? 1084 LEU B CD1   1 
ATOM   16651 C CD2   . LEU B  1 1086 ? -0.504  43.117  81.230  1.00 27.97 ? 1084 LEU B CD2   1 
ATOM   16652 N N     . PRO B  1 1087 ? -3.306  39.436  82.882  1.00 29.19 ? 1085 PRO B N     1 
ATOM   16653 C CA    . PRO B  1 1087 ? -3.908  38.162  83.298  1.00 27.86 ? 1085 PRO B CA    1 
ATOM   16654 C C     . PRO B  1 1087 ? -2.842  37.111  83.561  1.00 26.77 ? 1085 PRO B C     1 
ATOM   16655 O O     . PRO B  1 1087 ? -1.870  36.986  82.818  1.00 28.77 ? 1085 PRO B O     1 
ATOM   16656 C CB    . PRO B  1 1087 ? -4.793  37.772  82.103  1.00 28.44 ? 1085 PRO B CB    1 
ATOM   16657 C CG    . PRO B  1 1087 ? -4.992  39.040  81.332  1.00 33.11 ? 1085 PRO B CG    1 
ATOM   16658 C CD    . PRO B  1 1087 ? -3.738  39.838  81.528  1.00 31.39 ? 1085 PRO B CD    1 
ATOM   16659 N N     . GLY B  1 1088 ? -3.043  36.351  84.629  1.00 27.49 ? 1086 GLY B N     1 
ATOM   16660 C CA    . GLY B  1 1088 ? -2.132  35.299  85.018  1.00 25.74 ? 1086 GLY B CA    1 
ATOM   16661 C C     . GLY B  1 1088 ? -2.823  34.336  85.956  1.00 22.41 ? 1086 GLY B C     1 
ATOM   16662 O O     . GLY B  1 1088 ? -4.051  34.228  85.960  1.00 24.76 ? 1086 GLY B O     1 
ATOM   16663 N N     . PRO B  1 1089 ? -2.056  33.640  86.789  1.00 24.24 ? 1087 PRO B N     1 
ATOM   16664 C CA    . PRO B  1 1089 ? -2.655  32.667  87.709  1.00 24.30 ? 1087 PRO B CA    1 
ATOM   16665 C C     . PRO B  1 1089 ? -3.350  33.350  88.879  1.00 22.45 ? 1087 PRO B C     1 
ATOM   16666 O O     . PRO B  1 1089 ? -3.106  34.518  89.194  1.00 21.91 ? 1087 PRO B O     1 
ATOM   16667 C CB    . PRO B  1 1089 ? -1.444  31.858  88.204  1.00 21.42 ? 1087 PRO B CB    1 
ATOM   16668 C CG    . PRO B  1 1089 ? -0.308  32.888  88.184  1.00 27.25 ? 1087 PRO B CG    1 
ATOM   16669 C CD    . PRO B  1 1089 ? -0.596  33.765  86.969  1.00 24.85 ? 1087 PRO B CD    1 
ATOM   16670 N N     . VAL B  1 1090 ? -4.232  32.583  89.524  1.00 19.23 ? 1088 VAL B N     1 
ATOM   16671 C CA    . VAL B  1 1090 ? -4.771  33.010  90.804  1.00 19.07 ? 1088 VAL B CA    1 
ATOM   16672 C C     . VAL B  1 1090 ? -3.628  33.115  91.811  1.00 21.30 ? 1088 VAL B C     1 
ATOM   16673 O O     . VAL B  1 1090 ? -2.554  32.520  91.644  1.00 23.12 ? 1088 VAL B O     1 
ATOM   16674 C CB    . VAL B  1 1090 ? -5.850  32.047  91.319  1.00 24.79 ? 1088 VAL B CB    1 
ATOM   16675 C CG1   . VAL B  1 1090 ? -6.969  31.898  90.293  1.00 20.32 ? 1088 VAL B CG1   1 
ATOM   16676 C CG2   . VAL B  1 1090 ? -5.243  30.697  91.665  1.00 19.35 ? 1088 VAL B CG2   1 
ATOM   16677 N N     . GLY B  1 1091 ? -3.872  33.881  92.873  1.00 20.46 ? 1089 GLY B N     1 
ATOM   16678 C CA    . GLY B  1 1091 ? -2.866  34.030  93.915  1.00 19.05 ? 1089 GLY B CA    1 
ATOM   16679 C C     . GLY B  1 1091 ? -1.629  34.792  93.503  1.00 23.00 ? 1089 GLY B C     1 
ATOM   16680 O O     . GLY B  1 1091 ? -0.590  34.670  94.150  1.00 21.33 ? 1089 GLY B O     1 
ATOM   16681 N N     . GLU B  1 1092 ? -1.717  35.601  92.453  1.00 22.31 ? 1090 GLU B N     1 
ATOM   16682 C CA    . GLU B  1 1092 ? -0.604  36.403  91.991  1.00 21.21 ? 1090 GLU B CA    1 
ATOM   16683 C C     . GLU B  1 1092 ? -1.187  37.650  91.348  1.00 22.75 ? 1090 GLU B C     1 
ATOM   16684 O O     . GLU B  1 1092 ? -2.223  37.575  90.696  1.00 20.86 ? 1090 GLU B O     1 
ATOM   16685 C CB    . GLU B  1 1092 ? 0.257   35.613  90.986  1.00 23.79 ? 1090 GLU B CB    1 
ATOM   16686 C CG    . GLU B  1 1092 ? 1.723   36.009  90.904  1.00 25.91 ? 1090 GLU B CG    1 
ATOM   16687 C CD    . GLU B  1 1092 ? 2.511   35.121  89.917  1.00 25.38 ? 1090 GLU B CD    1 
ATOM   16688 O OE1   . GLU B  1 1092 ? 2.216   35.153  88.704  1.00 23.05 ? 1090 GLU B OE1   1 
ATOM   16689 O OE2   . GLU B  1 1092 ? 3.405   34.370  90.364  1.00 29.53 ? 1090 GLU B OE2   1 
ATOM   16690 N N     . ARG B  1 1093 ? -0.542  38.792  91.541  1.00 20.93 ? 1091 ARG B N     1 
ATOM   16691 C CA    . ARG B  1 1093 ? -0.908  40.009  90.817  1.00 23.18 ? 1091 ARG B CA    1 
ATOM   16692 C C     . ARG B  1 1093 ? 0.277   40.434  89.967  1.00 22.56 ? 1091 ARG B C     1 
ATOM   16693 O O     . ARG B  1 1093 ? 1.376   40.656  90.485  1.00 21.03 ? 1091 ARG B O     1 
ATOM   16694 C CB    . ARG B  1 1093 ? -1.331  41.135  91.766  1.00 25.76 ? 1091 ARG B CB    1 
ATOM   16695 C CG    . ARG B  1 1093 ? -2.781  41.038  92.237  1.00 39.44 ? 1091 ARG B CG    1 
ATOM   16696 C CD    . ARG B  1 1093 ? -3.144  42.223  93.129  1.00 43.86 ? 1091 ARG B CD    1 
ATOM   16697 N NE    . ARG B  1 1093 ? -2.695  43.490  92.559  1.00 46.28 ? 1091 ARG B NE    1 
ATOM   16698 C CZ    . ARG B  1 1093 ? -2.860  44.673  93.136  1.00 54.82 ? 1091 ARG B CZ    1 
ATOM   16699 N NH1   . ARG B  1 1093 ? -3.481  44.794  94.299  1.00 59.84 ? 1091 ARG B NH1   1 
ATOM   16700 N NH2   . ARG B  1 1093 ? -2.389  45.762  92.533  1.00 50.57 ? 1091 ARG B NH2   1 
ATOM   16701 N N     . ASN B  1 1094 ? 0.062   40.537  88.663  1.00 19.75 ? 1092 ASN B N     1 
ATOM   16702 C CA    . ASN B  1 1094 ? 1.137   40.838  87.725  1.00 18.07 ? 1092 ASN B CA    1 
ATOM   16703 C C     . ASN B  1 1094 ? 0.843   42.189  87.087  1.00 23.68 ? 1092 ASN B C     1 
ATOM   16704 O O     . ASN B  1 1094 ? -0.148  42.337  86.368  1.00 21.04 ? 1092 ASN B O     1 
ATOM   16705 C CB    . ASN B  1 1094 ? 1.262   39.723  86.690  1.00 19.53 ? 1092 ASN B CB    1 
ATOM   16706 C CG    . ASN B  1 1094 ? 1.824   38.476  87.310  1.00 21.00 ? 1092 ASN B CG    1 
ATOM   16707 O OD1   . ASN B  1 1094 ? 2.991   38.451  87.693  1.00 20.53 ? 1092 ASN B OD1   1 
ATOM   16708 N ND2   . ASN B  1 1094 ? 0.986   37.479  87.508  1.00 21.17 ? 1092 ASN B ND2   1 
ATOM   16709 N N     . LEU B  1 1095 ? 1.692   43.164  87.382  1.00 18.94 ? 1093 LEU B N     1 
ATOM   16710 C CA    . LEU B  1 1095 ? 1.505   44.553  86.995  1.00 20.51 ? 1093 LEU B CA    1 
ATOM   16711 C C     . LEU B  1 1095 ? 2.534   44.957  85.948  1.00 18.04 ? 1093 LEU B C     1 
ATOM   16712 O O     . LEU B  1 1095 ? 3.660   44.457  85.930  1.00 20.23 ? 1093 LEU B O     1 
ATOM   16713 C CB    . LEU B  1 1095 ? 1.613   45.467  88.222  1.00 23.06 ? 1093 LEU B CB    1 
ATOM   16714 C CG    . LEU B  1 1095 ? 0.722   44.994  89.384  1.00 26.60 ? 1093 LEU B CG    1 
ATOM   16715 C CD1   . LEU B  1 1095 ? 0.938   45.831  90.645  1.00 32.27 ? 1093 LEU B CD1   1 
ATOM   16716 C CD2   . LEU B  1 1095 ? -0.761  44.983  89.000  1.00 24.22 ? 1093 LEU B CD2   1 
ATOM   16717 N N     . TYR B  1 1096 ? 2.120   45.883  85.076  1.00 18.57 ? 1094 TYR B N     1 
ATOM   16718 C CA    . TYR B  1 1096 ? 2.921   46.386  83.970  1.00 16.53 ? 1094 TYR B CA    1 
ATOM   16719 C C     . TYR B  1 1096 ? 2.699   47.891  83.923  1.00 18.14 ? 1094 TYR B C     1 
ATOM   16720 O O     . TYR B  1 1096 ? 1.556   48.341  83.790  1.00 19.39 ? 1094 TYR B O     1 
ATOM   16721 C CB    . TYR B  1 1096 ? 2.509   45.715  82.642  1.00 17.60 ? 1094 TYR B CB    1 
ATOM   16722 C CG    . TYR B  1 1096 ? 3.215   46.232  81.412  1.00 19.20 ? 1094 TYR B CG    1 
ATOM   16723 C CD1   . TYR B  1 1096 ? 4.484   45.774  81.055  1.00 20.56 ? 1094 TYR B CD1   1 
ATOM   16724 C CD2   . TYR B  1 1096 ? 2.587   47.156  80.578  1.00 21.82 ? 1094 TYR B CD2   1 
ATOM   16725 C CE1   . TYR B  1 1096 ? 5.130   46.250  79.905  1.00 21.04 ? 1094 TYR B CE1   1 
ATOM   16726 C CE2   . TYR B  1 1096 ? 3.207   47.631  79.443  1.00 20.11 ? 1094 TYR B CE2   1 
ATOM   16727 C CZ    . TYR B  1 1096 ? 4.470   47.182  79.102  1.00 22.19 ? 1094 TYR B CZ    1 
ATOM   16728 O OH    . TYR B  1 1096 ? 5.065   47.679  77.966  1.00 22.74 ? 1094 TYR B OH    1 
ATOM   16729 N N     . THR B  1 1097 ? 3.777   48.668  84.073  1.00 17.78 ? 1095 THR B N     1 
ATOM   16730 C CA    . THR B  1 1097 ? 3.697   50.125  84.183  1.00 16.97 ? 1095 THR B CA    1 
ATOM   16731 C C     . THR B  1 1097 ? 4.741   50.798  83.290  1.00 18.70 ? 1095 THR B C     1 
ATOM   16732 O O     . THR B  1 1097 ? 5.819   50.254  83.035  1.00 19.58 ? 1095 THR B O     1 
ATOM   16733 C CB    . THR B  1 1097 ? 3.904   50.574  85.620  1.00 19.50 ? 1095 THR B CB    1 
ATOM   16734 O OG1   . THR B  1 1097 ? 5.133   50.023  86.103  1.00 24.80 ? 1095 THR B OG1   1 
ATOM   16735 C CG2   . THR B  1 1097 ? 2.763   50.084  86.522  1.00 23.26 ? 1095 THR B CG2   1 
ATOM   16736 N N     . LEU B  1 1098 ? 4.434   52.010  82.827  1.00 16.62 ? 1096 LEU B N     1 
ATOM   16737 C CA    . LEU B  1 1098 ? 5.375   52.756  81.999  1.00 16.53 ? 1096 LEU B CA    1 
ATOM   16738 C C     . LEU B  1 1098 ? 5.776   54.019  82.739  1.00 19.02 ? 1096 LEU B C     1 
ATOM   16739 O O     . LEU B  1 1098 ? 4.912   54.828  83.104  1.00 19.15 ? 1096 LEU B O     1 
ATOM   16740 C CB    . LEU B  1 1098 ? 4.786   53.120  80.634  1.00 18.00 ? 1096 LEU B CB    1 
ATOM   16741 C CG    . LEU B  1 1098 ? 4.436   51.925  79.757  1.00 18.07 ? 1096 LEU B CG    1 
ATOM   16742 C CD1   . LEU B  1 1098 ? 3.712   52.432  78.488  1.00 19.06 ? 1096 LEU B CD1   1 
ATOM   16743 C CD2   . LEU B  1 1098 ? 5.680   51.144  79.417  1.00 17.71 ? 1096 LEU B CD2   1 
ATOM   16744 N N     . HIS B  1 1099 ? 7.082   54.177  82.953  1.00 21.80 ? 1097 HIS B N     1 
ATOM   16745 C CA    . HIS B  1 1099 ? 7.664   55.289  83.685  1.00 21.86 ? 1097 HIS B CA    1 
ATOM   16746 C C     . HIS B  1 1099 ? 8.574   56.097  82.773  1.00 18.98 ? 1097 HIS B C     1 
ATOM   16747 O O     . HIS B  1 1099 ? 8.877   55.703  81.647  1.00 19.79 ? 1097 HIS B O     1 
ATOM   16748 C CB    . HIS B  1 1099 ? 8.486   54.796  84.875  1.00 21.10 ? 1097 HIS B CB    1 
ATOM   16749 C CG    . HIS B  1 1099 ? 7.747   53.864  85.783  1.00 25.95 ? 1097 HIS B CG    1 
ATOM   16750 N ND1   . HIS B  1 1099 ? 7.250   54.254  87.008  1.00 23.39 ? 1097 HIS B ND1   1 
ATOM   16751 C CD2   . HIS B  1 1099 ? 7.438   52.553  85.649  1.00 20.00 ? 1097 HIS B CD2   1 
ATOM   16752 C CE1   . HIS B  1 1099 ? 6.674   53.220  87.593  1.00 25.62 ? 1097 HIS B CE1   1 
ATOM   16753 N NE2   . HIS B  1 1099 ? 6.772   52.177  86.786  1.00 25.46 ? 1097 HIS B NE2   1 
ATOM   16754 N N     . ALA B  1 1100 ? 9.045   57.221  83.288  1.00 20.49 ? 1098 ALA B N     1 
ATOM   16755 C CA    . ALA B  1 1100 ? 10.076  57.957  82.569  1.00 26.30 ? 1098 ALA B CA    1 
ATOM   16756 C C     . ALA B  1 1100 ? 11.351  57.120  82.494  1.00 23.11 ? 1098 ALA B C     1 
ATOM   16757 O O     . ALA B  1 1100 ? 11.629  56.290  83.364  1.00 21.71 ? 1098 ALA B O     1 
ATOM   16758 C CB    . ALA B  1 1100 ? 10.352  59.297  83.256  1.00 27.01 ? 1098 ALA B CB    1 
ATOM   16759 N N     . ARG B  1 1101 ? 12.123  57.322  81.423  1.00 21.24 ? 1099 ARG B N     1 
ATOM   16760 C CA    . ARG B  1 1101 ? 13.367  56.577  81.285  1.00 25.13 ? 1099 ARG B CA    1 
ATOM   16761 C C     . ARG B  1 1101 ? 14.486  57.185  82.109  1.00 24.20 ? 1099 ARG B C     1 
ATOM   16762 O O     . ARG B  1 1101 ? 15.317  56.453  82.658  1.00 25.30 ? 1099 ARG B O     1 
ATOM   16763 C CB    . ARG B  1 1101 ? 13.781  56.499  79.824  1.00 26.63 ? 1099 ARG B CB    1 
ATOM   16764 C CG    . ARG B  1 1101 ? 13.298  55.248  79.168  1.00 28.89 ? 1099 ARG B CG    1 
ATOM   16765 C CD    . ARG B  1 1101 ? 13.709  55.227  77.731  1.00 28.77 ? 1099 ARG B CD    1 
ATOM   16766 N NE    . ARG B  1 1101 ? 14.826  54.327  77.471  1.00 32.23 ? 1099 ARG B NE    1 
ATOM   16767 C CZ    . ARG B  1 1101 ? 14.690  53.039  77.192  1.00 37.85 ? 1099 ARG B CZ    1 
ATOM   16768 N NH1   . ARG B  1 1101 ? 13.515  52.443  77.259  1.00 35.04 ? 1099 ARG B NH1   1 
ATOM   16769 N NH2   . ARG B  1 1101 ? 15.756  52.337  76.817  1.00 37.01 ? 1099 ARG B NH2   1 
ATOM   16770 N N     . GLY B  1 1102 ? 14.532  58.515  82.198  1.00 22.40 ? 1100 GLY B N     1 
ATOM   16771 C CA    . GLY B  1 1102 ? 15.621  59.194  82.872  1.00 26.04 ? 1100 GLY B CA    1 
ATOM   16772 C C     . GLY B  1 1102 ? 16.020  60.457  82.133  1.00 26.09 ? 1100 GLY B C     1 
ATOM   16773 O O     . GLY B  1 1102 ? 15.161  61.287  81.822  1.00 23.86 ? 1100 GLY B O     1 
ATOM   16774 N N     . ARG B  1 1103 ? 17.303  60.622  81.829  1.00 21.51 ? 1101 ARG B N     1 
ATOM   16775 C CA    . ARG B  1 1103 ? 17.780  61.801  81.110  1.00 22.70 ? 1101 ARG B CA    1 
ATOM   16776 C C     . ARG B  1 1103 ? 18.107  61.407  79.679  1.00 21.29 ? 1101 ARG B C     1 
ATOM   16777 O O     . ARG B  1 1103 ? 18.919  60.507  79.453  1.00 22.04 ? 1101 ARG B O     1 
ATOM   16778 C CB    . ARG B  1 1103 ? 19.004  62.425  81.791  1.00 25.08 ? 1101 ARG B CB    1 
ATOM   16779 C CG    . ARG B  1 1103 ? 19.380  63.786  81.183  1.00 25.13 ? 1101 ARG B CG    1 
ATOM   16780 C CD    . ARG B  1 1103 ? 20.446  64.491  82.002  1.00 27.68 ? 1101 ARG B CD    1 
ATOM   16781 N NE    . ARG B  1 1103 ? 20.005  64.760  83.366  1.00 32.68 ? 1101 ARG B NE    1 
ATOM   16782 C CZ    . ARG B  1 1103 ? 19.474  65.905  83.783  1.00 38.00 ? 1101 ARG B CZ    1 
ATOM   16783 N NH1   . ARG B  1 1103 ? 19.226  66.910  82.945  1.00 30.22 ? 1101 ARG B NH1   1 
ATOM   16784 N NH2   . ARG B  1 1103 ? 19.193  66.054  85.076  1.00 35.82 ? 1101 ARG B NH2   1 
ATOM   16785 N N     . ILE B  1 1104 ? 17.469  62.081  78.719  1.00 19.71 ? 1102 ILE B N     1 
ATOM   16786 C CA    . ILE B  1 1104 ? 17.606  61.776  77.301  1.00 19.03 ? 1102 ILE B CA    1 
ATOM   16787 C C     . ILE B  1 1104 ? 18.651  62.703  76.693  1.00 21.77 ? 1102 ILE B C     1 
ATOM   16788 O O     . ILE B  1 1104 ? 18.583  63.925  76.876  1.00 22.56 ? 1102 ILE B O     1 
ATOM   16789 C CB    . ILE B  1 1104 ? 16.258  61.939  76.585  1.00 19.83 ? 1102 ILE B CB    1 
ATOM   16790 C CG1   . ILE B  1 1104 ? 15.180  61.156  77.348  1.00 20.81 ? 1102 ILE B CG1   1 
ATOM   16791 C CG2   . ILE B  1 1104 ? 16.382  61.527  75.125  1.00 22.75 ? 1102 ILE B CG2   1 
ATOM   16792 C CD1   . ILE B  1 1104 ? 15.442  59.670  77.415  1.00 23.65 ? 1102 ILE B CD1   1 
ATOM   16793 N N     . LEU B  1 1105 ? 19.618  62.130  75.976  1.00 18.94 ? 1103 LEU B N     1 
ATOM   16794 C CA    . LEU B  1 1105 ? 20.590  62.934  75.247  1.00 19.20 ? 1103 LEU B CA    1 
ATOM   16795 C C     . LEU B  1 1105 ? 19.928  63.480  73.987  1.00 20.11 ? 1103 LEU B C     1 
ATOM   16796 O O     . LEU B  1 1105 ? 19.426  62.714  73.165  1.00 20.88 ? 1103 LEU B O     1 
ATOM   16797 C CB    . LEU B  1 1105 ? 21.824  62.106  74.891  1.00 19.60 ? 1103 LEU B CB    1 
ATOM   16798 C CG    . LEU B  1 1105 ? 22.883  62.788  74.009  1.00 23.34 ? 1103 LEU B CG    1 
ATOM   16799 C CD1   . LEU B  1 1105 ? 23.467  64.018  74.698  1.00 22.43 ? 1103 LEU B CD1   1 
ATOM   16800 C CD2   . LEU B  1 1105 ? 23.996  61.803  73.613  1.00 20.82 ? 1103 LEU B CD2   1 
ATOM   16801 N N     . LEU B  1 1106 ? 19.919  64.796  73.850  1.00 21.01 ? 1104 LEU B N     1 
ATOM   16802 C CA    . LEU B  1 1106 ? 19.353  65.478  72.695  1.00 20.70 ? 1104 LEU B CA    1 
ATOM   16803 C C     . LEU B  1 1106 ? 20.501  66.025  71.865  1.00 23.20 ? 1104 LEU B C     1 
ATOM   16804 O O     . LEU B  1 1106 ? 21.363  66.733  72.397  1.00 21.52 ? 1104 LEU B O     1 
ATOM   16805 C CB    . LEU B  1 1106 ? 18.438  66.626  73.127  1.00 21.54 ? 1104 LEU B CB    1 
ATOM   16806 C CG    . LEU B  1 1106 ? 16.940  66.394  73.285  1.00 26.09 ? 1104 LEU B CG    1 
ATOM   16807 C CD1   . LEU B  1 1106 ? 16.617  65.028  73.878  1.00 22.25 ? 1104 LEU B CD1   1 
ATOM   16808 C CD2   . LEU B  1 1106 ? 16.297  67.530  74.073  1.00 18.78 ? 1104 LEU B CD2   1 
ATOM   16809 N N     . VAL B  1 1107 ? 20.515  65.690  70.579  1.00 22.33 ? 1105 VAL B N     1 
ATOM   16810 C CA    . VAL B  1 1107 ? 21.543  66.178  69.661  1.00 19.89 ? 1105 VAL B CA    1 
ATOM   16811 C C     . VAL B  1 1107 ? 20.803  66.889  68.534  1.00 25.37 ? 1105 VAL B C     1 
ATOM   16812 O O     . VAL B  1 1107 ? 20.631  66.310  67.452  1.00 23.66 ? 1105 VAL B O     1 
ATOM   16813 C CB    . VAL B  1 1107 ? 22.432  65.037  69.138  1.00 22.33 ? 1105 VAL B CB    1 
ATOM   16814 C CG1   . VAL B  1 1107 ? 23.705  65.589  68.496  1.00 22.47 ? 1105 VAL B CG1   1 
ATOM   16815 C CG2   . VAL B  1 1107 ? 22.823  64.081  70.274  1.00 22.47 ? 1105 VAL B CG2   1 
ATOM   16816 N N     . PRO B  1 1108 ? 20.307  68.105  68.757  1.00 22.41 ? 1106 PRO B N     1 
ATOM   16817 C CA    . PRO B  1 1108 ? 19.575  68.814  67.702  1.00 25.09 ? 1106 PRO B CA    1 
ATOM   16818 C C     . PRO B  1 1108 ? 20.520  69.461  66.700  1.00 25.88 ? 1106 PRO B C     1 
ATOM   16819 O O     . PRO B  1 1108 ? 21.716  69.655  66.944  1.00 26.31 ? 1106 PRO B O     1 
ATOM   16820 C CB    . PRO B  1 1108 ? 18.796  69.888  68.471  1.00 23.24 ? 1106 PRO B CB    1 
ATOM   16821 C CG    . PRO B  1 1108 ? 19.705  70.193  69.633  1.00 26.54 ? 1106 PRO B CG    1 
ATOM   16822 C CD    . PRO B  1 1108 ? 20.300  68.856  70.026  1.00 23.37 ? 1106 PRO B CD    1 
ATOM   16823 N N     . ALA B  1 1109 ? 19.946  69.809  65.558  1.00 23.10 ? 1107 ALA B N     1 
ATOM   16824 C CA    . ALA B  1 1109 ? 20.624  70.627  64.563  1.00 29.96 ? 1107 ALA B CA    1 
ATOM   16825 C C     . ALA B  1 1109 ? 20.017  72.012  64.413  1.00 31.78 ? 1107 ALA B C     1 
ATOM   16826 O O     . ALA B  1 1109 ? 20.748  72.968  64.144  1.00 31.06 ? 1107 ALA B O     1 
ATOM   16827 C CB    . ALA B  1 1109 ? 20.599  69.926  63.198  1.00 28.75 ? 1107 ALA B CB    1 
ATOM   16828 N N     . THR B  1 1110 ? 18.698  72.133  64.579  1.00 30.75 ? 1108 THR B N     1 
ATOM   16829 C CA    . THR B  1 1110 ? 17.962  73.369  64.364  1.00 27.26 ? 1108 THR B CA    1 
ATOM   16830 C C     . THR B  1 1110 ? 17.136  73.692  65.601  1.00 31.28 ? 1108 THR B C     1 
ATOM   16831 O O     . THR B  1 1110 ? 16.875  72.825  66.440  1.00 26.25 ? 1108 THR B O     1 
ATOM   16832 C CB    . THR B  1 1110 ? 17.030  73.252  63.151  1.00 29.28 ? 1108 THR B CB    1 
ATOM   16833 O OG1   . THR B  1 1110 ? 16.082  72.196  63.377  1.00 28.98 ? 1108 THR B OG1   1 
ATOM   16834 C CG2   . THR B  1 1110 ? 17.825  72.950  61.885  1.00 30.61 ? 1108 THR B CG2   1 
ATOM   16835 N N     . GLU B  1 1111 ? 16.705  74.955  65.692  1.00 27.76 ? 1109 GLU B N     1 
ATOM   16836 C CA    . GLU B  1 1111 ? 15.864  75.369  66.811  1.00 29.28 ? 1109 GLU B CA    1 
ATOM   16837 C C     . GLU B  1 1111 ? 14.555  74.586  66.843  1.00 29.45 ? 1109 GLU B C     1 
ATOM   16838 O O     . GLU B  1 1111 ? 14.130  74.112  67.902  1.00 25.49 ? 1109 GLU B O     1 
ATOM   16839 C CB    . GLU B  1 1111 ? 15.579  76.869  66.739  1.00 29.37 ? 1109 GLU B CB    1 
ATOM   16840 C CG    . GLU B  1 1111 ? 14.699  77.367  67.885  1.00 32.03 ? 1109 GLU B CG    1 
ATOM   16841 C CD    . GLU B  1 1111 ? 14.464  78.872  67.829  1.00 34.28 ? 1109 GLU B CD    1 
ATOM   16842 O OE1   . GLU B  1 1111 ? 13.567  79.300  67.084  1.00 35.29 ? 1109 GLU B OE1   1 
ATOM   16843 O OE2   . GLU B  1 1111 ? 15.182  79.624  68.521  1.00 35.06 ? 1109 GLU B OE2   1 
ATOM   16844 N N     . SER B  1 1112 ? 13.889  74.459  65.692  1.00 26.81 ? 1110 SER B N     1 
ATOM   16845 C CA    . SER B  1 1112 ? 12.639  73.705  65.650  1.00 29.06 ? 1110 SER B CA    1 
ATOM   16846 C C     . SER B  1 1112 ? 12.872  72.227  65.938  1.00 30.25 ? 1110 SER B C     1 
ATOM   16847 O O     . SER B  1 1112 ? 12.058  71.581  66.610  1.00 27.11 ? 1110 SER B O     1 
ATOM   16848 C CB    . SER B  1 1112 ? 11.954  73.879  64.296  1.00 30.55 ? 1110 SER B CB    1 
ATOM   16849 O OG    . SER B  1 1112 ? 10.824  73.028  64.205  1.00 32.01 ? 1110 SER B OG    1 
ATOM   16850 N N     . GLY B  1 1113 ? 13.969  71.666  65.428  1.00 27.77 ? 1111 GLY B N     1 
ATOM   16851 C CA    . GLY B  1 1113 ? 14.315  70.301  65.790  1.00 24.73 ? 1111 GLY B CA    1 
ATOM   16852 C C     . GLY B  1 1113 ? 14.457  70.130  67.290  1.00 25.11 ? 1111 GLY B C     1 
ATOM   16853 O O     . GLY B  1 1113 ? 13.993  69.137  67.859  1.00 24.17 ? 1111 GLY B O     1 
ATOM   16854 N N     . LEU B  1 1114 ? 15.085  71.107  67.950  1.00 26.35 ? 1112 LEU B N     1 
ATOM   16855 C CA    . LEU B  1 1114 ? 15.283  71.041  69.395  1.00 25.72 ? 1112 LEU B CA    1 
ATOM   16856 C C     . LEU B  1 1114 ? 13.954  71.093  70.140  1.00 25.61 ? 1112 LEU B C     1 
ATOM   16857 O O     . LEU B  1 1114 ? 13.753  70.366  71.121  1.00 21.57 ? 1112 LEU B O     1 
ATOM   16858 C CB    . LEU B  1 1114 ? 16.185  72.186  69.852  1.00 24.56 ? 1112 LEU B CB    1 
ATOM   16859 C CG    . LEU B  1 1114 ? 16.358  72.393  71.366  1.00 27.63 ? 1112 LEU B CG    1 
ATOM   16860 C CD1   . LEU B  1 1114 ? 16.914  71.125  72.064  1.00 23.81 ? 1112 LEU B CD1   1 
ATOM   16861 C CD2   . LEU B  1 1114 ? 17.233  73.608  71.651  1.00 25.43 ? 1112 LEU B CD2   1 
ATOM   16862 N N     . TYR B  1 1115 ? 13.039  71.955  69.687  1.00 27.51 ? 1113 TYR B N     1 
ATOM   16863 C CA    . TYR B  1 1115 ? 11.715  72.029  70.302  1.00 26.59 ? 1113 TYR B CA    1 
ATOM   16864 C C     . TYR B  1 1115 ? 10.964  70.709  70.154  1.00 23.40 ? 1113 TYR B C     1 
ATOM   16865 O O     . TYR B  1 1115 ? 10.314  70.251  71.096  1.00 23.26 ? 1113 TYR B O     1 
ATOM   16866 C CB    . TYR B  1 1115 ? 10.906  73.176  69.684  1.00 25.06 ? 1113 TYR B CB    1 
ATOM   16867 C CG    . TYR B  1 1115 ? 11.434  74.584  69.951  1.00 25.12 ? 1113 TYR B CG    1 
ATOM   16868 C CD1   . TYR B  1 1115 ? 12.379  74.837  70.951  1.00 27.30 ? 1113 TYR B CD1   1 
ATOM   16869 C CD2   . TYR B  1 1115 ? 10.980  75.660  69.199  1.00 31.49 ? 1113 TYR B CD2   1 
ATOM   16870 C CE1   . TYR B  1 1115 ? 12.855  76.123  71.185  1.00 30.12 ? 1113 TYR B CE1   1 
ATOM   16871 C CE2   . TYR B  1 1115 ? 11.442  76.947  69.425  1.00 32.75 ? 1113 TYR B CE2   1 
ATOM   16872 C CZ    . TYR B  1 1115 ? 12.376  77.175  70.413  1.00 34.74 ? 1113 TYR B CZ    1 
ATOM   16873 O OH    . TYR B  1 1115 ? 12.832  78.458  70.619  1.00 36.92 ? 1113 TYR B OH    1 
ATOM   16874 N N     . HIS B  1 1116 ? 11.034  70.084  68.976  1.00 23.06 ? 1114 HIS B N     1 
ATOM   16875 C CA    . HIS B  1 1116 ? 10.364  68.802  68.790  1.00 23.77 ? 1114 HIS B CA    1 
ATOM   16876 C C     . HIS B  1 1116 ? 10.976  67.725  69.674  1.00 24.34 ? 1114 HIS B C     1 
ATOM   16877 O O     . HIS B  1 1116 ? 10.244  66.938  70.285  1.00 21.73 ? 1114 HIS B O     1 
ATOM   16878 C CB    . HIS B  1 1116 ? 10.410  68.371  67.328  1.00 25.11 ? 1114 HIS B CB    1 
ATOM   16879 C CG    . HIS B  1 1116 ? 9.431   69.086  66.454  1.00 27.92 ? 1114 HIS B CG    1 
ATOM   16880 N ND1   . HIS B  1 1116 ? 9.690   70.320  65.898  1.00 32.39 ? 1114 HIS B ND1   1 
ATOM   16881 C CD2   . HIS B  1 1116 ? 8.190   68.738  66.036  1.00 29.60 ? 1114 HIS B CD2   1 
ATOM   16882 C CE1   . HIS B  1 1116 ? 8.651   70.702  65.177  1.00 29.87 ? 1114 HIS B CE1   1 
ATOM   16883 N NE2   . HIS B  1 1116 ? 7.727   69.763  65.246  1.00 32.09 ? 1114 HIS B NE2   1 
ATOM   16884 N N     . GLN B  1 1117 ? 12.314  67.676  69.749  1.00 23.56 ? 1115 GLN B N     1 
ATOM   16885 C CA    . GLN B  1 1117 ? 12.994  66.691  70.590  1.00 21.05 ? 1115 GLN B CA    1 
ATOM   16886 C C     . GLN B  1 1117 ? 12.655  66.894  72.053  1.00 22.26 ? 1115 GLN B C     1 
ATOM   16887 O O     . GLN B  1 1117 ? 12.422  65.928  72.792  1.00 23.00 ? 1115 GLN B O     1 
ATOM   16888 C CB    . GLN B  1 1117 ? 14.512  66.783  70.411  1.00 22.45 ? 1115 GLN B CB    1 
ATOM   16889 C CG    . GLN B  1 1117 ? 15.021  66.433  69.028  1.00 22.79 ? 1115 GLN B CG    1 
ATOM   16890 C CD    . GLN B  1 1117 ? 16.547  66.526  68.914  1.00 23.77 ? 1115 GLN B CD    1 
ATOM   16891 O OE1   . GLN B  1 1117 ? 17.216  67.180  69.719  1.00 21.86 ? 1115 GLN B OE1   1 
ATOM   16892 N NE2   . GLN B  1 1117 ? 17.098  65.869  67.904  1.00 21.49 ? 1115 GLN B NE2   1 
ATOM   16893 N N     . LEU B  1 1118 ? 12.686  68.147  72.504  1.00 20.76 ? 1116 LEU B N     1 
ATOM   16894 C CA    . LEU B  1 1118 ? 12.365  68.426  73.892  1.00 22.26 ? 1116 LEU B CA    1 
ATOM   16895 C C     . LEU B  1 1118 ? 10.919  68.047  74.206  1.00 22.76 ? 1116 LEU B C     1 
ATOM   16896 O O     . LEU B  1 1118 ? 10.647  67.437  75.245  1.00 22.05 ? 1116 LEU B O     1 
ATOM   16897 C CB    . LEU B  1 1118 ? 12.644  69.903  74.194  1.00 22.54 ? 1116 LEU B CB    1 
ATOM   16898 C CG    . LEU B  1 1118 ? 12.647  70.356  75.652  1.00 28.90 ? 1116 LEU B CG    1 
ATOM   16899 C CD1   . LEU B  1 1118 ? 13.625  69.553  76.468  1.00 28.67 ? 1116 LEU B CD1   1 
ATOM   16900 C CD2   . LEU B  1 1118 ? 12.982  71.850  75.745  1.00 29.85 ? 1116 LEU B CD2   1 
ATOM   16901 N N     . ALA B  1 1119 ? 9.979   68.376  73.307  1.00 20.66 ? 1117 ALA B N     1 
ATOM   16902 C CA    . ALA B  1 1119 ? 8.593   67.961  73.505  1.00 21.21 ? 1117 ALA B CA    1 
ATOM   16903 C C     . ALA B  1 1119 ? 8.489   66.451  73.661  1.00 23.74 ? 1117 ALA B C     1 
ATOM   16904 O O     . ALA B  1 1119 ? 7.759   65.958  74.532  1.00 20.97 ? 1117 ALA B O     1 
ATOM   16905 C CB    . ALA B  1 1119 ? 7.719   68.419  72.332  1.00 19.59 ? 1117 ALA B CB    1 
ATOM   16906 N N     . ALA B  1 1120 ? 9.215   65.700  72.826  1.00 21.37 ? 1118 ALA B N     1 
ATOM   16907 C CA    . ALA B  1 1120 ? 9.121   64.245  72.883  1.00 22.78 ? 1118 ALA B CA    1 
ATOM   16908 C C     . ALA B  1 1120 ? 9.622   63.730  74.222  1.00 22.58 ? 1118 ALA B C     1 
ATOM   16909 O O     . ALA B  1 1120 ? 9.032   62.813  74.809  1.00 20.87 ? 1118 ALA B O     1 
ATOM   16910 C CB    . ALA B  1 1120 ? 9.917   63.619  71.743  1.00 20.21 ? 1118 ALA B CB    1 
ATOM   16911 N N     . ALA B  1 1121 ? 10.698  64.331  74.733  1.00 23.06 ? 1119 ALA B N     1 
ATOM   16912 C CA    . ALA B  1 1121 ? 11.297  63.847  75.968  1.00 18.61 ? 1119 ALA B CA    1 
ATOM   16913 C C     . ALA B  1 1121 ? 10.488  64.262  77.188  1.00 16.92 ? 1119 ALA B C     1 
ATOM   16914 O O     . ALA B  1 1121 ? 10.310  63.463  78.116  1.00 18.06 ? 1119 ALA B O     1 
ATOM   16915 C CB    . ALA B  1 1121 ? 12.731  64.355  76.081  1.00 18.97 ? 1119 ALA B CB    1 
ATOM   16916 N N     . LEU B  1 1122 ? 10.023  65.513  77.214  1.00 17.98 ? 1120 LEU B N     1 
ATOM   16917 C CA    . LEU B  1 1122 ? 9.205   65.984  78.323  1.00 20.30 ? 1120 LEU B CA    1 
ATOM   16918 C C     . LEU B  1 1122 ? 7.877   65.242  78.385  1.00 20.71 ? 1120 LEU B C     1 
ATOM   16919 O O     . LEU B  1 1122 ? 7.420   64.879  79.470  1.00 22.39 ? 1120 LEU B O     1 
ATOM   16920 C CB    . LEU B  1 1122 ? 8.965   67.488  78.202  1.00 22.66 ? 1120 LEU B CB    1 
ATOM   16921 C CG    . LEU B  1 1122 ? 10.204  68.379  78.263  1.00 22.93 ? 1120 LEU B CG    1 
ATOM   16922 C CD1   . LEU B  1 1122 ? 9.819   69.812  77.966  1.00 23.83 ? 1120 LEU B CD1   1 
ATOM   16923 C CD2   . LEU B  1 1122 ? 10.903  68.260  79.632  1.00 21.27 ? 1120 LEU B CD2   1 
ATOM   16924 N N     . ALA B  1 1123 ? 7.258   64.987  77.227  1.00 20.63 ? 1121 ALA B N     1 
ATOM   16925 C CA    . ALA B  1 1123 ? 5.983   64.274  77.201  1.00 22.86 ? 1121 ALA B CA    1 
ATOM   16926 C C     . ALA B  1 1123 ? 6.089   62.876  77.793  1.00 23.34 ? 1121 ALA B C     1 
ATOM   16927 O O     . ALA B  1 1123 ? 5.082   62.337  78.270  1.00 21.53 ? 1121 ALA B O     1 
ATOM   16928 C CB    . ALA B  1 1123 ? 5.457   64.172  75.767  1.00 20.31 ? 1121 ALA B CB    1 
ATOM   16929 N N     . THR B  1 1124 ? 7.282   62.284  77.788  1.00 17.50 ? 1122 THR B N     1 
ATOM   16930 C CA    . THR B  1 1124 ? 7.477   60.963  78.356  1.00 17.48 ? 1122 THR B CA    1 
ATOM   16931 C C     . THR B  1 1124 ? 8.134   61.025  79.736  1.00 16.69 ? 1122 THR B C     1 
ATOM   16932 O O     . THR B  1 1124 ? 8.660   60.019  80.205  1.00 19.80 ? 1122 THR B O     1 
ATOM   16933 C CB    . THR B  1 1124 ? 8.279   60.085  77.394  1.00 19.43 ? 1122 THR B CB    1 
ATOM   16934 O OG1   . THR B  1 1124 ? 9.389   60.829  76.869  1.00 20.94 ? 1122 THR B OG1   1 
ATOM   16935 C CG2   . THR B  1 1124 ? 7.378   59.633  76.209  1.00 19.58 ? 1122 THR B CG2   1 
ATOM   16936 N N     . GLY B  1 1125 ? 8.067   62.175  80.395  1.00 19.57 ? 1123 GLY B N     1 
ATOM   16937 C CA    . GLY B  1 1125 ? 8.497   62.316  81.775  1.00 19.09 ? 1123 GLY B CA    1 
ATOM   16938 C C     . GLY B  1 1125 ? 9.987   62.489  81.977  1.00 21.02 ? 1123 GLY B C     1 
ATOM   16939 O O     . GLY B  1 1125 ? 10.439  62.507  83.127  1.00 22.96 ? 1123 GLY B O     1 
ATOM   16940 N N     . ASN B  1 1126 ? 10.761  62.646  80.908  1.00 17.40 ? 1124 ASN B N     1 
ATOM   16941 C CA    . ASN B  1 1126 ? 12.215  62.642  80.994  1.00 19.00 ? 1124 ASN B CA    1 
ATOM   16942 C C     . ASN B  1 1126 ? 12.795  64.035  81.223  1.00 20.91 ? 1124 ASN B C     1 
ATOM   16943 O O     . ASN B  1 1126 ? 12.181  65.056  80.922  1.00 20.82 ? 1124 ASN B O     1 
ATOM   16944 C CB    . ASN B  1 1126 ? 12.810  62.047  79.720  1.00 18.89 ? 1124 ASN B CB    1 
ATOM   16945 C CG    . ASN B  1 1126 ? 12.363  60.622  79.487  1.00 19.35 ? 1124 ASN B CG    1 
ATOM   16946 O OD1   . ASN B  1 1126 ? 12.723  59.743  80.247  1.00 19.64 ? 1124 ASN B OD1   1 
ATOM   16947 N ND2   . ASN B  1 1126 ? 11.549  60.395  78.451  1.00 19.08 ? 1124 ASN B ND2   1 
ATOM   16948 N N     . SER B  1 1127 ? 13.994  64.057  81.804  1.00 22.76 ? 1125 SER B N     1 
ATOM   16949 C CA    . SER B  1 1127 ? 14.859  65.220  81.698  1.00 21.11 ? 1125 SER B CA    1 
ATOM   16950 C C     . SER B  1 1127 ? 15.735  65.057  80.452  1.00 24.56 ? 1125 SER B C     1 
ATOM   16951 O O     . SER B  1 1127 ? 15.710  64.019  79.788  1.00 22.93 ? 1125 SER B O     1 
ATOM   16952 C CB    . SER B  1 1127 ? 15.712  65.372  82.961  1.00 21.47 ? 1125 SER B CB    1 
ATOM   16953 O OG    . SER B  1 1127 ? 16.616  64.286  83.065  1.00 26.84 ? 1125 SER B OG    1 
ATOM   16954 N N     . VAL B  1 1128 ? 16.512  66.093  80.123  1.00 21.10 ? 1126 VAL B N     1 
ATOM   16955 C CA    . VAL B  1 1128 ? 17.329  66.075  78.913  1.00 20.54 ? 1126 VAL B CA    1 
ATOM   16956 C C     . VAL B  1 1128 ? 18.714  66.645  79.175  1.00 23.73 ? 1126 VAL B C     1 
ATOM   16957 O O     . VAL B  1 1128 ? 18.940  67.405  80.119  1.00 25.70 ? 1126 VAL B O     1 
ATOM   16958 C CB    . VAL B  1 1128 ? 16.681  66.844  77.743  1.00 22.68 ? 1126 VAL B CB    1 
ATOM   16959 C CG1   . VAL B  1 1128 ? 15.285  66.317  77.486  1.00 22.91 ? 1126 VAL B CG1   1 
ATOM   16960 C CG2   . VAL B  1 1128 ? 16.665  68.347  78.016  1.00 21.23 ? 1126 VAL B CG2   1 
ATOM   16961 N N     . ALA B  1 1129 ? 19.647  66.247  78.318  1.00 21.30 ? 1127 ALA B N     1 
ATOM   16962 C CA    . ALA B  1 1129 ? 20.938  66.908  78.192  1.00 23.72 ? 1127 ALA B CA    1 
ATOM   16963 C C     . ALA B  1 1129 ? 21.097  67.260  76.728  1.00 24.27 ? 1127 ALA B C     1 
ATOM   16964 O O     . ALA B  1 1129 ? 21.063  66.368  75.871  1.00 22.02 ? 1127 ALA B O     1 
ATOM   16965 C CB    . ALA B  1 1129 ? 22.078  66.011  78.662  1.00 23.38 ? 1127 ALA B CB    1 
ATOM   16966 N N     . ILE B  1 1130 ? 21.218  68.551  76.440  1.00 20.59 ? 1128 ILE B N     1 
ATOM   16967 C CA    . ILE B  1 1130 ? 21.285  69.042  75.075  1.00 21.83 ? 1128 ILE B CA    1 
ATOM   16968 C C     . ILE B  1 1130 ? 22.743  69.225  74.700  1.00 23.67 ? 1128 ILE B C     1 
ATOM   16969 O O     . ILE B  1 1130 ? 23.542  69.772  75.480  1.00 25.75 ? 1128 ILE B O     1 
ATOM   16970 C CB    . ILE B  1 1130 ? 20.496  70.352  74.904  1.00 25.41 ? 1128 ILE B CB    1 
ATOM   16971 C CG1   . ILE B  1 1130 ? 19.047  70.190  75.389  1.00 22.71 ? 1128 ILE B CG1   1 
ATOM   16972 C CG2   . ILE B  1 1130 ? 20.477  70.769  73.456  1.00 22.12 ? 1128 ILE B CG2   1 
ATOM   16973 C CD1   . ILE B  1 1130 ? 18.343  71.530  75.549  1.00 25.37 ? 1128 ILE B CD1   1 
ATOM   16974 N N     . ASP B  1 1131 ? 23.091  68.740  73.516  1.00 22.70 ? 1129 ASP B N     1 
ATOM   16975 C CA    . ASP B  1 1131 ? 24.435  68.895  72.982  1.00 23.75 ? 1129 ASP B CA    1 
ATOM   16976 C C     . ASP B  1 1131 ? 24.800  70.373  72.873  1.00 25.14 ? 1129 ASP B C     1 
ATOM   16977 O O     . ASP B  1 1131 ? 24.174  71.118  72.116  1.00 27.14 ? 1129 ASP B O     1 
ATOM   16978 C CB    . ASP B  1 1131 ? 24.500  68.219  71.613  1.00 24.81 ? 1129 ASP B CB    1 
ATOM   16979 C CG    . ASP B  1 1131 ? 25.875  68.291  70.993  1.00 26.45 ? 1129 ASP B CG    1 
ATOM   16980 O OD1   . ASP B  1 1131 ? 26.867  68.243  71.756  1.00 25.32 ? 1129 ASP B OD1   1 
ATOM   16981 O OD2   . ASP B  1 1131 ? 25.957  68.405  69.750  1.00 25.59 ? 1129 ASP B OD2   1 
ATOM   16982 N N     . ALA B  1 1132 ? 25.826  70.793  73.624  1.00 26.01 ? 1130 ALA B N     1 
ATOM   16983 C CA    . ALA B  1 1132 ? 26.207  72.207  73.639  1.00 27.41 ? 1130 ALA B CA    1 
ATOM   16984 C C     . ALA B  1 1132 ? 26.806  72.654  72.311  1.00 29.58 ? 1130 ALA B C     1 
ATOM   16985 O O     . ALA B  1 1132 ? 26.705  73.832  71.955  1.00 32.48 ? 1130 ALA B O     1 
ATOM   16986 C CB    . ALA B  1 1132 ? 27.197  72.479  74.771  1.00 27.65 ? 1130 ALA B CB    1 
ATOM   16987 N N     . ALA B  1 1133 ? 27.429  71.737  71.566  1.00 27.01 ? 1131 ALA B N     1 
ATOM   16988 C CA    . ALA B  1 1133 ? 27.984  72.085  70.263  1.00 32.26 ? 1131 ALA B CA    1 
ATOM   16989 C C     . ALA B  1 1133 ? 26.909  72.432  69.250  1.00 30.36 ? 1131 ALA B C     1 
ATOM   16990 O O     . ALA B  1 1133 ? 27.241  72.953  68.179  1.00 31.03 ? 1131 ALA B O     1 
ATOM   16991 C CB    . ALA B  1 1133 ? 28.840  70.937  69.720  1.00 32.94 ? 1131 ALA B CB    1 
ATOM   16992 N N     . SER B  1 1134 ? 25.638  72.152  69.553  1.00 30.96 ? 1132 SER B N     1 
ATOM   16993 C CA    . SER B  1 1134 ? 24.557  72.581  68.673  1.00 30.41 ? 1132 SER B CA    1 
ATOM   16994 C C     . SER B  1 1134 ? 24.507  74.098  68.545  1.00 27.43 ? 1132 SER B C     1 
ATOM   16995 O O     . SER B  1 1134 ? 24.002  74.609  67.544  1.00 30.62 ? 1132 SER B O     1 
ATOM   16996 C CB    . SER B  1 1134 ? 23.206  72.056  69.185  1.00 30.86 ? 1132 SER B CB    1 
ATOM   16997 O OG    . SER B  1 1134 ? 22.823  72.720  70.383  1.00 25.67 ? 1132 SER B OG    1 
ATOM   16998 N N     . GLY B  1 1135 ? 25.025  74.823  69.530  1.00 28.80 ? 1133 GLY B N     1 
ATOM   16999 C CA    . GLY B  1 1135 ? 24.989  76.270  69.504  1.00 30.24 ? 1133 GLY B CA    1 
ATOM   17000 C C     . GLY B  1 1135 ? 23.612  76.879  69.655  1.00 36.37 ? 1133 GLY B C     1 
ATOM   17001 O O     . GLY B  1 1135 ? 23.425  78.053  69.322  1.00 31.70 ? 1133 GLY B O     1 
ATOM   17002 N N     . LEU B  1 1136 ? 22.636  76.124  70.168  1.00 33.21 ? 1134 LEU B N     1 
ATOM   17003 C CA    . LEU B  1 1136 ? 21.253  76.584  70.229  1.00 33.81 ? 1134 LEU B CA    1 
ATOM   17004 C C     . LEU B  1 1136 ? 20.873  77.106  71.608  1.00 31.99 ? 1134 LEU B C     1 
ATOM   17005 O O     . LEU B  1 1136 ? 19.680  77.146  71.940  1.00 32.02 ? 1134 LEU B O     1 
ATOM   17006 C CB    . LEU B  1 1136 ? 20.311  75.456  69.809  1.00 30.19 ? 1134 LEU B CB    1 
ATOM   17007 C CG    . LEU B  1 1136 ? 20.434  75.060  68.341  1.00 30.13 ? 1134 LEU B CG    1 
ATOM   17008 C CD1   . LEU B  1 1136 ? 19.770  73.718  68.088  1.00 28.58 ? 1134 LEU B CD1   1 
ATOM   17009 C CD2   . LEU B  1 1136 ? 19.843  76.155  67.445  1.00 32.15 ? 1134 LEU B CD2   1 
ATOM   17010 N N     . GLN B  1 1137 ? 21.862  77.509  72.413  1.00 33.95 ? 1135 GLN B N     1 
ATOM   17011 C CA    . GLN B  1 1137 ? 21.599  77.906  73.795  1.00 33.54 ? 1135 GLN B CA    1 
ATOM   17012 C C     . GLN B  1 1137 ? 20.599  79.056  73.876  1.00 38.01 ? 1135 GLN B C     1 
ATOM   17013 O O     . GLN B  1 1137 ? 19.754  79.089  74.780  1.00 41.65 ? 1135 GLN B O     1 
ATOM   17014 C CB    . GLN B  1 1137 ? 22.909  78.279  74.496  1.00 33.38 ? 1135 GLN B CB    1 
ATOM   17015 C CG    . GLN B  1 1137 ? 23.796  77.094  74.908  1.00 34.87 ? 1135 GLN B CG    1 
ATOM   17016 C CD    . GLN B  1 1137 ? 24.647  76.563  73.764  1.00 33.36 ? 1135 GLN B CD    1 
ATOM   17017 O OE1   . GLN B  1 1137 ? 24.394  76.858  72.596  1.00 35.47 ? 1135 GLN B OE1   1 
ATOM   17018 N NE2   . GLN B  1 1137 ? 25.670  75.788  74.098  1.00 31.07 ? 1135 GLN B NE2   1 
ATOM   17019 N N     . ALA B  1 1138 ? 20.661  79.997  72.932  1.00 35.81 ? 1136 ALA B N     1 
ATOM   17020 C CA    . ALA B  1 1138 ? 19.773  81.154  72.968  1.00 38.73 ? 1136 ALA B CA    1 
ATOM   17021 C C     . ALA B  1 1138 ? 18.330  80.818  72.611  1.00 39.56 ? 1136 ALA B C     1 
ATOM   17022 O O     . ALA B  1 1138 ? 17.462  81.684  72.754  1.00 39.18 ? 1136 ALA B O     1 
ATOM   17023 C CB    . ALA B  1 1138 ? 20.287  82.240  72.027  1.00 32.85 ? 1136 ALA B CB    1 
ATOM   17024 N N     . SER B  1 1139 ? 18.051  79.596  72.148  1.00 39.23 ? 1137 SER B N     1 
ATOM   17025 C CA    . SER B  1 1139 ? 16.692  79.204  71.787  1.00 37.09 ? 1137 SER B CA    1 
ATOM   17026 C C     . SER B  1 1139 ? 15.833  78.871  72.995  1.00 34.00 ? 1137 SER B C     1 
ATOM   17027 O O     . SER B  1 1139 ? 14.612  78.763  72.859  1.00 36.28 ? 1137 SER B O     1 
ATOM   17028 C CB    . SER B  1 1139 ? 16.717  77.992  70.856  1.00 34.09 ? 1137 SER B CB    1 
ATOM   17029 O OG    . SER B  1 1139 ? 17.240  78.332  69.587  1.00 36.34 ? 1137 SER B OG    1 
ATOM   17030 N N     . LEU B  1 1140 ? 16.440  78.676  74.157  1.00 33.50 ? 1138 LEU B N     1 
ATOM   17031 C CA    . LEU B  1 1140 ? 15.723  78.350  75.381  1.00 39.53 ? 1138 LEU B CA    1 
ATOM   17032 C C     . LEU B  1 1140 ? 15.778  79.515  76.356  1.00 35.18 ? 1138 LEU B C     1 
ATOM   17033 O O     . LEU B  1 1140 ? 15.921  79.332  77.565  1.00 41.73 ? 1138 LEU B O     1 
ATOM   17034 C CB    . LEU B  1 1140 ? 16.279  77.079  76.018  1.00 34.63 ? 1138 LEU B CB    1 
ATOM   17035 C CG    . LEU B  1 1140 ? 16.124  75.841  75.135  1.00 35.45 ? 1138 LEU B CG    1 
ATOM   17036 C CD1   . LEU B  1 1140 ? 16.472  74.566  75.898  1.00 36.23 ? 1138 LEU B CD1   1 
ATOM   17037 C CD2   . LEU B  1 1140 ? 14.710  75.764  74.554  1.00 33.86 ? 1138 LEU B CD2   1 
ATOM   17038 N N     . LYS B  1 1141 ? 15.683  80.728  75.820  1.00 38.71 ? 1139 LYS B N     1 
ATOM   17039 C CA    . LYS B  1 1141 ? 15.691  81.924  76.649  1.00 40.98 ? 1139 LYS B CA    1 
ATOM   17040 C C     . LYS B  1 1141 ? 14.377  82.045  77.411  1.00 43.55 ? 1139 LYS B C     1 
ATOM   17041 O O     . LYS B  1 1141 ? 13.297  81.918  76.827  1.00 44.52 ? 1139 LYS B O     1 
ATOM   17042 C CB    . LYS B  1 1141 ? 15.912  83.166  75.782  1.00 39.75 ? 1139 LYS B CB    1 
ATOM   17043 N N     . ASN B  1 1142 ? 14.475  82.287  78.718  1.00 44.40 ? 1140 ASN B N     1 
ATOM   17044 C CA    . ASN B  1 1142 ? 13.314  82.590  79.558  1.00 46.63 ? 1140 ASN B CA    1 
ATOM   17045 C C     . ASN B  1 1142 ? 12.352  81.405  79.633  1.00 41.41 ? 1140 ASN B C     1 
ATOM   17046 O O     . ASN B  1 1142 ? 11.132  81.571  79.578  1.00 40.32 ? 1140 ASN B O     1 
ATOM   17047 C CB    . ASN B  1 1142 ? 12.592  83.850  79.074  1.00 47.22 ? 1140 ASN B CB    1 
ATOM   17048 N N     . LEU B  1 1143 ? 12.909  80.201  79.759  1.00 42.17 ? 1141 LEU B N     1 
ATOM   17049 C CA    . LEU B  1 1143 ? 12.105  79.011  79.997  1.00 42.65 ? 1141 LEU B CA    1 
ATOM   17050 C C     . LEU B  1 1143 ? 11.408  79.100  81.354  1.00 39.32 ? 1141 LEU B C     1 
ATOM   17051 O O     . LEU B  1 1143 ? 11.951  79.672  82.303  1.00 42.13 ? 1141 LEU B O     1 
ATOM   17052 C CB    . LEU B  1 1143 ? 12.978  77.757  79.980  1.00 38.16 ? 1141 LEU B CB    1 
ATOM   17053 C CG    . LEU B  1 1143 ? 13.170  76.911  78.724  1.00 36.96 ? 1141 LEU B CG    1 
ATOM   17054 C CD1   . LEU B  1 1143 ? 13.905  75.643  79.115  1.00 34.47 ? 1141 LEU B CD1   1 
ATOM   17055 C CD2   . LEU B  1 1143 ? 11.846  76.577  78.044  1.00 33.19 ? 1141 LEU B CD2   1 
ATOM   17056 N N     . PRO B  1 1144 ? 10.216  78.516  81.481  1.00 39.42 ? 1142 PRO B N     1 
ATOM   17057 C CA    . PRO B  1 1144 ? 9.636   78.331  82.816  1.00 35.95 ? 1142 PRO B CA    1 
ATOM   17058 C C     . PRO B  1 1144 ? 10.575  77.521  83.692  1.00 37.09 ? 1142 PRO B C     1 
ATOM   17059 O O     . PRO B  1 1144 ? 11.225  76.582  83.228  1.00 38.43 ? 1142 PRO B O     1 
ATOM   17060 C CB    . PRO B  1 1144 ? 8.332   77.571  82.540  1.00 39.25 ? 1142 PRO B CB    1 
ATOM   17061 C CG    . PRO B  1 1144 ? 8.011   77.875  81.111  1.00 36.94 ? 1142 PRO B CG    1 
ATOM   17062 C CD    . PRO B  1 1144 ? 9.333   78.006  80.416  1.00 39.21 ? 1142 PRO B CD    1 
ATOM   17063 N N     . GLN B  1 1145 ? 10.634  77.891  84.976  1.00 37.46 ? 1143 GLN B N     1 
ATOM   17064 C CA    . GLN B  1 1145 ? 11.520  77.202  85.907  1.00 33.80 ? 1143 GLN B CA    1 
ATOM   17065 C C     . GLN B  1 1145 ? 11.261  75.702  85.928  1.00 34.42 ? 1143 GLN B C     1 
ATOM   17066 O O     . GLN B  1 1145 ? 12.193  74.917  86.134  1.00 31.92 ? 1143 GLN B O     1 
ATOM   17067 C CB    . GLN B  1 1145 ? 11.366  77.781  87.315  1.00 40.87 ? 1143 GLN B CB    1 
ATOM   17068 N N     . THR B  1 1146 ? 10.008  75.288  85.722  1.00 33.81 ? 1144 THR B N     1 
ATOM   17069 C CA    . THR B  1 1146 ? 9.685   73.863  85.716  1.00 32.85 ? 1144 THR B CA    1 
ATOM   17070 C C     . THR B  1 1146 ? 10.348  73.158  84.545  1.00 29.96 ? 1144 THR B C     1 
ATOM   17071 O O     . THR B  1 1146 ? 10.792  72.012  84.674  1.00 32.01 ? 1144 THR B O     1 
ATOM   17072 C CB    . THR B  1 1146 ? 8.168   73.662  85.651  1.00 34.92 ? 1144 THR B CB    1 
ATOM   17073 O OG1   . THR B  1 1146 ? 7.634   74.491  84.616  1.00 32.62 ? 1144 THR B OG1   1 
ATOM   17074 C CG2   . THR B  1 1146 ? 7.511   74.036  86.973  1.00 37.33 ? 1144 THR B CG2   1 
ATOM   17075 N N     . VAL B  1 1147 ? 10.413  73.819  83.388  1.00 25.95 ? 1145 VAL B N     1 
ATOM   17076 C CA    . VAL B  1 1147 ? 11.088  73.207  82.252  1.00 30.07 ? 1145 VAL B CA    1 
ATOM   17077 C C     . VAL B  1 1147 ? 12.602  73.311  82.410  1.00 29.33 ? 1145 VAL B C     1 
ATOM   17078 O O     . VAL B  1 1147 ? 13.331  72.347  82.150  1.00 29.82 ? 1145 VAL B O     1 
ATOM   17079 C CB    . VAL B  1 1147 ? 10.602  73.832  80.930  1.00 30.90 ? 1145 VAL B CB    1 
ATOM   17080 C CG1   . VAL B  1 1147 ? 11.203  73.085  79.746  1.00 29.76 ? 1145 VAL B CG1   1 
ATOM   17081 C CG2   . VAL B  1 1147 ? 9.076   73.818  80.850  1.00 28.33 ? 1145 VAL B CG2   1 
ATOM   17082 N N     . GLY B  1 1148 ? 13.093  74.465  82.874  1.00 29.81 ? 1146 GLY B N     1 
ATOM   17083 C CA    . GLY B  1 1148 ? 14.528  74.627  83.066  1.00 30.07 ? 1146 GLY B CA    1 
ATOM   17084 C C     . GLY B  1 1148 ? 15.136  73.574  83.973  1.00 30.85 ? 1146 GLY B C     1 
ATOM   17085 O O     . GLY B  1 1148 ? 16.252  73.103  83.731  1.00 31.07 ? 1146 GLY B O     1 
ATOM   17086 N N     . LEU B  1 1149 ? 14.413  73.177  85.026  1.00 27.04 ? 1147 LEU B N     1 
ATOM   17087 C CA    . LEU B  1 1149 ? 14.960  72.203  85.965  1.00 27.86 ? 1147 LEU B CA    1 
ATOM   17088 C C     . LEU B  1 1149 ? 15.186  70.849  85.313  1.00 29.41 ? 1147 LEU B C     1 
ATOM   17089 O O     . LEU B  1 1149 ? 15.964  70.043  85.831  1.00 28.78 ? 1147 LEU B O     1 
ATOM   17090 C CB    . LEU B  1 1149 ? 14.039  72.048  87.182  1.00 31.89 ? 1147 LEU B CB    1 
ATOM   17091 N N     . ARG B  1 1150 ? 14.546  70.591  84.175  1.00 24.97 ? 1148 ARG B N     1 
ATOM   17092 C CA    . ARG B  1 1150 ? 14.739  69.347  83.444  1.00 28.54 ? 1148 ARG B CA    1 
ATOM   17093 C C     . ARG B  1 1150 ? 15.785  69.453  82.346  1.00 26.95 ? 1148 ARG B C     1 
ATOM   17094 O O     . ARG B  1 1150 ? 16.077  68.451  81.684  1.00 25.29 ? 1148 ARG B O     1 
ATOM   17095 C CB    . ARG B  1 1150 ? 13.416  68.899  82.831  1.00 23.31 ? 1148 ARG B CB    1 
ATOM   17096 C CG    . ARG B  1 1150 ? 12.434  68.334  83.838  1.00 28.71 ? 1148 ARG B CG    1 
ATOM   17097 C CD    . ARG B  1 1150 ? 11.711  67.161  83.217  1.00 27.75 ? 1148 ARG B CD    1 
ATOM   17098 N NE    . ARG B  1 1150 ? 10.513  66.789  83.955  1.00 26.34 ? 1148 ARG B NE    1 
ATOM   17099 C CZ    . ARG B  1 1150 ? 9.463   66.216  83.386  1.00 28.88 ? 1148 ARG B CZ    1 
ATOM   17100 N NH1   . ARG B  1 1150 ? 9.463   65.917  82.096  1.00 23.02 ? 1148 ARG B NH1   1 
ATOM   17101 N NH2   . ARG B  1 1150 ? 8.389   65.946  84.123  1.00 26.11 ? 1148 ARG B NH2   1 
ATOM   17102 N N     . VAL B  1 1151 ? 16.324  70.643  82.109  1.00 25.94 ? 1149 VAL B N     1 
ATOM   17103 C CA    . VAL B  1 1151 ? 17.182  70.901  80.962  1.00 26.66 ? 1149 VAL B CA    1 
ATOM   17104 C C     . VAL B  1 1151 ? 18.600  71.127  81.449  1.00 29.65 ? 1149 VAL B C     1 
ATOM   17105 O O     . VAL B  1 1151 ? 18.836  71.961  82.329  1.00 27.45 ? 1149 VAL B O     1 
ATOM   17106 C CB    . VAL B  1 1151 ? 16.694  72.111  80.150  1.00 29.08 ? 1149 VAL B CB    1 
ATOM   17107 C CG1   . VAL B  1 1151 ? 17.724  72.468  79.062  1.00 30.30 ? 1149 VAL B CG1   1 
ATOM   17108 C CG2   . VAL B  1 1151 ? 15.334  71.821  79.547  1.00 26.01 ? 1149 VAL B CG2   1 
ATOM   17109 N N     . SER B  1 1152 ? 19.538  70.383  80.882  1.00 26.39 ? 1150 SER B N     1 
ATOM   17110 C CA    . SER B  1 1152 ? 20.950  70.655  81.071  1.00 30.91 ? 1150 SER B CA    1 
ATOM   17111 C C     . SER B  1 1152 ? 21.621  70.682  79.706  1.00 29.49 ? 1150 SER B C     1 
ATOM   17112 O O     . SER B  1 1152 ? 21.070  70.209  78.707  1.00 26.55 ? 1150 SER B O     1 
ATOM   17113 C CB    . SER B  1 1152 ? 21.605  69.617  81.995  1.00 26.36 ? 1150 SER B CB    1 
ATOM   17114 O OG    . SER B  1 1152 ? 21.507  68.319  81.450  1.00 30.35 ? 1150 SER B OG    1 
ATOM   17115 N N     . TRP B  1 1153 ? 22.804  71.273  79.667  1.00 23.81 ? 1151 TRP B N     1 
ATOM   17116 C CA    . TRP B  1 1153 ? 23.616  71.344  78.464  1.00 25.39 ? 1151 TRP B CA    1 
ATOM   17117 C C     . TRP B  1 1153 ? 24.893  70.555  78.711  1.00 26.07 ? 1151 TRP B C     1 
ATOM   17118 O O     . TRP B  1 1153 ? 25.477  70.636  79.799  1.00 26.64 ? 1151 TRP B O     1 
ATOM   17119 C CB    . TRP B  1 1153 ? 23.932  72.805  78.091  1.00 25.62 ? 1151 TRP B CB    1 
ATOM   17120 C CG    . TRP B  1 1153 ? 22.695  73.571  77.671  1.00 33.06 ? 1151 TRP B CG    1 
ATOM   17121 C CD1   . TRP B  1 1153 ? 21.783  74.176  78.496  1.00 30.23 ? 1151 TRP B CD1   1 
ATOM   17122 C CD2   . TRP B  1 1153 ? 22.221  73.783  76.328  1.00 29.35 ? 1151 TRP B CD2   1 
ATOM   17123 N NE1   . TRP B  1 1153 ? 20.783  74.755  77.749  1.00 31.30 ? 1151 TRP B NE1   1 
ATOM   17124 C CE2   . TRP B  1 1153 ? 21.030  74.533  76.419  1.00 30.76 ? 1151 TRP B CE2   1 
ATOM   17125 C CE3   . TRP B  1 1153 ? 22.699  73.429  75.061  1.00 30.02 ? 1151 TRP B CE3   1 
ATOM   17126 C CZ2   . TRP B  1 1153 ? 20.306  74.928  75.291  1.00 32.31 ? 1151 TRP B CZ2   1 
ATOM   17127 C CZ3   . TRP B  1 1153 ? 21.973  73.827  73.937  1.00 26.87 ? 1151 TRP B CZ3   1 
ATOM   17128 C CH2   . TRP B  1 1153 ? 20.793  74.562  74.063  1.00 30.51 ? 1151 TRP B CH2   1 
ATOM   17129 N N     . SER B  1 1154 ? 25.311  69.778  77.713  1.00 22.83 ? 1152 SER B N     1 
ATOM   17130 C CA    . SER B  1 1154 ? 26.497  68.939  77.829  1.00 30.24 ? 1152 SER B CA    1 
ATOM   17131 C C     . SER B  1 1154 ? 27.468  69.195  76.684  1.00 26.14 ? 1152 SER B C     1 
ATOM   17132 O O     . SER B  1 1154 ? 27.089  69.105  75.510  1.00 27.56 ? 1152 SER B O     1 
ATOM   17133 C CB    . SER B  1 1154 ? 26.120  67.462  77.844  1.00 29.08 ? 1152 SER B CB    1 
ATOM   17134 O OG    . SER B  1 1154 ? 27.282  66.671  78.025  1.00 25.03 ? 1152 SER B OG    1 
ATOM   17135 N N     . LYS B  1 1155 ? 28.720  69.492  77.034  1.00 29.02 ? 1153 LYS B N     1 
ATOM   17136 C CA    . LYS B  1 1155 ? 29.840  69.473  76.100  1.00 27.67 ? 1153 LYS B CA    1 
ATOM   17137 C C     . LYS B  1 1155 ? 30.617  68.168  76.172  1.00 29.97 ? 1153 LYS B C     1 
ATOM   17138 O O     . LYS B  1 1155 ? 31.583  67.986  75.425  1.00 35.25 ? 1153 LYS B O     1 
ATOM   17139 C CB    . LYS B  1 1155 ? 30.795  70.644  76.381  1.00 27.81 ? 1153 LYS B CB    1 
ATOM   17140 N N     . ASP B  1 1156 ? 30.226  67.264  77.065  1.00 26.95 ? 1154 ASP B N     1 
ATOM   17141 C CA    . ASP B  1 1156 ? 31.015  66.073  77.380  1.00 25.78 ? 1154 ASP B CA    1 
ATOM   17142 C C     . ASP B  1 1156 ? 30.006  64.983  77.742  1.00 23.33 ? 1154 ASP B C     1 
ATOM   17143 O O     . ASP B  1 1156 ? 29.651  64.817  78.909  1.00 23.57 ? 1154 ASP B O     1 
ATOM   17144 C CB    . ASP B  1 1156 ? 32.003  66.357  78.509  1.00 25.28 ? 1154 ASP B CB    1 
ATOM   17145 C CG    . ASP B  1 1156 ? 32.917  65.178  78.811  1.00 21.75 ? 1154 ASP B CG    1 
ATOM   17146 O OD1   . ASP B  1 1156 ? 32.625  64.053  78.376  1.00 22.26 ? 1154 ASP B OD1   1 
ATOM   17147 O OD2   . ASP B  1 1156 ? 33.935  65.382  79.495  1.00 26.54 ? 1154 ASP B OD2   1 
ATOM   17148 N N     . TRP B  1 1157 ? 29.529  64.270  76.716  1.00 24.98 ? 1155 TRP B N     1 
ATOM   17149 C CA    . TRP B  1 1157 ? 28.437  63.327  76.914  1.00 26.29 ? 1155 TRP B CA    1 
ATOM   17150 C C     . TRP B  1 1157 ? 28.838  62.182  77.835  1.00 27.66 ? 1155 TRP B C     1 
ATOM   17151 O O     . TRP B  1 1157 ? 28.026  61.718  78.643  1.00 25.51 ? 1155 TRP B O     1 
ATOM   17152 C CB    . TRP B  1 1157 ? 27.967  62.766  75.574  1.00 24.14 ? 1155 TRP B CB    1 
ATOM   17153 C CG    . TRP B  1 1157 ? 27.596  63.776  74.543  1.00 22.82 ? 1155 TRP B CG    1 
ATOM   17154 C CD1   . TRP B  1 1157 ? 27.420  65.118  74.704  1.00 21.71 ? 1155 TRP B CD1   1 
ATOM   17155 C CD2   . TRP B  1 1157 ? 27.343  63.495  73.163  1.00 23.31 ? 1155 TRP B CD2   1 
ATOM   17156 N NE1   . TRP B  1 1157 ? 27.062  65.693  73.491  1.00 22.03 ? 1155 TRP B NE1   1 
ATOM   17157 C CE2   . TRP B  1 1157 ? 27.021  64.708  72.537  1.00 22.74 ? 1155 TRP B CE2   1 
ATOM   17158 C CE3   . TRP B  1 1157 ? 27.359  62.325  72.401  1.00 22.99 ? 1155 TRP B CE3   1 
ATOM   17159 C CZ2   . TRP B  1 1157 ? 26.714  64.783  71.176  1.00 22.61 ? 1155 TRP B CZ2   1 
ATOM   17160 C CZ3   . TRP B  1 1157 ? 27.057  62.404  71.053  1.00 24.96 ? 1155 TRP B CZ3   1 
ATOM   17161 C CH2   . TRP B  1 1157 ? 26.736  63.619  70.459  1.00 23.40 ? 1155 TRP B CH2   1 
ATOM   17162 N N     . ALA B  1 1158 ? 30.077  61.699  77.709  1.00 26.34 ? 1156 ALA B N     1 
ATOM   17163 C CA    . ALA B  1 1158 ? 30.515  60.567  78.520  1.00 28.01 ? 1156 ALA B CA    1 
ATOM   17164 C C     . ALA B  1 1158 ? 30.585  60.938  79.993  1.00 26.23 ? 1156 ALA B C     1 
ATOM   17165 O O     . ALA B  1 1158 ? 30.237  60.125  80.858  1.00 29.92 ? 1156 ALA B O     1 
ATOM   17166 C CB    . ALA B  1 1158 ? 31.875  60.060  78.038  1.00 24.59 ? 1156 ALA B CB    1 
ATOM   17167 N N     . ALA B  1 1159 ? 31.035  62.157  80.303  1.00 23.75 ? 1157 ALA B N     1 
ATOM   17168 C CA    . ALA B  1 1159 ? 31.123  62.580  81.695  1.00 27.05 ? 1157 ALA B CA    1 
ATOM   17169 C C     . ALA B  1 1159 ? 29.774  62.966  82.284  1.00 26.43 ? 1157 ALA B C     1 
ATOM   17170 O O     . ALA B  1 1159 ? 29.622  62.938  83.507  1.00 26.19 ? 1157 ALA B O     1 
ATOM   17171 C CB    . ALA B  1 1159 ? 32.095  63.754  81.846  1.00 25.80 ? 1157 ALA B CB    1 
ATOM   17172 N N     . ASP B  1 1160 ? 28.795  63.315  81.453  1.00 23.48 ? 1158 ASP B N     1 
ATOM   17173 C CA    . ASP B  1 1160 ? 27.517  63.817  81.930  1.00 26.22 ? 1158 ASP B CA    1 
ATOM   17174 C C     . ASP B  1 1160 ? 26.440  62.744  82.005  1.00 27.21 ? 1158 ASP B C     1 
ATOM   17175 O O     . ASP B  1 1160 ? 25.329  63.032  82.456  1.00 31.06 ? 1158 ASP B O     1 
ATOM   17176 C CB    . ASP B  1 1160 ? 27.050  64.972  81.035  1.00 25.10 ? 1158 ASP B CB    1 
ATOM   17177 C CG    . ASP B  1 1160 ? 27.930  66.209  81.191  1.00 28.92 ? 1158 ASP B CG    1 
ATOM   17178 O OD1   . ASP B  1 1160 ? 28.686  66.266  82.187  1.00 32.36 ? 1158 ASP B OD1   1 
ATOM   17179 O OD2   . ASP B  1 1160 ? 27.886  67.111  80.324  1.00 31.59 ? 1158 ASP B OD2   1 
ATOM   17180 N N     . GLY B  1 1161 ? 26.731  61.526  81.575  1.00 26.13 ? 1159 GLY B N     1 
ATOM   17181 C CA    . GLY B  1 1161 ? 25.751  60.471  81.603  1.00 24.09 ? 1159 GLY B CA    1 
ATOM   17182 C C     . GLY B  1 1161 ? 25.638  59.820  82.966  1.00 28.71 ? 1159 GLY B C     1 
ATOM   17183 O O     . GLY B  1 1161 ? 26.078  60.361  83.982  1.00 25.90 ? 1159 GLY B O     1 
ATOM   17184 N N     . PRO B  1 1162 ? 25.046  58.628  83.009  1.00 30.82 ? 1160 PRO B N     1 
ATOM   17185 C CA    . PRO B  1 1162 ? 24.509  57.880  81.868  1.00 26.73 ? 1160 PRO B CA    1 
ATOM   17186 C C     . PRO B  1 1162 ? 23.182  58.450  81.405  1.00 24.89 ? 1160 PRO B C     1 
ATOM   17187 O O     . PRO B  1 1162 ? 22.371  58.936  82.186  1.00 27.02 ? 1160 PRO B O     1 
ATOM   17188 C CB    . PRO B  1 1162 ? 24.358  56.461  82.431  1.00 29.94 ? 1160 PRO B CB    1 
ATOM   17189 C CG    . PRO B  1 1162 ? 24.038  56.686  83.884  1.00 31.43 ? 1160 PRO B CG    1 
ATOM   17190 C CD    . PRO B  1 1162 ? 24.826  57.917  84.285  1.00 30.79 ? 1160 PRO B CD    1 
ATOM   17191 N N     . PHE B  1 1163 ? 22.956  58.412  80.103  1.00 23.62 ? 1161 PHE B N     1 
ATOM   17192 C CA    . PHE B  1 1163 ? 21.668  58.790  79.560  1.00 22.50 ? 1161 PHE B CA    1 
ATOM   17193 C C     . PHE B  1 1163 ? 20.805  57.546  79.392  1.00 25.81 ? 1161 PHE B C     1 
ATOM   17194 O O     . PHE B  1 1163 ? 21.255  56.413  79.565  1.00 24.79 ? 1161 PHE B O     1 
ATOM   17195 C CB    . PHE B  1 1163 ? 21.870  59.545  78.247  1.00 22.03 ? 1161 PHE B CB    1 
ATOM   17196 C CG    . PHE B  1 1163 ? 22.842  60.689  78.380  1.00 26.48 ? 1161 PHE B CG    1 
ATOM   17197 C CD1   . PHE B  1 1163 ? 22.510  61.802  79.127  1.00 26.04 ? 1161 PHE B CD1   1 
ATOM   17198 C CD2   . PHE B  1 1163 ? 24.105  60.631  77.803  1.00 22.62 ? 1161 PHE B CD2   1 
ATOM   17199 C CE1   . PHE B  1 1163 ? 23.399  62.850  79.273  1.00 24.95 ? 1161 PHE B CE1   1 
ATOM   17200 C CE2   . PHE B  1 1163 ? 24.990  61.687  77.956  1.00 25.03 ? 1161 PHE B CE2   1 
ATOM   17201 C CZ    . PHE B  1 1163 ? 24.634  62.788  78.688  1.00 24.31 ? 1161 PHE B CZ    1 
ATOM   17202 N N     . ALA B  1 1164 ? 19.534  57.770  79.088  1.00 24.48 ? 1162 ALA B N     1 
ATOM   17203 C CA    . ALA B  1 1164 ? 18.569  56.688  78.957  1.00 25.39 ? 1162 ALA B CA    1 
ATOM   17204 C C     . ALA B  1 1164 ? 18.049  56.574  77.533  1.00 27.33 ? 1162 ALA B C     1 
ATOM   17205 O O     . ALA B  1 1164 ? 17.085  55.836  77.289  1.00 31.03 ? 1162 ALA B O     1 
ATOM   17206 C CB    . ALA B  1 1164 ? 17.410  56.892  79.945  1.00 22.91 ? 1162 ALA B CB    1 
ATOM   17207 N N     . GLY B  1 1165 ? 18.655  57.292  76.598  1.00 22.98 ? 1163 GLY B N     1 
ATOM   17208 C CA    . GLY B  1 1165 ? 18.197  57.337  75.222  1.00 21.15 ? 1163 GLY B CA    1 
ATOM   17209 C C     . GLY B  1 1165 ? 18.765  58.564  74.548  1.00 23.30 ? 1163 GLY B C     1 
ATOM   17210 O O     . GLY B  1 1165 ? 19.343  59.445  75.188  1.00 22.23 ? 1163 GLY B O     1 
ATOM   17211 N N     . ALA B  1 1166 ? 18.603  58.614  73.230  1.00 21.69 ? 1164 ALA B N     1 
ATOM   17212 C CA    . ALA B  1 1166 ? 19.130  59.740  72.476  1.00 18.44 ? 1164 ALA B CA    1 
ATOM   17213 C C     . ALA B  1 1166 ? 18.218  60.033  71.301  1.00 22.13 ? 1164 ALA B C     1 
ATOM   17214 O O     . ALA B  1 1166 ? 17.707  59.113  70.665  1.00 22.65 ? 1164 ALA B O     1 
ATOM   17215 C CB    . ALA B  1 1166 ? 20.552  59.485  71.959  1.00 20.28 ? 1164 ALA B CB    1 
ATOM   17216 N N     . LEU B  1 1167 ? 18.025  61.323  71.036  1.00 20.45 ? 1165 LEU B N     1 
ATOM   17217 C CA    . LEU B  1 1167 ? 17.294  61.823  69.880  1.00 19.51 ? 1165 LEU B CA    1 
ATOM   17218 C C     . LEU B  1 1167 ? 18.262  62.667  69.058  1.00 24.08 ? 1165 LEU B C     1 
ATOM   17219 O O     . LEU B  1 1167 ? 18.921  63.559  69.600  1.00 20.32 ? 1165 LEU B O     1 
ATOM   17220 C CB    . LEU B  1 1167 ? 16.092  62.669  70.321  1.00 22.48 ? 1165 LEU B CB    1 
ATOM   17221 C CG    . LEU B  1 1167 ? 15.043  61.984  71.217  1.00 18.03 ? 1165 LEU B CG    1 
ATOM   17222 C CD1   . LEU B  1 1167 ? 13.932  62.969  71.557  1.00 23.96 ? 1165 LEU B CD1   1 
ATOM   17223 C CD2   . LEU B  1 1167 ? 14.485  60.778  70.472  1.00 22.51 ? 1165 LEU B CD2   1 
ATOM   17224 N N     . VAL B  1 1168 ? 18.363  62.389  67.761  1.00 23.74 ? 1166 VAL B N     1 
ATOM   17225 C CA    . VAL B  1 1168 ? 19.389  63.013  66.931  1.00 22.21 ? 1166 VAL B CA    1 
ATOM   17226 C C     . VAL B  1 1168 ? 18.718  63.616  65.711  1.00 23.50 ? 1166 VAL B C     1 
ATOM   17227 O O     . VAL B  1 1168 ? 17.835  62.997  65.106  1.00 24.31 ? 1166 VAL B O     1 
ATOM   17228 C CB    . VAL B  1 1168 ? 20.479  62.006  66.508  1.00 23.71 ? 1166 VAL B CB    1 
ATOM   17229 C CG1   . VAL B  1 1168 ? 21.580  62.700  65.682  1.00 23.76 ? 1166 VAL B CG1   1 
ATOM   17230 C CG2   . VAL B  1 1168 ? 21.067  61.292  67.741  1.00 23.00 ? 1166 VAL B CG2   1 
ATOM   17231 N N     . GLU B  1 1169 ? 19.120  64.832  65.368  1.00 23.96 ? 1167 GLU B N     1 
ATOM   17232 C CA    . GLU B  1 1169 ? 18.657  65.514  64.166  1.00 26.38 ? 1167 GLU B CA    1 
ATOM   17233 C C     . GLU B  1 1169 ? 19.849  65.801  63.251  1.00 26.07 ? 1167 GLU B C     1 
ATOM   17234 O O     . GLU B  1 1169 ? 20.881  66.302  63.707  1.00 27.49 ? 1167 GLU B O     1 
ATOM   17235 C CB    . GLU B  1 1169 ? 17.939  66.815  64.525  1.00 23.63 ? 1167 GLU B CB    1 
ATOM   17236 C CG    . GLU B  1 1169 ? 17.445  67.582  63.301  1.00 26.74 ? 1167 GLU B CG    1 
ATOM   17237 C CD    . GLU B  1 1169 ? 17.119  69.034  63.611  1.00 27.36 ? 1167 GLU B CD    1 
ATOM   17238 O OE1   . GLU B  1 1169 ? 17.440  69.492  64.723  1.00 29.34 ? 1167 GLU B OE1   1 
ATOM   17239 O OE2   . GLU B  1 1169 ? 16.543  69.721  62.742  1.00 29.08 ? 1167 GLU B OE2   1 
ATOM   17240 N N     . GLY B  1 1170 ? 19.714  65.478  61.972  1.00 25.67 ? 1168 GLY B N     1 
ATOM   17241 C CA    . GLY B  1 1170 ? 20.767  65.781  61.021  1.00 29.38 ? 1168 GLY B CA    1 
ATOM   17242 C C     . GLY B  1 1170 ? 20.620  64.963  59.755  1.00 30.01 ? 1168 GLY B C     1 
ATOM   17243 O O     . GLY B  1 1170 ? 19.701  64.150  59.612  1.00 28.64 ? 1168 GLY B O     1 
ATOM   17244 N N     . ASP B  1 1171 ? 21.563  65.193  58.832  1.00 28.87 ? 1169 ASP B N     1 
ATOM   17245 C CA    . ASP B  1 1171 ? 21.626  64.403  57.610  1.00 29.95 ? 1169 ASP B CA    1 
ATOM   17246 C C     . ASP B  1 1171 ? 22.331  63.071  57.879  1.00 34.30 ? 1169 ASP B C     1 
ATOM   17247 O O     . ASP B  1 1171 ? 22.766  62.780  59.000  1.00 29.80 ? 1169 ASP B O     1 
ATOM   17248 C CB    . ASP B  1 1171 ? 22.303  65.191  56.480  1.00 32.49 ? 1169 ASP B CB    1 
ATOM   17249 C CG    . ASP B  1 1171 ? 23.745  65.611  56.789  1.00 35.31 ? 1169 ASP B CG    1 
ATOM   17250 O OD1   . ASP B  1 1171 ? 24.417  65.040  57.668  1.00 33.50 ? 1169 ASP B OD1   1 
ATOM   17251 O OD2   . ASP B  1 1171 ? 24.226  66.548  56.120  1.00 43.81 ? 1169 ASP B OD2   1 
ATOM   17252 N N     . ALA B  1 1172 ? 22.450  62.253  56.829  1.00 33.13 ? 1170 ALA B N     1 
ATOM   17253 C CA    . ALA B  1 1172 ? 23.038  60.923  56.980  1.00 33.87 ? 1170 ALA B CA    1 
ATOM   17254 C C     . ALA B  1 1172 ? 24.434  60.984  57.599  1.00 32.19 ? 1170 ALA B C     1 
ATOM   17255 O O     . ALA B  1 1172 ? 24.749  60.217  58.517  1.00 32.55 ? 1170 ALA B O     1 
ATOM   17256 C CB    . ALA B  1 1172 ? 23.079  60.214  55.626  1.00 31.16 ? 1170 ALA B CB    1 
ATOM   17257 N N     . GLU B  1 1173 ? 25.292  61.890  57.110  1.00 31.89 ? 1171 GLU B N     1 
ATOM   17258 C CA    . GLU B  1 1173 ? 26.642  61.969  57.654  1.00 30.57 ? 1171 GLU B CA    1 
ATOM   17259 C C     . GLU B  1 1173 ? 26.618  62.383  59.121  1.00 28.66 ? 1171 GLU B C     1 
ATOM   17260 O O     . GLU B  1 1173 ? 27.372  61.846  59.941  1.00 29.77 ? 1171 GLU B O     1 
ATOM   17261 C CB    . GLU B  1 1173 ? 27.494  62.943  56.838  1.00 37.55 ? 1171 GLU B CB    1 
ATOM   17262 N N     . ARG B  1 1174 ? 25.768  63.347  59.470  1.00 30.99 ? 1172 ARG B N     1 
ATOM   17263 C CA    . ARG B  1 1174 ? 25.691  63.780  60.862  1.00 30.80 ? 1172 ARG B CA    1 
ATOM   17264 C C     . ARG B  1 1174 ? 25.196  62.651  61.760  1.00 25.35 ? 1172 ARG B C     1 
ATOM   17265 O O     . ARG B  1 1174 ? 25.711  62.457  62.870  1.00 25.39 ? 1172 ARG B O     1 
ATOM   17266 C CB    . ARG B  1 1174 ? 24.786  65.008  60.970  1.00 29.27 ? 1172 ARG B CB    1 
ATOM   17267 C CG    . ARG B  1 1174 ? 24.555  65.485  62.385  1.00 27.15 ? 1172 ARG B CG    1 
ATOM   17268 C CD    . ARG B  1 1174 ? 25.852  65.955  63.034  1.00 29.10 ? 1172 ARG B CD    1 
ATOM   17269 N NE    . ARG B  1 1174 ? 25.611  66.439  64.388  1.00 30.20 ? 1172 ARG B NE    1 
ATOM   17270 C CZ    . ARG B  1 1174 ? 26.545  66.562  65.322  1.00 31.66 ? 1172 ARG B CZ    1 
ATOM   17271 N NH1   . ARG B  1 1174 ? 27.807  66.238  65.085  1.00 28.34 ? 1172 ARG B NH1   1 
ATOM   17272 N NH2   . ARG B  1 1174 ? 26.200  67.004  66.527  1.00 29.96 ? 1172 ARG B NH2   1 
ATOM   17273 N N     . ILE B  1 1175 ? 24.229  61.874  61.279  1.00 26.73 ? 1173 ILE B N     1 
ATOM   17274 C CA    . ILE B  1 1175 ? 23.643  60.808  62.087  1.00 26.70 ? 1173 ILE B CA    1 
ATOM   17275 C C     . ILE B  1 1175 ? 24.671  59.720  62.351  1.00 26.99 ? 1173 ILE B C     1 
ATOM   17276 O O     . ILE B  1 1175 ? 24.805  59.233  63.479  1.00 22.79 ? 1173 ILE B O     1 
ATOM   17277 C CB    . ILE B  1 1175 ? 22.391  60.251  61.388  1.00 27.82 ? 1173 ILE B CB    1 
ATOM   17278 C CG1   . ILE B  1 1175 ? 21.263  61.281  61.421  1.00 26.16 ? 1173 ILE B CG1   1 
ATOM   17279 C CG2   . ILE B  1 1175 ? 21.926  58.958  62.030  1.00 25.99 ? 1173 ILE B CG2   1 
ATOM   17280 C CD1   . ILE B  1 1175 ? 20.108  60.912  60.515  1.00 27.62 ? 1173 ILE B CD1   1 
ATOM   17281 N N     . ARG B  1 1176 ? 25.419  59.328  61.315  1.00 27.15 ? 1174 ARG B N     1 
ATOM   17282 C CA    . ARG B  1 1176 ? 26.431  58.292  61.476  1.00 27.68 ? 1174 ARG B CA    1 
ATOM   17283 C C     . ARG B  1 1176 ? 27.503  58.734  62.466  1.00 26.94 ? 1174 ARG B C     1 
ATOM   17284 O O     . ARG B  1 1176 ? 27.932  57.952  63.323  1.00 26.75 ? 1174 ARG B O     1 
ATOM   17285 C CB    . ARG B  1 1176 ? 27.043  57.965  60.108  1.00 30.70 ? 1174 ARG B CB    1 
ATOM   17286 C CG    . ARG B  1 1176 ? 28.163  56.946  60.125  1.00 32.49 ? 1174 ARG B CG    1 
ATOM   17287 C CD    . ARG B  1 1176 ? 28.835  56.799  58.744  1.00 40.64 ? 1174 ARG B CD    1 
ATOM   17288 N NE    . ARG B  1 1176 ? 27.967  56.143  57.771  1.00 46.20 ? 1174 ARG B NE    1 
ATOM   17289 C CZ    . ARG B  1 1176 ? 27.519  56.699  56.652  1.00 51.90 ? 1174 ARG B CZ    1 
ATOM   17290 N NH1   . ARG B  1 1176 ? 27.887  57.918  56.289  1.00 55.81 ? 1174 ARG B NH1   1 
ATOM   17291 N NH2   . ARG B  1 1176 ? 26.684  56.012  55.873  1.00 44.05 ? 1174 ARG B NH2   1 
ATOM   17292 N N     . ALA B  1 1177 ? 27.917  60.000  62.379  1.00 25.32 ? 1175 ALA B N     1 
ATOM   17293 C CA    . ALA B  1 1177 ? 28.951  60.523  63.263  1.00 26.51 ? 1175 ALA B CA    1 
ATOM   17294 C C     . ALA B  1 1177 ? 28.470  60.569  64.710  1.00 23.98 ? 1175 ALA B C     1 
ATOM   17295 O O     . ALA B  1 1177 ? 29.209  60.198  65.630  1.00 25.56 ? 1175 ALA B O     1 
ATOM   17296 C CB    . ALA B  1 1177 ? 29.381  61.915  62.788  1.00 26.17 ? 1175 ALA B CB    1 
ATOM   17297 N N     . VAL B  1 1178 ? 27.233  61.011  64.932  1.00 28.18 ? 1176 VAL B N     1 
ATOM   17298 C CA    . VAL B  1 1178 ? 26.686  61.025  66.287  1.00 26.40 ? 1176 VAL B CA    1 
ATOM   17299 C C     . VAL B  1 1178 ? 26.484  59.601  66.796  1.00 26.70 ? 1176 VAL B C     1 
ATOM   17300 O O     . VAL B  1 1178 ? 26.800  59.281  67.951  1.00 24.77 ? 1176 VAL B O     1 
ATOM   17301 C CB    . VAL B  1 1178 ? 25.377  61.839  66.313  1.00 23.31 ? 1176 VAL B CB    1 
ATOM   17302 C CG1   . VAL B  1 1178 ? 24.671  61.699  67.658  1.00 22.70 ? 1176 VAL B CG1   1 
ATOM   17303 C CG2   . VAL B  1 1178 ? 25.647  63.308  65.990  1.00 26.56 ? 1176 VAL B CG2   1 
ATOM   17304 N N     . ASN B  1 1179 ? 25.957  58.722  65.942  1.00 24.88 ? 1177 ASN B N     1 
ATOM   17305 C CA    . ASN B  1 1179 ? 25.762  57.328  66.325  1.00 25.65 ? 1177 ASN B CA    1 
ATOM   17306 C C     . ASN B  1 1179 ? 27.073  56.684  66.766  1.00 24.79 ? 1177 ASN B C     1 
ATOM   17307 O O     . ASN B  1 1179 ? 27.110  55.943  67.759  1.00 25.98 ? 1177 ASN B O     1 
ATOM   17308 C CB    . ASN B  1 1179 ? 25.153  56.561  65.152  1.00 26.74 ? 1177 ASN B CB    1 
ATOM   17309 C CG    . ASN B  1 1179 ? 24.412  55.318  65.588  1.00 28.43 ? 1177 ASN B CG    1 
ATOM   17310 O OD1   . ASN B  1 1179 ? 23.858  55.263  66.684  1.00 27.53 ? 1177 ASN B OD1   1 
ATOM   17311 N ND2   . ASN B  1 1179 ? 24.374  54.315  64.712  1.00 28.83 ? 1177 ASN B ND2   1 
ATOM   17312 N N     . LYS B  1 1180 ? 28.161  56.951  66.037  1.00 29.41 ? 1178 LYS B N     1 
ATOM   17313 C CA    . LYS B  1 1180 ? 29.464  56.410  66.414  1.00 24.62 ? 1178 LYS B CA    1 
ATOM   17314 C C     . LYS B  1 1180 ? 29.929  56.970  67.757  1.00 23.98 ? 1178 LYS B C     1 
ATOM   17315 O O     . LYS B  1 1180 ? 30.422  56.225  68.609  1.00 24.10 ? 1178 LYS B O     1 
ATOM   17316 C CB    . LYS B  1 1180 ? 30.494  56.696  65.312  1.00 25.32 ? 1178 LYS B CB    1 
ATOM   17317 N N     . ALA B  1 1181 ? 29.747  58.274  67.979  1.00 26.53 ? 1179 ALA B N     1 
ATOM   17318 C CA    . ALA B  1 1181 ? 30.094  58.861  69.273  1.00 24.51 ? 1179 ALA B CA    1 
ATOM   17319 C C     . ALA B  1 1181 ? 29.277  58.245  70.410  1.00 25.57 ? 1179 ALA B C     1 
ATOM   17320 O O     . ALA B  1 1181 ? 29.806  57.992  71.502  1.00 24.03 ? 1179 ALA B O     1 
ATOM   17321 C CB    . ALA B  1 1181 ? 29.886  60.377  69.229  1.00 27.64 ? 1179 ALA B CB    1 
ATOM   17322 N N     . ILE B  1 1182 ? 27.976  58.014  70.182  1.00 22.40 ? 1180 ILE B N     1 
ATOM   17323 C CA    . ILE B  1 1182 ? 27.131  57.432  71.222  1.00 21.97 ? 1180 ILE B CA    1 
ATOM   17324 C C     . ILE B  1 1182 ? 27.561  56.004  71.520  1.00 21.89 ? 1180 ILE B C     1 
ATOM   17325 O O     . ILE B  1 1182 ? 27.520  55.554  72.672  1.00 25.47 ? 1180 ILE B O     1 
ATOM   17326 C CB    . ILE B  1 1182 ? 25.646  57.509  70.807  1.00 23.48 ? 1180 ILE B CB    1 
ATOM   17327 C CG1   . ILE B  1 1182 ? 25.136  58.948  70.931  1.00 23.18 ? 1180 ILE B CG1   1 
ATOM   17328 C CG2   . ILE B  1 1182 ? 24.793  56.527  71.622  1.00 25.00 ? 1180 ILE B CG2   1 
ATOM   17329 C CD1   . ILE B  1 1182 ? 23.754  59.164  70.339  1.00 25.65 ? 1180 ILE B CD1   1 
ATOM   17330 N N     . ALA B  1 1183 ? 28.008  55.274  70.500  1.00 23.87 ? 1181 ALA B N     1 
ATOM   17331 C CA    . ALA B  1 1183 ? 28.467  53.907  70.720  1.00 28.40 ? 1181 ALA B CA    1 
ATOM   17332 C C     . ALA B  1 1183 ? 29.733  53.841  71.561  1.00 31.46 ? 1181 ALA B C     1 
ATOM   17333 O O     . ALA B  1 1183 ? 30.028  52.782  72.123  1.00 33.18 ? 1181 ALA B O     1 
ATOM   17334 C CB    . ALA B  1 1183 ? 28.707  53.199  69.387  1.00 30.67 ? 1181 ALA B CB    1 
ATOM   17335 N N     . ALA B  1 1184 ? 30.491  54.934  71.654  1.00 28.20 ? 1182 ALA B N     1 
ATOM   17336 C CA    . ALA B  1 1184 ? 31.692  54.969  72.479  1.00 25.96 ? 1182 ALA B CA    1 
ATOM   17337 C C     . ALA B  1 1184 ? 31.417  55.402  73.910  1.00 27.20 ? 1182 ALA B C     1 
ATOM   17338 O O     . ALA B  1 1184 ? 32.358  55.450  74.713  1.00 26.77 ? 1182 ALA B O     1 
ATOM   17339 C CB    . ALA B  1 1184 ? 32.740  55.907  71.867  1.00 28.76 ? 1182 ALA B CB    1 
ATOM   17340 N N     . LEU B  1 1185 ? 30.182  55.747  74.240  1.00 24.68 ? 1183 LEU B N     1 
ATOM   17341 C CA    . LEU B  1 1185 ? 29.885  56.205  75.592  1.00 27.58 ? 1183 LEU B CA    1 
ATOM   17342 C C     . LEU B  1 1185 ? 29.940  55.023  76.556  1.00 30.77 ? 1183 LEU B C     1 
ATOM   17343 O O     . LEU B  1 1185 ? 29.495  53.923  76.217  1.00 27.32 ? 1183 LEU B O     1 
ATOM   17344 C CB    . LEU B  1 1185 ? 28.501  56.864  75.681  1.00 27.67 ? 1183 LEU B CB    1 
ATOM   17345 C CG    . LEU B  1 1185 ? 28.200  58.128  74.867  1.00 25.11 ? 1183 LEU B CG    1 
ATOM   17346 C CD1   . LEU B  1 1185 ? 26.742  58.565  75.061  1.00 22.95 ? 1183 LEU B CD1   1 
ATOM   17347 C CD2   . LEU B  1 1185 ? 29.166  59.250  75.237  1.00 25.01 ? 1183 LEU B CD2   1 
ATOM   17348 N N     . PRO B  1 1186 ? 30.467  55.222  77.761  1.00 28.54 ? 1184 PRO B N     1 
ATOM   17349 C CA    . PRO B  1 1186 ? 30.496  54.135  78.740  1.00 29.79 ? 1184 PRO B CA    1 
ATOM   17350 C C     . PRO B  1 1186 ? 29.109  53.876  79.305  1.00 27.47 ? 1184 PRO B C     1 
ATOM   17351 O O     . PRO B  1 1186 ? 28.217  54.722  79.249  1.00 33.38 ? 1184 PRO B O     1 
ATOM   17352 C CB    . PRO B  1 1186 ? 31.435  54.669  79.824  1.00 33.33 ? 1184 PRO B CB    1 
ATOM   17353 C CG    . PRO B  1 1186 ? 31.221  56.161  79.774  1.00 33.94 ? 1184 PRO B CG    1 
ATOM   17354 C CD    . PRO B  1 1186 ? 30.991  56.487  78.310  1.00 28.67 ? 1184 PRO B CD    1 
ATOM   17355 N N     . GLY B  1 1187 ? 28.947  52.699  79.895  1.00 28.88 ? 1185 GLY B N     1 
ATOM   17356 C CA    . GLY B  1 1187 ? 27.716  52.375  80.573  1.00 30.54 ? 1185 GLY B CA    1 
ATOM   17357 C C     . GLY B  1 1187 ? 26.663  51.814  79.634  1.00 28.11 ? 1185 GLY B C     1 
ATOM   17358 O O     . GLY B  1 1187 ? 26.957  50.986  78.765  1.00 34.09 ? 1185 GLY B O     1 
ATOM   17359 N N     . PRO B  1 1188 ? 25.419  52.268  79.781  1.00 29.31 ? 1186 PRO B N     1 
ATOM   17360 C CA    . PRO B  1 1188 ? 24.318  51.644  79.038  1.00 30.80 ? 1186 PRO B CA    1 
ATOM   17361 C C     . PRO B  1 1188 ? 24.423  51.876  77.539  1.00 31.92 ? 1186 PRO B C     1 
ATOM   17362 O O     . PRO B  1 1188 ? 24.903  52.909  77.069  1.00 32.13 ? 1186 PRO B O     1 
ATOM   17363 C CB    . PRO B  1 1188 ? 23.074  52.335  79.603  1.00 31.81 ? 1186 PRO B CB    1 
ATOM   17364 C CG    . PRO B  1 1188 ? 23.576  53.692  79.986  1.00 31.86 ? 1186 PRO B CG    1 
ATOM   17365 C CD    . PRO B  1 1188 ? 24.965  53.447  80.537  1.00 30.59 ? 1186 PRO B CD    1 
ATOM   17366 N N     . LEU B  1 1189 ? 23.956  50.882  76.793  1.00 29.76 ? 1187 LEU B N     1 
ATOM   17367 C CA    . LEU B  1 1189 ? 23.816  50.969  75.348  1.00 32.10 ? 1187 LEU B CA    1 
ATOM   17368 C C     . LEU B  1 1189 ? 22.576  51.805  75.037  1.00 33.51 ? 1187 LEU B C     1 
ATOM   17369 O O     . LEU B  1 1189 ? 21.447  51.381  75.323  1.00 30.34 ? 1187 LEU B O     1 
ATOM   17370 C CB    . LEU B  1 1189 ? 23.703  49.557  74.780  1.00 30.33 ? 1187 LEU B CB    1 
ATOM   17371 C CG    . LEU B  1 1189 ? 24.470  49.167  73.534  1.00 37.06 ? 1187 LEU B CG    1 
ATOM   17372 C CD1   . LEU B  1 1189 ? 24.746  47.678  73.596  1.00 35.08 ? 1187 LEU B CD1   1 
ATOM   17373 C CD2   . LEU B  1 1189 ? 23.614  49.513  72.319  1.00 33.30 ? 1187 LEU B CD2   1 
ATOM   17374 N N     . LEU B  1 1190 ? 22.773  52.996  74.466  1.00 28.32 ? 1188 LEU B N     1 
ATOM   17375 C CA    . LEU B  1 1190 ? 21.663  53.916  74.246  1.00 25.92 ? 1188 LEU B CA    1 
ATOM   17376 C C     . LEU B  1 1190 ? 20.848  53.530  73.021  1.00 31.65 ? 1188 LEU B C     1 
ATOM   17377 O O     . LEU B  1 1190 ? 21.395  53.184  71.968  1.00 25.64 ? 1188 LEU B O     1 
ATOM   17378 C CB    . LEU B  1 1190 ? 22.159  55.353  74.072  1.00 26.89 ? 1188 LEU B CB    1 
ATOM   17379 C CG    . LEU B  1 1190 ? 22.859  55.985  75.276  1.00 24.56 ? 1188 LEU B CG    1 
ATOM   17380 C CD1   . LEU B  1 1190 ? 23.023  57.481  75.061  1.00 26.89 ? 1188 LEU B CD1   1 
ATOM   17381 C CD2   . LEU B  1 1190 ? 22.083  55.698  76.545  1.00 27.74 ? 1188 LEU B CD2   1 
ATOM   17382 N N     . LEU B  1 1191 ? 19.530  53.619  73.168  1.00 25.30 ? 1189 LEU B N     1 
ATOM   17383 C CA    . LEU B  1 1191 ? 18.598  53.464  72.057  1.00 24.58 ? 1189 LEU B CA    1 
ATOM   17384 C C     . LEU B  1 1191 ? 18.519  54.800  71.321  1.00 24.88 ? 1189 LEU B C     1 
ATOM   17385 O O     . LEU B  1 1191 ? 18.024  55.793  71.864  1.00 27.97 ? 1189 LEU B O     1 
ATOM   17386 C CB    . LEU B  1 1191 ? 17.245  53.009  72.595  1.00 24.97 ? 1189 LEU B CB    1 
ATOM   17387 C CG    . LEU B  1 1191 ? 16.170  52.375  71.697  1.00 30.51 ? 1189 LEU B CG    1 
ATOM   17388 C CD1   . LEU B  1 1191 ? 15.051  51.792  72.563  1.00 28.53 ? 1189 LEU B CD1   1 
ATOM   17389 C CD2   . LEU B  1 1191 ? 15.602  53.382  70.721  1.00 25.57 ? 1189 LEU B CD2   1 
ATOM   17390 N N     . VAL B  1 1192 ? 19.009  54.830  70.086  1.00 25.55 ? 1190 VAL B N     1 
ATOM   17391 C CA    . VAL B  1 1192 ? 19.199  56.065  69.332  1.00 26.21 ? 1190 VAL B CA    1 
ATOM   17392 C C     . VAL B  1 1192 ? 18.068  56.208  68.325  1.00 28.06 ? 1190 VAL B C     1 
ATOM   17393 O O     . VAL B  1 1192 ? 17.762  55.264  67.588  1.00 27.43 ? 1190 VAL B O     1 
ATOM   17394 C CB    . VAL B  1 1192 ? 20.564  56.077  68.624  1.00 26.46 ? 1190 VAL B CB    1 
ATOM   17395 C CG1   . VAL B  1 1192 ? 20.773  57.395  67.889  1.00 24.36 ? 1190 VAL B CG1   1 
ATOM   17396 C CG2   . VAL B  1 1192 ? 21.702  55.830  69.644  1.00 25.91 ? 1190 VAL B CG2   1 
ATOM   17397 N N     . GLN B  1 1193 ? 17.449  57.384  68.287  1.00 24.27 ? 1191 GLN B N     1 
ATOM   17398 C CA    . GLN B  1 1193 ? 16.441  57.697  67.281  1.00 22.51 ? 1191 GLN B CA    1 
ATOM   17399 C C     . GLN B  1 1193 ? 16.916  58.900  66.490  1.00 23.95 ? 1191 GLN B C     1 
ATOM   17400 O O     . GLN B  1 1193 ? 17.348  59.897  67.074  1.00 23.61 ? 1191 GLN B O     1 
ATOM   17401 C CB    . GLN B  1 1193 ? 15.080  58.011  67.897  1.00 23.81 ? 1191 GLN B CB    1 
ATOM   17402 C CG    . GLN B  1 1193 ? 14.426  56.874  68.616  1.00 24.65 ? 1191 GLN B CG    1 
ATOM   17403 C CD    . GLN B  1 1193 ? 12.981  57.192  68.911  1.00 26.35 ? 1191 GLN B CD    1 
ATOM   17404 O OE1   . GLN B  1 1193 ? 12.149  57.245  67.999  1.00 26.97 ? 1191 GLN B OE1   1 
ATOM   17405 N NE2   . GLN B  1 1193 ? 12.672  57.434  70.179  1.00 22.50 ? 1191 GLN B NE2   1 
ATOM   17406 N N     . ALA B  1 1194 ? 16.826  58.816  65.170  1.00 22.87 ? 1192 ALA B N     1 
ATOM   17407 C CA    . ALA B  1 1194 ? 17.382  59.853  64.322  1.00 24.07 ? 1192 ALA B CA    1 
ATOM   17408 C C     . ALA B  1 1194 ? 16.357  60.258  63.285  1.00 24.24 ? 1192 ALA B C     1 
ATOM   17409 O O     . ALA B  1 1194 ? 15.564  59.434  62.819  1.00 24.80 ? 1192 ALA B O     1 
ATOM   17410 C CB    . ALA B  1 1194 ? 18.660  59.399  63.620  1.00 25.33 ? 1192 ALA B CB    1 
ATOM   17411 N N     . ALA B  1 1195 ? 16.386  61.541  62.938  1.00 20.68 ? 1193 ALA B N     1 
ATOM   17412 C CA    . ALA B  1 1195 ? 15.524  62.054  61.887  1.00 22.46 ? 1193 ALA B CA    1 
ATOM   17413 C C     . ALA B  1 1195 ? 16.210  63.243  61.233  1.00 26.59 ? 1193 ALA B C     1 
ATOM   17414 O O     . ALA B  1 1195 ? 17.032  63.919  61.851  1.00 21.83 ? 1193 ALA B O     1 
ATOM   17415 C CB    . ALA B  1 1195 ? 14.157  62.462  62.441  1.00 25.30 ? 1193 ALA B CB    1 
ATOM   17416 N N     . SER B  1 1196 ? 15.868  63.493  59.976  1.00 25.25 ? 1194 SER B N     1 
ATOM   17417 C CA    . SER B  1 1196 ? 16.365  64.696  59.335  1.00 27.30 ? 1194 SER B CA    1 
ATOM   17418 C C     . SER B  1 1196 ? 15.505  65.886  59.738  1.00 27.81 ? 1194 SER B C     1 
ATOM   17419 O O     . SER B  1 1196 ? 14.376  65.731  60.219  1.00 28.56 ? 1194 SER B O     1 
ATOM   17420 C CB    . SER B  1 1196 ? 16.356  64.538  57.820  1.00 25.50 ? 1194 SER B CB    1 
ATOM   17421 O OG    . SER B  1 1196 ? 15.031  64.461  57.369  1.00 28.04 ? 1194 SER B OG    1 
ATOM   17422 N N     . SER B  1 1197 ? 16.048  67.092  59.531  1.00 25.73 ? 1195 SER B N     1 
ATOM   17423 C CA    . SER B  1 1197 ? 15.244  68.288  59.749  1.00 30.68 ? 1195 SER B CA    1 
ATOM   17424 C C     . SER B  1 1197 ? 13.958  68.217  58.938  1.00 31.94 ? 1195 SER B C     1 
ATOM   17425 O O     . SER B  1 1197 ? 12.884  68.597  59.419  1.00 32.73 ? 1195 SER B O     1 
ATOM   17426 C CB    . SER B  1 1197 ? 16.047  69.538  59.384  1.00 32.79 ? 1195 SER B CB    1 
ATOM   17427 O OG    . SER B  1 1197 ? 17.220  69.652  60.176  1.00 33.71 ? 1195 SER B OG    1 
ATOM   17428 N N     . GLY B  1 1198 ? 14.047  67.688  57.718  1.00 33.47 ? 1196 GLY B N     1 
ATOM   17429 C CA    . GLY B  1 1198 ? 12.864  67.568  56.882  1.00 33.71 ? 1196 GLY B CA    1 
ATOM   17430 C C     . GLY B  1 1198 ? 11.867  66.559  57.418  1.00 34.19 ? 1196 GLY B C     1 
ATOM   17431 O O     . GLY B  1 1198 ? 10.655  66.766  57.326  1.00 33.47 ? 1196 GLY B O     1 
ATOM   17432 N N     . GLU B  1 1199 ? 12.362  65.453  57.987  1.00 32.58 ? 1197 GLU B N     1 
ATOM   17433 C CA    . GLU B  1 1199 ? 11.460  64.459  58.558  1.00 29.32 ? 1197 GLU B CA    1 
ATOM   17434 C C     . GLU B  1 1199 ? 10.731  65.021  59.767  1.00 35.35 ? 1197 GLU B C     1 
ATOM   17435 O O     . GLU B  1 1199 ? 9.544   64.746  59.973  1.00 32.24 ? 1197 GLU B O     1 
ATOM   17436 C CB    . GLU B  1 1199 ? 12.233  63.195  58.936  1.00 33.12 ? 1197 GLU B CB    1 
ATOM   17437 N N     . ILE B  1 1200 ? 11.424  65.822  60.577  1.00 28.67 ? 1198 ILE B N     1 
ATOM   17438 C CA    . ILE B  1 1200 ? 10.794  66.397  61.758  1.00 28.81 ? 1198 ILE B CA    1 
ATOM   17439 C C     . ILE B  1 1200 ? 9.644   67.318  61.359  1.00 32.48 ? 1198 ILE B C     1 
ATOM   17440 O O     . ILE B  1 1200 ? 8.606   67.365  62.032  1.00 27.13 ? 1198 ILE B O     1 
ATOM   17441 C CB    . ILE B  1 1200 ? 11.846  67.125  62.612  1.00 29.16 ? 1198 ILE B CB    1 
ATOM   17442 C CG1   . ILE B  1 1200 ? 12.855  66.114  63.162  1.00 28.19 ? 1198 ILE B CG1   1 
ATOM   17443 C CG2   . ILE B  1 1200 ? 11.178  67.918  63.729  1.00 29.45 ? 1198 ILE B CG2   1 
ATOM   17444 C CD1   . ILE B  1 1200 ? 13.981  66.735  63.972  1.00 25.95 ? 1198 ILE B CD1   1 
ATOM   17445 N N     . ALA B  1 1201 ? 9.804   68.047  60.253  1.00 34.46 ? 1199 ALA B N     1 
ATOM   17446 C CA    . ALA B  1 1201 ? 8.783   68.985  59.801  1.00 34.08 ? 1199 ALA B CA    1 
ATOM   17447 C C     . ALA B  1 1201 ? 7.604   68.292  59.128  1.00 37.38 ? 1199 ALA B C     1 
ATOM   17448 O O     . ALA B  1 1201 ? 6.468   68.765  59.241  1.00 39.15 ? 1199 ALA B O     1 
ATOM   17449 C CB    . ALA B  1 1201 ? 9.397   70.005  58.842  1.00 34.22 ? 1199 ALA B CB    1 
ATOM   17450 N N     . ARG B  1 1202 ? 7.847   67.185  58.428  1.00 35.01 ? 1200 ARG B N     1 
ATOM   17451 C CA    . ARG B  1 1202 ? 6.802   66.522  57.658  1.00 35.38 ? 1200 ARG B CA    1 
ATOM   17452 C C     . ARG B  1 1202 ? 6.070   65.442  58.442  1.00 38.49 ? 1200 ARG B C     1 
ATOM   17453 O O     . ARG B  1 1202 ? 4.868   65.241  58.232  1.00 41.83 ? 1200 ARG B O     1 
ATOM   17454 C CB    . ARG B  1 1202 ? 7.401   65.892  56.398  1.00 37.96 ? 1200 ARG B CB    1 
ATOM   17455 C CG    . ARG B  1 1202 ? 8.021   66.872  55.418  1.00 44.87 ? 1200 ARG B CG    1 
ATOM   17456 C CD    . ARG B  1 1202 ? 8.530   66.132  54.183  1.00 47.83 ? 1200 ARG B CD    1 
ATOM   17457 N NE    . ARG B  1 1202 ? 9.320   64.960  54.548  1.00 43.31 ? 1200 ARG B NE    1 
ATOM   17458 C CZ    . ARG B  1 1202 ? 10.643  64.899  54.473  1.00 45.63 ? 1200 ARG B CZ    1 
ATOM   17459 N NH1   . ARG B  1 1202 ? 11.356  65.912  54.005  1.00 44.21 ? 1200 ARG B NH1   1 
ATOM   17460 N NH2   . ARG B  1 1202 ? 11.266  63.792  54.870  1.00 47.96 ? 1200 ARG B NH2   1 
ATOM   17461 N N     . ASN B  1 1203 ? 6.764   64.740  59.333  1.00 32.88 ? 1201 ASN B N     1 
ATOM   17462 C CA    . ASN B  1 1203 ? 6.240   63.523  59.946  1.00 35.74 ? 1201 ASN B CA    1 
ATOM   17463 C C     . ASN B  1 1203 ? 6.034   63.737  61.435  1.00 34.70 ? 1201 ASN B C     1 
ATOM   17464 O O     . ASN B  1 1203 ? 7.022   63.843  62.183  1.00 35.74 ? 1201 ASN B O     1 
ATOM   17465 C CB    . ASN B  1 1203 ? 7.195   62.350  59.695  1.00 34.95 ? 1201 ASN B CB    1 
ATOM   17466 C CG    . ASN B  1 1203 ? 6.718   61.038  60.321  1.00 39.77 ? 1201 ASN B CG    1 
ATOM   17467 O OD1   . ASN B  1 1203 ? 5.629   60.949  60.902  1.00 38.61 ? 1201 ASN B OD1   1 
ATOM   17468 N ND2   . ASN B  1 1203 ? 7.543   60.005  60.193  1.00 40.39 ? 1201 ASN B ND2   1 
ATOM   17469 N N     . PRO B  1 1204 ? 4.788   63.776  61.913  1.00 37.69 ? 1202 PRO B N     1 
ATOM   17470 C CA    . PRO B  1 1204 ? 4.555   63.954  63.356  1.00 32.23 ? 1202 PRO B CA    1 
ATOM   17471 C C     . PRO B  1 1204 ? 5.154   62.848  64.211  1.00 36.43 ? 1202 PRO B C     1 
ATOM   17472 O O     . PRO B  1 1204 ? 5.397   63.062  65.407  1.00 35.67 ? 1202 PRO B O     1 
ATOM   17473 C CB    . PRO B  1 1204 ? 3.022   63.984  63.463  1.00 39.23 ? 1202 PRO B CB    1 
ATOM   17474 C CG    . PRO B  1 1204 ? 2.541   63.246  62.250  1.00 39.12 ? 1202 PRO B CG    1 
ATOM   17475 C CD    . PRO B  1 1204 ? 3.535   63.565  61.163  1.00 36.52 ? 1202 PRO B CD    1 
ATOM   17476 N N     . ASP B  1 1205 ? 5.413   61.678  63.640  1.00 37.06 ? 1203 ASP B N     1 
ATOM   17477 C CA    . ASP B  1 1205 ? 6.018   60.569  64.366  1.00 35.71 ? 1203 ASP B CA    1 
ATOM   17478 C C     . ASP B  1 1205 ? 7.474   60.356  63.957  1.00 35.44 ? 1203 ASP B C     1 
ATOM   17479 O O     . ASP B  1 1205 ? 7.959   59.226  63.895  1.00 35.68 ? 1203 ASP B O     1 
ATOM   17480 C CB    . ASP B  1 1205 ? 5.203   59.298  64.166  1.00 39.90 ? 1203 ASP B CB    1 
ATOM   17481 C CG    . ASP B  1 1205 ? 3.819   59.399  64.784  1.00 39.32 ? 1203 ASP B CG    1 
ATOM   17482 O OD1   . ASP B  1 1205 ? 3.702   59.879  65.937  1.00 43.09 ? 1203 ASP B OD1   1 
ATOM   17483 O OD2   . ASP B  1 1205 ? 2.849   59.009  64.106  1.00 48.95 ? 1203 ASP B OD2   1 
ATOM   17484 N N     . ALA B  1 1206 ? 8.182   61.449  63.662  1.00 30.61 ? 1204 ALA B N     1 
ATOM   17485 C CA    . ALA B  1 1206 ? 9.608   61.345  63.367  1.00 30.07 ? 1204 ALA B CA    1 
ATOM   17486 C C     . ALA B  1 1206 ? 10.352  60.666  64.513  1.00 27.70 ? 1204 ALA B C     1 
ATOM   17487 O O     . ALA B  1 1206 ? 11.242  59.839  64.280  1.00 26.18 ? 1204 ALA B O     1 
ATOM   17488 C CB    . ALA B  1 1206 ? 10.192  62.730  63.091  1.00 32.25 ? 1204 ALA B CB    1 
ATOM   17489 N N     . TYR B  1 1207 ? 9.979   60.984  65.754  1.00 26.45 ? 1205 TYR B N     1 
ATOM   17490 C CA    . TYR B  1 1207 ? 10.507  60.332  66.948  1.00 22.93 ? 1205 TYR B CA    1 
ATOM   17491 C C     . TYR B  1 1207 ? 9.385   59.544  67.617  1.00 28.98 ? 1205 TYR B C     1 
ATOM   17492 O O     . TYR B  1 1207 ? 8.293   60.077  67.833  1.00 32.98 ? 1205 TYR B O     1 
ATOM   17493 C CB    . TYR B  1 1207 ? 11.101  61.354  67.930  1.00 23.68 ? 1205 TYR B CB    1 
ATOM   17494 C CG    . TYR B  1 1207 ? 12.295  62.105  67.373  1.00 25.91 ? 1205 TYR B CG    1 
ATOM   17495 C CD1   . TYR B  1 1207 ? 13.455  61.430  67.009  1.00 22.08 ? 1205 TYR B CD1   1 
ATOM   17496 C CD2   . TYR B  1 1207 ? 12.257  63.487  67.206  1.00 26.24 ? 1205 TYR B CD2   1 
ATOM   17497 C CE1   . TYR B  1 1207 ? 14.541  62.099  66.497  1.00 23.33 ? 1205 TYR B CE1   1 
ATOM   17498 C CE2   . TYR B  1 1207 ? 13.341  64.171  66.687  1.00 27.89 ? 1205 TYR B CE2   1 
ATOM   17499 C CZ    . TYR B  1 1207 ? 14.479  63.477  66.338  1.00 22.62 ? 1205 TYR B CZ    1 
ATOM   17500 O OH    . TYR B  1 1207 ? 15.560  64.159  65.823  1.00 24.29 ? 1205 TYR B OH    1 
ATOM   17501 N N     . CYS B  1 1208 ? 9.654   58.281  67.934  1.00 24.34 ? 1206 CYS B N     1 
ATOM   17502 C CA    . CYS B  1 1208 ? 8.651   57.394  68.499  1.00 24.67 ? 1206 CYS B CA    1 
ATOM   17503 C C     . CYS B  1 1208 ? 8.691   57.455  70.023  1.00 27.10 ? 1206 CYS B C     1 
ATOM   17504 O O     . CYS B  1 1208 ? 9.750   57.265  70.635  1.00 22.47 ? 1206 CYS B O     1 
ATOM   17505 C CB    . CYS B  1 1208 ? 8.881   55.963  68.022  1.00 30.08 ? 1206 CYS B CB    1 
ATOM   17506 S SG    . CYS B  1 1208 ? 7.647   54.810  68.638  1.00 31.75 ? 1206 CYS B SG    1 
ATOM   17507 N N     . LEU B  1 1209 ? 7.536   57.709  70.634  1.00 24.31 ? 1207 LEU B N     1 
ATOM   17508 C CA    . LEU B  1 1209 ? 7.490   57.813  72.088  1.00 24.89 ? 1207 LEU B CA    1 
ATOM   17509 C C     . LEU B  1 1209 ? 7.515   56.459  72.775  1.00 23.54 ? 1207 LEU B C     1 
ATOM   17510 O O     . LEU B  1 1209 ? 7.707   56.415  73.998  1.00 23.70 ? 1207 LEU B O     1 
ATOM   17511 C CB    . LEU B  1 1209 ? 6.249   58.574  72.540  1.00 19.11 ? 1207 LEU B CB    1 
ATOM   17512 C CG    . LEU B  1 1209 ? 6.033   59.968  71.928  1.00 23.59 ? 1207 LEU B CG    1 
ATOM   17513 C CD1   . LEU B  1 1209 ? 4.843   60.635  72.594  1.00 23.31 ? 1207 LEU B CD1   1 
ATOM   17514 C CD2   . LEU B  1 1209 ? 7.284   60.831  72.062  1.00 20.20 ? 1207 LEU B CD2   1 
ATOM   17515 N N     . ASN B  1 1210 ? 7.317   55.365  72.032  1.00 20.93 ? 1208 ASN B N     1 
ATOM   17516 C CA    . ASN B  1 1210 ? 7.433   54.029  72.621  1.00 23.62 ? 1208 ASN B CA    1 
ATOM   17517 C C     . ASN B  1 1210 ? 8.772   53.835  73.323  1.00 24.30 ? 1208 ASN B C     1 
ATOM   17518 O O     . ASN B  1 1210 ? 8.851   53.144  74.350  1.00 21.66 ? 1208 ASN B O     1 
ATOM   17519 C CB    . ASN B  1 1210 ? 7.279   52.945  71.543  1.00 28.03 ? 1208 ASN B CB    1 
ATOM   17520 C CG    . ASN B  1 1210 ? 5.901   52.931  70.895  1.00 29.32 ? 1208 ASN B CG    1 
ATOM   17521 O OD1   . ASN B  1 1210 ? 5.120   53.869  71.038  1.00 33.02 ? 1208 ASN B OD1   1 
ATOM   17522 N ND2   . ASN B  1 1210 ? 5.610   51.858  70.155  1.00 34.51 ? 1208 ASN B ND2   1 
ATOM   17523 N N     . TRP B  1 1211 ? 9.845   54.411  72.770  1.00 19.36 ? 1209 TRP B N     1 
ATOM   17524 C CA    . TRP B  1 1211 ? 11.207  54.150  73.222  1.00 19.82 ? 1209 TRP B CA    1 
ATOM   17525 C C     . TRP B  1 1211 ? 11.692  55.152  74.251  1.00 22.90 ? 1209 TRP B C     1 
ATOM   17526 O O     . TRP B  1 1211 ? 12.832  55.032  74.715  1.00 25.25 ? 1209 TRP B O     1 
ATOM   17527 C CB    . TRP B  1 1211 ? 12.172  54.142  72.020  1.00 21.08 ? 1209 TRP B CB    1 
ATOM   17528 C CG    . TRP B  1 1211 ? 11.564  53.448  70.833  1.00 24.90 ? 1209 TRP B CG    1 
ATOM   17529 C CD1   . TRP B  1 1211 ? 11.453  53.933  69.563  1.00 27.43 ? 1209 TRP B CD1   1 
ATOM   17530 C CD2   . TRP B  1 1211 ? 10.939  52.157  70.827  1.00 26.01 ? 1209 TRP B CD2   1 
ATOM   17531 N NE1   . TRP B  1 1211 ? 10.809  53.015  68.757  1.00 27.36 ? 1209 TRP B NE1   1 
ATOM   17532 C CE2   . TRP B  1 1211 ? 10.486  51.917  69.513  1.00 30.95 ? 1209 TRP B CE2   1 
ATOM   17533 C CE3   . TRP B  1 1211 ? 10.731  51.176  71.802  1.00 27.89 ? 1209 TRP B CE3   1 
ATOM   17534 C CZ2   . TRP B  1 1211 ? 9.832   50.740  69.154  1.00 29.46 ? 1209 TRP B CZ2   1 
ATOM   17535 C CZ3   . TRP B  1 1211 ? 10.083  50.007  71.443  1.00 25.88 ? 1209 TRP B CZ3   1 
ATOM   17536 C CH2   . TRP B  1 1211 ? 9.636   49.803  70.134  1.00 28.02 ? 1209 TRP B CH2   1 
ATOM   17537 N N     . LEU B  1 1212 ? 10.863  56.128  74.622  1.00 21.07 ? 1210 LEU B N     1 
ATOM   17538 C CA    . LEU B  1 1212 ? 11.230  57.143  75.597  1.00 17.97 ? 1210 LEU B CA    1 
ATOM   17539 C C     . LEU B  1 1212 ? 10.591  56.902  76.958  1.00 20.49 ? 1210 LEU B C     1 
ATOM   17540 O O     . LEU B  1 1212 ? 10.672  57.766  77.831  1.00 21.97 ? 1210 LEU B O     1 
ATOM   17541 C CB    . LEU B  1 1212 ? 10.858  58.524  75.065  1.00 16.66 ? 1210 LEU B CB    1 
ATOM   17542 C CG    . LEU B  1 1212 ? 11.730  58.931  73.870  1.00 16.30 ? 1210 LEU B CG    1 
ATOM   17543 C CD1   . LEU B  1 1212 ? 11.154  60.157  73.196  1.00 20.31 ? 1210 LEU B CD1   1 
ATOM   17544 C CD2   . LEU B  1 1212 ? 13.185  59.192  74.305  1.00 20.94 ? 1210 LEU B CD2   1 
ATOM   17545 N N     . VAL B  1 1213 ? 9.976   55.738  77.164  1.00 19.38 ? 1211 VAL B N     1 
ATOM   17546 C CA    . VAL B  1 1213 ? 9.436   55.345  78.455  1.00 21.41 ? 1211 VAL B CA    1 
ATOM   17547 C C     . VAL B  1 1213 ? 10.130  54.055  78.869  1.00 23.07 ? 1211 VAL B C     1 
ATOM   17548 O O     . VAL B  1 1213 ? 10.729  53.355  78.051  1.00 23.18 ? 1211 VAL B O     1 
ATOM   17549 C CB    . VAL B  1 1213 ? 7.897   55.162  78.425  1.00 20.99 ? 1211 VAL B CB    1 
ATOM   17550 C CG1   . VAL B  1 1213 ? 7.200   56.509  78.266  1.00 17.06 ? 1211 VAL B CG1   1 
ATOM   17551 C CG2   . VAL B  1 1213 ? 7.483   54.222  77.290  1.00 19.03 ? 1211 VAL B CG2   1 
ATOM   17552 N N     . GLU B  1 1214 ? 10.057  53.747  80.162  1.00 22.72 ? 1212 GLU B N     1 
ATOM   17553 C CA    . GLU B  1 1214 ? 10.632  52.515  80.691  1.00 24.87 ? 1212 GLU B CA    1 
ATOM   17554 C C     . GLU B  1 1214 ? 9.529   51.588  81.174  1.00 20.53 ? 1212 GLU B C     1 
ATOM   17555 O O     . GLU B  1 1214 ? 8.660   51.993  81.953  1.00 20.50 ? 1212 GLU B O     1 
ATOM   17556 C CB    . GLU B  1 1214 ? 11.605  52.793  81.834  1.00 26.37 ? 1212 GLU B CB    1 
ATOM   17557 C CG    . GLU B  1 1214 ? 12.137  51.505  82.477  1.00 32.61 ? 1212 GLU B CG    1 
ATOM   17558 C CD    . GLU B  1 1214 ? 13.236  51.740  83.509  1.00 45.39 ? 1212 GLU B CD    1 
ATOM   17559 O OE1   . GLU B  1 1214 ? 13.919  52.786  83.433  1.00 47.46 ? 1212 GLU B OE1   1 
ATOM   17560 O OE2   . GLU B  1 1214 ? 13.422  50.868  84.395  1.00 50.38 ? 1212 GLU B OE2   1 
ATOM   17561 N N     . GLU B  1 1215 ? 9.573   50.344  80.715  1.00 20.76 ? 1213 GLU B N     1 
ATOM   17562 C CA    . GLU B  1 1215 ? 8.646   49.323  81.175  1.00 17.99 ? 1213 GLU B CA    1 
ATOM   17563 C C     . GLU B  1 1215 ? 9.133   48.739  82.490  1.00 19.87 ? 1213 GLU B C     1 
ATOM   17564 O O     . GLU B  1 1215 ? 10.313  48.418  82.631  1.00 20.45 ? 1213 GLU B O     1 
ATOM   17565 C CB    . GLU B  1 1215 ? 8.556   48.198  80.158  1.00 21.53 ? 1213 GLU B CB    1 
ATOM   17566 C CG    . GLU B  1 1215 ? 8.169   48.620  78.785  1.00 21.63 ? 1213 GLU B CG    1 
ATOM   17567 C CD    . GLU B  1 1215 ? 8.411   47.500  77.795  1.00 21.09 ? 1213 GLU B CD    1 
ATOM   17568 O OE1   . GLU B  1 1215 ? 9.548   47.384  77.303  1.00 22.87 ? 1213 GLU B OE1   1 
ATOM   17569 O OE2   . GLU B  1 1215 ? 7.461   46.733  77.543  1.00 22.37 ? 1213 GLU B OE2   1 
ATOM   17570 N N     . VAL B  1 1216 ? 8.215   48.572  83.435  1.00 19.35 ? 1214 VAL B N     1 
ATOM   17571 C CA    . VAL B  1 1216 ? 8.492   47.888  84.690  1.00 19.01 ? 1214 VAL B CA    1 
ATOM   17572 C C     . VAL B  1 1216 ? 7.447   46.805  84.874  1.00 20.61 ? 1214 VAL B C     1 
ATOM   17573 O O     . VAL B  1 1216 ? 6.247   47.048  84.692  1.00 20.87 ? 1214 VAL B O     1 
ATOM   17574 C CB    . VAL B  1 1216 ? 8.493   48.854  85.885  1.00 19.92 ? 1214 VAL B CB    1 
ATOM   17575 C CG1   . VAL B  1 1216 ? 8.710   48.086  87.220  1.00 22.51 ? 1214 VAL B CG1   1 
ATOM   17576 C CG2   . VAL B  1 1216 ? 9.535   49.912  85.668  1.00 22.10 ? 1214 VAL B CG2   1 
ATOM   17577 N N     . SER B  1 1217 ? 7.907   45.602  85.185  1.00 17.78 ? 1215 SER B N     1 
ATOM   17578 C CA    . SER B  1 1217 ? 7.049   44.480  85.496  1.00 15.87 ? 1215 SER B CA    1 
ATOM   17579 C C     . SER B  1 1217 ? 7.178   44.176  86.981  1.00 18.68 ? 1215 SER B C     1 
ATOM   17580 O O     . SER B  1 1217 ? 8.288   44.161  87.523  1.00 20.56 ? 1215 SER B O     1 
ATOM   17581 C CB    . SER B  1 1217 ? 7.430   43.252  84.666  1.00 19.22 ? 1215 SER B CB    1 
ATOM   17582 O OG    . SER B  1 1217 ? 6.927   42.063  85.248  1.00 20.45 ? 1215 SER B OG    1 
ATOM   17583 N N     . ALA B  1 1218 ? 6.042   43.975  87.641  1.00 20.38 ? 1216 ALA B N     1 
ATOM   17584 C CA    . ALA B  1 1218 ? 6.023   43.620  89.053  1.00 19.13 ? 1216 ALA B CA    1 
ATOM   17585 C C     . ALA B  1 1218 ? 5.092   42.437  89.267  1.00 22.00 ? 1216 ALA B C     1 
ATOM   17586 O O     . ALA B  1 1218 ? 3.918   42.477  88.872  1.00 21.60 ? 1216 ALA B O     1 
ATOM   17587 C CB    . ALA B  1 1218 ? 5.589   44.808  89.923  1.00 18.50 ? 1216 ALA B CB    1 
ATOM   17588 N N     . SER B  1 1219 ? 5.610   41.390  89.910  1.00 19.86 ? 1217 SER B N     1 
ATOM   17589 C CA    . SER B  1 1219 ? 4.844   40.179  90.167  1.00 18.86 ? 1217 SER B CA    1 
ATOM   17590 C C     . SER B  1 1219 ? 4.765   39.975  91.674  1.00 18.97 ? 1217 SER B C     1 
ATOM   17591 O O     . SER B  1 1219 ? 5.795   39.809  92.333  1.00 20.86 ? 1217 SER B O     1 
ATOM   17592 C CB    . SER B  1 1219 ? 5.484   38.973  89.478  1.00 20.41 ? 1217 SER B CB    1 
ATOM   17593 O OG    . SER B  1 1219 ? 4.739   37.796  89.743  1.00 22.25 ? 1217 SER B OG    1 
ATOM   17594 N N     . ILE B  1 1220 ? 3.551   40.008  92.211  1.00 21.74 ? 1218 ILE B N     1 
ATOM   17595 C CA    . ILE B  1 1220 ? 3.316   39.929  93.650  1.00 21.04 ? 1218 ILE B CA    1 
ATOM   17596 C C     . ILE B  1 1220 ? 2.603   38.619  93.949  1.00 20.99 ? 1218 ILE B C     1 
ATOM   17597 O O     . ILE B  1 1220 ? 1.507   38.366  93.431  1.00 20.07 ? 1218 ILE B O     1 
ATOM   17598 C CB    . ILE B  1 1220 ? 2.495   41.121  94.165  1.00 23.58 ? 1218 ILE B CB    1 
ATOM   17599 C CG1   . ILE B  1 1220 ? 3.176   42.441  93.803  1.00 28.34 ? 1218 ILE B CG1   1 
ATOM   17600 C CG2   . ILE B  1 1220 ? 2.340   41.024  95.671  1.00 24.93 ? 1218 ILE B CG2   1 
ATOM   17601 C CD1   . ILE B  1 1220 ? 2.670   43.087  92.533  1.00 32.20 ? 1218 ILE B CD1   1 
ATOM   17602 N N     . ASN B  1 1221 ? 3.222   37.794  94.791  1.00 17.35 ? 1219 ASN B N     1 
ATOM   17603 C CA    . ASN B  1 1221 ? 2.595   36.586  95.318  1.00 21.69 ? 1219 ASN B CA    1 
ATOM   17604 C C     . ASN B  1 1221 ? 1.569   36.974  96.376  1.00 22.37 ? 1219 ASN B C     1 
ATOM   17605 O O     . ASN B  1 1221 ? 1.935   37.331  97.498  1.00 23.76 ? 1219 ASN B O     1 
ATOM   17606 C CB    . ASN B  1 1221 ? 3.665   35.670  95.916  1.00 20.89 ? 1219 ASN B CB    1 
ATOM   17607 C CG    . ASN B  1 1221 ? 3.088   34.361  96.471  1.00 23.58 ? 1219 ASN B CG    1 
ATOM   17608 O OD1   . ASN B  1 1221 ? 1.902   34.069  96.306  1.00 23.93 ? 1219 ASN B OD1   1 
ATOM   17609 N ND2   . ASN B  1 1221 ? 3.934   33.570  97.131  1.00 19.56 ? 1219 ASN B ND2   1 
ATOM   17610 N N     . THR B  1 1222 ? 0.284   36.885  96.040  1.00 19.00 ? 1220 THR B N     1 
ATOM   17611 C CA    . THR B  1 1222 ? -0.776  37.225  96.977  1.00 21.62 ? 1220 THR B CA    1 
ATOM   17612 C C     . THR B  1 1222 ? -1.308  36.006  97.726  1.00 28.30 ? 1220 THR B C     1 
ATOM   17613 O O     . THR B  1 1222 ? -2.297  36.119  98.465  1.00 30.04 ? 1220 THR B O     1 
ATOM   17614 C CB    . THR B  1 1222 ? -1.916  37.940  96.257  1.00 26.38 ? 1220 THR B CB    1 
ATOM   17615 O OG1   . THR B  1 1222 ? -2.418  37.106  95.207  1.00 26.23 ? 1220 THR B OG1   1 
ATOM   17616 C CG2   . THR B  1 1222 ? -1.437  39.276  95.674  1.00 27.66 ? 1220 THR B CG2   1 
ATOM   17617 N N     . ALA B  1 1223 ? -0.658  34.858  97.577  1.00 24.96 ? 1221 ALA B N     1 
ATOM   17618 C CA    . ALA B  1 1223 ? -1.051  33.647  98.290  1.00 30.37 ? 1221 ALA B CA    1 
ATOM   17619 C C     . ALA B  1 1223 ? -0.165  33.425  99.512  1.00 33.97 ? 1221 ALA B C     1 
ATOM   17620 O O     . ALA B  1 1223 ? 0.034   34.333  100.318 1.00 43.35 ? 1221 ALA B O     1 
ATOM   17621 C CB    . ALA B  1 1223 ? -0.980  32.449  97.371  1.00 27.07 ? 1221 ALA B CB    1 
HETATM 17622 P PA    . FAD C  2 .    ? -37.597 43.367  82.686  0.88 31.09 ? 2001 FAD A PA    1 
HETATM 17623 O O1A   . FAD C  2 .    ? -36.151 42.834  82.546  0.88 35.80 ? 2001 FAD A O1A   1 
HETATM 17624 O O2A   . FAD C  2 .    ? -38.670 42.475  83.038  0.88 30.09 ? 2001 FAD A O2A   1 
HETATM 17625 O O5B   . FAD C  2 .    ? -37.842 44.394  83.721  0.88 32.53 ? 2001 FAD A O5B   1 
HETATM 17626 C C5B   . FAD C  2 .    ? -36.817 45.322  84.053  0.88 28.83 ? 2001 FAD A C5B   1 
HETATM 17627 C C4B   . FAD C  2 .    ? -37.382 46.413  84.956  0.88 27.44 ? 2001 FAD A C4B   1 
HETATM 17628 O O4B   . FAD C  2 .    ? -37.441 45.995  86.290  0.88 27.50 ? 2001 FAD A O4B   1 
HETATM 17629 C C3B   . FAD C  2 .    ? -36.596 47.691  84.948  0.88 29.67 ? 2001 FAD A C3B   1 
HETATM 17630 O O3B   . FAD C  2 .    ? -36.895 48.537  83.898  0.88 28.97 ? 2001 FAD A O3B   1 
HETATM 17631 C C2B   . FAD C  2 .    ? -36.969 48.312  86.239  0.88 25.69 ? 2001 FAD A C2B   1 
HETATM 17632 O O2B   . FAD C  2 .    ? -38.155 49.019  86.184  0.88 28.13 ? 2001 FAD A O2B   1 
HETATM 17633 C C1B   . FAD C  2 .    ? -37.173 47.114  87.088  0.88 29.69 ? 2001 FAD A C1B   1 
HETATM 17634 N N9A   . FAD C  2 .    ? -36.048 46.829  87.930  0.88 29.72 ? 2001 FAD A N9A   1 
HETATM 17635 C C8A   . FAD C  2 .    ? -34.768 46.422  87.587  0.88 33.23 ? 2001 FAD A C8A   1 
HETATM 17636 N N7A   . FAD C  2 .    ? -34.039 46.266  88.704  0.88 29.66 ? 2001 FAD A N7A   1 
HETATM 17637 C C5A   . FAD C  2 .    ? -34.831 46.569  89.808  0.88 24.53 ? 2001 FAD A C5A   1 
HETATM 17638 C C6A   . FAD C  2 .    ? -34.650 46.592  91.176  0.88 28.08 ? 2001 FAD A C6A   1 
HETATM 17639 N N6A   . FAD C  2 .    ? -33.374 46.234  91.759  0.88 24.52 ? 2001 FAD A N6A   1 
HETATM 17640 N N1A   . FAD C  2 .    ? -35.678 46.944  91.975  0.88 24.20 ? 2001 FAD A N1A   1 
HETATM 17641 C C2A   . FAD C  2 .    ? -36.897 47.280  91.498  0.88 25.95 ? 2001 FAD A C2A   1 
HETATM 17642 N N3A   . FAD C  2 .    ? -37.106 47.280  90.156  0.88 25.53 ? 2001 FAD A N3A   1 
HETATM 17643 C C4A   . FAD C  2 .    ? -36.115 46.939  89.325  0.88 26.42 ? 2001 FAD A C4A   1 
HETATM 17644 N N1    . FAD C  2 .    ? -41.113 53.528  81.691  0.88 24.31 ? 2001 FAD A N1    1 
HETATM 17645 C C2    . FAD C  2 .    ? -41.385 54.784  82.320  0.88 21.09 ? 2001 FAD A C2    1 
HETATM 17646 O O2    . FAD C  2 .    ? -40.821 55.029  83.509  0.88 18.60 ? 2001 FAD A O2    1 
HETATM 17647 N N3    . FAD C  2 .    ? -42.195 55.726  81.726  0.88 22.54 ? 2001 FAD A N3    1 
HETATM 17648 C C4    . FAD C  2 .    ? -42.758 55.462  80.494  0.88 22.07 ? 2001 FAD A C4    1 
HETATM 17649 O O4    . FAD C  2 .    ? -43.576 56.407  79.936  0.88 26.41 ? 2001 FAD A O4    1 
HETATM 17650 C C4X   . FAD C  2 .    ? -42.529 54.148  79.813  0.88 23.82 ? 2001 FAD A C4X   1 
HETATM 17651 N N5    . FAD C  2 .    ? -43.117 53.811  78.596  0.88 24.79 ? 2001 FAD A N5    1 
HETATM 17652 C C5X   . FAD C  2 .    ? -42.874 52.547  78.040  0.88 26.83 ? 2001 FAD A C5X   1 
HETATM 17653 C C6    . FAD C  2 .    ? -43.470 52.210  76.815  0.88 22.89 ? 2001 FAD A C6    1 
HETATM 17654 C C7    . FAD C  2 .    ? -43.219 50.959  76.260  0.88 24.58 ? 2001 FAD A C7    1 
HETATM 17655 C C7M   . FAD C  2 .    ? -43.854 50.577  74.951  0.88 24.29 ? 2001 FAD A C7M   1 
HETATM 17656 C C8    . FAD C  2 .    ? -42.419 50.032  76.895  0.88 23.72 ? 2001 FAD A C8    1 
HETATM 17657 C C8M   . FAD C  2 .    ? -42.178 48.689  76.273  0.88 23.94 ? 2001 FAD A C8M   1 
HETATM 17658 C C9    . FAD C  2 .    ? -41.822 50.348  78.117  0.88 29.53 ? 2001 FAD A C9    1 
HETATM 17659 C C9A   . FAD C  2 .    ? -42.052 51.606  78.679  0.88 27.62 ? 2001 FAD A C9A   1 
HETATM 17660 N N10   . FAD C  2 .    ? -41.432 51.941  79.920  0.88 29.07 ? 2001 FAD A N10   1 
HETATM 17661 C C10   . FAD C  2 .    ? -41.686 53.197  80.492  0.88 23.35 ? 2001 FAD A C10   1 
HETATM 17662 C "C1'" . FAD C  2 .    ? -40.616 50.931  80.654  0.88 29.42 ? 2001 FAD A "C1'" 1 
HETATM 17663 C "C2'" . FAD C  2 .    ? -39.111 51.069  80.717  0.88 30.64 ? 2001 FAD A "C2'" 1 
HETATM 17664 O "O2'" . FAD C  2 .    ? -38.668 51.948  79.764  0.88 29.43 ? 2001 FAD A "O2'" 1 
HETATM 17665 C "C3'" . FAD C  2 .    ? -38.505 49.672  80.498  0.88 28.25 ? 2001 FAD A "C3'" 1 
HETATM 17666 O "O3'" . FAD C  2 .    ? -38.689 49.323  79.181  0.88 31.54 ? 2001 FAD A "O3'" 1 
HETATM 17667 C "C4'" . FAD C  2 .    ? -39.180 48.569  81.295  0.88 33.18 ? 2001 FAD A "C4'" 1 
HETATM 17668 O "O4'" . FAD C  2 .    ? -39.137 48.858  82.643  0.88 32.42 ? 2001 FAD A "O4'" 1 
HETATM 17669 C "C5'" . FAD C  2 .    ? -38.590 47.194  80.967  0.88 28.38 ? 2001 FAD A "C5'" 1 
HETATM 17670 O "O5'" . FAD C  2 .    ? -39.298 46.209  81.687  0.88 28.75 ? 2001 FAD A "O5'" 1 
HETATM 17671 P P     . FAD C  2 .    ? -39.580 44.708  81.164  0.88 30.34 ? 2001 FAD A P     1 
HETATM 17672 O O1P   . FAD C  2 .    ? -40.921 44.010  81.606  0.88 33.64 ? 2001 FAD A O1P   1 
HETATM 17673 O O2P   . FAD C  2 .    ? -39.330 44.954  79.636  0.88 29.18 ? 2001 FAD A O2P   1 
HETATM 17674 O O3P   . FAD C  2 .    ? -38.166 43.947  81.428  0.88 31.82 ? 2001 FAD A O3P   1 
HETATM 17675 C C1    . PEG D  3 .    ? -52.369 76.651  74.409  1.00 28.77 ? 2002 PEG A C1    1 
HETATM 17676 O O1    . PEG D  3 .    ? -52.491 77.957  74.932  1.00 39.94 ? 2002 PEG A O1    1 
HETATM 17677 C C2    . PEG D  3 .    ? -51.609 76.654  73.107  1.00 34.73 ? 2002 PEG A C2    1 
HETATM 17678 O O2    . PEG D  3 .    ? -50.224 76.570  73.333  1.00 38.57 ? 2002 PEG A O2    1 
HETATM 17679 C C3    . PEG D  3 .    ? -49.468 76.877  72.183  1.00 35.42 ? 2002 PEG A C3    1 
HETATM 17680 C C4    . PEG D  3 .    ? -48.012 76.605  72.448  1.00 40.40 ? 2002 PEG A C4    1 
HETATM 17681 O O4    . PEG D  3 .    ? -47.518 77.535  73.387  1.00 47.01 ? 2002 PEG A O4    1 
HETATM 17682 C C1    . PGE E  4 .    ? -3.046  60.229  95.361  1.00 37.90 ? 2003 PGE A C1    1 
HETATM 17683 O O1    . PGE E  4 .    ? -4.111  60.208  94.435  1.00 49.11 ? 2003 PGE A O1    1 
HETATM 17684 C C2    . PGE E  4 .    ? -2.967  61.569  96.057  1.00 34.75 ? 2003 PGE A C2    1 
HETATM 17685 O O2    . PGE E  4 .    ? -1.841  61.576  96.914  1.00 37.34 ? 2003 PGE A O2    1 
HETATM 17686 C C3    . PGE E  4 .    ? -1.004  62.699  96.838  1.00 30.07 ? 2003 PGE A C3    1 
HETATM 17687 C C4    . PGE E  4 .    ? 0.425   62.465  97.252  1.00 30.18 ? 2003 PGE A C4    1 
HETATM 17688 O O4    . PGE E  4 .    ? 1.751   59.202  96.219  1.00 47.10 ? 2003 PGE A O4    1 
HETATM 17689 C C6    . PGE E  4 .    ? 2.554   60.205  95.634  1.00 41.16 ? 2003 PGE A C6    1 
HETATM 17690 C C5    . PGE E  4 .    ? 2.387   61.429  96.505  1.00 36.93 ? 2003 PGE A C5    1 
HETATM 17691 O O3    . PGE E  4 .    ? 1.180   62.037  96.148  1.00 42.79 ? 2003 PGE A O3    1 
HETATM 17692 C C1    . PEG F  3 .    ? 13.554  87.637  109.960 1.00 36.46 ? 2004 PEG A C1    1 
HETATM 17693 O O1    . PEG F  3 .    ? 14.405  87.032  110.909 1.00 40.41 ? 2004 PEG A O1    1 
HETATM 17694 C C2    . PEG F  3 .    ? 12.916  88.862  110.560 1.00 40.44 ? 2004 PEG A C2    1 
HETATM 17695 O O2    . PEG F  3 .    ? 12.260  88.522  111.757 1.00 40.89 ? 2004 PEG A O2    1 
HETATM 17696 C C3    . PEG F  3 .    ? 10.866  88.665  111.679 1.00 35.96 ? 2004 PEG A C3    1 
HETATM 17697 C C4    . PEG F  3 .    ? 10.375  89.357  112.919 1.00 40.16 ? 2004 PEG A C4    1 
HETATM 17698 O O4    . PEG F  3 .    ? 11.211  90.461  113.179 1.00 46.74 ? 2004 PEG A O4    1 
HETATM 17699 N N1    A 8P4 G  5 .    ? -15.885 91.688  113.114 0.49 36.76 ? 2005 8P4 A N1    1 
HETATM 17700 N N1    B 8P4 G  5 .    ? -13.337 90.744  115.122 0.41 36.03 ? 2005 8P4 A N1    1 
HETATM 17701 C C4    A 8P4 G  5 .    ? -13.043 90.557  115.434 0.49 35.96 ? 2005 8P4 A C4    1 
HETATM 17702 C C4    B 8P4 G  5 .    ? -16.781 89.882  113.699 0.41 36.30 ? 2005 8P4 A C4    1 
HETATM 17703 C C5    A 8P4 G  5 .    ? -14.311 90.484  114.875 0.49 35.32 ? 2005 8P4 A C5    1 
HETATM 17704 C C5    B 8P4 G  5 .    ? -15.626 89.729  114.442 0.41 33.97 ? 2005 8P4 A C5    1 
HETATM 17705 C C6    A 8P4 G  5 .    ? -14.705 91.417  113.924 0.49 36.76 ? 2005 8P4 A C6    1 
HETATM 17706 C C6    B 8P4 G  5 .    ? -14.630 90.693  114.428 0.41 35.83 ? 2005 8P4 A C6    1 
HETATM 17707 C C7    A 8P4 G  5 .    ? -17.209 91.089  113.260 0.49 38.53 ? 2005 8P4 A C7    1 
HETATM 17708 C C7    B 8P4 G  5 .    ? -12.150 91.608  115.062 0.41 35.38 ? 2005 8P4 A C7    1 
HETATM 17709 C C1    A 8P4 G  5 .    ? -13.821 92.410  113.531 0.49 34.97 ? 2005 8P4 A C1    1 
HETATM 17710 C C1    B 8P4 G  5 .    ? -14.819 91.827  113.650 0.41 36.57 ? 2005 8P4 A C1    1 
HETATM 17711 C C2    A 8P4 G  5 .    ? -12.557 92.478  114.087 0.49 38.72 ? 2005 8P4 A C2    1 
HETATM 17712 C C2    B 8P4 G  5 .    ? -15.974 91.990  112.903 0.41 36.75 ? 2005 8P4 A C2    1 
HETATM 17713 C C3    A 8P4 G  5 .    ? -12.161 91.553  115.041 0.49 35.37 ? 2005 8P4 A C3    1 
HETATM 17714 C C3    B 8P4 G  5 .    ? -16.957 91.015  112.925 0.41 37.95 ? 2005 8P4 A C3    1 
HETATM 17715 N N2    A 8P4 G  5 .    ? -18.236 91.512  112.325 0.49 40.06 ? 2005 8P4 A N2    1 
HETATM 17716 N N2    B 8P4 G  5 .    ? -11.059 91.259  115.957 0.41 35.60 ? 2005 8P4 A N2    1 
HETATM 17717 S S1    A 8P4 G  5 .    ? -17.611 90.018  114.391 0.49 35.87 ? 2005 8P4 A S1    1 
HETATM 17718 S S1    B 8P4 G  5 .    ? -11.926 92.893  114.129 0.41 43.06 ? 2005 8P4 A S1    1 
HETATM 17719 F F1    A 8P4 G  5 .    ? -10.890 91.714  115.522 0.49 37.27 ? 2005 8P4 A F1    1 
HETATM 17720 F F1    B 8P4 G  5 .    ? -18.060 91.265  112.161 0.41 40.29 ? 2005 8P4 A F1    1 
HETATM 17721 C C     . FMT H  6 .    ? -37.079 67.470  98.648  1.00 33.08 ? 2006 FMT A C     1 
HETATM 17722 O O1    . FMT H  6 .    ? -36.330 67.179  99.603  1.00 38.10 ? 2006 FMT A O1    1 
HETATM 17723 O O2    . FMT H  6 .    ? -38.288 67.781  98.666  1.00 30.58 ? 2006 FMT A O2    1 
HETATM 17724 C C1    . PEG I  3 .    ? -38.368 82.235  122.153 1.00 42.65 ? 2007 PEG A C1    1 
HETATM 17725 O O1    . PEG I  3 .    ? -37.183 82.687  121.524 1.00 36.30 ? 2007 PEG A O1    1 
HETATM 17726 C C2    . PEG I  3 .    ? -39.199 81.449  121.168 1.00 41.99 ? 2007 PEG A C2    1 
HETATM 17727 O O2    . PEG I  3 .    ? -39.931 80.455  121.840 1.00 50.37 ? 2007 PEG A O2    1 
HETATM 17728 C C3    . PEG I  3 .    ? -39.641 79.151  121.402 1.00 43.66 ? 2007 PEG A C3    1 
HETATM 17729 C C4    . PEG I  3 .    ? -38.416 78.629  122.104 1.00 48.43 ? 2007 PEG A C4    1 
HETATM 17730 O O4    . PEG I  3 .    ? -37.783 77.677  121.276 1.00 46.58 ? 2007 PEG A O4    1 
HETATM 17731 C C     . FMT J  6 .    ? -18.268 55.634  86.238  1.00 45.73 ? 2008 FMT A C     1 
HETATM 17732 O O1    . FMT J  6 .    ? -17.792 55.001  87.200  1.00 50.26 ? 2008 FMT A O1    1 
HETATM 17733 O O2    . FMT J  6 .    ? -19.347 55.451  85.631  1.00 44.34 ? 2008 FMT A O2    1 
HETATM 17734 C C     . FMT K  6 .    ? -1.762  61.115  120.454 0.95 33.56 ? 2009 FMT A C     1 
HETATM 17735 O O1    . FMT K  6 .    ? -0.901  61.078  119.559 0.95 43.25 ? 2009 FMT A O1    1 
HETATM 17736 O O2    . FMT K  6 .    ? -2.725  60.344  120.615 0.95 32.68 ? 2009 FMT A O2    1 
HETATM 17737 C C     . FMT L  6 .    ? -25.023 54.503  114.687 1.00 41.89 ? 2010 FMT A C     1 
HETATM 17738 O O1    . FMT L  6 .    ? -26.020 54.088  114.074 1.00 43.91 ? 2010 FMT A O1    1 
HETATM 17739 O O2    . FMT L  6 .    ? -24.962 55.377  115.575 1.00 50.41 ? 2010 FMT A O2    1 
HETATM 17740 C C     . FMT M  6 .    ? -20.899 98.823  124.715 0.92 50.06 ? 2011 FMT A C     1 
HETATM 17741 O O1    . FMT M  6 .    ? -20.199 98.142  123.941 0.92 48.88 ? 2011 FMT A O1    1 
HETATM 17742 O O2    . FMT M  6 .    ? -20.536 99.521  125.681 0.92 51.55 ? 2011 FMT A O2    1 
HETATM 17743 C C1    . PEG N  3 .    ? -34.318 75.404  88.734  1.00 38.95 ? 2012 PEG A C1    1 
HETATM 17744 O O1    . PEG N  3 .    ? -34.992 76.137  87.730  1.00 33.41 ? 2012 PEG A O1    1 
HETATM 17745 C C2    . PEG N  3 .    ? -34.405 76.141  90.049  1.00 36.60 ? 2012 PEG A C2    1 
HETATM 17746 O O2    . PEG N  3 .    ? -33.153 76.230  90.692  1.00 43.32 ? 2012 PEG A O2    1 
HETATM 17747 C C3    . PEG N  3 .    ? -33.050 77.438  91.410  1.00 34.41 ? 2012 PEG A C3    1 
HETATM 17748 C C4    . PEG N  3 .    ? -31.719 77.547  92.104  1.00 30.58 ? 2012 PEG A C4    1 
HETATM 17749 O O4    . PEG N  3 .    ? -31.741 76.715  93.247  1.00 38.61 ? 2012 PEG A O4    1 
HETATM 17750 C C     . FMT O  6 .    ? -1.772  55.396  101.107 1.00 32.06 ? 2013 FMT A C     1 
HETATM 17751 O O1    . FMT O  6 .    ? -1.693  54.489  101.964 1.00 34.14 ? 2013 FMT A O1    1 
HETATM 17752 O O2    . FMT O  6 .    ? -2.704  55.656  100.310 1.00 39.06 ? 2013 FMT A O2    1 
HETATM 17753 C C     . FMT P  6 .    ? 0.572   53.651  63.251  1.00 36.70 ? 2014 FMT A C     1 
HETATM 17754 O O1    . FMT P  6 .    ? 0.146   52.481  63.179  1.00 32.93 ? 2014 FMT A O1    1 
HETATM 17755 O O2    . FMT P  6 .    ? 1.747   54.059  63.160  1.00 43.67 ? 2014 FMT A O2    1 
HETATM 17756 S S     . SO4 Q  7 .    ? -9.216  52.985  111.440 1.00 23.43 ? 2015 SO4 A S     1 
HETATM 17757 O O1    . SO4 Q  7 .    ? -8.124  53.225  110.465 1.00 23.71 ? 2015 SO4 A O1    1 
HETATM 17758 O O2    . SO4 Q  7 .    ? -10.304 52.146  110.885 1.00 25.03 ? 2015 SO4 A O2    1 
HETATM 17759 O O3    . SO4 Q  7 .    ? -8.662  52.277  112.651 1.00 21.90 ? 2015 SO4 A O3    1 
HETATM 17760 O O4    . SO4 Q  7 .    ? -9.765  54.312  111.843 1.00 23.96 ? 2015 SO4 A O4    1 
HETATM 17761 S S     . SO4 R  7 .    ? -21.977 74.963  100.417 0.71 30.78 ? 2016 SO4 A S     1 
HETATM 17762 O O1    . SO4 R  7 .    ? -21.214 73.736  100.028 0.71 29.43 ? 2016 SO4 A O1    1 
HETATM 17763 O O2    . SO4 R  7 .    ? -22.632 75.531  99.217  0.71 28.31 ? 2016 SO4 A O2    1 
HETATM 17764 O O3    . SO4 R  7 .    ? -23.026 74.574  101.413 0.71 36.31 ? 2016 SO4 A O3    1 
HETATM 17765 O O4    . SO4 R  7 .    ? -21.043 75.992  100.990 0.71 36.83 ? 2016 SO4 A O4    1 
HETATM 17766 S S     . SO4 S  7 .    ? -69.622 64.436  72.850  0.71 30.15 ? 2017 SO4 A S     1 
HETATM 17767 O O1    . SO4 S  7 .    ? -68.235 64.759  72.423  0.71 42.53 ? 2017 SO4 A O1    1 
HETATM 17768 O O2    . SO4 S  7 .    ? -70.214 63.508  71.815  0.71 29.29 ? 2017 SO4 A O2    1 
HETATM 17769 O O3    . SO4 S  7 .    ? -69.660 63.812  74.210  0.71 26.85 ? 2017 SO4 A O3    1 
HETATM 17770 O O4    . SO4 S  7 .    ? -70.441 65.693  72.915  0.71 34.78 ? 2017 SO4 A O4    1 
HETATM 17771 S S     . SO4 T  7 .    ? 29.719  71.073  106.325 0.81 52.15 ? 2018 SO4 A S     1 
HETATM 17772 O O1    . SO4 T  7 .    ? 30.093  70.371  105.059 0.81 55.28 ? 2018 SO4 A O1    1 
HETATM 17773 O O2    . SO4 T  7 .    ? 28.343  71.653  106.191 0.81 50.08 ? 2018 SO4 A O2    1 
HETATM 17774 O O3    . SO4 T  7 .    ? 29.761  70.095  107.462 0.81 47.95 ? 2018 SO4 A O3    1 
HETATM 17775 O O4    . SO4 T  7 .    ? 30.695  72.176  106.584 0.81 54.26 ? 2018 SO4 A O4    1 
HETATM 17776 S S     . SO4 U  7 .    ? 11.059  89.774  106.377 0.62 36.57 ? 2019 SO4 A S     1 
HETATM 17777 O O1    . SO4 U  7 .    ? 11.707  91.093  106.674 0.62 43.74 ? 2019 SO4 A O1    1 
HETATM 17778 O O2    . SO4 U  7 .    ? 10.581  89.789  104.963 0.62 30.72 ? 2019 SO4 A O2    1 
HETATM 17779 O O3    . SO4 U  7 .    ? 12.076  88.694  106.568 0.62 38.23 ? 2019 SO4 A O3    1 
HETATM 17780 O O4    . SO4 U  7 .    ? 9.909   89.543  107.313 0.62 37.12 ? 2019 SO4 A O4    1 
HETATM 17781 S S     . SO4 V  7 .    ? -41.977 23.814  82.132  0.60 53.00 ? 2020 SO4 A S     1 
HETATM 17782 O O1    . SO4 V  7 .    ? -40.616 23.454  81.613  0.60 48.65 ? 2020 SO4 A O1    1 
HETATM 17783 O O2    . SO4 V  7 .    ? -42.639 24.761  81.175  0.60 49.02 ? 2020 SO4 A O2    1 
HETATM 17784 O O3    . SO4 V  7 .    ? -42.815 22.577  82.268  0.60 51.18 ? 2020 SO4 A O3    1 
HETATM 17785 O O4    . SO4 V  7 .    ? -41.845 24.462  83.479  0.60 47.08 ? 2020 SO4 A O4    1 
HETATM 17786 S S     . SO4 W  7 .    ? -71.425 58.191  83.926  0.65 40.34 ? 2021 SO4 A S     1 
HETATM 17787 O O1    . SO4 W  7 .    ? -70.069 58.022  83.315  0.65 36.96 ? 2021 SO4 A O1    1 
HETATM 17788 O O2    . SO4 W  7 .    ? -72.400 57.414  83.102  0.65 36.79 ? 2021 SO4 A O2    1 
HETATM 17789 O O3    . SO4 W  7 .    ? -71.404 57.707  85.346  0.65 37.89 ? 2021 SO4 A O3    1 
HETATM 17790 O O4    . SO4 W  7 .    ? -71.823 59.634  83.930  0.65 37.88 ? 2021 SO4 A O4    1 
HETATM 17791 S S     . SO4 X  7 .    ? -31.718 68.282  101.089 0.63 31.68 ? 2022 SO4 A S     1 
HETATM 17792 O O1    . SO4 X  7 .    ? -30.259 68.211  100.799 0.63 34.23 ? 2022 SO4 A O1    1 
HETATM 17793 O O2    . SO4 X  7 .    ? -32.422 67.510  100.015 0.63 37.15 ? 2022 SO4 A O2    1 
HETATM 17794 O O3    . SO4 X  7 .    ? -32.071 67.639  102.374 0.63 24.70 ? 2022 SO4 A O3    1 
HETATM 17795 O O4    . SO4 X  7 .    ? -32.218 69.698  101.029 0.63 34.82 ? 2022 SO4 A O4    1 
HETATM 17796 S S     . SO4 Y  7 .    ? -28.014 67.647  103.127 0.52 34.68 ? 2023 SO4 A S     1 
HETATM 17797 O O1    . SO4 Y  7 .    ? -27.806 67.581  101.647 0.52 33.71 ? 2023 SO4 A O1    1 
HETATM 17798 O O2    . SO4 Y  7 .    ? -29.471 67.769  103.396 0.52 30.10 ? 2023 SO4 A O2    1 
HETATM 17799 O O3    . SO4 Y  7 .    ? -27.498 66.387  103.769 0.52 29.81 ? 2023 SO4 A O3    1 
HETATM 17800 O O4    . SO4 Y  7 .    ? -27.292 68.834  103.706 0.52 30.06 ? 2023 SO4 A O4    1 
HETATM 17801 S S     . SO4 Z  7 .    ? -25.640 51.856  98.835  0.68 32.49 ? 2024 SO4 A S     1 
HETATM 17802 O O1    . SO4 Z  7 .    ? -25.416 51.191  97.516  0.68 35.04 ? 2024 SO4 A O1    1 
HETATM 17803 O O2    . SO4 Z  7 .    ? -27.101 52.037  99.068  0.68 23.52 ? 2024 SO4 A O2    1 
HETATM 17804 O O3    . SO4 Z  7 .    ? -25.081 50.970  99.914  0.68 40.84 ? 2024 SO4 A O3    1 
HETATM 17805 O O4    . SO4 Z  7 .    ? -24.907 53.170  98.907  0.68 34.82 ? 2024 SO4 A O4    1 
HETATM 17806 S S     . SO4 AA 7 .    ? 12.828  75.229  126.435 0.79 42.79 ? 2025 SO4 A S     1 
HETATM 17807 O O1    . SO4 AA 7 .    ? 13.594  75.775  125.267 0.79 41.54 ? 2025 SO4 A O1    1 
HETATM 17808 O O2    . SO4 AA 7 .    ? 11.444  74.798  126.042 0.79 34.18 ? 2025 SO4 A O2    1 
HETATM 17809 O O3    . SO4 AA 7 .    ? 13.574  74.049  126.982 0.79 40.53 ? 2025 SO4 A O3    1 
HETATM 17810 O O4    . SO4 AA 7 .    ? 12.707  76.301  127.475 0.79 50.59 ? 2025 SO4 A O4    1 
HETATM 17811 S S     . SO4 BA 7 .    ? -41.670 83.627  86.321  0.51 41.73 ? 2026 SO4 A S     1 
HETATM 17812 O O1    . SO4 BA 7 .    ? -40.254 83.193  86.100  0.51 32.47 ? 2026 SO4 A O1    1 
HETATM 17813 O O2    . SO4 BA 7 .    ? -42.574 82.820  85.452  0.51 34.16 ? 2026 SO4 A O2    1 
HETATM 17814 O O3    . SO4 BA 7 .    ? -42.065 83.400  87.751  0.51 32.83 ? 2026 SO4 A O3    1 
HETATM 17815 O O4    . SO4 BA 7 .    ? -41.786 85.082  85.962  0.51 37.36 ? 2026 SO4 A O4    1 
HETATM 17816 S S     . SO4 CA 7 .    ? -37.864 71.811  87.662  0.56 36.75 ? 2027 SO4 A S     1 
HETATM 17817 O O1    . SO4 CA 7 .    ? -36.526 72.361  87.264  0.56 40.12 ? 2027 SO4 A O1    1 
HETATM 17818 O O2    . SO4 CA 7 .    ? -38.533 71.185  86.472  0.56 34.09 ? 2027 SO4 A O2    1 
HETATM 17819 O O3    . SO4 CA 7 .    ? -37.671 70.773  88.724  0.56 39.61 ? 2027 SO4 A O3    1 
HETATM 17820 O O4    . SO4 CA 7 .    ? -38.710 72.919  88.199  0.56 26.30 ? 2027 SO4 A O4    1 
HETATM 17821 S S     . SO4 DA 7 .    ? -33.609 24.838  79.728  0.74 59.48 ? 2028 SO4 A S     1 
HETATM 17822 O O1    . SO4 DA 7 .    ? -32.934 26.131  79.380  0.74 57.13 ? 2028 SO4 A O1    1 
HETATM 17823 O O2    . SO4 DA 7 .    ? -34.425 24.365  78.564  0.74 50.82 ? 2028 SO4 A O2    1 
HETATM 17824 O O3    . SO4 DA 7 .    ? -32.549 23.828  80.058  0.74 62.54 ? 2028 SO4 A O3    1 
HETATM 17825 O O4    . SO4 DA 7 .    ? -34.499 25.033  80.921  0.74 55.11 ? 2028 SO4 A O4    1 
HETATM 17826 S S     . SO4 EA 7 .    ? 6.851   75.750  122.890 0.57 36.87 ? 2029 SO4 A S     1 
HETATM 17827 O O1    . SO4 EA 7 .    ? 7.999   75.102  122.193 0.57 30.53 ? 2029 SO4 A O1    1 
HETATM 17828 O O2    . SO4 EA 7 .    ? 6.254   76.808  122.013 0.57 34.52 ? 2029 SO4 A O2    1 
HETATM 17829 O O3    . SO4 EA 7 .    ? 5.819   74.705  123.201 0.57 42.06 ? 2029 SO4 A O3    1 
HETATM 17830 O O4    . SO4 EA 7 .    ? 7.345   76.390  124.150 0.57 39.56 ? 2029 SO4 A O4    1 
HETATM 17831 S S     . SO4 FA 7 .    ? -12.532 75.758  70.503  0.63 36.48 ? 2030 SO4 A S     1 
HETATM 17832 O O1    . SO4 FA 7 .    ? -12.436 76.573  69.248  0.63 46.74 ? 2030 SO4 A O1    1 
HETATM 17833 O O2    . SO4 FA 7 .    ? -13.795 74.962  70.490  0.63 30.93 ? 2030 SO4 A O2    1 
HETATM 17834 O O3    . SO4 FA 7 .    ? -11.340 74.857  70.597  0.63 41.12 ? 2030 SO4 A O3    1 
HETATM 17835 O O4    . SO4 FA 7 .    ? -12.578 76.653  71.697  0.63 40.00 ? 2030 SO4 A O4    1 
HETATM 17836 P PA    . FAD GA 2 .    ? -17.055 23.166  104.399 1.00 34.57 ? 2001 FAD B PA    1 
HETATM 17837 O O1A   . FAD GA 2 .    ? -17.485 24.648  104.486 1.00 34.45 ? 2001 FAD B O1A   1 
HETATM 17838 O O2A   . FAD GA 2 .    ? -18.051 22.144  104.169 1.00 33.58 ? 2001 FAD B O2A   1 
HETATM 17839 O O5B   . FAD GA 2 .    ? -16.135 22.789  103.288 1.00 35.00 ? 2001 FAD B O5B   1 
HETATM 17840 C C5B   . FAD GA 2 .    ? -15.116 23.669  102.841 1.00 27.70 ? 2001 FAD B C5B   1 
HETATM 17841 C C4B   . FAD GA 2 .    ? -14.165 22.875  101.944 1.00 29.45 ? 2001 FAD B C4B   1 
HETATM 17842 O O4B   . FAD GA 2 .    ? -14.670 22.757  100.638 1.00 27.53 ? 2001 FAD B O4B   1 
HETATM 17843 C C3B   . FAD GA 2 .    ? -12.799 23.478  101.819 1.00 28.39 ? 2001 FAD B C3B   1 
HETATM 17844 O O3B   . FAD GA 2 .    ? -11.924 23.145  102.849 1.00 25.02 ? 2001 FAD B O3B   1 
HETATM 17845 C C2B   . FAD GA 2 .    ? -12.332 22.920  100.526 1.00 23.65 ? 2001 FAD B C2B   1 
HETATM 17846 O O2B   . FAD GA 2 .    ? -11.813 21.647  100.652 1.00 24.81 ? 2001 FAD B O2B   1 
HETATM 17847 C C1B   . FAD GA 2 .    ? -13.597 22.812  99.734  1.00 24.33 ? 2001 FAD B C1B   1 
HETATM 17848 N N9A   . FAD GA 2 .    ? -13.828 23.876  98.788  1.00 27.50 ? 2001 FAD B N9A   1 
HETATM 17849 C C8A   . FAD GA 2 .    ? -13.990 25.233  99.015  1.00 23.67 ? 2001 FAD B C8A   1 
HETATM 17850 N N7A   . FAD GA 2 .    ? -14.194 25.858  97.839  1.00 28.07 ? 2001 FAD B N7A   1 
HETATM 17851 C C5A   . FAD GA 2 .    ? -14.164 24.935  96.800  1.00 26.52 ? 2001 FAD B C5A   1 
HETATM 17852 C C6A   . FAD GA 2 .    ? -14.309 24.978  95.416  1.00 23.93 ? 2001 FAD B C6A   1 
HETATM 17853 N N6A   . FAD GA 2 .    ? -14.551 26.204  94.709  1.00 23.42 ? 2001 FAD B N6A   1 
HETATM 17854 N N1A   . FAD GA 2 .    ? -14.212 23.845  94.704  1.00 25.66 ? 2001 FAD B N1A   1 
HETATM 17855 C C2A   . FAD GA 2 .    ? -13.988 22.643  95.279  1.00 23.37 ? 2001 FAD B C2A   1 
HETATM 17856 N N3A   . FAD GA 2 .    ? -13.848 22.564  96.630  1.00 26.41 ? 2001 FAD B N3A   1 
HETATM 17857 C C4A   . FAD GA 2 .    ? -13.928 23.665  97.393  1.00 24.69 ? 2001 FAD B C4A   1 
HETATM 17858 N N1    . FAD GA 2 .    ? -7.450  18.509  105.063 1.00 27.15 ? 2001 FAD B N1    1 
HETATM 17859 C C2    . FAD GA 2 .    ? -6.289  17.993  104.399 1.00 23.30 ? 2001 FAD B C2    1 
HETATM 17860 O O2    . FAD GA 2 .    ? -5.987  18.423  103.160 1.00 23.75 ? 2001 FAD B O2    1 
HETATM 17861 N N3    . FAD GA 2 .    ? -5.467  17.072  105.017 1.00 26.19 ? 2001 FAD B N3    1 
HETATM 17862 C C4    . FAD GA 2 .    ? -5.754  16.632  106.293 1.00 27.23 ? 2001 FAD B C4    1 
HETATM 17863 O O4    . FAD GA 2 .    ? -4.947  15.711  106.891 1.00 25.82 ? 2001 FAD B O4    1 
HETATM 17864 C C4X   . FAD GA 2 .    ? -6.972  17.096  107.011 1.00 28.80 ? 2001 FAD B C4X   1 
HETATM 17865 N N5    . FAD GA 2 .    ? -7.311  16.606  108.276 1.00 28.19 ? 2001 FAD B N5    1 
HETATM 17866 C C5X   . FAD GA 2 .    ? -8.468  17.059  108.904 1.00 30.61 ? 2001 FAD B C5X   1 
HETATM 17867 C C6    . FAD GA 2 .    ? -8.801  16.562  110.180 1.00 26.01 ? 2001 FAD B C6    1 
HETATM 17868 C C7    . FAD GA 2 .    ? -9.960  17.013  110.797 1.00 29.42 ? 2001 FAD B C7    1 
HETATM 17869 C C7M   . FAD GA 2 .    ? -10.337 16.496  112.165 1.00 32.59 ? 2001 FAD B C7M   1 
HETATM 17870 C C8    . FAD GA 2 .    ? -10.793 17.920  110.168 1.00 31.18 ? 2001 FAD B C8    1 
HETATM 17871 C C8M   . FAD GA 2 .    ? -12.041 18.394  110.851 1.00 33.55 ? 2001 FAD B C8M   1 
HETATM 17872 C C9    . FAD GA 2 .    ? -10.474 18.415  108.898 1.00 30.33 ? 2001 FAD B C9    1 
HETATM 17873 C C9A   . FAD GA 2 .    ? -9.313  17.981  108.268 1.00 30.23 ? 2001 FAD B C9A   1 
HETATM 17874 N N10   . FAD GA 2 .    ? -8.979  18.501  106.966 1.00 30.20 ? 2001 FAD B N10   1 
HETATM 17875 C C10   . FAD GA 2 .    ? -7.816  18.043  106.322 1.00 27.29 ? 2001 FAD B C10   1 
HETATM 17876 C "C1'" . FAD GA 2 .    ? -9.910  19.424  106.267 1.00 28.47 ? 2001 FAD B "C1'" 1 
HETATM 17877 C "C2'" . FAD GA 2 .    ? -9.558  20.887  106.148 1.00 32.94 ? 2001 FAD B "C2'" 1 
HETATM 17878 O "O2'" . FAD GA 2 .    ? -8.641  21.244  107.109 1.00 33.12 ? 2001 FAD B "O2'" 1 
HETATM 17879 C "C3'" . FAD GA 2 .    ? -10.864 21.673  106.318 1.00 33.52 ? 2001 FAD B "C3'" 1 
HETATM 17880 O "O3'" . FAD GA 2 .    ? -11.211 21.659  107.652 1.00 37.88 ? 2001 FAD B "O3'" 1 
HETATM 17881 C "C4'" . FAD GA 2 .    ? -12.034 21.095  105.536 1.00 33.59 ? 2001 FAD B "C4'" 1 
HETATM 17882 O "O4'" . FAD GA 2 .    ? -11.731 21.033  104.190 1.00 35.20 ? 2001 FAD B "O4'" 1 
HETATM 17883 C "C5'" . FAD GA 2 .    ? -13.334 21.863  105.743 1.00 31.75 ? 2001 FAD B "C5'" 1 
HETATM 17884 O "O5'" . FAD GA 2 .    ? -14.407 21.040  105.304 1.00 33.91 ? 2001 FAD B "O5'" 1 
HETATM 17885 P P     . FAD GA 2 .    ? -15.885 21.103  105.955 1.00 31.87 ? 2001 FAD B P     1 
HETATM 17886 O O1P   . FAD GA 2 .    ? -16.860 19.888  105.711 1.00 35.23 ? 2001 FAD B O1P   1 
HETATM 17887 O O2P   . FAD GA 2 .    ? -15.460 21.414  107.440 1.00 33.21 ? 2001 FAD B O2P   1 
HETATM 17888 O O3P   . FAD GA 2 .    ? -16.378 22.609  105.627 1.00 32.14 ? 2001 FAD B O3P   1 
HETATM 17889 C C1    . PGE HA 4 .    ? 1.378   60.371  86.850  1.00 39.79 ? 2002 PGE B C1    1 
HETATM 17890 O O1    . PGE HA 4 .    ? 1.042   59.971  88.158  1.00 48.47 ? 2002 PGE B O1    1 
HETATM 17891 C C2    . PGE HA 4 .    ? 2.876   60.358  86.700  1.00 39.46 ? 2002 PGE B C2    1 
HETATM 17892 O O2    . PGE HA 4 .    ? 3.339   59.030  86.798  1.00 37.23 ? 2002 PGE B O2    1 
HETATM 17893 C C3    . PGE HA 4 .    ? 4.000   58.524  85.665  1.00 29.89 ? 2002 PGE B C3    1 
HETATM 17894 C C4    . PGE HA 4 .    ? 4.497   57.112  85.879  1.00 29.59 ? 2002 PGE B C4    1 
HETATM 17895 O O4    . PGE HA 4 .    ? 2.039   54.526  88.160  1.00 39.73 ? 2002 PGE B O4    1 
HETATM 17896 C C6    . PGE HA 4 .    ? 2.584   54.174  86.908  1.00 34.31 ? 2002 PGE B C6    1 
HETATM 17897 C C5    . PGE HA 4 .    ? 3.837   54.993  86.658  1.00 31.05 ? 2002 PGE B C5    1 
HETATM 17898 O O3    . PGE HA 4 .    ? 3.469   56.333  86.440  1.00 33.91 ? 2002 PGE B O3    1 
HETATM 17899 C C1    . PEG IA 3 .    ? -5.378  31.873  67.848  1.00 39.11 ? 2003 PEG B C1    1 
HETATM 17900 O O1    . PEG IA 3 .    ? -6.230  32.515  66.923  1.00 44.65 ? 2003 PEG B O1    1 
HETATM 17901 C C2    . PEG IA 3 .    ? -5.802  32.250  69.244  1.00 36.53 ? 2003 PEG B C2    1 
HETATM 17902 O O2    . PEG IA 3 .    ? -5.985  31.100  70.030  1.00 42.61 ? 2003 PEG B O2    1 
HETATM 17903 C C3    . PEG IA 3 .    ? -7.325  30.908  70.415  1.00 37.15 ? 2003 PEG B C3    1 
HETATM 17904 C C4    . PEG IA 3 .    ? -7.476  31.042  71.907  1.00 34.17 ? 2003 PEG B C4    1 
HETATM 17905 O O4    . PEG IA 3 .    ? -8.786  30.664  72.264  1.00 43.92 ? 2003 PEG B O4    1 
HETATM 17906 C C1    . PEG JA 3 .    ? 29.541  67.377  69.138  1.00 35.85 ? 2004 PEG B C1    1 
HETATM 17907 O O1    . PEG JA 3 .    ? 28.297  67.647  68.516  1.00 35.71 ? 2004 PEG B O1    1 
HETATM 17908 C C2    . PEG JA 3 .    ? 30.009  65.980  68.809  1.00 34.24 ? 2004 PEG B C2    1 
HETATM 17909 O O2    . PEG JA 3 .    ? 29.541  65.587  67.547  1.00 38.82 ? 2004 PEG B O2    1 
HETATM 17910 C C3    . PEG JA 3 .    ? 29.572  64.190  67.373  1.00 33.63 ? 2004 PEG B C3    1 
HETATM 17911 C C4    . PEG JA 3 .    ? 30.885  63.757  66.778  1.00 41.29 ? 2004 PEG B C4    1 
HETATM 17912 O O4    . PEG JA 3 .    ? 30.948  64.223  65.451  1.00 43.90 ? 2004 PEG B O4    1 
HETATM 17913 N N1    A 8P4 KA 5 .    ? 30.988  38.111  69.131  0.50 27.88 ? 2005 8P4 B N1    1 
HETATM 17914 N N1    B 8P4 KA 5 .    ? 29.442  38.456  68.068  0.40 29.64 ? 2005 8P4 B N1    1 
HETATM 17915 C C4    A 8P4 KA 5 .    ? 28.173  35.525  69.099  0.50 31.87 ? 2005 8P4 B C4    1 
HETATM 17916 C C4    B 8P4 KA 5 .    ? 29.828  35.473  70.451  0.40 32.33 ? 2005 8P4 B C4    1 
HETATM 17917 C C5    A 8P4 KA 5 .    ? 28.879  36.620  68.633  0.50 31.87 ? 2005 8P4 B C5    1 
HETATM 17918 C C5    B 8P4 KA 5 .    ? 30.101  36.745  69.976  0.40 32.59 ? 2005 8P4 B C5    1 
HETATM 17919 C C6    A 8P4 KA 5 .    ? 30.014  37.050  69.305  0.50 32.20 ? 2005 8P4 B C6    1 
HETATM 17920 C C6    B 8P4 KA 5 .    ? 29.437  37.235  68.858  0.40 32.02 ? 2005 8P4 B C6    1 
HETATM 17921 C C7    A 8P4 KA 5 .    ? 30.726  39.233  68.250  0.50 30.63 ? 2005 8P4 B C7    1 
HETATM 17922 C C7    B 8P4 KA 5 .    ? 30.623  39.310  68.024  0.40 30.70 ? 2005 8P4 B C7    1 
HETATM 17923 C C1    A 8P4 KA 5 .    ? 30.447  36.397  70.444  0.50 33.50 ? 2005 8P4 B C1    1 
HETATM 17924 C C1    B 8P4 KA 5 .    ? 28.504  36.445  68.215  0.40 31.21 ? 2005 8P4 B C1    1 
HETATM 17925 C C2    A 8P4 KA 5 .    ? 29.740  35.305  70.912  0.50 32.82 ? 2005 8P4 B C2    1 
HETATM 17926 C C2    B 8P4 KA 5 .    ? 28.234  35.174  68.689  0.40 30.43 ? 2005 8P4 B C2    1 
HETATM 17927 C C3    A 8P4 KA 5 .    ? 28.604  34.877  70.244  0.50 33.92 ? 2005 8P4 B C3    1 
HETATM 17928 C C3    B 8P4 KA 5 .    ? 28.890  34.683  69.806  0.40 33.93 ? 2005 8P4 B C3    1 
HETATM 17929 N N2    A 8P4 KA 5 .    ? 29.471  39.344  67.511  0.50 29.98 ? 2005 8P4 B N2    1 
HETATM 17930 N N2    B 8P4 KA 5 .    ? 31.818  38.974  68.786  0.40 30.58 ? 2005 8P4 B N2    1 
HETATM 17931 S S1    A 8P4 KA 5 .    ? 31.850  40.360  68.114  0.50 39.05 ? 2005 8P4 B S1    1 
HETATM 17932 S S1    B 8P4 KA 5 .    ? 30.592  40.641  67.133  0.40 36.34 ? 2005 8P4 B S1    1 
HETATM 17933 F F1    A 8P4 KA 5 .    ? 27.990  33.794  70.798  0.50 36.14 ? 2005 8P4 B F1    1 
HETATM 17934 F F1    B 8P4 KA 5 .    ? 28.539  33.412  70.177  0.40 33.11 ? 2005 8P4 B F1    1 
HETATM 17935 C C     . FMT LA 6 .    ? -3.078  55.947  83.008  1.00 25.46 ? 2006 FMT B C     1 
HETATM 17936 O O1    . FMT LA 6 .    ? -2.950  54.934  83.726  1.00 31.83 ? 2006 FMT B O1    1 
HETATM 17937 O O2    . FMT LA 6 .    ? -3.948  56.154  82.134  1.00 33.53 ? 2006 FMT B O2    1 
HETATM 17938 C C1    . PEG MA 3 .    ? 38.980  36.312  83.494  1.00 53.55 ? 2007 PEG B C1    1 
HETATM 17939 O O1    . PEG MA 3 .    ? 38.251  36.015  84.666  1.00 57.92 ? 2007 PEG B O1    1 
HETATM 17940 C C2    . PEG MA 3 .    ? 39.498  35.043  82.863  1.00 50.22 ? 2007 PEG B C2    1 
HETATM 17941 O O2    . PEG MA 3 .    ? 40.305  34.317  83.763  1.00 52.24 ? 2007 PEG B O2    1 
HETATM 17942 C C3    . PEG MA 3 .    ? 41.550  33.952  83.208  1.00 45.90 ? 2007 PEG B C3    1 
HETATM 17943 C C4    . PEG MA 3 .    ? 42.495  33.406  84.256  1.00 45.94 ? 2007 PEG B C4    1 
HETATM 17944 O O4    . PEG MA 3 .    ? 43.028  34.451  85.044  1.00 44.37 ? 2007 PEG B O4    1 
HETATM 17945 C C     . FMT NA 6 .    ? 5.916   19.550  87.294  1.00 33.93 ? 2008 FMT B C     1 
HETATM 17946 O O1    . FMT NA 6 .    ? 5.645   18.372  87.593  1.00 33.53 ? 2008 FMT B O1    1 
HETATM 17947 O O2    . FMT NA 6 .    ? 5.345   20.296  86.468  1.00 41.39 ? 2008 FMT B O2    1 
HETATM 17948 C C1    . PEG OA 3 .    ? 4.148   12.754  78.085  1.00 38.80 ? 2009 PEG B C1    1 
HETATM 17949 O O1    . PEG OA 3 .    ? 5.118   11.759  77.812  1.00 38.58 ? 2009 PEG B O1    1 
HETATM 17950 C C2    . PEG OA 3 .    ? 2.727   12.232  77.984  1.00 43.76 ? 2009 PEG B C2    1 
HETATM 17951 O O2    . PEG OA 3 .    ? 2.357   11.484  79.125  1.00 43.60 ? 2009 PEG B O2    1 
HETATM 17952 C C3    . PEG OA 3 .    ? 1.024   11.697  79.554  1.00 45.32 ? 2009 PEG B C3    1 
HETATM 17953 C C4    . PEG OA 3 .    ? 0.601   10.675  80.591  1.00 39.31 ? 2009 PEG B C4    1 
HETATM 17954 O O4    . PEG OA 3 .    ? -0.548  11.093  81.306  1.00 42.57 ? 2009 PEG B O4    1 
HETATM 17955 C C     . FMT PA 6 .    ? 23.898  72.223  82.738  1.00 39.05 ? 2010 FMT B C     1 
HETATM 17956 O O1    . FMT PA 6 .    ? 25.050  71.780  82.908  1.00 46.61 ? 2010 FMT B O1    1 
HETATM 17957 O O2    . FMT PA 6 .    ? 23.498  73.058  81.900  1.00 39.17 ? 2010 FMT B O2    1 
HETATM 17958 C C     . FMT QA 6 .    ? 25.183  25.365  49.672  1.00 41.76 ? 2011 FMT B C     1 
HETATM 17959 O O1    . FMT QA 6 .    ? 25.736  24.290  49.382  1.00 44.98 ? 2011 FMT B O1    1 
HETATM 17960 O O2    . FMT QA 6 .    ? 24.063  25.546  50.185  1.00 42.05 ? 2011 FMT B O2    1 
HETATM 17961 C C     . FMT RA 6 .    ? 36.189  30.679  58.217  0.85 40.15 ? 2012 FMT B C     1 
HETATM 17962 O O1    . FMT RA 6 .    ? 36.133  31.133  57.061  0.85 40.09 ? 2012 FMT B O1    1 
HETATM 17963 O O2    . FMT RA 6 .    ? 35.601  31.082  59.237  0.85 41.16 ? 2012 FMT B O2    1 
HETATM 17964 S S     . SO4 SA 7 .    ? -7.115  47.693  73.248  1.00 23.17 ? 2013 SO4 B S     1 
HETATM 17965 O O1    . SO4 SA 7 .    ? -5.888  46.942  72.839  1.00 26.43 ? 2013 SO4 B O1    1 
HETATM 17966 O O2    . SO4 SA 7 .    ? -7.874  48.146  72.028  1.00 22.86 ? 2013 SO4 B O2    1 
HETATM 17967 O O3    . SO4 SA 7 .    ? -7.979  46.758  74.002  1.00 22.16 ? 2013 SO4 B O3    1 
HETATM 17968 O O4    . SO4 SA 7 .    ? -6.726  48.881  74.053  1.00 27.91 ? 2013 SO4 B O4    1 
HETATM 17969 S S     . SO4 TA 7 .    ? 14.418  33.909  83.747  0.64 31.34 ? 2014 SO4 B S     1 
HETATM 17970 O O1    . SO4 TA 7 .    ? 15.634  34.673  83.315  0.64 32.20 ? 2014 SO4 B O1    1 
HETATM 17971 O O2    . SO4 TA 7 .    ? 13.932  33.071  82.605  0.64 38.90 ? 2014 SO4 B O2    1 
HETATM 17972 O O3    . SO4 TA 7 .    ? 14.784  33.012  84.864  0.64 28.67 ? 2014 SO4 B O3    1 
HETATM 17973 O O4    . SO4 TA 7 .    ? 13.322  34.849  84.159  0.64 28.06 ? 2014 SO4 B O4    1 
HETATM 17974 S S     . SO4 UA 7 .    ? 3.654   15.014  65.131  0.68 37.84 ? 2015 SO4 B S     1 
HETATM 17975 O O1    . SO4 UA 7 .    ? 3.905   13.541  64.988  0.68 38.03 ? 2015 SO4 B O1    1 
HETATM 17976 O O2    . SO4 UA 7 .    ? 3.766   15.681  63.790  0.68 35.70 ? 2015 SO4 B O2    1 
HETATM 17977 O O3    . SO4 UA 7 .    ? 2.273   15.222  65.683  0.68 46.68 ? 2015 SO4 B O3    1 
HETATM 17978 O O4    . SO4 UA 7 .    ? 4.648   15.608  66.084  0.68 34.48 ? 2015 SO4 B O4    1 
HETATM 17979 S S     . SO4 VA 7 .    ? -8.656  32.717  87.053  0.65 31.69 ? 2016 SO4 B S     1 
HETATM 17980 O O1    . SO4 VA 7 .    ? -7.256  33.235  86.893  0.65 33.98 ? 2016 SO4 B O1    1 
HETATM 17981 O O2    . SO4 VA 7 .    ? -9.480  33.244  85.914  0.65 38.54 ? 2016 SO4 B O2    1 
HETATM 17982 O O3    . SO4 VA 7 .    ? -8.685  31.232  87.074  0.65 22.08 ? 2016 SO4 B O3    1 
HETATM 17983 O O4    . SO4 VA 7 .    ? -9.214  33.219  88.346  0.65 37.16 ? 2016 SO4 B O4    1 
HETATM 17984 S S     . SO4 WA 7 .    ? 7.098   24.989  84.379  0.67 25.52 ? 2017 SO4 B S     1 
HETATM 17985 O O1    . SO4 WA 7 .    ? 7.831   26.086  83.712  0.67 34.91 ? 2017 SO4 B O1    1 
HETATM 17986 O O2    . SO4 WA 7 .    ? 5.987   24.486  83.520  0.67 26.44 ? 2017 SO4 B O2    1 
HETATM 17987 O O3    . SO4 WA 7 .    ? 8.029   23.854  84.717  0.67 34.46 ? 2017 SO4 B O3    1 
HETATM 17988 O O4    . SO4 WA 7 .    ? 6.510   25.545  85.651  0.67 28.50 ? 2017 SO4 B O4    1 
HETATM 17989 S S     . SO4 XA 7 .    ? 14.127  34.730  79.653  0.64 47.75 ? 2018 SO4 B S     1 
HETATM 17990 O O1    . SO4 XA 7 .    ? 15.186  35.274  80.565  0.64 33.61 ? 2018 SO4 B O1    1 
HETATM 17991 O O2    . SO4 XA 7 .    ? 14.026  35.556  78.402  0.64 38.47 ? 2018 SO4 B O2    1 
HETATM 17992 O O3    . SO4 XA 7 .    ? 14.477  33.317  79.296  0.64 39.08 ? 2018 SO4 B O3    1 
HETATM 17993 O O4    . SO4 XA 7 .    ? 12.793  34.758  80.341  0.64 40.75 ? 2018 SO4 B O4    1 
HETATM 17994 S S     . SO4 YA 7 .    ? 13.434  62.720  85.490  0.61 40.63 ? 2019 SO4 B S     1 
HETATM 17995 O O1    . SO4 YA 7 .    ? 14.882  62.957  85.169  0.61 34.51 ? 2019 SO4 B O1    1 
HETATM 17996 O O2    . SO4 YA 7 .    ? 12.978  61.500  84.753  0.61 33.43 ? 2019 SO4 B O2    1 
HETATM 17997 O O3    . SO4 YA 7 .    ? 13.270  62.511  86.963  0.61 43.60 ? 2019 SO4 B O3    1 
HETATM 17998 O O4    . SO4 YA 7 .    ? 12.599  63.890  85.069  0.61 33.91 ? 2019 SO4 B O4    1 
HETATM 17999 S S     . SO4 ZA 7 .    ? 6.723   28.576  81.774  0.48 32.11 ? 2020 SO4 B S     1 
HETATM 18000 O O1    . SO4 ZA 7 .    ? 7.759   29.311  80.978  0.48 27.47 ? 2020 SO4 B O1    1 
HETATM 18001 O O2    . SO4 ZA 7 .    ? 6.873   27.116  81.542  0.48 31.93 ? 2020 SO4 B O2    1 
HETATM 18002 O O3    . SO4 ZA 7 .    ? 5.362   29.011  81.297  0.48 27.75 ? 2020 SO4 B O3    1 
HETATM 18003 O O4    . SO4 ZA 7 .    ? 6.900   28.847  83.239  0.48 30.85 ? 2020 SO4 B O4    1 
HETATM 18004 S S     . SO4 AB 7 .    ? 3.141   30.548  54.402  0.60 44.03 ? 2021 SO4 B S     1 
HETATM 18005 O O1    . SO4 AB 7 .    ? 4.493   31.192  54.382  0.60 32.59 ? 2021 SO4 B O1    1 
HETATM 18006 O O2    . SO4 AB 7 .    ? 2.515   30.644  53.043  0.60 46.89 ? 2021 SO4 B O2    1 
HETATM 18007 O O3    . SO4 AB 7 .    ? 3.265   29.097  54.773  0.60 32.10 ? 2021 SO4 B O3    1 
HETATM 18008 O O4    . SO4 AB 7 .    ? 2.256   31.262  55.375  0.60 33.47 ? 2021 SO4 B O4    1 
HETATM 18009 S S     . SO4 BB 7 .    ? 15.553  59.932  58.430  0.61 36.86 ? 2022 SO4 B S     1 
HETATM 18010 O O1    . SO4 BB 7 .    ? 16.959  60.109  58.918  0.61 34.48 ? 2022 SO4 B O1    1 
HETATM 18011 O O2    . SO4 BB 7 .    ? 15.577  59.533  56.987  0.61 39.47 ? 2022 SO4 B O2    1 
HETATM 18012 O O3    . SO4 BB 7 .    ? 14.904  58.868  59.265  0.61 38.14 ? 2022 SO4 B O3    1 
HETATM 18013 O O4    . SO4 BB 7 .    ? 14.781  61.213  58.574  0.61 29.82 ? 2022 SO4 B O4    1 
HETATM 18014 O O     . HOH CB 8 .    ? -30.334 50.062  105.009 1.00 28.17 ? 2101 HOH A O     1 
HETATM 18015 O O     . HOH CB 8 .    ? -48.399 66.312  58.193  1.00 33.03 ? 2102 HOH A O     1 
HETATM 18016 O O     . HOH CB 8 .    ? -63.138 66.967  67.055  1.00 36.07 ? 2103 HOH A O     1 
HETATM 18017 O O     . HOH CB 8 .    ? -51.957 73.862  68.937  1.00 30.67 ? 2104 HOH A O     1 
HETATM 18018 O O     . HOH CB 8 .    ? -69.261 61.880  75.302  1.00 28.78 ? 2105 HOH A O     1 
HETATM 18019 O O     . HOH CB 8 .    ? -58.115 67.045  62.163  1.00 31.12 ? 2106 HOH A O     1 
HETATM 18020 O O     . HOH CB 8 .    ? -26.490 73.210  104.012 1.00 38.08 ? 2107 HOH A O     1 
HETATM 18021 O O     . HOH CB 8 .    ? -22.830 72.831  102.866 1.00 37.59 ? 2108 HOH A O     1 
HETATM 18022 O O     . HOH CB 8 .    ? -53.002 64.164  101.390 1.00 36.94 ? 2109 HOH A O     1 
HETATM 18023 O O     . HOH CB 8 .    ? -57.917 64.379  91.609  1.00 34.65 ? 2110 HOH A O     1 
HETATM 18024 O O     . HOH CB 8 .    ? -73.121 58.312  81.083  1.00 36.48 ? 2111 HOH A O     1 
HETATM 18025 O O     . HOH CB 8 .    ? -16.860 55.589  112.827 1.00 35.66 ? 2112 HOH A O     1 
HETATM 18026 O O     . HOH CB 8 .    ? -33.659 61.558  115.214 1.00 38.30 ? 2113 HOH A O     1 
HETATM 18027 O O     . HOH CB 8 .    ? -8.287  61.890  72.116  1.00 40.86 ? 2114 HOH A O     1 
HETATM 18028 O O     . HOH CB 8 .    ? -55.158 33.441  71.747  1.00 42.59 ? 2115 HOH A O     1 
HETATM 18029 O O     . HOH CB 8 .    ? -61.248 68.347  69.189  1.00 30.09 ? 2116 HOH A O     1 
HETATM 18030 O O     . HOH CB 8 .    ? 13.783  87.235  99.324  1.00 38.62 ? 2117 HOH A O     1 
HETATM 18031 O O     . HOH CB 8 .    ? -38.865 37.882  87.913  1.00 38.51 ? 2118 HOH A O     1 
HETATM 18032 O O     . HOH CB 8 .    ? -38.635 73.228  90.574  1.00 37.78 ? 2119 HOH A O     1 
HETATM 18033 O O     . HOH CB 8 .    ? -23.908 63.401  128.434 1.00 33.76 ? 2120 HOH A O     1 
HETATM 18034 O O     . HOH CB 8 .    ? -7.065  50.630  76.751  1.00 33.48 ? 2121 HOH A O     1 
HETATM 18035 O O     . HOH CB 8 .    ? -24.115 47.799  98.750  1.00 40.23 ? 2122 HOH A O     1 
HETATM 18036 O O     . HOH CB 8 .    ? -0.969  77.316  117.772 1.00 38.00 ? 2123 HOH A O     1 
HETATM 18037 O O     . HOH CB 8 .    ? -10.254 81.462  91.604  1.00 30.12 ? 2124 HOH A O     1 
HETATM 18038 O O     . HOH CB 8 .    ? -25.248 60.780  128.476 1.00 37.20 ? 2125 HOH A O     1 
HETATM 18039 O O     . HOH CB 8 .    ? 0.174   80.097  82.149  1.00 42.19 ? 2126 HOH A O     1 
HETATM 18040 O O     . HOH CB 8 .    ? -37.078 64.033  83.405  1.00 37.20 ? 2127 HOH A O     1 
HETATM 18041 O O     . HOH CB 8 .    ? -4.922  70.568  76.574  1.00 45.81 ? 2128 HOH A O     1 
HETATM 18042 O O     . HOH CB 8 .    ? -62.149 57.218  64.213  1.00 33.88 ? 2129 HOH A O     1 
HETATM 18043 O O     . HOH CB 8 .    ? -3.347  89.947  109.251 1.00 35.12 ? 2130 HOH A O     1 
HETATM 18044 O O     . HOH CB 8 .    ? -6.151  82.336  103.764 1.00 27.64 ? 2131 HOH A O     1 
HETATM 18045 O O     . HOH CB 8 .    ? -59.941 39.334  79.839  1.00 42.94 ? 2132 HOH A O     1 
HETATM 18046 O O     . HOH CB 8 .    ? -8.936  53.370  105.528 1.00 36.33 ? 2133 HOH A O     1 
HETATM 18047 O O     . HOH CB 8 .    ? -31.002 91.642  112.924 1.00 40.47 ? 2134 HOH A O     1 
HETATM 18048 O O     . HOH CB 8 .    ? -2.896  62.853  77.798  1.00 27.43 ? 2135 HOH A O     1 
HETATM 18049 O O     . HOH CB 8 .    ? -38.953 67.068  69.586  1.00 40.05 ? 2136 HOH A O     1 
HETATM 18050 O O     . HOH CB 8 .    ? -27.624 97.461  89.313  1.00 39.16 ? 2137 HOH A O     1 
HETATM 18051 O O     . HOH CB 8 .    ? -48.352 84.846  102.691 1.00 37.51 ? 2138 HOH A O     1 
HETATM 18052 O O     . HOH CB 8 .    ? -42.776 48.357  60.108  1.00 33.37 ? 2139 HOH A O     1 
HETATM 18053 O O     . HOH CB 8 .    ? -58.589 65.150  95.003  1.00 32.18 ? 2140 HOH A O     1 
HETATM 18054 O O     . HOH CB 8 .    ? -52.508 60.619  102.703 1.00 32.47 ? 2141 HOH A O     1 
HETATM 18055 O O     . HOH CB 8 .    ? 7.389   91.295  114.491 1.00 28.71 ? 2142 HOH A O     1 
HETATM 18056 O O     . HOH CB 8 .    ? -22.798 96.001  130.215 1.00 43.57 ? 2143 HOH A O     1 
HETATM 18057 O O     . HOH CB 8 .    ? -49.577 66.436  94.677  1.00 23.23 ? 2144 HOH A O     1 
HETATM 18058 O O     . HOH CB 8 .    ? -59.728 62.604  104.405 1.00 51.24 ? 2145 HOH A O     1 
HETATM 18059 O O     . HOH CB 8 .    ? -13.182 59.227  122.826 1.00 29.78 ? 2146 HOH A O     1 
HETATM 18060 O O     . HOH CB 8 .    ? -38.073 62.368  81.947  1.00 37.12 ? 2147 HOH A O     1 
HETATM 18061 O O     . HOH CB 8 .    ? -5.760  53.612  111.222 1.00 19.02 ? 2148 HOH A O     1 
HETATM 18062 O O     . HOH CB 8 .    ? -45.783 65.581  53.954  1.00 38.91 ? 2149 HOH A O     1 
HETATM 18063 O O     . HOH CB 8 .    ? -2.849  67.816  125.554 1.00 34.43 ? 2150 HOH A O     1 
HETATM 18064 O O     . HOH CB 8 .    ? -14.411 61.442  108.117 1.00 31.12 ? 2151 HOH A O     1 
HETATM 18065 O O     . HOH CB 8 .    ? -10.730 49.676  110.565 1.00 24.40 ? 2152 HOH A O     1 
HETATM 18066 O O     . HOH CB 8 .    ? -6.643  58.595  120.535 1.00 26.89 ? 2153 HOH A O     1 
HETATM 18067 O O     . HOH CB 8 .    ? -7.318  90.252  102.507 1.00 44.28 ? 2154 HOH A O     1 
HETATM 18068 O O     . HOH CB 8 .    ? -0.892  83.901  110.210 1.00 35.43 ? 2155 HOH A O     1 
HETATM 18069 O O     . HOH CB 8 .    ? 7.030   54.059  101.955 1.00 25.06 ? 2156 HOH A O     1 
HETATM 18070 O O     . HOH CB 8 .    ? -32.246 79.834  99.862  1.00 33.03 ? 2157 HOH A O     1 
HETATM 18071 O O     . HOH CB 8 .    ? -22.812 67.381  97.907  1.00 23.07 ? 2158 HOH A O     1 
HETATM 18072 O O     . HOH CB 8 .    ? -64.722 59.119  93.203  1.00 39.00 ? 2159 HOH A O     1 
HETATM 18073 O O     . HOH CB 8 .    ? -0.446  63.674  110.126 1.00 27.50 ? 2160 HOH A O     1 
HETATM 18074 O O     . HOH CB 8 .    ? -42.288 38.311  85.129  1.00 37.13 ? 2161 HOH A O     1 
HETATM 18075 O O     . HOH CB 8 .    ? -19.405 72.939  97.856  1.00 23.08 ? 2162 HOH A O     1 
HETATM 18076 O O     . HOH CB 8 .    ? -43.793 75.141  114.520 1.00 33.20 ? 2163 HOH A O     1 
HETATM 18077 O O     . HOH CB 8 .    ? -13.581 94.866  85.217  1.00 50.76 ? 2164 HOH A O     1 
HETATM 18078 O O     . HOH CB 8 .    ? -14.567 75.989  110.157 1.00 23.28 ? 2165 HOH A O     1 
HETATM 18079 O O     . HOH CB 8 .    ? -30.828 41.044  98.157  1.00 40.94 ? 2166 HOH A O     1 
HETATM 18080 O O     . HOH CB 8 .    ? -59.801 53.909  75.223  1.00 22.94 ? 2167 HOH A O     1 
HETATM 18081 O O     . HOH CB 8 .    ? -13.617 55.851  81.593  1.00 33.74 ? 2168 HOH A O     1 
HETATM 18082 O O     . HOH CB 8 .    ? -18.996 61.524  85.565  1.00 30.43 ? 2169 HOH A O     1 
HETATM 18083 O O     . HOH CB 8 .    ? -26.072 68.991  99.049  1.00 36.55 ? 2170 HOH A O     1 
HETATM 18084 O O     . HOH CB 8 .    ? -28.334 78.041  101.648 1.00 27.14 ? 2171 HOH A O     1 
HETATM 18085 O O     . HOH CB 8 .    ? -49.708 48.761  100.303 1.00 28.20 ? 2172 HOH A O     1 
HETATM 18086 O O     . HOH CB 8 .    ? -64.043 52.157  90.249  1.00 36.45 ? 2173 HOH A O     1 
HETATM 18087 O O     . HOH CB 8 .    ? -20.496 59.916  79.154  1.00 39.71 ? 2174 HOH A O     1 
HETATM 18088 O O     . HOH CB 8 .    ? -7.297  42.742  62.126  1.00 31.55 ? 2175 HOH A O     1 
HETATM 18089 O O     . HOH CB 8 .    ? -14.826 67.720  73.401  1.00 33.33 ? 2176 HOH A O     1 
HETATM 18090 O O     . HOH CB 8 .    ? -55.606 80.995  106.548 1.00 48.90 ? 2177 HOH A O     1 
HETATM 18091 O O     . HOH CB 8 .    ? -41.254 71.641  114.947 1.00 34.52 ? 2178 HOH A O     1 
HETATM 18092 O O     . HOH CB 8 .    ? -17.969 61.020  66.880  1.00 40.32 ? 2179 HOH A O     1 
HETATM 18093 O O     . HOH CB 8 .    ? -42.881 61.175  100.684 1.00 26.63 ? 2180 HOH A O     1 
HETATM 18094 O O     . HOH CB 8 .    ? -51.433 69.860  94.644  1.00 29.15 ? 2181 HOH A O     1 
HETATM 18095 O O     . HOH CB 8 .    ? -0.633  50.211  58.046  1.00 34.57 ? 2182 HOH A O     1 
HETATM 18096 O O     . HOH CB 8 .    ? -19.977 89.766  113.308 1.00 43.33 ? 2183 HOH A O     1 
HETATM 18097 O O     . HOH CB 8 .    ? -48.764 78.421  75.480  1.00 39.62 ? 2184 HOH A O     1 
HETATM 18098 O O     . HOH CB 8 .    ? -28.724 54.818  112.400 1.00 38.35 ? 2185 HOH A O     1 
HETATM 18099 O O     . HOH CB 8 .    ? -52.378 53.509  100.793 1.00 28.58 ? 2186 HOH A O     1 
HETATM 18100 O O     . HOH CB 8 .    ? -37.985 69.292  124.077 1.00 43.83 ? 2187 HOH A O     1 
HETATM 18101 O O     . HOH CB 8 .    ? -44.839 63.201  81.773  1.00 22.72 ? 2188 HOH A O     1 
HETATM 18102 O O     . HOH CB 8 .    ? 5.053   67.182  96.477  1.00 29.72 ? 2189 HOH A O     1 
HETATM 18103 O O     . HOH CB 8 .    ? -4.744  71.409  127.348 1.00 39.27 ? 2190 HOH A O     1 
HETATM 18104 O O     . HOH CB 8 .    ? -48.584 82.785  111.788 1.00 34.76 ? 2191 HOH A O     1 
HETATM 18105 O O     . HOH CB 8 .    ? -46.982 59.520  102.550 1.00 25.44 ? 2192 HOH A O     1 
HETATM 18106 O O     . HOH CB 8 .    ? -31.999 82.643  75.748  1.00 25.77 ? 2193 HOH A O     1 
HETATM 18107 O O     . HOH CB 8 .    ? -20.454 87.067  112.800 1.00 38.32 ? 2194 HOH A O     1 
HETATM 18108 O O     . HOH CB 8 .    ? -51.526 55.069  76.223  1.00 22.41 ? 2195 HOH A O     1 
HETATM 18109 O O     . HOH CB 8 .    ? -38.500 49.297  102.844 1.00 31.53 ? 2196 HOH A O     1 
HETATM 18110 O O     . HOH CB 8 .    ? -47.529 60.143  85.620  1.00 21.53 ? 2197 HOH A O     1 
HETATM 18111 O O     . HOH CB 8 .    ? -19.998 59.426  76.196  1.00 28.00 ? 2198 HOH A O     1 
HETATM 18112 O O     . HOH CB 8 .    ? -53.318 63.384  98.895  1.00 26.06 ? 2199 HOH A O     1 
HETATM 18113 O O     . HOH CB 8 .    ? -40.002 57.187  88.461  1.00 21.01 ? 2200 HOH A O     1 
HETATM 18114 O O     . HOH CB 8 .    ? -37.911 40.775  71.601  1.00 38.09 ? 2201 HOH A O     1 
HETATM 18115 O O     . HOH CB 8 .    ? -52.015 47.159  69.174  1.00 34.32 ? 2202 HOH A O     1 
HETATM 18116 O O     . HOH CB 8 .    ? -1.027  51.186  65.113  1.00 23.58 ? 2203 HOH A O     1 
HETATM 18117 O O     . HOH CB 8 .    ? -48.619 54.500  61.443  1.00 25.65 ? 2204 HOH A O     1 
HETATM 18118 O O     . HOH CB 8 .    ? -54.006 68.323  94.196  1.00 31.56 ? 2205 HOH A O     1 
HETATM 18119 O O     . HOH CB 8 .    ? -28.555 62.021  102.671 1.00 21.81 ? 2206 HOH A O     1 
HETATM 18120 O O     . HOH CB 8 .    ? 5.092   73.456  119.719 1.00 42.57 ? 2207 HOH A O     1 
HETATM 18121 O O     . HOH CB 8 .    ? -9.833  87.003  129.409 1.00 34.57 ? 2208 HOH A O     1 
HETATM 18122 O O     . HOH CB 8 .    ? -23.242 63.758  98.250  1.00 25.86 ? 2209 HOH A O     1 
HETATM 18123 O O     . HOH CB 8 .    ? -24.725 92.976  127.513 1.00 33.22 ? 2210 HOH A O     1 
HETATM 18124 O O     . HOH CB 8 .    ? -0.697  76.038  123.362 1.00 34.98 ? 2211 HOH A O     1 
HETATM 18125 O O     . HOH CB 8 .    ? -28.588 61.872  117.408 1.00 27.06 ? 2212 HOH A O     1 
HETATM 18126 O O     . HOH CB 8 .    ? -37.298 80.662  79.373  1.00 22.15 ? 2213 HOH A O     1 
HETATM 18127 O O     . HOH CB 8 .    ? -36.852 94.944  94.386  1.00 34.96 ? 2214 HOH A O     1 
HETATM 18128 O O     . HOH CB 8 .    ? -45.020 85.400  100.196 1.00 37.06 ? 2215 HOH A O     1 
HETATM 18129 O O     . HOH CB 8 .    ? -3.746  70.821  117.884 1.00 30.10 ? 2216 HOH A O     1 
HETATM 18130 O O     . HOH CB 8 .    ? -1.154  83.964  118.229 1.00 33.46 ? 2217 HOH A O     1 
HETATM 18131 O O     . HOH CB 8 .    ? -26.173 96.318  124.581 1.00 37.17 ? 2218 HOH A O     1 
HETATM 18132 O O     . HOH CB 8 .    ? 9.305   79.309  122.856 1.00 35.37 ? 2219 HOH A O     1 
HETATM 18133 O O     . HOH CB 8 .    ? 1.421   63.573  119.854 1.00 42.88 ? 2220 HOH A O     1 
HETATM 18134 O O     . HOH CB 8 .    ? -24.789 93.055  105.427 1.00 37.21 ? 2221 HOH A O     1 
HETATM 18135 O O     . HOH CB 8 .    ? -55.927 75.188  92.270  1.00 40.09 ? 2222 HOH A O     1 
HETATM 18136 O O     . HOH CB 8 .    ? -18.122 57.455  97.480  1.00 22.24 ? 2223 HOH A O     1 
HETATM 18137 O O     . HOH CB 8 .    ? -43.089 66.299  63.703  1.00 39.10 ? 2224 HOH A O     1 
HETATM 18138 O O     . HOH CB 8 .    ? -17.596 86.856  92.642  1.00 31.27 ? 2225 HOH A O     1 
HETATM 18139 O O     . HOH CB 8 .    ? -56.835 31.339  81.103  1.00 37.93 ? 2226 HOH A O     1 
HETATM 18140 O O     . HOH CB 8 .    ? -17.965 83.100  96.906  1.00 29.40 ? 2227 HOH A O     1 
HETATM 18141 O O     . HOH CB 8 .    ? -26.282 56.496  108.369 1.00 24.65 ? 2228 HOH A O     1 
HETATM 18142 O O     . HOH CB 8 .    ? -2.232  53.797  105.005 1.00 32.66 ? 2229 HOH A O     1 
HETATM 18143 O O     . HOH CB 8 .    ? -4.482  59.357  118.928 1.00 26.79 ? 2230 HOH A O     1 
HETATM 18144 O O     . HOH CB 8 .    ? -22.056 74.770  104.321 1.00 44.73 ? 2231 HOH A O     1 
HETATM 18145 O O     . HOH CB 8 .    ? -0.459  65.844  94.619  1.00 37.28 ? 2232 HOH A O     1 
HETATM 18146 O O     . HOH CB 8 .    ? -17.711 72.846  111.575 1.00 20.83 ? 2233 HOH A O     1 
HETATM 18147 O O     . HOH CB 8 .    ? -44.207 41.291  104.818 1.00 40.79 ? 2234 HOH A O     1 
HETATM 18148 O O     . HOH CB 8 .    ? -14.877 63.959  99.531  1.00 26.20 ? 2235 HOH A O     1 
HETATM 18149 O O     . HOH CB 8 .    ? -24.417 70.003  103.823 1.00 34.84 ? 2236 HOH A O     1 
HETATM 18150 O O     . HOH CB 8 .    ? -12.205 77.328  103.326 1.00 32.37 ? 2237 HOH A O     1 
HETATM 18151 O O     . HOH CB 8 .    ? -39.252 77.625  97.756  1.00 25.38 ? 2238 HOH A O     1 
HETATM 18152 O O     . HOH CB 8 .    ? -19.181 59.107  104.637 1.00 27.06 ? 2239 HOH A O     1 
HETATM 18153 O O     . HOH CB 8 .    ? 6.468   90.636  107.582 1.00 39.43 ? 2240 HOH A O     1 
HETATM 18154 O O     . HOH CB 8 .    ? -46.738 66.266  94.402  1.00 21.93 ? 2241 HOH A O     1 
HETATM 18155 O O     . HOH CB 8 .    ? -22.987 58.982  75.514  1.00 37.69 ? 2242 HOH A O     1 
HETATM 18156 O O     . HOH CB 8 .    ? -60.059 60.519  76.367  1.00 23.05 ? 2243 HOH A O     1 
HETATM 18157 O O     . HOH CB 8 .    ? -24.779 97.962  115.423 1.00 52.57 ? 2244 HOH A O     1 
HETATM 18158 O O     . HOH CB 8 .    ? -34.243 38.753  96.020  1.00 41.81 ? 2245 HOH A O     1 
HETATM 18159 O O     . HOH CB 8 .    ? -5.066  55.707  101.493 1.00 31.51 ? 2246 HOH A O     1 
HETATM 18160 O O     . HOH CB 8 .    ? 8.001   89.628  120.770 1.00 31.59 ? 2247 HOH A O     1 
HETATM 18161 O O     . HOH CB 8 .    ? -48.161 63.883  97.252  1.00 26.15 ? 2248 HOH A O     1 
HETATM 18162 O O     . HOH CB 8 .    ? -49.923 78.002  78.116  1.00 33.28 ? 2249 HOH A O     1 
HETATM 18163 O O     . HOH CB 8 .    ? -1.930  90.193  105.998 1.00 43.38 ? 2250 HOH A O     1 
HETATM 18164 O O     . HOH CB 8 .    ? -43.919 83.188  121.535 1.00 45.56 ? 2251 HOH A O     1 
HETATM 18165 O O     . HOH CB 8 .    ? -32.316 61.736  111.939 1.00 27.89 ? 2252 HOH A O     1 
HETATM 18166 O O     . HOH CB 8 .    ? -65.426 54.219  91.174  1.00 36.78 ? 2253 HOH A O     1 
HETATM 18167 O O     . HOH CB 8 .    ? -50.689 50.373  57.484  1.00 40.29 ? 2254 HOH A O     1 
HETATM 18168 O O     . HOH CB 8 .    ? 5.927   63.087  97.590  1.00 26.64 ? 2255 HOH A O     1 
HETATM 18169 O O     . HOH CB 8 .    ? -60.537 60.970  93.273  1.00 26.93 ? 2256 HOH A O     1 
HETATM 18170 O O     . HOH CB 8 .    ? -23.881 63.459  91.896  1.00 28.69 ? 2257 HOH A O     1 
HETATM 18171 O O     . HOH CB 8 .    ? -60.720 59.320  90.978  1.00 24.21 ? 2258 HOH A O     1 
HETATM 18172 O O     . HOH CB 8 .    ? -11.579 63.370  113.621 1.00 21.01 ? 2259 HOH A O     1 
HETATM 18173 O O     . HOH CB 8 .    ? -18.784 59.883  69.870  1.00 30.04 ? 2260 HOH A O     1 
HETATM 18174 O O     . HOH CB 8 .    ? 11.071  67.342  117.375 1.00 29.29 ? 2261 HOH A O     1 
HETATM 18175 O O     . HOH CB 8 .    ? -2.315  85.457  113.980 1.00 37.64 ? 2262 HOH A O     1 
HETATM 18176 O O     . HOH CB 8 .    ? -27.113 53.879  110.050 1.00 31.28 ? 2263 HOH A O     1 
HETATM 18177 O O     . HOH CB 8 .    ? -29.115 57.567  116.084 1.00 37.36 ? 2264 HOH A O     1 
HETATM 18178 O O     . HOH CB 8 .    ? -44.185 62.084  70.475  1.00 29.09 ? 2265 HOH A O     1 
HETATM 18179 O O     . HOH CB 8 .    ? 14.032  78.144  121.747 1.00 33.28 ? 2266 HOH A O     1 
HETATM 18180 O O     . HOH CB 8 .    ? -37.218 68.575  83.838  1.00 34.89 ? 2267 HOH A O     1 
HETATM 18181 O O     . HOH CB 8 .    ? 16.891  71.329  119.927 1.00 35.33 ? 2268 HOH A O     1 
HETATM 18182 O O     . HOH CB 8 .    ? -32.365 79.331  96.473  1.00 23.39 ? 2269 HOH A O     1 
HETATM 18183 O O     . HOH CB 8 .    ? -46.938 34.823  87.635  1.00 39.37 ? 2270 HOH A O     1 
HETATM 18184 O O     . HOH CB 8 .    ? -8.401  59.972  94.575  1.00 36.06 ? 2271 HOH A O     1 
HETATM 18185 O O     . HOH CB 8 .    ? -30.990 66.437  127.407 1.00 40.17 ? 2272 HOH A O     1 
HETATM 18186 O O     . HOH CB 8 .    ? -32.483 82.300  97.827  1.00 25.27 ? 2273 HOH A O     1 
HETATM 18187 O O     . HOH CB 8 .    ? -46.154 78.344  96.717  1.00 23.43 ? 2274 HOH A O     1 
HETATM 18188 O O     . HOH CB 8 .    ? -43.695 80.310  90.469  1.00 30.49 ? 2275 HOH A O     1 
HETATM 18189 O O     . HOH CB 8 .    ? -44.583 73.794  75.321  1.00 28.59 ? 2276 HOH A O     1 
HETATM 18190 O O     . HOH CB 8 .    ? -6.860  41.979  66.401  1.00 29.56 ? 2277 HOH A O     1 
HETATM 18191 O O     . HOH CB 8 .    ? -6.268  76.265  111.419 1.00 25.95 ? 2278 HOH A O     1 
HETATM 18192 O O     . HOH CB 8 .    ? -4.247  78.547  122.827 1.00 27.50 ? 2279 HOH A O     1 
HETATM 18193 O O     . HOH CB 8 .    ? -9.416  65.123  76.460  1.00 29.05 ? 2280 HOH A O     1 
HETATM 18194 O O     . HOH CB 8 .    ? -4.288  69.868  106.701 1.00 34.35 ? 2281 HOH A O     1 
HETATM 18195 O O     . HOH CB 8 .    ? -55.155 56.383  65.148  1.00 21.86 ? 2282 HOH A O     1 
HETATM 18196 O O     . HOH CB 8 .    ? -46.814 81.111  93.681  1.00 37.62 ? 2283 HOH A O     1 
HETATM 18197 O O     . HOH CB 8 .    ? -35.834 73.172  84.104  1.00 33.46 ? 2284 HOH A O     1 
HETATM 18198 O O     . HOH CB 8 .    ? -25.183 88.334  79.442  1.00 29.44 ? 2285 HOH A O     1 
HETATM 18199 O O     . HOH CB 8 .    ? -24.234 83.357  112.592 1.00 24.27 ? 2286 HOH A O     1 
HETATM 18200 O O     . HOH CB 8 .    ? -39.038 64.643  96.710  1.00 29.55 ? 2287 HOH A O     1 
HETATM 18201 O O     . HOH CB 8 .    ? -38.949 34.819  85.392  1.00 44.87 ? 2288 HOH A O     1 
HETATM 18202 O O     . HOH CB 8 .    ? -26.710 80.413  102.174 1.00 30.37 ? 2289 HOH A O     1 
HETATM 18203 O O     . HOH CB 8 .    ? -4.151  79.248  104.468 1.00 36.33 ? 2290 HOH A O     1 
HETATM 18204 O O     . HOH CB 8 .    ? -11.707 73.445  128.745 1.00 28.98 ? 2291 HOH A O     1 
HETATM 18205 O O     . HOH CB 8 .    ? -27.489 64.991  100.618 1.00 24.38 ? 2292 HOH A O     1 
HETATM 18206 O O     . HOH CB 8 .    ? -24.931 65.148  94.965  1.00 32.47 ? 2293 HOH A O     1 
HETATM 18207 O O     . HOH CB 8 .    ? -20.371 86.915  91.731  1.00 27.04 ? 2294 HOH A O     1 
HETATM 18208 O O     . HOH CB 8 .    ? -51.090 69.672  100.736 1.00 24.97 ? 2295 HOH A O     1 
HETATM 18209 O O     . HOH CB 8 .    ? -5.151  72.896  107.326 1.00 35.68 ? 2296 HOH A O     1 
HETATM 18210 O O     . HOH CB 8 .    ? -61.809 70.001  83.620  1.00 27.56 ? 2297 HOH A O     1 
HETATM 18211 O O     . HOH CB 8 .    ? -27.356 89.514  77.863  1.00 31.61 ? 2298 HOH A O     1 
HETATM 18212 O O     . HOH CB 8 .    ? -52.585 61.623  95.359  1.00 25.90 ? 2299 HOH A O     1 
HETATM 18213 O O     . HOH CB 8 .    ? -41.313 90.568  99.172  1.00 30.44 ? 2300 HOH A O     1 
HETATM 18214 O O     . HOH CB 8 .    ? -34.726 77.607  85.491  1.00 27.59 ? 2301 HOH A O     1 
HETATM 18215 O O     . HOH CB 8 .    ? -42.281 67.681  91.616  1.00 22.80 ? 2302 HOH A O     1 
HETATM 18216 O O     . HOH CB 8 .    ? -11.829 71.969  76.904  1.00 33.05 ? 2303 HOH A O     1 
HETATM 18217 O O     . HOH CB 8 .    ? 20.570  58.343  111.737 1.00 37.12 ? 2304 HOH A O     1 
HETATM 18218 O O     . HOH CB 8 .    ? -25.656 62.633  110.265 1.00 24.80 ? 2305 HOH A O     1 
HETATM 18219 O O     . HOH CB 8 .    ? -46.873 48.614  93.532  1.00 22.36 ? 2306 HOH A O     1 
HETATM 18220 O O     . HOH CB 8 .    ? -55.895 36.094  76.622  1.00 38.31 ? 2307 HOH A O     1 
HETATM 18221 O O     . HOH CB 8 .    ? -16.651 60.464  106.826 1.00 31.48 ? 2308 HOH A O     1 
HETATM 18222 O O     . HOH CB 8 .    ? -10.439 63.259  72.736  1.00 35.87 ? 2309 HOH A O     1 
HETATM 18223 O O     . HOH CB 8 .    ? -57.666 57.424  101.707 1.00 36.91 ? 2310 HOH A O     1 
HETATM 18224 O O     . HOH CB 8 .    ? 17.377  78.649  120.772 1.00 40.15 ? 2311 HOH A O     1 
HETATM 18225 O O     . HOH CB 8 .    ? -52.633 78.183  88.194  1.00 34.65 ? 2312 HOH A O     1 
HETATM 18226 O O     . HOH CB 8 .    ? -44.196 55.508  95.509  1.00 20.20 ? 2313 HOH A O     1 
HETATM 18227 O O     . HOH CB 8 .    ? -31.950 84.273  99.792  1.00 23.59 ? 2314 HOH A O     1 
HETATM 18228 O O     . HOH CB 8 .    ? -40.941 48.801  64.179  1.00 31.64 ? 2315 HOH A O     1 
HETATM 18229 O O     . HOH CB 8 .    ? -17.892 80.630  135.154 1.00 38.36 ? 2316 HOH A O     1 
HETATM 18230 O O     . HOH CB 8 .    ? -20.947 71.025  75.793  1.00 29.48 ? 2317 HOH A O     1 
HETATM 18231 O O     . HOH CB 8 .    ? -32.628 93.075  104.173 1.00 27.56 ? 2318 HOH A O     1 
HETATM 18232 O O     . HOH CB 8 .    ? -48.134 57.415  86.715  1.00 21.18 ? 2319 HOH A O     1 
HETATM 18233 O O     . HOH CB 8 .    ? 23.079  65.770  115.638 1.00 34.01 ? 2320 HOH A O     1 
HETATM 18234 O O     . HOH CB 8 .    ? 3.873   57.684  105.402 1.00 23.11 ? 2321 HOH A O     1 
HETATM 18235 O O     . HOH CB 8 .    ? -33.943 71.797  77.254  1.00 37.37 ? 2322 HOH A O     1 
HETATM 18236 O O     . HOH CB 8 .    ? -31.117 90.869  107.510 1.00 27.63 ? 2323 HOH A O     1 
HETATM 18237 O O     . HOH CB 8 .    ? -22.391 89.976  110.182 1.00 36.74 ? 2324 HOH A O     1 
HETATM 18238 O O     . HOH CB 8 .    ? -39.460 76.309  93.498  1.00 26.83 ? 2325 HOH A O     1 
HETATM 18239 O O     . HOH CB 8 .    ? -20.292 78.840  70.449  1.00 27.57 ? 2326 HOH A O     1 
HETATM 18240 O O     . HOH CB 8 .    ? -36.811 63.223  96.376  1.00 28.29 ? 2327 HOH A O     1 
HETATM 18241 O O     . HOH CB 8 .    ? -47.991 58.959  83.193  1.00 19.11 ? 2328 HOH A O     1 
HETATM 18242 O O     . HOH CB 8 .    ? -46.038 65.052  92.369  1.00 23.16 ? 2329 HOH A O     1 
HETATM 18243 O O     . HOH CB 8 .    ? -14.230 74.948  106.113 1.00 34.88 ? 2330 HOH A O     1 
HETATM 18244 O O     . HOH CB 8 .    ? -25.007 89.149  99.987  1.00 28.54 ? 2331 HOH A O     1 
HETATM 18245 O O     . HOH CB 8 .    ? -8.786  60.100  107.496 1.00 23.34 ? 2332 HOH A O     1 
HETATM 18246 O O     . HOH CB 8 .    ? -50.205 68.375  92.645  1.00 27.40 ? 2333 HOH A O     1 
HETATM 18247 O O     . HOH CB 8 .    ? -26.815 82.718  113.470 1.00 24.69 ? 2334 HOH A O     1 
HETATM 18248 O O     . HOH CB 8 .    ? 1.055   74.783  107.709 1.00 33.29 ? 2335 HOH A O     1 
HETATM 18249 O O     . HOH CB 8 .    ? -34.154 97.434  98.711  1.00 41.04 ? 2336 HOH A O     1 
HETATM 18250 O O     . HOH CB 8 .    ? -34.889 67.193  125.941 1.00 42.21 ? 2337 HOH A O     1 
HETATM 18251 O O     . HOH CB 8 .    ? 18.687  59.115  96.555  1.00 38.20 ? 2338 HOH A O     1 
HETATM 18252 O O     . HOH CB 8 .    ? -35.500 51.633  85.671  1.00 24.45 ? 2339 HOH A O     1 
HETATM 18253 O O     . HOH CB 8 .    ? 0.479   85.332  103.328 1.00 29.23 ? 2340 HOH A O     1 
HETATM 18254 O O     . HOH CB 8 .    ? -2.142  78.629  75.910  1.00 40.00 ? 2341 HOH A O     1 
HETATM 18255 O O     . HOH CB 8 .    ? -40.844 58.247  80.438  1.00 34.12 ? 2342 HOH A O     1 
HETATM 18256 O O     . HOH CB 8 .    ? -13.936 78.086  111.564 1.00 25.25 ? 2343 HOH A O     1 
HETATM 18257 O O     . HOH CB 8 .    ? -9.906  92.131  118.271 1.00 36.56 ? 2344 HOH A O     1 
HETATM 18258 O O     . HOH CB 8 .    ? 3.601   60.311  103.547 1.00 34.01 ? 2345 HOH A O     1 
HETATM 18259 O O     . HOH CB 8 .    ? -3.139  43.956  58.604  1.00 34.70 ? 2346 HOH A O     1 
HETATM 18260 O O     . HOH CB 8 .    ? -56.256 55.333  95.437  1.00 23.45 ? 2347 HOH A O     1 
HETATM 18261 O O     . HOH CB 8 .    ? -12.700 77.498  91.326  1.00 20.91 ? 2348 HOH A O     1 
HETATM 18262 O O     . HOH CB 8 .    ? -3.394  82.251  97.805  1.00 34.88 ? 2349 HOH A O     1 
HETATM 18263 O O     . HOH CB 8 .    ? -27.575 82.281  130.169 1.00 28.73 ? 2350 HOH A O     1 
HETATM 18264 O O     . HOH CB 8 .    ? -28.035 60.303  125.568 1.00 40.09 ? 2351 HOH A O     1 
HETATM 18265 O O     . HOH CB 8 .    ? -38.601 77.538  70.163  1.00 36.63 ? 2352 HOH A O     1 
HETATM 18266 O O     . HOH CB 8 .    ? -38.513 62.218  105.956 1.00 34.82 ? 2353 HOH A O     1 
HETATM 18267 O O     . HOH CB 8 .    ? -58.537 37.621  76.812  1.00 39.14 ? 2354 HOH A O     1 
HETATM 18268 O O     . HOH CB 8 .    ? -66.821 73.315  76.999  1.00 42.73 ? 2355 HOH A O     1 
HETATM 18269 O O     . HOH CB 8 .    ? -51.347 64.644  95.484  1.00 27.18 ? 2356 HOH A O     1 
HETATM 18270 O O     . HOH CB 8 .    ? -12.680 74.950  107.981 1.00 29.17 ? 2357 HOH A O     1 
HETATM 18271 O O     . HOH CB 8 .    ? 6.950   80.227  123.521 1.00 34.46 ? 2358 HOH A O     1 
HETATM 18272 O O     . HOH CB 8 .    ? -10.835 67.746  108.374 1.00 19.01 ? 2359 HOH A O     1 
HETATM 18273 O O     . HOH CB 8 .    ? -17.855 59.965  111.769 1.00 38.73 ? 2360 HOH A O     1 
HETATM 18274 O O     . HOH CB 8 .    ? 15.295  83.065  111.667 1.00 33.68 ? 2361 HOH A O     1 
HETATM 18275 O O     . HOH CB 8 .    ? -27.644 73.111  130.267 1.00 37.19 ? 2362 HOH A O     1 
HETATM 18276 O O     . HOH CB 8 .    ? -46.068 75.976  95.113  1.00 34.45 ? 2363 HOH A O     1 
HETATM 18277 O O     . HOH CB 8 .    ? -3.942  54.993  61.739  1.00 34.14 ? 2364 HOH A O     1 
HETATM 18278 O O     . HOH CB 8 .    ? 9.972   62.709  113.531 1.00 35.99 ? 2365 HOH A O     1 
HETATM 18279 O O     . HOH CB 8 .    ? -8.673  65.237  114.327 1.00 21.54 ? 2366 HOH A O     1 
HETATM 18280 O O     . HOH CB 8 .    ? -39.675 78.276  100.313 1.00 26.16 ? 2367 HOH A O     1 
HETATM 18281 O O     . HOH CB 8 .    ? -50.000 75.794  101.903 1.00 30.66 ? 2368 HOH A O     1 
HETATM 18282 O O     . HOH CB 8 .    ? -59.580 51.730  66.394  1.00 27.40 ? 2369 HOH A O     1 
HETATM 18283 O O     . HOH CB 8 .    ? -11.771 68.949  76.770  1.00 31.78 ? 2370 HOH A O     1 
HETATM 18284 O O     . HOH CB 8 .    ? -49.371 32.887  100.847 1.00 54.55 ? 2371 HOH A O     1 
HETATM 18285 O O     . HOH CB 8 .    ? -56.823 45.599  71.442  1.00 27.36 ? 2372 HOH A O     1 
HETATM 18286 O O     . HOH CB 8 .    ? 20.780  61.786  99.696  1.00 27.74 ? 2373 HOH A O     1 
HETATM 18287 O O     . HOH CB 8 .    ? -6.825  70.512  94.352  1.00 33.82 ? 2374 HOH A O     1 
HETATM 18288 O O     . HOH CB 8 .    ? -42.257 47.464  81.243  1.00 28.24 ? 2375 HOH A O     1 
HETATM 18289 O O     . HOH CB 8 .    ? -54.452 42.247  97.596  1.00 40.31 ? 2376 HOH A O     1 
HETATM 18290 O O     . HOH CB 8 .    ? -55.002 47.132  67.760  1.00 36.49 ? 2377 HOH A O     1 
HETATM 18291 O O     . HOH CB 8 .    ? -32.174 88.517  95.651  1.00 23.73 ? 2378 HOH A O     1 
HETATM 18292 O O     . HOH CB 8 .    ? -21.052 81.611  116.433 1.00 22.26 ? 2379 HOH A O     1 
HETATM 18293 O O     . HOH CB 8 .    ? -1.334  77.012  87.950  1.00 31.39 ? 2380 HOH A O     1 
HETATM 18294 O O     . HOH CB 8 .    ? -32.554 59.791  110.196 1.00 32.92 ? 2381 HOH A O     1 
HETATM 18295 O O     . HOH CB 8 .    ? -34.370 69.466  76.527  1.00 36.54 ? 2382 HOH A O     1 
HETATM 18296 O O     . HOH CB 8 .    ? -39.486 88.859  91.306  1.00 32.23 ? 2383 HOH A O     1 
HETATM 18297 O O     . HOH CB 8 .    ? -34.224 97.871  93.609  1.00 45.15 ? 2384 HOH A O     1 
HETATM 18298 O O     . HOH CB 8 .    ? -48.638 75.021  95.882  1.00 26.00 ? 2385 HOH A O     1 
HETATM 18299 O O     . HOH CB 8 .    ? 25.723  79.673  108.167 1.00 36.29 ? 2386 HOH A O     1 
HETATM 18300 O O     . HOH CB 8 .    ? -42.118 88.711  97.334  1.00 29.66 ? 2387 HOH A O     1 
HETATM 18301 O O     . HOH CB 8 .    ? -49.487 83.177  109.381 1.00 42.08 ? 2388 HOH A O     1 
HETATM 18302 O O     . HOH CB 8 .    ? -32.858 87.012  76.876  1.00 34.79 ? 2389 HOH A O     1 
HETATM 18303 O O     . HOH CB 8 .    ? -43.463 85.166  97.747  1.00 34.74 ? 2390 HOH A O     1 
HETATM 18304 O O     . HOH CB 8 .    ? -62.439 61.655  68.438  1.00 31.01 ? 2391 HOH A O     1 
HETATM 18305 O O     . HOH CB 8 .    ? -56.205 34.197  87.219  1.00 41.26 ? 2392 HOH A O     1 
HETATM 18306 O O     . HOH CB 8 .    ? -30.709 86.526  102.556 1.00 23.27 ? 2393 HOH A O     1 
HETATM 18307 O O     . HOH CB 8 .    ? -9.585  63.938  96.446  1.00 23.36 ? 2394 HOH A O     1 
HETATM 18308 O O     . HOH CB 8 .    ? -23.557 63.883  106.586 1.00 21.66 ? 2395 HOH A O     1 
HETATM 18309 O O     . HOH CB 8 .    ? -6.884  80.919  127.979 1.00 34.43 ? 2396 HOH A O     1 
HETATM 18310 O O     . HOH CB 8 .    ? -61.311 52.450  91.673  1.00 30.90 ? 2397 HOH A O     1 
HETATM 18311 O O     . HOH CB 8 .    ? -5.137  54.425  108.617 1.00 22.62 ? 2398 HOH A O     1 
HETATM 18312 O O     . HOH CB 8 .    ? -62.107 57.790  70.580  1.00 25.07 ? 2399 HOH A O     1 
HETATM 18313 O O     . HOH CB 8 .    ? -8.522  93.325  106.432 1.00 34.51 ? 2400 HOH A O     1 
HETATM 18314 O O     . HOH CB 8 .    ? -47.645 76.007  67.486  1.00 36.01 ? 2401 HOH A O     1 
HETATM 18315 O O     . HOH CB 8 .    ? -5.953  65.177  114.643 1.00 26.34 ? 2402 HOH A O     1 
HETATM 18316 O O     . HOH CB 8 .    ? -49.229 35.006  87.811  1.00 39.74 ? 2403 HOH A O     1 
HETATM 18317 O O     . HOH CB 8 .    ? -20.373 66.127  81.314  1.00 29.95 ? 2404 HOH A O     1 
HETATM 18318 O O     . HOH CB 8 .    ? -41.199 80.036  88.154  1.00 25.50 ? 2405 HOH A O     1 
HETATM 18319 O O     . HOH CB 8 .    ? -1.313  58.197  96.936  1.00 38.86 ? 2406 HOH A O     1 
HETATM 18320 O O     . HOH CB 8 .    ? -23.357 54.519  101.662 1.00 27.96 ? 2407 HOH A O     1 
HETATM 18321 O O     . HOH CB 8 .    ? -20.233 91.312  97.498  1.00 37.00 ? 2408 HOH A O     1 
HETATM 18322 O O     . HOH CB 8 .    ? -45.123 63.350  84.811  1.00 24.64 ? 2409 HOH A O     1 
HETATM 18323 O O     . HOH CB 8 .    ? 9.373   56.916  97.957  1.00 32.57 ? 2410 HOH A O     1 
HETATM 18324 O O     . HOH CB 8 .    ? -0.609  82.391  113.887 1.00 39.04 ? 2411 HOH A O     1 
HETATM 18325 O O     . HOH CB 8 .    ? 2.184   85.515  118.776 1.00 32.63 ? 2412 HOH A O     1 
HETATM 18326 O O     . HOH CB 8 .    ? 8.313   68.912  125.990 1.00 36.75 ? 2413 HOH A O     1 
HETATM 18327 O O     . HOH CB 8 .    ? -7.328  62.307  107.555 1.00 23.20 ? 2414 HOH A O     1 
HETATM 18328 O O     . HOH CB 8 .    ? -52.850 72.588  64.807  1.00 27.39 ? 2415 HOH A O     1 
HETATM 18329 O O     . HOH CB 8 .    ? -29.149 76.917  72.981  1.00 33.93 ? 2416 HOH A O     1 
HETATM 18330 O O     . HOH CB 8 .    ? -35.052 75.539  83.638  1.00 36.15 ? 2417 HOH A O     1 
HETATM 18331 O O     . HOH CB 8 .    ? -7.769  72.380  100.283 1.00 30.62 ? 2418 HOH A O     1 
HETATM 18332 O O     . HOH CB 8 .    ? -47.038 67.444  60.065  1.00 33.73 ? 2419 HOH A O     1 
HETATM 18333 O O     . HOH CB 8 .    ? -33.220 78.121  74.745  1.00 32.28 ? 2420 HOH A O     1 
HETATM 18334 O O     . HOH CB 8 .    ? -27.684 90.913  116.288 1.00 27.07 ? 2421 HOH A O     1 
HETATM 18335 O O     . HOH CB 8 .    ? -14.550 48.563  75.953  1.00 37.75 ? 2422 HOH A O     1 
HETATM 18336 O O     . HOH CB 8 .    ? -12.598 40.176  68.358  1.00 40.90 ? 2423 HOH A O     1 
HETATM 18337 O O     . HOH CB 8 .    ? -67.357 67.374  72.178  1.00 36.97 ? 2424 HOH A O     1 
HETATM 18338 O O     . HOH CB 8 .    ? 17.166  69.186  118.424 1.00 36.53 ? 2425 HOH A O     1 
HETATM 18339 O O     . HOH CB 8 .    ? -19.805 55.162  107.135 1.00 35.44 ? 2426 HOH A O     1 
HETATM 18340 O O     . HOH CB 8 .    ? -6.292  71.403  103.713 1.00 32.46 ? 2427 HOH A O     1 
HETATM 18341 O O     . HOH CB 8 .    ? -41.837 85.662  114.270 1.00 30.40 ? 2428 HOH A O     1 
HETATM 18342 O O     . HOH CB 8 .    ? -38.542 61.371  92.353  1.00 22.27 ? 2429 HOH A O     1 
HETATM 18343 O O     . HOH CB 8 .    ? -37.675 74.786  65.080  1.00 40.93 ? 2430 HOH A O     1 
HETATM 18344 O O     . HOH CB 8 .    ? -31.664 59.916  106.108 1.00 25.22 ? 2431 HOH A O     1 
HETATM 18345 O O     . HOH CB 8 .    ? -46.500 54.032  90.169  1.00 21.53 ? 2432 HOH A O     1 
HETATM 18346 O O     . HOH CB 8 .    ? -54.342 37.172  89.998  1.00 36.08 ? 2433 HOH A O     1 
HETATM 18347 O O     . HOH CB 8 .    ? -22.932 48.723  83.140  1.00 44.19 ? 2434 HOH A O     1 
HETATM 18348 O O     . HOH CB 8 .    ? -30.677 98.828  98.895  1.00 39.99 ? 2435 HOH A O     1 
HETATM 18349 O O     . HOH CB 8 .    ? -28.708 75.582  102.797 1.00 34.84 ? 2436 HOH A O     1 
HETATM 18350 O O     . HOH CB 8 .    ? -8.048  77.424  92.205  1.00 32.21 ? 2437 HOH A O     1 
HETATM 18351 O O     . HOH CB 8 .    ? -19.855 52.843  53.905  1.00 40.80 ? 2438 HOH A O     1 
HETATM 18352 O O     . HOH CB 8 .    ? -2.259  62.974  114.438 1.00 38.54 ? 2439 HOH A O     1 
HETATM 18353 O O     . HOH CB 8 .    ? -18.922 86.174  109.877 1.00 32.76 ? 2440 HOH A O     1 
HETATM 18354 O O     . HOH CB 8 .    ? -41.835 63.804  104.045 1.00 26.75 ? 2441 HOH A O     1 
HETATM 18355 O O     . HOH CB 8 .    ? -23.086 98.689  100.662 1.00 34.31 ? 2442 HOH A O     1 
HETATM 18356 O O     . HOH CB 8 .    ? -23.079 60.377  116.250 1.00 26.78 ? 2443 HOH A O     1 
HETATM 18357 O O     . HOH CB 8 .    ? -4.185  76.740  125.039 1.00 32.94 ? 2444 HOH A O     1 
HETATM 18358 O O     . HOH CB 8 .    ? -14.207 64.720  51.148  1.00 47.42 ? 2445 HOH A O     1 
HETATM 18359 O O     . HOH CB 8 .    ? -36.659 58.934  94.593  1.00 20.83 ? 2446 HOH A O     1 
HETATM 18360 O O     . HOH CB 8 .    ? -21.532 59.368  122.996 1.00 31.05 ? 2447 HOH A O     1 
HETATM 18361 O O     . HOH CB 8 .    ? -34.981 80.483  121.026 1.00 28.01 ? 2448 HOH A O     1 
HETATM 18362 O O     . HOH CB 8 .    ? 29.459  67.739  108.929 1.00 45.02 ? 2449 HOH A O     1 
HETATM 18363 O O     . HOH CB 8 .    ? -19.885 85.317  75.778  1.00 33.39 ? 2450 HOH A O     1 
HETATM 18364 O O     . HOH CB 8 .    ? -21.335 101.226 89.971  1.00 33.84 ? 2451 HOH A O     1 
HETATM 18365 O O     . HOH CB 8 .    ? -61.506 55.075  67.876  1.00 23.18 ? 2452 HOH A O     1 
HETATM 18366 O O     . HOH CB 8 .    ? -3.651  57.872  72.898  1.00 31.53 ? 2453 HOH A O     1 
HETATM 18367 O O     . HOH CB 8 .    ? -34.536 82.521  119.226 1.00 26.64 ? 2454 HOH A O     1 
HETATM 18368 O O     . HOH CB 8 .    ? -20.566 54.978  91.587  1.00 38.23 ? 2455 HOH A O     1 
HETATM 18369 O O     . HOH CB 8 .    ? 13.816  82.087  114.673 1.00 30.72 ? 2456 HOH A O     1 
HETATM 18370 O O     . HOH CB 8 .    ? -8.727  80.837  75.137  1.00 35.36 ? 2457 HOH A O     1 
HETATM 18371 O O     . HOH CB 8 .    ? -40.133 84.852  104.296 1.00 30.14 ? 2458 HOH A O     1 
HETATM 18372 O O     . HOH CB 8 .    ? -25.972 63.783  105.169 1.00 22.06 ? 2459 HOH A O     1 
HETATM 18373 O O     . HOH CB 8 .    ? -42.055 79.792  80.353  1.00 30.63 ? 2460 HOH A O     1 
HETATM 18374 O O     . HOH CB 8 .    ? 19.384  82.138  113.796 1.00 34.93 ? 2461 HOH A O     1 
HETATM 18375 O O     . HOH CB 8 .    ? -55.795 75.774  83.450  1.00 44.89 ? 2462 HOH A O     1 
HETATM 18376 O O     . HOH CB 8 .    ? -13.111 54.861  103.556 1.00 34.32 ? 2463 HOH A O     1 
HETATM 18377 O O     . HOH CB 8 .    ? 12.371  75.848  95.353  1.00 36.84 ? 2464 HOH A O     1 
HETATM 18378 O O     . HOH CB 8 .    ? -38.156 50.337  98.776  1.00 28.91 ? 2465 HOH A O     1 
HETATM 18379 O O     . HOH CB 8 .    ? -64.160 73.091  79.063  1.00 35.35 ? 2466 HOH A O     1 
HETATM 18380 O O     . HOH CB 8 .    ? -19.564 97.956  127.797 1.00 40.39 ? 2467 HOH A O     1 
HETATM 18381 O O     . HOH CB 8 .    ? -42.760 77.873  76.346  1.00 28.62 ? 2468 HOH A O     1 
HETATM 18382 O O     . HOH CB 8 .    ? -30.444 81.299  123.634 1.00 27.89 ? 2469 HOH A O     1 
HETATM 18383 O O     . HOH CB 8 .    ? -66.191 58.584  76.246  1.00 28.82 ? 2470 HOH A O     1 
HETATM 18384 O O     . HOH CB 8 .    ? -47.157 82.296  101.952 1.00 29.58 ? 2471 HOH A O     1 
HETATM 18385 O O     . HOH CB 8 .    ? -31.474 91.403  80.805  1.00 38.28 ? 2472 HOH A O     1 
HETATM 18386 O O     . HOH CB 8 .    ? -19.705 91.266  77.263  1.00 30.86 ? 2473 HOH A O     1 
HETATM 18387 O O     . HOH CB 8 .    ? -12.728 65.944  113.149 1.00 20.71 ? 2474 HOH A O     1 
HETATM 18388 O O     . HOH CB 8 .    ? -58.347 57.615  63.355  1.00 24.98 ? 2475 HOH A O     1 
HETATM 18389 O O     . HOH CB 8 .    ? -44.027 68.615  108.999 1.00 39.87 ? 2476 HOH A O     1 
HETATM 18390 O O     . HOH CB 8 .    ? -39.130 66.494  94.824  1.00 31.99 ? 2477 HOH A O     1 
HETATM 18391 O O     . HOH CB 8 .    ? 16.706  57.743  103.483 1.00 27.02 ? 2478 HOH A O     1 
HETATM 18392 O O     . HOH CB 8 .    ? 7.974   67.715  115.133 1.00 31.06 ? 2479 HOH A O     1 
HETATM 18393 O O     . HOH CB 8 .    ? 21.154  57.233  105.651 1.00 41.08 ? 2480 HOH A O     1 
HETATM 18394 O O     . HOH CB 8 .    ? -16.869 76.724  109.006 1.00 24.27 ? 2481 HOH A O     1 
HETATM 18395 O O     . HOH CB 8 .    ? -0.259  85.399  106.921 1.00 34.92 ? 2482 HOH A O     1 
HETATM 18396 O O     . HOH CB 8 .    ? -46.406 55.745  87.831  1.00 18.18 ? 2483 HOH A O     1 
HETATM 18397 O O     . HOH CB 8 .    ? 16.790  87.136  112.411 1.00 41.24 ? 2484 HOH A O     1 
HETATM 18398 O O     . HOH CB 8 .    ? 12.912  67.255  93.831  1.00 31.66 ? 2485 HOH A O     1 
HETATM 18399 O O     . HOH CB 8 .    ? -14.682 85.583  77.104  1.00 34.20 ? 2486 HOH A O     1 
HETATM 18400 O O     . HOH CB 8 .    ? -32.494 89.258  109.400 1.00 31.59 ? 2487 HOH A O     1 
HETATM 18401 O O     . HOH CB 8 .    ? -53.509 49.216  60.567  1.00 39.70 ? 2488 HOH A O     1 
HETATM 18402 O O     . HOH CB 8 .    ? -44.359 29.677  96.829  1.00 43.24 ? 2489 HOH A O     1 
HETATM 18403 O O     . HOH CB 8 .    ? -35.351 63.238  116.537 1.00 35.97 ? 2490 HOH A O     1 
HETATM 18404 O O     . HOH CB 8 .    ? -31.872 82.480  110.383 1.00 31.74 ? 2491 HOH A O     1 
HETATM 18405 O O     . HOH CB 8 .    ? -57.397 59.902  61.387  1.00 24.26 ? 2492 HOH A O     1 
HETATM 18406 O O     . HOH CB 8 .    ? -67.931 60.168  70.338  1.00 31.83 ? 2493 HOH A O     1 
HETATM 18407 O O     . HOH CB 8 .    ? -18.545 79.806  127.671 1.00 26.19 ? 2494 HOH A O     1 
HETATM 18408 O O     . HOH CB 8 .    ? -43.128 49.984  55.956  1.00 40.92 ? 2495 HOH A O     1 
HETATM 18409 O O     . HOH CB 8 .    ? -39.357 39.304  99.156  1.00 36.04 ? 2496 HOH A O     1 
HETATM 18410 O O     . HOH CB 8 .    ? -55.124 66.814  57.855  1.00 23.51 ? 2497 HOH A O     1 
HETATM 18411 O O     . HOH CB 8 .    ? -25.549 68.306  90.877  1.00 32.15 ? 2498 HOH A O     1 
HETATM 18412 O O     . HOH CB 8 .    ? -15.007 59.242  127.058 1.00 29.91 ? 2499 HOH A O     1 
HETATM 18413 O O     . HOH CB 8 .    ? -47.457 48.764  96.212  1.00 23.11 ? 2500 HOH A O     1 
HETATM 18414 O O     . HOH CB 8 .    ? -31.211 61.192  90.924  1.00 28.69 ? 2501 HOH A O     1 
HETATM 18415 O O     . HOH CB 8 .    ? -31.001 95.983  105.457 1.00 30.15 ? 2502 HOH A O     1 
HETATM 18416 O O     . HOH CB 8 .    ? -26.745 73.255  101.727 1.00 31.97 ? 2503 HOH A O     1 
HETATM 18417 O O     . HOH CB 8 .    ? -11.840 89.004  129.320 1.00 33.22 ? 2504 HOH A O     1 
HETATM 18418 O O     . HOH CB 8 .    ? -12.694 53.655  111.139 1.00 36.33 ? 2505 HOH A O     1 
HETATM 18419 O O     . HOH CB 8 .    ? -16.000 68.279  97.101  1.00 20.77 ? 2506 HOH A O     1 
HETATM 18420 O O     . HOH CB 8 .    ? -6.919  38.306  63.826  1.00 37.34 ? 2507 HOH A O     1 
HETATM 18421 O O     . HOH CB 8 .    ? -9.656  56.274  82.953  1.00 39.22 ? 2508 HOH A O     1 
HETATM 18422 O O     . HOH CB 8 .    ? -28.422 69.631  86.348  1.00 35.88 ? 2509 HOH A O     1 
HETATM 18423 O O     . HOH CB 8 .    ? -6.667  68.892  92.817  1.00 35.01 ? 2510 HOH A O     1 
HETATM 18424 O O     . HOH CB 8 .    ? -32.494 64.618  122.592 1.00 33.94 ? 2511 HOH A O     1 
HETATM 18425 O O     . HOH CB 8 .    ? -41.062 81.797  111.239 1.00 30.88 ? 2512 HOH A O     1 
HETATM 18426 O O     . HOH CB 8 .    ? -12.172 79.442  94.840  1.00 26.17 ? 2513 HOH A O     1 
HETATM 18427 O O     . HOH CB 8 .    ? 13.985  86.515  121.295 1.00 41.59 ? 2514 HOH A O     1 
HETATM 18428 O O     . HOH CB 8 .    ? -63.785 70.545  71.099  1.00 34.91 ? 2515 HOH A O     1 
HETATM 18429 O O     . HOH CB 8 .    ? 2.612   84.075  102.092 1.00 26.30 ? 2516 HOH A O     1 
HETATM 18430 O O     . HOH CB 8 .    ? -57.189 53.082  96.735  1.00 27.52 ? 2517 HOH A O     1 
HETATM 18431 O O     . HOH CB 8 .    ? -53.929 55.273  68.714  1.00 23.92 ? 2518 HOH A O     1 
HETATM 18432 O O     . HOH CB 8 .    ? -10.172 69.333  133.746 1.00 35.37 ? 2519 HOH A O     1 
HETATM 18433 O O     . HOH CB 8 .    ? -47.018 77.016  92.403  1.00 26.54 ? 2520 HOH A O     1 
HETATM 18434 O O     . HOH CB 8 .    ? -6.640  85.469  87.061  1.00 41.66 ? 2521 HOH A O     1 
HETATM 18435 O O     . HOH CB 8 .    ? -22.833 53.865  92.524  1.00 34.37 ? 2522 HOH A O     1 
HETATM 18436 O O     . HOH CB 8 .    ? 1.210   70.530  87.704  1.00 40.17 ? 2523 HOH A O     1 
HETATM 18437 O O     . HOH CB 8 .    ? -28.574 72.738  99.090  1.00 44.28 ? 2524 HOH A O     1 
HETATM 18438 O O     . HOH CB 8 .    ? 22.832  76.064  115.515 1.00 33.88 ? 2525 HOH A O     1 
HETATM 18439 O O     . HOH CB 8 .    ? -41.845 83.202  82.716  1.00 46.40 ? 2526 HOH A O     1 
HETATM 18440 O O     . HOH CB 8 .    ? -45.688 54.654  92.547  1.00 20.55 ? 2527 HOH A O     1 
HETATM 18441 O O     . HOH CB 8 .    ? 2.413   76.008  117.423 1.00 29.99 ? 2528 HOH A O     1 
HETATM 18442 O O     . HOH CB 8 .    ? -50.263 72.265  101.580 1.00 27.60 ? 2529 HOH A O     1 
HETATM 18443 O O     . HOH CB 8 .    ? -48.108 54.770  58.700  1.00 38.26 ? 2530 HOH A O     1 
HETATM 18444 O O     . HOH CB 8 .    ? -20.172 79.133  115.473 1.00 22.30 ? 2531 HOH A O     1 
HETATM 18445 O O     . HOH CB 8 .    ? 18.147  57.097  105.718 1.00 34.89 ? 2532 HOH A O     1 
HETATM 18446 O O     . HOH CB 8 .    ? -39.911 61.343  94.948  1.00 21.16 ? 2533 HOH A O     1 
HETATM 18447 O O     . HOH CB 8 .    ? -44.241 31.204  84.376  1.00 39.88 ? 2534 HOH A O     1 
HETATM 18448 O O     . HOH CB 8 .    ? 6.792   61.016  103.720 1.00 23.09 ? 2535 HOH A O     1 
HETATM 18449 O O     . HOH CB 8 .    ? -24.178 67.640  105.612 1.00 24.23 ? 2536 HOH A O     1 
HETATM 18450 O O     . HOH CB 8 .    ? -14.674 55.497  51.010  1.00 45.09 ? 2537 HOH A O     1 
HETATM 18451 O O     . HOH CB 8 .    ? -25.098 79.468  95.361  1.00 20.34 ? 2538 HOH A O     1 
HETATM 18452 O O     . HOH CB 8 .    ? -37.488 75.453  98.244  1.00 29.24 ? 2539 HOH A O     1 
HETATM 18453 O O     . HOH CB 8 .    ? -25.575 66.854  87.581  1.00 33.81 ? 2540 HOH A O     1 
HETATM 18454 O O     . HOH CB 8 .    ? -7.233  50.892  53.108  1.00 37.32 ? 2541 HOH A O     1 
HETATM 18455 O O     . HOH CB 8 .    ? -20.476 54.734  94.343  1.00 40.66 ? 2542 HOH A O     1 
HETATM 18456 O O     . HOH CB 8 .    ? -11.319 92.491  125.077 1.00 35.48 ? 2543 HOH A O     1 
HETATM 18457 O O     . HOH CB 8 .    ? -42.370 56.506  89.871  1.00 20.46 ? 2544 HOH A O     1 
HETATM 18458 O O     . HOH CB 8 .    ? -4.191  73.287  77.130  1.00 36.59 ? 2545 HOH A O     1 
HETATM 18459 O O     . HOH CB 8 .    ? -1.773  77.950  105.568 1.00 32.27 ? 2546 HOH A O     1 
HETATM 18460 O O     . HOH CB 8 .    ? -53.969 72.252  68.767  1.00 30.90 ? 2547 HOH A O     1 
HETATM 18461 O O     . HOH CB 8 .    ? -2.604  73.912  99.881  1.00 36.03 ? 2548 HOH A O     1 
HETATM 18462 O O     . HOH CB 8 .    ? -45.707 89.585  109.664 1.00 40.30 ? 2549 HOH A O     1 
HETATM 18463 O O     . HOH CB 8 .    ? -46.390 72.620  64.700  1.00 22.86 ? 2550 HOH A O     1 
HETATM 18464 O O     . HOH CB 8 .    ? -36.493 37.680  102.404 1.00 43.73 ? 2551 HOH A O     1 
HETATM 18465 O O     . HOH CB 8 .    ? 2.484   64.787  113.440 1.00 29.46 ? 2552 HOH A O     1 
HETATM 18466 O O     . HOH CB 8 .    ? -34.849 66.606  102.115 1.00 25.97 ? 2553 HOH A O     1 
HETATM 18467 O O     . HOH CB 8 .    ? -45.642 62.560  93.142  1.00 20.57 ? 2554 HOH A O     1 
HETATM 18468 O O     . HOH CB 8 .    ? -8.639  82.393  105.120 1.00 34.51 ? 2555 HOH A O     1 
HETATM 18469 O O     . HOH CB 8 .    ? -35.340 94.953  96.590  1.00 25.87 ? 2556 HOH A O     1 
HETATM 18470 O O     . HOH CB 8 .    ? -41.722 64.814  58.996  1.00 29.78 ? 2557 HOH A O     1 
HETATM 18471 O O     . HOH CB 8 .    ? -65.883 71.400  80.913  1.00 33.98 ? 2558 HOH A O     1 
HETATM 18472 O O     . HOH CB 8 .    ? -66.604 61.158  76.292  1.00 26.04 ? 2559 HOH A O     1 
HETATM 18473 O O     . HOH CB 8 .    ? -55.225 47.331  70.005  1.00 28.45 ? 2560 HOH A O     1 
HETATM 18474 O O     . HOH CB 8 .    ? -40.040 88.649  119.795 1.00 33.28 ? 2561 HOH A O     1 
HETATM 18475 O O     . HOH CB 8 .    ? -24.093 59.540  122.243 1.00 33.72 ? 2562 HOH A O     1 
HETATM 18476 O O     . HOH CB 8 .    ? -22.985 83.572  91.900  1.00 21.46 ? 2563 HOH A O     1 
HETATM 18477 O O     . HOH CB 8 .    ? -27.352 62.271  89.282  1.00 24.34 ? 2564 HOH A O     1 
HETATM 18478 O O     . HOH CB 8 .    ? -41.753 70.657  95.825  1.00 31.35 ? 2565 HOH A O     1 
HETATM 18479 O O     . HOH CB 8 .    ? 1.221   66.194  96.850  1.00 25.87 ? 2566 HOH A O     1 
HETATM 18480 O O     . HOH CB 8 .    ? -50.811 66.113  106.868 1.00 34.24 ? 2567 HOH A O     1 
HETATM 18481 O O     . HOH CB 8 .    ? -36.123 35.328  85.353  1.00 50.59 ? 2568 HOH A O     1 
HETATM 18482 O O     . HOH CB 8 .    ? -52.049 73.156  106.047 1.00 29.95 ? 2569 HOH A O     1 
HETATM 18483 O O     . HOH CB 8 .    ? -48.977 47.374  97.850  1.00 26.60 ? 2570 HOH A O     1 
HETATM 18484 O O     . HOH CB 8 .    ? -19.956 52.707  78.512  1.00 36.58 ? 2571 HOH A O     1 
HETATM 18485 O O     . HOH CB 8 .    ? -50.918 51.828  64.270  1.00 27.21 ? 2572 HOH A O     1 
HETATM 18486 O O     . HOH CB 8 .    ? -43.519 77.310  68.084  1.00 30.54 ? 2573 HOH A O     1 
HETATM 18487 O O     . HOH CB 8 .    ? -45.273 72.619  115.300 1.00 46.80 ? 2574 HOH A O     1 
HETATM 18488 O O     . HOH CB 8 .    ? -31.292 84.092  123.867 1.00 26.96 ? 2575 HOH A O     1 
HETATM 18489 O O     . HOH CB 8 .    ? -27.676 71.048  90.358  1.00 29.33 ? 2576 HOH A O     1 
HETATM 18490 O O     . HOH CB 8 .    ? 18.824  73.134  118.719 1.00 34.11 ? 2577 HOH A O     1 
HETATM 18491 O O     . HOH CB 8 .    ? -36.941 45.187  104.543 1.00 35.61 ? 2578 HOH A O     1 
HETATM 18492 O O     . HOH CB 8 .    ? -10.806 66.763  127.985 1.00 36.31 ? 2579 HOH A O     1 
HETATM 18493 O O     . HOH CB 8 .    ? -34.417 90.549  122.856 1.00 33.48 ? 2580 HOH A O     1 
HETATM 18494 O O     . HOH CB 8 .    ? -26.200 94.322  78.460  1.00 37.00 ? 2581 HOH A O     1 
HETATM 18495 O O     . HOH CB 8 .    ? -44.023 90.475  100.515 1.00 39.15 ? 2582 HOH A O     1 
HETATM 18496 O O     . HOH CB 8 .    ? 13.562  78.609  124.550 1.00 41.82 ? 2583 HOH A O     1 
HETATM 18497 O O     . HOH CB 8 .    ? 23.771  58.365  104.040 1.00 38.40 ? 2584 HOH A O     1 
HETATM 18498 O O     . HOH CB 8 .    ? -25.949 88.805  116.742 1.00 27.90 ? 2585 HOH A O     1 
HETATM 18499 O O     . HOH CB 8 .    ? -26.933 63.208  86.823  1.00 28.93 ? 2586 HOH A O     1 
HETATM 18500 O O     . HOH CB 8 .    ? 10.130  67.707  94.356  1.00 31.76 ? 2587 HOH A O     1 
HETATM 18501 O O     . HOH CB 8 .    ? -32.398 75.164  127.160 1.00 32.80 ? 2588 HOH A O     1 
HETATM 18502 O O     . HOH CB 8 .    ? 0.345   64.199  107.626 1.00 24.53 ? 2589 HOH A O     1 
HETATM 18503 O O     . HOH CB 8 .    ? -20.927 58.073  97.413  1.00 25.13 ? 2590 HOH A O     1 
HETATM 18504 O O     . HOH CB 8 .    ? -45.014 60.821  86.026  1.00 21.02 ? 2591 HOH A O     1 
HETATM 18505 O O     . HOH CB 8 .    ? -7.941  75.469  70.405  1.00 37.26 ? 2592 HOH A O     1 
HETATM 18506 O O     . HOH CB 8 .    ? 12.892  88.717  116.746 1.00 34.76 ? 2593 HOH A O     1 
HETATM 18507 O O     . HOH CB 8 .    ? 2.793   77.969  98.470  1.00 29.17 ? 2594 HOH A O     1 
HETATM 18508 O O     . HOH CB 8 .    ? -28.988 83.809  104.778 1.00 30.84 ? 2595 HOH A O     1 
HETATM 18509 O O     . HOH CB 8 .    ? -44.048 59.237  87.947  1.00 17.93 ? 2596 HOH A O     1 
HETATM 18510 O O     . HOH CB 8 .    ? -24.823 69.305  74.749  1.00 34.73 ? 2597 HOH A O     1 
HETATM 18511 O O     . HOH CB 8 .    ? -29.236 95.116  89.538  1.00 32.87 ? 2598 HOH A O     1 
HETATM 18512 O O     . HOH CB 8 .    ? -11.161 53.912  100.513 1.00 27.98 ? 2599 HOH A O     1 
HETATM 18513 O O     . HOH CB 8 .    ? -54.331 44.207  92.389  1.00 41.09 ? 2600 HOH A O     1 
HETATM 18514 O O     . HOH CB 8 .    ? -34.428 56.291  105.659 1.00 25.02 ? 2601 HOH A O     1 
HETATM 18515 O O     . HOH CB 8 .    ? -31.528 58.202  116.100 1.00 44.16 ? 2602 HOH A O     1 
HETATM 18516 O O     . HOH CB 8 .    ? -6.370  93.937  113.593 1.00 36.57 ? 2603 HOH A O     1 
HETATM 18517 O O     . HOH CB 8 .    ? -0.016  85.104  112.234 1.00 33.97 ? 2604 HOH A O     1 
HETATM 18518 O O     . HOH CB 8 .    ? -46.198 30.336  86.007  1.00 39.32 ? 2605 HOH A O     1 
HETATM 18519 O O     . HOH CB 8 .    ? -38.248 65.488  88.597  1.00 34.12 ? 2606 HOH A O     1 
HETATM 18520 O O     . HOH CB 8 .    ? 1.133   57.347  108.067 1.00 22.45 ? 2607 HOH A O     1 
HETATM 18521 O O     . HOH CB 8 .    ? -60.410 46.794  89.042  1.00 35.87 ? 2608 HOH A O     1 
HETATM 18522 O O     . HOH CB 8 .    ? -0.115  67.226  86.409  1.00 37.86 ? 2609 HOH A O     1 
HETATM 18523 O O     . HOH CB 8 .    ? -54.666 26.333  92.707  1.00 44.52 ? 2610 HOH A O     1 
HETATM 18524 O O     . HOH CB 8 .    ? -36.995 60.448  96.748  1.00 23.38 ? 2611 HOH A O     1 
HETATM 18525 O O     . HOH CB 8 .    ? -38.707 70.448  82.309  1.00 30.05 ? 2612 HOH A O     1 
HETATM 18526 O O     . HOH CB 8 .    ? -10.666 64.992  125.809 1.00 39.94 ? 2613 HOH A O     1 
HETATM 18527 O O     . HOH CB 8 .    ? -22.577 77.051  70.427  1.00 29.71 ? 2614 HOH A O     1 
HETATM 18528 O O     . HOH CB 8 .    ? -3.976  73.284  117.220 1.00 29.00 ? 2615 HOH A O     1 
HETATM 18529 O O     . HOH CB 8 .    ? -45.001 92.948  89.546  1.00 44.88 ? 2616 HOH A O     1 
HETATM 18530 O O     . HOH CB 8 .    ? 21.688  73.030  116.453 1.00 30.67 ? 2617 HOH A O     1 
HETATM 18531 O O     . HOH CB 8 .    ? -1.463  79.315  100.170 1.00 32.64 ? 2618 HOH A O     1 
HETATM 18532 O O     . HOH CB 8 .    ? -34.948 40.417  92.177  1.00 30.29 ? 2619 HOH A O     1 
HETATM 18533 O O     . HOH CB 8 .    ? -33.969 83.721  123.995 1.00 33.09 ? 2620 HOH A O     1 
HETATM 18534 O O     . HOH CB 8 .    ? -59.399 58.120  77.307  1.00 24.43 ? 2621 HOH A O     1 
HETATM 18535 O O     . HOH CB 8 .    ? -37.131 51.475  61.134  1.00 36.80 ? 2622 HOH A O     1 
HETATM 18536 O O     . HOH CB 8 .    ? -50.386 56.278  72.061  1.00 29.41 ? 2623 HOH A O     1 
HETATM 18537 O O     . HOH CB 8 .    ? -17.159 96.153  90.928  1.00 41.60 ? 2624 HOH A O     1 
HETATM 18538 O O     . HOH CB 8 .    ? 16.397  65.213  120.135 1.00 33.14 ? 2625 HOH A O     1 
HETATM 18539 O O     . HOH CB 8 .    ? -32.747 92.235  110.855 1.00 35.75 ? 2626 HOH A O     1 
HETATM 18540 O O     . HOH CB 8 .    ? -41.059 70.467  93.412  1.00 27.83 ? 2627 HOH A O     1 
HETATM 18541 O O     . HOH CB 8 .    ? -66.204 71.964  72.457  1.00 41.44 ? 2628 HOH A O     1 
HETATM 18542 O O     . HOH CB 8 .    ? -18.893 59.574  108.656 1.00 35.85 ? 2629 HOH A O     1 
HETATM 18543 O O     . HOH CB 8 .    ? -39.681 61.022  103.842 1.00 31.39 ? 2630 HOH A O     1 
HETATM 18544 O O     . HOH CB 8 .    ? -26.583 84.353  74.299  1.00 37.25 ? 2631 HOH A O     1 
HETATM 18545 O O     . HOH CB 8 .    ? 10.822  66.892  112.443 1.00 36.00 ? 2632 HOH A O     1 
HETATM 18546 O O     . HOH CB 8 .    ? -32.149 52.973  86.037  1.00 34.00 ? 2633 HOH A O     1 
HETATM 18547 O O     . HOH CB 8 .    ? -15.571 43.934  77.099  1.00 42.86 ? 2634 HOH A O     1 
HETATM 18548 O O     . HOH CB 8 .    ? -11.521 43.759  74.484  1.00 38.20 ? 2635 HOH A O     1 
HETATM 18549 O O     . HOH CB 8 .    ? -36.350 80.687  76.171  1.00 24.84 ? 2636 HOH A O     1 
HETATM 18550 O O     . HOH CB 8 .    ? -2.204  77.292  121.300 1.00 34.45 ? 2637 HOH A O     1 
HETATM 18551 O O     . HOH CB 8 .    ? -25.480 89.134  133.758 1.00 48.74 ? 2638 HOH A O     1 
HETATM 18552 O O     . HOH CB 8 .    ? 11.100  85.079  125.278 1.00 36.00 ? 2639 HOH A O     1 
HETATM 18553 O O     . HOH CB 8 .    ? 20.032  64.487  93.713  1.00 39.89 ? 2640 HOH A O     1 
HETATM 18554 O O     . HOH CB 8 .    ? -9.062  51.748  108.053 1.00 34.46 ? 2641 HOH A O     1 
HETATM 18555 O O     . HOH CB 8 .    ? -10.307 63.825  116.004 1.00 24.17 ? 2642 HOH A O     1 
HETATM 18556 O O     . HOH CB 8 .    ? -23.244 76.222  133.985 1.00 33.78 ? 2643 HOH A O     1 
HETATM 18557 O O     . HOH CB 8 .    ? -39.608 86.232  89.560  1.00 30.28 ? 2644 HOH A O     1 
HETATM 18558 O O     . HOH CB 8 .    ? -2.326  51.682  101.168 1.00 34.07 ? 2645 HOH A O     1 
HETATM 18559 O O     . HOH CB 8 .    ? -61.799 35.811  79.217  1.00 45.32 ? 2646 HOH A O     1 
HETATM 18560 O O     . HOH CB 8 .    ? -23.562 95.011  119.281 1.00 40.64 ? 2647 HOH A O     1 
HETATM 18561 O O     . HOH CB 8 .    ? -2.773  76.335  77.394  1.00 30.34 ? 2648 HOH A O     1 
HETATM 18562 O O     . HOH CB 8 .    ? -39.620 75.703  122.570 1.00 49.82 ? 2649 HOH A O     1 
HETATM 18563 O O     . HOH CB 8 .    ? -45.456 57.160  102.659 1.00 31.16 ? 2650 HOH A O     1 
HETATM 18564 O O     . HOH CB 8 .    ? -13.124 93.614  131.682 1.00 52.80 ? 2651 HOH A O     1 
HETATM 18565 O O     . HOH CB 8 .    ? -59.719 62.690  77.827  1.00 22.82 ? 2652 HOH A O     1 
HETATM 18566 O O     . HOH CB 8 .    ? -1.742  80.298  112.524 1.00 34.21 ? 2653 HOH A O     1 
HETATM 18567 O O     . HOH CB 8 .    ? -37.728 86.194  102.440 1.00 28.40 ? 2654 HOH A O     1 
HETATM 18568 O O     . HOH CB 8 .    ? -13.638 54.239  77.478  1.00 33.90 ? 2655 HOH A O     1 
HETATM 18569 O O     . HOH CB 8 .    ? -18.011 85.928  77.588  1.00 33.50 ? 2656 HOH A O     1 
HETATM 18570 O O     . HOH CB 8 .    ? 0.067   64.990  117.967 1.00 38.65 ? 2657 HOH A O     1 
HETATM 18571 O O     . HOH CB 8 .    ? -48.638 61.971  57.141  1.00 37.04 ? 2658 HOH A O     1 
HETATM 18572 O O     . HOH CB 8 .    ? -25.964 69.872  95.998  1.00 32.50 ? 2659 HOH A O     1 
HETATM 18573 O O     . HOH CB 8 .    ? -62.141 59.423  96.457  1.00 30.09 ? 2660 HOH A O     1 
HETATM 18574 O O     . HOH CB 8 .    ? -0.288  67.905  118.095 1.00 31.75 ? 2661 HOH A O     1 
HETATM 18575 O O     . HOH CB 8 .    ? -25.275 59.386  114.903 1.00 26.67 ? 2662 HOH A O     1 
HETATM 18576 O O     . HOH CB 8 .    ? -16.001 56.292  84.201  1.00 44.53 ? 2663 HOH A O     1 
HETATM 18577 O O     . HOH CB 8 .    ? -20.267 89.278  75.351  1.00 32.72 ? 2664 HOH A O     1 
HETATM 18578 O O     . HOH CB 8 .    ? -45.686 24.001  83.110  1.00 46.39 ? 2665 HOH A O     1 
HETATM 18579 O O     . HOH CB 8 .    ? 17.370  80.766  97.064  1.00 35.81 ? 2666 HOH A O     1 
HETATM 18580 O O     . HOH CB 8 .    ? 14.797  82.494  120.176 1.00 35.08 ? 2667 HOH A O     1 
HETATM 18581 O O     . HOH CB 8 .    ? -39.265 46.824  104.216 1.00 34.80 ? 2668 HOH A O     1 
HETATM 18582 O O     . HOH CB 8 .    ? -65.043 54.796  81.247  1.00 33.19 ? 2669 HOH A O     1 
HETATM 18583 O O     . HOH CB 8 .    ? 10.494  81.702  126.116 1.00 36.82 ? 2670 HOH A O     1 
HETATM 18584 O O     . HOH CB 8 .    ? -36.634 49.589  100.906 1.00 34.83 ? 2671 HOH A O     1 
HETATM 18585 O O     . HOH CB 8 .    ? -34.845 64.794  66.653  1.00 46.91 ? 2672 HOH A O     1 
HETATM 18586 O O     . HOH CB 8 .    ? -35.836 76.749  66.378  1.00 48.06 ? 2673 HOH A O     1 
HETATM 18587 O O     . HOH CB 8 .    ? -43.069 56.117  92.422  1.00 19.38 ? 2674 HOH A O     1 
HETATM 18588 O O     . HOH CB 8 .    ? -21.694 54.716  96.696  1.00 38.08 ? 2675 HOH A O     1 
HETATM 18589 O O     . HOH CB 8 .    ? -6.164  71.181  106.287 1.00 37.24 ? 2676 HOH A O     1 
HETATM 18590 O O     . HOH CB 8 .    ? 4.540   86.051  101.123 1.00 35.95 ? 2677 HOH A O     1 
HETATM 18591 O O     . HOH CB 8 .    ? -26.113 74.707  133.136 1.00 40.59 ? 2678 HOH A O     1 
HETATM 18592 O O     . HOH CB 8 .    ? -50.025 72.826  63.248  1.00 25.75 ? 2679 HOH A O     1 
HETATM 18593 O O     . HOH CB 8 .    ? 25.299  58.399  110.279 1.00 41.98 ? 2680 HOH A O     1 
HETATM 18594 O O     . HOH CB 8 .    ? -25.846 50.498  105.529 1.00 41.69 ? 2681 HOH A O     1 
HETATM 18595 O O     . HOH CB 8 .    ? 7.099   55.211  99.140  1.00 27.26 ? 2682 HOH A O     1 
HETATM 18596 O O     . HOH CB 8 .    ? 2.484   74.544  109.597 1.00 27.88 ? 2683 HOH A O     1 
HETATM 18597 O O     . HOH CB 8 .    ? -60.257 49.721  91.013  1.00 35.74 ? 2684 HOH A O     1 
HETATM 18598 O O     . HOH CB 8 .    ? -0.323  58.214  110.568 1.00 33.74 ? 2685 HOH A O     1 
HETATM 18599 O O     . HOH CB 8 .    ? -14.380 58.084  110.618 1.00 38.95 ? 2686 HOH A O     1 
HETATM 18600 O O     . HOH CB 8 .    ? -32.281 94.483  128.037 1.00 38.02 ? 2687 HOH A O     1 
HETATM 18601 O O     . HOH CB 8 .    ? 10.822  61.355  115.751 1.00 38.79 ? 2688 HOH A O     1 
HETATM 18602 O O     . HOH CB 8 .    ? -14.048 41.880  71.322  1.00 39.29 ? 2689 HOH A O     1 
HETATM 18603 O O     . HOH CB 8 .    ? -42.184 88.405  94.351  1.00 36.60 ? 2690 HOH A O     1 
HETATM 18604 O O     . HOH CB 8 .    ? -65.199 44.422  83.266  1.00 42.49 ? 2691 HOH A O     1 
HETATM 18605 O O     . HOH CB 8 .    ? -49.755 54.032  74.345  1.00 25.86 ? 2692 HOH A O     1 
HETATM 18606 O O     . HOH CB 8 .    ? -64.583 62.768  68.937  1.00 36.47 ? 2693 HOH A O     1 
HETATM 18607 O O     . HOH CB 8 .    ? -34.646 76.462  96.253  1.00 40.91 ? 2694 HOH A O     1 
HETATM 18608 O O     . HOH CB 8 .    ? -9.153  84.475  81.053  1.00 48.17 ? 2695 HOH A O     1 
HETATM 18609 O O     . HOH CB 8 .    ? -37.371 63.348  93.797  1.00 36.73 ? 2696 HOH A O     1 
HETATM 18610 O O     . HOH CB 8 .    ? -42.686 37.198  105.757 1.00 37.18 ? 2697 HOH A O     1 
HETATM 18611 O O     . HOH CB 8 .    ? -11.929 64.140  130.262 1.00 42.15 ? 2698 HOH A O     1 
HETATM 18612 O O     . HOH CB 8 .    ? -32.204 56.061  86.211  1.00 28.29 ? 2699 HOH A O     1 
HETATM 18613 O O     . HOH CB 8 .    ? -66.524 63.879  88.967  1.00 39.09 ? 2700 HOH A O     1 
HETATM 18614 O O     . HOH CB 8 .    ? -1.119  70.131  116.825 1.00 28.19 ? 2701 HOH A O     1 
HETATM 18615 O O     . HOH CB 8 .    ? -27.817 56.624  90.558  1.00 32.78 ? 2702 HOH A O     1 
HETATM 18616 O O     . HOH CB 8 .    ? -16.627 53.657  76.099  1.00 36.37 ? 2703 HOH A O     1 
HETATM 18617 O O     . HOH CB 8 .    ? -44.204 85.508  95.474  1.00 42.90 ? 2704 HOH A O     1 
HETATM 18618 O O     . HOH CB 8 .    ? -30.363 92.012  78.750  1.00 40.43 ? 2705 HOH A O     1 
HETATM 18619 O O     . HOH CB 8 .    ? 14.887  76.727  94.423  1.00 43.45 ? 2706 HOH A O     1 
HETATM 18620 O O     . HOH CB 8 .    ? -42.871 77.858  78.850  1.00 25.49 ? 2707 HOH A O     1 
HETATM 18621 O O     . HOH CB 8 .    ? -40.606 65.145  62.379  1.00 36.49 ? 2708 HOH A O     1 
HETATM 18622 O O     . HOH CB 8 .    ? -38.059 65.885  110.738 1.00 33.15 ? 2709 HOH A O     1 
HETATM 18623 O O     . HOH CB 8 .    ? -41.696 80.068  73.996  1.00 46.21 ? 2710 HOH A O     1 
HETATM 18624 O O     . HOH CB 8 .    ? -10.810 77.459  137.324 1.00 47.98 ? 2711 HOH A O     1 
HETATM 18625 O O     . HOH CB 8 .    ? -11.492 59.903  85.268  1.00 37.06 ? 2712 HOH A O     1 
HETATM 18626 O O     . HOH CB 8 .    ? -47.290 32.812  86.027  1.00 38.96 ? 2713 HOH A O     1 
HETATM 18627 O O     . HOH CB 8 .    ? -46.115 78.267  90.503  1.00 26.89 ? 2714 HOH A O     1 
HETATM 18628 O O     . HOH CB 8 .    ? -42.449 28.087  86.866  1.00 44.54 ? 2715 HOH A O     1 
HETATM 18629 O O     . HOH CB 8 .    ? -26.356 70.493  132.027 1.00 40.80 ? 2716 HOH A O     1 
HETATM 18630 O O     . HOH CB 8 .    ? -60.381 63.831  92.833  1.00 33.98 ? 2717 HOH A O     1 
HETATM 18631 O O     . HOH CB 8 .    ? -8.761  78.056  132.028 1.00 41.11 ? 2718 HOH A O     1 
HETATM 18632 O O     . HOH CB 8 .    ? -57.536 72.902  96.897  1.00 40.21 ? 2719 HOH A O     1 
HETATM 18633 O O     . HOH CB 8 .    ? 25.971  64.375  103.064 1.00 37.66 ? 2720 HOH A O     1 
HETATM 18634 O O     . HOH CB 8 .    ? -17.543 54.702  117.787 1.00 38.48 ? 2721 HOH A O     1 
HETATM 18635 O O     . HOH CB 8 .    ? -41.957 75.784  121.231 1.00 47.43 ? 2722 HOH A O     1 
HETATM 18636 O O     . HOH CB 8 .    ? -35.969 37.358  83.637  1.00 45.86 ? 2723 HOH A O     1 
HETATM 18637 O O     . HOH CB 8 .    ? -40.074 37.665  85.722  1.00 39.44 ? 2724 HOH A O     1 
HETATM 18638 O O     . HOH CB 8 .    ? -21.747 90.728  112.461 1.00 37.05 ? 2725 HOH A O     1 
HETATM 18639 O O     . HOH CB 8 .    ? -2.093  83.595  115.894 1.00 38.20 ? 2726 HOH A O     1 
HETATM 18640 O O     . HOH CB 8 .    ? -28.259 82.752  102.199 1.00 26.13 ? 2727 HOH A O     1 
HETATM 18641 O O     . HOH CB 8 .    ? -17.600 88.705  107.899 1.00 38.31 ? 2728 HOH A O     1 
HETATM 18642 O O     . HOH CB 8 .    ? 5.244   55.215  97.339  1.00 33.77 ? 2729 HOH A O     1 
HETATM 18643 O O     . HOH CB 8 .    ? -34.423 59.041  106.834 1.00 29.77 ? 2730 HOH A O     1 
HETATM 18644 O O     . HOH CB 8 .    ? -10.712 63.471  68.905  1.00 38.38 ? 2731 HOH A O     1 
HETATM 18645 O O     . HOH CB 8 .    ? -30.399 40.418  96.093  1.00 50.21 ? 2732 HOH A O     1 
HETATM 18646 O O     . HOH CB 8 .    ? -32.461 75.330  85.878  1.00 37.15 ? 2733 HOH A O     1 
HETATM 18647 O O     . HOH CB 8 .    ? -58.888 74.104  94.855  1.00 48.39 ? 2734 HOH A O     1 
HETATM 18648 O O     . HOH CB 8 .    ? 7.603   89.618  123.111 1.00 37.96 ? 2735 HOH A O     1 
HETATM 18649 O O     . HOH CB 8 .    ? -9.397  60.334  84.667  1.00 32.39 ? 2736 HOH A O     1 
HETATM 18650 O O     . HOH CB 8 .    ? -69.347 52.351  86.161  1.00 47.27 ? 2737 HOH A O     1 
HETATM 18651 O O     . HOH CB 8 .    ? -20.416 54.913  98.596  1.00 35.26 ? 2738 HOH A O     1 
HETATM 18652 O O     . HOH CB 8 .    ? -31.616 74.238  87.733  1.00 38.59 ? 2739 HOH A O     1 
HETATM 18653 O O     . HOH CB 8 .    ? -19.446 54.556  118.961 1.00 38.85 ? 2740 HOH A O     1 
HETATM 18654 O O     . HOH CB 8 .    ? 0.426   68.620  88.431  1.00 39.87 ? 2741 HOH A O     1 
HETATM 18655 O O     . HOH CB 8 .    ? -37.973 64.312  109.173 1.00 40.94 ? 2742 HOH A O     1 
HETATM 18656 O O     . HOH CB 8 .    ? -12.548 69.769  71.874  1.00 36.95 ? 2743 HOH A O     1 
HETATM 18657 O O     . HOH CB 8 .    ? -26.927 66.574  98.630  1.00 31.78 ? 2744 HOH A O     1 
HETATM 18658 O O     . HOH CB 8 .    ? -21.156 49.903  108.776 1.00 40.20 ? 2745 HOH A O     1 
HETATM 18659 O O     . HOH CB 8 .    ? -12.341 82.608  73.064  1.00 44.05 ? 2746 HOH A O     1 
HETATM 18660 O O     . HOH CB 8 .    ? -52.096 54.950  70.786  1.00 30.91 ? 2747 HOH A O     1 
HETATM 18661 O O     . HOH CB 8 .    ? 27.690  59.124  110.146 1.00 44.67 ? 2748 HOH A O     1 
HETATM 18662 O O     . HOH CB 8 .    ? -53.215 66.163  102.401 1.00 42.88 ? 2749 HOH A O     1 
HETATM 18663 O O     . HOH CB 8 .    ? -53.463 66.811  105.077 1.00 42.78 ? 2750 HOH A O     1 
HETATM 18664 O O     . HOH CB 8 .    ? -22.812 74.262  70.051  1.00 37.67 ? 2751 HOH A O     1 
HETATM 18665 O O     . HOH CB 8 .    ? -9.122  76.743  68.600  1.00 54.18 ? 2752 HOH A O     1 
HETATM 18666 O O     . HOH CB 8 .    ? -64.914 57.937  99.582  1.00 39.18 ? 2753 HOH A O     1 
HETATM 18667 O O     . HOH CB 8 .    ? -16.356 42.672  72.017  1.00 44.92 ? 2754 HOH A O     1 
HETATM 18668 O O     . HOH CB 8 .    ? -66.161 54.369  78.449  1.00 37.44 ? 2755 HOH A O     1 
HETATM 18669 O O     . HOH CB 8 .    ? -60.083 51.627  96.704  1.00 48.18 ? 2756 HOH A O     1 
HETATM 18670 O O     . HOH CB 8 .    ? -52.441 44.972  95.470  1.00 42.00 ? 2757 HOH A O     1 
HETATM 18671 O O     . HOH CB 8 .    ? -29.410 70.576  93.903  1.00 39.06 ? 2758 HOH A O     1 
HETATM 18672 O O     . HOH CB 8 .    ? -63.067 60.304  94.200  1.00 35.60 ? 2759 HOH A O     1 
HETATM 18673 O O     . HOH CB 8 .    ? -40.303 83.901  81.247  1.00 43.59 ? 2760 HOH A O     1 
HETATM 18674 O O     . HOH CB 8 .    ? -28.679 57.616  88.898  1.00 33.57 ? 2761 HOH A O     1 
HETATM 18675 O O     . HOH CB 8 .    ? -54.586 76.694  94.783  1.00 41.12 ? 2762 HOH A O     1 
HETATM 18676 O O     . HOH CB 8 .    ? -27.750 64.002  91.133  1.00 37.68 ? 2763 HOH A O     1 
HETATM 18677 O O     . HOH CB 8 .    ? -44.890 77.050  70.558  1.00 39.09 ? 2764 HOH A O     1 
HETATM 18678 O O     . HOH CB 8 .    ? -22.251 92.099  99.473  1.00 37.43 ? 2765 HOH A O     1 
HETATM 18679 O O     . HOH CB 8 .    ? -36.575 90.626  124.422 1.00 40.82 ? 2766 HOH A O     1 
HETATM 18680 O O     . HOH CB 8 .    ? -29.779 60.172  127.008 1.00 46.35 ? 2767 HOH A O     1 
HETATM 18681 O O     . HOH CB 8 .    ? -56.796 44.096  92.651  1.00 40.82 ? 2768 HOH A O     1 
HETATM 18682 O O     . HOH CB 8 .    ? -21.168 87.295  108.475 1.00 38.95 ? 2769 HOH A O     1 
HETATM 18683 O O     . HOH CB 8 .    ? -37.440 63.403  114.776 1.00 33.34 ? 2770 HOH A O     1 
HETATM 18684 O O     . HOH CB 8 .    ? -26.326 67.670  94.660  1.00 35.99 ? 2771 HOH A O     1 
HETATM 18685 O O     . HOH CB 8 .    ? -30.156 62.939  92.254  1.00 39.66 ? 2772 HOH A O     1 
HETATM 18686 O O     . HOH CB 8 .    ? -12.486 68.890  74.206  1.00 39.79 ? 2773 HOH A O     1 
HETATM 18687 O O     . HOH CB 8 .    ? -22.952 71.332  74.299  1.00 36.80 ? 2774 HOH A O     1 
HETATM 18688 O O     . HOH CB 8 .    ? -33.649 84.398  77.273  1.00 32.94 ? 2775 HOH A O     1 
HETATM 18689 O O     . HOH CB 8 .    ? -28.221 67.716  93.448  1.00 44.80 ? 2776 HOH A O     1 
HETATM 18690 O O     . HOH CB 8 .    ? -47.063 80.481  75.365  1.00 46.83 ? 2777 HOH A O     1 
HETATM 18691 O O     . HOH CB 8 .    ? -57.059 69.090  63.573  1.00 35.24 ? 2778 HOH A O     1 
HETATM 18692 O O     . HOH CB 8 .    ? -30.571 82.225  101.115 1.00 28.29 ? 2779 HOH A O     1 
HETATM 18693 O O     . HOH CB 8 .    ? -27.290 51.226  109.954 1.00 37.55 ? 2780 HOH A O     1 
HETATM 18694 O O     . HOH CB 8 .    ? -17.686 42.423  74.035  1.00 48.03 ? 2781 HOH A O     1 
HETATM 18695 O O     . HOH CB 8 .    ? -36.399 63.305  90.817  1.00 39.62 ? 2782 HOH A O     1 
HETATM 18696 O O     . HOH CB 8 .    ? -1.938  76.090  125.919 1.00 36.01 ? 2783 HOH A O     1 
HETATM 18697 O O     . HOH CB 8 .    ? -24.679 65.840  97.348  1.00 32.79 ? 2784 HOH A O     1 
HETATM 18698 O O     . HOH CB 8 .    ? -10.684 78.978  92.626  1.00 29.78 ? 2785 HOH A O     1 
HETATM 18699 O O     . HOH CB 8 .    ? -17.066 57.732  110.724 1.00 43.94 ? 2786 HOH A O     1 
HETATM 18700 O O     . HOH CB 8 .    ? -11.025 64.002  128.263 1.00 40.98 ? 2787 HOH A O     1 
HETATM 18701 O O     . HOH CB 8 .    ? -33.757 80.841  74.800  1.00 28.44 ? 2788 HOH A O     1 
HETATM 18702 O O     . HOH CB 8 .    ? -45.126 28.480  87.536  1.00 41.83 ? 2789 HOH A O     1 
HETATM 18703 O O     . HOH CB 8 .    ? -52.836 48.191  58.152  1.00 47.62 ? 2790 HOH A O     1 
HETATM 18704 O O     . HOH CB 8 .    ? -38.571 71.657  92.540  1.00 40.07 ? 2791 HOH A O     1 
HETATM 18705 O O     . HOH CB 8 .    ? -52.685 74.031  62.451  1.00 24.06 ? 2792 HOH A O     1 
HETATM 18706 O O     . HOH CB 8 .    ? -27.083 60.093  123.314 1.00 35.98 ? 2793 HOH A O     1 
HETATM 18707 O O     . HOH CB 8 .    ? -9.987  66.529  74.205  1.00 40.98 ? 2794 HOH A O     1 
HETATM 18708 O O     . HOH CB 8 .    ? -67.816 62.420  68.900  1.00 43.80 ? 2795 HOH A O     1 
HETATM 18709 O O     . HOH CB 8 .    ? -69.494 69.158  71.619  1.00 39.02 ? 2796 HOH A O     1 
HETATM 18710 O O     . HOH CB 8 .    ? 16.757  86.601  115.265 1.00 50.46 ? 2797 HOH A O     1 
HETATM 18711 O O     . HOH CB 8 .    ? -17.930 98.003  92.235  1.00 41.84 ? 2798 HOH A O     1 
HETATM 18712 O O     . HOH CB 8 .    ? -27.248 59.445  116.873 1.00 30.88 ? 2799 HOH A O     1 
HETATM 18713 O O     . HOH CB 8 .    ? -25.284 97.106  122.504 1.00 41.04 ? 2800 HOH A O     1 
HETATM 18714 O O     . HOH CB 8 .    ? -34.149 81.018  123.280 1.00 34.98 ? 2801 HOH A O     1 
HETATM 18715 O O     . HOH CB 8 .    ? -31.286 74.803  129.297 1.00 44.14 ? 2802 HOH A O     1 
HETATM 18716 O O     . HOH CB 8 .    ? -14.852 52.063  112.840 1.00 42.27 ? 2803 HOH A O     1 
HETATM 18717 O O     . HOH CB 8 .    ? -36.860 63.222  119.241 1.00 43.54 ? 2804 HOH A O     1 
HETATM 18718 O O     . HOH CB 8 .    ? -10.668 66.919  72.036  1.00 46.77 ? 2805 HOH A O     1 
HETATM 18719 O O     . HOH CB 8 .    ? -24.082 77.774  68.536  1.00 36.35 ? 2806 HOH A O     1 
HETATM 18720 O O     . HOH CB 8 .    ? 23.342  61.528  100.190 1.00 40.38 ? 2807 HOH A O     1 
HETATM 18721 O O     . HOH CB 8 .    ? -25.393 65.380  92.219  1.00 36.58 ? 2808 HOH A O     1 
HETATM 18722 O O     . HOH CB 8 .    ? -25.950 63.073  102.245 1.00 33.36 ? 2809 HOH A O     1 
HETATM 18723 O O     . HOH CB 8 .    ? -8.596  74.816  129.583 1.00 39.10 ? 2810 HOH A O     1 
HETATM 18724 O O     . HOH CB 8 .    ? -41.848 61.295  103.196 1.00 31.32 ? 2811 HOH A O     1 
HETATM 18725 O O     . HOH CB 8 .    ? 20.566  61.662  97.124  1.00 39.11 ? 2812 HOH A O     1 
HETATM 18726 O O     . HOH CB 8 .    ? -29.544 57.373  86.202  1.00 43.97 ? 2813 HOH A O     1 
HETATM 18727 O O     . HOH CB 8 .    ? 12.788  88.831  118.983 1.00 41.90 ? 2814 HOH A O     1 
HETATM 18728 O O     . HOH CB 8 .    ? -68.842 69.469  80.353  1.00 29.31 ? 2815 HOH A O     1 
HETATM 18729 O O     . HOH CB 8 .    ? -61.471 49.522  66.789  1.00 41.76 ? 2816 HOH A O     1 
HETATM 18730 O O     . HOH CB 8 .    ? -36.825 65.271  120.678 1.00 45.20 ? 2817 HOH A O     1 
HETATM 18731 O O     . HOH CB 8 .    ? 17.251  78.219  123.243 1.00 43.95 ? 2818 HOH A O     1 
HETATM 18732 O O     . HOH CB 8 .    ? -23.059 90.431  101.245 1.00 31.20 ? 2819 HOH A O     1 
HETATM 18733 O O     . HOH CB 8 .    ? -9.035  63.019  70.314  1.00 44.84 ? 2820 HOH A O     1 
HETATM 18734 O O     . HOH CB 8 .    ? -23.085 91.785  103.782 1.00 40.02 ? 2821 HOH A O     1 
HETATM 18735 O O     . HOH CB 8 .    ? -21.177 53.190  100.713 1.00 41.56 ? 2822 HOH A O     1 
HETATM 18736 O O     . HOH CB 8 .    ? -2.335  63.529  88.186  1.00 48.81 ? 2823 HOH A O     1 
HETATM 18737 O O     . HOH CB 8 .    ? -44.730 29.268  99.333  1.00 47.66 ? 2824 HOH A O     1 
HETATM 18738 O O     . HOH CB 8 .    ? -1.167  61.140  113.198 1.00 40.83 ? 2825 HOH A O     1 
HETATM 18739 O O     . HOH CB 8 .    ? -18.624 74.788  109.726 1.00 28.74 ? 2826 HOH A O     1 
HETATM 18740 O O     . HOH CB 8 .    ? -34.140 62.575  90.309  1.00 45.72 ? 2827 HOH A O     1 
HETATM 18741 O O     . HOH CB 8 .    ? -36.208 43.121  105.709 1.00 44.56 ? 2828 HOH A O     1 
HETATM 18742 O O     . HOH CB 8 .    ? 10.348  79.054  125.330 1.00 39.72 ? 2829 HOH A O     1 
HETATM 18743 O O     . HOH CB 8 .    ? -9.075  62.190  94.364  1.00 34.74 ? 2830 HOH A O     1 
HETATM 18744 O O     . HOH CB 8 .    ? -41.785 63.559  106.905 1.00 39.57 ? 2831 HOH A O     1 
HETATM 18745 O O     . HOH CB 8 .    ? -54.007 71.130  106.974 1.00 41.08 ? 2832 HOH A O     1 
HETATM 18746 O O     . HOH CB 8 .    ? -61.476 51.689  94.865  1.00 45.13 ? 2833 HOH A O     1 
HETATM 18747 O O     . HOH CB 8 .    ? -13.000 53.539  81.198  1.00 41.41 ? 2834 HOH A O     1 
HETATM 18748 O O     . HOH CB 8 .    ? -63.146 55.371  70.260  1.00 35.62 ? 2835 HOH A O     1 
HETATM 18749 O O     . HOH CB 8 .    ? -2.215  75.014  119.282 1.00 39.13 ? 2836 HOH A O     1 
HETATM 18750 O O     . HOH CB 8 .    ? -39.498 48.000  61.526  1.00 48.59 ? 2837 HOH A O     1 
HETATM 18751 O O     . HOH CB 8 .    ? -37.082 82.560  77.525  1.00 36.66 ? 2838 HOH A O     1 
HETATM 18752 O O     . HOH CB 8 .    ? 4.165   65.104  96.583  1.00 34.65 ? 2839 HOH A O     1 
HETATM 18753 O O     . HOH CB 8 .    ? -53.326 75.284  102.056 1.00 39.51 ? 2840 HOH A O     1 
HETATM 18754 O O     . HOH CB 8 .    ? 10.323  68.311  114.926 1.00 32.17 ? 2841 HOH A O     1 
HETATM 18755 O O     . HOH CB 8 .    ? -58.579 59.160  103.659 1.00 44.70 ? 2842 HOH A O     1 
HETATM 18756 O O     . HOH CB 8 .    ? -2.581  84.668  97.014  1.00 37.86 ? 2843 HOH A O     1 
HETATM 18757 O O     . HOH CB 8 .    ? -52.492 73.068  103.165 1.00 33.82 ? 2844 HOH A O     1 
HETATM 18758 O O     . HOH CB 8 .    ? -16.748 75.776  106.422 1.00 31.38 ? 2845 HOH A O     1 
HETATM 18759 O O     . HOH CB 8 .    ? -53.660 69.071  101.394 1.00 36.77 ? 2846 HOH A O     1 
HETATM 18760 O O     . HOH CB 8 .    ? -30.106 92.627  109.315 1.00 39.38 ? 2847 HOH A O     1 
HETATM 18761 O O     . HOH CB 8 .    ? -24.250 62.312  100.501 1.00 33.01 ? 2848 HOH A O     1 
HETATM 18762 O O     . HOH CB 8 .    ? -32.599 65.624  125.134 1.00 37.16 ? 2849 HOH A O     1 
HETATM 18763 O O     . HOH CB 8 .    ? -39.450 86.037  80.559  1.00 42.62 ? 2850 HOH A O     1 
HETATM 18764 O O     . HOH CB 8 .    ? -8.796  77.117  129.890 1.00 34.15 ? 2851 HOH A O     1 
HETATM 18765 O O     . HOH CB 8 .    ? 6.873   60.099  94.639  1.00 41.08 ? 2852 HOH A O     1 
HETATM 18766 O O     . HOH CB 8 .    ? -54.781 54.291  102.491 1.00 41.26 ? 2853 HOH A O     1 
HETATM 18767 O O     . HOH CB 8 .    ? -56.706 52.146  99.089  1.00 32.73 ? 2854 HOH A O     1 
HETATM 18768 O O     . HOH CB 8 .    ? 6.866   62.584  95.075  1.00 32.98 ? 2855 HOH A O     1 
HETATM 18769 O O     . HOH CB 8 .    ? -29.235 60.092  88.998  1.00 27.28 ? 2856 HOH A O     1 
HETATM 18770 O O     . HOH CB 8 .    ? -43.028 59.522  104.140 1.00 40.21 ? 2857 HOH A O     1 
HETATM 18771 O O     . HOH CB 8 .    ? -30.041 60.318  86.440  1.00 37.78 ? 2858 HOH A O     1 
HETATM 18772 O O     . HOH CB 8 .    ? -28.892 77.676  70.562  1.00 38.41 ? 2859 HOH A O     1 
HETATM 18773 O O     . HOH CB 8 .    ? -9.857  83.361  73.493  1.00 51.81 ? 2860 HOH A O     1 
HETATM 18774 O O     . HOH CB 8 .    ? -43.795 70.319  114.384 1.00 41.87 ? 2861 HOH A O     1 
HETATM 18775 O O     . HOH CB 8 .    ? -51.874 46.757  97.195  1.00 32.75 ? 2862 HOH A O     1 
HETATM 18776 O O     . HOH CB 8 .    ? -31.117 84.806  74.143  1.00 37.37 ? 2863 HOH A O     1 
HETATM 18777 O O     . HOH CB 8 .    ? -56.256 78.631  77.555  1.00 38.91 ? 2864 HOH A O     1 
HETATM 18778 O O     . HOH CB 8 .    ? -63.585 56.906  97.069  1.00 37.79 ? 2865 HOH A O     1 
HETATM 18779 O O     . HOH CB 8 .    ? -35.316 39.191  72.973  1.00 51.93 ? 2866 HOH A O     1 
HETATM 18780 O O     . HOH CB 8 .    ? -55.107 52.520  101.268 1.00 36.08 ? 2867 HOH A O     1 
HETATM 18781 O O     . HOH CB 8 .    ? -33.112 57.363  111.483 1.00 34.81 ? 2868 HOH A O     1 
HETATM 18782 O O     . HOH CB 8 .    ? -54.155 70.914  102.840 1.00 37.74 ? 2869 HOH A O     1 
HETATM 18783 O O     . HOH DB 8 .    ? -11.280 27.696  81.438  1.00 29.01 ? 2101 HOH B O     1 
HETATM 18784 O O     . HOH DB 8 .    ? 15.253  53.364  81.795  1.00 38.68 ? 2102 HOH B O     1 
HETATM 18785 O O     . HOH DB 8 .    ? -11.970 8.649   124.277 1.00 43.78 ? 2103 HOH B O     1 
HETATM 18786 O O     . HOH DB 8 .    ? -18.309 -4.279  110.235 1.00 49.81 ? 2104 HOH B O     1 
HETATM 18787 O O     . HOH DB 8 .    ? 13.132  51.282  86.609  1.00 38.37 ? 2105 HOH B O     1 
HETATM 18788 O O     . HOH DB 8 .    ? 0.851   30.776  57.100  1.00 27.52 ? 2106 HOH B O     1 
HETATM 18789 O O     . HOH DB 8 .    ? 6.938   15.842  124.513 1.00 38.60 ? 2107 HOH B O     1 
HETATM 18790 O O     . HOH DB 8 .    ? -5.871  37.251  77.933  1.00 31.76 ? 2108 HOH B O     1 
HETATM 18791 O O     . HOH DB 8 .    ? 32.830  18.884  57.917  1.00 37.84 ? 2109 HOH B O     1 
HETATM 18792 O O     . HOH DB 8 .    ? -7.121  -1.491  120.131 1.00 39.15 ? 2110 HOH B O     1 
HETATM 18793 O O     . HOH DB 8 .    ? 12.362  29.318  80.317  1.00 38.97 ? 2111 HOH B O     1 
HETATM 18794 O O     . HOH DB 8 .    ? 4.850   32.543  90.243  1.00 35.37 ? 2112 HOH B O     1 
HETATM 18795 O O     . HOH DB 8 .    ? 18.357  12.505  95.595  1.00 36.78 ? 2113 HOH B O     1 
HETATM 18796 O O     . HOH DB 8 .    ? 0.826   -0.291  96.294  1.00 37.07 ? 2114 HOH B O     1 
HETATM 18797 O O     . HOH DB 8 .    ? 11.818  33.032  81.588  1.00 36.21 ? 2115 HOH B O     1 
HETATM 18798 O O     . HOH DB 8 .    ? 26.926  36.805  107.057 1.00 42.37 ? 2116 HOH B O     1 
HETATM 18799 O O     . HOH DB 8 .    ? 9.467   30.534  110.074 1.00 45.13 ? 2117 HOH B O     1 
HETATM 18800 O O     . HOH DB 8 .    ? 4.286   72.515  85.955  1.00 38.11 ? 2118 HOH B O     1 
HETATM 18801 O O     . HOH DB 8 .    ? -16.828 4.682   116.719 1.00 41.56 ? 2119 HOH B O     1 
HETATM 18802 O O     . HOH DB 8 .    ? 29.165  59.915  56.558  1.00 44.47 ? 2120 HOH B O     1 
HETATM 18803 O O     . HOH DB 8 .    ? -10.430 39.535  127.353 1.00 47.21 ? 2121 HOH B O     1 
HETATM 18804 O O     . HOH DB 8 .    ? -2.153  29.865  57.298  1.00 37.92 ? 2122 HOH B O     1 
HETATM 18805 O O     . HOH DB 8 .    ? -3.817  24.727  70.334  1.00 38.49 ? 2123 HOH B O     1 
HETATM 18806 O O     . HOH DB 8 .    ? -7.181  8.317   111.414 1.00 32.19 ? 2124 HOH B O     1 
HETATM 18807 O O     . HOH DB 8 .    ? 30.131  27.274  56.006  1.00 30.10 ? 2125 HOH B O     1 
HETATM 18808 O O     . HOH DB 8 .    ? -4.365  -6.718  111.898 1.00 34.64 ? 2126 HOH B O     1 
HETATM 18809 O O     . HOH DB 8 .    ? 5.576   48.048  112.011 1.00 40.95 ? 2127 HOH B O     1 
HETATM 18810 O O     . HOH DB 8 .    ? 18.029  12.567  117.450 1.00 27.20 ? 2128 HOH B O     1 
HETATM 18811 O O     . HOH DB 8 .    ? -1.091  22.353  71.231  1.00 29.28 ? 2129 HOH B O     1 
HETATM 18812 O O     . HOH DB 8 .    ? 11.055  46.228  106.680 1.00 31.70 ? 2130 HOH B O     1 
HETATM 18813 O O     . HOH DB 8 .    ? -10.916 1.445   122.079 1.00 42.95 ? 2131 HOH B O     1 
HETATM 18814 O O     . HOH DB 8 .    ? 11.050  18.248  64.761  1.00 28.16 ? 2132 HOH B O     1 
HETATM 18815 O O     . HOH DB 8 .    ? -32.206 17.597  91.725  1.00 44.20 ? 2133 HOH B O     1 
HETATM 18816 O O     . HOH DB 8 .    ? 12.765  6.283   118.116 1.00 38.88 ? 2134 HOH B O     1 
HETATM 18817 O O     . HOH DB 8 .    ? 23.381  48.437  107.386 1.00 36.34 ? 2135 HOH B O     1 
HETATM 18818 O O     . HOH DB 8 .    ? 6.469   44.415  58.314  1.00 30.26 ? 2136 HOH B O     1 
HETATM 18819 O O     . HOH DB 8 .    ? 6.628   5.508   92.307  1.00 25.93 ? 2137 HOH B O     1 
HETATM 18820 O O     . HOH DB 8 .    ? -4.731  27.240  70.281  1.00 35.38 ? 2138 HOH B O     1 
HETATM 18821 O O     . HOH DB 8 .    ? -10.767 19.886  122.962 1.00 44.17 ? 2139 HOH B O     1 
HETATM 18822 O O     . HOH DB 8 .    ? 11.951  16.439  67.449  1.00 36.71 ? 2140 HOH B O     1 
HETATM 18823 O O     . HOH DB 8 .    ? -2.790  4.783   84.987  1.00 36.57 ? 2141 HOH B O     1 
HETATM 18824 O O     . HOH DB 8 .    ? 16.620  43.079  50.602  1.00 37.23 ? 2142 HOH B O     1 
HETATM 18825 O O     . HOH DB 8 .    ? 16.286  48.463  71.011  1.00 25.64 ? 2143 HOH B O     1 
HETATM 18826 O O     . HOH DB 8 .    ? 6.843   17.781  89.679  1.00 34.75 ? 2144 HOH B O     1 
HETATM 18827 O O     . HOH DB 8 .    ? -0.996  46.048  133.771 1.00 46.09 ? 2145 HOH B O     1 
HETATM 18828 O O     . HOH DB 8 .    ? 18.981  24.953  54.298  1.00 25.41 ? 2146 HOH B O     1 
HETATM 18829 O O     . HOH DB 8 .    ? 35.478  32.065  54.846  1.00 36.17 ? 2147 HOH B O     1 
HETATM 18830 O O     . HOH DB 8 .    ? -4.852  30.599  77.494  1.00 23.39 ? 2148 HOH B O     1 
HETATM 18831 O O     . HOH DB 8 .    ? 14.034  81.647  69.985  1.00 42.36 ? 2149 HOH B O     1 
HETATM 18832 O O     . HOH DB 8 .    ? -7.691  30.274  76.077  1.00 29.63 ? 2150 HOH B O     1 
HETATM 18833 O O     . HOH DB 8 .    ? 21.266  74.150  82.229  1.00 41.40 ? 2151 HOH B O     1 
HETATM 18834 O O     . HOH DB 8 .    ? 10.297  50.959  65.035  1.00 31.29 ? 2152 HOH B O     1 
HETATM 18835 O O     . HOH DB 8 .    ? 5.735   55.673  105.158 1.00 26.91 ? 2153 HOH B O     1 
HETATM 18836 O O     . HOH DB 8 .    ? 29.165  68.692  72.660  1.00 32.84 ? 2154 HOH B O     1 
HETATM 18837 O O     . HOH DB 8 .    ? 11.647  0.495   94.979  1.00 40.79 ? 2155 HOH B O     1 
HETATM 18838 O O     . HOH DB 8 .    ? -2.093  48.882  63.683  1.00 23.86 ? 2156 HOH B O     1 
HETATM 18839 O O     . HOH DB 8 .    ? 10.833  19.387  61.895  1.00 31.70 ? 2157 HOH B O     1 
HETATM 18840 O O     . HOH DB 8 .    ? -8.300  23.726  106.823 1.00 43.93 ? 2158 HOH B O     1 
HETATM 18841 O O     . HOH DB 8 .    ? -24.145 22.837  84.775  1.00 42.48 ? 2159 HOH B O     1 
HETATM 18842 O O     . HOH DB 8 .    ? 2.361   17.278  112.696 1.00 36.23 ? 2160 HOH B O     1 
HETATM 18843 O O     . HOH DB 8 .    ? -6.230  51.151  73.056  1.00 22.52 ? 2161 HOH B O     1 
HETATM 18844 O O     . HOH DB 8 .    ? 16.607  14.452  109.487 1.00 32.46 ? 2162 HOH B O     1 
HETATM 18845 O O     . HOH DB 8 .    ? -7.576  27.098  100.090 1.00 33.67 ? 2163 HOH B O     1 
HETATM 18846 O O     . HOH DB 8 .    ? 11.776  12.099  121.726 1.00 31.55 ? 2164 HOH B O     1 
HETATM 18847 O O     . HOH DB 8 .    ? -8.510  -5.830  106.969 1.00 37.85 ? 2165 HOH B O     1 
HETATM 18848 O O     . HOH DB 8 .    ? 1.366   -1.161  92.581  1.00 32.00 ? 2166 HOH B O     1 
HETATM 18849 O O     . HOH DB 8 .    ? 5.520   76.146  85.512  1.00 43.63 ? 2167 HOH B O     1 
HETATM 18850 O O     . HOH DB 8 .    ? 3.303   33.838  86.815  1.00 23.81 ? 2168 HOH B O     1 
HETATM 18851 O O     . HOH DB 8 .    ? 9.803   26.073  55.077  1.00 23.92 ? 2169 HOH B O     1 
HETATM 18852 O O     . HOH DB 8 .    ? 0.003   3.992   88.637  1.00 25.92 ? 2170 HOH B O     1 
HETATM 18853 O O     . HOH DB 8 .    ? 6.154   10.711  75.732  1.00 39.23 ? 2171 HOH B O     1 
HETATM 18854 O O     . HOH DB 8 .    ? 11.450  48.766  78.296  1.00 33.90 ? 2172 HOH B O     1 
HETATM 18855 O O     . HOH DB 8 .    ? 7.068   33.930  86.780  1.00 24.61 ? 2173 HOH B O     1 
HETATM 18856 O O     . HOH DB 8 .    ? 20.926  50.323  88.438  1.00 42.37 ? 2174 HOH B O     1 
HETATM 18857 O O     . HOH DB 8 .    ? -2.348  45.176  102.854 1.00 30.14 ? 2175 HOH B O     1 
HETATM 18858 O O     . HOH DB 8 .    ? 22.340  11.858  71.423  1.00 33.73 ? 2176 HOH B O     1 
HETATM 18859 O O     . HOH DB 8 .    ? 31.029  21.124  80.056  1.00 26.06 ? 2177 HOH B O     1 
HETATM 18860 O O     . HOH DB 8 .    ? 36.373  31.522  64.891  1.00 46.19 ? 2178 HOH B O     1 
HETATM 18861 O O     . HOH DB 8 .    ? -2.023  42.175  61.774  1.00 28.33 ? 2179 HOH B O     1 
HETATM 18862 O O     . HOH DB 8 .    ? 27.044  41.972  49.904  1.00 44.08 ? 2180 HOH B O     1 
HETATM 18863 O O     . HOH DB 8 .    ? -21.462 15.617  82.888  1.00 32.74 ? 2181 HOH B O     1 
HETATM 18864 O O     . HOH DB 8 .    ? -2.306  39.579  87.447  1.00 23.04 ? 2182 HOH B O     1 
HETATM 18865 O O     . HOH DB 8 .    ? 1.710   57.407  87.973  1.00 39.23 ? 2183 HOH B O     1 
HETATM 18866 O O     . HOH DB 8 .    ? 16.340  15.980  85.140  1.00 29.82 ? 2184 HOH B O     1 
HETATM 18867 O O     . HOH DB 8 .    ? -22.515 18.379  102.215 1.00 38.64 ? 2185 HOH B O     1 
HETATM 18868 O O     . HOH DB 8 .    ? 33.245  29.062  61.952  1.00 35.31 ? 2186 HOH B O     1 
HETATM 18869 O O     . HOH DB 8 .    ? -8.894  23.897  101.023 1.00 25.08 ? 2187 HOH B O     1 
HETATM 18870 O O     . HOH DB 8 .    ? 20.069  50.926  77.451  1.00 33.88 ? 2188 HOH B O     1 
HETATM 18871 O O     . HOH DB 8 .    ? -15.490 47.507  114.634 1.00 42.03 ? 2189 HOH B O     1 
HETATM 18872 O O     . HOH DB 8 .    ? 2.663   22.078  130.151 1.00 36.51 ? 2190 HOH B O     1 
HETATM 18873 O O     . HOH DB 8 .    ? 1.299   14.927  116.295 1.00 30.35 ? 2191 HOH B O     1 
HETATM 18874 O O     . HOH DB 8 .    ? 1.526   20.304  104.010 1.00 36.29 ? 2192 HOH B O     1 
HETATM 18875 O O     . HOH DB 8 .    ? -2.630  -2.479  94.595  1.00 38.27 ? 2193 HOH B O     1 
HETATM 18876 O O     . HOH DB 8 .    ? -10.495 52.809  128.772 1.00 39.80 ? 2194 HOH B O     1 
HETATM 18877 O O     . HOH DB 8 .    ? -14.149 54.268  118.586 1.00 33.70 ? 2195 HOH B O     1 
HETATM 18878 O O     . HOH DB 8 .    ? 23.328  55.983  99.725  1.00 37.43 ? 2196 HOH B O     1 
HETATM 18879 O O     . HOH DB 8 .    ? 22.674  48.639  78.145  1.00 31.59 ? 2197 HOH B O     1 
HETATM 18880 O O     . HOH DB 8 .    ? -13.383 17.924  106.058 1.00 30.69 ? 2198 HOH B O     1 
HETATM 18881 O O     . HOH DB 8 .    ? 0.956   55.643  110.826 1.00 29.39 ? 2199 HOH B O     1 
HETATM 18882 O O     . HOH DB 8 .    ? 25.896  55.274  77.419  1.00 30.96 ? 2200 HOH B O     1 
HETATM 18883 O O     . HOH DB 8 .    ? -14.134 7.101   120.574 1.00 43.83 ? 2201 HOH B O     1 
HETATM 18884 O O     . HOH DB 8 .    ? -1.384  14.456  86.140  1.00 25.31 ? 2202 HOH B O     1 
HETATM 18885 O O     . HOH DB 8 .    ? -5.325  55.431  78.739  1.00 25.65 ? 2203 HOH B O     1 
HETATM 18886 O O     . HOH DB 8 .    ? -6.233  11.754  125.763 1.00 38.72 ? 2204 HOH B O     1 
HETATM 18887 O O     . HOH DB 8 .    ? 4.141   -9.002  104.603 1.00 36.15 ? 2205 HOH B O     1 
HETATM 18888 O O     . HOH DB 8 .    ? 7.836   65.988  64.089  1.00 34.89 ? 2206 HOH B O     1 
HETATM 18889 O O     . HOH DB 8 .    ? 0.963   28.553  83.088  1.00 19.32 ? 2207 HOH B O     1 
HETATM 18890 O O     . HOH DB 8 .    ? -3.371  10.271  84.468  1.00 27.22 ? 2208 HOH B O     1 
HETATM 18891 O O     . HOH DB 8 .    ? 16.797  27.075  82.835  1.00 31.12 ? 2209 HOH B O     1 
HETATM 18892 O O     . HOH DB 8 .    ? 13.549  10.063  91.348  1.00 35.82 ? 2210 HOH B O     1 
HETATM 18893 O O     . HOH DB 8 .    ? 12.283  12.586  110.586 1.00 34.81 ? 2211 HOH B O     1 
HETATM 18894 O O     . HOH DB 8 .    ? 15.656  52.522  58.768  1.00 33.65 ? 2212 HOH B O     1 
HETATM 18895 O O     . HOH DB 8 .    ? 17.030  53.366  64.081  1.00 33.54 ? 2213 HOH B O     1 
HETATM 18896 O O     . HOH DB 8 .    ? -10.536 46.787  74.500  1.00 25.89 ? 2214 HOH B O     1 
HETATM 18897 O O     . HOH DB 8 .    ? 11.978  10.944  71.641  1.00 29.93 ? 2215 HOH B O     1 
HETATM 18898 O O     . HOH DB 8 .    ? 8.947   23.405  109.401 1.00 37.02 ? 2216 HOH B O     1 
HETATM 18899 O O     . HOH DB 8 .    ? 2.866   18.177  89.297  1.00 33.59 ? 2217 HOH B O     1 
HETATM 18900 O O     . HOH DB 8 .    ? -5.274  4.765   122.279 1.00 36.52 ? 2218 HOH B O     1 
HETATM 18901 O O     . HOH DB 8 .    ? 6.936   7.913   75.005  1.00 39.16 ? 2219 HOH B O     1 
HETATM 18902 O O     . HOH DB 8 .    ? 4.333   42.237  84.729  1.00 25.01 ? 2220 HOH B O     1 
HETATM 18903 O O     . HOH DB 8 .    ? 10.479  35.737  79.071  1.00 37.20 ? 2221 HOH B O     1 
HETATM 18904 O O     . HOH DB 8 .    ? 19.988  59.904  57.158  1.00 32.20 ? 2222 HOH B O     1 
HETATM 18905 O O     . HOH DB 8 .    ? 21.709  29.706  71.361  1.00 21.31 ? 2223 HOH B O     1 
HETATM 18906 O O     . HOH DB 8 .    ? -8.942  0.305   112.699 1.00 38.02 ? 2224 HOH B O     1 
HETATM 18907 O O     . HOH DB 8 .    ? 0.034   73.665  78.016  1.00 30.30 ? 2225 HOH B O     1 
HETATM 18908 O O     . HOH DB 8 .    ? 13.386  49.980  65.035  1.00 35.39 ? 2226 HOH B O     1 
HETATM 18909 O O     . HOH DB 8 .    ? 12.605  1.906   111.437 1.00 32.86 ? 2227 HOH B O     1 
HETATM 18910 O O     . HOH DB 8 .    ? 27.026  49.066  95.200  1.00 41.27 ? 2228 HOH B O     1 
HETATM 18911 O O     . HOH DB 8 .    ? 22.244  24.447  108.767 1.00 30.24 ? 2229 HOH B O     1 
HETATM 18912 O O     . HOH DB 8 .    ? 7.234   51.477  57.487  1.00 36.61 ? 2230 HOH B O     1 
HETATM 18913 O O     . HOH DB 8 .    ? -4.529  -2.234  96.908  1.00 32.53 ? 2231 HOH B O     1 
HETATM 18914 O O     . HOH DB 8 .    ? -4.175  64.501  81.180  1.00 21.36 ? 2232 HOH B O     1 
HETATM 18915 O O     . HOH DB 8 .    ? -6.262  12.443  84.590  1.00 30.27 ? 2233 HOH B O     1 
HETATM 18916 O O     . HOH DB 8 .    ? 31.273  42.225  63.581  1.00 38.23 ? 2234 HOH B O     1 
HETATM 18917 O O     . HOH DB 8 .    ? 8.468   45.349  133.009 1.00 43.45 ? 2235 HOH B O     1 
HETATM 18918 O O     . HOH DB 8 .    ? 12.274  55.762  65.838  1.00 41.19 ? 2236 HOH B O     1 
HETATM 18919 O O     . HOH DB 8 .    ? 37.065  27.644  93.686  1.00 40.03 ? 2237 HOH B O     1 
HETATM 18920 O O     . HOH DB 8 .    ? 22.526  9.612   85.175  1.00 41.54 ? 2238 HOH B O     1 
HETATM 18921 O O     . HOH DB 8 .    ? 26.050  8.176   78.700  1.00 41.03 ? 2239 HOH B O     1 
HETATM 18922 O O     . HOH DB 8 .    ? 4.699   48.807  137.908 1.00 58.23 ? 2240 HOH B O     1 
HETATM 18923 O O     . HOH DB 8 .    ? 23.588  52.801  70.570  1.00 36.84 ? 2241 HOH B O     1 
HETATM 18924 O O     . HOH DB 8 .    ? 18.746  47.853  90.325  1.00 30.43 ? 2242 HOH B O     1 
HETATM 18925 O O     . HOH DB 8 .    ? 29.437  69.150  79.730  1.00 29.58 ? 2243 HOH B O     1 
HETATM 18926 O O     . HOH DB 8 .    ? 3.688   7.712   92.423  1.00 25.25 ? 2244 HOH B O     1 
HETATM 18927 O O     . HOH DB 8 .    ? 15.464  16.521  87.932  1.00 27.00 ? 2245 HOH B O     1 
HETATM 18928 O O     . HOH DB 8 .    ? 30.646  50.068  71.751  1.00 31.37 ? 2246 HOH B O     1 
HETATM 18929 O O     . HOH DB 8 .    ? 4.229   19.261  97.292  1.00 37.36 ? 2247 HOH B O     1 
HETATM 18930 O O     . HOH DB 8 .    ? 19.431  54.846  94.096  1.00 28.98 ? 2248 HOH B O     1 
HETATM 18931 O O     . HOH DB 8 .    ? -6.529  35.388  69.476  1.00 36.27 ? 2249 HOH B O     1 
HETATM 18932 O O     . HOH DB 8 .    ? 4.008   55.506  73.017  1.00 28.46 ? 2250 HOH B O     1 
HETATM 18933 O O     . HOH DB 8 .    ? 24.264  68.912  67.783  1.00 28.17 ? 2251 HOH B O     1 
HETATM 18934 O O     . HOH DB 8 .    ? -9.242  10.001  123.399 1.00 34.79 ? 2252 HOH B O     1 
HETATM 18935 O O     . HOH DB 8 .    ? 28.903  31.060  104.247 1.00 39.03 ? 2253 HOH B O     1 
HETATM 18936 O O     . HOH DB 8 .    ? 9.901   43.615  110.528 1.00 33.01 ? 2254 HOH B O     1 
HETATM 18937 O O     . HOH DB 8 .    ? 1.251   30.691  75.066  1.00 23.88 ? 2255 HOH B O     1 
HETATM 18938 O O     . HOH DB 8 .    ? 1.979   76.546  84.640  1.00 42.19 ? 2256 HOH B O     1 
HETATM 18939 O O     . HOH DB 8 .    ? -2.355  24.157  76.507  1.00 27.34 ? 2257 HOH B O     1 
HETATM 18940 O O     . HOH DB 8 .    ? 18.918  5.539   74.407  1.00 35.92 ? 2258 HOH B O     1 
HETATM 18941 O O     . HOH DB 8 .    ? 17.226  43.503  79.782  1.00 33.62 ? 2259 HOH B O     1 
HETATM 18942 O O     . HOH DB 8 .    ? 19.899  18.884  66.172  1.00 22.26 ? 2260 HOH B O     1 
HETATM 18943 O O     . HOH DB 8 .    ? -20.405 25.535  102.168 1.00 45.12 ? 2261 HOH B O     1 
HETATM 18944 O O     . HOH DB 8 .    ? -4.690  60.151  125.795 1.00 35.01 ? 2262 HOH B O     1 
HETATM 18945 O O     . HOH DB 8 .    ? 7.683   45.067  75.488  1.00 18.42 ? 2263 HOH B O     1 
HETATM 18946 O O     . HOH DB 8 .    ? 12.831  36.615  86.268  1.00 22.45 ? 2264 HOH B O     1 
HETATM 18947 O O     . HOH DB 8 .    ? -8.843  24.115  77.280  1.00 40.50 ? 2265 HOH B O     1 
HETATM 18948 O O     . HOH DB 8 .    ? -1.488  5.287   92.142  1.00 26.44 ? 2266 HOH B O     1 
HETATM 18949 O O     . HOH DB 8 .    ? 5.021   63.169  84.534  1.00 24.82 ? 2267 HOH B O     1 
HETATM 18950 O O     . HOH DB 8 .    ? 34.516  62.217  78.730  1.00 23.75 ? 2268 HOH B O     1 
HETATM 18951 O O     . HOH DB 8 .    ? 21.746  79.812  70.399  1.00 38.97 ? 2269 HOH B O     1 
HETATM 18952 O O     . HOH DB 8 .    ? -4.163  18.570  98.158  1.00 20.05 ? 2270 HOH B O     1 
HETATM 18953 O O     . HOH DB 8 .    ? 9.355   37.387  131.759 1.00 43.66 ? 2271 HOH B O     1 
HETATM 18954 O O     . HOH DB 8 .    ? 2.705   44.117  70.537  1.00 22.53 ? 2272 HOH B O     1 
HETATM 18955 O O     . HOH DB 8 .    ? 6.450   5.446   86.172  1.00 25.12 ? 2273 HOH B O     1 
HETATM 18956 O O     . HOH DB 8 .    ? -3.415  -11.294 101.281 1.00 40.78 ? 2274 HOH B O     1 
HETATM 18957 O O     . HOH DB 8 .    ? 18.808  9.006   92.327  1.00 36.73 ? 2275 HOH B O     1 
HETATM 18958 O O     . HOH DB 8 .    ? 31.517  52.645  65.344  1.00 38.01 ? 2276 HOH B O     1 
HETATM 18959 O O     . HOH DB 8 .    ? 9.219   5.820   85.099  1.00 26.71 ? 2277 HOH B O     1 
HETATM 18960 O O     . HOH DB 8 .    ? 1.656   13.021  102.109 1.00 23.29 ? 2278 HOH B O     1 
HETATM 18961 O O     . HOH DB 8 .    ? 0.998   38.784  108.728 1.00 30.66 ? 2279 HOH B O     1 
HETATM 18962 O O     . HOH DB 8 .    ? 19.855  19.368  105.938 1.00 22.77 ? 2280 HOH B O     1 
HETATM 18963 O O     . HOH DB 8 .    ? -12.721 19.797  84.180  1.00 28.27 ? 2281 HOH B O     1 
HETATM 18964 O O     . HOH DB 8 .    ? 10.198  50.308  90.554  1.00 41.53 ? 2282 HOH B O     1 
HETATM 18965 O O     . HOH DB 8 .    ? 15.365  40.446  73.519  1.00 24.08 ? 2283 HOH B O     1 
HETATM 18966 O O     . HOH DB 8 .    ? 15.323  37.609  114.851 1.00 43.73 ? 2284 HOH B O     1 
HETATM 18967 O O     . HOH DB 8 .    ? 4.831   77.949  80.473  1.00 35.63 ? 2285 HOH B O     1 
HETATM 18968 O O     . HOH DB 8 .    ? 18.251  43.638  91.848  1.00 23.80 ? 2286 HOH B O     1 
HETATM 18969 O O     . HOH DB 8 .    ? -14.561 39.903  125.181 1.00 52.81 ? 2287 HOH B O     1 
HETATM 18970 O O     . HOH DB 8 .    ? -0.147  76.036  68.304  1.00 37.77 ? 2288 HOH B O     1 
HETATM 18971 O O     . HOH DB 8 .    ? 18.715  13.349  74.485  1.00 30.12 ? 2289 HOH B O     1 
HETATM 18972 O O     . HOH DB 8 .    ? 28.366  31.147  73.543  1.00 30.85 ? 2290 HOH B O     1 
HETATM 18973 O O     . HOH DB 8 .    ? -1.259  55.778  72.995  1.00 32.17 ? 2291 HOH B O     1 
HETATM 18974 O O     . HOH DB 8 .    ? 17.522  48.935  59.544  1.00 26.38 ? 2292 HOH B O     1 
HETATM 18975 O O     . HOH DB 8 .    ? 42.202  33.932  103.050 1.00 45.99 ? 2293 HOH B O     1 
HETATM 18976 O O     . HOH DB 8 .    ? 27.643  18.641  101.086 1.00 39.08 ? 2294 HOH B O     1 
HETATM 18977 O O     . HOH DB 8 .    ? 0.412   20.196  69.838  1.00 28.79 ? 2295 HOH B O     1 
HETATM 18978 O O     . HOH DB 8 .    ? 23.692  52.149  62.776  1.00 27.48 ? 2296 HOH B O     1 
HETATM 18979 O O     . HOH DB 8 .    ? -1.720  2.396   125.979 1.00 37.28 ? 2297 HOH B O     1 
HETATM 18980 O O     . HOH DB 8 .    ? -29.954 11.785  96.748  1.00 50.45 ? 2298 HOH B O     1 
HETATM 18981 O O     . HOH DB 8 .    ? 2.614   39.465  98.976  1.00 23.53 ? 2299 HOH B O     1 
HETATM 18982 O O     . HOH DB 8 .    ? 3.760   10.312  92.405  1.00 24.49 ? 2300 HOH B O     1 
HETATM 18983 O O     . HOH DB 8 .    ? 21.538  53.844  83.977  1.00 36.91 ? 2301 HOH B O     1 
HETATM 18984 O O     . HOH DB 8 .    ? 1.620   5.852   91.888  1.00 24.75 ? 2302 HOH B O     1 
HETATM 18985 O O     . HOH DB 8 .    ? 17.986  23.186  88.451  1.00 27.26 ? 2303 HOH B O     1 
HETATM 18986 O O     . HOH DB 8 .    ? 14.920  16.679  92.098  1.00 30.07 ? 2304 HOH B O     1 
HETATM 18987 O O     . HOH DB 8 .    ? 33.856  67.487  81.167  1.00 26.84 ? 2305 HOH B O     1 
HETATM 18988 O O     . HOH DB 8 .    ? 2.762   32.930  78.656  1.00 20.03 ? 2306 HOH B O     1 
HETATM 18989 O O     . HOH DB 8 .    ? 15.319  55.974  74.303  1.00 29.54 ? 2307 HOH B O     1 
HETATM 18990 O O     . HOH DB 8 .    ? 10.196  51.456  75.960  1.00 30.78 ? 2308 HOH B O     1 
HETATM 18991 O O     . HOH DB 8 .    ? -4.159  1.610   124.203 1.00 36.78 ? 2309 HOH B O     1 
HETATM 18992 O O     . HOH DB 8 .    ? 27.509  37.744  90.410  1.00 34.14 ? 2310 HOH B O     1 
HETATM 18993 O O     . HOH DB 8 .    ? -6.840  14.148  91.687  1.00 21.78 ? 2311 HOH B O     1 
HETATM 18994 O O     . HOH DB 8 .    ? 23.009  67.375  64.966  1.00 30.32 ? 2312 HOH B O     1 
HETATM 18995 O O     . HOH DB 8 .    ? 7.626   49.003  107.078 1.00 25.78 ? 2313 HOH B O     1 
HETATM 18996 O O     . HOH DB 8 .    ? 10.639  29.315  94.592  1.00 25.17 ? 2314 HOH B O     1 
HETATM 18997 O O     . HOH DB 8 .    ? 19.629  4.969   76.831  1.00 37.63 ? 2315 HOH B O     1 
HETATM 18998 O O     . HOH DB 8 .    ? -0.880  60.842  77.438  1.00 26.66 ? 2316 HOH B O     1 
HETATM 18999 O O     . HOH DB 8 .    ? 8.037   30.303  85.617  1.00 36.26 ? 2317 HOH B O     1 
HETATM 19000 O O     . HOH DB 8 .    ? 27.055  15.389  93.604  1.00 35.58 ? 2318 HOH B O     1 
HETATM 19001 O O     . HOH DB 8 .    ? 33.264  28.362  52.822  1.00 34.94 ? 2319 HOH B O     1 
HETATM 19002 O O     . HOH DB 8 .    ? -0.030  40.051  77.951  1.00 25.29 ? 2320 HOH B O     1 
HETATM 19003 O O     . HOH DB 8 .    ? -5.679  40.562  62.668  1.00 34.34 ? 2321 HOH B O     1 
HETATM 19004 O O     . HOH DB 8 .    ? 28.208  29.362  83.645  1.00 24.00 ? 2322 HOH B O     1 
HETATM 19005 O O     . HOH DB 8 .    ? 18.092  52.694  66.817  1.00 35.41 ? 2323 HOH B O     1 
HETATM 19006 O O     . HOH DB 8 .    ? -4.555  50.997  78.697  1.00 36.41 ? 2324 HOH B O     1 
HETATM 19007 O O     . HOH DB 8 .    ? 33.322  17.524  89.998  1.00 33.36 ? 2325 HOH B O     1 
HETATM 19008 O O     . HOH DB 8 .    ? 27.145  34.974  91.399  1.00 26.23 ? 2326 HOH B O     1 
HETATM 19009 O O     . HOH DB 8 .    ? 2.746   49.080  76.230  1.00 20.14 ? 2327 HOH B O     1 
HETATM 19010 O O     . HOH DB 8 .    ? 10.455  49.370  55.865  1.00 37.15 ? 2328 HOH B O     1 
HETATM 19011 O O     . HOH DB 8 .    ? 12.149  7.455   90.515  1.00 29.23 ? 2329 HOH B O     1 
HETATM 19012 O O     . HOH DB 8 .    ? 4.166   29.390  84.769  1.00 23.88 ? 2330 HOH B O     1 
HETATM 19013 O O     . HOH DB 8 .    ? 2.713   30.571  80.290  1.00 21.96 ? 2331 HOH B O     1 
HETATM 19014 O O     . HOH DB 8 .    ? 15.394  3.744   98.469  1.00 41.19 ? 2332 HOH B O     1 
HETATM 19015 O O     . HOH DB 8 .    ? -2.499  35.602  101.118 1.00 43.53 ? 2333 HOH B O     1 
HETATM 19016 O O     . HOH DB 8 .    ? 34.195  46.678  98.770  1.00 57.59 ? 2334 HOH B O     1 
HETATM 19017 O O     . HOH DB 8 .    ? 15.853  48.969  57.457  1.00 28.60 ? 2335 HOH B O     1 
HETATM 19018 O O     . HOH DB 8 .    ? 20.062  32.724  67.348  1.00 19.42 ? 2336 HOH B O     1 
HETATM 19019 O O     . HOH DB 8 .    ? -2.542  21.301  91.761  1.00 21.04 ? 2337 HOH B O     1 
HETATM 19020 O O     . HOH DB 8 .    ? 5.348   3.162   92.998  1.00 28.35 ? 2338 HOH B O     1 
HETATM 19021 O O     . HOH DB 8 .    ? 18.205  68.808  84.926  1.00 35.26 ? 2339 HOH B O     1 
HETATM 19022 O O     . HOH DB 8 .    ? 12.301  21.308  101.972 1.00 40.91 ? 2340 HOH B O     1 
HETATM 19023 O O     . HOH DB 8 .    ? 22.427  53.130  67.565  1.00 32.45 ? 2341 HOH B O     1 
HETATM 19024 O O     . HOH DB 8 .    ? -5.129  51.772  75.687  1.00 25.13 ? 2342 HOH B O     1 
HETATM 19025 O O     . HOH DB 8 .    ? 12.162  38.527  47.873  1.00 36.48 ? 2343 HOH B O     1 
HETATM 19026 O O     . HOH DB 8 .    ? 31.707  31.027  71.034  1.00 38.79 ? 2344 HOH B O     1 
HETATM 19027 O O     . HOH DB 8 .    ? -10.615 1.518   91.408  1.00 31.19 ? 2345 HOH B O     1 
HETATM 19028 O O     . HOH DB 8 .    ? 1.246   10.390  129.763 1.00 32.41 ? 2346 HOH B O     1 
HETATM 19029 O O     . HOH DB 8 .    ? 1.698   13.413  104.913 1.00 23.69 ? 2347 HOH B O     1 
HETATM 19030 O O     . HOH DB 8 .    ? -1.321  38.219  80.457  1.00 31.07 ? 2348 HOH B O     1 
HETATM 19031 O O     . HOH DB 8 .    ? -3.369  52.467  82.659  1.00 33.47 ? 2349 HOH B O     1 
HETATM 19032 O O     . HOH DB 8 .    ? -29.757 18.305  103.792 1.00 46.31 ? 2350 HOH B O     1 
HETATM 19033 O O     . HOH DB 8 .    ? 25.522  54.955  62.328  1.00 28.91 ? 2351 HOH B O     1 
HETATM 19034 O O     . HOH DB 8 .    ? -3.239  24.382  104.154 1.00 41.21 ? 2352 HOH B O     1 
HETATM 19035 O O     . HOH DB 8 .    ? -0.417  56.039  86.643  1.00 39.55 ? 2353 HOH B O     1 
HETATM 19036 O O     . HOH DB 8 .    ? 2.728   70.726  64.329  1.00 40.48 ? 2354 HOH B O     1 
HETATM 19037 O O     . HOH DB 8 .    ? 11.165  20.437  120.600 1.00 40.83 ? 2355 HOH B O     1 
HETATM 19038 O O     . HOH DB 8 .    ? -4.601  10.549  100.562 1.00 28.15 ? 2356 HOH B O     1 
HETATM 19039 O O     . HOH DB 8 .    ? 22.698  23.099  84.663  1.00 22.20 ? 2357 HOH B O     1 
HETATM 19040 O O     . HOH DB 8 .    ? 14.669  41.164  77.484  1.00 26.93 ? 2358 HOH B O     1 
HETATM 19041 O O     . HOH DB 8 .    ? 1.665   20.541  89.630  1.00 30.77 ? 2359 HOH B O     1 
HETATM 19042 O O     . HOH DB 8 .    ? 5.358   42.818  71.055  1.00 16.52 ? 2360 HOH B O     1 
HETATM 19043 O O     . HOH DB 8 .    ? 25.451  29.813  109.387 1.00 39.23 ? 2361 HOH B O     1 
HETATM 19044 O O     . HOH DB 8 .    ? 18.441  15.055  97.551  1.00 29.18 ? 2362 HOH B O     1 
HETATM 19045 O O     . HOH DB 8 .    ? 15.615  9.695   89.547  1.00 24.43 ? 2363 HOH B O     1 
HETATM 19046 O O     . HOH DB 8 .    ? 4.655   55.090  120.168 1.00 49.61 ? 2364 HOH B O     1 
HETATM 19047 O O     . HOH DB 8 .    ? 3.730   19.204  60.369  1.00 33.17 ? 2365 HOH B O     1 
HETATM 19048 O O     . HOH DB 8 .    ? -11.386 20.513  88.109  1.00 30.11 ? 2366 HOH B O     1 
HETATM 19049 O O     . HOH DB 8 .    ? -15.367 -5.832  102.767 1.00 51.99 ? 2367 HOH B O     1 
HETATM 19050 O O     . HOH DB 8 .    ? 11.312  5.563   122.196 1.00 36.72 ? 2368 HOH B O     1 
HETATM 19051 O O     . HOH DB 8 .    ? 30.711  40.580  57.152  1.00 36.97 ? 2369 HOH B O     1 
HETATM 19052 O O     . HOH DB 8 .    ? 11.045  38.299  96.052  1.00 29.72 ? 2370 HOH B O     1 
HETATM 19053 O O     . HOH DB 8 .    ? -2.787  31.452  63.607  1.00 30.53 ? 2371 HOH B O     1 
HETATM 19054 O O     . HOH DB 8 .    ? 22.389  45.521  90.954  1.00 31.30 ? 2372 HOH B O     1 
HETATM 19055 O O     . HOH DB 8 .    ? -13.326 53.965  122.877 1.00 36.03 ? 2373 HOH B O     1 
HETATM 19056 O O     . HOH DB 8 .    ? -0.031  18.165  80.372  1.00 34.15 ? 2374 HOH B O     1 
HETATM 19057 O O     . HOH DB 8 .    ? 0.452   -7.471  106.866 1.00 36.66 ? 2375 HOH B O     1 
HETATM 19058 O O     . HOH DB 8 .    ? 12.592  37.325  108.145 1.00 28.36 ? 2376 HOH B O     1 
HETATM 19059 O O     . HOH DB 8 .    ? 20.048  24.304  46.028  1.00 28.32 ? 2377 HOH B O     1 
HETATM 19060 O O     . HOH DB 8 .    ? -5.810  39.182  107.030 1.00 34.40 ? 2378 HOH B O     1 
HETATM 19061 O O     . HOH DB 8 .    ? 39.872  28.893  88.386  1.00 39.07 ? 2379 HOH B O     1 
HETATM 19062 O O     . HOH DB 8 .    ? -8.020  12.326  97.225  1.00 24.10 ? 2380 HOH B O     1 
HETATM 19063 O O     . HOH DB 8 .    ? 19.223  45.689  54.426  1.00 31.43 ? 2381 HOH B O     1 
HETATM 19064 O O     . HOH DB 8 .    ? 42.672  31.985  96.989  1.00 44.75 ? 2382 HOH B O     1 
HETATM 19065 O O     . HOH DB 8 .    ? 6.645   12.110  126.664 1.00 26.67 ? 2383 HOH B O     1 
HETATM 19066 O O     . HOH DB 8 .    ? -1.309  32.746  69.261  1.00 20.38 ? 2384 HOH B O     1 
HETATM 19067 O O     . HOH DB 8 .    ? 34.668  55.099  76.167  1.00 39.55 ? 2385 HOH B O     1 
HETATM 19068 O O     . HOH DB 8 .    ? 10.594  16.507  121.911 1.00 38.65 ? 2386 HOH B O     1 
HETATM 19069 O O     . HOH DB 8 .    ? 11.966  37.424  72.495  1.00 22.71 ? 2387 HOH B O     1 
HETATM 19070 O O     . HOH DB 8 .    ? 1.221   9.094   89.740  1.00 24.32 ? 2388 HOH B O     1 
HETATM 19071 O O     . HOH DB 8 .    ? -16.149 25.752  107.022 1.00 43.47 ? 2389 HOH B O     1 
HETATM 19072 O O     . HOH DB 8 .    ? 15.370  29.005  49.313  1.00 36.91 ? 2390 HOH B O     1 
HETATM 19073 O O     . HOH DB 8 .    ? 0.873   42.064  76.475  1.00 29.83 ? 2391 HOH B O     1 
HETATM 19074 O O     . HOH DB 8 .    ? 1.200   38.639  106.074 1.00 37.44 ? 2392 HOH B O     1 
HETATM 19075 O O     . HOH DB 8 .    ? 23.426  51.806  84.084  1.00 36.68 ? 2393 HOH B O     1 
HETATM 19076 O O     . HOH DB 8 .    ? 20.875  37.329  112.925 1.00 31.94 ? 2394 HOH B O     1 
HETATM 19077 O O     . HOH DB 8 .    ? 9.140   48.937  109.462 1.00 40.33 ? 2395 HOH B O     1 
HETATM 19078 O O     . HOH DB 8 .    ? 35.217  64.300  81.687  1.00 24.34 ? 2396 HOH B O     1 
HETATM 19079 O O     . HOH DB 8 .    ? 33.895  12.103  74.491  1.00 43.93 ? 2397 HOH B O     1 
HETATM 19080 O O     . HOH DB 8 .    ? -6.268  12.478  99.429  1.00 22.82 ? 2398 HOH B O     1 
HETATM 19081 O O     . HOH DB 8 .    ? 5.387   43.532  55.771  1.00 33.51 ? 2399 HOH B O     1 
HETATM 19082 O O     . HOH DB 8 .    ? -0.614  23.884  74.193  1.00 22.79 ? 2400 HOH B O     1 
HETATM 19083 O O     . HOH DB 8 .    ? 2.013   40.545  114.921 1.00 29.01 ? 2401 HOH B O     1 
HETATM 19084 O O     . HOH DB 8 .    ? 22.845  11.562  87.698  1.00 34.49 ? 2402 HOH B O     1 
HETATM 19085 O O     . HOH DB 8 .    ? 31.969  60.081  65.769  1.00 32.96 ? 2403 HOH B O     1 
HETATM 19086 O O     . HOH DB 8 .    ? -8.159  2.204   92.509  1.00 27.87 ? 2404 HOH B O     1 
HETATM 19087 O O     . HOH DB 8 .    ? -2.050  -7.451  110.934 1.00 39.34 ? 2405 HOH B O     1 
HETATM 19088 O O     . HOH DB 8 .    ? 5.124   49.436  68.909  1.00 23.27 ? 2406 HOH B O     1 
HETATM 19089 O O     . HOH DB 8 .    ? 2.795   11.410  94.483  1.00 27.97 ? 2407 HOH B O     1 
HETATM 19090 O O     . HOH DB 8 .    ? 4.833   47.612  87.429  1.00 20.41 ? 2408 HOH B O     1 
HETATM 19091 O O     . HOH DB 8 .    ? 20.812  27.344  70.958  1.00 22.09 ? 2409 HOH B O     1 
HETATM 19092 O O     . HOH DB 8 .    ? -6.540  6.064   118.645 1.00 33.07 ? 2410 HOH B O     1 
HETATM 19093 O O     . HOH DB 8 .    ? 17.375  34.271  56.077  1.00 21.23 ? 2411 HOH B O     1 
HETATM 19094 O O     . HOH DB 8 .    ? 14.367  26.712  81.961  1.00 31.97 ? 2412 HOH B O     1 
HETATM 19095 O O     . HOH DB 8 .    ? 25.141  45.223  109.201 1.00 43.12 ? 2413 HOH B O     1 
HETATM 19096 O O     . HOH DB 8 .    ? 28.904  22.573  76.554  1.00 28.09 ? 2414 HOH B O     1 
HETATM 19097 O O     . HOH DB 8 .    ? 15.504  49.276  78.927  1.00 35.82 ? 2415 HOH B O     1 
HETATM 19098 O O     . HOH DB 8 .    ? 8.547   40.826  87.133  1.00 21.74 ? 2416 HOH B O     1 
HETATM 19099 O O     . HOH DB 8 .    ? 18.515  23.089  84.970  1.00 28.49 ? 2417 HOH B O     1 
HETATM 19100 O O     . HOH DB 8 .    ? 19.118  7.891   84.022  1.00 32.65 ? 2418 HOH B O     1 
HETATM 19101 O O     . HOH DB 8 .    ? 7.607   20.340  102.338 1.00 32.50 ? 2419 HOH B O     1 
HETATM 19102 O O     . HOH DB 8 .    ? 4.799   21.879  83.888  1.00 26.42 ? 2420 HOH B O     1 
HETATM 19103 O O     . HOH DB 8 .    ? 5.711   -7.754  117.738 1.00 37.87 ? 2421 HOH B O     1 
HETATM 19104 O O     . HOH DB 8 .    ? -0.259  17.758  91.448  1.00 25.90 ? 2422 HOH B O     1 
HETATM 19105 O O     . HOH DB 8 .    ? 6.987   28.550  53.205  1.00 31.57 ? 2423 HOH B O     1 
HETATM 19106 O O     . HOH DB 8 .    ? -2.723  26.969  60.291  1.00 35.93 ? 2424 HOH B O     1 
HETATM 19107 O O     . HOH DB 8 .    ? 33.206  18.989  87.732  1.00 26.34 ? 2425 HOH B O     1 
HETATM 19108 O O     . HOH DB 8 .    ? 8.129   31.806  93.868  1.00 29.34 ? 2426 HOH B O     1 
HETATM 19109 O O     . HOH DB 8 .    ? 28.328  12.935  85.947  1.00 30.98 ? 2427 HOH B O     1 
HETATM 19110 O O     . HOH DB 8 .    ? 3.014   35.535  121.862 1.00 40.90 ? 2428 HOH B O     1 
HETATM 19111 O O     . HOH DB 8 .    ? 20.025  43.529  88.246  1.00 24.75 ? 2429 HOH B O     1 
HETATM 19112 O O     . HOH DB 8 .    ? 22.736  54.221  93.376  1.00 33.23 ? 2430 HOH B O     1 
HETATM 19113 O O     . HOH DB 8 .    ? -13.583 12.431  93.982  1.00 27.77 ? 2431 HOH B O     1 
HETATM 19114 O O     . HOH DB 8 .    ? -6.401  0.271   86.168  1.00 36.85 ? 2432 HOH B O     1 
HETATM 19115 O O     . HOH DB 8 .    ? -6.005  34.608  84.009  1.00 27.23 ? 2433 HOH B O     1 
HETATM 19116 O O     . HOH DB 8 .    ? 20.767  22.765  86.855  1.00 28.08 ? 2434 HOH B O     1 
HETATM 19117 O O     . HOH DB 8 .    ? 15.510  38.494  77.287  1.00 31.96 ? 2435 HOH B O     1 
HETATM 19118 O O     . HOH DB 8 .    ? 27.220  22.803  88.780  1.00 24.94 ? 2436 HOH B O     1 
HETATM 19119 O O     . HOH DB 8 .    ? -13.701 11.669  91.244  1.00 25.00 ? 2437 HOH B O     1 
HETATM 19120 O O     . HOH DB 8 .    ? 19.858  50.174  69.044  1.00 41.15 ? 2438 HOH B O     1 
HETATM 19121 O O     . HOH DB 8 .    ? 30.513  35.033  50.417  1.00 42.89 ? 2439 HOH B O     1 
HETATM 19122 O O     . HOH DB 8 .    ? 19.046  30.626  88.854  1.00 23.57 ? 2440 HOH B O     1 
HETATM 19123 O O     . HOH DB 8 .    ? 0.212   12.176  93.745  1.00 20.85 ? 2441 HOH B O     1 
HETATM 19124 O O     . HOH DB 8 .    ? 17.349  40.665  71.726  1.00 22.36 ? 2442 HOH B O     1 
HETATM 19125 O O     . HOH DB 8 .    ? 9.131   62.139  85.568  1.00 31.08 ? 2443 HOH B O     1 
HETATM 19126 O O     . HOH DB 8 .    ? -1.938  11.011  101.461 1.00 26.10 ? 2444 HOH B O     1 
HETATM 19127 O O     . HOH DB 8 .    ? 9.049   3.504   80.967  1.00 30.88 ? 2445 HOH B O     1 
HETATM 19128 O O     . HOH DB 8 .    ? -4.369  53.934  131.439 1.00 42.47 ? 2446 HOH B O     1 
HETATM 19129 O O     . HOH DB 8 .    ? 11.815  49.885  88.785  1.00 29.19 ? 2447 HOH B O     1 
HETATM 19130 O O     . HOH DB 8 .    ? 25.191  51.246  66.988  1.00 30.43 ? 2448 HOH B O     1 
HETATM 19131 O O     . HOH DB 8 .    ? 1.368   14.918  82.435  1.00 23.37 ? 2449 HOH B O     1 
HETATM 19132 O O     . HOH DB 8 .    ? 26.723  39.960  52.881  1.00 33.89 ? 2450 HOH B O     1 
HETATM 19133 O O     . HOH DB 8 .    ? -5.175  40.037  72.497  1.00 32.89 ? 2451 HOH B O     1 
HETATM 19134 O O     . HOH DB 8 .    ? 21.847  7.031   83.304  1.00 39.31 ? 2452 HOH B O     1 
HETATM 19135 O O     . HOH DB 8 .    ? 18.686  67.380  58.624  1.00 34.32 ? 2453 HOH B O     1 
HETATM 19136 O O     . HOH DB 8 .    ? 10.046  71.404  62.055  1.00 40.98 ? 2454 HOH B O     1 
HETATM 19137 O O     . HOH DB 8 .    ? 14.775  22.064  101.911 1.00 37.24 ? 2455 HOH B O     1 
HETATM 19138 O O     . HOH DB 8 .    ? -0.417  27.117  68.557  1.00 21.73 ? 2456 HOH B O     1 
HETATM 19139 O O     . HOH DB 8 .    ? 8.483   14.813  90.470  1.00 31.97 ? 2457 HOH B O     1 
HETATM 19140 O O     . HOH DB 8 .    ? -25.159 16.745  82.474  1.00 37.60 ? 2458 HOH B O     1 
HETATM 19141 O O     . HOH DB 8 .    ? -3.660  30.370  95.245  1.00 36.08 ? 2459 HOH B O     1 
HETATM 19142 O O     . HOH DB 8 .    ? 27.011  21.245  75.073  1.00 26.88 ? 2460 HOH B O     1 
HETATM 19143 O O     . HOH DB 8 .    ? 18.945  62.289  57.647  1.00 32.75 ? 2461 HOH B O     1 
HETATM 19144 O O     . HOH DB 8 .    ? -9.810  5.766   87.031  1.00 33.26 ? 2462 HOH B O     1 
HETATM 19145 O O     . HOH DB 8 .    ? -14.606 23.906  108.594 1.00 38.62 ? 2463 HOH B O     1 
HETATM 19146 O O     . HOH DB 8 .    ? 23.810  16.883  82.593  1.00 29.01 ? 2464 HOH B O     1 
HETATM 19147 O O     . HOH DB 8 .    ? 7.850   56.830  87.964  1.00 34.64 ? 2465 HOH B O     1 
HETATM 19148 O O     . HOH DB 8 .    ? 5.911   15.031  94.851  1.00 28.29 ? 2466 HOH B O     1 
HETATM 19149 O O     . HOH DB 8 .    ? 18.627  6.984   100.881 1.00 41.39 ? 2467 HOH B O     1 
HETATM 19150 O O     . HOH DB 8 .    ? 11.727  41.640  54.738  1.00 24.48 ? 2468 HOH B O     1 
HETATM 19151 O O     . HOH DB 8 .    ? 33.576  26.023  58.879  1.00 34.25 ? 2469 HOH B O     1 
HETATM 19152 O O     . HOH DB 8 .    ? 23.487  32.547  91.861  1.00 22.12 ? 2470 HOH B O     1 
HETATM 19153 O O     . HOH DB 8 .    ? 27.384  18.108  61.764  1.00 34.29 ? 2471 HOH B O     1 
HETATM 19154 O O     . HOH DB 8 .    ? 1.955   30.677  96.181  1.00 26.05 ? 2472 HOH B O     1 
HETATM 19155 O O     . HOH DB 8 .    ? 7.881   62.959  66.736  1.00 37.90 ? 2473 HOH B O     1 
HETATM 19156 O O     . HOH DB 8 .    ? 12.007  20.959  58.801  1.00 19.72 ? 2474 HOH B O     1 
HETATM 19157 O O     . HOH DB 8 .    ? 10.255  2.139   117.472 1.00 34.26 ? 2475 HOH B O     1 
HETATM 19158 O O     . HOH DB 8 .    ? 13.638  18.456  87.247  1.00 29.77 ? 2476 HOH B O     1 
HETATM 19159 O O     . HOH DB 8 .    ? -1.202  20.588  89.607  1.00 23.76 ? 2477 HOH B O     1 
HETATM 19160 O O     . HOH DB 8 .    ? 5.660   35.987  49.071  1.00 43.03 ? 2478 HOH B O     1 
HETATM 19161 O O     . HOH DB 8 .    ? 8.602   15.603  92.807  1.00 28.58 ? 2479 HOH B O     1 
HETATM 19162 O O     . HOH DB 8 .    ? -1.811  25.326  79.958  1.00 26.49 ? 2480 HOH B O     1 
HETATM 19163 O O     . HOH DB 8 .    ? -2.476  14.338  98.886  1.00 21.27 ? 2481 HOH B O     1 
HETATM 19164 O O     . HOH DB 8 .    ? 20.742  18.964  60.347  1.00 25.63 ? 2482 HOH B O     1 
HETATM 19165 O O     . HOH DB 8 .    ? -1.108  55.805  122.307 1.00 34.74 ? 2483 HOH B O     1 
HETATM 19166 O O     . HOH DB 8 .    ? 31.883  59.627  72.511  1.00 28.99 ? 2484 HOH B O     1 
HETATM 19167 O O     . HOH DB 8 .    ? -10.453 31.812  80.406  1.00 41.22 ? 2485 HOH B O     1 
HETATM 19168 O O     . HOH DB 8 .    ? 2.524   63.509  78.576  1.00 22.19 ? 2486 HOH B O     1 
HETATM 19169 O O     . HOH DB 8 .    ? 22.987  37.248  86.427  1.00 29.69 ? 2487 HOH B O     1 
HETATM 19170 O O     . HOH DB 8 .    ? 31.392  10.173  95.729  1.00 44.04 ? 2488 HOH B O     1 
HETATM 19171 O O     . HOH DB 8 .    ? 5.070   57.865  69.245  1.00 25.24 ? 2489 HOH B O     1 
HETATM 19172 O O     . HOH DB 8 .    ? 26.308  8.053   75.813  1.00 39.72 ? 2490 HOH B O     1 
HETATM 19173 O O     . HOH DB 8 .    ? -15.527 10.220  90.093  1.00 25.96 ? 2491 HOH B O     1 
HETATM 19174 O O     . HOH DB 8 .    ? 1.482   22.719  63.277  1.00 31.83 ? 2492 HOH B O     1 
HETATM 19175 O O     . HOH DB 8 .    ? 25.373  13.380  65.246  1.00 36.15 ? 2493 HOH B O     1 
HETATM 19176 O O     . HOH DB 8 .    ? -1.981  -9.516  109.178 1.00 37.12 ? 2494 HOH B O     1 
HETATM 19177 O O     . HOH DB 8 .    ? 24.214  18.798  98.660  1.00 39.61 ? 2495 HOH B O     1 
HETATM 19178 O O     . HOH DB 8 .    ? 37.571  22.810  84.430  1.00 38.89 ? 2496 HOH B O     1 
HETATM 19179 O O     . HOH DB 8 .    ? 19.496  28.605  82.336  1.00 28.91 ? 2497 HOH B O     1 
HETATM 19180 O O     . HOH DB 8 .    ? 0.411   27.008  94.917  1.00 22.88 ? 2498 HOH B O     1 
HETATM 19181 O O     . HOH DB 8 .    ? -2.944  10.750  103.945 1.00 27.90 ? 2499 HOH B O     1 
HETATM 19182 O O     . HOH DB 8 .    ? 5.595   7.096   94.318  1.00 28.41 ? 2500 HOH B O     1 
HETATM 19183 O O     . HOH DB 8 .    ? 18.047  23.872  110.763 1.00 34.69 ? 2501 HOH B O     1 
HETATM 19184 O O     . HOH DB 8 .    ? 6.542   31.867  79.510  1.00 23.59 ? 2502 HOH B O     1 
HETATM 19185 O O     . HOH DB 8 .    ? -22.594 25.888  103.800 1.00 42.13 ? 2503 HOH B O     1 
HETATM 19186 O O     . HOH DB 8 .    ? -0.985  67.048  84.433  1.00 35.26 ? 2504 HOH B O     1 
HETATM 19187 O O     . HOH DB 8 .    ? 2.070   20.307  92.544  1.00 36.23 ? 2505 HOH B O     1 
HETATM 19188 O O     . HOH DB 8 .    ? 0.203   47.861  76.791  1.00 23.01 ? 2506 HOH B O     1 
HETATM 19189 O O     . HOH DB 8 .    ? 8.013   58.151  85.778  1.00 27.60 ? 2507 HOH B O     1 
HETATM 19190 O O     . HOH DB 8 .    ? -10.535 10.776  130.340 1.00 50.74 ? 2508 HOH B O     1 
HETATM 19191 O O     . HOH DB 8 .    ? 26.888  20.091  54.505  1.00 37.20 ? 2509 HOH B O     1 
HETATM 19192 O O     . HOH DB 8 .    ? 12.199  29.292  83.133  1.00 36.74 ? 2510 HOH B O     1 
HETATM 19193 O O     . HOH DB 8 .    ? 3.676   33.737  93.135  1.00 24.11 ? 2511 HOH B O     1 
HETATM 19194 O O     . HOH DB 8 .    ? -14.294 9.205   87.529  1.00 34.98 ? 2512 HOH B O     1 
HETATM 19195 O O     . HOH DB 8 .    ? 28.553  25.142  67.548  1.00 22.62 ? 2513 HOH B O     1 
HETATM 19196 O O     . HOH DB 8 .    ? 27.146  38.451  105.288 1.00 38.08 ? 2514 HOH B O     1 
HETATM 19197 O O     . HOH DB 8 .    ? 14.836  42.591  75.293  1.00 30.23 ? 2515 HOH B O     1 
HETATM 19198 O O     . HOH DB 8 .    ? 4.958   18.655  124.125 1.00 38.45 ? 2516 HOH B O     1 
HETATM 19199 O O     . HOH DB 8 .    ? -9.031  45.254  108.982 1.00 36.86 ? 2517 HOH B O     1 
HETATM 19200 O O     . HOH DB 8 .    ? 12.556  5.628   84.505  1.00 30.41 ? 2518 HOH B O     1 
HETATM 19201 O O     . HOH DB 8 .    ? 13.158  48.268  82.338  1.00 33.55 ? 2519 HOH B O     1 
HETATM 19202 O O     . HOH DB 8 .    ? 14.265  46.159  106.599 1.00 32.79 ? 2520 HOH B O     1 
HETATM 19203 O O     . HOH DB 8 .    ? 20.949  4.643   67.900  1.00 43.00 ? 2521 HOH B O     1 
HETATM 19204 O O     . HOH DB 8 .    ? 7.563   43.347  49.768  1.00 34.05 ? 2522 HOH B O     1 
HETATM 19205 O O     . HOH DB 8 .    ? 14.121  72.864  61.386  1.00 37.09 ? 2523 HOH B O     1 
HETATM 19206 O O     . HOH DB 8 .    ? 27.344  41.859  105.556 1.00 39.80 ? 2524 HOH B O     1 
HETATM 19207 O O     . HOH DB 8 .    ? 29.476  65.554  62.846  1.00 37.40 ? 2525 HOH B O     1 
HETATM 19208 O O     . HOH DB 8 .    ? -22.582 20.632  88.512  1.00 36.52 ? 2526 HOH B O     1 
HETATM 19209 O O     . HOH DB 8 .    ? -4.699  37.906  93.647  1.00 38.64 ? 2527 HOH B O     1 
HETATM 19210 O O     . HOH DB 8 .    ? 17.401  54.818  97.679  1.00 31.59 ? 2528 HOH B O     1 
HETATM 19211 O O     . HOH DB 8 .    ? 3.079   31.218  98.551  1.00 29.08 ? 2529 HOH B O     1 
HETATM 19212 O O     . HOH DB 8 .    ? 23.458  12.109  67.958  1.00 28.80 ? 2530 HOH B O     1 
HETATM 19213 O O     . HOH DB 8 .    ? 7.814   54.417  64.662  1.00 35.07 ? 2531 HOH B O     1 
HETATM 19214 O O     . HOH DB 8 .    ? -4.946  42.668  72.947  1.00 35.04 ? 2532 HOH B O     1 
HETATM 19215 O O     . HOH DB 8 .    ? 20.954  21.653  60.754  1.00 20.70 ? 2533 HOH B O     1 
HETATM 19216 O O     . HOH DB 8 .    ? -7.059  27.973  74.466  1.00 36.87 ? 2534 HOH B O     1 
HETATM 19217 O O     . HOH DB 8 .    ? 4.907   46.834  69.373  1.00 19.89 ? 2535 HOH B O     1 
HETATM 19218 O O     . HOH DB 8 .    ? -5.519  22.968  80.697  1.00 26.38 ? 2536 HOH B O     1 
HETATM 19219 O O     . HOH DB 8 .    ? 4.856   61.163  68.246  1.00 41.68 ? 2537 HOH B O     1 
HETATM 19220 O O     . HOH DB 8 .    ? -5.296  9.509   115.287 1.00 31.91 ? 2538 HOH B O     1 
HETATM 19221 O O     . HOH DB 8 .    ? 2.503   42.329  54.206  1.00 33.41 ? 2539 HOH B O     1 
HETATM 19222 O O     . HOH DB 8 .    ? 34.197  36.861  83.469  1.00 53.16 ? 2540 HOH B O     1 
HETATM 19223 O O     . HOH DB 8 .    ? 25.748  53.852  74.193  1.00 26.60 ? 2541 HOH B O     1 
HETATM 19224 O O     . HOH DB 8 .    ? 30.510  23.558  103.615 1.00 44.32 ? 2542 HOH B O     1 
HETATM 19225 O O     . HOH DB 8 .    ? 8.048   13.522  71.598  1.00 29.62 ? 2543 HOH B O     1 
HETATM 19226 O O     . HOH DB 8 .    ? -0.923  13.423  100.843 1.00 24.40 ? 2544 HOH B O     1 
HETATM 19227 O O     . HOH DB 8 .    ? -1.147  67.625  75.811  1.00 38.81 ? 2545 HOH B O     1 
HETATM 19228 O O     . HOH DB 8 .    ? -10.622 36.468  76.659  1.00 38.04 ? 2546 HOH B O     1 
HETATM 19229 O O     . HOH DB 8 .    ? 24.580  15.899  95.486  1.00 32.63 ? 2547 HOH B O     1 
HETATM 19230 O O     . HOH DB 8 .    ? 5.970   17.299  96.134  1.00 38.17 ? 2548 HOH B O     1 
HETATM 19231 O O     . HOH DB 8 .    ? 9.897   23.590  121.947 1.00 38.94 ? 2549 HOH B O     1 
HETATM 19232 O O     . HOH DB 8 .    ? 3.391   44.363  58.531  1.00 36.98 ? 2550 HOH B O     1 
HETATM 19233 O O     . HOH DB 8 .    ? -6.747  44.130  73.923  1.00 33.01 ? 2551 HOH B O     1 
HETATM 19234 O O     . HOH DB 8 .    ? 34.197  22.516  78.151  1.00 30.22 ? 2552 HOH B O     1 
HETATM 19235 O O     . HOH DB 8 .    ? -11.962 21.829  85.706  1.00 32.19 ? 2553 HOH B O     1 
HETATM 19236 O O     . HOH DB 8 .    ? -25.248 10.459  87.355  1.00 38.13 ? 2554 HOH B O     1 
HETATM 19237 O O     . HOH DB 8 .    ? -15.975 4.121   92.737  1.00 42.66 ? 2555 HOH B O     1 
HETATM 19238 O O     . HOH DB 8 .    ? 32.107  53.891  68.189  1.00 34.63 ? 2556 HOH B O     1 
HETATM 19239 O O     . HOH DB 8 .    ? -2.765  33.897  62.663  1.00 23.94 ? 2557 HOH B O     1 
HETATM 19240 O O     . HOH DB 8 .    ? 11.295  24.688  108.694 1.00 39.96 ? 2558 HOH B O     1 
HETATM 19241 O O     . HOH DB 8 .    ? 4.405   77.894  63.652  1.00 40.87 ? 2559 HOH B O     1 
HETATM 19242 O O     . HOH DB 8 .    ? -2.040  36.832  87.778  1.00 25.19 ? 2560 HOH B O     1 
HETATM 19243 O O     . HOH DB 8 .    ? -16.484 21.676  82.655  1.00 36.77 ? 2561 HOH B O     1 
HETATM 19244 O O     . HOH DB 8 .    ? -1.916  57.877  75.263  1.00 21.64 ? 2562 HOH B O     1 
HETATM 19245 O O     . HOH DB 8 .    ? 31.405  67.242  82.594  1.00 40.22 ? 2563 HOH B O     1 
HETATM 19246 O O     . HOH DB 8 .    ? -21.872 32.318  101.177 1.00 47.29 ? 2564 HOH B O     1 
HETATM 19247 O O     . HOH DB 8 .    ? -5.584  46.809  84.412  1.00 32.50 ? 2565 HOH B O     1 
HETATM 19248 O O     . HOH DB 8 .    ? 36.751  19.755  90.120  1.00 45.10 ? 2566 HOH B O     1 
HETATM 19249 O O     . HOH DB 8 .    ? 26.610  27.223  67.056  1.00 23.64 ? 2567 HOH B O     1 
HETATM 19250 O O     . HOH DB 8 .    ? 25.554  35.108  73.583  1.00 35.39 ? 2568 HOH B O     1 
HETATM 19251 O O     . HOH DB 8 .    ? 19.185  54.372  104.942 1.00 32.72 ? 2569 HOH B O     1 
HETATM 19252 O O     . HOH DB 8 .    ? 4.600   -0.027  86.716  1.00 41.04 ? 2570 HOH B O     1 
HETATM 19253 O O     . HOH DB 8 .    ? -14.566 5.792   117.966 1.00 38.36 ? 2571 HOH B O     1 
HETATM 19254 O O     . HOH DB 8 .    ? 17.777  33.968  68.466  1.00 19.12 ? 2572 HOH B O     1 
HETATM 19255 O O     . HOH DB 8 .    ? 16.066  56.170  64.181  1.00 25.55 ? 2573 HOH B O     1 
HETATM 19256 O O     . HOH DB 8 .    ? 25.033  57.477  78.267  1.00 26.01 ? 2574 HOH B O     1 
HETATM 19257 O O     . HOH DB 8 .    ? 31.168  33.979  85.440  1.00 34.96 ? 2575 HOH B O     1 
HETATM 19258 O O     . HOH DB 8 .    ? 2.576   53.961  69.594  1.00 34.06 ? 2576 HOH B O     1 
HETATM 19259 O O     . HOH DB 8 .    ? 10.419  67.013  86.875  1.00 41.80 ? 2577 HOH B O     1 
HETATM 19260 O O     . HOH DB 8 .    ? 23.055  11.052  90.215  1.00 42.22 ? 2578 HOH B O     1 
HETATM 19261 O O     . HOH DB 8 .    ? 29.144  31.278  70.929  1.00 31.49 ? 2579 HOH B O     1 
HETATM 19262 O O     . HOH DB 8 .    ? -13.856 48.990  111.232 1.00 34.70 ? 2580 HOH B O     1 
HETATM 19263 O O     . HOH DB 8 .    ? -3.260  -2.771  85.234  1.00 45.67 ? 2581 HOH B O     1 
HETATM 19264 O O     . HOH DB 8 .    ? 26.029  33.175  70.574  1.00 34.85 ? 2582 HOH B O     1 
HETATM 19265 O O     . HOH DB 8 .    ? 16.775  51.256  60.916  1.00 31.27 ? 2583 HOH B O     1 
HETATM 19266 O O     . HOH DB 8 .    ? -10.057 18.381  131.398 1.00 45.22 ? 2584 HOH B O     1 
HETATM 19267 O O     . HOH DB 8 .    ? 24.885  63.446  54.644  1.00 41.95 ? 2585 HOH B O     1 
HETATM 19268 O O     . HOH DB 8 .    ? 34.436  37.687  61.469  1.00 39.76 ? 2586 HOH B O     1 
HETATM 19269 O O     . HOH DB 8 .    ? 25.001  23.907  81.825  1.00 21.91 ? 2587 HOH B O     1 
HETATM 19270 O O     . HOH DB 8 .    ? 11.557  26.611  51.924  1.00 28.01 ? 2588 HOH B O     1 
HETATM 19271 O O     . HOH DB 8 .    ? -1.276  49.446  101.236 1.00 34.69 ? 2589 HOH B O     1 
HETATM 19272 O O     . HOH DB 8 .    ? 29.775  60.366  59.078  1.00 37.40 ? 2590 HOH B O     1 
HETATM 19273 O O     . HOH DB 8 .    ? -6.233  35.631  93.143  1.00 37.83 ? 2591 HOH B O     1 
HETATM 19274 O O     . HOH DB 8 .    ? 0.100   19.246  94.024  1.00 24.56 ? 2592 HOH B O     1 
HETATM 19275 O O     . HOH DB 8 .    ? 8.455   37.372  79.599  1.00 24.16 ? 2593 HOH B O     1 
HETATM 19276 O O     . HOH DB 8 .    ? 19.725  79.782  68.915  1.00 39.55 ? 2594 HOH B O     1 
HETATM 19277 O O     . HOH DB 8 .    ? 27.380  58.851  78.955  1.00 30.37 ? 2595 HOH B O     1 
HETATM 19278 O O     . HOH DB 8 .    ? 12.156  70.817  61.230  1.00 40.73 ? 2596 HOH B O     1 
HETATM 19279 O O     . HOH DB 8 .    ? 33.024  28.551  64.432  1.00 35.49 ? 2597 HOH B O     1 
HETATM 19280 O O     . HOH DB 8 .    ? 10.172  33.343  109.926 1.00 31.16 ? 2598 HOH B O     1 
HETATM 19281 O O     . HOH DB 8 .    ? 14.418  75.904  63.164  1.00 35.49 ? 2599 HOH B O     1 
HETATM 19282 O O     . HOH DB 8 .    ? 4.888   56.352  75.175  1.00 20.44 ? 2600 HOH B O     1 
HETATM 19283 O O     . HOH DB 8 .    ? 23.263  51.365  65.608  1.00 30.09 ? 2601 HOH B O     1 
HETATM 19284 O O     . HOH DB 8 .    ? 3.279   45.094  67.963  1.00 23.04 ? 2602 HOH B O     1 
HETATM 19285 O O     . HOH DB 8 .    ? 18.494  35.208  113.397 1.00 37.33 ? 2603 HOH B O     1 
HETATM 19286 O O     . HOH DB 8 .    ? 16.887  46.236  54.394  1.00 38.50 ? 2604 HOH B O     1 
HETATM 19287 O O     . HOH DB 8 .    ? 0.557   28.209  121.939 1.00 50.15 ? 2605 HOH B O     1 
HETATM 19288 O O     . HOH DB 8 .    ? -7.414  10.236  113.011 1.00 30.85 ? 2606 HOH B O     1 
HETATM 19289 O O     . HOH DB 8 .    ? 9.486   28.904  98.652  1.00 36.25 ? 2607 HOH B O     1 
HETATM 19290 O O     . HOH DB 8 .    ? 16.597  44.112  76.456  1.00 30.73 ? 2608 HOH B O     1 
HETATM 19291 O O     . HOH DB 8 .    ? -5.030  16.243  96.961  1.00 22.19 ? 2609 HOH B O     1 
HETATM 19292 O O     . HOH DB 8 .    ? 7.798   65.889  68.942  1.00 36.74 ? 2610 HOH B O     1 
HETATM 19293 O O     . HOH DB 8 .    ? -19.394 -3.300  105.917 1.00 47.47 ? 2611 HOH B O     1 
HETATM 19294 O O     . HOH DB 8 .    ? 15.951  53.360  105.456 1.00 33.57 ? 2612 HOH B O     1 
HETATM 19295 O O     . HOH DB 8 .    ? -19.749 28.861  88.280  1.00 37.71 ? 2613 HOH B O     1 
HETATM 19296 O O     . HOH DB 8 .    ? 12.384  45.597  111.720 1.00 43.96 ? 2614 HOH B O     1 
HETATM 19297 O O     . HOH DB 8 .    ? -2.836  40.056  57.948  1.00 28.42 ? 2615 HOH B O     1 
HETATM 19298 O O     . HOH DB 8 .    ? 18.303  22.794  61.170  1.00 25.30 ? 2616 HOH B O     1 
HETATM 19299 O O     . HOH DB 8 .    ? 12.006  25.903  102.265 1.00 40.61 ? 2617 HOH B O     1 
HETATM 19300 O O     . HOH DB 8 .    ? 22.443  25.688  79.569  1.00 30.97 ? 2618 HOH B O     1 
HETATM 19301 O O     . HOH DB 8 .    ? 10.104  53.378  65.864  1.00 32.04 ? 2619 HOH B O     1 
HETATM 19302 O O     . HOH DB 8 .    ? 22.733  61.729  83.221  1.00 35.56 ? 2620 HOH B O     1 
HETATM 19303 O O     . HOH DB 8 .    ? -7.327  13.037  94.696  1.00 27.67 ? 2621 HOH B O     1 
HETATM 19304 O O     . HOH DB 8 .    ? -3.719  45.855  107.176 1.00 29.29 ? 2622 HOH B O     1 
HETATM 19305 O O     . HOH DB 8 .    ? 27.887  10.318  84.870  1.00 37.53 ? 2623 HOH B O     1 
HETATM 19306 O O     . HOH DB 8 .    ? 13.455  58.059  94.188  1.00 42.67 ? 2624 HOH B O     1 
HETATM 19307 O O     . HOH DB 8 .    ? -7.542  24.010  125.645 1.00 45.20 ? 2625 HOH B O     1 
HETATM 19308 O O     . HOH DB 8 .    ? -3.599  66.974  72.034  1.00 43.67 ? 2626 HOH B O     1 
HETATM 19309 O O     . HOH DB 8 .    ? 11.585  25.804  86.207  1.00 40.13 ? 2627 HOH B O     1 
HETATM 19310 O O     . HOH DB 8 .    ? 18.634  53.042  76.297  1.00 35.72 ? 2628 HOH B O     1 
HETATM 19311 O O     . HOH DB 8 .    ? 19.427  58.636  82.764  1.00 24.90 ? 2629 HOH B O     1 
HETATM 19312 O O     . HOH DB 8 .    ? 33.279  69.368  73.348  1.00 38.60 ? 2630 HOH B O     1 
HETATM 19313 O O     . HOH DB 8 .    ? 14.739  9.002   93.667  1.00 28.19 ? 2631 HOH B O     1 
HETATM 19314 O O     . HOH DB 8 .    ? 13.386  22.453  114.211 1.00 39.32 ? 2632 HOH B O     1 
HETATM 19315 O O     . HOH DB 8 .    ? 25.357  53.564  68.680  1.00 27.52 ? 2633 HOH B O     1 
HETATM 19316 O O     . HOH DB 8 .    ? -10.836 11.912  79.829  1.00 47.57 ? 2634 HOH B O     1 
HETATM 19317 O O     . HOH DB 8 .    ? -5.062  -4.150  91.830  1.00 40.96 ? 2635 HOH B O     1 
HETATM 19318 O O     . HOH DB 8 .    ? 16.367  21.531  100.067 1.00 29.88 ? 2636 HOH B O     1 
HETATM 19319 O O     . HOH DB 8 .    ? 31.241  19.608  55.829  1.00 39.00 ? 2637 HOH B O     1 
HETATM 19320 O O     . HOH DB 8 .    ? -2.855  64.712  83.603  1.00 23.11 ? 2638 HOH B O     1 
HETATM 19321 O O     . HOH DB 8 .    ? 35.640  25.261  77.978  1.00 30.42 ? 2639 HOH B O     1 
HETATM 19322 O O     . HOH DB 8 .    ? -1.059  37.648  76.370  1.00 33.01 ? 2640 HOH B O     1 
HETATM 19323 O O     . HOH DB 8 .    ? -2.518  63.044  85.516  1.00 29.70 ? 2641 HOH B O     1 
HETATM 19324 O O     . HOH DB 8 .    ? 12.792  53.252  61.859  1.00 40.25 ? 2642 HOH B O     1 
HETATM 19325 O O     . HOH DB 8 .    ? 28.685  41.904  53.451  1.00 41.67 ? 2643 HOH B O     1 
HETATM 19326 O O     . HOH DB 8 .    ? 19.215  14.296  105.481 1.00 39.12 ? 2644 HOH B O     1 
HETATM 19327 O O     . HOH DB 8 .    ? 15.979  38.066  74.878  1.00 24.07 ? 2645 HOH B O     1 
HETATM 19328 O O     . HOH DB 8 .    ? 26.257  20.104  52.202  1.00 35.05 ? 2646 HOH B O     1 
HETATM 19329 O O     . HOH DB 8 .    ? -5.880  15.317  94.612  1.00 19.28 ? 2647 HOH B O     1 
HETATM 19330 O O     . HOH DB 8 .    ? 17.475  33.790  48.533  1.00 33.47 ? 2648 HOH B O     1 
HETATM 19331 O O     . HOH DB 8 .    ? -23.077 20.986  102.377 1.00 40.88 ? 2649 HOH B O     1 
HETATM 19332 O O     . HOH DB 8 .    ? 4.683   17.833  91.097  1.00 34.41 ? 2650 HOH B O     1 
HETATM 19333 O O     . HOH DB 8 .    ? -2.422  30.760  70.676  1.00 21.83 ? 2651 HOH B O     1 
HETATM 19334 O O     . HOH DB 8 .    ? -5.237  37.385  86.470  1.00 34.42 ? 2652 HOH B O     1 
HETATM 19335 O O     . HOH DB 8 .    ? -1.172  17.280  82.625  1.00 30.42 ? 2653 HOH B O     1 
HETATM 19336 O O     . HOH DB 8 .    ? 18.123  77.188  64.181  1.00 39.78 ? 2654 HOH B O     1 
HETATM 19337 O O     . HOH DB 8 .    ? 1.504   46.465  99.074  1.00 36.61 ? 2655 HOH B O     1 
HETATM 19338 O O     . HOH DB 8 .    ? 25.943  12.659  91.071  1.00 43.62 ? 2656 HOH B O     1 
HETATM 19339 O O     . HOH DB 8 .    ? 21.256  62.882  54.094  1.00 37.56 ? 2657 HOH B O     1 
HETATM 19340 O O     . HOH DB 8 .    ? 35.044  13.056  81.076  1.00 39.45 ? 2658 HOH B O     1 
HETATM 19341 O O     . HOH DB 8 .    ? 13.959  45.744  78.811  1.00 34.03 ? 2659 HOH B O     1 
HETATM 19342 O O     . HOH DB 8 .    ? -15.841 8.521   85.841  1.00 41.08 ? 2660 HOH B O     1 
HETATM 19343 O O     . HOH DB 8 .    ? 26.461  12.451  88.049  1.00 33.66 ? 2661 HOH B O     1 
HETATM 19344 O O     . HOH DB 8 .    ? 22.164  14.360  81.169  1.00 32.51 ? 2662 HOH B O     1 
HETATM 19345 O O     . HOH DB 8 .    ? 34.007  33.143  70.295  1.00 42.02 ? 2663 HOH B O     1 
HETATM 19346 O O     . HOH DB 8 .    ? 13.513  3.094   84.345  1.00 45.41 ? 2664 HOH B O     1 
HETATM 19347 O O     . HOH DB 8 .    ? -16.097 52.629  124.235 1.00 42.11 ? 2665 HOH B O     1 
HETATM 19348 O O     . HOH DB 8 .    ? 8.322   35.668  110.393 1.00 45.34 ? 2666 HOH B O     1 
HETATM 19349 O O     . HOH DB 8 .    ? 13.548  52.939  106.112 1.00 46.96 ? 2667 HOH B O     1 
HETATM 19350 O O     . HOH DB 8 .    ? -6.661  39.009  67.496  1.00 38.70 ? 2668 HOH B O     1 
HETATM 19351 O O     . HOH DB 8 .    ? 2.795   23.311  58.953  1.00 35.88 ? 2669 HOH B O     1 
HETATM 19352 O O     . HOH DB 8 .    ? -0.527  14.635  131.173 1.00 36.38 ? 2670 HOH B O     1 
HETATM 19353 O O     . HOH DB 8 .    ? 13.215  25.444  96.704  1.00 38.31 ? 2671 HOH B O     1 
HETATM 19354 O O     . HOH DB 8 .    ? -4.538  -0.293  110.650 1.00 33.76 ? 2672 HOH B O     1 
HETATM 19355 O O     . HOH DB 8 .    ? 15.104  21.116  89.084  1.00 39.41 ? 2673 HOH B O     1 
HETATM 19356 O O     . HOH DB 8 .    ? 12.947  29.485  50.493  1.00 27.71 ? 2674 HOH B O     1 
HETATM 19357 O O     . HOH DB 8 .    ? -15.342 19.548  82.652  1.00 33.42 ? 2675 HOH B O     1 
HETATM 19358 O O     . HOH DB 8 .    ? 20.434  20.362  109.462 1.00 30.79 ? 2676 HOH B O     1 
HETATM 19359 O O     . HOH DB 8 .    ? -16.568 26.962  82.726  1.00 40.78 ? 2677 HOH B O     1 
HETATM 19360 O O     . HOH DB 8 .    ? -2.606  -5.834  89.589  1.00 38.06 ? 2678 HOH B O     1 
HETATM 19361 O O     . HOH DB 8 .    ? 30.918  41.236  79.788  1.00 39.48 ? 2679 HOH B O     1 
HETATM 19362 O O     . HOH DB 8 .    ? 29.806  29.272  105.804 1.00 42.96 ? 2680 HOH B O     1 
HETATM 19363 O O     . HOH DB 8 .    ? 7.832   77.397  86.525  1.00 42.37 ? 2681 HOH B O     1 
HETATM 19364 O O     . HOH DB 8 .    ? 2.296   24.558  129.535 1.00 47.14 ? 2682 HOH B O     1 
HETATM 19365 O O     . HOH DB 8 .    ? -4.099  26.532  100.017 1.00 30.01 ? 2683 HOH B O     1 
HETATM 19366 O O     . HOH DB 8 .    ? 33.155  9.482   74.400  1.00 44.73 ? 2684 HOH B O     1 
HETATM 19367 O O     . HOH DB 8 .    ? 22.731  46.424  76.921  1.00 36.63 ? 2685 HOH B O     1 
HETATM 19368 O O     . HOH DB 8 .    ? -6.893  45.697  81.751  1.00 51.12 ? 2686 HOH B O     1 
HETATM 19369 O O     . HOH DB 8 .    ? -28.951 12.786  102.178 1.00 46.28 ? 2687 HOH B O     1 
HETATM 19370 O O     . HOH DB 8 .    ? 35.345  17.526  67.964  1.00 45.17 ? 2688 HOH B O     1 
HETATM 19371 O O     . HOH DB 8 .    ? -8.915  33.421  69.155  1.00 45.45 ? 2689 HOH B O     1 
HETATM 19372 O O     . HOH DB 8 .    ? -24.652 2.861   112.008 1.00 48.67 ? 2690 HOH B O     1 
HETATM 19373 O O     . HOH DB 8 .    ? 2.953   57.159  71.175  1.00 35.48 ? 2691 HOH B O     1 
HETATM 19374 O O     . HOH DB 8 .    ? 5.916   48.326  114.852 1.00 36.83 ? 2692 HOH B O     1 
HETATM 19375 O O     . HOH DB 8 .    ? 15.171  57.203  72.171  1.00 26.30 ? 2693 HOH B O     1 
HETATM 19376 O O     . HOH DB 8 .    ? 30.687  22.580  70.199  1.00 42.71 ? 2694 HOH B O     1 
HETATM 19377 O O     . HOH DB 8 .    ? 2.305   48.917  99.276  1.00 33.90 ? 2695 HOH B O     1 
HETATM 19378 O O     . HOH DB 8 .    ? 30.539  35.758  83.888  1.00 45.75 ? 2696 HOH B O     1 
HETATM 19379 O O     . HOH DB 8 .    ? -2.358  42.430  74.603  1.00 44.05 ? 2697 HOH B O     1 
HETATM 19380 O O     . HOH DB 8 .    ? 9.326   30.676  88.833  1.00 36.23 ? 2698 HOH B O     1 
HETATM 19381 O O     . HOH DB 8 .    ? 16.444  14.107  107.057 1.00 31.16 ? 2699 HOH B O     1 
HETATM 19382 O O     . HOH DB 8 .    ? -17.395 -4.957  105.178 1.00 48.28 ? 2700 HOH B O     1 
HETATM 19383 O O     . HOH DB 8 .    ? -1.926  49.114  137.098 1.00 50.67 ? 2701 HOH B O     1 
HETATM 19384 O O     . HOH DB 8 .    ? 23.229  67.861  59.625  1.00 38.21 ? 2702 HOH B O     1 
HETATM 19385 O O     . HOH DB 8 .    ? 21.389  26.682  82.208  1.00 28.34 ? 2703 HOH B O     1 
HETATM 19386 O O     . HOH DB 8 .    ? 8.595   80.144  86.148  1.00 51.86 ? 2704 HOH B O     1 
HETATM 19387 O O     . HOH DB 8 .    ? 19.942  78.269  77.935  1.00 45.16 ? 2705 HOH B O     1 
HETATM 19388 O O     . HOH DB 8 .    ? 24.439  31.784  110.483 1.00 37.61 ? 2706 HOH B O     1 
HETATM 19389 O O     . HOH DB 8 .    ? 11.594  23.328  113.202 1.00 40.04 ? 2707 HOH B O     1 
HETATM 19390 O O     . HOH DB 8 .    ? -2.937  22.761  79.530  1.00 28.64 ? 2708 HOH B O     1 
HETATM 19391 O O     . HOH DB 8 .    ? -15.486 -3.938  112.307 1.00 45.76 ? 2709 HOH B O     1 
HETATM 19392 O O     . HOH DB 8 .    ? 29.718  20.957  73.419  1.00 30.53 ? 2710 HOH B O     1 
HETATM 19393 O O     . HOH DB 8 .    ? -26.884 13.462  100.223 1.00 46.76 ? 2711 HOH B O     1 
HETATM 19394 O O     . HOH DB 8 .    ? 7.902   -7.741  106.662 1.00 38.35 ? 2712 HOH B O     1 
HETATM 19395 O O     . HOH DB 8 .    ? 4.975   16.775  127.917 1.00 41.45 ? 2713 HOH B O     1 
HETATM 19396 O O     . HOH DB 8 .    ? 15.379  51.226  56.408  1.00 38.60 ? 2714 HOH B O     1 
HETATM 19397 O O     . HOH DB 8 .    ? 16.945  24.950  52.269  1.00 33.40 ? 2715 HOH B O     1 
HETATM 19398 O O     . HOH DB 8 .    ? 25.651  75.557  77.431  1.00 39.31 ? 2716 HOH B O     1 
HETATM 19399 O O     . HOH DB 8 .    ? -6.964  55.299  83.297  1.00 42.90 ? 2717 HOH B O     1 
HETATM 19400 O O     . HOH DB 8 .    ? 16.224  10.115  95.497  1.00 34.35 ? 2718 HOH B O     1 
HETATM 19401 O O     . HOH DB 8 .    ? -1.351  37.701  73.707  1.00 30.53 ? 2719 HOH B O     1 
HETATM 19402 O O     . HOH DB 8 .    ? -3.627  -4.911  93.995  1.00 39.97 ? 2720 HOH B O     1 
HETATM 19403 O O     . HOH DB 8 .    ? -7.176  36.902  66.703  1.00 37.83 ? 2721 HOH B O     1 
HETATM 19404 O O     . HOH DB 8 .    ? 11.221  45.502  109.308 1.00 38.56 ? 2722 HOH B O     1 
HETATM 19405 O O     . HOH DB 8 .    ? 31.363  31.696  84.060  1.00 35.83 ? 2723 HOH B O     1 
HETATM 19406 O O     . HOH DB 8 .    ? -0.024  28.166  54.352  1.00 44.34 ? 2724 HOH B O     1 
HETATM 19407 O O     . HOH DB 8 .    ? 0.519   4.092   85.815  1.00 39.54 ? 2725 HOH B O     1 
HETATM 19408 O O     . HOH DB 8 .    ? 7.366   30.592  90.263  1.00 39.86 ? 2726 HOH B O     1 
HETATM 19409 O O     . HOH DB 8 .    ? 21.287  5.693   73.201  1.00 43.39 ? 2727 HOH B O     1 
HETATM 19410 O O     . HOH DB 8 .    ? -7.616  12.477  82.817  1.00 39.22 ? 2728 HOH B O     1 
HETATM 19411 O O     . HOH DB 8 .    ? -6.576  8.016   116.446 1.00 35.74 ? 2729 HOH B O     1 
HETATM 19412 O O     . HOH DB 8 .    ? 33.135  58.883  67.555  1.00 34.63 ? 2730 HOH B O     1 
HETATM 19413 O O     . HOH DB 8 .    ? 10.156  5.859   72.192  1.00 42.61 ? 2731 HOH B O     1 
HETATM 19414 O O     . HOH DB 8 .    ? 12.277  27.223  88.146  1.00 42.19 ? 2732 HOH B O     1 
HETATM 19415 O O     . HOH DB 8 .    ? -2.453  29.693  96.943  1.00 35.22 ? 2733 HOH B O     1 
HETATM 19416 O O     . HOH DB 8 .    ? 25.970  32.811  74.866  1.00 33.19 ? 2734 HOH B O     1 
HETATM 19417 O O     . HOH DB 8 .    ? -2.710  25.653  101.931 1.00 39.51 ? 2735 HOH B O     1 
HETATM 19418 O O     . HOH DB 8 .    ? 22.061  77.928  78.558  1.00 39.73 ? 2736 HOH B O     1 
HETATM 19419 O O     . HOH DB 8 .    ? 28.905  8.547   86.309  1.00 43.36 ? 2737 HOH B O     1 
HETATM 19420 O O     . HOH DB 8 .    ? 20.001  45.348  90.188  1.00 28.59 ? 2738 HOH B O     1 
HETATM 19421 O O     . HOH DB 8 .    ? -2.117  61.072  124.289 1.00 39.22 ? 2739 HOH B O     1 
HETATM 19422 O O     . HOH DB 8 .    ? 23.865  22.563  107.262 1.00 38.00 ? 2740 HOH B O     1 
HETATM 19423 O O     . HOH DB 8 .    ? 3.578   29.791  94.412  1.00 39.80 ? 2741 HOH B O     1 
HETATM 19424 O O     . HOH DB 8 .    ? 20.229  22.863  110.256 1.00 35.79 ? 2742 HOH B O     1 
HETATM 19425 O O     . HOH DB 8 .    ? 33.894  58.653  74.102  1.00 38.68 ? 2743 HOH B O     1 
HETATM 19426 O O     . HOH DB 8 .    ? 0.299   18.430  71.837  1.00 35.13 ? 2744 HOH B O     1 
HETATM 19427 O O     . HOH DB 8 .    ? -14.856 6.550   86.220  1.00 46.74 ? 2745 HOH B O     1 
HETATM 19428 O O     . HOH DB 8 .    ? -15.757 52.061  115.672 1.00 41.80 ? 2746 HOH B O     1 
HETATM 19429 O O     . HOH DB 8 .    ? 2.647   43.545  56.394  1.00 37.14 ? 2747 HOH B O     1 
HETATM 19430 O O     . HOH DB 8 .    ? -0.939  43.930  75.625  1.00 39.61 ? 2748 HOH B O     1 
HETATM 19431 O O     . HOH DB 8 .    ? 6.955   28.846  91.791  1.00 41.39 ? 2749 HOH B O     1 
HETATM 19432 O O     . HOH DB 8 .    ? 24.119  69.169  62.467  1.00 37.00 ? 2750 HOH B O     1 
HETATM 19433 O O     . HOH DB 8 .    ? 20.860  24.447  83.388  1.00 27.61 ? 2751 HOH B O     1 
HETATM 19434 O O     . HOH DB 8 .    ? -10.216 29.998  76.296  1.00 41.16 ? 2752 HOH B O     1 
HETATM 19435 O O     . HOH DB 8 .    ? 18.623  6.919   98.449  1.00 37.74 ? 2753 HOH B O     1 
HETATM 19436 O O     . HOH DB 8 .    ? 6.296   13.064  69.192  1.00 43.93 ? 2754 HOH B O     1 
HETATM 19437 O O     . HOH DB 8 .    ? 5.837   29.801  86.651  1.00 29.30 ? 2755 HOH B O     1 
HETATM 19438 O O     . HOH DB 8 .    ? 5.038   43.945  51.095  1.00 39.40 ? 2756 HOH B O     1 
HETATM 19439 O O     . HOH DB 8 .    ? -10.823 36.665  127.570 1.00 50.94 ? 2757 HOH B O     1 
HETATM 19440 O O     . HOH DB 8 .    ? 6.954   63.261  69.206  1.00 42.41 ? 2758 HOH B O     1 
HETATM 19441 O O     . HOH DB 8 .    ? 5.318   32.164  87.680  1.00 34.28 ? 2759 HOH B O     1 
HETATM 19442 O O     . HOH DB 8 .    ? -3.270  40.084  74.654  1.00 41.60 ? 2760 HOH B O     1 
HETATM 19443 O O     . HOH DB 8 .    ? -7.401  22.421  78.694  1.00 34.08 ? 2761 HOH B O     1 
HETATM 19444 O O     . HOH DB 8 .    ? -7.489  2.922   85.041  1.00 41.24 ? 2762 HOH B O     1 
HETATM 19445 O O     . HOH DB 8 .    ? 7.299   72.151  62.311  1.00 49.02 ? 2763 HOH B O     1 
HETATM 19446 O O     . HOH DB 8 .    ? 21.630  18.241  111.108 1.00 43.83 ? 2764 HOH B O     1 
HETATM 19447 O O     . HOH DB 8 .    ? 8.166   7.638   72.846  1.00 41.99 ? 2765 HOH B O     1 
HETATM 19448 O O     . HOH DB 8 .    ? -16.111 6.613   122.161 1.00 48.92 ? 2766 HOH B O     1 
HETATM 19449 O O     . HOH DB 8 .    ? 19.899  33.642  115.333 1.00 38.67 ? 2767 HOH B O     1 
HETATM 19450 O O     . HOH DB 8 .    ? 13.505  56.215  63.551  1.00 40.97 ? 2768 HOH B O     1 
HETATM 19451 O O     . HOH DB 8 .    ? 12.497  44.011  53.935  1.00 33.81 ? 2769 HOH B O     1 
HETATM 19452 O O     . HOH DB 8 .    ? 6.000   28.184  94.983  1.00 46.98 ? 2770 HOH B O     1 
HETATM 19453 O O     . HOH DB 8 .    ? 12.649  47.002  53.160  1.00 46.86 ? 2771 HOH B O     1 
HETATM 19454 O O     . HOH DB 8 .    ? 20.935  69.163  58.924  1.00 42.82 ? 2772 HOH B O     1 
HETATM 19455 O O     . HOH DB 8 .    ? 15.098  22.032  97.698  1.00 36.10 ? 2773 HOH B O     1 
HETATM 19456 O O     . HOH DB 8 .    ? 2.264   30.742  83.051  1.00 32.90 ? 2774 HOH B O     1 
HETATM 19457 O O     . HOH DB 8 .    ? 5.033   31.941  93.036  1.00 38.01 ? 2775 HOH B O     1 
HETATM 19458 O O     . HOH DB 8 .    ? -2.747  28.635  68.903  1.00 29.32 ? 2776 HOH B O     1 
HETATM 19459 O O     . HOH DB 8 .    ? 21.568  19.451  107.488 1.00 34.03 ? 2777 HOH B O     1 
HETATM 19460 O O     . HOH DB 8 .    ? -1.296  15.152  83.473  1.00 30.69 ? 2778 HOH B O     1 
HETATM 19461 O O     . HOH DB 8 .    ? 33.690  19.576  54.270  1.00 38.72 ? 2779 HOH B O     1 
HETATM 19462 O O     . HOH DB 8 .    ? 15.374  35.056  114.356 1.00 46.65 ? 2780 HOH B O     1 
HETATM 19463 O O     . HOH DB 8 .    ? 4.546   25.317  128.802 1.00 36.27 ? 2781 HOH B O     1 
HETATM 19464 O O     . HOH DB 8 .    ? -2.926  14.223  82.221  1.00 41.61 ? 2782 HOH B O     1 
HETATM 19465 O O     . HOH DB 8 .    ? 18.662  64.172  55.503  1.00 37.96 ? 2783 HOH B O     1 
HETATM 19466 O O     . HOH DB 8 .    ? 18.717  2.651   77.709  1.00 41.25 ? 2784 HOH B O     1 
HETATM 19467 O O     . HOH DB 8 .    ? -4.072  22.832  72.176  1.00 38.74 ? 2785 HOH B O     1 
HETATM 19468 O O     . HOH DB 8 .    ? 6.466   15.715  92.082  1.00 35.98 ? 2786 HOH B O     1 
HETATM 19469 O O     . HOH DB 8 .    ? 30.437  23.293  74.510  1.00 37.47 ? 2787 HOH B O     1 
HETATM 19470 O O     . HOH DB 8 .    ? -25.366 12.603  86.873  1.00 34.88 ? 2788 HOH B O     1 
HETATM 19471 O O     . HOH DB 8 .    ? 13.872  36.377  74.250  1.00 29.29 ? 2789 HOH B O     1 
HETATM 19472 O O     . HOH DB 8 .    ? 6.772   61.078  85.636  1.00 32.37 ? 2790 HOH B O     1 
HETATM 19473 O O     . HOH DB 8 .    ? 14.491  7.262   92.048  1.00 41.16 ? 2791 HOH B O     1 
HETATM 19474 O O     . HOH DB 8 .    ? 32.330  43.099  80.696  1.00 47.58 ? 2792 HOH B O     1 
HETATM 19475 O O     . HOH DB 8 .    ? 8.376   76.811  89.294  1.00 47.98 ? 2793 HOH B O     1 
HETATM 19476 O O     . HOH DB 8 .    ? 9.383   3.598   83.815  1.00 34.08 ? 2794 HOH B O     1 
HETATM 19477 O O     . HOH DB 8 .    ? 8.907   65.197  66.450  1.00 31.84 ? 2795 HOH B O     1 
HETATM 19478 O O     . HOH DB 8 .    ? 18.813  66.486  55.876  1.00 38.23 ? 2796 HOH B O     1 
HETATM 19479 O O     . HOH DB 8 .    ? 4.309   64.327  87.140  1.00 36.73 ? 2797 HOH B O     1 
HETATM 19480 O O     . HOH DB 8 .    ? 15.362  44.404  53.030  1.00 38.38 ? 2798 HOH B O     1 
HETATM 19481 O O     . HOH DB 8 .    ? -11.731 1.793   89.116  1.00 39.49 ? 2799 HOH B O     1 
HETATM 19482 O O     . HOH DB 8 .    ? 1.407   44.702  97.527  1.00 40.58 ? 2800 HOH B O     1 
HETATM 19483 O O     . HOH DB 8 .    ? -1.990  18.963  78.397  1.00 39.33 ? 2801 HOH B O     1 
HETATM 19484 O O     . HOH DB 8 .    ? 21.253  25.607  44.608  1.00 39.45 ? 2802 HOH B O     1 
HETATM 19485 O O     . HOH DB 8 .    ? 12.623  55.471  105.968 1.00 36.01 ? 2803 HOH B O     1 
HETATM 19486 O O     . HOH DB 8 .    ? 7.310   19.066  96.505  1.00 48.98 ? 2804 HOH B O     1 
HETATM 19487 O O     . HOH DB 8 .    ? -7.146  25.377  75.030  1.00 39.52 ? 2805 HOH B O     1 
HETATM 19488 O O     . HOH DB 8 .    ? -10.933 47.009  77.193  1.00 40.81 ? 2806 HOH B O     1 
HETATM 19489 O O     . HOH DB 8 .    ? 24.475  71.696  62.227  1.00 47.79 ? 2807 HOH B O     1 
HETATM 19490 O O     . HOH DB 8 .    ? 9.668   16.617  89.782  1.00 37.08 ? 2808 HOH B O     1 
HETATM 19491 O O     . HOH DB 8 .    ? 5.875   2.794   85.592  1.00 35.65 ? 2809 HOH B O     1 
HETATM 19492 O O     . HOH DB 8 .    ? 14.479  51.858  62.919  1.00 35.55 ? 2810 HOH B O     1 
HETATM 19493 O O     . HOH DB 8 .    ? 35.014  26.781  61.218  1.00 39.72 ? 2811 HOH B O     1 
HETATM 19494 O O     . HOH DB 8 .    ? 2.348   21.976  61.019  1.00 35.89 ? 2812 HOH B O     1 
HETATM 19495 O O     . HOH DB 8 .    ? 5.295   49.940  113.442 1.00 38.77 ? 2813 HOH B O     1 
HETATM 19496 O O     . HOH DB 8 .    ? 14.166  24.316  98.440  1.00 39.40 ? 2814 HOH B O     1 
HETATM 19497 O O     . HOH DB 8 .    ? -10.654 3.449   86.524  1.00 43.96 ? 2815 HOH B O     1 
HETATM 19498 O O     . HOH DB 8 .    ? 13.760  75.325  61.089  1.00 43.33 ? 2816 HOH B O     1 
HETATM 19499 O O     . HOH DB 8 .    ? 19.836  10.043  96.114  1.00 52.11 ? 2817 HOH B O     1 
HETATM 19500 O O     . HOH DB 8 .    ? -0.005  28.861  96.787  1.00 30.39 ? 2818 HOH B O     1 
HETATM 19501 O O     . HOH DB 8 .    ? 0.224   16.071  71.182  1.00 41.80 ? 2819 HOH B O     1 
HETATM 19502 O O     . HOH DB 8 .    ? 34.485  24.410  76.101  1.00 41.19 ? 2820 HOH B O     1 
HETATM 19503 O O     . HOH DB 8 .    ? 9.396   74.265  90.219  1.00 51.24 ? 2821 HOH B O     1 
HETATM 19504 O O     . HOH DB 8 .    ? -9.895  -0.251  87.204  1.00 45.77 ? 2822 HOH B O     1 
HETATM 19505 O O     . HOH DB 8 .    ? -27.498 15.482  83.014  1.00 48.85 ? 2823 HOH B O     1 
HETATM 19506 O O     . HOH DB 8 .    ? 24.533  77.338  79.399  1.00 48.91 ? 2824 HOH B O     1 
HETATM 19507 O O     . HOH DB 8 .    ? -23.668 13.820  82.458  1.00 36.55 ? 2825 HOH B O     1 
HETATM 19508 O O     . HOH DB 8 .    ? -5.162  23.697  74.934  1.00 39.62 ? 2826 HOH B O     1 
HETATM 19509 O O     . HOH DB 8 .    ? 4.040   10.920  70.059  1.00 52.87 ? 2827 HOH B O     1 
HETATM 19510 O O     . HOH DB 8 .    ? 7.615   1.734   84.545  1.00 39.32 ? 2828 HOH B O     1 
HETATM 19511 O O     . HOH DB 8 .    ? -1.585  30.770  49.255  1.00 37.82 ? 2829 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   . ALA A 16   ? 0.7140 0.6929 0.7373 0.0543  -0.0105 -0.0473 14   ALA A N   
2     C CA  . ALA A 16   ? 0.7300 0.7097 0.7474 0.0512  -0.0087 -0.0451 14   ALA A CA  
3     C C   . ALA A 16   ? 0.7442 0.7310 0.7560 0.0495  -0.0047 -0.0413 14   ALA A C   
4     O O   . ALA A 16   ? 0.7631 0.7586 0.7734 0.0516  -0.0027 -0.0441 14   ALA A O   
5     C CB  . ALA A 16   ? 0.7049 0.6871 0.7213 0.0534  -0.0094 -0.0512 14   ALA A CB  
6     N N   . PRO A 17   ? 0.6889 0.6725 0.6981 0.0455  -0.0036 -0.0351 15   PRO A N   
7     C CA  . PRO A 17   ? 0.6182 0.6079 0.6229 0.0436  -0.0001 -0.0312 15   PRO A CA  
8     C C   . PRO A 17   ? 0.6120 0.6078 0.6113 0.0435  0.0021  -0.0326 15   PRO A C   
9     O O   . PRO A 17   ? 0.6051 0.5982 0.6027 0.0428  0.0012  -0.0338 15   PRO A O   
10    C CB  . PRO A 17   ? 0.6114 0.5949 0.6149 0.0396  -0.0001 -0.0250 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5835 0.5585 0.5918 0.0397  -0.0035 -0.0252 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.6381 0.6126 0.6488 0.0427  -0.0055 -0.0312 15   PRO A CD  
13    N N   . ALA A 18   ? 0.5693 0.5737 0.5663 0.0441  0.0049  -0.0325 16   ALA A N   
14    C CA  . ALA A 18   ? 0.4831 0.4942 0.4749 0.0438  0.0071  -0.0331 16   ALA A CA  
15    C C   . ALA A 18   ? 0.4710 0.4783 0.4585 0.0398  0.0080  -0.0281 16   ALA A C   
16    O O   . ALA A 18   ? 0.3815 0.3853 0.3689 0.0371  0.0085  -0.0231 16   ALA A O   
17    C CB  . ALA A 18   ? 0.4648 0.4858 0.4551 0.0447  0.0101  -0.0327 16   ALA A CB  
18    N N   . PRO A 19   ? 0.4360 0.4438 0.4200 0.0396  0.0080  -0.0294 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3777 0.3819 0.3580 0.0360  0.0086  -0.0249 17   PRO A CA  
20    C C   . PRO A 19   ? 0.3767 0.3850 0.3537 0.0336  0.0115  -0.0199 17   PRO A C   
21    O O   . PRO A 19   ? 0.3706 0.3869 0.3455 0.0346  0.0136  -0.0203 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3847 0.3910 0.3619 0.0370  0.0082  -0.0282 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.4329 0.4401 0.4138 0.0408  0.0062  -0.0347 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.4036 0.4150 0.3873 0.0427  0.0071  -0.0355 17   PRO A CD  
25    N N   . PHE A 20   ? 0.3491 0.3519 0.3257 0.0305  0.0115  -0.0151 18   PHE A N   
26    C CA  . PHE A 20   ? 0.3222 0.3272 0.2962 0.0278  0.0137  -0.0100 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3782 0.3881 0.3540 0.0282  0.0152  -0.0089 18   PHE A C   
28    O O   . PHE A 20   ? 0.3665 0.3792 0.3403 0.0261  0.0172  -0.0051 18   PHE A O   
29    C CB  . PHE A 20   ? 0.3430 0.3528 0.3120 0.0271  0.0154  -0.0092 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2864 0.2917 0.2531 0.0262  0.0141  -0.0095 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2894 0.2883 0.2555 0.0234  0.0135  -0.0059 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.3300 0.3380 0.2952 0.0283  0.0135  -0.0137 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.3125 0.3079 0.2769 0.0227  0.0123  -0.0063 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3099 0.3140 0.2732 0.0275  0.0122  -0.0140 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3178 0.3157 0.2808 0.0247  0.0116  -0.0103 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3379 0.3488 0.3177 0.0308  0.0142  -0.0122 19   ALA A N   
37    C CA  . ALA A 21   ? 0.4303 0.4462 0.4123 0.0313  0.0156  -0.0113 19   ALA A CA  
38    C C   . ALA A 21   ? 0.4075 0.4193 0.3906 0.0285  0.0156  -0.0066 19   ALA A C   
39    O O   . ALA A 21   ? 0.4571 0.4733 0.4410 0.0279  0.0172  -0.0047 19   ALA A O   
40    C CB  . ALA A 21   ? 0.4478 0.4653 0.4343 0.0350  0.0142  -0.0162 19   ALA A CB  
41    N N   . ASP A 22   ? 0.3464 0.3503 0.3297 0.0268  0.0139  -0.0048 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3782 0.3782 0.3623 0.0242  0.0137  -0.0006 20   ASP A CA  
43    C C   . ASP A 22   ? 0.3527 0.3485 0.3334 0.0212  0.0138  0.0026  20   ASP A C   
44    O O   . ASP A 22   ? 0.3574 0.3476 0.3388 0.0196  0.0127  0.0049  20   ASP A O   
45    C CB  . ASP A 22   ? 0.3998 0.3946 0.3882 0.0252  0.0113  -0.0012 20   ASP A CB  
46    N N   . PHE A 23   ? 0.3218 0.3205 0.2987 0.0206  0.0152  0.0028  21   PHE A N   
47    C CA  . PHE A 23   ? 0.3310 0.3256 0.3049 0.0183  0.0150  0.0051  21   PHE A CA  
48    C C   . PHE A 23   ? 0.3086 0.3006 0.2824 0.0155  0.0153  0.0094  21   PHE A C   
49    O O   . PHE A 23   ? 0.2959 0.2823 0.2700 0.0141  0.0140  0.0107  21   PHE A O   
50    C CB  . PHE A 23   ? 0.2885 0.2875 0.2584 0.0182  0.0165  0.0050  21   PHE A CB  
51    C CG  . PHE A 23   ? 0.2788 0.2740 0.2457 0.0159  0.0163  0.0075  21   PHE A CG  
52    C CD1 . PHE A 23   ? 0.3185 0.3081 0.2855 0.0158  0.0145  0.0064  21   PHE A CD1 
53    C CD2 . PHE A 23   ? 0.3341 0.3313 0.2984 0.0139  0.0179  0.0109  21   PHE A CD2 
54    C CE1 . PHE A 23   ? 0.2842 0.2708 0.2487 0.0139  0.0143  0.0084  21   PHE A CE1 
55    C CE2 . PHE A 23   ? 0.3340 0.3277 0.2959 0.0120  0.0175  0.0130  21   PHE A CE2 
56    C CZ  . PHE A 23   ? 0.2982 0.2867 0.2601 0.0121  0.0157  0.0117  21   PHE A CZ  
57    N N   . ALA A 24   ? 0.3088 0.3052 0.2825 0.0145  0.0170  0.0115  22   ALA A N   
58    C CA  . ALA A 24   ? 0.3428 0.3373 0.3163 0.0118  0.0174  0.0153  22   ALA A CA  
59    C C   . ALA A 24   ? 0.3511 0.3505 0.3264 0.0114  0.0187  0.0167  22   ALA A C   
60    O O   . ALA A 24   ? 0.3394 0.3406 0.3134 0.0093  0.0200  0.0194  22   ALA A O   
61    C CB  . ALA A 24   ? 0.3484 0.3420 0.3183 0.0099  0.0180  0.0174  22   ALA A CB  
62    N N   . PRO A 25   ? 0.3721 0.3737 0.3506 0.0131  0.0184  0.0150  23   PRO A N   
63    C CA  . PRO A 25   ? 0.3605 0.3674 0.3410 0.0127  0.0198  0.0162  23   PRO A CA  
64    C C   . PRO A 25   ? 0.3352 0.3396 0.3161 0.0100  0.0196  0.0196  23   PRO A C   
65    O O   . PRO A 25   ? 0.3361 0.3351 0.3175 0.0093  0.0180  0.0202  23   PRO A O   
66    C CB  . PRO A 25   ? 0.3798 0.3878 0.3640 0.0154  0.0188  0.0135  23   PRO A CB  
67    C CG  . PRO A 25   ? 0.3990 0.4001 0.3837 0.0160  0.0165  0.0124  23   PRO A CG  
68    C CD  . PRO A 25   ? 0.3298 0.3283 0.3109 0.0153  0.0166  0.0123  23   PRO A CD  
69    N N   . PRO A 26   ? 0.3192 0.3277 0.3002 0.0082  0.0211  0.0219  24   PRO A N   
70    C CA  . PRO A 26   ? 0.3248 0.3311 0.3066 0.0056  0.0208  0.0248  24   PRO A CA  
71    C C   . PRO A 26   ? 0.3236 0.3296 0.3089 0.0060  0.0198  0.0245  24   PRO A C   
72    O O   . PRO A 26   ? 0.2957 0.3047 0.2834 0.0082  0.0197  0.0226  24   PRO A O   
73    C CB  . PRO A 26   ? 0.3411 0.3526 0.3226 0.0039  0.0227  0.0270  24   PRO A CB  
74    C CG  . PRO A 26   ? 0.3731 0.3913 0.3553 0.0061  0.0241  0.0250  24   PRO A CG  
75    C CD  . PRO A 26   ? 0.3778 0.3935 0.3583 0.0085  0.0232  0.0219  24   PRO A CD  
76    N N   . VAL A 27   ? 0.3346 0.3372 0.3202 0.0041  0.0188  0.0265  25   VAL A N   
77    C CA  . VAL A 27   ? 0.3413 0.3438 0.3300 0.0042  0.0177  0.0266  25   VAL A CA  
78    C C   . VAL A 27   ? 0.3586 0.3675 0.3503 0.0045  0.0188  0.0266  25   VAL A C   
79    O O   . VAL A 27   ? 0.3402 0.3511 0.3348 0.0062  0.0182  0.0253  25   VAL A O   
80    C CB  . VAL A 27   ? 0.3707 0.3693 0.3589 0.0020  0.0166  0.0286  25   VAL A CB  
81    C CG1 . VAL A 27   ? 0.3245 0.3243 0.3159 0.0019  0.0156  0.0289  25   VAL A CG1 
82    C CG2 . VAL A 27   ? 0.3414 0.3343 0.3272 0.0021  0.0154  0.0282  25   VAL A CG2 
83    N N   . ARG A 28   ? 0.3418 0.3546 0.3332 0.0028  0.0205  0.0281  26   ARG A N   
84    C CA  . ARG A 28   ? 0.3499 0.3695 0.3444 0.0027  0.0218  0.0284  26   ARG A CA  
85    C C   . ARG A 28   ? 0.4253 0.4494 0.4182 0.0018  0.0239  0.0294  26   ARG A C   
86    O O   . ARG A 28   ? 0.3760 0.3972 0.3657 0.0006  0.0242  0.0306  26   ARG A O   
87    C CB  . ARG A 28   ? 0.4159 0.4357 0.4130 0.0005  0.0212  0.0302  26   ARG A CB  
88    C CG  . ARG A 28   ? 0.4106 0.4288 0.4065 -0.0027 0.0215  0.0329  26   ARG A CG  
89    C CD  . ARG A 28   ? 0.4108 0.4290 0.4096 -0.0047 0.0206  0.0342  26   ARG A CD  
90    N NE  . ARG A 28   ? 0.4471 0.4596 0.4451 -0.0048 0.0186  0.0338  26   ARG A NE  
91    C CZ  . ARG A 28   ? 0.5043 0.5163 0.5038 -0.0035 0.0172  0.0327  26   ARG A CZ  
92    N NH1 . ARG A 28   ? 0.5136 0.5301 0.5160 -0.0019 0.0174  0.0317  26   ARG A NH1 
93    N NH2 . ARG A 28   ? 0.4224 0.4295 0.4206 -0.0036 0.0155  0.0326  26   ARG A NH2 
94    N N   . PRO A 29   ? 0.4021 0.4336 0.3971 0.0024  0.0255  0.0291  27   PRO A N   
95    C CA  . PRO A 29   ? 0.4139 0.4505 0.4076 0.0011  0.0276  0.0308  27   PRO A CA  
96    C C   . PRO A 29   ? 0.3784 0.4128 0.3719 -0.0025 0.0277  0.0345  27   PRO A C   
97    O O   . PRO A 29   ? 0.3644 0.3972 0.3605 -0.0042 0.0267  0.0356  27   PRO A O   
98    C CB  . PRO A 29   ? 0.4000 0.4453 0.3971 0.0021  0.0291  0.0300  27   PRO A CB  
99    C CG  . PRO A 29   ? 0.4343 0.4786 0.4336 0.0051  0.0277  0.0268  27   PRO A CG  
100   C CD  . PRO A 29   ? 0.4437 0.4797 0.4426 0.0042  0.0254  0.0273  27   PRO A CD  
101   N N   . GLN A 30   ? 0.3780 0.4123 0.3684 -0.0037 0.0287  0.0363  28   GLN A N   
102   C CA  . GLN A 30   ? 0.3632 0.3941 0.3532 -0.0069 0.0283  0.0396  28   GLN A CA  
103   C C   . GLN A 30   ? 0.4056 0.4424 0.3985 -0.0094 0.0298  0.0425  28   GLN A C   
104   O O   . GLN A 30   ? 0.3674 0.4104 0.3596 -0.0094 0.0317  0.0437  28   GLN A O   
105   C CB  . GLN A 30   ? 0.3391 0.3670 0.3247 -0.0069 0.0285  0.0404  28   GLN A CB  
106   C CG  . GLN A 30   ? 0.3353 0.3572 0.3180 -0.0047 0.0270  0.0376  28   GLN A CG  
107   C CD  . GLN A 30   ? 0.3605 0.3755 0.3440 -0.0057 0.0250  0.0375  28   GLN A CD  
108   O OE1 . GLN A 30   ? 0.3354 0.3464 0.3180 -0.0076 0.0243  0.0394  28   GLN A OE1 
109   N NE2 . GLN A 30   ? 0.3746 0.3884 0.3598 -0.0042 0.0239  0.0354  28   GLN A NE2 
110   N N   . SER A 31   ? 0.3805 0.4158 0.3769 -0.0115 0.0288  0.0437  29   SER A N   
111   C CA  . SER A 31   ? 0.3669 0.4071 0.3668 -0.0142 0.0298  0.0466  29   SER A CA  
112   C C   . SER A 31   ? 0.3655 0.4049 0.3638 -0.0168 0.0305  0.0503  29   SER A C   
113   O O   . SER A 31   ? 0.3196 0.3536 0.3143 -0.0166 0.0298  0.0505  29   SER A O   
114   C CB  . SER A 31   ? 0.3705 0.4084 0.3745 -0.0159 0.0282  0.0467  29   SER A CB  
115   O OG  . SER A 31   ? 0.3320 0.3624 0.3349 -0.0175 0.0264  0.0476  29   SER A OG  
116   N N   . THR A 32   ? 0.3110 0.3562 0.3122 -0.0192 0.0319  0.0534  30   THR A N   
117   C CA  . THR A 32   ? 0.3521 0.3962 0.3528 -0.0222 0.0322  0.0576  30   THR A CA  
118   C C   . THR A 32   ? 0.3520 0.3868 0.3524 -0.0236 0.0298  0.0580  30   THR A C   
119   O O   . THR A 32   ? 0.2921 0.3230 0.2895 -0.0240 0.0294  0.0597  30   THR A O   
120   C CB  . THR A 32   ? 0.3883 0.4389 0.3936 -0.0252 0.0335  0.0609  30   THR A CB  
121   O OG1 . THR A 32   ? 0.4155 0.4755 0.4211 -0.0237 0.0358  0.0601  30   THR A OG1 
122   C CG2 . THR A 32   ? 0.3946 0.4444 0.3996 -0.0283 0.0338  0.0657  30   THR A CG2 
123   N N   . LEU A 33   ? 0.3179 0.3494 0.3214 -0.0240 0.0280  0.0565  31   LEU A N   
124   C CA  . LEU A 33   ? 0.3430 0.3664 0.3466 -0.0253 0.0257  0.0566  31   LEU A CA  
125   C C   . LEU A 33   ? 0.3030 0.3205 0.3019 -0.0228 0.0247  0.0542  31   LEU A C   
126   O O   . LEU A 33   ? 0.2896 0.3013 0.2869 -0.0236 0.0234  0.0550  31   LEU A O   
127   C CB  . LEU A 33   ? 0.3136 0.3358 0.3215 -0.0262 0.0241  0.0551  31   LEU A CB  
128   C CG  . LEU A 33   ? 0.3662 0.3925 0.3795 -0.0294 0.0244  0.0578  31   LEU A CG  
129   C CD1 . LEU A 33   ? 0.2921 0.3193 0.3095 -0.0295 0.0231  0.0556  31   LEU A CD1 
130   C CD2 . LEU A 33   ? 0.3320 0.3536 0.3464 -0.0324 0.0233  0.0609  31   LEU A CD2 
131   N N   . ARG A 34   ? 0.2833 0.3022 0.2801 -0.0199 0.0251  0.0511  32   ARG A N   
132   C CA  . ARG A 34   ? 0.2731 0.2869 0.2657 -0.0177 0.0243  0.0490  32   ARG A CA  
133   C C   . ARG A 34   ? 0.3041 0.3181 0.2929 -0.0174 0.0253  0.0505  32   ARG A C   
134   O O   . ARG A 34   ? 0.2963 0.3050 0.2822 -0.0170 0.0243  0.0502  32   ARG A O   
135   C CB  . ARG A 34   ? 0.3238 0.3390 0.3157 -0.0147 0.0243  0.0456  32   ARG A CB  
136   C CG  . ARG A 34   ? 0.3186 0.3323 0.3133 -0.0145 0.0228  0.0439  32   ARG A CG  
137   C CD  . ARG A 34   ? 0.3161 0.3227 0.3094 -0.0146 0.0208  0.0430  32   ARG A CD  
138   N NE  . ARG A 34   ? 0.3149 0.3183 0.3043 -0.0124 0.0205  0.0412  32   ARG A NE  
139   C CZ  . ARG A 34   ? 0.3581 0.3603 0.3471 -0.0103 0.0197  0.0389  32   ARG A CZ  
140   N NH1 . ARG A 34   ? 0.3434 0.3474 0.3352 -0.0099 0.0191  0.0380  32   ARG A NH1 
141   N NH2 . ARG A 34   ? 0.3443 0.3433 0.3301 -0.0087 0.0194  0.0376  32   ARG A NH2 
142   N N   . ARG A 35   ? 0.3042 0.3249 0.2928 -0.0175 0.0274  0.0520  33   ARG A N   
143   C CA  . ARG A 35   ? 0.3543 0.3760 0.3392 -0.0172 0.0284  0.0536  33   ARG A CA  
144   C C   . ARG A 35   ? 0.3219 0.3397 0.3068 -0.0198 0.0276  0.0572  33   ARG A C   
145   O O   . ARG A 35   ? 0.3065 0.3215 0.2879 -0.0193 0.0273  0.0579  33   ARG A O   
146   C CB  . ARG A 35   ? 0.3656 0.3963 0.3504 -0.0167 0.0308  0.0545  33   ARG A CB  
147   C CG  . ARG A 35   ? 0.4239 0.4586 0.4084 -0.0135 0.0316  0.0505  33   ARG A CG  
148   C CD  . ARG A 35   ? 0.4592 0.5030 0.4427 -0.0125 0.0340  0.0509  33   ARG A CD  
149   N NE  . ARG A 35   ? 0.5569 0.6005 0.5355 -0.0107 0.0343  0.0501  33   ARG A NE  
150   C CZ  . ARG A 35   ? 0.6051 0.6561 0.5815 -0.0098 0.0363  0.0505  33   ARG A CZ  
151   N NH1 . ARG A 35   ? 0.6261 0.6857 0.6047 -0.0105 0.0382  0.0519  33   ARG A NH1 
152   N NH2 . ARG A 35   ? 0.5930 0.6431 0.5648 -0.0080 0.0362  0.0494  33   ARG A NH2 
153   N N   . ALA A 36   ? 0.3025 0.3199 0.2916 -0.0226 0.0270  0.0595  34   ALA A N   
154   C CA  . ALA A 36   ? 0.3228 0.3359 0.3126 -0.0251 0.0259  0.0629  34   ALA A CA  
155   C C   . ALA A 36   ? 0.3220 0.3267 0.3103 -0.0243 0.0236  0.0609  34   ALA A C   
156   O O   . ALA A 36   ? 0.3003 0.3011 0.2872 -0.0250 0.0226  0.0627  34   ALA A O   
157   C CB  . ALA A 36   ? 0.3133 0.3277 0.3085 -0.0283 0.0256  0.0655  34   ALA A CB  
158   N N   . ILE A 37   ? 0.2876 0.2901 0.2764 -0.0229 0.0225  0.0572  35   ILE A N   
159   C CA  . ILE A 37   ? 0.2696 0.2653 0.2565 -0.0217 0.0207  0.0550  35   ILE A CA  
160   C C   . ILE A 37   ? 0.3177 0.3124 0.2996 -0.0197 0.0211  0.0543  35   ILE A C   
161   O O   . ILE A 37   ? 0.2701 0.2603 0.2503 -0.0199 0.0200  0.0550  35   ILE A O   
162   C CB  . ILE A 37   ? 0.2762 0.2710 0.2642 -0.0204 0.0198  0.0515  35   ILE A CB  
163   C CG1 . ILE A 37   ? 0.2594 0.2551 0.2523 -0.0225 0.0190  0.0520  35   ILE A CG1 
164   C CG2 . ILE A 37   ? 0.2699 0.2588 0.2555 -0.0191 0.0181  0.0492  35   ILE A CG2 
165   C CD1 . ILE A 37   ? 0.2588 0.2545 0.2529 -0.0212 0.0182  0.0489  35   ILE A CD1 
166   N N   . THR A 38   ? 0.3326 0.3317 0.3125 -0.0177 0.0226  0.0528  36   THR A N   
167   C CA  . THR A 38   ? 0.2798 0.2780 0.2553 -0.0156 0.0229  0.0515  36   THR A CA  
168   C C   . THR A 38   ? 0.3249 0.3237 0.2982 -0.0165 0.0233  0.0546  36   THR A C   
169   O O   . THR A 38   ? 0.2898 0.2851 0.2601 -0.0156 0.0225  0.0543  36   THR A O   
170   C CB  . THR A 38   ? 0.3123 0.3154 0.2865 -0.0133 0.0243  0.0491  36   THR A CB  
171   O OG1 . THR A 38   ? 0.3253 0.3278 0.3019 -0.0125 0.0237  0.0466  36   THR A OG1 
172   C CG2 . THR A 38   ? 0.3074 0.3089 0.2775 -0.0110 0.0241  0.0471  36   THR A CG2 
173   N N   . ALA A 39   ? 0.2877 0.2912 0.2627 -0.0183 0.0246  0.0580  37   ALA A N   
174   C CA  . ALA A 39   ? 0.3139 0.3186 0.2870 -0.0194 0.0251  0.0617  37   ALA A CA  
175   C C   . ALA A 39   ? 0.3367 0.3344 0.3100 -0.0206 0.0230  0.0633  37   ALA A C   
176   O O   . ALA A 39   ? 0.3298 0.3267 0.3004 -0.0205 0.0229  0.0652  37   ALA A O   
177   C CB  . ALA A 39   ? 0.3259 0.3369 0.3016 -0.0216 0.0268  0.0654  37   ALA A CB  
178   N N   . ALA A 40   ? 0.2899 0.2829 0.2665 -0.0216 0.0214  0.0623  38   ALA A N   
179   C CA  . ALA A 40   ? 0.3011 0.2875 0.2787 -0.0228 0.0192  0.0634  38   ALA A CA  
180   C C   . ALA A 40   ? 0.3163 0.2976 0.2913 -0.0207 0.0178  0.0601  38   ALA A C   
181   O O   . ALA A 40   ? 0.3391 0.3152 0.3149 -0.0212 0.0159  0.0604  38   ALA A O   
182   C CB  . ALA A 40   ? 0.3107 0.2950 0.2936 -0.0250 0.0180  0.0638  38   ALA A CB  
183   N N   . TYR A 41   ? 0.2972 0.2801 0.2695 -0.0184 0.0185  0.0569  39   TYR A N   
184   C CA  . TYR A 41   ? 0.2899 0.2685 0.2603 -0.0166 0.0172  0.0536  39   TYR A CA  
185   C C   . TYR A 41   ? 0.2777 0.2522 0.2462 -0.0164 0.0159  0.0546  39   TYR A C   
186   O O   . TYR A 41   ? 0.2956 0.2654 0.2652 -0.0165 0.0142  0.0533  39   TYR A O   
187   C CB  . TYR A 41   ? 0.2916 0.2731 0.2594 -0.0143 0.0184  0.0509  39   TYR A CB  
188   C CG  . TYR A 41   ? 0.3145 0.2928 0.2815 -0.0127 0.0174  0.0473  39   TYR A CG  
189   C CD1 . TYR A 41   ? 0.2742 0.2475 0.2411 -0.0127 0.0157  0.0464  39   TYR A CD1 
190   C CD2 . TYR A 41   ? 0.3385 0.3192 0.3050 -0.0111 0.0182  0.0448  39   TYR A CD2 
191   C CE1 . TYR A 41   ? 0.2542 0.2254 0.2203 -0.0114 0.0149  0.0434  39   TYR A CE1 
192   C CE2 . TYR A 41   ? 0.2723 0.2503 0.2383 -0.0099 0.0172  0.0420  39   TYR A CE2 
193   C CZ  . TYR A 41   ? 0.2740 0.2474 0.2397 -0.0101 0.0157  0.0415  39   TYR A CZ  
194   O OH  . TYR A 41   ? 0.2836 0.2549 0.2488 -0.0091 0.0149  0.0391  39   TYR A OH  
195   N N   . ARG A 42   ? 0.3095 0.2862 0.2754 -0.0162 0.0167  0.0568  40   ARG A N   
196   C CA  . ARG A 42   ? 0.3142 0.2876 0.2782 -0.0158 0.0155  0.0578  40   ARG A CA  
197   C C   . ARG A 42   ? 0.3366 0.3113 0.3009 -0.0174 0.0156  0.0626  40   ARG A C   
198   O O   . ARG A 42   ? 0.3408 0.3157 0.3022 -0.0168 0.0155  0.0642  40   ARG A O   
199   C CB  . ARG A 42   ? 0.3654 0.3399 0.3251 -0.0134 0.0159  0.0555  40   ARG A CB  
200   C CG  . ARG A 42   ? 0.3439 0.3159 0.3036 -0.0120 0.0152  0.0513  40   ARG A CG  
201   C CD  . ARG A 42   ? 0.3395 0.3132 0.2959 -0.0099 0.0157  0.0487  40   ARG A CD  
202   N NE  . ARG A 42   ? 0.2979 0.2705 0.2551 -0.0090 0.0155  0.0454  40   ARG A NE  
203   C CZ  . ARG A 42   ? 0.2984 0.2669 0.2563 -0.0088 0.0141  0.0435  40   ARG A CZ  
204   N NH1 . ARG A 42   ? 0.2981 0.2633 0.2559 -0.0091 0.0128  0.0442  40   ARG A NH1 
205   N NH2 . ARG A 42   ? 0.3055 0.2737 0.2642 -0.0082 0.0141  0.0410  40   ARG A NH2 
206   N N   . ARG A 43   ? 0.3066 0.2821 0.2746 -0.0197 0.0158  0.0651  41   ARG A N   
207   C CA  . ARG A 43   ? 0.3878 0.3647 0.3566 -0.0217 0.0160  0.0702  41   ARG A CA  
208   C C   . ARG A 43   ? 0.3376 0.3086 0.3068 -0.0220 0.0137  0.0718  41   ARG A C   
209   O O   . ARG A 43   ? 0.3403 0.3059 0.3113 -0.0217 0.0118  0.0694  41   ARG A O   
210   C CB  . ARG A 43   ? 0.3180 0.2966 0.2916 -0.0243 0.0165  0.0722  41   ARG A CB  
211   C CG  . ARG A 43   ? 0.3406 0.3202 0.3162 -0.0269 0.0165  0.0779  41   ARG A CG  
212   C CD  . ARG A 43   ? 0.3422 0.3246 0.3224 -0.0294 0.0172  0.0793  41   ARG A CD  
213   N NE  . ARG A 43   ? 0.3295 0.3192 0.3084 -0.0285 0.0198  0.0779  41   ARG A NE  
214   C CZ  . ARG A 43   ? 0.3855 0.3778 0.3679 -0.0295 0.0205  0.0768  41   ARG A CZ  
215   N NH1 . ARG A 43   ? 0.3470 0.3356 0.3344 -0.0315 0.0189  0.0770  41   ARG A NH1 
216   N NH2 . ARG A 43   ? 0.3334 0.3323 0.3145 -0.0283 0.0227  0.0753  41   ARG A NH2 
217   N N   . PRO A 44   ? 0.3897 0.3619 0.3572 -0.0225 0.0138  0.0760  42   PRO A N   
218   C CA  . PRO A 44   ? 0.3636 0.3302 0.3318 -0.0227 0.0114  0.0779  42   PRO A CA  
219   C C   . PRO A 44   ? 0.3773 0.3384 0.3510 -0.0246 0.0093  0.0784  42   PRO A C   
220   O O   . PRO A 44   ? 0.3546 0.3171 0.3320 -0.0269 0.0098  0.0803  42   PRO A O   
221   C CB  . PRO A 44   ? 0.3666 0.3369 0.3328 -0.0237 0.0122  0.0834  42   PRO A CB  
222   C CG  . PRO A 44   ? 0.3774 0.3550 0.3395 -0.0223 0.0148  0.0821  42   PRO A CG  
223   C CD  . PRO A 44   ? 0.3731 0.3525 0.3375 -0.0225 0.0160  0.0787  42   PRO A CD  
224   N N   . GLU A 45   ? 0.3854 0.3404 0.3598 -0.0236 0.0068  0.0764  43   GLU A N   
225   C CA  . GLU A 45   ? 0.3684 0.3179 0.3482 -0.0249 0.0045  0.0760  43   GLU A CA  
226   C C   . GLU A 45   ? 0.3472 0.2956 0.3308 -0.0277 0.0037  0.0816  43   GLU A C   
227   O O   . GLU A 45   ? 0.3648 0.3112 0.3535 -0.0298 0.0027  0.0820  43   GLU A O   
228   C CB  . GLU A 45   ? 0.4057 0.3496 0.3854 -0.0230 0.0021  0.0729  43   GLU A CB  
229   C CG  . GLU A 45   ? 0.4153 0.3566 0.3977 -0.0225 0.0010  0.0681  43   GLU A CG  
230   C CD  . GLU A 45   ? 0.3748 0.3119 0.3565 -0.0203 -0.0010 0.0644  43   GLU A CD  
231   O OE1 . GLU A 45   ? 0.3711 0.3092 0.3486 -0.0183 -0.0005 0.0636  43   GLU A OE1 
232   O OE2 . GLU A 45   ? 0.3707 0.3039 0.3562 -0.0204 -0.0030 0.0621  43   GLU A OE2 
233   N N   . THR A 46   ? 0.3680 0.3179 0.3492 -0.0280 0.0040  0.0862  44   THR A N   
234   C CA  . THR A 46   ? 0.3925 0.3420 0.3771 -0.0309 0.0034  0.0924  44   THR A CA  
235   C C   . THR A 46   ? 0.4114 0.3666 0.3979 -0.0334 0.0057  0.0947  44   THR A C   
236   O O   . THR A 46   ? 0.4486 0.4030 0.4396 -0.0364 0.0050  0.0991  44   THR A O   
237   C CB  . THR A 46   ? 0.3884 0.3395 0.3694 -0.0305 0.0035  0.0970  44   THR A CB  
238   O OG1 . THR A 46   ? 0.3860 0.3442 0.3612 -0.0290 0.0063  0.0963  44   THR A OG1 
239   C CG2 . THR A 46   ? 0.4154 0.3602 0.3955 -0.0284 0.0007  0.0956  44   THR A CG2 
240   N N   . GLU A 47   ? 0.3806 0.3418 0.3641 -0.0323 0.0083  0.0919  45   GLU A N   
241   C CA  . GLU A 47   ? 0.4049 0.3718 0.3906 -0.0345 0.0105  0.0935  45   GLU A CA  
242   C C   . GLU A 47   ? 0.3711 0.3358 0.3612 -0.0351 0.0098  0.0897  45   GLU A C   
243   O O   . GLU A 47   ? 0.3744 0.3417 0.3687 -0.0377 0.0104  0.0917  45   GLU A O   
244   C CB  . GLU A 47   ? 0.4137 0.3887 0.3944 -0.0329 0.0136  0.0926  45   GLU A CB  
245   C CG  . GLU A 47   ? 0.4557 0.4338 0.4316 -0.0320 0.0144  0.0960  45   GLU A CG  
246   C CD  . GLU A 47   ? 0.5082 0.4945 0.4792 -0.0303 0.0174  0.0946  45   GLU A CD  
247   O OE1 . GLU A 47   ? 0.4810 0.4701 0.4525 -0.0296 0.0187  0.0908  45   GLU A OE1 
248   O OE2 . GLU A 47   ? 0.6233 0.6134 0.5901 -0.0296 0.0182  0.0972  45   GLU A OE2 
249   N N   . CYS A 48   ? 0.3810 0.3416 0.3705 -0.0329 0.0085  0.0843  46   CYS A N   
250   C CA  . CYS A 48   ? 0.3577 0.3165 0.3510 -0.0333 0.0076  0.0805  46   CYS A CA  
251   C C   . CYS A 48   ? 0.3787 0.3322 0.3783 -0.0357 0.0050  0.0820  46   CYS A C   
252   O O   . CYS A 48   ? 0.3822 0.3364 0.3863 -0.0376 0.0048  0.0816  46   CYS A O   
253   C CB  . CYS A 48   ? 0.3106 0.2667 0.3013 -0.0304 0.0069  0.0747  46   CYS A CB  
254   S SG  . CYS A 48   ? 0.3678 0.3296 0.3524 -0.0277 0.0097  0.0718  46   CYS A SG  
255   N N   . LEU A 49   ? 0.3352 0.2830 0.3354 -0.0355 0.0026  0.0835  47   LEU A N   
256   C CA  . LEU A 49   ? 0.3829 0.3243 0.3891 -0.0369 -0.0005 0.0830  47   LEU A CA  
257   C C   . LEU A 49   ? 0.3532 0.2948 0.3652 -0.0407 -0.0010 0.0879  47   LEU A C   
258   O O   . LEU A 49   ? 0.3938 0.3330 0.4112 -0.0421 -0.0026 0.0861  47   LEU A O   
259   C CB  . LEU A 49   ? 0.3688 0.3039 0.3744 -0.0353 -0.0032 0.0828  47   LEU A CB  
260   C CG  . LEU A 49   ? 0.3826 0.3146 0.3868 -0.0323 -0.0044 0.0763  47   LEU A CG  
261   C CD1 . LEU A 49   ? 0.3899 0.3188 0.3994 -0.0330 -0.0065 0.0727  47   LEU A CD1 
262   C CD2 . LEU A 49   ? 0.3465 0.2836 0.3451 -0.0302 -0.0018 0.0732  47   LEU A CD2 
263   N N   . PRO A 50   ? 0.4188 0.3635 0.4301 -0.0425 0.0003  0.0941  48   PRO A N   
264   C CA  . PRO A 50   ? 0.3821 0.3266 0.3996 -0.0465 -0.0005 0.0993  48   PRO A CA  
265   C C   . PRO A 50   ? 0.3798 0.3278 0.4014 -0.0484 0.0005  0.0976  48   PRO A C   
266   O O   . PRO A 50   ? 0.3814 0.3257 0.4097 -0.0508 -0.0017 0.0982  48   PRO A O   
267   C CB  . PRO A 50   ? 0.4292 0.3790 0.4435 -0.0476 0.0017  0.1057  48   PRO A CB  
268   C CG  . PRO A 50   ? 0.3982 0.3464 0.4065 -0.0444 0.0015  0.1047  48   PRO A CG  
269   C CD  . PRO A 50   ? 0.3749 0.3226 0.3802 -0.0411 0.0019  0.0971  48   PRO A CD  
270   N N   . PRO A 51   ? 0.3678 0.3227 0.3860 -0.0473 0.0035  0.0954  49   PRO A N   
271   C CA  . PRO A 51   ? 0.4015 0.3594 0.4240 -0.0490 0.0040  0.0935  49   PRO A CA  
272   C C   . PRO A 51   ? 0.3918 0.3446 0.4170 -0.0478 0.0015  0.0876  49   PRO A C   
273   O O   . PRO A 51   ? 0.4344 0.3874 0.4651 -0.0499 0.0006  0.0867  49   PRO A O   
274   C CB  . PRO A 51   ? 0.3807 0.3469 0.3983 -0.0474 0.0076  0.0923  49   PRO A CB  
275   C CG  . PRO A 51   ? 0.4058 0.3715 0.4166 -0.0442 0.0083  0.0908  49   PRO A CG  
276   C CD  . PRO A 51   ? 0.3878 0.3485 0.3989 -0.0448 0.0064  0.0948  49   PRO A CD  
277   N N   . LEU A 52   ? 0.3768 0.3257 0.3984 -0.0447 0.0005  0.0833  50   LEU A N   
278   C CA  . LEU A 52   ? 0.3538 0.2981 0.3781 -0.0436 -0.0021 0.0779  50   LEU A CA  
279   C C   . LEU A 52   ? 0.3903 0.3279 0.4211 -0.0457 -0.0056 0.0793  50   LEU A C   
280   O O   . LEU A 52   ? 0.3857 0.3216 0.4219 -0.0470 -0.0074 0.0770  50   LEU A O   
281   C CB  . LEU A 52   ? 0.3481 0.2903 0.3670 -0.0398 -0.0023 0.0734  50   LEU A CB  
282   C CG  . LEU A 52   ? 0.3540 0.3019 0.3668 -0.0376 0.0007  0.0715  50   LEU A CG  
283   C CD1 . LEU A 52   ? 0.3017 0.2474 0.3094 -0.0342 0.0004  0.0680  50   LEU A CD1 
284   C CD2 . LEU A 52   ? 0.3243 0.2761 0.3388 -0.0379 0.0016  0.0684  50   LEU A CD2 
285   N N   . VAL A 53   ? 0.3732 0.3070 0.4038 -0.0460 -0.0067 0.0832  51   VAL A N   
286   C CA  . VAL A 53   ? 0.3854 0.3126 0.4226 -0.0480 -0.0102 0.0851  51   VAL A CA  
287   C C   . VAL A 53   ? 0.3996 0.3286 0.4435 -0.0520 -0.0104 0.0881  51   VAL A C   
288   O O   . VAL A 53   ? 0.4339 0.3586 0.4841 -0.0533 -0.0133 0.0859  51   VAL A O   
289   C CB  . VAL A 53   ? 0.4014 0.3254 0.4371 -0.0481 -0.0110 0.0902  51   VAL A CB  
290   C CG1 . VAL A 53   ? 0.4213 0.3386 0.4646 -0.0507 -0.0146 0.0932  51   VAL A CG1 
291   C CG2 . VAL A 53   ? 0.3969 0.3183 0.4273 -0.0442 -0.0115 0.0867  51   VAL A CG2 
292   N N   . GLU A 54   ? 0.3986 0.3342 0.4413 -0.0540 -0.0074 0.0928  52   GLU A N   
293   C CA  . GLU A 54   ? 0.4295 0.3676 0.4787 -0.0580 -0.0073 0.0960  52   GLU A CA  
294   C C   . GLU A 54   ? 0.4303 0.3700 0.4824 -0.0580 -0.0077 0.0904  52   GLU A C   
295   O O   . GLU A 54   ? 0.4474 0.3847 0.5068 -0.0606 -0.0100 0.0903  52   GLU A O   
296   C CB  . GLU A 54   ? 0.4298 0.3760 0.4765 -0.0598 -0.0036 0.1017  52   GLU A CB  
297   N N   . ALA A 55   ? 0.4052 0.3488 0.4520 -0.0550 -0.0057 0.0858  53   ALA A N   
298   C CA  . ALA A 55   ? 0.4302 0.3761 0.4792 -0.0547 -0.0059 0.0808  53   ALA A CA  
299   C C   . ALA A 55   ? 0.4256 0.3649 0.4782 -0.0538 -0.0097 0.0757  53   ALA A C   
300   O O   . ALA A 55   ? 0.4149 0.3548 0.4722 -0.0549 -0.0110 0.0727  53   ALA A O   
301   C CB  . ALA A 55   ? 0.3867 0.3382 0.4289 -0.0516 -0.0030 0.0776  53   ALA A CB  
302   N N   . ALA A 56   ? 0.4294 0.3628 0.4800 -0.0516 -0.0115 0.0742  54   ALA A N   
303   C CA  . ALA A 56   ? 0.4008 0.3282 0.4544 -0.0503 -0.0151 0.0689  54   ALA A CA  
304   C C   . ALA A 56   ? 0.4370 0.3581 0.4984 -0.0529 -0.0187 0.0711  54   ALA A C   
305   O O   . ALA A 56   ? 0.4467 0.3626 0.5114 -0.0519 -0.0220 0.0666  54   ALA A O   
306   C CB  . ALA A 56   ? 0.4044 0.3291 0.4521 -0.0464 -0.0154 0.0659  54   ALA A CB  
307   N N   . THR A 57   ? 0.4873 0.4089 0.5518 -0.0563 -0.0182 0.0777  55   THR A N   
308   C CA  . THR A 57   ? 0.4727 0.3877 0.5447 -0.0590 -0.0217 0.0806  55   THR A CA  
309   C C   . THR A 57   ? 0.4932 0.4076 0.5732 -0.0614 -0.0240 0.0780  55   THR A C   
310   O O   . THR A 57   ? 0.5341 0.4545 0.6155 -0.0635 -0.0220 0.0789  55   THR A O   
311   C CB  . THR A 57   ? 0.4529 0.3694 0.5256 -0.0620 -0.0202 0.0891  55   THR A CB  
312   O OG1 . THR A 57   ? 0.4865 0.4030 0.5520 -0.0596 -0.0187 0.0911  55   THR A OG1 
313   C CG2 . THR A 57   ? 0.4752 0.3849 0.5564 -0.0653 -0.0239 0.0928  55   THR A CG2 
314   N N   . GLN A 58   ? 0.4857 0.3929 0.5710 -0.0610 -0.0282 0.0744  56   GLN A N   
315   C CA  . GLN A 58   ? 0.5370 0.4427 0.6303 -0.0631 -0.0311 0.0712  56   GLN A CA  
316   C C   . GLN A 58   ? 0.5172 0.4155 0.6192 -0.0661 -0.0349 0.0747  56   GLN A C   
317   O O   . GLN A 58   ? 0.5315 0.4247 0.6329 -0.0657 -0.0360 0.0781  56   GLN A O   
318   C CB  . GLN A 58   ? 0.5395 0.4439 0.6318 -0.0595 -0.0330 0.0623  56   GLN A CB  
319   C CG  . GLN A 58   ? 0.4979 0.4091 0.5820 -0.0565 -0.0296 0.0589  56   GLN A CG  
320   C CD  . GLN A 58   ? 0.4565 0.3686 0.5413 -0.0544 -0.0313 0.0510  56   GLN A CD  
321   O OE1 . GLN A 58   ? 0.5325 0.4473 0.6219 -0.0563 -0.0320 0.0494  56   GLN A OE1 
322   N NE2 . GLN A 58   ? 0.5042 0.4145 0.5847 -0.0505 -0.0321 0.0461  56   GLN A NE2 
323   N N   . SER A 59   ? 0.5342 0.4318 0.6443 -0.0691 -0.0371 0.0737  57   SER A N   
324   C CA  . SER A 59   ? 0.5786 0.4695 0.6980 -0.0726 -0.0408 0.0774  57   SER A CA  
325   C C   . SER A 59   ? 0.5705 0.4522 0.6924 -0.0700 -0.0453 0.0732  57   SER A C   
326   O O   . SER A 59   ? 0.5364 0.4177 0.6545 -0.0659 -0.0460 0.0661  57   SER A O   
327   C CB  . SER A 59   ? 0.5717 0.4641 0.6997 -0.0762 -0.0424 0.0763  57   SER A CB  
328   O OG  . SER A 59   ? 0.5667 0.4572 0.6970 -0.0740 -0.0454 0.0675  57   SER A OG  
329   N N   . LYS A 60   ? 0.5651 0.4397 0.6938 -0.0725 -0.0484 0.0778  58   LYS A N   
330   C CA  . LYS A 60   ? 0.5952 0.4607 0.7275 -0.0703 -0.0531 0.0742  58   LYS A CA  
331   C C   . LYS A 60   ? 0.5455 0.4093 0.6820 -0.0684 -0.0564 0.0647  58   LYS A C   
332   O O   . LYS A 60   ? 0.5612 0.4224 0.6950 -0.0641 -0.0580 0.0582  58   LYS A O   
333   C CB  . LYS A 60   ? 0.5746 0.4327 0.7152 -0.0739 -0.0563 0.0809  58   LYS A CB  
334   C CG  . LYS A 60   ? 0.6557 0.5037 0.8017 -0.0718 -0.0618 0.0769  58   LYS A CG  
335   C CD  . LYS A 60   ? 0.6632 0.5098 0.8013 -0.0668 -0.0612 0.0745  58   LYS A CD  
336   C CE  . LYS A 60   ? 0.6784 0.5149 0.8224 -0.0647 -0.0667 0.0713  58   LYS A CE  
337   N NZ  . LYS A 60   ? 0.7256 0.5609 0.8623 -0.0601 -0.0662 0.0699  58   LYS A NZ  
338   N N   . GLU A 61   ? 0.5474 0.4130 0.6906 -0.0716 -0.0574 0.0636  59   GLU A N   
339   C CA  . GLU A 61   ? 0.5177 0.3824 0.6651 -0.0700 -0.0607 0.0545  59   GLU A CA  
340   C C   . GLU A 61   ? 0.5497 0.4205 0.6880 -0.0655 -0.0581 0.0478  59   GLU A C   
341   O O   . GLU A 61   ? 0.5778 0.4463 0.7160 -0.0619 -0.0607 0.0402  59   GLU A O   
342   C CB  . GLU A 61   ? 0.5385 0.4056 0.6938 -0.0744 -0.0616 0.0551  59   GLU A CB  
343   N N   . ILE A 62   ? 0.5435 0.4224 0.6744 -0.0655 -0.0531 0.0506  60   ILE A N   
344   C CA  . ILE A 62   ? 0.5104 0.3952 0.6329 -0.0615 -0.0506 0.0449  60   ILE A CA  
345   C C   . ILE A 62   ? 0.5079 0.3895 0.6244 -0.0572 -0.0508 0.0426  60   ILE A C   
346   O O   . ILE A 62   ? 0.5378 0.4205 0.6511 -0.0534 -0.0515 0.0354  60   ILE A O   
347   C CB  . ILE A 62   ? 0.4892 0.3828 0.6055 -0.0625 -0.0453 0.0489  60   ILE A CB  
348   C CG1 . ILE A 62   ? 0.5381 0.4362 0.6598 -0.0658 -0.0453 0.0486  60   ILE A CG1 
349   C CG2 . ILE A 62   ? 0.4884 0.3869 0.5949 -0.0582 -0.0424 0.0448  60   ILE A CG2 
350   C CD1 . ILE A 62   ? 0.5085 0.4155 0.6249 -0.0666 -0.0404 0.0519  60   ILE A CD1 
351   N N   . ARG A 63   ? 0.5083 0.3863 0.6233 -0.0576 -0.0502 0.0486  61   ARG A N   
352   C CA  . ARG A 63   ? 0.4962 0.3711 0.6058 -0.0535 -0.0505 0.0466  61   ARG A CA  
353   C C   . ARG A 63   ? 0.5230 0.3911 0.6384 -0.0514 -0.0556 0.0402  61   ARG A C   
354   O O   . ARG A 63   ? 0.5320 0.4001 0.6431 -0.0472 -0.0561 0.0345  61   ARG A O   
355   C CB  . ARG A 63   ? 0.5123 0.3850 0.6196 -0.0545 -0.0490 0.0546  61   ARG A CB  
356   C CG  . ARG A 63   ? 0.5763 0.4566 0.6754 -0.0548 -0.0436 0.0591  61   ARG A CG  
357   C CD  . ARG A 63   ? 0.5456 0.4243 0.6414 -0.0553 -0.0422 0.0664  61   ARG A CD  
358   N NE  . ARG A 63   ? 0.5608 0.4373 0.6628 -0.0599 -0.0430 0.0739  61   ARG A NE  
359   C CZ  . ARG A 63   ? 0.6299 0.4988 0.7373 -0.0610 -0.0463 0.0774  61   ARG A CZ  
360   N NH1 . ARG A 63   ? 0.6939 0.5565 0.8013 -0.0578 -0.0493 0.0740  61   ARG A NH1 
361   N NH2 . ARG A 63   ? 0.6446 0.5123 0.7575 -0.0656 -0.0468 0.0847  61   ARG A NH2 
362   N N   . ASP A 64   ? 0.5460 0.4083 0.6713 -0.0543 -0.0596 0.0409  62   ASP A N   
363   C CA  . ASP A 64   ? 0.5547 0.4105 0.6863 -0.0523 -0.0649 0.0343  62   ASP A CA  
364   C C   . ASP A 64   ? 0.5252 0.3855 0.6557 -0.0497 -0.0655 0.0250  62   ASP A C   
365   O O   . ASP A 64   ? 0.5293 0.3884 0.6580 -0.0455 -0.0672 0.0184  62   ASP A O   
366   C CB  . ASP A 64   ? 0.5938 0.4427 0.7368 -0.0563 -0.0690 0.0372  62   ASP A CB  
367   C CG  . ASP A 64   ? 0.5868 0.4290 0.7320 -0.0579 -0.0700 0.0450  62   ASP A CG  
368   O OD1 . ASP A 64   ? 0.6049 0.4487 0.7425 -0.0562 -0.0671 0.0488  62   ASP A OD1 
369   O OD2 . ASP A 64   ? 0.6574 0.4929 0.8122 -0.0609 -0.0740 0.0475  62   ASP A OD2 
370   N N   . ALA A 65   ? 0.4974 0.3633 0.6290 -0.0520 -0.0641 0.0245  63   ALA A N   
371   C CA  . ALA A 65   ? 0.5069 0.3780 0.6371 -0.0496 -0.0645 0.0162  63   ALA A CA  
372   C C   . ALA A 65   ? 0.5034 0.3800 0.6230 -0.0454 -0.0611 0.0133  63   ALA A C   
373   O O   . ALA A 65   ? 0.5278 0.4058 0.6458 -0.0419 -0.0625 0.0058  63   ALA A O   
374   C CB  . ALA A 65   ? 0.5104 0.3870 0.6430 -0.0530 -0.0631 0.0172  63   ALA A CB  
375   N N   . ALA A 66   ? 0.4941 0.3740 0.6064 -0.0457 -0.0566 0.0193  64   ALA A N   
376   C CA  . ALA A 66   ? 0.5297 0.4146 0.6324 -0.0420 -0.0534 0.0170  64   ALA A CA  
377   C C   . ALA A 66   ? 0.5093 0.3897 0.6107 -0.0382 -0.0556 0.0132  64   ALA A C   
378   O O   . ALA A 66   ? 0.5090 0.3929 0.6058 -0.0346 -0.0553 0.0073  64   ALA A O   
379   C CB  . ALA A 66   ? 0.4868 0.3754 0.5828 -0.0431 -0.0486 0.0242  64   ALA A CB  
380   N N   . ALA A 67   ? 0.5169 0.3899 0.6223 -0.0389 -0.0579 0.0167  65   ALA A N   
381   C CA  . ALA A 67   ? 0.5599 0.4287 0.6647 -0.0351 -0.0602 0.0131  65   ALA A CA  
382   C C   . ALA A 67   ? 0.5294 0.3967 0.6391 -0.0328 -0.0644 0.0041  65   ALA A C   
383   O O   . ALA A 67   ? 0.5442 0.4124 0.6508 -0.0287 -0.0650 -0.0014 65   ALA A O   
384   C CB  . ALA A 67   ? 0.4975 0.3584 0.6063 -0.0365 -0.0621 0.0190  65   ALA A CB  
385   N N   . SER A 68   ? 0.5419 0.4076 0.6595 -0.0352 -0.0672 0.0023  66   SER A N   
386   C CA  . SER A 68   ? 0.5483 0.4134 0.6708 -0.0330 -0.0712 -0.0068 66   SER A CA  
387   C C   . SER A 68   ? 0.5528 0.4267 0.6685 -0.0304 -0.0689 -0.0127 66   SER A C   
388   O O   . SER A 68   ? 0.5298 0.4051 0.6442 -0.0264 -0.0705 -0.0199 66   SER A O   
389   C CB  . SER A 68   ? 0.4758 0.3372 0.6083 -0.0366 -0.0748 -0.0070 66   SER A CB  
390   N N   . THR A 69   ? 0.5464 0.4268 0.6579 -0.0324 -0.0652 -0.0097 67   THR A N   
391   C CA  . THR A 69   ? 0.4971 0.3860 0.6022 -0.0300 -0.0629 -0.0145 67   THR A CA  
392   C C   . THR A 69   ? 0.5176 0.4091 0.6143 -0.0262 -0.0605 -0.0157 67   THR A C   
393   O O   . THR A 69   ? 0.5198 0.4157 0.6137 -0.0229 -0.0610 -0.0223 67   THR A O   
394   C CB  . THR A 69   ? 0.4557 0.3505 0.5579 -0.0329 -0.0592 -0.0101 67   THR A CB  
395   O OG1 . THR A 69   ? 0.4711 0.3639 0.5815 -0.0365 -0.0615 -0.0092 67   THR A OG1 
396   C CG2 . THR A 69   ? 0.4524 0.3558 0.5482 -0.0306 -0.0571 -0.0147 67   THR A CG2 
397   N N   . ALA A 70   ? 0.4932 0.3826 0.5860 -0.0266 -0.0580 -0.0093 68   ALA A N   
398   C CA  . ALA A 70   ? 0.5201 0.4118 0.6053 -0.0232 -0.0558 -0.0102 68   ALA A CA  
399   C C   . ALA A 70   ? 0.5612 0.4493 0.6491 -0.0197 -0.0594 -0.0161 68   ALA A C   
400   O O   . ALA A 70   ? 0.5421 0.4345 0.6248 -0.0163 -0.0584 -0.0203 68   ALA A O   
401   C CB  . ALA A 70   ? 0.4864 0.3764 0.5676 -0.0245 -0.0528 -0.0022 68   ALA A CB  
402   N N   . ARG A 71   ? 0.5588 0.4392 0.6549 -0.0206 -0.0636 -0.0163 69   ARG A N   
403   C CA  . ARG A 71   ? 0.5795 0.4563 0.6790 -0.0171 -0.0674 -0.0225 69   ARG A CA  
404   C C   . ARG A 71   ? 0.5379 0.4197 0.6384 -0.0147 -0.0693 -0.0317 69   ARG A C   
405   O O   . ARG A 71   ? 0.6230 0.5071 0.7211 -0.0107 -0.0700 -0.0375 69   ARG A O   
406   C CB  . ARG A 71   ? 0.5789 0.4460 0.6876 -0.0187 -0.0718 -0.0206 69   ARG A CB  
407   C CG  . ARG A 71   ? 0.6209 0.4838 0.7347 -0.0151 -0.0765 -0.0278 69   ARG A CG  
408   C CD  . ARG A 71   ? 0.5889 0.4415 0.7113 -0.0165 -0.0806 -0.0247 69   ARG A CD  
409   N NE  . ARG A 71   ? 0.6403 0.4895 0.7593 -0.0155 -0.0794 -0.0194 69   ARG A NE  
410   C CZ  . ARG A 71   ? 0.6613 0.5104 0.7778 -0.0113 -0.0802 -0.0233 69   ARG A CZ  
411   N NH1 . ARG A 71   ? 0.6948 0.5474 0.8117 -0.0075 -0.0820 -0.0324 69   ARG A NH1 
412   N NH2 . ARG A 71   ? 0.6977 0.5439 0.8113 -0.0107 -0.0791 -0.0179 69   ARG A NH2 
413   N N   . LYS A 72   ? 0.5308 0.4148 0.6346 -0.0169 -0.0700 -0.0331 70   LYS A N   
414   C CA  . LYS A 72   ? 0.5614 0.4510 0.6658 -0.0147 -0.0717 -0.0416 70   LYS A CA  
415   C C   . LYS A 72   ? 0.6023 0.5011 0.6970 -0.0122 -0.0678 -0.0435 70   LYS A C   
416   O O   . LYS A 72   ? 0.6044 0.5074 0.6975 -0.0086 -0.0689 -0.0507 70   LYS A O   
417   C CB  . LYS A 72   ? 0.5228 0.4133 0.6324 -0.0180 -0.0729 -0.0420 70   LYS A CB  
418   N N   . LEU A 73   ? 0.5777 0.4799 0.6659 -0.0140 -0.0632 -0.0371 71   LEU A N   
419   C CA  . LEU A 73   ? 0.5501 0.4607 0.6295 -0.0119 -0.0595 -0.0382 71   LEU A CA  
420   C C   . LEU A 73   ? 0.5701 0.4807 0.6454 -0.0084 -0.0589 -0.0398 71   LEU A C   
421   O O   . LEU A 73   ? 0.5578 0.4747 0.6289 -0.0054 -0.0583 -0.0448 71   LEU A O   
422   C CB  . LEU A 73   ? 0.4899 0.4033 0.5640 -0.0145 -0.0550 -0.0310 71   LEU A CB  
423   C CG  . LEU A 73   ? 0.4965 0.4114 0.5735 -0.0180 -0.0547 -0.0288 71   LEU A CG  
424   C CD1 . LEU A 73   ? 0.5287 0.4453 0.6007 -0.0202 -0.0503 -0.0211 71   LEU A CD1 
425   C CD2 . LEU A 73   ? 0.4915 0.4137 0.5675 -0.0167 -0.0552 -0.0348 71   LEU A CD2 
426   N N   . ILE A 74   ? 0.5569 0.4609 0.6332 -0.0088 -0.0590 -0.0352 72   ILE A N   
427   C CA  . ILE A 74   ? 0.5859 0.4901 0.6584 -0.0056 -0.0583 -0.0362 72   ILE A CA  
428   C C   . ILE A 74   ? 0.6680 0.5715 0.7447 -0.0021 -0.0624 -0.0444 72   ILE A C   
429   O O   . ILE A 74   ? 0.6436 0.5512 0.7163 0.0012  -0.0617 -0.0481 72   ILE A O   
430   C CB  . ILE A 74   ? 0.5887 0.4863 0.6614 -0.0070 -0.0577 -0.0291 72   ILE A CB  
431   N N   . GLU A 75   ? 0.7116 0.6100 0.7966 -0.0028 -0.0667 -0.0475 73   GLU A N   
432   C CA  . GLU A 75   ? 0.7380 0.6361 0.8276 0.0006  -0.0708 -0.0562 73   GLU A CA  
433   C C   . GLU A 75   ? 0.7296 0.6375 0.8154 0.0029  -0.0700 -0.0630 73   GLU A C   
434   O O   . GLU A 75   ? 0.7551 0.6671 0.8389 0.0067  -0.0706 -0.0688 73   GLU A O   
435   C CB  . GLU A 75   ? 0.7009 0.5913 0.8008 -0.0010 -0.0757 -0.0578 73   GLU A CB  
436   C CG  . GLU A 75   ? 0.7657 0.6462 0.8706 -0.0011 -0.0782 -0.0544 73   GLU A CG  
437   C CD  . GLU A 75   ? 0.8049 0.6769 0.9199 -0.0038 -0.0825 -0.0534 73   GLU A CD  
438   O OE1 . GLU A 75   ? 0.7545 0.6282 0.8727 -0.0060 -0.0834 -0.0551 73   GLU A OE1 
439   O OE2 . GLU A 75   ? 0.7994 0.6630 0.9193 -0.0039 -0.0851 -0.0508 73   GLU A OE2 
440   N N   . ALA A 76   ? 0.6670 0.5793 0.7518 0.0006  -0.0687 -0.0623 74   ALA A N   
441   C CA  . ALA A 76   ? 0.6601 0.5823 0.7403 0.0025  -0.0676 -0.0677 74   ALA A CA  
442   C C   . ALA A 76   ? 0.6718 0.6005 0.7432 0.0047  -0.0636 -0.0666 74   ALA A C   
443   O O   . ALA A 76   ? 0.7233 0.6587 0.7921 0.0080  -0.0638 -0.0727 74   ALA A O   
444   C CB  . ALA A 76   ? 0.6413 0.5667 0.7209 -0.0007 -0.0662 -0.0653 74   ALA A CB  
445   N N   . LEU A 77   ? 0.6662 0.5932 0.7329 0.0028  -0.0600 -0.0588 75   LEU A N   
446   C CA  . LEU A 77   ? 0.6613 0.5941 0.7199 0.0044  -0.0561 -0.0572 75   LEU A CA  
447   C C   . LEU A 77   ? 0.7042 0.6370 0.7630 0.0082  -0.0575 -0.0615 75   LEU A C   
448   O O   . LEU A 77   ? 0.6726 0.6129 0.7263 0.0107  -0.0559 -0.0646 75   LEU A O   
449   C CB  . LEU A 77   ? 0.6497 0.5796 0.7045 0.0018  -0.0526 -0.0483 75   LEU A CB  
450   C CG  . LEU A 77   ? 0.5925 0.5280 0.6416 -0.0002 -0.0488 -0.0443 75   LEU A CG  
451   C CD1 . LEU A 77   ? 0.5779 0.5101 0.6238 -0.0023 -0.0456 -0.0363 75   LEU A CD1 
452   C CD2 . LEU A 77   ? 0.6210 0.5657 0.6641 0.0022  -0.0469 -0.0479 75   LEU A CD2 
453   N N   . ARG A 78   ? 0.7065 0.6310 0.7710 0.0085  -0.0605 -0.0614 76   ARG A N   
454   C CA  . ARG A 78   ? 0.7181 0.6422 0.7832 0.0122  -0.0619 -0.0653 76   ARG A CA  
455   C C   . ARG A 78   ? 0.7185 0.6466 0.7869 0.0156  -0.0653 -0.0749 76   ARG A C   
456   O O   . ARG A 78   ? 0.7535 0.6849 0.8208 0.0191  -0.0657 -0.0792 76   ARG A O   
457   C CB  . ARG A 78   ? 0.7110 0.6248 0.7811 0.0115  -0.0641 -0.0616 76   ARG A CB  
458   C CG  . ARG A 78   ? 0.6792 0.5903 0.7448 0.0089  -0.0606 -0.0524 76   ARG A CG  
459   C CD  . ARG A 78   ? 0.6114 0.5140 0.6805 0.0091  -0.0624 -0.0490 76   ARG A CD  
460   N NE  . ARG A 78   ? 0.6200 0.5234 0.6826 0.0085  -0.0586 -0.0427 76   ARG A NE  
461   C CZ  . ARG A 78   ? 0.6465 0.5436 0.7102 0.0081  -0.0591 -0.0378 76   ARG A CZ  
462   N NH1 . ARG A 78   ? 0.6406 0.5296 0.7115 0.0081  -0.0631 -0.0378 76   ARG A NH1 
463   N NH2 . ARG A 78   ? 0.6629 0.5620 0.7203 0.0077  -0.0555 -0.0328 76   ARG A NH2 
464   N N   . GLY A 79   ? 0.7060 0.6347 0.7787 0.0147  -0.0677 -0.0787 77   GLY A N   
465   C CA  . GLY A 79   ? 0.7454 0.6788 0.8211 0.0180  -0.0708 -0.0882 77   GLY A CA  
466   C C   . GLY A 79   ? 0.7466 0.6919 0.8159 0.0192  -0.0683 -0.0915 77   GLY A C   
467   O O   . GLY A 79   ? 0.7555 0.7053 0.8270 0.0203  -0.0705 -0.0981 77   GLY A O   
468   N N   . LYS A 80   ? 0.7760 0.7264 0.8373 0.0189  -0.0637 -0.0869 78   LYS A N   
469   C CA  . LYS A 80   ? 0.7738 0.7357 0.8284 0.0199  -0.0610 -0.0890 78   LYS A CA  
470   C C   . LYS A 80   ? 0.7596 0.7250 0.8066 0.0196  -0.0564 -0.0834 78   LYS A C   
471   O O   . LYS A 80   ? 0.8449 0.8191 0.8870 0.0218  -0.0546 -0.0860 78   LYS A O   
472   C CB  . LYS A 80   ? 0.7685 0.7331 0.8227 0.0173  -0.0606 -0.0880 78   LYS A CB  
473   C CG  . LYS A 80   ? 0.7368 0.6957 0.7901 0.0131  -0.0583 -0.0792 78   LYS A CG  
474   C CD  . LYS A 80   ? 0.6891 0.6509 0.7427 0.0108  -0.0583 -0.0789 78   LYS A CD  
475   C CE  . LYS A 80   ? 0.6383 0.5962 0.6902 0.0069  -0.0555 -0.0702 78   LYS A CE  
476   N NZ  . LYS A 80   ? 0.5596 0.5208 0.6118 0.0047  -0.0554 -0.0698 78   LYS A NZ  
477   N N   . GLY A 85   ? 0.6255 0.6486 0.6292 0.0277  -0.0327 -0.0754 83   GLY A N   
478   C CA  . GLY A 85   ? 0.5781 0.6107 0.5759 0.0267  -0.0294 -0.0728 83   GLY A CA  
479   C C   . GLY A 85   ? 0.6144 0.6515 0.6095 0.0276  -0.0271 -0.0714 83   GLY A C   
480   O O   . GLY A 85   ? 0.5387 0.5836 0.5340 0.0303  -0.0275 -0.0766 83   GLY A O   
481   N N   . VAL A 86   ? 0.5775 0.6102 0.5702 0.0252  -0.0247 -0.0646 84   VAL A N   
482   C CA  . VAL A 86   ? 0.5603 0.5959 0.5514 0.0258  -0.0229 -0.0632 84   VAL A CA  
483   C C   . VAL A 86   ? 0.5462 0.5790 0.5418 0.0288  -0.0254 -0.0681 84   VAL A C   
484   O O   . VAL A 86   ? 0.5046 0.5436 0.4998 0.0308  -0.0247 -0.0705 84   VAL A O   
485   C CB  . VAL A 86   ? 0.5670 0.5967 0.5556 0.0228  -0.0205 -0.0555 84   VAL A CB  
486   C CG1 . VAL A 86   ? 0.5820 0.6149 0.5692 0.0234  -0.0187 -0.0541 84   VAL A CG1 
487   C CG2 . VAL A 86   ? 0.5952 0.6278 0.5799 0.0202  -0.0183 -0.0510 84   VAL A CG2 
488   N N   . GLU A 87   ? 0.5732 0.5968 0.5733 0.0292  -0.0284 -0.0697 85   GLU A N   
489   C CA  . GLU A 87   ? 0.5571 0.5770 0.5620 0.0321  -0.0311 -0.0740 85   GLU A CA  
490   C C   . GLU A 87   ? 0.5285 0.5572 0.5352 0.0357  -0.0328 -0.0823 85   GLU A C   
491   O O   . GLU A 87   ? 0.5490 0.5797 0.5577 0.0385  -0.0337 -0.0858 85   GLU A O   
492   C CB  . GLU A 87   ? 0.6037 0.6119 0.6135 0.0315  -0.0341 -0.0735 85   GLU A CB  
493   N N   . GLY A 88   ? 0.5285 0.5630 0.5345 0.0359  -0.0333 -0.0856 86   GLY A N   
494   C CA  . GLY A 88   ? 0.4898 0.5340 0.4969 0.0394  -0.0346 -0.0936 86   GLY A CA  
495   C C   . GLY A 88   ? 0.4691 0.5251 0.4720 0.0403  -0.0316 -0.0936 86   GLY A C   
496   O O   . GLY A 88   ? 0.4557 0.5188 0.4602 0.0437  -0.0326 -0.0998 86   GLY A O   
497   N N   . LEU A 89   ? 0.4747 0.5332 0.4724 0.0372  -0.0280 -0.0868 87   LEU A N   
498   C CA  . LEU A 89   ? 0.4348 0.5041 0.4287 0.0375  -0.0250 -0.0859 87   LEU A CA  
499   C C   . LEU A 89   ? 0.4091 0.4761 0.4048 0.0388  -0.0249 -0.0856 87   LEU A C   
500   O O   . LEU A 89   ? 0.3875 0.4633 0.3834 0.0413  -0.0245 -0.0897 87   LEU A O   
501   C CB  . LEU A 89   ? 0.4994 0.5705 0.4879 0.0337  -0.0216 -0.0783 87   LEU A CB  
502   C CG  . LEU A 89   ? 0.4840 0.5686 0.4679 0.0334  -0.0186 -0.0774 87   LEU A CG  
503   C CD1 . LEU A 89   ? 0.5152 0.5987 0.4948 0.0295  -0.0159 -0.0695 87   LEU A CD1 
504   C CD2 . LEU A 89   ? 0.5244 0.6148 0.5084 0.0348  -0.0173 -0.0782 87   LEU A CD2 
505   N N   . VAL A 90   ? 0.4433 0.4988 0.4404 0.0372  -0.0252 -0.0810 88   VAL A N   
506   C CA  . VAL A 90   ? 0.4039 0.4561 0.4030 0.0384  -0.0255 -0.0807 88   VAL A CA  
507   C C   . VAL A 90   ? 0.4752 0.5288 0.4794 0.0428  -0.0288 -0.0887 88   VAL A C   
508   O O   . VAL A 90   ? 0.4144 0.4732 0.4195 0.0450  -0.0285 -0.0913 88   VAL A O   
509   C CB  . VAL A 90   ? 0.4226 0.4618 0.4225 0.0361  -0.0258 -0.0747 88   VAL A CB  
510   C CG1 . VAL A 90   ? 0.4518 0.4867 0.4549 0.0380  -0.0271 -0.0754 88   VAL A CG1 
511   C CG2 . VAL A 90   ? 0.4082 0.4473 0.4032 0.0323  -0.0224 -0.0671 88   VAL A CG2 
512   N N   . GLN A 91   ? 0.4638 0.5126 0.4716 0.0440  -0.0320 -0.0929 89   GLN A N   
513   C CA  . GLN A 91   ? 0.4632 0.5127 0.4764 0.0483  -0.0355 -0.1010 89   GLN A CA  
514   C C   . GLN A 91   ? 0.4472 0.5112 0.4592 0.0511  -0.0348 -0.1073 89   GLN A C   
515   O O   . GLN A 91   ? 0.4308 0.4993 0.4454 0.0545  -0.0358 -0.1122 89   GLN A O   
516   C CB  . GLN A 91   ? 0.4918 0.5330 0.5095 0.0486  -0.0392 -0.1040 89   GLN A CB  
517   N N   . GLU A 92   ? 0.4613 0.5335 0.4695 0.0499  -0.0331 -0.1074 90   GLU A N   
518   C CA  . GLU A 92   ? 0.4085 0.4949 0.4157 0.0527  -0.0328 -0.1139 90   GLU A CA  
519   C C   . GLU A 92   ? 0.4554 0.5513 0.4602 0.0534  -0.0299 -0.1131 90   GLU A C   
520   O O   . GLU A 92   ? 0.4013 0.5068 0.4078 0.0570  -0.0306 -0.1197 90   GLU A O   
521   C CB  . GLU A 92   ? 0.4474 0.5406 0.4504 0.0509  -0.0313 -0.1131 90   GLU A CB  
522   C CG  . GLU A 92   ? 0.4625 0.5713 0.4641 0.0538  -0.0310 -0.1198 90   GLU A CG  
523   C CD  . GLU A 92   ? 0.5132 0.6291 0.5103 0.0521  -0.0296 -0.1187 90   GLU A CD  
524   O OE1 . GLU A 92   ? 0.5332 0.6423 0.5281 0.0484  -0.0286 -0.1121 90   GLU A OE1 
525   O OE2 . GLU A 92   ? 0.5390 0.6678 0.5349 0.0545  -0.0296 -0.1244 90   GLU A OE2 
526   N N   . TYR A 93   ? 0.4408 0.5347 0.4421 0.0500  -0.0268 -0.1051 91   TYR A N   
527   C CA  . TYR A 93   ? 0.3791 0.4823 0.3782 0.0501  -0.0239 -0.1036 91   TYR A CA  
528   C C   . TYR A 93   ? 0.3928 0.4888 0.3946 0.0506  -0.0244 -0.1017 91   TYR A C   
529   O O   . TYR A 93   ? 0.3594 0.4613 0.3595 0.0501  -0.0220 -0.0993 91   TYR A O   
530   C CB  . TYR A 93   ? 0.3665 0.4748 0.3596 0.0461  -0.0200 -0.0964 91   TYR A CB  
531   C CG  . TYR A 93   ? 0.3793 0.4986 0.3693 0.0463  -0.0191 -0.0989 91   TYR A CG  
532   C CD1 . TYR A 93   ? 0.3514 0.4860 0.3399 0.0481  -0.0176 -0.1024 91   TYR A CD1 
533   C CD2 . TYR A 93   ? 0.3911 0.5062 0.3800 0.0447  -0.0200 -0.0978 91   TYR A CD2 
534   C CE1 . TYR A 93   ? 0.4108 0.5562 0.3962 0.0483  -0.0169 -0.1047 91   TYR A CE1 
535   C CE2 . TYR A 93   ? 0.4416 0.5671 0.4277 0.0450  -0.0195 -0.1001 91   TYR A CE2 
536   C CZ  . TYR A 93   ? 0.4166 0.5572 0.4008 0.0468  -0.0179 -0.1035 91   TYR A CZ  
537   O OH  . TYR A 93   ? 0.4554 0.6069 0.4364 0.0472  -0.0173 -0.1056 91   TYR A OH  
538   N N   . SER A 94   ? 0.3745 0.4581 0.3807 0.0517  -0.0277 -0.1029 92   SER A N   
539   C CA  . SER A 94   ? 0.3791 0.4553 0.3882 0.0525  -0.0287 -0.1014 92   SER A CA  
540   C C   . SER A 94   ? 0.3298 0.4041 0.3351 0.0488  -0.0254 -0.0931 92   SER A C   
541   O O   . SER A 94   ? 0.3849 0.4613 0.3906 0.0494  -0.0245 -0.0922 92   SER A O   
542   C CB  . SER A 94   ? 0.4206 0.5047 0.4331 0.0569  -0.0299 -0.1083 92   SER A CB  
543   O OG  . SER A 94   ? 0.4533 0.5397 0.4696 0.0606  -0.0331 -0.1166 92   SER A OG  
544   N N   . LEU A 95   ? 0.3466 0.4168 0.3483 0.0450  -0.0237 -0.0872 93   LEU A N   
545   C CA  . LEU A 95   ? 0.3289 0.3971 0.3269 0.0413  -0.0207 -0.0793 93   LEU A CA  
546   C C   . LEU A 95   ? 0.3125 0.3681 0.3125 0.0406  -0.0220 -0.0757 93   LEU A C   
547   O O   . LEU A 95   ? 0.3383 0.3844 0.3412 0.0412  -0.0248 -0.0765 93   LEU A O   
548   C CB  . LEU A 95   ? 0.3490 0.4173 0.3427 0.0378  -0.0187 -0.0746 93   LEU A CB  
549   C CG  . LEU A 95   ? 0.3453 0.4259 0.3362 0.0378  -0.0171 -0.0767 93   LEU A CG  
550   C CD1 . LEU A 95   ? 0.3486 0.4271 0.3356 0.0341  -0.0153 -0.0709 93   LEU A CD1 
551   C CD2 . LEU A 95   ? 0.2740 0.3667 0.2632 0.0383  -0.0146 -0.0771 93   LEU A CD2 
552   N N   . SER A 96   ? 0.3053 0.3611 0.3038 0.0393  -0.0201 -0.0715 94   SER A N   
553   C CA  . SER A 96   ? 0.3482 0.3929 0.3472 0.0378  -0.0207 -0.0666 94   SER A CA  
554   C C   . SER A 96   ? 0.3086 0.3478 0.3042 0.0339  -0.0190 -0.0604 94   SER A C   
555   O O   . SER A 96   ? 0.3062 0.3507 0.2989 0.0323  -0.0173 -0.0595 94   SER A O   
556   C CB  . SER A 96   ? 0.2800 0.3275 0.2786 0.0378  -0.0193 -0.0646 94   SER A CB  
557   O OG  . SER A 96   ? 0.2692 0.3238 0.2637 0.0350  -0.0158 -0.0609 94   SER A OG  
558   N N   . SER A 97   ? 0.2707 0.2995 0.2666 0.0325  -0.0196 -0.0561 95   SER A N   
559   C CA  . SER A 97   ? 0.3609 0.3843 0.3537 0.0289  -0.0181 -0.0502 95   SER A CA  
560   C C   . SER A 97   ? 0.3133 0.3432 0.3020 0.0264  -0.0146 -0.0462 95   SER A C   
561   O O   . SER A 97   ? 0.2905 0.3222 0.2765 0.0242  -0.0131 -0.0439 95   SER A O   
562   C CB  . SER A 97   ? 0.4084 0.4207 0.4023 0.0280  -0.0192 -0.0462 95   SER A CB  
563   O OG  . SER A 97   ? 0.4722 0.4777 0.4698 0.0296  -0.0223 -0.0489 95   SER A OG  
564   N N   . GLN A 98   ? 0.2738 0.3072 0.2621 0.0266  -0.0135 -0.0453 96   GLN A N   
565   C CA  . GLN A 98   ? 0.2983 0.3377 0.2833 0.0240  -0.0104 -0.0415 96   GLN A CA  
566   C C   . GLN A 98   ? 0.2762 0.3264 0.2596 0.0241  -0.0090 -0.0437 96   GLN A C   
567   O O   . GLN A 98   ? 0.2622 0.3155 0.2425 0.0214  -0.0068 -0.0399 96   GLN A O   
568   C CB  . GLN A 98   ? 0.2903 0.3317 0.2757 0.0242  -0.0097 -0.0405 96   GLN A CB  
569   C CG  . GLN A 98   ? 0.2991 0.3305 0.2847 0.0233  -0.0103 -0.0368 96   GLN A CG  
570   C CD  . GLN A 98   ? 0.3113 0.3384 0.2938 0.0198  -0.0085 -0.0310 96   GLN A CD  
571   O OE1 . GLN A 98   ? 0.3116 0.3333 0.2935 0.0189  -0.0090 -0.0297 96   GLN A OE1 
572   N NE2 . GLN A 98   ? 0.3075 0.3372 0.2883 0.0179  -0.0065 -0.0276 96   GLN A NE2 
573   N N   . GLU A 99   ? 0.2921 0.3484 0.2777 0.0272  -0.0104 -0.0499 97   GLU A N   
574   C CA  . GLU A 99   ? 0.2783 0.3456 0.2622 0.0274  -0.0091 -0.0522 97   GLU A CA  
575   C C   . GLU A 99   ? 0.2843 0.3494 0.2665 0.0260  -0.0093 -0.0512 97   GLU A C   
576   O O   . GLU A 99   ? 0.2908 0.3625 0.2699 0.0242  -0.0073 -0.0490 97   GLU A O   
577   C CB  . GLU A 99   ? 0.2655 0.3400 0.2524 0.0313  -0.0108 -0.0596 97   GLU A CB  
578   C CG  . GLU A 99   ? 0.2651 0.3448 0.2535 0.0327  -0.0102 -0.0608 97   GLU A CG  
579   C CD  . GLU A 99   ? 0.2683 0.3537 0.2603 0.0370  -0.0122 -0.0685 97   GLU A CD  
580   O OE1 . GLU A 99   ? 0.2867 0.3700 0.2806 0.0392  -0.0146 -0.0731 97   GLU A OE1 
581   O OE2 . GLU A 99   ? 0.3036 0.3955 0.2969 0.0383  -0.0116 -0.0700 97   GLU A OE2 
582   N N   . GLY A 100  ? 0.2788 0.3350 0.2631 0.0269  -0.0118 -0.0527 98   GLY A N   
583   C CA  . GLY A 100  ? 0.2932 0.3468 0.2762 0.0254  -0.0120 -0.0515 98   GLY A CA  
584   C C   . GLY A 100  ? 0.3045 0.3553 0.2840 0.0217  -0.0096 -0.0444 98   GLY A C   
585   O O   . GLY A 100  ? 0.2769 0.3317 0.2539 0.0202  -0.0085 -0.0428 98   GLY A O   
586   N N   . VAL A 101  ? 0.2719 0.3160 0.2513 0.0203  -0.0090 -0.0402 99   VAL A N   
587   C CA  . VAL A 101  ? 0.2975 0.3388 0.2739 0.0169  -0.0069 -0.0338 99   VAL A CA  
588   C C   . VAL A 101  ? 0.3292 0.3803 0.3029 0.0156  -0.0044 -0.0319 99   VAL A C   
589   O O   . VAL A 101  ? 0.2838 0.3365 0.2549 0.0134  -0.0030 -0.0285 99   VAL A O   
590   C CB  . VAL A 101  ? 0.2557 0.2889 0.2327 0.0161  -0.0069 -0.0304 99   VAL A CB  
591   C CG1 . VAL A 101  ? 0.2580 0.2894 0.2321 0.0128  -0.0046 -0.0243 99   VAL A CG1 
592   C CG2 . VAL A 101  ? 0.3067 0.3300 0.2862 0.0169  -0.0092 -0.0311 99   VAL A CG2 
593   N N   . ALA A 102  ? 0.2696 0.3274 0.2440 0.0168  -0.0038 -0.0338 100  ALA A N   
594   C CA  . ALA A 102  ? 0.2838 0.3512 0.2560 0.0153  -0.0013 -0.0317 100  ALA A CA  
595   C C   . ALA A 102  ? 0.2740 0.3498 0.2445 0.0155  -0.0009 -0.0334 100  ALA A C   
596   O O   . ALA A 102  ? 0.3214 0.4018 0.2892 0.0132  0.0010  -0.0294 100  ALA A O   
597   C CB  . ALA A 102  ? 0.2545 0.3283 0.2283 0.0167  -0.0009 -0.0340 100  ALA A CB  
598   N N   . LEU A 103  ? 0.2921 0.3702 0.2643 0.0183  -0.0028 -0.0393 101  LEU A N   
599   C CA  . LEU A 103  ? 0.2952 0.3813 0.2656 0.0189  -0.0027 -0.0415 101  LEU A CA  
600   C C   . LEU A 103  ? 0.3053 0.3869 0.2735 0.0165  -0.0024 -0.0374 101  LEU A C   
601   O O   . LEU A 103  ? 0.2953 0.3839 0.2607 0.0151  -0.0010 -0.0352 101  LEU A O   
602   C CB  . LEU A 103  ? 0.2909 0.3782 0.2641 0.0225  -0.0053 -0.0490 101  LEU A CB  
603   C CG  . LEU A 103  ? 0.3242 0.4197 0.2960 0.0234  -0.0057 -0.0523 101  LEU A CG  
604   C CD1 . LEU A 103  ? 0.2739 0.3831 0.2430 0.0231  -0.0033 -0.0519 101  LEU A CD1 
605   C CD2 . LEU A 103  ? 0.3257 0.4208 0.3009 0.0271  -0.0087 -0.0600 101  LEU A CD2 
606   N N   . MET A 104  ? 0.2842 0.3545 0.2537 0.0160  -0.0038 -0.0362 102  MET A N   
607   C CA  . MET A 104  ? 0.3273 0.3932 0.2950 0.0139  -0.0036 -0.0324 102  MET A CA  
608   C C   . MET A 104  ? 0.3041 0.3704 0.2691 0.0108  -0.0011 -0.0258 102  MET A C   
609   O O   . MET A 104  ? 0.3198 0.3882 0.2826 0.0091  -0.0003 -0.0228 102  MET A O   
610   C CB  . MET A 104  ? 0.2957 0.3498 0.2657 0.0139  -0.0054 -0.0325 102  MET A CB  
611   C CG  . MET A 104  ? 0.3293 0.3820 0.3025 0.0167  -0.0082 -0.0388 102  MET A CG  
612   S SD  . MET A 104  ? 0.3994 0.4622 0.3717 0.0182  -0.0090 -0.0436 102  MET A SD  
613   C CE  . MET A 104  ? 0.4748 0.5317 0.4459 0.0158  -0.0092 -0.0399 102  MET A CE  
614   N N   . CYS A 105  ? 0.2535 0.3179 0.2189 0.0099  -0.0001 -0.0233 103  CYS A N   
615   C CA  . CYS A 105  ? 0.2967 0.3619 0.2600 0.0070  0.0021  -0.0173 103  CYS A CA  
616   C C   . CYS A 105  ? 0.3644 0.4414 0.3257 0.0064  0.0036  -0.0166 103  CYS A C   
617   O O   . CYS A 105  ? 0.3651 0.4436 0.3243 0.0041  0.0049  -0.0118 103  CYS A O   
618   C CB  . CYS A 105  ? 0.3071 0.3688 0.2717 0.0064  0.0027  -0.0155 103  CYS A CB  
619   S SG  . CYS A 105  ? 0.3034 0.3518 0.2697 0.0066  0.0013  -0.0148 103  CYS A SG  
620   N N   . LEU A 106  ? 0.3276 0.4133 0.2896 0.0085  0.0035  -0.0212 104  LEU A N   
621   C CA  . LEU A 106  ? 0.3032 0.4013 0.2631 0.0081  0.0050  -0.0207 104  LEU A CA  
622   C C   . LEU A 106  ? 0.3701 0.4715 0.3279 0.0081  0.0046  -0.0210 104  LEU A C   
623   O O   . LEU A 106  ? 0.3739 0.4812 0.3291 0.0062  0.0061  -0.0170 104  LEU A O   
624   C CB  . LEU A 106  ? 0.3082 0.4151 0.2695 0.0107  0.0049  -0.0262 104  LEU A CB  
625   C CG  . LEU A 106  ? 0.3354 0.4566 0.2945 0.0108  0.0063  -0.0268 104  LEU A CG  
626   C CD1 . LEU A 106  ? 0.2961 0.4219 0.2536 0.0074  0.0088  -0.0202 104  LEU A CD1 
627   C CD2 . LEU A 106  ? 0.3253 0.4554 0.2861 0.0140  0.0058  -0.0335 104  LEU A CD2 
628   N N   . ALA A 107  ? 0.3140 0.4116 0.2730 0.0102  0.0025  -0.0256 105  ALA A N   
629   C CA  . ALA A 107  ? 0.3574 0.4575 0.3147 0.0104  0.0017  -0.0262 105  ALA A CA  
630   C C   . ALA A 107  ? 0.4273 0.5218 0.3827 0.0074  0.0025  -0.0198 105  ALA A C   
631   O O   . ALA A 107  ? 0.4239 0.5244 0.3768 0.0064  0.0032  -0.0173 105  ALA A O   
632   C CB  . ALA A 107  ? 0.3424 0.4374 0.3020 0.0129  -0.0009 -0.0321 105  ALA A CB  
633   N N   . GLU A 108  ? 0.3910 0.4744 0.3479 0.0062  0.0023  -0.0170 106  GLU A N   
634   C CA  . GLU A 108  ? 0.4580 0.5358 0.4135 0.0037  0.0030  -0.0111 106  GLU A CA  
635   C C   . GLU A 108  ? 0.4717 0.5563 0.4249 0.0015  0.0051  -0.0060 106  GLU A C   
636   O O   . GLU A 108  ? 0.4370 0.5237 0.3882 0.0001  0.0054  -0.0026 106  GLU A O   
637   C CB  . GLU A 108  ? 0.4216 0.4879 0.3789 0.0029  0.0028  -0.0091 106  GLU A CB  
638   C CG  . GLU A 108  ? 0.4738 0.5346 0.4300 0.0003  0.0037  -0.0030 106  GLU A CG  
639   C CD  . GLU A 108  ? 0.5421 0.5943 0.4998 -0.0006 0.0040  -0.0009 106  GLU A CD  
640   O OE1 . GLU A 108  ? 0.4882 0.5364 0.4478 0.0009  0.0030  -0.0041 106  GLU A OE1 
641   O OE2 . GLU A 108  ? 0.5512 0.6009 0.5082 -0.0027 0.0050  0.0040  106  GLU A OE2 
642   N N   . ALA A 109  ? 0.4121 0.5005 0.3658 0.0010  0.0063  -0.0053 107  ALA A N   
643   C CA  . ALA A 109  ? 0.5023 0.5967 0.4544 -0.0014 0.0082  0.0000  107  ALA A CA  
644   C C   . ALA A 109  ? 0.5090 0.6154 0.4586 -0.0011 0.0088  -0.0004 107  ALA A C   
645   O O   . ALA A 109  ? 0.5086 0.6184 0.4563 -0.0032 0.0098  0.0048  107  ALA A O   
646   C CB  . ALA A 109  ? 0.5367 0.6328 0.4903 -0.0019 0.0093  0.0004  107  ALA A CB  
647   N N   . LEU A 110  ? 0.4254 0.5387 0.3751 0.0016  0.0081  -0.0064 108  LEU A N   
648   C CA  . LEU A 110  ? 0.4810 0.6064 0.4282 0.0022  0.0085  -0.0074 108  LEU A CA  
649   C C   . LEU A 110  ? 0.5288 0.6522 0.4741 0.0017  0.0075  -0.0058 108  LEU A C   
650   O O   . LEU A 110  ? 0.5412 0.6727 0.4838 0.0007  0.0083  -0.0027 108  LEU A O   
651   C CB  . LEU A 110  ? 0.4193 0.5516 0.3673 0.0055  0.0075  -0.0151 108  LEU A CB  
652   C CG  . LEU A 110  ? 0.4009 0.5392 0.3503 0.0062  0.0087  -0.0169 108  LEU A CG  
653   C CD1 . LEU A 110  ? 0.3532 0.4941 0.3047 0.0100  0.0071  -0.0253 108  LEU A CD1 
654   C CD2 . LEU A 110  ? 0.4051 0.5566 0.3521 0.0047  0.0109  -0.0135 108  LEU A CD2 
655   N N   . LEU A 111  ? 0.4940 0.6072 0.4408 0.0025  0.0058  -0.0076 109  LEU A N   
656   C CA  . LEU A 111  ? 0.5542 0.6650 0.4997 0.0021  0.0048  -0.0062 109  LEU A CA  
657   C C   . LEU A 111  ? 0.5891 0.6963 0.5334 -0.0009 0.0059  0.0014  109  LEU A C   
658   O O   . LEU A 111  ? 0.6420 0.7501 0.5847 -0.0014 0.0054  0.0035  109  LEU A O   
659   C CB  . LEU A 111  ? 0.5036 0.6045 0.4516 0.0035  0.0028  -0.0100 109  LEU A CB  
660   C CG  . LEU A 111  ? 0.4578 0.5623 0.4072 0.0065  0.0011  -0.0178 109  LEU A CG  
661   C CD1 . LEU A 111  ? 0.4675 0.5611 0.4200 0.0075  -0.0009 -0.0209 109  LEU A CD1 
662   C CD2 . LEU A 111  ? 0.4886 0.6029 0.4356 0.0075  0.0005  -0.0198 109  LEU A CD2 
663   N N   . ARG A 112  ? 0.5896 0.6931 0.5348 -0.0027 0.0072  0.0054  110  ARG A N   
664   C CA  . ARG A 112  ? 0.6032 0.7042 0.5475 -0.0055 0.0081  0.0125  110  ARG A CA  
665   C C   . ARG A 112  ? 0.6945 0.8067 0.6362 -0.0067 0.0093  0.0162  110  ARG A C   
666   O O   . ARG A 112  ? 0.7213 0.8326 0.6620 -0.0087 0.0095  0.0219  110  ARG A O   
667   C CB  . ARG A 112  ? 0.5947 0.6884 0.5410 -0.0071 0.0089  0.0154  110  ARG A CB  
668   C CG  . ARG A 112  ? 0.6602 0.7416 0.6086 -0.0066 0.0078  0.0141  110  ARG A CG  
669   C CD  . ARG A 112  ? 0.6938 0.7683 0.6437 -0.0085 0.0086  0.0182  110  ARG A CD  
670   N NE  . ARG A 112  ? 0.7310 0.8087 0.6819 -0.0086 0.0096  0.0172  110  ARG A NE  
671   C CZ  . ARG A 112  ? 0.7888 0.8618 0.7416 -0.0074 0.0091  0.0138  110  ARG A CZ  
672   N NH1 . ARG A 112  ? 0.7555 0.8201 0.7093 -0.0061 0.0079  0.0114  110  ARG A NH1 
673   N NH2 . ARG A 112  ? 0.8031 0.8800 0.7569 -0.0075 0.0100  0.0131  110  ARG A NH2 
674   N N   . ILE A 113  ? 0.6988 0.8219 0.6396 -0.0056 0.0099  0.0131  111  ILE A N   
675   C CA  . ILE A 113  ? 0.6784 0.8137 0.6163 -0.0065 0.0110  0.0162  111  ILE A CA  
676   C C   . ILE A 113  ? 0.7672 0.9049 0.7028 -0.0057 0.0098  0.0159  111  ILE A C   
677   O O   . ILE A 113  ? 0.7568 0.8950 0.6926 -0.0032 0.0083  0.0098  111  ILE A O   
678   C CB  . ILE A 113  ? 0.6616 0.8087 0.5991 -0.0051 0.0120  0.0120  111  ILE A CB  
679   C CG1 . ILE A 113  ? 0.5448 0.6905 0.4846 -0.0063 0.0133  0.0134  111  ILE A CG1 
680   C CG2 . ILE A 113  ? 0.6497 0.8107 0.5839 -0.0056 0.0129  0.0143  111  ILE A CG2 
681   C CD1 . ILE A 113  ? 0.5480 0.7040 0.4881 -0.0045 0.0141  0.0086  111  ILE A CD1 
682   N N   . PRO A 114  ? 0.8204 0.9598 0.7543 -0.0078 0.0101  0.0222  112  PRO A N   
683   C CA  . PRO A 114  ? 0.7944 0.9348 0.7264 -0.0070 0.0087  0.0222  112  PRO A CA  
684   C C   . PRO A 114  ? 0.8104 0.9631 0.7399 -0.0048 0.0083  0.0174  112  PRO A C   
685   O O   . PRO A 114  ? 0.8075 0.9587 0.7371 -0.0026 0.0066  0.0121  112  PRO A O   
686   C CB  . PRO A 114  ? 0.8516 0.9921 0.7824 -0.0098 0.0093  0.0306  112  PRO A CB  
687   C CG  . PRO A 114  ? 0.8542 1.0000 0.7851 -0.0118 0.0113  0.0343  112  PRO A CG  
688   C CD  . PRO A 114  ? 0.7529 0.8936 0.6867 -0.0109 0.0116  0.0297  112  PRO A CD  
689   N N   . ASP A 115  ? 0.8228 0.9879 0.7501 -0.0053 0.0097  0.0190  113  ASP A N   
690   C CA  . ASP A 115  ? 0.7829 0.9614 0.7072 -0.0034 0.0095  0.0154  113  ASP A CA  
691   C C   . ASP A 115  ? 0.7495 0.9322 0.6748 -0.0004 0.0092  0.0068  113  ASP A C   
692   O O   . ASP A 115  ? 0.7311 0.9153 0.6580 -0.0005 0.0105  0.0058  113  ASP A O   
693   C CB  . ASP A 115  ? 0.7578 0.9485 0.6791 -0.0054 0.0113  0.0214  113  ASP A CB  
694   C CG  . ASP A 115  ? 0.8319 1.0382 0.7500 -0.0033 0.0114  0.0173  113  ASP A CG  
695   O OD1 . ASP A 115  ? 0.8771 1.0861 0.7933 -0.0016 0.0098  0.0146  113  ASP A OD1 
696   O OD2 . ASP A 115  ? 0.8343 1.0507 0.7518 -0.0032 0.0131  0.0165  113  ASP A OD2 
697   N N   . THR A 116  ? 0.7359 0.9211 0.6607 0.0023  0.0073  0.0004  114  THR A N   
698   C CA  . THR A 116  ? 0.7110 0.8989 0.6375 0.0055  0.0065  -0.0084 114  THR A CA  
699   C C   . THR A 116  ? 0.7261 0.9282 0.6511 0.0062  0.0082  -0.0100 114  THR A C   
700   O O   . THR A 116  ? 0.7243 0.9262 0.6517 0.0074  0.0087  -0.0139 114  THR A O   
701   C CB  . THR A 116  ? 0.7224 0.9116 0.6485 0.0081  0.0040  -0.0147 114  THR A CB  
702   O OG1 . THR A 116  ? 0.7298 0.9053 0.6582 0.0076  0.0024  -0.0140 114  THR A OG1 
703   C CG2 . THR A 116  ? 0.7462 0.9396 0.6742 0.0115  0.0030  -0.0240 114  THR A CG2 
704   N N   . ALA A 117  ? 0.7241 0.9391 0.6452 0.0056  0.0092  -0.0069 115  ALA A N   
705   C CA  . ALA A 117  ? 0.7207 0.9507 0.6402 0.0063  0.0110  -0.0084 115  ALA A CA  
706   C C   . ALA A 117  ? 0.6875 0.9159 0.6088 0.0038  0.0133  -0.0037 115  ALA A C   
707   O O   . ALA A 117  ? 0.6630 0.8993 0.5851 0.0050  0.0144  -0.0072 115  ALA A O   
708   C CB  . ALA A 117  ? 0.7316 0.9758 0.6464 0.0057  0.0118  -0.0049 115  ALA A CB  
709   N N   . THR A 118  ? 0.7015 0.9201 0.6236 0.0005  0.0139  0.0040  116  THR A N   
710   C CA  . THR A 118  ? 0.6968 0.9124 0.6211 -0.0019 0.0157  0.0082  116  THR A CA  
711   C C   . THR A 118  ? 0.6577 0.8651 0.5860 0.0000  0.0150  0.0021  116  THR A C   
712   O O   . THR A 118  ? 0.6322 0.8447 0.5619 0.0002  0.0163  0.0006  116  THR A O   
713   C CB  . THR A 118  ? 0.6702 0.8757 0.5950 -0.0055 0.0159  0.0169  116  THR A CB  
714   O OG1 . THR A 118  ? 0.7771 0.9907 0.6985 -0.0072 0.0164  0.0229  116  THR A OG1 
715   C CG2 . THR A 118  ? 0.6022 0.8045 0.5297 -0.0080 0.0176  0.0210  116  THR A CG2 
716   N N   . ARG A 119  ? 0.6399 0.8348 0.5699 0.0013  0.0130  -0.0011 117  ARG A N   
717   C CA  . ARG A 119  ? 0.6441 0.8307 0.5779 0.0032  0.0120  -0.0068 117  ARG A CA  
718   C C   . ARG A 119  ? 0.6363 0.8331 0.5705 0.0065  0.0118  -0.0147 117  ARG A C   
719   O O   . ARG A 119  ? 0.5741 0.7708 0.5108 0.0073  0.0124  -0.0172 117  ARG A O   
720   C CB  . ARG A 119  ? 0.6422 0.8157 0.5774 0.0042  0.0097  -0.0091 117  ARG A CB  
721   C CG  . ARG A 119  ? 0.5698 0.7335 0.5088 0.0059  0.0085  -0.0142 117  ARG A CG  
722   C CD  . ARG A 119  ? 0.5581 0.7109 0.4985 0.0070  0.0061  -0.0169 117  ARG A CD  
723   N NE  . ARG A 119  ? 0.5966 0.7444 0.5354 0.0046  0.0061  -0.0108 117  ARG A NE  
724   C CZ  . ARG A 119  ? 0.6393 0.7885 0.5766 0.0052  0.0048  -0.0117 117  ARG A CZ  
725   N NH1 . ARG A 119  ? 0.6079 0.7623 0.5451 0.0081  0.0032  -0.0185 117  ARG A NH1 
726   N NH2 . ARG A 119  ? 0.7339 0.8790 0.6698 0.0031  0.0049  -0.0057 117  ARG A NH2 
727   N N   . ASP A 120  ? 0.6316 0.8375 0.5635 0.0087  0.0109  -0.0190 118  ASP A N   
728   C CA  . ASP A 120  ? 0.5930 0.8093 0.5254 0.0123  0.0105  -0.0272 118  ASP A CA  
729   C C   . ASP A 120  ? 0.6094 0.8389 0.5410 0.0115  0.0131  -0.0255 118  ASP A C   
730   O O   . ASP A 120  ? 0.6011 0.8358 0.5346 0.0140  0.0132  -0.0314 118  ASP A O   
731   C CB  . ASP A 120  ? 0.6426 0.8668 0.5725 0.0146  0.0090  -0.0317 118  ASP A CB  
732   C CG  . ASP A 120  ? 0.7448 0.9567 0.6761 0.0154  0.0063  -0.0341 118  ASP A CG  
733   O OD1 . ASP A 120  ? 0.6837 0.8813 0.6176 0.0141  0.0058  -0.0318 118  ASP A OD1 
734   O OD2 . ASP A 120  ? 0.7951 1.0121 0.7250 0.0174  0.0047  -0.0384 118  ASP A OD2 
735   N N   . ALA A 121  ? 0.6132 0.8483 0.5420 0.0082  0.0152  -0.0173 119  ALA A N   
736   C CA  . ALA A 121  ? 0.6372 0.8845 0.5656 0.0069  0.0178  -0.0147 119  ALA A CA  
737   C C   . ALA A 121  ? 0.5720 0.8116 0.5042 0.0056  0.0186  -0.0133 119  ALA A C   
738   O O   . ALA A 121  ? 0.5842 0.8321 0.5178 0.0066  0.0199  -0.0160 119  ALA A O   
739   C CB  . ALA A 121  ? 0.6001 0.8544 0.5249 0.0033  0.0196  -0.0056 119  ALA A CB  
740   N N   . LEU A 122  ? 0.6116 0.8357 0.5456 0.0036  0.0179  -0.0093 120  LEU A N   
741   C CA  . LEU A 122  ? 0.5581 0.7743 0.4957 0.0025  0.0185  -0.0081 120  LEU A CA  
742   C C   . LEU A 122  ? 0.5536 0.7670 0.4942 0.0062  0.0171  -0.0168 120  LEU A C   
743   O O   . LEU A 122  ? 0.5434 0.7586 0.4865 0.0064  0.0180  -0.0180 120  LEU A O   
744   C CB  . LEU A 122  ? 0.6080 0.8084 0.5466 -0.0001 0.0178  -0.0025 120  LEU A CB  
745   C CG  . LEU A 122  ? 0.5690 0.7620 0.5108 -0.0021 0.0187  0.0006  120  LEU A CG  
746   C CD1 . LEU A 122  ? 0.6170 0.8205 0.5584 -0.0050 0.0211  0.0061  120  LEU A CD1 
747   C CD2 . LEU A 122  ? 0.5992 0.7766 0.5419 -0.0041 0.0177  0.0050  120  LEU A CD2 
748   N N   . ILE A 123  ? 0.5470 0.7560 0.4877 0.0092  0.0147  -0.0227 121  ILE A N   
749   C CA  . ILE A 123  ? 0.5547 0.7609 0.4987 0.0129  0.0130  -0.0311 121  ILE A CA  
750   C C   . ILE A 123  ? 0.5782 0.8000 0.5221 0.0154  0.0140  -0.0364 121  ILE A C   
751   O O   . ILE A 123  ? 0.5035 0.7261 0.4504 0.0167  0.0142  -0.0395 121  ILE A O   
752   C CB  . ILE A 123  ? 0.5185 0.7172 0.4628 0.0153  0.0102  -0.0360 121  ILE A CB  
753   C CG1 . ILE A 123  ? 0.5193 0.7015 0.4644 0.0131  0.0093  -0.0315 121  ILE A CG1 
754   C CG2 . ILE A 123  ? 0.4967 0.6950 0.4442 0.0194  0.0082  -0.0453 121  ILE A CG2 
755   C CD1 . ILE A 123  ? 0.4825 0.6576 0.4279 0.0147  0.0067  -0.0352 121  ILE A CD1 
756   N N   . ARG A 124  ? 0.5660 0.8011 0.5066 0.0160  0.0146  -0.0373 122  ARG A N   
757   C CA  . ARG A 124  ? 0.5908 0.8420 0.5311 0.0188  0.0154  -0.0430 122  ARG A CA  
758   C C   . ARG A 124  ? 0.5848 0.8448 0.5256 0.0166  0.0183  -0.0386 122  ARG A C   
759   O O   . ARG A 124  ? 0.5987 0.8652 0.5418 0.0188  0.0187  -0.0437 122  ARG A O   
760   C CB  . ARG A 124  ? 0.5557 0.8193 0.4919 0.0198  0.0154  -0.0444 122  ARG A CB  
761   N N   . ASP A 125  ? 0.6792 0.9393 0.6181 0.0122  0.0203  -0.0294 123  ASP A N   
762   C CA  . ASP A 125  ? 0.6747 0.9454 0.6136 0.0096  0.0231  -0.0246 123  ASP A CA  
763   C C   . ASP A 125  ? 0.6595 0.9200 0.6019 0.0071  0.0238  -0.0204 123  ASP A C   
764   O O   . ASP A 125  ? 0.7812 1.0500 0.7246 0.0050  0.0260  -0.0170 123  ASP A O   
765   C CB  . ASP A 125  ? 0.7035 0.9827 0.6382 0.0062  0.0249  -0.0167 123  ASP A CB  
766   N N   . LYS A 126  ? 0.5816 0.8251 0.5261 0.0070  0.0219  -0.0205 124  LYS A N   
767   C CA  . LYS A 126  ? 0.6129 0.8470 0.5603 0.0045  0.0225  -0.0162 124  LYS A CA  
768   C C   . LYS A 126  ? 0.6561 0.8760 0.6068 0.0068  0.0202  -0.0210 124  LYS A C   
769   O O   . LYS A 126  ? 0.6652 0.8843 0.6191 0.0074  0.0204  -0.0229 124  LYS A O   
770   C CB  . LYS A 126  ? 0.6264 0.8535 0.5723 0.0000  0.0232  -0.0068 124  LYS A CB  
771   N N   . ILE A 127  ? 0.6371 0.8462 0.5872 0.0080  0.0180  -0.0227 125  ILE A N   
772   C CA  . ILE A 127  ? 0.5901 0.7852 0.5433 0.0097  0.0159  -0.0263 125  ILE A CA  
773   C C   . ILE A 127  ? 0.5942 0.7938 0.5499 0.0140  0.0147  -0.0350 125  ILE A C   
774   O O   . ILE A 127  ? 0.5960 0.7911 0.5549 0.0149  0.0143  -0.0369 125  ILE A O   
775   C CB  . ILE A 127  ? 0.5164 0.6999 0.4684 0.0099  0.0139  -0.0260 125  ILE A CB  
776   C CG1 . ILE A 127  ? 0.5357 0.7144 0.4856 0.0058  0.0150  -0.0175 125  ILE A CG1 
777   C CG2 . ILE A 127  ? 0.4938 0.6635 0.4491 0.0116  0.0118  -0.0294 125  ILE A CG2 
778   C CD1 . ILE A 127  ? 0.5377 0.7083 0.4895 0.0030  0.0158  -0.0122 125  ILE A CD1 
779   N N   . ALA A 128  ? 0.5669 0.7755 0.5213 0.0170  0.0140  -0.0407 126  ALA A N   
780   C CA  . ALA A 128  ? 0.5379 0.7509 0.4950 0.0214  0.0125  -0.0496 126  ALA A CA  
781   C C   . ALA A 128  ? 0.5795 0.8031 0.5385 0.0219  0.0142  -0.0508 126  ALA A C   
782   O O   . ALA A 128  ? 0.4937 0.7198 0.4556 0.0257  0.0129  -0.0580 126  ALA A O   
783   C CB  . ALA A 128  ? 0.5052 0.7274 0.4603 0.0243  0.0115  -0.0553 126  ALA A CB  
784   N N   . ASP A 129  ? 0.6177 0.8475 0.5753 0.0183  0.0170  -0.0439 127  ASP A N   
785   C CA  . ASP A 129  ? 0.6423 0.8819 0.6020 0.0181  0.0188  -0.0441 127  ASP A CA  
786   C C   . ASP A 129  ? 0.6451 0.8737 0.6080 0.0165  0.0187  -0.0412 127  ASP A C   
787   O O   . ASP A 129  ? 0.6712 0.9067 0.6359 0.0154  0.0203  -0.0399 127  ASP A O   
788   C CB  . ASP A 129  ? 0.6299 0.8834 0.5867 0.0148  0.0219  -0.0383 127  ASP A CB  
789   N N   . GLY A 130  ? 0.6846 0.8968 0.6482 0.0162  0.0167  -0.0403 128  GLY A N   
790   C CA  . GLY A 130  ? 0.6434 0.8446 0.6097 0.0147  0.0164  -0.0374 128  GLY A CA  
791   C C   . GLY A 130  ? 0.7352 0.9314 0.7002 0.0098  0.0180  -0.0285 128  GLY A C   
792   O O   . GLY A 130  ? 0.7129 0.8968 0.6794 0.0085  0.0172  -0.0259 128  GLY A O   
793   N N   . ASN A 131  ? 0.8947 1.1003 0.8571 0.0071  0.0201  -0.0237 129  ASN A N   
794   C CA  . ASN A 131  ? 0.9125 1.1138 0.8740 0.0023  0.0214  -0.0150 129  ASN A CA  
795   C C   . ASN A 131  ? 0.9064 1.0945 0.8660 0.0014  0.0200  -0.0123 129  ASN A C   
796   O O   . ASN A 131  ? 0.9668 1.1570 0.9236 -0.0007 0.0207  -0.0077 129  ASN A O   
797   C CB  . ASN A 131  ? 0.7859 1.0016 0.7452 -0.0002 0.0239  -0.0105 129  ASN A CB  
798   N N   . TRP A 132  ? 0.7431 0.9181 0.7044 0.0030  0.0180  -0.0149 130  TRP A N   
799   C CA  . TRP A 132  ? 0.7103 0.8728 0.6701 0.0022  0.0167  -0.0125 130  TRP A CA  
800   C C   . TRP A 132  ? 0.7311 0.8843 0.6916 -0.0014 0.0172  -0.0058 130  TRP A C   
801   O O   . TRP A 132  ? 0.7304 0.8767 0.6892 -0.0032 0.0169  -0.0018 130  TRP A O   
802   C CB  . TRP A 132  ? 0.6848 0.8379 0.6461 0.0056  0.0142  -0.0185 130  TRP A CB  
803   C CG  . TRP A 132  ? 0.5451 0.6914 0.5097 0.0069  0.0132  -0.0209 130  TRP A CG  
804   C CD1 . TRP A 132  ? 0.4888 0.6398 0.4559 0.0099  0.0126  -0.0268 130  TRP A CD1 
805   C CD2 . TRP A 132  ? 0.5023 0.6360 0.4681 0.0052  0.0127  -0.0175 130  TRP A CD2 
806   N NE1 . TRP A 132  ? 0.4499 0.5920 0.4197 0.0102  0.0116  -0.0270 130  TRP A NE1 
807   C CE2 . TRP A 132  ? 0.4040 0.5357 0.3729 0.0074  0.0117  -0.0214 130  TRP A CE2 
808   C CE3 . TRP A 132  ? 0.5090 0.6335 0.4738 0.0023  0.0128  -0.0118 130  TRP A CE3 
809   C CZ2 . TRP A 132  ? 0.3743 0.4953 0.3448 0.0066  0.0110  -0.0195 130  TRP A CZ2 
810   C CZ3 . TRP A 132  ? 0.4796 0.5936 0.4460 0.0016  0.0121  -0.0103 130  TRP A CZ3 
811   C CH2 . TRP A 132  ? 0.3921 0.5045 0.3612 0.0037  0.0112  -0.0140 130  TRP A CH2 
812   N N   . LYS A 133  ? 0.7553 0.9083 0.7183 -0.0025 0.0179  -0.0046 131  LYS A N   
813   C CA  . LYS A 133  ? 0.7956 0.9407 0.7596 -0.0060 0.0183  0.0014  131  LYS A CA  
814   C C   . LYS A 133  ? 0.8589 1.0092 0.8212 -0.0096 0.0199  0.0082  131  LYS A C   
815   O O   . LYS A 133  ? 0.8597 1.0017 0.8216 -0.0121 0.0197  0.0132  131  LYS A O   
816   C CB  . LYS A 133  ? 0.7429 0.8883 0.7101 -0.0062 0.0186  0.0007  131  LYS A CB  
817   N N   . SER A 134  ? 0.9231 1.0874 0.8844 -0.0099 0.0215  0.0084  132  SER A N   
818   C CA  . SER A 134  ? 0.8997 1.0704 0.8600 -0.0137 0.0232  0.0153  132  SER A CA  
819   C C   . SER A 134  ? 0.9286 1.0937 0.8860 -0.0148 0.0225  0.0191  132  SER A C   
820   O O   . SER A 134  ? 0.9179 1.0783 0.8755 -0.0181 0.0228  0.0255  132  SER A O   
821   C CB  . SER A 134  ? 0.8740 1.0617 0.8333 -0.0133 0.0249  0.0142  132  SER A CB  
822   N N   . HIS A 135  ? 0.9366 1.1021 0.8916 -0.0119 0.0215  0.0150  133  HIS A N   
823   C CA  . HIS A 135  ? 0.9153 1.0783 0.8675 -0.0128 0.0210  0.0182  133  HIS A CA  
824   C C   . HIS A 135  ? 0.8942 1.0417 0.8467 -0.0127 0.0193  0.0188  133  HIS A C   
825   O O   . HIS A 135  ? 0.8747 1.0180 0.8259 -0.0145 0.0191  0.0236  133  HIS A O   
826   C CB  . HIS A 135  ? 0.8329 1.0047 0.7823 -0.0099 0.0207  0.0136  133  HIS A CB  
827   N N   . LEU A 136  ? 0.8832 1.0224 0.8376 -0.0106 0.0181  0.0142  134  LEU A N   
828   C CA  . LEU A 136  ? 0.8429 0.9685 0.7975 -0.0101 0.0165  0.0142  134  LEU A CA  
829   C C   . LEU A 136  ? 0.8475 0.9634 0.8048 -0.0109 0.0161  0.0148  134  LEU A C   
830   O O   . LEU A 136  ? 0.8427 0.9532 0.8008 -0.0136 0.0164  0.0199  134  LEU A O   
831   C CB  . LEU A 136  ? 0.7559 0.8797 0.7098 -0.0066 0.0149  0.0077  134  LEU A CB  
832   C CG  . LEU A 136  ? 0.7256 0.8603 0.6771 -0.0050 0.0150  0.0052  134  LEU A CG  
833   C CD1 . LEU A 136  ? 0.5874 0.7216 0.5396 -0.0012 0.0134  -0.0025 134  LEU A CD1 
834   C CD2 . LEU A 136  ? 0.6990 0.8325 0.6480 -0.0065 0.0148  0.0094  134  LEU A CD2 
835   N N   . ARG A 140  ? 0.4096 0.4776 0.3720 -0.0187 0.0138  0.0307  138  ARG A N   
836   C CA  . ARG A 140  ? 0.4599 0.5205 0.4222 -0.0162 0.0127  0.0266  138  ARG A CA  
837   C C   . ARG A 140  ? 0.4942 0.5598 0.4563 -0.0136 0.0126  0.0212  138  ARG A C   
838   O O   . ARG A 140  ? 0.5203 0.5951 0.4815 -0.0131 0.0132  0.0200  138  ARG A O   
839   C CB  . ARG A 140  ? 0.4329 0.4881 0.3935 -0.0155 0.0119  0.0270  138  ARG A CB  
840   N N   . SER A 141  ? 0.4877 0.5476 0.4510 -0.0120 0.0117  0.0179  139  SER A N   
841   C CA  . SER A 141  ? 0.4404 0.5036 0.4041 -0.0092 0.0112  0.0126  139  SER A CA  
842   C C   . SER A 141  ? 0.4244 0.4896 0.3865 -0.0073 0.0105  0.0099  139  SER A C   
843   O O   . SER A 141  ? 0.4062 0.4664 0.3670 -0.0076 0.0100  0.0112  139  SER A O   
844   C CB  . SER A 141  ? 0.4116 0.4667 0.3767 -0.0078 0.0100  0.0103  139  SER A CB  
845   O OG  . SER A 141  ? 0.3979 0.4555 0.3638 -0.0050 0.0092  0.0053  139  SER A OG  
846   N N   . LEU A 142  ? 0.4021 0.4750 0.3644 -0.0054 0.0105  0.0058  140  LEU A N   
847   C CA  . LEU A 142  ? 0.3827 0.4569 0.3440 -0.0031 0.0095  0.0018  140  LEU A CA  
848   C C   . LEU A 142  ? 0.3686 0.4324 0.3306 -0.0016 0.0078  -0.0003 140  LEU A C   
849   O O   . LEU A 142  ? 0.3352 0.3972 0.2966 -0.0005 0.0068  -0.0021 140  LEU A O   
850   C CB  . LEU A 142  ? 0.3932 0.4764 0.3553 -0.0008 0.0094  -0.0032 140  LEU A CB  
851   C CG  . LEU A 142  ? 0.4896 0.5854 0.4503 -0.0009 0.0106  -0.0035 140  LEU A CG  
852   C CD1 . LEU A 142  ? 0.4603 0.5614 0.4218 0.0026  0.0095  -0.0103 140  LEU A CD1 
853   C CD2 . LEU A 142  ? 0.4924 0.5889 0.4505 -0.0024 0.0109  -0.0001 140  LEU A CD2 
854   N N   . PHE A 143  ? 0.3214 0.3786 0.2849 -0.0015 0.0074  -0.0001 141  PHE A N   
855   C CA  . PHE A 143  ? 0.3446 0.3935 0.3092 0.0003  0.0057  -0.0027 141  PHE A CA  
856   C C   . PHE A 143  ? 0.3304 0.3697 0.2945 -0.0012 0.0056  0.0008  141  PHE A C   
857   O O   . PHE A 143  ? 0.2717 0.3039 0.2368 -0.0002 0.0045  -0.0002 141  PHE A O   
858   C CB  . PHE A 143  ? 0.2972 0.3463 0.2639 0.0018  0.0052  -0.0054 141  PHE A CB  
859   C CG  . PHE A 143  ? 0.2739 0.3332 0.2414 0.0033  0.0055  -0.0089 141  PHE A CG  
860   C CD1 . PHE A 143  ? 0.2522 0.3154 0.2197 0.0055  0.0045  -0.0132 141  PHE A CD1 
861   C CD2 . PHE A 143  ? 0.2628 0.3284 0.2310 0.0024  0.0067  -0.0080 141  PHE A CD2 
862   C CE1 . PHE A 143  ? 0.2953 0.3686 0.2634 0.0071  0.0049  -0.0168 141  PHE A CE1 
863   C CE2 . PHE A 143  ? 0.2928 0.3686 0.2617 0.0038  0.0072  -0.0112 141  PHE A CE2 
864   C CZ  . PHE A 143  ? 0.3030 0.3829 0.2718 0.0063  0.0062  -0.0158 141  PHE A CZ  
865   N N   . VAL A 144  ? 0.3385 0.3780 0.3012 -0.0033 0.0065  0.0048  142  VAL A N   
866   C CA  . VAL A 144  ? 0.3659 0.3969 0.3283 -0.0046 0.0064  0.0080  142  VAL A CA  
867   C C   . VAL A 144  ? 0.3326 0.3573 0.2950 -0.0033 0.0051  0.0063  142  VAL A C   
868   O O   . VAL A 144  ? 0.3532 0.3704 0.3160 -0.0035 0.0047  0.0075  142  VAL A O   
869   C CB  . VAL A 144  ? 0.4045 0.4369 0.3657 -0.0069 0.0074  0.0125  142  VAL A CB  
870   C CG1 . VAL A 144  ? 0.4070 0.4443 0.3687 -0.0086 0.0086  0.0149  142  VAL A CG1 
871   C CG2 . VAL A 144  ? 0.3870 0.4244 0.3468 -0.0066 0.0074  0.0120  142  VAL A CG2 
872   N N   . ASN A 145  ? 0.3526 0.3805 0.3149 -0.0020 0.0044  0.0034  143  ASN A N   
873   C CA  . ASN A 145  ? 0.3703 0.3928 0.3331 -0.0009 0.0030  0.0017  143  ASN A CA  
874   C C   . ASN A 145  ? 0.3750 0.3966 0.3396 0.0014  0.0015  -0.0029 143  ASN A C   
875   O O   . ASN A 145  ? 0.3400 0.3591 0.3056 0.0025  0.0002  -0.0051 143  ASN A O   
876   C CB  . ASN A 145  ? 0.3955 0.4213 0.3572 -0.0012 0.0030  0.0018  143  ASN A CB  
877   C CG  . ASN A 145  ? 0.4247 0.4487 0.3851 -0.0033 0.0039  0.0065  143  ASN A CG  
878   O OD1 . ASN A 145  ? 0.4643 0.4814 0.4249 -0.0041 0.0040  0.0088  143  ASN A OD1 
879   N ND2 . ASN A 145  ? 0.4746 0.5050 0.4335 -0.0041 0.0046  0.0080  143  ASN A ND2 
880   N N   . ALA A 146  ? 0.3396 0.3634 0.3052 0.0023  0.0016  -0.0044 144  ALA A N   
881   C CA  . ALA A 146  ? 0.3519 0.3752 0.3195 0.0048  0.0000  -0.0089 144  ALA A CA  
882   C C   . ALA A 146  ? 0.3256 0.3397 0.2946 0.0053  -0.0015 -0.0090 144  ALA A C   
883   O O   . ALA A 146  ? 0.3604 0.3731 0.3313 0.0072  -0.0032 -0.0126 144  ALA A O   
884   C CB  . ALA A 146  ? 0.3107 0.3375 0.2792 0.0054  0.0004  -0.0098 144  ALA A CB  
885   N N   . ALA A 147  ? 0.3271 0.3352 0.2953 0.0038  -0.0009 -0.0052 145  ALA A N   
886   C CA  . ALA A 147  ? 0.3744 0.3744 0.3436 0.0041  -0.0021 -0.0048 145  ALA A CA  
887   C C   . ALA A 147  ? 0.3789 0.3773 0.3490 0.0044  -0.0032 -0.0062 145  ALA A C   
888   O O   . ALA A 147  ? 0.4284 0.4227 0.4006 0.0057  -0.0050 -0.0082 145  ALA A O   
889   C CB  . ALA A 147  ? 0.4243 0.4193 0.3922 0.0023  -0.0011 -0.0005 145  ALA A CB  
890   N N   . THR A 148  ? 0.3410 0.3428 0.3097 0.0033  -0.0024 -0.0052 146  THR A N   
891   C CA  . THR A 148  ? 0.3578 0.3589 0.3273 0.0035  -0.0035 -0.0067 146  THR A CA  
892   C C   . THR A 148  ? 0.3761 0.3810 0.3474 0.0057  -0.0051 -0.0119 146  THR A C   
893   O O   . THR A 148  ? 0.3912 0.3924 0.3648 0.0066  -0.0069 -0.0142 146  THR A O   
894   C CB  . THR A 148  ? 0.4324 0.4371 0.3999 0.0020  -0.0022 -0.0045 146  THR A CB  
895   O OG1 . THR A 148  ? 0.4967 0.4974 0.4629 0.0002  -0.0010 0.0000  146  THR A OG1 
896   C CG2 . THR A 148  ? 0.4596 0.4639 0.4280 0.0022  -0.0035 -0.0061 146  THR A CG2 
897   N N   . TRP A 149  ? 0.3464 0.3590 0.3170 0.0066  -0.0045 -0.0138 147  TRP A N   
898   C CA  . TRP A 149  ? 0.3388 0.3557 0.3112 0.0089  -0.0060 -0.0192 147  TRP A CA  
899   C C   . TRP A 149  ? 0.3251 0.3371 0.3003 0.0107  -0.0077 -0.0217 147  TRP A C   
900   O O   . TRP A 149  ? 0.3686 0.3799 0.3464 0.0126  -0.0099 -0.0259 147  TRP A O   
901   C CB  . TRP A 149  ? 0.3167 0.3436 0.2875 0.0094  -0.0047 -0.0205 147  TRP A CB  
902   C CG  . TRP A 149  ? 0.3372 0.3697 0.3056 0.0080  -0.0035 -0.0187 147  TRP A CG  
903   C CD1 . TRP A 149  ? 0.3855 0.4218 0.3513 0.0061  -0.0014 -0.0146 147  TRP A CD1 
904   C CD2 . TRP A 149  ? 0.3362 0.3706 0.3045 0.0084  -0.0045 -0.0208 147  TRP A CD2 
905   N NE1 . TRP A 149  ? 0.3691 0.4099 0.3332 0.0053  -0.0010 -0.0138 147  TRP A NE1 
906   C CE2 . TRP A 149  ? 0.3557 0.3956 0.3212 0.0067  -0.0029 -0.0177 147  TRP A CE2 
907   C CE3 . TRP A 149  ? 0.3521 0.3843 0.3228 0.0100  -0.0067 -0.0250 147  TRP A CE3 
908   C CZ2 . TRP A 149  ? 0.3907 0.4341 0.3553 0.0067  -0.0034 -0.0186 147  TRP A CZ2 
909   C CZ3 . TRP A 149  ? 0.4144 0.4500 0.3843 0.0099  -0.0073 -0.0262 147  TRP A CZ3 
910   C CH2 . TRP A 149  ? 0.3904 0.4317 0.3572 0.0083  -0.0056 -0.0230 147  TRP A CH2 
911   N N   . GLY A 150  ? 0.3154 0.3240 0.2903 0.0103  -0.0071 -0.0191 148  GLY A N   
912   C CA  . GLY A 150  ? 0.3181 0.3212 0.2956 0.0118  -0.0089 -0.0206 148  GLY A CA  
913   C C   . GLY A 150  ? 0.4008 0.3963 0.3804 0.0118  -0.0107 -0.0206 148  GLY A C   
914   O O   . GLY A 150  ? 0.4034 0.3963 0.3861 0.0137  -0.0130 -0.0239 148  GLY A O   
915   N N   . LEU A 151  ? 0.4017 0.3935 0.3799 0.0096  -0.0098 -0.0168 149  LEU A N   
916   C CA  . LEU A 151  ? 0.4262 0.4113 0.4065 0.0092  -0.0114 -0.0164 149  LEU A CA  
917   C C   . LEU A 151  ? 0.4044 0.3918 0.3869 0.0103  -0.0131 -0.0208 149  LEU A C   
918   O O   . LEU A 151  ? 0.4082 0.3911 0.3941 0.0113  -0.0155 -0.0229 149  LEU A O   
919   C CB  . LEU A 151  ? 0.4369 0.4189 0.4152 0.0067  -0.0098 -0.0117 149  LEU A CB  
920   C CG  . LEU A 151  ? 0.4970 0.4723 0.4773 0.0058  -0.0110 -0.0102 149  LEU A CG  
921   C CD1 . LEU A 151  ? 0.4733 0.4424 0.4558 0.0065  -0.0125 -0.0098 149  LEU A CD1 
922   C CD2 . LEU A 151  ? 0.5551 0.5290 0.5331 0.0035  -0.0091 -0.0057 149  LEU A CD2 
923   N N   . VAL A 152  ? 0.3780 0.3728 0.3588 0.0103  -0.0122 -0.0223 150  VAL A N   
924   C CA  . VAL A 152  ? 0.4009 0.3992 0.3834 0.0117  -0.0139 -0.0270 150  VAL A CA  
925   C C   . VAL A 152  ? 0.4323 0.4315 0.4179 0.0145  -0.0160 -0.0323 150  VAL A C   
926   O O   . VAL A 152  ? 0.4353 0.4318 0.4244 0.0158  -0.0185 -0.0358 150  VAL A O   
927   C CB  . VAL A 152  ? 0.4258 0.4330 0.4054 0.0113  -0.0122 -0.0274 150  VAL A CB  
928   C CG1 . VAL A 152  ? 0.4442 0.4565 0.4254 0.0131  -0.0140 -0.0330 150  VAL A CG1 
929   C CG2 . VAL A 152  ? 0.4418 0.4475 0.4190 0.0087  -0.0107 -0.0226 150  VAL A CG2 
930   N N   . VAL A 153  ? 0.4105 0.4135 0.3952 0.0157  -0.0152 -0.0329 151  VAL A N   
931   C CA  . VAL A 153  ? 0.4280 0.4337 0.4156 0.0187  -0.0171 -0.0385 151  VAL A CA  
932   C C   . VAL A 153  ? 0.4282 0.4254 0.4193 0.0198  -0.0193 -0.0387 151  VAL A C   
933   O O   . VAL A 153  ? 0.4370 0.4327 0.4320 0.0220  -0.0221 -0.0433 151  VAL A O   
934   C CB  . VAL A 153  ? 0.3673 0.3814 0.3528 0.0196  -0.0153 -0.0393 151  VAL A CB  
935   C CG1 . VAL A 153  ? 0.3785 0.3951 0.3672 0.0229  -0.0173 -0.0450 151  VAL A CG1 
936   C CG2 . VAL A 153  ? 0.3603 0.3836 0.3429 0.0189  -0.0135 -0.0396 151  VAL A CG2 
937   N N   . THR A 154  ? 0.3962 0.3878 0.3862 0.0183  -0.0184 -0.0338 152  THR A N   
938   C CA  . THR A 154  ? 0.4274 0.4119 0.4203 0.0193  -0.0203 -0.0335 152  THR A CA  
939   C C   . THR A 154  ? 0.4512 0.4267 0.4451 0.0175  -0.0210 -0.0295 152  THR A C   
940   O O   . THR A 154  ? 0.4665 0.4358 0.4632 0.0183  -0.0230 -0.0292 152  THR A O   
941   C CB  . THR A 154  ? 0.4402 0.4259 0.4313 0.0196  -0.0189 -0.0314 152  THR A CB  
942   O OG1 . THR A 154  ? 0.4892 0.4729 0.4769 0.0168  -0.0166 -0.0257 152  THR A OG1 
943   C CG2 . THR A 154  ? 0.4423 0.4376 0.4323 0.0210  -0.0178 -0.0347 152  THR A CG2 
944   N N   . GLY A 155  ? 0.4465 0.4215 0.4382 0.0150  -0.0195 -0.0263 153  GLY A N   
945   C CA  . GLY A 155  ? 0.4453 0.4126 0.4376 0.0130  -0.0197 -0.0221 153  GLY A CA  
946   C C   . GLY A 155  ? 0.5096 0.4736 0.4997 0.0119  -0.0183 -0.0172 153  GLY A C   
947   O O   . GLY A 155  ? 0.5666 0.5247 0.5573 0.0105  -0.0185 -0.0136 153  GLY A O   
948   N N   . LYS A 156  ? 0.4739 0.4421 0.4617 0.0125  -0.0168 -0.0171 154  LYS A N   
949   C CA  . LYS A 156  ? 0.4907 0.4564 0.4763 0.0116  -0.0155 -0.0130 154  LYS A CA  
950   C C   . LYS A 156  ? 0.4741 0.4444 0.4559 0.0100  -0.0126 -0.0106 154  LYS A C   
951   O O   . LYS A 156  ? 0.4522 0.4289 0.4329 0.0103  -0.0117 -0.0127 154  LYS A O   
952   C CB  . LYS A 156  ? 0.4561 0.4221 0.4429 0.0138  -0.0167 -0.0147 154  LYS A CB  
953   N N   . LEU A 157  ? 0.4802 0.4472 0.4598 0.0083  -0.0113 -0.0062 155  LEU A N   
954   C CA  . LEU A 157  ? 0.4999 0.4702 0.4762 0.0066  -0.0088 -0.0037 155  LEU A CA  
955   C C   . LEU A 157  ? 0.5230 0.4937 0.4979 0.0068  -0.0080 -0.0023 155  LEU A C   
956   O O   . LEU A 157  ? 0.5237 0.4902 0.4993 0.0074  -0.0090 -0.0013 155  LEU A O   
957   C CB  . LEU A 157  ? 0.5001 0.4671 0.4753 0.0045  -0.0078 -0.0002 155  LEU A CB  
958   C CG  . LEU A 157  ? 0.5692 0.5394 0.5415 0.0029  -0.0055 0.0020  155  LEU A CG  
959   C CD1 . LEU A 157  ? 0.5085 0.4849 0.4805 0.0031  -0.0051 -0.0002 155  LEU A CD1 
960   C CD2 . LEU A 157  ? 0.6658 0.6326 0.6374 0.0012  -0.0047 0.0053  155  LEU A CD2 
961   N N   . THR A 158  ? 0.4862 0.4622 0.4594 0.0063  -0.0063 -0.0022 156  THR A N   
962   C CA  . THR A 158  ? 0.5013 0.4780 0.4731 0.0060  -0.0054 -0.0005 156  THR A CA  
963   C C   . THR A 158  ? 0.4572 0.4354 0.4266 0.0039  -0.0033 0.0023  156  THR A C   
964   O O   . THR A 158  ? 0.4679 0.4490 0.4368 0.0031  -0.0026 0.0022  156  THR A O   
965   C CB  . THR A 158  ? 0.5218 0.5037 0.4945 0.0075  -0.0057 -0.0034 156  THR A CB  
966   O OG1 . THR A 158  ? 0.5582 0.5466 0.5304 0.0071  -0.0046 -0.0048 156  THR A OG1 
967   C CG2 . THR A 158  ? 0.5376 0.5179 0.5129 0.0099  -0.0080 -0.0066 156  THR A CG2 
968   N N   . SER A 159  ? 0.4552 0.4316 0.4233 0.0031  -0.0025 0.0047  157  SER A N   
969   C CA  . SER A 159  ? 0.4492 0.4268 0.4156 0.0012  -0.0008 0.0072  157  SER A CA  
970   C C   . SER A 159  ? 0.4018 0.3854 0.3679 0.0008  0.0001  0.0065  157  SER A C   
971   O O   . SER A 159  ? 0.4574 0.4434 0.4227 -0.0006 0.0012  0.0079  157  SER A O   
972   C CB  . SER A 159  ? 0.5017 0.4754 0.4668 0.0006  -0.0004 0.0097  157  SER A CB  
973   O OG  . SER A 159  ? 0.5475 0.5222 0.5129 0.0013  -0.0008 0.0090  157  SER A OG  
974   N N   . THR A 160  ? 0.4193 0.4058 0.3864 0.0019  -0.0004 0.0046  158  THR A N   
975   C CA  . THR A 160  ? 0.3545 0.3476 0.3218 0.0014  0.0006  0.0040  158  THR A CA  
976   C C   . THR A 160  ? 0.3816 0.3794 0.3504 0.0032  -0.0002 0.0003  158  THR A C   
977   O O   . THR A 160  ? 0.4025 0.3980 0.3726 0.0050  -0.0018 -0.0019 158  THR A O   
978   C CB  . THR A 160  ? 0.4186 0.4118 0.3858 0.0007  0.0010  0.0052  158  THR A CB  
979   O OG1 . THR A 160  ? 0.3528 0.3437 0.3209 0.0024  -0.0003 0.0038  158  THR A OG1 
980   C CG2 . THR A 160  ? 0.3983 0.3875 0.3641 -0.0010 0.0018  0.0084  158  THR A CG2 
981   N N   . VAL A 161  ? 0.3353 0.3401 0.3043 0.0027  0.0008  -0.0002 159  VAL A N   
982   C CA  . VAL A 161  ? 0.3288 0.3400 0.2987 0.0040  0.0005  -0.0035 159  VAL A CA  
983   C C   . VAL A 161  ? 0.3153 0.3317 0.2865 0.0048  0.0006  -0.0051 159  VAL A C   
984   O O   . VAL A 161  ? 0.2859 0.3044 0.2568 0.0031  0.0018  -0.0029 159  VAL A O   
985   C CB  . VAL A 161  ? 0.3138 0.3298 0.2824 0.0026  0.0018  -0.0024 159  VAL A CB  
986   C CG1 . VAL A 161  ? 0.3894 0.4145 0.3586 0.0035  0.0021  -0.0051 159  VAL A CG1 
987   C CG2 . VAL A 161  ? 0.3945 0.4063 0.3624 0.0026  0.0012  -0.0022 159  VAL A CG2 
988   N N   . ASN A 162  ? 0.2784 0.2970 0.2514 0.0073  -0.0007 -0.0090 160  ASN A N   
989   C CA  . ASN A 162  ? 0.2907 0.3152 0.2652 0.0081  -0.0006 -0.0109 160  ASN A CA  
990   C C   . ASN A 162  ? 0.2784 0.3125 0.2529 0.0078  0.0007  -0.0121 160  ASN A C   
991   O O   . ASN A 162  ? 0.2480 0.2864 0.2234 0.0098  0.0000  -0.0159 160  ASN A O   
992   C CB  . ASN A 162  ? 0.2635 0.2862 0.2403 0.0112  -0.0026 -0.0145 160  ASN A CB  
993   C CG  . ASN A 162  ? 0.2897 0.3185 0.2682 0.0121  -0.0026 -0.0163 160  ASN A CG  
994   O OD1 . ASN A 162  ? 0.2653 0.3019 0.2438 0.0109  -0.0010 -0.0160 160  ASN A OD1 
995   N ND2 . ASN A 162  ? 0.2756 0.3012 0.2559 0.0142  -0.0043 -0.0180 160  ASN A ND2 
996   N N   . ASP A 163  ? 0.2491 0.2866 0.2224 0.0051  0.0026  -0.0087 161  ASP A N   
997   C CA  . ASP A 163  ? 0.2439 0.2906 0.2167 0.0043  0.0040  -0.0089 161  ASP A CA  
998   C C   . ASP A 163  ? 0.2444 0.3000 0.2190 0.0056  0.0042  -0.0119 161  ASP A C   
999   O O   . ASP A 163  ? 0.2450 0.3091 0.2195 0.0060  0.0050  -0.0136 161  ASP A O   
1000  C CB  . ASP A 163  ? 0.2661 0.3136 0.2375 0.0010  0.0057  -0.0040 161  ASP A CB  
1001  C CG  . ASP A 163  ? 0.3160 0.3600 0.2881 -0.0007 0.0060  -0.0012 161  ASP A CG  
1002  O OD1 . ASP A 163  ? 0.2674 0.3046 0.2400 0.0003  0.0048  -0.0018 161  ASP A OD1 
1003  O OD2 . ASP A 163  ? 0.3474 0.3954 0.3196 -0.0031 0.0073  0.0017  161  ASP A OD2 
1004  N N   . ARG A 164  ? 0.2442 0.2988 0.2206 0.0064  0.0036  -0.0128 162  ARG A N   
1005  C CA  . ARG A 164  ? 0.2447 0.3081 0.2233 0.0080  0.0037  -0.0161 162  ARG A CA  
1006  C C   . ARG A 164  ? 0.2465 0.3111 0.2263 0.0116  0.0020  -0.0214 162  ARG A C   
1007  O O   . ARG A 164  ? 0.2505 0.3245 0.2313 0.0130  0.0025  -0.0247 162  ARG A O   
1008  C CB  . ARG A 164  ? 0.2440 0.3061 0.2244 0.0078  0.0034  -0.0156 162  ARG A CB  
1009  C CG  . ARG A 164  ? 0.3068 0.3692 0.2867 0.0043  0.0049  -0.0109 162  ARG A CG  
1010  C CD  . ARG A 164  ? 0.3885 0.4583 0.3675 0.0019  0.0069  -0.0086 162  ARG A CD  
1011  N NE  . ARG A 164  ? 0.4191 0.5003 0.3992 0.0029  0.0077  -0.0114 162  ARG A NE  
1012  C CZ  . ARG A 164  ? 0.4301 0.5188 0.4090 0.0019  0.0091  -0.0106 162  ARG A CZ  
1013  N NH1 . ARG A 164  ? 0.4145 0.5003 0.3910 -0.0002 0.0098  -0.0070 162  ARG A NH1 
1014  N NH2 . ARG A 164  ? 0.3748 0.4746 0.3549 0.0031  0.0098  -0.0135 162  ARG A NH2 
1015  N N   . SER A 165  ? 0.2474 0.3028 0.2274 0.0131  0.0001  -0.0224 163  SER A N   
1016  C CA  . SER A 165  ? 0.2545 0.3096 0.2360 0.0164  -0.0018 -0.0273 163  SER A CA  
1017  C C   . SER A 165  ? 0.2502 0.3102 0.2305 0.0165  -0.0012 -0.0287 163  SER A C   
1018  O O   . SER A 165  ? 0.2519 0.3183 0.2335 0.0189  -0.0019 -0.0335 163  SER A O   
1019  C CB  . SER A 165  ? 0.2505 0.2942 0.2324 0.0174  -0.0039 -0.0269 163  SER A CB  
1020  O OG  . SER A 165  ? 0.2770 0.3196 0.2609 0.0205  -0.0060 -0.0315 163  SER A OG  
1021  N N   . LEU A 166  ? 0.2491 0.3063 0.2269 0.0139  -0.0001 -0.0249 164  LEU A N   
1022  C CA  . LEU A 166  ? 0.2499 0.3115 0.2262 0.0138  0.0003  -0.0259 164  LEU A CA  
1023  C C   . LEU A 166  ? 0.2498 0.3239 0.2255 0.0133  0.0021  -0.0265 164  LEU A C   
1024  O O   . LEU A 166  ? 0.2513 0.3322 0.2269 0.0149  0.0020  -0.0300 164  LEU A O   
1025  C CB  . LEU A 166  ? 0.2488 0.3043 0.2226 0.0112  0.0010  -0.0214 164  LEU A CB  
1026  C CG  . LEU A 166  ? 0.2706 0.3148 0.2448 0.0117  -0.0008 -0.0211 164  LEU A CG  
1027  C CD1 . LEU A 166  ? 0.2986 0.3377 0.2707 0.0090  0.0002  -0.0162 164  LEU A CD1 
1028  C CD2 . LEU A 166  ? 0.2516 0.2951 0.2273 0.0143  -0.0028 -0.0258 164  LEU A CD2 
1029  N N   . ALA A 167  ? 0.2483 0.3260 0.2238 0.0111  0.0039  -0.0231 165  ALA A N   
1030  C CA  . ALA A 167  ? 0.2604 0.3504 0.2355 0.0104  0.0057  -0.0232 165  ALA A CA  
1031  C C   . ALA A 167  ? 0.2500 0.3477 0.2276 0.0137  0.0050  -0.0291 165  ALA A C   
1032  O O   . ALA A 167  ? 0.2512 0.3592 0.2284 0.0147  0.0057  -0.0317 165  ALA A O   
1033  C CB  . ALA A 167  ? 0.2469 0.3385 0.2220 0.0072  0.0075  -0.0182 165  ALA A CB  
1034  N N   . ALA A 168  ? 0.2501 0.3434 0.2302 0.0156  0.0035  -0.0314 166  ALA A N   
1035  C CA  . ALA A 168  ? 0.2518 0.3512 0.2346 0.0192  0.0023  -0.0374 166  ALA A CA  
1036  C C   . ALA A 168  ? 0.2541 0.3538 0.2371 0.0221  0.0007  -0.0423 166  ALA A C   
1037  O O   . ALA A 168  ? 0.2557 0.3652 0.2397 0.0244  0.0007  -0.0470 166  ALA A O   
1038  C CB  . ALA A 168  ? 0.2517 0.3446 0.2373 0.0209  0.0006  -0.0386 166  ALA A CB  
1039  N N   . ALA A 169  ? 0.2544 0.3436 0.2367 0.0221  -0.0008 -0.0415 167  ALA A N   
1040  C CA  . ALA A 169  ? 0.2568 0.3454 0.2398 0.0247  -0.0027 -0.0463 167  ALA A CA  
1041  C C   . ALA A 169  ? 0.2573 0.3556 0.2380 0.0240  -0.0012 -0.0469 167  ALA A C   
1042  O O   . ALA A 169  ? 0.2596 0.3645 0.2413 0.0268  -0.0022 -0.0525 167  ALA A O   
1043  C CB  . ALA A 169  ? 0.2570 0.3327 0.2398 0.0241  -0.0044 -0.0445 167  ALA A CB  
1044  N N   . LEU A 170  ? 0.2636 0.3631 0.2412 0.0205  0.0010  -0.0413 168  LEU A N   
1045  C CA  . LEU A 170  ? 0.2618 0.3703 0.2369 0.0197  0.0023  -0.0411 168  LEU A CA  
1046  C C   . LEU A 170  ? 0.2572 0.3800 0.2327 0.0209  0.0036  -0.0441 168  LEU A C   
1047  O O   . LEU A 170  ? 0.2831 0.4143 0.2582 0.0229  0.0034  -0.0484 168  LEU A O   
1048  C CB  . LEU A 170  ? 0.2542 0.3605 0.2263 0.0156  0.0043  -0.0340 168  LEU A CB  
1049  C CG  . LEU A 170  ? 0.2933 0.4075 0.2624 0.0145  0.0055  -0.0329 168  LEU A CG  
1050  C CD1 . LEU A 170  ? 0.2786 0.3907 0.2477 0.0168  0.0035  -0.0373 168  LEU A CD1 
1051  C CD2 . LEU A 170  ? 0.3327 0.4430 0.2994 0.0106  0.0070  -0.0256 168  LEU A CD2 
1052  N N   . THR A 171  ? 0.2558 0.3822 0.2325 0.0198  0.0050  -0.0422 169  THR A N   
1053  C CA  . THR A 171  ? 0.2568 0.3970 0.2344 0.0211  0.0062  -0.0451 169  THR A CA  
1054  C C   . THR A 171  ? 0.2830 0.4263 0.2634 0.0259  0.0041  -0.0533 169  THR A C   
1055  O O   . THR A 171  ? 0.2612 0.4160 0.2413 0.0277  0.0045  -0.0574 169  THR A O   
1056  C CB  . THR A 171  ? 0.2979 0.4395 0.2771 0.0193  0.0076  -0.0420 169  THR A CB  
1057  O OG1 . THR A 171  ? 0.3288 0.4690 0.3058 0.0149  0.0095  -0.0348 169  THR A OG1 
1058  C CG2 . THR A 171  ? 0.2842 0.4404 0.2651 0.0209  0.0087  -0.0455 169  THR A CG2 
1059  N N   . ARG A 172  ? 0.2595 0.3924 0.2426 0.0279  0.0016  -0.0557 170  ARG A N   
1060  C CA  . ARG A 172  ? 0.2623 0.3967 0.2486 0.0326  -0.0009 -0.0633 170  ARG A CA  
1061  C C   . ARG A 172  ? 0.2647 0.4018 0.2502 0.0344  -0.0020 -0.0676 170  ARG A C   
1062  O O   . ARG A 172  ? 0.2671 0.4142 0.2538 0.0375  -0.0024 -0.0736 170  ARG A O   
1063  C CB  . ARG A 172  ? 0.2625 0.3837 0.2517 0.0341  -0.0035 -0.0641 170  ARG A CB  
1064  C CG  . ARG A 172  ? 0.2832 0.4057 0.2766 0.0389  -0.0063 -0.0716 170  ARG A CG  
1065  C CD  . ARG A 172  ? 0.2662 0.3752 0.2625 0.0402  -0.0091 -0.0717 170  ARG A CD  
1066  N NE  . ARG A 172  ? 0.2634 0.3663 0.2588 0.0374  -0.0080 -0.0657 170  ARG A NE  
1067  C CZ  . ARG A 172  ? 0.2619 0.3540 0.2553 0.0346  -0.0079 -0.0603 170  ARG A CZ  
1068  N NH1 . ARG A 172  ? 0.2625 0.3490 0.2545 0.0339  -0.0086 -0.0596 170  ARG A NH1 
1069  N NH2 . ARG A 172  ? 0.2598 0.3472 0.2528 0.0326  -0.0072 -0.0557 170  ARG A NH2 
1070  N N   . LEU A 173  ? 0.2644 0.3927 0.2479 0.0327  -0.0026 -0.0648 171  LEU A N   
1071  C CA  . LEU A 173  ? 0.2670 0.3965 0.2502 0.0346  -0.0042 -0.0692 171  LEU A CA  
1072  C C   . LEU A 173  ? 0.2732 0.4169 0.2534 0.0341  -0.0021 -0.0698 171  LEU A C   
1073  O O   . LEU A 173  ? 0.2704 0.4210 0.2512 0.0370  -0.0032 -0.0759 171  LEU A O   
1074  C CB  . LEU A 173  ? 0.2664 0.3831 0.2486 0.0328  -0.0054 -0.0659 171  LEU A CB  
1075  C CG  . LEU A 173  ? 0.2640 0.3797 0.2421 0.0287  -0.0031 -0.0590 171  LEU A CG  
1076  C CD1 . LEU A 173  ? 0.2882 0.4112 0.2639 0.0289  -0.0030 -0.0608 171  LEU A CD1 
1077  C CD2 . LEU A 173  ? 0.2843 0.3854 0.2623 0.0266  -0.0040 -0.0545 171  LEU A CD2 
1078  N N   . ILE A 174  ? 0.2654 0.4139 0.2425 0.0305  0.0009  -0.0634 172  ILE A N   
1079  C CA  . ILE A 174  ? 0.2663 0.4290 0.2405 0.0299  0.0030  -0.0633 172  ILE A CA  
1080  C C   . ILE A 174  ? 0.2892 0.4653 0.2652 0.0327  0.0035  -0.0687 172  ILE A C   
1081  O O   . ILE A 174  ? 0.3148 0.5018 0.2901 0.0349  0.0035  -0.0736 172  ILE A O   
1082  C CB  . ILE A 174  ? 0.2882 0.4520 0.2591 0.0251  0.0059  -0.0547 172  ILE A CB  
1083  C CG1 . ILE A 174  ? 0.3185 0.4707 0.2875 0.0228  0.0052  -0.0503 172  ILE A CG1 
1084  C CG2 . ILE A 174  ? 0.3095 0.4892 0.2777 0.0243  0.0082  -0.0541 172  ILE A CG2 
1085  C CD1 . ILE A 174  ? 0.3250 0.4758 0.2913 0.0183  0.0075  -0.0418 172  ILE A CD1 
1086  N N   . SER A 175  ? 0.2668 0.4427 0.2454 0.0329  0.0039  -0.0684 173  SER A N   
1087  C CA  . SER A 175  ? 0.2682 0.4574 0.2489 0.0357  0.0045  -0.0736 173  SER A CA  
1088  C C   . SER A 175  ? 0.2715 0.4618 0.2552 0.0409  0.0016  -0.0829 173  SER A C   
1089  O O   . SER A 175  ? 0.2759 0.4795 0.2603 0.0436  0.0020  -0.0883 173  SER A O   
1090  C CB  . SER A 175  ? 0.2729 0.4605 0.2562 0.0349  0.0052  -0.0715 173  SER A CB  
1091  O OG  . SER A 175  ? 0.3485 0.5372 0.3296 0.0302  0.0080  -0.0635 173  SER A OG  
1092  N N   . ARG A 176  ? 0.2723 0.4489 0.2577 0.0423  -0.0015 -0.0848 174  ARG A N   
1093  C CA  . ARG A 176  ? 0.2887 0.4640 0.2778 0.0471  -0.0048 -0.0934 174  ARG A CA  
1094  C C   . ARG A 176  ? 0.2909 0.4698 0.2783 0.0484  -0.0058 -0.0972 174  ARG A C   
1095  O O   . ARG A 176  ? 0.3065 0.4937 0.2956 0.0523  -0.0072 -0.1050 174  ARG A O   
1096  C CB  . ARG A 176  ? 0.3093 0.4677 0.3016 0.0478  -0.0077 -0.0932 174  ARG A CB  
1097  C CG  . ARG A 176  ? 0.3288 0.4838 0.3256 0.0528  -0.0116 -0.1017 174  ARG A CG  
1098  C CD  . ARG A 176  ? 0.2824 0.4210 0.2825 0.0530  -0.0143 -0.1002 174  ARG A CD  
1099  N NE  . ARG A 176  ? 0.2793 0.4058 0.2780 0.0507  -0.0154 -0.0967 174  ARG A NE  
1100  C CZ  . ARG A 176  ? 0.3300 0.4465 0.3268 0.0470  -0.0144 -0.0892 174  ARG A CZ  
1101  N NH1 . ARG A 176  ? 0.2833 0.3989 0.2795 0.0452  -0.0126 -0.0845 174  ARG A NH1 
1102  N NH2 . ARG A 176  ? 0.3503 0.4576 0.3460 0.0453  -0.0153 -0.0867 174  ARG A NH2 
1103  N N   . CYS A 177  ? 0.3350 0.5081 0.3189 0.0451  -0.0052 -0.0919 175  CYS A N   
1104  C CA  . CYS A 177  ? 0.2963 0.4707 0.2789 0.0462  -0.0066 -0.0953 175  CYS A CA  
1105  C C   . CYS A 177  ? 0.3652 0.5506 0.3427 0.0437  -0.0038 -0.0918 175  CYS A C   
1106  O O   . CYS A 177  ? 0.3497 0.5404 0.3260 0.0452  -0.0048 -0.0959 175  CYS A O   
1107  C CB  . CYS A 177  ? 0.3397 0.4976 0.3232 0.0450  -0.0089 -0.0933 175  CYS A CB  
1108  S SG  . CYS A 177  ? 0.4069 0.5503 0.3964 0.0476  -0.0124 -0.0964 175  CYS A SG  
1109  N N   . GLY A 178  ? 0.3402 0.5290 0.3148 0.0399  -0.0006 -0.0843 176  GLY A N   
1110  C CA  . GLY A 178  ? 0.3624 0.5630 0.3324 0.0377  0.0020  -0.0809 176  GLY A CA  
1111  C C   . GLY A 178  ? 0.3237 0.5191 0.2906 0.0356  0.0016  -0.0775 176  GLY A C   
1112  O O   . GLY A 178  ? 0.3253 0.5065 0.2930 0.0347  0.0000  -0.0756 176  GLY A O   
1113  N N   . GLU A 179  ? 0.3780 0.5858 0.3411 0.0349  0.0032  -0.0766 177  GLU A N   
1114  C CA  . GLU A 179  ? 0.3374 0.5424 0.2971 0.0329  0.0031  -0.0732 177  GLU A CA  
1115  C C   . GLU A 179  ? 0.3511 0.5461 0.3127 0.0350  -0.0004 -0.0781 177  GLU A C   
1116  O O   . GLU A 179  ? 0.3504 0.5357 0.3107 0.0326  -0.0008 -0.0735 177  GLU A O   
1117  C CB  . GLU A 179  ? 0.3899 0.6120 0.3456 0.0329  0.0049  -0.0732 177  GLU A CB  
1118  C CG  . GLU A 179  ? 0.4274 0.6489 0.3792 0.0308  0.0049  -0.0693 177  GLU A CG  
1119  C CD  . GLU A 179  ? 0.5530 0.7924 0.5007 0.0310  0.0067  -0.0694 177  GLU A CD  
1120  O OE1 . GLU A 179  ? 0.5603 0.8111 0.5073 0.0305  0.0091  -0.0681 177  GLU A OE1 
1121  O OE2 . GLU A 179  ? 0.6266 0.8691 0.5718 0.0315  0.0057  -0.0708 177  GLU A OE2 
1122  N N   . PRO A 180  ? 0.3151 0.5118 0.2799 0.0393  -0.0030 -0.0871 178  PRO A N   
1123  C CA  . PRO A 180  ? 0.2840 0.4708 0.2510 0.0409  -0.0064 -0.0913 178  PRO A CA  
1124  C C   . PRO A 180  ? 0.3542 0.5232 0.3232 0.0388  -0.0075 -0.0868 178  PRO A C   
1125  O O   . PRO A 180  ? 0.3434 0.5048 0.3122 0.0378  -0.0090 -0.0859 178  PRO A O   
1126  C CB  . PRO A 180  ? 0.3514 0.5423 0.3226 0.0459  -0.0088 -0.1013 178  PRO A CB  
1127  C CG  . PRO A 180  ? 0.3217 0.5303 0.2907 0.0471  -0.0065 -0.1033 178  PRO A CG  
1128  C CD  . PRO A 180  ? 0.3175 0.5274 0.2838 0.0430  -0.0029 -0.0941 178  PRO A CD  
1129  N N   . VAL A 181  ? 0.3080 0.4705 0.2791 0.0380  -0.0069 -0.0841 179  VAL A N   
1130  C CA  . VAL A 181  ? 0.3096 0.4559 0.2824 0.0361  -0.0079 -0.0800 179  VAL A CA  
1131  C C   . VAL A 181  ? 0.3134 0.4559 0.2823 0.0316  -0.0056 -0.0711 179  VAL A C   
1132  O O   . VAL A 181  ? 0.3210 0.4519 0.2903 0.0300  -0.0066 -0.0681 179  VAL A O   
1133  C CB  . VAL A 181  ? 0.3117 0.4521 0.2880 0.0371  -0.0083 -0.0805 179  VAL A CB  
1134  C CG1 . VAL A 181  ? 0.2958 0.4412 0.2700 0.0346  -0.0051 -0.0747 179  VAL A CG1 
1135  C CG2 . VAL A 181  ? 0.3337 0.4577 0.3126 0.0364  -0.0104 -0.0787 179  VAL A CG2 
1136  N N   . ILE A 182  ? 0.3183 0.4708 0.2837 0.0296  -0.0026 -0.0667 180  ILE A N   
1137  C CA  . ILE A 182  ? 0.2978 0.4474 0.2598 0.0255  -0.0006 -0.0584 180  ILE A CA  
1138  C C   . ILE A 182  ? 0.3333 0.4828 0.2933 0.0251  -0.0016 -0.0584 180  ILE A C   
1139  O O   . ILE A 182  ? 0.3452 0.4851 0.3045 0.0229  -0.0019 -0.0539 180  ILE A O   
1140  C CB  . ILE A 182  ? 0.3477 0.5089 0.3070 0.0235  0.0025  -0.0540 180  ILE A CB  
1141  C CG1 . ILE A 182  ? 0.3044 0.4651 0.2661 0.0237  0.0035  -0.0537 180  ILE A CG1 
1142  C CG2 . ILE A 182  ? 0.3204 0.4791 0.2764 0.0194  0.0043  -0.0455 180  ILE A CG2 
1143  C CD1 . ILE A 182  ? 0.3149 0.4889 0.2748 0.0224  0.0063  -0.0511 180  ILE A CD1 
1144  N N   . ARG A 183  ? 0.3452 0.5057 0.3042 0.0275  -0.0023 -0.0639 181  ARG A N   
1145  C CA  . ARG A 183  ? 0.3398 0.5011 0.2969 0.0275  -0.0035 -0.0647 181  ARG A CA  
1146  C C   . ARG A 183  ? 0.3713 0.5191 0.3317 0.0282  -0.0065 -0.0672 181  ARG A C   
1147  O O   . ARG A 183  ? 0.4244 0.5665 0.3836 0.0263  -0.0069 -0.0639 181  ARG A O   
1148  C CB  . ARG A 183  ? 0.3302 0.5063 0.2860 0.0304  -0.0039 -0.0712 181  ARG A CB  
1149  N N   . ARG A 184  ? 0.3575 0.5001 0.3223 0.0309  -0.0086 -0.0729 182  ARG A N   
1150  C CA  . ARG A 184  ? 0.3516 0.4811 0.3199 0.0313  -0.0115 -0.0748 182  ARG A CA  
1151  C C   . ARG A 184  ? 0.4046 0.5215 0.3729 0.0280  -0.0106 -0.0673 182  ARG A C   
1152  O O   . ARG A 184  ? 0.3873 0.4956 0.3563 0.0268  -0.0119 -0.0658 182  ARG A O   
1153  C CB  . ARG A 184  ? 0.4212 0.5479 0.3944 0.0348  -0.0140 -0.0820 182  ARG A CB  
1154  C CG  . ARG A 184  ? 0.4664 0.6027 0.4408 0.0385  -0.0159 -0.0907 182  ARG A CG  
1155  C CD  . ARG A 184  ? 0.4465 0.5765 0.4231 0.0391  -0.0190 -0.0940 182  ARG A CD  
1156  N NE  . ARG A 184  ? 0.5164 0.6354 0.4987 0.0409  -0.0222 -0.0982 182  ARG A NE  
1157  C CZ  . ARG A 184  ? 0.5384 0.6435 0.5230 0.0390  -0.0233 -0.0946 182  ARG A CZ  
1158  N NH1 . ARG A 184  ? 0.6039 0.7040 0.5856 0.0354  -0.0217 -0.0873 182  ARG A NH1 
1159  N NH2 . ARG A 184  ? 0.4763 0.5724 0.4663 0.0409  -0.0263 -0.0985 182  ARG A NH2 
1160  N N   . GLY A 185  ? 0.3672 0.4830 0.3348 0.0265  -0.0085 -0.0628 183  GLY A N   
1161  C CA  . GLY A 185  ? 0.3239 0.4288 0.2911 0.0234  -0.0075 -0.0558 183  GLY A CA  
1162  C C   . GLY A 185  ? 0.3997 0.5049 0.3634 0.0205  -0.0062 -0.0503 183  GLY A C   
1163  O O   . GLY A 185  ? 0.3362 0.4317 0.3004 0.0189  -0.0069 -0.0473 183  GLY A O   
1164  N N   . VAL A 186  ? 0.3630 0.4798 0.3233 0.0200  -0.0045 -0.0489 184  VAL A N   
1165  C CA  . VAL A 186  ? 0.4121 0.5299 0.3690 0.0174  -0.0033 -0.0434 184  VAL A CA  
1166  C C   . VAL A 186  ? 0.3855 0.4997 0.3431 0.0180  -0.0056 -0.0460 184  VAL A C   
1167  O O   . VAL A 186  ? 0.4332 0.5406 0.3901 0.0159  -0.0056 -0.0416 184  VAL A O   
1168  C CB  . VAL A 186  ? 0.4338 0.5659 0.3870 0.0169  -0.0013 -0.0419 184  VAL A CB  
1169  C CG1 . VAL A 186  ? 0.3990 0.5334 0.3489 0.0150  -0.0008 -0.0376 184  VAL A CG1 
1170  C CG2 . VAL A 186  ? 0.3923 0.5264 0.3449 0.0152  0.0012  -0.0373 184  VAL A CG2 
1171  N N   . ASP A 187  ? 0.4263 0.5450 0.3855 0.0210  -0.0077 -0.0534 185  ASP A N   
1172  C CA  . ASP A 187  ? 0.3797 0.4951 0.3400 0.0217  -0.0101 -0.0564 185  ASP A CA  
1173  C C   . ASP A 187  ? 0.4248 0.5255 0.3886 0.0208  -0.0116 -0.0553 185  ASP A C   
1174  O O   . ASP A 187  ? 0.4118 0.5073 0.3757 0.0193  -0.0123 -0.0531 185  ASP A O   
1175  C CB  . ASP A 187  ? 0.4021 0.5251 0.3640 0.0253  -0.0123 -0.0652 185  ASP A CB  
1176  C CG  . ASP A 187  ? 0.5141 0.6528 0.4722 0.0261  -0.0108 -0.0664 185  ASP A CG  
1177  O OD1 . ASP A 187  ? 0.6037 0.7469 0.5578 0.0237  -0.0085 -0.0602 185  ASP A OD1 
1178  O OD2 . ASP A 187  ? 0.5703 0.7171 0.5295 0.0293  -0.0120 -0.0736 185  ASP A OD2 
1179  N N   . MET A 188  ? 0.3807 0.4750 0.3475 0.0216  -0.0121 -0.0565 186  MET A N   
1180  C CA  . MET A 188  ? 0.4143 0.4953 0.3845 0.0207  -0.0135 -0.0552 186  MET A CA  
1181  C C   . MET A 188  ? 0.4868 0.5614 0.4549 0.0174  -0.0115 -0.0472 186  MET A C   
1182  O O   . MET A 188  ? 0.4797 0.5467 0.4489 0.0161  -0.0125 -0.0454 186  MET A O   
1183  C CB  . MET A 188  ? 0.4858 0.5622 0.4592 0.0224  -0.0142 -0.0577 186  MET A CB  
1184  C CG  . MET A 188  ? 0.5041 0.5671 0.4811 0.0217  -0.0159 -0.0565 186  MET A CG  
1185  S SD  . MET A 188  ? 0.7270 0.7861 0.7086 0.0236  -0.0198 -0.0631 186  MET A SD  
1186  C CE  . MET A 188  ? 0.6026 0.6695 0.5865 0.0278  -0.0215 -0.0715 186  MET A CE  
1187  N N   . ALA A 189  ? 0.4390 0.5167 0.4043 0.0159  -0.0089 -0.0426 187  ALA A N   
1188  C CA  . ALA A 189  ? 0.4272 0.4988 0.3910 0.0129  -0.0072 -0.0354 187  ALA A CA  
1189  C C   . ALA A 189  ? 0.4651 0.5387 0.4267 0.0115  -0.0071 -0.0327 187  ALA A C   
1190  O O   . ALA A 189  ? 0.4575 0.5236 0.4191 0.0096  -0.0069 -0.0285 187  ALA A O   
1191  C CB  . ALA A 189  ? 0.4242 0.4994 0.3859 0.0117  -0.0047 -0.0312 187  ALA A CB  
1192  N N   . MET A 190  ? 0.4369 0.5207 0.3964 0.0125  -0.0072 -0.0352 188  MET A N   
1193  C CA  . MET A 190  ? 0.4929 0.5796 0.4502 0.0113  -0.0071 -0.0327 188  MET A CA  
1194  C C   . MET A 190  ? 0.4879 0.5679 0.4478 0.0116  -0.0095 -0.0351 188  MET A C   
1195  O O   . MET A 190  ? 0.4963 0.5725 0.4555 0.0098  -0.0094 -0.0312 188  MET A O   
1196  C CB  . MET A 190  ? 0.4518 0.5520 0.4062 0.0125  -0.0068 -0.0350 188  MET A CB  
1197  C CG  . MET A 190  ? 0.5085 0.6130 0.4597 0.0110  -0.0063 -0.0311 188  MET A CG  
1198  S SD  . MET A 190  ? 0.6484 0.7694 0.5963 0.0128  -0.0063 -0.0346 188  MET A SD  
1199  C CE  . MET A 190  ? 0.5654 0.6930 0.5091 0.0102  -0.0032 -0.0264 188  MET A CE  
1200  N N   . ARG A 191  ? 0.4451 0.5237 0.4083 0.0138  -0.0118 -0.0416 189  ARG A N   
1201  C CA  . ARG A 191  ? 0.5271 0.5989 0.4935 0.0139  -0.0142 -0.0439 189  ARG A CA  
1202  C C   . ARG A 191  ? 0.5407 0.6004 0.5092 0.0120  -0.0140 -0.0397 189  ARG A C   
1203  O O   . ARG A 191  ? 0.5112 0.5657 0.4808 0.0107  -0.0147 -0.0379 189  ARG A O   
1204  C CB  . ARG A 191  ? 0.4673 0.5402 0.4372 0.0167  -0.0169 -0.0519 189  ARG A CB  
1205  N N   . MET A 192  ? 0.4823 0.5377 0.4513 0.0119  -0.0129 -0.0381 190  MET A N   
1206  C CA  . MET A 192  ? 0.4861 0.5305 0.4570 0.0103  -0.0128 -0.0344 190  MET A CA  
1207  C C   . MET A 192  ? 0.5095 0.5519 0.4778 0.0077  -0.0107 -0.0277 190  MET A C   
1208  O O   . MET A 192  ? 0.5089 0.5442 0.4786 0.0063  -0.0111 -0.0252 190  MET A O   
1209  C CB  . MET A 192  ? 0.4889 0.5300 0.4610 0.0110  -0.0123 -0.0347 190  MET A CB  
1210  C CG  . MET A 192  ? 0.4761 0.5173 0.4516 0.0137  -0.0147 -0.0412 190  MET A CG  
1211  S SD  . MET A 192  ? 0.6482 0.6827 0.6256 0.0141  -0.0144 -0.0402 190  MET A SD  
1212  C CE  . MET A 192  ? 0.5532 0.5751 0.5334 0.0123  -0.0155 -0.0369 190  MET A CE  
1213  N N   . MET A 193  ? 0.4763 0.5249 0.4411 0.0070  -0.0087 -0.0246 191  MET A N   
1214  C CA  . MET A 193  ? 0.5406 0.5871 0.5032 0.0047  -0.0068 -0.0181 191  MET A CA  
1215  C C   . MET A 193  ? 0.5367 0.5859 0.4980 0.0039  -0.0072 -0.0167 191  MET A C   
1216  O O   . MET A 193  ? 0.5083 0.5528 0.4692 0.0023  -0.0065 -0.0123 191  MET A O   
1217  C CB  . MET A 193  ? 0.5102 0.5619 0.4701 0.0041  -0.0047 -0.0151 191  MET A CB  
1218  C CG  . MET A 193  ? 0.5345 0.5820 0.4954 0.0043  -0.0040 -0.0149 191  MET A CG  
1219  S SD  . MET A 193  ? 0.6487 0.6999 0.6069 0.0026  -0.0014 -0.0096 191  MET A SD  
1220  C CE  . MET A 193  ? 0.5370 0.6018 0.4931 0.0038  -0.0009 -0.0122 191  MET A CE  
1221  N N   . GLY A 194  ? 0.5083 0.5654 0.4688 0.0053  -0.0082 -0.0204 192  GLY A N   
1222  C CA  . GLY A 194  ? 0.5148 0.5755 0.4738 0.0047  -0.0086 -0.0190 192  GLY A CA  
1223  C C   . GLY A 194  ? 0.5346 0.5922 0.4965 0.0052  -0.0110 -0.0226 192  GLY A C   
1224  O O   . GLY A 194  ? 0.4873 0.5464 0.4485 0.0045  -0.0114 -0.0211 192  GLY A O   
1225  N N   . GLU A 195  ? 0.4527 0.5060 0.4181 0.0064  -0.0126 -0.0272 193  GLU A N   
1226  C CA  . GLU A 195  ? 0.4993 0.5501 0.4681 0.0070  -0.0152 -0.0313 193  GLU A CA  
1227  C C   . GLU A 195  ? 0.4724 0.5127 0.4455 0.0065  -0.0162 -0.0318 193  GLU A C   
1228  O O   . GLU A 195  ? 0.3705 0.4069 0.3464 0.0059  -0.0178 -0.0326 193  GLU A O   
1229  C CB  . GLU A 195  ? 0.5494 0.6077 0.5188 0.0094  -0.0170 -0.0382 193  GLU A CB  
1230  C CG  . GLU A 195  ? 0.5976 0.6675 0.5629 0.0100  -0.0163 -0.0383 193  GLU A CG  
1231  C CD  . GLU A 195  ? 0.6453 0.7235 0.6104 0.0127  -0.0174 -0.0449 193  GLU A CD  
1232  O OE1 . GLU A 195  ? 0.6224 0.6972 0.5914 0.0143  -0.0195 -0.0504 193  GLU A OE1 
1233  O OE2 . GLU A 195  ? 0.6593 0.7475 0.6205 0.0133  -0.0161 -0.0444 193  GLU A OE2 
1234  N N   . GLN A 196  ? 0.5198 0.5557 0.4935 0.0067  -0.0155 -0.0311 194  GLN A N   
1235  C CA  . GLN A 196  ? 0.5223 0.5488 0.4999 0.0064  -0.0165 -0.0314 194  GLN A CA  
1236  C C   . GLN A 196  ? 0.5064 0.5260 0.4833 0.0043  -0.0147 -0.0252 194  GLN A C   
1237  O O   . GLN A 196  ? 0.5259 0.5387 0.5055 0.0031  -0.0153 -0.0238 194  GLN A O   
1238  C CB  . GLN A 196  ? 0.5064 0.5326 0.4856 0.0083  -0.0173 -0.0352 194  GLN A CB  
1239  N N   . PHE A 197  ? 0.4522 0.4738 0.4258 0.0038  -0.0123 -0.0216 195  PHE A N   
1240  C CA  . PHE A 197  ? 0.4787 0.4943 0.4515 0.0020  -0.0106 -0.0161 195  PHE A CA  
1241  C C   . PHE A 197  ? 0.4291 0.4449 0.4009 0.0005  -0.0101 -0.0127 195  PHE A C   
1242  O O   . PHE A 197  ? 0.4448 0.4546 0.4178 -0.0009 -0.0097 -0.0096 195  PHE A O   
1243  C CB  . PHE A 197  ? 0.4715 0.4893 0.4415 0.0019  -0.0086 -0.0136 195  PHE A CB  
1244  C CG  . PHE A 197  ? 0.5560 0.5730 0.5271 0.0034  -0.0090 -0.0165 195  PHE A CG  
1245  C CD1 . PHE A 197  ? 0.5538 0.5655 0.5285 0.0043  -0.0110 -0.0195 195  PHE A CD1 
1246  C CD2 . PHE A 197  ? 0.5401 0.5619 0.5090 0.0038  -0.0076 -0.0160 195  PHE A CD2 
1247  C CE1 . PHE A 197  ? 0.5012 0.5121 0.4772 0.0058  -0.0116 -0.0221 195  PHE A CE1 
1248  C CE2 . PHE A 197  ? 0.5333 0.5548 0.5035 0.0053  -0.0081 -0.0188 195  PHE A CE2 
1249  C CZ  . PHE A 197  ? 0.4867 0.5026 0.4604 0.0064  -0.0101 -0.0218 195  PHE A CZ  
1250  N N   . VAL A 198  ? 0.4192 0.4423 0.3890 0.0007  -0.0100 -0.0132 196  VAL A N   
1251  C CA  . VAL A 198  ? 0.4232 0.4471 0.3922 -0.0005 -0.0098 -0.0103 196  VAL A CA  
1252  C C   . VAL A 198  ? 0.4031 0.4315 0.3733 0.0004  -0.0119 -0.0144 196  VAL A C   
1253  O O   . VAL A 198  ? 0.4242 0.4578 0.3943 0.0020  -0.0129 -0.0189 196  VAL A O   
1254  C CB  . VAL A 198  ? 0.3922 0.4206 0.3574 -0.0012 -0.0079 -0.0060 196  VAL A CB  
1255  C CG1 . VAL A 198  ? 0.4454 0.4691 0.4098 -0.0020 -0.0061 -0.0022 196  VAL A CG1 
1256  C CG2 . VAL A 198  ? 0.4259 0.4634 0.3886 0.0000  -0.0079 -0.0082 196  VAL A CG2 
1257  N N   . THR A 199  ? 0.3515 0.3781 0.3230 -0.0006 -0.0125 -0.0132 197  THR A N   
1258  C CA  . THR A 199  ? 0.3739 0.4056 0.3461 0.0001  -0.0144 -0.0165 197  THR A CA  
1259  C C   . THR A 199  ? 0.4247 0.4656 0.3929 0.0007  -0.0137 -0.0158 197  THR A C   
1260  O O   . THR A 199  ? 0.4713 0.5189 0.4390 0.0020  -0.0151 -0.0199 197  THR A O   
1261  C CB  . THR A 199  ? 0.4045 0.4324 0.3792 -0.0013 -0.0151 -0.0148 197  THR A CB  
1262  O OG1 . THR A 199  ? 0.3799 0.3998 0.3584 -0.0020 -0.0156 -0.0152 197  THR A OG1 
1263  C CG2 . THR A 199  ? 0.3848 0.4180 0.3607 -0.0006 -0.0173 -0.0186 197  THR A CG2 
1264  N N   . GLY A 200  ? 0.4152 0.4565 0.3805 -0.0003 -0.0117 -0.0105 198  GLY A N   
1265  C CA  . GLY A 200  ? 0.4126 0.4622 0.3740 0.0000  -0.0110 -0.0088 198  GLY A CA  
1266  C C   . GLY A 200  ? 0.4366 0.4849 0.3957 -0.0011 -0.0087 -0.0033 198  GLY A C   
1267  O O   . GLY A 200  ? 0.4340 0.4748 0.3943 -0.0022 -0.0078 -0.0004 198  GLY A O   
1268  N N   . GLU A 201  ? 0.4318 0.4876 0.3875 -0.0009 -0.0078 -0.0019 199  GLU A N   
1269  C CA  . GLU A 201  ? 0.4813 0.5367 0.4349 -0.0021 -0.0059 0.0035  199  GLU A CA  
1270  C C   . GLU A 201  ? 0.4381 0.4910 0.3913 -0.0033 -0.0056 0.0085  199  GLU A C   
1271  O O   . GLU A 201  ? 0.4150 0.4632 0.3682 -0.0044 -0.0043 0.0128  199  GLU A O   
1272  C CB  . GLU A 201  ? 0.5033 0.5682 0.4537 -0.0016 -0.0051 0.0035  199  GLU A CB  
1273  C CG  . GLU A 201  ? 0.5709 0.6367 0.5194 -0.0029 -0.0032 0.0090  199  GLU A CG  
1274  C CD  . GLU A 201  ? 0.7451 0.8214 0.6907 -0.0025 -0.0025 0.0088  199  GLU A CD  
1275  O OE1 . GLU A 201  ? 0.7545 0.8349 0.7001 -0.0011 -0.0028 0.0039  199  GLU A OE1 
1276  O OE2 . GLU A 201  ? 0.7704 0.8510 0.7136 -0.0036 -0.0017 0.0136  199  GLU A OE2 
1277  N N   . THR A 202  ? 0.4074 0.4635 0.3606 -0.0030 -0.0069 0.0079  200  THR A N   
1278  C CA  . THR A 202  ? 0.4326 0.4868 0.3860 -0.0038 -0.0071 0.0121  200  THR A CA  
1279  C C   . THR A 202  ? 0.3746 0.4261 0.3307 -0.0035 -0.0087 0.0094  200  THR A C   
1280  O O   . THR A 202  ? 0.3585 0.4117 0.3160 -0.0026 -0.0100 0.0043  200  THR A O   
1281  C CB  . THR A 202  ? 0.3912 0.4535 0.3414 -0.0038 -0.0071 0.0151  200  THR A CB  
1282  O OG1 . THR A 202  ? 0.4134 0.4830 0.3628 -0.0025 -0.0087 0.0109  200  THR A OG1 
1283  C CG2 . THR A 202  ? 0.4489 0.5147 0.3965 -0.0043 -0.0055 0.0178  200  THR A CG2 
1284  N N   . ILE A 203  ? 0.3528 0.4005 0.3102 -0.0042 -0.0088 0.0126  201  ILE A N   
1285  C CA  . ILE A 203  ? 0.3449 0.3908 0.3052 -0.0041 -0.0103 0.0103  201  ILE A CA  
1286  C C   . ILE A 203  ? 0.3472 0.4010 0.3067 -0.0031 -0.0121 0.0072  201  ILE A C   
1287  O O   . ILE A 203  ? 0.3736 0.4273 0.3356 -0.0027 -0.0137 0.0027  201  ILE A O   
1288  C CB  . ILE A 203  ? 0.3683 0.4099 0.3299 -0.0049 -0.0099 0.0145  201  ILE A CB  
1289  C CG1 . ILE A 203  ? 0.2917 0.3307 0.2570 -0.0050 -0.0113 0.0121  201  ILE A CG1 
1290  C CG2 . ILE A 203  ? 0.3639 0.4106 0.3230 -0.0048 -0.0101 0.0185  201  ILE A CG2 
1291  C CD1 . ILE A 203  ? 0.2787 0.3123 0.2468 -0.0053 -0.0113 0.0088  201  ILE A CD1 
1292  N N   . ARG A 204  ? 0.3433 0.4043 0.2993 -0.0027 -0.0120 0.0093  202  ARG A N   
1293  C CA  . ARG A 204  ? 0.3968 0.4664 0.3514 -0.0016 -0.0137 0.0062  202  ARG A CA  
1294  C C   . ARG A 204  ? 0.4207 0.4930 0.3759 -0.0005 -0.0145 0.0000  202  ARG A C   
1295  O O   . ARG A 204  ? 0.3911 0.4658 0.3479 0.0003  -0.0164 -0.0047 202  ARG A O   
1296  C CB  . ARG A 204  ? 0.4383 0.5155 0.3888 -0.0015 -0.0132 0.0102  202  ARG A CB  
1297  C CG  . ARG A 204  ? 0.5024 0.5833 0.4524 -0.0013 -0.0145 0.0124  202  ARG A CG  
1298  C CD  . ARG A 204  ? 0.5570 0.6390 0.5045 -0.0021 -0.0135 0.0192  202  ARG A CD  
1299  N NE  . ARG A 204  ? 0.5102 0.5893 0.4593 -0.0023 -0.0143 0.0223  202  ARG A NE  
1300  C CZ  . ARG A 204  ? 0.4883 0.5590 0.4401 -0.0031 -0.0136 0.0247  202  ARG A CZ  
1301  N NH1 . ARG A 204  ? 0.4179 0.4819 0.3709 -0.0038 -0.0121 0.0247  202  ARG A NH1 
1302  N NH2 . ARG A 204  ? 0.4751 0.5445 0.4285 -0.0030 -0.0146 0.0271  202  ARG A NH2 
1303  N N   . GLU A 205  ? 0.3887 0.4606 0.3427 -0.0004 -0.0131 -0.0003 203  GLU A N   
1304  C CA  . GLU A 205  ? 0.3870 0.4612 0.3416 0.0008  -0.0138 -0.0063 203  GLU A CA  
1305  C C   . GLU A 205  ? 0.3701 0.4368 0.3293 0.0008  -0.0150 -0.0101 203  GLU A C   
1306  O O   . GLU A 205  ? 0.4022 0.4712 0.3633 0.0019  -0.0170 -0.0158 203  GLU A O   
1307  C CB  . GLU A 205  ? 0.4416 0.5164 0.3943 0.0008  -0.0119 -0.0053 203  GLU A CB  
1308  C CG  . GLU A 205  ? 0.4698 0.5498 0.4225 0.0025  -0.0126 -0.0113 203  GLU A CG  
1309  C CD  . GLU A 205  ? 0.4922 0.5739 0.4429 0.0025  -0.0107 -0.0099 203  GLU A CD  
1310  O OE1 . GLU A 205  ? 0.4759 0.5500 0.4283 0.0018  -0.0097 -0.0087 203  GLU A OE1 
1311  O OE2 . GLU A 205  ? 0.6129 0.7039 0.5603 0.0031  -0.0101 -0.0099 203  GLU A OE2 
1312  N N   . ALA A 206  ? 0.3652 0.4231 0.3265 -0.0005 -0.0140 -0.0071 204  ALA A N   
1313  C CA  . ALA A 206  ? 0.3899 0.4405 0.3557 -0.0008 -0.0151 -0.0100 204  ALA A CA  
1314  C C   . ALA A 206  ? 0.3629 0.4146 0.3313 -0.0008 -0.0172 -0.0123 204  ALA A C   
1315  O O   . ALA A 206  ? 0.3285 0.3785 0.3003 -0.0004 -0.0190 -0.0171 204  ALA A O   
1316  C CB  . ALA A 206  ? 0.3925 0.4345 0.3594 -0.0022 -0.0134 -0.0057 204  ALA A CB  
1317  N N   . LEU A 207  ? 0.3241 0.3787 0.2912 -0.0012 -0.0172 -0.0091 205  LEU A N   
1318  C CA  . LEU A 207  ? 0.3512 0.4073 0.3208 -0.0012 -0.0193 -0.0112 205  LEU A CA  
1319  C C   . LEU A 207  ? 0.4056 0.4691 0.3750 0.0003  -0.0214 -0.0171 205  LEU A C   
1320  O O   . LEU A 207  ? 0.3785 0.4415 0.3515 0.0004  -0.0236 -0.0211 205  LEU A O   
1321  C CB  . LEU A 207  ? 0.3711 0.4295 0.3391 -0.0017 -0.0189 -0.0065 205  LEU A CB  
1322  C CG  . LEU A 207  ? 0.3297 0.3805 0.2994 -0.0031 -0.0174 -0.0018 205  LEU A CG  
1323  C CD1 . LEU A 207  ? 0.3380 0.3915 0.3057 -0.0033 -0.0169 0.0031  205  LEU A CD1 
1324  C CD2 . LEU A 207  ? 0.2909 0.3366 0.2657 -0.0040 -0.0185 -0.0039 205  LEU A CD2 
1325  N N   . LYS A 208  ? 0.3805 0.4513 0.3458 0.0015  -0.0209 -0.0176 206  LYS A N   
1326  C CA  . LYS A 208  ? 0.3973 0.4759 0.3622 0.0032  -0.0229 -0.0236 206  LYS A CA  
1327  C C   . LYS A 208  ? 0.3551 0.4298 0.3235 0.0039  -0.0241 -0.0294 206  LYS A C   
1328  O O   . LYS A 208  ? 0.4266 0.5041 0.3975 0.0049  -0.0266 -0.0352 206  LYS A O   
1329  C CB  . LYS A 208  ? 0.4319 0.5198 0.3914 0.0043  -0.0219 -0.0226 206  LYS A CB  
1330  N N   . ARG A 209  ? 0.4030 0.4712 0.3722 0.0034  -0.0226 -0.0280 207  ARG A N   
1331  C CA  . ARG A 209  ? 0.4048 0.4690 0.3775 0.0041  -0.0238 -0.0331 207  ARG A CA  
1332  C C   . ARG A 209  ? 0.4379 0.4936 0.4162 0.0029  -0.0252 -0.0342 207  ARG A C   
1333  O O   . ARG A 209  ? 0.4195 0.4721 0.4014 0.0036  -0.0270 -0.0390 207  ARG A O   
1334  C CB  . ARG A 209  ? 0.4163 0.4773 0.3874 0.0041  -0.0216 -0.0311 207  ARG A CB  
1335  C CG  . ARG A 209  ? 0.4592 0.5293 0.4256 0.0055  -0.0205 -0.0315 207  ARG A CG  
1336  C CD  . ARG A 209  ? 0.4693 0.5364 0.4342 0.0052  -0.0182 -0.0286 207  ARG A CD  
1337  N NE  . ARG A 209  ? 0.5988 0.6749 0.5600 0.0065  -0.0173 -0.0296 207  ARG A NE  
1338  C CZ  . ARG A 209  ? 0.6198 0.6954 0.5796 0.0065  -0.0155 -0.0280 207  ARG A CZ  
1339  N NH1 . ARG A 209  ? 0.5346 0.6013 0.4962 0.0054  -0.0144 -0.0255 207  ARG A NH1 
1340  N NH2 . ARG A 209  ? 0.6124 0.6973 0.5690 0.0077  -0.0147 -0.0291 207  ARG A NH2 
1341  N N   . SER A 210  ? 0.3969 0.4491 0.3762 0.0012  -0.0247 -0.0300 208  SER A N   
1342  C CA  . SER A 210  ? 0.3611 0.4061 0.3458 -0.0002 -0.0260 -0.0305 208  SER A CA  
1343  C C   . SER A 210  ? 0.4003 0.4485 0.3884 0.0002  -0.0290 -0.0354 208  SER A C   
1344  O O   . SER A 210  ? 0.3539 0.3965 0.3473 -0.0008 -0.0306 -0.0372 208  SER A O   
1345  C CB  . SER A 210  ? 0.3604 0.4012 0.3450 -0.0020 -0.0242 -0.0243 208  SER A CB  
1346  O OG  . SER A 210  ? 0.3550 0.3930 0.3365 -0.0023 -0.0215 -0.0198 208  SER A OG  
1347  N N   . LYS A 211  ? 0.3784 0.4357 0.3637 0.0015  -0.0300 -0.0375 209  LYS A N   
1348  C CA  . LYS A 211  ? 0.4197 0.4806 0.4080 0.0018  -0.0329 -0.0422 209  LYS A CA  
1349  C C   . LYS A 211  ? 0.4512 0.5089 0.4446 0.0024  -0.0355 -0.0487 209  LYS A C   
1350  O O   . LYS A 211  ? 0.4436 0.4990 0.4422 0.0016  -0.0379 -0.0513 209  LYS A O   
1351  C CB  . LYS A 211  ? 0.3896 0.4616 0.3735 0.0035  -0.0335 -0.0437 209  LYS A CB  
1352  N N   . GLU A 212  ? 0.4257 0.4831 0.4182 0.0038  -0.0353 -0.0513 210  GLU A N   
1353  C CA  . GLU A 212  ? 0.4987 0.5539 0.4960 0.0049  -0.0380 -0.0581 210  GLU A CA  
1354  C C   . GLU A 212  ? 0.4849 0.5296 0.4885 0.0028  -0.0390 -0.0572 210  GLU A C   
1355  O O   . GLU A 212  ? 0.4704 0.5134 0.4794 0.0024  -0.0419 -0.0611 210  GLU A O   
1356  C CB  . GLU A 212  ? 0.5132 0.5699 0.5081 0.0069  -0.0373 -0.0604 210  GLU A CB  
1357  C CG  . GLU A 212  ? 0.5441 0.5972 0.5444 0.0081  -0.0401 -0.0671 210  GLU A CG  
1358  C CD  . GLU A 212  ? 0.6371 0.6910 0.6355 0.0100  -0.0393 -0.0691 210  GLU A CD  
1359  O OE1 . GLU A 212  ? 0.6933 0.7496 0.6865 0.0100  -0.0362 -0.0646 210  GLU A OE1 
1360  O OE2 . GLU A 212  ? 0.7061 0.7584 0.7085 0.0116  -0.0418 -0.0752 210  GLU A OE2 
1361  N N   . LEU A 213  ? 0.4973 0.5349 0.5004 0.0015  -0.0366 -0.0519 211  LEU A N   
1362  C CA  . LEU A 213  ? 0.4548 0.4828 0.4636 -0.0005 -0.0373 -0.0506 211  LEU A CA  
1363  C C   . LEU A 213  ? 0.4350 0.4615 0.4463 -0.0028 -0.0373 -0.0473 211  LEU A C   
1364  O O   . LEU A 213  ? 0.4475 0.4680 0.4646 -0.0045 -0.0388 -0.0476 211  LEU A O   
1365  C CB  . LEU A 213  ? 0.4068 0.4284 0.4143 -0.0010 -0.0348 -0.0462 211  LEU A CB  
1366  C CG  . LEU A 213  ? 0.4426 0.4646 0.4490 0.0012  -0.0352 -0.0499 211  LEU A CG  
1367  C CD1 . LEU A 213  ? 0.4173 0.4330 0.4223 0.0006  -0.0328 -0.0453 211  LEU A CD1 
1368  C CD2 . LEU A 213  ? 0.4734 0.4932 0.4857 0.0022  -0.0388 -0.0566 211  LEU A CD2 
1369  N N   . GLU A 214  ? 0.4032 0.4351 0.4104 -0.0029 -0.0358 -0.0441 212  GLU A N   
1370  C CA  . GLU A 214  ? 0.4288 0.4606 0.4387 -0.0048 -0.0362 -0.0418 212  GLU A CA  
1371  C C   . GLU A 214  ? 0.4290 0.4635 0.4436 -0.0046 -0.0398 -0.0478 212  GLU A C   
1372  O O   . GLU A 214  ? 0.3962 0.4272 0.4162 -0.0065 -0.0411 -0.0474 212  GLU A O   
1373  C CB  . GLU A 214  ? 0.4144 0.4518 0.4190 -0.0046 -0.0342 -0.0375 212  GLU A CB  
1374  C CG  . GLU A 214  ? 0.3567 0.3900 0.3582 -0.0054 -0.0308 -0.0310 212  GLU A CG  
1375  C CD  . GLU A 214  ? 0.4102 0.4480 0.4075 -0.0054 -0.0291 -0.0266 212  GLU A CD  
1376  O OE1 . GLU A 214  ? 0.4149 0.4600 0.4106 -0.0044 -0.0304 -0.0284 212  GLU A OE1 
1377  O OE2 . GLU A 214  ? 0.4289 0.4631 0.4247 -0.0063 -0.0267 -0.0213 212  GLU A OE2 
1378  N N   . GLU A 215  ? 0.4722 0.5133 0.4851 -0.0023 -0.0416 -0.0534 213  GLU A N   
1379  C CA  . GLU A 215  ? 0.4705 0.5144 0.4881 -0.0019 -0.0454 -0.0598 213  GLU A CA  
1380  C C   . GLU A 215  ? 0.5055 0.5416 0.5302 -0.0027 -0.0477 -0.0633 213  GLU A C   
1381  O O   . GLU A 215  ? 0.5189 0.5550 0.5492 -0.0032 -0.0509 -0.0677 213  GLU A O   
1382  C CB  . GLU A 215  ? 0.4859 0.5394 0.4997 0.0010  -0.0466 -0.0652 213  GLU A CB  
1383  N N   . LYS A 216  ? 0.5689 0.5981 0.5937 -0.0029 -0.0463 -0.0612 214  LYS A N   
1384  C CA  . LYS A 216  ? 0.5369 0.5578 0.5684 -0.0039 -0.0484 -0.0633 214  LYS A CA  
1385  C C   . LYS A 216  ? 0.5565 0.5696 0.5916 -0.0071 -0.0471 -0.0572 214  LYS A C   
1386  O O   . LYS A 216  ? 0.5919 0.5976 0.6326 -0.0083 -0.0485 -0.0577 214  LYS A O   
1387  C CB  . LYS A 216  ? 0.4946 0.5129 0.5247 -0.0020 -0.0480 -0.0651 214  LYS A CB  
1388  N N   . GLY A 217  ? 0.4278 0.4426 0.4599 -0.0085 -0.0445 -0.0516 215  GLY A N   
1389  C CA  . GLY A 217  ? 0.4554 0.4643 0.4908 -0.0114 -0.0433 -0.0462 215  GLY A CA  
1390  C C   . GLY A 217  ? 0.4534 0.4581 0.4853 -0.0121 -0.0397 -0.0398 215  GLY A C   
1391  O O   . GLY A 217  ? 0.4833 0.4830 0.5180 -0.0145 -0.0386 -0.0354 215  GLY A O   
1392  N N   . PHE A 218  ? 0.4252 0.4320 0.4510 -0.0102 -0.0377 -0.0390 216  PHE A N   
1393  C CA  . PHE A 218  ? 0.4056 0.4092 0.4274 -0.0107 -0.0343 -0.0330 216  PHE A CA  
1394  C C   . PHE A 218  ? 0.3691 0.3774 0.3869 -0.0110 -0.0321 -0.0289 216  PHE A C   
1395  O O   . PHE A 218  ? 0.3805 0.3952 0.3973 -0.0103 -0.0330 -0.0308 216  PHE A O   
1396  C CB  . PHE A 218  ? 0.3618 0.3655 0.3793 -0.0086 -0.0333 -0.0339 216  PHE A CB  
1397  C CG  . PHE A 218  ? 0.4164 0.4146 0.4377 -0.0082 -0.0350 -0.0369 216  PHE A CG  
1398  C CD1 . PHE A 218  ? 0.4162 0.4158 0.4408 -0.0069 -0.0383 -0.0436 216  PHE A CD1 
1399  C CD2 . PHE A 218  ? 0.3566 0.3480 0.3780 -0.0090 -0.0336 -0.0333 216  PHE A CD2 
1400  C CE1 . PHE A 218  ? 0.4643 0.4585 0.4928 -0.0063 -0.0402 -0.0464 216  PHE A CE1 
1401  C CE2 . PHE A 218  ? 0.4353 0.4214 0.4603 -0.0085 -0.0354 -0.0358 216  PHE A CE2 
1402  C CZ  . PHE A 218  ? 0.4404 0.4277 0.4691 -0.0072 -0.0387 -0.0423 216  PHE A CZ  
1403  N N   . SER A 219  ? 0.3503 0.3553 0.3659 -0.0119 -0.0292 -0.0234 217  SER A N   
1404  C CA  . SER A 219  ? 0.3326 0.3412 0.3437 -0.0117 -0.0268 -0.0193 217  SER A CA  
1405  C C   . SER A 219  ? 0.3230 0.3299 0.3291 -0.0108 -0.0243 -0.0164 217  SER A C   
1406  O O   . SER A 219  ? 0.3099 0.3131 0.3162 -0.0104 -0.0244 -0.0176 217  SER A O   
1407  C CB  . SER A 219  ? 0.3584 0.3651 0.3723 -0.0138 -0.0259 -0.0154 217  SER A CB  
1408  O OG  . SER A 219  ? 0.3653 0.3655 0.3813 -0.0153 -0.0247 -0.0124 217  SER A OG  
1409  N N   . TYR A 220  ? 0.2999 0.3095 0.3019 -0.0105 -0.0222 -0.0126 218  TYR A N   
1410  C CA  . TYR A 220  ? 0.2780 0.2870 0.2751 -0.0096 -0.0199 -0.0101 218  TYR A CA  
1411  C C   . TYR A 220  ? 0.2982 0.3052 0.2939 -0.0106 -0.0175 -0.0047 218  TYR A C   
1412  O O   . TYR A 220  ? 0.3044 0.3130 0.3013 -0.0113 -0.0175 -0.0030 218  TYR A O   
1413  C CB  . TYR A 220  ? 0.3191 0.3350 0.3118 -0.0078 -0.0201 -0.0117 218  TYR A CB  
1414  C CG  . TYR A 220  ? 0.3422 0.3599 0.3351 -0.0065 -0.0217 -0.0167 218  TYR A CG  
1415  C CD1 . TYR A 220  ? 0.3234 0.3445 0.3190 -0.0059 -0.0244 -0.0218 218  TYR A CD1 
1416  C CD2 . TYR A 220  ? 0.2979 0.3139 0.2885 -0.0056 -0.0206 -0.0167 218  TYR A CD2 
1417  C CE1 . TYR A 220  ? 0.3463 0.3691 0.3422 -0.0044 -0.0260 -0.0269 218  TYR A CE1 
1418  C CE2 . TYR A 220  ? 0.3407 0.3585 0.3316 -0.0041 -0.0221 -0.0216 218  TYR A CE2 
1419  C CZ  . TYR A 220  ? 0.3456 0.3668 0.3392 -0.0034 -0.0248 -0.0267 218  TYR A CZ  
1420  O OH  . TYR A 220  ? 0.4014 0.4246 0.3954 -0.0017 -0.0263 -0.0320 218  TYR A OH  
1421  N N   . SER A 221  ? 0.3020 0.3055 0.2954 -0.0104 -0.0156 -0.0023 219  SER A N   
1422  C CA  . SER A 221  ? 0.3155 0.3176 0.3064 -0.0107 -0.0132 0.0024  219  SER A CA  
1423  C C   . SER A 221  ? 0.3427 0.3459 0.3291 -0.0096 -0.0120 0.0032  219  SER A C   
1424  O O   . SER A 221  ? 0.3676 0.3683 0.3537 -0.0092 -0.0119 0.0018  219  SER A O   
1425  C CB  . SER A 221  ? 0.3042 0.3004 0.2975 -0.0121 -0.0122 0.0048  219  SER A CB  
1426  O OG  . SER A 221  ? 0.3798 0.3750 0.3708 -0.0122 -0.0100 0.0088  219  SER A OG  
1427  N N   . TYR A 222  ? 0.3161 0.3229 0.2993 -0.0090 -0.0111 0.0054  220  TYR A N   
1428  C CA  . TYR A 222  ? 0.3308 0.3396 0.3099 -0.0081 -0.0101 0.0061  220  TYR A CA  
1429  C C   . TYR A 222  ? 0.3250 0.3298 0.3027 -0.0085 -0.0080 0.0100  220  TYR A C   
1430  O O   . TYR A 222  ? 0.2932 0.2965 0.2714 -0.0090 -0.0072 0.0129  220  TYR A O   
1431  C CB  . TYR A 222  ? 0.3023 0.3178 0.2790 -0.0073 -0.0106 0.0066  220  TYR A CB  
1432  C CG  . TYR A 222  ? 0.2788 0.2989 0.2567 -0.0067 -0.0128 0.0023  220  TYR A CG  
1433  C CD1 . TYR A 222  ? 0.2828 0.3054 0.2598 -0.0058 -0.0136 -0.0015 220  TYR A CD1 
1434  C CD2 . TYR A 222  ? 0.3012 0.3231 0.2815 -0.0071 -0.0141 0.0016  220  TYR A CD2 
1435  C CE1 . TYR A 222  ? 0.3283 0.3552 0.3066 -0.0050 -0.0157 -0.0060 220  TYR A CE1 
1436  C CE2 . TYR A 222  ? 0.2883 0.3144 0.2699 -0.0065 -0.0163 -0.0027 220  TYR A CE2 
1437  C CZ  . TYR A 222  ? 0.2887 0.3172 0.2693 -0.0055 -0.0171 -0.0066 220  TYR A CZ  
1438  O OH  . TYR A 222  ? 0.3070 0.3399 0.2891 -0.0047 -0.0195 -0.0113 220  TYR A OH  
1439  N N   . ASP A 223  ? 0.3350 0.3383 0.3108 -0.0081 -0.0073 0.0097  221  ASP A N   
1440  C CA  . ASP A 223  ? 0.3593 0.3590 0.3337 -0.0083 -0.0054 0.0128  221  ASP A CA  
1441  C C   . ASP A 223  ? 0.4023 0.4056 0.3732 -0.0078 -0.0047 0.0140  221  ASP A C   
1442  O O   . ASP A 223  ? 0.3751 0.3808 0.3447 -0.0071 -0.0050 0.0118  221  ASP A O   
1443  C CB  . ASP A 223  ? 0.4141 0.4090 0.3897 -0.0085 -0.0052 0.0116  221  ASP A CB  
1444  C CG  . ASP A 223  ? 0.4944 0.4860 0.4682 -0.0086 -0.0035 0.0144  221  ASP A CG  
1445  O OD1 . ASP A 223  ? 0.5026 0.4949 0.4748 -0.0087 -0.0024 0.0172  221  ASP A OD1 
1446  O OD2 . ASP A 223  ? 0.5229 0.5111 0.4972 -0.0086 -0.0033 0.0136  221  ASP A OD2 
1447  N N   . MET A 224  ? 0.3826 0.3862 0.3522 -0.0080 -0.0038 0.0175  222  MET A N   
1448  C CA  . MET A 224  ? 0.4380 0.4450 0.4047 -0.0078 -0.0032 0.0194  222  MET A CA  
1449  C C   . MET A 224  ? 0.4634 0.4673 0.4289 -0.0079 -0.0018 0.0206  222  MET A C   
1450  O O   . MET A 224  ? 0.5588 0.5647 0.5224 -0.0081 -0.0012 0.0228  222  MET A O   
1451  C CB  . MET A 224  ? 0.4111 0.4194 0.3774 -0.0079 -0.0031 0.0227  222  MET A CB  
1452  C CG  . MET A 224  ? 0.4204 0.4326 0.3877 -0.0076 -0.0045 0.0215  222  MET A CG  
1453  S SD  . MET A 224  ? 0.4859 0.5056 0.4513 -0.0069 -0.0058 0.0186  222  MET A SD  
1454  C CE  . MET A 224  ? 0.4244 0.4478 0.3864 -0.0070 -0.0049 0.0226  222  MET A CE  
1455  N N   . LEU A 225  ? 0.4874 0.4867 0.4543 -0.0081 -0.0015 0.0194  223  LEU A N   
1456  C CA  . LEU A 225  ? 0.4942 0.4910 0.4602 -0.0080 -0.0006 0.0195  223  LEU A CA  
1457  C C   . LEU A 225  ? 0.5049 0.4992 0.4700 -0.0085 0.0006  0.0229  223  LEU A C   
1458  O O   . LEU A 225  ? 0.5536 0.5464 0.5179 -0.0085 0.0014  0.0231  223  LEU A O   
1459  C CB  . LEU A 225  ? 0.4980 0.4993 0.4624 -0.0075 -0.0008 0.0176  223  LEU A CB  
1460  C CG  . LEU A 225  ? 0.4949 0.4974 0.4605 -0.0067 -0.0021 0.0133  223  LEU A CG  
1461  C CD1 . LEU A 225  ? 0.4676 0.4745 0.4317 -0.0059 -0.0022 0.0112  223  LEU A CD1 
1462  C CD2 . LEU A 225  ? 0.4580 0.4545 0.4260 -0.0068 -0.0024 0.0123  223  LEU A CD2 
1463  N N   . GLY A 226  ? 0.5194 0.5131 0.4850 -0.0087 0.0008  0.0253  224  GLY A N   
1464  C CA  . GLY A 226  ? 0.4485 0.4391 0.4138 -0.0090 0.0018  0.0280  224  GLY A CA  
1465  C C   . GLY A 226  ? 0.4572 0.4429 0.4237 -0.0090 0.0024  0.0276  224  GLY A C   
1466  O O   . GLY A 226  ? 0.4546 0.4389 0.4226 -0.0091 0.0021  0.0264  224  GLY A O   
1467  N N   . GLU A 227  ? 0.4594 0.4425 0.4252 -0.0091 0.0032  0.0286  225  GLU A N   
1468  C CA  . GLU A 227  ? 0.4040 0.3829 0.3705 -0.0091 0.0039  0.0288  225  GLU A CA  
1469  C C   . GLU A 227  ? 0.4052 0.3822 0.3708 -0.0091 0.0046  0.0301  225  GLU A C   
1470  O O   . GLU A 227  ? 0.4509 0.4295 0.4155 -0.0093 0.0046  0.0305  225  GLU A O   
1471  C CB  . GLU A 227  ? 0.4635 0.4406 0.4305 -0.0090 0.0037  0.0267  225  GLU A CB  
1472  C CG  . GLU A 227  ? 0.4907 0.4682 0.4566 -0.0088 0.0036  0.0254  225  GLU A CG  
1473  C CD  . GLU A 227  ? 0.5250 0.5007 0.4919 -0.0087 0.0031  0.0234  225  GLU A CD  
1474  O OE1 . GLU A 227  ? 0.5534 0.5257 0.5206 -0.0087 0.0035  0.0238  225  GLU A OE1 
1475  O OE2 . GLU A 227  ? 0.5321 0.5100 0.4995 -0.0084 0.0022  0.0213  225  GLU A OE2 
1476  N N   . ALA A 228  ? 0.3840 0.3579 0.3503 -0.0089 0.0051  0.0307  226  ALA A N   
1477  C CA  . ALA A 228  ? 0.3805 0.3521 0.3462 -0.0088 0.0056  0.0313  226  ALA A CA  
1478  C C   . ALA A 228  ? 0.3845 0.3572 0.3501 -0.0091 0.0054  0.0331  226  ALA A C   
1479  O O   . ALA A 228  ? 0.3772 0.3502 0.3420 -0.0095 0.0055  0.0333  226  ALA A O   
1480  C CB  . ALA A 228  ? 0.3800 0.3508 0.3448 -0.0088 0.0058  0.0300  226  ALA A CB  
1481  N N   . ALA A 229  ? 0.3350 0.3083 0.3015 -0.0089 0.0051  0.0344  227  ALA A N   
1482  C CA  . ALA A 229  ? 0.3333 0.3068 0.3002 -0.0092 0.0047  0.0365  227  ALA A CA  
1483  C C   . ALA A 229  ? 0.3200 0.2903 0.2874 -0.0092 0.0049  0.0368  227  ALA A C   
1484  O O   . ALA A 229  ? 0.3163 0.2841 0.2842 -0.0085 0.0053  0.0358  227  ALA A O   
1485  C CB  . ALA A 229  ? 0.3200 0.2941 0.2882 -0.0088 0.0041  0.0379  227  ALA A CB  
1486  N N   . THR A 230  ? 0.3215 0.2923 0.2888 -0.0099 0.0047  0.0381  228  THR A N   
1487  C CA  . THR A 230  ? 0.3801 0.3481 0.3482 -0.0101 0.0047  0.0383  228  THR A CA  
1488  C C   . THR A 230  ? 0.3260 0.2922 0.2960 -0.0101 0.0039  0.0404  228  THR A C   
1489  O O   . THR A 230  ? 0.2950 0.2581 0.2664 -0.0097 0.0036  0.0399  228  THR A O   
1490  C CB  . THR A 230  ? 0.3957 0.3654 0.3629 -0.0111 0.0048  0.0385  228  THR A CB  
1491  O OG1 . THR A 230  ? 0.4425 0.4138 0.4082 -0.0109 0.0054  0.0364  228  THR A OG1 
1492  C CG2 . THR A 230  ? 0.3962 0.3632 0.3644 -0.0114 0.0047  0.0384  228  THR A CG2 
1493  N N   . THR A 231  ? 0.2927 0.2609 0.2632 -0.0104 0.0032  0.0425  229  THR A N   
1494  C CA  . THR A 231  ? 0.2905 0.2570 0.2631 -0.0104 0.0022  0.0449  229  THR A CA  
1495  C C   . THR A 231  ? 0.2545 0.2222 0.2278 -0.0095 0.0016  0.0456  229  THR A C   
1496  O O   . THR A 231  ? 0.2683 0.2386 0.2402 -0.0092 0.0020  0.0447  229  THR A O   
1497  C CB  . THR A 231  ? 0.2874 0.2557 0.2601 -0.0119 0.0017  0.0477  229  THR A CB  
1498  O OG1 . THR A 231  ? 0.3104 0.2834 0.2813 -0.0124 0.0018  0.0488  229  THR A OG1 
1499  C CG2 . THR A 231  ? 0.2762 0.2443 0.2484 -0.0129 0.0023  0.0469  229  THR A CG2 
1500  N N   . ALA A 232  ? 0.2676 0.2331 0.2432 -0.0090 0.0005  0.0473  230  ALA A N   
1501  C CA  . ALA A 232  ? 0.3125 0.2794 0.2889 -0.0082 -0.0002 0.0485  230  ALA A CA  
1502  C C   . ALA A 232  ? 0.3370 0.3085 0.3117 -0.0092 -0.0005 0.0506  230  ALA A C   
1503  O O   . ALA A 232  ? 0.3159 0.2901 0.2900 -0.0086 -0.0006 0.0503  230  ALA A O   
1504  C CB  . ALA A 232  ? 0.3208 0.2845 0.3003 -0.0075 -0.0017 0.0503  230  ALA A CB  
1505  N N   . ALA A 233  ? 0.3339 0.3067 0.3078 -0.0106 -0.0005 0.0526  231  ALA A N   
1506  C CA  . ALA A 233  ? 0.3077 0.2856 0.2798 -0.0115 -0.0007 0.0546  231  ALA A CA  
1507  C C   . ALA A 233  ? 0.3402 0.3218 0.3098 -0.0113 0.0003  0.0518  231  ALA A C   
1508  O O   . ALA A 233  ? 0.3441 0.3298 0.3125 -0.0112 0.0000  0.0521  231  ALA A O   
1509  C CB  . ALA A 233  ? 0.3168 0.2959 0.2888 -0.0132 -0.0008 0.0575  231  ALA A CB  
1510  N N   . ASP A 234  ? 0.2831 0.2631 0.2521 -0.0113 0.0013  0.0490  232  ASP A N   
1511  C CA  . ASP A 234  ? 0.3456 0.3283 0.3127 -0.0111 0.0020  0.0462  232  ASP A CA  
1512  C C   . ASP A 234  ? 0.2901 0.2727 0.2577 -0.0100 0.0018  0.0447  232  ASP A C   
1513  O O   . ASP A 234  ? 0.3348 0.3209 0.3014 -0.0099 0.0017  0.0436  232  ASP A O   
1514  C CB  . ASP A 234  ? 0.3376 0.3182 0.3043 -0.0112 0.0030  0.0437  232  ASP A CB  
1515  C CG  . ASP A 234  ? 0.4340 0.4157 0.4000 -0.0123 0.0033  0.0446  232  ASP A CG  
1516  O OD1 . ASP A 234  ? 0.4220 0.4080 0.3871 -0.0131 0.0031  0.0464  232  ASP A OD1 
1517  O OD2 . ASP A 234  ? 0.4870 0.4658 0.4534 -0.0124 0.0038  0.0435  232  ASP A OD2 
1518  N N   . ALA A 235  ? 0.2714 0.2503 0.2409 -0.0092 0.0017  0.0444  233  ALA A N   
1519  C CA  . ALA A 235  ? 0.2800 0.2592 0.2504 -0.0083 0.0016  0.0431  233  ALA A CA  
1520  C C   . ALA A 235  ? 0.3058 0.2883 0.2765 -0.0081 0.0005  0.0449  233  ALA A C   
1521  O O   . ALA A 235  ? 0.2967 0.2817 0.2672 -0.0078 0.0003  0.0436  233  ALA A O   
1522  C CB  . ALA A 235  ? 0.2759 0.2512 0.2483 -0.0073 0.0018  0.0426  233  ALA A CB  
1523  N N   . GLU A 236  ? 0.2880 0.2704 0.2592 -0.0083 -0.0003 0.0479  234  GLU A N   
1524  C CA  . GLU A 236  ? 0.3353 0.3212 0.3066 -0.0080 -0.0015 0.0500  234  GLU A CA  
1525  C C   . GLU A 236  ? 0.3268 0.3180 0.2956 -0.0087 -0.0015 0.0497  234  GLU A C   
1526  O O   . GLU A 236  ? 0.3334 0.3283 0.3019 -0.0083 -0.0022 0.0495  234  GLU A O   
1527  C CB  . GLU A 236  ? 0.3907 0.3751 0.3633 -0.0082 -0.0025 0.0537  234  GLU A CB  
1528  N N   . ARG A 237  ? 0.2862 0.2784 0.2532 -0.0097 -0.0007 0.0495  235  ARG A N   
1529  C CA  . ARG A 237  ? 0.3549 0.3527 0.3196 -0.0102 -0.0006 0.0487  235  ARG A CA  
1530  C C   . ARG A 237  ? 0.3467 0.3456 0.3113 -0.0095 -0.0005 0.0449  235  ARG A C   
1531  O O   . ARG A 237  ? 0.3094 0.3128 0.2731 -0.0093 -0.0012 0.0441  235  ARG A O   
1532  C CB  . ARG A 237  ? 0.3524 0.3511 0.3157 -0.0112 0.0002  0.0488  235  ARG A CB  
1533  C CG  . ARG A 237  ? 0.3732 0.3778 0.3341 -0.0114 0.0005  0.0471  235  ARG A CG  
1534  C CD  . ARG A 237  ? 0.4526 0.4593 0.4124 -0.0125 0.0012  0.0483  235  ARG A CD  
1535  N NE  . ARG A 237  ? 0.5251 0.5272 0.4858 -0.0127 0.0021  0.0469  235  ARG A NE  
1536  C CZ  . ARG A 237  ? 0.6185 0.6207 0.5786 -0.0124 0.0027  0.0434  235  ARG A CZ  
1537  N NH1 . ARG A 237  ? 0.6531 0.6592 0.6120 -0.0118 0.0026  0.0407  235  ARG A NH1 
1538  N NH2 . ARG A 237  ? 0.5601 0.5582 0.5210 -0.0126 0.0034  0.0426  235  ARG A NH2 
1539  N N   . TYR A 238  ? 0.3064 0.3013 0.2719 -0.0093 0.0003  0.0425  236  TYR A N   
1540  C CA  . TYR A 238  ? 0.2899 0.2852 0.2557 -0.0089 0.0003  0.0393  236  TYR A CA  
1541  C C   . TYR A 238  ? 0.3176 0.3139 0.2851 -0.0083 -0.0006 0.0395  236  TYR A C   
1542  O O   . TYR A 238  ? 0.3456 0.3448 0.3131 -0.0081 -0.0012 0.0375  236  TYR A O   
1543  C CB  . TYR A 238  ? 0.3096 0.3003 0.2762 -0.0089 0.0012  0.0374  236  TYR A CB  
1544  C CG  . TYR A 238  ? 0.3073 0.2976 0.2726 -0.0094 0.0019  0.0366  236  TYR A CG  
1545  C CD1 . TYR A 238  ? 0.4104 0.4048 0.3740 -0.0096 0.0017  0.0355  236  TYR A CD1 
1546  C CD2 . TYR A 238  ? 0.3521 0.3381 0.3177 -0.0095 0.0027  0.0367  236  TYR A CD2 
1547  C CE1 . TYR A 238  ? 0.4469 0.4413 0.4095 -0.0099 0.0024  0.0346  236  TYR A CE1 
1548  C CE2 . TYR A 238  ? 0.4018 0.3876 0.3663 -0.0098 0.0033  0.0359  236  TYR A CE2 
1549  C CZ  . TYR A 238  ? 0.4576 0.4475 0.4207 -0.0101 0.0031  0.0349  236  TYR A CZ  
1550  O OH  . TYR A 238  ? 0.4824 0.4726 0.4447 -0.0103 0.0036  0.0340  236  TYR A OH  
1551  N N   . TYR A 239  ? 0.2710 0.2649 0.2400 -0.0078 -0.0008 0.0416  237  TYR A N   
1552  C CA  . TYR A 239  ? 0.2870 0.2822 0.2576 -0.0071 -0.0017 0.0419  237  TYR A CA  
1553  C C   . TYR A 239  ? 0.3561 0.3568 0.3256 -0.0071 -0.0029 0.0428  237  TYR A C   
1554  O O   . TYR A 239  ? 0.2873 0.2909 0.2574 -0.0068 -0.0036 0.0412  237  TYR A O   
1555  C CB  . TYR A 239  ? 0.3274 0.3195 0.3000 -0.0064 -0.0020 0.0440  237  TYR A CB  
1556  C CG  . TYR A 239  ? 0.3501 0.3441 0.3247 -0.0055 -0.0030 0.0442  237  TYR A CG  
1557  C CD1 . TYR A 239  ? 0.3519 0.3495 0.3263 -0.0052 -0.0044 0.0463  237  TYR A CD1 
1558  C CD2 . TYR A 239  ? 0.2935 0.2864 0.2703 -0.0050 -0.0026 0.0423  237  TYR A CD2 
1559  C CE1 . TYR A 239  ? 0.3506 0.3502 0.3269 -0.0043 -0.0054 0.0464  237  TYR A CE1 
1560  C CE2 . TYR A 239  ? 0.3353 0.3303 0.3142 -0.0042 -0.0035 0.0424  237  TYR A CE2 
1561  C CZ  . TYR A 239  ? 0.3670 0.3653 0.3457 -0.0038 -0.0049 0.0443  237  TYR A CZ  
1562  O OH  . TYR A 239  ? 0.3936 0.3944 0.3745 -0.0029 -0.0060 0.0443  237  TYR A OH  
1563  N N   . ARG A 240  ? 0.3102 0.3127 0.2780 -0.0075 -0.0032 0.0454  238  ARG A N   
1564  C CA  . ARG A 240  ? 0.3025 0.3107 0.2690 -0.0073 -0.0044 0.0466  238  ARG A CA  
1565  C C   . ARG A 240  ? 0.3310 0.3436 0.2957 -0.0076 -0.0044 0.0435  238  ARG A C   
1566  O O   . ARG A 240  ? 0.3092 0.3267 0.2734 -0.0072 -0.0055 0.0429  238  ARG A O   
1567  C CB  . ARG A 240  ? 0.3634 0.3729 0.3288 -0.0078 -0.0048 0.0508  238  ARG A CB  
1568  C CG  . ARG A 240  ? 0.3365 0.3465 0.3000 -0.0089 -0.0038 0.0513  238  ARG A CG  
1569  C CD  . ARG A 240  ? 0.3267 0.3386 0.2894 -0.0095 -0.0044 0.0561  238  ARG A CD  
1570  N NE  . ARG A 240  ? 0.3737 0.3856 0.3353 -0.0107 -0.0034 0.0570  238  ARG A NE  
1571  C CZ  . ARG A 240  ? 0.3960 0.4028 0.3592 -0.0113 -0.0029 0.0586  238  ARG A CZ  
1572  N NH1 . ARG A 240  ? 0.3464 0.3477 0.3122 -0.0107 -0.0035 0.0594  238  ARG A NH1 
1573  N NH2 . ARG A 240  ? 0.4769 0.4845 0.4390 -0.0125 -0.0020 0.0592  238  ARG A NH2 
1574  N N   . ASP A 241  ? 0.3297 0.3408 0.2937 -0.0080 -0.0033 0.0413  239  ASP A N   
1575  C CA  . ASP A 241  ? 0.3405 0.3550 0.3035 -0.0080 -0.0034 0.0377  239  ASP A CA  
1576  C C   . ASP A 241  ? 0.3116 0.3255 0.2767 -0.0076 -0.0041 0.0348  239  ASP A C   
1577  O O   . ASP A 241  ? 0.2992 0.3175 0.2640 -0.0073 -0.0051 0.0326  239  ASP A O   
1578  C CB  . ASP A 241  ? 0.3513 0.3635 0.3135 -0.0084 -0.0022 0.0360  239  ASP A CB  
1579  C CG  . ASP A 241  ? 0.4806 0.4946 0.4408 -0.0090 -0.0016 0.0383  239  ASP A CG  
1580  O OD1 . ASP A 241  ? 0.4488 0.4666 0.4079 -0.0092 -0.0021 0.0413  239  ASP A OD1 
1581  O OD2 . ASP A 241  ? 0.5373 0.5491 0.4973 -0.0094 -0.0006 0.0374  239  ASP A OD2 
1582  N N   . TYR A 242  ? 0.2718 0.2805 0.2391 -0.0076 -0.0035 0.0346  240  TYR A N   
1583  C CA  . TYR A 242  ? 0.2543 0.2624 0.2241 -0.0075 -0.0040 0.0324  240  TYR A CA  
1584  C C   . TYR A 242  ? 0.2477 0.2598 0.2183 -0.0069 -0.0054 0.0332  240  TYR A C   
1585  O O   . TYR A 242  ? 0.2599 0.2749 0.2315 -0.0069 -0.0064 0.0308  240  TYR A O   
1586  C CB  . TYR A 242  ? 0.2736 0.2764 0.2455 -0.0076 -0.0030 0.0329  240  TYR A CB  
1587  C CG  . TYR A 242  ? 0.2650 0.2640 0.2367 -0.0080 -0.0019 0.0314  240  TYR A CG  
1588  C CD1 . TYR A 242  ? 0.3089 0.3089 0.2799 -0.0083 -0.0021 0.0287  240  TYR A CD1 
1589  C CD2 . TYR A 242  ? 0.2742 0.2688 0.2466 -0.0081 -0.0008 0.0325  240  TYR A CD2 
1590  C CE1 . TYR A 242  ? 0.3557 0.3521 0.3267 -0.0087 -0.0013 0.0275  240  TYR A CE1 
1591  C CE2 . TYR A 242  ? 0.3140 0.3053 0.2861 -0.0084 0.0001  0.0313  240  TYR A CE2 
1592  C CZ  . TYR A 242  ? 0.2875 0.2796 0.2590 -0.0087 -0.0001 0.0290  240  TYR A CZ  
1593  O OH  . TYR A 242  ? 0.2961 0.2848 0.2674 -0.0090 0.0007  0.0281  240  TYR A OH  
1594  N N   . GLU A 243  ? 0.2676 0.2797 0.2380 -0.0065 -0.0056 0.0366  241  GLU A N   
1595  C CA  . GLU A 243  ? 0.2644 0.2801 0.2356 -0.0059 -0.0070 0.0377  241  GLU A CA  
1596  C C   . GLU A 243  ? 0.2967 0.3189 0.2659 -0.0058 -0.0082 0.0368  241  GLU A C   
1597  O O   . GLU A 243  ? 0.2540 0.2797 0.2243 -0.0054 -0.0095 0.0352  241  GLU A O   
1598  C CB  . GLU A 243  ? 0.2885 0.3027 0.2599 -0.0054 -0.0072 0.0418  241  GLU A CB  
1599  C CG  . GLU A 243  ? 0.2605 0.2782 0.2329 -0.0045 -0.0088 0.0435  241  GLU A CG  
1600  C CD  . GLU A 243  ? 0.3257 0.3416 0.2983 -0.0040 -0.0092 0.0478  241  GLU A CD  
1601  O OE1 . GLU A 243  ? 0.3706 0.3842 0.3417 -0.0046 -0.0085 0.0497  241  GLU A OE1 
1602  O OE2 . GLU A 243  ? 0.3513 0.3679 0.3258 -0.0030 -0.0104 0.0492  241  GLU A OE2 
1603  N N   . SER A 244  ? 0.2969 0.3212 0.2632 -0.0061 -0.0078 0.0375  242  SER A N   
1604  C CA  . SER A 244  ? 0.2717 0.3029 0.2355 -0.0058 -0.0089 0.0365  242  SER A CA  
1605  C C   . SER A 244  ? 0.2956 0.3283 0.2602 -0.0058 -0.0093 0.0315  242  SER A C   
1606  O O   . SER A 244  ? 0.2727 0.3108 0.2371 -0.0053 -0.0107 0.0295  242  SER A O   
1607  C CB  . SER A 244  ? 0.3034 0.3370 0.2641 -0.0063 -0.0081 0.0386  242  SER A CB  
1608  O OG  . SER A 244  ? 0.3698 0.4001 0.3302 -0.0068 -0.0068 0.0369  242  SER A OG  
1609  N N   . ALA A 245  ? 0.2615 0.2897 0.2272 -0.0063 -0.0083 0.0293  243  ALA A N   
1610  C CA  . ALA A 245  ? 0.2979 0.3265 0.2649 -0.0063 -0.0089 0.0247  243  ALA A CA  
1611  C C   . ALA A 245  ? 0.2511 0.2795 0.2214 -0.0063 -0.0100 0.0233  243  ALA A C   
1612  O O   . ALA A 245  ? 0.2751 0.3070 0.2464 -0.0061 -0.0114 0.0200  243  ALA A O   
1613  C CB  . ALA A 245  ? 0.2622 0.2853 0.2300 -0.0068 -0.0076 0.0233  243  ALA A CB  
1614  N N   . ILE A 246  ? 0.2501 0.2748 0.2224 -0.0064 -0.0095 0.0257  244  ILE A N   
1615  C CA  . ILE A 246  ? 0.2498 0.2749 0.2255 -0.0065 -0.0105 0.0246  244  ILE A CA  
1616  C C   . ILE A 246  ? 0.2817 0.3133 0.2569 -0.0058 -0.0123 0.0243  244  ILE A C   
1617  O O   . ILE A 246  ? 0.2522 0.2863 0.2294 -0.0059 -0.0137 0.0213  244  ILE A O   
1618  C CB  . ILE A 246  ? 0.2506 0.2715 0.2284 -0.0065 -0.0095 0.0272  244  ILE A CB  
1619  C CG1 . ILE A 246  ? 0.2520 0.2671 0.2307 -0.0073 -0.0079 0.0267  244  ILE A CG1 
1620  C CG2 . ILE A 246  ? 0.2878 0.3105 0.2691 -0.0065 -0.0106 0.0263  244  ILE A CG2 
1621  C CD1 . ILE A 246  ? 0.2741 0.2856 0.2549 -0.0072 -0.0069 0.0287  244  ILE A CD1 
1622  N N   . HIS A 247  ? 0.2531 0.2877 0.2255 -0.0051 -0.0125 0.0274  245  HIS A N   
1623  C CA  . HIS A 247  ? 0.2605 0.3019 0.2319 -0.0044 -0.0144 0.0274  245  HIS A CA  
1624  C C   . HIS A 247  ? 0.2682 0.3145 0.2382 -0.0043 -0.0153 0.0234  245  HIS A C   
1625  O O   . HIS A 247  ? 0.3115 0.3622 0.2827 -0.0039 -0.0171 0.0208  245  HIS A O   
1626  C CB  . HIS A 247  ? 0.2570 0.3005 0.2256 -0.0039 -0.0144 0.0320  245  HIS A CB  
1627  C CG  . HIS A 247  ? 0.2804 0.3207 0.2510 -0.0035 -0.0143 0.0356  245  HIS A CG  
1628  N ND1 . HIS A 247  ? 0.2671 0.3094 0.2400 -0.0029 -0.0157 0.0358  245  HIS A ND1 
1629  C CD2 . HIS A 247  ? 0.2563 0.2918 0.2270 -0.0036 -0.0131 0.0390  245  HIS A CD2 
1630  C CE1 . HIS A 247  ? 0.3137 0.3526 0.2882 -0.0024 -0.0154 0.0390  245  HIS A CE1 
1631  N NE2 . HIS A 247  ? 0.2778 0.3123 0.2509 -0.0029 -0.0139 0.0410  245  HIS A NE2 
1632  N N   . ALA A 248  ? 0.2564 0.3023 0.2241 -0.0045 -0.0144 0.0225  246  ALA A N   
1633  C CA  . ALA A 248  ? 0.2958 0.3467 0.2621 -0.0041 -0.0153 0.0183  246  ALA A CA  
1634  C C   . ALA A 248  ? 0.2812 0.3302 0.2512 -0.0044 -0.0163 0.0135  246  ALA A C   
1635  O O   . ALA A 248  ? 0.2885 0.3424 0.2590 -0.0038 -0.0181 0.0099  246  ALA A O   
1636  C CB  . ALA A 248  ? 0.2972 0.3475 0.2608 -0.0042 -0.0138 0.0183  246  ALA A CB  
1637  N N   . ILE A 249  ? 0.2551 0.2970 0.2279 -0.0052 -0.0152 0.0135  247  ILE A N   
1638  C CA  . ILE A 249  ? 0.2548 0.2943 0.2316 -0.0058 -0.0161 0.0096  247  ILE A CA  
1639  C C   . ILE A 249  ? 0.2994 0.3411 0.2792 -0.0059 -0.0177 0.0091  247  ILE A C   
1640  O O   . ILE A 249  ? 0.3013 0.3454 0.2833 -0.0060 -0.0195 0.0052  247  ILE A O   
1641  C CB  . ILE A 249  ? 0.2649 0.2966 0.2435 -0.0068 -0.0145 0.0106  247  ILE A CB  
1642  C CG1 . ILE A 249  ? 0.2774 0.3075 0.2533 -0.0066 -0.0133 0.0102  247  ILE A CG1 
1643  C CG2 . ILE A 249  ? 0.2664 0.2952 0.2497 -0.0077 -0.0154 0.0076  247  ILE A CG2 
1644  C CD1 . ILE A 249  ? 0.2505 0.2737 0.2271 -0.0073 -0.0114 0.0124  247  ILE A CD1 
1645  N N   . GLY A 250  ? 0.2758 0.3169 0.2558 -0.0059 -0.0171 0.0130  248  GLY A N   
1646  C CA  . GLY A 250  ? 0.2801 0.3237 0.2631 -0.0059 -0.0186 0.0127  248  GLY A CA  
1647  C C   . GLY A 250  ? 0.2953 0.3466 0.2769 -0.0049 -0.0207 0.0108  248  GLY A C   
1648  O O   . GLY A 250  ? 0.2660 0.3200 0.2507 -0.0051 -0.0225 0.0083  248  GLY A O   
1649  N N   . LYS A 251  ? 0.3254 0.3809 0.3025 -0.0040 -0.0207 0.0121  249  LYS A N   
1650  C CA  . LYS A 251  ? 0.2837 0.3474 0.2588 -0.0030 -0.0227 0.0102  249  LYS A CA  
1651  C C   . LYS A 251  ? 0.3057 0.3714 0.2819 -0.0030 -0.0241 0.0043  249  LYS A C   
1652  O O   . LYS A 251  ? 0.3205 0.3914 0.2981 -0.0025 -0.0263 0.0011  249  LYS A O   
1653  C CB  . LYS A 251  ? 0.2902 0.3580 0.2600 -0.0022 -0.0220 0.0133  249  LYS A CB  
1654  C CG  . LYS A 251  ? 0.3008 0.3682 0.2693 -0.0019 -0.0215 0.0191  249  LYS A CG  
1655  C CD  . LYS A 251  ? 0.3522 0.4245 0.3157 -0.0014 -0.0211 0.0218  249  LYS A CD  
1656  C CE  . LYS A 251  ? 0.3630 0.4313 0.3254 -0.0017 -0.0196 0.0277  249  LYS A CE  
1657  N NZ  . LYS A 251  ? 0.3874 0.4601 0.3453 -0.0016 -0.0190 0.0302  249  LYS A NZ  
1658  N N   . ALA A 252  ? 0.2916 0.3536 0.2675 -0.0033 -0.0229 0.0025  250  ALA A N   
1659  C CA  . ALA A 252  ? 0.2632 0.3262 0.2408 -0.0032 -0.0243 -0.0033 250  ALA A CA  
1660  C C   . ALA A 252  ? 0.2757 0.3349 0.2590 -0.0043 -0.0255 -0.0060 250  ALA A C   
1661  O O   . ALA A 252  ? 0.3237 0.3858 0.3094 -0.0041 -0.0278 -0.0108 250  ALA A O   
1662  C CB  . ALA A 252  ? 0.2640 0.3234 0.2401 -0.0032 -0.0228 -0.0041 250  ALA A CB  
1663  N N   . SER A 253  ? 0.2604 0.3133 0.2464 -0.0055 -0.0241 -0.0029 251  SER A N   
1664  C CA  . SER A 253  ? 0.2922 0.3418 0.2838 -0.0068 -0.0251 -0.0047 251  SER A CA  
1665  C C   . SER A 253  ? 0.3083 0.3637 0.3022 -0.0066 -0.0275 -0.0067 251  SER A C   
1666  O O   . SER A 253  ? 0.3313 0.3868 0.3294 -0.0072 -0.0293 -0.0108 251  SER A O   
1667  C CB  . SER A 253  ? 0.2843 0.3280 0.2778 -0.0079 -0.0231 -0.0005 251  SER A CB  
1668  O OG  . SER A 253  ? 0.2912 0.3325 0.2902 -0.0094 -0.0239 -0.0021 251  SER A OG  
1669  N N   . ALA A 254  ? 0.2772 0.3373 0.2684 -0.0056 -0.0276 -0.0039 252  ALA A N   
1670  C CA  . ALA A 254  ? 0.3033 0.3700 0.2958 -0.0050 -0.0299 -0.0055 252  ALA A CA  
1671  C C   . ALA A 254  ? 0.3243 0.3888 0.3231 -0.0065 -0.0310 -0.0070 252  ALA A C   
1672  O O   . ALA A 254  ? 0.3157 0.3839 0.3174 -0.0066 -0.0334 -0.0111 252  ALA A O   
1673  C CB  . ALA A 254  ? 0.2843 0.3575 0.2748 -0.0039 -0.0320 -0.0102 252  ALA A CB  
1674  N N   . GLY A 255  ? 0.2954 0.3543 0.2965 -0.0076 -0.0291 -0.0037 253  GLY A N   
1675  C CA  . GLY A 255  ? 0.2996 0.3571 0.3067 -0.0090 -0.0297 -0.0042 253  GLY A CA  
1676  C C   . GLY A 255  ? 0.3518 0.4053 0.3636 -0.0108 -0.0304 -0.0077 253  GLY A C   
1677  O O   . GLY A 255  ? 0.3430 0.3968 0.3602 -0.0121 -0.0315 -0.0089 253  GLY A O   
1678  N N   . ARG A 256  ? 0.3251 0.3749 0.3353 -0.0108 -0.0297 -0.0091 254  ARG A N   
1679  C CA  . ARG A 256  ? 0.3153 0.3606 0.3303 -0.0125 -0.0305 -0.0121 254  ARG A CA  
1680  C C   . ARG A 256  ? 0.3486 0.3877 0.3668 -0.0144 -0.0285 -0.0088 254  ARG A C   
1681  O O   . ARG A 256  ? 0.3274 0.3631 0.3506 -0.0161 -0.0293 -0.0105 254  ARG A O   
1682  C CB  . ARG A 256  ? 0.2983 0.3414 0.3108 -0.0118 -0.0306 -0.0148 254  ARG A CB  
1683  C CG  . ARG A 256  ? 0.3336 0.3822 0.3455 -0.0105 -0.0334 -0.0202 254  ARG A CG  
1684  C CD  . ARG A 256  ? 0.3629 0.4099 0.3721 -0.0095 -0.0333 -0.0227 254  ARG A CD  
1685  N NE  . ARG A 256  ? 0.3576 0.4072 0.3602 -0.0079 -0.0314 -0.0199 254  ARG A NE  
1686  C CZ  . ARG A 256  ? 0.3855 0.4341 0.3849 -0.0069 -0.0306 -0.0209 254  ARG A CZ  
1687  N NH1 . ARG A 256  ? 0.4138 0.4584 0.4158 -0.0072 -0.0314 -0.0244 254  ARG A NH1 
1688  N NH2 . ARG A 256  ? 0.3767 0.4285 0.3703 -0.0057 -0.0290 -0.0182 254  ARG A NH2 
1689  N N   . GLY A 257  ? 0.2764 0.3142 0.2921 -0.0140 -0.0261 -0.0041 255  GLY A N   
1690  C CA  . GLY A 257  ? 0.2858 0.3189 0.3044 -0.0156 -0.0241 -0.0010 255  GLY A CA  
1691  C C   . GLY A 257  ? 0.2970 0.3240 0.3139 -0.0160 -0.0224 0.0000  255  GLY A C   
1692  O O   . GLY A 257  ? 0.3141 0.3401 0.3279 -0.0151 -0.0228 -0.0019 255  GLY A O   
1693  N N   . ILE A 258  ? 0.2906 0.3135 0.3095 -0.0174 -0.0205 0.0029  256  ILE A N   
1694  C CA  . ILE A 258  ? 0.2982 0.3157 0.3149 -0.0175 -0.0185 0.0048  256  ILE A CA  
1695  C C   . ILE A 258  ? 0.2991 0.3124 0.3183 -0.0187 -0.0195 0.0024  256  ILE A C   
1696  O O   . ILE A 258  ? 0.2916 0.3007 0.3084 -0.0185 -0.0184 0.0032  256  ILE A O   
1697  C CB  . ILE A 258  ? 0.2937 0.3092 0.3114 -0.0183 -0.0161 0.0088  256  ILE A CB  
1698  C CG1 . ILE A 258  ? 0.3100 0.3252 0.3339 -0.0206 -0.0166 0.0088  256  ILE A CG1 
1699  C CG2 . ILE A 258  ? 0.2786 0.2976 0.2937 -0.0168 -0.0152 0.0112  256  ILE A CG2 
1700  C CD1 . ILE A 258  ? 0.3499 0.3647 0.3750 -0.0213 -0.0143 0.0124  256  ILE A CD1 
1701  N N   . TYR A 259  ? 0.3219 0.3360 0.3462 -0.0200 -0.0218 -0.0004 257  TYR A N   
1702  C CA  . TYR A 259  ? 0.2847 0.2943 0.3122 -0.0213 -0.0231 -0.0027 257  TYR A CA  
1703  C C   . TYR A 259  ? 0.3300 0.3410 0.3563 -0.0198 -0.0254 -0.0075 257  TYR A C   
1704  O O   . TYR A 259  ? 0.3539 0.3613 0.3788 -0.0193 -0.0254 -0.0086 257  TYR A O   
1705  C CB  . TYR A 259  ? 0.3121 0.3212 0.3467 -0.0238 -0.0243 -0.0029 257  TYR A CB  
1706  C CG  . TYR A 259  ? 0.2720 0.2805 0.3081 -0.0253 -0.0220 0.0017  257  TYR A CG  
1707  C CD1 . TYR A 259  ? 0.2963 0.3008 0.3299 -0.0254 -0.0194 0.0052  257  TYR A CD1 
1708  C CD2 . TYR A 259  ? 0.3141 0.3268 0.3539 -0.0263 -0.0223 0.0023  257  TYR A CD2 
1709  C CE1 . TYR A 259  ? 0.2835 0.2882 0.3182 -0.0265 -0.0172 0.0091  257  TYR A CE1 
1710  C CE2 . TYR A 259  ? 0.3079 0.3208 0.3491 -0.0274 -0.0200 0.0063  257  TYR A CE2 
1711  C CZ  . TYR A 259  ? 0.2965 0.3055 0.3351 -0.0275 -0.0174 0.0096  257  TYR A CZ  
1712  O OH  . TYR A 259  ? 0.3257 0.3357 0.3655 -0.0284 -0.0152 0.0133  257  TYR A OH  
1713  N N   . GLU A 260  ? 0.3585 0.3752 0.3852 -0.0190 -0.0274 -0.0104 258  GLU A N   
1714  C CA  . GLU A 260  ? 0.3913 0.4105 0.4166 -0.0174 -0.0296 -0.0153 258  GLU A CA  
1715  C C   . GLU A 260  ? 0.3656 0.3881 0.3839 -0.0150 -0.0284 -0.0148 258  GLU A C   
1716  O O   . GLU A 260  ? 0.4689 0.4927 0.4852 -0.0136 -0.0295 -0.0183 258  GLU A O   
1717  C CB  . GLU A 260  ? 0.3993 0.4237 0.4283 -0.0176 -0.0325 -0.0191 258  GLU A CB  
1718  C CG  . GLU A 260  ? 0.4789 0.5014 0.5151 -0.0203 -0.0335 -0.0187 258  GLU A CG  
1719  C CD  . GLU A 260  ? 0.5878 0.6100 0.6296 -0.0211 -0.0370 -0.0241 258  GLU A CD  
1720  O OE1 . GLU A 260  ? 0.6025 0.6232 0.6434 -0.0199 -0.0384 -0.0278 258  GLU A OE1 
1721  O OE2 . GLU A 260  ? 0.6224 0.6461 0.6698 -0.0228 -0.0386 -0.0248 258  GLU A OE2 
1722  N N   . GLY A 261  ? 0.3331 0.3571 0.3478 -0.0146 -0.0262 -0.0105 259  GLY A N   
1723  C CA  . GLY A 261  ? 0.3134 0.3406 0.3219 -0.0126 -0.0251 -0.0094 259  GLY A CA  
1724  C C   . GLY A 261  ? 0.3290 0.3515 0.3343 -0.0124 -0.0226 -0.0065 259  GLY A C   
1725  O O   . GLY A 261  ? 0.3207 0.3375 0.3281 -0.0137 -0.0215 -0.0048 259  GLY A O   
1726  N N   . PRO A 262  ? 0.3125 0.3375 0.3125 -0.0108 -0.0218 -0.0058 260  PRO A N   
1727  C CA  . PRO A 262  ? 0.2963 0.3172 0.2930 -0.0106 -0.0196 -0.0034 260  PRO A CA  
1728  C C   . PRO A 262  ? 0.2647 0.2834 0.2603 -0.0110 -0.0173 0.0017  260  PRO A C   
1729  O O   . PRO A 262  ? 0.2834 0.3048 0.2795 -0.0110 -0.0173 0.0035  260  PRO A O   
1730  C CB  . PRO A 262  ? 0.2980 0.3238 0.2900 -0.0088 -0.0197 -0.0046 260  PRO A CB  
1731  C CG  . PRO A 262  ? 0.2884 0.3210 0.2798 -0.0082 -0.0211 -0.0051 260  PRO A CG  
1732  C CD  . PRO A 262  ? 0.3460 0.3783 0.3428 -0.0093 -0.0229 -0.0074 260  PRO A CD  
1733  N N   . GLY A 263  ? 0.2522 0.2659 0.2466 -0.0113 -0.0154 0.0037  261  GLY A N   
1734  C CA  . GLY A 263  ? 0.2739 0.2853 0.2669 -0.0115 -0.0132 0.0080  261  GLY A CA  
1735  C C   . GLY A 263  ? 0.2725 0.2821 0.2613 -0.0107 -0.0116 0.0096  261  GLY A C   
1736  O O   . GLY A 263  ? 0.2598 0.2709 0.2464 -0.0099 -0.0121 0.0076  261  GLY A O   
1737  N N   . ILE A 264  ? 0.2475 0.2543 0.2354 -0.0109 -0.0098 0.0131  262  ILE A N   
1738  C CA  . ILE A 264  ? 0.3131 0.3180 0.2975 -0.0103 -0.0082 0.0150  262  ILE A CA  
1739  C C   . ILE A 264  ? 0.2828 0.2822 0.2682 -0.0110 -0.0067 0.0166  262  ILE A C   
1740  O O   . ILE A 264  ? 0.2543 0.2522 0.2425 -0.0119 -0.0064 0.0175  262  ILE A O   
1741  C CB  . ILE A 264  ? 0.2586 0.2661 0.2404 -0.0095 -0.0076 0.0179  262  ILE A CB  
1742  C CG1 . ILE A 264  ? 0.2518 0.2583 0.2300 -0.0090 -0.0064 0.0194  262  ILE A CG1 
1743  C CG2 . ILE A 264  ? 0.2452 0.2511 0.2288 -0.0097 -0.0068 0.0206  262  ILE A CG2 
1744  C CD1 . ILE A 264  ? 0.2805 0.2896 0.2562 -0.0083 -0.0062 0.0224  262  ILE A CD1 
1745  N N   . SER A 265  ? 0.2755 0.2724 0.2585 -0.0107 -0.0058 0.0169  263  SER A N   
1746  C CA  . SER A 265  ? 0.3054 0.2975 0.2885 -0.0112 -0.0043 0.0186  263  SER A CA  
1747  C C   . SER A 265  ? 0.2593 0.2509 0.2392 -0.0105 -0.0029 0.0210  263  SER A C   
1748  O O   . SER A 265  ? 0.3006 0.2943 0.2780 -0.0098 -0.0030 0.0207  263  SER A O   
1749  C CB  . SER A 265  ? 0.3002 0.2894 0.2839 -0.0114 -0.0047 0.0166  263  SER A CB  
1750  O OG  . SER A 265  ? 0.3843 0.3726 0.3717 -0.0124 -0.0059 0.0149  263  SER A OG  
1751  N N   . ILE A 266  ? 0.2647 0.2539 0.2449 -0.0106 -0.0015 0.0233  264  ILE A N   
1752  C CA  . ILE A 266  ? 0.2654 0.2537 0.2432 -0.0100 -0.0004 0.0254  264  ILE A CA  
1753  C C   . ILE A 266  ? 0.2914 0.2755 0.2690 -0.0103 0.0009  0.0262  264  ILE A C   
1754  O O   . ILE A 266  ? 0.2655 0.2479 0.2451 -0.0109 0.0011  0.0259  264  ILE A O   
1755  C CB  . ILE A 266  ? 0.2715 0.2614 0.2498 -0.0096 -0.0003 0.0274  264  ILE A CB  
1756  C CG1 . ILE A 266  ? 0.2933 0.2821 0.2743 -0.0099 0.0003  0.0280  264  ILE A CG1 
1757  C CG2 . ILE A 266  ? 0.2994 0.2938 0.2777 -0.0093 -0.0017 0.0269  264  ILE A CG2 
1758  C CD1 . ILE A 266  ? 0.3503 0.3399 0.3319 -0.0091 0.0006  0.0299  264  ILE A CD1 
1759  N N   . LYS A 267  ? 0.2841 0.2669 0.2594 -0.0098 0.0016  0.0272  265  LYS A N   
1760  C CA  . LYS A 267  ? 0.2424 0.2217 0.2171 -0.0098 0.0028  0.0280  265  LYS A CA  
1761  C C   . LYS A 267  ? 0.2623 0.2413 0.2368 -0.0092 0.0036  0.0299  265  LYS A C   
1762  O O   . LYS A 267  ? 0.2592 0.2393 0.2326 -0.0088 0.0033  0.0308  265  LYS A O   
1763  C CB  . LYS A 267  ? 0.3234 0.3014 0.2962 -0.0097 0.0029  0.0272  265  LYS A CB  
1764  C CG  . LYS A 267  ? 0.3601 0.3377 0.3337 -0.0100 0.0021  0.0251  265  LYS A CG  
1765  C CD  . LYS A 267  ? 0.4043 0.3806 0.3762 -0.0097 0.0023  0.0243  265  LYS A CD  
1766  C CE  . LYS A 267  ? 0.4576 0.4327 0.4307 -0.0099 0.0013  0.0222  265  LYS A CE  
1767  N NZ  . LYS A 267  ? 0.4418 0.4199 0.4164 -0.0099 0.0000  0.0202  265  LYS A NZ  
1768  N N   . LEU A 268  ? 0.2396 0.2170 0.2152 -0.0092 0.0045  0.0305  266  LEU A N   
1769  C CA  . LEU A 268  ? 0.2396 0.2167 0.2153 -0.0084 0.0050  0.0319  266  LEU A CA  
1770  C C   . LEU A 268  ? 0.2635 0.2386 0.2372 -0.0080 0.0053  0.0324  266  LEU A C   
1771  O O   . LEU A 268  ? 0.2466 0.2217 0.2203 -0.0073 0.0052  0.0335  266  LEU A O   
1772  C CB  . LEU A 268  ? 0.2395 0.2160 0.2167 -0.0083 0.0060  0.0320  266  LEU A CB  
1773  C CG  . LEU A 268  ? 0.2739 0.2527 0.2536 -0.0089 0.0058  0.0318  266  LEU A CG  
1774  C CD1 . LEU A 268  ? 0.2854 0.2642 0.2664 -0.0090 0.0070  0.0323  266  LEU A CD1 
1775  C CD2 . LEU A 268  ? 0.2418 0.2232 0.2227 -0.0083 0.0050  0.0322  266  LEU A CD2 
1776  N N   . SER A 269  ? 0.2557 0.2292 0.2280 -0.0083 0.0057  0.0317  267  SER A N   
1777  C CA  . SER A 269  ? 0.2941 0.2660 0.2647 -0.0080 0.0059  0.0321  267  SER A CA  
1778  C C   . SER A 269  ? 0.2877 0.2613 0.2576 -0.0081 0.0051  0.0328  267  SER A C   
1779  O O   . SER A 269  ? 0.2932 0.2658 0.2624 -0.0080 0.0052  0.0337  267  SER A O   
1780  C CB  . SER A 269  ? 0.2735 0.2438 0.2429 -0.0083 0.0062  0.0311  267  SER A CB  
1781  O OG  . SER A 269  ? 0.2911 0.2627 0.2600 -0.0087 0.0055  0.0301  267  SER A OG  
1782  N N   . ALA A 270  ? 0.2743 0.2507 0.2444 -0.0084 0.0044  0.0325  268  ALA A N   
1783  C CA  . ALA A 270  ? 0.2797 0.2586 0.2489 -0.0085 0.0037  0.0335  268  ALA A CA  
1784  C C   . ALA A 270  ? 0.2763 0.2554 0.2465 -0.0080 0.0033  0.0356  268  ALA A C   
1785  O O   . ALA A 270  ? 0.2660 0.2462 0.2356 -0.0082 0.0029  0.0372  268  ALA A O   
1786  C CB  . ALA A 270  ? 0.2664 0.2488 0.2354 -0.0087 0.0029  0.0324  268  ALA A CB  
1787  N N   . LEU A 271  ? 0.2561 0.2342 0.2281 -0.0075 0.0035  0.0356  269  LEU A N   
1788  C CA  . LEU A 271  ? 0.2825 0.2613 0.2559 -0.0068 0.0029  0.0371  269  LEU A CA  
1789  C C   . LEU A 271  ? 0.2736 0.2493 0.2479 -0.0061 0.0031  0.0380  269  LEU A C   
1790  O O   . LEU A 271  ? 0.2756 0.2514 0.2514 -0.0054 0.0024  0.0392  269  LEU A O   
1791  C CB  . LEU A 271  ? 0.2439 0.2245 0.2191 -0.0065 0.0026  0.0364  269  LEU A CB  
1792  C CG  . LEU A 271  ? 0.3189 0.3028 0.2937 -0.0071 0.0019  0.0356  269  LEU A CG  
1793  C CD1 . LEU A 271  ? 0.3044 0.2900 0.2815 -0.0070 0.0016  0.0348  269  LEU A CD1 
1794  C CD2 . LEU A 271  ? 0.3061 0.2927 0.2797 -0.0071 0.0008  0.0372  269  LEU A CD2 
1795  N N   . HIS A 272  ? 0.2427 0.2158 0.2163 -0.0062 0.0040  0.0371  270  HIS A N   
1796  C CA  . HIS A 272  ? 0.2630 0.2335 0.2375 -0.0054 0.0040  0.0374  270  HIS A CA  
1797  C C   . HIS A 272  ? 0.2461 0.2145 0.2190 -0.0059 0.0046  0.0368  270  HIS A C   
1798  O O   . HIS A 272  ? 0.2769 0.2454 0.2487 -0.0063 0.0053  0.0355  270  HIS A O   
1799  C CB  . HIS A 272  ? 0.2776 0.2476 0.2537 -0.0043 0.0045  0.0364  270  HIS A CB  
1800  C CG  . HIS A 272  ? 0.3278 0.2958 0.3055 -0.0032 0.0041  0.0366  270  HIS A CG  
1801  N ND1 . HIS A 272  ? 0.3409 0.3062 0.3181 -0.0030 0.0044  0.0358  270  HIS A ND1 
1802  C CD2 . HIS A 272  ? 0.3334 0.3014 0.3134 -0.0020 0.0033  0.0373  270  HIS A CD2 
1803  C CE1 . HIS A 272  ? 0.3409 0.3047 0.3202 -0.0018 0.0037  0.0358  270  HIS A CE1 
1804  N NE2 . HIS A 272  ? 0.3343 0.2995 0.3153 -0.0011 0.0030  0.0367  270  HIS A NE2 
1805  N N   . PRO A 273  ? 0.2790 0.2454 0.2523 -0.0059 0.0042  0.0376  271  PRO A N   
1806  C CA  . PRO A 273  ? 0.2900 0.2548 0.2620 -0.0064 0.0046  0.0368  271  PRO A CA  
1807  C C   . PRO A 273  ? 0.3640 0.3270 0.3360 -0.0056 0.0054  0.0350  271  PRO A C   
1808  O O   . PRO A 273  ? 0.2801 0.2422 0.2507 -0.0060 0.0058  0.0341  271  PRO A O   
1809  C CB  . PRO A 273  ? 0.3454 0.3088 0.3184 -0.0068 0.0037  0.0385  271  PRO A CB  
1810  C CG  . PRO A 273  ? 0.2817 0.2445 0.2569 -0.0058 0.0029  0.0395  271  PRO A CG  
1811  C CD  . PRO A 273  ? 0.3046 0.2702 0.2795 -0.0056 0.0030  0.0395  271  PRO A CD  
1812  N N   . ARG A 274  ? 0.3053 0.2682 0.2787 -0.0045 0.0055  0.0344  272  ARG A N   
1813  C CA  . ARG A 274  ? 0.2963 0.2583 0.2694 -0.0037 0.0063  0.0327  272  ARG A CA  
1814  C C   . ARG A 274  ? 0.3197 0.2838 0.2929 -0.0034 0.0072  0.0322  272  ARG A C   
1815  O O   . ARG A 274  ? 0.2952 0.2599 0.2696 -0.0023 0.0075  0.0315  272  ARG A O   
1816  C CB  . ARG A 274  ? 0.2932 0.2535 0.2682 -0.0024 0.0058  0.0321  272  ARG A CB  
1817  C CG  . ARG A 274  ? 0.3172 0.2751 0.2926 -0.0029 0.0048  0.0328  272  ARG A CG  
1818  C CD  . ARG A 274  ? 0.3011 0.2582 0.2746 -0.0037 0.0052  0.0320  272  ARG A CD  
1819  N NE  . ARG A 274  ? 0.3179 0.2751 0.2904 -0.0028 0.0061  0.0300  272  ARG A NE  
1820  C CZ  . ARG A 274  ? 0.3136 0.2695 0.2869 -0.0017 0.0058  0.0283  272  ARG A CZ  
1821  N NH1 . ARG A 274  ? 0.3188 0.2727 0.2944 -0.0012 0.0046  0.0283  272  ARG A NH1 
1822  N NH2 . ARG A 274  ? 0.2840 0.2407 0.2559 -0.0009 0.0067  0.0267  272  ARG A NH2 
1823  N N   . TYR A 275  ? 0.2867 0.2520 0.2589 -0.0045 0.0075  0.0324  273  TYR A N   
1824  C CA  . TYR A 275  ? 0.2670 0.2342 0.2396 -0.0046 0.0082  0.0322  273  TYR A CA  
1825  C C   . TYR A 275  ? 0.3048 0.2715 0.2762 -0.0046 0.0092  0.0314  273  TYR A C   
1826  O O   . TYR A 275  ? 0.3071 0.2731 0.2770 -0.0054 0.0093  0.0313  273  TYR A O   
1827  C CB  . TYR A 275  ? 0.2873 0.2559 0.2598 -0.0057 0.0077  0.0326  273  TYR A CB  
1828  C CG  . TYR A 275  ? 0.2628 0.2329 0.2361 -0.0062 0.0083  0.0324  273  TYR A CG  
1829  C CD1 . TYR A 275  ? 0.2794 0.2511 0.2545 -0.0056 0.0088  0.0324  273  TYR A CD1 
1830  C CD2 . TYR A 275  ? 0.2728 0.2428 0.2455 -0.0072 0.0082  0.0321  273  TYR A CD2 
1831  C CE1 . TYR A 275  ? 0.2859 0.2594 0.2622 -0.0063 0.0093  0.0325  273  TYR A CE1 
1832  C CE2 . TYR A 275  ? 0.2777 0.2487 0.2516 -0.0078 0.0085  0.0321  273  TYR A CE2 
1833  C CZ  . TYR A 275  ? 0.3036 0.2765 0.2793 -0.0075 0.0091  0.0324  273  TYR A CZ  
1834  O OH  . TYR A 275  ? 0.3306 0.3048 0.3079 -0.0084 0.0094  0.0327  273  TYR A OH  
1835  N N   . SER A 276  ? 0.2817 0.2490 0.2536 -0.0035 0.0098  0.0308  274  SER A N   
1836  C CA  . SER A 276  ? 0.3009 0.2683 0.2714 -0.0034 0.0108  0.0302  274  SER A CA  
1837  C C   . SER A 276  ? 0.2616 0.2314 0.2333 -0.0022 0.0116  0.0296  274  SER A C   
1838  O O   . SER A 276  ? 0.3009 0.2714 0.2744 -0.0012 0.0113  0.0292  274  SER A O   
1839  C CB  . SER A 276  ? 0.3187 0.2839 0.2875 -0.0031 0.0105  0.0294  274  SER A CB  
1840  O OG  . SER A 276  ? 0.3399 0.3046 0.3097 -0.0018 0.0102  0.0284  274  SER A OG  
1841  N N   . ARG A 277  ? 0.2693 0.2405 0.2399 -0.0023 0.0127  0.0297  275  ARG A N   
1842  C CA  . ARG A 277  ? 0.2829 0.2572 0.2543 -0.0012 0.0137  0.0290  275  ARG A CA  
1843  C C   . ARG A 277  ? 0.3090 0.2828 0.2804 0.0006  0.0134  0.0271  275  ARG A C   
1844  O O   . ARG A 277  ? 0.2631 0.2392 0.2363 0.0020  0.0136  0.0262  275  ARG A O   
1845  C CB  . ARG A 277  ? 0.2459 0.2221 0.2157 -0.0018 0.0149  0.0298  275  ARG A CB  
1846  C CG  . ARG A 277  ? 0.2473 0.2275 0.2173 -0.0006 0.0161  0.0291  275  ARG A CG  
1847  C CD  . ARG A 277  ? 0.2795 0.2629 0.2523 -0.0004 0.0166  0.0293  275  ARG A CD  
1848  N NE  . ARG A 277  ? 0.2483 0.2365 0.2215 0.0008  0.0179  0.0284  275  ARG A NE  
1849  C CZ  . ARG A 277  ? 0.2780 0.2674 0.2518 0.0030  0.0178  0.0261  275  ARG A CZ  
1850  N NH1 . ARG A 277  ? 0.2959 0.2817 0.2701 0.0041  0.0164  0.0246  275  ARG A NH1 
1851  N NH2 . ARG A 277  ? 0.2842 0.2787 0.2583 0.0042  0.0191  0.0252  275  ARG A NH2 
1852  N N   . ALA A 278  ? 0.2756 0.2467 0.2456 0.0008  0.0127  0.0264  276  ALA A N   
1853  C CA  . ALA A 278  ? 0.2944 0.2646 0.2649 0.0025  0.0121  0.0243  276  ALA A CA  
1854  C C   . ALA A 278  ? 0.2880 0.2572 0.2613 0.0033  0.0111  0.0241  276  ALA A C   
1855  O O   . ALA A 278  ? 0.3223 0.2917 0.2972 0.0050  0.0106  0.0223  276  ALA A O   
1856  C CB  . ALA A 278  ? 0.2953 0.2626 0.2642 0.0022  0.0114  0.0237  276  ALA A CB  
1857  N N   . GLN A 279  ? 0.3087 0.2770 0.2828 0.0021  0.0105  0.0258  277  GLN A N   
1858  C CA  . GLN A 279  ? 0.2622 0.2295 0.2389 0.0026  0.0093  0.0262  277  GLN A CA  
1859  C C   . GLN A 279  ? 0.3202 0.2905 0.2985 0.0026  0.0097  0.0270  277  GLN A C   
1860  O O   . GLN A 279  ? 0.3256 0.2955 0.3054 0.0024  0.0088  0.0281  277  GLN A O   
1861  C CB  . GLN A 279  ? 0.2744 0.2390 0.2506 0.0013  0.0082  0.0277  277  GLN A CB  
1862  C CG  . GLN A 279  ? 0.2666 0.2284 0.2414 0.0010  0.0078  0.0270  277  GLN A CG  
1863  C CD  . GLN A 279  ? 0.3674 0.3274 0.3442 0.0025  0.0068  0.0255  277  GLN A CD  
1864  O OE1 . GLN A 279  ? 0.3694 0.3287 0.3487 0.0032  0.0058  0.0260  277  GLN A OE1 
1865  N NE2 . GLN A 279  ? 0.2996 0.2591 0.2755 0.0032  0.0070  0.0236  277  GLN A NE2 
1866  N N   . ALA A 280  ? 0.2933 0.2670 0.2716 0.0030  0.0111  0.0264  278  ALA A N   
1867  C CA  . ALA A 280  ? 0.3016 0.2785 0.2815 0.0026  0.0116  0.0273  278  ALA A CA  
1868  C C   . ALA A 280  ? 0.2985 0.2760 0.2815 0.0041  0.0105  0.0269  278  ALA A C   
1869  O O   . ALA A 280  ? 0.2877 0.2663 0.2720 0.0035  0.0101  0.0281  278  ALA A O   
1870  C CB  . ALA A 280  ? 0.2600 0.2409 0.2397 0.0028  0.0132  0.0268  278  ALA A CB  
1871  N N   . ALA A 281  ? 0.2980 0.2746 0.2821 0.0060  0.0100  0.0252  279  ALA A N   
1872  C CA  . ALA A 281  ? 0.3000 0.2767 0.2873 0.0076  0.0087  0.0248  279  ALA A CA  
1873  C C   . ALA A 281  ? 0.3239 0.2978 0.3116 0.0066  0.0071  0.0269  279  ALA A C   
1874  O O   . ALA A 281  ? 0.3195 0.2948 0.3091 0.0068  0.0065  0.0279  279  ALA A O   
1875  C CB  . ALA A 281  ? 0.3106 0.2861 0.2993 0.0099  0.0080  0.0224  279  ALA A CB  
1876  N N   . ARG A 282  ? 0.2907 0.2609 0.2766 0.0055  0.0066  0.0277  280  ARG A N   
1877  C CA  . ARG A 282  ? 0.3342 0.3025 0.3202 0.0045  0.0052  0.0298  280  ARG A CA  
1878  C C   . ARG A 282  ? 0.3036 0.2742 0.2885 0.0028  0.0057  0.0313  280  ARG A C   
1879  O O   . ARG A 282  ? 0.3014 0.2725 0.2872 0.0025  0.0047  0.0328  280  ARG A O   
1880  C CB  . ARG A 282  ? 0.3235 0.2882 0.3080 0.0036  0.0046  0.0303  280  ARG A CB  
1881  C CG  . ARG A 282  ? 0.3248 0.2865 0.3110 0.0050  0.0035  0.0291  280  ARG A CG  
1882  C CD  . ARG A 282  ? 0.3086 0.2670 0.2937 0.0036  0.0028  0.0302  280  ARG A CD  
1883  N NE  . ARG A 282  ? 0.3404 0.2984 0.3259 0.0024  0.0018  0.0330  280  ARG A NE  
1884  C CZ  . ARG A 282  ? 0.3781 0.3346 0.3623 0.0008  0.0014  0.0347  280  ARG A CZ  
1885  N NH1 . ARG A 282  ? 0.3207 0.2757 0.3035 0.0001  0.0018  0.0338  280  ARG A NH1 
1886  N NH2 . ARG A 282  ? 0.3186 0.2757 0.3029 -0.0002 0.0006  0.0374  280  ARG A NH2 
1887  N N   . VAL A 283  ? 0.2871 0.2593 0.2703 0.0019  0.0072  0.0308  281  VAL A N   
1888  C CA  . VAL A 283  ? 0.2442 0.2182 0.2268 0.0003  0.0075  0.0318  281  VAL A CA  
1889  C C   . VAL A 283  ? 0.2788 0.2561 0.2639 0.0009  0.0073  0.0320  281  VAL A C   
1890  O O   . VAL A 283  ? 0.2818 0.2602 0.2675 0.0002  0.0064  0.0331  281  VAL A O   
1891  C CB  . VAL A 283  ? 0.2896 0.2642 0.2703 -0.0008 0.0088  0.0314  281  VAL A CB  
1892  C CG1 . VAL A 283  ? 0.2978 0.2746 0.2789 -0.0022 0.0091  0.0321  281  VAL A CG1 
1893  C CG2 . VAL A 283  ? 0.2872 0.2588 0.2653 -0.0016 0.0087  0.0314  281  VAL A CG2 
1894  N N   . MET A 284  ? 0.2542 0.2337 0.2411 0.0022  0.0080  0.0308  282  MET A N   
1895  C CA  . MET A 284  ? 0.2913 0.2743 0.2810 0.0028  0.0078  0.0309  282  MET A CA  
1896  C C   . MET A 284  ? 0.3052 0.2874 0.2969 0.0042  0.0060  0.0314  282  MET A C   
1897  O O   . MET A 284  ? 0.2923 0.2768 0.2857 0.0041  0.0053  0.0322  282  MET A O   
1898  C CB  . MET A 284  ? 0.2829 0.2692 0.2740 0.0040  0.0092  0.0294  282  MET A CB  
1899  C CG  . MET A 284  ? 0.2750 0.2625 0.2642 0.0026  0.0110  0.0293  282  MET A CG  
1900  S SD  . MET A 284  ? 0.3379 0.3266 0.3268 -0.0001 0.0112  0.0309  282  MET A SD  
1901  C CE  . MET A 284  ? 0.2938 0.2875 0.2866 0.0002  0.0112  0.0310  282  MET A CE  
1902  N N   . GLY A 285  ? 0.3312 0.3100 0.3229 0.0053  0.0052  0.0312  283  GLY A N   
1903  C CA  . GLY A 285  ? 0.2984 0.2761 0.2923 0.0066  0.0033  0.0320  283  GLY A CA  
1904  C C   . GLY A 285  ? 0.3188 0.2949 0.3115 0.0053  0.0020  0.0344  283  GLY A C   
1905  O O   . GLY A 285  ? 0.3215 0.2980 0.3159 0.0060  0.0005  0.0357  283  GLY A O   
1906  N N   . GLU A 286  ? 0.2615 0.2360 0.2512 0.0035  0.0026  0.0350  284  GLU A N   
1907  C CA  . GLU A 286  ? 0.2796 0.2529 0.2680 0.0024  0.0014  0.0371  284  GLU A CA  
1908  C C   . GLU A 286  ? 0.3399 0.3154 0.3262 0.0006  0.0020  0.0376  284  GLU A C   
1909  O O   . GLU A 286  ? 0.3686 0.3454 0.3545 0.0000  0.0009  0.0391  284  GLU A O   
1910  C CB  . GLU A 286  ? 0.2954 0.2649 0.2826 0.0020  0.0012  0.0375  284  GLU A CB  
1911  C CG  . GLU A 286  ? 0.3168 0.2835 0.3064 0.0037  0.0002  0.0370  284  GLU A CG  
1912  C CD  . GLU A 286  ? 0.3529 0.3161 0.3415 0.0032  0.0003  0.0366  284  GLU A CD  
1913  O OE1 . GLU A 286  ? 0.3479 0.3104 0.3342 0.0015  0.0004  0.0379  284  GLU A OE1 
1914  O OE2 . GLU A 286  ? 0.3663 0.3276 0.3565 0.0046  0.0001  0.0349  284  GLU A OE2 
1915  N N   . LEU A 287  ? 0.2531 0.2289 0.2378 -0.0003 0.0034  0.0362  285  LEU A N   
1916  C CA  . LEU A 287  ? 0.2873 0.2648 0.2705 -0.0019 0.0037  0.0363  285  LEU A CA  
1917  C C   . LEU A 287  ? 0.2621 0.2431 0.2471 -0.0019 0.0036  0.0360  285  LEU A C   
1918  O O   . LEU A 287  ? 0.2927 0.2757 0.2774 -0.0027 0.0028  0.0364  285  LEU A O   
1919  C CB  . LEU A 287  ? 0.2709 0.2470 0.2522 -0.0028 0.0050  0.0352  285  LEU A CB  
1920  C CG  . LEU A 287  ? 0.2933 0.2705 0.2734 -0.0043 0.0054  0.0347  285  LEU A CG  
1921  C CD1 . LEU A 287  ? 0.3400 0.3185 0.3194 -0.0049 0.0043  0.0354  285  LEU A CD1 
1922  C CD2 . LEU A 287  ? 0.2925 0.2674 0.2705 -0.0048 0.0062  0.0341  285  LEU A CD2 
1923  N N   . LEU A 288  ? 0.2822 0.2646 0.2693 -0.0011 0.0043  0.0350  286  LEU A N   
1924  C CA  . LEU A 288  ? 0.2635 0.2496 0.2527 -0.0013 0.0043  0.0347  286  LEU A CA  
1925  C C   . LEU A 288  ? 0.3080 0.2961 0.2986 -0.0008 0.0027  0.0357  286  LEU A C   
1926  O O   . LEU A 288  ? 0.2832 0.2736 0.2740 -0.0018 0.0022  0.0357  286  LEU A O   
1927  C CB  . LEU A 288  ? 0.2872 0.2749 0.2786 -0.0003 0.0055  0.0337  286  LEU A CB  
1928  C CG  . LEU A 288  ? 0.3812 0.3733 0.3756 -0.0003 0.0055  0.0335  286  LEU A CG  
1929  C CD1 . LEU A 288  ? 0.2773 0.2708 0.2715 -0.0024 0.0058  0.0334  286  LEU A CD1 
1930  C CD2 . LEU A 288  ? 0.4372 0.4313 0.4335 0.0009  0.0067  0.0325  286  LEU A CD2 
1931  N N   . PRO A 289  ? 0.3091 0.2963 0.3007 0.0008  0.0016  0.0366  287  PRO A N   
1932  C CA  . PRO A 289  ? 0.2548 0.2441 0.2475 0.0012  -0.0001 0.0379  287  PRO A CA  
1933  C C   . PRO A 289  ? 0.2780 0.2678 0.2682 -0.0001 -0.0009 0.0389  287  PRO A C   
1934  O O   . PRO A 289  ? 0.2574 0.2503 0.2482 -0.0002 -0.0020 0.0394  287  PRO A O   
1935  C CB  . PRO A 289  ? 0.2893 0.2764 0.2832 0.0030  -0.0012 0.0389  287  PRO A CB  
1936  C CG  . PRO A 289  ? 0.3703 0.3553 0.3649 0.0039  0.0001  0.0374  287  PRO A CG  
1937  C CD  . PRO A 289  ? 0.2938 0.2780 0.2858 0.0022  0.0017  0.0365  287  PRO A CD  
1938  N N   . ARG A 290  ? 0.2625 0.2497 0.2500 -0.0011 -0.0003 0.0391  288  ARG A N   
1939  C CA  . ARG A 290  ? 0.2659 0.2542 0.2509 -0.0024 -0.0009 0.0396  288  ARG A CA  
1940  C C   . ARG A 290  ? 0.2634 0.2543 0.2484 -0.0035 -0.0006 0.0379  288  ARG A C   
1941  O O   . ARG A 290  ? 0.2955 0.2893 0.2801 -0.0039 -0.0016 0.0380  288  ARG A O   
1942  C CB  . ARG A 290  ? 0.2859 0.2712 0.2684 -0.0030 -0.0003 0.0400  288  ARG A CB  
1943  C CG  . ARG A 290  ? 0.3182 0.3008 0.3010 -0.0022 -0.0009 0.0419  288  ARG A CG  
1944  C CD  . ARG A 290  ? 0.3602 0.3400 0.3409 -0.0031 -0.0003 0.0422  288  ARG A CD  
1945  N NE  . ARG A 290  ? 0.4328 0.4097 0.4145 -0.0024 -0.0010 0.0438  288  ARG A NE  
1946  C CZ  . ARG A 290  ? 0.4636 0.4372 0.4449 -0.0026 -0.0005 0.0435  288  ARG A CZ  
1947  N NH1 . ARG A 290  ? 0.3359 0.3087 0.3155 -0.0033 0.0008  0.0418  288  ARG A NH1 
1948  N NH2 . ARG A 290  ? 0.4336 0.4044 0.4165 -0.0020 -0.0014 0.0449  288  ARG A NH2 
1949  N N   . VAL A 291  ? 0.2425 0.2323 0.2279 -0.0040 0.0007  0.0364  289  VAL A N   
1950  C CA  . VAL A 291  ? 0.2459 0.2377 0.2320 -0.0052 0.0008  0.0350  289  VAL A CA  
1951  C C   . VAL A 291  ? 0.2458 0.2413 0.2347 -0.0049 -0.0001 0.0348  289  VAL A C   
1952  O O   . VAL A 291  ? 0.2683 0.2665 0.2577 -0.0056 -0.0010 0.0340  289  VAL A O   
1953  C CB  . VAL A 291  ? 0.3141 0.3040 0.3005 -0.0059 0.0023  0.0340  289  VAL A CB  
1954  C CG1 . VAL A 291  ? 0.2712 0.2627 0.2587 -0.0074 0.0021  0.0326  289  VAL A CG1 
1955  C CG2 . VAL A 291  ? 0.3100 0.2964 0.2938 -0.0060 0.0031  0.0341  289  VAL A CG2 
1956  N N   . LYS A 292  ? 0.2683 0.2644 0.2594 -0.0036 0.0000  0.0354  290  LYS A N   
1957  C CA  . LYS A 292  ? 0.2425 0.2424 0.2364 -0.0031 -0.0010 0.0353  290  LYS A CA  
1958  C C   . LYS A 292  ? 0.2564 0.2586 0.2495 -0.0028 -0.0028 0.0362  290  LYS A C   
1959  O O   . LYS A 292  ? 0.2727 0.2785 0.2672 -0.0032 -0.0038 0.0354  290  LYS A O   
1960  C CB  . LYS A 292  ? 0.2429 0.2431 0.2393 -0.0014 -0.0006 0.0357  290  LYS A CB  
1961  C CG  . LYS A 292  ? 0.2645 0.2690 0.2641 -0.0007 -0.0017 0.0356  290  LYS A CG  
1962  C CD  . LYS A 292  ? 0.2585 0.2637 0.2609 0.0012  -0.0015 0.0356  290  LYS A CD  
1963  C CE  . LYS A 292  ? 0.2557 0.2655 0.2614 0.0022  -0.0029 0.0356  290  LYS A CE  
1964  N NZ  . LYS A 292  ? 0.3104 0.3217 0.3194 0.0039  -0.0023 0.0350  290  LYS A NZ  
1965  N N   . ALA A 293  ? 0.2634 0.2638 0.2543 -0.0021 -0.0034 0.0378  291  ALA A N   
1966  C CA  . ALA A 293  ? 0.2488 0.2519 0.2386 -0.0019 -0.0051 0.0391  291  ALA A CA  
1967  C C   . ALA A 293  ? 0.2465 0.2518 0.2344 -0.0032 -0.0055 0.0377  291  ALA A C   
1968  O O   . ALA A 293  ? 0.2665 0.2759 0.2548 -0.0032 -0.0069 0.0375  291  ALA A O   
1969  C CB  . ALA A 293  ? 0.2590 0.2598 0.2471 -0.0012 -0.0056 0.0416  291  ALA A CB  
1970  N N   . LEU A 294  ? 0.2448 0.2477 0.2310 -0.0043 -0.0043 0.0366  292  LEU A N   
1971  C CA  . LEU A 294  ? 0.2471 0.2520 0.2320 -0.0054 -0.0047 0.0348  292  LEU A CA  
1972  C C   . LEU A 294  ? 0.2443 0.2513 0.2320 -0.0060 -0.0051 0.0327  292  LEU A C   
1973  O O   . LEU A 294  ? 0.2446 0.2551 0.2324 -0.0063 -0.0065 0.0313  292  LEU A O   
1974  C CB  . LEU A 294  ? 0.2546 0.2561 0.2375 -0.0062 -0.0035 0.0340  292  LEU A CB  
1975  C CG  . LEU A 294  ? 0.2696 0.2692 0.2495 -0.0059 -0.0032 0.0358  292  LEU A CG  
1976  C CD1 . LEU A 294  ? 0.2627 0.2592 0.2411 -0.0067 -0.0019 0.0347  292  LEU A CD1 
1977  C CD2 . LEU A 294  ? 0.2458 0.2493 0.2238 -0.0058 -0.0044 0.0366  292  LEU A CD2 
1978  N N   . ALA A 295  ? 0.2429 0.2484 0.2332 -0.0062 -0.0041 0.0323  293  ALA A N   
1979  C CA  . ALA A 295  ? 0.2519 0.2596 0.2454 -0.0071 -0.0044 0.0307  293  ALA A CA  
1980  C C   . ALA A 295  ? 0.2433 0.2556 0.2389 -0.0064 -0.0060 0.0308  293  ALA A C   
1981  O O   . ALA A 295  ? 0.2585 0.2737 0.2558 -0.0072 -0.0071 0.0290  293  ALA A O   
1982  C CB  . ALA A 295  ? 0.2416 0.2474 0.2373 -0.0075 -0.0027 0.0308  293  ALA A CB  
1983  N N   . LEU A 296  ? 0.2440 0.2568 0.2395 -0.0049 -0.0063 0.0327  294  LEU A N   
1984  C CA  . LEU A 296  ? 0.2450 0.2622 0.2423 -0.0040 -0.0080 0.0331  294  LEU A CA  
1985  C C   . LEU A 296  ? 0.2626 0.2829 0.2577 -0.0042 -0.0097 0.0325  294  LEU A C   
1986  O O   . LEU A 296  ? 0.2793 0.3039 0.2762 -0.0042 -0.0112 0.0313  294  LEU A O   
1987  C CB  . LEU A 296  ? 0.2460 0.2625 0.2434 -0.0021 -0.0083 0.0355  294  LEU A CB  
1988  C CG  . LEU A 296  ? 0.2748 0.2900 0.2752 -0.0014 -0.0070 0.0356  294  LEU A CG  
1989  C CD1 . LEU A 296  ? 0.2507 0.2641 0.2509 0.0005  -0.0074 0.0377  294  LEU A CD1 
1990  C CD2 . LEU A 296  ? 0.3079 0.3274 0.3125 -0.0015 -0.0074 0.0343  294  LEU A CD2 
1991  N N   . LEU A 297  ? 0.2468 0.2657 0.2381 -0.0042 -0.0096 0.0332  295  LEU A N   
1992  C CA  . LEU A 297  ? 0.2489 0.2715 0.2380 -0.0044 -0.0110 0.0323  295  LEU A CA  
1993  C C   . LEU A 297  ? 0.2757 0.2995 0.2658 -0.0056 -0.0113 0.0289  295  LEU A C   
1994  O O   . LEU A 297  ? 0.2572 0.2854 0.2478 -0.0056 -0.0130 0.0272  295  LEU A O   
1995  C CB  . LEU A 297  ? 0.2916 0.3128 0.2766 -0.0042 -0.0105 0.0340  295  LEU A CB  
1996  N N   . ALA A 298  ? 0.2462 0.2660 0.2370 -0.0067 -0.0099 0.0277  296  ALA A N   
1997  C CA  . ALA A 298  ? 0.2461 0.2664 0.2388 -0.0080 -0.0104 0.0246  296  ALA A CA  
1998  C C   . ALA A 298  ? 0.2814 0.3045 0.2785 -0.0084 -0.0114 0.0235  296  ALA A C   
1999  O O   . ALA A 298  ? 0.2668 0.2926 0.2654 -0.0090 -0.0129 0.0209  296  ALA A O   
2000  C CB  . ALA A 298  ? 0.2450 0.2602 0.2379 -0.0090 -0.0088 0.0241  296  ALA A CB  
2001  N N   . LYS A 299  ? 0.2454 0.2682 0.2447 -0.0080 -0.0106 0.0253  297  LYS A N   
2002  C CA  . LYS A 299  ? 0.2455 0.2717 0.2491 -0.0083 -0.0115 0.0245  297  LYS A CA  
2003  C C   . LYS A 299  ? 0.2991 0.3306 0.3025 -0.0074 -0.0138 0.0238  297  LYS A C   
2004  O O   . LYS A 299  ? 0.3062 0.3409 0.3124 -0.0082 -0.0152 0.0215  297  LYS A O   
2005  C CB  . LYS A 299  ? 0.2531 0.2787 0.2587 -0.0075 -0.0103 0.0266  297  LYS A CB  
2006  C CG  . LYS A 299  ? 0.2817 0.3120 0.2916 -0.0074 -0.0114 0.0261  297  LYS A CG  
2007  C CD  . LYS A 299  ? 0.2890 0.3192 0.3011 -0.0064 -0.0101 0.0278  297  LYS A CD  
2008  C CE  . LYS A 299  ? 0.2752 0.3107 0.2908 -0.0055 -0.0116 0.0276  297  LYS A CE  
2009  N NZ  . LYS A 299  ? 0.3390 0.3747 0.3571 -0.0045 -0.0103 0.0288  297  LYS A NZ  
2010  N N   . ASN A 300  ? 0.2636 0.2963 0.2637 -0.0059 -0.0143 0.0257  298  ASN A N   
2011  C CA  A ASN A 300  ? 0.2835 0.3217 0.2831 -0.0049 -0.0165 0.0256  298  ASN A CA  
2012  C CA  B ASN A 300  ? 0.2827 0.3209 0.2826 -0.0050 -0.0165 0.0255  298  ASN A CA  
2013  C C   . ASN A 300  ? 0.2810 0.3222 0.2795 -0.0056 -0.0180 0.0225  298  ASN A C   
2014  O O   . ASN A 300  ? 0.2905 0.3369 0.2902 -0.0052 -0.0200 0.0211  298  ASN A O   
2015  C CB  A ASN A 300  ? 0.2997 0.3381 0.2959 -0.0033 -0.0167 0.0289  298  ASN A CB  
2016  C CB  B ASN A 300  ? 0.3017 0.3405 0.2985 -0.0033 -0.0169 0.0288  298  ASN A CB  
2017  C CG  A ASN A 300  ? 0.3046 0.3412 0.3027 -0.0022 -0.0160 0.0315  298  ASN A CG  
2018  C CG  B ASN A 300  ? 0.3309 0.3757 0.3283 -0.0022 -0.0192 0.0292  298  ASN A CG  
2019  O OD1 A ASN A 300  ? 0.3347 0.3717 0.3368 -0.0024 -0.0158 0.0308  298  ASN A OD1 
2020  O OD1 B ASN A 300  ? 0.3776 0.4238 0.3781 -0.0014 -0.0197 0.0300  298  ASN A OD1 
2021  N ND2 A ASN A 300  ? 0.3432 0.3780 0.3388 -0.0011 -0.0159 0.0345  298  ASN A ND2 
2022  N ND2 B ASN A 300  ? 0.2898 0.3385 0.2842 -0.0020 -0.0206 0.0284  298  ASN A ND2 
2023  N N   . TYR A 301  ? 0.2506 0.2890 0.2468 -0.0063 -0.0172 0.0213  299  TYR A N   
2024  C CA  . TYR A 301  ? 0.2966 0.3375 0.2921 -0.0068 -0.0186 0.0178  299  TYR A CA  
2025  C C   . TYR A 301  ? 0.2916 0.3306 0.2911 -0.0084 -0.0188 0.0146  299  TYR A C   
2026  O O   . TYR A 301  ? 0.2915 0.3326 0.2914 -0.0088 -0.0203 0.0111  299  TYR A O   
2027  C CB  . TYR A 301  ? 0.2521 0.2915 0.2431 -0.0065 -0.0178 0.0179  299  TYR A CB  
2028  C CG  . TYR A 301  ? 0.2534 0.2960 0.2402 -0.0052 -0.0181 0.0205  299  TYR A CG  
2029  C CD1 . TYR A 301  ? 0.2566 0.3056 0.2416 -0.0044 -0.0200 0.0193  299  TYR A CD1 
2030  C CD2 . TYR A 301  ? 0.2538 0.2929 0.2383 -0.0048 -0.0165 0.0242  299  TYR A CD2 
2031  C CE1 . TYR A 301  ? 0.2818 0.3341 0.2629 -0.0034 -0.0202 0.0222  299  TYR A CE1 
2032  C CE2 . TYR A 301  ? 0.3112 0.3531 0.2922 -0.0039 -0.0168 0.0270  299  TYR A CE2 
2033  C CZ  . TYR A 301  ? 0.3099 0.3584 0.2891 -0.0032 -0.0186 0.0262  299  TYR A CZ  
2034  O OH  . TYR A 301  ? 0.2963 0.3479 0.2719 -0.0024 -0.0190 0.0295  299  TYR A OH  
2035  N N   . ASP A 302  ? 0.2660 0.3012 0.2686 -0.0094 -0.0173 0.0158  300  ASP A N   
2036  C CA  . ASP A 302  ? 0.2843 0.3172 0.2911 -0.0112 -0.0173 0.0137  300  ASP A CA  
2037  C C   . ASP A 302  ? 0.2744 0.3040 0.2799 -0.0119 -0.0172 0.0116  300  ASP A C   
2038  O O   . ASP A 302  ? 0.2811 0.3115 0.2888 -0.0127 -0.0188 0.0082  300  ASP A O   
2039  C CB  . ASP A 302  ? 0.3036 0.3411 0.3148 -0.0118 -0.0194 0.0113  300  ASP A CB  
2040  C CG  . ASP A 302  ? 0.3368 0.3720 0.3535 -0.0139 -0.0190 0.0105  300  ASP A CG  
2041  O OD1 . ASP A 302  ? 0.3298 0.3616 0.3471 -0.0145 -0.0169 0.0131  300  ASP A OD1 
2042  O OD2 . ASP A 302  ? 0.3312 0.3682 0.3516 -0.0151 -0.0209 0.0075  300  ASP A OD2 
2043  N N   . ILE A 303  ? 0.2543 0.2801 0.2563 -0.0114 -0.0153 0.0135  301  ILE A N   
2044  C CA  . ILE A 303  ? 0.2493 0.2716 0.2499 -0.0119 -0.0150 0.0119  301  ILE A CA  
2045  C C   . ILE A 303  ? 0.2479 0.2646 0.2492 -0.0128 -0.0129 0.0140  301  ILE A C   
2046  O O   . ILE A 303  ? 0.2466 0.2626 0.2485 -0.0127 -0.0115 0.0167  301  ILE A O   
2047  C CB  . ILE A 303  ? 0.2627 0.2863 0.2581 -0.0105 -0.0149 0.0119  301  ILE A CB  
2048  C CG1 . ILE A 303  ? 0.2484 0.2700 0.2407 -0.0098 -0.0130 0.0159  301  ILE A CG1 
2049  C CG2 . ILE A 303  ? 0.2654 0.2954 0.2596 -0.0095 -0.0170 0.0102  301  ILE A CG2 
2050  C CD1 . ILE A 303  ? 0.2699 0.2912 0.2577 -0.0090 -0.0124 0.0163  301  ILE A CD1 
2051  N N   . GLY A 304  ? 0.3014 0.3145 0.3029 -0.0135 -0.0127 0.0125  302  GLY A N   
2052  C CA  . GLY A 304  ? 0.3010 0.3090 0.3026 -0.0143 -0.0108 0.0145  302  GLY A CA  
2053  C C   . GLY A 304  ? 0.2630 0.2693 0.2601 -0.0131 -0.0091 0.0168  302  GLY A C   
2054  O O   . GLY A 304  ? 0.2463 0.2542 0.2400 -0.0120 -0.0095 0.0163  302  GLY A O   
2055  N N   . LEU A 305  ? 0.2711 0.2746 0.2683 -0.0134 -0.0072 0.0194  303  LEU A N   
2056  C CA  . LEU A 305  ? 0.2492 0.2503 0.2428 -0.0125 -0.0056 0.0214  303  LEU A CA  
2057  C C   . LEU A 305  ? 0.2433 0.2400 0.2377 -0.0134 -0.0042 0.0222  303  LEU A C   
2058  O O   . LEU A 305  ? 0.2429 0.2393 0.2396 -0.0140 -0.0033 0.0236  303  LEU A O   
2059  C CB  . LEU A 305  ? 0.2582 0.2608 0.2508 -0.0114 -0.0049 0.0238  303  LEU A CB  
2060  C CG  . LEU A 305  ? 0.3033 0.3034 0.2925 -0.0105 -0.0036 0.0257  303  LEU A CG  
2061  C CD1 . LEU A 305  ? 0.2985 0.3009 0.2860 -0.0092 -0.0039 0.0274  303  LEU A CD1 
2062  C CD2 . LEU A 305  ? 0.3216 0.3185 0.3117 -0.0107 -0.0018 0.0272  303  LEU A CD2 
2063  N N   . ASN A 306  ? 0.2438 0.2376 0.2361 -0.0134 -0.0040 0.0215  304  ASN A N   
2064  C CA  . ASN A 306  ? 0.2577 0.2474 0.2506 -0.0142 -0.0030 0.0221  304  ASN A CA  
2065  C C   . ASN A 306  ? 0.2426 0.2301 0.2322 -0.0133 -0.0014 0.0239  304  ASN A C   
2066  O O   . ASN A 306  ? 0.2951 0.2830 0.2817 -0.0124 -0.0015 0.0236  304  ASN A O   
2067  C CB  . ASN A 306  ? 0.2479 0.2359 0.2418 -0.0148 -0.0043 0.0197  304  ASN A CB  
2068  C CG  . ASN A 306  ? 0.2706 0.2542 0.2644 -0.0154 -0.0034 0.0207  304  ASN A CG  
2069  O OD1 . ASN A 306  ? 0.3159 0.2976 0.3068 -0.0146 -0.0029 0.0207  304  ASN A OD1 
2070  N ND2 . ASN A 306  ? 0.2462 0.2284 0.2432 -0.0168 -0.0031 0.0218  304  ASN A ND2 
2071  N N   . ILE A 307  ? 0.2426 0.2282 0.2327 -0.0137 0.0001  0.0257  305  ILE A N   
2072  C CA  . ILE A 307  ? 0.2492 0.2324 0.2365 -0.0130 0.0016  0.0271  305  ILE A CA  
2073  C C   . ILE A 307  ? 0.2837 0.2635 0.2704 -0.0136 0.0017  0.0267  305  ILE A C   
2074  O O   . ILE A 307  ? 0.2594 0.2378 0.2482 -0.0146 0.0020  0.0273  305  ILE A O   
2075  C CB  . ILE A 307  ? 0.2595 0.2431 0.2476 -0.0128 0.0031  0.0290  305  ILE A CB  
2076  C CG1 . ILE A 307  ? 0.3059 0.2928 0.2949 -0.0121 0.0027  0.0294  305  ILE A CG1 
2077  C CG2 . ILE A 307  ? 0.2935 0.2746 0.2789 -0.0121 0.0044  0.0300  305  ILE A CG2 
2078  C CD1 . ILE A 307  ? 0.3453 0.3333 0.3358 -0.0117 0.0040  0.0307  305  ILE A CD1 
2079  N N   . ASP A 308  ? 0.2777 0.2563 0.2618 -0.0128 0.0014  0.0258  306  ASP A N   
2080  C CA  . ASP A 308  ? 0.2657 0.2412 0.2492 -0.0131 0.0014  0.0253  306  ASP A CA  
2081  C C   . ASP A 308  ? 0.2945 0.2677 0.2769 -0.0131 0.0029  0.0272  306  ASP A C   
2082  O O   . ASP A 308  ? 0.2735 0.2473 0.2547 -0.0125 0.0040  0.0285  306  ASP A O   
2083  C CB  . ASP A 308  ? 0.3067 0.2823 0.2876 -0.0121 0.0008  0.0238  306  ASP A CB  
2084  C CG  . ASP A 308  ? 0.4052 0.3831 0.3871 -0.0121 -0.0009 0.0213  306  ASP A CG  
2085  O OD1 . ASP A 308  ? 0.4173 0.3959 0.4021 -0.0128 -0.0019 0.0203  306  ASP A OD1 
2086  O OD2 . ASP A 308  ? 0.4517 0.4311 0.4315 -0.0113 -0.0013 0.0201  306  ASP A OD2 
2087  N N   . ALA A 309  ? 0.2590 0.2295 0.2420 -0.0137 0.0028  0.0273  307  ALA A N   
2088  C CA  . ALA A 309  ? 0.3088 0.2773 0.2907 -0.0137 0.0041  0.0291  307  ALA A CA  
2089  C C   . ALA A 309  ? 0.3017 0.2682 0.2806 -0.0127 0.0042  0.0286  307  ALA A C   
2090  O O   . ALA A 309  ? 0.2715 0.2373 0.2502 -0.0125 0.0031  0.0269  307  ALA A O   
2091  C CB  . ALA A 309  ? 0.2675 0.2344 0.2519 -0.0150 0.0039  0.0301  307  ALA A CB  
2092  N N   . GLU A 310  ? 0.2977 0.2639 0.2746 -0.0121 0.0056  0.0299  308  GLU A N   
2093  C CA  . GLU A 310  ? 0.3031 0.2679 0.2773 -0.0112 0.0057  0.0294  308  GLU A CA  
2094  C C   . GLU A 310  ? 0.2737 0.2365 0.2469 -0.0112 0.0065  0.0306  308  GLU A C   
2095  O O   . GLU A 310  ? 0.2790 0.2406 0.2536 -0.0120 0.0062  0.0314  308  GLU A O   
2096  C CB  . GLU A 310  ? 0.2786 0.2449 0.2513 -0.0104 0.0062  0.0294  308  GLU A CB  
2097  C CG  . GLU A 310  ? 0.3282 0.2968 0.3016 -0.0104 0.0053  0.0285  308  GLU A CG  
2098  C CD  . GLU A 310  ? 0.3252 0.2951 0.2972 -0.0097 0.0055  0.0289  308  GLU A CD  
2099  O OE1 . GLU A 310  ? 0.3247 0.2943 0.2950 -0.0094 0.0055  0.0285  308  GLU A OE1 
2100  O OE2 . GLU A 310  ? 0.3158 0.2873 0.2888 -0.0096 0.0057  0.0296  308  GLU A OE2 
2101  N N   . GLU A 311  ? 0.2635 0.2261 0.2345 -0.0104 0.0073  0.0309  309  GLU A N   
2102  C CA  . GLU A 311  ? 0.2659 0.2270 0.2356 -0.0102 0.0078  0.0318  309  GLU A CA  
2103  C C   . GLU A 311  ? 0.2452 0.2074 0.2156 -0.0107 0.0089  0.0336  309  GLU A C   
2104  O O   . GLU A 311  ? 0.2524 0.2167 0.2241 -0.0108 0.0094  0.0339  309  GLU A O   
2105  C CB  . GLU A 311  ? 0.2850 0.2458 0.2522 -0.0091 0.0083  0.0314  309  GLU A CB  
2106  C CG  . GLU A 311  ? 0.3378 0.2980 0.3042 -0.0087 0.0074  0.0299  309  GLU A CG  
2107  C CD  . GLU A 311  ? 0.3855 0.3474 0.3521 -0.0086 0.0073  0.0293  309  GLU A CD  
2108  O OE1 . GLU A 311  ? 0.3417 0.3049 0.3095 -0.0088 0.0075  0.0298  309  GLU A OE1 
2109  O OE2 . GLU A 311  ? 0.4208 0.3830 0.3866 -0.0084 0.0068  0.0284  309  GLU A OE2 
2110  N N   . ALA A 312  ? 0.2602 0.2214 0.2300 -0.0109 0.0092  0.0348  310  ALA A N   
2111  C CA  . ALA A 312  ? 0.2530 0.2158 0.2235 -0.0115 0.0102  0.0368  310  ALA A CA  
2112  C C   . ALA A 312  ? 0.2472 0.2127 0.2168 -0.0107 0.0116  0.0367  310  ALA A C   
2113  O O   . ALA A 312  ? 0.2825 0.2506 0.2534 -0.0112 0.0125  0.0378  310  ALA A O   
2114  C CB  . ALA A 312  ? 0.2502 0.2117 0.2196 -0.0118 0.0102  0.0384  310  ALA A CB  
2115  N N   . ASP A 313  ? 0.2637 0.2289 0.2313 -0.0093 0.0117  0.0354  311  ASP A N   
2116  C CA  . ASP A 313  ? 0.2600 0.2275 0.2270 -0.0083 0.0128  0.0350  311  ASP A CA  
2117  C C   . ASP A 313  ? 0.2597 0.2285 0.2285 -0.0081 0.0127  0.0343  311  ASP A C   
2118  O O   . ASP A 313  ? 0.2711 0.2417 0.2400 -0.0070 0.0133  0.0337  311  ASP A O   
2119  C CB  . ASP A 313  ? 0.2917 0.2581 0.2562 -0.0070 0.0128  0.0338  311  ASP A CB  
2120  C CG  . ASP A 313  ? 0.3547 0.3191 0.3190 -0.0068 0.0117  0.0325  311  ASP A CG  
2121  O OD1 . ASP A 313  ? 0.2951 0.2590 0.2607 -0.0074 0.0110  0.0324  311  ASP A OD1 
2122  O OD2 . ASP A 313  ? 0.3471 0.3106 0.3099 -0.0059 0.0115  0.0316  311  ASP A OD2 
2123  N N   . ARG A 314  ? 0.2507 0.2189 0.2211 -0.0090 0.0118  0.0342  312  ARG A N   
2124  C CA  . ARG A 314  ? 0.2604 0.2303 0.2327 -0.0089 0.0116  0.0338  312  ARG A CA  
2125  C C   . ARG A 314  ? 0.2431 0.2149 0.2181 -0.0101 0.0117  0.0347  312  ARG A C   
2126  O O   . ARG A 314  ? 0.2764 0.2501 0.2531 -0.0099 0.0115  0.0344  312  ARG A O   
2127  C CB  . ARG A 314  ? 0.2707 0.2392 0.2428 -0.0089 0.0103  0.0328  312  ARG A CB  
2128  C CG  . ARG A 314  ? 0.2885 0.2558 0.2588 -0.0078 0.0102  0.0321  312  ARG A CG  
2129  C CD  . ARG A 314  ? 0.2827 0.2489 0.2523 -0.0081 0.0091  0.0314  312  ARG A CD  
2130  N NE  . ARG A 314  ? 0.2988 0.2646 0.2676 -0.0073 0.0090  0.0312  312  ARG A NE  
2131  C CZ  . ARG A 314  ? 0.3133 0.2786 0.2812 -0.0075 0.0083  0.0309  312  ARG A CZ  
2132  N NH1 . ARG A 314  ? 0.3166 0.2818 0.2841 -0.0080 0.0078  0.0303  312  ARG A NH1 
2133  N NH2 . ARG A 314  ? 0.2961 0.2611 0.2639 -0.0070 0.0081  0.0311  312  ARG A NH2 
2134  N N   . LEU A 315  ? 0.2531 0.2245 0.2286 -0.0112 0.0119  0.0359  313  LEU A N   
2135  C CA  . LEU A 315  ? 0.2450 0.2181 0.2235 -0.0127 0.0118  0.0369  313  LEU A CA  
2136  C C   . LEU A 315  ? 0.3009 0.2779 0.2808 -0.0123 0.0130  0.0373  313  LEU A C   
2137  O O   . LEU A 315  ? 0.2671 0.2460 0.2494 -0.0125 0.0126  0.0369  313  LEU A O   
2138  C CB  . LEU A 315  ? 0.2496 0.2216 0.2285 -0.0140 0.0119  0.0386  313  LEU A CB  
2139  C CG  . LEU A 315  ? 0.2622 0.2343 0.2446 -0.0159 0.0111  0.0395  313  LEU A CG  
2140  C CD1 . LEU A 315  ? 0.2785 0.2485 0.2613 -0.0172 0.0108  0.0414  313  LEU A CD1 
2141  C CD2 . LEU A 315  ? 0.3214 0.2976 0.3068 -0.0167 0.0119  0.0402  313  LEU A CD2 
2142  N N   . GLU A 316  ? 0.2822 0.2610 0.2607 -0.0116 0.0144  0.0380  314  GLU A N   
2143  C CA  . GLU A 316  ? 0.3125 0.2957 0.2928 -0.0114 0.0156  0.0384  314  GLU A CA  
2144  C C   . GLU A 316  ? 0.3123 0.2966 0.2930 -0.0097 0.0154  0.0367  314  GLU A C   
2145  O O   . GLU A 316  ? 0.3075 0.2952 0.2908 -0.0096 0.0158  0.0366  314  GLU A O   
2146  C CB  . GLU A 316  ? 0.2942 0.2796 0.2728 -0.0110 0.0172  0.0394  314  GLU A CB  
2147  C CG  . GLU A 316  ? 0.2908 0.2757 0.2695 -0.0129 0.0173  0.0418  314  GLU A CG  
2148  C CD  . GLU A 316  ? 0.3356 0.3236 0.3127 -0.0127 0.0189  0.0433  314  GLU A CD  
2149  O OE1 . GLU A 316  ? 0.3380 0.3305 0.3152 -0.0116 0.0203  0.0427  314  GLU A OE1 
2150  O OE2 . GLU A 316  ? 0.3171 0.3034 0.2929 -0.0136 0.0188  0.0450  314  GLU A OE2 
2151  N N   . LEU A 317  ? 0.2754 0.2570 0.2541 -0.0084 0.0147  0.0354  315  LEU A N   
2152  C CA  . LEU A 317  ? 0.2995 0.2814 0.2790 -0.0071 0.0141  0.0341  315  LEU A CA  
2153  C C   . LEU A 317  ? 0.2420 0.2242 0.2236 -0.0079 0.0130  0.0342  315  LEU A C   
2154  O O   . LEU A 317  ? 0.2589 0.2433 0.2424 -0.0072 0.0128  0.0338  315  LEU A O   
2155  C CB  . LEU A 317  ? 0.2869 0.2654 0.2639 -0.0060 0.0134  0.0331  315  LEU A CB  
2156  C CG  . LEU A 317  ? 0.2964 0.2744 0.2742 -0.0048 0.0125  0.0323  315  LEU A CG  
2157  C CD1 . LEU A 317  ? 0.2631 0.2438 0.2425 -0.0032 0.0131  0.0316  315  LEU A CD1 
2158  C CD2 . LEU A 317  ? 0.3269 0.3015 0.3024 -0.0042 0.0119  0.0317  315  LEU A CD2 
2159  N N   . SER A 318  ? 0.2695 0.2496 0.2509 -0.0092 0.0121  0.0344  316  SER A N   
2160  C CA  . SER A 318  ? 0.2623 0.2432 0.2458 -0.0100 0.0109  0.0342  316  SER A CA  
2161  C C   . SER A 318  ? 0.2806 0.2651 0.2673 -0.0108 0.0113  0.0348  316  SER A C   
2162  O O   . SER A 318  ? 0.2521 0.2383 0.2409 -0.0110 0.0105  0.0344  316  SER A O   
2163  C CB  . SER A 318  ? 0.2713 0.2496 0.2541 -0.0111 0.0098  0.0339  316  SER A CB  
2164  O OG  . SER A 318  ? 0.2791 0.2571 0.2630 -0.0126 0.0101  0.0347  316  SER A OG  
2165  N N   . LEU A 319  ? 0.2434 0.2293 0.2307 -0.0115 0.0126  0.0359  317  LEU A N   
2166  C CA  . LEU A 319  ? 0.2665 0.2564 0.2572 -0.0125 0.0132  0.0367  317  LEU A CA  
2167  C C   . LEU A 319  ? 0.2681 0.2615 0.2600 -0.0109 0.0137  0.0360  317  LEU A C   
2168  O O   . LEU A 319  ? 0.2981 0.2947 0.2931 -0.0113 0.0135  0.0360  317  LEU A O   
2169  C CB  . LEU A 319  ? 0.2766 0.2677 0.2674 -0.0137 0.0146  0.0384  317  LEU A CB  
2170  C CG  . LEU A 319  ? 0.2996 0.2874 0.2902 -0.0155 0.0139  0.0395  317  LEU A CG  
2171  C CD1 . LEU A 319  ? 0.2562 0.2454 0.2466 -0.0166 0.0153  0.0417  317  LEU A CD1 
2172  C CD2 . LEU A 319  ? 0.2505 0.2381 0.2445 -0.0172 0.0124  0.0392  317  LEU A CD2 
2173  N N   . ASP A 320  ? 0.2925 0.2854 0.2823 -0.0089 0.0143  0.0353  318  ASP A N   
2174  C CA  . ASP A 320  ? 0.3047 0.3005 0.2959 -0.0071 0.0144  0.0343  318  ASP A CA  
2175  C C   . ASP A 320  ? 0.2855 0.2808 0.2781 -0.0066 0.0128  0.0338  318  ASP A C   
2176  O O   . ASP A 320  ? 0.2992 0.2977 0.2944 -0.0059 0.0126  0.0334  318  ASP A O   
2177  C CB  . ASP A 320  ? 0.2950 0.2898 0.2840 -0.0050 0.0150  0.0333  318  ASP A CB  
2178  C CG  . ASP A 320  ? 0.3762 0.3737 0.3646 -0.0050 0.0168  0.0337  318  ASP A CG  
2179  O OD1 . ASP A 320  ? 0.3690 0.3714 0.3598 -0.0052 0.0178  0.0340  318  ASP A OD1 
2180  O OD2 . ASP A 320  ? 0.3646 0.3599 0.3501 -0.0048 0.0172  0.0336  318  ASP A OD2 
2181  N N   . LEU A 321  ? 0.2736 0.2652 0.2642 -0.0070 0.0115  0.0336  319  LEU A N   
2182  C CA  . LEU A 321  ? 0.2658 0.2575 0.2574 -0.0067 0.0099  0.0333  319  LEU A CA  
2183  C C   . LEU A 321  ? 0.2640 0.2582 0.2583 -0.0082 0.0094  0.0335  319  LEU A C   
2184  O O   . LEU A 321  ? 0.2851 0.2819 0.2816 -0.0077 0.0085  0.0333  319  LEU A O   
2185  C CB  . LEU A 321  ? 0.3196 0.3075 0.3084 -0.0068 0.0089  0.0332  319  LEU A CB  
2186  C CG  . LEU A 321  ? 0.3302 0.3156 0.3169 -0.0052 0.0089  0.0331  319  LEU A CG  
2187  C CD1 . LEU A 321  ? 0.3605 0.3432 0.3447 -0.0056 0.0098  0.0330  319  LEU A CD1 
2188  C CD2 . LEU A 321  ? 0.3393 0.3233 0.3250 -0.0050 0.0074  0.0333  319  LEU A CD2 
2189  N N   . LEU A 322  ? 0.2572 0.2507 0.2518 -0.0101 0.0097  0.0339  320  LEU A N   
2190  C CA  . LEU A 322  ? 0.2550 0.2507 0.2527 -0.0118 0.0089  0.0339  320  LEU A CA  
2191  C C   . LEU A 322  ? 0.2403 0.2408 0.2414 -0.0117 0.0097  0.0343  320  LEU A C   
2192  O O   . LEU A 322  ? 0.2565 0.2597 0.2604 -0.0120 0.0087  0.0338  320  LEU A O   
2193  C CB  . LEU A 322  ? 0.2540 0.2477 0.2517 -0.0138 0.0091  0.0345  320  LEU A CB  
2194  C CG  . LEU A 322  ? 0.3195 0.3148 0.3210 -0.0158 0.0081  0.0344  320  LEU A CG  
2195  C CD1 . LEU A 322  ? 0.2597 0.2544 0.2611 -0.0156 0.0060  0.0328  320  LEU A CD1 
2196  C CD2 . LEU A 322  ? 0.2610 0.2543 0.2632 -0.0178 0.0084  0.0354  320  LEU A CD2 
2197  N N   . GLU A 323  ? 0.2570 0.2590 0.2580 -0.0111 0.0114  0.0349  321  GLU A N   
2198  C CA  . GLU A 323  ? 0.3057 0.3130 0.3100 -0.0109 0.0124  0.0351  321  GLU A CA  
2199  C C   . GLU A 323  ? 0.3072 0.3166 0.3127 -0.0089 0.0115  0.0340  321  GLU A C   
2200  O O   . GLU A 323  ? 0.2923 0.3056 0.3013 -0.0092 0.0111  0.0339  321  GLU A O   
2201  C CB  . GLU A 323  ? 0.3250 0.3338 0.3282 -0.0105 0.0145  0.0357  321  GLU A CB  
2202  C CG  . GLU A 323  ? 0.3650 0.3798 0.3711 -0.0093 0.0156  0.0354  321  GLU A CG  
2203  C CD  . GLU A 323  ? 0.4121 0.4310 0.4199 -0.0111 0.0174  0.0369  321  GLU A CD  
2204  O OE1 . GLU A 323  ? 0.5146 0.5314 0.5206 -0.0126 0.0180  0.0383  321  GLU A OE1 
2205  O OE2 . GLU A 323  ? 0.4783 0.5029 0.4894 -0.0109 0.0181  0.0369  321  GLU A OE2 
2206  N N   . VAL A 324  ? 0.2791 0.2858 0.2821 -0.0068 0.0111  0.0334  322  VAL A N   
2207  C CA  . VAL A 324  ? 0.2483 0.2564 0.2527 -0.0048 0.0100  0.0327  322  VAL A CA  
2208  C C   . VAL A 324  ? 0.2738 0.2824 0.2794 -0.0056 0.0081  0.0327  322  VAL A C   
2209  O O   . VAL A 324  ? 0.3354 0.3477 0.3441 -0.0049 0.0074  0.0324  322  VAL A O   
2210  C CB  . VAL A 324  ? 0.2755 0.2799 0.2771 -0.0028 0.0096  0.0323  322  VAL A CB  
2211  C CG1 . VAL A 324  ? 0.3294 0.3348 0.3327 -0.0008 0.0081  0.0320  322  VAL A CG1 
2212  C CG2 . VAL A 324  ? 0.2937 0.2984 0.2945 -0.0017 0.0113  0.0318  322  VAL A CG2 
2213  N N   . LEU A 325  ? 0.2587 0.2640 0.2621 -0.0068 0.0072  0.0328  323  LEU A N   
2214  C CA  . LEU A 325  ? 0.2819 0.2880 0.2861 -0.0073 0.0054  0.0325  323  LEU A CA  
2215  C C   . LEU A 325  ? 0.2713 0.2815 0.2794 -0.0088 0.0052  0.0323  323  LEU A C   
2216  O O   . LEU A 325  ? 0.2505 0.2637 0.2608 -0.0085 0.0039  0.0319  323  LEU A O   
2217  C CB  . LEU A 325  ? 0.2677 0.2701 0.2688 -0.0083 0.0046  0.0324  323  LEU A CB  
2218  C CG  . LEU A 325  ? 0.3034 0.3021 0.3009 -0.0071 0.0045  0.0327  323  LEU A CG  
2219  C CD1 . LEU A 325  ? 0.2622 0.2578 0.2570 -0.0083 0.0043  0.0324  323  LEU A CD1 
2220  C CD2 . LEU A 325  ? 0.2408 0.2405 0.2381 -0.0056 0.0030  0.0330  323  LEU A CD2 
2221  N N   . CYS A 326  ? 0.2826 0.2929 0.2918 -0.0107 0.0064  0.0327  324  CYS A N   
2222  C CA  . CYS A 326  ? 0.2917 0.3056 0.3051 -0.0125 0.0061  0.0326  324  CYS A CA  
2223  C C   . CYS A 326  ? 0.3031 0.3223 0.3200 -0.0117 0.0067  0.0327  324  CYS A C   
2224  O O   . CYS A 326  ? 0.2763 0.2992 0.2970 -0.0127 0.0059  0.0323  324  CYS A O   
2225  C CB  . CYS A 326  ? 0.2770 0.2894 0.2909 -0.0149 0.0071  0.0334  324  CYS A CB  
2226  S SG  . CYS A 326  ? 0.3397 0.3468 0.3512 -0.0162 0.0056  0.0327  324  CYS A SG  
2227  N N   . LEU A 327  ? 0.2884 0.3083 0.3043 -0.0097 0.0080  0.0328  325  LEU A N   
2228  C CA  . LEU A 327  ? 0.2846 0.3098 0.3038 -0.0084 0.0085  0.0326  325  LEU A CA  
2229  C C   . LEU A 327  ? 0.2957 0.3215 0.3152 -0.0059 0.0069  0.0318  325  LEU A C   
2230  O O   . LEU A 327  ? 0.2815 0.3118 0.3042 -0.0046 0.0070  0.0314  325  LEU A O   
2231  C CB  . LEU A 327  ? 0.3440 0.3704 0.3626 -0.0075 0.0108  0.0329  325  LEU A CB  
2232  C CG  . LEU A 327  ? 0.3675 0.3945 0.3862 -0.0099 0.0126  0.0341  325  LEU A CG  
2233  C CD1 . LEU A 327  ? 0.3952 0.4232 0.4122 -0.0086 0.0147  0.0342  325  LEU A CD1 
2234  C CD2 . LEU A 327  ? 0.3815 0.4136 0.4050 -0.0121 0.0128  0.0347  325  LEU A CD2 
2235  N N   . ASP A 328  ? 0.2872 0.3089 0.3037 -0.0053 0.0054  0.0318  326  ASP A N   
2236  C CA  . ASP A 328  ? 0.2806 0.3025 0.2971 -0.0030 0.0038  0.0316  326  ASP A CA  
2237  C C   . ASP A 328  ? 0.2555 0.2813 0.2749 -0.0035 0.0020  0.0313  326  ASP A C   
2238  O O   . ASP A 328  ? 0.2970 0.3222 0.3159 -0.0052 0.0010  0.0311  326  ASP A O   
2239  C CB  . ASP A 328  ? 0.3014 0.3181 0.3136 -0.0025 0.0029  0.0321  326  ASP A CB  
2240  C CG  . ASP A 328  ? 0.3494 0.3658 0.3615 -0.0001 0.0013  0.0325  326  ASP A CG  
2241  O OD1 . ASP A 328  ? 0.3487 0.3685 0.3632 0.0006  -0.0001 0.0325  326  ASP A OD1 
2242  O OD2 . ASP A 328  ? 0.3495 0.3622 0.3593 0.0012  0.0014  0.0330  326  ASP A OD2 
2243  N N   . GLY A 329  ? 0.2815 0.3115 0.3042 -0.0018 0.0016  0.0310  327  GLY A N   
2244  C CA  . GLY A 329  ? 0.2760 0.3104 0.3019 -0.0021 -0.0001 0.0306  327  GLY A CA  
2245  C C   . GLY A 329  ? 0.2989 0.3318 0.3227 -0.0017 -0.0024 0.0308  327  GLY A C   
2246  O O   . GLY A 329  ? 0.2778 0.3135 0.3032 -0.0028 -0.0039 0.0302  327  GLY A O   
2247  N N   . ASP A 330  ? 0.2857 0.3145 0.3059 -0.0003 -0.0029 0.0317  328  ASP A N   
2248  C CA  . ASP A 330  ? 0.3228 0.3507 0.3406 0.0000  -0.0050 0.0323  328  ASP A CA  
2249  C C   . ASP A 330  ? 0.2577 0.2847 0.2737 -0.0024 -0.0053 0.0316  328  ASP A C   
2250  O O   . ASP A 330  ? 0.2698 0.2981 0.2847 -0.0024 -0.0071 0.0315  328  ASP A O   
2251  C CB  . ASP A 330  ? 0.3342 0.3577 0.3486 0.0016  -0.0053 0.0337  328  ASP A CB  
2252  C CG  . ASP A 330  ? 0.3798 0.4039 0.3963 0.0042  -0.0058 0.0343  328  ASP A CG  
2253  O OD1 . ASP A 330  ? 0.4206 0.4491 0.4407 0.0052  -0.0066 0.0339  328  ASP A OD1 
2254  O OD2 . ASP A 330  ? 0.3970 0.4171 0.4118 0.0054  -0.0054 0.0351  328  ASP A OD2 
2255  N N   . LEU A 331  ? 0.2550 0.2801 0.2707 -0.0042 -0.0036 0.0310  329  LEU A N   
2256  C CA  . LEU A 331  ? 0.2615 0.2852 0.2759 -0.0063 -0.0040 0.0301  329  LEU A CA  
2257  C C   . LEU A 331  ? 0.2991 0.3263 0.3175 -0.0083 -0.0044 0.0288  329  LEU A C   
2258  O O   . LEU A 331  ? 0.2747 0.3007 0.2929 -0.0101 -0.0048 0.0278  329  LEU A O   
2259  C CB  . LEU A 331  ? 0.2408 0.2597 0.2523 -0.0072 -0.0023 0.0304  329  LEU A CB  
2260  C CG  . LEU A 331  ? 0.2412 0.2562 0.2482 -0.0059 -0.0024 0.0314  329  LEU A CG  
2261  C CD1 . LEU A 331  ? 0.2406 0.2514 0.2455 -0.0065 -0.0005 0.0317  329  LEU A CD1 
2262  C CD2 . LEU A 331  ? 0.2418 0.2569 0.2465 -0.0062 -0.0041 0.0309  329  LEU A CD2 
2263  N N   . SER A 332  ? 0.3146 0.3462 0.3371 -0.0079 -0.0043 0.0288  330  SER A N   
2264  C CA  . SER A 332  ? 0.3137 0.3488 0.3407 -0.0099 -0.0045 0.0278  330  SER A CA  
2265  C C   . SER A 332  ? 0.2955 0.3325 0.3233 -0.0108 -0.0070 0.0263  330  SER A C   
2266  O O   . SER A 332  ? 0.2753 0.3129 0.3008 -0.0092 -0.0086 0.0261  330  SER A O   
2267  C CB  . SER A 332  ? 0.3168 0.3569 0.3482 -0.0091 -0.0040 0.0281  330  SER A CB  
2268  O OG  . SER A 332  ? 0.3723 0.4151 0.4040 -0.0068 -0.0057 0.0281  330  SER A OG  
2269  N N   . GLY A 333  ? 0.2716 0.3097 0.3027 -0.0132 -0.0073 0.0251  331  GLY A N   
2270  C CA  . GLY A 333  ? 0.3126 0.3528 0.3451 -0.0141 -0.0098 0.0231  331  GLY A CA  
2271  C C   . GLY A 333  ? 0.2868 0.3231 0.3157 -0.0147 -0.0106 0.0219  331  GLY A C   
2272  O O   . GLY A 333  ? 0.2652 0.3033 0.2948 -0.0152 -0.0128 0.0198  331  GLY A O   
2273  N N   . TRP A 334  ? 0.2823 0.3136 0.3077 -0.0147 -0.0090 0.0229  332  TRP A N   
2274  C CA  . TRP A 334  ? 0.2612 0.2889 0.2832 -0.0150 -0.0096 0.0218  332  TRP A CA  
2275  C C   . TRP A 334  ? 0.2656 0.2889 0.2878 -0.0167 -0.0080 0.0223  332  TRP A C   
2276  O O   . TRP A 334  ? 0.2845 0.3061 0.3060 -0.0164 -0.0059 0.0243  332  TRP A O   
2277  C CB  . TRP A 334  ? 0.2733 0.2994 0.2899 -0.0128 -0.0094 0.0229  332  TRP A CB  
2278  C CG  . TRP A 334  ? 0.2440 0.2662 0.2566 -0.0129 -0.0093 0.0223  332  TRP A CG  
2279  C CD1 . TRP A 334  ? 0.2752 0.2979 0.2866 -0.0132 -0.0110 0.0201  332  TRP A CD1 
2280  C CD2 . TRP A 334  ? 0.2432 0.2609 0.2524 -0.0125 -0.0075 0.0238  332  TRP A CD2 
2281  N NE1 . TRP A 334  ? 0.2463 0.2653 0.2539 -0.0129 -0.0103 0.0201  332  TRP A NE1 
2282  C CE2 . TRP A 334  ? 0.2438 0.2596 0.2501 -0.0126 -0.0082 0.0225  332  TRP A CE2 
2283  C CE3 . TRP A 334  ? 0.2422 0.2578 0.2507 -0.0119 -0.0055 0.0259  332  TRP A CE3 
2284  C CZ2 . TRP A 334  ? 0.2434 0.2550 0.2461 -0.0123 -0.0069 0.0233  332  TRP A CZ2 
2285  C CZ3 . TRP A 334  ? 0.2752 0.2864 0.2801 -0.0116 -0.0043 0.0266  332  TRP A CZ3 
2286  C CH2 . TRP A 334  ? 0.2456 0.2549 0.2478 -0.0118 -0.0050 0.0255  332  TRP A CH2 
2287  N N   . ASN A 335  ? 0.2479 0.2695 0.2715 -0.0184 -0.0091 0.0205  333  ASN A N   
2288  C CA  . ASN A 335  ? 0.2803 0.2976 0.3046 -0.0201 -0.0080 0.0211  333  ASN A CA  
2289  C C   . ASN A 335  ? 0.2863 0.2992 0.3062 -0.0195 -0.0082 0.0203  333  ASN A C   
2290  O O   . ASN A 335  ? 0.2812 0.2905 0.3020 -0.0209 -0.0081 0.0201  333  ASN A O   
2291  C CB  . ASN A 335  ? 0.2997 0.3178 0.3296 -0.0227 -0.0094 0.0198  333  ASN A CB  
2292  C CG  . ASN A 335  ? 0.3231 0.3450 0.3578 -0.0239 -0.0085 0.0213  333  ASN A CG  
2293  O OD1 . ASN A 335  ? 0.3102 0.3325 0.3442 -0.0235 -0.0063 0.0237  333  ASN A OD1 
2294  N ND2 . ASN A 335  ? 0.3357 0.3606 0.3754 -0.0254 -0.0103 0.0197  333  ASN A ND2 
2295  N N   . GLY A 336  ? 0.2477 0.2611 0.2633 -0.0175 -0.0085 0.0200  334  GLY A N   
2296  C CA  . GLY A 336  ? 0.2455 0.2559 0.2573 -0.0169 -0.0087 0.0191  334  GLY A CA  
2297  C C   . GLY A 336  ? 0.2727 0.2788 0.2813 -0.0165 -0.0066 0.0211  334  GLY A C   
2298  O O   . GLY A 336  ? 0.2496 0.2530 0.2553 -0.0161 -0.0068 0.0203  334  GLY A O   
2299  N N   . MET A 337  ? 0.2591 0.2649 0.2682 -0.0165 -0.0048 0.0234  335  MET A N   
2300  C CA  A MET A 337  ? 0.2566 0.2587 0.2627 -0.0160 -0.0029 0.0251  335  MET A CA  
2301  C CA  B MET A 337  ? 0.2563 0.2585 0.2624 -0.0160 -0.0029 0.0251  335  MET A CA  
2302  C C   . MET A 337  ? 0.2723 0.2708 0.2793 -0.0176 -0.0026 0.0250  335  MET A C   
2303  O O   . MET A 337  ? 0.2518 0.2505 0.2626 -0.0193 -0.0026 0.0252  335  MET A O   
2304  C CB  A MET A 337  ? 0.2836 0.2870 0.2904 -0.0154 -0.0011 0.0272  335  MET A CB  
2305  C CB  B MET A 337  ? 0.2850 0.2883 0.2918 -0.0154 -0.0011 0.0272  335  MET A CB  
2306  C CG  A MET A 337  ? 0.3078 0.3079 0.3115 -0.0147 0.0007  0.0287  335  MET A CG  
2307  C CG  B MET A 337  ? 0.3111 0.3108 0.3152 -0.0151 0.0008  0.0287  335  MET A CG  
2308  S SD  A MET A 337  ? 0.3260 0.3242 0.3248 -0.0128 0.0005  0.0286  335  MET A SD  
2309  S SD  B MET A 337  ? 0.3269 0.3271 0.3284 -0.0127 0.0019  0.0300  335  MET A SD  
2310  C CE  A MET A 337  ? 0.2751 0.2762 0.2742 -0.0110 0.0006  0.0298  335  MET A CE  
2311  C CE  B MET A 337  ? 0.2756 0.2759 0.2741 -0.0115 0.0001  0.0291  335  MET A CE  
2312  N N   . GLY A 338  ? 0.2706 0.2656 0.2741 -0.0170 -0.0023 0.0247  336  GLY A N   
2313  C CA  . GLY A 338  ? 0.2456 0.2369 0.2496 -0.0181 -0.0023 0.0245  336  GLY A CA  
2314  C C   . GLY A 338  ? 0.2441 0.2322 0.2448 -0.0175 -0.0005 0.0263  336  GLY A C   
2315  O O   . GLY A 338  ? 0.2428 0.2314 0.2405 -0.0160 0.0004  0.0270  336  GLY A O   
2316  N N   . PHE A 339  ? 0.2451 0.2303 0.2468 -0.0187 0.0000  0.0271  337  PHE A N   
2317  C CA  . PHE A 339  ? 0.2448 0.2274 0.2437 -0.0183 0.0016  0.0288  337  PHE A CA  
2318  C C   . PHE A 339  ? 0.2488 0.2275 0.2482 -0.0192 0.0010  0.0286  337  PHE A C   
2319  O O   . PHE A 339  ? 0.2764 0.2544 0.2794 -0.0209 0.0001  0.0287  337  PHE A O   
2320  C CB  . PHE A 339  ? 0.2444 0.2289 0.2446 -0.0187 0.0034  0.0311  337  PHE A CB  
2321  C CG  . PHE A 339  ? 0.2440 0.2268 0.2409 -0.0178 0.0052  0.0326  337  PHE A CG  
2322  C CD1 . PHE A 339  ? 0.2931 0.2768 0.2872 -0.0159 0.0060  0.0325  337  PHE A CD1 
2323  C CD2 . PHE A 339  ? 0.2452 0.2261 0.2422 -0.0188 0.0060  0.0342  337  PHE A CD2 
2324  C CE1 . PHE A 339  ? 0.2887 0.2710 0.2802 -0.0151 0.0074  0.0335  337  PHE A CE1 
2325  C CE2 . PHE A 339  ? 0.2995 0.2794 0.2934 -0.0178 0.0076  0.0353  337  PHE A CE2 
2326  C CZ  . PHE A 339  ? 0.2735 0.2542 0.2647 -0.0160 0.0082  0.0348  337  PHE A CZ  
2327  N N   . VAL A 340  ? 0.2804 0.2565 0.2763 -0.0182 0.0014  0.0285  338  VAL A N   
2328  C CA  . VAL A 340  ? 0.2884 0.2606 0.2844 -0.0187 0.0007  0.0283  338  VAL A CA  
2329  C C   . VAL A 340  ? 0.2607 0.2315 0.2562 -0.0193 0.0023  0.0312  338  VAL A C   
2330  O O   . VAL A 340  ? 0.2609 0.2328 0.2539 -0.0184 0.0040  0.0324  338  VAL A O   
2331  C CB  . VAL A 340  ? 0.2592 0.2299 0.2519 -0.0172 0.0002  0.0265  338  VAL A CB  
2332  C CG1 . VAL A 340  ? 0.2635 0.2304 0.2565 -0.0175 -0.0006 0.0263  338  VAL A CG1 
2333  C CG2 . VAL A 340  ? 0.2495 0.2225 0.2423 -0.0165 -0.0013 0.0238  338  VAL A CG2 
2334  N N   . VAL A 341  ? 0.2688 0.2372 0.2669 -0.0208 0.0016  0.0321  339  VAL A N   
2335  C CA  . VAL A 341  ? 0.2558 0.2225 0.2531 -0.0214 0.0028  0.0349  339  VAL A CA  
2336  C C   . VAL A 341  ? 0.2684 0.2307 0.2655 -0.0213 0.0015  0.0344  339  VAL A C   
2337  O O   . VAL A 341  ? 0.2607 0.2212 0.2606 -0.0219 -0.0006 0.0326  339  VAL A O   
2338  C CB  . VAL A 341  ? 0.2836 0.2520 0.2845 -0.0235 0.0035  0.0375  339  VAL A CB  
2339  C CG1 . VAL A 341  ? 0.2766 0.2498 0.2783 -0.0234 0.0046  0.0375  339  VAL A CG1 
2340  C CG2 . VAL A 341  ? 0.3557 0.3221 0.3613 -0.0254 0.0014  0.0372  339  VAL A CG2 
2341  N N   . GLN A 342  ? 0.2543 0.2150 0.2484 -0.0206 0.0024  0.0358  340  GLN A N   
2342  C CA  . GLN A 342  ? 0.2938 0.2505 0.2871 -0.0201 0.0012  0.0351  340  GLN A CA  
2343  C C   . GLN A 342  ? 0.2592 0.2135 0.2545 -0.0216 0.0010  0.0382  340  GLN A C   
2344  O O   . GLN A 342  ? 0.2783 0.2338 0.2719 -0.0218 0.0027  0.0410  340  GLN A O   
2345  C CB  . GLN A 342  ? 0.2542 0.2108 0.2429 -0.0181 0.0022  0.0346  340  GLN A CB  
2346  C CG  . GLN A 342  ? 0.2515 0.2102 0.2382 -0.0168 0.0023  0.0320  340  GLN A CG  
2347  C CD  . GLN A 342  ? 0.2496 0.2094 0.2324 -0.0154 0.0039  0.0325  340  GLN A CD  
2348  O OE1 . GLN A 342  ? 0.2493 0.2105 0.2312 -0.0156 0.0054  0.0344  340  GLN A OE1 
2349  N NE2 . GLN A 342  ? 0.2728 0.2321 0.2533 -0.0141 0.0035  0.0307  340  GLN A NE2 
2350  N N   . ALA A 343  ? 0.2619 0.2131 0.2608 -0.0225 -0.0012 0.0376  341  ALA A N   
2351  C CA  . ALA A 343  ? 0.2655 0.2142 0.2669 -0.0242 -0.0016 0.0409  341  ALA A CA  
2352  C C   . ALA A 343  ? 0.2883 0.2346 0.2866 -0.0232 -0.0014 0.0424  341  ALA A C   
2353  O O   . ALA A 343  ? 0.2932 0.2383 0.2923 -0.0244 -0.0012 0.0461  341  ALA A O   
2354  C CB  . ALA A 343  ? 0.2855 0.2310 0.2921 -0.0255 -0.0044 0.0397  341  ALA A CB  
2355  N N   . TYR A 344  ? 0.2706 0.2163 0.2654 -0.0210 -0.0015 0.0400  342  TYR A N   
2356  C CA  . TYR A 344  ? 0.2971 0.2410 0.2891 -0.0201 -0.0011 0.0417  342  TYR A CA  
2357  C C   . TYR A 344  ? 0.3092 0.2564 0.2977 -0.0200 0.0015  0.0443  342  TYR A C   
2358  O O   . TYR A 344  ? 0.2948 0.2411 0.2805 -0.0193 0.0019  0.0458  342  TYR A O   
2359  C CB  . TYR A 344  ? 0.2893 0.2316 0.2789 -0.0179 -0.0021 0.0384  342  TYR A CB  
2360  C CG  . TYR A 344  ? 0.2806 0.2260 0.2664 -0.0163 -0.0007 0.0362  342  TYR A CG  
2361  C CD1 . TYR A 344  ? 0.2902 0.2392 0.2748 -0.0166 0.0012  0.0366  342  TYR A CD1 
2362  C CD2 . TYR A 344  ? 0.2806 0.2252 0.2645 -0.0145 -0.0013 0.0336  342  TYR A CD2 
2363  C CE1 . TYR A 344  ? 0.2822 0.2334 0.2638 -0.0152 0.0022  0.0348  342  TYR A CE1 
2364  C CE2 . TYR A 344  ? 0.3095 0.2567 0.2904 -0.0133 -0.0002 0.0319  342  TYR A CE2 
2365  C CZ  . TYR A 344  ? 0.2906 0.2408 0.2703 -0.0137 0.0015  0.0326  342  TYR A CZ  
2366  O OH  . TYR A 344  ? 0.2800 0.2324 0.2572 -0.0126 0.0024  0.0312  342  TYR A OH  
2367  N N   . GLY A 345  ? 0.2639 0.2149 0.2525 -0.0206 0.0030  0.0446  343  GLY A N   
2368  C CA  . GLY A 345  ? 0.2795 0.2340 0.2650 -0.0202 0.0054  0.0464  343  GLY A CA  
2369  C C   . GLY A 345  ? 0.3083 0.2645 0.2955 -0.0222 0.0063  0.0503  343  GLY A C   
2370  O O   . GLY A 345  ? 0.3054 0.2616 0.2968 -0.0241 0.0056  0.0513  343  GLY A O   
2371  N N   . LYS A 346  ? 0.2680 0.2260 0.2521 -0.0217 0.0078  0.0526  344  LYS A N   
2372  C CA  . LYS A 346  ? 0.2791 0.2395 0.2644 -0.0235 0.0089  0.0568  344  LYS A CA  
2373  C C   . LYS A 346  ? 0.3030 0.2684 0.2901 -0.0245 0.0106  0.0573  344  LYS A C   
2374  O O   . LYS A 346  ? 0.2994 0.2671 0.2888 -0.0266 0.0112  0.0607  344  LYS A O   
2375  C CB  . LYS A 346  ? 0.3156 0.2775 0.2966 -0.0225 0.0101  0.0586  344  LYS A CB  
2376  C CG  . LYS A 346  ? 0.3273 0.2845 0.3074 -0.0219 0.0083  0.0592  344  LYS A CG  
2377  C CD  . LYS A 346  ? 0.3380 0.2970 0.3133 -0.0204 0.0094  0.0602  344  LYS A CD  
2378  C CE  . LYS A 346  ? 0.3461 0.3007 0.3206 -0.0198 0.0076  0.0610  344  LYS A CE  
2379  N NZ  . LYS A 346  ? 0.3435 0.3005 0.3134 -0.0183 0.0086  0.0620  344  LYS A NZ  
2380  N N   . ARG A 347  ? 0.2755 0.2428 0.2617 -0.0232 0.0112  0.0542  345  ARG A N   
2381  C CA  . ARG A 347  ? 0.2839 0.2562 0.2719 -0.0239 0.0126  0.0544  345  ARG A CA  
2382  C C   . ARG A 347  ? 0.2778 0.2495 0.2706 -0.0255 0.0113  0.0536  345  ARG A C   
2383  O O   . ARG A 347  ? 0.2941 0.2699 0.2891 -0.0264 0.0124  0.0542  345  ARG A O   
2384  C CB  . ARG A 347  ? 0.2635 0.2383 0.2485 -0.0215 0.0138  0.0516  345  ARG A CB  
2385  C CG  . ARG A 347  ? 0.2772 0.2539 0.2580 -0.0201 0.0153  0.0523  345  ARG A CG  
2386  C CD  . ARG A 347  ? 0.2563 0.2337 0.2344 -0.0177 0.0158  0.0492  345  ARG A CD  
2387  N NE  . ARG A 347  ? 0.2785 0.2514 0.2551 -0.0166 0.0143  0.0469  345  ARG A NE  
2388  C CZ  . ARG A 347  ? 0.2896 0.2622 0.2645 -0.0149 0.0142  0.0443  345  ARG A CZ  
2389  N NH1 . ARG A 347  ? 0.2540 0.2300 0.2285 -0.0138 0.0154  0.0433  345  ARG A NH1 
2390  N NH2 . ARG A 347  ? 0.2761 0.2449 0.2498 -0.0142 0.0129  0.0425  345  ARG A NH2 
2391  N N   . CYS A 348  ? 0.2622 0.2292 0.2566 -0.0257 0.0091  0.0521  346  CYS A N   
2392  C CA  . CYS A 348  ? 0.2876 0.2539 0.2860 -0.0267 0.0076  0.0502  346  CYS A CA  
2393  C C   . CYS A 348  ? 0.2670 0.2365 0.2700 -0.0292 0.0080  0.0525  346  CYS A C   
2394  O O   . CYS A 348  ? 0.2857 0.2581 0.2906 -0.0292 0.0081  0.0508  346  CYS A O   
2395  C CB  . CYS A 348  ? 0.2812 0.2420 0.2810 -0.0268 0.0050  0.0487  346  CYS A CB  
2396  S SG  . CYS A 348  ? 0.3573 0.3179 0.3610 -0.0271 0.0030  0.0450  346  CYS A SG  
2397  N N   . PRO A 349  ? 0.2852 0.2545 0.2904 -0.0313 0.0081  0.0563  347  PRO A N   
2398  C CA  . PRO A 349  ? 0.2955 0.2683 0.3056 -0.0339 0.0085  0.0584  347  PRO A CA  
2399  C C   . PRO A 349  ? 0.2834 0.2629 0.2924 -0.0335 0.0111  0.0589  347  PRO A C   
2400  O O   . PRO A 349  ? 0.3109 0.2938 0.3237 -0.0348 0.0112  0.0587  347  PRO A O   
2401  C CB  . PRO A 349  ? 0.3193 0.2902 0.3313 -0.0363 0.0082  0.0629  347  PRO A CB  
2402  C CG  . PRO A 349  ? 0.3110 0.2795 0.3180 -0.0345 0.0085  0.0636  347  PRO A CG  
2403  C CD  . PRO A 349  ? 0.2696 0.2358 0.2732 -0.0316 0.0079  0.0591  347  PRO A CD  
2404  N N   . PHE A 350  ? 0.3032 0.2851 0.3075 -0.0317 0.0130  0.0593  348  PHE A N   
2405  C CA  . PHE A 350  ? 0.2963 0.2846 0.2996 -0.0308 0.0153  0.0592  348  PHE A CA  
2406  C C   . PHE A 350  ? 0.2667 0.2556 0.2694 -0.0288 0.0150  0.0551  348  PHE A C   
2407  O O   . PHE A 350  ? 0.2953 0.2891 0.2997 -0.0287 0.0161  0.0546  348  PHE A O   
2408  C CB  . PHE A 350  ? 0.2972 0.2876 0.2957 -0.0293 0.0172  0.0605  348  PHE A CB  
2409  C CG  . PHE A 350  ? 0.2971 0.2860 0.2955 -0.0310 0.0172  0.0646  348  PHE A CG  
2410  C CD1 . PHE A 350  ? 0.3305 0.3240 0.3315 -0.0335 0.0185  0.0686  348  PHE A CD1 
2411  C CD2 . PHE A 350  ? 0.2967 0.2799 0.2927 -0.0303 0.0157  0.0645  348  PHE A CD2 
2412  C CE1 . PHE A 350  ? 0.3770 0.3691 0.3781 -0.0352 0.0183  0.0728  348  PHE A CE1 
2413  C CE2 . PHE A 350  ? 0.3192 0.3009 0.3153 -0.0319 0.0155  0.0684  348  PHE A CE2 
2414  C CZ  . PHE A 350  ? 0.3515 0.3376 0.3501 -0.0343 0.0167  0.0727  348  PHE A CZ  
2415  N N   . VAL A 351  ? 0.2578 0.2420 0.2584 -0.0272 0.0135  0.0524  349  VAL A N   
2416  C CA  . VAL A 351  ? 0.2549 0.2393 0.2553 -0.0256 0.0128  0.0490  349  VAL A CA  
2417  C C   . VAL A 351  ? 0.2552 0.2406 0.2606 -0.0274 0.0115  0.0484  349  VAL A C   
2418  O O   . VAL A 351  ? 0.2777 0.2666 0.2843 -0.0268 0.0118  0.0470  349  VAL A O   
2419  C CB  . VAL A 351  ? 0.2537 0.2334 0.2510 -0.0239 0.0114  0.0465  349  VAL A CB  
2420  C CG1 . VAL A 351  ? 0.2511 0.2314 0.2482 -0.0225 0.0107  0.0434  349  VAL A CG1 
2421  C CG2 . VAL A 351  ? 0.2539 0.2329 0.2465 -0.0222 0.0126  0.0469  349  VAL A CG2 
2422  N N   . LEU A 352  ? 0.2781 0.2605 0.2867 -0.0295 0.0100  0.0495  350  LEU A N   
2423  C CA  . LEU A 352  ? 0.2580 0.2412 0.2717 -0.0313 0.0086  0.0488  350  LEU A CA  
2424  C C   . LEU A 352  ? 0.3039 0.2932 0.3209 -0.0328 0.0102  0.0509  350  LEU A C   
2425  O O   . LEU A 352  ? 0.2893 0.2817 0.3092 -0.0331 0.0097  0.0494  350  LEU A O   
2426  C CB  . LEU A 352  ? 0.3028 0.2812 0.3196 -0.0333 0.0064  0.0495  350  LEU A CB  
2427  C CG  . LEU A 352  ? 0.3120 0.2853 0.3268 -0.0317 0.0044  0.0464  350  LEU A CG  
2428  C CD1 . LEU A 352  ? 0.3277 0.2960 0.3457 -0.0334 0.0022  0.0471  350  LEU A CD1 
2429  C CD2 . LEU A 352  ? 0.2769 0.2516 0.2924 -0.0306 0.0032  0.0426  350  LEU A CD2 
2430  N N   . ASP A 353  ? 0.2831 0.2747 0.2997 -0.0339 0.0120  0.0544  351  ASP A N   
2431  C CA  . ASP A 353  ? 0.2949 0.2932 0.3141 -0.0351 0.0139  0.0564  351  ASP A CA  
2432  C C   . ASP A 353  ? 0.2932 0.2959 0.3109 -0.0326 0.0150  0.0538  351  ASP A C   
2433  O O   . ASP A 353  ? 0.3178 0.3250 0.3391 -0.0333 0.0152  0.0534  351  ASP A O   
2434  C CB  . ASP A 353  ? 0.2624 0.2633 0.2800 -0.0359 0.0160  0.0603  351  ASP A CB  
2435  C CG  . ASP A 353  ? 0.3137 0.3119 0.3344 -0.0390 0.0151  0.0639  351  ASP A CG  
2436  O OD1 . ASP A 353  ? 0.3368 0.3319 0.3620 -0.0408 0.0129  0.0634  351  ASP A OD1 
2437  O OD2 . ASP A 353  ? 0.4167 0.4158 0.4353 -0.0395 0.0164  0.0672  351  ASP A OD2 
2438  N N   . PHE A 354  ? 0.2658 0.2672 0.2784 -0.0298 0.0156  0.0521  352  PHE A N   
2439  C CA  . PHE A 354  ? 0.2756 0.2804 0.2868 -0.0273 0.0164  0.0498  352  PHE A CA  
2440  C C   . PHE A 354  ? 0.2507 0.2548 0.2641 -0.0269 0.0145  0.0471  352  PHE A C   
2441  O O   . PHE A 354  ? 0.2665 0.2751 0.2820 -0.0263 0.0149  0.0461  352  PHE A O   
2442  C CB  . PHE A 354  ? 0.2513 0.2540 0.2570 -0.0246 0.0170  0.0485  352  PHE A CB  
2443  C CG  . PHE A 354  ? 0.2925 0.2968 0.2969 -0.0219 0.0172  0.0458  352  PHE A CG  
2444  C CD1 . PHE A 354  ? 0.3051 0.3150 0.3096 -0.0206 0.0190  0.0457  352  PHE A CD1 
2445  C CD2 . PHE A 354  ? 0.2748 0.2755 0.2780 -0.0207 0.0154  0.0434  352  PHE A CD2 
2446  C CE1 . PHE A 354  ? 0.3518 0.3628 0.3555 -0.0181 0.0188  0.0433  352  PHE A CE1 
2447  C CE2 . PHE A 354  ? 0.3057 0.3077 0.3079 -0.0183 0.0154  0.0413  352  PHE A CE2 
2448  C CZ  . PHE A 354  ? 0.3127 0.3196 0.3153 -0.0170 0.0170  0.0413  352  PHE A CZ  
2449  N N   . ILE A 355  ? 0.2509 0.2496 0.2639 -0.0272 0.0124  0.0457  353  ILE A N   
2450  C CA  . ILE A 355  ? 0.2494 0.2478 0.2639 -0.0266 0.0106  0.0429  353  ILE A CA  
2451  C C   . ILE A 355  ? 0.2614 0.2631 0.2816 -0.0288 0.0098  0.0433  353  ILE A C   
2452  O O   . ILE A 355  ? 0.2700 0.2748 0.2920 -0.0281 0.0092  0.0416  353  ILE A O   
2453  C CB  . ILE A 355  ? 0.2496 0.2422 0.2622 -0.0262 0.0086  0.0412  353  ILE A CB  
2454  C CG1 . ILE A 355  ? 0.2684 0.2585 0.2756 -0.0238 0.0092  0.0405  353  ILE A CG1 
2455  C CG2 . ILE A 355  ? 0.2487 0.2418 0.2632 -0.0259 0.0065  0.0384  353  ILE A CG2 
2456  C CD1 . ILE A 355  ? 0.2723 0.2572 0.2775 -0.0234 0.0075  0.0388  353  ILE A CD1 
2457  N N   . ILE A 356  ? 0.2616 0.2626 0.2850 -0.0316 0.0097  0.0456  354  ILE A N   
2458  C CA  . ILE A 356  ? 0.2616 0.2657 0.2911 -0.0340 0.0088  0.0460  354  ILE A CA  
2459  C C   . ILE A 356  ? 0.2652 0.2764 0.2964 -0.0339 0.0108  0.0469  354  ILE A C   
2460  O O   . ILE A 356  ? 0.2638 0.2785 0.2986 -0.0343 0.0100  0.0457  354  ILE A O   
2461  C CB  . ILE A 356  ? 0.2697 0.2712 0.3024 -0.0372 0.0083  0.0488  354  ILE A CB  
2462  C CG1 . ILE A 356  ? 0.2806 0.2750 0.3125 -0.0371 0.0058  0.0471  354  ILE A CG1 
2463  C CG2 . ILE A 356  ? 0.3159 0.3211 0.3553 -0.0402 0.0078  0.0499  354  ILE A CG2 
2464  C CD1 . ILE A 356  ? 0.2725 0.2629 0.3065 -0.0396 0.0052  0.0500  354  ILE A CD1 
2465  N N   . ASP A 357  ? 0.2738 0.2876 0.3024 -0.0330 0.0133  0.0488  355  ASP A N   
2466  C CA  . ASP A 357  ? 0.2945 0.3155 0.3243 -0.0323 0.0152  0.0492  355  ASP A CA  
2467  C C   . ASP A 357  ? 0.3113 0.3336 0.3396 -0.0293 0.0148  0.0461  355  ASP A C   
2468  O O   . ASP A 357  ? 0.2868 0.3145 0.3183 -0.0290 0.0150  0.0454  355  ASP A O   
2469  C CB  . ASP A 357  ? 0.2731 0.2965 0.2998 -0.0317 0.0178  0.0514  355  ASP A CB  
2470  C CG  . ASP A 357  ? 0.3121 0.3433 0.3398 -0.0304 0.0199  0.0513  355  ASP A CG  
2471  O OD1 . ASP A 357  ? 0.3384 0.3751 0.3706 -0.0325 0.0208  0.0531  355  ASP A OD1 
2472  O OD2 . ASP A 357  ? 0.3363 0.3682 0.3606 -0.0272 0.0206  0.0492  355  ASP A OD2 
2473  N N   . LEU A 358  ? 0.2849 0.3025 0.3085 -0.0270 0.0141  0.0443  356  LEU A N   
2474  C CA  . LEU A 358  ? 0.2859 0.3042 0.3083 -0.0243 0.0133  0.0417  356  LEU A CA  
2475  C C   . LEU A 358  ? 0.2817 0.3005 0.3076 -0.0251 0.0111  0.0401  356  LEU A C   
2476  O O   . LEU A 358  ? 0.2443 0.2669 0.2718 -0.0238 0.0108  0.0388  356  LEU A O   
2477  C CB  . LEU A 358  ? 0.2611 0.2739 0.2781 -0.0222 0.0128  0.0404  356  LEU A CB  
2478  C CG  . LEU A 358  ? 0.2887 0.3013 0.3041 -0.0196 0.0117  0.0382  356  LEU A CG  
2479  C CD1 . LEU A 358  ? 0.2844 0.3021 0.3006 -0.0177 0.0130  0.0379  356  LEU A CD1 
2480  C CD2 . LEU A 358  ? 0.2486 0.2557 0.2589 -0.0180 0.0113  0.0373  356  LEU A CD2 
2481  N N   . ALA A 359  ? 0.2765 0.2919 0.3040 -0.0272 0.0094  0.0400  357  ALA A N   
2482  C CA  . ALA A 359  ? 0.3117 0.3279 0.3428 -0.0281 0.0072  0.0383  357  ALA A CA  
2483  C C   . ALA A 359  ? 0.3061 0.3287 0.3428 -0.0296 0.0077  0.0391  357  ALA A C   
2484  O O   . ALA A 359  ? 0.3035 0.3293 0.3423 -0.0290 0.0065  0.0374  357  ALA A O   
2485  C CB  . ALA A 359  ? 0.2585 0.2699 0.2908 -0.0301 0.0053  0.0379  357  ALA A CB  
2486  N N   . ARG A 360  ? 0.2712 0.2960 0.3101 -0.0317 0.0094  0.0418  358  ARG A N   
2487  C CA  . ARG A 360  ? 0.2549 0.2866 0.2993 -0.0333 0.0101  0.0428  358  ARG A CA  
2488  C C   . ARG A 360  ? 0.2982 0.3354 0.3419 -0.0306 0.0114  0.0419  358  ARG A C   
2489  O O   . ARG A 360  ? 0.3535 0.3953 0.4010 -0.0305 0.0107  0.0408  358  ARG A O   
2490  C CB  . ARG A 360  ? 0.2877 0.3210 0.3342 -0.0361 0.0119  0.0464  358  ARG A CB  
2491  C CG  . ARG A 360  ? 0.3406 0.3687 0.3891 -0.0391 0.0104  0.0477  358  ARG A CG  
2492  C CD  . ARG A 360  ? 0.4165 0.4472 0.4681 -0.0422 0.0121  0.0518  358  ARG A CD  
2493  N NE  . ARG A 360  ? 0.4701 0.4945 0.5224 -0.0445 0.0107  0.0535  358  ARG A NE  
2494  C CZ  . ARG A 360  ? 0.5246 0.5467 0.5821 -0.0473 0.0084  0.0533  358  ARG A CZ  
2495  N NH1 . ARG A 360  ? 0.4585 0.4843 0.5210 -0.0483 0.0072  0.0517  358  ARG A NH1 
2496  N NH2 . ARG A 360  ? 0.4768 0.4927 0.5347 -0.0490 0.0071  0.0547  358  ARG A NH2 
2497  N N   . ARG A 361  ? 0.2851 0.3218 0.3242 -0.0282 0.0132  0.0422  359  ARG A N   
2498  C CA  . ARG A 361  ? 0.3033 0.3449 0.3420 -0.0254 0.0143  0.0411  359  ARG A CA  
2499  C C   . ARG A 361  ? 0.2743 0.3152 0.3127 -0.0232 0.0123  0.0385  359  ARG A C   
2500  O O   . ARG A 361  ? 0.3175 0.3637 0.3589 -0.0222 0.0121  0.0376  359  ARG A O   
2501  C CB  . ARG A 361  ? 0.3233 0.3634 0.3569 -0.0232 0.0162  0.0415  359  ARG A CB  
2502  C CG  . ARG A 361  ? 0.3568 0.3992 0.3903 -0.0249 0.0185  0.0441  359  ARG A CG  
2503  C CD  . ARG A 361  ? 0.3802 0.4224 0.4090 -0.0223 0.0203  0.0439  359  ARG A CD  
2504  N NE  . ARG A 361  ? 0.3909 0.4258 0.4147 -0.0216 0.0196  0.0437  359  ARG A NE  
2505  C CZ  . ARG A 361  ? 0.3706 0.4021 0.3905 -0.0188 0.0191  0.0417  359  ARG A CZ  
2506  N NH1 . ARG A 361  ? 0.3435 0.3775 0.3639 -0.0162 0.0188  0.0397  359  ARG A NH1 
2507  N NH2 . ARG A 361  ? 0.3416 0.3672 0.3573 -0.0185 0.0187  0.0419  359  ARG A NH2 
2508  N N   . SER A 362  ? 0.2781 0.3129 0.3128 -0.0224 0.0107  0.0373  360  SER A N   
2509  C CA  . SER A 362  ? 0.2649 0.2989 0.2986 -0.0202 0.0088  0.0352  360  SER A CA  
2510  C C   . SER A 362  ? 0.2688 0.3047 0.3066 -0.0217 0.0066  0.0341  360  SER A C   
2511  O O   . SER A 362  ? 0.2908 0.3285 0.3290 -0.0200 0.0051  0.0326  360  SER A O   
2512  C CB  . SER A 362  ? 0.3229 0.3504 0.3512 -0.0189 0.0080  0.0346  360  SER A CB  
2513  O OG  . SER A 362  ? 0.2645 0.2879 0.2925 -0.0210 0.0069  0.0346  360  SER A OG  
2514  N N   . GLY A 363  ? 0.2627 0.2982 0.3037 -0.0249 0.0061  0.0348  361  GLY A N   
2515  C CA  . GLY A 363  ? 0.2806 0.3169 0.3251 -0.0263 0.0037  0.0333  361  GLY A CA  
2516  C C   . GLY A 363  ? 0.3160 0.3473 0.3574 -0.0256 0.0014  0.0314  361  GLY A C   
2517  O O   . GLY A 363  ? 0.3149 0.3474 0.3587 -0.0261 -0.0008 0.0295  361  GLY A O   
2518  N N   . ARG A 364  ? 0.3229 0.3491 0.3592 -0.0244 0.0020  0.0316  362  ARG A N   
2519  C CA  . ARG A 364  ? 0.3291 0.3510 0.3621 -0.0238 0.0001  0.0298  362  ARG A CA  
2520  C C   . ARG A 364  ? 0.3531 0.3705 0.3866 -0.0260 -0.0003 0.0300  362  ARG A C   
2521  O O   . ARG A 364  ? 0.3385 0.3538 0.3712 -0.0268 0.0014  0.0321  362  ARG A O   
2522  C CB  . ARG A 364  ? 0.3527 0.3721 0.3800 -0.0210 0.0008  0.0299  362  ARG A CB  
2523  C CG  . ARG A 364  ? 0.4009 0.4240 0.4279 -0.0187 0.0016  0.0303  362  ARG A CG  
2524  C CD  . ARG A 364  ? 0.3073 0.3297 0.3311 -0.0163 0.0002  0.0292  362  ARG A CD  
2525  N NE  . ARG A 364  ? 0.2619 0.2880 0.2866 -0.0142 0.0006  0.0296  362  ARG A NE  
2526  C CZ  . ARG A 364  ? 0.3017 0.3263 0.3232 -0.0118 0.0011  0.0302  362  ARG A CZ  
2527  N NH1 . ARG A 364  ? 0.2400 0.2597 0.2570 -0.0113 0.0014  0.0304  362  ARG A NH1 
2528  N NH2 . ARG A 364  ? 0.2427 0.2707 0.2659 -0.0100 0.0013  0.0304  362  ARG A NH2 
2529  N N   . ARG A 365  ? 0.2916 0.3076 0.3265 -0.0268 -0.0027 0.0278  363  ARG A N   
2530  C CA  . ARG A 365  ? 0.3181 0.3296 0.3539 -0.0286 -0.0036 0.0276  363  ARG A CA  
2531  C C   . ARG A 365  ? 0.2984 0.3051 0.3285 -0.0269 -0.0035 0.0270  363  ARG A C   
2532  O O   . ARG A 365  ? 0.3137 0.3192 0.3419 -0.0258 -0.0052 0.0246  363  ARG A O   
2533  C CB  . ARG A 365  ? 0.2907 0.3029 0.3307 -0.0300 -0.0065 0.0249  363  ARG A CB  
2534  C CG  . ARG A 365  ? 0.2994 0.3067 0.3411 -0.0318 -0.0078 0.0242  363  ARG A CG  
2535  C CD  . ARG A 365  ? 0.3397 0.3485 0.3883 -0.0345 -0.0098 0.0233  363  ARG A CD  
2536  N NE  . ARG A 365  ? 0.3389 0.3426 0.3899 -0.0364 -0.0112 0.0229  363  ARG A NE  
2537  C CZ  . ARG A 365  ? 0.3195 0.3204 0.3704 -0.0359 -0.0137 0.0195  363  ARG A CZ  
2538  N NH1 . ARG A 365  ? 0.3334 0.3366 0.3820 -0.0338 -0.0151 0.0162  363  ARG A NH1 
2539  N NH2 . ARG A 365  ? 0.3243 0.3201 0.3777 -0.0375 -0.0150 0.0194  363  ARG A NH2 
2540  N N   . ILE A 366  ? 0.2791 0.2834 0.3064 -0.0266 -0.0014 0.0293  364  ILE A N   
2541  C CA  . ILE A 366  ? 0.2702 0.2707 0.2922 -0.0249 -0.0010 0.0290  364  ILE A CA  
2542  C C   . ILE A 366  ? 0.2634 0.2597 0.2855 -0.0257 -0.0028 0.0273  364  ILE A C   
2543  O O   . ILE A 366  ? 0.2759 0.2703 0.3015 -0.0278 -0.0034 0.0279  364  ILE A O   
2544  C CB  . ILE A 366  ? 0.2669 0.2662 0.2863 -0.0245 0.0016  0.0316  364  ILE A CB  
2545  C CG1 . ILE A 366  ? 0.3024 0.3062 0.3218 -0.0233 0.0031  0.0326  364  ILE A CG1 
2546  C CG2 . ILE A 366  ? 0.2832 0.2783 0.2974 -0.0229 0.0018  0.0312  364  ILE A CG2 
2547  C CD1 . ILE A 366  ? 0.2837 0.2876 0.3013 -0.0229 0.0057  0.0349  364  ILE A CD1 
2548  N N   . MET A 367  ? 0.2482 0.2431 0.2667 -0.0239 -0.0038 0.0252  365  MET A N   
2549  C CA  . MET A 367  ? 0.2498 0.2409 0.2679 -0.0242 -0.0054 0.0233  365  MET A CA  
2550  C C   . MET A 367  ? 0.2671 0.2541 0.2822 -0.0239 -0.0039 0.0251  365  MET A C   
2551  O O   . MET A 367  ? 0.2869 0.2738 0.2977 -0.0222 -0.0025 0.0259  365  MET A O   
2552  C CB  . MET A 367  ? 0.2493 0.2417 0.2649 -0.0224 -0.0069 0.0203  365  MET A CB  
2553  C CG  . MET A 367  ? 0.2835 0.2808 0.3015 -0.0223 -0.0084 0.0187  365  MET A CG  
2554  S SD  . MET A 367  ? 0.3368 0.3368 0.3515 -0.0202 -0.0101 0.0156  365  MET A SD  
2555  C CE  . MET A 367  ? 0.3253 0.3237 0.3431 -0.0212 -0.0130 0.0117  365  MET A CE  
2556  N N   . VAL A 368  ? 0.2772 0.2608 0.2947 -0.0255 -0.0043 0.0258  366  VAL A N   
2557  C CA  . VAL A 368  ? 0.2522 0.2321 0.2671 -0.0254 -0.0030 0.0278  366  VAL A CA  
2558  C C   . VAL A 368  ? 0.2614 0.2372 0.2759 -0.0251 -0.0048 0.0257  366  VAL A C   
2559  O O   . VAL A 368  ? 0.2662 0.2400 0.2847 -0.0265 -0.0067 0.0247  366  VAL A O   
2560  C CB  . VAL A 368  ? 0.2660 0.2455 0.2838 -0.0275 -0.0019 0.0311  366  VAL A CB  
2561  C CG1 . VAL A 368  ? 0.2543 0.2302 0.2689 -0.0271 -0.0007 0.0331  366  VAL A CG1 
2562  C CG2 . VAL A 368  ? 0.2778 0.2621 0.2964 -0.0278 -0.0001 0.0329  366  VAL A CG2 
2563  N N   . ARG A 369  ? 0.2651 0.2396 0.2749 -0.0231 -0.0044 0.0248  367  ARG A N   
2564  C CA  . ARG A 369  ? 0.2595 0.2305 0.2688 -0.0225 -0.0060 0.0226  367  ARG A CA  
2565  C C   . ARG A 369  ? 0.2940 0.2611 0.3025 -0.0229 -0.0051 0.0250  367  ARG A C   
2566  O O   . ARG A 369  ? 0.2819 0.2490 0.2867 -0.0220 -0.0032 0.0268  367  ARG A O   
2567  C CB  . ARG A 369  ? 0.3180 0.2904 0.3231 -0.0203 -0.0061 0.0203  367  ARG A CB  
2568  C CG  . ARG A 369  ? 0.2856 0.2552 0.2902 -0.0195 -0.0077 0.0177  367  ARG A CG  
2569  C CD  . ARG A 369  ? 0.3443 0.3149 0.3440 -0.0174 -0.0071 0.0166  367  ARG A CD  
2570  N NE  . ARG A 369  ? 0.3137 0.2888 0.3122 -0.0165 -0.0076 0.0147  367  ARG A NE  
2571  C CZ  . ARG A 369  ? 0.3808 0.3582 0.3753 -0.0151 -0.0065 0.0150  367  ARG A CZ  
2572  N NH1 . ARG A 369  ? 0.3661 0.3417 0.3575 -0.0145 -0.0050 0.0166  367  ARG A NH1 
2573  N NH2 . ARG A 369  ? 0.3435 0.3252 0.3372 -0.0144 -0.0071 0.0137  367  ARG A NH2 
2574  N N   . LEU A 370  ? 0.2788 0.2425 0.2909 -0.0243 -0.0067 0.0251  368  LEU A N   
2575  C CA  . LEU A 370  ? 0.3030 0.2627 0.3147 -0.0248 -0.0062 0.0275  368  LEU A CA  
2576  C C   . LEU A 370  ? 0.2951 0.2519 0.3047 -0.0230 -0.0075 0.0250  368  LEU A C   
2577  O O   . LEU A 370  ? 0.2936 0.2493 0.3057 -0.0228 -0.0099 0.0217  368  LEU A O   
2578  C CB  . LEU A 370  ? 0.3246 0.2821 0.3416 -0.0273 -0.0073 0.0295  368  LEU A CB  
2579  C CG  . LEU A 370  ? 0.3229 0.2766 0.3399 -0.0281 -0.0069 0.0328  368  LEU A CG  
2580  C CD1 . LEU A 370  ? 0.3275 0.2834 0.3408 -0.0280 -0.0040 0.0364  368  LEU A CD1 
2581  C CD2 . LEU A 370  ? 0.3244 0.2756 0.3475 -0.0308 -0.0086 0.0346  368  LEU A CD2 
2582  N N   . VAL A 371  ? 0.2708 0.2266 0.2761 -0.0217 -0.0061 0.0262  369  VAL A N   
2583  C CA  . VAL A 371  ? 0.2600 0.2135 0.2633 -0.0200 -0.0070 0.0241  369  VAL A CA  
2584  C C   . VAL A 371  ? 0.2711 0.2211 0.2735 -0.0203 -0.0064 0.0271  369  VAL A C   
2585  O O   . VAL A 371  ? 0.2829 0.2332 0.2852 -0.0215 -0.0049 0.0306  369  VAL A O   
2586  C CB  . VAL A 371  ? 0.2844 0.2407 0.2830 -0.0180 -0.0059 0.0224  369  VAL A CB  
2587  C CG1 . VAL A 371  ? 0.2871 0.2475 0.2860 -0.0179 -0.0062 0.0205  369  VAL A CG1 
2588  C CG2 . VAL A 371  ? 0.2765 0.2335 0.2713 -0.0177 -0.0034 0.0254  369  VAL A CG2 
2589  N N   . LYS A 372  ? 0.2927 0.2399 0.2942 -0.0190 -0.0076 0.0255  370  LYS A N   
2590  C CA  . LYS A 372  ? 0.3002 0.2445 0.3001 -0.0189 -0.0070 0.0282  370  LYS A CA  
2591  C C   . LYS A 372  ? 0.2815 0.2280 0.2761 -0.0175 -0.0047 0.0291  370  LYS A C   
2592  O O   . LYS A 372  ? 0.3255 0.2729 0.3185 -0.0181 -0.0028 0.0322  370  LYS A O   
2593  C CB  . LYS A 372  ? 0.3459 0.2862 0.3477 -0.0180 -0.0094 0.0264  370  LYS A CB  
2594  C CG  . LYS A 372  ? 0.3492 0.2864 0.3569 -0.0199 -0.0116 0.0268  370  LYS A CG  
2595  C CD  . LYS A 372  ? 0.3499 0.2827 0.3606 -0.0191 -0.0145 0.0247  370  LYS A CD  
2596  C CE  . LYS A 372  ? 0.3890 0.3188 0.4061 -0.0211 -0.0168 0.0250  370  LYS A CE  
2597  N NZ  . LYS A 372  ? 0.3910 0.3162 0.4118 -0.0202 -0.0201 0.0222  370  LYS A NZ  
2598  N N   . GLY A 373  ? 0.2774 0.2254 0.2694 -0.0158 -0.0047 0.0263  371  GLY A N   
2599  C CA  . GLY A 373  ? 0.2724 0.2226 0.2600 -0.0147 -0.0027 0.0269  371  GLY A CA  
2600  C C   . GLY A 373  ? 0.2883 0.2383 0.2735 -0.0129 -0.0031 0.0246  371  GLY A C   
2601  O O   . GLY A 373  ? 0.3352 0.2826 0.3214 -0.0123 -0.0046 0.0235  371  GLY A O   
2602  N N   . ALA A 374  ? 0.2638 0.2166 0.2459 -0.0120 -0.0019 0.0239  372  ALA A N   
2603  C CA  . ALA A 374  ? 0.3410 0.2949 0.3212 -0.0105 -0.0022 0.0215  372  ALA A CA  
2604  C C   . ALA A 374  ? 0.3213 0.2750 0.2982 -0.0097 -0.0010 0.0226  372  ALA A C   
2605  O O   . ALA A 374  ? 0.3038 0.2587 0.2793 -0.0086 -0.0012 0.0208  372  ALA A O   
2606  C CB  . ALA A 374  ? 0.3128 0.2707 0.2923 -0.0102 -0.0020 0.0198  372  ALA A CB  
2607  N N   . TYR A 375  ? 0.2833 0.2361 0.2591 -0.0102 0.0003  0.0254  373  TYR A N   
2608  C CA  . TYR A 375  ? 0.2732 0.2263 0.2459 -0.0095 0.0015  0.0262  373  TYR A CA  
2609  C C   . TYR A 375  ? 0.2862 0.2367 0.2585 -0.0093 0.0013  0.0278  373  TYR A C   
2610  O O   . TYR A 375  ? 0.2799 0.2307 0.2499 -0.0089 0.0025  0.0290  373  TYR A O   
2611  C CB  . TYR A 375  ? 0.2744 0.2295 0.2458 -0.0098 0.0032  0.0277  373  TYR A CB  
2612  C CG  . TYR A 375  ? 0.2856 0.2433 0.2572 -0.0099 0.0034  0.0266  373  TYR A CG  
2613  C CD1 . TYR A 375  ? 0.3083 0.2669 0.2822 -0.0107 0.0029  0.0266  373  TYR A CD1 
2614  C CD2 . TYR A 375  ? 0.3585 0.3180 0.3282 -0.0092 0.0038  0.0259  373  TYR A CD2 
2615  C CE1 . TYR A 375  ? 0.3250 0.2863 0.2991 -0.0107 0.0029  0.0257  373  TYR A CE1 
2616  C CE2 . TYR A 375  ? 0.3951 0.3572 0.3650 -0.0093 0.0039  0.0254  373  TYR A CE2 
2617  C CZ  . TYR A 375  ? 0.3771 0.3401 0.3490 -0.0100 0.0034  0.0253  373  TYR A CZ  
2618  O OH  . TYR A 375  ? 0.4172 0.3831 0.3892 -0.0099 0.0033  0.0248  373  TYR A OH  
2619  N N   . TRP A 376  ? 0.2594 0.2073 0.2339 -0.0095 -0.0002 0.0277  374  TRP A N   
2620  C CA  . TRP A 376  ? 0.2718 0.2172 0.2463 -0.0096 -0.0005 0.0300  374  TRP A CA  
2621  C C   . TRP A 376  ? 0.3125 0.2580 0.2840 -0.0083 -0.0001 0.0299  374  TRP A C   
2622  O O   . TRP A 376  ? 0.3074 0.2531 0.2770 -0.0084 0.0010  0.0320  374  TRP A O   
2623  C CB  . TRP A 376  ? 0.2773 0.2195 0.2551 -0.0097 -0.0027 0.0295  374  TRP A CB  
2624  C CG  . TRP A 376  ? 0.2803 0.2198 0.2583 -0.0100 -0.0031 0.0325  374  TRP A CG  
2625  C CD1 . TRP A 376  ? 0.3202 0.2591 0.2991 -0.0116 -0.0026 0.0359  374  TRP A CD1 
2626  C CD2 . TRP A 376  ? 0.3328 0.2702 0.3100 -0.0088 -0.0042 0.0325  374  TRP A CD2 
2627  N NE1 . TRP A 376  ? 0.3209 0.2575 0.2994 -0.0114 -0.0032 0.0383  374  TRP A NE1 
2628  C CE2 . TRP A 376  ? 0.3199 0.2554 0.2974 -0.0097 -0.0043 0.0362  374  TRP A CE2 
2629  C CE3 . TRP A 376  ? 0.3780 0.3153 0.3543 -0.0070 -0.0050 0.0298  374  TRP A CE3 
2630  C CZ2 . TRP A 376  ? 0.3265 0.2598 0.3034 -0.0087 -0.0054 0.0374  374  TRP A CZ2 
2631  C CZ3 . TRP A 376  ? 0.3595 0.2947 0.3354 -0.0061 -0.0061 0.0307  374  TRP A CZ3 
2632  C CH2 . TRP A 376  ? 0.3681 0.3011 0.3442 -0.0069 -0.0064 0.0345  374  TRP A CH2 
2633  N N   . ASP A 377  ? 0.3099 0.2556 0.2811 -0.0071 -0.0009 0.0272  375  ASP A N   
2634  C CA  . ASP A 377  ? 0.3497 0.2957 0.3186 -0.0059 -0.0008 0.0269  375  ASP A CA  
2635  C C   . ASP A 377  ? 0.2949 0.2431 0.2610 -0.0060 0.0011  0.0278  375  ASP A C   
2636  O O   . ASP A 377  ? 0.2808 0.2287 0.2450 -0.0055 0.0015  0.0290  375  ASP A O   
2637  C CB  . ASP A 377  ? 0.3523 0.2996 0.3215 -0.0047 -0.0017 0.0236  375  ASP A CB  
2638  C CG  . ASP A 377  ? 0.4237 0.3687 0.3954 -0.0040 -0.0038 0.0222  375  ASP A CG  
2639  O OD1 . ASP A 377  ? 0.5744 0.5167 0.5465 -0.0037 -0.0046 0.0239  375  ASP A OD1 
2640  O OD2 . ASP A 377  ? 0.5493 0.4953 0.5227 -0.0035 -0.0047 0.0195  375  ASP A OD2 
2641  N N   . ALA A 378  ? 0.3141 0.2644 0.2801 -0.0065 0.0021  0.0273  376  ALA A N   
2642  C CA  . ALA A 378  ? 0.2985 0.2505 0.2624 -0.0065 0.0036  0.0279  376  ALA A CA  
2643  C C   . ALA A 378  ? 0.2707 0.2224 0.2339 -0.0070 0.0045  0.0303  376  ALA A C   
2644  O O   . ALA A 378  ? 0.2778 0.2304 0.2390 -0.0065 0.0054  0.0308  376  ALA A O   
2645  C CB  . ALA A 378  ? 0.3145 0.2687 0.2788 -0.0069 0.0041  0.0270  376  ALA A CB  
2646  N N   . GLU A 379  ? 0.2830 0.2339 0.2479 -0.0079 0.0044  0.0317  377  GLU A N   
2647  C CA  . GLU A 379  ? 0.2549 0.2064 0.2192 -0.0085 0.0054  0.0342  377  GLU A CA  
2648  C C   . GLU A 379  ? 0.2609 0.2113 0.2236 -0.0079 0.0052  0.0356  377  GLU A C   
2649  O O   . GLU A 379  ? 0.2655 0.2174 0.2262 -0.0076 0.0062  0.0368  377  GLU A O   
2650  C CB  . GLU A 379  ? 0.2537 0.2048 0.2207 -0.0098 0.0052  0.0357  377  GLU A CB  
2651  C CG  . GLU A 379  ? 0.2754 0.2279 0.2442 -0.0104 0.0054  0.0345  377  GLU A CG  
2652  C CD  . GLU A 379  ? 0.3055 0.2607 0.2731 -0.0102 0.0069  0.0345  377  GLU A CD  
2653  O OE1 . GLU A 379  ? 0.3009 0.2571 0.2665 -0.0097 0.0080  0.0354  377  GLU A OE1 
2654  O OE2 . GLU A 379  ? 0.2916 0.2480 0.2603 -0.0105 0.0069  0.0335  377  GLU A OE2 
2655  N N   . ILE A 380  ? 0.2563 0.2043 0.2200 -0.0076 0.0036  0.0354  378  ILE A N   
2656  C CA  . ILE A 380  ? 0.2586 0.2056 0.2208 -0.0070 0.0031  0.0368  378  ILE A CA  
2657  C C   . ILE A 380  ? 0.2954 0.2440 0.2547 -0.0057 0.0037  0.0355  378  ILE A C   
2658  O O   . ILE A 380  ? 0.3057 0.2554 0.2628 -0.0054 0.0043  0.0368  378  ILE A O   
2659  C CB  . ILE A 380  ? 0.2708 0.2148 0.2349 -0.0065 0.0010  0.0363  378  ILE A CB  
2660  C CG1 . ILE A 380  ? 0.3237 0.2657 0.2911 -0.0078 0.0001  0.0373  378  ILE A CG1 
2661  C CG2 . ILE A 380  ? 0.2791 0.2222 0.2415 -0.0057 0.0004  0.0379  378  ILE A CG2 
2662  C CD1 . ILE A 380  ? 0.2933 0.2356 0.2611 -0.0092 0.0009  0.0410  378  ILE A CD1 
2663  N N   . LYS A 381  ? 0.2578 0.2068 0.2172 -0.0052 0.0035  0.0328  379  LYS A N   
2664  C CA  . LYS A 381  ? 0.3050 0.2554 0.2623 -0.0042 0.0038  0.0315  379  LYS A CA  
2665  C C   . LYS A 381  ? 0.2812 0.2336 0.2370 -0.0044 0.0054  0.0320  379  LYS A C   
2666  O O   . LYS A 381  ? 0.2700 0.2234 0.2238 -0.0036 0.0057  0.0320  379  LYS A O   
2667  C CB  . LYS A 381  ? 0.2640 0.2149 0.2220 -0.0039 0.0034  0.0290  379  LYS A CB  
2668  C CG  . LYS A 381  ? 0.2691 0.2216 0.2256 -0.0033 0.0038  0.0277  379  LYS A CG  
2669  C CD  . LYS A 381  ? 0.3117 0.2652 0.2691 -0.0032 0.0034  0.0256  379  LYS A CD  
2670  C CE  . LYS A 381  ? 0.3062 0.2611 0.2625 -0.0027 0.0035  0.0245  379  LYS A CE  
2671  N NZ  . LYS A 381  ? 0.2891 0.2456 0.2465 -0.0028 0.0033  0.0229  379  LYS A NZ  
2672  N N   . ARG A 382  ? 0.2601 0.2134 0.2169 -0.0051 0.0062  0.0322  380  ARG A N   
2673  C CA  . ARG A 382  ? 0.2541 0.2092 0.2098 -0.0050 0.0075  0.0322  380  ARG A CA  
2674  C C   . ARG A 382  ? 0.2687 0.2250 0.2229 -0.0049 0.0082  0.0340  380  ARG A C   
2675  O O   . ARG A 382  ? 0.3001 0.2580 0.2525 -0.0041 0.0089  0.0335  380  ARG A O   
2676  C CB  . ARG A 382  ? 0.3221 0.2780 0.2796 -0.0058 0.0081  0.0322  380  ARG A CB  
2677  C CG  . ARG A 382  ? 0.3792 0.3370 0.3361 -0.0055 0.0093  0.0320  380  ARG A CG  
2678  C CD  . ARG A 382  ? 0.5288 0.4868 0.4858 -0.0051 0.0092  0.0302  380  ARG A CD  
2679  N NE  . ARG A 382  ? 0.4962 0.4540 0.4515 -0.0042 0.0088  0.0292  380  ARG A NE  
2680  C CZ  . ARG A 382  ? 0.6089 0.5665 0.5643 -0.0040 0.0085  0.0278  380  ARG A CZ  
2681  N NH1 . ARG A 382  ? 0.6793 0.6370 0.6361 -0.0044 0.0085  0.0275  380  ARG A NH1 
2682  N NH2 . ARG A 382  ? 0.6246 0.5822 0.5788 -0.0033 0.0082  0.0268  380  ARG A NH2 
2683  N N   . ALA A 383  ? 0.2650 0.2208 0.2200 -0.0056 0.0081  0.0362  381  ALA A N   
2684  C CA  . ALA A 383  ? 0.2573 0.2148 0.2108 -0.0056 0.0089  0.0385  381  ALA A CA  
2685  C C   . ALA A 383  ? 0.2645 0.2222 0.2155 -0.0045 0.0084  0.0384  381  ALA A C   
2686  O O   . ALA A 383  ? 0.2886 0.2489 0.2374 -0.0039 0.0092  0.0388  381  ALA A O   
2687  C CB  . ALA A 383  ? 0.2746 0.2312 0.2299 -0.0070 0.0086  0.0412  381  ALA A CB  
2688  N N   . GLN A 384  ? 0.2740 0.2293 0.2253 -0.0041 0.0069  0.0377  382  GLN A N   
2689  C CA  . GLN A 384  ? 0.2695 0.2250 0.2186 -0.0030 0.0062  0.0375  382  GLN A CA  
2690  C C   . GLN A 384  ? 0.3078 0.2652 0.2554 -0.0020 0.0067  0.0349  382  GLN A C   
2691  O O   . GLN A 384  ? 0.3506 0.3100 0.2959 -0.0011 0.0070  0.0350  382  GLN A O   
2692  C CB  . GLN A 384  ? 0.2610 0.2137 0.2113 -0.0026 0.0045  0.0369  382  GLN A CB  
2693  C CG  . GLN A 384  ? 0.3160 0.2667 0.2678 -0.0033 0.0035  0.0397  382  GLN A CG  
2694  C CD  . GLN A 384  ? 0.3203 0.2681 0.2737 -0.0027 0.0016  0.0388  382  GLN A CD  
2695  O OE1 . GLN A 384  ? 0.3330 0.2806 0.2870 -0.0021 0.0012  0.0360  382  GLN A OE1 
2696  N NE2 . GLN A 384  ? 0.3376 0.2832 0.2920 -0.0029 0.0004  0.0412  382  GLN A NE2 
2697  N N   . LEU A 385  ? 0.2883 0.2452 0.2373 -0.0022 0.0068  0.0328  383  LEU A N   
2698  C CA  . LEU A 385  ? 0.2979 0.2560 0.2460 -0.0015 0.0071  0.0306  383  LEU A CA  
2699  C C   . LEU A 385  ? 0.3305 0.2911 0.2773 -0.0011 0.0083  0.0307  383  LEU A C   
2700  O O   . LEU A 385  ? 0.3163 0.2785 0.2617 -0.0001 0.0083  0.0292  383  LEU A O   
2701  C CB  . LEU A 385  ? 0.2941 0.2514 0.2442 -0.0020 0.0070  0.0289  383  LEU A CB  
2702  C CG  . LEU A 385  ? 0.3518 0.3078 0.3030 -0.0020 0.0059  0.0279  383  LEU A CG  
2703  C CD1 . LEU A 385  ? 0.3612 0.3171 0.3140 -0.0027 0.0061  0.0269  383  LEU A CD1 
2704  C CD2 . LEU A 385  ? 0.3666 0.3231 0.3165 -0.0011 0.0052  0.0267  383  LEU A CD2 
2705  N N   . ASP A 386  ? 0.3040 0.2655 0.2517 -0.0018 0.0093  0.0321  384  ASP A N   
2706  C CA  . ASP A 386  ? 0.2877 0.2520 0.2346 -0.0013 0.0105  0.0319  384  ASP A CA  
2707  C C   . ASP A 386  ? 0.3098 0.2768 0.2545 -0.0009 0.0111  0.0337  384  ASP A C   
2708  O O   . ASP A 386  ? 0.2787 0.2490 0.2226 -0.0004 0.0122  0.0335  384  ASP A O   
2709  C CB  . ASP A 386  ? 0.3341 0.2986 0.2832 -0.0022 0.0113  0.0324  384  ASP A CB  
2710  C CG  . ASP A 386  ? 0.3869 0.3496 0.3379 -0.0024 0.0109  0.0306  384  ASP A CG  
2711  O OD1 . ASP A 386  ? 0.4068 0.3688 0.3574 -0.0017 0.0102  0.0287  384  ASP A OD1 
2712  O OD2 . ASP A 386  ? 0.3451 0.3073 0.2980 -0.0032 0.0111  0.0311  384  ASP A OD2 
2713  N N   . GLY A 387  ? 0.3034 0.2695 0.2472 -0.0011 0.0103  0.0356  385  GLY A N   
2714  C CA  . GLY A 387  ? 0.3150 0.2839 0.2564 -0.0008 0.0107  0.0378  385  GLY A CA  
2715  C C   . GLY A 387  ? 0.3074 0.2789 0.2492 -0.0017 0.0121  0.0402  385  GLY A C   
2716  O O   . GLY A 387  ? 0.3169 0.2926 0.2566 -0.0011 0.0132  0.0409  385  GLY A O   
2717  N N   . LEU A 388  ? 0.2995 0.2690 0.2441 -0.0031 0.0122  0.0414  386  LEU A N   
2718  C CA  . LEU A 388  ? 0.3118 0.2840 0.2574 -0.0042 0.0136  0.0434  386  LEU A CA  
2719  C C   . LEU A 388  ? 0.3443 0.3168 0.2897 -0.0053 0.0135  0.0475  386  LEU A C   
2720  O O   . LEU A 388  ? 0.3624 0.3322 0.3073 -0.0053 0.0121  0.0487  386  LEU A O   
2721  C CB  . LEU A 388  ? 0.2855 0.2557 0.2344 -0.0052 0.0137  0.0426  386  LEU A CB  
2722  C CG  . LEU A 388  ? 0.3277 0.2980 0.2768 -0.0040 0.0138  0.0391  386  LEU A CG  
2723  C CD1 . LEU A 388  ? 0.2973 0.2662 0.2494 -0.0049 0.0138  0.0385  386  LEU A CD1 
2724  C CD2 . LEU A 388  ? 0.3208 0.2955 0.2682 -0.0027 0.0150  0.0379  386  LEU A CD2 
2725  N N   . ALA A 389  ? 0.3250 0.3011 0.2709 -0.0063 0.0149  0.0499  387  ALA A N   
2726  C CA  . ALA A 389  ? 0.3157 0.2932 0.2612 -0.0075 0.0150  0.0543  387  ALA A CA  
2727  C C   . ALA A 389  ? 0.3442 0.3164 0.2925 -0.0090 0.0134  0.0564  387  ALA A C   
2728  O O   . ALA A 389  ? 0.3485 0.3195 0.2962 -0.0094 0.0124  0.0593  387  ALA A O   
2729  C CB  . ALA A 389  ? 0.3543 0.3370 0.3005 -0.0085 0.0170  0.0562  387  ALA A CB  
2730  N N   . ASP A 390  ? 0.2803 0.2494 0.2318 -0.0097 0.0129  0.0548  388  ASP A N   
2731  C CA  . ASP A 390  ? 0.3329 0.2974 0.2876 -0.0111 0.0112  0.0562  388  ASP A CA  
2732  C C   . ASP A 390  ? 0.3059 0.2676 0.2628 -0.0110 0.0107  0.0528  388  ASP A C   
2733  O O   . ASP A 390  ? 0.2932 0.2566 0.2493 -0.0100 0.0116  0.0500  388  ASP A O   
2734  C CB  . ASP A 390  ? 0.3281 0.2937 0.2851 -0.0133 0.0117  0.0604  388  ASP A CB  
2735  C CG  . ASP A 390  ? 0.3751 0.3358 0.3347 -0.0145 0.0096  0.0628  388  ASP A CG  
2736  O OD1 . ASP A 390  ? 0.4003 0.3565 0.3614 -0.0139 0.0078  0.0605  388  ASP A OD1 
2737  O OD2 . ASP A 390  ? 0.4238 0.3854 0.3842 -0.0160 0.0097  0.0672  388  ASP A OD2 
2738  N N   . PHE A 391  ? 0.2837 0.2415 0.2437 -0.0120 0.0091  0.0531  389  PHE A N   
2739  C CA  . PHE A 391  ? 0.2751 0.2308 0.2374 -0.0120 0.0084  0.0501  389  PHE A CA  
2740  C C   . PHE A 391  ? 0.3059 0.2634 0.2709 -0.0135 0.0093  0.0507  389  PHE A C   
2741  O O   . PHE A 391  ? 0.2785 0.2375 0.2447 -0.0150 0.0099  0.0539  389  PHE A O   
2742  C CB  . PHE A 391  ? 0.3029 0.2539 0.2674 -0.0121 0.0062  0.0497  389  PHE A CB  
2743  C CG  . PHE A 391  ? 0.2823 0.2317 0.2445 -0.0105 0.0052  0.0489  389  PHE A CG  
2744  C CD1 . PHE A 391  ? 0.2846 0.2342 0.2451 -0.0090 0.0052  0.0455  389  PHE A CD1 
2745  C CD2 . PHE A 391  ? 0.3508 0.2987 0.3125 -0.0106 0.0042  0.0518  389  PHE A CD2 
2746  C CE1 . PHE A 391  ? 0.3373 0.2858 0.2958 -0.0076 0.0042  0.0447  389  PHE A CE1 
2747  C CE2 . PHE A 391  ? 0.3107 0.2575 0.2705 -0.0090 0.0031  0.0510  389  PHE A CE2 
2748  C CZ  . PHE A 391  ? 0.3351 0.2823 0.2933 -0.0075 0.0032  0.0473  389  PHE A CZ  
2749  N N   . PRO A 392  ? 0.2776 0.2353 0.2435 -0.0131 0.0095  0.0478  390  PRO A N   
2750  C CA  . PRO A 392  ? 0.2739 0.2332 0.2427 -0.0144 0.0101  0.0480  390  PRO A CA  
2751  C C   . PRO A 392  ? 0.2949 0.2511 0.2674 -0.0157 0.0083  0.0478  390  PRO A C   
2752  O O   . PRO A 392  ? 0.2997 0.2569 0.2749 -0.0168 0.0085  0.0477  390  PRO A O   
2753  C CB  . PRO A 392  ? 0.2574 0.2182 0.2251 -0.0132 0.0108  0.0449  390  PRO A CB  
2754  C CG  . PRO A 392  ? 0.2564 0.2143 0.2227 -0.0119 0.0095  0.0427  390  PRO A CG  
2755  C CD  . PRO A 392  ? 0.2701 0.2272 0.2343 -0.0115 0.0092  0.0445  390  PRO A CD  
2756  N N   . VAL A 393  ? 0.2841 0.2364 0.2569 -0.0153 0.0066  0.0475  391  VAL A N   
2757  C CA  . VAL A 393  ? 0.2642 0.2132 0.2407 -0.0162 0.0046  0.0469  391  VAL A CA  
2758  C C   . VAL A 393  ? 0.3179 0.2639 0.2953 -0.0168 0.0033  0.0496  391  VAL A C   
2759  O O   . VAL A 393  ? 0.2994 0.2458 0.2739 -0.0161 0.0038  0.0514  391  VAL A O   
2760  C CB  . VAL A 393  ? 0.2861 0.2334 0.2625 -0.0148 0.0033  0.0430  391  VAL A CB  
2761  C CG1 . VAL A 393  ? 0.3059 0.2560 0.2817 -0.0145 0.0044  0.0407  391  VAL A CG1 
2762  C CG2 . VAL A 393  ? 0.2680 0.2142 0.2413 -0.0131 0.0031  0.0421  391  VAL A CG2 
2763  N N   . PHE A 394  ? 0.2840 0.2270 0.2655 -0.0180 0.0015  0.0500  392  PHE A N   
2764  C CA  . PHE A 394  ? 0.3098 0.2491 0.2929 -0.0184 -0.0003 0.0524  392  PHE A CA  
2765  C C   . PHE A 394  ? 0.3290 0.2656 0.3103 -0.0163 -0.0017 0.0499  392  PHE A C   
2766  O O   . PHE A 394  ? 0.3085 0.2458 0.2885 -0.0148 -0.0016 0.0461  392  PHE A O   
2767  C CB  . PHE A 394  ? 0.2773 0.2137 0.2658 -0.0203 -0.0021 0.0530  392  PHE A CB  
2768  C CG  . PHE A 394  ? 0.2877 0.2271 0.2782 -0.0226 -0.0007 0.0556  392  PHE A CG  
2769  C CD1 . PHE A 394  ? 0.2800 0.2215 0.2698 -0.0239 0.0006  0.0602  392  PHE A CD1 
2770  C CD2 . PHE A 394  ? 0.2936 0.2343 0.2867 -0.0234 -0.0007 0.0534  392  PHE A CD2 
2771  C CE1 . PHE A 394  ? 0.3085 0.2534 0.3002 -0.0260 0.0020  0.0627  392  PHE A CE1 
2772  C CE2 . PHE A 394  ? 0.3155 0.2595 0.3107 -0.0254 0.0006  0.0557  392  PHE A CE2 
2773  C CZ  . PHE A 394  ? 0.2781 0.2242 0.2727 -0.0268 0.0020  0.0603  392  PHE A CZ  
2774  N N   . THR A 395  ? 0.3190 0.2531 0.3002 -0.0161 -0.0029 0.0523  393  THR A N   
2775  C CA  . THR A 395  ? 0.3563 0.2880 0.3363 -0.0140 -0.0044 0.0502  393  THR A CA  
2776  C C   . THR A 395  ? 0.3239 0.2505 0.3081 -0.0140 -0.0074 0.0496  393  THR A C   
2777  O O   . THR A 395  ? 0.3164 0.2411 0.3003 -0.0121 -0.0089 0.0472  393  THR A O   
2778  C CB  . THR A 395  ? 0.3415 0.2742 0.3176 -0.0131 -0.0037 0.0527  393  THR A CB  
2779  O OG1 . THR A 395  ? 0.3455 0.2771 0.3229 -0.0146 -0.0042 0.0576  393  THR A OG1 
2780  C CG2 . THR A 395  ? 0.3302 0.2677 0.3020 -0.0126 -0.0010 0.0522  393  THR A CG2 
2781  N N   . ARG A 396  ? 0.3462 0.2708 0.3348 -0.0160 -0.0084 0.0516  394  ARG A N   
2782  C CA  . ARG A 396  ? 0.3716 0.2913 0.3651 -0.0160 -0.0115 0.0505  394  ARG A CA  
2783  C C   . ARG A 396  ? 0.3475 0.2674 0.3444 -0.0168 -0.0120 0.0473  394  ARG A C   
2784  O O   . ARG A 396  ? 0.3422 0.2645 0.3398 -0.0187 -0.0106 0.0487  394  ARG A O   
2785  C CB  . ARG A 396  ? 0.3700 0.2864 0.3666 -0.0178 -0.0129 0.0556  394  ARG A CB  
2786  C CG  . ARG A 396  ? 0.4056 0.3211 0.3992 -0.0168 -0.0131 0.0588  394  ARG A CG  
2787  C CD  . ARG A 396  ? 0.3886 0.2999 0.3862 -0.0184 -0.0153 0.0636  394  ARG A CD  
2788  N NE  . ARG A 396  ? 0.5459 0.4577 0.5400 -0.0179 -0.0149 0.0679  394  ARG A NE  
2789  C CZ  . ARG A 396  ? 0.6233 0.5314 0.6180 -0.0164 -0.0173 0.0687  394  ARG A CZ  
2790  N NH1 . ARG A 396  ? 0.6531 0.5565 0.6517 -0.0151 -0.0202 0.0653  394  ARG A NH1 
2791  N NH2 . ARG A 396  ? 0.4874 0.3969 0.4786 -0.0161 -0.0167 0.0728  394  ARG A NH2 
2792  N N   . LYS A 397  ? 0.3376 0.2554 0.3365 -0.0153 -0.0141 0.0428  395  LYS A N   
2793  C CA  . LYS A 397  ? 0.3623 0.2807 0.3643 -0.0158 -0.0148 0.0392  395  LYS A CA  
2794  C C   . LYS A 397  ? 0.3515 0.2677 0.3587 -0.0184 -0.0159 0.0416  395  LYS A C   
2795  O O   . LYS A 397  ? 0.3525 0.2709 0.3614 -0.0197 -0.0154 0.0405  395  LYS A O   
2796  C CB  . LYS A 397  ? 0.3600 0.2767 0.3636 -0.0135 -0.0171 0.0340  395  LYS A CB  
2797  C CG  . LYS A 397  ? 0.4448 0.3638 0.4500 -0.0134 -0.0174 0.0295  395  LYS A CG  
2798  C CD  . LYS A 397  ? 0.4398 0.3552 0.4513 -0.0145 -0.0202 0.0284  395  LYS A CD  
2799  C CE  . LYS A 397  ? 0.3843 0.3026 0.3970 -0.0142 -0.0206 0.0236  395  LYS A CE  
2800  N NZ  . LYS A 397  ? 0.4082 0.3229 0.4274 -0.0151 -0.0237 0.0219  395  LYS A NZ  
2801  N N   . ILE A 398  ? 0.3499 0.2618 0.3601 -0.0193 -0.0177 0.0451  396  ILE A N   
2802  C CA  . ILE A 398  ? 0.3524 0.2619 0.3681 -0.0221 -0.0191 0.0476  396  ILE A CA  
2803  C C   . ILE A 398  ? 0.3350 0.2486 0.3494 -0.0245 -0.0162 0.0517  396  ILE A C   
2804  O O   . ILE A 398  ? 0.3441 0.2578 0.3628 -0.0269 -0.0166 0.0527  396  ILE A O   
2805  C CB  . ILE A 398  ? 0.3752 0.2787 0.3945 -0.0225 -0.0218 0.0507  396  ILE A CB  
2806  C CG1 . ILE A 398  ? 0.4403 0.3400 0.4670 -0.0248 -0.0244 0.0513  396  ILE A CG1 
2807  C CG2 . ILE A 398  ? 0.3873 0.2919 0.4035 -0.0235 -0.0201 0.0569  396  ILE A CG2 
2808  C CD1 . ILE A 398  ? 0.4809 0.3739 0.5122 -0.0249 -0.0279 0.0534  396  ILE A CD1 
2809  N N   . HIS A 399  ? 0.3144 0.2318 0.3232 -0.0240 -0.0134 0.0539  397  HIS A N   
2810  C CA  . HIS A 399  ? 0.3171 0.2392 0.3245 -0.0259 -0.0106 0.0571  397  HIS A CA  
2811  C C   . HIS A 399  ? 0.3125 0.2382 0.3200 -0.0259 -0.0094 0.0535  397  HIS A C   
2812  O O   . HIS A 399  ? 0.3301 0.2580 0.3401 -0.0281 -0.0086 0.0551  397  HIS A O   
2813  C CB  . HIS A 399  ? 0.2961 0.2215 0.2975 -0.0249 -0.0081 0.0595  397  HIS A CB  
2814  C CG  . HIS A 399  ? 0.3429 0.2658 0.3441 -0.0252 -0.0090 0.0640  397  HIS A CG  
2815  N ND1 . HIS A 399  ? 0.3664 0.2916 0.3623 -0.0239 -0.0074 0.0660  397  HIS A ND1 
2816  C CD2 . HIS A 399  ? 0.3665 0.2847 0.3721 -0.0266 -0.0114 0.0671  397  HIS A CD2 
2817  C CE1 . HIS A 399  ? 0.3459 0.2683 0.3428 -0.0245 -0.0087 0.0702  397  HIS A CE1 
2818  N NE2 . HIS A 399  ? 0.3533 0.2712 0.3561 -0.0261 -0.0112 0.0711  397  HIS A NE2 
2819  N N   . THR A 400  ? 0.3328 0.2594 0.3376 -0.0235 -0.0094 0.0488  398  THR A N   
2820  C CA  . THR A 400  ? 0.3375 0.2672 0.3424 -0.0233 -0.0087 0.0452  398  THR A CA  
2821  C C   . THR A 400  ? 0.3196 0.2474 0.3306 -0.0249 -0.0109 0.0437  398  THR A C   
2822  O O   . THR A 400  ? 0.3023 0.2332 0.3149 -0.0262 -0.0101 0.0433  398  THR A O   
2823  C CB  . THR A 400  ? 0.3329 0.2634 0.3344 -0.0206 -0.0088 0.0407  398  THR A CB  
2824  O OG1 . THR A 400  ? 0.3087 0.2417 0.3049 -0.0194 -0.0065 0.0419  398  THR A OG1 
2825  C CG2 . THR A 400  ? 0.2822 0.2156 0.2842 -0.0203 -0.0086 0.0369  398  THR A CG2 
2826  N N   . ASP A 401  ? 0.3444 0.2672 0.3593 -0.0248 -0.0139 0.0429  399  ASP A N   
2827  C CA  . ASP A 401  ? 0.3599 0.2804 0.3811 -0.0263 -0.0164 0.0412  399  ASP A CA  
2828  C C   . ASP A 401  ? 0.3556 0.2766 0.3804 -0.0297 -0.0159 0.0459  399  ASP A C   
2829  O O   . ASP A 401  ? 0.3543 0.2769 0.3827 -0.0312 -0.0163 0.0447  399  ASP A O   
2830  C CB  . ASP A 401  ? 0.3897 0.3044 0.4146 -0.0254 -0.0199 0.0394  399  ASP A CB  
2831  C CG  . ASP A 401  ? 0.4151 0.3299 0.4375 -0.0222 -0.0208 0.0338  399  ASP A CG  
2832  O OD1 . ASP A 401  ? 0.4345 0.3536 0.4542 -0.0211 -0.0195 0.0304  399  ASP A OD1 
2833  O OD2 . ASP A 401  ? 0.4503 0.3611 0.4739 -0.0207 -0.0229 0.0328  399  ASP A OD2 
2834  N N   . VAL A 402  ? 0.3891 0.3091 0.4132 -0.0309 -0.0150 0.0513  400  VAL A N   
2835  C CA  . VAL A 402  ? 0.3343 0.2558 0.3615 -0.0342 -0.0141 0.0562  400  VAL A CA  
2836  C C   . VAL A 402  ? 0.3596 0.2878 0.3842 -0.0347 -0.0110 0.0562  400  VAL A C   
2837  O O   . VAL A 402  ? 0.3151 0.2454 0.3436 -0.0369 -0.0108 0.0570  400  VAL A O   
2838  C CB  . VAL A 402  ? 0.3569 0.2768 0.3831 -0.0352 -0.0137 0.0622  400  VAL A CB  
2839  C CG1 . VAL A 402  ? 0.4036 0.3266 0.4325 -0.0386 -0.0122 0.0676  400  VAL A CG1 
2840  C CG2 . VAL A 402  ? 0.3664 0.2793 0.3965 -0.0349 -0.0172 0.0624  400  VAL A CG2 
2841  N N   . SER A 403  ? 0.3429 0.2746 0.3613 -0.0325 -0.0086 0.0552  401  SER A N   
2842  C CA  . SER A 403  ? 0.3151 0.2528 0.3309 -0.0325 -0.0058 0.0548  401  SER A CA  
2843  C C   . SER A 403  ? 0.3174 0.2562 0.3361 -0.0326 -0.0068 0.0507  401  SER A C   
2844  O O   . SER A 403  ? 0.3210 0.2636 0.3419 -0.0343 -0.0058 0.0515  401  SER A O   
2845  C CB  . SER A 403  ? 0.3136 0.2537 0.3227 -0.0298 -0.0038 0.0534  401  SER A CB  
2846  O OG  . SER A 403  ? 0.2954 0.2409 0.3023 -0.0296 -0.0014 0.0529  401  SER A OG  
2847  N N   . TYR A 404  ? 0.2926 0.2286 0.3117 -0.0309 -0.0090 0.0461  402  TYR A N   
2848  C CA  . TYR A 404  ? 0.3514 0.2889 0.3729 -0.0307 -0.0101 0.0419  402  TYR A CA  
2849  C C   . TYR A 404  ? 0.3257 0.2625 0.3540 -0.0336 -0.0117 0.0429  402  TYR A C   
2850  O O   . TYR A 404  ? 0.3114 0.2520 0.3413 -0.0346 -0.0111 0.0421  402  TYR A O   
2851  C CB  . TYR A 404  ? 0.3202 0.2550 0.3412 -0.0284 -0.0123 0.0370  402  TYR A CB  
2852  C CG  . TYR A 404  ? 0.3111 0.2487 0.3327 -0.0276 -0.0130 0.0323  402  TYR A CG  
2853  C CD1 . TYR A 404  ? 0.3384 0.2752 0.3657 -0.0290 -0.0153 0.0303  402  TYR A CD1 
2854  C CD2 . TYR A 404  ? 0.3177 0.2588 0.3344 -0.0254 -0.0115 0.0299  402  TYR A CD2 
2855  C CE1 . TYR A 404  ? 0.3555 0.2953 0.3832 -0.0281 -0.0161 0.0260  402  TYR A CE1 
2856  C CE2 . TYR A 404  ? 0.3223 0.2663 0.3393 -0.0247 -0.0122 0.0260  402  TYR A CE2 
2857  C CZ  . TYR A 404  ? 0.3141 0.2577 0.3364 -0.0259 -0.0145 0.0240  402  TYR A CZ  
2858  O OH  . TYR A 404  ? 0.3350 0.2821 0.3574 -0.0250 -0.0152 0.0200  402  TYR A OH  
2859  N N   . ILE A 405  ? 0.2994 0.2312 0.3319 -0.0350 -0.0139 0.0448  403  ILE A N   
2860  C CA  . ILE A 405  ? 0.3513 0.2818 0.3909 -0.0381 -0.0157 0.0461  403  ILE A CA  
2861  C C   . ILE A 405  ? 0.3358 0.2708 0.3759 -0.0406 -0.0131 0.0509  403  ILE A C   
2862  O O   . ILE A 405  ? 0.3243 0.2620 0.3686 -0.0426 -0.0133 0.0507  403  ILE A O   
2863  C CB  . ILE A 405  ? 0.3743 0.2980 0.4183 -0.0390 -0.0186 0.0476  403  ILE A CB  
2864  C CG1 . ILE A 405  ? 0.3929 0.3126 0.4363 -0.0361 -0.0212 0.0424  403  ILE A CG1 
2865  C CG2 . ILE A 405  ? 0.3445 0.2666 0.3966 -0.0423 -0.0207 0.0489  403  ILE A CG2 
2866  C CD1 . ILE A 405  ? 0.4380 0.3581 0.4847 -0.0355 -0.0234 0.0365  403  ILE A CD1 
2867  N N   . ALA A 406  ? 0.3433 0.2799 0.3792 -0.0405 -0.0106 0.0551  404  ALA A N   
2868  C CA  . ALA A 406  ? 0.3724 0.3142 0.4085 -0.0427 -0.0079 0.0596  404  ALA A CA  
2869  C C   . ALA A 406  ? 0.3507 0.2985 0.3852 -0.0420 -0.0060 0.0570  404  ALA A C   
2870  O O   . ALA A 406  ? 0.3735 0.3251 0.4115 -0.0442 -0.0053 0.0585  404  ALA A O   
2871  C CB  . ALA A 406  ? 0.3639 0.3070 0.3949 -0.0420 -0.0056 0.0637  404  ALA A CB  
2872  N N   . CYS A 407  ? 0.3340 0.2829 0.3634 -0.0389 -0.0053 0.0532  405  CYS A N   
2873  C CA  . CYS A 407  ? 0.2850 0.2393 0.3126 -0.0379 -0.0037 0.0509  405  CYS A CA  
2874  C C   . CYS A 407  ? 0.3434 0.2980 0.3757 -0.0387 -0.0057 0.0475  405  CYS A C   
2875  O O   . CYS A 407  ? 0.3050 0.2643 0.3385 -0.0394 -0.0047 0.0472  405  CYS A O   
2876  C CB  . CYS A 407  ? 0.2974 0.2522 0.3185 -0.0346 -0.0025 0.0483  405  CYS A CB  
2877  S SG  . CYS A 407  ? 0.3643 0.3206 0.3799 -0.0338 0.0004  0.0522  405  CYS A SG  
2878  N N   . ALA A 408  ? 0.3423 0.2921 0.3773 -0.0384 -0.0088 0.0446  406  ALA A N   
2879  C CA  . ALA A 408  ? 0.3423 0.2922 0.3822 -0.0393 -0.0111 0.0411  406  ALA A CA  
2880  C C   . ALA A 408  ? 0.3296 0.2808 0.3759 -0.0428 -0.0114 0.0442  406  ALA A C   
2881  O O   . ALA A 408  ? 0.3384 0.2931 0.3877 -0.0437 -0.0118 0.0424  406  ALA A O   
2882  C CB  . ALA A 408  ? 0.3395 0.2839 0.3815 -0.0383 -0.0145 0.0375  406  ALA A CB  
2883  N N   . ALA A 409  ? 0.3361 0.2848 0.3845 -0.0450 -0.0113 0.0489  407  ALA A N   
2884  C CA  . ALA A 409  ? 0.3601 0.3108 0.4145 -0.0487 -0.0112 0.0526  407  ALA A CA  
2885  C C   . ALA A 409  ? 0.3402 0.2985 0.3931 -0.0491 -0.0081 0.0541  407  ALA A C   
2886  O O   . ALA A 409  ? 0.3368 0.2984 0.3945 -0.0512 -0.0084 0.0541  407  ALA A O   
2887  C CB  . ALA A 409  ? 0.3673 0.3146 0.4232 -0.0507 -0.0112 0.0582  407  ALA A CB  
2888  N N   . LYS A 410  ? 0.3325 0.2938 0.3789 -0.0470 -0.0052 0.0552  408  LYS A N   
2889  C CA  . LYS A 410  ? 0.2907 0.2592 0.3355 -0.0469 -0.0023 0.0561  408  LYS A CA  
2890  C C   . LYS A 410  ? 0.3167 0.2879 0.3621 -0.0457 -0.0031 0.0515  408  LYS A C   
2891  O O   . LYS A 410  ? 0.3292 0.3057 0.3775 -0.0469 -0.0023 0.0518  408  LYS A O   
2892  C CB  . LYS A 410  ? 0.3405 0.3109 0.3782 -0.0446 0.0005  0.0574  408  LYS A CB  
2893  C CG  . LYS A 410  ? 0.3496 0.3274 0.3856 -0.0441 0.0034  0.0582  408  LYS A CG  
2894  C CD  . LYS A 410  ? 0.3585 0.3372 0.3875 -0.0414 0.0057  0.0585  408  LYS A CD  
2895  C CE  . LYS A 410  ? 0.3529 0.3303 0.3805 -0.0424 0.0066  0.0629  408  LYS A CE  
2896  N NZ  . LYS A 410  ? 0.3569 0.3401 0.3871 -0.0449 0.0086  0.0672  408  LYS A NZ  
2897  N N   . LEU A 411  ? 0.3175 0.2856 0.3602 -0.0432 -0.0047 0.0471  409  LEU A N   
2898  C CA  . LEU A 411  ? 0.2704 0.2413 0.3132 -0.0417 -0.0055 0.0427  409  LEU A CA  
2899  C C   . LEU A 411  ? 0.3038 0.2749 0.3536 -0.0440 -0.0080 0.0412  409  LEU A C   
2900  O O   . LEU A 411  ? 0.3023 0.2781 0.3538 -0.0441 -0.0079 0.0396  409  LEU A O   
2901  C CB  . LEU A 411  ? 0.3210 0.2888 0.3592 -0.0387 -0.0066 0.0388  409  LEU A CB  
2902  C CG  . LEU A 411  ? 0.3036 0.2730 0.3349 -0.0360 -0.0042 0.0389  409  LEU A CG  
2903  C CD1 . LEU A 411  ? 0.3336 0.2993 0.3612 -0.0335 -0.0055 0.0357  409  LEU A CD1 
2904  C CD2 . LEU A 411  ? 0.2620 0.2372 0.2922 -0.0350 -0.0029 0.0379  409  LEU A CD2 
2905  N N   . LEU A 412  ? 0.3038 0.2698 0.3580 -0.0458 -0.0105 0.0414  410  LEU A N   
2906  C CA  . LEU A 412  ? 0.3370 0.3027 0.3984 -0.0480 -0.0132 0.0396  410  LEU A CA  
2907  C C   . LEU A 412  ? 0.3278 0.2979 0.3941 -0.0513 -0.0120 0.0433  410  LEU A C   
2908  O O   . LEU A 412  ? 0.3625 0.3345 0.4343 -0.0529 -0.0138 0.0414  410  LEU A O   
2909  C CB  . LEU A 412  ? 0.3001 0.2586 0.3654 -0.0491 -0.0164 0.0390  410  LEU A CB  
2910  C CG  . LEU A 412  ? 0.3204 0.2751 0.3826 -0.0460 -0.0184 0.0339  410  LEU A CG  
2911  C CD1 . LEU A 412  ? 0.3659 0.3135 0.4320 -0.0467 -0.0214 0.0335  410  LEU A CD1 
2912  C CD2 . LEU A 412  ? 0.3577 0.3157 0.4209 -0.0447 -0.0200 0.0285  410  LEU A CD2 
2913  N N   . ALA A 413  ? 0.2970 0.2694 0.3615 -0.0522 -0.0091 0.0483  411  ALA A N   
2914  C CA  . ALA A 413  ? 0.3799 0.3579 0.4486 -0.0551 -0.0076 0.0517  411  ALA A CA  
2915  C C   . ALA A 413  ? 0.3678 0.3530 0.4342 -0.0535 -0.0056 0.0501  411  ALA A C   
2916  O O   . ALA A 413  ? 0.3389 0.3297 0.4087 -0.0554 -0.0042 0.0524  411  ALA A O   
2917  C CB  . ALA A 413  ? 0.3603 0.3389 0.4280 -0.0567 -0.0051 0.0578  411  ALA A CB  
2918  N N   . ALA A 414  ? 0.3251 0.3103 0.3860 -0.0499 -0.0054 0.0463  412  ALA A N   
2919  C CA  . ALA A 414  ? 0.3271 0.3185 0.3853 -0.0480 -0.0035 0.0452  412  ALA A CA  
2920  C C   . ALA A 414  ? 0.3167 0.3086 0.3744 -0.0460 -0.0055 0.0400  412  ALA A C   
2921  O O   . ALA A 414  ? 0.3016 0.2967 0.3550 -0.0434 -0.0043 0.0385  412  ALA A O   
2922  C CB  . ALA A 414  ? 0.3458 0.3380 0.3969 -0.0455 -0.0006 0.0467  412  ALA A CB  
2923  N N   . THR A 415  ? 0.3024 0.2912 0.3643 -0.0471 -0.0088 0.0373  413  THR A N   
2924  C CA  . THR A 415  ? 0.3339 0.3235 0.3949 -0.0450 -0.0108 0.0322  413  THR A CA  
2925  C C   . THR A 415  ? 0.3473 0.3437 0.4102 -0.0449 -0.0105 0.0312  413  THR A C   
2926  O O   . THR A 415  ? 0.3352 0.3333 0.3961 -0.0428 -0.0116 0.0276  413  THR A O   
2927  C CB  . THR A 415  ? 0.3682 0.3534 0.4335 -0.0460 -0.0145 0.0290  413  THR A CB  
2928  O OG1 . THR A 415  ? 0.3532 0.3386 0.4262 -0.0497 -0.0157 0.0306  413  THR A OG1 
2929  C CG2 . THR A 415  ? 0.3412 0.3196 0.4037 -0.0451 -0.0151 0.0290  413  THR A CG2 
2930  N N   . ASP A 416  ? 0.3584 0.3590 0.4253 -0.0472 -0.0090 0.0343  414  ASP A N   
2931  C CA  . ASP A 416  ? 0.3754 0.3829 0.4439 -0.0468 -0.0085 0.0333  414  ASP A CA  
2932  C C   . ASP A 416  ? 0.3630 0.3735 0.4251 -0.0435 -0.0061 0.0335  414  ASP A C   
2933  O O   . ASP A 416  ? 0.3363 0.3513 0.3983 -0.0420 -0.0064 0.0315  414  ASP A O   
2934  C CB  . ASP A 416  ? 0.3749 0.3866 0.4498 -0.0502 -0.0076 0.0366  414  ASP A CB  
2935  C CG  . ASP A 416  ? 0.4536 0.4659 0.5267 -0.0510 -0.0044 0.0414  414  ASP A CG  
2936  O OD1 . ASP A 416  ? 0.4641 0.4712 0.5332 -0.0504 -0.0039 0.0427  414  ASP A OD1 
2937  O OD2 . ASP A 416  ? 0.5553 0.5738 0.6309 -0.0522 -0.0024 0.0439  414  ASP A OD2 
2938  N N   . VAL A 417  ? 0.3102 0.3184 0.3673 -0.0423 -0.0039 0.0357  415  VAL A N   
2939  C CA  . VAL A 417  ? 0.3697 0.3806 0.4213 -0.0393 -0.0017 0.0359  415  VAL A CA  
2940  C C   . VAL A 417  ? 0.3078 0.3141 0.3529 -0.0365 -0.0019 0.0342  415  VAL A C   
2941  O O   . VAL A 417  ? 0.3268 0.3349 0.3677 -0.0339 -0.0008 0.0337  415  VAL A O   
2942  C CB  . VAL A 417  ? 0.3335 0.3475 0.3847 -0.0399 0.0014  0.0397  415  VAL A CB  
2943  C CG1 . VAL A 417  ? 0.4079 0.4277 0.4655 -0.0425 0.0018  0.0413  415  VAL A CG1 
2944  C CG2 . VAL A 417  ? 0.3699 0.3791 0.4192 -0.0409 0.0023  0.0424  415  VAL A CG2 
2945  N N   . VAL A 418  ? 0.2919 0.2924 0.3362 -0.0370 -0.0033 0.0336  416  VAL A N   
2946  C CA  . VAL A 418  ? 0.2581 0.2549 0.2968 -0.0344 -0.0038 0.0316  416  VAL A CA  
2947  C C   . VAL A 418  ? 0.2724 0.2659 0.3130 -0.0348 -0.0069 0.0283  416  VAL A C   
2948  O O   . VAL A 418  ? 0.3239 0.3165 0.3701 -0.0372 -0.0086 0.0280  416  VAL A O   
2949  C CB  . VAL A 418  ? 0.2553 0.2484 0.2899 -0.0339 -0.0019 0.0340  416  VAL A CB  
2950  C CG1 . VAL A 418  ? 0.2984 0.2952 0.3311 -0.0333 0.0010  0.0368  416  VAL A CG1 
2951  C CG2 . VAL A 418  ? 0.2587 0.2476 0.2964 -0.0364 -0.0027 0.0358  416  VAL A CG2 
2952  N N   . PHE A 419  ? 0.2560 0.2481 0.2922 -0.0324 -0.0076 0.0257  417  PHE A N   
2953  C CA  . PHE A 419  ? 0.2626 0.2519 0.2995 -0.0320 -0.0104 0.0221  417  PHE A CA  
2954  C C   . PHE A 419  ? 0.2799 0.2638 0.3136 -0.0313 -0.0102 0.0224  417  PHE A C   
2955  O O   . PHE A 419  ? 0.2824 0.2660 0.3106 -0.0290 -0.0090 0.0222  417  PHE A O   
2956  C CB  . PHE A 419  ? 0.2907 0.2834 0.3249 -0.0297 -0.0114 0.0189  417  PHE A CB  
2957  C CG  . PHE A 419  ? 0.2982 0.2890 0.3325 -0.0290 -0.0141 0.0148  417  PHE A CG  
2958  C CD1 . PHE A 419  ? 0.3172 0.3072 0.3572 -0.0307 -0.0167 0.0125  417  PHE A CD1 
2959  C CD2 . PHE A 419  ? 0.2567 0.2471 0.2857 -0.0265 -0.0141 0.0131  417  PHE A CD2 
2960  C CE1 . PHE A 419  ? 0.3037 0.2924 0.3439 -0.0298 -0.0193 0.0083  417  PHE A CE1 
2961  C CE2 . PHE A 419  ? 0.2761 0.2656 0.3050 -0.0257 -0.0164 0.0091  417  PHE A CE2 
2962  C CZ  . PHE A 419  ? 0.3058 0.2945 0.3403 -0.0272 -0.0191 0.0065  417  PHE A CZ  
2963  N N   . PRO A 420  ? 0.2709 0.2506 0.3080 -0.0331 -0.0112 0.0231  418  PRO A N   
2964  C CA  . PRO A 420  ? 0.2624 0.2371 0.2965 -0.0322 -0.0111 0.0235  418  PRO A CA  
2965  C C   . PRO A 420  ? 0.2925 0.2656 0.3249 -0.0303 -0.0133 0.0191  418  PRO A C   
2966  O O   . PRO A 420  ? 0.2841 0.2582 0.3197 -0.0305 -0.0157 0.0157  418  PRO A O   
2967  C CB  . PRO A 420  ? 0.2705 0.2414 0.3095 -0.0349 -0.0119 0.0259  418  PRO A CB  
2968  C CG  . PRO A 420  ? 0.2954 0.2704 0.3390 -0.0373 -0.0113 0.0281  418  PRO A CG  
2969  C CD  . PRO A 420  ? 0.2644 0.2437 0.3082 -0.0362 -0.0123 0.0245  418  PRO A CD  
2970  N N   . GLN A 421  ? 0.2710 0.2420 0.2984 -0.0284 -0.0124 0.0191  419  GLN A N   
2971  C CA  . GLN A 421  ? 0.2620 0.2322 0.2870 -0.0263 -0.0139 0.0151  419  GLN A CA  
2972  C C   . GLN A 421  ? 0.3039 0.2689 0.3276 -0.0258 -0.0139 0.0159  419  GLN A C   
2973  O O   . GLN A 421  ? 0.3038 0.2682 0.3232 -0.0250 -0.0118 0.0183  419  GLN A O   
2974  C CB  . GLN A 421  ? 0.2804 0.2545 0.3000 -0.0241 -0.0126 0.0144  419  GLN A CB  
2975  C CG  . GLN A 421  ? 0.2613 0.2407 0.2822 -0.0243 -0.0128 0.0137  419  GLN A CG  
2976  C CD  . GLN A 421  ? 0.2914 0.2742 0.3072 -0.0224 -0.0110 0.0145  419  GLN A CD  
2977  O OE1 . GLN A 421  ? 0.2867 0.2689 0.2997 -0.0221 -0.0087 0.0174  419  GLN A OE1 
2978  N NE2 . GLN A 421  ? 0.2540 0.2406 0.2686 -0.0212 -0.0122 0.0118  419  GLN A NE2 
2979  N N   . PHE A 422  ? 0.2671 0.2285 0.2946 -0.0264 -0.0165 0.0138  420  PHE A N   
2980  C CA  . PHE A 422  ? 0.2714 0.2274 0.2988 -0.0263 -0.0168 0.0149  420  PHE A CA  
2981  C C   . PHE A 422  ? 0.3136 0.2692 0.3376 -0.0236 -0.0177 0.0112  420  PHE A C   
2982  O O   . PHE A 422  ? 0.3156 0.2703 0.3421 -0.0229 -0.0203 0.0070  420  PHE A O   
2983  C CB  . PHE A 422  ? 0.3287 0.2806 0.3627 -0.0285 -0.0192 0.0152  420  PHE A CB  
2984  C CG  . PHE A 422  ? 0.3478 0.3007 0.3854 -0.0314 -0.0183 0.0192  420  PHE A CG  
2985  C CD1 . PHE A 422  ? 0.3576 0.3104 0.3931 -0.0322 -0.0156 0.0242  420  PHE A CD1 
2986  C CD2 . PHE A 422  ? 0.3227 0.2773 0.3658 -0.0331 -0.0199 0.0178  420  PHE A CD2 
2987  C CE1 . PHE A 422  ? 0.3293 0.2838 0.3680 -0.0349 -0.0145 0.0279  420  PHE A CE1 
2988  C CE2 . PHE A 422  ? 0.3344 0.2906 0.3809 -0.0359 -0.0189 0.0215  420  PHE A CE2 
2989  C CZ  . PHE A 422  ? 0.3311 0.2874 0.3754 -0.0367 -0.0161 0.0266  420  PHE A CZ  
2990  N N   . ALA A 423  ? 0.2930 0.2495 0.3114 -0.0221 -0.0155 0.0126  421  ALA A N   
2991  C CA  . ALA A 423  ? 0.2698 0.2268 0.2844 -0.0196 -0.0157 0.0097  421  ALA A CA  
2992  C C   . ALA A 423  ? 0.3656 0.3174 0.3809 -0.0192 -0.0166 0.0100  421  ALA A C   
2993  O O   . ALA A 423  ? 0.3518 0.3015 0.3652 -0.0195 -0.0150 0.0136  421  ALA A O   
2994  C CB  . ALA A 423  ? 0.2743 0.2345 0.2831 -0.0184 -0.0130 0.0114  421  ALA A CB  
2995  N N   . THR A 424  ? 0.3328 0.2828 0.3512 -0.0184 -0.0194 0.0060  422  THR A N   
2996  C CA  . THR A 424  ? 0.3371 0.2821 0.3563 -0.0177 -0.0206 0.0059  422  THR A CA  
2997  C C   . THR A 424  ? 0.3934 0.3382 0.4148 -0.0159 -0.0235 0.0002  422  THR A C   
2998  O O   . THR A 424  ? 0.3774 0.3241 0.4018 -0.0160 -0.0253 -0.0033 422  THR A O   
2999  C CB  . THR A 424  ? 0.4243 0.3642 0.4479 -0.0199 -0.0213 0.0095  422  THR A CB  
3000  O OG1 . THR A 424  ? 0.4307 0.3659 0.4544 -0.0190 -0.0223 0.0099  422  THR A OG1 
3001  C CG2 . THR A 424  ? 0.3580 0.2966 0.3883 -0.0216 -0.0241 0.0076  422  THR A CG2 
3002  N N   . HIS A 425  ? 0.3566 0.2994 0.3765 -0.0140 -0.0239 -0.0010 423  HIS A N   
3003  C CA  . HIS A 425  ? 0.4066 0.3485 0.4287 -0.0120 -0.0267 -0.0063 423  HIS A CA  
3004  C C   . HIS A 425  ? 0.4436 0.3787 0.4708 -0.0124 -0.0292 -0.0059 423  HIS A C   
3005  O O   . HIS A 425  ? 0.4690 0.4026 0.4986 -0.0106 -0.0318 -0.0103 423  HIS A O   
3006  C CB  . HIS A 425  ? 0.4222 0.3675 0.4394 -0.0094 -0.0256 -0.0084 423  HIS A CB  
3007  C CG  . HIS A 425  ? 0.3936 0.3457 0.4062 -0.0088 -0.0236 -0.0092 423  HIS A CG  
3008  N ND1 . HIS A 425  ? 0.4401 0.3950 0.4472 -0.0079 -0.0210 -0.0074 423  HIS A ND1 
3009  C CD2 . HIS A 425  ? 0.3932 0.3497 0.4061 -0.0090 -0.0240 -0.0114 423  HIS A CD2 
3010  C CE1 . HIS A 425  ? 0.4433 0.4040 0.4477 -0.0076 -0.0199 -0.0083 423  HIS A CE1 
3011  N NE2 . HIS A 425  ? 0.3686 0.3306 0.3763 -0.0083 -0.0217 -0.0107 423  HIS A NE2 
3012  N N   . ASN A 426  ? 0.4085 0.3397 0.4374 -0.0148 -0.0286 -0.0007 424  ASN A N   
3013  C CA  . ASN A 426  ? 0.4450 0.3694 0.4783 -0.0154 -0.0307 0.0010  424  ASN A CA  
3014  C C   . ASN A 426  ? 0.4319 0.3536 0.4723 -0.0173 -0.0336 -0.0004 424  ASN A C   
3015  O O   . ASN A 426  ? 0.4487 0.3713 0.4907 -0.0199 -0.0328 0.0025  424  ASN A O   
3016  C CB  . ASN A 426  ? 0.3863 0.3086 0.4173 -0.0170 -0.0283 0.0077  424  ASN A CB  
3017  C CG  . ASN A 426  ? 0.4543 0.3699 0.4892 -0.0177 -0.0304 0.0102  424  ASN A CG  
3018  O OD1 . ASN A 426  ? 0.4404 0.3520 0.4816 -0.0186 -0.0334 0.0090  424  ASN A OD1 
3019  N ND2 . ASN A 426  ? 0.3665 0.2807 0.3978 -0.0172 -0.0288 0.0140  424  ASN A ND2 
3020  N N   . ALA A 427  ? 0.4228 0.3413 0.4677 -0.0159 -0.0372 -0.0050 425  ALA A N   
3021  C CA  . ALA A 427  ? 0.4420 0.3580 0.4942 -0.0174 -0.0404 -0.0072 425  ALA A CA  
3022  C C   . ALA A 427  ? 0.4487 0.3593 0.5055 -0.0208 -0.0409 -0.0014 425  ALA A C   
3023  O O   . ALA A 427  ? 0.3892 0.2993 0.4511 -0.0232 -0.0422 -0.0012 425  ALA A O   
3024  C CB  . ALA A 427  ? 0.4837 0.3970 0.5402 -0.0150 -0.0443 -0.0135 425  ALA A CB  
3025  N N   . GLN A 428  ? 0.4322 0.3391 0.4876 -0.0211 -0.0399 0.0035  426  GLN A N   
3026  C CA  . GLN A 428  ? 0.4442 0.3466 0.5034 -0.0244 -0.0401 0.0098  426  GLN A CA  
3027  C C   . GLN A 428  ? 0.4394 0.3464 0.4961 -0.0270 -0.0367 0.0143  426  GLN A C   
3028  O O   . GLN A 428  ? 0.4088 0.3147 0.4704 -0.0301 -0.0373 0.0171  426  GLN A O   
3029  C CB  . GLN A 428  ? 0.4602 0.3582 0.5179 -0.0238 -0.0399 0.0138  426  GLN A CB  
3030  C CG  . GLN A 428  ? 0.4658 0.3581 0.5288 -0.0268 -0.0413 0.0196  426  GLN A CG  
3031  C CD  . GLN A 428  ? 0.4795 0.3748 0.5405 -0.0300 -0.0380 0.0261  426  GLN A CD  
3032  O OE1 . GLN A 428  ? 0.4985 0.3988 0.5528 -0.0293 -0.0343 0.0277  426  GLN A OE1 
3033  N NE2 . GLN A 428  ? 0.4289 0.3215 0.4962 -0.0334 -0.0393 0.0296  426  GLN A NE2 
3034  N N   . THR A 429  ? 0.4851 0.3973 0.5346 -0.0257 -0.0331 0.0150  427  THR A N   
3035  C CA  . THR A 429  ? 0.3873 0.3043 0.4341 -0.0276 -0.0299 0.0184  427  THR A CA  
3036  C C   . THR A 429  ? 0.4240 0.3440 0.4745 -0.0288 -0.0310 0.0153  427  THR A C   
3037  O O   . THR A 429  ? 0.4108 0.3317 0.4645 -0.0317 -0.0305 0.0185  427  THR A O   
3038  C CB  . THR A 429  ? 0.4398 0.3616 0.4787 -0.0255 -0.0266 0.0183  427  THR A CB  
3039  O OG1 . THR A 429  ? 0.4534 0.3725 0.4891 -0.0240 -0.0261 0.0202  427  THR A OG1 
3040  C CG2 . THR A 429  ? 0.3938 0.3200 0.4300 -0.0272 -0.0234 0.0223  427  THR A CG2 
3041  N N   . LEU A 430  ? 0.3883 0.3104 0.4386 -0.0266 -0.0326 0.0091  428  LEU A N   
3042  C CA  . LEU A 430  ? 0.3733 0.2986 0.4270 -0.0273 -0.0340 0.0054  428  LEU A CA  
3043  C C   . LEU A 430  ? 0.4091 0.3301 0.4712 -0.0302 -0.0369 0.0062  428  LEU A C   
3044  O O   . LEU A 430  ? 0.4356 0.3590 0.5005 -0.0326 -0.0365 0.0077  428  LEU A O   
3045  C CB  . LEU A 430  ? 0.3830 0.3104 0.4355 -0.0242 -0.0358 -0.0017 428  LEU A CB  
3046  C CG  . LEU A 430  ? 0.4226 0.3552 0.4762 -0.0237 -0.0369 -0.0067 428  LEU A CG  
3047  C CD1 . LEU A 430  ? 0.4249 0.3603 0.4751 -0.0202 -0.0378 -0.0125 428  LEU A CD1 
3048  C CD2 . LEU A 430  ? 0.4275 0.3574 0.4892 -0.0257 -0.0404 -0.0088 428  LEU A CD2 
3049  N N   . ALA A 431  ? 0.4147 0.3293 0.4813 -0.0299 -0.0399 0.0052  429  ALA A N   
3050  C CA  . ALA A 431  ? 0.3976 0.3075 0.4728 -0.0327 -0.0431 0.0058  429  ALA A CA  
3051  C C   . ALA A 431  ? 0.3867 0.2959 0.4636 -0.0364 -0.0412 0.0133  429  ALA A C   
3052  O O   . ALA A 431  ? 0.3839 0.2935 0.4665 -0.0394 -0.0423 0.0142  429  ALA A O   
3053  C CB  . ALA A 431  ? 0.4493 0.3519 0.5287 -0.0314 -0.0468 0.0040  429  ALA A CB  
3054  N N   . ALA A 432  ? 0.3989 0.3079 0.4710 -0.0364 -0.0384 0.0187  430  ALA A N   
3055  C CA  . ALA A 432  ? 0.3835 0.2927 0.4566 -0.0398 -0.0363 0.0259  430  ALA A CA  
3056  C C   . ALA A 432  ? 0.3717 0.2876 0.4439 -0.0414 -0.0339 0.0266  430  ALA A C   
3057  O O   . ALA A 432  ? 0.4187 0.3350 0.4960 -0.0448 -0.0340 0.0300  430  ALA A O   
3058  C CB  . ALA A 432  ? 0.3888 0.2977 0.4556 -0.0389 -0.0335 0.0306  430  ALA A CB  
3059  N N   . ILE A 433  ? 0.4139 0.3353 0.4802 -0.0390 -0.0319 0.0234  431  ILE A N   
3060  C CA  . ILE A 433  ? 0.3955 0.3234 0.4606 -0.0401 -0.0297 0.0239  431  ILE A CA  
3061  C C   . ILE A 433  ? 0.4025 0.3313 0.4739 -0.0414 -0.0325 0.0199  431  ILE A C   
3062  O O   . ILE A 433  ? 0.3806 0.3123 0.4556 -0.0441 -0.0319 0.0221  431  ILE A O   
3063  C CB  . ILE A 433  ? 0.3810 0.3139 0.4381 -0.0370 -0.0270 0.0217  431  ILE A CB  
3064  C CG1 . ILE A 433  ? 0.3469 0.2795 0.3981 -0.0362 -0.0241 0.0260  431  ILE A CG1 
3065  C CG2 . ILE A 433  ? 0.3921 0.3315 0.4486 -0.0376 -0.0255 0.0211  431  ILE A CG2 
3066  C CD1 . ILE A 433  ? 0.4247 0.3620 0.4686 -0.0336 -0.0214 0.0247  431  ILE A CD1 
3067  N N   . TYR A 434  ? 0.3985 0.3254 0.4716 -0.0393 -0.0356 0.0138  432  TYR A N   
3068  C CA  . TYR A 434  ? 0.4057 0.3333 0.4850 -0.0402 -0.0387 0.0093  432  TYR A CA  
3069  C C   . TYR A 434  ? 0.4334 0.3574 0.5212 -0.0443 -0.0405 0.0126  432  TYR A C   
3070  O O   . TYR A 434  ? 0.3765 0.3038 0.4684 -0.0465 -0.0409 0.0124  432  TYR A O   
3071  C CB  . TYR A 434  ? 0.4125 0.3377 0.4926 -0.0373 -0.0420 0.0024  432  TYR A CB  
3072  C CG  . TYR A 434  ? 0.4229 0.3478 0.5101 -0.0380 -0.0459 -0.0029 432  TYR A CG  
3073  C CD1 . TYR A 434  ? 0.4106 0.3419 0.4972 -0.0377 -0.0458 -0.0064 432  TYR A CD1 
3074  C CD2 . TYR A 434  ? 0.4433 0.3614 0.5379 -0.0389 -0.0499 -0.0046 432  TYR A CD2 
3075  C CE1 . TYR A 434  ? 0.4287 0.3601 0.5220 -0.0383 -0.0496 -0.0116 432  TYR A CE1 
3076  C CE2 . TYR A 434  ? 0.4396 0.3574 0.5411 -0.0395 -0.0538 -0.0099 432  TYR A CE2 
3077  C CZ  . TYR A 434  ? 0.4863 0.4109 0.5871 -0.0392 -0.0536 -0.0135 432  TYR A CZ  
3078  O OH  . TYR A 434  ? 0.5560 0.4803 0.6636 -0.0398 -0.0576 -0.0190 432  TYR A OH  
3079  N N   . HIS A 435  ? 0.3897 0.3071 0.4803 -0.0454 -0.0417 0.0161  433  HIS A N   
3080  C CA  . HIS A 435  ? 0.4027 0.3166 0.5016 -0.0495 -0.0434 0.0199  433  HIS A CA  
3081  C C   . HIS A 435  ? 0.4558 0.3738 0.5536 -0.0525 -0.0398 0.0270  433  HIS A C   
3082  O O   . HIS A 435  ? 0.4306 0.3491 0.5348 -0.0561 -0.0405 0.0295  433  HIS A O   
3083  C CB  . HIS A 435  ? 0.4210 0.3265 0.5239 -0.0498 -0.0462 0.0214  433  HIS A CB  
3084  C CG  . HIS A 435  ? 0.4497 0.3508 0.5573 -0.0480 -0.0509 0.0144  433  HIS A CG  
3085  N ND1 . HIS A 435  ? 0.4758 0.3750 0.5923 -0.0501 -0.0546 0.0115  433  HIS A ND1 
3086  C CD2 . HIS A 435  ? 0.5008 0.3997 0.6057 -0.0441 -0.0524 0.0092  433  HIS A CD2 
3087  C CE1 . HIS A 435  ? 0.4362 0.3319 0.5551 -0.0475 -0.0583 0.0047  433  HIS A CE1 
3088  N NE2 . HIS A 435  ? 0.4310 0.3267 0.5430 -0.0438 -0.0570 0.0032  433  HIS A NE2 
3089  N N   . MET A 436  ? 0.4300 0.3511 0.5198 -0.0510 -0.0358 0.0300  434  MET A N   
3090  C CA  . MET A 436  ? 0.4256 0.3514 0.5138 -0.0533 -0.0322 0.0361  434  MET A CA  
3091  C C   . MET A 436  ? 0.4348 0.3674 0.5243 -0.0543 -0.0313 0.0343  434  MET A C   
3092  O O   . MET A 436  ? 0.4434 0.3790 0.5364 -0.0575 -0.0301 0.0384  434  MET A O   
3093  C CB  . MET A 436  ? 0.3904 0.3184 0.4696 -0.0510 -0.0285 0.0387  434  MET A CB  
3094  C CG  . MET A 436  ? 0.4177 0.3514 0.4947 -0.0528 -0.0246 0.0442  434  MET A CG  
3095  S SD  . MET A 436  ? 0.4774 0.4135 0.5442 -0.0499 -0.0205 0.0466  434  MET A SD  
3096  C CE  . MET A 436  ? 0.4417 0.3701 0.5091 -0.0500 -0.0222 0.0498  434  MET A CE  
3097  N N   . ALA A 437  ? 0.4058 0.3410 0.4926 -0.0515 -0.0320 0.0281  435  ALA A N   
3098  C CA  . ALA A 437  ? 0.4477 0.3897 0.5348 -0.0518 -0.0311 0.0262  435  ALA A CA  
3099  C C   . ALA A 437  ? 0.4560 0.3979 0.5522 -0.0549 -0.0341 0.0248  435  ALA A C   
3100  O O   . ALA A 437  ? 0.4101 0.3579 0.5080 -0.0562 -0.0331 0.0249  435  ALA A O   
3101  C CB  . ALA A 437  ? 0.4200 0.3650 0.5015 -0.0479 -0.0312 0.0203  435  ALA A CB  
3102  N N   . GLY A 438  ? 0.4635 0.3990 0.5661 -0.0561 -0.0378 0.0234  436  GLY A N   
3103  C CA  . GLY A 438  ? 0.4595 0.3942 0.5713 -0.0592 -0.0409 0.0222  436  GLY A CA  
3104  C C   . GLY A 438  ? 0.5322 0.4695 0.6456 -0.0574 -0.0436 0.0144  436  GLY A C   
3105  O O   . GLY A 438  ? 0.4336 0.3729 0.5409 -0.0536 -0.0433 0.0099  436  GLY A O   
3106  N N   . LYS A 439  ? 0.5428 0.4805 0.6646 -0.0604 -0.0463 0.0131  437  LYS A N   
3107  C CA  . LYS A 439  ? 0.5133 0.4524 0.6383 -0.0591 -0.0498 0.0055  437  LYS A CA  
3108  C C   . LYS A 439  ? 0.5670 0.5149 0.6891 -0.0582 -0.0482 0.0033  437  LYS A C   
3109  O O   . LYS A 439  ? 0.5761 0.5265 0.6974 -0.0558 -0.0503 -0.0032 437  LYS A O   
3110  C CB  . LYS A 439  ? 0.5864 0.5211 0.7227 -0.0626 -0.0541 0.0045  437  LYS A CB  
3111  N N   . ASP A 440  ? 0.5209 0.4738 0.6414 -0.0600 -0.0447 0.0086  438  ASP A N   
3112  C CA  . ASP A 440  ? 0.5005 0.4617 0.6183 -0.0590 -0.0431 0.0069  438  ASP A CA  
3113  C C   . ASP A 440  ? 0.5028 0.4668 0.6105 -0.0546 -0.0408 0.0051  438  ASP A C   
3114  O O   . ASP A 440  ? 0.5023 0.4659 0.6041 -0.0538 -0.0374 0.0094  438  ASP A O   
3115  C CB  . ASP A 440  ? 0.5729 0.5386 0.6925 -0.0621 -0.0401 0.0129  438  ASP A CB  
3116  C CG  . ASP A 440  ? 0.5822 0.5477 0.7123 -0.0665 -0.0426 0.0138  438  ASP A CG  
3117  O OD1 . ASP A 440  ? 0.5554 0.5165 0.6915 -0.0671 -0.0468 0.0096  438  ASP A OD1 
3118  O OD2 . ASP A 440  ? 0.6281 0.5979 0.7607 -0.0693 -0.0403 0.0186  438  ASP A OD2 
3119  N N   . PHE A 441  ? 0.4300 0.3969 0.5356 -0.0519 -0.0426 -0.0011 439  PHE A N   
3120  C CA  . PHE A 441  ? 0.4426 0.4125 0.5389 -0.0479 -0.0405 -0.0027 439  PHE A CA  
3121  C C   . PHE A 441  ? 0.4326 0.4099 0.5276 -0.0464 -0.0411 -0.0067 439  PHE A C   
3122  O O   . PHE A 441  ? 0.3995 0.3784 0.5002 -0.0474 -0.0442 -0.0107 439  PHE A O   
3123  C CB  . PHE A 441  ? 0.4337 0.3990 0.5267 -0.0450 -0.0420 -0.0063 439  PHE A CB  
3124  C CG  . PHE A 441  ? 0.4369 0.4055 0.5206 -0.0413 -0.0395 -0.0072 439  PHE A CG  
3125  C CD1 . PHE A 441  ? 0.3852 0.3530 0.4631 -0.0407 -0.0359 -0.0022 439  PHE A CD1 
3126  C CD2 . PHE A 441  ? 0.4294 0.4024 0.5101 -0.0386 -0.0409 -0.0127 439  PHE A CD2 
3127  C CE1 . PHE A 441  ? 0.3396 0.3104 0.4094 -0.0376 -0.0337 -0.0028 439  PHE A CE1 
3128  C CE2 . PHE A 441  ? 0.3612 0.3375 0.4336 -0.0355 -0.0386 -0.0129 439  PHE A CE2 
3129  C CZ  . PHE A 441  ? 0.3556 0.3305 0.4227 -0.0351 -0.0351 -0.0079 439  PHE A CZ  
3130  N N   . HIS A 442  ? 0.4276 0.4092 0.5149 -0.0439 -0.0381 -0.0056 440  HIS A N   
3131  C CA  . HIS A 442  ? 0.3881 0.3764 0.4724 -0.0417 -0.0386 -0.0092 440  HIS A CA  
3132  C C   . HIS A 442  ? 0.4064 0.3964 0.4815 -0.0385 -0.0358 -0.0083 440  HIS A C   
3133  O O   . HIS A 442  ? 0.3918 0.3793 0.4632 -0.0384 -0.0329 -0.0038 440  HIS A O   
3134  C CB  . HIS A 442  ? 0.3908 0.3849 0.4785 -0.0436 -0.0379 -0.0074 440  HIS A CB  
3135  C CG  . HIS A 442  ? 0.3489 0.3443 0.4340 -0.0445 -0.0339 -0.0012 440  HIS A CG  
3136  N ND1 . HIS A 442  ? 0.4012 0.4006 0.4793 -0.0420 -0.0311 0.0003  440  HIS A ND1 
3137  C CD2 . HIS A 442  ? 0.3279 0.3217 0.4168 -0.0475 -0.0322 0.0038  440  HIS A CD2 
3138  C CE1 . HIS A 442  ? 0.3488 0.3488 0.4265 -0.0433 -0.0280 0.0056  440  HIS A CE1 
3139  N NE2 . HIS A 442  ? 0.3957 0.3927 0.4797 -0.0466 -0.0285 0.0078  440  HIS A NE2 
3140  N N   . VAL A 443  ? 0.4197 0.4140 0.4909 -0.0357 -0.0368 -0.0125 441  VAL A N   
3141  C CA  . VAL A 443  ? 0.4020 0.3983 0.4647 -0.0328 -0.0344 -0.0115 441  VAL A CA  
3142  C C   . VAL A 443  ? 0.3983 0.3973 0.4587 -0.0333 -0.0310 -0.0063 441  VAL A C   
3143  O O   . VAL A 443  ? 0.3958 0.3992 0.4595 -0.0345 -0.0312 -0.0056 441  VAL A O   
3144  C CB  . VAL A 443  ? 0.4386 0.4403 0.4981 -0.0301 -0.0361 -0.0165 441  VAL A CB  
3145  C CG1 . VAL A 443  ? 0.3711 0.3759 0.4225 -0.0276 -0.0334 -0.0144 441  VAL A CG1 
3146  C CG2 . VAL A 443  ? 0.4897 0.4885 0.5502 -0.0289 -0.0389 -0.0216 441  VAL A CG2 
3147  N N   . GLY A 444  ? 0.3278 0.3246 0.3829 -0.0323 -0.0281 -0.0027 442  GLY A N   
3148  C CA  . GLY A 444  ? 0.3234 0.3220 0.3765 -0.0327 -0.0249 0.0022  442  GLY A CA  
3149  C C   . GLY A 444  ? 0.3350 0.3297 0.3912 -0.0353 -0.0233 0.0065  442  GLY A C   
3150  O O   . GLY A 444  ? 0.3602 0.3562 0.4140 -0.0353 -0.0203 0.0105  442  GLY A O   
3151  N N   . LYS A 445  ? 0.3415 0.3318 0.4029 -0.0374 -0.0252 0.0059  443  LYS A N   
3152  C CA  . LYS A 445  ? 0.2964 0.2831 0.3604 -0.0398 -0.0236 0.0105  443  LYS A CA  
3153  C C   . LYS A 445  ? 0.3325 0.3149 0.3908 -0.0383 -0.0217 0.0126  443  LYS A C   
3154  O O   . LYS A 445  ? 0.3206 0.3032 0.3767 -0.0387 -0.0188 0.0170  443  LYS A O   
3155  C CB  . LYS A 445  ? 0.3231 0.3061 0.3949 -0.0426 -0.0265 0.0095  443  LYS A CB  
3156  C CG  . LYS A 445  ? 0.3444 0.3251 0.4200 -0.0458 -0.0251 0.0148  443  LYS A CG  
3157  C CD  . LYS A 445  ? 0.4055 0.3818 0.4891 -0.0487 -0.0282 0.0141  443  LYS A CD  
3158  C CE  . LYS A 445  ? 0.4741 0.4494 0.5616 -0.0522 -0.0266 0.0201  443  LYS A CE  
3159  N NZ  . LYS A 445  ? 0.5349 0.5052 0.6305 -0.0552 -0.0297 0.0201  443  LYS A NZ  
3160  N N   . TYR A 446  ? 0.3238 0.3028 0.3801 -0.0366 -0.0233 0.0094  444  TYR A N   
3161  C CA  . TYR A 446  ? 0.2957 0.2714 0.3461 -0.0347 -0.0217 0.0106  444  TYR A CA  
3162  C C   . TYR A 446  ? 0.3162 0.2911 0.3644 -0.0322 -0.0239 0.0055  444  TYR A C   
3163  O O   . TYR A 446  ? 0.3078 0.2844 0.3592 -0.0321 -0.0266 0.0013  444  TYR A O   
3164  C CB  . TYR A 446  ? 0.3070 0.2773 0.3593 -0.0364 -0.0212 0.0143  444  TYR A CB  
3165  C CG  . TYR A 446  ? 0.3157 0.2810 0.3740 -0.0379 -0.0245 0.0122  444  TYR A CG  
3166  C CD1 . TYR A 446  ? 0.3598 0.3209 0.4167 -0.0361 -0.0263 0.0091  444  TYR A CD1 
3167  C CD2 . TYR A 446  ? 0.3685 0.3335 0.4342 -0.0410 -0.0260 0.0131  444  TYR A CD2 
3168  C CE1 . TYR A 446  ? 0.3926 0.3489 0.4555 -0.0372 -0.0296 0.0069  444  TYR A CE1 
3169  C CE2 . TYR A 446  ? 0.3623 0.3224 0.4340 -0.0424 -0.0293 0.0112  444  TYR A CE2 
3170  C CZ  . TYR A 446  ? 0.4218 0.3774 0.4921 -0.0404 -0.0312 0.0079  444  TYR A CZ  
3171  O OH  . TYR A 446  ? 0.4875 0.4380 0.5644 -0.0416 -0.0347 0.0058  444  TYR A OH  
3172  N N   . GLU A 447  ? 0.2700 0.2427 0.3130 -0.0302 -0.0227 0.0058  445  GLU A N   
3173  C CA  . GLU A 447  ? 0.3173 0.2896 0.3581 -0.0279 -0.0245 0.0011  445  GLU A CA  
3174  C C   . GLU A 447  ? 0.2741 0.2414 0.3120 -0.0269 -0.0237 0.0024  445  GLU A C   
3175  O O   . GLU A 447  ? 0.3150 0.2803 0.3514 -0.0277 -0.0215 0.0069  445  GLU A O   
3176  C CB  . GLU A 447  ? 0.2679 0.2460 0.3034 -0.0255 -0.0237 -0.0008 445  GLU A CB  
3177  C CG  . GLU A 447  ? 0.3091 0.2879 0.3382 -0.0241 -0.0205 0.0025  445  GLU A CG  
3178  C CD  . GLU A 447  ? 0.2843 0.2687 0.3087 -0.0221 -0.0199 0.0011  445  GLU A CD  
3179  O OE1 . GLU A 447  ? 0.3009 0.2894 0.3270 -0.0219 -0.0217 -0.0018 445  GLU A OE1 
3180  O OE2 . GLU A 447  ? 0.2808 0.2656 0.3000 -0.0207 -0.0178 0.0031  445  GLU A OE2 
3181  N N   . PHE A 448  ? 0.3281 0.2941 0.3654 -0.0251 -0.0256 -0.0017 446  PHE A N   
3182  C CA  . PHE A 448  ? 0.3109 0.2736 0.3446 -0.0235 -0.0249 -0.0013 446  PHE A CA  
3183  C C   . PHE A 448  ? 0.3049 0.2720 0.3320 -0.0210 -0.0234 -0.0026 446  PHE A C   
3184  O O   . PHE A 448  ? 0.3131 0.2854 0.3389 -0.0202 -0.0235 -0.0045 446  PHE A O   
3185  C CB  . PHE A 448  ? 0.3428 0.3012 0.3804 -0.0230 -0.0280 -0.0050 446  PHE A CB  
3186  C CG  . PHE A 448  ? 0.3470 0.3001 0.3912 -0.0257 -0.0295 -0.0030 446  PHE A CG  
3187  C CD1 . PHE A 448  ? 0.3564 0.3046 0.4004 -0.0266 -0.0284 0.0014  446  PHE A CD1 
3188  C CD2 . PHE A 448  ? 0.3597 0.3128 0.4101 -0.0273 -0.0321 -0.0052 446  PHE A CD2 
3189  C CE1 . PHE A 448  ? 0.3715 0.3150 0.4215 -0.0292 -0.0297 0.0039  446  PHE A CE1 
3190  C CE2 . PHE A 448  ? 0.3765 0.3247 0.4334 -0.0300 -0.0336 -0.0029 446  PHE A CE2 
3191  C CZ  . PHE A 448  ? 0.3987 0.3421 0.4553 -0.0310 -0.0323 0.0019  446  PHE A CZ  
3192  N N   . GLN A 449  ? 0.2823 0.2474 0.3055 -0.0196 -0.0220 -0.0014 447  GLN A N   
3193  C CA  . GLN A 449  ? 0.2912 0.2600 0.3085 -0.0173 -0.0206 -0.0025 447  GLN A CA  
3194  C C   . GLN A 449  ? 0.3344 0.3003 0.3501 -0.0157 -0.0211 -0.0041 447  GLN A C   
3195  O O   . GLN A 449  ? 0.3286 0.2892 0.3465 -0.0164 -0.0216 -0.0028 447  GLN A O   
3196  C CB  . GLN A 449  ? 0.2709 0.2414 0.2838 -0.0175 -0.0174 0.0019  447  GLN A CB  
3197  C CG  . GLN A 449  ? 0.3031 0.2767 0.3174 -0.0189 -0.0168 0.0037  447  GLN A CG  
3198  C CD  . GLN A 449  ? 0.3236 0.3000 0.3333 -0.0182 -0.0141 0.0067  447  GLN A CD  
3199  O OE1 . GLN A 449  ? 0.2777 0.2526 0.2836 -0.0173 -0.0124 0.0084  447  GLN A OE1 
3200  N NE2 . GLN A 449  ? 0.2583 0.2386 0.2684 -0.0187 -0.0137 0.0074  447  GLN A NE2 
3201  N N   . CYS A 450  ? 0.3015 0.2714 0.3133 -0.0135 -0.0209 -0.0068 448  CYS A N   
3202  C CA  . CYS A 450  ? 0.3431 0.3118 0.3530 -0.0117 -0.0212 -0.0089 448  CYS A CA  
3203  C C   . CYS A 450  ? 0.3441 0.3181 0.3483 -0.0100 -0.0195 -0.0091 448  CYS A C   
3204  O O   . CYS A 450  ? 0.3577 0.3363 0.3599 -0.0102 -0.0186 -0.0084 448  CYS A O   
3205  C CB  . CYS A 450  ? 0.3136 0.2816 0.3275 -0.0106 -0.0245 -0.0143 448  CYS A CB  
3206  S SG  . CYS A 450  ? 0.3913 0.3672 0.4045 -0.0090 -0.0261 -0.0200 448  CYS A SG  
3207  N N   . LEU A 451  ? 0.3745 0.3480 0.3763 -0.0085 -0.0190 -0.0098 449  LEU A N   
3208  C CA  . LEU A 451  ? 0.3607 0.3393 0.3575 -0.0071 -0.0174 -0.0100 449  LEU A CA  
3209  C C   . LEU A 451  ? 0.3508 0.3345 0.3474 -0.0053 -0.0192 -0.0153 449  LEU A C   
3210  O O   . LEU A 451  ? 0.3646 0.3469 0.3646 -0.0045 -0.0215 -0.0193 449  LEU A O   
3211  C CB  . LEU A 451  ? 0.4150 0.3910 0.4092 -0.0064 -0.0160 -0.0081 449  LEU A CB  
3212  N N   . HIS A 452  ? 0.3468 0.3369 0.3396 -0.0046 -0.0180 -0.0152 450  HIS A N   
3213  C CA  . HIS A 452  ? 0.3872 0.3837 0.3789 -0.0028 -0.0192 -0.0198 450  HIS A CA  
3214  C C   . HIS A 452  ? 0.4167 0.4127 0.4081 -0.0010 -0.0197 -0.0226 450  HIS A C   
3215  O O   . HIS A 452  ? 0.3680 0.3619 0.3575 -0.0010 -0.0180 -0.0199 450  HIS A O   
3216  C CB  . HIS A 452  ? 0.3613 0.3645 0.3482 -0.0026 -0.0175 -0.0179 450  HIS A CB  
3217  C CG  . HIS A 452  ? 0.3844 0.3950 0.3692 -0.0006 -0.0181 -0.0219 450  HIS A CG  
3218  N ND1 . HIS A 452  ? 0.4068 0.4228 0.3924 0.0002  -0.0200 -0.0259 450  HIS A ND1 
3219  C CD2 . HIS A 452  ? 0.4013 0.4151 0.3832 0.0007  -0.0171 -0.0225 450  HIS A CD2 
3220  C CE1 . HIS A 452  ? 0.3983 0.4210 0.3814 0.0020  -0.0200 -0.0288 450  HIS A CE1 
3221  N NE2 . HIS A 452  ? 0.4107 0.4322 0.3916 0.0022  -0.0182 -0.0267 450  HIS A NE2 
3222  N N   . GLY A 453  ? 0.5038 0.5023 0.4976 0.0005  -0.0221 -0.0283 451  GLY A N   
3223  C CA  . GLY A 453  ? 0.4769 0.4753 0.4711 0.0025  -0.0229 -0.0316 451  GLY A CA  
3224  C C   . GLY A 453  ? 0.5242 0.5144 0.5230 0.0023  -0.0245 -0.0321 451  GLY A C   
3225  O O   . GLY A 453  ? 0.6561 0.6455 0.6581 0.0039  -0.0269 -0.0370 451  GLY A O   
3226  N N   . MET A 454  ? 0.5250 0.5090 0.5242 0.0003  -0.0233 -0.0270 452  MET A N   
3227  C CA  . MET A 454  ? 0.4868 0.4631 0.4898 0.0000  -0.0245 -0.0263 452  MET A CA  
3228  C C   . MET A 454  ? 0.5059 0.4780 0.5146 -0.0012 -0.0271 -0.0279 452  MET A C   
3229  O O   . MET A 454  ? 0.4828 0.4512 0.4957 -0.0002 -0.0298 -0.0312 452  MET A O   
3230  C CB  . MET A 454  ? 0.4473 0.4195 0.4479 -0.0016 -0.0220 -0.0202 452  MET A CB  
3231  C CG  . MET A 454  ? 0.4769 0.4422 0.4800 -0.0015 -0.0228 -0.0190 452  MET A CG  
3232  S SD  . MET A 454  ? 0.7994 0.7664 0.8015 0.0014  -0.0235 -0.0228 452  MET A SD  
3233  C CE  . MET A 454  ? 0.6494 0.6223 0.6449 0.0015  -0.0199 -0.0199 452  MET A CE  
3234  N N   . GLY A 455  ? 0.4570 0.4295 0.4662 -0.0031 -0.0267 -0.0256 453  GLY A N   
3235  C CA  . GLY A 455  ? 0.4340 0.4018 0.4489 -0.0048 -0.0288 -0.0257 453  GLY A CA  
3236  C C   . GLY A 455  ? 0.4477 0.4180 0.4665 -0.0043 -0.0318 -0.0312 453  GLY A C   
3237  O O   . GLY A 455  ? 0.4478 0.4136 0.4722 -0.0056 -0.0340 -0.0318 453  GLY A O   
3238  N N   . GLU A 456  ? 0.4720 0.4496 0.4880 -0.0025 -0.0319 -0.0351 454  GLU A N   
3239  C CA  . GLU A 456  ? 0.4951 0.4758 0.5145 -0.0018 -0.0348 -0.0407 454  GLU A CA  
3240  C C   . GLU A 456  ? 0.4947 0.4708 0.5203 -0.0009 -0.0384 -0.0455 454  GLU A C   
3241  O O   . GLU A 456  ? 0.5118 0.4861 0.5426 -0.0019 -0.0410 -0.0478 454  GLU A O   
3242  C CB  . GLU A 456  ? 0.4982 0.4884 0.5132 0.0003  -0.0343 -0.0442 454  GLU A CB  
3243  C CG  . GLU A 456  ? 0.5046 0.4998 0.5144 -0.0007 -0.0315 -0.0401 454  GLU A CG  
3244  C CD  . GLU A 456  ? 0.4649 0.4618 0.4691 -0.0001 -0.0284 -0.0365 454  GLU A CD  
3245  O OE1 . GLU A 456  ? 0.4578 0.4499 0.4625 0.0002  -0.0280 -0.0354 454  GLU A OE1 
3246  O OE2 . GLU A 456  ? 0.5197 0.5227 0.5193 0.0001  -0.0266 -0.0347 454  GLU A OE2 
3247  N N   . PRO A 457  ? 0.4934 0.4673 0.5191 0.0010  -0.0389 -0.0473 455  PRO A N   
3248  C CA  . PRO A 457  ? 0.5420 0.5106 0.5742 0.0019  -0.0427 -0.0518 455  PRO A CA  
3249  C C   . PRO A 457  ? 0.4952 0.4557 0.5332 -0.0009 -0.0442 -0.0486 455  PRO A C   
3250  O O   . PRO A 457  ? 0.4581 0.4160 0.5023 -0.0011 -0.0476 -0.0525 455  PRO A O   
3251  C CB  . PRO A 457  ? 0.4845 0.4514 0.5152 0.0040  -0.0422 -0.0521 455  PRO A CB  
3252  C CG  . PRO A 457  ? 0.5535 0.5275 0.5768 0.0050  -0.0389 -0.0506 455  PRO A CG  
3253  C CD  . PRO A 457  ? 0.5050 0.4808 0.5253 0.0025  -0.0364 -0.0455 455  PRO A CD  
3254  N N   . LEU A 458  ? 0.4851 0.4417 0.5214 -0.0032 -0.0416 -0.0416 456  LEU A N   
3255  C CA  . LEU A 458  ? 0.4867 0.4364 0.5282 -0.0061 -0.0426 -0.0379 456  LEU A CA  
3256  C C   . LEU A 458  ? 0.4708 0.4231 0.5145 -0.0081 -0.0432 -0.0382 456  LEU A C   
3257  O O   . LEU A 458  ? 0.4717 0.4206 0.5221 -0.0093 -0.0462 -0.0402 456  LEU A O   
3258  C CB  . LEU A 458  ? 0.4283 0.3745 0.4668 -0.0078 -0.0395 -0.0304 456  LEU A CB  
3259  C CG  . LEU A 458  ? 0.4350 0.3751 0.4779 -0.0111 -0.0398 -0.0254 456  LEU A CG  
3260  C CD1 . LEU A 458  ? 0.4442 0.3776 0.4947 -0.0114 -0.0438 -0.0278 456  LEU A CD1 
3261  C CD2 . LEU A 458  ? 0.4249 0.3626 0.4640 -0.0122 -0.0367 -0.0187 456  LEU A CD2 
3262  N N   . TYR A 459  ? 0.4612 0.4198 0.4998 -0.0084 -0.0405 -0.0364 457  TYR A N   
3263  C CA  . TYR A 459  ? 0.4352 0.3961 0.4758 -0.0105 -0.0407 -0.0357 457  TYR A CA  
3264  C C   . TYR A 459  ? 0.4357 0.4014 0.4787 -0.0092 -0.0436 -0.0425 457  TYR A C   
3265  O O   . TYR A 459  ? 0.4818 0.4488 0.5280 -0.0109 -0.0447 -0.0428 457  TYR A O   
3266  C CB  . TYR A 459  ? 0.4211 0.3864 0.4559 -0.0113 -0.0369 -0.0308 457  TYR A CB  
3267  C CG  . TYR A 459  ? 0.3931 0.3532 0.4276 -0.0134 -0.0347 -0.0241 457  TYR A CG  
3268  C CD1 . TYR A 459  ? 0.3978 0.3546 0.4369 -0.0163 -0.0351 -0.0209 457  TYR A CD1 
3269  C CD2 . TYR A 459  ? 0.3930 0.3518 0.4229 -0.0125 -0.0323 -0.0210 457  TYR A CD2 
3270  C CE1 . TYR A 459  ? 0.3626 0.3154 0.4013 -0.0182 -0.0330 -0.0148 457  TYR A CE1 
3271  C CE2 . TYR A 459  ? 0.3845 0.3390 0.4140 -0.0143 -0.0304 -0.0152 457  TYR A CE2 
3272  C CZ  . TYR A 459  ? 0.3801 0.3318 0.4139 -0.0171 -0.0307 -0.0120 457  TYR A CZ  
3273  O OH  . TYR A 459  ? 0.3814 0.3296 0.4145 -0.0188 -0.0286 -0.0062 457  TYR A OH  
3274  N N   . GLU A 460  ? 0.4640 0.4328 0.5059 -0.0061 -0.0451 -0.0482 458  GLU A N   
3275  C CA  . GLU A 460  ? 0.4766 0.4487 0.5222 -0.0048 -0.0486 -0.0555 458  GLU A CA  
3276  C C   . GLU A 460  ? 0.5100 0.4749 0.5644 -0.0062 -0.0523 -0.0575 458  GLU A C   
3277  O O   . GLU A 460  ? 0.5436 0.5103 0.6023 -0.0062 -0.0554 -0.0625 458  GLU A O   
3278  C CB  . GLU A 460  ? 0.5292 0.5062 0.5719 -0.0011 -0.0493 -0.0613 458  GLU A CB  
3279  C CG  . GLU A 460  ? 0.6100 0.5964 0.6451 0.0003  -0.0465 -0.0610 458  GLU A CG  
3280  C CD  . GLU A 460  ? 0.6715 0.6627 0.7034 0.0038  -0.0467 -0.0658 458  GLU A CD  
3281  O OE1 . GLU A 460  ? 0.6706 0.6577 0.7064 0.0053  -0.0490 -0.0695 458  GLU A OE1 
3282  O OE2 . GLU A 460  ? 0.7246 0.7240 0.7505 0.0050  -0.0446 -0.0658 458  GLU A OE2 
3283  N N   . GLU A 461  ? 0.5007 0.4574 0.5578 -0.0075 -0.0523 -0.0536 459  GLU A N   
3284  C CA  . GLU A 461  ? 0.5132 0.4622 0.5788 -0.0095 -0.0556 -0.0538 459  GLU A CA  
3285  C C   . GLU A 461  ? 0.5511 0.4979 0.6193 -0.0135 -0.0546 -0.0481 459  GLU A C   
3286  O O   . GLU A 461  ? 0.5246 0.4646 0.5997 -0.0157 -0.0568 -0.0467 459  GLU A O   
3287  C CB  . GLU A 461  ? 0.5223 0.4637 0.5895 -0.0089 -0.0561 -0.0518 459  GLU A CB  
3288  C CG  . GLU A 461  ? 0.5268 0.4705 0.5909 -0.0050 -0.0565 -0.0567 459  GLU A CG  
3289  C CD  . GLU A 461  ? 0.6342 0.5790 0.7034 -0.0027 -0.0609 -0.0654 459  GLU A CD  
3290  O OE1 . GLU A 461  ? 0.5917 0.5322 0.6683 -0.0044 -0.0642 -0.0670 459  GLU A OE1 
3291  O OE2 . GLU A 461  ? 0.6447 0.5948 0.7108 0.0008  -0.0611 -0.0707 459  GLU A OE2 
3292  N N   . VAL A 462  ? 0.4908 0.4431 0.5539 -0.0144 -0.0513 -0.0447 460  VAL A N   
3293  C CA  . VAL A 462  ? 0.4629 0.4139 0.5275 -0.0179 -0.0496 -0.0386 460  VAL A CA  
3294  C C   . VAL A 462  ? 0.4736 0.4314 0.5381 -0.0185 -0.0497 -0.0404 460  VAL A C   
3295  O O   . VAL A 462  ? 0.4799 0.4364 0.5503 -0.0210 -0.0515 -0.0403 460  VAL A O   
3296  C CB  . VAL A 462  ? 0.4571 0.4078 0.5154 -0.0184 -0.0453 -0.0316 460  VAL A CB  
3297  C CG1 . VAL A 462  ? 0.4177 0.3685 0.4771 -0.0217 -0.0433 -0.0259 460  VAL A CG1 
3298  C CG2 . VAL A 462  ? 0.4586 0.4027 0.5174 -0.0179 -0.0453 -0.0295 460  VAL A CG2 
3299  N N   . VAL A 463  ? 0.4494 0.4145 0.5072 -0.0163 -0.0479 -0.0419 461  VAL A N   
3300  C CA  . VAL A 463  ? 0.4629 0.4351 0.5196 -0.0166 -0.0478 -0.0432 461  VAL A CA  
3301  C C   . VAL A 463  ? 0.5031 0.4771 0.5652 -0.0160 -0.0520 -0.0504 461  VAL A C   
3302  O O   . VAL A 463  ? 0.5482 0.5214 0.6116 -0.0137 -0.0545 -0.0560 461  VAL A O   
3303  C CB  . VAL A 463  ? 0.4271 0.4063 0.4752 -0.0143 -0.0450 -0.0428 461  VAL A CB  
3304  C CG1 . VAL A 463  ? 0.4567 0.4434 0.5035 -0.0144 -0.0450 -0.0440 461  VAL A CG1 
3305  C CG2 . VAL A 463  ? 0.3547 0.3319 0.3979 -0.0149 -0.0410 -0.0360 461  VAL A CG2 
3306  N N   . GLY A 464  ? 0.4952 0.4719 0.5606 -0.0178 -0.0530 -0.0507 462  GLY A N   
3307  C CA  . GLY A 464  ? 0.5433 0.5232 0.6131 -0.0170 -0.0570 -0.0579 462  GLY A CA  
3308  C C   . GLY A 464  ? 0.5759 0.5496 0.6554 -0.0197 -0.0603 -0.0588 462  GLY A C   
3309  O O   . GLY A 464  ? 0.5690 0.5348 0.6522 -0.0214 -0.0605 -0.0556 462  GLY A O   
3310  N N   . ARG A 465  ? 0.5795 0.5570 0.6633 -0.0203 -0.0631 -0.0632 463  ARG A N   
3311  C CA  . ARG A 465  ? 0.5810 0.5534 0.6746 -0.0232 -0.0665 -0.0642 463  ARG A CA  
3312  C C   . ARG A 465  ? 0.5856 0.5508 0.6849 -0.0224 -0.0701 -0.0684 463  ARG A C   
3313  O O   . ARG A 465  ? 0.6295 0.5882 0.7372 -0.0252 -0.0725 -0.0675 463  ARG A O   
3314  C CB  . ARG A 465  ? 0.5212 0.5000 0.6179 -0.0236 -0.0690 -0.0689 463  ARG A CB  
3315  N N   . GLY A 466  ? 0.5873 0.5539 0.6827 -0.0187 -0.0705 -0.0729 464  GLY A N   
3316  C CA  . GLY A 466  ? 0.5445 0.5045 0.6451 -0.0175 -0.0739 -0.0772 464  GLY A CA  
3317  C C   . GLY A 466  ? 0.6516 0.6041 0.7512 -0.0179 -0.0721 -0.0718 464  GLY A C   
3318  O O   . GLY A 466  ? 0.6334 0.5797 0.7375 -0.0169 -0.0749 -0.0747 464  GLY A O   
3319  N N   . LYS A 467  ? 0.5900 0.5428 0.6838 -0.0192 -0.0676 -0.0641 465  LYS A N   
3320  C CA  . LYS A 467  ? 0.5190 0.4656 0.6110 -0.0194 -0.0656 -0.0588 465  LYS A CA  
3321  C C   . LYS A 467  ? 0.5536 0.4952 0.6487 -0.0236 -0.0639 -0.0509 465  LYS A C   
3322  O O   . LYS A 467  ? 0.6089 0.5454 0.7124 -0.0262 -0.0668 -0.0507 465  LYS A O   
3323  C CB  . LYS A 467  ? 0.5271 0.4787 0.6092 -0.0168 -0.0616 -0.0572 465  LYS A CB  
3324  C CG  . LYS A 467  ? 0.6115 0.5678 0.6906 -0.0126 -0.0631 -0.0646 465  LYS A CG  
3325  C CD  . LYS A 467  ? 0.5724 0.5219 0.6561 -0.0110 -0.0660 -0.0680 465  LYS A CD  
3326  C CE  . LYS A 467  ? 0.6003 0.5550 0.6808 -0.0066 -0.0672 -0.0753 465  LYS A CE  
3327  N NZ  . LYS A 467  ? 0.6222 0.5706 0.7052 -0.0047 -0.0689 -0.0771 465  LYS A NZ  
3328  N N   . LEU A 468  ? 0.5240 0.4673 0.6127 -0.0243 -0.0594 -0.0443 466  LEU A N   
3329  C CA  . LEU A 468  ? 0.5227 0.4631 0.6135 -0.0281 -0.0575 -0.0367 466  LEU A CA  
3330  C C   . LEU A 468  ? 0.5240 0.4710 0.6131 -0.0297 -0.0555 -0.0348 466  LEU A C   
3331  O O   . LEU A 468  ? 0.4659 0.4115 0.5577 -0.0330 -0.0541 -0.0293 466  LEU A O   
3332  C CB  . LEU A 468  ? 0.4750 0.4123 0.5604 -0.0280 -0.0540 -0.0305 466  LEU A CB  
3333  C CG  . LEU A 468  ? 0.4888 0.4190 0.5759 -0.0267 -0.0557 -0.0310 466  LEU A CG  
3334  C CD1 . LEU A 468  ? 0.4698 0.3977 0.5518 -0.0270 -0.0520 -0.0242 466  LEU A CD1 
3335  C CD2 . LEU A 468  ? 0.5303 0.4533 0.6275 -0.0290 -0.0598 -0.0316 466  LEU A CD2 
3336  N N   . ASP A 469  ? 0.5398 0.4942 0.6246 -0.0274 -0.0553 -0.0392 467  ASP A N   
3337  C CA  . ASP A 469  ? 0.5159 0.4773 0.5992 -0.0284 -0.0538 -0.0382 467  ASP A CA  
3338  C C   . ASP A 469  ? 0.4346 0.3971 0.5130 -0.0297 -0.0493 -0.0306 467  ASP A C   
3339  O O   . ASP A 469  ? 0.4307 0.3950 0.5113 -0.0323 -0.0483 -0.0273 467  ASP A O   
3340  C CB  . ASP A 469  ? 0.4841 0.4451 0.5760 -0.0311 -0.0570 -0.0401 467  ASP A CB  
3341  C CG  . ASP A 469  ? 0.5766 0.5460 0.6671 -0.0308 -0.0570 -0.0426 467  ASP A CG  
3342  O OD1 . ASP A 469  ? 0.5636 0.5389 0.6465 -0.0281 -0.0550 -0.0434 467  ASP A OD1 
3343  O OD2 . ASP A 469  ? 0.6547 0.6249 0.7518 -0.0332 -0.0591 -0.0435 467  ASP A OD2 
3344  N N   . ARG A 470  ? 0.4520 0.4136 0.5239 -0.0279 -0.0466 -0.0282 468  ARG A N   
3345  C CA  . ARG A 470  ? 0.3959 0.3591 0.4621 -0.0284 -0.0423 -0.0220 468  ARG A CA  
3346  C C   . ARG A 470  ? 0.3629 0.3315 0.4209 -0.0252 -0.0403 -0.0234 468  ARG A C   
3347  O O   . ARG A 470  ? 0.3891 0.3572 0.4447 -0.0227 -0.0412 -0.0269 468  ARG A O   
3348  C CB  . ARG A 470  ? 0.3635 0.3201 0.4299 -0.0296 -0.0408 -0.0168 468  ARG A CB  
3349  C CG  . ARG A 470  ? 0.3944 0.3459 0.4688 -0.0332 -0.0424 -0.0141 468  ARG A CG  
3350  C CD  . ARG A 470  ? 0.4053 0.3608 0.4822 -0.0359 -0.0413 -0.0112 468  ARG A CD  
3351  N NE  . ARG A 470  ? 0.4320 0.3831 0.5167 -0.0395 -0.0427 -0.0082 468  ARG A NE  
3352  C CZ  . ARG A 470  ? 0.4816 0.4317 0.5740 -0.0413 -0.0462 -0.0113 468  ARG A CZ  
3353  N NH1 . ARG A 470  ? 0.4587 0.4123 0.5520 -0.0397 -0.0487 -0.0178 468  ARG A NH1 
3354  N NH2 . ARG A 470  ? 0.4401 0.3861 0.5395 -0.0449 -0.0472 -0.0077 468  ARG A NH2 
3355  N N   . PRO A 471  ? 0.3767 0.3505 0.4305 -0.0252 -0.0377 -0.0207 469  PRO A N   
3356  C CA  . PRO A 471  ? 0.3344 0.3134 0.3808 -0.0224 -0.0360 -0.0217 469  PRO A CA  
3357  C C   . PRO A 471  ? 0.3827 0.3588 0.4238 -0.0214 -0.0332 -0.0182 469  PRO A C   
3358  O O   . PRO A 471  ? 0.3686 0.3401 0.4106 -0.0230 -0.0317 -0.0137 469  PRO A O   
3359  C CB  . PRO A 471  ? 0.3037 0.2882 0.3484 -0.0232 -0.0343 -0.0192 469  PRO A CB  
3360  C CG  . PRO A 471  ? 0.3591 0.3403 0.4082 -0.0262 -0.0334 -0.0146 469  PRO A CG  
3361  C CD  . PRO A 471  ? 0.3926 0.3683 0.4487 -0.0278 -0.0364 -0.0167 469  PRO A CD  
3362  N N   . CYS A 472  ? 0.3386 0.3180 0.3741 -0.0187 -0.0326 -0.0203 470  CYS A N   
3363  C CA  . CYS A 472  ? 0.3125 0.2902 0.3427 -0.0175 -0.0300 -0.0176 470  CYS A CA  
3364  C C   . CYS A 472  ? 0.3077 0.2916 0.3314 -0.0159 -0.0280 -0.0169 470  CYS A C   
3365  O O   . CYS A 472  ? 0.3561 0.3453 0.3784 -0.0143 -0.0292 -0.0207 470  CYS A O   
3366  C CB  . CYS A 472  ? 0.3379 0.3125 0.3685 -0.0158 -0.0316 -0.0210 470  CYS A CB  
3367  S SG  . CYS A 472  ? 0.3545 0.3273 0.3789 -0.0144 -0.0287 -0.0178 470  CYS A SG  
3368  N N   . ARG A 473  ? 0.2938 0.2770 0.3138 -0.0162 -0.0249 -0.0119 471  ARG A N   
3369  C CA  . ARG A 473  ? 0.3112 0.2993 0.3252 -0.0147 -0.0229 -0.0106 471  ARG A CA  
3370  C C   . ARG A 473  ? 0.3127 0.2996 0.3225 -0.0131 -0.0217 -0.0105 471  ARG A C   
3371  O O   . ARG A 473  ? 0.3301 0.3119 0.3400 -0.0136 -0.0207 -0.0082 471  ARG A O   
3372  C CB  . ARG A 473  ? 0.2852 0.2737 0.2979 -0.0159 -0.0205 -0.0056 471  ARG A CB  
3373  C CG  . ARG A 473  ? 0.2683 0.2617 0.2755 -0.0145 -0.0188 -0.0042 471  ARG A CG  
3374  C CD  . ARG A 473  ? 0.2561 0.2499 0.2628 -0.0155 -0.0168 0.0002  471  ARG A CD  
3375  N NE  . ARG A 473  ? 0.2795 0.2741 0.2909 -0.0171 -0.0179 0.0001  471  ARG A NE  
3376  C CZ  . ARG A 473  ? 0.2986 0.2982 0.3109 -0.0168 -0.0191 -0.0016 471  ARG A CZ  
3377  N NH1 . ARG A 473  ? 0.3034 0.3078 0.3117 -0.0151 -0.0192 -0.0025 471  ARG A NH1 
3378  N NH2 . ARG A 473  ? 0.2970 0.2971 0.3143 -0.0184 -0.0204 -0.0021 471  ARG A NH2 
3379  N N   . ILE A 474  ? 0.3066 0.2986 0.3126 -0.0112 -0.0218 -0.0129 472  ILE A N   
3380  C CA  . ILE A 474  ? 0.3062 0.2983 0.3085 -0.0096 -0.0209 -0.0135 472  ILE A CA  
3381  C C   . ILE A 474  ? 0.3003 0.2937 0.2976 -0.0095 -0.0180 -0.0090 472  ILE A C   
3382  O O   . ILE A 474  ? 0.3197 0.3179 0.3147 -0.0092 -0.0174 -0.0080 472  ILE A O   
3383  C CB  . ILE A 474  ? 0.2995 0.2970 0.3006 -0.0076 -0.0226 -0.0186 472  ILE A CB  
3384  C CG1 . ILE A 474  ? 0.3796 0.3749 0.3859 -0.0073 -0.0257 -0.0236 472  ILE A CG1 
3385  C CG2 . ILE A 474  ? 0.3201 0.3191 0.3168 -0.0060 -0.0211 -0.0185 472  ILE A CG2 
3386  C CD1 . ILE A 474  ? 0.3956 0.3973 0.4014 -0.0053 -0.0277 -0.0294 472  ILE A CD1 
3387  N N   . TYR A 475  ? 0.2640 0.2532 0.2599 -0.0096 -0.0164 -0.0064 473  TYR A N   
3388  C CA  . TYR A 475  ? 0.3169 0.3070 0.3084 -0.0094 -0.0138 -0.0026 473  TYR A CA  
3389  C C   . TYR A 475  ? 0.3640 0.3585 0.3518 -0.0077 -0.0136 -0.0045 473  TYR A C   
3390  O O   . TYR A 475  ? 0.3185 0.3118 0.3062 -0.0067 -0.0141 -0.0067 473  TYR A O   
3391  C CB  . TYR A 475  ? 0.3349 0.3190 0.3265 -0.0101 -0.0124 0.0005  473  TYR A CB  
3392  C CG  . TYR A 475  ? 0.4262 0.4102 0.4141 -0.0102 -0.0099 0.0045  473  TYR A CG  
3393  C CD1 . TYR A 475  ? 0.3966 0.3801 0.3848 -0.0112 -0.0086 0.0078  473  TYR A CD1 
3394  C CD2 . TYR A 475  ? 0.4437 0.4282 0.4282 -0.0091 -0.0089 0.0047  473  TYR A CD2 
3395  C CE1 . TYR A 475  ? 0.4115 0.3947 0.3966 -0.0111 -0.0066 0.0111  473  TYR A CE1 
3396  C CE2 . TYR A 475  ? 0.4383 0.4225 0.4199 -0.0092 -0.0068 0.0082  473  TYR A CE2 
3397  C CZ  . TYR A 475  ? 0.4621 0.4454 0.4441 -0.0102 -0.0057 0.0112  473  TYR A CZ  
3398  O OH  . TYR A 475  ? 0.4998 0.4826 0.4792 -0.0101 -0.0039 0.0142  473  TYR A OH  
3399  N N   . ALA A 476  ? 0.3191 0.3190 0.3040 -0.0073 -0.0130 -0.0036 474  ALA A N   
3400  C CA  . ALA A 476  ? 0.3113 0.3170 0.2929 -0.0058 -0.0130 -0.0055 474  ALA A CA  
3401  C C   . ALA A 476  ? 0.3084 0.3151 0.2860 -0.0057 -0.0108 -0.0017 474  ALA A C   
3402  O O   . ALA A 476  ? 0.2999 0.3087 0.2759 -0.0062 -0.0099 0.0013  474  ALA A O   
3403  C CB  . ALA A 476  ? 0.3193 0.3313 0.3009 -0.0054 -0.0144 -0.0076 474  ALA A CB  
3404  N N   . PRO A 477  ? 0.3154 0.3206 0.2916 -0.0052 -0.0099 -0.0016 475  PRO A N   
3405  C CA  . PRO A 477  ? 0.2820 0.2885 0.2546 -0.0053 -0.0079 0.0018  475  PRO A CA  
3406  C C   . PRO A 477  ? 0.3155 0.3296 0.2853 -0.0046 -0.0079 0.0015  475  PRO A C   
3407  O O   . PRO A 477  ? 0.3550 0.3739 0.3248 -0.0036 -0.0092 -0.0023 475  PRO A O   
3408  C CB  . PRO A 477  ? 0.3684 0.3721 0.3408 -0.0048 -0.0074 0.0010  475  PRO A CB  
3409  C CG  . PRO A 477  ? 0.3328 0.3326 0.3087 -0.0046 -0.0090 -0.0022 475  PRO A CG  
3410  C CD  . PRO A 477  ? 0.3172 0.3197 0.2951 -0.0045 -0.0108 -0.0048 475  PRO A CD  
3411  N N   . VAL A 478  ? 0.3553 0.3708 0.3227 -0.0052 -0.0065 0.0055  476  VAL A N   
3412  C CA  . VAL A 478  ? 0.3817 0.4043 0.3463 -0.0048 -0.0064 0.0064  476  VAL A CA  
3413  C C   . VAL A 478  ? 0.4032 0.4260 0.3653 -0.0053 -0.0047 0.0101  476  VAL A C   
3414  O O   . VAL A 478  ? 0.3975 0.4157 0.3598 -0.0061 -0.0036 0.0135  476  VAL A O   
3415  C CB  . VAL A 478  ? 0.4216 0.4458 0.3865 -0.0052 -0.0071 0.0082  476  VAL A CB  
3416  C CG1 . VAL A 478  ? 0.4343 0.4661 0.3961 -0.0049 -0.0070 0.0096  476  VAL A CG1 
3417  C CG2 . VAL A 478  ? 0.2999 0.3238 0.2679 -0.0050 -0.0089 0.0046  476  VAL A CG2 
3418  N N   . GLY A 479  ? 0.4165 0.4449 0.3764 -0.0047 -0.0043 0.0092  477  GLY A N   
3419  C CA  . GLY A 479  ? 0.5226 0.5516 0.4806 -0.0054 -0.0027 0.0127  477  GLY A CA  
3420  C C   . GLY A 479  ? 0.5141 0.5489 0.4704 -0.0047 -0.0024 0.0107  477  GLY A C   
3421  O O   . GLY A 479  ? 0.4494 0.4870 0.4064 -0.0035 -0.0033 0.0062  477  GLY A O   
3422  N N   . THR A 480  ? 0.5489 0.5860 0.5034 -0.0055 -0.0010 0.0142  478  THR A N   
3423  C CA  . THR A 480  ? 0.6321 0.6759 0.5849 -0.0051 -0.0004 0.0132  478  THR A CA  
3424  C C   . THR A 480  ? 0.7093 0.7497 0.6632 -0.0047 0.0001  0.0111  478  THR A C   
3425  O O   . THR A 480  ? 0.7102 0.7431 0.6661 -0.0047 -0.0001 0.0105  478  THR A O   
3426  C CB  . THR A 480  ? 0.5751 0.6229 0.5258 -0.0064 0.0008  0.0182  478  THR A CB  
3427  O OG1 . THR A 480  ? 0.6156 0.6568 0.5673 -0.0076 0.0018  0.0217  478  THR A OG1 
3428  C CG2 . THR A 480  ? 0.5880 0.6388 0.5376 -0.0067 0.0001  0.0207  478  THR A CG2 
3429  N N   . HIS A 481  ? 0.8040 0.8505 0.7567 -0.0043 0.0008  0.0101  479  HIS A N   
3430  C CA  . HIS A 481  ? 0.7580 0.8025 0.7119 -0.0037 0.0012  0.0078  479  HIS A CA  
3431  C C   . HIS A 481  ? 0.7817 0.8195 0.7363 -0.0050 0.0022  0.0114  479  HIS A C   
3432  O O   . HIS A 481  ? 0.8379 0.8706 0.7941 -0.0046 0.0021  0.0097  479  HIS A O   
3433  C CB  . HIS A 481  ? 0.7679 0.8215 0.7204 -0.0031 0.0018  0.0063  479  HIS A CB  
3434  C CG  . HIS A 481  ? 0.7948 0.8562 0.7464 -0.0016 0.0008  0.0022  479  HIS A CG  
3435  N ND1 . HIS A 481  ? 0.7638 0.8349 0.7139 -0.0008 0.0013  0.0004  479  HIS A ND1 
3436  C CD2 . HIS A 481  ? 0.7662 0.8275 0.7183 -0.0006 -0.0008 -0.0005 479  HIS A CD2 
3437  C CE1 . HIS A 481  ? 0.8208 0.8976 0.7705 0.0007  0.0001  -0.0034 479  HIS A CE1 
3438  N NE2 . HIS A 481  ? 0.8588 0.9296 0.8097 0.0008  -0.0013 -0.0041 479  HIS A NE2 
3439  N N   . GLU A 482  ? 0.7562 0.7939 0.7098 -0.0066 0.0031  0.0163  480  GLU A N   
3440  C CA  . GLU A 482  ? 0.7532 0.7843 0.7076 -0.0078 0.0039  0.0194  480  GLU A CA  
3441  C C   . GLU A 482  ? 0.7483 0.7711 0.7044 -0.0075 0.0033  0.0187  480  GLU A C   
3442  O O   . GLU A 482  ? 0.7949 0.8126 0.7522 -0.0073 0.0034  0.0178  480  GLU A O   
3443  C CB  . GLU A 482  ? 0.7367 0.7691 0.6902 -0.0095 0.0046  0.0245  480  GLU A CB  
3444  N N   . THR A 483  ? 0.7258 0.7476 0.6820 -0.0075 0.0025  0.0191  481  THR A N   
3445  C CA  . THR A 483  ? 0.7510 0.7656 0.7089 -0.0075 0.0021  0.0191  481  THR A CA  
3446  C C   . THR A 483  ? 0.7711 0.7830 0.7306 -0.0064 0.0012  0.0150  481  THR A C   
3447  O O   . THR A 483  ? 0.7657 0.7714 0.7264 -0.0064 0.0013  0.0151  481  THR A O   
3448  C CB  . THR A 483  ? 0.6853 0.7004 0.6432 -0.0077 0.0014  0.0204  481  THR A CB  
3449  N N   . LEU A 484  ? 0.7805 0.7970 0.7400 -0.0053 0.0003  0.0114  482  LEU A N   
3450  C CA  . LEU A 484  ? 0.7509 0.7646 0.7123 -0.0042 -0.0009 0.0074  482  LEU A CA  
3451  C C   . LEU A 484  ? 0.7889 0.7991 0.7509 -0.0039 -0.0004 0.0068  482  LEU A C   
3452  O O   . LEU A 484  ? 0.7621 0.7662 0.7259 -0.0038 -0.0008 0.0065  482  LEU A O   
3453  C CB  . LEU A 484  ? 0.6772 0.6972 0.6387 -0.0029 -0.0020 0.0032  482  LEU A CB  
3454  N N   . LEU A 485  ? 0.7796 0.7942 0.7404 -0.0037 0.0004  0.0068  483  LEU A N   
3455  C CA  . LEU A 485  ? 0.8118 0.8241 0.7733 -0.0032 0.0006  0.0059  483  LEU A CA  
3456  C C   . LEU A 485  ? 0.8618 0.8676 0.8236 -0.0042 0.0014  0.0091  483  LEU A C   
3457  O O   . LEU A 485  ? 0.7963 0.7987 0.7589 -0.0037 0.0013  0.0082  483  LEU A O   
3458  C CB  . LEU A 485  ? 0.7237 0.7429 0.6839 -0.0030 0.0015  0.0056  483  LEU A CB  
3459  N N   . ALA A 486  ? 0.9599 0.9639 0.9210 -0.0055 0.0021  0.0126  484  ALA A N   
3460  C CA  . ALA A 486  ? 0.8736 0.8719 0.8349 -0.0063 0.0028  0.0153  484  ALA A CA  
3461  C C   . ALA A 486  ? 0.8886 0.8809 0.8513 -0.0058 0.0021  0.0141  484  ALA A C   
3462  O O   . ALA A 486  ? 0.9314 0.9214 0.8944 -0.0054 0.0022  0.0135  484  ALA A O   
3463  C CB  . ALA A 486  ? 0.7756 0.7732 0.7363 -0.0074 0.0032  0.0186  484  ALA A CB  
3464  N N   . TYR A 487  ? 0.7987 0.7888 0.7623 -0.0059 0.0015  0.0139  485  TYR A N   
3465  C CA  . TYR A 487  ? 0.7507 0.7353 0.7159 -0.0057 0.0009  0.0134  485  TYR A CA  
3466  C C   . TYR A 487  ? 0.7831 0.7679 0.7502 -0.0047 -0.0006 0.0100  485  TYR A C   
3467  O O   . TYR A 487  ? 0.7733 0.7542 0.7420 -0.0049 -0.0014 0.0098  485  TYR A O   
3468  C CB  . TYR A 487  ? 0.7903 0.7720 0.7559 -0.0066 0.0013  0.0158  485  TYR A CB  
3469  N N   . LEU A 488  ? 0.7722 0.7614 0.7390 -0.0037 -0.0012 0.0072  486  LEU A N   
3470  C CA  . LEU A 488  ? 0.7610 0.7503 0.7300 -0.0026 -0.0030 0.0034  486  LEU A CA  
3471  C C   . LEU A 488  ? 0.7444 0.7286 0.7150 -0.0020 -0.0037 0.0025  486  LEU A C   
3472  O O   . LEU A 488  ? 0.6759 0.6575 0.6490 -0.0014 -0.0053 0.0004  486  LEU A O   
3473  C CB  . LEU A 488  ? 0.7429 0.7390 0.7113 -0.0015 -0.0034 0.0003  486  LEU A CB  
3474  C CG  . LEU A 488  ? 0.6946 0.6913 0.6653 0.0001  -0.0054 -0.0044 486  LEU A CG  
3475  C CD1 . LEU A 488  ? 0.6767 0.6707 0.6495 -0.0004 -0.0067 -0.0051 486  LEU A CD1 
3476  C CD2 . LEU A 488  ? 0.6044 0.6090 0.5741 0.0013  -0.0055 -0.0075 486  LEU A CD2 
3477  N N   . VAL A 489  ? 0.7407 0.7235 0.7102 -0.0020 -0.0028 0.0041  487  VAL A N   
3478  C CA  . VAL A 489  ? 0.7200 0.6983 0.6908 -0.0013 -0.0035 0.0037  487  VAL A CA  
3479  C C   . VAL A 489  ? 0.7539 0.7265 0.7263 -0.0021 -0.0041 0.0052  487  VAL A C   
3480  O O   . VAL A 489  ? 0.7765 0.7463 0.7514 -0.0015 -0.0058 0.0035  487  VAL A O   
3481  C CB  . VAL A 489  ? 0.6727 0.6505 0.6418 -0.0015 -0.0023 0.0056  487  VAL A CB  
3482  N N   . ARG A 490  ? 0.7515 0.7228 0.7228 -0.0034 -0.0028 0.0084  488  ARG A N   
3483  C CA  . ARG A 490  ? 0.7524 0.7195 0.7252 -0.0044 -0.0031 0.0102  488  ARG A CA  
3484  C C   . ARG A 490  ? 0.7564 0.7235 0.7318 -0.0044 -0.0047 0.0080  488  ARG A C   
3485  O O   . ARG A 490  ? 0.7273 0.6904 0.7051 -0.0047 -0.0057 0.0083  488  ARG A O   
3486  C CB  . ARG A 490  ? 0.7303 0.6975 0.7015 -0.0056 -0.0014 0.0133  488  ARG A CB  
3487  C CG  . ARG A 490  ? 0.7173 0.6807 0.6896 -0.0066 -0.0013 0.0156  488  ARG A CG  
3488  C CD  . ARG A 490  ? 0.6529 0.6172 0.6238 -0.0074 0.0003  0.0182  488  ARG A CD  
3489  N NE  . ARG A 490  ? 0.6670 0.6343 0.6383 -0.0078 0.0002  0.0177  488  ARG A NE  
3490  C CZ  . ARG A 490  ? 0.6318 0.6011 0.6018 -0.0081 0.0012  0.0192  488  ARG A CZ  
3491  N NH1 . ARG A 490  ? 0.5022 0.4708 0.4705 -0.0081 0.0024  0.0210  488  ARG A NH1 
3492  N NH2 . ARG A 490  ? 0.5787 0.5508 0.5492 -0.0083 0.0009  0.0188  488  ARG A NH2 
3493  N N   . ARG A 491  ? 0.7320 0.7036 0.7071 -0.0040 -0.0050 0.0059  489  ARG A N   
3494  C CA  . ARG A 491  ? 0.7549 0.7272 0.7326 -0.0040 -0.0066 0.0035  489  ARG A CA  
3495  C C   . ARG A 491  ? 0.7102 0.6805 0.6907 -0.0028 -0.0087 0.0002  489  ARG A C   
3496  O O   . ARG A 491  ? 0.7626 0.7319 0.7460 -0.0028 -0.0104 -0.0019 489  ARG A O   
3497  C CB  . ARG A 491  ? 0.6880 0.6666 0.6643 -0.0037 -0.0065 0.0018  489  ARG A CB  
3498  N N   . GLY A 496  ? 0.8502 0.8004 0.8435 0.0005  -0.0169 -0.0042 494  GLY A N   
3499  C CA  . GLY A 496  ? 0.8413 0.7918 0.8356 0.0028  -0.0184 -0.0076 494  GLY A CA  
3500  C C   . GLY A 496  ? 0.9334 0.8796 0.9277 0.0033  -0.0187 -0.0052 494  GLY A C   
3501  O O   . GLY A 496  ? 0.9487 0.8961 0.9429 0.0053  -0.0193 -0.0075 494  GLY A O   
3502  N N   . ALA A 497  ? 0.8182 0.7600 0.8127 0.0015  -0.0182 -0.0007 495  ALA A N   
3503  C CA  . ALA A 497  ? 0.7312 0.6688 0.7256 0.0019  -0.0186 0.0019  495  ALA A CA  
3504  C C   . ALA A 497  ? 0.6891 0.6210 0.6885 0.0022  -0.0217 0.0015  495  ALA A C   
3505  O O   . ALA A 497  ? 0.6951 0.6256 0.6980 0.0015  -0.0232 0.0000  495  ALA A O   
3506  C CB  . ALA A 497  ? 0.7182 0.6548 0.7096 0.0000  -0.0163 0.0072  495  ALA A CB  
3507  N N   . ASN A 498  ? 0.6803 0.6088 0.6802 0.0032  -0.0227 0.0029  496  ASN A N   
3508  C CA  . ASN A 498  ? 0.7082 0.6310 0.7130 0.0038  -0.0260 0.0025  496  ASN A CA  
3509  C C   . ASN A 498  ? 0.6445 0.5631 0.6523 0.0012  -0.0266 0.0058  496  ASN A C   
3510  O O   . ASN A 498  ? 0.6242 0.5387 0.6372 0.0013  -0.0295 0.0044  496  ASN A O   
3511  C CB  . ASN A 498  ? 0.6873 0.6073 0.6917 0.0051  -0.0268 0.0044  496  ASN A CB  
3512  N N   . SER A 499  ? 0.6246 0.5443 0.6294 -0.0010 -0.0241 0.0101  497  SER A N   
3513  C CA  . SER A 499  ? 0.6039 0.5205 0.6113 -0.0037 -0.0243 0.0136  497  SER A CA  
3514  C C   . SER A 499  ? 0.6093 0.5282 0.6184 -0.0048 -0.0242 0.0111  497  SER A C   
3515  O O   . SER A 499  ? 0.5782 0.4946 0.5905 -0.0069 -0.0249 0.0132  497  SER A O   
3516  C CB  . SER A 499  ? 0.5538 0.4710 0.5573 -0.0054 -0.0216 0.0192  497  SER A CB  
3517  O OG  . SER A 499  ? 0.5599 0.4825 0.5585 -0.0052 -0.0187 0.0186  497  SER A OG  
3518  N N   . SER A 500  ? 0.6122 0.5361 0.6194 -0.0035 -0.0235 0.0069  498  SER A N   
3519  C CA  . SER A 500  ? 0.5713 0.4981 0.5796 -0.0044 -0.0234 0.0047  498  SER A CA  
3520  C C   . SER A 500  ? 0.5925 0.5164 0.6067 -0.0040 -0.0268 0.0010  498  SER A C   
3521  O O   . SER A 500  ? 0.6090 0.5311 0.6256 -0.0020 -0.0292 -0.0022 498  SER A O   
3522  C CB  . SER A 500  ? 0.6042 0.5374 0.6086 -0.0030 -0.0217 0.0014  498  SER A CB  
3523  O OG  . SER A 500  ? 0.7069 0.6426 0.7063 -0.0036 -0.0187 0.0048  498  SER A OG  
3524  N N   . PHE A 501  ? 0.5223 0.4459 0.5391 -0.0060 -0.0272 0.0014  499  PHE A N   
3525  C CA  . PHE A 501  ? 0.5540 0.4755 0.5767 -0.0059 -0.0305 -0.0025 499  PHE A CA  
3526  C C   . PHE A 501  ? 0.6064 0.5321 0.6288 -0.0031 -0.0316 -0.0091 499  PHE A C   
3527  O O   . PHE A 501  ? 0.6201 0.5434 0.6467 -0.0015 -0.0347 -0.0132 499  PHE A O   
3528  C CB  . PHE A 501  ? 0.4951 0.4172 0.5202 -0.0085 -0.0303 -0.0013 499  PHE A CB  
3529  C CG  . PHE A 501  ? 0.5368 0.4564 0.5684 -0.0086 -0.0339 -0.0053 499  PHE A CG  
3530  C CD1 . PHE A 501  ? 0.5240 0.4370 0.5614 -0.0101 -0.0364 -0.0031 499  PHE A CD1 
3531  C CD2 . PHE A 501  ? 0.5462 0.4702 0.5784 -0.0073 -0.0349 -0.0111 499  PHE A CD2 
3532  C CE1 . PHE A 501  ? 0.5072 0.4175 0.5511 -0.0103 -0.0399 -0.0070 499  PHE A CE1 
3533  C CE2 . PHE A 501  ? 0.5235 0.4452 0.5618 -0.0072 -0.0384 -0.0152 499  PHE A CE2 
3534  C CZ  . PHE A 501  ? 0.5443 0.4589 0.5887 -0.0088 -0.0410 -0.0132 499  PHE A CZ  
3535  N N   . VAL A 502  ? 0.5839 0.5161 0.6014 -0.0025 -0.0291 -0.0103 500  VAL A N   
3536  C CA  . VAL A 502  ? 0.6219 0.5594 0.6389 -0.0002 -0.0299 -0.0163 500  VAL A CA  
3537  C C   . VAL A 502  ? 0.6471 0.5841 0.6639 0.0026  -0.0309 -0.0188 500  VAL A C   
3538  O O   . VAL A 502  ? 0.7422 0.6810 0.7611 0.0048  -0.0331 -0.0245 500  VAL A O   
3539  C CB  . VAL A 502  ? 0.6738 0.6184 0.6854 -0.0004 -0.0270 -0.0160 500  VAL A CB  
3540  N N   . HIS A 503  ? 0.6364 0.5712 0.6506 0.0025  -0.0295 -0.0149 501  HIS A N   
3541  C CA  . HIS A 503  ? 0.6643 0.5982 0.6789 0.0051  -0.0307 -0.0169 501  HIS A CA  
3542  C C   . HIS A 503  ? 0.7017 0.6287 0.7224 0.0056  -0.0344 -0.0180 501  HIS A C   
3543  O O   . HIS A 503  ? 0.7089 0.6359 0.7323 0.0083  -0.0368 -0.0229 501  HIS A O   
3544  C CB  . HIS A 503  ? 0.6929 0.6268 0.7030 0.0048  -0.0282 -0.0124 501  HIS A CB  
3545  C CG  . HIS A 503  ? 0.7741 0.7063 0.7850 0.0071  -0.0295 -0.0137 501  HIS A CG  
3546  N ND1 . HIS A 503  ? 0.7866 0.7120 0.8010 0.0073  -0.0318 -0.0118 501  HIS A ND1 
3547  C CD2 . HIS A 503  ? 0.7790 0.7157 0.7877 0.0094  -0.0289 -0.0165 501  HIS A CD2 
3548  C CE1 . HIS A 503  ? 0.8009 0.7265 0.8151 0.0097  -0.0326 -0.0136 501  HIS A CE1 
3549  N NE2 . HIS A 503  ? 0.8393 0.7718 0.8502 0.0110  -0.0309 -0.0166 501  HIS A NE2 
3550  N N   . ARG A 504  ? 0.6525 0.5737 0.6757 0.0032  -0.0350 -0.0136 502  ARG A N   
3551  C CA  . ARG A 504  ? 0.6403 0.5543 0.6695 0.0034  -0.0385 -0.0136 502  ARG A CA  
3552  C C   . ARG A 504  ? 0.6932 0.6064 0.7283 0.0042  -0.0419 -0.0192 502  ARG A C   
3553  O O   . ARG A 504  ? 0.6804 0.5893 0.7203 0.0059  -0.0453 -0.0221 502  ARG A O   
3554  C CB  . ARG A 504  ? 0.6427 0.5515 0.6729 0.0003  -0.0380 -0.0067 502  ARG A CB  
3555  C CG  . ARG A 504  ? 0.6249 0.5332 0.6506 0.0001  -0.0357 -0.0015 502  ARG A CG  
3556  C CD  . ARG A 504  ? 0.6392 0.5451 0.6644 -0.0032 -0.0341 0.0053  502  ARG A CD  
3557  N NE  . ARG A 504  ? 0.6693 0.5691 0.7007 -0.0049 -0.0369 0.0070  502  ARG A NE  
3558  C CZ  . ARG A 504  ? 0.7138 0.6076 0.7488 -0.0045 -0.0395 0.0089  502  ARG A CZ  
3559  N NH1 . ARG A 504  ? 0.6747 0.5678 0.7078 -0.0022 -0.0398 0.0088  502  ARG A NH1 
3560  N NH2 . ARG A 504  ? 0.7221 0.6106 0.7630 -0.0066 -0.0419 0.0111  502  ARG A NH2 
3561  N N   . ILE A 505  ? 0.6650 0.5820 0.6997 0.0030  -0.0412 -0.0211 503  ILE A N   
3562  C CA  . ILE A 505  ? 0.6875 0.6043 0.7277 0.0039  -0.0445 -0.0270 503  ILE A CA  
3563  C C   . ILE A 505  ? 0.7193 0.6397 0.7597 0.0078  -0.0460 -0.0339 503  ILE A C   
3564  O O   . ILE A 505  ? 0.6936 0.6114 0.7396 0.0094  -0.0497 -0.0389 503  ILE A O   
3565  C CB  . ILE A 505  ? 0.6541 0.5753 0.6934 0.0020  -0.0433 -0.0277 503  ILE A CB  
3566  C CG1 . ILE A 505  ? 0.6223 0.5431 0.6677 0.0028  -0.0470 -0.0339 503  ILE A CG1 
3567  C CG2 . ILE A 505  ? 0.6605 0.5903 0.6931 0.0030  -0.0400 -0.0288 503  ILE A CG2 
3568  C CD1 . ILE A 505  ? 0.6072 0.5235 0.6576 -0.0004 -0.0485 -0.0315 503  ILE A CD1 
3569  N N   . ASN A 506  ? 0.6982 0.6247 0.7327 0.0093  -0.0433 -0.0342 504  ASN A N   
3570  C CA  . ASN A 506  ? 0.7412 0.6722 0.7753 0.0129  -0.0442 -0.0402 504  ASN A CA  
3571  C C   . ASN A 506  ? 0.7595 0.6858 0.7958 0.0149  -0.0460 -0.0402 504  ASN A C   
3572  O O   . ASN A 506  ? 0.7370 0.6667 0.7739 0.0182  -0.0472 -0.0456 504  ASN A O   
3573  C CB  . ASN A 506  ? 0.7525 0.6922 0.7796 0.0134  -0.0404 -0.0401 504  ASN A CB  
3574  C CG  . ASN A 506  ? 0.8095 0.7559 0.8350 0.0129  -0.0396 -0.0430 504  ASN A CG  
3575  O OD1 . ASN A 506  ? 0.8136 0.7580 0.8427 0.0118  -0.0414 -0.0444 504  ASN A OD1 
3576  N ND2 . ASN A 506  ? 0.8430 0.7975 0.8633 0.0138  -0.0370 -0.0439 504  ASN A ND2 
3577  N N   . ASP A 507  ? 0.7372 0.6565 0.7746 0.0132  -0.0462 -0.0344 505  ASP A N   
3578  C CA  . ASP A 507  ? 0.7788 0.6936 0.8179 0.0151  -0.0478 -0.0336 505  ASP A CA  
3579  C C   . ASP A 507  ? 0.7997 0.7079 0.8467 0.0164  -0.0527 -0.0370 505  ASP A C   
3580  O O   . ASP A 507  ? 0.7429 0.6451 0.7939 0.0139  -0.0542 -0.0343 505  ASP A O   
3581  C CB  . ASP A 507  ? 0.7729 0.6835 0.8094 0.0128  -0.0459 -0.0257 505  ASP A CB  
3582  C CG  . ASP A 507  ? 0.8001 0.7080 0.8367 0.0149  -0.0469 -0.0246 505  ASP A CG  
3583  O OD1 . ASP A 507  ? 0.8018 0.7070 0.8433 0.0176  -0.0504 -0.0289 505  ASP A OD1 
3584  O OD2 . ASP A 507  ? 0.8046 0.7131 0.8365 0.0140  -0.0443 -0.0197 505  ASP A OD2 
3585  N N   . PRO A 508  ? 0.8800 0.7890 0.9298 0.0201  -0.0552 -0.0429 506  PRO A N   
3586  C CA  . PRO A 508  ? 0.8504 0.7527 0.9083 0.0215  -0.0602 -0.0465 506  PRO A CA  
3587  C C   . PRO A 508  ? 0.8222 0.7151 0.8837 0.0204  -0.0622 -0.0409 506  PRO A C   
3588  O O   . PRO A 508  ? 0.8269 0.7127 0.8954 0.0203  -0.0662 -0.0419 506  PRO A O   
3589  C CB  . PRO A 508  ? 0.8501 0.7571 0.9091 0.0261  -0.0618 -0.0543 506  PRO A CB  
3590  C CG  . PRO A 508  ? 0.8741 0.7914 0.9256 0.0265  -0.0575 -0.0551 506  PRO A CG  
3591  C CD  . PRO A 508  ? 0.8583 0.7748 0.9043 0.0232  -0.0537 -0.0469 506  PRO A CD  
3592  N N   . LYS A 509  ? 0.7672 0.6597 0.8240 0.0197  -0.0597 -0.0349 507  LYS A N   
3593  C CA  . LYS A 509  ? 0.8101 0.6944 0.8693 0.0185  -0.0612 -0.0288 507  LYS A CA  
3594  C C   . LYS A 509  ? 0.7807 0.6612 0.8400 0.0140  -0.0600 -0.0218 507  LYS A C   
3595  O O   . LYS A 509  ? 0.7893 0.6638 0.8496 0.0125  -0.0606 -0.0156 507  LYS A O   
3596  C CB  . LYS A 509  ? 0.8007 0.6869 0.8550 0.0198  -0.0592 -0.0257 507  LYS A CB  
3597  N N   . VAL A 510  ? 0.7677 0.6518 0.8256 0.0119  -0.0582 -0.0226 508  VAL A N   
3598  C CA  . VAL A 510  ? 0.7275 0.6088 0.7858 0.0077  -0.0570 -0.0166 508  VAL A CA  
3599  C C   . VAL A 510  ? 0.7228 0.6006 0.7884 0.0067  -0.0604 -0.0200 508  VAL A C   
3600  O O   . VAL A 510  ? 0.7527 0.6351 0.8187 0.0078  -0.0608 -0.0262 508  VAL A O   
3601  C CB  . VAL A 510  ? 0.7335 0.6219 0.7847 0.0058  -0.0522 -0.0143 508  VAL A CB  
3602  C CG1 . VAL A 510  ? 0.6920 0.5781 0.7442 0.0016  -0.0512 -0.0090 508  VAL A CG1 
3603  C CG2 . VAL A 510  ? 0.6674 0.5587 0.7119 0.0065  -0.0491 -0.0108 508  VAL A CG2 
3604  N N   . SER A 511  ? 0.6817 0.5515 0.7531 0.0047  -0.0631 -0.0159 509  SER A N   
3605  C CA  . SER A 511  ? 0.6694 0.5350 0.7483 0.0034  -0.0666 -0.0185 509  SER A CA  
3606  C C   . SER A 511  ? 0.6623 0.5311 0.7396 -0.0004 -0.0640 -0.0159 509  SER A C   
3607  O O   . SER A 511  ? 0.6902 0.5630 0.7613 -0.0022 -0.0598 -0.0109 509  SER A O   
3608  C CB  . SER A 511  ? 0.7264 0.5822 0.8125 0.0022  -0.0704 -0.0145 509  SER A CB  
3609  O OG  . SER A 511  ? 0.6919 0.5457 0.7760 -0.0016 -0.0681 -0.0054 509  SER A OG  
3610  N N   . ILE A 512  ? 0.6183 0.4855 0.7018 -0.0014 -0.0667 -0.0196 510  ILE A N   
3611  C CA  . ILE A 512  ? 0.6575 0.5271 0.7408 -0.0051 -0.0649 -0.0171 510  ILE A CA  
3612  C C   . ILE A 512  ? 0.6679 0.5327 0.7523 -0.0090 -0.0639 -0.0079 510  ILE A C   
3613  O O   . ILE A 512  ? 0.6391 0.5077 0.7193 -0.0117 -0.0603 -0.0033 510  ILE A O   
3614  C CB  . ILE A 512  ? 0.6510 0.5197 0.7413 -0.0052 -0.0685 -0.0233 510  ILE A CB  
3615  C CG1 . ILE A 512  ? 0.6369 0.5117 0.7253 -0.0011 -0.0690 -0.0324 510  ILE A CG1 
3616  C CG2 . ILE A 512  ? 0.6321 0.5032 0.7226 -0.0091 -0.0667 -0.0205 510  ILE A CG2 
3617  C CD1 . ILE A 512  ? 0.6914 0.5657 0.7864 -0.0007 -0.0729 -0.0394 510  ILE A CD1 
3618  N N   . ASP A 513  ? 0.6487 0.5054 0.7387 -0.0093 -0.0672 -0.0051 511  ASP A N   
3619  C CA  . ASP A 513  ? 0.6246 0.4770 0.7159 -0.0131 -0.0665 0.0039  511  ASP A CA  
3620  C C   . ASP A 513  ? 0.6163 0.4732 0.6988 -0.0136 -0.0616 0.0097  511  ASP A C   
3621  O O   . ASP A 513  ? 0.6412 0.4989 0.7222 -0.0171 -0.0592 0.0163  511  ASP A O   
3622  C CB  . ASP A 513  ? 0.6605 0.5037 0.7585 -0.0126 -0.0709 0.0060  511  ASP A CB  
3623  C CG  . ASP A 513  ? 0.7337 0.5711 0.8418 -0.0131 -0.0760 0.0017  511  ASP A CG  
3624  O OD1 . ASP A 513  ? 0.7092 0.5480 0.8201 -0.0159 -0.0759 0.0010  511  ASP A OD1 
3625  O OD2 . ASP A 513  ? 0.8116 0.6427 0.9250 -0.0107 -0.0803 -0.0010 511  ASP A OD2 
3626  N N   . GLU A 514  ? 0.6297 0.4900 0.7064 -0.0102 -0.0602 0.0072  512  GLU A N   
3627  C CA  . GLU A 514  ? 0.6165 0.4818 0.6847 -0.0104 -0.0555 0.0116  512  GLU A CA  
3628  C C   . GLU A 514  ? 0.6148 0.4875 0.6783 -0.0118 -0.0517 0.0109  512  GLU A C   
3629  O O   . GLU A 514  ? 0.6261 0.5021 0.6843 -0.0135 -0.0480 0.0160  512  GLU A O   
3630  C CB  . GLU A 514  ? 0.6359 0.5031 0.6998 -0.0064 -0.0552 0.0086  512  GLU A CB  
3631  C CG  . GLU A 514  ? 0.7084 0.5686 0.7764 -0.0047 -0.0588 0.0098  512  GLU A CG  
3632  C CD  . GLU A 514  ? 0.7544 0.6172 0.8185 -0.0007 -0.0585 0.0063  512  GLU A CD  
3633  O OE1 . GLU A 514  ? 0.8139 0.6835 0.8731 0.0010  -0.0561 0.0018  512  GLU A OE1 
3634  O OE2 . GLU A 514  ? 0.8114 0.6695 0.8773 0.0009  -0.0607 0.0081  512  GLU A OE2 
3635  N N   . LEU A 515  ? 0.6262 0.5017 0.6915 -0.0109 -0.0527 0.0044  513  LEU A N   
3636  C CA  . LEU A 515  ? 0.6480 0.5308 0.7088 -0.0118 -0.0494 0.0032  513  LEU A CA  
3637  C C   . LEU A 515  ? 0.5814 0.4638 0.6454 -0.0158 -0.0490 0.0068  513  LEU A C   
3638  O O   . LEU A 515  ? 0.5490 0.4367 0.6086 -0.0173 -0.0455 0.0089  513  LEU A O   
3639  C CB  . LEU A 515  ? 0.6373 0.5243 0.6983 -0.0090 -0.0506 -0.0052 513  LEU A CB  
3640  C CG  . LEU A 515  ? 0.5965 0.4871 0.6528 -0.0051 -0.0498 -0.0093 513  LEU A CG  
3641  C CD1 . LEU A 515  ? 0.5917 0.4858 0.6499 -0.0026 -0.0518 -0.0177 513  LEU A CD1 
3642  C CD2 . LEU A 515  ? 0.5812 0.4779 0.6291 -0.0053 -0.0451 -0.0063 513  LEU A CD2 
3643  N N   . ILE A 516  ? 0.5502 0.4264 0.6221 -0.0176 -0.0525 0.0075  514  ILE A N   
3644  C CA  . ILE A 516  ? 0.5957 0.4714 0.6715 -0.0216 -0.0524 0.0111  514  ILE A CA  
3645  C C   . ILE A 516  ? 0.5183 0.3909 0.5942 -0.0246 -0.0511 0.0199  514  ILE A C   
3646  O O   . ILE A 516  ? 0.5495 0.4210 0.6294 -0.0282 -0.0512 0.0238  514  ILE A O   
3647  C CB  . ILE A 516  ? 0.5675 0.4389 0.6524 -0.0223 -0.0570 0.0068  514  ILE A CB  
3648  C CG1 . ILE A 516  ? 0.5372 0.3998 0.6282 -0.0219 -0.0610 0.0080  514  ILE A CG1 
3649  C CG2 . ILE A 516  ? 0.6110 0.4865 0.6954 -0.0192 -0.0581 -0.0022 514  ILE A CG2 
3650  C CD1 . ILE A 516  ? 0.5753 0.4325 0.6764 -0.0235 -0.0657 0.0054  514  ILE A CD1 
3651  N N   . ALA A 517  ? 0.5154 0.3868 0.5870 -0.0232 -0.0500 0.0232  515  ALA A N   
3652  C CA  . ALA A 517  ? 0.5342 0.4036 0.6050 -0.0258 -0.0485 0.0317  515  ALA A CA  
3653  C C   . ALA A 517  ? 0.5414 0.4171 0.6079 -0.0283 -0.0442 0.0356  515  ALA A C   
3654  O O   . ALA A 517  ? 0.4817 0.3635 0.5420 -0.0269 -0.0412 0.0332  515  ALA A O   
3655  C CB  . ALA A 517  ? 0.5393 0.4077 0.6053 -0.0233 -0.0478 0.0337  515  ALA A CB  
3656  N N   . ASP A 518  ? 0.5286 0.4028 0.5986 -0.0321 -0.0440 0.0417  516  ASP A N   
3657  C CA  . ASP A 518  ? 0.4898 0.3699 0.5567 -0.0348 -0.0402 0.0458  516  ASP A CA  
3658  C C   . ASP A 518  ? 0.4851 0.3688 0.5442 -0.0340 -0.0365 0.0501  516  ASP A C   
3659  O O   . ASP A 518  ? 0.4612 0.3422 0.5205 -0.0351 -0.0366 0.0560  516  ASP A O   
3660  C CB  . ASP A 518  ? 0.4851 0.3626 0.5589 -0.0391 -0.0414 0.0511  516  ASP A CB  
3661  C CG  . ASP A 518  ? 0.5059 0.3900 0.5780 -0.0419 -0.0378 0.0540  516  ASP A CG  
3662  O OD1 . ASP A 518  ? 0.4755 0.3658 0.5405 -0.0405 -0.0342 0.0533  516  ASP A OD1 
3663  O OD2 . ASP A 518  ? 0.4944 0.3774 0.5726 -0.0455 -0.0388 0.0571  516  ASP A OD2 
3664  N N   . PRO A 519  ? 0.4368 0.3268 0.4891 -0.0323 -0.0332 0.0478  517  PRO A N   
3665  C CA  . PRO A 519  ? 0.4568 0.3502 0.5020 -0.0317 -0.0297 0.0518  517  PRO A CA  
3666  C C   . PRO A 519  ? 0.4356 0.3308 0.4810 -0.0351 -0.0277 0.0591  517  PRO A C   
3667  O O   . PRO A 519  ? 0.4162 0.3119 0.4578 -0.0349 -0.0263 0.0637  517  PRO A O   
3668  C CB  . PRO A 519  ? 0.4195 0.3192 0.4590 -0.0298 -0.0269 0.0475  517  PRO A CB  
3669  C CG  . PRO A 519  ? 0.4451 0.3461 0.4888 -0.0310 -0.0278 0.0440  517  PRO A CG  
3670  C CD  . PRO A 519  ? 0.4893 0.3838 0.5404 -0.0314 -0.0323 0.0421  517  PRO A CD  
3671  N N   . VAL A 520  ? 0.4292 0.3259 0.4789 -0.0381 -0.0276 0.0603  518  VAL A N   
3672  C CA  . VAL A 520  ? 0.4515 0.3508 0.5020 -0.0415 -0.0256 0.0673  518  VAL A CA  
3673  C C   . VAL A 520  ? 0.4887 0.3825 0.5424 -0.0430 -0.0277 0.0731  518  VAL A C   
3674  O O   . VAL A 520  ? 0.4757 0.3717 0.5262 -0.0440 -0.0256 0.0790  518  VAL A O   
3675  C CB  . VAL A 520  ? 0.4392 0.3406 0.4950 -0.0445 -0.0257 0.0670  518  VAL A CB  
3676  C CG1 . VAL A 520  ? 0.4674 0.3720 0.5244 -0.0482 -0.0236 0.0744  518  VAL A CG1 
3677  C CG2 . VAL A 520  ? 0.4353 0.3423 0.4877 -0.0429 -0.0237 0.0616  518  VAL A CG2 
3678  N N   . GLU A 521  ? 0.5061 0.3929 0.5665 -0.0432 -0.0319 0.0714  519  GLU A N   
3679  C CA  . GLU A 521  ? 0.4815 0.3626 0.5460 -0.0448 -0.0343 0.0772  519  GLU A CA  
3680  C C   . GLU A 521  ? 0.4701 0.3486 0.5299 -0.0417 -0.0348 0.0778  519  GLU A C   
3681  O O   . GLU A 521  ? 0.5106 0.3869 0.5707 -0.0429 -0.0352 0.0841  519  GLU A O   
3682  C CB  . GLU A 521  ? 0.5128 0.3867 0.5867 -0.0461 -0.0390 0.0752  519  GLU A CB  
3683  C CG  . GLU A 521  ? 0.5146 0.3904 0.5942 -0.0496 -0.0390 0.0753  519  GLU A CG  
3684  C CD  . GLU A 521  ? 0.5943 0.4744 0.6738 -0.0536 -0.0362 0.0834  519  GLU A CD  
3685  O OE1 . GLU A 521  ? 0.5904 0.4694 0.6684 -0.0546 -0.0357 0.0900  519  GLU A OE1 
3686  O OE2 . GLU A 521  ? 0.6749 0.5600 0.7559 -0.0558 -0.0345 0.0831  519  GLU A OE2 
3687  N N   . VAL A 522  ? 0.4361 0.3153 0.4918 -0.0378 -0.0347 0.0714  520  VAL A N   
3688  C CA  . VAL A 522  ? 0.4501 0.3283 0.5008 -0.0348 -0.0346 0.0718  520  VAL A CA  
3689  C C   . VAL A 522  ? 0.5165 0.4006 0.5601 -0.0353 -0.0306 0.0768  520  VAL A C   
3690  O O   . VAL A 522  ? 0.5056 0.3883 0.5474 -0.0352 -0.0308 0.0818  520  VAL A O   
3691  C CB  . VAL A 522  ? 0.4734 0.3520 0.5212 -0.0308 -0.0351 0.0638  520  VAL A CB  
3692  C CG1 . VAL A 522  ? 0.4375 0.3156 0.4803 -0.0278 -0.0350 0.0642  520  VAL A CG1 
3693  C CG2 . VAL A 522  ? 0.4750 0.3483 0.5299 -0.0300 -0.0393 0.0584  520  VAL A CG2 
3694  N N   . VAL A 523  ? 0.4719 0.3627 0.5114 -0.0357 -0.0270 0.0756  521  VAL A N   
3695  C CA  . VAL A 523  ? 0.4576 0.3545 0.4906 -0.0359 -0.0232 0.0797  521  VAL A CA  
3696  C C   . VAL A 523  ? 0.5090 0.4063 0.5442 -0.0394 -0.0228 0.0878  521  VAL A C   
3697  O O   . VAL A 523  ? 0.5032 0.4025 0.5341 -0.0392 -0.0214 0.0924  521  VAL A O   
3698  C CB  . VAL A 523  ? 0.4654 0.3692 0.4948 -0.0358 -0.0198 0.0765  521  VAL A CB  
3699  C CG1 . VAL A 523  ? 0.4316 0.3418 0.4556 -0.0366 -0.0160 0.0812  521  VAL A CG1 
3700  C CG2 . VAL A 523  ? 0.4269 0.3313 0.4524 -0.0322 -0.0196 0.0698  521  VAL A CG2 
3701  N N   . ARG A 524  ? 0.4937 0.3892 0.5357 -0.0427 -0.0241 0.0897  522  ARG A N   
3702  C CA  . ARG A 524  ? 0.5536 0.4502 0.5979 -0.0464 -0.0235 0.0977  522  ARG A CA  
3703  C C   . ARG A 524  ? 0.5434 0.4348 0.5887 -0.0463 -0.0259 0.1028  522  ARG A C   
3704  O O   . ARG A 524  ? 0.5723 0.4664 0.6161 -0.0483 -0.0245 0.1099  522  ARG A O   
3705  C CB  . ARG A 524  ? 0.5156 0.4107 0.5679 -0.0500 -0.0249 0.0984  522  ARG A CB  
3706  C CG  . ARG A 524  ? 0.6022 0.5005 0.6568 -0.0542 -0.0235 0.1067  522  ARG A CG  
3707  C CD  . ARG A 524  ? 0.5857 0.4800 0.6498 -0.0579 -0.0262 0.1081  522  ARG A CD  
3708  N NE  . ARG A 524  ? 0.6342 0.5299 0.7009 -0.0577 -0.0262 0.1015  522  ARG A NE  
3709  C CZ  . ARG A 524  ? 0.5502 0.4527 0.6167 -0.0596 -0.0234 0.1017  522  ARG A CZ  
3710  N NH1 . ARG A 524  ? 0.5679 0.4770 0.6319 -0.0618 -0.0201 0.1077  522  ARG A NH1 
3711  N NH2 . ARG A 524  ? 0.5834 0.4866 0.6525 -0.0593 -0.0240 0.0956  522  ARG A NH2 
3712  N N   . ALA A 525  ? 0.5365 0.4209 0.5841 -0.0439 -0.0294 0.0992  523  ALA A N   
3713  C CA  . ALA A 525  ? 0.5622 0.4408 0.6116 -0.0437 -0.0323 0.1037  523  ALA A CA  
3714  C C   . ALA A 525  ? 0.5621 0.4424 0.6040 -0.0402 -0.0312 0.1036  523  ALA A C   
3715  O O   . ALA A 525  ? 0.5484 0.4242 0.5912 -0.0396 -0.0336 0.1071  523  ALA A O   
3716  C CB  . ALA A 525  ? 0.5084 0.3781 0.5654 -0.0430 -0.0373 0.1000  523  ALA A CB  
3717  N N   . MET A 526  ? 0.4830 0.3695 0.5180 -0.0381 -0.0279 0.0997  524  MET A N   
3718  C CA  . MET A 526  ? 0.5709 0.4591 0.5991 -0.0349 -0.0270 0.0994  524  MET A CA  
3719  C C   . MET A 526  ? 0.5675 0.4597 0.5919 -0.0364 -0.0251 0.1072  524  MET A C   
3720  O O   . MET A 526  ? 0.5452 0.4414 0.5703 -0.0397 -0.0231 0.1118  524  MET A O   
3721  C CB  . MET A 526  ? 0.5507 0.4442 0.5730 -0.0324 -0.0241 0.0931  524  MET A CB  
3722  C CG  . MET A 526  ? 0.5222 0.4124 0.5474 -0.0304 -0.0261 0.0854  524  MET A CG  
3723  S SD  . MET A 526  ? 0.6583 0.5544 0.6766 -0.0274 -0.0230 0.0786  524  MET A SD  
3724  C CE  . MET A 526  ? 0.5474 0.4389 0.5705 -0.0255 -0.0261 0.0707  524  MET A CE  
3725  N N   . PRO A 527  ? 0.5336 0.4252 0.5538 -0.0341 -0.0256 0.1088  525  PRO A N   
3726  C CA  . PRO A 527  ? 0.5589 0.4546 0.5753 -0.0354 -0.0240 0.1164  525  PRO A CA  
3727  C C   . PRO A 527  ? 0.5798 0.4850 0.5903 -0.0361 -0.0194 0.1170  525  PRO A C   
3728  O O   . PRO A 527  ? 0.5818 0.4913 0.5917 -0.0387 -0.0176 0.1234  525  PRO A O   
3729  C CB  . PRO A 527  ? 0.5595 0.4530 0.5722 -0.0320 -0.0257 0.1160  525  PRO A CB  
3730  C CG  . PRO A 527  ? 0.5878 0.4743 0.6048 -0.0297 -0.0291 0.1097  525  PRO A CG  
3731  C CD  . PRO A 527  ? 0.5865 0.4742 0.6054 -0.0302 -0.0278 0.1038  525  PRO A CD  
3732  N N   . VAL A 528  ? 0.5748 0.4834 0.5810 -0.0336 -0.0173 0.1105  526  VAL A N   
3733  C CA  . VAL A 528  ? 0.5018 0.4189 0.5031 -0.0340 -0.0131 0.1100  526  VAL A CA  
3734  C C   . VAL A 528  ? 0.4683 0.3855 0.4716 -0.0339 -0.0124 0.1037  526  VAL A C   
3735  O O   . VAL A 528  ? 0.4645 0.3800 0.4666 -0.0311 -0.0130 0.0974  526  VAL A O   
3736  C CB  . VAL A 528  ? 0.4959 0.4175 0.4894 -0.0309 -0.0113 0.1084  526  VAL A CB  
3737  C CG1 . VAL A 528  ? 0.5293 0.4596 0.5182 -0.0315 -0.0071 0.1085  526  VAL A CG1 
3738  C CG2 . VAL A 528  ? 0.5230 0.4434 0.5146 -0.0304 -0.0128 0.1139  526  VAL A CG2 
3739  N N   . VAL A 529  ? 0.4495 0.3692 0.4563 -0.0369 -0.0112 0.1055  527  VAL A N   
3740  C CA  . VAL A 529  ? 0.4635 0.3838 0.4725 -0.0370 -0.0105 0.1000  527  VAL A CA  
3741  C C   . VAL A 529  ? 0.4446 0.3709 0.4472 -0.0346 -0.0074 0.0957  527  VAL A C   
3742  O O   . VAL A 529  ? 0.4414 0.3740 0.4394 -0.0347 -0.0046 0.0983  527  VAL A O   
3743  C CB  . VAL A 529  ? 0.4260 0.3484 0.4399 -0.0409 -0.0097 0.1033  527  VAL A CB  
3744  C CG1 . VAL A 529  ? 0.4576 0.3820 0.4729 -0.0408 -0.0087 0.0977  527  VAL A CG1 
3745  C CG2 . VAL A 529  ? 0.4739 0.3894 0.4952 -0.0433 -0.0133 0.1070  527  VAL A CG2 
3746  N N   . GLY A 530  ? 0.4373 0.3616 0.4395 -0.0323 -0.0081 0.0891  528  GLY A N   
3747  C CA  . GLY A 530  ? 0.3795 0.3086 0.3764 -0.0301 -0.0056 0.0849  528  GLY A CA  
3748  C C   . GLY A 530  ? 0.4011 0.3310 0.3921 -0.0273 -0.0052 0.0840  528  GLY A C   
3749  O O   . GLY A 530  ? 0.3585 0.2930 0.3450 -0.0257 -0.0029 0.0813  528  GLY A O   
3750  N N   . ALA A 531  ? 0.4081 0.3338 0.3994 -0.0265 -0.0074 0.0861  529  ALA A N   
3751  C CA  . ALA A 531  ? 0.4090 0.3354 0.3950 -0.0237 -0.0073 0.0850  529  ALA A CA  
3752  C C   . ALA A 531  ? 0.4440 0.3703 0.4283 -0.0211 -0.0072 0.0782  529  ALA A C   
3753  O O   . ALA A 531  ? 0.4024 0.3251 0.3902 -0.0209 -0.0088 0.0744  529  ALA A O   
3754  C CB  . ALA A 531  ? 0.4553 0.3765 0.4431 -0.0232 -0.0104 0.0879  529  ALA A CB  
3755  N N   . LYS A 532  ? 0.3860 0.3165 0.3647 -0.0193 -0.0052 0.0766  530  LYS A N   
3756  C CA  . LYS A 532  ? 0.4417 0.3724 0.4183 -0.0169 -0.0051 0.0707  530  LYS A CA  
3757  C C   . LYS A 532  ? 0.4053 0.3306 0.3838 -0.0152 -0.0081 0.0684  530  LYS A C   
3758  O O   . LYS A 532  ? 0.3804 0.3025 0.3602 -0.0151 -0.0101 0.0714  530  LYS A O   
3759  C CB  . LYS A 532  ? 0.4365 0.3722 0.4071 -0.0153 -0.0029 0.0704  530  LYS A CB  
3760  C CG  . LYS A 532  ? 0.4990 0.4348 0.4671 -0.0128 -0.0029 0.0651  530  LYS A CG  
3761  C CD  . LYS A 532  ? 0.3989 0.3396 0.3617 -0.0115 -0.0010 0.0649  530  LYS A CD  
3762  C CE  . LYS A 532  ? 0.4061 0.3465 0.3666 -0.0106 -0.0021 0.0679  530  LYS A CE  
3763  N NZ  . LYS A 532  ? 0.3861 0.3222 0.3477 -0.0089 -0.0046 0.0657  530  LYS A NZ  
3764  N N   . HIS A 533  ? 0.4009 0.3255 0.3798 -0.0137 -0.0084 0.0630  531  HIS A N   
3765  C CA  . HIS A 533  ? 0.3835 0.3043 0.3638 -0.0117 -0.0109 0.0600  531  HIS A CA  
3766  C C   . HIS A 533  ? 0.4168 0.3382 0.3934 -0.0099 -0.0112 0.0613  531  HIS A C   
3767  O O   . HIS A 533  ? 0.3934 0.3190 0.3654 -0.0092 -0.0092 0.0612  531  HIS A O   
3768  C CB  . HIS A 533  ? 0.3870 0.3087 0.3672 -0.0104 -0.0106 0.0541  531  HIS A CB  
3769  C CG  . HIS A 533  ? 0.4489 0.3671 0.4316 -0.0085 -0.0133 0.0507  531  HIS A CG  
3770  N ND1 . HIS A 533  ? 0.4039 0.3214 0.3847 -0.0063 -0.0143 0.0500  531  HIS A ND1 
3771  C CD2 . HIS A 533  ? 0.4345 0.3498 0.4215 -0.0083 -0.0152 0.0475  531  HIS A CD2 
3772  C CE1 . HIS A 533  ? 0.4483 0.3629 0.4323 -0.0049 -0.0167 0.0465  531  HIS A CE1 
3773  N NE2 . HIS A 533  ? 0.5106 0.4238 0.4983 -0.0060 -0.0173 0.0449  531  HIS A NE2 
3774  N N   . ASP A 534  ? 0.4455 0.3626 0.4244 -0.0090 -0.0141 0.0623  532  ASP A N   
3775  C CA  . ASP A 534  ? 0.4649 0.3823 0.4407 -0.0073 -0.0148 0.0640  532  ASP A CA  
3776  C C   . ASP A 534  ? 0.4467 0.3669 0.4189 -0.0049 -0.0140 0.0596  532  ASP A C   
3777  O O   . ASP A 534  ? 0.4716 0.3942 0.4400 -0.0038 -0.0135 0.0608  532  ASP A O   
3778  C CB  . ASP A 534  ? 0.5110 0.4227 0.4907 -0.0066 -0.0183 0.0655  532  ASP A CB  
3779  C CG  . ASP A 534  ? 0.5902 0.5000 0.5717 -0.0087 -0.0191 0.0719  532  ASP A CG  
3780  O OD1 . ASP A 534  ? 0.5834 0.4970 0.5626 -0.0106 -0.0167 0.0753  532  ASP A OD1 
3781  O OD2 . ASP A 534  ? 0.7307 0.6352 0.7162 -0.0085 -0.0222 0.0737  532  ASP A OD2 
3782  N N   . ARG A 535  ? 0.3791 0.2992 0.3527 -0.0042 -0.0139 0.0545  533  ARG A N   
3783  C CA  . ARG A 535  ? 0.3921 0.3144 0.3634 -0.0020 -0.0137 0.0503  533  ARG A CA  
3784  C C   . ARG A 535  ? 0.4413 0.3683 0.4092 -0.0023 -0.0108 0.0482  533  ARG A C   
3785  O O   . ARG A 535  ? 0.4120 0.3410 0.3783 -0.0009 -0.0104 0.0447  533  ARG A O   
3786  C CB  . ARG A 535  ? 0.4567 0.3763 0.4317 -0.0006 -0.0158 0.0460  533  ARG A CB  
3787  N N   . ILE A 536  ? 0.3595 0.2883 0.3266 -0.0042 -0.0088 0.0504  534  ILE A N   
3788  C CA  A ILE A 536  ? 0.4036 0.3366 0.3679 -0.0045 -0.0062 0.0487  534  ILE A CA  
3789  C CA  B ILE A 536  ? 0.4036 0.3367 0.3680 -0.0045 -0.0062 0.0487  534  ILE A CA  
3790  C C   . ILE A 536  ? 0.3970 0.3333 0.3576 -0.0048 -0.0046 0.0519  534  ILE A C   
3791  O O   . ILE A 536  ? 0.4016 0.3378 0.3626 -0.0062 -0.0044 0.0560  534  ILE A O   
3792  C CB  A ILE A 536  ? 0.3804 0.3137 0.3470 -0.0061 -0.0052 0.0479  534  ILE A CB  
3793  C CB  B ILE A 536  ? 0.3803 0.3135 0.3469 -0.0062 -0.0052 0.0480  534  ILE A CB  
3794  C CG1 A ILE A 536  ? 0.3813 0.3117 0.3516 -0.0057 -0.0070 0.0445  534  ILE A CG1 
3795  C CG1 B ILE A 536  ? 0.3814 0.3121 0.3515 -0.0057 -0.0068 0.0444  534  ILE A CG1 
3796  C CG2 A ILE A 536  ? 0.3859 0.3232 0.3498 -0.0062 -0.0028 0.0461  534  ILE A CG2 
3797  C CG2 B ILE A 536  ? 0.3860 0.3234 0.3498 -0.0064 -0.0027 0.0467  534  ILE A CG2 
3798  C CD1 A ILE A 536  ? 0.3540 0.2845 0.3269 -0.0072 -0.0065 0.0438  534  ILE A CD1 
3799  C CD1 B ILE A 536  ? 0.3546 0.2875 0.3231 -0.0043 -0.0062 0.0401  534  ILE A CD1 
3800  N N   . ALA A 537  ? 0.3712 0.3106 0.3284 -0.0035 -0.0036 0.0500  535  ALA A N   
3801  C CA  . ALA A 537  ? 0.3923 0.3352 0.3457 -0.0035 -0.0021 0.0523  535  ALA A CA  
3802  C C   . ALA A 537  ? 0.3454 0.2916 0.2980 -0.0047 0.0003  0.0523  535  ALA A C   
3803  O O   . ALA A 537  ? 0.3422 0.2890 0.2953 -0.0047 0.0011  0.0491  535  ALA A O   
3804  C CB  . ALA A 537  ? 0.3282 0.2731 0.2785 -0.0016 -0.0023 0.0499  535  ALA A CB  
3805  N N   . LEU A 538  ? 0.3265 0.2751 0.2778 -0.0057 0.0014  0.0559  536  LEU A N   
3806  C CA  . LEU A 538  ? 0.3522 0.3051 0.3019 -0.0062 0.0038  0.0557  536  LEU A CA  
3807  C C   . LEU A 538  ? 0.3552 0.3107 0.3018 -0.0045 0.0044  0.0523  536  LEU A C   
3808  O O   . LEU A 538  ? 0.3517 0.3069 0.2964 -0.0031 0.0034  0.0517  536  LEU A O   
3809  C CB  . LEU A 538  ? 0.3410 0.2971 0.2892 -0.0072 0.0048  0.0602  536  LEU A CB  
3810  C CG  . LEU A 538  ? 0.3553 0.3098 0.3070 -0.0094 0.0046  0.0639  536  LEU A CG  
3811  C CD1 . LEU A 538  ? 0.4312 0.3895 0.3811 -0.0104 0.0056  0.0688  536  LEU A CD1 
3812  C CD2 . LEU A 538  ? 0.3845 0.3393 0.3388 -0.0106 0.0057  0.0620  536  LEU A CD2 
3813  N N   . PRO A 539  ? 0.3154 0.2732 0.2617 -0.0045 0.0060  0.0499  537  PRO A N   
3814  C CA  . PRO A 539  ? 0.3018 0.2616 0.2457 -0.0030 0.0065  0.0466  537  PRO A CA  
3815  C C   . PRO A 539  ? 0.3022 0.2650 0.2425 -0.0018 0.0065  0.0475  537  PRO A C   
3816  O O   . PRO A 539  ? 0.3286 0.2913 0.2676 -0.0004 0.0056  0.0453  537  PRO A O   
3817  C CB  . PRO A 539  ? 0.3109 0.2729 0.2553 -0.0034 0.0082  0.0451  537  PRO A CB  
3818  C CG  . PRO A 539  ? 0.2858 0.2454 0.2337 -0.0050 0.0081  0.0461  537  PRO A CG  
3819  C CD  . PRO A 539  ? 0.2755 0.2333 0.2243 -0.0059 0.0071  0.0497  537  PRO A CD  
3820  N N   . ALA A 540  ? 0.2772 0.2431 0.2160 -0.0023 0.0074  0.0508  538  ALA A N   
3821  C CA  . ALA A 540  ? 0.3353 0.3050 0.2704 -0.0011 0.0075  0.0517  538  ALA A CA  
3822  C C   . ALA A 540  ? 0.3520 0.3193 0.2863 -0.0003 0.0054  0.0532  538  ALA A C   
3823  O O   . ALA A 540  ? 0.3561 0.3263 0.2872 0.0010  0.0051  0.0532  538  ALA A O   
3824  C CB  . ALA A 540  ? 0.3963 0.3703 0.3300 -0.0019 0.0090  0.0555  538  ALA A CB  
3825  N N   . GLU A 541  ? 0.3283 0.2908 0.2656 -0.0011 0.0039  0.0542  539  GLU A N   
3826  C CA  . GLU A 541  ? 0.3724 0.3323 0.3097 -0.0003 0.0018  0.0557  539  GLU A CA  
3827  C C   . GLU A 541  ? 0.3671 0.3239 0.3059 0.0008  0.0003  0.0518  539  GLU A C   
3828  O O   . GLU A 541  ? 0.3305 0.2843 0.2704 0.0014  -0.0017 0.0524  539  GLU A O   
3829  C CB  . GLU A 541  ? 0.3748 0.3318 0.3146 -0.0018 0.0009  0.0601  539  GLU A CB  
3830  C CG  . GLU A 541  ? 0.4370 0.3977 0.3755 -0.0032 0.0025  0.0643  539  GLU A CG  
3831  C CD  . GLU A 541  ? 0.5535 0.5113 0.4950 -0.0051 0.0016  0.0691  539  GLU A CD  
3832  O OE1 . GLU A 541  ? 0.6123 0.5647 0.5572 -0.0052 -0.0004 0.0688  539  GLU A OE1 
3833  O OE2 . GLU A 541  ? 0.5889 0.5501 0.5295 -0.0064 0.0029  0.0731  539  GLU A OE2 
3834  N N   . LEU A 542  ? 0.3268 0.2845 0.2658 0.0011  0.0013  0.0479  540  LEU A N   
3835  C CA  A LEU A 542  ? 0.3375 0.2928 0.2782 0.0018  0.0002  0.0444  540  LEU A CA  
3836  C CA  B LEU A 542  ? 0.3375 0.2928 0.2781 0.0018  0.0002  0.0444  540  LEU A CA  
3837  C C   . LEU A 542  ? 0.3451 0.3006 0.2844 0.0034  -0.0015 0.0436  540  LEU A C   
3838  O O   . LEU A 542  ? 0.3557 0.3088 0.2969 0.0040  -0.0029 0.0420  540  LEU A O   
3839  C CB  A LEU A 542  ? 0.3114 0.2682 0.2521 0.0017  0.0016  0.0409  540  LEU A CB  
3840  C CB  B LEU A 542  ? 0.3134 0.2703 0.2541 0.0018  0.0015  0.0408  540  LEU A CB  
3841  C CG  A LEU A 542  ? 0.3246 0.2792 0.2680 0.0016  0.0011  0.0379  540  LEU A CG  
3842  C CG  B LEU A 542  ? 0.3227 0.2780 0.2662 0.0005  0.0023  0.0399  540  LEU A CG  
3843  C CD1 A LEU A 542  ? 0.3355 0.2872 0.2819 0.0004  0.0008  0.0391  540  LEU A CD1 
3844  C CD1 B LEU A 542  ? 0.2933 0.2498 0.2368 0.0007  0.0031  0.0365  540  LEU A CD1 
3845  C CD2 A LEU A 542  ? 0.2880 0.2444 0.2312 0.0014  0.0025  0.0352  540  LEU A CD2 
3846  C CD2 B LEU A 542  ? 0.3342 0.2857 0.2806 0.0002  0.0008  0.0399  540  LEU A CD2 
3847  N N   . PHE A 543  ? 0.3236 0.2823 0.2596 0.0043  -0.0014 0.0447  541  PHE A N   
3848  C CA  . PHE A 543  ? 0.3285 0.2880 0.2630 0.0059  -0.0030 0.0439  541  PHE A CA  
3849  C C   . PHE A 543  ? 0.3761 0.3350 0.3095 0.0064  -0.0044 0.0480  541  PHE A C   
3850  O O   . PHE A 543  ? 0.3954 0.3556 0.3271 0.0078  -0.0058 0.0478  541  PHE A O   
3851  C CB  . PHE A 543  ? 0.3243 0.2881 0.2559 0.0068  -0.0022 0.0414  541  PHE A CB  
3852  C CG  . PHE A 543  ? 0.3167 0.2807 0.2497 0.0063  -0.0009 0.0378  541  PHE A CG  
3853  C CD1 . PHE A 543  ? 0.3233 0.2847 0.2591 0.0061  -0.0015 0.0354  541  PHE A CD1 
3854  C CD2 . PHE A 543  ? 0.3541 0.3209 0.2856 0.0060  0.0008  0.0370  541  PHE A CD2 
3855  C CE1 . PHE A 543  ? 0.3260 0.2874 0.2631 0.0055  -0.0005 0.0326  541  PHE A CE1 
3856  C CE2 . PHE A 543  ? 0.3023 0.2688 0.2354 0.0056  0.0017  0.0339  541  PHE A CE2 
3857  C CZ  . PHE A 543  ? 0.3677 0.3314 0.3035 0.0052  0.0011  0.0319  541  PHE A CZ  
3858  N N   . GLY A 544  ? 0.4122 0.3692 0.3470 0.0050  -0.0043 0.0517  542  GLY A N   
3859  C CA  . GLY A 544  ? 0.4057 0.3616 0.3401 0.0052  -0.0058 0.0562  542  GLY A CA  
3860  C C   . GLY A 544  ? 0.4737 0.4344 0.4037 0.0060  -0.0056 0.0584  542  GLY A C   
3861  O O   . GLY A 544  ? 0.4134 0.3785 0.3408 0.0057  -0.0036 0.0583  542  GLY A O   
3862  N N   . ASP A 545  ? 0.4438 0.4039 0.3729 0.0073  -0.0077 0.0603  543  ASP A N   
3863  C CA  . ASP A 545  ? 0.4722 0.4370 0.3970 0.0083  -0.0079 0.0627  543  ASP A CA  
3864  C C   . ASP A 545  ? 0.4384 0.4075 0.3602 0.0099  -0.0075 0.0583  543  ASP A C   
3865  O O   . ASP A 545  ? 0.4634 0.4376 0.3813 0.0107  -0.0072 0.0596  543  ASP A O   
3866  C CB  . ASP A 545  ? 0.4866 0.4492 0.4117 0.0093  -0.0106 0.0661  543  ASP A CB  
3867  C CG  . ASP A 545  ? 0.6267 0.5851 0.5546 0.0077  -0.0114 0.0712  543  ASP A CG  
3868  O OD1 . ASP A 545  ? 0.6718 0.6306 0.6005 0.0057  -0.0095 0.0730  543  ASP A OD1 
3869  O OD2 . ASP A 545  ? 0.7465 0.7013 0.6764 0.0084  -0.0140 0.0732  543  ASP A OD2 
3870  N N   . ALA A 546  ? 0.4160 0.3836 0.3397 0.0103  -0.0075 0.0534  544  ALA A N   
3871  C CA  . ALA A 546  ? 0.4106 0.3820 0.3321 0.0117  -0.0074 0.0492  544  ALA A CA  
3872  C C   . ALA A 546  ? 0.4405 0.4168 0.3593 0.0113  -0.0051 0.0485  544  ALA A C   
3873  O O   . ALA A 546  ? 0.4113 0.3923 0.3265 0.0125  -0.0052 0.0479  544  ALA A O   
3874  C CB  . ALA A 546  ? 0.3886 0.3575 0.3133 0.0117  -0.0076 0.0444  544  ALA A CB  
3875  N N   . ARG A 547  ? 0.4141 0.3894 0.3343 0.0098  -0.0032 0.0485  545  ARG A N   
3876  C CA  . ARG A 547  ? 0.3486 0.3284 0.2668 0.0096  -0.0012 0.0472  545  ARG A CA  
3877  C C   . ARG A 547  ? 0.3816 0.3596 0.3022 0.0078  0.0006  0.0481  545  ARG A C   
3878  O O   . ARG A 547  ? 0.3430 0.3162 0.2670 0.0068  0.0002  0.0483  545  ARG A O   
3879  C CB  . ARG A 547  ? 0.3946 0.3760 0.3125 0.0107  -0.0012 0.0417  545  ARG A CB  
3880  C CG  . ARG A 547  ? 0.3863 0.3633 0.3081 0.0100  -0.0013 0.0388  545  ARG A CG  
3881  C CD  . ARG A 547  ? 0.4148 0.3932 0.3368 0.0109  -0.0015 0.0338  545  ARG A CD  
3882  N NE  . ARG A 547  ? 0.3895 0.3639 0.3150 0.0103  -0.0021 0.0316  545  ARG A NE  
3883  C CZ  . ARG A 547  ? 0.3506 0.3236 0.2785 0.0093  -0.0011 0.0294  545  ARG A CZ  
3884  N NH1 . ARG A 547  ? 0.3765 0.3513 0.3037 0.0090  0.0005  0.0287  545  ARG A NH1 
3885  N NH2 . ARG A 547  ? 0.3825 0.3525 0.3134 0.0088  -0.0016 0.0278  545  ARG A NH2 
3886  N N   . THR A 548  ? 0.3605 0.3428 0.2792 0.0075  0.0025  0.0486  546  THR A N   
3887  C CA  . THR A 548  ? 0.3186 0.3003 0.2394 0.0059  0.0043  0.0494  546  THR A CA  
3888  C C   . THR A 548  ? 0.3128 0.2934 0.2355 0.0060  0.0050  0.0446  546  THR A C   
3889  O O   . THR A 548  ? 0.3077 0.2913 0.2287 0.0073  0.0053  0.0411  546  THR A O   
3890  C CB  . THR A 548  ? 0.3623 0.3498 0.2804 0.0056  0.0061  0.0520  546  THR A CB  
3891  O OG1 . THR A 548  ? 0.4025 0.3914 0.3185 0.0056  0.0053  0.0568  546  THR A OG1 
3892  C CG2 . THR A 548  ? 0.3616 0.3485 0.2823 0.0038  0.0079  0.0534  546  THR A CG2 
3893  N N   . ASN A 549  ? 0.3137 0.2900 0.2399 0.0047  0.0052  0.0444  547  ASN A N   
3894  C CA  . ASN A 549  ? 0.3293 0.3045 0.2575 0.0046  0.0059  0.0405  547  ASN A CA  
3895  C C   . ASN A 549  ? 0.3042 0.2835 0.2314 0.0047  0.0078  0.0396  547  ASN A C   
3896  O O   . ASN A 549  ? 0.3239 0.3061 0.2499 0.0042  0.0089  0.0425  547  ASN A O   
3897  C CB  . ASN A 549  ? 0.3199 0.2903 0.2518 0.0031  0.0057  0.0410  547  ASN A CB  
3898  C CG  . ASN A 549  ? 0.3425 0.3114 0.2766 0.0030  0.0060  0.0373  547  ASN A CG  
3899  O OD1 . ASN A 549  ? 0.2858 0.2561 0.2190 0.0040  0.0060  0.0343  547  ASN A OD1 
3900  N ND2 . ASN A 549  ? 0.2879 0.2537 0.2248 0.0018  0.0062  0.0377  547  ASN A ND2 
3901  N N   . SER A 550  ? 0.2897 0.2695 0.2175 0.0054  0.0080  0.0355  548  SER A N   
3902  C CA  . SER A 550  ? 0.2751 0.2584 0.2026 0.0057  0.0096  0.0342  548  SER A CA  
3903  C C   . SER A 550  ? 0.3015 0.2830 0.2317 0.0041  0.0108  0.0358  548  SER A C   
3904  O O   . SER A 550  ? 0.3352 0.3124 0.2679 0.0030  0.0102  0.0365  548  SER A O   
3905  C CB  . SER A 550  ? 0.2984 0.2819 0.2264 0.0069  0.0093  0.0294  548  SER A CB  
3906  O OG  . SER A 550  ? 0.3084 0.2872 0.2395 0.0061  0.0085  0.0280  548  SER A OG  
3907  N N   . ALA A 551  ? 0.2896 0.2751 0.2194 0.0042  0.0124  0.0362  549  ALA A N   
3908  C CA  . ALA A 551  ? 0.3262 0.3110 0.2587 0.0027  0.0135  0.0376  549  ALA A CA  
3909  C C   . ALA A 551  ? 0.3248 0.3097 0.2590 0.0034  0.0141  0.0339  549  ALA A C   
3910  O O   . ALA A 551  ? 0.3106 0.2985 0.2436 0.0050  0.0142  0.0310  549  ALA A O   
3911  C CB  . ALA A 551  ? 0.3394 0.3288 0.2707 0.0021  0.0151  0.0410  549  ALA A CB  
3912  N N   . GLY A 552  ? 0.2934 0.2749 0.2307 0.0022  0.0141  0.0340  550  GLY A N   
3913  C CA  . GLY A 552  ? 0.3068 0.2883 0.2461 0.0026  0.0146  0.0313  550  GLY A CA  
3914  C C   . GLY A 552  ? 0.3099 0.2945 0.2504 0.0021  0.0162  0.0327  550  GLY A C   
3915  O O   . GLY A 552  ? 0.3309 0.3189 0.2703 0.0016  0.0172  0.0355  550  GLY A O   
3916  N N   . LEU A 553  ? 0.3159 0.2994 0.2590 0.0021  0.0164  0.0309  551  LEU A N   
3917  C CA  . LEU A 553  ? 0.3245 0.3108 0.2695 0.0017  0.0177  0.0319  551  LEU A CA  
3918  C C   . LEU A 553  ? 0.3157 0.2981 0.2638 0.0005  0.0172  0.0320  551  LEU A C   
3919  O O   . LEU A 553  ? 0.3113 0.2900 0.2602 0.0007  0.0161  0.0301  551  LEU A O   
3920  C CB  . LEU A 553  ? 0.3513 0.3419 0.2962 0.0036  0.0185  0.0289  551  LEU A CB  
3921  C CG  . LEU A 553  ? 0.3608 0.3566 0.3025 0.0051  0.0191  0.0281  551  LEU A CG  
3922  C CD1 . LEU A 553  ? 0.3387 0.3376 0.2813 0.0072  0.0194  0.0241  551  LEU A CD1 
3923  C CD2 . LEU A 553  ? 0.3672 0.3677 0.3076 0.0041  0.0206  0.0318  551  LEU A CD2 
3924  N N   . ASP A 554  ? 0.3345 0.3179 0.2843 -0.0008 0.0180  0.0341  552  ASP A N   
3925  C CA  . ASP A 554  ? 0.3586 0.3388 0.3113 -0.0019 0.0175  0.0344  552  ASP A CA  
3926  C C   . ASP A 554  ? 0.2807 0.2629 0.2354 -0.0010 0.0180  0.0324  552  ASP A C   
3927  O O   . ASP A 554  ? 0.2903 0.2765 0.2459 -0.0010 0.0193  0.0331  552  ASP A O   
3928  C CB  . ASP A 554  ? 0.3175 0.2976 0.2715 -0.0039 0.0178  0.0377  552  ASP A CB  
3929  C CG  . ASP A 554  ? 0.3324 0.3095 0.2894 -0.0051 0.0171  0.0377  552  ASP A CG  
3930  O OD1 . ASP A 554  ? 0.3426 0.3180 0.3005 -0.0044 0.0165  0.0355  552  ASP A OD1 
3931  O OD2 . ASP A 554  ? 0.3536 0.3300 0.3120 -0.0067 0.0170  0.0400  552  ASP A OD2 
3932  N N   . LEU A 555  ? 0.3293 0.3087 0.2848 -0.0002 0.0170  0.0300  553  LEU A N   
3933  C CA  . LEU A 555  ? 0.3137 0.2943 0.2712 0.0009  0.0172  0.0282  553  LEU A CA  
3934  C C   . LEU A 555  ? 0.3454 0.3253 0.3058 -0.0003 0.0172  0.0294  553  LEU A C   
3935  O O   . LEU A 555  ? 0.3166 0.2971 0.2790 0.0006  0.0171  0.0280  553  LEU A O   
3936  C CB  . LEU A 555  ? 0.3168 0.2946 0.2745 0.0021  0.0160  0.0255  553  LEU A CB  
3937  C CG  . LEU A 555  ? 0.3130 0.2919 0.2684 0.0035  0.0158  0.0236  553  LEU A CG  
3938  C CD1 . LEU A 555  ? 0.3860 0.3622 0.3425 0.0046  0.0145  0.0208  553  LEU A CD1 
3939  C CD2 . LEU A 555  ? 0.3248 0.3093 0.2793 0.0048  0.0171  0.0229  553  LEU A CD2 
3940  N N   . SER A 556  ? 0.3671 0.3457 0.3278 -0.0021 0.0171  0.0317  554  SER A N   
3941  C CA  . SER A 556  ? 0.3357 0.3145 0.2990 -0.0033 0.0171  0.0328  554  SER A CA  
3942  C C   . SER A 556  ? 0.3443 0.3272 0.3085 -0.0042 0.0185  0.0348  554  SER A C   
3943  O O   . SER A 556  ? 0.3050 0.2888 0.2718 -0.0052 0.0186  0.0357  554  SER A O   
3944  C CB  . SER A 556  ? 0.3211 0.2960 0.2848 -0.0047 0.0160  0.0338  554  SER A CB  
3945  O OG  . SER A 556  ? 0.3363 0.3110 0.2994 -0.0060 0.0161  0.0358  554  SER A OG  
3946  N N   . ASN A 557  ? 0.3163 0.3021 0.2786 -0.0038 0.0195  0.0356  555  ASN A N   
3947  C CA  . ASN A 557  ? 0.3006 0.2907 0.2635 -0.0049 0.0208  0.0379  555  ASN A CA  
3948  C C   . ASN A 557  ? 0.3394 0.3350 0.3030 -0.0034 0.0221  0.0365  555  ASN A C   
3949  O O   . ASN A 557  ? 0.3012 0.2985 0.2629 -0.0014 0.0224  0.0343  555  ASN A O   
3950  C CB  . ASN A 557  ? 0.2899 0.2805 0.2501 -0.0054 0.0211  0.0400  555  ASN A CB  
3951  C CG  . ASN A 557  ? 0.2844 0.2796 0.2451 -0.0068 0.0225  0.0431  555  ASN A CG  
3952  O OD1 . ASN A 557  ? 0.3059 0.3067 0.2673 -0.0062 0.0240  0.0427  555  ASN A OD1 
3953  N ND2 . ASN A 557  ? 0.3030 0.2964 0.2637 -0.0087 0.0221  0.0462  555  ASN A ND2 
3954  N N   . GLU A 558  ? 0.3557 0.3541 0.3222 -0.0041 0.0228  0.0372  556  GLU A N   
3955  C CA  . GLU A 558  ? 0.3215 0.3252 0.2893 -0.0025 0.0239  0.0355  556  GLU A CA  
3956  C C   . GLU A 558  ? 0.3184 0.3281 0.2842 -0.0018 0.0256  0.0359  556  GLU A C   
3957  O O   . GLU A 558  ? 0.3304 0.3438 0.2958 0.0005  0.0262  0.0333  556  GLU A O   
3958  C CB  . GLU A 558  ? 0.3513 0.3573 0.3229 -0.0035 0.0242  0.0363  556  GLU A CB  
3959  C CG  . GLU A 558  ? 0.3745 0.3760 0.3482 -0.0037 0.0227  0.0354  556  GLU A CG  
3960  C CD  . GLU A 558  ? 0.3631 0.3631 0.3371 -0.0013 0.0218  0.0322  556  GLU A CD  
3961  O OE1 . GLU A 558  ? 0.3519 0.3546 0.3250 0.0008  0.0223  0.0302  556  GLU A OE1 
3962  O OE2 . GLU A 558  ? 0.3444 0.3405 0.3196 -0.0015 0.0204  0.0318  556  GLU A OE2 
3963  N N   . GLU A 559  ? 0.3131 0.3242 0.2777 -0.0036 0.0263  0.0393  557  GLU A N   
3964  C CA  . GLU A 559  ? 0.3592 0.3763 0.3213 -0.0030 0.0279  0.0401  557  GLU A CA  
3965  C C   . GLU A 559  ? 0.3380 0.3541 0.2966 -0.0008 0.0273  0.0374  557  GLU A C   
3966  O O   . GLU A 559  ? 0.3191 0.3406 0.2763 0.0012  0.0283  0.0354  557  GLU A O   
3967  C CB  . GLU A 559  ? 0.3231 0.3410 0.2846 -0.0056 0.0284  0.0447  557  GLU A CB  
3968  C CG  . GLU A 559  ? 0.4077 0.4270 0.3729 -0.0081 0.0289  0.0476  557  GLU A CG  
3969  C CD  . GLU A 559  ? 0.5481 0.5759 0.5151 -0.0078 0.0309  0.0477  557  GLU A CD  
3970  O OE1 . GLU A 559  ? 0.5506 0.5842 0.5152 -0.0060 0.0323  0.0466  557  GLU A OE1 
3971  O OE2 . GLU A 559  ? 0.5702 0.5991 0.5410 -0.0092 0.0312  0.0486  557  GLU A OE2 
3972  N N   . THR A 560  ? 0.3253 0.3348 0.2826 -0.0010 0.0257  0.0372  558  THR A N   
3973  C CA  . THR A 560  ? 0.3173 0.3254 0.2717 0.0009  0.0249  0.0345  558  THR A CA  
3974  C C   . THR A 560  ? 0.3028 0.3112 0.2584 0.0033  0.0245  0.0302  558  THR A C   
3975  O O   . THR A 560  ? 0.2904 0.3019 0.2442 0.0055  0.0247  0.0275  558  THR A O   
3976  C CB  . THR A 560  ? 0.2796 0.2807 0.2331 0.0000  0.0231  0.0350  558  THR A CB  
3977  O OG1 . THR A 560  ? 0.3298 0.3303 0.2825 -0.0020 0.0233  0.0389  558  THR A OG1 
3978  C CG2 . THR A 560  ? 0.2890 0.2887 0.2398 0.0019  0.0223  0.0322  558  THR A CG2 
3979  N N   . LEU A 561  ? 0.2782 0.2837 0.2370 0.0031  0.0238  0.0294  559  LEU A N   
3980  C CA  . LEU A 561  ? 0.2670 0.2723 0.2274 0.0054  0.0231  0.0256  559  LEU A CA  
3981  C C   . LEU A 561  ? 0.2904 0.3029 0.2514 0.0072  0.0245  0.0238  559  LEU A C   
3982  O O   . LEU A 561  ? 0.3273 0.3410 0.2881 0.0097  0.0241  0.0202  559  LEU A O   
3983  C CB  . LEU A 561  ? 0.2621 0.2631 0.2257 0.0047  0.0220  0.0256  559  LEU A CB  
3984  C CG  . LEU A 561  ? 0.3132 0.3074 0.2761 0.0034  0.0205  0.0265  559  LEU A CG  
3985  C CD1 . LEU A 561  ? 0.2780 0.2690 0.2438 0.0025  0.0196  0.0271  559  LEU A CD1 
3986  C CD2 . LEU A 561  ? 0.2817 0.2730 0.2431 0.0049  0.0193  0.0239  559  LEU A CD2 
3987  N N   . ALA A 562  ? 0.2816 0.2992 0.2435 0.0061  0.0262  0.0263  560  ALA A N   
3988  C CA  . ALA A 562  ? 0.3263 0.3519 0.2888 0.0077  0.0277  0.0247  560  ALA A CA  
3989  C C   . ALA A 562  ? 0.3334 0.3636 0.2923 0.0092  0.0285  0.0236  560  ALA A C   
3990  O O   . ALA A 562  ? 0.3345 0.3687 0.2933 0.0120  0.0287  0.0198  560  ALA A O   
3991  C CB  . ALA A 562  ? 0.3341 0.3644 0.2986 0.0057  0.0294  0.0281  560  ALA A CB  
3992  N N   . SER A 563  ? 0.2665 0.2964 0.2224 0.0075  0.0289  0.0268  561  SER A N   
3993  C CA  . SER A 563  ? 0.3395 0.3737 0.2915 0.0088  0.0295  0.0260  561  SER A CA  
3994  C C   . SER A 563  ? 0.3502 0.3809 0.3009 0.0111  0.0278  0.0216  561  SER A C   
3995  O O   . SER A 563  ? 0.3679 0.4035 0.3168 0.0135  0.0282  0.0185  561  SER A O   
3996  C CB  . SER A 563  ? 0.3669 0.4002 0.3163 0.0063  0.0298  0.0307  561  SER A CB  
3997  O OG  . SER A 563  ? 0.5065 0.5412 0.4518 0.0076  0.0295  0.0297  561  SER A OG  
3998  N N   . LEU A 564  ? 0.3268 0.3493 0.2785 0.0105  0.0260  0.0212  562  LEU A N   
3999  C CA  . LEU A 564  ? 0.3052 0.3240 0.2561 0.0123  0.0242  0.0174  562  LEU A CA  
4000  C C   . LEU A 564  ? 0.3142 0.3343 0.2678 0.0150  0.0237  0.0129  562  LEU A C   
4001  O O   . LEU A 564  ? 0.3369 0.3582 0.2895 0.0173  0.0230  0.0090  562  LEU A O   
4002  C CB  . LEU A 564  ? 0.3042 0.3145 0.2556 0.0107  0.0225  0.0187  562  LEU A CB  
4003  C CG  . LEU A 564  ? 0.3295 0.3349 0.2805 0.0118  0.0206  0.0157  562  LEU A CG  
4004  C CD1 . LEU A 564  ? 0.2910 0.2995 0.2385 0.0131  0.0205  0.0142  562  LEU A CD1 
4005  C CD2 . LEU A 564  ? 0.3043 0.3027 0.2558 0.0097  0.0194  0.0179  562  LEU A CD2 
4006  N N   . THR A 565  ? 0.2735 0.2934 0.2306 0.0148  0.0239  0.0131  563  THR A N   
4007  C CA  . THR A 565  ? 0.3403 0.3616 0.3003 0.0175  0.0234  0.0089  563  THR A CA  
4008  C C   . THR A 565  ? 0.3336 0.3631 0.2923 0.0200  0.0245  0.0058  563  THR A C   
4009  O O   . THR A 565  ? 0.3459 0.3755 0.3053 0.0228  0.0233  0.0011  563  THR A O   
4010  C CB  . THR A 565  ? 0.3186 0.3404 0.2824 0.0168  0.0238  0.0102  563  THR A CB  
4011  O OG1 . THR A 565  ? 0.3790 0.3934 0.3442 0.0148  0.0225  0.0124  563  THR A OG1 
4012  C CG2 . THR A 565  ? 0.3658 0.3899 0.3328 0.0199  0.0232  0.0058  563  THR A CG2 
4013  N N   . GLU A 566  ? 0.2933 0.3299 0.2500 0.0192  0.0267  0.0083  564  GLU A N   
4014  C CA  . GLU A 566  ? 0.3094 0.3551 0.2645 0.0216  0.0280  0.0057  564  GLU A CA  
4015  C C   . GLU A 566  ? 0.3628 0.4086 0.3141 0.0229  0.0272  0.0034  564  GLU A C   
4016  O O   . GLU A 566  ? 0.3643 0.4137 0.3154 0.0260  0.0267  -0.0015 564  GLU A O   
4017  C CB  . GLU A 566  ? 0.3230 0.3763 0.2768 0.0199  0.0306  0.0097  564  GLU A CB  
4018  N N   . ALA A 567  ? 0.3594 0.4013 0.3078 0.0207  0.0269  0.0068  565  ALA A N   
4019  C CA  . ALA A 567  ? 0.3742 0.4160 0.3190 0.0218  0.0259  0.0048  565  ALA A CA  
4020  C C   . ALA A 567  ? 0.3512 0.3874 0.2980 0.0238  0.0234  -0.0002 565  ALA A C   
4021  O O   . ALA A 567  ? 0.3378 0.3766 0.2831 0.0262  0.0227  -0.0043 565  ALA A O   
4022  C CB  . ALA A 567  ? 0.3797 0.4176 0.3217 0.0191  0.0257  0.0095  565  ALA A CB  
4023  N N   . LEU A 568  ? 0.3218 0.3505 0.2722 0.0229  0.0221  0.0001  566  LEU A N   
4024  C CA  . LEU A 568  ? 0.2956 0.3186 0.2484 0.0244  0.0197  -0.0041 566  LEU A CA  
4025  C C   . LEU A 568  ? 0.3266 0.3536 0.2821 0.0277  0.0193  -0.0093 566  LEU A C   
4026  O O   . LEU A 568  ? 0.3039 0.3301 0.2598 0.0299  0.0177  -0.0139 566  LEU A O   
4027  C CB  . LEU A 568  ? 0.2835 0.2981 0.2393 0.0223  0.0185  -0.0018 566  LEU A CB  
4028  C CG  . LEU A 568  ? 0.3032 0.3124 0.2571 0.0194  0.0181  0.0022  566  LEU A CG  
4029  C CD1 . LEU A 568  ? 0.2680 0.2703 0.2250 0.0177  0.0172  0.0042  566  LEU A CD1 
4030  C CD2 . LEU A 568  ? 0.3117 0.3186 0.2635 0.0199  0.0167  0.0003  566  LEU A CD2 
4031  N N   . ARG A 569  ? 0.3447 0.3760 0.3022 0.0282  0.0208  -0.0089 567  ARG A N   
4032  C CA  . ARG A 569  ? 0.3384 0.3746 0.2985 0.0317  0.0205  -0.0140 567  ARG A CA  
4033  C C   . ARG A 569  ? 0.3503 0.3943 0.3070 0.0341  0.0212  -0.0175 567  ARG A C   
4034  O O   . ARG A 569  ? 0.3406 0.3860 0.2989 0.0372  0.0198  -0.0232 567  ARG A O   
4035  C CB  . ARG A 569  ? 0.4160 0.4569 0.3786 0.0317  0.0222  -0.0126 567  ARG A CB  
4036  C CG  . ARG A 569  ? 0.4193 0.4534 0.3859 0.0302  0.0213  -0.0104 567  ARG A CG  
4037  C CD  . ARG A 569  ? 0.4447 0.4842 0.4146 0.0316  0.0224  -0.0113 567  ARG A CD  
4038  N NE  . ARG A 569  ? 0.5276 0.5633 0.4999 0.0293  0.0225  -0.0073 567  ARG A NE  
4039  C CZ  . ARG A 569  ? 0.5804 0.6188 0.5565 0.0302  0.0228  -0.0077 567  ARG A CZ  
4040  N NH1 . ARG A 569  ? 0.5878 0.6323 0.5660 0.0336  0.0230  -0.0121 567  ARG A NH1 
4041  N NH2 . ARG A 569  ? 0.5548 0.5898 0.5327 0.0279  0.0228  -0.0040 567  ARG A NH2 
4042  N N   . GLU A 570  ? 0.3352 0.3846 0.2875 0.0326  0.0232  -0.0140 568  GLU A N   
4043  C CA  . GLU A 570  ? 0.3652 0.4228 0.3138 0.0347  0.0239  -0.0168 568  GLU A CA  
4044  C C   . GLU A 570  ? 0.3909 0.4441 0.3382 0.0359  0.0215  -0.0204 568  GLU A C   
4045  O O   . GLU A 570  ? 0.3267 0.3848 0.2733 0.0390  0.0209  -0.0258 568  GLU A O   
4046  C CB  . GLU A 570  ? 0.3996 0.4630 0.3437 0.0325  0.0264  -0.0114 568  GLU A CB  
4047  C CG  . GLU A 570  ? 0.4885 0.5589 0.4338 0.0318  0.0290  -0.0087 568  GLU A CG  
4048  C CD  . GLU A 570  ? 0.5376 0.6113 0.4797 0.0286  0.0311  -0.0020 568  GLU A CD  
4049  O OE1 . GLU A 570  ? 0.6366 0.7066 0.5754 0.0270  0.0305  0.0006  568  GLU A OE1 
4050  O OE2 . GLU A 570  ? 0.6270 0.7069 0.5700 0.0277  0.0333  0.0006  568  GLU A OE2 
4051  N N   . SER A 571  ? 0.3471 0.3915 0.2943 0.0335  0.0201  -0.0178 569  SER A N   
4052  C CA  . SER A 571  ? 0.3594 0.3999 0.3058 0.0343  0.0178  -0.0210 569  SER A CA  
4053  C C   . SER A 571  ? 0.3651 0.4026 0.3158 0.0371  0.0155  -0.0272 569  SER A C   
4054  O O   . SER A 571  ? 0.3388 0.3768 0.2889 0.0390  0.0138  -0.0318 569  SER A O   
4055  C CB  . SER A 571  ? 0.2994 0.3312 0.2454 0.0311  0.0168  -0.0168 569  SER A CB  
4056  O OG  . SER A 571  ? 0.3697 0.3937 0.3202 0.0301  0.0157  -0.0162 569  SER A OG  
4057  N N   . ALA A 572  ? 0.3571 0.3919 0.3124 0.0374  0.0152  -0.0276 570  ALA A N   
4058  C CA  . ALA A 572  ? 0.3994 0.4307 0.3594 0.0399  0.0128  -0.0331 570  ALA A CA  
4059  C C   . ALA A 572  ? 0.4180 0.4579 0.3787 0.0439  0.0131  -0.0389 570  ALA A C   
4060  O O   . ALA A 572  ? 0.4283 0.4660 0.3928 0.0465  0.0108  -0.0444 570  ALA A O   
4061  C CB  . ALA A 572  ? 0.3638 0.3886 0.3286 0.0388  0.0121  -0.0310 570  ALA A CB  
4062  N N   . ALA A 573  ? 0.3939 0.4436 0.3511 0.0444  0.0159  -0.0376 571  ALA A N   
4063  C CA  . ALA A 573  ? 0.4113 0.4709 0.3680 0.0481  0.0166  -0.0430 571  ALA A CA  
4064  C C   . ALA A 573  ? 0.4566 0.5215 0.4086 0.0494  0.0164  -0.0456 571  ALA A C   
4065  O O   . ALA A 573  ? 0.5289 0.6031 0.4796 0.0525  0.0171  -0.0501 571  ALA A O   
4066  C CB  . ALA A 573  ? 0.4209 0.4894 0.3765 0.0479  0.0198  -0.0401 571  ALA A CB  
4067  N N   . MET A 574  ? 0.4057 0.4652 0.3550 0.0471  0.0155  -0.0430 572  MET A N   
4068  C CA  . MET A 574  ? 0.4500 0.5142 0.3947 0.0481  0.0152  -0.0452 572  MET A CA  
4069  C C   . MET A 574  ? 0.4019 0.4623 0.3494 0.0507  0.0118  -0.0523 572  MET A C   
4070  O O   . MET A 574  ? 0.4035 0.4546 0.3559 0.0502  0.0095  -0.0534 572  MET A O   
4071  C CB  . MET A 574  ? 0.4095 0.4702 0.3503 0.0446  0.0157  -0.0390 572  MET A CB  
4072  C CG  . MET A 574  ? 0.4297 0.4958 0.3670 0.0424  0.0189  -0.0325 572  MET A CG  
4073  S SD  . MET A 574  ? 0.4955 0.5565 0.4291 0.0382  0.0193  -0.0251 572  MET A SD  
4074  C CE  . MET A 574  ? 0.5327 0.6011 0.4637 0.0362  0.0229  -0.0186 572  MET A CE  
4075  N N   . LYS A 575  ? 0.4199 0.4879 0.3645 0.0534  0.0115  -0.0571 573  LYS A N   
4076  C CA  . LYS A 575  ? 0.4225 0.4881 0.3699 0.0561  0.0082  -0.0645 573  LYS A CA  
4077  C C   . LYS A 575  ? 0.3959 0.4567 0.3406 0.0543  0.0066  -0.0633 573  LYS A C   
4078  O O   . LYS A 575  ? 0.3996 0.4662 0.3406 0.0558  0.0061  -0.0663 573  LYS A O   
4079  C CB  . LYS A 575  ? 0.5006 0.5774 0.4467 0.0605  0.0085  -0.0713 573  LYS A CB  
4080  N N   . TRP A 576  ? 0.3220 0.3725 0.2689 0.0510  0.0057  -0.0589 574  TRP A N   
4081  C CA  . TRP A 576  ? 0.3642 0.4098 0.3092 0.0489  0.0043  -0.0572 574  TRP A CA  
4082  C C   . TRP A 576  ? 0.3429 0.3874 0.2901 0.0513  0.0010  -0.0645 574  TRP A C   
4083  O O   . TRP A 576  ? 0.3786 0.4192 0.3314 0.0530  -0.0011 -0.0693 574  TRP A O   
4084  C CB  . TRP A 576  ? 0.3617 0.3967 0.3097 0.0453  0.0039  -0.0520 574  TRP A CB  
4085  C CG  . TRP A 576  ? 0.3446 0.3800 0.2907 0.0427  0.0067  -0.0448 574  TRP A CG  
4086  C CD1 . TRP A 576  ? 0.3297 0.3620 0.2791 0.0418  0.0076  -0.0424 574  TRP A CD1 
4087  C CD2 . TRP A 576  ? 0.3145 0.3530 0.2552 0.0405  0.0088  -0.0392 574  TRP A CD2 
4088  N NE1 . TRP A 576  ? 0.3359 0.3695 0.2825 0.0392  0.0102  -0.0359 574  TRP A NE1 
4089  C CE2 . TRP A 576  ? 0.3303 0.3675 0.2716 0.0384  0.0109  -0.0337 574  TRP A CE2 
4090  C CE3 . TRP A 576  ? 0.3098 0.3522 0.2455 0.0403  0.0090  -0.0382 574  TRP A CE3 
4091  C CZ2 . TRP A 576  ? 0.3129 0.3521 0.2503 0.0359  0.0131  -0.0274 574  TRP A CZ2 
4092  C CZ3 . TRP A 576  ? 0.3548 0.3990 0.2863 0.0379  0.0111  -0.0316 574  TRP A CZ3 
4093  C CH2 . TRP A 576  ? 0.3798 0.4224 0.3124 0.0357  0.0131  -0.0264 574  TRP A CH2 
4094  N N   . THR A 577  ? 0.3772 0.4251 0.3201 0.0514  0.0005  -0.0653 575  THR A N   
4095  C CA  . THR A 577  ? 0.3609 0.4079 0.3056 0.0534  -0.0027 -0.0721 575  THR A CA  
4096  C C   . THR A 577  ? 0.3313 0.3753 0.2733 0.0511  -0.0037 -0.0695 575  THR A C   
4097  O O   . THR A 577  ? 0.3220 0.3676 0.2593 0.0489  -0.0017 -0.0634 575  THR A O   
4098  C CB  . THR A 577  ? 0.4257 0.4836 0.3679 0.0576  -0.0028 -0.0788 575  THR A CB  
4099  O OG1 . THR A 577  ? 0.3942 0.4607 0.3291 0.0573  -0.0006 -0.0756 575  THR A OG1 
4100  C CG2 . THR A 577  ? 0.4362 0.4988 0.3807 0.0603  -0.0016 -0.0816 575  THR A CG2 
4101  N N   . ALA A 578  ? 0.3495 0.3892 0.2948 0.0517  -0.0070 -0.0744 576  ALA A N   
4102  C CA  . ALA A 578  ? 0.3225 0.3606 0.2655 0.0502  -0.0084 -0.0735 576  ALA A CA  
4103  C C   . ALA A 578  ? 0.3441 0.3855 0.2882 0.0532  -0.0113 -0.0818 576  ALA A C   
4104  O O   . ALA A 578  ? 0.3487 0.3867 0.2985 0.0548  -0.0137 -0.0875 576  ALA A O   
4105  C CB  . ALA A 578  ? 0.3187 0.3458 0.2657 0.0465  -0.0096 -0.0697 576  ALA A CB  
4106  N N   . LEU A 579  ? 0.3720 0.4201 0.3107 0.0541  -0.0113 -0.0826 577  LEU A N   
4107  C CA  . LEU A 579  ? 0.3873 0.4401 0.3262 0.0571  -0.0140 -0.0906 577  LEU A CA  
4108  C C   . LEU A 579  ? 0.3509 0.4020 0.2877 0.0554  -0.0157 -0.0895 577  LEU A C   
4109  O O   . LEU A 579  ? 0.3316 0.3814 0.2651 0.0527  -0.0140 -0.0825 577  LEU A O   
4110  C CB  . LEU A 579  ? 0.3681 0.4337 0.3016 0.0607  -0.0124 -0.0937 577  LEU A CB  
4111  C CG  . LEU A 579  ? 0.3988 0.4689 0.3323 0.0623  -0.0099 -0.0935 577  LEU A CG  
4112  C CD1 . LEU A 579  ? 0.4783 0.5622 0.4059 0.0657  -0.0084 -0.0966 577  LEU A CD1 
4113  C CD2 . LEU A 579  ? 0.4305 0.4948 0.3718 0.0638  -0.0120 -0.0989 577  LEU A CD2 
4114  N N   . PRO A 580  ? 0.3462 0.3976 0.2854 0.0571  -0.0190 -0.0964 578  PRO A N   
4115  C CA  . PRO A 580  ? 0.3398 0.3923 0.2761 0.0561  -0.0204 -0.0960 578  PRO A CA  
4116  C C   . PRO A 580  ? 0.4172 0.4809 0.3450 0.0577  -0.0183 -0.0941 578  PRO A C   
4117  O O   . PRO A 580  ? 0.4141 0.4867 0.3395 0.0613  -0.0184 -0.0995 578  PRO A O   
4118  C CB  . PRO A 580  ? 0.3921 0.4437 0.3332 0.0582  -0.0246 -0.1049 578  PRO A CB  
4119  C CG  . PRO A 580  ? 0.3690 0.4159 0.3169 0.0593  -0.0255 -0.1088 578  PRO A CG  
4120  C CD  . PRO A 580  ? 0.3785 0.4299 0.3231 0.0601  -0.0218 -0.1052 578  PRO A CD  
4121  N N   . GLN A 581  ? 0.3770 0.4404 0.3005 0.0552  -0.0163 -0.0864 579  GLN A N   
4122  C CA  . GLN A 581  ? 0.3594 0.4327 0.2749 0.0561  -0.0140 -0.0830 579  GLN A CA  
4123  C C   . GLN A 581  ? 0.4006 0.4757 0.3132 0.0559  -0.0160 -0.0833 579  GLN A C   
4124  O O   . GLN A 581  ? 0.3473 0.4180 0.2588 0.0531  -0.0157 -0.0773 579  GLN A O   
4125  C CB  . GLN A 581  ? 0.3596 0.4312 0.2725 0.0535  -0.0105 -0.0740 579  GLN A CB  
4126  C CG  . GLN A 581  ? 0.3335 0.4046 0.2488 0.0538  -0.0084 -0.0734 579  GLN A CG  
4127  C CD  . GLN A 581  ? 0.3832 0.4657 0.2950 0.0573  -0.0069 -0.0770 579  GLN A CD  
4128  O OE1 . GLN A 581  ? 0.4483 0.5398 0.3553 0.0595  -0.0074 -0.0796 579  GLN A OE1 
4129  N NE2 . GLN A 581  ? 0.3885 0.4713 0.3028 0.0579  -0.0053 -0.0774 579  GLN A NE2 
4130  N N   . LEU A 582  ? 0.4134 0.4952 0.3248 0.0590  -0.0182 -0.0905 580  LEU A N   
4131  C CA  . LEU A 582  ? 0.3945 0.4794 0.3029 0.0593  -0.0203 -0.0917 580  LEU A CA  
4132  C C   . LEU A 582  ? 0.4164 0.5114 0.3161 0.0602  -0.0182 -0.0872 580  LEU A C   
4133  O O   . LEU A 582  ? 0.3973 0.4979 0.2934 0.0608  -0.0152 -0.0841 580  LEU A O   
4134  C CB  . LEU A 582  ? 0.3759 0.4639 0.2871 0.0623  -0.0239 -0.1018 580  LEU A CB  
4135  C CG  . LEU A 582  ? 0.4796 0.5572 0.3991 0.0608  -0.0272 -0.1058 580  LEU A CG  
4136  C CD1 . LEU A 582  ? 0.4492 0.5185 0.3751 0.0597  -0.0266 -0.1055 580  LEU A CD1 
4137  C CD2 . LEU A 582  ? 0.5056 0.5872 0.4271 0.0638  -0.0310 -0.1156 580  LEU A CD2 
4138  N N   . ALA A 583  ? 0.3957 0.4932 0.2923 0.0601  -0.0198 -0.0866 581  ALA A N   
4139  C CA  . ALA A 583  ? 0.4028 0.5100 0.2911 0.0610  -0.0182 -0.0823 581  ALA A CA  
4140  C C   . ALA A 583  ? 0.4996 0.6190 0.3836 0.0648  -0.0174 -0.0870 581  ALA A C   
4141  O O   . ALA A 583  ? 0.5035 0.6310 0.3813 0.0653  -0.0147 -0.0822 581  ALA A O   
4142  C CB  . ALA A 583  ? 0.4040 0.5118 0.2902 0.0607  -0.0207 -0.0820 581  ALA A CB  
4143  N N   . THR A 584  ? 0.4387 0.5599 0.3262 0.0675  -0.0197 -0.0964 582  THR A N   
4144  C CA  . THR A 584  ? 0.4728 0.6060 0.3568 0.0716  -0.0194 -0.1024 582  THR A CA  
4145  C C   . THR A 584  ? 0.5014 0.6358 0.3871 0.0724  -0.0168 -0.1027 582  THR A C   
4146  O O   . THR A 584  ? 0.5580 0.7030 0.4410 0.0758  -0.0161 -0.1076 582  THR A O   
4147  C CB  . THR A 584  ? 0.5233 0.6577 0.4109 0.0743  -0.0236 -0.1130 582  THR A CB  
4148  O OG1 . THR A 584  ? 0.5018 0.6238 0.3982 0.0727  -0.0255 -0.1158 582  THR A OG1 
4149  C CG2 . THR A 584  ? 0.4730 0.6101 0.3572 0.0744  -0.0260 -0.1132 582  THR A CG2 
4150  N N   . GLY A 585  ? 0.4321 0.5566 0.3222 0.0694  -0.0152 -0.0979 583  GLY A N   
4151  C CA  . GLY A 585  ? 0.4367 0.5616 0.3289 0.0700  -0.0128 -0.0978 583  GLY A CA  
4152  C C   . GLY A 585  ? 0.4634 0.5767 0.3644 0.0690  -0.0144 -0.1011 583  GLY A C   
4153  O O   . GLY A 585  ? 0.4282 0.5328 0.3338 0.0675  -0.0173 -0.1028 583  GLY A O   
4154  N N   . PRO A 586  ? 0.4622 0.5752 0.3659 0.0696  -0.0126 -0.1016 584  PRO A N   
4155  C CA  . PRO A 586  ? 0.4757 0.5780 0.3878 0.0689  -0.0142 -0.1045 584  PRO A CA  
4156  C C   . PRO A 586  ? 0.4798 0.5817 0.3965 0.0718  -0.0182 -0.1148 584  PRO A C   
4157  O O   . PRO A 586  ? 0.4978 0.6096 0.4113 0.0753  -0.0192 -0.1209 584  PRO A O   
4158  C CB  . PRO A 586  ? 0.5029 0.6082 0.4157 0.0699  -0.0113 -0.1035 584  PRO A CB  
4159  C CG  . PRO A 586  ? 0.4927 0.6096 0.3974 0.0703  -0.0079 -0.0987 584  PRO A CG  
4160  C CD  . PRO A 586  ? 0.5134 0.6370 0.4126 0.0714  -0.0092 -0.1001 584  PRO A CD  
4161  N N   . ALA A 587  ? 0.4428 0.5331 0.3672 0.0702  -0.0207 -0.1166 585  ALA A N   
4162  C CA  . ALA A 587  ? 0.4779 0.5663 0.4078 0.0725  -0.0249 -0.1262 585  ALA A CA  
4163  C C   . ALA A 587  ? 0.5059 0.5883 0.4432 0.0734  -0.0257 -0.1298 585  ALA A C   
4164  O O   . ALA A 587  ? 0.5092 0.5860 0.4484 0.0713  -0.0235 -0.1242 585  ALA A O   
4165  C CB  . ALA A 587  ? 0.4983 0.5785 0.4314 0.0699  -0.0280 -0.1261 585  ALA A CB  
4166  N N   . ALA A 588  ? 0.5075 0.5913 0.4491 0.0768  -0.0289 -0.1395 586  ALA A N   
4167  C CA  . ALA A 588  ? 0.5381 0.6158 0.4876 0.0780  -0.0304 -0.1439 586  ALA A CA  
4168  C C   . ALA A 588  ? 0.4483 0.5119 0.4057 0.0748  -0.0334 -0.1429 586  ALA A C   
4169  O O   . ALA A 588  ? 0.5129 0.5730 0.4703 0.0725  -0.0351 -0.1416 586  ALA A O   
4170  C CB  . ALA A 588  ? 0.5103 0.5953 0.4615 0.0832  -0.0329 -0.1550 586  ALA A CB  
4171  N N   . GLY A 589  ? 0.4889 0.5449 0.4532 0.0746  -0.0341 -0.1435 587  GLY A N   
4172  C CA  . GLY A 589  ? 0.4905 0.5334 0.4625 0.0714  -0.0368 -0.1421 587  GLY A CA  
4173  C C   . GLY A 589  ? 0.4663 0.5021 0.4451 0.0716  -0.0372 -0.1423 587  GLY A C   
4174  O O   . GLY A 589  ? 0.4531 0.4942 0.4312 0.0747  -0.0357 -0.1446 587  GLY A O   
4175  N N   . GLU A 590  ? 0.4616 0.4855 0.4471 0.0683  -0.0392 -0.1396 588  GLU A N   
4176  C CA  . GLU A 590  ? 0.4733 0.4892 0.4656 0.0680  -0.0398 -0.1387 588  GLU A CA  
4177  C C   . GLU A 590  ? 0.4768 0.4925 0.4653 0.0658  -0.0354 -0.1297 588  GLU A C   
4178  O O   . GLU A 590  ? 0.4721 0.4855 0.4571 0.0621  -0.0335 -0.1222 588  GLU A O   
4179  C CB  . GLU A 590  ? 0.5750 0.5788 0.5756 0.0649  -0.0434 -0.1383 588  GLU A CB  
4180  N N   . THR A 591  ? 0.5032 0.5213 0.4925 0.0683  -0.0341 -0.1307 589  THR A N   
4181  C CA  . THR A 591  ? 0.4377 0.4572 0.4234 0.0669  -0.0299 -0.1233 589  THR A CA  
4182  C C   . THR A 591  ? 0.4715 0.4809 0.4643 0.0653  -0.0308 -0.1204 589  THR A C   
4183  O O   . THR A 591  ? 0.4911 0.4972 0.4906 0.0677  -0.0337 -0.1261 589  THR A O   
4184  C CB  . THR A 591  ? 0.4591 0.4905 0.4402 0.0708  -0.0274 -0.1262 589  THR A CB  
4185  O OG1 . THR A 591  ? 0.4458 0.4869 0.4195 0.0719  -0.0262 -0.1277 589  THR A OG1 
4186  C CG2 . THR A 591  ? 0.4460 0.4785 0.4242 0.0693  -0.0233 -0.1188 589  THR A CG2 
4187  N N   . ARG A 592  ? 0.4614 0.4661 0.4526 0.0614  -0.0285 -0.1116 590  ARG A N   
4188  C CA  . ARG A 592  ? 0.4439 0.4401 0.4409 0.0598  -0.0289 -0.1081 590  ARG A CA  
4189  C C   . ARG A 592  ? 0.4192 0.4172 0.4116 0.0578  -0.0247 -0.1000 590  ARG A C   
4190  O O   . ARG A 592  ? 0.4062 0.4101 0.3914 0.0567  -0.0217 -0.0963 590  ARG A O   
4191  C CB  . ARG A 592  ? 0.5371 0.5222 0.5399 0.0564  -0.0318 -0.1060 590  ARG A CB  
4192  C CG  . ARG A 592  ? 0.5040 0.4873 0.5027 0.0521  -0.0303 -0.0994 590  ARG A CG  
4193  C CD  . ARG A 592  ? 0.6075 0.5799 0.6123 0.0484  -0.0323 -0.0954 590  ARG A CD  
4194  N NE  . ARG A 592  ? 0.6277 0.5985 0.6289 0.0444  -0.0309 -0.0892 590  ARG A NE  
4195  C CZ  . ARG A 592  ? 0.6378 0.6080 0.6354 0.0418  -0.0277 -0.0816 590  ARG A CZ  
4196  N NH1 . ARG A 592  ? 0.5555 0.5265 0.5525 0.0424  -0.0256 -0.0789 590  ARG A NH1 
4197  N NH2 . ARG A 592  ? 0.6032 0.5723 0.5980 0.0385  -0.0268 -0.0769 590  ARG A NH2 
4198  N N   . THR A 593  ? 0.4033 0.3960 0.3999 0.0573  -0.0245 -0.0973 591  THR A N   
4199  C CA  . THR A 593  ? 0.4284 0.4226 0.4214 0.0555  -0.0208 -0.0902 591  THR A CA  
4200  C C   . THR A 593  ? 0.4244 0.4117 0.4168 0.0507  -0.0202 -0.0825 591  THR A C   
4201  O O   . THR A 593  ? 0.4285 0.4080 0.4252 0.0487  -0.0228 -0.0823 591  THR A O   
4202  C CB  . THR A 593  ? 0.4558 0.4484 0.4534 0.0574  -0.0210 -0.0910 591  THR A CB  
4203  O OG1 . THR A 593  ? 0.4932 0.4757 0.4987 0.0567  -0.0246 -0.0920 591  THR A OG1 
4204  C CG2 . THR A 593  ? 0.5002 0.5015 0.4977 0.0624  -0.0211 -0.0985 591  THR A CG2 
4205  N N   . VAL A 594  ? 0.3648 0.3552 0.3517 0.0488  -0.0166 -0.0762 592  VAL A N   
4206  C CA  . VAL A 594  ? 0.3526 0.3374 0.3385 0.0444  -0.0155 -0.0687 592  VAL A CA  
4207  C C   . VAL A 594  ? 0.3622 0.3443 0.3501 0.0436  -0.0141 -0.0644 592  VAL A C   
4208  O O   . VAL A 594  ? 0.3627 0.3507 0.3484 0.0454  -0.0119 -0.0643 592  VAL A O   
4209  C CB  . VAL A 594  ? 0.3266 0.3168 0.3051 0.0429  -0.0128 -0.0650 592  VAL A CB  
4210  C CG1 . VAL A 594  ? 0.3268 0.3115 0.3044 0.0387  -0.0117 -0.0576 592  VAL A CG1 
4211  C CG2 . VAL A 594  ? 0.3743 0.3677 0.3508 0.0440  -0.0144 -0.0696 592  VAL A CG2 
4212  N N   . LEU A 595  ? 0.3295 0.3031 0.3218 0.0411  -0.0155 -0.0610 593  LEU A N   
4213  C CA  . LEU A 595  ? 0.3325 0.3026 0.3276 0.0405  -0.0149 -0.0575 593  LEU A CA  
4214  C C   . LEU A 595  ? 0.3445 0.3125 0.3366 0.0366  -0.0127 -0.0498 593  LEU A C   
4215  O O   . LEU A 595  ? 0.3361 0.3020 0.3264 0.0340  -0.0127 -0.0472 593  LEU A O   
4216  C CB  . LEU A 595  ? 0.3443 0.3063 0.3472 0.0406  -0.0185 -0.0594 593  LEU A CB  
4217  C CG  . LEU A 595  ? 0.3828 0.3454 0.3901 0.0445  -0.0214 -0.0674 593  LEU A CG  
4218  C CD1 . LEU A 595  ? 0.4006 0.3544 0.4162 0.0443  -0.0250 -0.0682 593  LEU A CD1 
4219  C CD2 . LEU A 595  ? 0.3452 0.3159 0.3507 0.0483  -0.0198 -0.0711 593  LEU A CD2 
4220  N N   . ASN A 596  ? 0.3011 0.2699 0.2931 0.0365  -0.0109 -0.0464 594  ASN A N   
4221  C CA  . ASN A 596  ? 0.3164 0.2826 0.3065 0.0331  -0.0091 -0.0394 594  ASN A CA  
4222  C C   . ASN A 596  ? 0.3025 0.2602 0.2975 0.0308  -0.0115 -0.0372 594  ASN A C   
4223  O O   . ASN A 596  ? 0.3541 0.3079 0.3546 0.0319  -0.0136 -0.0388 594  ASN A O   
4224  C CB  . ASN A 596  ? 0.3311 0.3004 0.3208 0.0339  -0.0070 -0.0373 594  ASN A CB  
4225  C CG  . ASN A 596  ? 0.3067 0.2747 0.2939 0.0306  -0.0050 -0.0305 594  ASN A CG  
4226  O OD1 . ASN A 596  ? 0.3184 0.2812 0.3061 0.0278  -0.0057 -0.0271 594  ASN A OD1 
4227  N ND2 . ASN A 596  ? 0.3329 0.3058 0.3176 0.0310  -0.0025 -0.0285 594  ASN A ND2 
4228  N N   . PRO A 597  ? 0.3094 0.2641 0.3028 0.0276  -0.0113 -0.0336 595  PRO A N   
4229  C CA  . PRO A 597  ? 0.3095 0.2567 0.3076 0.0252  -0.0135 -0.0312 595  PRO A CA  
4230  C C   . PRO A 597  ? 0.3263 0.2707 0.3266 0.0243  -0.0131 -0.0270 595  PRO A C   
4231  O O   . PRO A 597  ? 0.3114 0.2500 0.3169 0.0235  -0.0153 -0.0261 595  PRO A O   
4232  C CB  . PRO A 597  ? 0.3042 0.2508 0.2992 0.0222  -0.0128 -0.0281 595  PRO A CB  
4233  C CG  . PRO A 597  ? 0.3754 0.3284 0.3640 0.0226  -0.0099 -0.0273 595  PRO A CG  
4234  C CD  . PRO A 597  ? 0.3157 0.2740 0.3034 0.0261  -0.0095 -0.0318 595  PRO A CD  
4235  N N   . GLY A 598  ? 0.3506 0.2991 0.3473 0.0245  -0.0104 -0.0244 596  GLY A N   
4236  C CA  . GLY A 598  ? 0.3056 0.2523 0.3042 0.0239  -0.0100 -0.0208 596  GLY A CA  
4237  C C   . GLY A 598  ? 0.3768 0.3234 0.3796 0.0270  -0.0113 -0.0240 596  GLY A C   
4238  O O   . GLY A 598  ? 0.3573 0.3016 0.3628 0.0267  -0.0116 -0.0213 596  GLY A O   
4239  N N   . ASP A 599  ? 0.3568 0.3063 0.3604 0.0301  -0.0121 -0.0299 597  ASP A N   
4240  C CA  . ASP A 599  ? 0.3697 0.3200 0.3774 0.0335  -0.0133 -0.0338 597  ASP A CA  
4241  C C   . ASP A 599  ? 0.3438 0.2966 0.3523 0.0366  -0.0148 -0.0407 597  ASP A C   
4242  O O   . ASP A 599  ? 0.3309 0.2909 0.3353 0.0382  -0.0128 -0.0433 597  ASP A O   
4243  C CB  . ASP A 599  ? 0.3376 0.2939 0.3427 0.0347  -0.0106 -0.0325 597  ASP A CB  
4244  C CG  . ASP A 599  ? 0.3943 0.3512 0.4041 0.0380  -0.0119 -0.0356 597  ASP A CG  
4245  O OD1 . ASP A 599  ? 0.3746 0.3288 0.3891 0.0404  -0.0148 -0.0404 597  ASP A OD1 
4246  O OD2 . ASP A 599  ? 0.4356 0.3958 0.4445 0.0383  -0.0101 -0.0334 597  ASP A OD2 
4247  N N   . HIS A 600  ? 0.3129 0.2601 0.3270 0.0373  -0.0182 -0.0439 598  HIS A N   
4248  C CA  . HIS A 600  ? 0.3749 0.3242 0.3902 0.0400  -0.0199 -0.0509 598  HIS A CA  
4249  C C   . HIS A 600  ? 0.3833 0.3386 0.3992 0.0444  -0.0196 -0.0563 598  HIS A C   
4250  O O   . HIS A 600  ? 0.4290 0.3881 0.4445 0.0470  -0.0204 -0.0624 598  HIS A O   
4251  C CB  . HIS A 600  ? 0.3406 0.2818 0.3623 0.0395  -0.0240 -0.0528 598  HIS A CB  
4252  C CG  . HIS A 600  ? 0.3675 0.3048 0.3883 0.0356  -0.0243 -0.0492 598  HIS A CG  
4253  N ND1 . HIS A 600  ? 0.4175 0.3481 0.4436 0.0344  -0.0277 -0.0504 598  HIS A ND1 
4254  C CD2 . HIS A 600  ? 0.3563 0.2956 0.3715 0.0326  -0.0217 -0.0446 598  HIS A CD2 
4255  C CE1 . HIS A 600  ? 0.4404 0.3695 0.4642 0.0308  -0.0270 -0.0466 598  HIS A CE1 
4256  N NE2 . HIS A 600  ? 0.3984 0.3326 0.4156 0.0298  -0.0234 -0.0431 598  HIS A NE2 
4257  N N   . ARG A 601  ? 0.3422 0.2992 0.3589 0.0454  -0.0184 -0.0544 599  ARG A N   
4258  C CA  . ARG A 601  ? 0.3870 0.3512 0.4037 0.0495  -0.0176 -0.0593 599  ARG A CA  
4259  C C   . ARG A 601  ? 0.3504 0.3242 0.3599 0.0498  -0.0139 -0.0593 599  ARG A C   
4260  O O   . ARG A 601  ? 0.4026 0.3836 0.4113 0.0533  -0.0132 -0.0643 599  ARG A O   
4261  C CB  . ARG A 601  ? 0.3671 0.3306 0.3869 0.0503  -0.0173 -0.0569 599  ARG A CB  
4262  C CG  . ARG A 601  ? 0.3775 0.3317 0.4044 0.0502  -0.0209 -0.0563 599  ARG A CG  
4263  C CD  . ARG A 601  ? 0.3733 0.3267 0.4021 0.0501  -0.0203 -0.0523 599  ARG A CD  
4264  N NE  . ARG A 601  ? 0.3729 0.3281 0.3964 0.0466  -0.0171 -0.0455 599  ARG A NE  
4265  C CZ  . ARG A 601  ? 0.4871 0.4426 0.5109 0.0459  -0.0160 -0.0413 599  ARG A CZ  
4266  N NH1 . ARG A 601  ? 0.4794 0.4339 0.5083 0.0485  -0.0177 -0.0428 599  ARG A NH1 
4267  N NH2 . ARG A 601  ? 0.4780 0.4350 0.4969 0.0427  -0.0132 -0.0356 599  ARG A NH2 
4268  N N   . ASP A 602  ? 0.3457 0.3197 0.3500 0.0463  -0.0117 -0.0538 600  ASP A N   
4269  C CA  . ASP A 602  ? 0.3361 0.3185 0.3336 0.0460  -0.0082 -0.0525 600  ASP A CA  
4270  C C   . ASP A 602  ? 0.3642 0.3489 0.3587 0.0464  -0.0087 -0.0559 600  ASP A C   
4271  O O   . ASP A 602  ? 0.3830 0.3635 0.3763 0.0436  -0.0093 -0.0535 600  ASP A O   
4272  C CB  . ASP A 602  ? 0.3363 0.3172 0.3305 0.0421  -0.0058 -0.0449 600  ASP A CB  
4273  C CG  . ASP A 602  ? 0.3733 0.3619 0.3609 0.0413  -0.0025 -0.0428 600  ASP A CG  
4274  O OD1 . ASP A 602  ? 0.4053 0.4017 0.3909 0.0439  -0.0013 -0.0464 600  ASP A OD1 
4275  O OD2 . ASP A 602  ? 0.3861 0.3729 0.3706 0.0380  -0.0011 -0.0373 600  ASP A OD2 
4276  N N   . VAL A 603  ? 0.3891 0.3811 0.3827 0.0499  -0.0085 -0.0618 601  VAL A N   
4277  C CA  . VAL A 603  ? 0.3780 0.3737 0.3683 0.0508  -0.0090 -0.0656 601  VAL A CA  
4278  C C   . VAL A 603  ? 0.3782 0.3805 0.3612 0.0490  -0.0055 -0.0614 601  VAL A C   
4279  O O   . VAL A 603  ? 0.3994 0.4089 0.3795 0.0499  -0.0028 -0.0603 601  VAL A O   
4280  C CB  . VAL A 603  ? 0.3269 0.3285 0.3192 0.0555  -0.0103 -0.0738 601  VAL A CB  
4281  C CG1 . VAL A 603  ? 0.3765 0.3820 0.3654 0.0564  -0.0110 -0.0779 601  VAL A CG1 
4282  C CG2 . VAL A 603  ? 0.4367 0.4314 0.4369 0.0574  -0.0139 -0.0778 601  VAL A CG2 
4283  N N   . VAL A 604  ? 0.3658 0.3656 0.3458 0.0465  -0.0057 -0.0591 602  VAL A N   
4284  C CA  . VAL A 604  ? 0.3343 0.3391 0.3076 0.0446  -0.0028 -0.0547 602  VAL A CA  
4285  C C   . VAL A 604  ? 0.3627 0.3761 0.3317 0.0470  -0.0023 -0.0589 602  VAL A C   
4286  O O   . VAL A 604  ? 0.3487 0.3695 0.3125 0.0469  0.0005  -0.0565 602  VAL A O   
4287  C CB  . VAL A 604  ? 0.3661 0.3643 0.3384 0.0407  -0.0031 -0.0496 602  VAL A CB  
4288  C CG1 . VAL A 604  ? 0.3602 0.3628 0.3261 0.0387  -0.0002 -0.0445 602  VAL A CG1 
4289  C CG2 . VAL A 604  ? 0.3244 0.3141 0.3013 0.0386  -0.0040 -0.0461 602  VAL A CG2 
4290  N N   . GLY A 605  ? 0.3427 0.3553 0.3139 0.0491  -0.0051 -0.0651 603  GLY A N   
4291  C CA  . GLY A 605  ? 0.3750 0.3957 0.3421 0.0514  -0.0050 -0.0694 603  GLY A CA  
4292  C C   . GLY A 605  ? 0.3642 0.3821 0.3351 0.0534  -0.0087 -0.0764 603  GLY A C   
4293  O O   . GLY A 605  ? 0.3664 0.3769 0.3437 0.0536  -0.0112 -0.0786 603  GLY A O   
4294  N N   . SER A 606  ? 0.3574 0.3811 0.3245 0.0548  -0.0091 -0.0799 604  SER A N   
4295  C CA  . SER A 606  ? 0.3816 0.4033 0.3521 0.0566  -0.0127 -0.0869 604  SER A CA  
4296  C C   . SER A 606  ? 0.3751 0.3980 0.3414 0.0552  -0.0131 -0.0861 604  SER A C   
4297  O O   . SER A 606  ? 0.3723 0.4016 0.3319 0.0545  -0.0105 -0.0826 604  SER A O   
4298  C CB  . SER A 606  ? 0.4510 0.4805 0.4223 0.0615  -0.0134 -0.0949 604  SER A CB  
4299  O OG  . SER A 606  ? 0.5239 0.5647 0.4881 0.0629  -0.0109 -0.0951 604  SER A OG  
4300  N N   . VAL A 607  ? 0.3332 0.3497 0.3034 0.0545  -0.0164 -0.0890 605  VAL A N   
4301  C CA  . VAL A 607  ? 0.3352 0.3525 0.3022 0.0532  -0.0173 -0.0890 605  VAL A CA  
4302  C C   . VAL A 607  ? 0.4006 0.4205 0.3699 0.0564  -0.0206 -0.0979 605  VAL A C   
4303  O O   . VAL A 607  ? 0.3795 0.3946 0.3556 0.0578  -0.0234 -0.1028 605  VAL A O   
4304  C CB  . VAL A 607  ? 0.3272 0.3349 0.2967 0.0490  -0.0182 -0.0838 605  VAL A CB  
4305  C CG1 . VAL A 607  ? 0.3597 0.3581 0.3375 0.0484  -0.0211 -0.0857 605  VAL A CG1 
4306  C CG2 . VAL A 607  ? 0.3258 0.3346 0.2929 0.0481  -0.0196 -0.0847 605  VAL A CG2 
4307  N N   . THR A 608  ? 0.3569 0.3846 0.3207 0.0577  -0.0204 -0.0999 606  THR A N   
4308  C CA  . THR A 608  ? 0.4338 0.4640 0.3991 0.0602  -0.0236 -0.1081 606  THR A CA  
4309  C C   . THR A 608  ? 0.3895 0.4152 0.3547 0.0573  -0.0253 -0.1062 606  THR A C   
4310  O O   . THR A 608  ? 0.3599 0.3885 0.3192 0.0555  -0.0232 -0.1009 606  THR A O   
4311  C CB  . THR A 608  ? 0.4126 0.4557 0.3717 0.0639  -0.0223 -0.1121 606  THR A CB  
4312  O OG1 . THR A 608  ? 0.4344 0.4820 0.3943 0.0667  -0.0209 -0.1144 606  THR A OG1 
4313  C CG2 . THR A 608  ? 0.4299 0.4759 0.3902 0.0665  -0.0259 -0.1206 606  THR A CG2 
4314  N N   . GLU A 609  ? 0.3962 0.4149 0.3682 0.0569  -0.0291 -0.1103 607  GLU A N   
4315  C CA  . GLU A 609  ? 0.3886 0.4016 0.3618 0.0535  -0.0306 -0.1076 607  GLU A CA  
4316  C C   . GLU A 609  ? 0.3966 0.4149 0.3680 0.0551  -0.0329 -0.1134 607  GLU A C   
4317  O O   . GLU A 609  ? 0.4106 0.4342 0.3825 0.0589  -0.0346 -0.1211 607  GLU A O   
4318  C CB  . GLU A 609  ? 0.4394 0.4410 0.4213 0.0511  -0.0331 -0.1071 607  GLU A CB  
4319  C CG  . GLU A 609  ? 0.4769 0.4734 0.4593 0.0485  -0.0304 -0.0994 607  GLU A CG  
4320  C CD  . GLU A 609  ? 0.5362 0.5217 0.5264 0.0457  -0.0325 -0.0973 607  GLU A CD  
4321  O OE1 . GLU A 609  ? 0.5570 0.5383 0.5539 0.0466  -0.0361 -0.1029 607  GLU A OE1 
4322  O OE2 . GLU A 609  ? 0.5193 0.5005 0.5091 0.0424  -0.0305 -0.0900 607  GLU A OE2 
4323  N N   . THR A 610  ? 0.3978 0.4150 0.3668 0.0525  -0.0330 -0.1097 608  THR A N   
4324  C CA  . THR A 610  ? 0.4031 0.4265 0.3688 0.0538  -0.0346 -0.1138 608  THR A CA  
4325  C C   . THR A 610  ? 0.3981 0.4169 0.3711 0.0540  -0.0392 -0.1207 608  THR A C   
4326  O O   . THR A 610  ? 0.4291 0.4386 0.4087 0.0511  -0.0408 -0.1189 608  THR A O   
4327  C CB  . THR A 610  ? 0.4104 0.4342 0.3712 0.0509  -0.0330 -0.1070 608  THR A CB  
4328  O OG1 . THR A 610  ? 0.3737 0.4000 0.3291 0.0501  -0.0289 -0.0999 608  THR A OG1 
4329  C CG2 . THR A 610  ? 0.4120 0.4439 0.3679 0.0527  -0.0342 -0.1106 608  THR A CG2 
4330  N N   . SER A 611  ? 0.4681 0.4937 0.4400 0.0575  -0.0414 -0.1286 609  SER A N   
4331  C CA  . SER A 611  ? 0.4683 0.4902 0.4469 0.0576  -0.0460 -0.1353 609  SER A CA  
4332  C C   . SER A 611  ? 0.4929 0.5136 0.4704 0.0546  -0.0468 -0.1324 609  SER A C   
4333  O O   . SER A 611  ? 0.4662 0.4921 0.4364 0.0540  -0.0444 -0.1276 609  SER A O   
4334  C CB  . SER A 611  ? 0.4754 0.5055 0.4532 0.0624  -0.0482 -0.1452 609  SER A CB  
4335  O OG  . SER A 611  ? 0.4643 0.5043 0.4342 0.0638  -0.0473 -0.1458 609  SER A OG  
4336  N N   . GLU A 612  ? 0.4803 0.4940 0.4655 0.0527  -0.0505 -0.1352 610  GLU A N   
4337  C CA  . GLU A 612  ? 0.5047 0.5174 0.4898 0.0500  -0.0517 -0.1332 610  GLU A CA  
4338  C C   . GLU A 612  ? 0.4684 0.4917 0.4468 0.0527  -0.0521 -0.1370 610  GLU A C   
4339  O O   . GLU A 612  ? 0.4299 0.4558 0.4035 0.0511  -0.0510 -0.1325 610  GLU A O   
4340  C CB  . GLU A 612  ? 0.5445 0.5492 0.5397 0.0480  -0.0560 -0.1372 610  GLU A CB  
4341  C CG  . GLU A 612  ? 0.5927 0.5953 0.5895 0.0447  -0.0575 -0.1350 610  GLU A CG  
4342  C CD  . GLU A 612  ? 0.7221 0.7180 0.7291 0.0432  -0.0621 -0.1400 610  GLU A CD  
4343  O OE1 . GLU A 612  ? 0.8132 0.8013 0.8271 0.0422  -0.0631 -0.1400 610  GLU A OE1 
4344  O OE2 . GLU A 612  ? 0.7137 0.7122 0.7220 0.0430  -0.0649 -0.1441 610  GLU A OE2 
4345  N N   . GLU A 613  ? 0.3947 0.4244 0.3722 0.0569  -0.0537 -0.1451 611  GLU A N   
4346  C CA  . GLU A 613  ? 0.4587 0.4994 0.4293 0.0598  -0.0541 -0.1488 611  GLU A CA  
4347  C C   . GLU A 613  ? 0.4352 0.4829 0.3959 0.0601  -0.0496 -0.1418 611  GLU A C   
4348  O O   . GLU A 613  ? 0.4131 0.4664 0.3681 0.0600  -0.0493 -0.1398 611  GLU A O   
4349  C CB  . GLU A 613  ? 0.4551 0.5017 0.4268 0.0645  -0.0565 -0.1590 611  GLU A CB  
4350  N N   . ASP A 614  ? 0.4671 0.5145 0.4258 0.0605  -0.0463 -0.1379 612  ASP A N   
4351  C CA  . ASP A 614  ? 0.4102 0.4642 0.3598 0.0607  -0.0421 -0.1312 612  ASP A CA  
4352  C C   . ASP A 614  ? 0.3906 0.4397 0.3386 0.0565  -0.0402 -0.1220 612  ASP A C   
4353  O O   . ASP A 614  ? 0.3945 0.4495 0.3352 0.0565  -0.0381 -0.1174 612  ASP A O   
4354  C CB  . ASP A 614  ? 0.4699 0.5255 0.4185 0.0622  -0.0392 -0.1300 612  ASP A CB  
4355  C CG  . ASP A 614  ? 0.4664 0.5313 0.4131 0.0671  -0.0400 -0.1382 612  ASP A CG  
4356  O OD1 . ASP A 614  ? 0.5740 0.6463 0.5178 0.0694  -0.0419 -0.1434 612  ASP A OD1 
4357  O OD2 . ASP A 614  ? 0.5183 0.5835 0.4666 0.0688  -0.0388 -0.1398 612  ASP A OD2 
4358  N N   . ALA A 615  ? 0.3947 0.4334 0.3494 0.0531  -0.0411 -0.1193 613  ALA A N   
4359  C CA  . ALA A 615  ? 0.3689 0.4033 0.3226 0.0493  -0.0398 -0.1116 613  ALA A CA  
4360  C C   . ALA A 615  ? 0.3947 0.4335 0.3456 0.0493  -0.0416 -0.1127 613  ALA A C   
4361  O O   . ALA A 615  ? 0.3642 0.4060 0.3094 0.0484  -0.0397 -0.1069 613  ALA A O   
4362  C CB  . ALA A 615  ? 0.4141 0.4373 0.3760 0.0458  -0.0409 -0.1095 613  ALA A CB  
4363  N N   . ARG A 616  ? 0.3869 0.4262 0.3421 0.0503  -0.0455 -0.1202 614  ARG A N   
4364  C CA  . ARG A 616  ? 0.4246 0.4685 0.3775 0.0506  -0.0475 -0.1220 614  ARG A CA  
4365  C C   . ARG A 616  ? 0.4151 0.4705 0.3588 0.0539  -0.0462 -0.1226 614  ARG A C   
4366  O O   . ARG A 616  ? 0.3869 0.4465 0.3259 0.0535  -0.0462 -0.1197 614  ARG A O   
4367  C CB  . ARG A 616  ? 0.4169 0.4591 0.3768 0.0512  -0.0522 -0.1306 614  ARG A CB  
4368  C CG  . ARG A 616  ? 0.5287 0.5599 0.4982 0.0475  -0.0539 -0.1298 614  ARG A CG  
4369  C CD  . ARG A 616  ? 0.5427 0.5727 0.5188 0.0476  -0.0586 -0.1375 614  ARG A CD  
4370  N NE  . ARG A 616  ? 0.5972 0.6324 0.5737 0.0518  -0.0608 -0.1465 614  ARG A NE  
4371  C CZ  . ARG A 616  ? 0.6023 0.6332 0.5843 0.0529  -0.0619 -0.1507 614  ARG A CZ  
4372  N NH1 . ARG A 616  ? 0.6263 0.6477 0.6142 0.0500  -0.0612 -0.1467 614  ARG A NH1 
4373  N NH2 . ARG A 616  ? 0.6630 0.6996 0.6449 0.0571  -0.0639 -0.1594 614  ARG A NH2 
4374  N N   . ARG A 617  ? 0.3609 0.4218 0.3019 0.0572  -0.0453 -0.1262 615  ARG A N   
4375  C CA  . ARG A 617  ? 0.3871 0.4595 0.3191 0.0603  -0.0437 -0.1261 615  ARG A CA  
4376  C C   . ARG A 617  ? 0.3853 0.4587 0.3110 0.0585  -0.0397 -0.1162 615  ARG A C   
4377  O O   . ARG A 617  ? 0.3752 0.4558 0.2940 0.0594  -0.0390 -0.1136 615  ARG A O   
4378  C CB  . ARG A 617  ? 0.4165 0.4947 0.3478 0.0640  -0.0433 -0.1320 615  ARG A CB  
4379  C CG  . ARG A 617  ? 0.5083 0.5993 0.4302 0.0672  -0.0414 -0.1320 615  ARG A CG  
4380  C CD  . ARG A 617  ? 0.5658 0.6646 0.4877 0.0717  -0.0429 -0.1415 615  ARG A CD  
4381  N NE  . ARG A 617  ? 0.6255 0.7215 0.5507 0.0725  -0.0414 -0.1427 615  ARG A NE  
4382  C CZ  . ARG A 617  ? 0.6632 0.7654 0.5833 0.0739  -0.0377 -0.1395 615  ARG A CZ  
4383  N NH1 . ARG A 617  ? 0.6096 0.7211 0.5209 0.0746  -0.0352 -0.1348 615  ARG A NH1 
4384  N NH2 . ARG A 617  ? 0.5486 0.6478 0.4726 0.0746  -0.0366 -0.1409 615  ARG A NH2 
4385  N N   . ALA A 618  ? 0.3727 0.4387 0.3009 0.0561  -0.0372 -0.1106 616  ALA A N   
4386  C CA  . ALA A 618  ? 0.3848 0.4508 0.3078 0.0542  -0.0337 -0.1014 616  ALA A CA  
4387  C C   . ALA A 618  ? 0.3516 0.4159 0.2733 0.0520  -0.0344 -0.0969 616  ALA A C   
4388  O O   . ALA A 618  ? 0.3462 0.4151 0.2614 0.0520  -0.0326 -0.0915 616  ALA A O   
4389  C CB  . ALA A 618  ? 0.3443 0.4021 0.2712 0.0519  -0.0314 -0.0969 616  ALA A CB  
4390  N N   . VAL A 619  ? 0.3649 0.4226 0.2929 0.0500  -0.0371 -0.0990 617  VAL A N   
4391  C CA  . VAL A 619  ? 0.3437 0.4001 0.2710 0.0479  -0.0378 -0.0951 617  VAL A CA  
4392  C C   . VAL A 619  ? 0.3481 0.4141 0.2695 0.0505  -0.0393 -0.0976 617  VAL A C   
4393  O O   . VAL A 619  ? 0.3469 0.4156 0.2635 0.0500  -0.0384 -0.0923 617  VAL A O   
4394  C CB  . VAL A 619  ? 0.3421 0.3904 0.2778 0.0453  -0.0405 -0.0972 617  VAL A CB  
4395  C CG1 . VAL A 619  ? 0.3441 0.3922 0.2790 0.0435  -0.0414 -0.0938 617  VAL A CG1 
4396  C CG2 . VAL A 619  ? 0.3378 0.3768 0.2788 0.0425  -0.0389 -0.0938 617  VAL A CG2 
4397  N N   . ARG A 620  ? 0.3535 0.4250 0.2752 0.0535  -0.0417 -0.1058 618  ARG A N   
4398  C CA  . ARG A 620  ? 0.3768 0.4583 0.2925 0.0562  -0.0432 -0.1084 618  ARG A CA  
4399  C C   . ARG A 620  ? 0.3998 0.4893 0.3066 0.0579  -0.0400 -0.1035 618  ARG A C   
4400  O O   . ARG A 620  ? 0.4132 0.5086 0.3142 0.0586  -0.0401 -0.1005 618  ARG A O   
4401  C CB  . ARG A 620  ? 0.4396 0.5256 0.3579 0.0591  -0.0465 -0.1187 618  ARG A CB  
4402  C CG  . ARG A 620  ? 0.5300 0.6078 0.4579 0.0573  -0.0498 -0.1237 618  ARG A CG  
4403  C CD  . ARG A 620  ? 0.5890 0.6719 0.5190 0.0602  -0.0537 -0.1341 618  ARG A CD  
4404  N NE  . ARG A 620  ? 0.6443 0.7343 0.5709 0.0640  -0.0529 -0.1388 618  ARG A NE  
4405  C CZ  . ARG A 620  ? 0.5774 0.6638 0.5090 0.0649  -0.0533 -0.1434 618  ARG A CZ  
4406  N NH1 . ARG A 620  ? 0.5129 0.5887 0.4534 0.0622  -0.0546 -0.1440 618  ARG A NH1 
4407  N NH2 . ARG A 620  ? 0.5913 0.6855 0.5191 0.0686  -0.0523 -0.1475 618  ARG A NH2 
4408  N N   . LEU A 621  ? 0.3709 0.4607 0.2768 0.0586  -0.0373 -0.1024 619  LEU A N   
4409  C CA  . LEU A 621  ? 0.3989 0.4958 0.2968 0.0597  -0.0340 -0.0968 619  LEU A CA  
4410  C C   . LEU A 621  ? 0.3984 0.4911 0.2941 0.0567  -0.0319 -0.0871 619  LEU A C   
4411  O O   . LEU A 621  ? 0.3798 0.4789 0.2687 0.0574  -0.0307 -0.0824 619  LEU A O   
4412  C CB  . LEU A 621  ? 0.3934 0.4910 0.2917 0.0606  -0.0315 -0.0976 619  LEU A CB  
4413  C CG  . LEU A 621  ? 0.4088 0.5129 0.3078 0.0643  -0.0329 -0.1068 619  LEU A CG  
4414  C CD1 . LEU A 621  ? 0.4426 0.5450 0.3436 0.0647  -0.0304 -0.1067 619  LEU A CD1 
4415  C CD2 . LEU A 621  ? 0.4496 0.5669 0.3405 0.0676  -0.0329 -0.1085 619  LEU A CD2 
4416  N N   . ALA A 622  ? 0.3535 0.4357 0.2550 0.0535  -0.0316 -0.0840 620  ALA A N   
4417  C CA  . ALA A 622  ? 0.3487 0.4265 0.2488 0.0508  -0.0299 -0.0755 620  ALA A CA  
4418  C C   . ALA A 622  ? 0.3880 0.4682 0.2859 0.0508  -0.0321 -0.0746 620  ALA A C   
4419  O O   . ALA A 622  ? 0.3881 0.4708 0.2810 0.0505  -0.0309 -0.0683 620  ALA A O   
4420  C CB  . ALA A 622  ? 0.3390 0.4056 0.2460 0.0475  -0.0293 -0.0732 620  ALA A CB  
4421  N N   . ALA A 623  ? 0.3967 0.4766 0.2986 0.0512  -0.0355 -0.0809 621  ALA A N   
4422  C CA  . ALA A 623  ? 0.3883 0.4713 0.2883 0.0516  -0.0378 -0.0807 621  ALA A CA  
4423  C C   . ALA A 623  ? 0.4183 0.5123 0.3099 0.0545  -0.0377 -0.0800 621  ALA A C   
4424  O O   . ALA A 623  ? 0.4156 0.5120 0.3030 0.0544  -0.0378 -0.0751 621  ALA A O   
4425  C CB  . ALA A 623  ? 0.3532 0.4347 0.2591 0.0516  -0.0417 -0.0884 621  ALA A CB  
4426  N N   . ASP A 624  ? 0.4089 0.5099 0.2978 0.0573  -0.0374 -0.0849 622  ASP A N   
4427  C CA  A ASP A 624  ? 0.4510 0.5635 0.3316 0.0603  -0.0372 -0.0844 622  ASP A CA  
4428  C CA  B ASP A 624  ? 0.4510 0.5636 0.3317 0.0603  -0.0372 -0.0844 622  ASP A CA  
4429  C C   . ASP A 624  ? 0.4440 0.5578 0.3189 0.0593  -0.0339 -0.0749 622  ASP A C   
4430  O O   . ASP A 624  ? 0.4956 0.6161 0.3644 0.0604  -0.0340 -0.0712 622  ASP A O   
4431  C CB  A ASP A 624  ? 0.4624 0.5822 0.3416 0.0634  -0.0372 -0.0915 622  ASP A CB  
4432  C CB  B ASP A 624  ? 0.4624 0.5822 0.3417 0.0634  -0.0372 -0.0915 622  ASP A CB  
4433  C CG  A ASP A 624  ? 0.4591 0.5781 0.3440 0.0645  -0.0409 -0.1014 622  ASP A CG  
4434  C CG  B ASP A 624  ? 0.4734 0.6059 0.3458 0.0668  -0.0387 -0.0947 622  ASP A CG  
4435  O OD1 A ASP A 624  ? 0.5064 0.6225 0.3944 0.0636  -0.0438 -0.1030 622  ASP A OD1 
4436  O OD1 B ASP A 624  ? 0.4974 0.6340 0.3644 0.0669  -0.0386 -0.0892 622  ASP A OD1 
4437  O OD2 A ASP A 624  ? 0.4839 0.6053 0.3705 0.0665  -0.0411 -0.1077 622  ASP A OD2 
4438  O OD2 B ASP A 624  ? 0.5317 0.6701 0.4042 0.0697  -0.0400 -0.1027 622  ASP A OD2 
4439  N N   . ALA A 625  ? 0.4374 0.5449 0.3145 0.0573  -0.0310 -0.0706 623  ALA A N   
4440  C CA  . ALA A 625  ? 0.4671 0.5751 0.3397 0.0562  -0.0278 -0.0617 623  ALA A CA  
4441  C C   . ALA A 625  ? 0.4206 0.5211 0.2947 0.0533  -0.0276 -0.0547 623  ALA A C   
4442  O O   . ALA A 625  ? 0.4545 0.5552 0.3250 0.0524  -0.0254 -0.0472 623  ALA A O   
4443  C CB  . ALA A 625  ? 0.4834 0.5886 0.3578 0.0554  -0.0247 -0.0608 623  ALA A CB  
4444  N N   . ALA A 626  ? 0.4149 0.5090 0.2944 0.0520  -0.0300 -0.0571 624  ALA A N   
4445  C CA  . ALA A 626  ? 0.3922 0.4789 0.2738 0.0494  -0.0298 -0.0510 624  ALA A CA  
4446  C C   . ALA A 626  ? 0.3832 0.4743 0.2588 0.0500  -0.0298 -0.0447 624  ALA A C   
4447  O O   . ALA A 626  ? 0.4138 0.5008 0.2887 0.0482  -0.0279 -0.0375 624  ALA A O   
4448  C CB  . ALA A 626  ? 0.4232 0.5042 0.3113 0.0481  -0.0325 -0.0552 624  ALA A CB  
4449  N N   . PRO A 627  ? 0.4370 0.5362 0.3083 0.0524  -0.0320 -0.0468 625  PRO A N   
4450  C CA  . PRO A 627  ? 0.4320 0.5350 0.2977 0.0529  -0.0321 -0.0401 625  PRO A CA  
4451  C C   . PRO A 627  ? 0.4444 0.5503 0.3052 0.0527  -0.0289 -0.0334 625  PRO A C   
4452  O O   . PRO A 627  ? 0.4464 0.5500 0.3054 0.0516  -0.0281 -0.0259 625  PRO A O   
4453  C CB  . PRO A 627  ? 0.4255 0.5382 0.2873 0.0559  -0.0349 -0.0449 625  PRO A CB  
4454  C CG  . PRO A 627  ? 0.4177 0.5291 0.2848 0.0563  -0.0369 -0.0541 625  PRO A CG  
4455  C CD  . PRO A 627  ? 0.4345 0.5400 0.3058 0.0548  -0.0346 -0.0553 625  PRO A CD  
4456  N N   . ASP A 628  ? 0.4019 0.5130 0.2606 0.0539  -0.0271 -0.0360 626  ASP A N   
4457  C CA  . ASP A 628  ? 0.3865 0.5011 0.2406 0.0536  -0.0240 -0.0297 626  ASP A CA  
4458  C C   . ASP A 628  ? 0.4469 0.5518 0.3046 0.0505  -0.0217 -0.0237 626  ASP A C   
4459  O O   . ASP A 628  ? 0.4317 0.5366 0.2866 0.0495  -0.0202 -0.0160 626  ASP A O   
4460  C CB  . ASP A 628  ? 0.4249 0.5467 0.2771 0.0555  -0.0226 -0.0347 626  ASP A CB  
4461  C CG  . ASP A 628  ? 0.5724 0.7042 0.4213 0.0588  -0.0250 -0.0415 626  ASP A CG  
4462  O OD1 . ASP A 628  ? 0.5969 0.7263 0.4494 0.0594  -0.0279 -0.0478 626  ASP A OD1 
4463  O OD2 . ASP A 628  ? 0.5209 0.6631 0.3634 0.0608  -0.0240 -0.0405 626  ASP A OD2 
4464  N N   . TRP A 629  ? 0.3735 0.4703 0.2377 0.0489  -0.0215 -0.0272 627  TRP A N   
4465  C CA  . TRP A 629  ? 0.3565 0.4445 0.2242 0.0461  -0.0194 -0.0219 627  TRP A CA  
4466  C C   . TRP A 629  ? 0.4037 0.4858 0.2729 0.0445  -0.0206 -0.0171 627  TRP A C   
4467  O O   . TRP A 629  ? 0.3762 0.4542 0.2453 0.0428  -0.0190 -0.0103 627  TRP A O   
4468  C CB  . TRP A 629  ? 0.3709 0.4523 0.2450 0.0449  -0.0189 -0.0267 627  TRP A CB  
4469  C CG  . TRP A 629  ? 0.3611 0.4339 0.2388 0.0421  -0.0168 -0.0217 627  TRP A CG  
4470  C CD1 . TRP A 629  ? 0.3584 0.4221 0.2419 0.0399  -0.0175 -0.0220 627  TRP A CD1 
4471  C CD2 . TRP A 629  ? 0.3896 0.4623 0.2652 0.0409  -0.0139 -0.0156 627  TRP A CD2 
4472  N NE1 . TRP A 629  ? 0.3866 0.4448 0.2716 0.0378  -0.0152 -0.0167 627  TRP A NE1 
4473  C CE2 . TRP A 629  ? 0.3480 0.4113 0.2284 0.0383  -0.0130 -0.0128 627  TRP A CE2 
4474  C CE3 . TRP A 629  ? 0.3689 0.4490 0.2391 0.0419  -0.0119 -0.0122 627  TRP A CE3 
4475  C CZ2 . TRP A 629  ? 0.3778 0.4385 0.2580 0.0366  -0.0104 -0.0070 627  TRP A CZ2 
4476  C CZ3 . TRP A 629  ? 0.3674 0.4449 0.2377 0.0400  -0.0093 -0.0062 627  TRP A CZ3 
4477  C CH2 . TRP A 629  ? 0.3619 0.4297 0.2373 0.0374  -0.0086 -0.0038 627  TRP A CH2 
4478  N N   . ALA A 630  ? 0.3772 0.4588 0.2480 0.0452  -0.0236 -0.0206 628  ALA A N   
4479  C CA  . ALA A 630  ? 0.3742 0.4510 0.2464 0.0441  -0.0250 -0.0164 628  ALA A CA  
4480  C C   . ALA A 630  ? 0.4139 0.4951 0.2803 0.0448  -0.0248 -0.0094 628  ALA A C   
4481  O O   . ALA A 630  ? 0.4062 0.4824 0.2737 0.0435  -0.0249 -0.0039 628  ALA A O   
4482  C CB  . ALA A 630  ? 0.4194 0.4965 0.2943 0.0449  -0.0283 -0.0219 628  ALA A CB  
4483  N N   . ALA A 631  ? 0.4026 0.4932 0.2631 0.0469  -0.0245 -0.0095 629  ALA A N   
4484  C CA  . ALA A 631  ? 0.4277 0.5232 0.2824 0.0476  -0.0244 -0.0026 629  ALA A CA  
4485  C C   . ALA A 631  ? 0.4301 0.5233 0.2837 0.0458  -0.0214 0.0046  629  ALA A C   
4486  O O   . ALA A 631  ? 0.4560 0.5509 0.3061 0.0457  -0.0214 0.0116  629  ALA A O   
4487  C CB  . ALA A 631  ? 0.4846 0.5919 0.3330 0.0505  -0.0252 -0.0051 629  ALA A CB  
4488  N N   . VAL A 632  ? 0.3981 0.4875 0.2548 0.0443  -0.0190 0.0033  630  VAL A N   
4489  C CA  . VAL A 632  ? 0.3814 0.4680 0.2378 0.0423  -0.0162 0.0102  630  VAL A CA  
4490  C C   . VAL A 632  ? 0.4210 0.4983 0.2811 0.0403  -0.0169 0.0150  630  VAL A C   
4491  O O   . VAL A 632  ? 0.3931 0.4635 0.2585 0.0395  -0.0179 0.0116  630  VAL A O   
4492  C CB  . VAL A 632  ? 0.3507 0.4356 0.2099 0.0414  -0.0137 0.0072  630  VAL A CB  
4493  C CG1 . VAL A 632  ? 0.3491 0.4303 0.2089 0.0391  -0.0110 0.0142  630  VAL A CG1 
4494  C CG2 . VAL A 632  ? 0.3869 0.4820 0.2422 0.0437  -0.0130 0.0026  630  VAL A CG2 
4495  N N   . PRO A 633  ? 0.3878 0.4650 0.2455 0.0396  -0.0166 0.0227  631  PRO A N   
4496  C CA  . PRO A 633  ? 0.3457 0.4144 0.2070 0.0381  -0.0176 0.0270  631  PRO A CA  
4497  C C   . PRO A 633  ? 0.3675 0.4275 0.2347 0.0358  -0.0161 0.0258  631  PRO A C   
4498  O O   . PRO A 633  ? 0.3799 0.4400 0.2476 0.0348  -0.0135 0.0257  631  PRO A O   
4499  C CB  . PRO A 633  ? 0.3625 0.4332 0.2202 0.0376  -0.0169 0.0356  631  PRO A CB  
4500  C CG  . PRO A 633  ? 0.4090 0.4909 0.2601 0.0395  -0.0167 0.0355  631  PRO A CG  
4501  C CD  . PRO A 633  ? 0.3786 0.4640 0.2303 0.0403  -0.0154 0.0279  631  PRO A CD  
4502  N N   . PRO A 634  ? 0.3607 0.4133 0.2325 0.0351  -0.0176 0.0249  632  PRO A N   
4503  C CA  . PRO A 634  ? 0.3295 0.3743 0.2069 0.0330  -0.0162 0.0235  632  PRO A CA  
4504  C C   . PRO A 634  ? 0.3608 0.4028 0.2385 0.0311  -0.0137 0.0288  632  PRO A C   
4505  O O   . PRO A 634  ? 0.3344 0.3734 0.2149 0.0298  -0.0118 0.0268  632  PRO A O   
4506  C CB  . PRO A 634  ? 0.3684 0.4072 0.2496 0.0327  -0.0184 0.0236  632  PRO A CB  
4507  C CG  . PRO A 634  ? 0.4400 0.4842 0.3185 0.0349  -0.0211 0.0214  632  PRO A CG  
4508  C CD  . PRO A 634  ? 0.3738 0.4257 0.2460 0.0362  -0.0206 0.0247  632  PRO A CD  
4509  N N   . SER A 635  ? 0.3602 0.4031 0.2353 0.0308  -0.0137 0.0356  633  SER A N   
4510  C CA  . SER A 635  ? 0.3848 0.4250 0.2607 0.0288  -0.0114 0.0406  633  SER A CA  
4511  C C   . SER A 635  ? 0.3881 0.4342 0.2615 0.0287  -0.0088 0.0396  633  SER A C   
4512  O O   . SER A 635  ? 0.3510 0.3942 0.2267 0.0269  -0.0066 0.0409  633  SER A O   
4513  C CB  . SER A 635  ? 0.4096 0.4496 0.2835 0.0284  -0.0122 0.0483  633  SER A CB  
4514  O OG  . SER A 635  ? 0.5067 0.5554 0.3748 0.0299  -0.0125 0.0504  633  SER A OG  
4515  N N   . GLU A 636  ? 0.3615 0.4160 0.2305 0.0307  -0.0090 0.0370  634  GLU A N   
4516  C CA  . GLU A 636  ? 0.3881 0.4491 0.2549 0.0310  -0.0066 0.0353  634  GLU A CA  
4517  C C   . GLU A 636  ? 0.3710 0.4297 0.2415 0.0311  -0.0060 0.0280  634  GLU A C   
4518  O O   . GLU A 636  ? 0.3902 0.4497 0.2615 0.0304  -0.0037 0.0273  634  GLU A O   
4519  C CB  . GLU A 636  ? 0.3903 0.4618 0.2509 0.0334  -0.0072 0.0349  634  GLU A CB  
4520  C CG  . GLU A 636  ? 0.5189 0.5944 0.3754 0.0330  -0.0070 0.0430  634  GLU A CG  
4521  C CD  . GLU A 636  ? 0.6138 0.6908 0.4700 0.0311  -0.0040 0.0482  634  GLU A CD  
4522  O OE1 . GLU A 636  ? 0.5758 0.6522 0.4343 0.0304  -0.0019 0.0449  634  GLU A OE1 
4523  O OE2 . GLU A 636  ? 0.7060 0.7849 0.5597 0.0302  -0.0038 0.0556  634  GLU A OE2 
4524  N N   . ARG A 637  ? 0.3423 0.3981 0.2151 0.0320  -0.0082 0.0228  635  ARG A N   
4525  C CA  . ARG A 637  ? 0.3350 0.3869 0.2123 0.0316  -0.0078 0.0167  635  ARG A CA  
4526  C C   . ARG A 637  ? 0.3256 0.3696 0.2073 0.0291  -0.0062 0.0193  635  ARG A C   
4527  O O   . ARG A 637  ? 0.3184 0.3613 0.2022 0.0285  -0.0045 0.0168  635  ARG A O   
4528  C CB  . ARG A 637  ? 0.3244 0.3739 0.2040 0.0325  -0.0105 0.0117  635  ARG A CB  
4529  C CG  . ARG A 637  ? 0.3294 0.3867 0.2047 0.0350  -0.0124 0.0089  635  ARG A CG  
4530  C CD  . ARG A 637  ? 0.3605 0.4163 0.2389 0.0358  -0.0149 0.0023  635  ARG A CD  
4531  N NE  . ARG A 637  ? 0.3736 0.4224 0.2559 0.0346  -0.0163 0.0036  635  ARG A NE  
4532  C CZ  . ARG A 637  ? 0.4053 0.4549 0.2868 0.0355  -0.0188 0.0040  635  ARG A CZ  
4533  N NH1 . ARG A 637  ? 0.3974 0.4544 0.2742 0.0376  -0.0202 0.0035  635  ARG A NH1 
4534  N NH2 . ARG A 637  ? 0.3555 0.3987 0.2411 0.0343  -0.0198 0.0048  635  ARG A NH2 
4535  N N   . ALA A 638  ? 0.3201 0.3588 0.2031 0.0278  -0.0068 0.0243  636  ALA A N   
4536  C CA  . ALA A 638  ? 0.3159 0.3475 0.2030 0.0254  -0.0054 0.0268  636  ALA A CA  
4537  C C   . ALA A 638  ? 0.3400 0.3740 0.2257 0.0244  -0.0028 0.0304  636  ALA A C   
4538  O O   . ALA A 638  ? 0.3136 0.3439 0.2026 0.0230  -0.0012 0.0300  636  ALA A O   
4539  C CB  . ALA A 638  ? 0.3156 0.3416 0.2043 0.0245  -0.0068 0.0311  636  ALA A CB  
4540  N N   . ALA A 639  ? 0.3601 0.4007 0.2412 0.0251  -0.0023 0.0343  637  ALA A N   
4541  C CA  . ALA A 639  ? 0.3651 0.4094 0.2448 0.0242  0.0003  0.0377  637  ALA A CA  
4542  C C   . ALA A 639  ? 0.3630 0.4106 0.2433 0.0248  0.0020  0.0323  637  ALA A C   
4543  O O   . ALA A 639  ? 0.3810 0.4276 0.2632 0.0235  0.0041  0.0336  637  ALA A O   
4544  C CB  . ALA A 639  ? 0.3827 0.4346 0.2570 0.0249  0.0004  0.0426  637  ALA A CB  
4545  N N   . CYS A 640  ? 0.3320 0.3833 0.2111 0.0270  0.0009  0.0262  638  CYS A N   
4546  C CA  . CYS A 640  ? 0.3278 0.3814 0.2084 0.0279  0.0020  0.0205  638  CYS A CA  
4547  C C   . CYS A 640  ? 0.3440 0.3891 0.2303 0.0261  0.0025  0.0189  638  CYS A C   
4548  O O   . CYS A 640  ? 0.3524 0.3978 0.2403 0.0256  0.0044  0.0183  638  CYS A O   
4549  C CB  . CYS A 640  ? 0.3321 0.3895 0.2114 0.0303  0.0002  0.0137  638  CYS A CB  
4550  S SG  . CYS A 640  ? 0.3850 0.4541 0.2573 0.0329  -0.0004 0.0140  638  CYS A SG  
4551  N N   . LEU A 641  ? 0.3378 0.3757 0.2271 0.0253  0.0007  0.0183  639  LEU A N   
4552  C CA  . LEU A 641  ? 0.3068 0.3371 0.2013 0.0237  0.0011  0.0172  639  LEU A CA  
4553  C C   . LEU A 641  ? 0.3240 0.3517 0.2197 0.0216  0.0031  0.0225  639  LEU A C   
4554  O O   . LEU A 641  ? 0.3024 0.3278 0.2010 0.0207  0.0045  0.0213  639  LEU A O   
4555  C CB  . LEU A 641  ? 0.3197 0.3438 0.2171 0.0231  -0.0010 0.0163  639  LEU A CB  
4556  C CG  . LEU A 641  ? 0.3034 0.3267 0.2027 0.0241  -0.0028 0.0100  639  LEU A CG  
4557  C CD1 . LEU A 641  ? 0.3389 0.3695 0.2343 0.0265  -0.0039 0.0071  639  LEU A CD1 
4558  C CD2 . LEU A 641  ? 0.3051 0.3223 0.2075 0.0231  -0.0045 0.0103  639  LEU A CD2 
4559  N N   . ASP A 642  ? 0.3076 0.3356 0.2013 0.0208  0.0031  0.0283  640  ASP A N   
4560  C CA  . ASP A 642  ? 0.3338 0.3592 0.2289 0.0187  0.0048  0.0334  640  ASP A CA  
4561  C C   . ASP A 642  ? 0.3185 0.3497 0.2123 0.0187  0.0072  0.0338  640  ASP A C   
4562  O O   . ASP A 642  ? 0.3051 0.3338 0.2018 0.0172  0.0088  0.0350  640  ASP A O   
4563  C CB  . ASP A 642  ? 0.3340 0.3586 0.2275 0.0179  0.0039  0.0397  640  ASP A CB  
4564  C CG  . ASP A 642  ? 0.3765 0.3933 0.2731 0.0172  0.0020  0.0401  640  ASP A CG  
4565  O OD1 . ASP A 642  ? 0.3431 0.3548 0.2437 0.0165  0.0020  0.0369  640  ASP A OD1 
4566  O OD2 . ASP A 642  ? 0.3666 0.3827 0.2620 0.0173  0.0005  0.0438  640  ASP A OD2 
4567  N N   . ARG A 643  ? 0.3118 0.3514 0.2014 0.0205  0.0076  0.0327  641  ARG A N   
4568  C CA  . ARG A 643  ? 0.3130 0.3593 0.2015 0.0209  0.0099  0.0324  641  ARG A CA  
4569  C C   . ARG A 643  ? 0.3379 0.3822 0.2298 0.0214  0.0105  0.0265  641  ARG A C   
4570  O O   . ARG A 643  ? 0.3706 0.4159 0.2642 0.0206  0.0124  0.0271  641  ARG A O   
4571  C CB  . ARG A 643  ? 0.3943 0.4506 0.2773 0.0230  0.0101  0.0319  641  ARG A CB  
4572  C CG  . ARG A 643  ? 0.3723 0.4323 0.2517 0.0221  0.0105  0.0392  641  ARG A CG  
4573  C CD  . ARG A 643  ? 0.3805 0.4518 0.2542 0.0241  0.0111  0.0390  641  ARG A CD  
4574  N NE  . ARG A 643  ? 0.3524 0.4258 0.2240 0.0266  0.0089  0.0338  641  ARG A NE  
4575  C CZ  . ARG A 643  ? 0.3970 0.4714 0.2656 0.0273  0.0069  0.0360  641  ARG A CZ  
4576  N NH1 . ARG A 643  ? 0.3502 0.4231 0.2176 0.0257  0.0067  0.0433  641  ARG A NH1 
4577  N NH2 . ARG A 643  ? 0.3722 0.4489 0.2391 0.0296  0.0049  0.0306  641  ARG A NH2 
4578  N N   . ALA A 644  ? 0.3257 0.3672 0.2191 0.0227  0.0086  0.0210  642  ALA A N   
4579  C CA  . ALA A 644  ? 0.3177 0.3565 0.2148 0.0231  0.0088  0.0157  642  ALA A CA  
4580  C C   . ALA A 644  ? 0.3001 0.3316 0.2017 0.0207  0.0096  0.0179  642  ALA A C   
4581  O O   . ALA A 644  ? 0.3041 0.3354 0.2081 0.0206  0.0109  0.0162  642  ALA A O   
4582  C CB  . ALA A 644  ? 0.3243 0.3607 0.2227 0.0244  0.0064  0.0101  642  ALA A CB  
4583  N N   . ALA A 645  ? 0.3348 0.3603 0.2375 0.0191  0.0087  0.0215  643  ALA A N   
4584  C CA  . ALA A 645  ? 0.3152 0.3341 0.2219 0.0169  0.0093  0.0236  643  ALA A CA  
4585  C C   . ALA A 645  ? 0.3342 0.3556 0.2409 0.0157  0.0116  0.0273  643  ALA A C   
4586  O O   . ALA A 645  ? 0.3392 0.3577 0.2492 0.0147  0.0126  0.0267  643  ALA A O   
4587  C CB  . ALA A 645  ? 0.3232 0.3364 0.2306 0.0156  0.0079  0.0270  643  ALA A CB  
4588  N N   . GLU A 646  ? 0.3194 0.3463 0.2226 0.0157  0.0125  0.0313  644  GLU A N   
4589  C CA  . GLU A 646  ? 0.3765 0.4069 0.2797 0.0145  0.0147  0.0350  644  GLU A CA  
4590  C C   . GLU A 646  ? 0.3696 0.4051 0.2734 0.0158  0.0162  0.0309  644  GLU A C   
4591  O O   . GLU A 646  ? 0.3615 0.3964 0.2679 0.0147  0.0178  0.0318  644  GLU A O   
4592  C CB  . GLU A 646  ? 0.3670 0.4033 0.2662 0.0143  0.0152  0.0401  644  GLU A CB  
4593  C CG  . GLU A 646  ? 0.4554 0.4867 0.3544 0.0131  0.0136  0.0446  644  GLU A CG  
4594  C CD  . GLU A 646  ? 0.4840 0.5085 0.3871 0.0105  0.0139  0.0480  644  GLU A CD  
4595  O OE1 . GLU A 646  ? 0.6002 0.6264 0.5048 0.0093  0.0158  0.0496  644  GLU A OE1 
4596  O OE2 . GLU A 646  ? 0.5522 0.5699 0.4572 0.0098  0.0121  0.0487  644  GLU A OE2 
4597  N N   . LEU A 647  ? 0.3346 0.3751 0.2360 0.0183  0.0158  0.0263  645  LEU A N   
4598  C CA  . LEU A 647  ? 0.3431 0.3882 0.2453 0.0200  0.0169  0.0217  645  LEU A CA  
4599  C C   . LEU A 647  ? 0.3493 0.3876 0.2566 0.0196  0.0164  0.0183  645  LEU A C   
4600  O O   . LEU A 647  ? 0.3713 0.4109 0.2808 0.0195  0.0178  0.0174  645  LEU A O   
4601  C CB  . LEU A 647  ? 0.3148 0.3662 0.2137 0.0229  0.0160  0.0168  645  LEU A CB  
4602  C CG  . LEU A 647  ? 0.3586 0.4189 0.2521 0.0236  0.0167  0.0198  645  LEU A CG  
4603  C CD1 . LEU A 647  ? 0.3626 0.4282 0.2531 0.0266  0.0153  0.0144  645  LEU A CD1 
4604  C CD2 . LEU A 647  ? 0.4072 0.4750 0.2997 0.0233  0.0195  0.0225  645  LEU A CD2 
4605  N N   . MET A 648  ? 0.3236 0.3547 0.2328 0.0192  0.0144  0.0166  646  MET A N   
4606  C CA  . MET A 648  ? 0.3629 0.3876 0.2767 0.0187  0.0139  0.0139  646  MET A CA  
4607  C C   . MET A 648  ? 0.3238 0.3449 0.2403 0.0164  0.0152  0.0180  646  MET A C   
4608  O O   . MET A 648  ? 0.3103 0.3299 0.2298 0.0162  0.0159  0.0163  646  MET A O   
4609  C CB  . MET A 648  ? 0.3258 0.3441 0.2412 0.0185  0.0116  0.0118  646  MET A CB  
4610  C CG  . MET A 648  ? 0.3833 0.4041 0.2978 0.0207  0.0101  0.0064  646  MET A CG  
4611  S SD  . MET A 648  ? 0.3846 0.3975 0.3029 0.0202  0.0077  0.0031  646  MET A SD  
4612  C CE  . MET A 648  ? 0.3622 0.3802 0.2783 0.0229  0.0060  -0.0024 646  MET A CE  
4613  N N   . GLN A 649  ? 0.3425 0.3620 0.2578 0.0145  0.0154  0.0232  647  GLN A N   
4614  C CA  . GLN A 649  ? 0.3122 0.3282 0.2302 0.0123  0.0164  0.0271  647  GLN A CA  
4615  C C   . GLN A 649  ? 0.3393 0.3611 0.2575 0.0122  0.0187  0.0281  647  GLN A C   
4616  O O   . GLN A 649  ? 0.3240 0.3436 0.2455 0.0113  0.0194  0.0281  647  GLN A O   
4617  C CB  . GLN A 649  ? 0.3406 0.3543 0.2575 0.0106  0.0160  0.0323  647  GLN A CB  
4618  C CG  . GLN A 649  ? 0.3216 0.3315 0.2415 0.0082  0.0167  0.0361  647  GLN A CG  
4619  C CD  . GLN A 649  ? 0.3334 0.3357 0.2568 0.0074  0.0155  0.0344  647  GLN A CD  
4620  O OE1 . GLN A 649  ? 0.3220 0.3199 0.2456 0.0070  0.0140  0.0351  647  GLN A OE1 
4621  N NE2 . GLN A 649  ? 0.3671 0.3683 0.2934 0.0073  0.0161  0.0321  647  GLN A NE2 
4622  N N   . ALA A 650  ? 0.3487 0.3783 0.2633 0.0132  0.0197  0.0291  648  ALA A N   
4623  C CA  . ALA A 650  ? 0.4086 0.4450 0.3232 0.0133  0.0220  0.0299  648  ALA A CA  
4624  C C   . ALA A 650  ? 0.3929 0.4307 0.3098 0.0152  0.0222  0.0243  648  ALA A C   
4625  O O   . ALA A 650  ? 0.4005 0.4401 0.3198 0.0148  0.0237  0.0246  648  ALA A O   
4626  C CB  . ALA A 650  ? 0.3780 0.4233 0.2880 0.0142  0.0229  0.0318  648  ALA A CB  
4627  N N   . ARG A 651  ? 0.3886 0.4254 0.3052 0.0173  0.0207  0.0191  649  ARG A N   
4628  C CA  . ARG A 651  ? 0.3527 0.3905 0.2716 0.0193  0.0205  0.0134  649  ARG A CA  
4629  C C   . ARG A 651  ? 0.3512 0.3803 0.2746 0.0185  0.0193  0.0119  649  ARG A C   
4630  O O   . ARG A 651  ? 0.3614 0.3898 0.2873 0.0201  0.0186  0.0071  649  ARG A O   
4631  C CB  . ARG A 651  ? 0.3920 0.4333 0.3085 0.0221  0.0192  0.0084  649  ARG A CB  
4632  C CG  . ARG A 651  ? 0.4650 0.5109 0.3828 0.0247  0.0195  0.0027  649  ARG A CG  
4633  C CD  . ARG A 651  ? 0.4551 0.5089 0.3691 0.0274  0.0192  -0.0008 649  ARG A CD  
4634  N NE  . ARG A 651  ? 0.4589 0.5153 0.3749 0.0303  0.0186  -0.0075 649  ARG A NE  
4635  C CZ  . ARG A 651  ? 0.5074 0.5699 0.4244 0.0316  0.0203  -0.0090 649  ARG A CZ  
4636  N NH1 . ARG A 651  ? 0.4884 0.5552 0.4045 0.0301  0.0227  -0.0042 649  ARG A NH1 
4637  N NH2 . ARG A 651  ? 0.5632 0.6276 0.4824 0.0345  0.0193  -0.0156 649  ARG A NH2 
4638  N N   . MET A 652  ? 0.3463 0.3692 0.2711 0.0160  0.0190  0.0157  650  MET A N   
4639  C CA  . MET A 652  ? 0.3279 0.3430 0.2565 0.0152  0.0177  0.0143  650  MET A CA  
4640  C C   . MET A 652  ? 0.3407 0.3559 0.2729 0.0159  0.0182  0.0119  650  MET A C   
4641  O O   . MET A 652  ? 0.3351 0.3467 0.2698 0.0169  0.0168  0.0081  650  MET A O   
4642  C CB  . MET A 652  ? 0.3351 0.3446 0.2647 0.0126  0.0175  0.0188  650  MET A CB  
4643  C CG  . MET A 652  ? 0.3371 0.3393 0.2703 0.0117  0.0163  0.0175  650  MET A CG  
4644  S SD  . MET A 652  ? 0.3846 0.3808 0.3190 0.0090  0.0159  0.0221  650  MET A SD  
4645  C CE  . MET A 652  ? 0.3440 0.3383 0.2758 0.0092  0.0142  0.0219  650  MET A CE  
4646  N N   . PRO A 653  ? 0.3292 0.3482 0.2620 0.0154  0.0201  0.0139  651  PRO A N   
4647  C CA  . PRO A 653  ? 0.3500 0.3687 0.2866 0.0162  0.0204  0.0115  651  PRO A CA  
4648  C C   . PRO A 653  ? 0.3071 0.3282 0.2444 0.0192  0.0195  0.0057  651  PRO A C   
4649  O O   . PRO A 653  ? 0.3010 0.3178 0.2418 0.0198  0.0183  0.0029  651  PRO A O   
4650  C CB  . PRO A 653  ? 0.3304 0.3549 0.2670 0.0154  0.0227  0.0146  651  PRO A CB  
4651  C CG  . PRO A 653  ? 0.3361 0.3595 0.2705 0.0129  0.0231  0.0200  651  PRO A CG  
4652  C CD  . PRO A 653  ? 0.3069 0.3303 0.2378 0.0139  0.0219  0.0188  651  PRO A CD  
4653  N N   . THR A 654  ? 0.3529 0.3807 0.2870 0.0210  0.0200  0.0037  652  THR A N   
4654  C CA  . THR A 654  ? 0.3351 0.3654 0.2699 0.0241  0.0189  -0.0024 652  THR A CA  
4655  C C   . THR A 654  ? 0.3556 0.3792 0.2916 0.0244  0.0163  -0.0054 652  THR A C   
4656  O O   . THR A 654  ? 0.3296 0.3506 0.2690 0.0259  0.0149  -0.0097 652  THR A O   
4657  C CB  . THR A 654  ? 0.3539 0.3935 0.2845 0.0260  0.0200  -0.0037 652  THR A CB  
4658  O OG1 . THR A 654  ? 0.3668 0.4131 0.2965 0.0254  0.0225  -0.0006 652  THR A OG1 
4659  C CG2 . THR A 654  ? 0.4057 0.4484 0.3373 0.0294  0.0188  -0.0106 652  THR A CG2 
4660  N N   . LEU A 655  ? 0.3337 0.3546 0.2673 0.0230  0.0156  -0.0031 653  LEU A N   
4661  C CA  . LEU A 655  ? 0.3390 0.3538 0.2739 0.0229  0.0132  -0.0055 653  LEU A CA  
4662  C C   . LEU A 655  ? 0.3195 0.3267 0.2590 0.0216  0.0123  -0.0053 653  LEU A C   
4663  O O   . LEU A 655  ? 0.3098 0.3132 0.2520 0.0223  0.0104  -0.0088 653  LEU A O   
4664  C CB  . LEU A 655  ? 0.3076 0.3210 0.2394 0.0215  0.0128  -0.0025 653  LEU A CB  
4665  C CG  . LEU A 655  ? 0.3312 0.3520 0.2582 0.0227  0.0134  -0.0023 653  LEU A CG  
4666  C CD1 . LEU A 655  ? 0.3818 0.4004 0.3062 0.0212  0.0128  0.0011  653  LEU A CD1 
4667  C CD2 . LEU A 655  ? 0.3937 0.4181 0.3203 0.0256  0.0122  -0.0084 653  LEU A CD2 
4668  N N   . LEU A 656  ? 0.2986 0.3038 0.2392 0.0196  0.0136  -0.0010 654  LEU A N   
4669  C CA  . LEU A 656  ? 0.3396 0.3386 0.2843 0.0184  0.0128  -0.0005 654  LEU A CA  
4670  C C   . LEU A 656  ? 0.3503 0.3495 0.2984 0.0205  0.0121  -0.0047 654  LEU A C   
4671  O O   . LEU A 656  ? 0.3500 0.3438 0.3015 0.0204  0.0104  -0.0064 654  LEU A O   
4672  C CB  . LEU A 656  ? 0.3347 0.3331 0.2797 0.0164  0.0144  0.0041  654  LEU A CB  
4673  C CG  . LEU A 656  ? 0.3758 0.3734 0.3184 0.0143  0.0151  0.0086  654  LEU A CG  
4674  C CD1 . LEU A 656  ? 0.2939 0.2906 0.2379 0.0124  0.0163  0.0124  654  LEU A CD1 
4675  C CD2 . LEU A 656  ? 0.3191 0.3111 0.2618 0.0133  0.0134  0.0086  654  LEU A CD2 
4676  N N   . GLY A 657  ? 0.3026 0.3081 0.2502 0.0223  0.0134  -0.0062 655  GLY A N   
4677  C CA  . GLY A 657  ? 0.3414 0.3476 0.2926 0.0245  0.0127  -0.0103 655  GLY A CA  
4678  C C   . GLY A 657  ? 0.3071 0.3112 0.2596 0.0263  0.0104  -0.0154 655  GLY A C   
4679  O O   . GLY A 657  ? 0.3139 0.3137 0.2707 0.0270  0.0088  -0.0178 655  GLY A O   
4680  N N   . LEU A 658  ? 0.2954 0.3026 0.2446 0.0270  0.0101  -0.0169 656  LEU A N   
4681  C CA  . LEU A 658  ? 0.3008 0.3061 0.2514 0.0286  0.0077  -0.0219 656  LEU A CA  
4682  C C   . LEU A 658  ? 0.2884 0.2853 0.2417 0.0266  0.0058  -0.0209 656  LEU A C   
4683  O O   . LEU A 658  ? 0.2998 0.2926 0.2571 0.0274  0.0037  -0.0242 656  LEU A O   
4684  C CB  . LEU A 658  ? 0.2883 0.2993 0.2343 0.0298  0.0078  -0.0236 656  LEU A CB  
4685  C CG  . LEU A 658  ? 0.3538 0.3647 0.3011 0.0320  0.0054  -0.0297 656  LEU A CG  
4686  C CD1 . LEU A 658  ? 0.3390 0.3505 0.2906 0.0346  0.0045  -0.0346 656  LEU A CD1 
4687  C CD2 . LEU A 658  ? 0.2946 0.3132 0.2369 0.0335  0.0059  -0.0312 656  LEU A CD2 
4688  N N   . ILE A 659  ? 0.2902 0.2844 0.2416 0.0239  0.0064  -0.0162 657  ILE A N   
4689  C CA  . ILE A 659  ? 0.2825 0.2696 0.2362 0.0219  0.0048  -0.0151 657  ILE A CA  
4690  C C   . ILE A 659  ? 0.2853 0.2674 0.2437 0.0212  0.0042  -0.0144 657  ILE A C   
4691  O O   . ILE A 659  ? 0.2780 0.2550 0.2399 0.0207  0.0022  -0.0157 657  ILE A O   
4692  C CB  . ILE A 659  ? 0.2766 0.2627 0.2273 0.0195  0.0057  -0.0104 657  ILE A CB  
4693  C CG1 . ILE A 659  ? 0.2948 0.2853 0.2412 0.0204  0.0057  -0.0114 657  ILE A CG1 
4694  C CG2 . ILE A 659  ? 0.2746 0.2540 0.2279 0.0174  0.0043  -0.0091 657  ILE A CG2 
4695  C CD1 . ILE A 659  ? 0.3499 0.3400 0.2934 0.0184  0.0065  -0.0069 657  ILE A CD1 
4696  N N   . ILE A 660  ? 0.3025 0.2862 0.2612 0.0211  0.0058  -0.0122 658  ILE A N   
4697  C CA  . ILE A 660  ? 0.2749 0.2542 0.2377 0.0205  0.0053  -0.0112 658  ILE A CA  
4698  C C   . ILE A 660  ? 0.3042 0.2820 0.2712 0.0227  0.0033  -0.0159 658  ILE A C   
4699  O O   . ILE A 660  ? 0.3063 0.2784 0.2772 0.0219  0.0015  -0.0159 658  ILE A O   
4700  C CB  . ILE A 660  ? 0.2955 0.2779 0.2577 0.0202  0.0074  -0.0084 658  ILE A CB  
4701  C CG1 . ILE A 660  ? 0.3280 0.3096 0.2875 0.0176  0.0087  -0.0034 658  ILE A CG1 
4702  C CG2 . ILE A 660  ? 0.3075 0.2872 0.2742 0.0207  0.0067  -0.0087 658  ILE A CG2 
4703  C CD1 . ILE A 660  ? 0.3438 0.3292 0.3023 0.0172  0.0109  -0.0006 658  ILE A CD1 
4704  N N   . ARG A 661  ? 0.2922 0.2753 0.2586 0.0255  0.0034  -0.0199 659  ARG A N   
4705  C CA  . ARG A 661  ? 0.3362 0.3182 0.3068 0.0280  0.0015  -0.0249 659  ARG A CA  
4706  C C   . ARG A 661  ? 0.3459 0.3252 0.3179 0.0285  -0.0010 -0.0288 659  ARG A C   
4707  O O   . ARG A 661  ? 0.3546 0.3292 0.3315 0.0291  -0.0034 -0.0311 659  ARG A O   
4708  C CB  . ARG A 661  ? 0.3104 0.2998 0.2801 0.0310  0.0027  -0.0280 659  ARG A CB  
4709  C CG  . ARG A 661  ? 0.3357 0.3267 0.3063 0.0307  0.0045  -0.0251 659  ARG A CG  
4710  C CD  . ARG A 661  ? 0.3193 0.3189 0.2886 0.0334  0.0062  -0.0276 659  ARG A CD  
4711  N NE  . ARG A 661  ? 0.3319 0.3328 0.3045 0.0369  0.0044  -0.0339 659  ARG A NE  
4712  C CZ  . ARG A 661  ? 0.3559 0.3631 0.3265 0.0394  0.0045  -0.0385 659  ARG A CZ  
4713  N NH1 . ARG A 661  ? 0.3599 0.3727 0.3251 0.0389  0.0063  -0.0371 659  ARG A NH1 
4714  N NH2 . ARG A 661  ? 0.3376 0.3456 0.3117 0.0427  0.0026  -0.0446 659  ARG A NH2 
4715  N N   . GLU A 662  ? 0.2874 0.2698 0.2555 0.0284  -0.0007 -0.0295 660  GLU A N   
4716  C CA  . GLU A 662  ? 0.3092 0.2894 0.2788 0.0290  -0.0032 -0.0335 660  GLU A CA  
4717  C C   . GLU A 662  ? 0.3159 0.2889 0.2880 0.0261  -0.0047 -0.0308 660  GLU A C   
4718  O O   . GLU A 662  ? 0.3002 0.2689 0.2765 0.0262  -0.0072 -0.0336 660  GLU A O   
4719  C CB  . GLU A 662  ? 0.3382 0.3243 0.3029 0.0300  -0.0027 -0.0353 660  GLU A CB  
4720  C CG  . GLU A 662  ? 0.3324 0.3166 0.2988 0.0306  -0.0054 -0.0397 660  GLU A CG  
4721  C CD  . GLU A 662  ? 0.3637 0.3542 0.3252 0.0318  -0.0051 -0.0417 660  GLU A CD  
4722  O OE1 . GLU A 662  ? 0.3600 0.3534 0.3168 0.0305  -0.0031 -0.0376 660  GLU A OE1 
4723  O OE2 . GLU A 662  ? 0.3499 0.3425 0.3124 0.0341  -0.0070 -0.0475 660  GLU A OE2 
4724  N N   . ALA A 663  ? 0.2893 0.2611 0.2590 0.0234  -0.0032 -0.0254 661  ALA A N   
4725  C CA  . ALA A 663  ? 0.3334 0.2997 0.3048 0.0207  -0.0043 -0.0230 661  ALA A CA  
4726  C C   . ALA A 663  ? 0.3175 0.2790 0.2919 0.0188  -0.0042 -0.0192 661  ALA A C   
4727  O O   . ALA A 663  ? 0.3135 0.2706 0.2898 0.0165  -0.0052 -0.0171 661  ALA A O   
4728  C CB  . ALA A 663  ? 0.3410 0.3093 0.3077 0.0191  -0.0030 -0.0202 661  ALA A CB  
4729  N N   . GLY A 664  ? 0.3284 0.2909 0.3034 0.0197  -0.0031 -0.0183 662  GLY A N   
4730  C CA  . GLY A 664  ? 0.2968 0.2553 0.2745 0.0181  -0.0031 -0.0147 662  GLY A CA  
4731  C C   . GLY A 664  ? 0.2898 0.2480 0.2647 0.0155  -0.0014 -0.0096 662  GLY A C   
4732  O O   . GLY A 664  ? 0.3337 0.2881 0.3108 0.0136  -0.0018 -0.0066 662  GLY A O   
4733  N N   . LYS A 665  ? 0.3111 0.2735 0.2814 0.0154  0.0005  -0.0084 663  LYS A N   
4734  C CA  . LYS A 665  ? 0.3467 0.3086 0.3146 0.0131  0.0019  -0.0039 663  LYS A CA  
4735  C C   . LYS A 665  ? 0.3341 0.2981 0.3012 0.0130  0.0037  -0.0014 663  LYS A C   
4736  O O   . LYS A 665  ? 0.2971 0.2646 0.2639 0.0149  0.0045  -0.0031 663  LYS A O   
4737  C CB  . LYS A 665  ? 0.3389 0.3036 0.3026 0.0128  0.0026  -0.0037 663  LYS A CB  
4738  C CG  . LYS A 665  ? 0.3460 0.3097 0.3104 0.0131  0.0008  -0.0067 663  LYS A CG  
4739  C CD  . LYS A 665  ? 0.4253 0.3912 0.3857 0.0125  0.0013  -0.0058 663  LYS A CD  
4740  C CE  . LYS A 665  ? 0.4108 0.3733 0.3725 0.0106  0.0000  -0.0050 663  LYS A CE  
4741  N NZ  . LYS A 665  ? 0.4078 0.3724 0.3657 0.0101  0.0007  -0.0034 663  LYS A NZ  
4742  N N   . SER A 666  ? 0.3153 0.2775 0.2820 0.0109  0.0044  0.0025  664  SER A N   
4743  C CA  . SER A 666  ? 0.3594 0.3235 0.3252 0.0105  0.0061  0.0051  664  SER A CA  
4744  C C   . SER A 666  ? 0.3424 0.3107 0.3042 0.0106  0.0078  0.0060  664  SER A C   
4745  O O   . SER A 666  ? 0.3225 0.2918 0.2819 0.0106  0.0077  0.0054  664  SER A O   
4746  C CB  . SER A 666  ? 0.3494 0.3103 0.3163 0.0083  0.0060  0.0085  664  SER A CB  
4747  O OG  . SER A 666  ? 0.3871 0.3473 0.3517 0.0067  0.0061  0.0100  664  SER A OG  
4748  N N   . ALA A 667  ? 0.2976 0.2686 0.2590 0.0105  0.0093  0.0078  665  ALA A N   
4749  C CA  . ALA A 667  ? 0.3619 0.3371 0.3199 0.0105  0.0109  0.0091  665  ALA A CA  
4750  C C   . ALA A 667  ? 0.3425 0.3161 0.2982 0.0086  0.0110  0.0117  665  ALA A C   
4751  O O   . ALA A 667  ? 0.3137 0.2896 0.2665 0.0089  0.0114  0.0117  665  ALA A O   
4752  C CB  . ALA A 667  ? 0.3140 0.2921 0.2725 0.0103  0.0124  0.0109  665  ALA A CB  
4753  N N   . LEU A 668  ? 0.3053 0.2753 0.2623 0.0069  0.0106  0.0138  666  LEU A N   
4754  C CA  A LEU A 668  ? 0.3297 0.2982 0.2848 0.0054  0.0105  0.0159  666  LEU A CA  
4755  C CA  B LEU A 668  ? 0.3297 0.2982 0.2849 0.0054  0.0105  0.0159  666  LEU A CA  
4756  C C   . LEU A 668  ? 0.3196 0.2873 0.2736 0.0058  0.0094  0.0141  666  LEU A C   
4757  O O   . LEU A 668  ? 0.3227 0.2914 0.2742 0.0055  0.0096  0.0150  666  LEU A O   
4758  C CB  A LEU A 668  ? 0.3515 0.3168 0.3084 0.0037  0.0102  0.0178  666  LEU A CB  
4759  C CB  B LEU A 668  ? 0.3515 0.3167 0.3085 0.0037  0.0101  0.0178  666  LEU A CB  
4760  C CG  A LEU A 668  ? 0.3688 0.3330 0.3242 0.0022  0.0102  0.0200  666  LEU A CG  
4761  C CG  B LEU A 668  ? 0.3501 0.3161 0.3073 0.0027  0.0111  0.0203  666  LEU A CG  
4762  C CD1 A LEU A 668  ? 0.3641 0.3309 0.3173 0.0022  0.0113  0.0216  666  LEU A CD1 
4763  C CD1 B LEU A 668  ? 0.3453 0.3087 0.3047 0.0015  0.0106  0.0214  666  LEU A CD1 
4764  C CD2 A LEU A 668  ? 0.3516 0.3138 0.3088 0.0008  0.0100  0.0216  666  LEU A CD2 
4765  C CD2 B LEU A 668  ? 0.3824 0.3492 0.3373 0.0018  0.0117  0.0222  666  LEU A CD2 
4766  N N   . ASN A 669  ? 0.3121 0.2780 0.2681 0.0064  0.0082  0.0117  667  ASN A N   
4767  C CA  . ASN A 669  ? 0.3167 0.2819 0.2721 0.0066  0.0070  0.0098  667  ASN A CA  
4768  C C   . ASN A 669  ? 0.3213 0.2902 0.2742 0.0084  0.0071  0.0076  667  ASN A C   
4769  O O   . ASN A 669  ? 0.2950 0.2645 0.2461 0.0085  0.0066  0.0071  667  ASN A O   
4770  C CB  . ASN A 669  ? 0.3258 0.2878 0.2846 0.0066  0.0054  0.0079  667  ASN A CB  
4771  C CG  . ASN A 669  ? 0.4192 0.3781 0.3799 0.0046  0.0050  0.0103  667  ASN A CG  
4772  O OD1 . ASN A 669  ? 0.4707 0.4294 0.4299 0.0034  0.0053  0.0121  667  ASN A OD1 
4773  N ND2 . ASN A 669  ? 0.3788 0.3354 0.3426 0.0043  0.0043  0.0102  667  ASN A ND2 
4774  N N   . ALA A 670  ? 0.2865 0.2584 0.2393 0.0099  0.0079  0.0064  668  ALA A N   
4775  C CA  . ALA A 670  ? 0.3103 0.2869 0.2604 0.0116  0.0083  0.0046  668  ALA A CA  
4776  C C   . ALA A 670  ? 0.3157 0.2948 0.2622 0.0109  0.0096  0.0077  668  ALA A C   
4777  O O   . ALA A 670  ? 0.2834 0.2651 0.2271 0.0116  0.0094  0.0071  668  ALA A O   
4778  C CB  . ALA A 670  ? 0.3119 0.2918 0.2629 0.0135  0.0090  0.0024  668  ALA A CB  
4779  N N   . ILE A 671  ? 0.2964 0.2748 0.2431 0.0095  0.0107  0.0111  669  ILE A N   
4780  C CA  . ILE A 671  ? 0.2660 0.2460 0.2099 0.0085  0.0116  0.0144  669  ILE A CA  
4781  C C   . ILE A 671  ? 0.2691 0.2467 0.2119 0.0079  0.0104  0.0148  669  ILE A C   
4782  O O   . ILE A 671  ? 0.3042 0.2841 0.2441 0.0083  0.0104  0.0155  669  ILE A O   
4783  C CB  . ILE A 671  ? 0.2970 0.2759 0.2421 0.0069  0.0126  0.0177  669  ILE A CB  
4784  C CG1 . ILE A 671  ? 0.3249 0.3073 0.2709 0.0077  0.0139  0.0174  669  ILE A CG1 
4785  C CG2 . ILE A 671  ? 0.2815 0.2607 0.2245 0.0057  0.0130  0.0211  669  ILE A CG2 
4786  C CD1 . ILE A 671  ? 0.2928 0.2739 0.2410 0.0062  0.0146  0.0198  669  ILE A CD1 
4787  N N   . ALA A 672  ? 0.2617 0.2351 0.2068 0.0069  0.0093  0.0144  670  ALA A N   
4788  C CA  . ALA A 672  ? 0.3262 0.2976 0.2706 0.0063  0.0082  0.0146  670  ALA A CA  
4789  C C   . ALA A 672  ? 0.2669 0.2402 0.2098 0.0078  0.0072  0.0118  670  ALA A C   
4790  O O   . ALA A 672  ? 0.3005 0.2746 0.2414 0.0079  0.0067  0.0123  670  ALA A O   
4791  C CB  . ALA A 672  ? 0.3404 0.3078 0.2878 0.0051  0.0074  0.0145  670  ALA A CB  
4792  N N   . GLU A 673  ? 0.3033 0.2775 0.2475 0.0090  0.0068  0.0086  671  GLU A N   
4793  C CA  . GLU A 673  ? 0.3004 0.2768 0.2435 0.0105  0.0057  0.0053  671  GLU A CA  
4794  C C   . GLU A 673  ? 0.3616 0.3430 0.3006 0.0117  0.0065  0.0059  671  GLU A C   
4795  O O   . GLU A 673  ? 0.2956 0.2784 0.2324 0.0123  0.0056  0.0052  671  GLU A O   
4796  C CB  . GLU A 673  ? 0.3226 0.2989 0.2681 0.0118  0.0051  0.0016  671  GLU A CB  
4797  C CG  . GLU A 673  ? 0.3527 0.3319 0.2971 0.0136  0.0039  -0.0023 671  GLU A CG  
4798  C CD  . GLU A 673  ? 0.3638 0.3397 0.3118 0.0136  0.0019  -0.0055 671  GLU A CD  
4799  O OE1 . GLU A 673  ? 0.4602 0.4323 0.4117 0.0126  0.0016  -0.0052 671  GLU A OE1 
4800  O OE2 . GLU A 673  ? 0.3453 0.3226 0.2927 0.0145  0.0005  -0.0083 671  GLU A OE2 
4801  N N   . VAL A 674  ? 0.2819 0.2663 0.2198 0.0121  0.0081  0.0073  672  VAL A N   
4802  C CA  . VAL A 674  ? 0.2852 0.2750 0.2192 0.0131  0.0090  0.0084  672  VAL A CA  
4803  C C   . VAL A 674  ? 0.2910 0.2797 0.2230 0.0118  0.0090  0.0123  672  VAL A C   
4804  O O   . VAL A 674  ? 0.2750 0.2664 0.2039 0.0126  0.0085  0.0126  672  VAL A O   
4805  C CB  . VAL A 674  ? 0.2864 0.2801 0.2199 0.0136  0.0108  0.0093  672  VAL A CB  
4806  C CG1 . VAL A 674  ? 0.2842 0.2839 0.2136 0.0143  0.0119  0.0112  672  VAL A CG1 
4807  C CG2 . VAL A 674  ? 0.2807 0.2759 0.2163 0.0153  0.0106  0.0049  672  VAL A CG2 
4808  N N   . ARG A 675  ? 0.2781 0.2628 0.2118 0.0100  0.0093  0.0152  673  ARG A N   
4809  C CA  . ARG A 675  ? 0.3164 0.2994 0.2489 0.0089  0.0089  0.0184  673  ARG A CA  
4810  C C   . ARG A 675  ? 0.3085 0.2902 0.2406 0.0094  0.0071  0.0167  673  ARG A C   
4811  O O   . ARG A 675  ? 0.3035 0.2863 0.2333 0.0096  0.0066  0.0184  673  ARG A O   
4812  C CB  . ARG A 675  ? 0.2901 0.2689 0.2253 0.0071  0.0092  0.0207  673  ARG A CB  
4813  C CG  . ARG A 675  ? 0.2915 0.2718 0.2269 0.0064  0.0108  0.0233  673  ARG A CG  
4814  C CD  . ARG A 675  ? 0.2981 0.2744 0.2358 0.0046  0.0109  0.0257  673  ARG A CD  
4815  N NE  . ARG A 675  ? 0.3419 0.3166 0.2786 0.0040  0.0101  0.0281  673  ARG A NE  
4816  C CZ  . ARG A 675  ? 0.3266 0.2975 0.2651 0.0028  0.0094  0.0292  673  ARG A CZ  
4817  N NH1 . ARG A 675  ? 0.2978 0.2664 0.2389 0.0020  0.0095  0.0282  673  ARG A NH1 
4818  N NH2 . ARG A 675  ? 0.2645 0.2342 0.2022 0.0025  0.0086  0.0312  673  ARG A NH2 
4819  N N   . GLU A 676  ? 0.2757 0.2551 0.2101 0.0094  0.0061  0.0136  674  GLU A N   
4820  C CA  . GLU A 676  ? 0.2790 0.2575 0.2136 0.0097  0.0044  0.0119  674  GLU A CA  
4821  C C   . GLU A 676  ? 0.2726 0.2554 0.2041 0.0114  0.0038  0.0101  674  GLU A C   
4822  O O   . GLU A 676  ? 0.2911 0.2744 0.2211 0.0117  0.0027  0.0105  674  GLU A O   
4823  C CB  . GLU A 676  ? 0.2676 0.2432 0.2058 0.0092  0.0035  0.0090  674  GLU A CB  
4824  C CG  . GLU A 676  ? 0.3628 0.3371 0.3018 0.0090  0.0018  0.0076  674  GLU A CG  
4825  C CD  . GLU A 676  ? 0.4519 0.4233 0.3948 0.0081  0.0010  0.0055  674  GLU A CD  
4826  O OE1 . GLU A 676  ? 0.5459 0.5155 0.4909 0.0074  0.0017  0.0058  674  GLU A OE1 
4827  O OE2 . GLU A 676  ? 0.5720 0.5430 0.5162 0.0079  -0.0004 0.0036  674  GLU A OE2 
4828  N N   . ALA A 677  ? 0.2797 0.2659 0.2102 0.0128  0.0044  0.0080  675  ALA A N   
4829  C CA  . ALA A 677  ? 0.2783 0.2696 0.2056 0.0146  0.0039  0.0062  675  ALA A CA  
4830  C C   . ALA A 677  ? 0.2799 0.2740 0.2034 0.0147  0.0045  0.0101  675  ALA A C   
4831  O O   . ALA A 677  ? 0.2820 0.2784 0.2031 0.0155  0.0034  0.0100  675  ALA A O   
4832  C CB  . ALA A 677  ? 0.2798 0.2748 0.2070 0.0162  0.0046  0.0032  675  ALA A CB  
4833  N N   . ILE A 678  ? 0.2893 0.2835 0.2125 0.0137  0.0062  0.0138  676  ILE A N   
4834  C CA  . ILE A 678  ? 0.3033 0.2997 0.2236 0.0134  0.0067  0.0182  676  ILE A CA  
4835  C C   . ILE A 678  ? 0.2806 0.2734 0.2011 0.0127  0.0053  0.0201  676  ILE A C   
4836  O O   . ILE A 678  ? 0.2833 0.2783 0.2010 0.0132  0.0046  0.0221  676  ILE A O   
4837  C CB  . ILE A 678  ? 0.2803 0.2766 0.2013 0.0121  0.0086  0.0217  676  ILE A CB  
4838  C CG1 . ILE A 678  ? 0.3255 0.3268 0.2457 0.0131  0.0101  0.0201  676  ILE A CG1 
4839  C CG2 . ILE A 678  ? 0.2826 0.2794 0.2017 0.0112  0.0088  0.0269  676  ILE A CG2 
4840  C CD1 . ILE A 678  ? 0.3171 0.3174 0.2396 0.0117  0.0118  0.0223  676  ILE A CD1 
4841  N N   . ASP A 679  ? 0.2844 0.2720 0.2083 0.0114  0.0048  0.0197  677  ASP A N   
4842  C CA  . ASP A 679  ? 0.3189 0.3032 0.2434 0.0109  0.0034  0.0210  677  ASP A CA  
4843  C C   . ASP A 679  ? 0.2864 0.2724 0.2096 0.0122  0.0016  0.0185  677  ASP A C   
4844  O O   . ASP A 679  ? 0.2799 0.2663 0.2015 0.0126  0.0006  0.0203  677  ASP A O   
4845  C CB  . ASP A 679  ? 0.2727 0.2520 0.2011 0.0094  0.0033  0.0206  677  ASP A CB  
4846  C CG  . ASP A 679  ? 0.3284 0.3058 0.2581 0.0080  0.0047  0.0235  677  ASP A CG  
4847  O OD1 . ASP A 679  ? 0.2990 0.2780 0.2270 0.0079  0.0054  0.0267  677  ASP A OD1 
4848  O OD2 . ASP A 679  ? 0.3355 0.3100 0.2682 0.0070  0.0050  0.0227  677  ASP A OD2 
4849  N N   . PHE A 680  ? 0.2780 0.2650 0.2022 0.0129  0.0011  0.0142  678  PHE A N   
4850  C CA  . PHE A 680  ? 0.2798 0.2689 0.2030 0.0142  -0.0006 0.0113  678  PHE A CA  
4851  C C   . PHE A 680  ? 0.2838 0.2780 0.2026 0.0157  -0.0008 0.0126  678  PHE A C   
4852  O O   . PHE A 680  ? 0.2855 0.2807 0.2028 0.0165  -0.0023 0.0128  678  PHE A O   
4853  C CB  . PHE A 680  ? 0.2797 0.2693 0.2047 0.0148  -0.0011 0.0065  678  PHE A CB  
4854  C CG  . PHE A 680  ? 0.2766 0.2619 0.2060 0.0135  -0.0019 0.0047  678  PHE A CG  
4855  C CD1 . PHE A 680  ? 0.2755 0.2588 0.2062 0.0129  -0.0031 0.0050  678  PHE A CD1 
4856  C CD2 . PHE A 680  ? 0.2752 0.2587 0.2075 0.0130  -0.0014 0.0027  678  PHE A CD2 
4857  C CE1 . PHE A 680  ? 0.3172 0.2973 0.2520 0.0116  -0.0037 0.0035  678  PHE A CE1 
4858  C CE2 . PHE A 680  ? 0.3148 0.2945 0.2511 0.0117  -0.0021 0.0014  678  PHE A CE2 
4859  C CZ  . PHE A 680  ? 0.3185 0.2967 0.2560 0.0109  -0.0032 0.0018  678  PHE A CZ  
4860  N N   . LEU A 681  ? 0.2890 0.2870 0.2055 0.0163  0.0006  0.0132  679  LEU A N   
4861  C CA  . LEU A 681  ? 0.2899 0.2937 0.2019 0.0178  0.0006  0.0145  679  LEU A CA  
4862  C C   . LEU A 681  ? 0.2911 0.2940 0.2015 0.0172  0.0003  0.0196  679  LEU A C   
4863  O O   . LEU A 681  ? 0.3123 0.3175 0.2201 0.0183  -0.0011 0.0202  679  LEU A O   
4864  C CB  . LEU A 681  ? 0.2971 0.3053 0.2073 0.0183  0.0026  0.0148  679  LEU A CB  
4865  C CG  . LEU A 681  ? 0.3077 0.3181 0.2190 0.0195  0.0027  0.0093  679  LEU A CG  
4866  C CD1 . LEU A 681  ? 0.3176 0.3307 0.2287 0.0195  0.0048  0.0099  679  LEU A CD1 
4867  C CD2 . LEU A 681  ? 0.2953 0.3113 0.2035 0.0217  0.0013  0.0060  679  LEU A CD2 
4868  N N   . ARG A 682  ? 0.2893 0.2884 0.2013 0.0155  0.0013  0.0233  680  ARG A N   
4869  C CA  . ARG A 682  ? 0.2908 0.2884 0.2019 0.0148  0.0009  0.0282  680  ARG A CA  
4870  C C   . ARG A 682  ? 0.2897 0.2836 0.2026 0.0149  -0.0012 0.0277  680  ARG A C   
4871  O O   . ARG A 682  ? 0.3085 0.3026 0.2197 0.0154  -0.0023 0.0306  680  ARG A O   
4872  C CB  . ARG A 682  ? 0.2892 0.2837 0.2023 0.0130  0.0024  0.0317  680  ARG A CB  
4873  C CG  . ARG A 682  ? 0.3278 0.3271 0.2388 0.0129  0.0044  0.0337  680  ARG A CG  
4874  C CD  . ARG A 682  ? 0.3481 0.3444 0.2617 0.0109  0.0058  0.0366  680  ARG A CD  
4875  N NE  . ARG A 682  ? 0.3253 0.3265 0.2372 0.0107  0.0078  0.0385  680  ARG A NE  
4876  C CZ  . ARG A 682  ? 0.3898 0.3899 0.3040 0.0092  0.0093  0.0400  680  ARG A CZ  
4877  N NH1 . ARG A 682  ? 0.3130 0.3072 0.2309 0.0079  0.0091  0.0398  680  ARG A NH1 
4878  N NH2 . ARG A 682  ? 0.3737 0.3793 0.2863 0.0091  0.0112  0.0416  680  ARG A NH2 
4879  N N   . TYR A 683  ? 0.2861 0.2766 0.2024 0.0144  -0.0016 0.0243  681  TYR A N   
4880  C CA  . TYR A 683  ? 0.2927 0.2803 0.2109 0.0145  -0.0034 0.0235  681  TYR A CA  
4881  C C   . TYR A 683  ? 0.2876 0.2787 0.2036 0.0162  -0.0052 0.0215  681  TYR A C   
4882  O O   . TYR A 683  ? 0.2894 0.2804 0.2045 0.0168  -0.0067 0.0233  681  TYR A O   
4883  C CB  . TYR A 683  ? 0.2807 0.2646 0.2029 0.0134  -0.0033 0.0206  681  TYR A CB  
4884  C CG  . TYR A 683  ? 0.2809 0.2626 0.2053 0.0134  -0.0050 0.0194  681  TYR A CG  
4885  C CD1 . TYR A 683  ? 0.2786 0.2571 0.2046 0.0128  -0.0054 0.0220  681  TYR A CD1 
4886  C CD2 . TYR A 683  ? 0.2792 0.2624 0.2044 0.0141  -0.0063 0.0156  681  TYR A CD2 
4887  C CE1 . TYR A 683  ? 0.2805 0.2576 0.2086 0.0130  -0.0069 0.0207  681  TYR A CE1 
4888  C CE2 . TYR A 683  ? 0.2780 0.2599 0.2055 0.0140  -0.0077 0.0146  681  TYR A CE2 
4889  C CZ  . TYR A 683  ? 0.2771 0.2561 0.2059 0.0136  -0.0080 0.0171  681  TYR A CZ  
4890  O OH  . TYR A 683  ? 0.3319 0.3102 0.2631 0.0137  -0.0094 0.0159  681  TYR A OH  
4891  N N   . TYR A 684  ? 0.2882 0.2826 0.2033 0.0171  -0.0052 0.0176  682  TYR A N   
4892  C CA  . TYR A 684  ? 0.2909 0.2890 0.2040 0.0188  -0.0070 0.0152  682  TYR A CA  
4893  C C   . TYR A 684  ? 0.3108 0.3134 0.2192 0.0200  -0.0073 0.0184  682  TYR A C   
4894  O O   . TYR A 684  ? 0.2980 0.3029 0.2047 0.0213  -0.0091 0.0182  682  TYR A O   
4895  C CB  . TYR A 684  ? 0.2914 0.2920 0.2050 0.0194  -0.0072 0.0100  682  TYR A CB  
4896  C CG  . TYR A 684  ? 0.2869 0.2834 0.2054 0.0182  -0.0073 0.0068  682  TYR A CG  
4897  C CD1 . TYR A 684  ? 0.2846 0.2776 0.2061 0.0173  -0.0084 0.0069  682  TYR A CD1 
4898  C CD2 . TYR A 684  ? 0.2859 0.2822 0.2061 0.0179  -0.0065 0.0038  682  TYR A CD2 
4899  C CE1 . TYR A 684  ? 0.2899 0.2796 0.2157 0.0160  -0.0085 0.0045  682  TYR A CE1 
4900  C CE2 . TYR A 684  ? 0.2829 0.2753 0.2075 0.0167  -0.0068 0.0014  682  TYR A CE2 
4901  C CZ  . TYR A 684  ? 0.2806 0.2700 0.2079 0.0156  -0.0077 0.0019  682  TYR A CZ  
4902  O OH  . TYR A 684  ? 0.2998 0.2859 0.2315 0.0141  -0.0079 0.0000  682  TYR A OH  
4903  N N   . ALA A 685  ? 0.2969 0.3011 0.2032 0.0196  -0.0055 0.0216  683  ALA A N   
4904  C CA  . ALA A 685  ? 0.3015 0.3098 0.2036 0.0205  -0.0056 0.0258  683  ALA A CA  
4905  C C   . ALA A 685  ? 0.3022 0.3069 0.2050 0.0201  -0.0070 0.0299  683  ALA A C   
4906  O O   . ALA A 685  ? 0.3057 0.3129 0.2061 0.0213  -0.0086 0.0315  683  ALA A O   
4907  C CB  . ALA A 685  ? 0.3288 0.3396 0.2292 0.0198  -0.0033 0.0287  683  ALA A CB  
4908  N N   . GLU A 686  ? 0.2991 0.2979 0.2055 0.0185  -0.0065 0.0316  684  GLU A N   
4909  C CA  . GLU A 686  ? 0.3621 0.3571 0.2698 0.0183  -0.0080 0.0349  684  GLU A CA  
4910  C C   . GLU A 686  ? 0.3046 0.2990 0.2136 0.0194  -0.0103 0.0320  684  GLU A C   
4911  O O   . GLU A 686  ? 0.3476 0.3421 0.2557 0.0204  -0.0121 0.0343  684  GLU A O   
4912  C CB  . GLU A 686  ? 0.3313 0.3205 0.2428 0.0164  -0.0070 0.0367  684  GLU A CB  
4913  C CG  . GLU A 686  ? 0.3408 0.3257 0.2546 0.0164  -0.0088 0.0390  684  GLU A CG  
4914  C CD  . GLU A 686  ? 0.4515 0.4369 0.3631 0.0167  -0.0098 0.0445  684  GLU A CD  
4915  O OE1 . GLU A 686  ? 0.4332 0.4227 0.3413 0.0168  -0.0088 0.0472  684  GLU A OE1 
4916  O OE2 . GLU A 686  ? 0.4954 0.4772 0.4089 0.0170  -0.0116 0.0463  684  GLU A OE2 
4917  N N   . GLN A 687  ? 0.2959 0.2898 0.2072 0.0193  -0.0103 0.0270  685  GLN A N   
4918  C CA  . GLN A 687  ? 0.3007 0.2946 0.2135 0.0203  -0.0124 0.0242  685  GLN A CA  
4919  C C   . GLN A 687  ? 0.3026 0.3018 0.2116 0.0222  -0.0140 0.0238  685  GLN A C   
4920  O O   . GLN A 687  ? 0.3087 0.3082 0.2178 0.0233  -0.0161 0.0240  685  GLN A O   
4921  C CB  . GLN A 687  ? 0.3469 0.3397 0.2630 0.0195  -0.0121 0.0192  685  GLN A CB  
4922  C CG  . GLN A 687  ? 0.2872 0.2748 0.2072 0.0177  -0.0110 0.0195  685  GLN A CG  
4923  C CD  . GLN A 687  ? 0.3271 0.3116 0.2492 0.0177  -0.0122 0.0217  685  GLN A CD  
4924  O OE1 . GLN A 687  ? 0.3217 0.3068 0.2449 0.0186  -0.0140 0.0202  685  GLN A OE1 
4925  N NE2 . GLN A 687  ? 0.3637 0.3450 0.2864 0.0168  -0.0112 0.0252  685  GLN A NE2 
4926  N N   . THR A 688  ? 0.3019 0.3058 0.2075 0.0228  -0.0131 0.0232  686  THR A N   
4927  C CA  . THR A 688  ? 0.3065 0.3163 0.2079 0.0248  -0.0145 0.0229  686  THR A CA  
4928  C C   . THR A 688  ? 0.3128 0.3231 0.2116 0.0254  -0.0154 0.0287  686  THR A C   
4929  O O   . THR A 688  ? 0.3135 0.3260 0.2108 0.0269  -0.0176 0.0289  686  THR A O   
4930  C CB  . THR A 688  ? 0.3204 0.3354 0.2187 0.0253  -0.0130 0.0211  686  THR A CB  
4931  O OG1 . THR A 688  ? 0.3124 0.3270 0.2134 0.0251  -0.0128 0.0153  686  THR A OG1 
4932  C CG2 . THR A 688  ? 0.3134 0.3354 0.2068 0.0274  -0.0142 0.0213  686  THR A CG2 
4933  N N   . ARG A 689  ? 0.3124 0.3207 0.2108 0.0241  -0.0138 0.0334  687  ARG A N   
4934  C CA  . ARG A 689  ? 0.3344 0.3424 0.2310 0.0244  -0.0148 0.0394  687  ARG A CA  
4935  C C   . ARG A 689  ? 0.3806 0.3837 0.2804 0.0247  -0.0170 0.0402  687  ARG A C   
4936  O O   . ARG A 689  ? 0.3527 0.3562 0.2511 0.0256  -0.0187 0.0441  687  ARG A O   
4937  C CB  . ARG A 689  ? 0.3568 0.3631 0.2533 0.0227  -0.0127 0.0441  687  ARG A CB  
4938  C CG  . ARG A 689  ? 0.3427 0.3553 0.2353 0.0227  -0.0106 0.0448  687  ARG A CG  
4939  C CD  . ARG A 689  ? 0.3607 0.3718 0.2534 0.0208  -0.0089 0.0503  687  ARG A CD  
4940  N NE  . ARG A 689  ? 0.3937 0.3989 0.2909 0.0190  -0.0076 0.0491  687  ARG A NE  
4941  C CZ  . ARG A 689  ? 0.4161 0.4221 0.3141 0.0181  -0.0054 0.0468  687  ARG A CZ  
4942  N NH1 . ARG A 689  ? 0.3872 0.3997 0.2819 0.0189  -0.0040 0.0452  687  ARG A NH1 
4943  N NH2 . ARG A 689  ? 0.3517 0.3522 0.2540 0.0166  -0.0045 0.0460  687  ARG A NH2 
4944  N N   . ARG A 690  ? 0.3151 0.3140 0.2194 0.0240  -0.0170 0.0366  688  ARG A N   
4945  C CA  . ARG A 690  ? 0.3396 0.3346 0.2472 0.0244  -0.0190 0.0367  688  ARG A CA  
4946  C C   . ARG A 690  ? 0.3542 0.3522 0.2614 0.0262  -0.0213 0.0334  688  ARG A C   
4947  O O   . ARG A 690  ? 0.3469 0.3430 0.2560 0.0272  -0.0234 0.0343  688  ARG A O   
4948  C CB  . ARG A 690  ? 0.3384 0.3282 0.2509 0.0229  -0.0180 0.0343  688  ARG A CB  
4949  C CG  . ARG A 690  ? 0.3828 0.3685 0.2966 0.0211  -0.0163 0.0376  688  ARG A CG  
4950  C CD  . ARG A 690  ? 0.4330 0.4153 0.3478 0.0213  -0.0177 0.0424  688  ARG A CD  
4951  N NE  . ARG A 690  ? 0.4226 0.4017 0.3410 0.0221  -0.0196 0.0408  688  ARG A NE  
4952  C CZ  . ARG A 690  ? 0.4464 0.4261 0.3645 0.0239  -0.0222 0.0419  688  ARG A CZ  
4953  N NH1 . ARG A 690  ? 0.4289 0.4119 0.3431 0.0250  -0.0232 0.0450  688  ARG A NH1 
4954  N NH2 . ARG A 690  ? 0.3944 0.3717 0.3163 0.0246  -0.0238 0.0398  688  ARG A NH2 
4955  N N   . THR A 691  ? 0.3099 0.3127 0.2151 0.0269  -0.0211 0.0294  689  THR A N   
4956  C CA  . THR A 691  ? 0.3188 0.3237 0.2254 0.0281  -0.0231 0.0251  689  THR A CA  
4957  C C   . THR A 691  ? 0.3870 0.3986 0.2896 0.0299  -0.0244 0.0235  689  THR A C   
4958  O O   . THR A 691  ? 0.3546 0.3681 0.2570 0.0314  -0.0268 0.0226  689  THR A O   
4959  C CB  . THR A 691  ? 0.3553 0.3585 0.2660 0.0268  -0.0223 0.0200  689  THR A CB  
4960  O OG1 . THR A 691  ? 0.3349 0.3397 0.2442 0.0260  -0.0203 0.0181  689  THR A OG1 
4961  C CG2 . THR A 691  ? 0.3170 0.3142 0.2322 0.0253  -0.0215 0.0208  689  THR A CG2 
4962  N N   . LEU A 692  ? 0.3458 0.3611 0.2450 0.0298  -0.0229 0.0226  690  LEU A N   
4963  C CA  . LEU A 692  ? 0.3242 0.3460 0.2206 0.0315  -0.0241 0.0189  690  LEU A CA  
4964  C C   . LEU A 692  ? 0.3964 0.4232 0.2876 0.0334  -0.0255 0.0226  690  LEU A C   
4965  O O   . LEU A 692  ? 0.3627 0.3898 0.2511 0.0331  -0.0245 0.0279  690  LEU A O   
4966  C CB  . LEU A 692  ? 0.3806 0.4048 0.2760 0.0310  -0.0222 0.0155  690  LEU A CB  
4967  C CG  . LEU A 692  ? 0.3618 0.3817 0.2624 0.0293  -0.0212 0.0113  690  LEU A CG  
4968  C CD1 . LEU A 692  ? 0.3836 0.4064 0.2833 0.0293  -0.0200 0.0073  690  LEU A CD1 
4969  C CD2 . LEU A 692  ? 0.3747 0.3934 0.2790 0.0295  -0.0233 0.0078  690  LEU A CD2 
4970  N N   . GLY A 693  ? 0.3724 0.4033 0.2627 0.0352  -0.0280 0.0199  691  GLY A N   
4971  C CA  . GLY A 693  ? 0.3963 0.4328 0.2815 0.0372  -0.0297 0.0228  691  GLY A CA  
4972  C C   . GLY A 693  ? 0.4831 0.5266 0.3661 0.0389  -0.0310 0.0174  691  GLY A C   
4973  O O   . GLY A 693  ? 0.4687 0.5123 0.3540 0.0383  -0.0304 0.0117  691  GLY A O   
4974  N N   . PRO A 694  ? 0.5297 0.5791 0.4083 0.0410  -0.0330 0.0190  692  PRO A N   
4975  C CA  . PRO A 694  ? 0.5253 0.5820 0.4013 0.0428  -0.0344 0.0136  692  PRO A CA  
4976  C C   . PRO A 694  ? 0.4932 0.5488 0.3739 0.0430  -0.0364 0.0075  692  PRO A C   
4977  O O   . PRO A 694  ? 0.5256 0.5854 0.4062 0.0436  -0.0370 0.0016  692  PRO A O   
4978  C CB  . PRO A 694  ? 0.5591 0.6220 0.4295 0.0450  -0.0362 0.0178  692  PRO A CB  
4979  C CG  . PRO A 694  ? 0.5831 0.6423 0.4523 0.0440  -0.0350 0.0258  692  PRO A CG  
4980  C CD  . PRO A 694  ? 0.5554 0.6054 0.4309 0.0419  -0.0340 0.0259  692  PRO A CD  
4981  N N   . GLY A 695  ? 0.4400 0.4905 0.3252 0.0424  -0.0376 0.0085  693  GLY A N   
4982  C CA  . GLY A 695  ? 0.4095 0.4594 0.2994 0.0423  -0.0394 0.0031  693  GLY A CA  
4983  C C   . GLY A 695  ? 0.4665 0.5124 0.3613 0.0402  -0.0378 -0.0014 693  GLY A C   
4984  O O   . GLY A 695  ? 0.4597 0.5056 0.3587 0.0399  -0.0392 -0.0062 693  GLY A O   
4985  N N   . HIS A 696  ? 0.3891 0.4316 0.2838 0.0386  -0.0349 0.0001  694  HIS A N   
4986  C CA  . HIS A 696  ? 0.4164 0.4549 0.3158 0.0365  -0.0333 -0.0036 694  HIS A CA  
4987  C C   . HIS A 696  ? 0.4538 0.4965 0.3508 0.0370  -0.0326 -0.0076 694  HIS A C   
4988  O O   . HIS A 696  ? 0.4534 0.4959 0.3483 0.0365  -0.0303 -0.0061 694  HIS A O   
4989  C CB  . HIS A 696  ? 0.4097 0.4417 0.3110 0.0346  -0.0308 0.0004  694  HIS A CB  
4990  C CG  . HIS A 696  ? 0.4065 0.4350 0.3092 0.0346  -0.0316 0.0048  694  HIS A CG  
4991  N ND1 . HIS A 696  ? 0.3614 0.3887 0.2612 0.0349  -0.0310 0.0108  694  HIS A ND1 
4992  C CD2 . HIS A 696  ? 0.3711 0.3974 0.2780 0.0344  -0.0331 0.0038  694  HIS A CD2 
4993  C CE1 . HIS A 696  ? 0.3916 0.4155 0.2938 0.0350  -0.0322 0.0132  694  HIS A CE1 
4994  N NE2 . HIS A 696  ? 0.4112 0.4347 0.3177 0.0348  -0.0334 0.0089  694  HIS A NE2 
4995  N N   . GLY A 697  ? 0.4165 0.4636 0.3141 0.0381  -0.0348 -0.0130 695  GLY A N   
4996  C CA  . GLY A 697  ? 0.4019 0.4538 0.2973 0.0391  -0.0348 -0.0175 695  GLY A CA  
4997  C C   . GLY A 697  ? 0.3443 0.3921 0.2439 0.0373  -0.0332 -0.0211 695  GLY A C   
4998  O O   . GLY A 697  ? 0.4121 0.4545 0.3173 0.0353  -0.0330 -0.0219 695  GLY A O   
4999  N N   . PRO A 698  ? 0.4011 0.4518 0.2982 0.0379  -0.0320 -0.0231 696  PRO A N   
5000  C CA  . PRO A 698  ? 0.3704 0.4173 0.2717 0.0364  -0.0307 -0.0267 696  PRO A CA  
5001  C C   . PRO A 698  ? 0.3649 0.4119 0.2711 0.0362  -0.0331 -0.0334 696  PRO A C   
5002  O O   . PRO A 698  ? 0.3787 0.4303 0.2841 0.0377  -0.0356 -0.0363 696  PRO A O   
5003  C CB  . PRO A 698  ? 0.3932 0.4447 0.2900 0.0379  -0.0292 -0.0274 696  PRO A CB  
5004  C CG  . PRO A 698  ? 0.4702 0.5260 0.3608 0.0392  -0.0287 -0.0218 696  PRO A CG  
5005  C CD  . PRO A 698  ? 0.4315 0.4888 0.3219 0.0400  -0.0314 -0.0214 696  PRO A CD  
5006  N N   . LEU A 699  ? 0.3432 0.3849 0.2546 0.0342  -0.0322 -0.0356 697  LEU A N   
5007  C CA  . LEU A 699  ? 0.3177 0.3589 0.2342 0.0337  -0.0343 -0.0419 697  LEU A CA  
5008  C C   . LEU A 699  ? 0.3377 0.3842 0.2522 0.0358  -0.0354 -0.0475 697  LEU A C   
5009  O O   . LEU A 699  ? 0.3522 0.4020 0.2685 0.0367  -0.0381 -0.0527 697  LEU A O   
5010  C CB  . LEU A 699  ? 0.3502 0.3842 0.2730 0.0309  -0.0331 -0.0420 697  LEU A CB  
5011  C CG  . LEU A 699  ? 0.3623 0.3911 0.2879 0.0287  -0.0320 -0.0374 697  LEU A CG  
5012  C CD1 . LEU A 699  ? 0.3413 0.3639 0.2716 0.0263  -0.0304 -0.0373 697  LEU A CD1 
5013  C CD2 . LEU A 699  ? 0.3963 0.4260 0.3250 0.0282  -0.0344 -0.0388 697  LEU A CD2 
5014  N N   . GLY A 700  ? 0.3231 0.3710 0.2343 0.0367  -0.0333 -0.0466 698  GLY A N   
5015  C CA  . GLY A 700  ? 0.3269 0.3793 0.2369 0.0387  -0.0340 -0.0523 698  GLY A CA  
5016  C C   . GLY A 700  ? 0.3368 0.3848 0.2496 0.0376  -0.0319 -0.0530 698  GLY A C   
5017  O O   . GLY A 700  ? 0.3395 0.3822 0.2534 0.0357  -0.0296 -0.0482 698  GLY A O   
5018  N N   . PRO A 701  ? 0.3310 0.3811 0.2452 0.0390  -0.0329 -0.0592 699  PRO A N   
5019  C CA  . PRO A 701  ? 0.3259 0.3720 0.2430 0.0383  -0.0312 -0.0602 699  PRO A CA  
5020  C C   . PRO A 701  ? 0.3249 0.3619 0.2485 0.0350  -0.0307 -0.0583 699  PRO A C   
5021  O O   . PRO A 701  ? 0.3202 0.3544 0.2489 0.0337  -0.0329 -0.0607 699  PRO A O   
5022  C CB  . PRO A 701  ? 0.3302 0.3798 0.2490 0.0404  -0.0333 -0.0683 699  PRO A CB  
5023  C CG  . PRO A 701  ? 0.3402 0.3985 0.2535 0.0430  -0.0351 -0.0704 699  PRO A CG  
5024  C CD  . PRO A 701  ? 0.3413 0.3982 0.2542 0.0415  -0.0356 -0.0658 699  PRO A CD  
5025  N N   . ILE A 702  ? 0.3178 0.3509 0.2413 0.0338  -0.0279 -0.0538 700  ILE A N   
5026  C CA  . ILE A 702  ? 0.3131 0.3382 0.2421 0.0308  -0.0271 -0.0513 700  ILE A CA  
5027  C C   . ILE A 702  ? 0.3129 0.3349 0.2451 0.0307  -0.0263 -0.0536 700  ILE A C   
5028  O O   . ILE A 702  ? 0.3140 0.3388 0.2428 0.0322  -0.0245 -0.0531 700  ILE A O   
5029  C CB  . ILE A 702  ? 0.3094 0.3321 0.2361 0.0293  -0.0248 -0.0439 700  ILE A CB  
5030  C CG1 . ILE A 702  ? 0.3098 0.3348 0.2344 0.0294  -0.0261 -0.0420 700  ILE A CG1 
5031  C CG2 . ILE A 702  ? 0.3049 0.3200 0.2368 0.0264  -0.0237 -0.0417 700  ILE A CG2 
5032  C CD1 . ILE A 702  ? 0.3631 0.3844 0.2875 0.0277  -0.0245 -0.0356 700  ILE A CD1 
5033  N N   . VAL A 703  ? 0.3118 0.3284 0.2506 0.0289  -0.0277 -0.0562 701  VAL A N   
5034  C CA  . VAL A 703  ? 0.3116 0.3242 0.2543 0.0286  -0.0272 -0.0580 701  VAL A CA  
5035  C C   . VAL A 703  ? 0.3067 0.3135 0.2509 0.0260  -0.0248 -0.0521 701  VAL A C   
5036  O O   . VAL A 703  ? 0.3037 0.3069 0.2506 0.0236  -0.0249 -0.0493 701  VAL A O   
5037  C CB  . VAL A 703  ? 0.3135 0.3231 0.2631 0.0279  -0.0302 -0.0637 701  VAL A CB  
5038  C CG1 . VAL A 703  ? 0.3133 0.3181 0.2672 0.0275  -0.0297 -0.0650 701  VAL A CG1 
5039  C CG2 . VAL A 703  ? 0.3187 0.3343 0.2668 0.0307  -0.0326 -0.0702 701  VAL A CG2 
5040  N N   . CYS A 704  ? 0.3060 0.3125 0.2484 0.0266  -0.0225 -0.0503 702  CYS A N   
5041  C CA  . CYS A 704  ? 0.3017 0.3034 0.2451 0.0245  -0.0202 -0.0449 702  CYS A CA  
5042  C C   . CYS A 704  ? 0.3017 0.2990 0.2500 0.0241  -0.0203 -0.0470 702  CYS A C   
5043  O O   . CYS A 704  ? 0.3040 0.3038 0.2514 0.0262  -0.0200 -0.0498 702  CYS A O   
5044  C CB  . CYS A 704  ? 0.3008 0.3058 0.2382 0.0254  -0.0175 -0.0404 702  CYS A CB  
5045  S SG  . CYS A 704  ? 0.3163 0.3256 0.2481 0.0258  -0.0175 -0.0369 702  CYS A SG  
5046  N N   . ILE A 705  ? 0.2992 0.2905 0.2529 0.0214  -0.0208 -0.0457 703  ILE A N   
5047  C CA  . ILE A 705  ? 0.2994 0.2858 0.2584 0.0207  -0.0213 -0.0472 703  ILE A CA  
5048  C C   . ILE A 705  ? 0.2951 0.2775 0.2545 0.0187  -0.0189 -0.0414 703  ILE A C   
5049  O O   . ILE A 705  ? 0.2921 0.2722 0.2524 0.0164  -0.0185 -0.0378 703  ILE A O   
5050  C CB  . ILE A 705  ? 0.3074 0.2901 0.2729 0.0192  -0.0242 -0.0504 703  ILE A CB  
5051  C CG1 . ILE A 705  ? 0.3297 0.3167 0.2950 0.0213  -0.0267 -0.0566 703  ILE A CG1 
5052  C CG2 . ILE A 705  ? 0.3311 0.3083 0.3024 0.0183  -0.0247 -0.0512 703  ILE A CG2 
5053  C CD1 . ILE A 705  ? 0.3784 0.3624 0.3502 0.0196  -0.0298 -0.0598 703  ILE A CD1 
5054  N N   . SER A 706  ? 0.2950 0.2771 0.2537 0.0196  -0.0174 -0.0409 704  SER A N   
5055  C CA  . SER A 706  ? 0.2912 0.2706 0.2492 0.0181  -0.0150 -0.0355 704  SER A CA  
5056  C C   . SER A 706  ? 0.2988 0.2731 0.2620 0.0171  -0.0153 -0.0357 704  SER A C   
5057  O O   . SER A 706  ? 0.3019 0.2753 0.2684 0.0184  -0.0170 -0.0402 704  SER A O   
5058  C CB  . SER A 706  ? 0.3011 0.2850 0.2534 0.0198  -0.0126 -0.0334 704  SER A CB  
5059  O OG  . SER A 706  ? 0.3287 0.3160 0.2802 0.0224  -0.0129 -0.0376 704  SER A OG  
5060  N N   . PRO A 707  ? 0.3006 0.2713 0.2648 0.0150  -0.0138 -0.0309 705  PRO A N   
5061  C CA  . PRO A 707  ? 0.3236 0.2893 0.2927 0.0139  -0.0141 -0.0304 705  PRO A CA  
5062  C C   . PRO A 707  ? 0.3141 0.2804 0.2820 0.0153  -0.0124 -0.0296 705  PRO A C   
5063  O O   . PRO A 707  ? 0.3068 0.2772 0.2698 0.0167  -0.0107 -0.0287 705  PRO A O   
5064  C CB  . PRO A 707  ? 0.3153 0.2779 0.2857 0.0108  -0.0134 -0.0255 705  PRO A CB  
5065  C CG  . PRO A 707  ? 0.2956 0.2617 0.2603 0.0111  -0.0114 -0.0225 705  PRO A CG  
5066  C CD  . PRO A 707  ? 0.3029 0.2739 0.2642 0.0134  -0.0121 -0.0259 705  PRO A CD  
5067  N N   . TRP A 708  ? 0.3223 0.2843 0.2948 0.0147  -0.0131 -0.0296 706  TRP A N   
5068  C CA  . TRP A 708  ? 0.3121 0.2743 0.2843 0.0161  -0.0118 -0.0293 706  TRP A CA  
5069  C C   . TRP A 708  ? 0.3039 0.2648 0.2746 0.0144  -0.0095 -0.0237 706  TRP A C   
5070  O O   . TRP A 708  ? 0.3063 0.2685 0.2759 0.0155  -0.0081 -0.0228 706  TRP A O   
5071  C CB  . TRP A 708  ? 0.3302 0.2884 0.3085 0.0166  -0.0139 -0.0323 706  TRP A CB  
5072  C CG  . TRP A 708  ? 0.3547 0.3072 0.3380 0.0138  -0.0154 -0.0303 706  TRP A CG  
5073  C CD1 . TRP A 708  ? 0.3826 0.3328 0.3698 0.0129  -0.0180 -0.0329 706  TRP A CD1 
5074  C CD2 . TRP A 708  ? 0.2933 0.2422 0.2781 0.0113  -0.0145 -0.0252 706  TRP A CD2 
5075  N NE1 . TRP A 708  ? 0.3788 0.3244 0.3701 0.0099  -0.0186 -0.0294 706  TRP A NE1 
5076  C CE2 . TRP A 708  ? 0.3408 0.2856 0.3305 0.0090  -0.0164 -0.0247 706  TRP A CE2 
5077  C CE3 . TRP A 708  ? 0.3473 0.2963 0.3300 0.0109  -0.0122 -0.0211 706  TRP A CE3 
5078  C CZ2 . TRP A 708  ? 0.3208 0.2621 0.3129 0.0062  -0.0160 -0.0200 706  TRP A CZ2 
5079  C CZ3 . TRP A 708  ? 0.3378 0.2832 0.3229 0.0083  -0.0120 -0.0168 706  TRP A CZ3 
5080  C CH2 . TRP A 708  ? 0.4007 0.3424 0.3903 0.0060  -0.0138 -0.0162 706  TRP A CH2 
5081  N N   . ASN A 709  ? 0.3112 0.2700 0.2821 0.0118  -0.0092 -0.0200 707  ASN A N   
5082  C CA  . ASN A 709  ? 0.3158 0.2733 0.2858 0.0102  -0.0073 -0.0150 707  ASN A CA  
5083  C C   . ASN A 709  ? 0.3516 0.3129 0.3162 0.0105  -0.0052 -0.0125 707  ASN A C   
5084  O O   . ASN A 709  ? 0.3294 0.2903 0.2929 0.0098  -0.0035 -0.0091 707  ASN A O   
5085  C CB  . ASN A 709  ? 0.3185 0.2725 0.2914 0.0073  -0.0080 -0.0123 707  ASN A CB  
5086  C CG  . ASN A 709  ? 0.3560 0.3116 0.3271 0.0064  -0.0083 -0.0121 707  ASN A CG  
5087  O OD1 . ASN A 709  ? 0.3904 0.3489 0.3595 0.0078  -0.0089 -0.0150 707  ASN A OD1 
5088  N ND2 . ASN A 709  ? 0.3450 0.2992 0.3169 0.0040  -0.0078 -0.0087 707  ASN A ND2 
5089  N N   . PHE A 710  ? 0.3065 0.2712 0.2678 0.0115  -0.0053 -0.0140 708  PHE A N   
5090  C CA  . PHE A 710  ? 0.3139 0.2826 0.2701 0.0122  -0.0035 -0.0120 708  PHE A CA  
5091  C C   . PHE A 710  ? 0.3457 0.3190 0.2993 0.0147  -0.0039 -0.0157 708  PHE A C   
5092  O O   . PHE A 710  ? 0.3105 0.2864 0.2615 0.0152  -0.0045 -0.0165 708  PHE A O   
5093  C CB  . PHE A 710  ? 0.3500 0.3185 0.3044 0.0106  -0.0032 -0.0090 708  PHE A CB  
5094  C CG  . PHE A 710  ? 0.3506 0.3156 0.3067 0.0084  -0.0025 -0.0053 708  PHE A CG  
5095  C CD1 . PHE A 710  ? 0.4205 0.3858 0.3749 0.0081  -0.0006 -0.0021 708  PHE A CD1 
5096  C CD2 . PHE A 710  ? 0.4520 0.4139 0.4117 0.0066  -0.0036 -0.0051 708  PHE A CD2 
5097  C CE1 . PHE A 710  ? 0.4341 0.3966 0.3901 0.0062  0.0000  0.0010  708  PHE A CE1 
5098  C CE2 . PHE A 710  ? 0.4590 0.4185 0.4201 0.0046  -0.0029 -0.0017 708  PHE A CE2 
5099  C CZ  . PHE A 710  ? 0.4646 0.4244 0.4237 0.0045  -0.0011 0.0011  708  PHE A CZ  
5100  N N   . PRO A 711  ? 0.3330 0.3078 0.2872 0.0165  -0.0037 -0.0181 709  PRO A N   
5101  C CA  . PRO A 711  ? 0.3239 0.3033 0.2767 0.0191  -0.0045 -0.0226 709  PRO A CA  
5102  C C   . PRO A 711  ? 0.3079 0.2934 0.2550 0.0204  -0.0029 -0.0214 709  PRO A C   
5103  O O   . PRO A 711  ? 0.3008 0.2910 0.2458 0.0226  -0.0035 -0.0251 709  PRO A O   
5104  C CB  . PRO A 711  ? 0.3341 0.3128 0.2899 0.0206  -0.0047 -0.0253 709  PRO A CB  
5105  C CG  . PRO A 711  ? 0.2925 0.2693 0.2486 0.0192  -0.0028 -0.0208 709  PRO A CG  
5106  C CD  . PRO A 711  ? 0.3264 0.2990 0.2831 0.0164  -0.0029 -0.0170 709  PRO A CD  
5107  N N   . LEU A 712  ? 0.3256 0.3114 0.2701 0.0191  -0.0009 -0.0165 710  LEU A N   
5108  C CA  . LEU A 712  ? 0.2827 0.2736 0.2219 0.0198  0.0003  -0.0145 710  LEU A CA  
5109  C C   . LEU A 712  ? 0.3030 0.2926 0.2405 0.0183  0.0001  -0.0113 710  LEU A C   
5110  O O   . LEU A 712  ? 0.2948 0.2881 0.2290 0.0192  -0.0004 -0.0117 710  LEU A O   
5111  C CB  . LEU A 712  ? 0.2825 0.2756 0.2202 0.0197  0.0027  -0.0113 710  LEU A CB  
5112  C CG  . LEU A 712  ? 0.3315 0.3302 0.2641 0.0202  0.0042  -0.0085 710  LEU A CG  
5113  C CD1 . LEU A 712  ? 0.2871 0.2921 0.2169 0.0228  0.0036  -0.0124 710  LEU A CD1 
5114  C CD2 . LEU A 712  ? 0.3408 0.3411 0.2728 0.0197  0.0065  -0.0051 710  LEU A CD2 
5115  N N   . ALA A 713  ? 0.2791 0.2637 0.2189 0.0161  0.0002  -0.0084 711  ALA A N   
5116  C CA  . ALA A 713  ? 0.2980 0.2815 0.2362 0.0147  0.0002  -0.0051 711  ALA A CA  
5117  C C   . ALA A 713  ? 0.2890 0.2724 0.2277 0.0149  -0.0018 -0.0074 711  ALA A C   
5118  O O   . ALA A 713  ? 0.3210 0.3070 0.2566 0.0154  -0.0022 -0.0066 711  ALA A O   
5119  C CB  . ALA A 713  ? 0.3119 0.2907 0.2525 0.0125  0.0009  -0.0018 711  ALA A CB  
5120  N N   . ILE A 714  ? 0.2940 0.2742 0.2368 0.0143  -0.0033 -0.0102 712  ILE A N   
5121  C CA  . ILE A 714  ? 0.2781 0.2584 0.2219 0.0142  -0.0053 -0.0125 712  ILE A CA  
5122  C C   . ILE A 714  ? 0.3048 0.2897 0.2464 0.0165  -0.0064 -0.0165 712  ILE A C   
5123  O O   . ILE A 714  ? 0.3014 0.2886 0.2412 0.0170  -0.0075 -0.0173 712  ILE A O   
5124  C CB  . ILE A 714  ? 0.3038 0.2795 0.2530 0.0126  -0.0066 -0.0139 712  ILE A CB  
5125  C CG1 . ILE A 714  ? 0.3636 0.3359 0.3142 0.0103  -0.0056 -0.0097 712  ILE A CG1 
5126  C CG2 . ILE A 714  ? 0.2800 0.2563 0.2307 0.0126  -0.0088 -0.0171 712  ILE A CG2 
5127  C CD1 . ILE A 714  ? 0.4383 0.4066 0.3940 0.0084  -0.0067 -0.0102 712  ILE A CD1 
5128  N N   . PHE A 715  ? 0.2952 0.2818 0.2369 0.0181  -0.0061 -0.0191 713  PHE A N   
5129  C CA  . PHE A 715  ? 0.3305 0.3228 0.2694 0.0206  -0.0067 -0.0228 713  PHE A CA  
5130  C C   . PHE A 715  ? 0.2953 0.2923 0.2286 0.0213  -0.0058 -0.0201 713  PHE A C   
5131  O O   . PHE A 715  ? 0.2947 0.2949 0.2260 0.0224  -0.0072 -0.0219 713  PHE A O   
5132  C CB  . PHE A 715  ? 0.2985 0.2926 0.2378 0.0222  -0.0058 -0.0248 713  PHE A CB  
5133  C CG  . PHE A 715  ? 0.3241 0.3248 0.2603 0.0250  -0.0062 -0.0288 713  PHE A CG  
5134  C CD1 . PHE A 715  ? 0.3271 0.3286 0.2656 0.0265  -0.0085 -0.0347 713  PHE A CD1 
5135  C CD2 . PHE A 715  ? 0.3445 0.3510 0.2756 0.0262  -0.0043 -0.0266 713  PHE A CD2 
5136  C CE1 . PHE A 715  ? 0.3506 0.3588 0.2861 0.0293  -0.0089 -0.0388 713  PHE A CE1 
5137  C CE2 . PHE A 715  ? 0.3466 0.3601 0.2746 0.0289  -0.0045 -0.0302 713  PHE A CE2 
5138  C CZ  . PHE A 715  ? 0.3084 0.3230 0.2385 0.0306  -0.0068 -0.0365 713  PHE A CZ  
5139  N N   . THR A 716  ? 0.2918 0.2893 0.2228 0.0207  -0.0036 -0.0155 714  THR A N   
5140  C CA  . THR A 716  ? 0.2930 0.2946 0.2189 0.0213  -0.0028 -0.0122 714  THR A CA  
5141  C C   . THR A 716  ? 0.2901 0.2901 0.2155 0.0203  -0.0039 -0.0102 714  THR A C   
5142  O O   . THR A 716  ? 0.3082 0.3122 0.2300 0.0214  -0.0045 -0.0098 714  THR A O   
5143  C CB  . THR A 716  ? 0.3052 0.3067 0.2299 0.0204  -0.0004 -0.0076 714  THR A CB  
5144  O OG1 . THR A 716  ? 0.2878 0.2916 0.2130 0.0215  0.0007  -0.0096 714  THR A OG1 
5145  C CG2 . THR A 716  ? 0.2886 0.2941 0.2084 0.0206  0.0004  -0.0036 714  THR A CG2 
5146  N N   . GLY A 717  ? 0.2842 0.2787 0.2131 0.0183  -0.0041 -0.0087 715  GLY A N   
5147  C CA  . GLY A 717  ? 0.3040 0.2969 0.2327 0.0174  -0.0051 -0.0068 715  GLY A CA  
5148  C C   . GLY A 717  ? 0.2856 0.2809 0.2141 0.0185  -0.0073 -0.0104 715  GLY A C   
5149  O O   . GLY A 717  ? 0.2888 0.2869 0.2143 0.0193  -0.0080 -0.0092 715  GLY A O   
5150  N N   . GLN A 718  ? 0.2861 0.2803 0.2180 0.0186  -0.0087 -0.0148 716  GLN A N   
5151  C CA  . GLN A 718  ? 0.2884 0.2850 0.2207 0.0195  -0.0110 -0.0187 716  GLN A CA  
5152  C C   . GLN A 718  ? 0.3096 0.3126 0.2369 0.0220  -0.0113 -0.0200 716  GLN A C   
5153  O O   . GLN A 718  ? 0.2942 0.3001 0.2193 0.0228  -0.0126 -0.0202 716  GLN A O   
5154  C CB  . GLN A 718  ? 0.2889 0.2832 0.2261 0.0192  -0.0124 -0.0234 716  GLN A CB  
5155  C CG  . GLN A 718  ? 0.3169 0.3054 0.2591 0.0166  -0.0124 -0.0218 716  GLN A CG  
5156  C CD  . GLN A 718  ? 0.3066 0.2924 0.2540 0.0160  -0.0140 -0.0260 716  GLN A CD  
5157  O OE1 . GLN A 718  ? 0.3113 0.2940 0.2628 0.0141  -0.0150 -0.0259 716  GLN A OE1 
5158  N NE2 . GLN A 718  ? 0.2891 0.2765 0.2366 0.0178  -0.0144 -0.0296 716  GLN A NE2 
5159  N N   . ILE A 719  ? 0.2941 0.2998 0.2196 0.0233  -0.0100 -0.0210 717  ILE A N   
5160  C CA  . ILE A 719  ? 0.3176 0.3304 0.2384 0.0257  -0.0102 -0.0227 717  ILE A CA  
5161  C C   . ILE A 719  ? 0.2990 0.3147 0.2149 0.0259  -0.0094 -0.0176 717  ILE A C   
5162  O O   . ILE A 719  ? 0.3021 0.3224 0.2147 0.0273  -0.0106 -0.0183 717  ILE A O   
5163  C CB  . ILE A 719  ? 0.3419 0.3573 0.2622 0.0270  -0.0089 -0.0246 717  ILE A CB  
5164  C CG1 . ILE A 719  ? 0.3680 0.3812 0.2931 0.0274  -0.0104 -0.0304 717  ILE A CG1 
5165  C CG2 . ILE A 719  ? 0.3941 0.4177 0.3087 0.0294  -0.0083 -0.0250 717  ILE A CG2 
5166  C CD1 . ILE A 719  ? 0.4284 0.4432 0.3539 0.0287  -0.0092 -0.0324 717  ILE A CD1 
5167  N N   . ALA A 720  ? 0.2964 0.3093 0.2121 0.0244  -0.0075 -0.0125 718  ALA A N   
5168  C CA  . ALA A 720  ? 0.2974 0.3123 0.2090 0.0244  -0.0067 -0.0073 718  ALA A CA  
5169  C C   . ALA A 720  ? 0.2975 0.3114 0.2090 0.0242  -0.0086 -0.0064 718  ALA A C   
5170  O O   . ALA A 720  ? 0.3105 0.3285 0.2180 0.0253  -0.0092 -0.0046 718  ALA A O   
5171  C CB  . ALA A 720  ? 0.2944 0.3054 0.2070 0.0225  -0.0046 -0.0024 718  ALA A CB  
5172  N N   . ALA A 721  ? 0.2944 0.3032 0.2104 0.0227  -0.0096 -0.0076 719  ALA A N   
5173  C CA  . ALA A 721  ? 0.2943 0.3025 0.2108 0.0226  -0.0114 -0.0072 719  ALA A CA  
5174  C C   . ALA A 721  ? 0.2981 0.3114 0.2125 0.0246  -0.0135 -0.0111 719  ALA A C   
5175  O O   . ALA A 721  ? 0.3020 0.3184 0.2134 0.0256  -0.0145 -0.0094 719  ALA A O   
5176  C CB  . ALA A 721  ? 0.2905 0.2931 0.2123 0.0207  -0.0120 -0.0083 719  ALA A CB  
5177  N N   . ALA A 722  ? 0.2990 0.3134 0.2154 0.0252  -0.0143 -0.0164 720  ALA A N   
5178  C CA  . ALA A 722  ? 0.3028 0.3223 0.2176 0.0271  -0.0165 -0.0208 720  ALA A CA  
5179  C C   . ALA A 722  ? 0.3227 0.3492 0.2313 0.0293  -0.0160 -0.0194 720  ALA A C   
5180  O O   . ALA A 722  ? 0.3099 0.3405 0.2155 0.0307  -0.0177 -0.0196 720  ALA A O   
5181  C CB  . ALA A 722  ? 0.3034 0.3227 0.2218 0.0275  -0.0174 -0.0269 720  ALA A CB  
5182  N N   . LEU A 723  ? 0.3075 0.3356 0.2138 0.0296  -0.0138 -0.0178 721  LEU A N   
5183  C CA  . LEU A 723  ? 0.3117 0.3470 0.2120 0.0315  -0.0131 -0.0161 721  LEU A CA  
5184  C C   . LEU A 723  ? 0.3288 0.3648 0.2259 0.0312  -0.0132 -0.0102 721  LEU A C   
5185  O O   . LEU A 723  ? 0.3480 0.3897 0.2409 0.0329  -0.0143 -0.0098 721  LEU A O   
5186  C CB  . LEU A 723  ? 0.3115 0.3481 0.2108 0.0315  -0.0105 -0.0148 721  LEU A CB  
5187  C CG  . LEU A 723  ? 0.3175 0.3560 0.2186 0.0326  -0.0104 -0.0206 721  LEU A CG  
5188  C CD1 . LEU A 723  ? 0.3385 0.3779 0.2386 0.0323  -0.0076 -0.0181 721  LEU A CD1 
5189  C CD2 . LEU A 723  ? 0.3175 0.3640 0.2150 0.0354  -0.0119 -0.0252 721  LEU A CD2 
5190  N N   . VAL A 724  ? 0.3091 0.3392 0.2082 0.0292  -0.0121 -0.0055 722  VAL A N   
5191  C CA  . VAL A 724  ? 0.3104 0.3407 0.2067 0.0290  -0.0121 0.0003  722  VAL A CA  
5192  C C   . VAL A 724  ? 0.3117 0.3418 0.2084 0.0296  -0.0148 -0.0005 722  VAL A C   
5193  O O   . VAL A 724  ? 0.3494 0.3822 0.2427 0.0305  -0.0156 0.0030  722  VAL A O   
5194  C CB  . VAL A 724  ? 0.3069 0.3310 0.2054 0.0268  -0.0104 0.0051  722  VAL A CB  
5195  C CG1 . VAL A 724  ? 0.3114 0.3289 0.2148 0.0254  -0.0114 0.0045  722  VAL A CG1 
5196  C CG2 . VAL A 724  ? 0.3409 0.3668 0.2357 0.0268  -0.0097 0.0116  722  VAL A CG2 
5197  N N   . ALA A 725  ? 0.3286 0.3561 0.2295 0.0292  -0.0163 -0.0051 723  ALA A N   
5198  C CA  . ALA A 725  ? 0.3414 0.3698 0.2429 0.0300  -0.0189 -0.0066 723  ALA A CA  
5199  C C   . ALA A 725  ? 0.3735 0.4094 0.2710 0.0324  -0.0205 -0.0097 723  ALA A C   
5200  O O   . ALA A 725  ? 0.3229 0.3605 0.2205 0.0333  -0.0229 -0.0111 723  ALA A O   
5201  C CB  . ALA A 725  ? 0.3418 0.3658 0.2493 0.0286  -0.0199 -0.0106 723  ALA A CB  
5202  N N   . GLY A 726  ? 0.3177 0.3586 0.2117 0.0336  -0.0194 -0.0107 724  GLY A N   
5203  C CA  . GLY A 726  ? 0.3227 0.3717 0.2125 0.0361  -0.0208 -0.0137 724  GLY A CA  
5204  C C   . GLY A 726  ? 0.3349 0.3859 0.2268 0.0371  -0.0221 -0.0213 724  GLY A C   
5205  O O   . GLY A 726  ? 0.3471 0.4046 0.2362 0.0392  -0.0239 -0.0247 724  GLY A O   
5206  N N   . ASN A 727  ? 0.3413 0.3871 0.2383 0.0356  -0.0214 -0.0241 725  ASN A N   
5207  C CA  . ASN A 727  ? 0.3456 0.3922 0.2457 0.0363  -0.0229 -0.0314 725  ASN A CA  
5208  C C   . ASN A 727  ? 0.3308 0.3800 0.2300 0.0373  -0.0212 -0.0338 725  ASN A C   
5209  O O   . ASN A 727  ? 0.3196 0.3657 0.2190 0.0361  -0.0187 -0.0303 725  ASN A O   
5210  C CB  . ASN A 727  ? 0.3397 0.3788 0.2469 0.0340  -0.0236 -0.0332 725  ASN A CB  
5211  C CG  . ASN A 727  ? 0.3708 0.4072 0.2796 0.0329  -0.0249 -0.0308 725  ASN A CG  
5212  O OD1 . ASN A 727  ? 0.3283 0.3676 0.2375 0.0338  -0.0274 -0.0338 725  ASN A OD1 
5213  N ND2 . ASN A 727  ? 0.3107 0.3417 0.2210 0.0310  -0.0234 -0.0258 725  ASN A ND2 
5214  N N   . PRO A 728  ? 0.3257 0.3802 0.2240 0.0394  -0.0225 -0.0398 726  PRO A N   
5215  C CA  . PRO A 728  ? 0.3264 0.3821 0.2254 0.0403  -0.0212 -0.0431 726  PRO A CA  
5216  C C   . PRO A 728  ? 0.3229 0.3709 0.2292 0.0385  -0.0217 -0.0462 726  PRO A C   
5217  O O   . PRO A 728  ? 0.3355 0.3792 0.2461 0.0372  -0.0236 -0.0478 726  PRO A O   
5218  C CB  . PRO A 728  ? 0.3320 0.3964 0.2279 0.0434  -0.0229 -0.0491 726  PRO A CB  
5219  C CG  . PRO A 728  ? 0.3331 0.3980 0.2297 0.0436  -0.0259 -0.0510 726  PRO A CG  
5220  C CD  . PRO A 728  ? 0.3297 0.3899 0.2264 0.0414  -0.0254 -0.0443 726  PRO A CD  
5221  N N   . VAL A 729  ? 0.3219 0.3684 0.2296 0.0384  -0.0198 -0.0467 727  VAL A N   
5222  C CA  . VAL A 729  ? 0.3182 0.3566 0.2324 0.0364  -0.0197 -0.0476 727  VAL A CA  
5223  C C   . VAL A 729  ? 0.3205 0.3600 0.2375 0.0380  -0.0204 -0.0541 727  VAL A C   
5224  O O   . VAL A 729  ? 0.3234 0.3689 0.2369 0.0402  -0.0193 -0.0557 727  VAL A O   
5225  C CB  . VAL A 729  ? 0.3141 0.3480 0.2282 0.0344  -0.0167 -0.0411 727  VAL A CB  
5226  C CG1 . VAL A 729  ? 0.3110 0.3380 0.2313 0.0328  -0.0164 -0.0425 727  VAL A CG1 
5227  C CG2 . VAL A 729  ? 0.3114 0.3426 0.2246 0.0325  -0.0165 -0.0354 727  VAL A CG2 
5228  N N   . LEU A 730  ? 0.3195 0.3532 0.2429 0.0368  -0.0223 -0.0578 728  LEU A N   
5229  C CA  . LEU A 730  ? 0.3210 0.3530 0.2487 0.0378  -0.0230 -0.0632 728  LEU A CA  
5230  C C   . LEU A 730  ? 0.3165 0.3405 0.2484 0.0352  -0.0214 -0.0594 728  LEU A C   
5231  O O   . LEU A 730  ? 0.3149 0.3328 0.2510 0.0326  -0.0222 -0.0577 728  LEU A O   
5232  C CB  . LEU A 730  ? 0.3237 0.3547 0.2562 0.0382  -0.0265 -0.0700 728  LEU A CB  
5233  C CG  . LEU A 730  ? 0.3284 0.3669 0.2576 0.0407  -0.0288 -0.0747 728  LEU A CG  
5234  C CD1 . LEU A 730  ? 0.3455 0.3928 0.2681 0.0439  -0.0272 -0.0755 728  LEU A CD1 
5235  C CD2 . LEU A 730  ? 0.3272 0.3662 0.2542 0.0395  -0.0295 -0.0712 728  LEU A CD2 
5236  N N   . ALA A 731  ? 0.3275 0.3522 0.2585 0.0358  -0.0192 -0.0581 729  ALA A N   
5237  C CA  . ALA A 731  ? 0.3117 0.3297 0.2458 0.0336  -0.0174 -0.0540 729  ALA A CA  
5238  C C   . ALA A 731  ? 0.3150 0.3291 0.2551 0.0340  -0.0187 -0.0587 729  ALA A C   
5239  O O   . ALA A 731  ? 0.3422 0.3599 0.2817 0.0364  -0.0184 -0.0622 729  ALA A O   
5240  C CB  . ALA A 731  ? 0.3103 0.3313 0.2399 0.0338  -0.0142 -0.0491 729  ALA A CB  
5241  N N   . LYS A 732  ? 0.3313 0.3381 0.2773 0.0316  -0.0202 -0.0585 730  LYS A N   
5242  C CA  . LYS A 732  ? 0.3119 0.3137 0.2643 0.0315  -0.0216 -0.0622 730  LYS A CA  
5243  C C   . LYS A 732  ? 0.3076 0.3034 0.2624 0.0292  -0.0197 -0.0569 730  LYS A C   
5244  O O   . LYS A 732  ? 0.3046 0.2954 0.2618 0.0263  -0.0198 -0.0534 730  LYS A O   
5245  C CB  . LYS A 732  ? 0.3377 0.3359 0.2957 0.0304  -0.0249 -0.0659 730  LYS A CB  
5246  C CG  . LYS A 732  ? 0.3620 0.3585 0.3254 0.0320  -0.0276 -0.0727 730  LYS A CG  
5247  C CD  . LYS A 732  ? 0.4059 0.3969 0.3736 0.0313  -0.0268 -0.0714 730  LYS A CD  
5248  C CE  . LYS A 732  ? 0.3955 0.3785 0.3685 0.0276  -0.0273 -0.0676 730  LYS A CE  
5249  N NZ  . LYS A 732  ? 0.4127 0.3902 0.3905 0.0272  -0.0272 -0.0670 730  LYS A NZ  
5250  N N   . PRO A 733  ? 0.3074 0.3040 0.2616 0.0303  -0.0180 -0.0563 731  PRO A N   
5251  C CA  . PRO A 733  ? 0.3037 0.2947 0.2602 0.0282  -0.0163 -0.0516 731  PRO A CA  
5252  C C   . PRO A 733  ? 0.3190 0.3034 0.2828 0.0273  -0.0184 -0.0540 731  PRO A C   
5253  O O   . PRO A 733  ? 0.3499 0.3342 0.3171 0.0288  -0.0209 -0.0598 731  PRO A O   
5254  C CB  . PRO A 733  ? 0.3038 0.2993 0.2568 0.0301  -0.0139 -0.0508 731  PRO A CB  
5255  C CG  . PRO A 733  ? 0.3263 0.3278 0.2782 0.0335  -0.0151 -0.0571 731  PRO A CG  
5256  C CD  . PRO A 733  ? 0.3108 0.3140 0.2619 0.0337  -0.0174 -0.0601 731  PRO A CD  
5257  N N   . ALA A 734  ? 0.3010 0.2799 0.2674 0.0248  -0.0174 -0.0493 732  ALA A N   
5258  C CA  . ALA A 734  ? 0.3295 0.3020 0.3028 0.0238  -0.0192 -0.0505 732  ALA A CA  
5259  C C   . ALA A 734  ? 0.3055 0.2790 0.2808 0.0268  -0.0200 -0.0554 732  ALA A C   
5260  O O   . ALA A 734  ? 0.3270 0.3054 0.2985 0.0289  -0.0181 -0.0556 732  ALA A O   
5261  C CB  . ALA A 734  ? 0.3210 0.2887 0.2956 0.0211  -0.0176 -0.0444 732  ALA A CB  
5262  N N   . GLU A 735  ? 0.3086 0.2776 0.2904 0.0268  -0.0229 -0.0592 733  GLU A N   
5263  C CA  . GLU A 735  ? 0.3563 0.3258 0.3410 0.0298  -0.0241 -0.0644 733  GLU A CA  
5264  C C   . GLU A 735  ? 0.3488 0.3175 0.3332 0.0302  -0.0220 -0.0613 733  GLU A C   
5265  O O   . GLU A 735  ? 0.3127 0.2852 0.2965 0.0333  -0.0216 -0.0648 733  GLU A O   
5266  C CB  . GLU A 735  ? 0.3861 0.3493 0.3787 0.0292  -0.0278 -0.0681 733  GLU A CB  
5267  C CG  . GLU A 735  ? 0.5317 0.4959 0.5277 0.0328  -0.0300 -0.0752 733  GLU A CG  
5268  C CD  . GLU A 735  ? 0.5714 0.5285 0.5759 0.0320  -0.0339 -0.0785 733  GLU A CD  
5269  O OE1 . GLU A 735  ? 0.6433 0.5956 0.6508 0.0285  -0.0349 -0.0753 733  GLU A OE1 
5270  O OE2 . GLU A 735  ? 0.6738 0.6302 0.6824 0.0348  -0.0360 -0.0841 733  GLU A OE2 
5271  N N   . GLU A 736  ? 0.3565 0.3211 0.3413 0.0273  -0.0205 -0.0550 734  GLU A N   
5272  C CA  . GLU A 736  ? 0.3486 0.3118 0.3338 0.0273  -0.0187 -0.0517 734  GLU A CA  
5273  C C   . GLU A 736  ? 0.3741 0.3438 0.3528 0.0285  -0.0154 -0.0495 734  GLU A C   
5274  O O   . GLU A 736  ? 0.3275 0.2981 0.3065 0.0297  -0.0141 -0.0489 734  GLU A O   
5275  C CB  . GLU A 736  ? 0.3358 0.2928 0.3235 0.0237  -0.0184 -0.0457 734  GLU A CB  
5276  C CG  . GLU A 736  ? 0.4022 0.3525 0.3970 0.0220  -0.0215 -0.0468 734  GLU A CG  
5277  C CD  . GLU A 736  ? 0.4541 0.4035 0.4495 0.0199  -0.0229 -0.0470 734  GLU A CD  
5278  O OE1 . GLU A 736  ? 0.3749 0.3291 0.3653 0.0203  -0.0219 -0.0475 734  GLU A OE1 
5279  O OE2 . GLU A 736  ? 0.5113 0.4551 0.5123 0.0178  -0.0251 -0.0465 734  GLU A OE2 
5280  N N   . THR A 737  ? 0.3083 0.2826 0.2815 0.0281  -0.0140 -0.0480 735  THR A N   
5281  C CA  . THR A 737  ? 0.3142 0.2937 0.2814 0.0284  -0.0108 -0.0444 735  THR A CA  
5282  C C   . THR A 737  ? 0.3042 0.2915 0.2661 0.0305  -0.0103 -0.0471 735  THR A C   
5283  O O   . THR A 737  ? 0.3175 0.3077 0.2745 0.0295  -0.0086 -0.0435 735  THR A O   
5284  C CB  . THR A 737  ? 0.3040 0.2807 0.2694 0.0251  -0.0093 -0.0378 735  THR A CB  
5285  O OG1 . THR A 737  ? 0.3086 0.2838 0.2739 0.0235  -0.0106 -0.0378 735  THR A OG1 
5286  C CG2 . THR A 737  ? 0.3148 0.2854 0.2845 0.0232  -0.0093 -0.0346 735  THR A CG2 
5287  N N   . PRO A 738  ? 0.3044 0.2954 0.2671 0.0336  -0.0116 -0.0533 736  PRO A N   
5288  C CA  . PRO A 738  ? 0.3293 0.3285 0.2866 0.0358  -0.0111 -0.0559 736  PRO A CA  
5289  C C   . PRO A 738  ? 0.3384 0.3446 0.2903 0.0368  -0.0079 -0.0531 736  PRO A C   
5290  O O   . PRO A 738  ? 0.3160 0.3285 0.2625 0.0375  -0.0070 -0.0526 736  PRO A O   
5291  C CB  . PRO A 738  ? 0.3120 0.3129 0.2725 0.0389  -0.0137 -0.0638 736  PRO A CB  
5292  C CG  . PRO A 738  ? 0.3119 0.3081 0.2780 0.0392  -0.0141 -0.0645 736  PRO A CG  
5293  C CD  . PRO A 738  ? 0.3325 0.3209 0.3010 0.0355  -0.0138 -0.0584 736  PRO A CD  
5294  N N   . LEU A 739  ? 0.3043 0.3100 0.2576 0.0369  -0.0063 -0.0511 737  LEU A N   
5295  C CA  . LEU A 739  ? 0.3138 0.3271 0.2626 0.0382  -0.0035 -0.0495 737  LEU A CA  
5296  C C   . LEU A 739  ? 0.3013 0.3159 0.2451 0.0358  -0.0012 -0.0428 737  LEU A C   
5297  O O   . LEU A 739  ? 0.3026 0.3247 0.2414 0.0368  0.0004  -0.0420 737  LEU A O   
5298  C CB  . LEU A 739  ? 0.3109 0.3234 0.2630 0.0389  -0.0025 -0.0495 737  LEU A CB  
5299  C CG  . LEU A 739  ? 0.3125 0.3230 0.2700 0.0415  -0.0049 -0.0561 737  LEU A CG  
5300  C CD1 . LEU A 739  ? 0.3344 0.3428 0.2955 0.0417  -0.0041 -0.0549 737  LEU A CD1 
5301  C CD2 . LEU A 739  ? 0.3249 0.3436 0.2805 0.0452  -0.0055 -0.0626 737  LEU A CD2 
5302  N N   . ILE A 740  ? 0.3158 0.3236 0.2612 0.0327  -0.0009 -0.0380 738  ILE A N   
5303  C CA  . ILE A 740  ? 0.2947 0.3034 0.2359 0.0306  0.0009  -0.0319 738  ILE A CA  
5304  C C   . ILE A 740  ? 0.2962 0.3073 0.2340 0.0307  -0.0001 -0.0325 738  ILE A C   
5305  O O   . ILE A 740  ? 0.3284 0.3435 0.2614 0.0303  0.0014  -0.0290 738  ILE A O   
5306  C CB  . ILE A 740  ? 0.3495 0.3508 0.2933 0.0275  0.0013  -0.0271 738  ILE A CB  
5307  C CG1 . ILE A 740  ? 0.3652 0.3675 0.3051 0.0256  0.0031  -0.0212 738  ILE A CG1 
5308  C CG2 . ILE A 740  ? 0.3362 0.3308 0.2838 0.0263  -0.0012 -0.0285 738  ILE A CG2 
5309  C CD1 . ILE A 740  ? 0.3525 0.3596 0.2900 0.0258  0.0058  -0.0182 738  ILE A CD1 
5310  N N   . ALA A 741  ? 0.2981 0.3069 0.2383 0.0313  -0.0027 -0.0370 739  ALA A N   
5311  C CA  . ALA A 741  ? 0.3141 0.3257 0.2511 0.0317  -0.0039 -0.0382 739  ALA A CA  
5312  C C   . ALA A 741  ? 0.3172 0.3382 0.2493 0.0345  -0.0031 -0.0404 739  ALA A C   
5313  O O   . ALA A 741  ? 0.3101 0.3353 0.2374 0.0343  -0.0024 -0.0377 739  ALA A O   
5314  C CB  . ALA A 741  ? 0.3017 0.3094 0.2429 0.0320  -0.0071 -0.0430 739  ALA A CB  
5315  N N   . ALA A 742  ? 0.3067 0.3314 0.2401 0.0371  -0.0033 -0.0454 740  ALA A N   
5316  C CA  . ALA A 742  ? 0.3410 0.3757 0.2698 0.0399  -0.0024 -0.0478 740  ALA A CA  
5317  C C   . ALA A 742  ? 0.3276 0.3670 0.2516 0.0390  0.0008  -0.0417 740  ALA A C   
5318  O O   . ALA A 742  ? 0.3400 0.3867 0.2588 0.0399  0.0016  -0.0406 740  ALA A O   
5319  C CB  . ALA A 742  ? 0.3178 0.3552 0.2495 0.0429  -0.0030 -0.0542 740  ALA A CB  
5320  N N   . GLU A 743  ? 0.3056 0.3411 0.2317 0.0372  0.0025  -0.0375 741  GLU A N   
5321  C CA  . GLU A 743  ? 0.3173 0.3564 0.2397 0.0359  0.0053  -0.0314 741  GLU A CA  
5322  C C   . GLU A 743  ? 0.3496 0.3869 0.2688 0.0337  0.0054  -0.0261 741  GLU A C   
5323  O O   . GLU A 743  ? 0.3461 0.3889 0.2607 0.0335  0.0070  -0.0222 741  GLU A O   
5324  C CB  . GLU A 743  ? 0.3007 0.3356 0.2266 0.0344  0.0068  -0.0285 741  GLU A CB  
5325  C CG  . GLU A 743  ? 0.3940 0.4313 0.3170 0.0326  0.0095  -0.0218 741  GLU A CG  
5326  C CD  . GLU A 743  ? 0.3792 0.4270 0.2981 0.0343  0.0116  -0.0217 741  GLU A CD  
5327  O OE1 . GLU A 743  ? 0.3754 0.4293 0.2938 0.0373  0.0111  -0.0273 741  GLU A OE1 
5328  O OE2 . GLU A 743  ? 0.4243 0.4747 0.3407 0.0327  0.0137  -0.0160 741  GLU A OE2 
5329  N N   . GLY A 744  ? 0.3348 0.3645 0.2566 0.0321  0.0036  -0.0258 742  GLY A N   
5330  C CA  . GLY A 744  ? 0.2998 0.3281 0.2188 0.0304  0.0033  -0.0217 742  GLY A CA  
5331  C C   . GLY A 744  ? 0.3298 0.3649 0.2443 0.0323  0.0024  -0.0236 742  GLY A C   
5332  O O   . GLY A 744  ? 0.3046 0.3427 0.2149 0.0317  0.0032  -0.0192 742  GLY A O   
5333  N N   . VAL A 745  ? 0.3069 0.3445 0.2222 0.0346  0.0006  -0.0301 743  VAL A N   
5334  C CA  . VAL A 745  ? 0.3479 0.3928 0.2587 0.0367  -0.0003 -0.0324 743  VAL A CA  
5335  C C   . VAL A 745  ? 0.3330 0.3874 0.2388 0.0380  0.0020  -0.0305 743  VAL A C   
5336  O O   . VAL A 745  ? 0.3499 0.4095 0.2507 0.0383  0.0023  -0.0277 743  VAL A O   
5337  C CB  . VAL A 745  ? 0.3215 0.3671 0.2349 0.0389  -0.0030 -0.0404 743  VAL A CB  
5338  C CG1 . VAL A 745  ? 0.3201 0.3753 0.2285 0.0417  -0.0036 -0.0436 743  VAL A CG1 
5339  C CG2 . VAL A 745  ? 0.3119 0.3494 0.2292 0.0372  -0.0054 -0.0413 743  VAL A CG2 
5340  N N   . ARG A 746  ? 0.3212 0.3782 0.2283 0.0389  0.0037  -0.0317 744  ARG A N   
5341  C CA  . ARG A 746  ? 0.3889 0.4553 0.2915 0.0400  0.0062  -0.0295 744  ARG A CA  
5342  C C   . ARG A 746  ? 0.3601 0.4263 0.2594 0.0375  0.0079  -0.0212 744  ARG A C   
5343  O O   . ARG A 746  ? 0.3532 0.4271 0.2473 0.0381  0.0089  -0.0186 744  ARG A O   
5344  C CB  . ARG A 746  ? 0.3301 0.3980 0.2356 0.0408  0.0078  -0.0313 744  ARG A CB  
5345  C CG  . ARG A 746  ? 0.4031 0.4822 0.3042 0.0423  0.0103  -0.0300 744  ARG A CG  
5346  C CD  . ARG A 746  ? 0.4189 0.4993 0.3230 0.0425  0.0124  -0.0302 744  ARG A CD  
5347  N NE  . ARG A 746  ? 0.4338 0.5073 0.3401 0.0392  0.0137  -0.0238 744  ARG A NE  
5348  C CZ  . ARG A 746  ? 0.4858 0.5615 0.3892 0.0370  0.0157  -0.0168 744  ARG A CZ  
5349  N NH1 . ARG A 746  ? 0.4878 0.5726 0.3858 0.0377  0.0169  -0.0147 744  ARG A NH1 
5350  N NH2 . ARG A 746  ? 0.4547 0.5233 0.3606 0.0341  0.0165  -0.0118 744  ARG A NH2 
5351  N N   . ILE A 747  ? 0.3454 0.4031 0.2479 0.0347  0.0082  -0.0170 745  ILE A N   
5352  C CA  . ILE A 747  ? 0.3350 0.3917 0.2352 0.0322  0.0096  -0.0093 745  ILE A CA  
5353  C C   . ILE A 747  ? 0.3510 0.4081 0.2477 0.0321  0.0081  -0.0074 745  ILE A C   
5354  O O   . ILE A 747  ? 0.3403 0.4020 0.2328 0.0317  0.0091  -0.0025 745  ILE A O   
5355  C CB  . ILE A 747  ? 0.3444 0.3918 0.2491 0.0295  0.0100  -0.0063 745  ILE A CB  
5356  C CG1 . ILE A 747  ? 0.3588 0.4080 0.2658 0.0296  0.0121  -0.0065 745  ILE A CG1 
5357  C CG2 . ILE A 747  ? 0.3408 0.3852 0.2439 0.0271  0.0105  0.0007  745  ILE A CG2 
5358  C CD1 . ILE A 747  ? 0.3478 0.3885 0.2594 0.0274  0.0123  -0.0045 745  ILE A CD1 
5359  N N   . LEU A 748  ? 0.3786 0.4310 0.2772 0.0324  0.0056  -0.0110 746  LEU A N   
5360  C CA  . LEU A 748  ? 0.3453 0.3984 0.2409 0.0325  0.0040  -0.0096 746  LEU A CA  
5361  C C   . LEU A 748  ? 0.3617 0.4251 0.2519 0.0350  0.0039  -0.0111 746  LEU A C   
5362  O O   . LEU A 748  ? 0.3272 0.3936 0.2132 0.0348  0.0038  -0.0070 746  LEU A O   
5363  C CB  . LEU A 748  ? 0.3107 0.3576 0.2098 0.0324  0.0013  -0.0138 746  LEU A CB  
5364  C CG  . LEU A 748  ? 0.3663 0.4035 0.2694 0.0297  0.0010  -0.0106 746  LEU A CG  
5365  C CD1 . LEU A 748  ? 0.4418 0.4733 0.3494 0.0295  -0.0012 -0.0152 746  LEU A CD1 
5366  C CD2 . LEU A 748  ? 0.3724 0.4088 0.2729 0.0284  0.0009  -0.0048 746  LEU A CD2 
5367  N N   . ARG A 749  ? 0.3244 0.3934 0.2145 0.0374  0.0039  -0.0170 747  ARG A N   
5368  C CA  . ARG A 749  ? 0.3501 0.4301 0.2347 0.0399  0.0041  -0.0185 747  ARG A CA  
5369  C C   . ARG A 749  ? 0.3749 0.4612 0.2555 0.0392  0.0069  -0.0122 747  ARG A C   
5370  O O   . ARG A 749  ? 0.3583 0.4510 0.2337 0.0397  0.0071  -0.0089 747  ARG A O   
5371  C CB  . ARG A 749  ? 0.3983 0.4830 0.2840 0.0429  0.0033  -0.0268 747  ARG A CB  
5372  C CG  . ARG A 749  ? 0.4117 0.4929 0.2999 0.0441  0.0000  -0.0332 747  ARG A CG  
5373  C CD  . ARG A 749  ? 0.4251 0.5112 0.3146 0.0472  -0.0009 -0.0415 747  ARG A CD  
5374  N NE  . ARG A 749  ? 0.3729 0.4553 0.2655 0.0481  -0.0042 -0.0477 747  ARG A NE  
5375  C CZ  . ARG A 749  ? 0.4274 0.5138 0.3212 0.0509  -0.0059 -0.0557 747  ARG A CZ  
5376  N NH1 . ARG A 749  ? 0.4168 0.5111 0.3091 0.0534  -0.0045 -0.0587 747  ARG A NH1 
5377  N NH2 . ARG A 749  ? 0.4078 0.4906 0.3046 0.0514  -0.0091 -0.0608 747  ARG A NH2 
5378  N N   . GLU A 750  ? 0.3559 0.4406 0.2390 0.0380  0.0092  -0.0101 748  GLU A N   
5379  C CA  . GLU A 750  ? 0.3627 0.4530 0.2428 0.0368  0.0119  -0.0036 748  GLU A CA  
5380  C C   . GLU A 750  ? 0.3391 0.4258 0.2172 0.0344  0.0117  0.0040  748  GLU A C   
5381  O O   . GLU A 750  ? 0.3706 0.4638 0.2445 0.0340  0.0130  0.0092  748  GLU A O   
5382  C CB  . GLU A 750  ? 0.3698 0.4575 0.2539 0.0355  0.0140  -0.0027 748  GLU A CB  
5383  C CG  . GLU A 750  ? 0.4144 0.5078 0.2961 0.0341  0.0169  0.0038  748  GLU A CG  
5384  C CD  . GLU A 750  ? 0.4574 0.5479 0.3434 0.0327  0.0188  0.0048  748  GLU A CD  
5385  O OE1 . GLU A 750  ? 0.5399 0.6263 0.4302 0.0336  0.0181  -0.0005 748  GLU A OE1 
5386  O OE2 . GLU A 750  ? 0.5310 0.6234 0.4164 0.0306  0.0209  0.0111  748  GLU A OE2 
5387  N N   . ALA A 751  ? 0.3334 0.4100 0.2147 0.0328  0.0100  0.0047  749  ALA A N   
5388  C CA  . ALA A 751  ? 0.3428 0.4156 0.2229 0.0308  0.0095  0.0113  749  ALA A CA  
5389  C C   . ALA A 751  ? 0.3391 0.4166 0.2145 0.0322  0.0077  0.0115  749  ALA A C   
5390  O O   . ALA A 751  ? 0.3570 0.4326 0.2308 0.0310  0.0071  0.0173  749  ALA A O   
5391  C CB  . ALA A 751  ? 0.3601 0.4214 0.2451 0.0288  0.0082  0.0116  749  ALA A CB  
5392  N N   . GLY A 752  ? 0.3331 0.4163 0.2067 0.0350  0.0065  0.0053  750  GLY A N   
5393  C CA  . GLY A 752  ? 0.4002 0.4891 0.2690 0.0366  0.0048  0.0054  750  GLY A CA  
5394  C C   . GLY A 752  ? 0.3585 0.4450 0.2286 0.0382  0.0018  -0.0010 750  GLY A C   
5395  O O   . GLY A 752  ? 0.3677 0.4594 0.2339 0.0398  0.0002  -0.0015 750  GLY A O   
5396  N N   . ILE A 753  ? 0.3663 0.4453 0.2419 0.0377  0.0009  -0.0056 751  ILE A N   
5397  C CA  . ILE A 753  ? 0.3294 0.4064 0.2067 0.0391  -0.0020 -0.0118 751  ILE A CA  
5398  C C   . ILE A 753  ? 0.3456 0.4316 0.2206 0.0422  -0.0025 -0.0184 751  ILE A C   
5399  O O   . ILE A 753  ? 0.3755 0.4637 0.2520 0.0430  -0.0011 -0.0217 751  ILE A O   
5400  C CB  . ILE A 753  ? 0.3432 0.4102 0.2273 0.0376  -0.0028 -0.0148 751  ILE A CB  
5401  C CG1 . ILE A 753  ? 0.3247 0.3833 0.2111 0.0346  -0.0022 -0.0087 751  ILE A CG1 
5402  C CG2 . ILE A 753  ? 0.3372 0.4025 0.2234 0.0387  -0.0058 -0.0210 751  ILE A CG2 
5403  C CD1 . ILE A 753  ? 0.3205 0.3771 0.2057 0.0341  -0.0041 -0.0059 751  ILE A CD1 
5404  N N   . PRO A 754  ? 0.3602 0.4519 0.2317 0.0442  -0.0045 -0.0209 752  PRO A N   
5405  C CA  . PRO A 754  ? 0.3699 0.4705 0.2392 0.0474  -0.0052 -0.0278 752  PRO A CA  
5406  C C   . PRO A 754  ? 0.4215 0.5175 0.2967 0.0481  -0.0066 -0.0358 752  PRO A C   
5407  O O   . PRO A 754  ? 0.3673 0.4540 0.2476 0.0465  -0.0081 -0.0368 752  PRO A O   
5408  C CB  . PRO A 754  ? 0.3690 0.4749 0.2341 0.0489  -0.0075 -0.0284 752  PRO A CB  
5409  C CG  . PRO A 754  ? 0.4234 0.5262 0.2864 0.0468  -0.0070 -0.0199 752  PRO A CG  
5410  C CD  . PRO A 754  ? 0.3600 0.4516 0.2285 0.0437  -0.0060 -0.0168 752  PRO A CD  
5411  N N   . ALA A 755  ? 0.4194 0.5224 0.2939 0.0507  -0.0062 -0.0415 753  ALA A N   
5412  C CA  . ALA A 755  ? 0.3702 0.4698 0.2501 0.0519  -0.0079 -0.0496 753  ALA A CA  
5413  C C   . ALA A 755  ? 0.3848 0.4807 0.2671 0.0523  -0.0115 -0.0544 753  ALA A C   
5414  O O   . ALA A 755  ? 0.4127 0.5011 0.3013 0.0516  -0.0131 -0.0585 753  ALA A O   
5415  C CB  . ALA A 755  ? 0.3472 0.4570 0.2250 0.0553  -0.0072 -0.0554 753  ALA A CB  
5416  N N   . SER A 756  ? 0.3465 0.4480 0.2243 0.0533  -0.0129 -0.0538 754  SER A N   
5417  C CA  . SER A 756  ? 0.3519 0.4506 0.2321 0.0536  -0.0164 -0.0583 754  SER A CA  
5418  C C   . SER A 756  ? 0.3954 0.4835 0.2796 0.0504  -0.0171 -0.0541 754  SER A C   
5419  O O   . SER A 756  ? 0.3916 0.4753 0.2799 0.0500  -0.0198 -0.0581 754  SER A O   
5420  C CB  . SER A 756  ? 0.3976 0.5060 0.2715 0.0558  -0.0178 -0.0591 754  SER A CB  
5421  O OG  . SER A 756  ? 0.4173 0.5274 0.2862 0.0546  -0.0162 -0.0506 754  SER A OG  
5422  N N   . ALA A 757  ? 0.3388 0.4230 0.2221 0.0480  -0.0147 -0.0462 755  ALA A N   
5423  C CA  . ALA A 757  ? 0.3351 0.4097 0.2221 0.0451  -0.0152 -0.0421 755  ALA A CA  
5424  C C   . ALA A 757  ? 0.3293 0.3951 0.2227 0.0431  -0.0144 -0.0427 755  ALA A C   
5425  O O   . ALA A 757  ? 0.3255 0.3834 0.2230 0.0408  -0.0152 -0.0412 755  ALA A O   
5426  C CB  . ALA A 757  ? 0.3332 0.4079 0.2162 0.0436  -0.0134 -0.0334 755  ALA A CB  
5427  N N   . LEU A 758  ? 0.3296 0.3968 0.2239 0.0439  -0.0128 -0.0449 756  LEU A N   
5428  C CA  . LEU A 758  ? 0.3253 0.3843 0.2255 0.0421  -0.0121 -0.0450 756  LEU A CA  
5429  C C   . LEU A 758  ? 0.3275 0.3889 0.2303 0.0442  -0.0125 -0.0520 756  LEU A C   
5430  O O   . LEU A 758  ? 0.3369 0.4043 0.2369 0.0458  -0.0107 -0.0524 756  LEU A O   
5431  C CB  . LEU A 758  ? 0.3298 0.3866 0.2288 0.0402  -0.0090 -0.0378 756  LEU A CB  
5432  C CG  . LEU A 758  ? 0.3180 0.3673 0.2226 0.0385  -0.0080 -0.0376 756  LEU A CG  
5433  C CD1 . LEU A 758  ? 0.3153 0.3564 0.2256 0.0368  -0.0103 -0.0398 756  LEU A CD1 
5434  C CD2 . LEU A 758  ? 0.3487 0.3958 0.2519 0.0363  -0.0054 -0.0301 756  LEU A CD2 
5435  N N   . GLN A 759  ? 0.3355 0.3921 0.2437 0.0442  -0.0151 -0.0576 757  GLN A N   
5436  C CA  . GLN A 759  ? 0.3298 0.3873 0.2415 0.0463  -0.0162 -0.0648 757  GLN A CA  
5437  C C   . GLN A 759  ? 0.3260 0.3738 0.2447 0.0442  -0.0162 -0.0647 757  GLN A C   
5438  O O   . GLN A 759  ? 0.3315 0.3718 0.2537 0.0416  -0.0172 -0.0625 757  GLN A O   
5439  C CB  . GLN A 759  ? 0.3343 0.3949 0.2469 0.0483  -0.0196 -0.0721 757  GLN A CB  
5440  C CG  . GLN A 759  ? 0.3385 0.4099 0.2440 0.0508  -0.0196 -0.0729 757  GLN A CG  
5441  C CD  . GLN A 759  ? 0.3714 0.4457 0.2778 0.0527  -0.0232 -0.0801 757  GLN A CD  
5442  O OE1 . GLN A 759  ? 0.3577 0.4369 0.2648 0.0555  -0.0245 -0.0872 757  GLN A OE1 
5443  N NE2 . GLN A 759  ? 0.3417 0.4133 0.2485 0.0512  -0.0250 -0.0786 757  GLN A NE2 
5444  N N   . LEU A 760  ? 0.3332 0.3815 0.2538 0.0454  -0.0152 -0.0669 758  LEU A N   
5445  C CA  . LEU A 760  ? 0.3234 0.3632 0.2504 0.0438  -0.0152 -0.0667 758  LEU A CA  
5446  C C   . LEU A 760  ? 0.3266 0.3643 0.2592 0.0454  -0.0182 -0.0747 758  LEU A C   
5447  O O   . LEU A 760  ? 0.3543 0.3985 0.2858 0.0486  -0.0188 -0.0805 758  LEU A O   
5448  C CB  . LEU A 760  ? 0.3219 0.3630 0.2477 0.0439  -0.0121 -0.0636 758  LEU A CB  
5449  C CG  . LEU A 760  ? 0.3187 0.3513 0.2508 0.0423  -0.0120 -0.0628 758  LEU A CG  
5450  C CD1 . LEU A 760  ? 0.3286 0.3539 0.2619 0.0385  -0.0111 -0.0559 758  LEU A CD1 
5451  C CD2 . LEU A 760  ? 0.3267 0.3625 0.2585 0.0437  -0.0098 -0.0627 758  LEU A CD2 
5452  N N   . LEU A 761  ? 0.3582 0.3871 0.2970 0.0432  -0.0201 -0.0750 759  LEU A N   
5453  C CA  . LEU A 761  ? 0.3434 0.3692 0.2885 0.0442  -0.0234 -0.0822 759  LEU A CA  
5454  C C   . LEU A 761  ? 0.3253 0.3420 0.2770 0.0422  -0.0235 -0.0808 759  LEU A C   
5455  O O   . LEU A 761  ? 0.3602 0.3697 0.3164 0.0394  -0.0249 -0.0791 759  LEU A O   
5456  C CB  . LEU A 761  ? 0.3350 0.3596 0.2814 0.0433  -0.0263 -0.0845 759  LEU A CB  
5457  C CG  . LEU A 761  ? 0.3578 0.3910 0.2985 0.0453  -0.0270 -0.0866 759  LEU A CG  
5458  C CD1 . LEU A 761  ? 0.3492 0.3909 0.2868 0.0493  -0.0270 -0.0925 759  LEU A CD1 
5459  C CD2 . LEU A 761  ? 0.3813 0.4170 0.3157 0.0438  -0.0245 -0.0792 759  LEU A CD2 
5460  N N   . PRO A 762  ? 0.3327 0.3498 0.2854 0.0436  -0.0222 -0.0814 760  PRO A N   
5461  C CA  . PRO A 762  ? 0.3236 0.3323 0.2826 0.0420  -0.0225 -0.0801 760  PRO A CA  
5462  C C   . PRO A 762  ? 0.3897 0.3933 0.3562 0.0423  -0.0264 -0.0862 760  PRO A C   
5463  O O   . PRO A 762  ? 0.3678 0.3753 0.3346 0.0449  -0.0287 -0.0930 760  PRO A O   
5464  C CB  . PRO A 762  ? 0.3446 0.3568 0.3024 0.0442  -0.0204 -0.0804 760  PRO A CB  
5465  C CG  . PRO A 762  ? 0.3249 0.3472 0.2748 0.0461  -0.0181 -0.0797 760  PRO A CG  
5466  C CD  . PRO A 762  ? 0.3278 0.3536 0.2755 0.0467  -0.0202 -0.0828 760  PRO A CD  
5467  N N   . GLY A 763  ? 0.3517 0.3465 0.3241 0.0397  -0.0272 -0.0837 761  GLY A N   
5468  C CA  . GLY A 763  ? 0.4042 0.3932 0.3844 0.0396  -0.0309 -0.0886 761  GLY A CA  
5469  C C   . GLY A 763  ? 0.4437 0.4241 0.4287 0.0355  -0.0317 -0.0840 761  GLY A C   
5470  O O   . GLY A 763  ? 0.4225 0.4011 0.4050 0.0329  -0.0293 -0.0771 761  GLY A O   
5471  N N   . ASP A 764  ? 0.4605 0.4357 0.4526 0.0349  -0.0353 -0.0881 762  ASP A N   
5472  C CA  . ASP A 764  ? 0.4922 0.4594 0.4899 0.0309  -0.0364 -0.0841 762  ASP A CA  
5473  C C   . ASP A 764  ? 0.5353 0.5033 0.5326 0.0289  -0.0376 -0.0839 762  ASP A C   
5474  O O   . ASP A 764  ? 0.4754 0.4501 0.4668 0.0302  -0.0368 -0.0849 762  ASP A O   
5475  C CB  . ASP A 764  ? 0.5474 0.5079 0.5538 0.0311  -0.0396 -0.0877 762  ASP A CB  
5476  C CG  . ASP A 764  ? 0.5594 0.5218 0.5690 0.0340  -0.0431 -0.0966 762  ASP A CG  
5477  O OD1 . ASP A 764  ? 0.5931 0.5581 0.6020 0.0336  -0.0447 -0.0993 762  ASP A OD1 
5478  O OD2 . ASP A 764  ? 0.5999 0.5614 0.6129 0.0367  -0.0445 -0.1012 762  ASP A OD2 
5479  N N   . GLY A 765  ? 0.5004 0.4619 0.5041 0.0257  -0.0396 -0.0825 763  GLY A N   
5480  C CA  . GLY A 765  ? 0.4603 0.4224 0.4642 0.0233  -0.0406 -0.0815 763  GLY A CA  
5481  C C   . GLY A 765  ? 0.4590 0.4251 0.4634 0.0253  -0.0435 -0.0887 763  GLY A C   
5482  O O   . GLY A 765  ? 0.4946 0.4638 0.4968 0.0243  -0.0437 -0.0883 763  GLY A O   
5483  N N   . ARG A 766  ? 0.4712 0.4373 0.4788 0.0282  -0.0458 -0.0955 764  ARG A N   
5484  C CA  . ARG A 766  ? 0.4991 0.4703 0.5065 0.0307  -0.0485 -0.1031 764  ARG A CA  
5485  C C   . ARG A 766  ? 0.4717 0.4520 0.4695 0.0329  -0.0462 -0.1027 764  ARG A C   
5486  O O   . ARG A 766  ? 0.4083 0.3929 0.4045 0.0332  -0.0476 -0.1055 764  ARG A O   
5487  C CB  . ARG A 766  ? 0.4674 0.4379 0.4790 0.0340  -0.0511 -0.1105 764  ARG A CB  
5488  N N   . VAL A 767  ? 0.4556 0.4390 0.4475 0.0341  -0.0426 -0.0990 765  VAL A N   
5489  C CA  . VAL A 767  ? 0.4201 0.4118 0.4030 0.0357  -0.0402 -0.0974 765  VAL A CA  
5490  C C   . VAL A 767  ? 0.4061 0.3973 0.3866 0.0326  -0.0390 -0.0915 765  VAL A C   
5491  O O   . VAL A 767  ? 0.4109 0.4076 0.3872 0.0334  -0.0394 -0.0925 765  VAL A O   
5492  C CB  . VAL A 767  ? 0.4184 0.4131 0.3963 0.0375  -0.0367 -0.0945 765  VAL A CB  
5493  C CG1 . VAL A 767  ? 0.3772 0.3806 0.3461 0.0391  -0.0344 -0.0928 765  VAL A CG1 
5494  C CG2 . VAL A 767  ? 0.4199 0.4151 0.4008 0.0407  -0.0379 -0.1006 765  VAL A CG2 
5495  N N   . GLY A 768  ? 0.3921 0.3771 0.3751 0.0293  -0.0377 -0.0853 766  GLY A N   
5496  C CA  . GLY A 768  ? 0.4005 0.3850 0.3818 0.0264  -0.0367 -0.0799 766  GLY A CA  
5497  C C   . GLY A 768  ? 0.4010 0.3858 0.3857 0.0254  -0.0398 -0.0834 766  GLY A C   
5498  O O   . GLY A 768  ? 0.3696 0.3587 0.3503 0.0253  -0.0395 -0.0822 766  GLY A O   
5499  N N   . ALA A 769  ? 0.4129 0.3934 0.4052 0.0248  -0.0429 -0.0879 767  ALA A N   
5500  C CA  . ALA A 769  ? 0.4052 0.3855 0.4018 0.0234  -0.0461 -0.0912 767  ALA A CA  
5501  C C   . ALA A 769  ? 0.4283 0.4163 0.4207 0.0267  -0.0476 -0.0970 767  ALA A C   
5502  O O   . ALA A 769  ? 0.4107 0.4016 0.4023 0.0259  -0.0487 -0.0973 767  ALA A O   
5503  C CB  . ALA A 769  ? 0.3945 0.3680 0.4006 0.0220  -0.0493 -0.0946 767  ALA A CB  
5504  N N   . ALA A 770  ? 0.4026 0.3944 0.3924 0.0304  -0.0478 -0.1017 768  ALA A N   
5505  C CA  . ALA A 770  ? 0.4124 0.4124 0.3976 0.0337  -0.0491 -0.1073 768  ALA A CA  
5506  C C   . ALA A 770  ? 0.4136 0.4197 0.3903 0.0340  -0.0465 -0.1026 768  ALA A C   
5507  O O   . ALA A 770  ? 0.3938 0.4051 0.3682 0.0348  -0.0481 -0.1050 768  ALA A O   
5508  C CB  . ALA A 770  ? 0.4152 0.4187 0.3987 0.0377  -0.0491 -0.1127 768  ALA A CB  
5509  N N   . LEU A 771  ? 0.3918 0.3974 0.3641 0.0334  -0.0428 -0.0960 769  LEU A N   
5510  C CA  . LEU A 771  ? 0.3601 0.3708 0.3249 0.0335  -0.0405 -0.0910 769  LEU A CA  
5511  C C   . LEU A 771  ? 0.3767 0.3855 0.3433 0.0306  -0.0413 -0.0880 769  LEU A C   
5512  O O   . LEU A 771  ? 0.4081 0.4223 0.3705 0.0315  -0.0418 -0.0880 769  LEU A O   
5513  C CB  . LEU A 771  ? 0.3492 0.3587 0.3103 0.0331  -0.0366 -0.0845 769  LEU A CB  
5514  C CG  . LEU A 771  ? 0.3381 0.3510 0.2962 0.0361  -0.0352 -0.0867 769  LEU A CG  
5515  C CD1 . LEU A 771  ? 0.3239 0.3339 0.2802 0.0348  -0.0316 -0.0802 769  LEU A CD1 
5516  C CD2 . LEU A 771  ? 0.3501 0.3727 0.3009 0.0394  -0.0349 -0.0891 769  LEU A CD2 
5517  N N   . VAL A 772  ? 0.3436 0.3451 0.3165 0.0272  -0.0416 -0.0853 770  VAL A N   
5518  C CA  . VAL A 772  ? 0.3739 0.3739 0.3488 0.0244  -0.0420 -0.0821 770  VAL A CA  
5519  C C   . VAL A 772  ? 0.3924 0.3954 0.3698 0.0248  -0.0456 -0.0878 770  VAL A C   
5520  O O   . VAL A 772  ? 0.3799 0.3863 0.3551 0.0244  -0.0460 -0.0865 770  VAL A O   
5521  C CB  . VAL A 772  ? 0.3762 0.3682 0.3575 0.0206  -0.0415 -0.0783 770  VAL A CB  
5522  C CG1 . VAL A 772  ? 0.3933 0.3842 0.3780 0.0176  -0.0426 -0.0763 770  VAL A CG1 
5523  C CG2 . VAL A 772  ? 0.3746 0.3646 0.3524 0.0201  -0.0379 -0.0720 770  VAL A CG2 
5524  N N   . ALA A 773  ? 0.3782 0.3804 0.3604 0.0259  -0.0485 -0.0945 771  ALA A N   
5525  C CA  . ALA A 773  ? 0.3494 0.3540 0.3350 0.0261  -0.0522 -0.1003 771  ALA A CA  
5526  C C   . ALA A 773  ? 0.4546 0.4682 0.4335 0.0298  -0.0530 -0.1042 771  ALA A C   
5527  O O   . ALA A 773  ? 0.4622 0.4789 0.4428 0.0301  -0.0559 -0.1085 771  ALA A O   
5528  C CB  . ALA A 773  ? 0.3992 0.3993 0.3929 0.0259  -0.0553 -0.1064 771  ALA A CB  
5529  N N   . ALA A 774  ? 0.3979 0.4160 0.3693 0.0326  -0.0505 -0.1030 772  ALA A N   
5530  C CA  . ALA A 774  ? 0.4009 0.4280 0.3659 0.0363  -0.0513 -0.1069 772  ALA A CA  
5531  C C   . ALA A 774  ? 0.3780 0.4092 0.3398 0.0357  -0.0518 -0.1044 772  ALA A C   
5532  O O   . ALA A 774  ? 0.4012 0.4299 0.3620 0.0334  -0.0498 -0.0978 772  ALA A O   
5533  C CB  . ALA A 774  ? 0.3895 0.4210 0.3471 0.0389  -0.0482 -0.1048 772  ALA A CB  
5534  N N   . ALA A 775  ? 0.3978 0.4355 0.3582 0.0379  -0.0546 -0.1102 773  ALA A N   
5535  C CA  . ALA A 775  ? 0.3876 0.4288 0.3463 0.0373  -0.0558 -0.1086 773  ALA A CA  
5536  C C   . ALA A 775  ? 0.4044 0.4495 0.3548 0.0381  -0.0527 -0.1017 773  ALA A C   
5537  O O   . ALA A 775  ? 0.3843 0.4290 0.3343 0.0364  -0.0526 -0.0975 773  ALA A O   
5538  C CB  . ALA A 775  ? 0.4028 0.4508 0.3614 0.0398  -0.0595 -0.1164 773  ALA A CB  
5539  N N   . GLU A 776  ? 0.3907 0.4396 0.3346 0.0405  -0.0504 -0.1004 774  GLU A N   
5540  C CA  . GLU A 776  ? 0.3409 0.3936 0.2769 0.0413  -0.0478 -0.0939 774  GLU A CA  
5541  C C   . GLU A 776  ? 0.3472 0.3936 0.2833 0.0388  -0.0443 -0.0863 774  GLU A C   
5542  O O   . GLU A 776  ? 0.3561 0.4048 0.2862 0.0393  -0.0420 -0.0805 774  GLU A O   
5543  C CB  . GLU A 776  ? 0.3766 0.4376 0.3053 0.0450  -0.0470 -0.0959 774  GLU A CB  
5544  C CG  . GLU A 776  ? 0.4132 0.4824 0.3397 0.0477  -0.0503 -0.1020 774  GLU A CG  
5545  C CD  . GLU A 776  ? 0.5192 0.5960 0.4412 0.0514  -0.0504 -0.1070 774  GLU A CD  
5546  O OE1 . GLU A 776  ? 0.5947 0.6688 0.5196 0.0518  -0.0497 -0.1100 774  GLU A OE1 
5547  O OE2 . GLU A 776  ? 0.6524 0.7382 0.5681 0.0541  -0.0511 -0.1081 774  GLU A OE2 
5548  N N   . THR A 777  ? 0.3604 0.3989 0.3033 0.0362  -0.0441 -0.0860 775  THR A N   
5549  C CA  . THR A 777  ? 0.3411 0.3737 0.2845 0.0337  -0.0411 -0.0790 775  THR A CA  
5550  C C   . THR A 777  ? 0.3708 0.4023 0.3146 0.0317  -0.0411 -0.0744 775  THR A C   
5551  O O   . THR A 777  ? 0.3519 0.3819 0.3008 0.0301  -0.0435 -0.0767 775  THR A O   
5552  C CB  . THR A 777  ? 0.3367 0.3618 0.2873 0.0315  -0.0411 -0.0801 775  THR A CB  
5553  O OG1 . THR A 777  ? 0.3382 0.3646 0.2879 0.0338  -0.0408 -0.0839 775  THR A OG1 
5554  C CG2 . THR A 777  ? 0.3199 0.3390 0.2714 0.0288  -0.0382 -0.0730 775  THR A CG2 
5555  N N   . ALA A 778  ? 0.3321 0.3646 0.2705 0.0318  -0.0387 -0.0682 776  ALA A N   
5556  C CA  . ALA A 778  ? 0.3192 0.3518 0.2569 0.0307  -0.0388 -0.0641 776  ALA A CA  
5557  C C   . ALA A 778  ? 0.3202 0.3462 0.2607 0.0278  -0.0366 -0.0584 776  ALA A C   
5558  O O   . ALA A 778  ? 0.3800 0.4055 0.3211 0.0266  -0.0368 -0.0554 776  ALA A O   
5559  C CB  . ALA A 778  ? 0.3212 0.3600 0.2509 0.0331  -0.0381 -0.0611 776  ALA A CB  
5560  N N   . GLY A 779  ? 0.3165 0.3378 0.2590 0.0266  -0.0347 -0.0573 777  GLY A N   
5561  C CA  . GLY A 779  ? 0.3071 0.3226 0.2519 0.0240  -0.0326 -0.0521 777  GLY A CA  
5562  C C   . GLY A 779  ? 0.3063 0.3176 0.2533 0.0234  -0.0311 -0.0524 777  GLY A C   
5563  O O   . GLY A 779  ? 0.3091 0.3227 0.2538 0.0254  -0.0310 -0.0552 777  GLY A O   
5564  N N   . VAL A 780  ? 0.3151 0.3205 0.2666 0.0206  -0.0302 -0.0498 778  VAL A N   
5565  C CA  . VAL A 780  ? 0.3017 0.3026 0.2561 0.0197  -0.0290 -0.0498 778  VAL A CA  
5566  C C   . VAL A 780  ? 0.2972 0.2943 0.2512 0.0178  -0.0263 -0.0437 778  VAL A C   
5567  O O   . VAL A 780  ? 0.2945 0.2900 0.2506 0.0159  -0.0263 -0.0410 778  VAL A O   
5568  C CB  . VAL A 780  ? 0.3118 0.3089 0.2736 0.0180  -0.0311 -0.0536 778  VAL A CB  
5569  C CG1 . VAL A 780  ? 0.3018 0.2938 0.2664 0.0171  -0.0299 -0.0528 778  VAL A CG1 
5570  C CG2 . VAL A 780  ? 0.3076 0.3084 0.2702 0.0200  -0.0340 -0.0603 778  VAL A CG2 
5571  N N   . MET A 781  ? 0.2964 0.2926 0.2480 0.0185  -0.0242 -0.0416 779  MET A N   
5572  C CA  . MET A 781  ? 0.2924 0.2847 0.2441 0.0167  -0.0218 -0.0364 779  MET A CA  
5573  C C   . MET A 781  ? 0.2922 0.2801 0.2479 0.0158  -0.0214 -0.0374 779  MET A C   
5574  O O   . MET A 781  ? 0.2945 0.2836 0.2492 0.0176  -0.0213 -0.0400 779  MET A O   
5575  C CB  . MET A 781  ? 0.2919 0.2867 0.2374 0.0181  -0.0196 -0.0326 779  MET A CB  
5576  C CG  . MET A 781  ? 0.2929 0.2920 0.2344 0.0192  -0.0202 -0.0315 779  MET A CG  
5577  S SD  . MET A 781  ? 0.3349 0.3375 0.2691 0.0211  -0.0180 -0.0275 779  MET A SD  
5578  C CE  . MET A 781  ? 0.2890 0.2866 0.2242 0.0187  -0.0159 -0.0214 779  MET A CE  
5579  N N   . PHE A 782  ? 0.2896 0.2730 0.2503 0.0131  -0.0214 -0.0356 780  PHE A N   
5580  C CA  . PHE A 782  ? 0.2897 0.2686 0.2551 0.0120  -0.0215 -0.0364 780  PHE A CA  
5581  C C   . PHE A 782  ? 0.2868 0.2621 0.2529 0.0099  -0.0194 -0.0312 780  PHE A C   
5582  O O   . PHE A 782  ? 0.2832 0.2580 0.2500 0.0081  -0.0190 -0.0283 780  PHE A O   
5583  C CB  . PHE A 782  ? 0.2991 0.2759 0.2708 0.0105  -0.0242 -0.0398 780  PHE A CB  
5584  C CG  . PHE A 782  ? 0.2918 0.2632 0.2690 0.0089  -0.0245 -0.0398 780  PHE A CG  
5585  C CD1 . PHE A 782  ? 0.3144 0.2847 0.2932 0.0105  -0.0255 -0.0436 780  PHE A CD1 
5586  C CD2 . PHE A 782  ? 0.2963 0.2641 0.2773 0.0058  -0.0240 -0.0360 780  PHE A CD2 
5587  C CE1 . PHE A 782  ? 0.3138 0.2791 0.2980 0.0092  -0.0261 -0.0434 780  PHE A CE1 
5588  C CE2 . PHE A 782  ? 0.3333 0.2964 0.3194 0.0043  -0.0244 -0.0356 780  PHE A CE2 
5589  C CZ  . PHE A 782  ? 0.3498 0.3113 0.3376 0.0059  -0.0256 -0.0392 780  PHE A CZ  
5590  N N   . THR A 783  ? 0.3054 0.2785 0.2715 0.0102  -0.0181 -0.0302 781  THR A N   
5591  C CA  . THR A 783  ? 0.3312 0.3005 0.2991 0.0081  -0.0165 -0.0259 781  THR A CA  
5592  C C   . THR A 783  ? 0.3069 0.2723 0.2797 0.0076  -0.0174 -0.0276 781  THR A C   
5593  O O   . THR A 783  ? 0.3211 0.2869 0.2931 0.0096  -0.0175 -0.0301 781  THR A O   
5594  C CB  . THR A 783  ? 0.3417 0.3121 0.3048 0.0089  -0.0139 -0.0223 781  THR A CB  
5595  O OG1 . THR A 783  ? 0.3199 0.2937 0.2787 0.0096  -0.0134 -0.0209 781  THR A OG1 
5596  C CG2 . THR A 783  ? 0.3300 0.2968 0.2950 0.0067  -0.0125 -0.0181 781  THR A CG2 
5597  N N   . GLY A 784  ? 0.3213 0.2831 0.2991 0.0049  -0.0181 -0.0262 782  GLY A N   
5598  C CA  . GLY A 784  ? 0.3419 0.2996 0.3251 0.0042  -0.0194 -0.0275 782  GLY A CA  
5599  C C   . GLY A 784  ? 0.3369 0.2916 0.3254 0.0009  -0.0202 -0.0253 782  GLY A C   
5600  O O   . GLY A 784  ? 0.3631 0.3187 0.3505 -0.0008 -0.0190 -0.0218 782  GLY A O   
5601  N N   . SER A 785  ? 0.3528 0.3040 0.3471 0.0000  -0.0224 -0.0273 783  SER A N   
5602  C CA  . SER A 785  ? 0.3946 0.3429 0.3944 -0.0034 -0.0233 -0.0249 783  SER A CA  
5603  C C   . SER A 785  ? 0.3950 0.3458 0.3963 -0.0048 -0.0245 -0.0260 783  SER A C   
5604  O O   . SER A 785  ? 0.3742 0.3278 0.3743 -0.0031 -0.0258 -0.0301 783  SER A O   
5605  C CB  . SER A 785  ? 0.4447 0.3883 0.4508 -0.0039 -0.0255 -0.0267 783  SER A CB  
5606  O OG  . SER A 785  ? 0.4587 0.4028 0.4661 -0.0019 -0.0278 -0.0325 783  SER A OG  
5607  N N   . THR A 786  ? 0.4115 0.3618 0.4158 -0.0079 -0.0241 -0.0223 784  THR A N   
5608  C CA  . THR A 786  ? 0.4240 0.3769 0.4306 -0.0095 -0.0253 -0.0232 784  THR A CA  
5609  C C   . THR A 786  ? 0.3912 0.3425 0.4032 -0.0098 -0.0286 -0.0278 784  THR A C   
5610  O O   . THR A 786  ? 0.4007 0.3551 0.4132 -0.0096 -0.0300 -0.0307 784  THR A O   
5611  C CB  . THR A 786  ? 0.4536 0.4065 0.4632 -0.0130 -0.0244 -0.0185 784  THR A CB  
5612  O OG1 . THR A 786  ? 0.5611 0.5096 0.5765 -0.0153 -0.0255 -0.0170 784  THR A OG1 
5613  C CG2 . THR A 786  ? 0.4105 0.3651 0.4152 -0.0128 -0.0214 -0.0143 784  THR A CG2 
5614  N N   . GLU A 787  ? 0.4218 0.3685 0.4385 -0.0103 -0.0300 -0.0286 785  GLU A N   
5615  C CA  . GLU A 787  ? 0.4495 0.3940 0.4723 -0.0108 -0.0334 -0.0329 785  GLU A CA  
5616  C C   . GLU A 787  ? 0.3920 0.3391 0.4120 -0.0073 -0.0348 -0.0391 785  GLU A C   
5617  O O   . GLU A 787  ? 0.3900 0.3388 0.4124 -0.0074 -0.0370 -0.0429 785  GLU A O   
5618  C CB  . GLU A 787  ? 0.4743 0.4128 0.5029 -0.0119 -0.0348 -0.0322 785  GLU A CB  
5619  C CG  . GLU A 787  ? 0.5517 0.4882 0.5769 -0.0095 -0.0333 -0.0315 785  GLU A CG  
5620  C CD  . GLU A 787  ? 0.6459 0.5764 0.6770 -0.0109 -0.0346 -0.0298 785  GLU A CD  
5621  O OE1 . GLU A 787  ? 0.6925 0.6209 0.7283 -0.0144 -0.0349 -0.0258 785  GLU A OE1 
5622  O OE2 . GLU A 787  ? 0.6683 0.5964 0.6995 -0.0084 -0.0353 -0.0325 785  GLU A OE2 
5623  N N   . VAL A 788  ? 0.4070 0.3550 0.4216 -0.0041 -0.0334 -0.0402 786  VAL A N   
5624  C CA  . VAL A 788  ? 0.3812 0.3326 0.3923 -0.0006 -0.0344 -0.0457 786  VAL A CA  
5625  C C   . VAL A 788  ? 0.3438 0.3008 0.3502 -0.0001 -0.0336 -0.0457 786  VAL A C   
5626  O O   . VAL A 788  ? 0.3660 0.3261 0.3720 0.0014  -0.0355 -0.0504 786  VAL A O   
5627  C CB  . VAL A 788  ? 0.4374 0.3890 0.4439 0.0025  -0.0328 -0.0463 786  VAL A CB  
5628  C CG1 . VAL A 788  ? 0.3836 0.3403 0.3853 0.0061  -0.0332 -0.0512 786  VAL A CG1 
5629  C CG2 . VAL A 788  ? 0.5134 0.4597 0.5252 0.0025  -0.0342 -0.0476 786  VAL A CG2 
5630  N N   . ALA A 789  ? 0.3460 0.3046 0.3487 -0.0011 -0.0310 -0.0406 787  ALA A N   
5631  C CA  . ALA A 789  ? 0.3323 0.2958 0.3311 -0.0007 -0.0305 -0.0403 787  ALA A CA  
5632  C C   . ALA A 789  ? 0.3117 0.2762 0.3156 -0.0026 -0.0329 -0.0425 787  ALA A C   
5633  O O   . ALA A 789  ? 0.3253 0.2940 0.3273 -0.0013 -0.0340 -0.0454 787  ALA A O   
5634  C CB  . ALA A 789  ? 0.3535 0.3177 0.3489 -0.0018 -0.0275 -0.0346 787  ALA A CB  
5635  N N   . ARG A 790  ? 0.3431 0.3040 0.3538 -0.0059 -0.0339 -0.0409 788  ARG A N   
5636  C CA  . ARG A 790  ? 0.3829 0.3449 0.3991 -0.0081 -0.0362 -0.0428 788  ARG A CA  
5637  C C   . ARG A 790  ? 0.3478 0.3097 0.3667 -0.0065 -0.0395 -0.0494 788  ARG A C   
5638  O O   . ARG A 790  ? 0.3824 0.3475 0.4029 -0.0067 -0.0414 -0.0524 788  ARG A O   
5639  C CB  . ARG A 790  ? 0.4007 0.3589 0.4236 -0.0121 -0.0363 -0.0390 788  ARG A CB  
5640  C CG  . ARG A 790  ? 0.4924 0.4525 0.5210 -0.0151 -0.0380 -0.0393 788  ARG A CG  
5641  C CD  . ARG A 790  ? 0.4628 0.4196 0.4976 -0.0192 -0.0378 -0.0348 788  ARG A CD  
5642  N NE  . ARG A 790  ? 0.4951 0.4525 0.5262 -0.0200 -0.0345 -0.0290 788  ARG A NE  
5643  C CZ  . ARG A 790  ? 0.5480 0.5097 0.5773 -0.0211 -0.0328 -0.0261 788  ARG A CZ  
5644  N NH1 . ARG A 790  ? 0.5354 0.5013 0.5661 -0.0216 -0.0339 -0.0281 788  ARG A NH1 
5645  N NH2 . ARG A 790  ? 0.5878 0.5498 0.6141 -0.0216 -0.0300 -0.0213 788  ARG A NH2 
5646  N N   . LEU A 791  ? 0.3438 0.3024 0.3634 -0.0048 -0.0403 -0.0519 789  LEU A N   
5647  C CA  . LEU A 791  ? 0.3814 0.3404 0.4032 -0.0028 -0.0434 -0.0588 789  LEU A CA  
5648  C C   . LEU A 791  ? 0.3546 0.3198 0.3695 0.0007  -0.0432 -0.0621 789  LEU A C   
5649  O O   . LEU A 791  ? 0.3605 0.3283 0.3769 0.0017  -0.0459 -0.0674 789  LEU A O   
5650  C CB  . LEU A 791  ? 0.4007 0.3552 0.4247 -0.0014 -0.0442 -0.0608 789  LEU A CB  
5651  C CG  . LEU A 791  ? 0.4477 0.3955 0.4798 -0.0045 -0.0455 -0.0589 789  LEU A CG  
5652  C CD1 . LEU A 791  ? 0.4807 0.4245 0.5134 -0.0025 -0.0456 -0.0601 789  LEU A CD1 
5653  C CD2 . LEU A 791  ? 0.4409 0.3875 0.4809 -0.0064 -0.0494 -0.0629 789  LEU A CD2 
5654  N N   . ILE A 792  ? 0.3276 0.2953 0.3350 0.0026  -0.0402 -0.0591 790  ILE A N   
5655  C CA  . ILE A 792  ? 0.3477 0.3214 0.3483 0.0057  -0.0399 -0.0613 790  ILE A CA  
5656  C C   . ILE A 792  ? 0.3357 0.3132 0.3363 0.0045  -0.0406 -0.0608 790  ILE A C   
5657  O O   . ILE A 792  ? 0.3163 0.2981 0.3155 0.0063  -0.0425 -0.0651 790  ILE A O   
5658  C CB  . ILE A 792  ? 0.3371 0.3122 0.3304 0.0075  -0.0365 -0.0575 790  ILE A CB  
5659  C CG1 . ILE A 792  ? 0.3579 0.3308 0.3508 0.0095  -0.0362 -0.0595 790  ILE A CG1 
5660  C CG2 . ILE A 792  ? 0.3041 0.2855 0.2904 0.0100  -0.0359 -0.0580 790  ILE A CG2 
5661  C CD1 . ILE A 792  ? 0.3371 0.3100 0.3244 0.0104  -0.0328 -0.0550 790  ILE A CD1 
5662  N N   . GLN A 793  ? 0.3125 0.2888 0.3147 0.0016  -0.0392 -0.0558 791  GLN A N   
5663  C CA  . GLN A 793  ? 0.3287 0.3086 0.3316 0.0004  -0.0398 -0.0552 791  GLN A CA  
5664  C C   . GLN A 793  ? 0.3401 0.3209 0.3490 -0.0004 -0.0434 -0.0604 791  GLN A C   
5665  O O   . GLN A 793  ? 0.3428 0.3283 0.3503 0.0006  -0.0448 -0.0629 791  GLN A O   
5666  C CB  . GLN A 793  ? 0.3591 0.3374 0.3643 -0.0028 -0.0379 -0.0495 791  GLN A CB  
5667  C CG  . GLN A 793  ? 0.4021 0.3837 0.4101 -0.0047 -0.0388 -0.0490 791  GLN A CG  
5668  C CD  . GLN A 793  ? 0.4991 0.4786 0.5117 -0.0085 -0.0375 -0.0443 791  GLN A CD  
5669  O OE1 . GLN A 793  ? 0.5019 0.4769 0.5191 -0.0106 -0.0376 -0.0432 791  GLN A OE1 
5670  N NE2 . GLN A 793  ? 0.4902 0.4733 0.5016 -0.0093 -0.0363 -0.0415 791  GLN A NE2 
5671  N N   . ALA A 794  ? 0.3778 0.3538 0.3936 -0.0024 -0.0451 -0.0620 792  ALA A N   
5672  C CA  . ALA A 794  ? 0.3753 0.3516 0.3978 -0.0035 -0.0488 -0.0669 792  ALA A CA  
5673  C C   . ALA A 794  ? 0.3939 0.3736 0.4134 0.0002  -0.0510 -0.0736 792  ALA A C   
5674  O O   . ALA A 794  ? 0.3823 0.3654 0.4041 0.0003  -0.0536 -0.0776 792  ALA A O   
5675  C CB  . ALA A 794  ? 0.4259 0.3958 0.4566 -0.0063 -0.0503 -0.0669 792  ALA A CB  
5676  N N   . GLN A 795  ? 0.3860 0.3654 0.4007 0.0033  -0.0500 -0.0749 793  GLN A N   
5677  C CA  . GLN A 795  ? 0.3813 0.3650 0.3926 0.0071  -0.0518 -0.0812 793  GLN A CA  
5678  C C   . GLN A 795  ? 0.4049 0.3955 0.4093 0.0090  -0.0511 -0.0807 793  GLN A C   
5679  O O   . GLN A 795  ? 0.4227 0.4178 0.4264 0.0109  -0.0535 -0.0858 793  GLN A O   
5680  C CB  . GLN A 795  ? 0.4490 0.4314 0.4567 0.0099  -0.0506 -0.0823 793  GLN A CB  
5681  C CG  . GLN A 795  ? 0.5107 0.4869 0.5253 0.0091  -0.0523 -0.0848 793  GLN A CG  
5682  C CD  . GLN A 795  ? 0.6022 0.5783 0.6233 0.0090  -0.0567 -0.0918 793  GLN A CD  
5683  O OE1 . GLN A 795  ? 0.5608 0.5421 0.5792 0.0119  -0.0584 -0.0973 793  GLN A OE1 
5684  N NE2 . GLN A 795  ? 0.5485 0.5188 0.5785 0.0056  -0.0585 -0.0914 793  GLN A NE2 
5685  N N   . LEU A 796  ? 0.3577 0.3491 0.3573 0.0087  -0.0479 -0.0746 794  LEU A N   
5686  C CA  . LEU A 796  ? 0.3681 0.3656 0.3611 0.0106  -0.0472 -0.0736 794  LEU A CA  
5687  C C   . LEU A 796  ? 0.4201 0.4202 0.4166 0.0088  -0.0490 -0.0742 794  LEU A C   
5688  O O   . LEU A 796  ? 0.4485 0.4543 0.4410 0.0108  -0.0499 -0.0756 794  LEU A O   
5689  C CB  . LEU A 796  ? 0.3635 0.3606 0.3508 0.0107  -0.0435 -0.0671 794  LEU A CB  
5690  C CG  . LEU A 796  ? 0.3382 0.3343 0.3206 0.0129  -0.0413 -0.0661 794  LEU A CG  
5691  C CD1 . LEU A 796  ? 0.3507 0.3468 0.3278 0.0128  -0.0380 -0.0597 794  LEU A CD1 
5692  C CD2 . LEU A 796  ? 0.4006 0.4017 0.3785 0.0166  -0.0426 -0.0711 794  LEU A CD2 
5693  N N   . ALA A 797  ? 0.3605 0.3570 0.3643 0.0051  -0.0496 -0.0727 795  ALA A N   
5694  C CA  . ALA A 797  ? 0.4238 0.4233 0.4313 0.0032  -0.0511 -0.0729 795  ALA A CA  
5695  C C   . ALA A 797  ? 0.4354 0.4383 0.4454 0.0044  -0.0549 -0.0797 795  ALA A C   
5696  O O   . ALA A 797  ? 0.4863 0.4935 0.4977 0.0039  -0.0564 -0.0806 795  ALA A O   
5697  C CB  . ALA A 797  ? 0.3690 0.3643 0.3840 -0.0012 -0.0508 -0.0697 795  ALA A CB  
5698  N N   . ASP A 798  ? 0.4028 0.4044 0.4136 0.0061  -0.0567 -0.0847 796  ASP A N   
5699  C CA  . ASP A 798  ? 0.4393 0.4445 0.4522 0.0076  -0.0604 -0.0919 796  ASP A CA  
5700  C C   . ASP A 798  ? 0.4727 0.4850 0.4773 0.0116  -0.0606 -0.0939 796  ASP A C   
5701  O O   . ASP A 798  ? 0.4190 0.4356 0.4246 0.0129  -0.0638 -0.0995 796  ASP A O   
5702  C CB  . ASP A 798  ? 0.4129 0.4140 0.4294 0.0083  -0.0622 -0.0967 796  ASP A CB  
5703  C CG  . ASP A 798  ? 0.5356 0.5390 0.5570 0.0089  -0.0666 -0.1044 796  ASP A CG  
5704  O OD1 . ASP A 798  ? 0.5708 0.5741 0.5989 0.0059  -0.0687 -0.1050 796  ASP A OD1 
5705  O OD2 . ASP A 798  ? 0.5910 0.5966 0.6098 0.0123  -0.0681 -0.1100 796  ASP A OD2 
5706  N N   . ARG A 799  ? 0.4306 0.4445 0.4274 0.0134  -0.0575 -0.0893 797  ARG A N   
5707  C CA  . ARG A 799  ? 0.4649 0.4853 0.4535 0.0173  -0.0574 -0.0907 797  ARG A CA  
5708  C C   . ARG A 799  ? 0.4038 0.4275 0.3877 0.0175  -0.0558 -0.0855 797  ARG A C   
5709  O O   . ARG A 799  ? 0.4035 0.4240 0.3887 0.0151  -0.0536 -0.0801 797  ARG A O   
5710  C CB  . ARG A 799  ? 0.5222 0.5420 0.5050 0.0200  -0.0554 -0.0905 797  ARG A CB  
5711  C CG  . ARG A 799  ? 0.5243 0.5403 0.5117 0.0200  -0.0567 -0.0952 797  ARG A CG  
5712  C CD  . ARG A 799  ? 0.4914 0.5107 0.4726 0.0240  -0.0561 -0.0981 797  ARG A CD  
5713  N NE  . ARG A 799  ? 0.5631 0.5800 0.5401 0.0243  -0.0524 -0.0930 797  ARG A NE  
5714  C CZ  . ARG A 799  ? 0.4921 0.5123 0.4614 0.0257  -0.0498 -0.0883 797  ARG A CZ  
5715  N NH1 . ARG A 799  ? 0.4842 0.5104 0.4490 0.0271  -0.0504 -0.0879 797  ARG A NH1 
5716  N NH2 . ARG A 799  ? 0.4107 0.4282 0.3772 0.0257  -0.0466 -0.0839 797  ARG A NH2 
5717  N N   . LEU A 800  ? 0.3981 0.4283 0.3764 0.0205  -0.0569 -0.0874 798  LEU A N   
5718  C CA  . LEU A 800  ? 0.3926 0.4264 0.3656 0.0214  -0.0556 -0.0827 798  LEU A CA  
5719  C C   . LEU A 800  ? 0.4007 0.4388 0.3646 0.0252  -0.0545 -0.0820 798  LEU A C   
5720  O O   . LEU A 800  ? 0.3607 0.4014 0.3225 0.0274  -0.0556 -0.0865 798  LEU A O   
5721  C CB  . LEU A 800  ? 0.4108 0.4492 0.3863 0.0212  -0.0585 -0.0850 798  LEU A CB  
5722  C CG  . LEU A 800  ? 0.4123 0.4477 0.3963 0.0173  -0.0592 -0.0843 798  LEU A CG  
5723  C CD1 . LEU A 800  ? 0.4053 0.4464 0.3915 0.0176  -0.0622 -0.0872 798  LEU A CD1 
5724  C CD2 . LEU A 800  ? 0.4008 0.4326 0.3847 0.0154  -0.0559 -0.0773 798  LEU A CD2 
5725  N N   . SER A 801  ? 0.4025 0.4416 0.3612 0.0258  -0.0524 -0.0762 799  SER A N   
5726  C CA  . SER A 801  ? 0.4389 0.4822 0.3891 0.0290  -0.0512 -0.0744 799  SER A CA  
5727  C C   . SER A 801  ? 0.5434 0.5943 0.4906 0.0317  -0.0542 -0.0783 799  SER A C   
5728  O O   . SER A 801  ? 0.4930 0.5456 0.4448 0.0309  -0.0569 -0.0816 799  SER A O   
5729  C CB  . SER A 801  ? 0.4812 0.5230 0.4276 0.0287  -0.0485 -0.0669 799  SER A CB  
5730  O OG  . SER A 801  ? 0.5029 0.5473 0.4496 0.0287  -0.0498 -0.0655 799  SER A OG  
5731  N N   . PRO A 802  ? 0.5685 0.6247 0.5081 0.0348  -0.0538 -0.0781 800  PRO A N   
5732  C CA  . PRO A 802  ? 0.5455 0.6095 0.4813 0.0375  -0.0565 -0.0809 800  PRO A CA  
5733  C C   . PRO A 802  ? 0.5538 0.6192 0.4905 0.0370  -0.0576 -0.0780 800  PRO A C   
5734  O O   . PRO A 802  ? 0.6417 0.7123 0.5788 0.0382  -0.0607 -0.0818 800  PRO A O   
5735  C CB  . PRO A 802  ? 0.5719 0.6405 0.4989 0.0404  -0.0548 -0.0785 800  PRO A CB  
5736  C CG  . PRO A 802  ? 0.5920 0.6561 0.5196 0.0397  -0.0523 -0.0783 800  PRO A CG  
5737  C CD  . PRO A 802  ? 0.5268 0.5825 0.4612 0.0361  -0.0510 -0.0758 800  PRO A CD  
5738  N N   . ALA A 803  ? 0.5321 0.5931 0.4691 0.0353  -0.0553 -0.0717 801  ALA A N   
5739  C CA  . ALA A 803  ? 0.5330 0.5950 0.4713 0.0349  -0.0563 -0.0690 801  ALA A CA  
5740  C C   . ALA A 803  ? 0.5797 0.6384 0.5268 0.0318  -0.0573 -0.0709 801  ALA A C   
5741  O O   . ALA A 803  ? 0.5705 0.6300 0.5195 0.0312  -0.0581 -0.0690 801  ALA A O   
5742  C CB  . ALA A 803  ? 0.5532 0.6125 0.4877 0.0349  -0.0535 -0.0614 801  ALA A CB  
5743  N N   . GLY A 804  ? 0.5504 0.6055 0.5029 0.0298  -0.0575 -0.0747 802  GLY A N   
5744  C CA  . GLY A 804  ? 0.4572 0.5095 0.4183 0.0266  -0.0586 -0.0764 802  GLY A CA  
5745  C C   . GLY A 804  ? 0.4563 0.5024 0.4208 0.0236  -0.0558 -0.0714 802  GLY A C   
5746  O O   . GLY A 804  ? 0.4534 0.4984 0.4244 0.0210  -0.0565 -0.0715 802  GLY A O   
5747  N N   . ARG A 805  ? 0.4422 0.4847 0.4028 0.0238  -0.0528 -0.0672 803  ARG A N   
5748  C CA  . ARG A 805  ? 0.4431 0.4799 0.4064 0.0212  -0.0500 -0.0625 803  ARG A CA  
5749  C C   . ARG A 805  ? 0.3883 0.4199 0.3547 0.0194  -0.0488 -0.0636 803  ARG A C   
5750  O O   . ARG A 805  ? 0.3948 0.4269 0.3595 0.0208  -0.0495 -0.0671 803  ARG A O   
5751  C CB  . ARG A 805  ? 0.4535 0.4896 0.4105 0.0226  -0.0475 -0.0566 803  ARG A CB  
5752  C CG  . ARG A 805  ? 0.4972 0.5378 0.4511 0.0245  -0.0486 -0.0547 803  ARG A CG  
5753  C CD  . ARG A 805  ? 0.4986 0.5368 0.4493 0.0248  -0.0461 -0.0484 803  ARG A CD  
5754  N NE  . ARG A 805  ? 0.6444 0.6869 0.5922 0.0269  -0.0476 -0.0468 803  ARG A NE  
5755  C CZ  . ARG A 805  ? 0.6988 0.7450 0.6401 0.0298  -0.0483 -0.0460 803  ARG A CZ  
5756  N NH1 . ARG A 805  ? 0.6631 0.7097 0.5999 0.0310  -0.0474 -0.0464 803  ARG A NH1 
5757  N NH2 . ARG A 805  ? 0.6827 0.7327 0.6222 0.0317  -0.0501 -0.0447 803  ARG A NH2 
5758  N N   . PRO A 806  ? 0.3538 0.3805 0.3249 0.0163  -0.0471 -0.0608 804  PRO A N   
5759  C CA  . PRO A 806  ? 0.3841 0.4054 0.3577 0.0147  -0.0458 -0.0610 804  PRO A CA  
5760  C C   . PRO A 806  ? 0.4139 0.4342 0.3809 0.0169  -0.0436 -0.0590 804  PRO A C   
5761  O O   . PRO A 806  ? 0.3493 0.3713 0.3105 0.0186  -0.0422 -0.0553 804  PRO A O   
5762  C CB  . PRO A 806  ? 0.3645 0.3819 0.3427 0.0115  -0.0440 -0.0568 804  PRO A CB  
5763  C CG  . PRO A 806  ? 0.4018 0.4229 0.3829 0.0107  -0.0456 -0.0571 804  PRO A CG  
5764  C CD  . PRO A 806  ? 0.3995 0.4259 0.3744 0.0142  -0.0467 -0.0578 804  PRO A CD  
5765  N N   . ILE A 807  ? 0.3656 0.3832 0.3339 0.0168  -0.0435 -0.0615 805  ILE A N   
5766  C CA  . ILE A 807  ? 0.3751 0.3915 0.3382 0.0185  -0.0413 -0.0597 805  ILE A CA  
5767  C C   . ILE A 807  ? 0.3485 0.3601 0.3119 0.0165  -0.0383 -0.0539 805  ILE A C   
5768  O O   . ILE A 807  ? 0.3379 0.3450 0.3070 0.0138  -0.0379 -0.0533 805  ILE A O   
5769  C CB  . ILE A 807  ? 0.3370 0.3521 0.3020 0.0191  -0.0422 -0.0645 805  ILE A CB  
5770  C CG1 . ILE A 807  ? 0.4054 0.4253 0.3711 0.0208  -0.0456 -0.0710 805  ILE A CG1 
5771  C CG2 . ILE A 807  ? 0.3295 0.3451 0.2885 0.0213  -0.0400 -0.0629 805  ILE A CG2 
5772  C CD1 . ILE A 807  ? 0.4001 0.4268 0.3585 0.0240  -0.0460 -0.0712 805  ILE A CD1 
5773  N N   . PRO A 808  ? 0.3656 0.3780 0.3231 0.0178  -0.0361 -0.0495 806  PRO A N   
5774  C CA  . PRO A 808  ? 0.3485 0.3565 0.3064 0.0161  -0.0334 -0.0443 806  PRO A CA  
5775  C C   . PRO A 808  ? 0.3225 0.3261 0.2821 0.0151  -0.0320 -0.0444 806  PRO A C   
5776  O O   . PRO A 808  ? 0.3084 0.3130 0.2654 0.0169  -0.0319 -0.0466 806  PRO A O   
5777  C CB  . PRO A 808  ? 0.3379 0.3481 0.2889 0.0181  -0.0319 -0.0404 806  PRO A CB  
5778  C CG  . PRO A 808  ? 0.3764 0.3924 0.3246 0.0203  -0.0341 -0.0427 806  PRO A CG  
5779  C CD  . PRO A 808  ? 0.3564 0.3740 0.3073 0.0207  -0.0363 -0.0489 806  PRO A CD  
5780  N N   . LEU A 809  ? 0.3572 0.3563 0.3212 0.0124  -0.0309 -0.0420 807  LEU A N   
5781  C CA  . LEU A 809  ? 0.3032 0.2978 0.2690 0.0113  -0.0294 -0.0411 807  LEU A CA  
5782  C C   . LEU A 809  ? 0.2963 0.2882 0.2608 0.0101  -0.0267 -0.0355 807  LEU A C   
5783  O O   . LEU A 809  ? 0.2851 0.2766 0.2522 0.0082  -0.0266 -0.0333 807  LEU A O   
5784  C CB  . LEU A 809  ? 0.3465 0.3380 0.3196 0.0090  -0.0310 -0.0437 807  LEU A CB  
5785  C CG  . LEU A 809  ? 0.3150 0.3011 0.2910 0.0073  -0.0295 -0.0417 807  LEU A CG  
5786  C CD1 . LEU A 809  ? 0.3166 0.3019 0.2905 0.0093  -0.0293 -0.0440 807  LEU A CD1 
5787  C CD2 . LEU A 809  ? 0.3748 0.3581 0.3583 0.0043  -0.0311 -0.0429 807  LEU A CD2 
5788  N N   . ILE A 810  ? 0.2896 0.2804 0.2504 0.0111  -0.0247 -0.0333 808  ILE A N   
5789  C CA  . ILE A 810  ? 0.3097 0.2975 0.2698 0.0099  -0.0223 -0.0285 808  ILE A CA  
5790  C C   . ILE A 810  ? 0.2899 0.2736 0.2534 0.0086  -0.0216 -0.0288 808  ILE A C   
5791  O O   . ILE A 810  ? 0.3142 0.2978 0.2759 0.0101  -0.0213 -0.0303 808  ILE A O   
5792  C CB  . ILE A 810  ? 0.3020 0.2914 0.2559 0.0118  -0.0205 -0.0255 808  ILE A CB  
5793  C CG1 . ILE A 810  ? 0.3311 0.3246 0.2813 0.0134  -0.0215 -0.0253 808  ILE A CG1 
5794  C CG2 . ILE A 810  ? 0.3210 0.3072 0.2749 0.0103  -0.0183 -0.0209 808  ILE A CG2 
5795  C CD1 . ILE A 810  ? 0.3457 0.3405 0.2903 0.0150  -0.0198 -0.0219 808  ILE A CD1 
5796  N N   . ALA A 811  ? 0.3400 0.3207 0.3082 0.0059  -0.0214 -0.0272 809  ALA A N   
5797  C CA  . ALA A 811  ? 0.3138 0.2903 0.2860 0.0044  -0.0212 -0.0272 809  ALA A CA  
5798  C C   . ALA A 811  ? 0.3156 0.2896 0.2879 0.0027  -0.0190 -0.0224 809  ALA A C   
5799  O O   . ALA A 811  ? 0.3417 0.3162 0.3157 0.0010  -0.0187 -0.0203 809  ALA A O   
5800  C CB  . ALA A 811  ? 0.3370 0.3123 0.3156 0.0025  -0.0234 -0.0299 809  ALA A CB  
5801  N N   . GLU A 812  ? 0.3108 0.2827 0.2814 0.0032  -0.0174 -0.0210 810  GLU A N   
5802  C CA  . GLU A 812  ? 0.3426 0.3121 0.3133 0.0018  -0.0154 -0.0167 810  GLU A CA  
5803  C C   . GLU A 812  ? 0.3386 0.3043 0.3138 0.0003  -0.0157 -0.0169 810  GLU A C   
5804  O O   . GLU A 812  ? 0.3127 0.2772 0.2880 0.0016  -0.0162 -0.0192 810  GLU A O   
5805  C CB  . GLU A 812  ? 0.3728 0.3431 0.3382 0.0035  -0.0135 -0.0146 810  GLU A CB  
5806  N N   . THR A 813  ? 0.3585 0.3225 0.3376 -0.0023 -0.0156 -0.0146 811  THR A N   
5807  C CA  . THR A 813  ? 0.3426 0.3031 0.3268 -0.0040 -0.0164 -0.0147 811  THR A CA  
5808  C C   . THR A 813  ? 0.3573 0.3158 0.3420 -0.0057 -0.0146 -0.0103 811  THR A C   
5809  O O   . THR A 813  ? 0.3729 0.3325 0.3536 -0.0051 -0.0127 -0.0079 811  THR A O   
5810  C CB  . THR A 813  ? 0.4300 0.3906 0.4195 -0.0058 -0.0186 -0.0167 811  THR A CB  
5811  O OG1 . THR A 813  ? 0.3900 0.3534 0.3794 -0.0072 -0.0181 -0.0148 811  THR A OG1 
5812  C CG2 . THR A 813  ? 0.3948 0.3568 0.3842 -0.0039 -0.0207 -0.0218 811  THR A CG2 
5813  N N   . GLY A 814  ? 0.4244 0.3799 0.4139 -0.0078 -0.0152 -0.0092 812  GLY A N   
5814  C CA  . GLY A 814  ? 0.4619 0.4157 0.4517 -0.0090 -0.0137 -0.0053 812  GLY A CA  
5815  C C   . GLY A 814  ? 0.4777 0.4339 0.4668 -0.0107 -0.0123 -0.0019 812  GLY A C   
5816  O O   . GLY A 814  ? 0.4438 0.4031 0.4318 -0.0107 -0.0123 -0.0025 812  GLY A O   
5817  N N   . GLY A 815  ? 0.3378 0.2928 0.3275 -0.0121 -0.0110 0.0016  813  GLY A N   
5818  C CA  . GLY A 815  ? 0.3917 0.3489 0.3818 -0.0140 -0.0099 0.0047  813  GLY A CA  
5819  C C   . GLY A 815  ? 0.3580 0.3133 0.3510 -0.0161 -0.0095 0.0081  813  GLY A C   
5820  O O   . GLY A 815  ? 0.3915 0.3435 0.3849 -0.0155 -0.0097 0.0083  813  GLY A O   
5821  N N   . GLN A 816  ? 0.3311 0.2887 0.3260 -0.0185 -0.0090 0.0106  814  GLN A N   
5822  C CA  . GLN A 816  ? 0.3325 0.2895 0.3295 -0.0205 -0.0084 0.0145  814  GLN A CA  
5823  C C   . GLN A 816  ? 0.3033 0.2634 0.2965 -0.0202 -0.0063 0.0167  814  GLN A C   
5824  O O   . GLN A 816  ? 0.3023 0.2661 0.2962 -0.0218 -0.0055 0.0186  814  GLN A O   
5825  C CB  . GLN A 816  ? 0.3641 0.3220 0.3663 -0.0237 -0.0094 0.0161  814  GLN A CB  
5826  C CG  . GLN A 816  ? 0.3672 0.3238 0.3722 -0.0259 -0.0092 0.0202  814  GLN A CG  
5827  C CD  . GLN A 816  ? 0.4989 0.4499 0.5063 -0.0255 -0.0108 0.0197  814  GLN A CD  
5828  O OE1 . GLN A 816  ? 0.4561 0.4048 0.4607 -0.0233 -0.0103 0.0191  814  GLN A OE1 
5829  N NE2 . GLN A 816  ? 0.4765 0.4252 0.4896 -0.0275 -0.0127 0.0199  814  GLN A NE2 
5830  N N   . ASN A 817  ? 0.3230 0.2818 0.3121 -0.0179 -0.0054 0.0162  815  ASN A N   
5831  C CA  . ASN A 817  ? 0.2553 0.2169 0.2404 -0.0169 -0.0037 0.0170  815  ASN A CA  
5832  C C   . ASN A 817  ? 0.2785 0.2414 0.2639 -0.0184 -0.0026 0.0205  815  ASN A C   
5833  O O   . ASN A 817  ? 0.3053 0.2658 0.2921 -0.0190 -0.0027 0.0223  815  ASN A O   
5834  C CB  . ASN A 817  ? 0.2546 0.2146 0.2359 -0.0143 -0.0033 0.0155  815  ASN A CB  
5835  C CG  . ASN A 817  ? 0.2872 0.2460 0.2682 -0.0128 -0.0045 0.0121  815  ASN A CG  
5836  O OD1 . ASN A 817  ? 0.2762 0.2371 0.2576 -0.0128 -0.0051 0.0106  815  ASN A OD1 
5837  N ND2 . ASN A 817  ? 0.2693 0.2253 0.2498 -0.0114 -0.0049 0.0109  815  ASN A ND2 
5838  N N   . ALA A 818  ? 0.2752 0.2423 0.2594 -0.0187 -0.0015 0.0213  816  ALA A N   
5839  C CA  . ALA A 818  ? 0.2801 0.2497 0.2644 -0.0201 -0.0004 0.0243  816  ALA A CA  
5840  C C   . ALA A 818  ? 0.2491 0.2204 0.2295 -0.0185 0.0009  0.0242  816  ALA A C   
5841  O O   . ALA A 818  ? 0.2625 0.2340 0.2406 -0.0166 0.0009  0.0220  816  ALA A O   
5842  C CB  . ALA A 818  ? 0.3054 0.2795 0.2925 -0.0224 -0.0004 0.0256  816  ALA A CB  
5843  N N   . MET A 819  ? 0.2486 0.2212 0.2285 -0.0192 0.0017  0.0266  817  MET A N   
5844  C CA  . MET A 819  ? 0.2489 0.2239 0.2259 -0.0181 0.0028  0.0266  817  MET A CA  
5845  C C   . MET A 819  ? 0.2464 0.2264 0.2244 -0.0198 0.0036  0.0288  817  MET A C   
5846  O O   . MET A 819  ? 0.3035 0.2835 0.2835 -0.0217 0.0035  0.0315  817  MET A O   
5847  C CB  . MET A 819  ? 0.2464 0.2182 0.2214 -0.0169 0.0031  0.0271  817  MET A CB  
5848  C CG  . MET A 819  ? 0.3043 0.2783 0.2766 -0.0157 0.0040  0.0268  817  MET A CG  
5849  S SD  . MET A 819  ? 0.3354 0.3062 0.3060 -0.0147 0.0044  0.0277  817  MET A SD  
5850  C CE  . MET A 819  ? 0.3145 0.2812 0.2838 -0.0128 0.0039  0.0253  817  MET A CE  
5851  N N   . ILE A 820  ? 0.2511 0.2355 0.2278 -0.0192 0.0042  0.0278  818  ILE A N   
5852  C CA  . ILE A 820  ? 0.2531 0.2432 0.2302 -0.0204 0.0051  0.0294  818  ILE A CA  
5853  C C   . ILE A 820  ? 0.2469 0.2381 0.2212 -0.0190 0.0058  0.0292  818  ILE A C   
5854  O O   . ILE A 820  ? 0.2425 0.2325 0.2148 -0.0170 0.0058  0.0268  818  ILE A O   
5855  C CB  . ILE A 820  ? 0.2776 0.2730 0.2560 -0.0208 0.0053  0.0281  818  ILE A CB  
5856  C CG1 . ILE A 820  ? 0.2774 0.2718 0.2590 -0.0225 0.0045  0.0284  818  ILE A CG1 
5857  C CG2 . ILE A 820  ? 0.2674 0.2696 0.2458 -0.0219 0.0064  0.0296  818  ILE A CG2 
5858  C CD1 . ILE A 820  ? 0.3000 0.3002 0.2835 -0.0232 0.0046  0.0275  818  ILE A CD1 
5859  N N   . VAL A 821  ? 0.2441 0.2375 0.2183 -0.0201 0.0064  0.0317  819  VAL A N   
5860  C CA  . VAL A 821  ? 0.2765 0.2711 0.2482 -0.0190 0.0069  0.0316  819  VAL A CA  
5861  C C   . VAL A 821  ? 0.2860 0.2879 0.2578 -0.0200 0.0077  0.0328  819  VAL A C   
5862  O O   . VAL A 821  ? 0.2705 0.2748 0.2439 -0.0222 0.0079  0.0358  819  VAL A O   
5863  C CB  . VAL A 821  ? 0.2871 0.2776 0.2585 -0.0191 0.0067  0.0336  819  VAL A CB  
5864  C CG1 . VAL A 821  ? 0.2484 0.2410 0.2176 -0.0182 0.0071  0.0335  819  VAL A CG1 
5865  C CG2 . VAL A 821  ? 0.2677 0.2517 0.2389 -0.0179 0.0060  0.0322  819  VAL A CG2 
5866  N N   . ASP A 822  ? 0.2840 0.2897 0.2542 -0.0185 0.0081  0.0304  820  ASP A N   
5867  C CA  . ASP A 822  ? 0.2840 0.2975 0.2541 -0.0192 0.0089  0.0311  820  ASP A CA  
5868  C C   . ASP A 822  ? 0.3310 0.3456 0.2990 -0.0184 0.0092  0.0315  820  ASP A C   
5869  O O   . ASP A 822  ? 0.2709 0.2803 0.2379 -0.0175 0.0087  0.0314  820  ASP A O   
5870  C CB  . ASP A 822  ? 0.2784 0.2968 0.2487 -0.0180 0.0092  0.0279  820  ASP A CB  
5871  C CG  . ASP A 822  ? 0.2907 0.3077 0.2594 -0.0153 0.0087  0.0243  820  ASP A CG  
5872  O OD1 . ASP A 822  ? 0.2893 0.3033 0.2563 -0.0144 0.0085  0.0242  820  ASP A OD1 
5873  O OD2 . ASP A 822  ? 0.3051 0.3241 0.2742 -0.0139 0.0085  0.0214  820  ASP A OD2 
5874  N N   . SER A 823  ? 0.2758 0.2979 0.2431 -0.0188 0.0099  0.0319  821  SER A N   
5875  C CA  . SER A 823  ? 0.2890 0.3132 0.2544 -0.0183 0.0100  0.0324  821  SER A CA  
5876  C C   . SER A 823  ? 0.3096 0.3323 0.2734 -0.0157 0.0095  0.0285  821  SER A C   
5877  O O   . SER A 823  ? 0.3349 0.3590 0.2973 -0.0151 0.0094  0.0284  821  SER A O   
5878  C CB  . SER A 823  ? 0.3300 0.3637 0.2951 -0.0194 0.0109  0.0339  821  SER A CB  
5879  O OG  . SER A 823  ? 0.3291 0.3685 0.2944 -0.0183 0.0113  0.0307  821  SER A OG  
5880  N N   . SER A 824  ? 0.3195 0.3396 0.2839 -0.0142 0.0091  0.0253  822  SER A N   
5881  C CA  . SER A 824  ? 0.2785 0.2964 0.2419 -0.0119 0.0084  0.0219  822  SER A CA  
5882  C C   . SER A 824  ? 0.3376 0.3472 0.3006 -0.0114 0.0077  0.0222  822  SER A C   
5883  O O   . SER A 824  ? 0.3162 0.3235 0.2786 -0.0099 0.0071  0.0201  822  SER A O   
5884  C CB  . SER A 824  ? 0.3031 0.3228 0.2673 -0.0103 0.0081  0.0184  822  SER A CB  
5885  O OG  . SER A 824  ? 0.2798 0.2941 0.2449 -0.0103 0.0077  0.0184  822  SER A OG  
5886  N N   . ALA A 825  ? 0.2911 0.2965 0.2548 -0.0127 0.0078  0.0247  823  ALA A N   
5887  C CA  . ALA A 825  ? 0.3047 0.3029 0.2682 -0.0122 0.0073  0.0249  823  ALA A CA  
5888  C C   . ALA A 825  ? 0.2918 0.2887 0.2544 -0.0123 0.0072  0.0262  823  ALA A C   
5889  O O   . ALA A 825  ? 0.3350 0.3356 0.2973 -0.0132 0.0076  0.0281  823  ALA A O   
5890  C CB  . ALA A 825  ? 0.2949 0.2896 0.2596 -0.0133 0.0072  0.0267  823  ALA A CB  
5891  N N   . LEU A 826  ? 0.3442 0.3362 0.3063 -0.0112 0.0068  0.0253  824  LEU A N   
5892  C CA  . LEU A 826  ? 0.3875 0.3781 0.3492 -0.0112 0.0067  0.0264  824  LEU A CA  
5893  C C   . LEU A 826  ? 0.3945 0.3818 0.3568 -0.0123 0.0068  0.0292  824  LEU A C   
5894  O O   . LEU A 826  ? 0.3322 0.3150 0.2949 -0.0121 0.0066  0.0291  824  LEU A O   
5895  C CB  . LEU A 826  ? 0.4435 0.4306 0.4048 -0.0099 0.0062  0.0245  824  LEU A CB  
5896  C CG  . LEU A 826  ? 0.5005 0.4862 0.4616 -0.0098 0.0060  0.0252  824  LEU A CG  
5897  C CD1 . LEU A 826  ? 0.5080 0.4989 0.4686 -0.0100 0.0060  0.0255  824  LEU A CD1 
5898  C CD2 . LEU A 826  ? 0.5657 0.5484 0.5270 -0.0086 0.0055  0.0232  824  LEU A CD2 
5899  N N   . ALA A 827  ? 0.3393 0.3291 0.3017 -0.0133 0.0069  0.0317  825  ALA A N   
5900  C CA  . ALA A 827  ? 0.3383 0.3254 0.3018 -0.0144 0.0067  0.0345  825  ALA A CA  
5901  C C   . ALA A 827  ? 0.3780 0.3594 0.3417 -0.0135 0.0064  0.0341  825  ALA A C   
5902  O O   . ALA A 827  ? 0.3459 0.3237 0.3107 -0.0137 0.0062  0.0347  825  ALA A O   
5903  C CB  . ALA A 827  ? 0.3752 0.3658 0.3386 -0.0153 0.0067  0.0372  825  ALA A CB  
5904  N N   . GLU A 828  ? 0.3436 0.3245 0.3065 -0.0125 0.0063  0.0329  826  GLU A N   
5905  C CA  . GLU A 828  ? 0.3693 0.3457 0.3325 -0.0118 0.0062  0.0327  826  GLU A CA  
5906  C C   . GLU A 828  ? 0.3593 0.3324 0.3226 -0.0111 0.0063  0.0312  826  GLU A C   
5907  O O   . GLU A 828  ? 0.3460 0.3157 0.3098 -0.0109 0.0062  0.0315  826  GLU A O   
5908  C CB  . GLU A 828  ? 0.4051 0.3822 0.3678 -0.0110 0.0061  0.0318  826  GLU A CB  
5909  C CG  . GLU A 828  ? 0.4682 0.4481 0.4309 -0.0114 0.0058  0.0334  826  GLU A CG  
5910  C CD  . GLU A 828  ? 0.4967 0.4820 0.4584 -0.0118 0.0058  0.0333  826  GLU A CD  
5911  O OE1 . GLU A 828  ? 0.4594 0.4464 0.4208 -0.0118 0.0061  0.0319  826  GLU A OE1 
5912  O OE2 . GLU A 828  ? 0.6200 0.6083 0.5815 -0.0121 0.0056  0.0347  826  GLU A OE2 
5913  N N   . GLN A 829  ? 0.3617 0.3359 0.3243 -0.0107 0.0064  0.0293  827  GLN A N   
5914  C CA  . GLN A 829  ? 0.3803 0.3517 0.3427 -0.0101 0.0063  0.0280  827  GLN A CA  
5915  C C   . GLN A 829  ? 0.3225 0.2933 0.2858 -0.0108 0.0063  0.0287  827  GLN A C   
5916  O O   . GLN A 829  ? 0.3625 0.3302 0.3260 -0.0104 0.0061  0.0283  827  GLN A O   
5917  C CB  . GLN A 829  ? 0.3401 0.3131 0.3019 -0.0094 0.0062  0.0260  827  GLN A CB  
5918  C CG  . GLN A 829  ? 0.4431 0.4140 0.4047 -0.0087 0.0060  0.0247  827  GLN A CG  
5919  C CD  . GLN A 829  ? 0.4897 0.4622 0.4510 -0.0079 0.0056  0.0228  827  GLN A CD  
5920  O OE1 . GLN A 829  ? 0.5231 0.4990 0.4847 -0.0079 0.0055  0.0221  827  GLN A OE1 
5921  N NE2 . GLN A 829  ? 0.5749 0.5453 0.5359 -0.0071 0.0053  0.0218  827  GLN A NE2 
5922  N N   . VAL A 830  ? 0.3366 0.3104 0.3006 -0.0119 0.0063  0.0297  828  VAL A N   
5923  C CA  . VAL A 830  ? 0.3323 0.3056 0.2977 -0.0129 0.0061  0.0306  828  VAL A CA  
5924  C C   . VAL A 830  ? 0.2901 0.2598 0.2567 -0.0131 0.0057  0.0320  828  VAL A C   
5925  O O   . VAL A 830  ? 0.2868 0.2539 0.2544 -0.0131 0.0053  0.0314  828  VAL A O   
5926  C CB  . VAL A 830  ? 0.2922 0.2700 0.2584 -0.0144 0.0063  0.0321  828  VAL A CB  
5927  C CG1 . VAL A 830  ? 0.3054 0.2822 0.2738 -0.0159 0.0059  0.0339  828  VAL A CG1 
5928  C CG2 . VAL A 830  ? 0.3003 0.2820 0.2658 -0.0140 0.0066  0.0303  828  VAL A CG2 
5929  N N   . VAL A 831  ? 0.2812 0.2510 0.2479 -0.0132 0.0057  0.0335  829  VAL A N   
5930  C CA  . VAL A 831  ? 0.2856 0.2522 0.2538 -0.0133 0.0052  0.0348  829  VAL A CA  
5931  C C   . VAL A 831  ? 0.2984 0.2615 0.2662 -0.0118 0.0052  0.0329  829  VAL A C   
5932  O O   . VAL A 831  ? 0.2884 0.2488 0.2575 -0.0117 0.0047  0.0326  829  VAL A O   
5933  C CB  . VAL A 831  ? 0.2800 0.2479 0.2483 -0.0135 0.0051  0.0369  829  VAL A CB  
5934  C CG1 . VAL A 831  ? 0.3192 0.2835 0.2891 -0.0130 0.0045  0.0377  829  VAL A CG1 
5935  C CG2 . VAL A 831  ? 0.2931 0.2646 0.2619 -0.0151 0.0050  0.0392  829  VAL A CG2 
5936  N N   . GLY A 832  ? 0.2501 0.2135 0.2162 -0.0108 0.0057  0.0316  830  GLY A N   
5937  C CA  . GLY A 832  ? 0.2666 0.2274 0.2322 -0.0096 0.0058  0.0302  830  GLY A CA  
5938  C C   . GLY A 832  ? 0.2882 0.2480 0.2537 -0.0093 0.0056  0.0287  830  GLY A C   
5939  O O   . GLY A 832  ? 0.2622 0.2198 0.2280 -0.0086 0.0054  0.0278  830  GLY A O   
5940  N N   . ASP A 833  ? 0.2431 0.2046 0.2081 -0.0098 0.0056  0.0281  831  ASP A N   
5941  C CA  . ASP A 833  ? 0.2492 0.2100 0.2142 -0.0095 0.0053  0.0267  831  ASP A CA  
5942  C C   . ASP A 833  ? 0.2650 0.2247 0.2321 -0.0104 0.0046  0.0270  831  ASP A C   
5943  O O   . ASP A 833  ? 0.2815 0.2397 0.2490 -0.0098 0.0041  0.0256  831  ASP A O   
5944  C CB  . ASP A 833  ? 0.2607 0.2239 0.2249 -0.0097 0.0054  0.0260  831  ASP A CB  
5945  C CG  . ASP A 833  ? 0.3078 0.2712 0.2703 -0.0087 0.0057  0.0252  831  ASP A CG  
5946  O OD1 . ASP A 833  ? 0.2983 0.2598 0.2600 -0.0079 0.0059  0.0252  831  ASP A OD1 
5947  O OD2 . ASP A 833  ? 0.3364 0.3019 0.2985 -0.0086 0.0057  0.0247  831  ASP A OD2 
5948  N N   . VAL A 834  ? 0.2556 0.2161 0.2243 -0.0117 0.0044  0.0290  832  VAL A N   
5949  C CA  . VAL A 834  ? 0.2798 0.2390 0.2512 -0.0127 0.0036  0.0297  832  VAL A CA  
5950  C C   . VAL A 834  ? 0.2988 0.2545 0.2713 -0.0118 0.0030  0.0293  832  VAL A C   
5951  O O   . VAL A 834  ? 0.2503 0.2040 0.2244 -0.0116 0.0022  0.0281  832  VAL A O   
5952  C CB  . VAL A 834  ? 0.2653 0.2267 0.2381 -0.0145 0.0035  0.0325  832  VAL A CB  
5953  C CG1 . VAL A 834  ? 0.2597 0.2187 0.2356 -0.0156 0.0025  0.0338  832  VAL A CG1 
5954  C CG2 . VAL A 834  ? 0.2629 0.2282 0.2352 -0.0155 0.0040  0.0324  832  VAL A CG2 
5955  N N   . ILE A 835  ? 0.2721 0.2274 0.2442 -0.0112 0.0033  0.0303  833  ILE A N   
5956  C CA  . ILE A 835  ? 0.2965 0.2491 0.2697 -0.0101 0.0028  0.0297  833  ILE A CA  
5957  C C   . ILE A 835  ? 0.3065 0.2580 0.2787 -0.0085 0.0029  0.0269  833  ILE A C   
5958  O O   . ILE A 835  ? 0.2729 0.2224 0.2468 -0.0079 0.0020  0.0255  833  ILE A O   
5959  C CB  . ILE A 835  ? 0.3300 0.2833 0.3025 -0.0095 0.0033  0.0309  833  ILE A CB  
5960  C CG1 . ILE A 835  ? 0.3287 0.2828 0.3027 -0.0108 0.0029  0.0338  833  ILE A CG1 
5961  C CG2 . ILE A 835  ? 0.3165 0.2678 0.2896 -0.0078 0.0032  0.0295  833  ILE A CG2 
5962  C CD1 . ILE A 835  ? 0.3247 0.2761 0.3019 -0.0112 0.0016  0.0348  833  ILE A CD1 
5963  N N   . THR A 836  ? 0.2734 0.2265 0.2429 -0.0079 0.0038  0.0260  834  THR A N   
5964  C CA  . THR A 836  ? 0.3015 0.2541 0.2696 -0.0065 0.0039  0.0237  834  THR A CA  
5965  C C   . THR A 836  ? 0.2927 0.2449 0.2616 -0.0068 0.0031  0.0222  834  THR A C   
5966  O O   . THR A 836  ? 0.2902 0.2412 0.2595 -0.0057 0.0025  0.0203  834  THR A O   
5967  C CB  . THR A 836  ? 0.2699 0.2242 0.2353 -0.0061 0.0049  0.0237  834  THR A CB  
5968  O OG1 . THR A 836  ? 0.3421 0.2968 0.3070 -0.0057 0.0056  0.0247  834  THR A OG1 
5969  C CG2 . THR A 836  ? 0.3030 0.2574 0.2666 -0.0049 0.0050  0.0219  834  THR A CG2 
5970  N N   . SER A 837  ? 0.2493 0.2027 0.2185 -0.0081 0.0029  0.0229  835  SER A N   
5971  C CA  . SER A 837  ? 0.2502 0.2036 0.2202 -0.0083 0.0021  0.0213  835  SER A CA  
5972  C C   . SER A 837  ? 0.2778 0.2290 0.2511 -0.0089 0.0008  0.0209  835  SER A C   
5973  O O   . SER A 837  ? 0.2647 0.2152 0.2388 -0.0084 -0.0001 0.0187  835  SER A O   
5974  C CB  . SER A 837  ? 0.2490 0.2048 0.2189 -0.0096 0.0023  0.0221  835  SER A CB  
5975  O OG  . SER A 837  ? 0.2604 0.2178 0.2276 -0.0089 0.0031  0.0220  835  SER A OG  
5976  N N   . ALA A 838  ? 0.2531 0.2034 0.2287 -0.0099 0.0006  0.0230  836  ALA A N   
5977  C CA  . ALA A 838  ? 0.2603 0.2080 0.2396 -0.0106 -0.0009 0.0229  836  ALA A CA  
5978  C C   . ALA A 838  ? 0.2576 0.2028 0.2379 -0.0089 -0.0016 0.0212  836  ALA A C   
5979  O O   . ALA A 838  ? 0.2940 0.2370 0.2769 -0.0087 -0.0030 0.0194  836  ALA A O   
5980  C CB  . ALA A 838  ? 0.2796 0.2275 0.2612 -0.0126 -0.0011 0.0264  836  ALA A CB  
5981  N N   . PHE A 839  ? 0.2599 0.2053 0.2384 -0.0077 -0.0007 0.0216  837  PHE A N   
5982  C CA  . PHE A 839  ? 0.2727 0.2161 0.2529 -0.0061 -0.0014 0.0204  837  PHE A CA  
5983  C C   . PHE A 839  ? 0.2839 0.2284 0.2615 -0.0039 -0.0006 0.0178  837  PHE A C   
5984  O O   . PHE A 839  ? 0.2770 0.2203 0.2560 -0.0023 -0.0012 0.0159  837  PHE A O   
5985  C CB  . PHE A 839  ? 0.2948 0.2375 0.2761 -0.0066 -0.0013 0.0232  837  PHE A CB  
5986  C CG  . PHE A 839  ? 0.3306 0.2727 0.3144 -0.0088 -0.0021 0.0262  837  PHE A CG  
5987  C CD1 . PHE A 839  ? 0.3136 0.2532 0.3010 -0.0097 -0.0037 0.0259  837  PHE A CD1 
5988  C CD2 . PHE A 839  ? 0.3221 0.2662 0.3047 -0.0100 -0.0012 0.0292  837  PHE A CD2 
5989  C CE1 . PHE A 839  ? 0.2792 0.2185 0.2691 -0.0121 -0.0044 0.0291  837  PHE A CE1 
5990  C CE2 . PHE A 839  ? 0.2829 0.2271 0.2676 -0.0121 -0.0018 0.0322  837  PHE A CE2 
5991  C CZ  . PHE A 839  ? 0.3374 0.2792 0.3257 -0.0132 -0.0033 0.0324  837  PHE A CZ  
5992  N N   . ASP A 840  ? 0.2868 0.2337 0.2609 -0.0037 0.0007  0.0177  838  ASP A N   
5993  C CA  . ASP A 840  ? 0.2870 0.2355 0.2587 -0.0018 0.0014  0.0156  838  ASP A CA  
5994  C C   . ASP A 840  ? 0.2956 0.2434 0.2683 -0.0006 0.0002  0.0123  838  ASP A C   
5995  O O   . ASP A 840  ? 0.2884 0.2354 0.2626 -0.0015 -0.0009 0.0116  838  ASP A O   
5996  C CB  . ASP A 840  ? 0.3200 0.2707 0.2881 -0.0020 0.0025  0.0162  838  ASP A CB  
5997  C CG  . ASP A 840  ? 0.4036 0.3562 0.3692 -0.0003 0.0032  0.0145  838  ASP A CG  
5998  O OD1 . ASP A 840  ? 0.4074 0.3604 0.3725 0.0005  0.0026  0.0122  838  ASP A OD1 
5999  O OD2 . ASP A 840  ? 0.4190 0.3728 0.3830 0.0002  0.0044  0.0155  838  ASP A OD2 
6000  N N   . SER A 841  ? 0.2607 0.2092 0.2331 0.0014  0.0004  0.0102  839  SER A N   
6001  C CA  . SER A 841  ? 0.2973 0.2457 0.2706 0.0029  -0.0008 0.0065  839  SER A CA  
6002  C C   . SER A 841  ? 0.2856 0.2306 0.2635 0.0022  -0.0029 0.0057  839  SER A C   
6003  O O   . SER A 841  ? 0.3438 0.2881 0.3231 0.0026  -0.0042 0.0030  839  SER A O   
6004  C CB  . SER A 841  ? 0.3210 0.2716 0.2916 0.0031  -0.0007 0.0051  839  SER A CB  
6005  O OG  . SER A 841  ? 0.3314 0.2848 0.2979 0.0036  0.0010  0.0062  839  SER A OG  
6006  N N   . ALA A 842  ? 0.2721 0.2149 0.2526 0.0012  -0.0032 0.0082  840  ALA A N   
6007  C CA  . ALA A 842  ? 0.2684 0.2076 0.2537 0.0003  -0.0052 0.0083  840  ALA A CA  
6008  C C   . ALA A 842  ? 0.2866 0.2250 0.2730 -0.0017 -0.0060 0.0087  840  ALA A C   
6009  O O   . ALA A 842  ? 0.3277 0.2635 0.3179 -0.0021 -0.0080 0.0073  840  ALA A O   
6010  C CB  . ALA A 842  ? 0.2790 0.2165 0.2671 0.0024  -0.0067 0.0046  840  ALA A CB  
6011  N N   . GLY A 843  ? 0.2710 0.2117 0.2544 -0.0030 -0.0047 0.0105  841  GLY A N   
6012  C CA  . GLY A 843  ? 0.2802 0.2210 0.2644 -0.0048 -0.0053 0.0108  841  GLY A CA  
6013  C C   . GLY A 843  ? 0.2869 0.2282 0.2714 -0.0039 -0.0064 0.0070  841  GLY A C   
6014  O O   . GLY A 843  ? 0.2966 0.2377 0.2829 -0.0054 -0.0074 0.0068  841  GLY A O   
6015  N N   . GLN A 844  ? 0.2779 0.2202 0.2605 -0.0014 -0.0063 0.0040  842  GLN A N   
6016  C CA  . GLN A 844  ? 0.3052 0.2484 0.2878 -0.0003 -0.0075 0.0001  842  GLN A CA  
6017  C C   . GLN A 844  ? 0.3417 0.2885 0.3198 0.0001  -0.0063 -0.0002 842  GLN A C   
6018  O O   . GLN A 844  ? 0.4143 0.3630 0.3905 0.0019  -0.0067 -0.0033 842  GLN A O   
6019  C CB  . GLN A 844  ? 0.3001 0.2431 0.2834 0.0023  -0.0082 -0.0035 842  GLN A CB  
6020  C CG  . GLN A 844  ? 0.3016 0.2405 0.2901 0.0022  -0.0098 -0.0037 842  GLN A CG  
6021  C CD  . GLN A 844  ? 0.3284 0.2675 0.3176 0.0051  -0.0105 -0.0074 842  GLN A CD  
6022  O OE1 . GLN A 844  ? 0.3231 0.2594 0.3167 0.0058  -0.0127 -0.0102 842  GLN A OE1 
6023  N NE2 . GLN A 844  ? 0.3398 0.2824 0.3250 0.0069  -0.0086 -0.0077 842  GLN A NE2 
6024  N N   . ARG A 845  ? 0.3624 0.3103 0.3387 -0.0014 -0.0051 0.0030  843  ARG A N   
6025  C CA  . ARG A 845  ? 0.3390 0.2896 0.3119 -0.0013 -0.0044 0.0029  843  ARG A CA  
6026  C C   . ARG A 845  ? 0.3044 0.2549 0.2797 -0.0030 -0.0056 0.0026  843  ARG A C   
6027  O O   . ARG A 845  ? 0.3400 0.2889 0.3186 -0.0050 -0.0061 0.0045  843  ARG A O   
6028  C CB  . ARG A 845  ? 0.3411 0.2931 0.3110 -0.0017 -0.0026 0.0060  843  ARG A CB  
6029  C CG  . ARG A 845  ? 0.3809 0.3337 0.3482 -0.0001 -0.0013 0.0064  843  ARG A CG  
6030  C CD  . ARG A 845  ? 0.3816 0.3353 0.3465 -0.0008 0.0002  0.0094  843  ARG A CD  
6031  N NE  . ARG A 845  ? 0.4202 0.3748 0.3832 0.0003  0.0015  0.0100  843  ARG A NE  
6032  C CZ  . ARG A 845  ? 0.4149 0.3717 0.3746 0.0014  0.0023  0.0100  843  ARG A CZ  
6033  N NH1 . ARG A 845  ? 0.4262 0.3845 0.3840 0.0018  0.0020  0.0092  843  ARG A NH1 
6034  N NH2 . ARG A 845  ? 0.4521 0.4098 0.4105 0.0022  0.0035  0.0109  843  ARG A NH2 
6035  N N   . CYS A 846  ? 0.3018 0.2545 0.2755 -0.0022 -0.0062 0.0005  844  CYS A N   
6036  C CA  . CYS A 846  ? 0.3268 0.2801 0.3025 -0.0038 -0.0072 0.0003  844  CYS A CA  
6037  C C   . CYS A 846  ? 0.2891 0.2433 0.2644 -0.0055 -0.0060 0.0038  844  CYS A C   
6038  O O   . CYS A 846  ? 0.3350 0.2894 0.3133 -0.0075 -0.0066 0.0047  844  CYS A O   
6039  C CB  . CYS A 846  ? 0.3660 0.3220 0.3394 -0.0023 -0.0079 -0.0024 844  CYS A CB  
6040  S SG  . CYS A 846  ? 0.6711 0.6270 0.6446 0.0000  -0.0094 -0.0071 844  CYS A SG  
6041  N N   . SER A 847  ? 0.3077 0.2629 0.2796 -0.0048 -0.0043 0.0056  845  SER A N   
6042  C CA  . SER A 847  ? 0.2828 0.2391 0.2540 -0.0060 -0.0032 0.0085  845  SER A CA  
6043  C C   . SER A 847  ? 0.3150 0.2697 0.2880 -0.0074 -0.0026 0.0111  845  SER A C   
6044  O O   . SER A 847  ? 0.2609 0.2169 0.2333 -0.0084 -0.0016 0.0133  845  SER A O   
6045  C CB  . SER A 847  ? 0.3479 0.3055 0.3148 -0.0045 -0.0020 0.0091  845  SER A CB  
6046  O OG  . SER A 847  ? 0.3932 0.3498 0.3587 -0.0032 -0.0014 0.0089  845  SER A OG  
6047  N N   . ALA A 848  ? 0.2729 0.2251 0.2481 -0.0075 -0.0032 0.0108  846  ALA A N   
6048  C CA  . ALA A 848  ? 0.2943 0.2451 0.2709 -0.0085 -0.0027 0.0135  846  ALA A CA  
6049  C C   . ALA A 848  ? 0.2820 0.2338 0.2609 -0.0109 -0.0027 0.0159  846  ALA A C   
6050  O O   . ALA A 848  ? 0.2838 0.2362 0.2650 -0.0121 -0.0036 0.0153  846  ALA A O   
6051  C CB  . ALA A 848  ? 0.2701 0.2179 0.2494 -0.0080 -0.0037 0.0125  846  ALA A CB  
6052  N N   . LEU A 849  ? 0.2592 0.2115 0.2375 -0.0116 -0.0016 0.0187  847  LEU A N   
6053  C CA  . LEU A 849  ? 0.2570 0.2112 0.2370 -0.0138 -0.0014 0.0212  847  LEU A CA  
6054  C C   . LEU A 849  ? 0.2813 0.2333 0.2657 -0.0155 -0.0026 0.0225  847  LEU A C   
6055  O O   . LEU A 849  ? 0.3312 0.2805 0.3166 -0.0151 -0.0030 0.0234  847  LEU A O   
6056  C CB  . LEU A 849  ? 0.2523 0.2080 0.2302 -0.0139 0.0000  0.0235  847  LEU A CB  
6057  C CG  . LEU A 849  ? 0.2520 0.2102 0.2314 -0.0160 0.0003  0.0264  847  LEU A CG  
6058  C CD1 . LEU A 849  ? 0.2511 0.2129 0.2306 -0.0169 0.0005  0.0260  847  LEU A CD1 
6059  C CD2 . LEU A 849  ? 0.2505 0.2099 0.2278 -0.0157 0.0014  0.0283  847  LEU A CD2 
6060  N N   . ARG A 850  ? 0.2637 0.2167 0.2509 -0.0173 -0.0034 0.0227  848  ARG A N   
6061  C CA  . ARG A 850  ? 0.2787 0.2295 0.2706 -0.0192 -0.0049 0.0241  848  ARG A CA  
6062  C C   . ARG A 850  ? 0.2745 0.2277 0.2680 -0.0218 -0.0043 0.0282  848  ARG A C   
6063  O O   . ARG A 850  ? 0.2894 0.2405 0.2861 -0.0232 -0.0052 0.0306  848  ARG A O   
6064  C CB  . ARG A 850  ? 0.3146 0.2647 0.3093 -0.0197 -0.0064 0.0217  848  ARG A CB  
6065  C CG  . ARG A 850  ? 0.3156 0.2643 0.3085 -0.0172 -0.0070 0.0175  848  ARG A CG  
6066  C CD  . ARG A 850  ? 0.3000 0.2450 0.2932 -0.0155 -0.0076 0.0166  848  ARG A CD  
6067  N NE  . ARG A 850  ? 0.3243 0.2685 0.3161 -0.0132 -0.0082 0.0124  848  ARG A NE  
6068  C CZ  . ARG A 850  ? 0.3356 0.2779 0.3265 -0.0110 -0.0083 0.0107  848  ARG A CZ  
6069  N NH1 . ARG A 850  ? 0.2739 0.2144 0.2651 -0.0109 -0.0080 0.0128  848  ARG A NH1 
6070  N NH2 . ARG A 850  ? 0.3080 0.2506 0.2974 -0.0089 -0.0089 0.0069  848  ARG A NH2 
6071  N N   . VAL A 851  ? 0.2583 0.2161 0.2498 -0.0223 -0.0030 0.0289  849  VAL A N   
6072  C CA  . VAL A 851  ? 0.2983 0.2596 0.2912 -0.0248 -0.0024 0.0326  849  VAL A CA  
6073  C C   . VAL A 851  ? 0.2871 0.2524 0.2759 -0.0239 -0.0006 0.0332  849  VAL A C   
6074  O O   . VAL A 851  ? 0.2598 0.2276 0.2463 -0.0228 0.0001  0.0310  849  VAL A O   
6075  C CB  . VAL A 851  ? 0.3069 0.2711 0.3029 -0.0270 -0.0029 0.0328  849  VAL A CB  
6076  C CG1 . VAL A 851  ? 0.3086 0.2766 0.3063 -0.0297 -0.0022 0.0371  849  VAL A CG1 
6077  C CG2 . VAL A 851  ? 0.3107 0.2708 0.3108 -0.0276 -0.0049 0.0314  849  VAL A CG2 
6078  N N   . LEU A 852  ? 0.2706 0.2365 0.2588 -0.0244 0.0000  0.0361  850  LEU A N   
6079  C CA  . LEU A 852  ? 0.2699 0.2399 0.2548 -0.0239 0.0015  0.0368  850  LEU A CA  
6080  C C   . LEU A 852  ? 0.2580 0.2335 0.2442 -0.0262 0.0021  0.0397  850  LEU A C   
6081  O O   . LEU A 852  ? 0.2573 0.2326 0.2462 -0.0283 0.0016  0.0430  850  LEU A O   
6082  C CB  . LEU A 852  ? 0.2569 0.2248 0.2400 -0.0227 0.0017  0.0379  850  LEU A CB  
6083  C CG  . LEU A 852  ? 0.2629 0.2347 0.2428 -0.0221 0.0030  0.0384  850  LEU A CG  
6084  C CD1 . LEU A 852  ? 0.2485 0.2216 0.2257 -0.0202 0.0037  0.0351  850  LEU A CD1 
6085  C CD2 . LEU A 852  ? 0.2628 0.2324 0.2418 -0.0212 0.0030  0.0397  850  LEU A CD2 
6086  N N   . CYS A 853  ? 0.2516 0.2321 0.2360 -0.0259 0.0031  0.0385  851  CYS A N   
6087  C CA  . CYS A 853  ? 0.2549 0.2419 0.2403 -0.0279 0.0039  0.0408  851  CYS A CA  
6088  C C   . CYS A 853  ? 0.2879 0.2791 0.2700 -0.0269 0.0052  0.0412  851  CYS A C   
6089  O O   . CYS A 853  ? 0.2626 0.2547 0.2421 -0.0249 0.0057  0.0382  851  CYS A O   
6090  C CB  . CYS A 853  ? 0.2750 0.2654 0.2616 -0.0283 0.0040  0.0388  851  CYS A CB  
6091  S SG  . CYS A 853  ? 0.3480 0.3334 0.3378 -0.0286 0.0024  0.0368  851  CYS A SG  
6092  N N   . LEU A 854  ? 0.2859 0.2794 0.2683 -0.0284 0.0055  0.0447  852  LEU A N   
6093  C CA  . LEU A 854  ? 0.2862 0.2834 0.2655 -0.0274 0.0064  0.0452  852  LEU A CA  
6094  C C   . LEU A 854  ? 0.2608 0.2664 0.2402 -0.0289 0.0074  0.0469  852  LEU A C   
6095  O O   . LEU A 854  ? 0.2677 0.2755 0.2495 -0.0315 0.0074  0.0504  852  LEU A O   
6096  C CB  . LEU A 854  ? 0.2822 0.2762 0.2612 -0.0275 0.0059  0.0479  852  LEU A CB  
6097  C CG  . LEU A 854  ? 0.3303 0.3169 0.3090 -0.0257 0.0051  0.0461  852  LEU A CG  
6098  C CD1 . LEU A 854  ? 0.2595 0.2436 0.2383 -0.0258 0.0045  0.0489  852  LEU A CD1 
6099  C CD2 . LEU A 854  ? 0.2999 0.2858 0.2755 -0.0232 0.0056  0.0422  852  LEU A CD2 
6100  N N   . GLN A 855  ? 0.2622 0.2725 0.2390 -0.0274 0.0083  0.0444  853  GLN A N   
6101  C CA  . GLN A 855  ? 0.2747 0.2938 0.2513 -0.0285 0.0094  0.0457  853  GLN A CA  
6102  C C   . GLN A 855  ? 0.2760 0.2974 0.2522 -0.0300 0.0096  0.0500  853  GLN A C   
6103  O O   . GLN A 855  ? 0.2895 0.3073 0.2640 -0.0289 0.0092  0.0504  853  GLN A O   
6104  C CB  . GLN A 855  ? 0.2769 0.3005 0.2509 -0.0262 0.0101  0.0419  853  GLN A CB  
6105  C CG  . GLN A 855  ? 0.2845 0.3180 0.2587 -0.0272 0.0113  0.0425  853  GLN A CG  
6106  C CD  . GLN A 855  ? 0.3485 0.3867 0.3204 -0.0247 0.0118  0.0384  853  GLN A CD  
6107  O OE1 . GLN A 855  ? 0.3728 0.4073 0.3441 -0.0225 0.0112  0.0346  853  GLN A OE1 
6108  N NE2 . GLN A 855  ? 0.3330 0.3795 0.3036 -0.0250 0.0127  0.0392  853  GLN A NE2 
6109  N N   . GLU A 856  ? 0.2941 0.3216 0.2719 -0.0325 0.0102  0.0534  854  GLU A N   
6110  C CA  . GLU A 856  ? 0.3716 0.4006 0.3498 -0.0344 0.0101  0.0586  854  GLU A CA  
6111  C C   . GLU A 856  ? 0.3815 0.4134 0.3560 -0.0328 0.0105  0.0585  854  GLU A C   
6112  O O   . GLU A 856  ? 0.3905 0.4198 0.3648 -0.0333 0.0098  0.0615  854  GLU A O   
6113  C CB  . GLU A 856  ? 0.3623 0.3989 0.3426 -0.0374 0.0109  0.0622  854  GLU A CB  
6114  C CG  . GLU A 856  ? 0.4633 0.5029 0.4439 -0.0396 0.0108  0.0681  854  GLU A CG  
6115  C CD  . GLU A 856  ? 0.5003 0.5312 0.4837 -0.0409 0.0092  0.0714  854  GLU A CD  
6116  O OE1 . GLU A 856  ? 0.5148 0.5395 0.5012 -0.0412 0.0083  0.0701  854  GLU A OE1 
6117  O OE2 . GLU A 856  ? 0.4967 0.5270 0.4793 -0.0413 0.0087  0.0750  854  GLU A OE2 
6118  N N   . ASP A 857  ? 0.3371 0.3743 0.3091 -0.0309 0.0113  0.0547  855  ASP A N   
6119  C CA  . ASP A 857  ? 0.3439 0.3848 0.3127 -0.0295 0.0116  0.0543  855  ASP A CA  
6120  C C   . ASP A 857  ? 0.3664 0.3995 0.3341 -0.0277 0.0106  0.0532  855  ASP A C   
6121  O O   . ASP A 857  ? 0.4074 0.4421 0.3731 -0.0273 0.0104  0.0545  855  ASP A O   
6122  C CB  . ASP A 857  ? 0.4350 0.4825 0.4017 -0.0275 0.0125  0.0499  855  ASP A CB  
6123  N N   . VAL A 858  ? 0.3060 0.3311 0.2747 -0.0267 0.0099  0.0509  856  VAL A N   
6124  C CA  . VAL A 858  ? 0.2977 0.3159 0.2654 -0.0251 0.0091  0.0497  856  VAL A CA  
6125  C C   . VAL A 858  ? 0.3201 0.3308 0.2902 -0.0260 0.0081  0.0520  856  VAL A C   
6126  O O   . VAL A 858  ? 0.3421 0.3470 0.3119 -0.0247 0.0074  0.0510  856  VAL A O   
6127  C CB  . VAL A 858  ? 0.3593 0.3748 0.3258 -0.0226 0.0091  0.0446  856  VAL A CB  
6128  C CG1 . VAL A 858  ? 0.3372 0.3594 0.3015 -0.0212 0.0097  0.0419  856  VAL A CG1 
6129  C CG2 . VAL A 858  ? 0.3135 0.3266 0.2818 -0.0228 0.0090  0.0428  856  VAL A CG2 
6130  N N   . ALA A 859  ? 0.3432 0.3540 0.3160 -0.0283 0.0079  0.0550  857  ALA A N   
6131  C CA  . ALA A 859  ? 0.3340 0.3374 0.3097 -0.0290 0.0067  0.0564  857  ALA A CA  
6132  C C   . ALA A 859  ? 0.3623 0.3623 0.3380 -0.0288 0.0058  0.0590  857  ALA A C   
6133  O O   . ALA A 859  ? 0.3586 0.3517 0.3351 -0.0277 0.0049  0.0578  857  ALA A O   
6134  C CB  . ALA A 859  ? 0.3236 0.3284 0.3027 -0.0318 0.0065  0.0593  857  ALA A CB  
6135  N N   . ASP A 860  ? 0.3346 0.3395 0.3095 -0.0299 0.0060  0.0626  858  ASP A N   
6136  C CA  . ASP A 860  ? 0.3586 0.3604 0.3338 -0.0298 0.0050  0.0656  858  ASP A CA  
6137  C C   . ASP A 860  ? 0.3326 0.3314 0.3056 -0.0271 0.0049  0.0624  858  ASP A C   
6138  O O   . ASP A 860  ? 0.3479 0.3407 0.3221 -0.0262 0.0038  0.0625  858  ASP A O   
6139  C CB  . ASP A 860  ? 0.3786 0.3872 0.3530 -0.0314 0.0052  0.0702  858  ASP A CB  
6140  C CG  . ASP A 860  ? 0.4642 0.4740 0.4418 -0.0344 0.0049  0.0749  858  ASP A CG  
6141  O OD1 . ASP A 860  ? 0.5203 0.5235 0.5014 -0.0352 0.0038  0.0756  858  ASP A OD1 
6142  O OD2 . ASP A 860  ? 0.5486 0.5662 0.5254 -0.0360 0.0057  0.0778  858  ASP A OD2 
6143  N N   . ARG A 861  ? 0.3227 0.3258 0.2927 -0.0257 0.0058  0.0592  859  ARG A N   
6144  C CA  . ARG A 861  ? 0.3409 0.3416 0.3090 -0.0234 0.0057  0.0562  859  ARG A CA  
6145  C C   . ARG A 861  ? 0.3406 0.3340 0.3098 -0.0221 0.0053  0.0532  859  ARG A C   
6146  O O   . ARG A 861  ? 0.3232 0.3123 0.2925 -0.0209 0.0047  0.0527  859  ARG A O   
6147  C CB  . ARG A 861  ? 0.3755 0.3821 0.3408 -0.0223 0.0066  0.0532  859  ARG A CB  
6148  C CG  . ARG A 861  ? 0.4495 0.4532 0.4134 -0.0201 0.0064  0.0495  859  ARG A CG  
6149  C CD  . ARG A 861  ? 0.5886 0.5983 0.5501 -0.0192 0.0067  0.0481  859  ARG A CD  
6150  N NE  . ARG A 861  ? 0.6594 0.6659 0.6201 -0.0173 0.0063  0.0452  859  ARG A NE  
6151  C CZ  . ARG A 861  ? 0.6017 0.6062 0.5622 -0.0161 0.0065  0.0413  859  ARG A CZ  
6152  N NH1 . ARG A 861  ? 0.6255 0.6306 0.5862 -0.0162 0.0070  0.0396  859  ARG A NH1 
6153  N NH2 . ARG A 861  ? 0.5898 0.5915 0.5499 -0.0147 0.0061  0.0393  859  ARG A NH2 
6154  N N   . ILE A 862  ? 0.2889 0.2815 0.2588 -0.0224 0.0057  0.0513  860  ILE A N   
6155  C CA  . ILE A 862  ? 0.2973 0.2837 0.2680 -0.0211 0.0053  0.0485  860  ILE A CA  
6156  C C   . ILE A 862  ? 0.2668 0.2477 0.2402 -0.0217 0.0042  0.0504  860  ILE A C   
6157  O O   . ILE A 862  ? 0.2934 0.2695 0.2671 -0.0203 0.0038  0.0489  860  ILE A O   
6158  C CB  . ILE A 862  ? 0.3050 0.2925 0.2757 -0.0212 0.0059  0.0460  860  ILE A CB  
6159  C CG1 . ILE A 862  ? 0.3372 0.3290 0.3054 -0.0200 0.0067  0.0432  860  ILE A CG1 
6160  C CG2 . ILE A 862  ? 0.3232 0.3048 0.2950 -0.0203 0.0054  0.0437  860  ILE A CG2 
6161  C CD1 . ILE A 862  ? 0.3614 0.3548 0.3297 -0.0198 0.0071  0.0406  860  ILE A CD1 
6162  N N   . LEU A 863  ? 0.2947 0.2764 0.2705 -0.0237 0.0037  0.0538  861  LEU A N   
6163  C CA  . LEU A 863  ? 0.3076 0.2837 0.2866 -0.0242 0.0024  0.0556  861  LEU A CA  
6164  C C   . LEU A 863  ? 0.2930 0.2667 0.2717 -0.0230 0.0017  0.0567  861  LEU A C   
6165  O O   . LEU A 863  ? 0.2721 0.2405 0.2525 -0.0219 0.0008  0.0556  861  LEU A O   
6166  C CB  . LEU A 863  ? 0.3316 0.3092 0.3134 -0.0269 0.0018  0.0596  861  LEU A CB  
6167  C CG  . LEU A 863  ? 0.4598 0.4345 0.4448 -0.0281 0.0012  0.0589  861  LEU A CG  
6168  C CD1 . LEU A 863  ? 0.4419 0.4191 0.4297 -0.0311 0.0008  0.0635  861  LEU A CD1 
6169  C CD2 . LEU A 863  ? 0.3830 0.3501 0.3703 -0.0269 -0.0002 0.0572  861  LEU A CD2 
6170  N N   . THR A 864  ? 0.2939 0.2721 0.2708 -0.0232 0.0020  0.0588  862  THR A N   
6171  C CA  . THR A 864  ? 0.3046 0.2812 0.2813 -0.0220 0.0013  0.0599  862  THR A CA  
6172  C C   . THR A 864  ? 0.2646 0.2382 0.2401 -0.0197 0.0015  0.0559  862  THR A C   
6173  O O   . THR A 864  ? 0.2894 0.2588 0.2663 -0.0186 0.0007  0.0558  862  THR A O   
6174  C CB  . THR A 864  ? 0.3217 0.3045 0.2962 -0.0225 0.0017  0.0623  862  THR A CB  
6175  O OG1 . THR A 864  ? 0.3395 0.3249 0.3154 -0.0248 0.0013  0.0668  862  THR A OG1 
6176  C CG2 . THR A 864  ? 0.3763 0.3581 0.3502 -0.0210 0.0010  0.0628  862  THR A CG2 
6177  N N   . MET A 865  ? 0.2869 0.2627 0.2599 -0.0190 0.0027  0.0528  863  MET A N   
6178  C CA  . MET A 865  ? 0.2954 0.2688 0.2674 -0.0171 0.0030  0.0493  863  MET A CA  
6179  C C   . MET A 865  ? 0.2781 0.2461 0.2519 -0.0164 0.0026  0.0475  863  MET A C   
6180  O O   . MET A 865  ? 0.2781 0.2430 0.2523 -0.0150 0.0023  0.0462  863  MET A O   
6181  C CB  . MET A 865  ? 0.3017 0.2785 0.2711 -0.0166 0.0041  0.0466  863  MET A CB  
6182  C CG  . MET A 865  ? 0.3677 0.3427 0.3359 -0.0149 0.0044  0.0436  863  MET A CG  
6183  S SD  . MET A 865  ? 0.5444 0.5235 0.5101 -0.0144 0.0053  0.0408  863  MET A SD  
6184  C CE  . MET A 865  ? 0.3430 0.3285 0.3080 -0.0158 0.0054  0.0433  863  MET A CE  
6185  N N   . LEU A 866  ? 0.2884 0.2556 0.2635 -0.0175 0.0025  0.0476  864  LEU A N   
6186  C CA  A LEU A 866  ? 0.2731 0.2356 0.2499 -0.0169 0.0019  0.0456  864  LEU A CA  
6187  C CA  B LEU A 866  ? 0.2790 0.2416 0.2559 -0.0170 0.0019  0.0457  864  LEU A CA  
6188  C C   . LEU A 866  ? 0.2866 0.2451 0.2662 -0.0165 0.0006  0.0469  864  LEU A C   
6189  O O   . LEU A 866  ? 0.2613 0.2163 0.2416 -0.0150 0.0003  0.0446  864  LEU A O   
6190  C CB  A LEU A 866  ? 0.2859 0.2489 0.2641 -0.0184 0.0018  0.0457  864  LEU A CB  
6191  C CB  B LEU A 866  ? 0.2743 0.2373 0.2526 -0.0185 0.0018  0.0459  864  LEU A CB  
6192  C CG  A LEU A 866  ? 0.2995 0.2584 0.2790 -0.0177 0.0013  0.0429  864  LEU A CG  
6193  C CG  B LEU A 866  ? 0.2795 0.2448 0.2559 -0.0184 0.0028  0.0433  864  LEU A CG  
6194  C CD1 A LEU A 866  ? 0.2818 0.2406 0.2586 -0.0158 0.0022  0.0396  864  LEU A CD1 
6195  C CD1 B LEU A 866  ? 0.2780 0.2432 0.2568 -0.0200 0.0023  0.0438  864  LEU A CD1 
6196  C CD2 A LEU A 866  ? 0.2577 0.2175 0.2388 -0.0193 0.0011  0.0431  864  LEU A CD2 
6197  C CD2 B LEU A 866  ? 0.2756 0.2384 0.2506 -0.0164 0.0030  0.0399  864  LEU A CD2 
6198  N N   . LYS A 867  ? 0.2606 0.2196 0.2421 -0.0179 -0.0003 0.0506  865  LYS A N   
6199  C CA  . LYS A 867  ? 0.2909 0.2458 0.2754 -0.0174 -0.0018 0.0520  865  LYS A CA  
6200  C C   . LYS A 867  ? 0.2870 0.2415 0.2705 -0.0153 -0.0017 0.0510  865  LYS A C   
6201  O O   . LYS A 867  ? 0.2835 0.2343 0.2688 -0.0138 -0.0025 0.0495  865  LYS A O   
6202  C CB  . LYS A 867  ? 0.2839 0.2398 0.2705 -0.0194 -0.0028 0.0568  865  LYS A CB  
6203  C CG  . LYS A 867  ? 0.3108 0.2668 0.2994 -0.0216 -0.0031 0.0581  865  LYS A CG  
6204  C CD  . LYS A 867  ? 0.3696 0.3269 0.3602 -0.0238 -0.0040 0.0634  865  LYS A CD  
6205  C CE  . LYS A 867  ? 0.4420 0.3998 0.4350 -0.0263 -0.0042 0.0647  865  LYS A CE  
6206  N NZ  . LYS A 867  ? 0.4551 0.4161 0.4494 -0.0289 -0.0046 0.0703  865  LYS A NZ  
6207  N N   . GLY A 868  ? 0.2822 0.2407 0.2628 -0.0152 -0.0008 0.0516  866  GLY A N   
6208  C CA  . GLY A 868  ? 0.2968 0.2554 0.2766 -0.0134 -0.0006 0.0504  866  GLY A CA  
6209  C C   . GLY A 868  ? 0.2703 0.2269 0.2494 -0.0118 0.0000  0.0465  866  GLY A C   
6210  O O   . GLY A 868  ? 0.3083 0.2630 0.2884 -0.0102 -0.0003 0.0454  866  GLY A O   
6211  N N   . ALA A 869  ? 0.2702 0.2276 0.2475 -0.0121 0.0011  0.0444  867  ALA A N   
6212  C CA  . ALA A 869  ? 0.2784 0.2342 0.2548 -0.0107 0.0017  0.0410  867  ALA A CA  
6213  C C   . ALA A 869  ? 0.2850 0.2368 0.2639 -0.0098 0.0008  0.0398  867  ALA A C   
6214  O O   . ALA A 869  ? 0.2786 0.2292 0.2576 -0.0082 0.0010  0.0375  867  ALA A O   
6215  C CB  . ALA A 869  ? 0.2687 0.2262 0.2429 -0.0112 0.0027  0.0394  867  ALA A CB  
6216  N N   . LEU A 870  ? 0.2988 0.2489 0.2800 -0.0110 -0.0002 0.0410  868  LEU A N   
6217  C CA  . LEU A 870  ? 0.3279 0.2740 0.3120 -0.0103 -0.0014 0.0396  868  LEU A CA  
6218  C C   . LEU A 870  ? 0.2957 0.2400 0.2817 -0.0085 -0.0023 0.0394  868  LEU A C   
6219  O O   . LEU A 870  ? 0.2787 0.2210 0.2656 -0.0068 -0.0026 0.0366  868  LEU A O   
6220  C CB  . LEU A 870  ? 0.2984 0.2431 0.2854 -0.0121 -0.0027 0.0418  868  LEU A CB  
6221  C CG  . LEU A 870  ? 0.3091 0.2494 0.2997 -0.0117 -0.0043 0.0403  868  LEU A CG  
6222  C CD1 . LEU A 870  ? 0.3160 0.2562 0.3059 -0.0118 -0.0039 0.0374  868  LEU A CD1 
6223  C CD2 . LEU A 870  ? 0.3148 0.2530 0.3093 -0.0135 -0.0060 0.0438  868  LEU A CD2 
6224  N N   . HIS A 871  ? 0.2829 0.2282 0.2693 -0.0088 -0.0027 0.0423  869  HIS A N   
6225  C CA  . HIS A 871  ? 0.3080 0.2516 0.2968 -0.0072 -0.0037 0.0423  869  HIS A CA  
6226  C C   . HIS A 871  ? 0.3311 0.2764 0.3180 -0.0053 -0.0026 0.0401  869  HIS A C   
6227  O O   . HIS A 871  ? 0.2974 0.2418 0.2864 -0.0037 -0.0033 0.0396  869  HIS A O   
6228  C CB  . HIS A 871  ? 0.2704 0.2144 0.2605 -0.0082 -0.0048 0.0465  869  HIS A CB  
6229  C CG  . HIS A 871  ? 0.2945 0.2358 0.2876 -0.0098 -0.0063 0.0490  869  HIS A CG  
6230  N ND1 . HIS A 871  ? 0.3454 0.2822 0.3428 -0.0090 -0.0082 0.0485  869  HIS A ND1 
6231  C CD2 . HIS A 871  ? 0.2926 0.2354 0.2855 -0.0122 -0.0063 0.0520  869  HIS A CD2 
6232  C CE1 . HIS A 871  ? 0.4002 0.3352 0.3999 -0.0110 -0.0094 0.0512  869  HIS A CE1 
6233  N NE2 . HIS A 871  ? 0.3438 0.2828 0.3409 -0.0130 -0.0082 0.0536  869  HIS A NE2 
6234  N N   . GLU A 872  ? 0.3284 0.2763 0.3121 -0.0055 -0.0009 0.0386  870  GLU A N   
6235  C CA  . GLU A 872  ? 0.3211 0.2708 0.3034 -0.0040 0.0002  0.0366  870  GLU A CA  
6236  C C   . GLU A 872  ? 0.3188 0.2674 0.3010 -0.0027 0.0006  0.0332  870  GLU A C   
6237  O O   . GLU A 872  ? 0.3350 0.2852 0.3160 -0.0015 0.0017  0.0316  870  GLU A O   
6238  C CB  . GLU A 872  ? 0.2937 0.2467 0.2728 -0.0050 0.0016  0.0370  870  GLU A CB  
6239  C CG  . GLU A 872  ? 0.3036 0.2587 0.2824 -0.0060 0.0012  0.0399  870  GLU A CG  
6240  C CD  . GLU A 872  ? 0.3652 0.3206 0.3458 -0.0049 0.0005  0.0408  870  GLU A CD  
6241  O OE1 . GLU A 872  ? 0.3719 0.3271 0.3532 -0.0034 0.0008  0.0389  870  GLU A OE1 
6242  O OE2 . GLU A 872  ? 0.3638 0.3201 0.3450 -0.0056 -0.0004 0.0435  870  GLU A OE2 
6243  N N   . LEU A 873  ? 0.3180 0.2641 0.3014 -0.0028 -0.0001 0.0322  871  LEU A N   
6244  C CA  . LEU A 873  ? 0.3104 0.2559 0.2934 -0.0015 0.0002  0.0288  871  LEU A CA  
6245  C C   . LEU A 873  ? 0.3131 0.2573 0.2989 0.0006  -0.0007 0.0270  871  LEU A C   
6246  O O   . LEU A 873  ? 0.3266 0.2684 0.3156 0.0009  -0.0023 0.0281  871  LEU A O   
6247  C CB  . LEU A 873  ? 0.2902 0.2339 0.2737 -0.0025 -0.0004 0.0281  871  LEU A CB  
6248  C CG  . LEU A 873  ? 0.3255 0.2708 0.3065 -0.0044 0.0004  0.0295  871  LEU A CG  
6249  C CD1 . LEU A 873  ? 0.3321 0.2757 0.3142 -0.0054 -0.0005 0.0289  871  LEU A CD1 
6250  C CD2 . LEU A 873  ? 0.3734 0.3212 0.3509 -0.0039 0.0020  0.0282  871  LEU A CD2 
6251  N N   . HIS A 874  ? 0.2944 0.2403 0.2790 0.0023  0.0003  0.0242  872  HIS A N   
6252  C CA  . HIS A 874  ? 0.2997 0.2454 0.2867 0.0047  -0.0004 0.0217  872  HIS A CA  
6253  C C   . HIS A 874  ? 0.2788 0.2230 0.2664 0.0056  -0.0011 0.0185  872  HIS A C   
6254  O O   . HIS A 874  ? 0.2618 0.2079 0.2466 0.0056  0.0001  0.0170  872  HIS A O   
6255  C CB  . HIS A 874  ? 0.3180 0.2675 0.3033 0.0059  0.0012  0.0208  872  HIS A CB  
6256  C CG  . HIS A 874  ? 0.3240 0.2743 0.3118 0.0085  0.0008  0.0181  872  HIS A CG  
6257  N ND1 . HIS A 874  ? 0.3879 0.3422 0.3749 0.0098  0.0022  0.0172  872  HIS A ND1 
6258  C CD2 . HIS A 874  ? 0.4020 0.3498 0.3931 0.0102  -0.0010 0.0159  872  HIS A CD2 
6259  C CE1 . HIS A 874  ? 0.4044 0.3591 0.3940 0.0122  0.0014  0.0145  872  HIS A CE1 
6260  N NE2 . HIS A 874  ? 0.4513 0.4020 0.4436 0.0126  -0.0006 0.0135  872  HIS A NE2 
6261  N N   . ILE A 875  ? 0.3077 0.2487 0.2992 0.0064  -0.0031 0.0175  873  ILE A N   
6262  C CA  . ILE A 875  ? 0.3097 0.2489 0.3025 0.0073  -0.0042 0.0141  873  ILE A CA  
6263  C C   . ILE A 875  ? 0.3470 0.2869 0.3420 0.0104  -0.0049 0.0106  873  ILE A C   
6264  O O   . ILE A 875  ? 0.3355 0.2741 0.3337 0.0114  -0.0059 0.0112  873  ILE A O   
6265  C CB  . ILE A 875  ? 0.3174 0.2521 0.3136 0.0058  -0.0064 0.0154  873  ILE A CB  
6266  C CG1 . ILE A 875  ? 0.3479 0.2829 0.3417 0.0031  -0.0057 0.0177  873  ILE A CG1 
6267  C CG2 . ILE A 875  ? 0.3543 0.2866 0.3535 0.0073  -0.0082 0.0114  873  ILE A CG2 
6268  C CD1 . ILE A 875  ? 0.3614 0.2985 0.3523 0.0014  -0.0041 0.0213  873  ILE A CD1 
6269  N N   . GLY A 876  ? 0.3014 0.2437 0.2949 0.0119  -0.0042 0.0068  874  GLY A N   
6270  C CA  . GLY A 876  ? 0.2980 0.2418 0.2934 0.0150  -0.0047 0.0030  874  GLY A CA  
6271  C C   . GLY A 876  ? 0.2908 0.2382 0.2834 0.0164  -0.0037 -0.0007 874  GLY A C   
6272  O O   . GLY A 876  ? 0.2962 0.2443 0.2857 0.0150  -0.0029 -0.0003 874  GLY A O   
6273  N N   . ARG A 877  ? 0.3287 0.2788 0.3227 0.0194  -0.0038 -0.0045 875  ARG A N   
6274  C CA  . ARG A 877  ? 0.3463 0.3010 0.3374 0.0210  -0.0027 -0.0081 875  ARG A CA  
6275  C C   . ARG A 877  ? 0.3088 0.2679 0.2948 0.0196  0.0001  -0.0054 875  ARG A C   
6276  O O   . ARG A 877  ? 0.3077 0.2683 0.2932 0.0189  0.0014  -0.0026 875  ARG A O   
6277  C CB  . ARG A 877  ? 0.3323 0.2901 0.3258 0.0245  -0.0031 -0.0123 875  ARG A CB  
6278  C CG  . ARG A 877  ? 0.3775 0.3393 0.3692 0.0266  -0.0029 -0.0172 875  ARG A CG  
6279  C CD  . ARG A 877  ? 0.3864 0.3518 0.3807 0.0303  -0.0033 -0.0217 875  ARG A CD  
6280  N NE  . ARG A 877  ? 0.4276 0.3992 0.4197 0.0310  -0.0008 -0.0207 875  ARG A NE  
6281  C CZ  . ARG A 877  ? 0.4840 0.4604 0.4778 0.0341  -0.0005 -0.0242 875  ARG A CZ  
6282  N NH1 . ARG A 877  ? 0.4184 0.3935 0.4163 0.0370  -0.0028 -0.0292 875  ARG A NH1 
6283  N NH2 . ARG A 877  ? 0.4516 0.4343 0.4431 0.0343  0.0021  -0.0228 875  ARG A NH2 
6284  N N   . THR A 878  ? 0.2857 0.2469 0.2682 0.0192  0.0009  -0.0064 876  THR A N   
6285  C CA  . THR A 878  ? 0.2805 0.2441 0.2585 0.0173  0.0030  -0.0031 876  THR A CA  
6286  C C   . THR A 878  ? 0.2984 0.2683 0.2737 0.0184  0.0053  -0.0033 876  THR A C   
6287  O O   . THR A 878  ? 0.3112 0.2833 0.2830 0.0169  0.0069  -0.0008 876  THR A O   
6288  C CB  . THR A 878  ? 0.3203 0.2829 0.2959 0.0161  0.0027  -0.0034 876  THR A CB  
6289  O OG1 . THR A 878  ? 0.3145 0.2791 0.2900 0.0183  0.0019  -0.0079 876  THR A OG1 
6290  C CG2 . THR A 878  ? 0.3406 0.2975 0.3184 0.0142  0.0010  -0.0018 876  THR A CG2 
6291  N N   . ASP A 879  ? 0.3023 0.2755 0.2794 0.0209  0.0054  -0.0061 877  ASP A N   
6292  C CA  . ASP A 879  ? 0.3057 0.2856 0.2805 0.0217  0.0077  -0.0059 877  ASP A CA  
6293  C C   . ASP A 879  ? 0.3080 0.2882 0.2837 0.0205  0.0088  -0.0024 877  ASP A C   
6294  O O   . ASP A 879  ? 0.3129 0.2982 0.2887 0.0216  0.0102  -0.0027 877  ASP A O   
6295  C CB  . ASP A 879  ? 0.3309 0.3153 0.3071 0.0251  0.0075  -0.0108 877  ASP A CB  
6296  C CG  . ASP A 879  ? 0.3881 0.3702 0.3694 0.0270  0.0058  -0.0128 877  ASP A CG  
6297  O OD1 . ASP A 879  ? 0.4276 0.4033 0.4118 0.0260  0.0040  -0.0116 877  ASP A OD1 
6298  O OD2 . ASP A 879  ? 0.3848 0.3718 0.3673 0.0295  0.0064  -0.0155 877  ASP A OD2 
6299  N N   . ARG A 880  ? 0.2805 0.2559 0.2570 0.0182  0.0081  0.0009  878  ARG A N   
6300  C CA  . ARG A 880  ? 0.3223 0.2977 0.2993 0.0167  0.0090  0.0044  878  ARG A CA  
6301  C C   . ARG A 880  ? 0.3040 0.2772 0.2785 0.0139  0.0094  0.0080  878  ARG A C   
6302  O O   . ARG A 880  ? 0.2989 0.2678 0.2733 0.0128  0.0082  0.0084  878  ARG A O   
6303  C CB  . ARG A 880  ? 0.3713 0.3433 0.3526 0.0172  0.0073  0.0046  878  ARG A CB  
6304  C CG  . ARG A 880  ? 0.4202 0.3954 0.4043 0.0196  0.0073  0.0027  878  ARG A CG  
6305  C CD  . ARG A 880  ? 0.4920 0.4625 0.4805 0.0203  0.0050  0.0025  878  ARG A CD  
6306  N NE  . ARG A 880  ? 0.6030 0.5760 0.5946 0.0219  0.0050  0.0022  878  ARG A NE  
6307  C CZ  . ARG A 880  ? 0.6654 0.6411 0.6595 0.0250  0.0046  -0.0016 878  ARG A CZ  
6308  N NH1 . ARG A 880  ? 0.6660 0.6429 0.6597 0.0268  0.0042  -0.0055 878  ARG A NH1 
6309  N NH2 . ARG A 880  ? 0.6867 0.6643 0.6839 0.0263  0.0043  -0.0016 878  ARG A NH2 
6310  N N   . LEU A 881  ? 0.2981 0.2742 0.2709 0.0126  0.0111  0.0105  879  LEU A N   
6311  C CA  . LEU A 881  ? 0.2622 0.2363 0.2328 0.0101  0.0115  0.0136  879  LEU A CA  
6312  C C   . LEU A 881  ? 0.3017 0.2712 0.2740 0.0087  0.0102  0.0153  879  LEU A C   
6313  O O   . LEU A 881  ? 0.2652 0.2321 0.2361 0.0071  0.0099  0.0167  879  LEU A O   
6314  C CB  . LEU A 881  ? 0.2552 0.2331 0.2244 0.0090  0.0133  0.0159  879  LEU A CB  
6315  C CG  . LEU A 881  ? 0.2987 0.2747 0.2660 0.0066  0.0136  0.0189  879  LEU A CG  
6316  C CD1 . LEU A 881  ? 0.3136 0.2893 0.2778 0.0063  0.0138  0.0186  879  LEU A CD1 
6317  C CD2 . LEU A 881  ? 0.3104 0.2896 0.2779 0.0055  0.0150  0.0211  879  LEU A CD2 
6318  N N   . SER A 882  ? 0.3271 0.2957 0.3026 0.0095  0.0093  0.0151  880  SER A N   
6319  C CA  . SER A 882  ? 0.3407 0.3056 0.3177 0.0082  0.0081  0.0172  880  SER A CA  
6320  C C   . SER A 882  ? 0.3238 0.2844 0.3015 0.0080  0.0065  0.0165  880  SER A C   
6321  O O   . SER A 882  ? 0.3212 0.2790 0.2998 0.0066  0.0056  0.0186  880  SER A O   
6322  C CB  . SER A 882  ? 0.3216 0.2871 0.3019 0.0093  0.0075  0.0174  880  SER A CB  
6323  O OG  . SER A 882  ? 0.2845 0.2497 0.2672 0.0116  0.0066  0.0145  880  SER A OG  
6324  N N   . VAL A 883  ? 0.3081 0.2685 0.2857 0.0092  0.0060  0.0138  881  VAL A N   
6325  C CA  . VAL A 883  ? 0.2996 0.2559 0.2786 0.0089  0.0043  0.0130  881  VAL A CA  
6326  C C   . VAL A 883  ? 0.3032 0.2586 0.2796 0.0069  0.0046  0.0144  881  VAL A C   
6327  O O   . VAL A 883  ? 0.3395 0.2970 0.3129 0.0069  0.0057  0.0138  881  VAL A O   
6328  C CB  . VAL A 883  ? 0.3391 0.2956 0.3194 0.0112  0.0034  0.0090  881  VAL A CB  
6329  C CG1 . VAL A 883  ? 0.3131 0.2657 0.2946 0.0105  0.0017  0.0082  881  VAL A CG1 
6330  C CG2 . VAL A 883  ? 0.3284 0.2850 0.3123 0.0133  0.0025  0.0075  881  VAL A CG2 
6331  N N   . ASP A 884  ? 0.2579 0.2100 0.2354 0.0053  0.0035  0.0163  882  ASP A N   
6332  C CA  . ASP A 884  ? 0.2872 0.2386 0.2626 0.0035  0.0037  0.0175  882  ASP A CA  
6333  C C   . ASP A 884  ? 0.2897 0.2392 0.2659 0.0036  0.0025  0.0154  882  ASP A C   
6334  O O   . ASP A 884  ? 0.3360 0.2864 0.3098 0.0032  0.0030  0.0148  882  ASP A O   
6335  C CB  . ASP A 884  ? 0.2565 0.2066 0.2326 0.0016  0.0034  0.0206  882  ASP A CB  
6336  C CG  . ASP A 884  ? 0.3253 0.2774 0.3009 0.0015  0.0044  0.0224  882  ASP A CG  
6337  O OD1 . ASP A 884  ? 0.3190 0.2735 0.2921 0.0014  0.0057  0.0225  882  ASP A OD1 
6338  O OD2 . ASP A 884  ? 0.2975 0.2489 0.2753 0.0015  0.0037  0.0237  882  ASP A OD2 
6339  N N   . VAL A 885  ? 0.3138 0.2607 0.2935 0.0042  0.0009  0.0144  883  VAL A N   
6340  C CA  . VAL A 885  ? 0.2978 0.2424 0.2791 0.0041  -0.0006 0.0125  883  VAL A CA  
6341  C C   . VAL A 885  ? 0.3226 0.2666 0.3065 0.0065  -0.0018 0.0089  883  VAL A C   
6342  O O   . VAL A 885  ? 0.2893 0.2321 0.2760 0.0075  -0.0026 0.0090  883  VAL A O   
6343  C CB  . VAL A 885  ? 0.3397 0.2811 0.3236 0.0020  -0.0019 0.0150  883  VAL A CB  
6344  C CG1 . VAL A 885  ? 0.2949 0.2339 0.2812 0.0018  -0.0037 0.0130  883  VAL A CG1 
6345  C CG2 . VAL A 885  ? 0.3298 0.2726 0.3111 -0.0001 -0.0007 0.0181  883  VAL A CG2 
6346  N N   . GLY A 886  ? 0.2676 0.2127 0.2505 0.0077  -0.0021 0.0056  884  GLY A N   
6347  C CA  . GLY A 886  ? 0.2772 0.2221 0.2626 0.0101  -0.0033 0.0015  884  GLY A CA  
6348  C C   . GLY A 886  ? 0.2876 0.2282 0.2772 0.0098  -0.0058 0.0000  884  GLY A C   
6349  O O   . GLY A 886  ? 0.2821 0.2196 0.2735 0.0075  -0.0067 0.0028  884  GLY A O   
6350  N N   . PRO A 887  ? 0.3063 0.2471 0.2976 0.0120  -0.0071 -0.0045 885  PRO A N   
6351  C CA  . PRO A 887  ? 0.3025 0.2389 0.2985 0.0119  -0.0099 -0.0065 885  PRO A CA  
6352  C C   . PRO A 887  ? 0.3349 0.2710 0.3300 0.0103  -0.0104 -0.0072 885  PRO A C   
6353  O O   . PRO A 887  ? 0.2931 0.2327 0.2836 0.0100  -0.0087 -0.0069 885  PRO A O   
6354  C CB  . PRO A 887  ? 0.3265 0.2641 0.3244 0.0153  -0.0109 -0.0118 885  PRO A CB  
6355  C CG  . PRO A 887  ? 0.3071 0.2509 0.2996 0.0166  -0.0085 -0.0131 885  PRO A CG  
6356  C CD  . PRO A 887  ? 0.3016 0.2469 0.2906 0.0147  -0.0061 -0.0081 885  PRO A CD  
6357  N N   . VAL A 888  ? 0.2837 0.2156 0.2833 0.0094  -0.0129 -0.0080 886  VAL A N   
6358  C CA  . VAL A 888  ? 0.3001 0.2320 0.2995 0.0084  -0.0137 -0.0099 886  VAL A CA  
6359  C C   . VAL A 888  ? 0.2878 0.2214 0.2876 0.0115  -0.0149 -0.0159 886  VAL A C   
6360  O O   . VAL A 888  ? 0.2896 0.2237 0.2906 0.0140  -0.0152 -0.0183 886  VAL A O   
6361  C CB  . VAL A 888  ? 0.3361 0.2634 0.3403 0.0057  -0.0158 -0.0078 886  VAL A CB  
6362  C CG1 . VAL A 888  ? 0.2961 0.2233 0.2988 0.0028  -0.0142 -0.0019 886  VAL A CG1 
6363  C CG2 . VAL A 888  ? 0.3066 0.2291 0.3170 0.0064  -0.0184 -0.0090 886  VAL A CG2 
6364  N N   . ILE A 889  ? 0.2948 0.2298 0.2935 0.0114  -0.0155 -0.0186 887  ILE A N   
6365  C CA  . ILE A 889  ? 0.3068 0.2456 0.3038 0.0144  -0.0157 -0.0241 887  ILE A CA  
6366  C C   . ILE A 889  ? 0.3149 0.2510 0.3174 0.0165  -0.0186 -0.0290 887  ILE A C   
6367  O O   . ILE A 889  ? 0.3156 0.2549 0.3172 0.0197  -0.0185 -0.0332 887  ILE A O   
6368  C CB  . ILE A 889  ? 0.2974 0.2391 0.2911 0.0138  -0.0155 -0.0253 887  ILE A CB  
6369  C CG1 . ILE A 889  ? 0.3235 0.2701 0.3145 0.0170  -0.0155 -0.0306 887  ILE A CG1 
6370  C CG2 . ILE A 889  ? 0.3063 0.2440 0.3044 0.0116  -0.0179 -0.0256 887  ILE A CG2 
6371  C CD1 . ILE A 889  ? 0.3389 0.2907 0.3249 0.0187  -0.0128 -0.0297 887  ILE A CD1 
6372  N N   . THR A 890  ? 0.2984 0.2287 0.3067 0.0149  -0.0212 -0.0286 888  THR A N   
6373  C CA  . THR A 890  ? 0.3038 0.2308 0.3181 0.0167  -0.0244 -0.0335 888  THR A CA  
6374  C C   . THR A 890  ? 0.3058 0.2260 0.3265 0.0148  -0.0264 -0.0304 888  THR A C   
6375  O O   . THR A 890  ? 0.3165 0.2348 0.3372 0.0117  -0.0256 -0.0248 888  THR A O   
6376  C CB  . THR A 890  ? 0.3245 0.2516 0.3404 0.0168  -0.0265 -0.0381 888  THR A CB  
6377  O OG1 . THR A 890  ? 0.3241 0.2489 0.3410 0.0131  -0.0268 -0.0344 888  THR A OG1 
6378  C CG2 . THR A 890  ? 0.3251 0.2591 0.3350 0.0192  -0.0250 -0.0418 888  THR A CG2 
6379  N N   . SER A 891  ? 0.3208 0.2376 0.3473 0.0169  -0.0293 -0.0344 889  SER A N   
6380  C CA  . SER A 891  ? 0.3658 0.2756 0.3994 0.0151  -0.0320 -0.0319 889  SER A CA  
6381  C C   . SER A 891  ? 0.3569 0.2635 0.3932 0.0114  -0.0334 -0.0298 889  SER A C   
6382  O O   . SER A 891  ? 0.3437 0.2462 0.3831 0.0084  -0.0340 -0.0245 889  SER A O   
6383  C CB  . SER A 891  ? 0.3822 0.2887 0.4218 0.0182  -0.0352 -0.0374 889  SER A CB  
6384  O OG  . SER A 891  ? 0.5077 0.4169 0.5455 0.0215  -0.0340 -0.0388 889  SER A OG  
6385  N N   . GLU A 892  ? 0.3626 0.2714 0.3981 0.0116  -0.0341 -0.0339 890  GLU A N   
6386  C CA  . GLU A 892  ? 0.3765 0.2831 0.4146 0.0081  -0.0354 -0.0322 890  GLU A CA  
6387  C C   . GLU A 892  ? 0.3758 0.2844 0.4095 0.0048  -0.0325 -0.0255 890  GLU A C   
6388  O O   . GLU A 892  ? 0.3554 0.2609 0.3926 0.0013  -0.0332 -0.0212 890  GLU A O   
6389  C CB  . GLU A 892  ? 0.4011 0.3107 0.4383 0.0093  -0.0364 -0.0381 890  GLU A CB  
6390  C CG  . GLU A 892  ? 0.5053 0.4148 0.5450 0.0133  -0.0387 -0.0456 890  GLU A CG  
6391  C CD  . GLU A 892  ? 0.4680 0.3838 0.5012 0.0170  -0.0362 -0.0483 890  GLU A CD  
6392  O OE1 . GLU A 892  ? 0.6437 0.5654 0.6707 0.0174  -0.0340 -0.0489 890  GLU A OE1 
6393  O OE2 . GLU A 892  ? 0.4742 0.3892 0.5088 0.0195  -0.0364 -0.0495 890  GLU A OE2 
6394  N N   . ALA A 893  ? 0.3433 0.2574 0.3698 0.0059  -0.0292 -0.0247 891  ALA A N   
6395  C CA  . ALA A 893  ? 0.3372 0.2533 0.3596 0.0032  -0.0265 -0.0187 891  ALA A CA  
6396  C C   . ALA A 893  ? 0.4037 0.3163 0.4286 0.0015  -0.0264 -0.0133 891  ALA A C   
6397  O O   . ALA A 893  ? 0.3724 0.2840 0.3983 -0.0018 -0.0260 -0.0084 891  ALA A O   
6398  C CB  . ALA A 893  ? 0.2966 0.2186 0.3115 0.0050  -0.0233 -0.0190 891  ALA A CB  
6399  N N   . LYS A 894  ? 0.3319 0.2430 0.3582 0.0038  -0.0268 -0.0141 892  LYS A N   
6400  C CA  . LYS A 894  ? 0.3591 0.2674 0.3873 0.0025  -0.0266 -0.0089 892  LYS A CA  
6401  C C   . LYS A 894  ? 0.3917 0.2945 0.4267 -0.0004 -0.0293 -0.0063 892  LYS A C   
6402  O O   . LYS A 894  ? 0.3728 0.2749 0.4079 -0.0034 -0.0286 -0.0005 892  LYS A O   
6403  C CB  . LYS A 894  ? 0.3240 0.2316 0.3531 0.0058  -0.0270 -0.0110 892  LYS A CB  
6404  C CG  . LYS A 894  ? 0.3604 0.2644 0.3927 0.0048  -0.0276 -0.0062 892  LYS A CG  
6405  C CD  . LYS A 894  ? 0.3798 0.2832 0.4136 0.0084  -0.0283 -0.0088 892  LYS A CD  
6406  C CE  . LYS A 894  ? 0.4131 0.3128 0.4504 0.0075  -0.0293 -0.0040 892  LYS A CE  
6407  N NZ  . LYS A 894  ? 0.5017 0.4009 0.5408 0.0112  -0.0301 -0.0070 892  LYS A NZ  
6408  N N   . ASP A 895  ? 0.3865 0.2855 0.4271 0.0005  -0.0326 -0.0105 893  ASP A N   
6409  C CA  . ASP A 895  ? 0.3931 0.2865 0.4411 -0.0024 -0.0355 -0.0081 893  ASP A CA  
6410  C C   . ASP A 895  ? 0.3791 0.2739 0.4265 -0.0063 -0.0347 -0.0046 893  ASP A C   
6411  O O   . ASP A 895  ? 0.4243 0.3166 0.4749 -0.0096 -0.0353 0.0009  893  ASP A O   
6412  C CB  . ASP A 895  ? 0.4149 0.3042 0.4690 -0.0005 -0.0392 -0.0141 893  ASP A CB  
6413  C CG  . ASP A 895  ? 0.5597 0.4470 0.6158 0.0033  -0.0405 -0.0174 893  ASP A CG  
6414  O OD1 . ASP A 895  ? 0.5690 0.4563 0.6237 0.0038  -0.0392 -0.0137 893  ASP A OD1 
6415  O OD2 . ASP A 895  ? 0.5987 0.4848 0.6580 0.0060  -0.0428 -0.0240 893  ASP A OD2 
6416  N N   . ASN A 896  ? 0.3484 0.2474 0.3918 -0.0061 -0.0335 -0.0076 894  ASN A N   
6417  C CA  . ASN A 896  ? 0.3877 0.2889 0.4305 -0.0096 -0.0326 -0.0047 894  ASN A CA  
6418  C C   . ASN A 896  ? 0.3722 0.2759 0.4112 -0.0118 -0.0299 0.0020  894  ASN A C   
6419  O O   . ASN A 896  ? 0.3557 0.2587 0.3973 -0.0153 -0.0300 0.0066  894  ASN A O   
6420  C CB  . ASN A 896  ? 0.4388 0.3448 0.4771 -0.0083 -0.0316 -0.0091 894  ASN A CB  
6421  C CG  . ASN A 896  ? 0.5315 0.4401 0.5691 -0.0116 -0.0308 -0.0066 894  ASN A CG  
6422  O OD1 . ASN A 896  ? 0.5975 0.5100 0.6301 -0.0126 -0.0280 -0.0031 894  ASN A OD1 
6423  N ND2 . ASN A 896  ? 0.5001 0.4068 0.5429 -0.0132 -0.0333 -0.0087 894  ASN A ND2 
6424  N N   . ILE A 897  ? 0.3685 0.2754 0.4016 -0.0097 -0.0273 0.0024  895  ILE A N   
6425  C CA  . ILE A 897  ? 0.3363 0.2458 0.3657 -0.0114 -0.0247 0.0081  895  ILE A CA  
6426  C C   . ILE A 897  ? 0.3722 0.2779 0.4059 -0.0132 -0.0258 0.0130  895  ILE A C   
6427  O O   . ILE A 897  ? 0.3538 0.2604 0.3877 -0.0163 -0.0251 0.0182  895  ILE A O   
6428  C CB  . ILE A 897  ? 0.3502 0.2635 0.3729 -0.0088 -0.0220 0.0071  895  ILE A CB  
6429  C CG1 . ILE A 897  ? 0.3166 0.2340 0.3347 -0.0075 -0.0207 0.0033  895  ILE A CG1 
6430  C CG2 . ILE A 897  ? 0.3566 0.2722 0.3760 -0.0104 -0.0196 0.0126  895  ILE A CG2 
6431  C CD1 . ILE A 897  ? 0.3278 0.2481 0.3409 -0.0043 -0.0189 0.0009  895  ILE A CD1 
6432  N N   . GLU A 898  ? 0.3588 0.2603 0.3960 -0.0112 -0.0278 0.0114  896  GLU A N   
6433  C CA  . GLU A 898  ? 0.4040 0.3019 0.4451 -0.0125 -0.0290 0.0163  896  GLU A CA  
6434  C C   . GLU A 898  ? 0.3729 0.2671 0.4204 -0.0160 -0.0314 0.0193  896  GLU A C   
6435  O O   . GLU A 898  ? 0.3843 0.2775 0.4336 -0.0185 -0.0315 0.0253  896  GLU A O   
6436  C CB  . GLU A 898  ? 0.4024 0.2969 0.4458 -0.0091 -0.0306 0.0135  896  GLU A CB  
6437  C CG  . GLU A 898  ? 0.4171 0.3160 0.4542 -0.0060 -0.0280 0.0114  896  GLU A CG  
6438  C CD  . GLU A 898  ? 0.4974 0.3940 0.5363 -0.0030 -0.0290 0.0103  896  GLU A CD  
6439  O OE1 . GLU A 898  ? 0.5163 0.4086 0.5605 -0.0013 -0.0319 0.0068  896  GLU A OE1 
6440  O OE2 . GLU A 898  ? 0.5319 0.4312 0.5671 -0.0023 -0.0270 0.0127  896  GLU A OE2 
6441  N N   . LYS A 899  ? 0.3564 0.2490 0.4075 -0.0164 -0.0333 0.0155  897  LYS A N   
6442  C CA  . LYS A 899  ? 0.3456 0.2353 0.4029 -0.0202 -0.0355 0.0184  897  LYS A CA  
6443  C C   . LYS A 899  ? 0.3559 0.2504 0.4101 -0.0237 -0.0330 0.0236  897  LYS A C   
6444  O O   . LYS A 899  ? 0.3724 0.2658 0.4304 -0.0271 -0.0337 0.0292  897  LYS A O   
6445  C CB  . LYS A 899  ? 0.3788 0.2666 0.4400 -0.0198 -0.0378 0.0126  897  LYS A CB  
6446  N N   . HIS A 900  ? 0.3552 0.2554 0.4028 -0.0230 -0.0301 0.0220  898  HIS A N   
6447  C CA  . HIS A 900  ? 0.3501 0.2554 0.3946 -0.0259 -0.0277 0.0264  898  HIS A CA  
6448  C C   . HIS A 900  ? 0.3436 0.2498 0.3866 -0.0268 -0.0264 0.0324  898  HIS A C   
6449  O O   . HIS A 900  ? 0.3785 0.2862 0.4231 -0.0302 -0.0261 0.0378  898  HIS A O   
6450  C CB  . HIS A 900  ? 0.3425 0.2533 0.3803 -0.0243 -0.0251 0.0233  898  HIS A CB  
6451  C CG  . HIS A 900  ? 0.4077 0.3241 0.4417 -0.0265 -0.0224 0.0275  898  HIS A CG  
6452  N ND1 . HIS A 900  ? 0.3974 0.3162 0.4335 -0.0297 -0.0224 0.0295  898  HIS A ND1 
6453  C CD2 . HIS A 900  ? 0.3677 0.2878 0.3961 -0.0259 -0.0198 0.0300  898  HIS A CD2 
6454  C CE1 . HIS A 900  ? 0.4187 0.3427 0.4506 -0.0308 -0.0198 0.0328  898  HIS A CE1 
6455  N NE2 . HIS A 900  ? 0.3677 0.2925 0.3949 -0.0285 -0.0182 0.0330  898  HIS A NE2 
6456  N N   . ILE A 901  ? 0.3433 0.2491 0.3830 -0.0239 -0.0256 0.0316  899  ILE A N   
6457  C CA  . ILE A 901  ? 0.3531 0.2602 0.3908 -0.0245 -0.0243 0.0370  899  ILE A CA  
6458  C C   . ILE A 901  ? 0.3958 0.2988 0.4398 -0.0269 -0.0267 0.0419  899  ILE A C   
6459  O O   . ILE A 901  ? 0.3884 0.2938 0.4321 -0.0296 -0.0258 0.0477  899  ILE A O   
6460  C CB  . ILE A 901  ? 0.3519 0.2591 0.3859 -0.0208 -0.0234 0.0348  899  ILE A CB  
6461  C CG1 . ILE A 901  ? 0.3394 0.2513 0.3668 -0.0189 -0.0207 0.0310  899  ILE A CG1 
6462  C CG2 . ILE A 901  ? 0.3301 0.2382 0.3630 -0.0215 -0.0226 0.0402  899  ILE A CG2 
6463  C CD1 . ILE A 901  ? 0.2988 0.2106 0.3234 -0.0152 -0.0201 0.0276  899  ILE A CD1 
6464  N N   . GLU A 902  ? 0.3558 0.2526 0.4058 -0.0260 -0.0299 0.0396  900  GLU A N   
6465  C CA  . GLU A 902  ? 0.4050 0.2970 0.4615 -0.0283 -0.0325 0.0443  900  GLU A CA  
6466  C C   . GLU A 902  ? 0.3573 0.2505 0.4173 -0.0328 -0.0329 0.0484  900  GLU A C   
6467  O O   . GLU A 902  ? 0.4147 0.3074 0.4775 -0.0356 -0.0336 0.0548  900  GLU A O   
6468  C CB  . GLU A 902  ? 0.3939 0.2789 0.4565 -0.0260 -0.0361 0.0403  900  GLU A CB  
6469  C CG  . GLU A 902  ? 0.4840 0.3680 0.5442 -0.0218 -0.0359 0.0376  900  GLU A CG  
6470  C CD  . GLU A 902  ? 0.5002 0.3864 0.5573 -0.0221 -0.0343 0.0432  900  GLU A CD  
6471  O OE1 . GLU A 902  ? 0.5507 0.4351 0.6113 -0.0248 -0.0355 0.0494  900  GLU A OE1 
6472  O OE2 . GLU A 902  ? 0.4815 0.3714 0.5326 -0.0196 -0.0319 0.0417  900  GLU A OE2 
6473  N N   . ARG A 903  ? 0.3821 0.2772 0.4421 -0.0337 -0.0326 0.0449  901  ARG A N   
6474  C CA  . ARG A 903  ? 0.3687 0.2658 0.4319 -0.0380 -0.0328 0.0487  901  ARG A CA  
6475  C C   . ARG A 903  ? 0.4427 0.3467 0.5010 -0.0401 -0.0296 0.0542  901  ARG A C   
6476  O O   . ARG A 903  ? 0.4356 0.3407 0.4970 -0.0438 -0.0299 0.0602  901  ARG A O   
6477  C CB  . ARG A 903  ? 0.4449 0.3434 0.5086 -0.0382 -0.0330 0.0434  901  ARG A CB  
6478  N N   . MET A 904  ? 0.4232 0.3321 0.4740 -0.0378 -0.0267 0.0522  902  MET A N   
6479  C CA  . MET A 904  ? 0.3824 0.2978 0.4283 -0.0393 -0.0238 0.0568  902  MET A CA  
6480  C C   . MET A 904  ? 0.4516 0.3659 0.4985 -0.0401 -0.0243 0.0627  902  MET A C   
6481  O O   . MET A 904  ? 0.4779 0.3959 0.5253 -0.0433 -0.0235 0.0686  902  MET A O   
6482  C CB  . MET A 904  ? 0.3751 0.2949 0.4134 -0.0363 -0.0209 0.0530  902  MET A CB  
6483  C CG  . MET A 904  ? 0.3708 0.2931 0.4072 -0.0357 -0.0201 0.0481  902  MET A CG  
6484  S SD  . MET A 904  ? 0.4902 0.4181 0.5282 -0.0399 -0.0192 0.0511  902  MET A SD  
6485  C CE  . MET A 904  ? 0.4729 0.3955 0.5189 -0.0415 -0.0226 0.0486  902  MET A CE  
6486  N N   . ARG A 905  ? 0.4139 0.3234 0.4612 -0.0373 -0.0256 0.0614  903  ARG A N   
6487  C CA  . ARG A 905  ? 0.4357 0.3438 0.4844 -0.0379 -0.0264 0.0670  903  ARG A CA  
6488  C C   . ARG A 905  ? 0.4522 0.3568 0.5083 -0.0415 -0.0290 0.0720  903  ARG A C   
6489  O O   . ARG A 905  ? 0.4520 0.3586 0.5086 -0.0439 -0.0289 0.0787  903  ARG A O   
6490  C CB  . ARG A 905  ? 0.3950 0.2984 0.4437 -0.0340 -0.0276 0.0640  903  ARG A CB  
6491  C CG  . ARG A 905  ? 0.4667 0.3701 0.5147 -0.0338 -0.0278 0.0693  903  ARG A CG  
6492  C CD  . ARG A 905  ? 0.4725 0.3703 0.5225 -0.0303 -0.0298 0.0666  903  ARG A CD  
6493  N NE  . ARG A 905  ? 0.4653 0.3629 0.5126 -0.0267 -0.0290 0.0592  903  ARG A NE  
6494  C CZ  . ARG A 905  ? 0.4217 0.3232 0.4629 -0.0242 -0.0266 0.0569  903  ARG A CZ  
6495  N NH1 . ARG A 905  ? 0.4400 0.3462 0.4768 -0.0248 -0.0246 0.0609  903  ARG A NH1 
6496  N NH2 . ARG A 905  ? 0.4927 0.3936 0.5322 -0.0210 -0.0262 0.0506  903  ARG A NH2 
6497  N N   . GLY A 906  ? 0.4087 0.3082 0.4706 -0.0421 -0.0315 0.0690  904  GLY A N   
6498  C CA  . GLY A 906  ? 0.4647 0.3605 0.5344 -0.0458 -0.0342 0.0736  904  GLY A CA  
6499  C C   . GLY A 906  ? 0.4618 0.3638 0.5312 -0.0502 -0.0326 0.0790  904  GLY A C   
6500  O O   . GLY A 906  ? 0.4937 0.3947 0.5679 -0.0536 -0.0340 0.0855  904  GLY A O   
6501  N N   . LEU A 907  ? 0.4267 0.3356 0.4908 -0.0502 -0.0296 0.0766  905  LEU A N   
6502  C CA  . LEU A 907  ? 0.4483 0.3644 0.5115 -0.0540 -0.0276 0.0811  905  LEU A CA  
6503  C C   . LEU A 907  ? 0.4270 0.3493 0.4848 -0.0544 -0.0251 0.0864  905  LEU A C   
6504  O O   . LEU A 907  ? 0.5219 0.4515 0.5781 -0.0572 -0.0231 0.0898  905  LEU A O   
6505  C CB  . LEU A 907  ? 0.4866 0.4074 0.5466 -0.0535 -0.0256 0.0760  905  LEU A CB  
6506  C CG  . LEU A 907  ? 0.5006 0.4167 0.5659 -0.0536 -0.0280 0.0710  905  LEU A CG  
6507  C CD1 . LEU A 907  ? 0.5131 0.4338 0.5740 -0.0522 -0.0260 0.0654  905  LEU A CD1 
6508  C CD2 . LEU A 907  ? 0.4599 0.3746 0.5330 -0.0583 -0.0301 0.0756  905  LEU A CD2 
6509  N N   . GLY A 908  ? 0.4337 0.3538 0.4890 -0.0517 -0.0253 0.0868  906  GLY A N   
6510  C CA  . GLY A 908  ? 0.4901 0.4161 0.5405 -0.0519 -0.0232 0.0915  906  GLY A CA  
6511  C C   . GLY A 908  ? 0.4496 0.3821 0.4919 -0.0496 -0.0199 0.0880  906  GLY A C   
6512  O O   . GLY A 908  ? 0.4549 0.3933 0.4930 -0.0499 -0.0180 0.0915  906  GLY A O   
6513  N N   . ARG A 909  ? 0.4381 0.3699 0.4783 -0.0472 -0.0192 0.0812  907  ARG A N   
6514  C CA  . ARG A 909  ? 0.4111 0.3483 0.4440 -0.0448 -0.0163 0.0778  907  ARG A CA  
6515  C C   . ARG A 909  ? 0.4410 0.3764 0.4705 -0.0416 -0.0161 0.0772  907  ARG A C   
6516  O O   . ARG A 909  ? 0.4562 0.3851 0.4885 -0.0399 -0.0182 0.0760  907  ARG A O   
6517  C CB  . ARG A 909  ? 0.4168 0.3533 0.4484 -0.0430 -0.0158 0.0710  907  ARG A CB  
6518  C CG  . ARG A 909  ? 0.4350 0.3730 0.4703 -0.0458 -0.0161 0.0707  907  ARG A CG  
6519  C CD  . ARG A 909  ? 0.5043 0.4507 0.5374 -0.0484 -0.0139 0.0743  907  ARG A CD  
6520  N NE  . ARG A 909  ? 0.5853 0.5336 0.6216 -0.0507 -0.0141 0.0731  907  ARG A NE  
6521  C CZ  . ARG A 909  ? 0.6179 0.5656 0.6602 -0.0544 -0.0155 0.0770  907  ARG A CZ  
6522  N NH1 . ARG A 909  ? 0.5738 0.5191 0.6196 -0.0564 -0.0170 0.0828  907  ARG A NH1 
6523  N NH2 . ARG A 909  ? 0.6952 0.6448 0.7404 -0.0562 -0.0157 0.0753  907  ARG A NH2 
6524  N N   . LYS A 910  ? 0.4014 0.3430 0.4249 -0.0407 -0.0136 0.0776  908  LYS A N   
6525  C CA  . LYS A 910  ? 0.4064 0.3472 0.4263 -0.0377 -0.0132 0.0764  908  LYS A CA  
6526  C C   . LYS A 910  ? 0.3892 0.3266 0.4075 -0.0343 -0.0131 0.0697  908  LYS A C   
6527  O O   . LYS A 910  ? 0.3729 0.3130 0.3885 -0.0337 -0.0116 0.0659  908  LYS A O   
6528  C CB  . LYS A 910  ? 0.4397 0.3882 0.4539 -0.0377 -0.0107 0.0783  908  LYS A CB  
6529  C CG  . LYS A 910  ? 0.5031 0.4559 0.5183 -0.0407 -0.0108 0.0852  908  LYS A CG  
6530  C CD  . LYS A 910  ? 0.5676 0.5277 0.5770 -0.0400 -0.0086 0.0864  908  LYS A CD  
6531  C CE  . LYS A 910  ? 0.5704 0.5282 0.5769 -0.0366 -0.0086 0.0839  908  LYS A CE  
6532  N NZ  . LYS A 910  ? 0.7132 0.6779 0.7148 -0.0361 -0.0070 0.0855  908  LYS A NZ  
6533  N N   . VAL A 911  ? 0.3707 0.3026 0.3906 -0.0320 -0.0147 0.0683  909  VAL A N   
6534  C CA  . VAL A 911  ? 0.3275 0.2562 0.3465 -0.0288 -0.0148 0.0622  909  VAL A CA  
6535  C C   . VAL A 911  ? 0.3769 0.3059 0.3926 -0.0261 -0.0142 0.0618  909  VAL A C   
6536  O O   . VAL A 911  ? 0.3693 0.2961 0.3873 -0.0259 -0.0156 0.0649  909  VAL A O   
6537  C CB  . VAL A 911  ? 0.3290 0.2508 0.3539 -0.0284 -0.0177 0.0602  909  VAL A CB  
6538  C CG1 . VAL A 911  ? 0.3386 0.2577 0.3623 -0.0247 -0.0178 0.0541  909  VAL A CG1 
6539  C CG2 . VAL A 911  ? 0.3409 0.2626 0.3692 -0.0312 -0.0183 0.0601  909  VAL A CG2 
6540  N N   . GLU A 912  ? 0.3129 0.2448 0.3238 -0.0241 -0.0122 0.0581  910  GLU A N   
6541  C CA  . GLU A 912  ? 0.3514 0.2839 0.3594 -0.0215 -0.0115 0.0569  910  GLU A CA  
6542  C C   . GLU A 912  ? 0.3628 0.2920 0.3709 -0.0186 -0.0118 0.0514  910  GLU A C   
6543  O O   . GLU A 912  ? 0.3402 0.2702 0.3468 -0.0183 -0.0110 0.0478  910  GLU A O   
6544  C CB  . GLU A 912  ? 0.3433 0.2819 0.3457 -0.0215 -0.0090 0.0571  910  GLU A CB  
6545  C CG  . GLU A 912  ? 0.3365 0.2762 0.3362 -0.0193 -0.0083 0.0565  910  GLU A CG  
6546  C CD  . GLU A 912  ? 0.4077 0.3481 0.4083 -0.0200 -0.0092 0.0613  910  GLU A CD  
6547  O OE1 . GLU A 912  ? 0.4058 0.3473 0.4080 -0.0225 -0.0097 0.0655  910  GLU A OE1 
6548  O OE2 . GLU A 912  ? 0.4424 0.3827 0.4421 -0.0180 -0.0093 0.0610  910  GLU A OE2 
6549  N N   . GLN A 913  ? 0.3061 0.2321 0.3160 -0.0165 -0.0131 0.0507  911  GLN A N   
6550  C CA  . GLN A 913  ? 0.3369 0.2606 0.3470 -0.0136 -0.0134 0.0455  911  GLN A CA  
6551  C C   . GLN A 913  ? 0.3440 0.2686 0.3524 -0.0112 -0.0128 0.0451  911  GLN A C   
6552  O O   . GLN A 913  ? 0.3382 0.2626 0.3477 -0.0114 -0.0136 0.0486  911  GLN A O   
6553  C CB  . GLN A 913  ? 0.3127 0.2307 0.3286 -0.0131 -0.0161 0.0439  911  GLN A CB  
6554  C CG  . GLN A 913  ? 0.4170 0.3334 0.4355 -0.0153 -0.0170 0.0437  911  GLN A CG  
6555  C CD  . GLN A 913  ? 0.4024 0.3135 0.4262 -0.0140 -0.0196 0.0403  911  GLN A CD  
6556  O OE1 . GLN A 913  ? 0.4860 0.3929 0.5142 -0.0135 -0.0219 0.0417  911  GLN A OE1 
6557  N NE2 . GLN A 913  ? 0.3605 0.2715 0.3837 -0.0133 -0.0195 0.0357  911  GLN A NE2 
6558  N N   . ILE A 914  ? 0.3799 0.3056 0.3859 -0.0089 -0.0117 0.0407  912  ILE A N   
6559  C CA  . ILE A 914  ? 0.3655 0.2920 0.3706 -0.0065 -0.0113 0.0398  912  ILE A CA  
6560  C C   . ILE A 914  ? 0.3946 0.3167 0.4043 -0.0044 -0.0136 0.0379  912  ILE A C   
6561  O O   . ILE A 914  ? 0.3834 0.3025 0.3960 -0.0041 -0.0149 0.0352  912  ILE A O   
6562  C CB  . ILE A 914  ? 0.4138 0.3438 0.4143 -0.0051 -0.0090 0.0365  912  ILE A CB  
6563  C CG1 . ILE A 914  ? 0.4082 0.3372 0.4086 -0.0043 -0.0090 0.0323  912  ILE A CG1 
6564  C CG2 . ILE A 914  ? 0.4352 0.3694 0.4317 -0.0069 -0.0071 0.0387  912  ILE A CG2 
6565  C CD1 . ILE A 914  ? 0.4521 0.3817 0.4520 -0.0014 -0.0085 0.0283  912  ILE A CD1 
6566  N N   . GLY A 915  ? 0.3959 0.3178 0.4068 -0.0030 -0.0142 0.0392  913  GLY A N   
6567  C CA  . GLY A 915  ? 0.4147 0.3329 0.4301 -0.0006 -0.0164 0.0369  913  GLY A CA  
6568  C C   . GLY A 915  ? 0.3988 0.3187 0.4126 0.0022  -0.0153 0.0314  913  GLY A C   
6569  O O   . GLY A 915  ? 0.4241 0.3483 0.4337 0.0028  -0.0130 0.0306  913  GLY A O   
6570  N N   . LEU A 916  ? 0.3628 0.2796 0.3801 0.0039  -0.0169 0.0276  914  LEU A N   
6571  C CA  . LEU A 916  ? 0.4229 0.3417 0.4389 0.0067  -0.0160 0.0222  914  LEU A CA  
6572  C C   . LEU A 916  ? 0.4277 0.3463 0.4465 0.0098  -0.0170 0.0206  914  LEU A C   
6573  O O   . LEU A 916  ? 0.4465 0.3613 0.4699 0.0103  -0.0195 0.0222  914  LEU A O   
6574  C CB  . LEU A 916  ? 0.4266 0.3431 0.4446 0.0072  -0.0172 0.0182  914  LEU A CB  
6575  C CG  . LEU A 916  ? 0.4046 0.3220 0.4196 0.0046  -0.0161 0.0188  914  LEU A CG  
6576  C CD1 . LEU A 916  ? 0.4112 0.3272 0.4280 0.0056  -0.0172 0.0140  914  LEU A CD1 
6577  C CD2 . LEU A 916  ? 0.3966 0.3193 0.4055 0.0041  -0.0129 0.0194  914  LEU A CD2 
6578  N N   . ALA A 917  ? 0.4310 0.3538 0.4471 0.0119  -0.0152 0.0174  915  ALA A N   
6579  C CA  . ALA A 917  ? 0.4691 0.3928 0.4878 0.0151  -0.0159 0.0151  915  ALA A CA  
6580  C C   . ALA A 917  ? 0.4669 0.3872 0.4904 0.0175  -0.0184 0.0106  915  ALA A C   
6581  O O   . ALA A 917  ? 0.4276 0.3463 0.4512 0.0171  -0.0188 0.0081  915  ALA A O   
6582  C CB  . ALA A 917  ? 0.4630 0.3927 0.4776 0.0164  -0.0131 0.0131  915  ALA A CB  
6583  N N   . SER A 918  ? 0.4500 0.3691 0.4777 0.0202  -0.0201 0.0094  916  SER A N   
6584  C CA  . SER A 918  ? 0.4665 0.3824 0.4993 0.0229  -0.0227 0.0047  916  SER A CA  
6585  C C   . SER A 918  ? 0.4294 0.3493 0.4599 0.0250  -0.0213 -0.0013 916  SER A C   
6586  O O   . SER A 918  ? 0.4281 0.3455 0.4614 0.0262  -0.0231 -0.0054 916  SER A O   
6587  C CB  . SER A 918  ? 0.4961 0.4108 0.5336 0.0257  -0.0246 0.0043  916  SER A CB  
6588  O OG  . SER A 918  ? 0.5814 0.5024 0.6162 0.0277  -0.0224 0.0029  916  SER A OG  
6589  N N   . GLU A 919  ? 0.4173 0.3436 0.4427 0.0252  -0.0181 -0.0017 917  GLU A N   
6590  C CA  . GLU A 919  ? 0.4469 0.3779 0.4696 0.0271  -0.0166 -0.0068 917  GLU A CA  
6591  C C   . GLU A 919  ? 0.4260 0.3557 0.4470 0.0256  -0.0166 -0.0081 917  GLU A C   
6592  O O   . GLU A 919  ? 0.4197 0.3525 0.4394 0.0274  -0.0161 -0.0129 917  GLU A O   
6593  C CB  . GLU A 919  ? 0.4663 0.4042 0.4839 0.0270  -0.0131 -0.0057 917  GLU A CB  
6594  C CG  . GLU A 919  ? 0.5284 0.4699 0.5477 0.0296  -0.0127 -0.0067 917  GLU A CG  
6595  C CD  . GLU A 919  ? 0.6168 0.5567 0.6372 0.0283  -0.0130 -0.0017 917  GLU A CD  
6596  O OE1 . GLU A 919  ? 0.5673 0.5026 0.5880 0.0256  -0.0141 0.0024  917  GLU A OE1 
6597  O OE2 . GLU A 919  ? 0.7078 0.6516 0.7286 0.0299  -0.0122 -0.0018 917  GLU A OE2 
6598  N N   . THR A 920  ? 0.3955 0.3213 0.4161 0.0223  -0.0171 -0.0041 918  THR A N   
6599  C CA  . THR A 920  ? 0.3888 0.3136 0.4079 0.0207  -0.0172 -0.0054 918  THR A CA  
6600  C C   . THR A 920  ? 0.3900 0.3104 0.4144 0.0221  -0.0204 -0.0095 918  THR A C   
6601  O O   . THR A 920  ? 0.3684 0.2890 0.3919 0.0218  -0.0206 -0.0123 918  THR A O   
6602  C CB  . THR A 920  ? 0.3994 0.3221 0.4169 0.0167  -0.0167 0.0001  918  THR A CB  
6603  O OG1 . THR A 920  ? 0.4150 0.3324 0.4372 0.0156  -0.0191 0.0034  918  THR A OG1 
6604  C CG2 . THR A 920  ? 0.3450 0.2721 0.3571 0.0153  -0.0136 0.0035  918  THR A CG2 
6605  N N   . GLY A 921  ? 0.3596 0.2762 0.3898 0.0238  -0.0230 -0.0102 919  GLY A N   
6606  C CA  . GLY A 921  ? 0.4015 0.3133 0.4375 0.0253  -0.0264 -0.0143 919  GLY A CA  
6607  C C   . GLY A 921  ? 0.3940 0.3094 0.4292 0.0282  -0.0264 -0.0214 919  GLY A C   
6608  O O   . GLY A 921  ? 0.4241 0.3360 0.4629 0.0287  -0.0289 -0.0250 919  GLY A O   
6609  N N   . VAL A 922  ? 0.4027 0.3251 0.4333 0.0302  -0.0236 -0.0235 920  VAL A N   
6610  C CA  . VAL A 922  ? 0.3898 0.3166 0.4192 0.0331  -0.0233 -0.0301 920  VAL A CA  
6611  C C   . VAL A 922  ? 0.3867 0.3157 0.4113 0.0312  -0.0219 -0.0306 920  VAL A C   
6612  O O   . VAL A 922  ? 0.3889 0.3214 0.4123 0.0334  -0.0220 -0.0360 920  VAL A O   
6613  C CB  . VAL A 922  ? 0.3732 0.3073 0.3997 0.0360  -0.0209 -0.0321 920  VAL A CB  
6614  C CG1 . VAL A 922  ? 0.3931 0.3254 0.4251 0.0387  -0.0228 -0.0333 920  VAL A CG1 
6615  C CG2 . VAL A 922  ? 0.3448 0.2830 0.3653 0.0336  -0.0173 -0.0270 920  VAL A CG2 
6616  N N   . GLY A 923  ? 0.3713 0.2987 0.3932 0.0274  -0.0208 -0.0252 921  GLY A N   
6617  C CA  . GLY A 923  ? 0.3671 0.2962 0.3850 0.0256  -0.0197 -0.0254 921  GLY A CA  
6618  C C   . GLY A 923  ? 0.3479 0.2711 0.3684 0.0222  -0.0214 -0.0222 921  GLY A C   
6619  O O   . GLY A 923  ? 0.3825 0.3000 0.4086 0.0217  -0.0240 -0.0208 921  GLY A O   
6620  N N   . THR A 924  ? 0.3122 0.2369 0.3288 0.0199  -0.0201 -0.0207 922  THR A N   
6621  C CA  . THR A 924  ? 0.3401 0.2603 0.3592 0.0166  -0.0216 -0.0179 922  THR A CA  
6622  C C   . THR A 924  ? 0.3401 0.2617 0.3549 0.0135  -0.0191 -0.0119 922  THR A C   
6623  O O   . THR A 924  ? 0.3054 0.2305 0.3153 0.0125  -0.0172 -0.0117 922  THR A O   
6624  C CB  . THR A 924  ? 0.3455 0.2660 0.3648 0.0167  -0.0228 -0.0223 922  THR A CB  
6625  O OG1 . THR A 924  ? 0.3022 0.2289 0.3150 0.0175  -0.0202 -0.0237 922  THR A OG1 
6626  C CG2 . THR A 924  ? 0.3342 0.2526 0.3585 0.0198  -0.0258 -0.0284 922  THR A CG2 
6627  N N   . PHE A 925  ? 0.3204 0.2394 0.3369 0.0120  -0.0192 -0.0072 923  PHE A N   
6628  C CA  . PHE A 925  ? 0.3211 0.2418 0.3339 0.0093  -0.0170 -0.0018 923  PHE A CA  
6629  C C   . PHE A 925  ? 0.3326 0.2492 0.3485 0.0060  -0.0184 0.0024  923  PHE A C   
6630  O O   . PHE A 925  ? 0.3418 0.2536 0.3632 0.0058  -0.0210 0.0028  923  PHE A O   
6631  C CB  . PHE A 925  ? 0.2974 0.2197 0.3088 0.0103  -0.0156 0.0007  923  PHE A CB  
6632  C CG  . PHE A 925  ? 0.2879 0.2152 0.2959 0.0130  -0.0137 -0.0024 923  PHE A CG  
6633  C CD1 . PHE A 925  ? 0.2891 0.2167 0.2997 0.0163  -0.0149 -0.0070 923  PHE A CD1 
6634  C CD2 . PHE A 925  ? 0.2882 0.2200 0.2906 0.0123  -0.0108 -0.0008 923  PHE A CD2 
6635  C CE1 . PHE A 925  ? 0.3065 0.2396 0.3139 0.0187  -0.0130 -0.0096 923  PHE A CE1 
6636  C CE2 . PHE A 925  ? 0.2804 0.2171 0.2798 0.0145  -0.0091 -0.0031 923  PHE A CE2 
6637  C CZ  . PHE A 925  ? 0.2834 0.2210 0.2852 0.0177  -0.0100 -0.0074 923  PHE A CZ  
6638  N N   . VAL A 926  ? 0.2869 0.2056 0.2992 0.0035  -0.0166 0.0055  924  VAL A N   
6639  C CA  . VAL A 926  ? 0.3333 0.2498 0.3474 0.0001  -0.0171 0.0103  924  VAL A CA  
6640  C C   . VAL A 926  ? 0.3348 0.2543 0.3450 -0.0009 -0.0148 0.0147  924  VAL A C   
6641  O O   . VAL A 926  ? 0.2909 0.2144 0.2960 -0.0006 -0.0125 0.0142  924  VAL A O   
6642  C CB  . VAL A 926  ? 0.3211 0.2381 0.3348 -0.0020 -0.0173 0.0100  924  VAL A CB  
6643  C CG1 . VAL A 926  ? 0.3315 0.2475 0.3467 -0.0056 -0.0174 0.0153  924  VAL A CG1 
6644  C CG2 . VAL A 926  ? 0.3466 0.2606 0.3646 -0.0010 -0.0199 0.0054  924  VAL A CG2 
6645  N N   . PRO A 927  ? 0.3417 0.2593 0.3540 -0.0021 -0.0155 0.0189  925  PRO A N   
6646  C CA  . PRO A 927  ? 0.3271 0.2479 0.3357 -0.0031 -0.0134 0.0227  925  PRO A CA  
6647  C C   . PRO A 927  ? 0.3438 0.2672 0.3494 -0.0057 -0.0119 0.0248  925  PRO A C   
6648  O O   . PRO A 927  ? 0.2977 0.2195 0.3057 -0.0078 -0.0130 0.0259  925  PRO A O   
6649  C CB  . PRO A 927  ? 0.3406 0.2586 0.3529 -0.0039 -0.0149 0.0267  925  PRO A CB  
6650  C CG  . PRO A 927  ? 0.3750 0.2882 0.3929 -0.0046 -0.0177 0.0263  925  PRO A CG  
6651  C CD  . PRO A 927  ? 0.3257 0.2383 0.3441 -0.0027 -0.0183 0.0205  925  PRO A CD  
6652  N N   . PRO A 928  ? 0.3065 0.2341 0.3071 -0.0056 -0.0095 0.0252  926  PRO A N   
6653  C CA  . PRO A 928  ? 0.2926 0.2228 0.2905 -0.0079 -0.0082 0.0275  926  PRO A CA  
6654  C C   . PRO A 928  ? 0.3026 0.2321 0.3030 -0.0105 -0.0090 0.0321  926  PRO A C   
6655  O O   . PRO A 928  ? 0.2855 0.2141 0.2873 -0.0105 -0.0095 0.0348  926  PRO A O   
6656  C CB  . PRO A 928  ? 0.3120 0.2460 0.3053 -0.0070 -0.0059 0.0278  926  PRO A CB  
6657  C CG  . PRO A 928  ? 0.3591 0.2930 0.3517 -0.0043 -0.0058 0.0240  926  PRO A CG  
6658  C CD  . PRO A 928  ? 0.2961 0.2262 0.2935 -0.0032 -0.0080 0.0230  926  PRO A CD  
6659  N N   . THR A 929  ? 0.3048 0.2349 0.3059 -0.0127 -0.0091 0.0330  927  THR A N   
6660  C CA  . THR A 929  ? 0.3237 0.2529 0.3281 -0.0154 -0.0102 0.0371  927  THR A CA  
6661  C C   . THR A 929  ? 0.3342 0.2678 0.3359 -0.0176 -0.0086 0.0391  927  THR A C   
6662  O O   . THR A 929  ? 0.3237 0.2593 0.3231 -0.0174 -0.0076 0.0365  927  THR A O   
6663  C CB  . THR A 929  ? 0.3197 0.2447 0.3293 -0.0161 -0.0126 0.0358  927  THR A CB  
6664  O OG1 . THR A 929  ? 0.3353 0.2563 0.3476 -0.0138 -0.0142 0.0336  927  THR A OG1 
6665  C CG2 . THR A 929  ? 0.3351 0.2591 0.3485 -0.0193 -0.0138 0.0404  927  THR A CG2 
6666  N N   . ILE A 930  ? 0.2922 0.2275 0.2943 -0.0196 -0.0084 0.0437  928  ILE A N   
6667  C CA  . ILE A 930  ? 0.2950 0.2350 0.2955 -0.0219 -0.0071 0.0458  928  ILE A CA  
6668  C C   . ILE A 930  ? 0.3405 0.2795 0.3454 -0.0248 -0.0086 0.0496  928  ILE A C   
6669  O O   . ILE A 930  ? 0.3470 0.2841 0.3544 -0.0254 -0.0097 0.0530  928  ILE A O   
6670  C CB  . ILE A 930  ? 0.3006 0.2451 0.2969 -0.0217 -0.0054 0.0479  928  ILE A CB  
6671  C CG1 . ILE A 930  ? 0.3355 0.2810 0.3277 -0.0192 -0.0040 0.0445  928  ILE A CG1 
6672  C CG2 . ILE A 930  ? 0.2987 0.2484 0.2939 -0.0241 -0.0042 0.0502  928  ILE A CG2 
6673  C CD1 . ILE A 930  ? 0.3154 0.2644 0.3045 -0.0188 -0.0028 0.0462  928  ILE A CD1 
6674  N N   . ILE A 931  ? 0.2976 0.2381 0.3037 -0.0265 -0.0085 0.0492  929  ILE A N   
6675  C CA  . ILE A 931  ? 0.3280 0.2681 0.3387 -0.0297 -0.0098 0.0527  929  ILE A CA  
6676  C C   . ILE A 931  ? 0.3484 0.2952 0.3571 -0.0318 -0.0080 0.0550  929  ILE A C   
6677  O O   . ILE A 931  ? 0.2991 0.2487 0.3054 -0.0314 -0.0068 0.0520  929  ILE A O   
6678  C CB  . ILE A 931  ? 0.3236 0.2595 0.3388 -0.0300 -0.0117 0.0499  929  ILE A CB  
6679  C CG1 . ILE A 931  ? 0.3213 0.2513 0.3384 -0.0274 -0.0135 0.0470  929  ILE A CG1 
6680  C CG2 . ILE A 931  ? 0.3565 0.2921 0.3770 -0.0336 -0.0131 0.0540  929  ILE A CG2 
6681  C CD1 . ILE A 931  ? 0.3311 0.2571 0.3521 -0.0273 -0.0154 0.0431  929  ILE A CD1 
6682  N N   . GLU A 932  ? 0.3410 0.2905 0.3507 -0.0341 -0.0079 0.0602  930  GLU A N   
6683  C CA  . GLU A 932  ? 0.3479 0.3045 0.3556 -0.0361 -0.0061 0.0625  930  GLU A CA  
6684  C C   . GLU A 932  ? 0.3732 0.3304 0.3857 -0.0393 -0.0070 0.0645  930  GLU A C   
6685  O O   . GLU A 932  ? 0.3933 0.3475 0.4104 -0.0414 -0.0087 0.0682  930  GLU A O   
6686  C CB  . GLU A 932  ? 0.3257 0.2861 0.3315 -0.0368 -0.0053 0.0671  930  GLU A CB  
6687  C CG  . GLU A 932  ? 0.3686 0.3291 0.3698 -0.0338 -0.0044 0.0650  930  GLU A CG  
6688  C CD  . GLU A 932  ? 0.4309 0.3943 0.4307 -0.0342 -0.0042 0.0694  930  GLU A CD  
6689  O OE1 . GLU A 932  ? 0.4342 0.4037 0.4332 -0.0363 -0.0032 0.0728  930  GLU A OE1 
6690  O OE2 . GLU A 932  ? 0.4213 0.3812 0.4207 -0.0325 -0.0049 0.0694  930  GLU A OE2 
6691  N N   . LEU A 933  ? 0.3231 0.2840 0.3349 -0.0398 -0.0060 0.0620  931  LEU A N   
6692  C CA  . LEU A 933  ? 0.4091 0.3708 0.4255 -0.0427 -0.0068 0.0632  931  LEU A CA  
6693  C C   . LEU A 933  ? 0.4560 0.4260 0.4717 -0.0454 -0.0052 0.0670  931  LEU A C   
6694  O O   . LEU A 933  ? 0.4357 0.4113 0.4468 -0.0443 -0.0032 0.0668  931  LEU A O   
6695  C CB  . LEU A 933  ? 0.4251 0.3856 0.4417 -0.0416 -0.0071 0.0578  931  LEU A CB  
6696  C CG  . LEU A 933  ? 0.4129 0.3661 0.4305 -0.0391 -0.0088 0.0535  931  LEU A CG  
6697  C CD1 . LEU A 933  ? 0.3807 0.3343 0.3977 -0.0379 -0.0088 0.0484  931  LEU A CD1 
6698  C CD2 . LEU A 933  ? 0.4298 0.3770 0.4535 -0.0406 -0.0114 0.0556  931  LEU A CD2 
6699  N N   . GLU A 934  ? 0.4692 0.4401 0.4900 -0.0488 -0.0061 0.0703  932  GLU A N   
6700  C CA  . GLU A 934  ? 0.4679 0.4474 0.4886 -0.0516 -0.0044 0.0737  932  GLU A CA  
6701  C C   . GLU A 934  ? 0.5841 0.5683 0.6034 -0.0510 -0.0032 0.0695  932  GLU A C   
6702  O O   . GLU A 934  ? 0.5411 0.5327 0.5567 -0.0505 -0.0011 0.0693  932  GLU A O   
6703  C CB  . GLU A 934  ? 0.5205 0.4996 0.5475 -0.0557 -0.0059 0.0791  932  GLU A CB  
6704  N N   . LYS A 935  ? 0.5393 0.5193 0.5615 -0.0508 -0.0045 0.0658  933  LYS A N   
6705  C CA  . LYS A 935  ? 0.5858 0.5698 0.6071 -0.0501 -0.0037 0.0618  933  LYS A CA  
6706  C C   . LYS A 935  ? 0.5240 0.5019 0.5443 -0.0471 -0.0048 0.0560  933  LYS A C   
6707  O O   . LYS A 935  ? 0.5104 0.4811 0.5330 -0.0465 -0.0067 0.0552  933  LYS A O   
6708  C CB  . LYS A 935  ? 0.5634 0.5508 0.5903 -0.0539 -0.0043 0.0637  933  LYS A CB  
6709  N N   . LEU A 936  ? 0.5089 0.4900 0.5260 -0.0451 -0.0037 0.0518  934  LEU A N   
6710  C CA  . LEU A 936  ? 0.5667 0.5431 0.5829 -0.0424 -0.0047 0.0465  934  LEU A CA  
6711  C C   . LEU A 936  ? 0.5575 0.5298 0.5793 -0.0439 -0.0070 0.0454  934  LEU A C   
6712  O O   . LEU A 936  ? 0.5312 0.4981 0.5529 -0.0418 -0.0084 0.0416  934  LEU A O   
6713  C CB  . LEU A 936  ? 0.5491 0.5303 0.5615 -0.0404 -0.0034 0.0429  934  LEU A CB  
6714  N N   . SER A 937  ? 0.5608 0.5357 0.5875 -0.0476 -0.0076 0.0486  935  SER A N   
6715  C CA  . SER A 937  ? 0.5556 0.5267 0.5885 -0.0495 -0.0100 0.0477  935  SER A CA  
6716  C C   . SER A 937  ? 0.5457 0.5091 0.5822 -0.0499 -0.0121 0.0493  935  SER A C   
6717  O O   . SER A 937  ? 0.5681 0.5268 0.6094 -0.0507 -0.0145 0.0475  935  SER A O   
6718  C CB  . SER A 937  ? 0.5647 0.5416 0.6022 -0.0535 -0.0097 0.0510  935  SER A CB  
6719  O OG  . SER A 937  ? 0.5987 0.5803 0.6354 -0.0555 -0.0081 0.0565  935  SER A OG  
6720  N N   . ASP A 938  ? 0.5505 0.5123 0.5847 -0.0494 -0.0115 0.0525  936  ASP A N   
6721  C CA  . ASP A 938  ? 0.5345 0.4887 0.5717 -0.0491 -0.0137 0.0534  936  ASP A CA  
6722  C C   . ASP A 938  ? 0.5136 0.4620 0.5496 -0.0456 -0.0150 0.0475  936  ASP A C   
6723  O O   . ASP A 938  ? 0.5276 0.4695 0.5677 -0.0454 -0.0174 0.0468  936  ASP A O   
6724  C CB  . ASP A 938  ? 0.5225 0.4767 0.5569 -0.0487 -0.0126 0.0576  936  ASP A CB  
6725  C CG  . ASP A 938  ? 0.6074 0.5682 0.6422 -0.0519 -0.0112 0.0635  936  ASP A CG  
6726  O OD1 . ASP A 938  ? 0.6283 0.5931 0.6665 -0.0548 -0.0111 0.0648  936  ASP A OD1 
6727  O OD2 . ASP A 938  ? 0.6172 0.5797 0.6490 -0.0515 -0.0100 0.0668  936  ASP A OD2 
6728  N N   . LEU A 939  ? 0.4793 0.4302 0.5100 -0.0427 -0.0135 0.0434  937  LEU A N   
6729  C CA  A LEU A 939  ? 0.5027 0.4495 0.5315 -0.0393 -0.0144 0.0379  937  LEU A CA  
6730  C CA  B LEU A 939  ? 0.5026 0.4493 0.5314 -0.0393 -0.0144 0.0379  937  LEU A CA  
6731  C C   . LEU A 939  ? 0.5095 0.4564 0.5410 -0.0396 -0.0157 0.0339  937  LEU A C   
6732  O O   . LEU A 939  ? 0.5145 0.4666 0.5438 -0.0395 -0.0145 0.0325  937  LEU A O   
6733  C CB  A LEU A 939  ? 0.4679 0.4172 0.4896 -0.0361 -0.0121 0.0361  937  LEU A CB  
6734  C CB  B LEU A 939  ? 0.4683 0.4176 0.4899 -0.0361 -0.0121 0.0360  937  LEU A CB  
6735  C CG  A LEU A 939  ? 0.4628 0.4083 0.4819 -0.0325 -0.0127 0.0312  937  LEU A CG  
6736  C CG  B LEU A 939  ? 0.4508 0.3956 0.4697 -0.0329 -0.0124 0.0338  937  LEU A CG  
6737  C CD1 A LEU A 939  ? 0.4430 0.3825 0.4646 -0.0318 -0.0143 0.0318  937  LEU A CD1 
6738  C CD1 B LEU A 939  ? 0.4348 0.3826 0.4473 -0.0300 -0.0104 0.0313  937  LEU A CD1 
6739  C CD2 A LEU A 939  ? 0.4357 0.3842 0.4481 -0.0299 -0.0104 0.0301  937  LEU A CD2 
6740  C CD2 B LEU A 939  ? 0.4513 0.3906 0.4737 -0.0317 -0.0149 0.0300  937  LEU A CD2 
6741  N N   . GLN A 940  ? 0.4890 0.4306 0.5255 -0.0398 -0.0184 0.0318  938  GLN A N   
6742  C CA  . GLN A 940  ? 0.5461 0.4876 0.5860 -0.0404 -0.0201 0.0282  938  GLN A CA  
6743  C C   . GLN A 940  ? 0.6051 0.5431 0.6437 -0.0369 -0.0215 0.0220  938  GLN A C   
6744  O O   . GLN A 940  ? 0.6082 0.5455 0.6502 -0.0372 -0.0234 0.0185  938  GLN A O   
6745  C CB  . GLN A 940  ? 0.5552 0.4940 0.6032 -0.0442 -0.0225 0.0308  938  GLN A CB  
6746  N N   . ARG A 941  ? 0.5789 0.5151 0.6127 -0.0336 -0.0206 0.0205  939  ARG A N   
6747  C CA  . ARG A 941  ? 0.5669 0.5006 0.5991 -0.0302 -0.0218 0.0148  939  ARG A CA  
6748  C C   . ARG A 941  ? 0.5086 0.4438 0.5337 -0.0270 -0.0195 0.0140  939  ARG A C   
6749  O O   . ARG A 941  ? 0.4854 0.4211 0.5082 -0.0272 -0.0179 0.0177  939  ARG A O   
6750  C CB  . ARG A 941  ? 0.5755 0.5028 0.6130 -0.0299 -0.0246 0.0134  939  ARG A CB  
6751  N N   . GLU A 942  ? 0.5486 0.4847 0.5702 -0.0242 -0.0195 0.0093  940  GLU A N   
6752  C CA  . GLU A 942  ? 0.5300 0.4671 0.5455 -0.0211 -0.0176 0.0085  940  GLU A CA  
6753  C C   . GLU A 942  ? 0.5116 0.4441 0.5283 -0.0195 -0.0185 0.0080  940  GLU A C   
6754  O O   . GLU A 942  ? 0.5323 0.4613 0.5530 -0.0189 -0.0209 0.0050  940  GLU A O   
6755  C CB  . GLU A 942  ? 0.5814 0.5209 0.5929 -0.0185 -0.0175 0.0039  940  GLU A CB  
6756  C CG  . GLU A 942  ? 0.5893 0.5310 0.5942 -0.0161 -0.0151 0.0042  940  GLU A CG  
6757  C CD  . GLU A 942  ? 0.6548 0.5983 0.6558 -0.0132 -0.0151 -0.0001 940  GLU A CD  
6758  O OE1 . GLU A 942  ? 0.6719 0.6144 0.6752 -0.0124 -0.0171 -0.0040 940  GLU A OE1 
6759  O OE2 . GLU A 942  ? 0.5958 0.5420 0.5916 -0.0118 -0.0132 0.0005  940  GLU A OE2 
6760  N N   . VAL A 943  ? 0.4377 0.3703 0.4513 -0.0189 -0.0168 0.0108  941  VAL A N   
6761  C CA  . VAL A 943  ? 0.4099 0.3387 0.4244 -0.0173 -0.0174 0.0107  941  VAL A CA  
6762  C C   . VAL A 943  ? 0.4001 0.3310 0.4086 -0.0141 -0.0156 0.0088  941  VAL A C   
6763  O O   . VAL A 943  ? 0.3476 0.2810 0.3521 -0.0142 -0.0134 0.0114  941  VAL A O   
6764  C CB  . VAL A 943  ? 0.3635 0.2908 0.3801 -0.0193 -0.0171 0.0160  941  VAL A CB  
6765  C CG1 . VAL A 943  ? 0.3803 0.3040 0.3976 -0.0173 -0.0178 0.0157  941  VAL A CG1 
6766  C CG2 . VAL A 943  ? 0.4681 0.3936 0.4909 -0.0226 -0.0190 0.0182  941  VAL A CG2 
6767  N N   . PHE A 944  ? 0.3662 0.2962 0.3742 -0.0115 -0.0165 0.0041  942  PHE A N   
6768  C CA  . PHE A 944  ? 0.3467 0.2796 0.3490 -0.0087 -0.0148 0.0020  942  PHE A CA  
6769  C C   . PHE A 944  ? 0.3364 0.2678 0.3380 -0.0069 -0.0142 0.0026  942  PHE A C   
6770  O O   . PHE A 944  ? 0.3461 0.2766 0.3478 -0.0044 -0.0150 -0.0009 942  PHE A O   
6771  C CB  . PHE A 944  ? 0.3343 0.2683 0.3360 -0.0067 -0.0160 -0.0032 942  PHE A CB  
6772  C CG  . PHE A 944  ? 0.3460 0.2843 0.3416 -0.0049 -0.0141 -0.0044 942  PHE A CG  
6773  C CD1 . PHE A 944  ? 0.3431 0.2843 0.3360 -0.0061 -0.0129 -0.0027 942  PHE A CD1 
6774  C CD2 . PHE A 944  ? 0.3385 0.2779 0.3310 -0.0020 -0.0135 -0.0070 942  PHE A CD2 
6775  C CE1 . PHE A 944  ? 0.3634 0.3081 0.3509 -0.0045 -0.0114 -0.0034 942  PHE A CE1 
6776  C CE2 . PHE A 944  ? 0.3344 0.2777 0.3214 -0.0005 -0.0118 -0.0075 942  PHE A CE2 
6777  C CZ  . PHE A 944  ? 0.3239 0.2695 0.3085 -0.0018 -0.0109 -0.0056 942  PHE A CZ  
6778  N N   . GLY A 945  ? 0.2784 0.2099 0.2791 -0.0082 -0.0129 0.0069  943  GLY A N   
6779  C CA  . GLY A 945  ? 0.2975 0.2275 0.2981 -0.0069 -0.0125 0.0080  943  GLY A CA  
6780  C C   . GLY A 945  ? 0.2944 0.2261 0.2925 -0.0082 -0.0105 0.0126  943  GLY A C   
6781  O O   . GLY A 945  ? 0.3043 0.2385 0.3007 -0.0099 -0.0095 0.0146  943  GLY A O   
6782  N N   . PRO A 946  ? 0.2832 0.2140 0.2812 -0.0073 -0.0101 0.0141  944  PRO A N   
6783  C CA  . PRO A 946  ? 0.2837 0.2166 0.2790 -0.0082 -0.0083 0.0179  944  PRO A CA  
6784  C C   . PRO A 946  ? 0.3034 0.2352 0.3016 -0.0109 -0.0089 0.0222  944  PRO A C   
6785  O O   . PRO A 946  ? 0.2892 0.2196 0.2891 -0.0112 -0.0093 0.0248  944  PRO A O   
6786  C CB  . PRO A 946  ? 0.2700 0.2023 0.2647 -0.0059 -0.0080 0.0173  944  PRO A CB  
6787  C CG  . PRO A 946  ? 0.2811 0.2096 0.2805 -0.0049 -0.0103 0.0152  944  PRO A CG  
6788  C CD  . PRO A 946  ? 0.2930 0.2207 0.2940 -0.0054 -0.0116 0.0122  944  PRO A CD  
6789  N N   . VAL A 947  ? 0.2983 0.2313 0.2973 -0.0130 -0.0091 0.0230  945  VAL A N   
6790  C CA  . VAL A 947  ? 0.2891 0.2215 0.2912 -0.0159 -0.0097 0.0270  945  VAL A CA  
6791  C C   . VAL A 947  ? 0.3140 0.2509 0.3136 -0.0177 -0.0081 0.0288  945  VAL A C   
6792  O O   . VAL A 947  ? 0.3317 0.2700 0.3312 -0.0182 -0.0082 0.0269  945  VAL A O   
6793  C CB  . VAL A 947  ? 0.3079 0.2368 0.3158 -0.0171 -0.0122 0.0262  945  VAL A CB  
6794  C CG1 . VAL A 947  ? 0.2946 0.2235 0.3057 -0.0204 -0.0128 0.0310  945  VAL A CG1 
6795  C CG2 . VAL A 947  ? 0.2804 0.2048 0.2912 -0.0151 -0.0140 0.0241  945  VAL A CG2 
6796  N N   . LEU A 948  ? 0.3010 0.2403 0.2986 -0.0185 -0.0068 0.0322  946  LEU A N   
6797  C CA  . LEU A 948  ? 0.3018 0.2459 0.2969 -0.0199 -0.0052 0.0338  946  LEU A CA  
6798  C C   . LEU A 948  ? 0.2919 0.2372 0.2902 -0.0229 -0.0057 0.0378  946  LEU A C   
6799  O O   . LEU A 948  ? 0.3036 0.2476 0.3037 -0.0238 -0.0063 0.0411  946  LEU A O   
6800  C CB  . LEU A 948  ? 0.2995 0.2462 0.2904 -0.0188 -0.0035 0.0348  946  LEU A CB  
6801  C CG  . LEU A 948  ? 0.2838 0.2356 0.2724 -0.0200 -0.0020 0.0362  946  LEU A CG  
6802  C CD1 . LEU A 948  ? 0.2576 0.2111 0.2448 -0.0197 -0.0016 0.0332  946  LEU A CD1 
6803  C CD2 . LEU A 948  ? 0.2926 0.2465 0.2776 -0.0190 -0.0007 0.0370  946  LEU A CD2 
6804  N N   . HIS A 949  ? 0.3104 0.2585 0.3093 -0.0246 -0.0055 0.0377  947  HIS A N   
6805  C CA  . HIS A 949  ? 0.2933 0.2438 0.2950 -0.0276 -0.0056 0.0416  947  HIS A CA  
6806  C C   . HIS A 949  ? 0.2911 0.2477 0.2891 -0.0281 -0.0036 0.0432  947  HIS A C   
6807  O O   . HIS A 949  ? 0.3160 0.2750 0.3106 -0.0267 -0.0024 0.0405  947  HIS A O   
6808  C CB  . HIS A 949  ? 0.2921 0.2422 0.2976 -0.0294 -0.0069 0.0406  947  HIS A CB  
6809  C CG  . HIS A 949  ? 0.3198 0.2640 0.3289 -0.0286 -0.0091 0.0382  947  HIS A CG  
6810  N ND1 . HIS A 949  ? 0.3251 0.2673 0.3327 -0.0261 -0.0094 0.0334  947  HIS A ND1 
6811  C CD2 . HIS A 949  ? 0.3128 0.2527 0.3271 -0.0299 -0.0111 0.0399  947  HIS A CD2 
6812  C CE1 . HIS A 949  ? 0.3384 0.2757 0.3500 -0.0257 -0.0116 0.0318  947  HIS A CE1 
6813  N NE2 . HIS A 949  ? 0.3426 0.2781 0.3585 -0.0280 -0.0127 0.0357  947  HIS A NE2 
6814  N N   . VAL A 950  ? 0.2899 0.2491 0.2887 -0.0301 -0.0032 0.0476  948  VAL A N   
6815  C CA  . VAL A 950  ? 0.3023 0.2678 0.2977 -0.0304 -0.0014 0.0491  948  VAL A CA  
6816  C C   . VAL A 950  ? 0.3215 0.2916 0.3195 -0.0336 -0.0012 0.0525  948  VAL A C   
6817  O O   . VAL A 950  ? 0.3164 0.2851 0.3181 -0.0357 -0.0023 0.0562  948  VAL A O   
6818  C CB  . VAL A 950  ? 0.3135 0.2793 0.3066 -0.0295 -0.0009 0.0512  948  VAL A CB  
6819  C CG1 . VAL A 950  ? 0.3116 0.2842 0.3012 -0.0296 0.0009  0.0521  948  VAL A CG1 
6820  C CG2 . VAL A 950  ? 0.2850 0.2465 0.2762 -0.0266 -0.0011 0.0481  948  VAL A CG2 
6821  N N   . ILE A 951  ? 0.3008 0.2767 0.2970 -0.0338 0.0002  0.0514  949  ILE A N   
6822  C CA  . ILE A 951  ? 0.3275 0.3096 0.3254 -0.0366 0.0008  0.0545  949  ILE A CA  
6823  C C   . ILE A 951  ? 0.3401 0.3291 0.3338 -0.0358 0.0027  0.0545  949  ILE A C   
6824  O O   . ILE A 951  ? 0.3127 0.3015 0.3028 -0.0332 0.0034  0.0512  949  ILE A O   
6825  C CB  . ILE A 951  ? 0.3818 0.3650 0.3827 -0.0379 0.0004  0.0528  949  ILE A CB  
6826  C CG1 . ILE A 951  ? 0.3601 0.3451 0.3578 -0.0356 0.0013  0.0481  949  ILE A CG1 
6827  C CG2 . ILE A 951  ? 0.4021 0.3783 0.4072 -0.0385 -0.0017 0.0522  949  ILE A CG2 
6828  C CD1 . ILE A 951  ? 0.4150 0.4012 0.4156 -0.0365 0.0007  0.0460  949  ILE A CD1 
6829  N N   . ARG A 952  ? 0.3096 0.3049 0.3041 -0.0381 0.0035  0.0582  950  ARG A N   
6830  C CA  . ARG A 952  ? 0.3377 0.3406 0.3286 -0.0375 0.0053  0.0582  950  ARG A CA  
6831  C C   . ARG A 952  ? 0.3522 0.3620 0.3442 -0.0389 0.0062  0.0576  950  ARG A C   
6832  O O   . ARG A 952  ? 0.3264 0.3366 0.3224 -0.0414 0.0056  0.0595  950  ARG A O   
6833  C CB  . ARG A 952  ? 0.3826 0.3886 0.3729 -0.0388 0.0056  0.0630  950  ARG A CB  
6834  C CG  . ARG A 952  ? 0.4482 0.4472 0.4387 -0.0380 0.0043  0.0644  950  ARG A CG  
6835  C CD  . ARG A 952  ? 0.4512 0.4520 0.4432 -0.0404 0.0039  0.0704  950  ARG A CD  
6836  N NE  . ARG A 952  ? 0.4923 0.4996 0.4805 -0.0398 0.0051  0.0717  950  ARG A NE  
6837  C CZ  . ARG A 952  ? 0.4535 0.4588 0.4395 -0.0383 0.0048  0.0725  950  ARG A CZ  
6838  N NH1 . ARG A 952  ? 0.4570 0.4544 0.4444 -0.0373 0.0033  0.0722  950  ARG A NH1 
6839  N NH2 . ARG A 952  ? 0.4237 0.4357 0.4063 -0.0378 0.0058  0.0733  950  ARG A NH2 
6840  N N   . TYR A 953  ? 0.3420 0.3576 0.3309 -0.0372 0.0075  0.0549  951  TYR A N   
6841  C CA  . TYR A 953  ? 0.3349 0.3576 0.3248 -0.0381 0.0085  0.0539  951  TYR A CA  
6842  C C   . TYR A 953  ? 0.3426 0.3741 0.3295 -0.0373 0.0101  0.0538  951  TYR A C   
6843  O O   . TYR A 953  ? 0.3607 0.3918 0.3441 -0.0351 0.0103  0.0523  951  TYR A O   
6844  C CB  . TYR A 953  ? 0.3387 0.3589 0.3289 -0.0362 0.0080  0.0490  951  TYR A CB  
6845  C CG  . TYR A 953  ? 0.3337 0.3533 0.3198 -0.0327 0.0084  0.0447  951  TYR A CG  
6846  C CD1 . TYR A 953  ? 0.2708 0.2831 0.2549 -0.0307 0.0077  0.0432  951  TYR A CD1 
6847  C CD2 . TYR A 953  ? 0.3023 0.3287 0.2869 -0.0315 0.0095  0.0423  951  TYR A CD2 
6848  C CE1 . TYR A 953  ? 0.2779 0.2895 0.2587 -0.0278 0.0080  0.0398  951  TYR A CE1 
6849  C CE2 . TYR A 953  ? 0.2761 0.3015 0.2575 -0.0283 0.0096  0.0385  951  TYR A CE2 
6850  C CZ  . TYR A 953  ? 0.2465 0.2644 0.2261 -0.0267 0.0088  0.0374  951  TYR A CZ  
6851  O OH  . TYR A 953  ? 0.2828 0.2994 0.2596 -0.0238 0.0088  0.0341  951  TYR A OH  
6852  N N   . ARG A 954  ? 0.3704 0.4103 0.3589 -0.0392 0.0111  0.0550  952  ARG A N   
6853  C CA  . ARG A 954  ? 0.3963 0.4456 0.3822 -0.0382 0.0126  0.0540  952  ARG A CA  
6854  C C   . ARG A 954  ? 0.3558 0.4063 0.3405 -0.0354 0.0128  0.0482  952  ARG A C   
6855  O O   . ARG A 954  ? 0.3832 0.4311 0.3701 -0.0353 0.0122  0.0461  952  ARG A O   
6856  C CB  . ARG A 954  ? 0.4362 0.4948 0.4243 -0.0414 0.0137  0.0578  952  ARG A CB  
6857  C CG  . ARG A 954  ? 0.5091 0.5663 0.4991 -0.0445 0.0133  0.0641  952  ARG A CG  
6858  C CD  . ARG A 954  ? 0.6143 0.6827 0.6037 -0.0464 0.0148  0.0680  952  ARG A CD  
6859  N NE  . ARG A 954  ? 0.6709 0.7381 0.6597 -0.0480 0.0145  0.0734  952  ARG A NE  
6860  C CZ  . ARG A 954  ? 0.6633 0.7279 0.6486 -0.0460 0.0142  0.0731  952  ARG A CZ  
6861  N NH1 . ARG A 954  ? 0.6013 0.6630 0.5835 -0.0424 0.0141  0.0677  952  ARG A NH1 
6862  N NH2 . ARG A 954  ? 0.6473 0.7121 0.6324 -0.0477 0.0138  0.0785  952  ARG A NH2 
6863  N N   . ARG A 955  ? 0.3762 0.4309 0.3576 -0.0329 0.0135  0.0456  953  ARG A N   
6864  C CA  . ARG A 955  ? 0.3610 0.4158 0.3412 -0.0299 0.0134  0.0400  953  ARG A CA  
6865  C C   . ARG A 955  ? 0.3767 0.4371 0.3596 -0.0306 0.0138  0.0386  953  ARG A C   
6866  O O   . ARG A 955  ? 0.4523 0.5092 0.4360 -0.0290 0.0130  0.0351  953  ARG A O   
6867  C CB  . ARG A 955  ? 0.4253 0.4849 0.4022 -0.0275 0.0140  0.0376  953  ARG A CB  
6868  C CG  . ARG A 955  ? 0.4744 0.5348 0.4504 -0.0243 0.0137  0.0319  953  ARG A CG  
6869  C CD  . ARG A 955  ? 0.4607 0.5116 0.4373 -0.0230 0.0124  0.0297  953  ARG A CD  
6870  N NE  . ARG A 955  ? 0.5557 0.6064 0.5318 -0.0199 0.0119  0.0248  953  ARG A NE  
6871  C CZ  . ARG A 955  ? 0.5572 0.6092 0.5352 -0.0194 0.0116  0.0226  953  ARG A CZ  
6872  N NH1 . ARG A 955  ? 0.4875 0.5421 0.4684 -0.0218 0.0119  0.0246  953  ARG A NH1 
6873  N NH2 . ARG A 955  ? 0.5108 0.5613 0.4883 -0.0165 0.0108  0.0184  953  ARG A NH2 
6874  N N   . ASP A 956  ? 0.3580 0.4275 0.3425 -0.0329 0.0150  0.0413  954  ASP A N   
6875  C CA  . ASP A 956  ? 0.3888 0.4645 0.3762 -0.0336 0.0154  0.0399  954  ASP A CA  
6876  C C   . ASP A 956  ? 0.3975 0.4672 0.3885 -0.0354 0.0143  0.0407  954  ASP A C   
6877  O O   . ASP A 956  ? 0.4298 0.5025 0.4232 -0.0353 0.0142  0.0385  954  ASP A O   
6878  C CB  . ASP A 956  ? 0.4043 0.4917 0.3928 -0.0360 0.0170  0.0430  954  ASP A CB  
6879  C CG  . ASP A 956  ? 0.4217 0.5175 0.4070 -0.0337 0.0182  0.0406  954  ASP A CG  
6880  O OD1 . ASP A 956  ? 0.4360 0.5288 0.4190 -0.0302 0.0176  0.0359  954  ASP A OD1 
6881  O OD2 . ASP A 956  ? 0.5199 0.6254 0.5051 -0.0354 0.0196  0.0435  954  ASP A OD2 
6882  N N   . ASP A 957  ? 0.3728 0.4342 0.3644 -0.0368 0.0133  0.0436  955  ASP A N   
6883  C CA  . ASP A 957  ? 0.3571 0.4123 0.3522 -0.0384 0.0120  0.0442  955  ASP A CA  
6884  C C   . ASP A 957  ? 0.3327 0.3789 0.3265 -0.0356 0.0106  0.0402  955  ASP A C   
6885  O O   . ASP A 957  ? 0.3411 0.3813 0.3373 -0.0366 0.0093  0.0403  955  ASP A O   
6886  C CB  . ASP A 957  ? 0.3840 0.4353 0.3812 -0.0415 0.0115  0.0495  955  ASP A CB  
6887  C CG  . ASP A 957  ? 0.4555 0.5152 0.4553 -0.0451 0.0125  0.0541  955  ASP A CG  
6888  O OD1 . ASP A 957  ? 0.4780 0.5453 0.4798 -0.0459 0.0133  0.0532  955  ASP A OD1 
6889  O OD2 . ASP A 957  ? 0.4868 0.5460 0.4867 -0.0471 0.0126  0.0589  955  ASP A OD2 
6890  N N   . LEU A 958  ? 0.3176 0.3631 0.3078 -0.0322 0.0108  0.0366  956  LEU A N   
6891  C CA  . LEU A 958  ? 0.3153 0.3526 0.3040 -0.0297 0.0095  0.0333  956  LEU A CA  
6892  C C   . LEU A 958  ? 0.3301 0.3664 0.3215 -0.0297 0.0086  0.0310  956  LEU A C   
6893  O O   . LEU A 958  ? 0.2919 0.3211 0.2839 -0.0294 0.0073  0.0304  956  LEU A O   
6894  C CB  . LEU A 958  ? 0.3535 0.3915 0.3386 -0.0263 0.0098  0.0299  956  LEU A CB  
6895  C CG  . LEU A 958  ? 0.3613 0.3916 0.3447 -0.0236 0.0087  0.0267  956  LEU A CG  
6896  C CD1 . LEU A 958  ? 0.2804 0.3023 0.2632 -0.0241 0.0079  0.0285  956  LEU A CD1 
6897  C CD2 . LEU A 958  ? 0.3318 0.3634 0.3122 -0.0206 0.0089  0.0238  956  LEU A CD2 
6898  N N   . ASP A 959  ? 0.3255 0.3695 0.3185 -0.0298 0.0092  0.0296  957  ASP A N   
6899  C CA  . ASP A 959  ? 0.3264 0.3699 0.3219 -0.0295 0.0082  0.0272  957  ASP A CA  
6900  C C   . ASP A 959  ? 0.2829 0.3236 0.2823 -0.0327 0.0073  0.0297  957  ASP A C   
6901  O O   . ASP A 959  ? 0.3196 0.3552 0.3200 -0.0322 0.0059  0.0279  957  ASP A O   
6902  C CB  . ASP A 959  ? 0.3671 0.4201 0.3639 -0.0290 0.0089  0.0252  957  ASP A CB  
6903  C CG  . ASP A 959  ? 0.3584 0.4107 0.3571 -0.0278 0.0077  0.0220  957  ASP A CG  
6904  O OD1 . ASP A 959  ? 0.3675 0.4136 0.3641 -0.0252 0.0066  0.0193  957  ASP A OD1 
6905  O OD2 . ASP A 959  ? 0.4657 0.5238 0.4681 -0.0297 0.0079  0.0223  957  ASP A OD2 
6906  N N   . ARG A 960  ? 0.3016 0.3456 0.3031 -0.0359 0.0080  0.0339  958  ARG A N   
6907  C CA  . ARG A 960  ? 0.3214 0.3618 0.3269 -0.0390 0.0070  0.0366  958  ARG A CA  
6908  C C   . ARG A 960  ? 0.3655 0.3956 0.3699 -0.0382 0.0056  0.0366  958  ARG A C   
6909  O O   . ARG A 960  ? 0.3591 0.3840 0.3661 -0.0390 0.0041  0.0360  958  ARG A O   
6910  C CB  . ARG A 960  ? 0.3709 0.4170 0.3789 -0.0427 0.0080  0.0416  958  ARG A CB  
6911  C CG  . ARG A 960  ? 0.4320 0.4754 0.4452 -0.0463 0.0068  0.0445  958  ARG A CG  
6912  C CD  . ARG A 960  ? 0.5238 0.5727 0.5393 -0.0500 0.0079  0.0502  958  ARG A CD  
6913  N NE  . ARG A 960  ? 0.5966 0.6570 0.6119 -0.0504 0.0098  0.0505  958  ARG A NE  
6914  C CZ  . ARG A 960  ? 0.5883 0.6553 0.6073 -0.0521 0.0100  0.0500  958  ARG A CZ  
6915  N NH1 . ARG A 960  ? 0.6135 0.6768 0.6367 -0.0534 0.0084  0.0489  958  ARG A NH1 
6916  N NH2 . ARG A 960  ? 0.6029 0.6811 0.6216 -0.0524 0.0119  0.0504  958  ARG A NH2 
6917  N N   . LEU A 961  ? 0.3275 0.3546 0.3280 -0.0366 0.0061  0.0372  959  LEU A N   
6918  C CA  . LEU A 961  ? 0.3375 0.3553 0.3368 -0.0356 0.0050  0.0370  959  LEU A CA  
6919  C C   . LEU A 961  ? 0.3388 0.3519 0.3372 -0.0332 0.0038  0.0327  959  LEU A C   
6920  O O   . LEU A 961  ? 0.3481 0.3550 0.3480 -0.0334 0.0024  0.0323  959  LEU A O   
6921  C CB  . LEU A 961  ? 0.3238 0.3403 0.3191 -0.0341 0.0058  0.0380  959  LEU A CB  
6922  C CG  . LEU A 961  ? 0.3391 0.3468 0.3324 -0.0323 0.0048  0.0370  959  LEU A CG  
6923  C CD1 . LEU A 961  ? 0.3737 0.3761 0.3703 -0.0344 0.0035  0.0395  959  LEU A CD1 
6924  C CD2 . LEU A 961  ? 0.3295 0.3370 0.3189 -0.0307 0.0057  0.0375  959  LEU A CD2 
6925  N N   . VAL A 962  ? 0.3030 0.3190 0.2990 -0.0307 0.0042  0.0295  960  VAL A N   
6926  C CA  . VAL A 962  ? 0.3331 0.3454 0.3282 -0.0283 0.0031  0.0258  960  VAL A CA  
6927  C C   . VAL A 962  ? 0.3452 0.3572 0.3444 -0.0300 0.0018  0.0251  960  VAL A C   
6928  O O   . VAL A 962  ? 0.3076 0.3142 0.3069 -0.0291 0.0004  0.0233  960  VAL A O   
6929  C CB  . VAL A 962  ? 0.3355 0.3516 0.3281 -0.0256 0.0036  0.0228  960  VAL A CB  
6930  C CG1 . VAL A 962  ? 0.2893 0.3022 0.2813 -0.0234 0.0023  0.0193  960  VAL A CG1 
6931  C CG2 . VAL A 962  ? 0.3445 0.3595 0.3332 -0.0238 0.0045  0.0230  960  VAL A CG2 
6932  N N   . ASP A 963  ? 0.3447 0.3631 0.3475 -0.0325 0.0022  0.0266  961  ASP A N   
6933  C CA  . ASP A 963  ? 0.3415 0.3600 0.3490 -0.0347 0.0010  0.0264  961  ASP A CA  
6934  C C   . ASP A 963  ? 0.3622 0.3736 0.3718 -0.0363 -0.0004 0.0281  961  ASP A C   
6935  O O   . ASP A 963  ? 0.3842 0.3919 0.3959 -0.0364 -0.0021 0.0261  961  ASP A O   
6936  C CB  . ASP A 963  ? 0.3259 0.3527 0.3372 -0.0377 0.0018  0.0286  961  ASP A CB  
6937  C CG  . ASP A 963  ? 0.3945 0.4285 0.4050 -0.0360 0.0027  0.0261  961  ASP A CG  
6938  O OD1 . ASP A 963  ? 0.4493 0.4814 0.4571 -0.0328 0.0021  0.0224  961  ASP A OD1 
6939  O OD2 . ASP A 963  ? 0.4848 0.5269 0.4977 -0.0380 0.0038  0.0278  961  ASP A OD2 
6940  N N   . ASP A 964  ? 0.3426 0.3525 0.3519 -0.0377 0.0003  0.0318  962  ASP A N   
6941  C CA  . ASP A 964  ? 0.4162 0.4194 0.4279 -0.0392 -0.0011 0.0335  962  ASP A CA  
6942  C C   . ASP A 964  ? 0.4056 0.4015 0.4146 -0.0362 -0.0022 0.0303  962  ASP A C   
6943  O O   . ASP A 964  ? 0.4565 0.4474 0.4681 -0.0366 -0.0040 0.0292  962  ASP A O   
6944  C CB  . ASP A 964  ? 0.4156 0.4188 0.4271 -0.0408 -0.0002 0.0380  962  ASP A CB  
6945  C CG  . ASP A 964  ? 0.4682 0.4787 0.4826 -0.0441 0.0008  0.0419  962  ASP A CG  
6946  O OD1 . ASP A 964  ? 0.4879 0.5032 0.5055 -0.0456 0.0007  0.0412  962  ASP A OD1 
6947  O OD2 . ASP A 964  ? 0.5552 0.5672 0.5688 -0.0453 0.0018  0.0458  962  ASP A OD2 
6948  N N   . VAL A 965  ? 0.3414 0.3368 0.3453 -0.0332 -0.0012 0.0287  963  VAL A N   
6949  C CA  . VAL A 965  ? 0.3766 0.3661 0.3777 -0.0304 -0.0021 0.0257  963  VAL A CA  
6950  C C   . VAL A 965  ? 0.3737 0.3628 0.3760 -0.0295 -0.0035 0.0222  963  VAL A C   
6951  O O   . VAL A 965  ? 0.3740 0.3583 0.3773 -0.0290 -0.0050 0.0204  963  VAL A O   
6952  C CB  . VAL A 965  ? 0.3416 0.3315 0.3375 -0.0276 -0.0008 0.0249  963  VAL A CB  
6953  C CG1 . VAL A 965  ? 0.3481 0.3327 0.3410 -0.0248 -0.0015 0.0221  963  VAL A CG1 
6954  C CG2 . VAL A 965  ? 0.3325 0.3224 0.3271 -0.0284 0.0004  0.0282  963  VAL A CG2 
6955  N N   . ASN A 966  ? 0.3627 0.3574 0.3650 -0.0292 -0.0030 0.0208  964  ASN A N   
6956  C CA  . ASN A 966  ? 0.3853 0.3805 0.3888 -0.0283 -0.0044 0.0174  964  ASN A CA  
6957  C C   . ASN A 966  ? 0.4009 0.3946 0.4096 -0.0309 -0.0061 0.0175  964  ASN A C   
6958  O O   . ASN A 966  ? 0.3854 0.3766 0.3947 -0.0299 -0.0077 0.0144  964  ASN A O   
6959  C CB  . ASN A 966  ? 0.3576 0.3596 0.3609 -0.0278 -0.0037 0.0163  964  ASN A CB  
6960  C CG  . ASN A 966  ? 0.3385 0.3412 0.3369 -0.0247 -0.0027 0.0150  964  ASN A CG  
6961  O OD1 . ASN A 966  ? 0.3384 0.3361 0.3333 -0.0225 -0.0029 0.0142  964  ASN A OD1 
6962  N ND2 . ASN A 966  ? 0.3240 0.3329 0.3224 -0.0244 -0.0018 0.0149  964  ASN A ND2 
6963  N N   . ALA A 967  ? 0.3558 0.3511 0.3684 -0.0342 -0.0058 0.0209  965  ALA A N   
6964  C CA  . ALA A 967  ? 0.4374 0.4320 0.4560 -0.0370 -0.0075 0.0211  965  ALA A CA  
6965  C C   . ALA A 967  ? 0.4061 0.3930 0.4259 -0.0367 -0.0094 0.0200  965  ALA A C   
6966  O O   . ALA A 967  ? 0.4159 0.4014 0.4406 -0.0385 -0.0112 0.0191  965  ALA A O   
6967  C CB  . ALA A 967  ? 0.4010 0.3994 0.4236 -0.0409 -0.0067 0.0257  965  ALA A CB  
6968  N N   . THR A 968  ? 0.4289 0.4112 0.4447 -0.0344 -0.0090 0.0198  966  THR A N   
6969  C CA  . THR A 968  ? 0.4249 0.4005 0.4416 -0.0335 -0.0108 0.0180  966  THR A CA  
6970  C C   . THR A 968  ? 0.4311 0.4059 0.4478 -0.0317 -0.0124 0.0132  966  THR A C   
6971  O O   . THR A 968  ? 0.4546 0.4249 0.4736 -0.0315 -0.0144 0.0112  966  THR A O   
6972  C CB  . THR A 968  ? 0.4566 0.4284 0.4687 -0.0311 -0.0099 0.0182  966  THR A CB  
6973  O OG1 . THR A 968  ? 0.4622 0.4353 0.4691 -0.0279 -0.0091 0.0155  966  THR A OG1 
6974  C CG2 . THR A 968  ? 0.3891 0.3622 0.4003 -0.0324 -0.0082 0.0227  966  THR A CG2 
6975  N N   . GLY A 969  ? 0.4305 0.4096 0.4445 -0.0302 -0.0118 0.0112  967  GLY A N   
6976  C CA  . GLY A 969  ? 0.4004 0.3792 0.4134 -0.0281 -0.0133 0.0069  967  GLY A CA  
6977  C C   . GLY A 969  ? 0.4102 0.3862 0.4175 -0.0244 -0.0130 0.0048  967  GLY A C   
6978  O O   . GLY A 969  ? 0.3738 0.3508 0.3790 -0.0223 -0.0138 0.0016  967  GLY A O   
6979  N N   . TYR A 970  ? 0.3682 0.3410 0.3731 -0.0237 -0.0119 0.0066  968  TYR A N   
6980  C CA  . TYR A 970  ? 0.3825 0.3531 0.3820 -0.0206 -0.0113 0.0053  968  TYR A CA  
6981  C C   . TYR A 970  ? 0.3921 0.3661 0.3873 -0.0191 -0.0096 0.0062  968  TYR A C   
6982  O O   . TYR A 970  ? 0.3772 0.3552 0.3735 -0.0205 -0.0087 0.0078  968  TYR A O   
6983  C CB  . TYR A 970  ? 0.4134 0.3796 0.4126 -0.0205 -0.0109 0.0070  968  TYR A CB  
6984  C CG  . TYR A 970  ? 0.4267 0.3887 0.4297 -0.0211 -0.0128 0.0055  968  TYR A CG  
6985  C CD1 . TYR A 970  ? 0.4317 0.3917 0.4332 -0.0187 -0.0141 0.0017  968  TYR A CD1 
6986  C CD2 . TYR A 970  ? 0.4495 0.4096 0.4575 -0.0239 -0.0136 0.0078  968  TYR A CD2 
6987  C CE1 . TYR A 970  ? 0.4929 0.4491 0.4980 -0.0189 -0.0160 -0.0003 968  TYR A CE1 
6988  C CE2 . TYR A 970  ? 0.4428 0.3986 0.4548 -0.0243 -0.0156 0.0062  968  TYR A CE2 
6989  C CZ  . TYR A 970  ? 0.5597 0.5135 0.5703 -0.0217 -0.0169 0.0019  968  TYR A CZ  
6990  O OH  . TYR A 970  ? 0.5874 0.5370 0.6020 -0.0218 -0.0192 -0.0002 968  TYR A OH  
6991  N N   . GLY A 971  ? 0.3795 0.3521 0.3700 -0.0164 -0.0091 0.0051  969  GLY A N   
6992  C CA  . GLY A 971  ? 0.3610 0.3361 0.3478 -0.0149 -0.0078 0.0057  969  GLY A CA  
6993  C C   . GLY A 971  ? 0.3578 0.3309 0.3398 -0.0121 -0.0075 0.0047  969  GLY A C   
6994  O O   . GLY A 971  ? 0.3289 0.3036 0.3085 -0.0102 -0.0078 0.0033  969  GLY A O   
6995  N N   . LEU A 972  ? 0.3599 0.3296 0.3408 -0.0118 -0.0069 0.0057  970  LEU A N   
6996  C CA  . LEU A 972  ? 0.2968 0.2647 0.2734 -0.0093 -0.0065 0.0050  970  LEU A CA  
6997  C C   . LEU A 972  ? 0.3699 0.3382 0.3438 -0.0088 -0.0048 0.0073  970  LEU A C   
6998  O O   . LEU A 972  ? 0.3338 0.3039 0.3054 -0.0076 -0.0045 0.0072  970  LEU A O   
6999  C CB  . LEU A 972  ? 0.3258 0.2903 0.3029 -0.0090 -0.0069 0.0043  970  LEU A CB  
7000  C CG  . LEU A 972  ? 0.3611 0.3246 0.3343 -0.0065 -0.0067 0.0030  970  LEU A CG  
7001  C CD1 . LEU A 972  ? 0.3087 0.2747 0.2795 -0.0048 -0.0075 0.0009  970  LEU A CD1 
7002  C CD2 . LEU A 972  ? 0.3414 0.3023 0.3163 -0.0062 -0.0076 0.0013  970  LEU A CD2 
7003  N N   . THR A 973  ? 0.3252 0.2916 0.2994 -0.0096 -0.0039 0.0093  971  THR A N   
7004  C CA  . THR A 973  ? 0.3057 0.2723 0.2776 -0.0092 -0.0025 0.0112  971  THR A CA  
7005  C C   . THR A 973  ? 0.3091 0.2773 0.2831 -0.0112 -0.0018 0.0134  971  THR A C   
7006  O O   . THR A 973  ? 0.3010 0.2690 0.2783 -0.0131 -0.0022 0.0142  971  THR A O   
7007  C CB  . THR A 973  ? 0.3068 0.2705 0.2767 -0.0082 -0.0018 0.0118  971  THR A CB  
7008  O OG1 . THR A 973  ? 0.3222 0.2838 0.2947 -0.0094 -0.0021 0.0124  971  THR A OG1 
7009  C CG2 . THR A 973  ? 0.3204 0.2833 0.2877 -0.0061 -0.0023 0.0099  971  THR A CG2 
7010  N N   . PHE A 974  ? 0.2775 0.2477 0.2500 -0.0108 -0.0008 0.0144  972  PHE A N   
7011  C CA  . PHE A 974  ? 0.2470 0.2199 0.2210 -0.0125 0.0000  0.0162  972  PHE A CA  
7012  C C   . PHE A 974  ? 0.2456 0.2185 0.2170 -0.0115 0.0011  0.0172  972  PHE A C   
7013  O O   . PHE A 974  ? 0.2452 0.2177 0.2143 -0.0097 0.0011  0.0162  972  PHE A O   
7014  C CB  . PHE A 974  ? 0.2631 0.2403 0.2388 -0.0131 -0.0002 0.0155  972  PHE A CB  
7015  C CG  . PHE A 974  ? 0.2455 0.2265 0.2223 -0.0145 0.0007  0.0172  972  PHE A CG  
7016  C CD1 . PHE A 974  ? 0.2462 0.2282 0.2258 -0.0169 0.0009  0.0193  972  PHE A CD1 
7017  C CD2 . PHE A 974  ? 0.2484 0.2321 0.2235 -0.0134 0.0014  0.0169  972  PHE A CD2 
7018  C CE1 . PHE A 974  ? 0.2513 0.2375 0.2315 -0.0182 0.0019  0.0211  972  PHE A CE1 
7019  C CE2 . PHE A 974  ? 0.2433 0.2313 0.2192 -0.0144 0.0024  0.0181  972  PHE A CE2 
7020  C CZ  . PHE A 974  ? 0.2681 0.2576 0.2464 -0.0169 0.0027  0.0204  972  PHE A CZ  
7021  N N   . GLY A 975  ? 0.2493 0.2227 0.2213 -0.0127 0.0018  0.0192  973  GLY A N   
7022  C CA  . GLY A 975  ? 0.2576 0.2314 0.2276 -0.0120 0.0027  0.0200  973  GLY A CA  
7023  C C   . GLY A 975  ? 0.2460 0.2243 0.2168 -0.0130 0.0034  0.0209  973  GLY A C   
7024  O O   . GLY A 975  ? 0.2435 0.2242 0.2166 -0.0149 0.0035  0.0223  973  GLY A O   
7025  N N   . LEU A 976  ? 0.2571 0.2369 0.2263 -0.0118 0.0038  0.0203  974  LEU A N   
7026  C CA  . LEU A 976  ? 0.2414 0.2260 0.2110 -0.0124 0.0045  0.0208  974  LEU A CA  
7027  C C   . LEU A 976  ? 0.2408 0.2248 0.2085 -0.0115 0.0049  0.0210  974  LEU A C   
7028  O O   . LEU A 976  ? 0.2406 0.2224 0.2068 -0.0098 0.0046  0.0196  974  LEU A O   
7029  C CB  . LEU A 976  ? 0.2410 0.2295 0.2113 -0.0116 0.0042  0.0188  974  LEU A CB  
7030  C CG  . LEU A 976  ? 0.2639 0.2579 0.2343 -0.0117 0.0048  0.0185  974  LEU A CG  
7031  C CD1 . LEU A 976  ? 0.2639 0.2619 0.2361 -0.0141 0.0056  0.0208  974  LEU A CD1 
7032  C CD2 . LEU A 976  ? 0.2639 0.2611 0.2351 -0.0104 0.0043  0.0160  974  LEU A CD2 
7033  N N   . HIS A 977  ? 0.2414 0.2275 0.2094 -0.0126 0.0055  0.0228  975  HIS A N   
7034  C CA  . HIS A 977  ? 0.2715 0.2579 0.2379 -0.0118 0.0059  0.0227  975  HIS A CA  
7035  C C   . HIS A 977  ? 0.2472 0.2400 0.2140 -0.0120 0.0063  0.0222  975  HIS A C   
7036  O O   . HIS A 977  ? 0.2553 0.2517 0.2229 -0.0137 0.0069  0.0241  975  HIS A O   
7037  C CB  . HIS A 977  ? 0.2406 0.2248 0.2068 -0.0127 0.0061  0.0250  975  HIS A CB  
7038  C CG  . HIS A 977  ? 0.2786 0.2574 0.2439 -0.0117 0.0058  0.0247  975  HIS A CG  
7039  N ND1 . HIS A 977  ? 0.3786 0.3539 0.3442 -0.0115 0.0054  0.0244  975  HIS A ND1 
7040  C CD2 . HIS A 977  ? 0.3073 0.2840 0.2713 -0.0108 0.0059  0.0247  975  HIS A CD2 
7041  C CE1 . HIS A 977  ? 0.2934 0.2652 0.2579 -0.0106 0.0053  0.0243  975  HIS A CE1 
7042  N NE2 . HIS A 977  ? 0.3262 0.2986 0.2898 -0.0102 0.0057  0.0246  975  HIS A NE2 
7043  N N   . THR A 978  ? 0.2396 0.2336 0.2057 -0.0103 0.0061  0.0198  976  THR A N   
7044  C CA  . THR A 978  ? 0.2551 0.2552 0.2213 -0.0099 0.0063  0.0185  976  THR A CA  
7045  C C   . THR A 978  ? 0.2637 0.2625 0.2292 -0.0077 0.0056  0.0158  976  THR A C   
7046  O O   . THR A 978  ? 0.2675 0.2616 0.2327 -0.0066 0.0049  0.0150  976  THR A O   
7047  C CB  . THR A 978  ? 0.2532 0.2581 0.2210 -0.0104 0.0065  0.0178  976  THR A CB  
7048  O OG1 . THR A 978  ? 0.2897 0.3014 0.2577 -0.0098 0.0069  0.0162  976  THR A OG1 
7049  C CG2 . THR A 978  ? 0.2636 0.2660 0.2319 -0.0091 0.0057  0.0158  976  THR A CG2 
7050  N N   . ARG A 979  ? 0.3077 0.3109 0.2729 -0.0071 0.0058  0.0144  977  ARG A N   
7051  C CA  . ARG A 979  ? 0.3147 0.3176 0.2800 -0.0049 0.0048  0.0114  977  ARG A CA  
7052  C C   . ARG A 979  ? 0.3253 0.3333 0.2918 -0.0037 0.0046  0.0086  977  ARG A C   
7053  O O   . ARG A 979  ? 0.2925 0.3005 0.2595 -0.0018 0.0036  0.0057  977  ARG A O   
7054  C CB  . ARG A 979  ? 0.3523 0.3566 0.3168 -0.0047 0.0048  0.0109  977  ARG A CB  
7055  C CG  . ARG A 979  ? 0.3622 0.3620 0.3257 -0.0057 0.0051  0.0134  977  ARG A CG  
7056  C CD  . ARG A 979  ? 0.4950 0.4975 0.4580 -0.0054 0.0050  0.0127  977  ARG A CD  
7057  N NE  . ARG A 979  ? 0.6139 0.6122 0.5761 -0.0062 0.0050  0.0148  977  ARG A NE  
7058  C CZ  . ARG A 979  ? 0.5853 0.5849 0.5472 -0.0061 0.0048  0.0146  977  ARG A CZ  
7059  N NH1 . ARG A 979  ? 0.5205 0.5252 0.4824 -0.0052 0.0045  0.0122  977  ARG A NH1 
7060  N NH2 . ARG A 979  ? 0.5873 0.5830 0.5487 -0.0067 0.0049  0.0165  977  ARG A NH2 
7061  N N   . LEU A 980  ? 0.2743 0.2867 0.2416 -0.0049 0.0053  0.0094  978  LEU A N   
7062  C CA  . LEU A 980  ? 0.2562 0.2752 0.2249 -0.0039 0.0053  0.0069  978  LEU A CA  
7063  C C   . LEU A 980  ? 0.2469 0.2637 0.2168 -0.0031 0.0045  0.0058  978  LEU A C   
7064  O O   . LEU A 980  ? 0.2545 0.2698 0.2248 -0.0046 0.0048  0.0078  978  LEU A O   
7065  C CB  . LEU A 980  ? 0.2597 0.2861 0.2288 -0.0059 0.0066  0.0087  978  LEU A CB  
7066  C CG  . LEU A 980  ? 0.2859 0.3145 0.2535 -0.0068 0.0074  0.0103  978  LEU A CG  
7067  C CD1 . LEU A 980  ? 0.3713 0.4070 0.3393 -0.0091 0.0087  0.0129  978  LEU A CD1 
7068  C CD2 . LEU A 980  ? 0.3321 0.3636 0.2992 -0.0047 0.0068  0.0069  978  LEU A CD2 
7069  N N   . ASP A 981  ? 0.2770 0.2938 0.2477 -0.0006 0.0033  0.0026  979  ASP A N   
7070  C CA  . ASP A 981  ? 0.2789 0.2939 0.2507 0.0005  0.0024  0.0014  979  ASP A CA  
7071  C C   . ASP A 981  ? 0.2422 0.2632 0.2156 -0.0006 0.0031  0.0016  979  ASP A C   
7072  O O   . ASP A 981  ? 0.2847 0.3037 0.2587 -0.0009 0.0027  0.0021  979  ASP A O   
7073  C CB  . ASP A 981  ? 0.2760 0.2907 0.2489 0.0034  0.0008  -0.0021 979  ASP A CB  
7074  C CG  . ASP A 981  ? 0.3232 0.3307 0.2952 0.0044  -0.0003 -0.0020 979  ASP A CG  
7075  O OD1 . ASP A 981  ? 0.3288 0.3312 0.2993 0.0030  0.0001  0.0007  979  ASP A OD1 
7076  O OD2 . ASP A 981  ? 0.3728 0.3797 0.3457 0.0066  -0.0016 -0.0048 979  ASP A OD2 
7077  N N   . GLU A 982  ? 0.2600 0.2889 0.2340 -0.0012 0.0041  0.0011  980  GLU A N   
7078  C CA  . GLU A 982  ? 0.2691 0.3043 0.2450 -0.0025 0.0049  0.0015  980  GLU A CA  
7079  C C   . GLU A 982  ? 0.3127 0.3453 0.2886 -0.0054 0.0056  0.0053  980  GLU A C   
7080  O O   . GLU A 982  ? 0.2727 0.3060 0.2502 -0.0062 0.0054  0.0056  980  GLU A O   
7081  C CB  . GLU A 982  ? 0.3057 0.3505 0.2822 -0.0028 0.0061  0.0007  980  GLU A CB  
7082  C CG  . GLU A 982  ? 0.3419 0.3938 0.3206 -0.0044 0.0070  0.0014  980  GLU A CG  
7083  C CD  . GLU A 982  ? 0.3920 0.4538 0.3710 -0.0057 0.0086  0.0020  980  GLU A CD  
7084  O OE1 . GLU A 982  ? 0.4337 0.4956 0.4109 -0.0071 0.0094  0.0045  980  GLU A OE1 
7085  O OE2 . GLU A 982  ? 0.3874 0.4573 0.3682 -0.0051 0.0090  0.0001  980  GLU A OE2 
7086  N N   . THR A 983  ? 0.2820 0.3112 0.2562 -0.0069 0.0062  0.0080  981  THR A N   
7087  C CA  . THR A 983  ? 0.2815 0.3073 0.2560 -0.0094 0.0065  0.0113  981  THR A CA  
7088  C C   . THR A 983  ? 0.3132 0.3317 0.2874 -0.0087 0.0054  0.0110  981  THR A C   
7089  O O   . THR A 983  ? 0.2927 0.3101 0.2682 -0.0101 0.0052  0.0121  981  THR A O   
7090  C CB  . THR A 983  ? 0.3528 0.3768 0.3257 -0.0108 0.0072  0.0141  981  THR A CB  
7091  O OG1 . THR A 983  ? 0.3373 0.3688 0.3103 -0.0116 0.0083  0.0146  981  THR A OG1 
7092  C CG2 . THR A 983  ? 0.3051 0.3252 0.2787 -0.0132 0.0074  0.0174  981  THR A CG2 
7093  N N   . ILE A 984  ? 0.2724 0.2860 0.2451 -0.0065 0.0045  0.0095  982  ILE A N   
7094  C CA  . ILE A 984  ? 0.2987 0.3060 0.2709 -0.0057 0.0034  0.0093  982  ILE A CA  
7095  C C   . ILE A 984  ? 0.3157 0.3255 0.2897 -0.0051 0.0027  0.0076  982  ILE A C   
7096  O O   . ILE A 984  ? 0.2667 0.2743 0.2412 -0.0059 0.0023  0.0084  982  ILE A O   
7097  C CB  . ILE A 984  ? 0.2777 0.2802 0.2483 -0.0036 0.0026  0.0082  982  ILE A CB  
7098  C CG1 . ILE A 984  ? 0.2887 0.2878 0.2576 -0.0044 0.0032  0.0101  982  ILE A CG1 
7099  C CG2 . ILE A 984  ? 0.2837 0.2813 0.2538 -0.0025 0.0014  0.0078  982  ILE A CG2 
7100  C CD1 . ILE A 984  ? 0.3398 0.3354 0.3076 -0.0027 0.0025  0.0090  982  ILE A CD1 
7101  N N   . ALA A 985  ? 0.2562 0.2707 0.2312 -0.0035 0.0024  0.0051  983  ALA A N   
7102  C CA  . ALA A 985  ? 0.3263 0.3435 0.3031 -0.0025 0.0016  0.0033  983  ALA A CA  
7103  C C   . ALA A 985  ? 0.2993 0.3204 0.2782 -0.0050 0.0023  0.0047  983  ALA A C   
7104  O O   . ALA A 985  ? 0.3066 0.3261 0.2864 -0.0053 0.0015  0.0046  983  ALA A O   
7105  C CB  . ALA A 985  ? 0.2668 0.2892 0.2448 -0.0003 0.0012  0.0002  983  ALA A CB  
7106  N N   . HIS A 986  ? 0.2870 0.3130 0.2666 -0.0070 0.0037  0.0061  984  HIS A N   
7107  C CA  . HIS A 986  ? 0.3111 0.3411 0.2931 -0.0098 0.0043  0.0079  984  HIS A CA  
7108  C C   . HIS A 986  ? 0.3344 0.3582 0.3163 -0.0115 0.0039  0.0101  984  HIS A C   
7109  O O   . HIS A 986  ? 0.3341 0.3578 0.3179 -0.0122 0.0032  0.0098  984  HIS A O   
7110  C CB  . HIS A 986  ? 0.3161 0.3523 0.2984 -0.0116 0.0059  0.0097  984  HIS A CB  
7111  C CG  . HIS A 986  ? 0.3201 0.3592 0.3047 -0.0150 0.0067  0.0127  984  HIS A CG  
7112  N ND1 . HIS A 986  ? 0.3714 0.4139 0.3560 -0.0172 0.0080  0.0156  984  HIS A ND1 
7113  C CD2 . HIS A 986  ? 0.3527 0.3919 0.3399 -0.0166 0.0062  0.0132  984  HIS A CD2 
7114  C CE1 . HIS A 986  ? 0.4190 0.4633 0.4063 -0.0201 0.0082  0.0181  984  HIS A CE1 
7115  N NE2 . HIS A 986  ? 0.3821 0.4243 0.3711 -0.0198 0.0071  0.0166  984  HIS A NE2 
7116  N N   . VAL A 987  ? 0.3036 0.3224 0.2835 -0.0120 0.0042  0.0120  985  VAL A N   
7117  C CA  . VAL A 987  ? 0.3184 0.3319 0.2985 -0.0137 0.0039  0.0140  985  VAL A CA  
7118  C C   . VAL A 987  ? 0.2939 0.3025 0.2734 -0.0121 0.0025  0.0123  985  VAL A C   
7119  O O   . VAL A 987  ? 0.3031 0.3106 0.2843 -0.0132 0.0019  0.0125  985  VAL A O   
7120  C CB  . VAL A 987  ? 0.3006 0.3101 0.2787 -0.0142 0.0045  0.0162  985  VAL A CB  
7121  C CG1 . VAL A 987  ? 0.3062 0.3094 0.2844 -0.0152 0.0038  0.0174  985  VAL A CG1 
7122  C CG2 . VAL A 987  ? 0.2809 0.2955 0.2600 -0.0163 0.0057  0.0185  985  VAL A CG2 
7123  N N   . THR A 988  ? 0.2863 0.2923 0.2636 -0.0095 0.0020  0.0106  986  THR A N   
7124  C CA  . THR A 988  ? 0.3144 0.3160 0.2907 -0.0080 0.0007  0.0094  986  THR A CA  
7125  C C   . THR A 988  ? 0.3507 0.3559 0.3291 -0.0075 -0.0002 0.0075  986  THR A C   
7126  O O   . THR A 988  ? 0.3523 0.3548 0.3305 -0.0071 -0.0013 0.0068  986  THR A O   
7127  C CB  . THR A 988  ? 0.3306 0.3284 0.3042 -0.0056 0.0002  0.0086  986  THR A CB  
7128  O OG1 . THR A 988  ? 0.3272 0.3287 0.3014 -0.0040 0.0000  0.0068  986  THR A OG1 
7129  C CG2 . THR A 988  ? 0.3104 0.3047 0.2822 -0.0061 0.0010  0.0103  986  THR A CG2 
7130  N N   . SER A 989  ? 0.2929 0.3044 0.2732 -0.0076 0.0001  0.0066  987  SER A N   
7131  C CA  . SER A 989  ? 0.3290 0.3443 0.3117 -0.0073 -0.0007 0.0048  987  SER A CA  
7132  C C   . SER A 989  ? 0.3744 0.3918 0.3599 -0.0101 -0.0006 0.0059  987  SER A C   
7133  O O   . SER A 989  ? 0.3765 0.3953 0.3639 -0.0101 -0.0016 0.0046  987  SER A O   
7134  C CB  . SER A 989  ? 0.3433 0.3651 0.3273 -0.0059 -0.0005 0.0029  987  SER A CB  
7135  O OG  . SER A 989  ? 0.4280 0.4556 0.4137 -0.0080 0.0010  0.0040  987  SER A OG  
7136  N N   . ARG A 990  ? 0.3143 0.3316 0.3004 -0.0127 0.0005  0.0085  988  ARG A N   
7137  C CA  . ARG A 990  ? 0.3441 0.3633 0.3336 -0.0157 0.0006  0.0100  988  ARG A CA  
7138  C C   . ARG A 990  ? 0.3705 0.3831 0.3597 -0.0168 -0.0002 0.0110  988  ARG A C   
7139  O O   . ARG A 990  ? 0.3583 0.3712 0.3505 -0.0185 -0.0009 0.0111  988  ARG A O   
7140  C CB  . ARG A 990  ? 0.3191 0.3432 0.3100 -0.0181 0.0021  0.0124  988  ARG A CB  
7141  C CG  . ARG A 990  ? 0.4188 0.4506 0.4103 -0.0172 0.0030  0.0111  988  ARG A CG  
7142  C CD  . ARG A 990  ? 0.4408 0.4786 0.4361 -0.0182 0.0026  0.0101  988  ARG A CD  
7143  N NE  . ARG A 990  ? 0.4156 0.4596 0.4138 -0.0214 0.0039  0.0126  988  ARG A NE  
7144  C CZ  . ARG A 990  ? 0.4367 0.4873 0.4388 -0.0230 0.0039  0.0124  988  ARG A CZ  
7145  N NH1 . ARG A 990  ? 0.4102 0.4619 0.4139 -0.0217 0.0027  0.0096  988  ARG A NH1 
7146  N NH2 . ARG A 990  ? 0.3789 0.4354 0.3833 -0.0260 0.0053  0.0153  988  ARG A NH2 
7147  N N   . ILE A 991  ? 0.2937 0.3006 0.2798 -0.0157 0.0000  0.0117  989  ILE A N   
7148  C CA  . ILE A 991  ? 0.3043 0.3053 0.2901 -0.0164 -0.0007 0.0124  989  ILE A CA  
7149  C C   . ILE A 991  ? 0.3355 0.3344 0.3211 -0.0149 -0.0023 0.0099  989  ILE A C   
7150  O O   . ILE A 991  ? 0.3485 0.3479 0.3322 -0.0125 -0.0028 0.0081  989  ILE A O   
7151  C CB  . ILE A 991  ? 0.3390 0.3354 0.3216 -0.0154 -0.0001 0.0136  989  ILE A CB  
7152  C CG1 . ILE A 991  ? 0.3214 0.3127 0.3045 -0.0165 -0.0005 0.0146  989  ILE A CG1 
7153  C CG2 . ILE A 991  ? 0.3343 0.3284 0.3135 -0.0124 -0.0004 0.0118  989  ILE A CG2 
7154  C CD1 . ILE A 991  ? 0.3149 0.3074 0.3012 -0.0196 -0.0002 0.0172  989  ILE A CD1 
7155  N N   . LYS A 992  ? 0.2747 0.2713 0.2623 -0.0163 -0.0032 0.0098  990  LYS A N   
7156  C CA  . LYS A 992  ? 0.3366 0.3314 0.3240 -0.0149 -0.0048 0.0074  990  LYS A CA  
7157  C C   . LYS A 992  ? 0.3717 0.3604 0.3568 -0.0142 -0.0052 0.0073  990  LYS A C   
7158  O O   . LYS A 992  ? 0.4553 0.4417 0.4425 -0.0156 -0.0059 0.0074  990  LYS A O   
7159  C CB  . LYS A 992  ? 0.3581 0.3556 0.3499 -0.0170 -0.0059 0.0065  990  LYS A CB  
7160  N N   . ALA A 993  ? 0.3120 0.2985 0.2931 -0.0118 -0.0048 0.0071  991  ALA A N   
7161  C CA  . ALA A 993  ? 0.2721 0.2537 0.2508 -0.0109 -0.0049 0.0072  991  ALA A CA  
7162  C C   . ALA A 993  ? 0.2935 0.2741 0.2683 -0.0081 -0.0053 0.0060  991  ALA A C   
7163  O O   . ALA A 993  ? 0.2880 0.2704 0.2614 -0.0069 -0.0050 0.0061  991  ALA A O   
7164  C CB  . ALA A 993  ? 0.3322 0.3117 0.3102 -0.0117 -0.0036 0.0096  991  ALA A CB  
7165  N N   . GLY A 994  ? 0.2829 0.2606 0.2560 -0.0070 -0.0059 0.0050  992  GLY A N   
7166  C CA  . GLY A 994  ? 0.3241 0.3011 0.2935 -0.0045 -0.0063 0.0042  992  GLY A CA  
7167  C C   . GLY A 994  ? 0.2932 0.2681 0.2595 -0.0035 -0.0052 0.0060  992  GLY A C   
7168  O O   . GLY A 994  ? 0.2521 0.2271 0.2159 -0.0017 -0.0054 0.0060  992  GLY A O   
7169  N N   . ASN A 995  ? 0.2509 0.2239 0.2175 -0.0046 -0.0040 0.0075  993  ASN A N   
7170  C CA  . ASN A 995  ? 0.2921 0.2631 0.2562 -0.0038 -0.0030 0.0092  993  ASN A CA  
7171  C C   . ASN A 995  ? 0.2642 0.2358 0.2298 -0.0052 -0.0019 0.0108  993  ASN A C   
7172  O O   . ASN A 995  ? 0.2929 0.2639 0.2604 -0.0068 -0.0015 0.0115  993  ASN A O   
7173  C CB  . ASN A 995  ? 0.2600 0.2283 0.2226 -0.0033 -0.0027 0.0092  993  ASN A CB  
7174  C CG  . ASN A 995  ? 0.3084 0.2767 0.2683 -0.0014 -0.0035 0.0080  993  ASN A CG  
7175  O OD1 . ASN A 995  ? 0.2785 0.2477 0.2390 -0.0011 -0.0046 0.0061  993  ASN A OD1 
7176  N ND2 . ASN A 995  ? 0.3102 0.2777 0.2672 -0.0002 -0.0029 0.0092  993  ASN A ND2 
7177  N N   . LEU A 996  ? 0.2648 0.2377 0.2297 -0.0046 -0.0015 0.0113  994  LEU A N   
7178  C CA  . LEU A 996  ? 0.2754 0.2495 0.2412 -0.0057 -0.0005 0.0125  994  LEU A CA  
7179  C C   . LEU A 996  ? 0.2454 0.2173 0.2092 -0.0050 0.0002  0.0137  994  LEU A C   
7180  O O   . LEU A 996  ? 0.2461 0.2164 0.2078 -0.0034 -0.0001 0.0136  994  LEU A O   
7181  C CB  . LEU A 996  ? 0.2485 0.2265 0.2156 -0.0055 -0.0007 0.0117  994  LEU A CB  
7182  C CG  . LEU A 996  ? 0.3903 0.3712 0.3595 -0.0059 -0.0016 0.0103  994  LEU A CG  
7183  C CD1 . LEU A 996  ? 0.3438 0.3289 0.3142 -0.0053 -0.0017 0.0094  994  LEU A CD1 
7184  C CD2 . LEU A 996  ? 0.3313 0.3128 0.3031 -0.0082 -0.0014 0.0110  994  LEU A CD2 
7185  N N   . TYR A 997  ? 0.2498 0.2217 0.2142 -0.0061 0.0011  0.0151  995  TYR A N   
7186  C CA  . TYR A 997  ? 0.2777 0.2476 0.2405 -0.0057 0.0018  0.0162  995  TYR A CA  
7187  C C   . TYR A 997  ? 0.2429 0.2152 0.2066 -0.0065 0.0025  0.0168  995  TYR A C   
7188  O O   . TYR A 997  ? 0.2565 0.2308 0.2219 -0.0080 0.0028  0.0175  995  TYR A O   
7189  C CB  . TYR A 997  ? 0.2539 0.2211 0.2164 -0.0061 0.0022  0.0171  995  TYR A CB  
7190  C CG  . TYR A 997  ? 0.2593 0.2246 0.2206 -0.0052 0.0016  0.0162  995  TYR A CG  
7191  C CD1 . TYR A 997  ? 0.2698 0.2337 0.2288 -0.0038 0.0017  0.0163  995  TYR A CD1 
7192  C CD2 . TYR A 997  ? 0.2624 0.2278 0.2251 -0.0057 0.0010  0.0152  995  TYR A CD2 
7193  C CE1 . TYR A 997  ? 0.2952 0.2582 0.2529 -0.0028 0.0012  0.0155  995  TYR A CE1 
7194  C CE2 . TYR A 997  ? 0.3049 0.2692 0.2666 -0.0047 0.0004  0.0140  995  TYR A CE2 
7195  C CZ  . TYR A 997  ? 0.3008 0.2641 0.2597 -0.0032 0.0006  0.0142  995  TYR A CZ  
7196  O OH  . TYR A 997  ? 0.3379 0.3010 0.2954 -0.0021 0.0001  0.0130  995  TYR A OH  
7197  N N   . ILE A 998  ? 0.2425 0.2151 0.2054 -0.0054 0.0025  0.0165  996  ILE A N   
7198  C CA  A ILE A 998  ? 0.2484 0.2239 0.2120 -0.0058 0.0030  0.0165  996  ILE A CA  
7199  C CA  B ILE A 998  ? 0.2464 0.2218 0.2099 -0.0058 0.0030  0.0166  996  ILE A CA  
7200  C C   . ILE A 998  ? 0.2414 0.2148 0.2039 -0.0058 0.0034  0.0176  996  ILE A C   
7201  O O   . ILE A 998  ? 0.2420 0.2127 0.2033 -0.0047 0.0031  0.0174  996  ILE A O   
7202  C CB  A ILE A 998  ? 0.2444 0.2222 0.2083 -0.0045 0.0023  0.0147  996  ILE A CB  
7203  C CB  B ILE A 998  ? 0.2478 0.2258 0.2118 -0.0046 0.0024  0.0148  996  ILE A CB  
7204  C CG1 A ILE A 998  ? 0.2513 0.2311 0.2163 -0.0044 0.0017  0.0136  996  ILE A CG1 
7205  C CG1 B ILE A 998  ? 0.2538 0.2346 0.2192 -0.0048 0.0019  0.0138  996  ILE A CG1 
7206  C CG2 A ILE A 998  ? 0.2491 0.2309 0.2139 -0.0049 0.0028  0.0144  996  ILE A CG2 
7207  C CG2 B ILE A 998  ? 0.2486 0.2299 0.2132 -0.0047 0.0028  0.0144  996  ILE A CG2 
7208  C CD1 A ILE A 998  ? 0.2513 0.2346 0.2181 -0.0062 0.0022  0.0141  996  ILE A CD1 
7209  C CD1 B ILE A 998  ? 0.2836 0.2674 0.2498 -0.0035 0.0013  0.0118  996  ILE A CD1 
7210  N N   . ASN A 999  ? 0.2528 0.2276 0.2158 -0.0070 0.0041  0.0188  997  ASN A N   
7211  C CA  . ASN A 999  ? 0.2642 0.2380 0.2266 -0.0071 0.0045  0.0196  997  ASN A CA  
7212  C C   . ASN A 999  ? 0.2639 0.2334 0.2252 -0.0067 0.0046  0.0205  997  ASN A C   
7213  O O   . ASN A 999  ? 0.2449 0.2130 0.2056 -0.0062 0.0047  0.0207  997  ASN A O   
7214  C CB  . ASN A 999  ? 0.2432 0.2184 0.2054 -0.0060 0.0042  0.0183  997  ASN A CB  
7215  C CG  . ASN A 999  ? 0.2703 0.2507 0.2335 -0.0064 0.0044  0.0174  997  ASN A CG  
7216  O OD1 . ASN A 999  ? 0.2663 0.2492 0.2300 -0.0078 0.0050  0.0187  997  ASN A OD1 
7217  N ND2 . ASN A 999  ? 0.2765 0.2586 0.2400 -0.0051 0.0038  0.0154  997  ASN A ND2 
7218  N N   . ARG A 1000 ? 0.2469 0.2148 0.2083 -0.0071 0.0046  0.0209  998  ARG A N   
7219  C CA  . ARG A 1000 ? 0.2421 0.2068 0.2027 -0.0067 0.0047  0.0215  998  ARG A CA  
7220  C C   . ARG A 1000 ? 0.2427 0.2066 0.2042 -0.0074 0.0046  0.0218  998  ARG A C   
7221  O O   . ARG A 1000 ? 0.2716 0.2372 0.2346 -0.0083 0.0044  0.0218  998  ARG A O   
7222  C CB  . ARG A 1000 ? 0.2429 0.2060 0.2021 -0.0053 0.0043  0.0207  998  ARG A CB  
7223  C CG  . ARG A 1000 ? 0.2609 0.2250 0.2202 -0.0048 0.0036  0.0194  998  ARG A CG  
7224  C CD  . ARG A 1000 ? 0.2706 0.2329 0.2283 -0.0037 0.0032  0.0192  998  ARG A CD  
7225  N NE  . ARG A 1000 ? 0.2718 0.2329 0.2292 -0.0038 0.0035  0.0194  998  ARG A NE  
7226  C CZ  . ARG A 1000 ? 0.3103 0.2705 0.2661 -0.0029 0.0033  0.0191  998  ARG A CZ  
7227  N NH1 . ARG A 1000 ? 0.2658 0.2259 0.2202 -0.0019 0.0029  0.0192  998  ARG A NH1 
7228  N NH2 . ARG A 1000 ? 0.3048 0.2644 0.2606 -0.0029 0.0035  0.0188  998  ARG A NH2 
7229  N N   . ASN A 1001 ? 0.2434 0.2050 0.2044 -0.0069 0.0047  0.0220  999  ASN A N   
7230  C CA  . ASN A 1001 ? 0.2444 0.2050 0.2067 -0.0073 0.0044  0.0217  999  ASN A CA  
7231  C C   . ASN A 1001 ? 0.2505 0.2115 0.2126 -0.0068 0.0037  0.0201  999  ASN A C   
7232  O O   . ASN A 1001 ? 0.2450 0.2068 0.2059 -0.0060 0.0035  0.0194  999  ASN A O   
7233  C CB  . ASN A 1001 ? 0.2469 0.2054 0.2088 -0.0066 0.0046  0.0218  999  ASN A CB  
7234  C CG  . ASN A 1001 ? 0.3354 0.2933 0.2952 -0.0052 0.0047  0.0210  999  ASN A CG  
7235  O OD1 . ASN A 1001 ? 0.3203 0.2785 0.2792 -0.0046 0.0043  0.0198  999  ASN A OD1 
7236  N ND2 . ASN A 1001 ? 0.3439 0.3012 0.3029 -0.0047 0.0054  0.0217  999  ASN A ND2 
7237  N N   . ILE A 1002 ? 0.2463 0.2066 0.2100 -0.0073 0.0030  0.0194  1000 ILE A N   
7238  C CA  . ILE A 1002 ? 0.2475 0.2083 0.2114 -0.0070 0.0022  0.0178  1000 ILE A CA  
7239  C C   . ILE A 1002 ? 0.2763 0.2357 0.2394 -0.0058 0.0017  0.0162  1000 ILE A C   
7240  O O   . ILE A 1002 ? 0.2501 0.2098 0.2138 -0.0056 0.0008  0.0146  1000 ILE A O   
7241  C CB  . ILE A 1002 ? 0.2772 0.2392 0.2440 -0.0086 0.0016  0.0179  1000 ILE A CB  
7242  C CG1 . ILE A 1002 ? 0.2487 0.2087 0.2179 -0.0095 0.0012  0.0184  1000 ILE A CG1 
7243  C CG2 . ILE A 1002 ? 0.2460 0.2106 0.2133 -0.0097 0.0022  0.0192  1000 ILE A CG2 
7244  C CD1 . ILE A 1002 ? 0.2496 0.2104 0.2221 -0.0113 0.0004  0.0186  1000 ILE A CD1 
7245  N N   . ILE A 1003 ? 0.2518 0.2100 0.2135 -0.0048 0.0023  0.0166  1001 ILE A N   
7246  C CA  . ILE A 1003 ? 0.2679 0.2254 0.2287 -0.0035 0.0020  0.0150  1001 ILE A CA  
7247  C C   . ILE A 1003 ? 0.3217 0.2799 0.2793 -0.0022 0.0026  0.0152  1001 ILE A C   
7248  O O   . ILE A 1003 ? 0.3630 0.3215 0.3194 -0.0023 0.0032  0.0166  1001 ILE A O   
7249  C CB  . ILE A 1003 ? 0.2836 0.2395 0.2459 -0.0036 0.0021  0.0151  1001 ILE A CB  
7250  C CG1 . ILE A 1003 ? 0.3097 0.2654 0.2712 -0.0036 0.0032  0.0170  1001 ILE A CG1 
7251  C CG2 . ILE A 1003 ? 0.2521 0.2069 0.2179 -0.0051 0.0013  0.0152  1001 ILE A CG2 
7252  C CD1 . ILE A 1003 ? 0.3442 0.2985 0.3068 -0.0030 0.0033  0.0167  1001 ILE A CD1 
7253  N N   . GLY A 1004 ? 0.3103 0.2689 0.2666 -0.0009 0.0024  0.0137  1002 GLY A N   
7254  C CA  . GLY A 1004 ? 0.3839 0.3436 0.3373 0.0003  0.0030  0.0143  1002 GLY A CA  
7255  C C   . GLY A 1004 ? 0.3847 0.3455 0.3362 0.0008  0.0026  0.0146  1002 GLY A C   
7256  O O   . GLY A 1004 ? 0.3612 0.3222 0.3111 0.0010  0.0032  0.0164  1002 GLY A O   
7257  N N   . ALA A 1005 ? 0.3703 0.3318 0.3225 0.0008  0.0015  0.0131  1003 ALA A N   
7258  C CA  . ALA A 1005 ? 0.3270 0.2896 0.2776 0.0014  0.0009  0.0133  1003 ALA A CA  
7259  C C   . ALA A 1005 ? 0.3577 0.3215 0.3051 0.0028  0.0011  0.0138  1003 ALA A C   
7260  O O   . ALA A 1005 ? 0.3709 0.3356 0.3173 0.0036  0.0013  0.0127  1003 ALA A O   
7261  C CB  . ALA A 1005 ? 0.3440 0.3076 0.2958 0.0014  -0.0004 0.0112  1003 ALA A CB  
7262  N N   . VAL A 1006 ? 0.2961 0.2599 0.2420 0.0032  0.0012  0.0157  1004 VAL A N   
7263  C CA  . VAL A 1006 ? 0.2592 0.2241 0.2022 0.0042  0.0015  0.0172  1004 VAL A CA  
7264  C C   . VAL A 1006 ? 0.2725 0.2390 0.2137 0.0054  0.0003  0.0166  1004 VAL A C   
7265  O O   . VAL A 1006 ? 0.3055 0.2717 0.2476 0.0053  -0.0007 0.0164  1004 VAL A O   
7266  C CB  . VAL A 1006 ? 0.2656 0.2290 0.2085 0.0036  0.0021  0.0200  1004 VAL A CB  
7267  C CG1 . VAL A 1006 ? 0.2902 0.2548 0.2304 0.0044  0.0024  0.0221  1004 VAL A CG1 
7268  C CG2 . VAL A 1006 ? 0.3174 0.2796 0.2620 0.0025  0.0033  0.0205  1004 VAL A CG2 
7269  N N   . VAL A 1007 ? 0.2841 0.2529 0.2227 0.0065  0.0003  0.0164  1005 VAL A N   
7270  C CA  . VAL A 1007 ? 0.2663 0.2373 0.2028 0.0078  -0.0009 0.0160  1005 VAL A CA  
7271  C C   . VAL A 1007 ? 0.2735 0.2435 0.2093 0.0079  -0.0015 0.0186  1005 VAL A C   
7272  O O   . VAL A 1007 ? 0.2889 0.2577 0.2244 0.0075  -0.0008 0.0214  1005 VAL A O   
7273  C CB  . VAL A 1007 ? 0.2780 0.2522 0.2114 0.0090  -0.0005 0.0157  1005 VAL A CB  
7274  C CG1 . VAL A 1007 ? 0.2720 0.2489 0.2028 0.0104  -0.0018 0.0158  1005 VAL A CG1 
7275  C CG2 . VAL A 1007 ? 0.2689 0.2440 0.2034 0.0092  -0.0003 0.0124  1005 VAL A CG2 
7276  N N   . GLY A 1008 ? 0.2729 0.2436 0.2089 0.0086  -0.0031 0.0176  1006 GLY A N   
7277  C CA  . GLY A 1008 ? 0.2684 0.2381 0.2043 0.0090  -0.0040 0.0197  1006 GLY A CA  
7278  C C   . GLY A 1008 ? 0.3014 0.2681 0.2400 0.0080  -0.0038 0.0205  1006 GLY A C   
7279  O O   . GLY A 1008 ? 0.3020 0.2675 0.2409 0.0085  -0.0047 0.0221  1006 GLY A O   
7280  N N   . VAL A 1009 ? 0.2923 0.2579 0.2330 0.0067  -0.0027 0.0195  1007 VAL A N   
7281  C CA  . VAL A 1009 ? 0.2827 0.2462 0.2258 0.0058  -0.0024 0.0201  1007 VAL A CA  
7282  C C   . VAL A 1009 ? 0.2586 0.2225 0.2043 0.0050  -0.0025 0.0177  1007 VAL A C   
7283  O O   . VAL A 1009 ? 0.2639 0.2278 0.2114 0.0050  -0.0031 0.0172  1007 VAL A O   
7284  C CB  . VAL A 1009 ? 0.2976 0.2596 0.2407 0.0048  -0.0009 0.0218  1007 VAL A CB  
7285  C CG1 . VAL A 1009 ? 0.2923 0.2523 0.2379 0.0040  -0.0008 0.0222  1007 VAL A CG1 
7286  C CG2 . VAL A 1009 ? 0.2800 0.2422 0.2208 0.0053  -0.0007 0.0245  1007 VAL A CG2 
7287  N N   . GLN A 1010 ? 0.2833 0.2479 0.2295 0.0044  -0.0019 0.0163  1008 GLN A N   
7288  C CA  . GLN A 1010 ? 0.2733 0.2387 0.2219 0.0036  -0.0022 0.0142  1008 GLN A CA  
7289  C C   . GLN A 1010 ? 0.2589 0.2260 0.2068 0.0042  -0.0030 0.0123  1008 GLN A C   
7290  O O   . GLN A 1010 ? 0.3023 0.2693 0.2506 0.0038  -0.0025 0.0112  1008 GLN A O   
7291  C CB  . GLN A 1010 ? 0.2876 0.2519 0.2381 0.0021  -0.0011 0.0143  1008 GLN A CB  
7292  C CG  . GLN A 1010 ? 0.2814 0.2445 0.2327 0.0014  -0.0003 0.0159  1008 GLN A CG  
7293  C CD  . GLN A 1010 ? 0.3241 0.2858 0.2741 0.0014  0.0007  0.0176  1008 GLN A CD  
7294  O OE1 . GLN A 1010 ? 0.2911 0.2527 0.2403 0.0014  0.0012  0.0174  1008 GLN A OE1 
7295  N NE2 . GLN A 1010 ? 0.2826 0.2432 0.2326 0.0014  0.0009  0.0191  1008 GLN A NE2 
7296  N N   . PRO A 1011 ? 0.2744 0.2431 0.2212 0.0054  -0.0042 0.0116  1009 PRO A N   
7297  C CA  . PRO A 1011 ? 0.2772 0.2479 0.2235 0.0060  -0.0052 0.0093  1009 PRO A CA  
7298  C C   . PRO A 1011 ? 0.2787 0.2492 0.2283 0.0046  -0.0052 0.0073  1009 PRO A C   
7299  O O   . PRO A 1011 ? 0.2798 0.2501 0.2320 0.0034  -0.0052 0.0074  1009 PRO A O   
7300  C CB  . PRO A 1011 ? 0.2624 0.2348 0.2082 0.0071  -0.0067 0.0089  1009 PRO A CB  
7301  C CG  . PRO A 1011 ? 0.2834 0.2545 0.2281 0.0077  -0.0065 0.0116  1009 PRO A CG  
7302  C CD  . PRO A 1011 ? 0.2846 0.2534 0.2309 0.0063  -0.0051 0.0127  1009 PRO A CD  
7303  N N   . PHE A 1012 ? 0.2997 0.2705 0.2492 0.0047  -0.0054 0.0055  1010 PHE A N   
7304  C CA  . PHE A 1012 ? 0.3080 0.2777 0.2608 0.0032  -0.0053 0.0043  1010 PHE A CA  
7305  C C   . PHE A 1012 ? 0.3223 0.2934 0.2771 0.0031  -0.0069 0.0013  1010 PHE A C   
7306  O O   . PHE A 1012 ? 0.3093 0.2821 0.2623 0.0045  -0.0079 -0.0005 1010 PHE A O   
7307  C CB  . PHE A 1012 ? 0.3091 0.2772 0.2612 0.0033  -0.0043 0.0045  1010 PHE A CB  
7308  C CG  . PHE A 1012 ? 0.3555 0.3219 0.3112 0.0017  -0.0043 0.0037  1010 PHE A CG  
7309  C CD1 . PHE A 1012 ? 0.3347 0.2996 0.2922 0.0002  -0.0033 0.0058  1010 PHE A CD1 
7310  C CD2 . PHE A 1012 ? 0.3659 0.3323 0.3234 0.0018  -0.0054 0.0010  1010 PHE A CD2 
7311  C CE1 . PHE A 1012 ? 0.3820 0.3453 0.3428 -0.0012 -0.0034 0.0056  1010 PHE A CE1 
7312  C CE2 . PHE A 1012 ? 0.3743 0.3387 0.3356 0.0003  -0.0056 0.0006  1010 PHE A CE2 
7313  C CZ  . PHE A 1012 ? 0.3332 0.2960 0.2960 -0.0013 -0.0046 0.0032  1010 PHE A CZ  
7314  N N   . GLY A 1013 ? 0.3419 0.3126 0.3005 0.0013  -0.0072 0.0010  1011 GLY A N   
7315  C CA  . GLY A 1013 ? 0.3638 0.3358 0.3252 0.0007  -0.0088 -0.0016 1011 GLY A CA  
7316  C C   . GLY A 1013 ? 0.3313 0.3041 0.2962 -0.0011 -0.0089 -0.0010 1011 GLY A C   
7317  O O   . GLY A 1013 ? 0.3742 0.3481 0.3386 -0.0011 -0.0083 0.0006  1011 GLY A O   
7318  N N   . GLY A 1014 ? 0.3412 0.3138 0.3101 -0.0028 -0.0098 -0.0024 1012 GLY A N   
7319  C CA  . GLY A 1014 ? 0.3837 0.3575 0.3564 -0.0050 -0.0097 -0.0015 1012 GLY A CA  
7320  C C   . GLY A 1014 ? 0.4154 0.3920 0.3908 -0.0054 -0.0114 -0.0038 1012 GLY A C   
7321  O O   . GLY A 1014 ? 0.4253 0.4031 0.3992 -0.0038 -0.0127 -0.0061 1012 GLY A O   
7322  N N   . ARG A 1015 ? 0.3986 0.3766 0.3781 -0.0077 -0.0114 -0.0030 1013 ARG A N   
7323  C CA  . ARG A 1015 ? 0.3798 0.3607 0.3627 -0.0087 -0.0129 -0.0048 1013 ARG A CA  
7324  C C   . ARG A 1015 ? 0.3933 0.3730 0.3814 -0.0115 -0.0136 -0.0048 1013 ARG A C   
7325  O O   . ARG A 1015 ? 0.3330 0.3096 0.3219 -0.0125 -0.0129 -0.0033 1013 ARG A O   
7326  C CB  . ARG A 1015 ? 0.4177 0.4026 0.4011 -0.0090 -0.0123 -0.0037 1013 ARG A CB  
7327  C CG  . ARG A 1015 ? 0.4496 0.4346 0.4339 -0.0106 -0.0105 -0.0007 1013 ARG A CG  
7328  C CD  . ARG A 1015 ? 0.4560 0.4458 0.4437 -0.0122 -0.0103 -0.0003 1013 ARG A CD  
7329  N NE  . ARG A 1015 ? 0.4735 0.4645 0.4663 -0.0147 -0.0114 -0.0009 1013 ARG A NE  
7330  C CZ  . ARG A 1015 ? 0.4914 0.4810 0.4874 -0.0174 -0.0110 0.0009  1013 ARG A CZ  
7331  N NH1 . ARG A 1015 ? 0.4914 0.4788 0.4859 -0.0178 -0.0095 0.0035  1013 ARG A NH1 
7332  N NH2 . ARG A 1015 ? 0.5220 0.5126 0.5230 -0.0197 -0.0122 0.0004  1013 ARG A NH2 
7333  N N   . GLY A 1016 ? 0.3550 0.3373 0.3470 -0.0127 -0.0150 -0.0065 1014 GLY A N   
7334  C CA  . GLY A 1016 ? 0.3859 0.3672 0.3835 -0.0157 -0.0158 -0.0062 1014 GLY A CA  
7335  C C   . GLY A 1016 ? 0.3954 0.3723 0.3937 -0.0153 -0.0170 -0.0080 1014 GLY A C   
7336  O O   . GLY A 1016 ? 0.4009 0.3774 0.3971 -0.0131 -0.0183 -0.0111 1014 GLY A O   
7337  N N   . LEU A 1017 ? 0.3663 0.3399 0.3674 -0.0173 -0.0168 -0.0060 1015 LEU A N   
7338  C CA  . LEU A 1017 ? 0.3794 0.3485 0.3817 -0.0168 -0.0180 -0.0078 1015 LEU A CA  
7339  C C   . LEU A 1017 ? 0.3816 0.3487 0.3785 -0.0139 -0.0170 -0.0082 1015 LEU A C   
7340  O O   . LEU A 1017 ? 0.4139 0.3777 0.4112 -0.0130 -0.0179 -0.0100 1015 LEU A O   
7341  C CB  . LEU A 1017 ? 0.3997 0.3658 0.4068 -0.0197 -0.0181 -0.0051 1015 LEU A CB  
7342  C CG  . LEU A 1017 ? 0.4280 0.3955 0.4416 -0.0232 -0.0192 -0.0042 1015 LEU A CG  
7343  C CD1 . LEU A 1017 ? 0.4083 0.3728 0.4257 -0.0259 -0.0189 -0.0004 1015 LEU A CD1 
7344  C CD2 . LEU A 1017 ? 0.3867 0.3538 0.4040 -0.0232 -0.0220 -0.0084 1015 LEU A CD2 
7345  N N   . SER A 1018 ? 0.3421 0.3109 0.3341 -0.0124 -0.0152 -0.0065 1016 SER A N   
7346  C CA  . SER A 1018 ? 0.3740 0.3411 0.3613 -0.0101 -0.0140 -0.0063 1016 SER A CA  
7347  C C   . SER A 1018 ? 0.3725 0.3411 0.3557 -0.0072 -0.0147 -0.0091 1016 SER A C   
7348  O O   . SER A 1018 ? 0.3658 0.3332 0.3455 -0.0053 -0.0140 -0.0094 1016 SER A O   
7349  C CB  . SER A 1018 ? 0.3744 0.3421 0.3588 -0.0101 -0.0118 -0.0028 1016 SER A CB  
7350  O OG  . SER A 1018 ? 0.3774 0.3438 0.3650 -0.0126 -0.0111 0.0000  1016 SER A OG  
7351  N N   . GLY A 1019 ? 0.3583 0.3300 0.3419 -0.0069 -0.0159 -0.0111 1017 GLY A N   
7352  C CA  . GLY A 1019 ? 0.3657 0.3391 0.3454 -0.0041 -0.0167 -0.0137 1017 GLY A CA  
7353  C C   . GLY A 1019 ? 0.3564 0.3337 0.3365 -0.0039 -0.0179 -0.0152 1017 GLY A C   
7354  O O   . GLY A 1019 ? 0.3515 0.3304 0.3345 -0.0057 -0.0179 -0.0140 1017 GLY A O   
7355  N N   . THR A 1020 ? 0.3177 0.2969 0.2946 -0.0015 -0.0190 -0.0178 1018 THR A N   
7356  C CA  . THR A 1020 ? 0.3511 0.3342 0.3272 -0.0005 -0.0202 -0.0191 1018 THR A CA  
7357  C C   . THR A 1020 ? 0.3763 0.3609 0.3477 0.0012  -0.0190 -0.0166 1018 THR A C   
7358  O O   . THR A 1020 ? 0.3741 0.3618 0.3454 0.0017  -0.0197 -0.0167 1018 THR A O   
7359  C CB  . THR A 1020 ? 0.3341 0.3189 0.3089 0.0014  -0.0222 -0.0231 1018 THR A CB  
7360  O OG1 . THR A 1020 ? 0.3057 0.2899 0.2754 0.0037  -0.0213 -0.0229 1018 THR A OG1 
7361  C CG2 . THR A 1020 ? 0.3590 0.3420 0.3391 -0.0001 -0.0239 -0.0261 1018 THR A CG2 
7362  N N   . GLY A 1021 ? 0.3182 0.3009 0.2858 0.0022  -0.0174 -0.0145 1019 GLY A N   
7363  C CA  . GLY A 1021 ? 0.3198 0.3037 0.2826 0.0042  -0.0167 -0.0127 1019 GLY A CA  
7364  C C   . GLY A 1021 ? 0.3215 0.3081 0.2811 0.0066  -0.0182 -0.0150 1019 GLY A C   
7365  O O   . GLY A 1021 ? 0.3228 0.3104 0.2839 0.0067  -0.0197 -0.0184 1019 GLY A O   
7366  N N   . PRO A 1022 ? 0.3000 0.2879 0.2551 0.0085  -0.0178 -0.0132 1020 PRO A N   
7367  C CA  . PRO A 1022 ? 0.3180 0.3044 0.2713 0.0085  -0.0162 -0.0094 1020 PRO A CA  
7368  C C   . PRO A 1022 ? 0.3307 0.3140 0.2827 0.0081  -0.0142 -0.0074 1020 PRO A C   
7369  O O   . PRO A 1022 ? 0.3419 0.3244 0.2938 0.0081  -0.0140 -0.0089 1020 PRO A O   
7370  C CB  . PRO A 1022 ? 0.3040 0.2928 0.2530 0.0109  -0.0170 -0.0085 1020 PRO A CB  
7371  C CG  . PRO A 1022 ? 0.3402 0.3315 0.2872 0.0123  -0.0182 -0.0113 1020 PRO A CG  
7372  C CD  . PRO A 1022 ? 0.2761 0.2672 0.2276 0.0108  -0.0192 -0.0149 1020 PRO A CD  
7373  N N   . LYS A 1023 ? 0.2865 0.2680 0.2377 0.0077  -0.0128 -0.0042 1021 LYS A N   
7374  C CA  . LYS A 1023 ? 0.3089 0.2877 0.2593 0.0071  -0.0110 -0.0022 1021 LYS A CA  
7375  C C   . LYS A 1023 ? 0.3003 0.2796 0.2464 0.0088  -0.0105 -0.0017 1021 LYS A C   
7376  O O   . LYS A 1023 ? 0.2808 0.2619 0.2237 0.0103  -0.0109 -0.0007 1021 LYS A O   
7377  C CB  . LYS A 1023 ? 0.2800 0.2573 0.2305 0.0066  -0.0098 0.0008  1021 LYS A CB  
7378  C CG  . LYS A 1023 ? 0.2787 0.2556 0.2332 0.0047  -0.0097 0.0007  1021 LYS A CG  
7379  C CD  . LYS A 1023 ? 0.2775 0.2534 0.2317 0.0046  -0.0087 0.0033  1021 LYS A CD  
7380  C CE  . LYS A 1023 ? 0.2929 0.2690 0.2508 0.0028  -0.0082 0.0034  1021 LYS A CE  
7381  N NZ  . LYS A 1023 ? 0.2986 0.2725 0.2576 0.0012  -0.0068 0.0042  1021 LYS A NZ  
7382  N N   . ALA A 1024 ? 0.2962 0.2742 0.2426 0.0084  -0.0096 -0.0023 1022 ALA A N   
7383  C CA  . ALA A 1024 ? 0.3006 0.2794 0.2432 0.0097  -0.0086 -0.0013 1022 ALA A CA  
7384  C C   . ALA A 1024 ? 0.3034 0.2808 0.2443 0.0096  -0.0072 0.0026  1022 ALA A C   
7385  O O   . ALA A 1024 ? 0.3042 0.2791 0.2472 0.0082  -0.0065 0.0041  1022 ALA A O   
7386  C CB  . ALA A 1024 ? 0.3151 0.2927 0.2589 0.0094  -0.0080 -0.0030 1022 ALA A CB  
7387  N N   . GLY A 1025 ? 0.3025 0.2816 0.2394 0.0109  -0.0069 0.0042  1023 GLY A N   
7388  C CA  . GLY A 1025 ? 0.2708 0.2484 0.2064 0.0107  -0.0059 0.0081  1023 GLY A CA  
7389  C C   . GLY A 1025 ? 0.2700 0.2467 0.2066 0.0106  -0.0067 0.0094  1023 GLY A C   
7390  O O   . GLY A 1025 ? 0.2686 0.2430 0.2058 0.0099  -0.0060 0.0118  1023 GLY A O   
7391  N N   . GLY A 1026 ? 0.2710 0.2496 0.2079 0.0113  -0.0084 0.0076  1024 GLY A N   
7392  C CA  . GLY A 1026 ? 0.2706 0.2490 0.2085 0.0116  -0.0095 0.0084  1024 GLY A CA  
7393  C C   . GLY A 1026 ? 0.2738 0.2551 0.2092 0.0134  -0.0112 0.0082  1024 GLY A C   
7394  O O   . GLY A 1026 ? 0.2762 0.2601 0.2092 0.0143  -0.0116 0.0069  1024 GLY A O   
7395  N N   . PRO A 1027 ? 0.2740 0.2552 0.2101 0.0140  -0.0124 0.0092  1025 PRO A N   
7396  C CA  . PRO A 1027 ? 0.2928 0.2765 0.2262 0.0159  -0.0140 0.0101  1025 PRO A CA  
7397  C C   . PRO A 1027 ? 0.2786 0.2656 0.2124 0.0167  -0.0157 0.0068  1025 PRO A C   
7398  O O   . PRO A 1027 ? 0.2818 0.2714 0.2131 0.0184  -0.0172 0.0072  1025 PRO A O   
7399  C CB  . PRO A 1027 ? 0.2910 0.2725 0.2255 0.0163  -0.0146 0.0125  1025 PRO A CB  
7400  C CG  . PRO A 1027 ? 0.2993 0.2792 0.2381 0.0148  -0.0140 0.0109  1025 PRO A CG  
7401  C CD  . PRO A 1027 ? 0.2715 0.2503 0.2106 0.0132  -0.0122 0.0101  1025 PRO A CD  
7402  N N   . LEU A 1028 ? 0.2762 0.2634 0.2135 0.0155  -0.0157 0.0036  1026 LEU A N   
7403  C CA  . LEU A 1028 ? 0.2785 0.2690 0.2167 0.0160  -0.0175 0.0002  1026 LEU A CA  
7404  C C   . LEU A 1028 ? 0.3105 0.3027 0.2472 0.0162  -0.0175 -0.0023 1026 LEU A C   
7405  O O   . LEU A 1028 ? 0.2859 0.2810 0.2230 0.0169  -0.0191 -0.0053 1026 LEU A O   
7406  C CB  . LEU A 1028 ? 0.2745 0.2647 0.2177 0.0145  -0.0178 -0.0020 1026 LEU A CB  
7407  C CG  . LEU A 1028 ? 0.3110 0.3005 0.2564 0.0144  -0.0180 -0.0005 1026 LEU A CG  
7408  C CD1 . LEU A 1028 ? 0.2752 0.2660 0.2254 0.0129  -0.0184 -0.0031 1026 LEU A CD1 
7409  C CD2 . LEU A 1028 ? 0.3230 0.3141 0.2663 0.0166  -0.0197 0.0007  1026 LEU A CD2 
7410  N N   . TYR A 1029 ? 0.2789 0.2696 0.2141 0.0158  -0.0158 -0.0012 1027 TYR A N   
7411  C CA  . TYR A 1029 ? 0.2854 0.2773 0.2199 0.0159  -0.0156 -0.0041 1027 TYR A CA  
7412  C C   . TYR A 1029 ? 0.2947 0.2912 0.2255 0.0181  -0.0170 -0.0055 1027 TYR A C   
7413  O O   . TYR A 1029 ? 0.2857 0.2845 0.2175 0.0185  -0.0183 -0.0095 1027 TYR A O   
7414  C CB  . TYR A 1029 ? 0.3541 0.3439 0.2876 0.0153  -0.0135 -0.0023 1027 TYR A CB  
7415  C CG  . TYR A 1029 ? 0.3058 0.2954 0.2408 0.0149  -0.0130 -0.0053 1027 TYR A CG  
7416  C CD1 . TYR A 1029 ? 0.3338 0.3211 0.2734 0.0132  -0.0133 -0.0075 1027 TYR A CD1 
7417  C CD2 . TYR A 1029 ? 0.3297 0.3213 0.2616 0.0161  -0.0123 -0.0058 1027 TYR A CD2 
7418  C CE1 . TYR A 1029 ? 0.2881 0.2746 0.2295 0.0128  -0.0131 -0.0101 1027 TYR A CE1 
7419  C CE2 . TYR A 1029 ? 0.3041 0.2953 0.2376 0.0159  -0.0121 -0.0088 1027 TYR A CE2 
7420  C CZ  . TYR A 1029 ? 0.3225 0.3108 0.2609 0.0143  -0.0125 -0.0109 1027 TYR A CZ  
7421  O OH  . TYR A 1029 ? 0.3382 0.3256 0.2786 0.0142  -0.0125 -0.0138 1027 TYR A OH  
7422  N N   . LEU A 1030 ? 0.2866 0.2846 0.2132 0.0194  -0.0168 -0.0023 1028 LEU A N   
7423  C CA  . LEU A 1030 ? 0.2908 0.2939 0.2133 0.0215  -0.0179 -0.0033 1028 LEU A CA  
7424  C C   . LEU A 1030 ? 0.2923 0.2981 0.2156 0.0224  -0.0204 -0.0059 1028 LEU A C   
7425  O O   . LEU A 1030 ? 0.2953 0.3054 0.2167 0.0238  -0.0217 -0.0088 1028 LEU A O   
7426  C CB  . LEU A 1030 ? 0.2933 0.2976 0.2112 0.0225  -0.0172 0.0013  1028 LEU A CB  
7427  C CG  . LEU A 1030 ? 0.3317 0.3339 0.2484 0.0216  -0.0147 0.0042  1028 LEU A CG  
7428  C CD1 . LEU A 1030 ? 0.3218 0.3260 0.2342 0.0226  -0.0144 0.0088  1028 LEU A CD1 
7429  C CD2 . LEU A 1030 ? 0.3371 0.3413 0.2535 0.0218  -0.0139 0.0009  1028 LEU A CD2 
7430  N N   . GLY A 1031 ? 0.2903 0.2942 0.2164 0.0218  -0.0212 -0.0050 1029 GLY A N   
7431  C CA  . GLY A 1031 ? 0.2916 0.2985 0.2188 0.0228  -0.0237 -0.0072 1029 GLY A CA  
7432  C C   . GLY A 1031 ? 0.2914 0.2999 0.2217 0.0222  -0.0248 -0.0124 1029 GLY A C   
7433  O O   . GLY A 1031 ? 0.2935 0.3057 0.2239 0.0233  -0.0270 -0.0150 1029 GLY A O   
7434  N N   . ARG A 1032 ? 0.2892 0.2949 0.2223 0.0205  -0.0235 -0.0140 1030 ARG A N   
7435  C CA  . ARG A 1032 ? 0.2922 0.2988 0.2286 0.0198  -0.0247 -0.0189 1030 ARG A CA  
7436  C C   . ARG A 1032 ? 0.2933 0.3036 0.2266 0.0216  -0.0254 -0.0218 1030 ARG A C   
7437  O O   . ARG A 1032 ? 0.2952 0.3069 0.2309 0.0215  -0.0270 -0.0264 1030 ARG A O   
7438  C CB  . ARG A 1032 ? 0.2862 0.2884 0.2270 0.0174  -0.0232 -0.0191 1030 ARG A CB  
7439  C CG  . ARG A 1032 ? 0.3296 0.3316 0.2753 0.0161  -0.0246 -0.0235 1030 ARG A CG  
7440  C CD  . ARG A 1032 ? 0.3400 0.3430 0.2897 0.0150  -0.0261 -0.0242 1030 ARG A CD  
7441  N NE  . ARG A 1032 ? 0.3720 0.3740 0.3273 0.0131  -0.0270 -0.0276 1030 ARG A NE  
7442  C CZ  . ARG A 1032 ? 0.3686 0.3734 0.3265 0.0131  -0.0294 -0.0314 1030 ARG A CZ  
7443  N NH1 . ARG A 1032 ? 0.3622 0.3714 0.3176 0.0151  -0.0311 -0.0325 1030 ARG A NH1 
7444  N NH2 . ARG A 1032 ? 0.3700 0.3733 0.3335 0.0110  -0.0302 -0.0340 1030 ARG A NH2 
7445  N N   . LEU A 1033 ? 0.2954 0.3074 0.2234 0.0231  -0.0244 -0.0194 1031 LEU A N   
7446  C CA  . LEU A 1033 ? 0.2990 0.3148 0.2238 0.0248  -0.0246 -0.0222 1031 LEU A CA  
7447  C C   . LEU A 1033 ? 0.3184 0.3402 0.2385 0.0272  -0.0262 -0.0222 1031 LEU A C   
7448  O O   . LEU A 1033 ? 0.3115 0.3375 0.2275 0.0289  -0.0262 -0.0235 1031 LEU A O   
7449  C CB  . LEU A 1033 ? 0.2986 0.3131 0.2209 0.0247  -0.0221 -0.0197 1031 LEU A CB  
7450  C CG  . LEU A 1033 ? 0.3120 0.3208 0.2387 0.0224  -0.0205 -0.0194 1031 LEU A CG  
7451  C CD1 . LEU A 1033 ? 0.2944 0.3025 0.2186 0.0225  -0.0181 -0.0169 1031 LEU A CD1 
7452  C CD2 . LEU A 1033 ? 0.3104 0.3184 0.2416 0.0218  -0.0217 -0.0247 1031 LEU A CD2 
7453  N N   . VAL A 1034 ? 0.3032 0.3255 0.2235 0.0275  -0.0277 -0.0208 1032 VAL A N   
7454  C CA  . VAL A 1034 ? 0.3105 0.3384 0.2269 0.0298  -0.0296 -0.0208 1032 VAL A CA  
7455  C C   . VAL A 1034 ? 0.3334 0.3624 0.2535 0.0296  -0.0322 -0.0239 1032 VAL A C   
7456  O O   . VAL A 1034 ? 0.3242 0.3496 0.2498 0.0277  -0.0322 -0.0248 1032 VAL A O   
7457  C CB  . VAL A 1034 ? 0.3430 0.3710 0.2552 0.0306  -0.0289 -0.0147 1032 VAL A CB  
7458  C CG1 . VAL A 1034 ? 0.3333 0.3615 0.2415 0.0308  -0.0265 -0.0117 1032 VAL A CG1 
7459  C CG2 . VAL A 1034 ? 0.3092 0.3320 0.2250 0.0291  -0.0285 -0.0115 1032 VAL A CG2 
7460  N N   . THR A 1035 ? 0.3324 0.3671 0.2497 0.0318  -0.0345 -0.0255 1033 THR A N   
7461  C CA  . THR A 1035 ? 0.3584 0.3949 0.2792 0.0318  -0.0371 -0.0289 1033 THR A CA  
7462  C C   . THR A 1035 ? 0.3538 0.3888 0.2761 0.0316  -0.0377 -0.0253 1033 THR A C   
7463  O O   . THR A 1035 ? 0.4246 0.4592 0.3517 0.0306  -0.0390 -0.0275 1033 THR A O   
7464  C CB  . THR A 1035 ? 0.3619 0.4054 0.2793 0.0343  -0.0395 -0.0323 1033 THR A CB  
7465  O OG1 . THR A 1035 ? 0.4362 0.4829 0.3469 0.0363  -0.0392 -0.0281 1033 THR A OG1 
7466  C CG2 . THR A 1035 ? 0.3470 0.3918 0.2645 0.0344  -0.0393 -0.0372 1033 THR A CG2 
7467  N N   . THR A 1036 ? 0.3577 0.3918 0.2762 0.0325  -0.0367 -0.0200 1034 THR A N   
7468  C CA  . THR A 1036 ? 0.3479 0.3800 0.2678 0.0325  -0.0371 -0.0163 1034 THR A CA  
7469  C C   . THR A 1036 ? 0.3432 0.3698 0.2631 0.0312  -0.0344 -0.0118 1034 THR A C   
7470  O O   . THR A 1036 ? 0.3482 0.3747 0.2637 0.0319  -0.0332 -0.0083 1034 THR A O   
7471  C CB  . THR A 1036 ? 0.4228 0.4592 0.3381 0.0352  -0.0391 -0.0139 1034 THR A CB  
7472  O OG1 . THR A 1036 ? 0.4937 0.5358 0.4086 0.0365  -0.0416 -0.0184 1034 THR A OG1 
7473  C CG2 . THR A 1036 ? 0.4603 0.4944 0.3777 0.0355  -0.0400 -0.0107 1034 THR A CG2 
7474  N N   . ALA A 1037 ? 0.3015 0.3238 0.2263 0.0292  -0.0336 -0.0119 1035 ALA A N   
7475  C CA  . ALA A 1037 ? 0.3312 0.3483 0.2565 0.0278  -0.0311 -0.0082 1035 ALA A CA  
7476  C C   . ALA A 1037 ? 0.3430 0.3590 0.2659 0.0291  -0.0313 -0.0032 1035 ALA A C   
7477  O O   . ALA A 1037 ? 0.3676 0.3850 0.2915 0.0303  -0.0333 -0.0029 1035 ALA A O   
7478  C CB  . ALA A 1037 ? 0.3477 0.3613 0.2789 0.0255  -0.0302 -0.0097 1035 ALA A CB  
7479  N N   . PRO A 1038 ? 0.3602 0.3737 0.2803 0.0288  -0.0295 0.0007  1036 PRO A N   
7480  C CA  . PRO A 1038 ? 0.3424 0.3538 0.2613 0.0296  -0.0297 0.0057  1036 PRO A CA  
7481  C C   . PRO A 1038 ? 0.3572 0.3638 0.2808 0.0283  -0.0291 0.0063  1036 PRO A C   
7482  O O   . PRO A 1038 ? 0.3585 0.3637 0.2859 0.0266  -0.0281 0.0035  1036 PRO A O   
7483  C CB  . PRO A 1038 ? 0.3333 0.3438 0.2481 0.0294  -0.0278 0.0092  1036 PRO A CB  
7484  C CG  . PRO A 1038 ? 0.3590 0.3682 0.2756 0.0275  -0.0257 0.0062  1036 PRO A CG  
7485  C CD  . PRO A 1038 ? 0.3178 0.3303 0.2364 0.0277  -0.0272 0.0008  1036 PRO A CD  
7486  N N   . VAL A 1039 ? 0.3199 0.3244 0.2434 0.0292  -0.0298 0.0100  1037 VAL A N   
7487  C CA  . VAL A 1039 ? 0.3543 0.3543 0.2818 0.0283  -0.0291 0.0109  1037 VAL A CA  
7488  C C   . VAL A 1039 ? 0.3070 0.3031 0.2337 0.0267  -0.0266 0.0135  1037 VAL A C   
7489  O O   . VAL A 1039 ? 0.2978 0.2932 0.2213 0.0272  -0.0264 0.0175  1037 VAL A O   
7490  C CB  . VAL A 1039 ? 0.3434 0.3426 0.2716 0.0301  -0.0312 0.0135  1037 VAL A CB  
7491  C CG1 . VAL A 1039 ? 0.3603 0.3556 0.2930 0.0294  -0.0307 0.0134  1037 VAL A CG1 
7492  C CG2 . VAL A 1039 ? 0.3236 0.3274 0.2520 0.0320  -0.0339 0.0112  1037 VAL A CG2 
7493  N N   . PRO A 1040 ? 0.3183 0.3121 0.2479 0.0247  -0.0247 0.0118  1038 PRO A N   
7494  C CA  . PRO A 1040 ? 0.3221 0.3126 0.2510 0.0233  -0.0224 0.0141  1038 PRO A CA  
7495  C C   . PRO A 1040 ? 0.3370 0.3237 0.2665 0.0235  -0.0226 0.0179  1038 PRO A C   
7496  O O   . PRO A 1040 ? 0.3495 0.3355 0.2813 0.0246  -0.0243 0.0179  1038 PRO A O   
7497  C CB  . PRO A 1040 ? 0.2894 0.2785 0.2219 0.0212  -0.0209 0.0111  1038 PRO A CB  
7498  C CG  . PRO A 1040 ? 0.3005 0.2931 0.2347 0.0215  -0.0222 0.0071  1038 PRO A CG  
7499  C CD  . PRO A 1040 ? 0.2960 0.2908 0.2295 0.0236  -0.0247 0.0075  1038 PRO A CD  
7500  N N   . PRO A 1041 ? 0.3101 0.2944 0.2380 0.0226  -0.0210 0.0210  1039 PRO A N   
7501  C CA  . PRO A 1041 ? 0.3485 0.3285 0.2780 0.0225  -0.0211 0.0242  1039 PRO A CA  
7502  C C   . PRO A 1041 ? 0.3233 0.3010 0.2574 0.0218  -0.0210 0.0218  1039 PRO A C   
7503  O O   . PRO A 1041 ? 0.3087 0.2870 0.2446 0.0205  -0.0197 0.0188  1039 PRO A O   
7504  C CB  . PRO A 1041 ? 0.3523 0.3306 0.2800 0.0210  -0.0189 0.0267  1039 PRO A CB  
7505  C CG  . PRO A 1041 ? 0.3440 0.3264 0.2679 0.0212  -0.0182 0.0259  1039 PRO A CG  
7506  C CD  . PRO A 1041 ? 0.3487 0.3340 0.2738 0.0217  -0.0191 0.0214  1039 PRO A CD  
7507  N N   . GLN A 1042 ? 0.3013 0.2768 0.2375 0.0228  -0.0225 0.0232  1040 GLN A N   
7508  C CA  . GLN A 1042 ? 0.2854 0.2589 0.2259 0.0226  -0.0225 0.0213  1040 GLN A CA  
7509  C C   . GLN A 1042 ? 0.3077 0.2845 0.2507 0.0225  -0.0227 0.0170  1040 GLN A C   
7510  O O   . GLN A 1042 ? 0.3221 0.2984 0.2684 0.0217  -0.0220 0.0151  1040 GLN A O   
7511  C CB  . GLN A 1042 ? 0.3385 0.3088 0.2801 0.0206  -0.0204 0.0220  1040 GLN A CB  
7512  C CG  . GLN A 1042 ? 0.3435 0.3106 0.2835 0.0204  -0.0201 0.0263  1040 GLN A CG  
7513  C CD  . GLN A 1042 ? 0.4272 0.3913 0.3688 0.0186  -0.0182 0.0265  1040 GLN A CD  
7514  O OE1 . GLN A 1042 ? 0.4796 0.4435 0.4193 0.0172  -0.0164 0.0277  1040 GLN A OE1 
7515  N NE2 . GLN A 1042 ? 0.4463 0.4084 0.3915 0.0188  -0.0188 0.0253  1040 GLN A NE2 
7516  N N   . HIS A 1043 ? 0.2834 0.2640 0.2250 0.0233  -0.0237 0.0155  1041 HIS A N   
7517  C CA  . HIS A 1043 ? 0.3039 0.2879 0.2479 0.0227  -0.0237 0.0115  1041 HIS A CA  
7518  C C   . HIS A 1043 ? 0.3178 0.3040 0.2641 0.0247  -0.0261 0.0102  1041 HIS A C   
7519  O O   . HIS A 1043 ? 0.3036 0.2923 0.2481 0.0262  -0.0279 0.0102  1041 HIS A O   
7520  C CB  . HIS A 1043 ? 0.3182 0.3050 0.2597 0.0223  -0.0234 0.0101  1041 HIS A CB  
7521  C CG  . HIS A 1043 ? 0.3172 0.3072 0.2613 0.0215  -0.0236 0.0062  1041 HIS A CG  
7522  N ND1 . HIS A 1043 ? 0.2793 0.2689 0.2257 0.0193  -0.0219 0.0044  1041 HIS A ND1 
7523  C CD2 . HIS A 1043 ? 0.3166 0.3105 0.2617 0.0225  -0.0255 0.0038  1041 HIS A CD2 
7524  C CE1 . HIS A 1043 ? 0.3000 0.2929 0.2489 0.0189  -0.0226 0.0012  1041 HIS A CE1 
7525  N NE2 . HIS A 1043 ? 0.2988 0.2944 0.2470 0.0208  -0.0248 0.0007  1041 HIS A NE2 
7526  N N   . SER A 1044 ? 0.2912 0.2768 0.2413 0.0246  -0.0261 0.0089  1042 SER A N   
7527  C CA  . SER A 1044 ? 0.3033 0.2911 0.2564 0.0265  -0.0282 0.0072  1042 SER A CA  
7528  C C   . SER A 1044 ? 0.3242 0.3121 0.2815 0.0257  -0.0272 0.0053  1042 SER A C   
7529  O O   . SER A 1044 ? 0.3236 0.3088 0.2810 0.0242  -0.0253 0.0060  1042 SER A O   
7530  C CB  . SER A 1044 ? 0.3108 0.2967 0.2628 0.0290  -0.0305 0.0099  1042 SER A CB  
7531  O OG  . SER A 1044 ? 0.3418 0.3232 0.2949 0.0289  -0.0300 0.0118  1042 SER A OG  
7532  N N   . SER A 1045 ? 0.3287 0.3199 0.2893 0.0270  -0.0286 0.0028  1043 SER A N   
7533  C CA  . SER A 1045 ? 0.3293 0.3216 0.2939 0.0266  -0.0278 0.0008  1043 SER A CA  
7534  C C   . SER A 1045 ? 0.2894 0.2841 0.2570 0.0293  -0.0302 -0.0007 1043 SER A C   
7535  O O   . SER A 1045 ? 0.2866 0.2843 0.2542 0.0306  -0.0320 -0.0016 1043 SER A O   
7536  C CB  . SER A 1045 ? 0.2936 0.2897 0.2602 0.0242  -0.0260 -0.0016 1043 SER A CB  
7537  O OG  . SER A 1045 ? 0.2996 0.2979 0.2700 0.0241  -0.0254 -0.0036 1043 SER A OG  
7538  N N   . VAL A 1046 ? 0.2753 0.2687 0.2455 0.0303  -0.0303 -0.0013 1044 VAL A N   
7539  C CA  . VAL A 1046 ? 0.3216 0.3176 0.2953 0.0330  -0.0325 -0.0034 1044 VAL A CA  
7540  C C   . VAL A 1046 ? 0.2973 0.2997 0.2749 0.0323  -0.0316 -0.0071 1044 VAL A C   
7541  O O   . VAL A 1046 ? 0.3055 0.3112 0.2864 0.0345  -0.0333 -0.0093 1044 VAL A O   
7542  C CB  . VAL A 1046 ? 0.3086 0.3006 0.2839 0.0349  -0.0336 -0.0026 1044 VAL A CB  
7543  C CG1 . VAL A 1046 ? 0.3615 0.3474 0.3333 0.0354  -0.0347 0.0015  1044 VAL A CG1 
7544  C CG2 . VAL A 1046 ? 0.2789 0.2704 0.2557 0.0332  -0.0313 -0.0038 1044 VAL A CG2 
7545  N N   . HIS A 1047 ? 0.2807 0.2848 0.2580 0.0292  -0.0291 -0.0076 1045 HIS A N   
7546  C CA  . HIS A 1047 ? 0.3048 0.3153 0.2858 0.0280  -0.0281 -0.0106 1045 HIS A CA  
7547  C C   . HIS A 1047 ? 0.3446 0.3594 0.3262 0.0278  -0.0290 -0.0119 1045 HIS A C   
7548  O O   . HIS A 1047 ? 0.3402 0.3533 0.3189 0.0269  -0.0292 -0.0105 1045 HIS A O   
7549  C CB  . HIS A 1047 ? 0.3308 0.3410 0.3115 0.0248  -0.0251 -0.0102 1045 HIS A CB  
7550  C CG  . HIS A 1047 ? 0.3573 0.3737 0.3409 0.0227  -0.0238 -0.0123 1045 HIS A CG  
7551  N ND1 . HIS A 1047 ? 0.3419 0.3638 0.3295 0.0229  -0.0233 -0.0146 1045 HIS A ND1 
7552  C CD2 . HIS A 1047 ? 0.3760 0.3943 0.3596 0.0202  -0.0230 -0.0123 1045 HIS A CD2 
7553  C CE1 . HIS A 1047 ? 0.3849 0.4118 0.3746 0.0205  -0.0222 -0.0156 1045 HIS A CE1 
7554  N NE2 . HIS A 1047 ? 0.2813 0.3058 0.2688 0.0188  -0.0221 -0.0142 1045 HIS A NE2 
7555  N N   . THR A 1048 ? 0.3280 0.3489 0.3137 0.0286  -0.0298 -0.0147 1046 THR A N   
7556  C CA  . THR A 1048 ? 0.2923 0.3184 0.2797 0.0281  -0.0306 -0.0164 1046 THR A CA  
7557  C C   . THR A 1048 ? 0.3131 0.3447 0.3040 0.0253  -0.0286 -0.0181 1046 THR A C   
7558  O O   . THR A 1048 ? 0.3195 0.3543 0.3133 0.0256  -0.0277 -0.0195 1046 THR A O   
7559  C CB  . THR A 1048 ? 0.3183 0.3477 0.3079 0.0314  -0.0335 -0.0180 1046 THR A CB  
7560  O OG1 . THR A 1048 ? 0.3107 0.3346 0.2973 0.0341  -0.0354 -0.0158 1046 THR A OG1 
7561  C CG2 . THR A 1048 ? 0.3060 0.3401 0.2966 0.0309  -0.0347 -0.0195 1046 THR A CG2 
7562  N N   . ASP A 1049 ? 0.2755 0.3084 0.2663 0.0226  -0.0278 -0.0181 1047 ASP A N   
7563  C CA  . ASP A 1049 ? 0.2733 0.3114 0.2677 0.0197  -0.0260 -0.0193 1047 ASP A CA  
7564  C C   . ASP A 1049 ? 0.2583 0.3040 0.2575 0.0210  -0.0270 -0.0221 1047 ASP A C   
7565  O O   . ASP A 1049 ? 0.2601 0.3080 0.2601 0.0228  -0.0293 -0.0234 1047 ASP A O   
7566  C CB  . ASP A 1049 ? 0.2582 0.2961 0.2523 0.0168  -0.0257 -0.0190 1047 ASP A CB  
7567  C CG  . ASP A 1049 ? 0.2782 0.3210 0.2764 0.0133  -0.0239 -0.0197 1047 ASP A CG  
7568  O OD1 . ASP A 1049 ? 0.2740 0.3232 0.2762 0.0131  -0.0246 -0.0217 1047 ASP A OD1 
7569  O OD2 . ASP A 1049 ? 0.3160 0.3563 0.3133 0.0109  -0.0217 -0.0180 1047 ASP A OD2 
7570  N N   . PRO A 1050 ? 0.2584 0.3087 0.2607 0.0202  -0.0255 -0.0231 1048 PRO A N   
7571  C CA  . PRO A 1050 ? 0.2561 0.3144 0.2631 0.0217  -0.0263 -0.0259 1048 PRO A CA  
7572  C C   . PRO A 1050 ? 0.2729 0.3374 0.2835 0.0194  -0.0265 -0.0272 1048 PRO A C   
7573  O O   . PRO A 1050 ? 0.2781 0.3486 0.2922 0.0210  -0.0281 -0.0295 1048 PRO A O   
7574  C CB  . PRO A 1050 ? 0.3097 0.3713 0.3186 0.0212  -0.0242 -0.0265 1048 PRO A CB  
7575  C CG  . PRO A 1050 ? 0.2845 0.3415 0.2906 0.0181  -0.0219 -0.0239 1048 PRO A CG  
7576  C CD  . PRO A 1050 ? 0.2721 0.3208 0.2737 0.0186  -0.0229 -0.0218 1048 PRO A CD  
7577  N N   . VAL A 1051 ? 0.2541 0.3174 0.2644 0.0156  -0.0251 -0.0258 1049 VAL A N   
7578  C CA  . VAL A 1051 ? 0.2538 0.3225 0.2679 0.0133  -0.0256 -0.0270 1049 VAL A CA  
7579  C C   . VAL A 1051 ? 0.2563 0.3230 0.2690 0.0150  -0.0284 -0.0279 1049 VAL A C   
7580  O O   . VAL A 1051 ? 0.2568 0.3294 0.2731 0.0154  -0.0300 -0.0300 1049 VAL A O   
7581  C CB  . VAL A 1051 ? 0.2523 0.3199 0.2670 0.0088  -0.0235 -0.0252 1049 VAL A CB  
7582  C CG1 . VAL A 1051 ? 0.2893 0.3621 0.3085 0.0062  -0.0242 -0.0264 1049 VAL A CG1 
7583  C CG2 . VAL A 1051 ? 0.2502 0.3204 0.2660 0.0073  -0.0208 -0.0242 1049 VAL A CG2 
7584  N N   . LEU A 1052 ? 0.2579 0.3171 0.2654 0.0163  -0.0291 -0.0263 1050 LEU A N   
7585  C CA  . LEU A 1052 ? 0.2607 0.3185 0.2662 0.0186  -0.0319 -0.0270 1050 LEU A CA  
7586  C C   . LEU A 1052 ? 0.2620 0.3242 0.2696 0.0222  -0.0340 -0.0288 1050 LEU A C   
7587  O O   . LEU A 1052 ? 0.2634 0.3295 0.2728 0.0232  -0.0362 -0.0306 1050 LEU A O   
7588  C CB  . LEU A 1052 ? 0.2624 0.3120 0.2618 0.0199  -0.0321 -0.0246 1050 LEU A CB  
7589  C CG  . LEU A 1052 ? 0.2918 0.3395 0.2879 0.0226  -0.0348 -0.0246 1050 LEU A CG  
7590  C CD1 . LEU A 1052 ? 0.2679 0.3162 0.2638 0.0266  -0.0369 -0.0248 1050 LEU A CD1 
7591  C CD2 . LEU A 1052 ? 0.2665 0.3187 0.2650 0.0214  -0.0363 -0.0269 1050 LEU A CD2 
7592  N N   . LEU A 1053 ? 0.2617 0.3234 0.2693 0.0244  -0.0335 -0.0286 1051 LEU A N   
7593  C CA  . LEU A 1053 ? 0.2805 0.3459 0.2904 0.0281  -0.0357 -0.0305 1051 LEU A CA  
7594  C C   . LEU A 1053 ? 0.2619 0.3368 0.2778 0.0274  -0.0358 -0.0333 1051 LEU A C   
7595  O O   . LEU A 1053 ? 0.2636 0.3425 0.2815 0.0297  -0.0383 -0.0352 1051 LEU A O   
7596  C CB  . LEU A 1053 ? 0.2862 0.3490 0.2954 0.0303  -0.0350 -0.0300 1051 LEU A CB  
7597  C CG  . LEU A 1053 ? 0.3130 0.3670 0.3171 0.0321  -0.0357 -0.0273 1051 LEU A CG  
7598  C CD1 . LEU A 1053 ? 0.2720 0.3240 0.2765 0.0339  -0.0350 -0.0273 1051 LEU A CD1 
7599  C CD2 . LEU A 1053 ? 0.2951 0.3471 0.2973 0.0352  -0.0389 -0.0270 1051 LEU A CD2 
7600  N N   . ASP A 1054 ? 0.2591 0.3380 0.2778 0.0240  -0.0332 -0.0336 1052 ASP A N   
7601  C CA  . ASP A 1054 ? 0.2578 0.3463 0.2825 0.0226  -0.0331 -0.0359 1052 ASP A CA  
7602  C C   . ASP A 1054 ? 0.2589 0.3489 0.2847 0.0213  -0.0349 -0.0367 1052 ASP A C   
7603  O O   . ASP A 1054 ? 0.2664 0.3634 0.2964 0.0222  -0.0365 -0.0391 1052 ASP A O   
7604  C CB  . ASP A 1054 ? 0.2824 0.3745 0.3096 0.0187  -0.0299 -0.0352 1052 ASP A CB  
7605  C CG  . ASP A 1054 ? 0.3000 0.3927 0.3269 0.0201  -0.0282 -0.0352 1052 ASP A CG  
7606  O OD1 . ASP A 1054 ? 0.2929 0.3843 0.3190 0.0242  -0.0298 -0.0363 1052 ASP A OD1 
7607  O OD2 . ASP A 1054 ? 0.2974 0.3919 0.3252 0.0172  -0.0255 -0.0340 1052 ASP A OD2 
7608  N N   . PHE A 1055 ? 0.2594 0.3433 0.2817 0.0193  -0.0348 -0.0350 1053 PHE A N   
7609  C CA  . PHE A 1055 ? 0.2655 0.3506 0.2887 0.0181  -0.0366 -0.0360 1053 PHE A CA  
7610  C C   . PHE A 1055 ? 0.2637 0.3489 0.2854 0.0220  -0.0399 -0.0373 1053 PHE A C   
7611  O O   . PHE A 1055 ? 0.2646 0.3552 0.2895 0.0221  -0.0418 -0.0395 1053 PHE A O   
7612  C CB  . PHE A 1055 ? 0.2609 0.3392 0.2806 0.0154  -0.0356 -0.0341 1053 PHE A CB  
7613  C CG  . PHE A 1055 ? 0.2626 0.3416 0.2830 0.0141  -0.0376 -0.0356 1053 PHE A CG  
7614  C CD1 . PHE A 1055 ? 0.3051 0.3909 0.3315 0.0116  -0.0381 -0.0376 1053 PHE A CD1 
7615  C CD2 . PHE A 1055 ? 0.2649 0.3380 0.2802 0.0154  -0.0389 -0.0350 1053 PHE A CD2 
7616  C CE1 . PHE A 1055 ? 0.2639 0.3501 0.2912 0.0105  -0.0401 -0.0392 1053 PHE A CE1 
7617  C CE2 . PHE A 1055 ? 0.2668 0.3407 0.2826 0.0144  -0.0408 -0.0367 1053 PHE A CE2 
7618  C CZ  . PHE A 1055 ? 0.2663 0.3466 0.2882 0.0120  -0.0415 -0.0390 1053 PHE A CZ  
7619  N N   . ALA A 1056 ? 0.3060 0.3855 0.3230 0.0254  -0.0407 -0.0359 1054 ALA A N   
7620  C CA  . ALA A 1056 ? 0.2688 0.3484 0.2841 0.0292  -0.0440 -0.0366 1054 ALA A CA  
7621  C C   . ALA A 1056 ? 0.2689 0.3563 0.2894 0.0316  -0.0456 -0.0392 1054 ALA A C   
7622  O O   . ALA A 1056 ? 0.2710 0.3621 0.2928 0.0332  -0.0483 -0.0409 1054 ALA A O   
7623  C CB  . ALA A 1056 ? 0.2709 0.3428 0.2806 0.0321  -0.0445 -0.0340 1054 ALA A CB  
7624  N N   . LYS A 1057 ? 0.3314 0.4215 0.3548 0.0320  -0.0440 -0.0398 1055 LYS A N   
7625  C CA  . LYS A 1057 ? 0.3228 0.4213 0.3517 0.0341  -0.0452 -0.0426 1055 LYS A CA  
7626  C C   . LYS A 1057 ? 0.3189 0.4255 0.3530 0.0313  -0.0453 -0.0448 1055 LYS A C   
7627  O O   . LYS A 1057 ? 0.3567 0.4694 0.3942 0.0332  -0.0476 -0.0472 1055 LYS A O   
7628  C CB  . LYS A 1057 ? 0.3191 0.4196 0.3501 0.0348  -0.0432 -0.0431 1055 LYS A CB  
7629  C CG  . LYS A 1057 ? 0.3197 0.4136 0.3473 0.0386  -0.0441 -0.0419 1055 LYS A CG  
7630  C CD  . LYS A 1057 ? 0.3364 0.4335 0.3668 0.0398  -0.0426 -0.0433 1055 LYS A CD  
7631  C CE  . LYS A 1057 ? 0.3075 0.4060 0.3384 0.0355  -0.0388 -0.0424 1055 LYS A CE  
7632  N NZ  . LYS A 1057 ? 0.3592 0.4588 0.3911 0.0368  -0.0372 -0.0432 1055 LYS A NZ  
7633  N N   . TRP A 1058 ? 0.3092 0.4160 0.3442 0.0266  -0.0428 -0.0440 1056 TRP A N   
7634  C CA  . TRP A 1058 ? 0.3065 0.4201 0.3466 0.0234  -0.0429 -0.0457 1056 TRP A CA  
7635  C C   . TRP A 1058 ? 0.3025 0.4155 0.3416 0.0243  -0.0461 -0.0468 1056 TRP A C   
7636  O O   . TRP A 1058 ? 0.3485 0.4688 0.3923 0.0244  -0.0479 -0.0493 1056 TRP A O   
7637  C CB  . TRP A 1058 ? 0.2907 0.4029 0.3315 0.0183  -0.0400 -0.0440 1056 TRP A CB  
7638  C CG  . TRP A 1058 ? 0.3639 0.4824 0.4103 0.0145  -0.0402 -0.0454 1056 TRP A CG  
7639  C CD1 . TRP A 1058 ? 0.3044 0.4323 0.3575 0.0125  -0.0392 -0.0467 1056 TRP A CD1 
7640  C CD2 . TRP A 1058 ? 0.3474 0.4635 0.3936 0.0122  -0.0417 -0.0457 1056 TRP A CD2 
7641  N NE1 . TRP A 1058 ? 0.3537 0.4849 0.4109 0.0089  -0.0400 -0.0475 1056 TRP A NE1 
7642  C CE2 . TRP A 1058 ? 0.3371 0.4609 0.3903 0.0087  -0.0416 -0.0472 1056 TRP A CE2 
7643  C CE3 . TRP A 1058 ? 0.3071 0.4156 0.3481 0.0128  -0.0430 -0.0450 1056 TRP A CE3 
7644  C CZ2 . TRP A 1058 ? 0.3437 0.4673 0.3990 0.0059  -0.0430 -0.0481 1056 TRP A CZ2 
7645  C CZ3 . TRP A 1058 ? 0.2862 0.3948 0.3290 0.0102  -0.0444 -0.0463 1056 TRP A CZ3 
7646  C CH2 . TRP A 1058 ? 0.3169 0.4328 0.3669 0.0068  -0.0444 -0.0479 1056 TRP A CH2 
7647  N N   . LEU A 1059 ? 0.2837 0.3886 0.3167 0.0251  -0.0469 -0.0451 1057 LEU A N   
7648  C CA  . LEU A 1059 ? 0.2722 0.3767 0.3035 0.0262  -0.0499 -0.0462 1057 LEU A CA  
7649  C C   . LEU A 1059 ? 0.3352 0.4440 0.3677 0.0306  -0.0530 -0.0479 1057 LEU A C   
7650  O O   . LEU A 1059 ? 0.3119 0.4262 0.3473 0.0309  -0.0554 -0.0503 1057 LEU A O   
7651  C CB  . LEU A 1059 ? 0.3075 0.4028 0.3315 0.0268  -0.0500 -0.0438 1057 LEU A CB  
7652  C CG  . LEU A 1059 ? 0.2704 0.3612 0.2930 0.0226  -0.0477 -0.0425 1057 LEU A CG  
7653  C CD1 . LEU A 1059 ? 0.2721 0.3544 0.2874 0.0239  -0.0476 -0.0400 1057 LEU A CD1 
7654  C CD2 . LEU A 1059 ? 0.2710 0.3656 0.2971 0.0199  -0.0490 -0.0449 1057 LEU A CD2 
7655  N N   . ASP A 1060 ? 0.3427 0.4492 0.3733 0.0342  -0.0532 -0.0468 1058 ASP A N   
7656  C CA  . ASP A 1060 ? 0.3850 0.4954 0.4170 0.0386  -0.0562 -0.0483 1058 ASP A CA  
7657  C C   . ASP A 1060 ? 0.3716 0.4924 0.4113 0.0381  -0.0565 -0.0516 1058 ASP A C   
7658  O O   . ASP A 1060 ? 0.4099 0.5360 0.4520 0.0402  -0.0594 -0.0537 1058 ASP A O   
7659  C CB  . ASP A 1060 ? 0.3607 0.4665 0.3902 0.0422  -0.0562 -0.0466 1058 ASP A CB  
7660  C CG  . ASP A 1060 ? 0.4283 0.5265 0.4513 0.0450  -0.0582 -0.0440 1058 ASP A CG  
7661  O OD1 . ASP A 1060 ? 0.4055 0.5046 0.4268 0.0458  -0.0607 -0.0444 1058 ASP A OD1 
7662  O OD2 . ASP A 1060 ? 0.4142 0.5058 0.4338 0.0462  -0.0573 -0.0416 1058 ASP A OD2 
7663  N N   . GLY A 1061 ? 0.3429 0.4673 0.3865 0.0352  -0.0534 -0.0520 1059 GLY A N   
7664  C CA  . GLY A 1061 ? 0.3530 0.4879 0.4039 0.0342  -0.0533 -0.0548 1059 GLY A CA  
7665  C C   . GLY A 1061 ? 0.3789 0.5186 0.4331 0.0316  -0.0548 -0.0566 1059 GLY A C   
7666  O O   . GLY A 1061 ? 0.3823 0.5303 0.4417 0.0326  -0.0566 -0.0593 1059 GLY A O   
7667  N N   . LYS A 1062 ? 0.3458 0.4804 0.3972 0.0283  -0.0542 -0.0553 1060 LYS A N   
7668  C CA  . LYS A 1062 ? 0.3726 0.5109 0.4271 0.0257  -0.0558 -0.0571 1060 LYS A CA  
7669  C C   . LYS A 1062 ? 0.3669 0.5043 0.4185 0.0291  -0.0597 -0.0584 1060 LYS A C   
7670  O O   . LYS A 1062 ? 0.4257 0.5666 0.4798 0.0275  -0.0615 -0.0604 1060 LYS A O   
7671  C CB  . LYS A 1062 ? 0.3666 0.4997 0.4197 0.0209  -0.0538 -0.0555 1060 LYS A CB  
7672  C CG  . LYS A 1062 ? 0.3906 0.5259 0.4475 0.0167  -0.0502 -0.0543 1060 LYS A CG  
7673  C CD  . LYS A 1062 ? 0.4281 0.5741 0.4935 0.0144  -0.0503 -0.0566 1060 LYS A CD  
7674  C CE  . LYS A 1062 ? 0.4166 0.5650 0.4857 0.0096  -0.0467 -0.0549 1060 LYS A CE  
7675  N NZ  . LYS A 1062 ? 0.4526 0.6121 0.5302 0.0070  -0.0466 -0.0568 1060 LYS A NZ  
7676  N N   . GLY A 1063 ? 0.3576 0.4906 0.4042 0.0336  -0.0612 -0.0571 1061 GLY A N   
7677  C CA  . GLY A 1063 ? 0.3768 0.5088 0.4199 0.0369  -0.0648 -0.0577 1061 GLY A CA  
7678  C C   . GLY A 1063 ? 0.3690 0.4929 0.4051 0.0363  -0.0650 -0.0557 1061 GLY A C   
7679  O O   . GLY A 1063 ? 0.3253 0.4485 0.3579 0.0390  -0.0680 -0.0559 1061 GLY A O   
7680  N N   . ALA A 1064 ? 0.3527 0.4710 0.3867 0.0330  -0.0619 -0.0538 1062 ALA A N   
7681  C CA  . ALA A 1064 ? 0.3000 0.4107 0.3275 0.0324  -0.0617 -0.0520 1062 ALA A CA  
7682  C C   . ALA A 1064 ? 0.3047 0.4087 0.3258 0.0359  -0.0617 -0.0488 1062 ALA A C   
7683  O O   . ALA A 1064 ? 0.2815 0.3793 0.2995 0.0348  -0.0591 -0.0462 1062 ALA A O   
7684  C CB  . ALA A 1064 ? 0.2843 0.3919 0.3127 0.0275  -0.0586 -0.0513 1062 ALA A CB  
7685  N N   . ARG A 1065 ? 0.3038 0.4093 0.3231 0.0401  -0.0648 -0.0489 1063 ARG A N   
7686  C CA  . ARG A 1065 ? 0.3112 0.4114 0.3260 0.0437  -0.0652 -0.0458 1063 ARG A CA  
7687  C C   . ARG A 1065 ? 0.3377 0.4300 0.3450 0.0436  -0.0645 -0.0427 1063 ARG A C   
7688  O O   . ARG A 1065 ? 0.3546 0.4409 0.3589 0.0441  -0.0628 -0.0398 1063 ARG A O   
7689  C CB  . ARG A 1065 ? 0.3285 0.4328 0.3440 0.0482  -0.0690 -0.0467 1063 ARG A CB  
7690  N N   . ALA A 1066 ? 0.3170 0.4097 0.3214 0.0430  -0.0659 -0.0435 1064 ALA A N   
7691  C CA  . ALA A 1066 ? 0.2943 0.3803 0.2916 0.0429  -0.0652 -0.0407 1064 ALA A CA  
7692  C C   . ALA A 1066 ? 0.3149 0.3961 0.3119 0.0392  -0.0614 -0.0397 1064 ALA A C   
7693  O O   . ALA A 1066 ? 0.3126 0.3874 0.3049 0.0394  -0.0598 -0.0365 1064 ALA A O   
7694  C CB  . ALA A 1066 ? 0.3396 0.4279 0.3341 0.0431  -0.0674 -0.0424 1064 ALA A CB  
7695  N N   . GLU A 1067 ? 0.3261 0.4105 0.3285 0.0357  -0.0600 -0.0422 1065 GLU A N   
7696  C CA  . GLU A 1067 ? 0.2842 0.3643 0.2868 0.0320  -0.0565 -0.0411 1065 GLU A CA  
7697  C C   . GLU A 1067 ? 0.2818 0.3589 0.2847 0.0325  -0.0543 -0.0387 1065 GLU A C   
7698  O O   . GLU A 1067 ? 0.3080 0.3792 0.3078 0.0312  -0.0518 -0.0363 1065 GLU A O   
7699  C CB  . GLU A 1067 ? 0.3230 0.4076 0.3318 0.0282  -0.0558 -0.0440 1065 GLU A CB  
7700  C CG  . GLU A 1067 ? 0.3009 0.3869 0.3095 0.0269  -0.0576 -0.0465 1065 GLU A CG  
7701  C CD  . GLU A 1067 ? 0.3976 0.4901 0.4079 0.0292  -0.0612 -0.0492 1065 GLU A CD  
7702  O OE1 . GLU A 1067 ? 0.3589 0.4550 0.3709 0.0319  -0.0624 -0.0492 1065 GLU A OE1 
7703  O OE2 . GLU A 1067 ? 0.3724 0.4665 0.3825 0.0284  -0.0630 -0.0517 1065 GLU A OE2 
7704  N N   . ALA A 1068 ? 0.2813 0.3627 0.2880 0.0344  -0.0551 -0.0395 1066 ALA A N   
7705  C CA  . ALA A 1068 ? 0.2796 0.3584 0.2866 0.0354  -0.0533 -0.0377 1066 ALA A CA  
7706  C C   . ALA A 1068 ? 0.2925 0.3640 0.2933 0.0379  -0.0536 -0.0343 1066 ALA A C   
7707  O O   . ALA A 1068 ? 0.2888 0.3552 0.2878 0.0371  -0.0512 -0.0322 1066 ALA A O   
7708  C CB  . ALA A 1068 ? 0.3083 0.3934 0.3205 0.0376  -0.0546 -0.0397 1066 ALA A CB  
7709  N N   . GLU A 1069 ? 0.2862 0.3573 0.2835 0.0409  -0.0564 -0.0336 1067 GLU A N   
7710  C CA  . GLU A 1069 ? 0.3144 0.3790 0.3058 0.0430  -0.0568 -0.0299 1067 GLU A CA  
7711  C C   . GLU A 1069 ? 0.3389 0.3980 0.3256 0.0405  -0.0545 -0.0280 1067 GLU A C   
7712  O O   . GLU A 1069 ? 0.3248 0.3780 0.3084 0.0406  -0.0530 -0.0250 1067 GLU A O   
7713  C CB  . GLU A 1069 ? 0.3525 0.4187 0.3412 0.0466  -0.0605 -0.0294 1067 GLU A CB  
7714  C CG  . GLU A 1069 ? 0.3551 0.4151 0.3373 0.0484  -0.0610 -0.0253 1067 GLU A CG  
7715  C CD  . GLU A 1069 ? 0.5174 0.5735 0.4998 0.0510  -0.0614 -0.0227 1067 GLU A CD  
7716  O OE1 . GLU A 1069 ? 0.5741 0.6325 0.5617 0.0517  -0.0614 -0.0245 1067 GLU A OE1 
7717  O OE2 . GLU A 1069 ? 0.5977 0.6484 0.5752 0.0523  -0.0619 -0.0188 1067 GLU A OE2 
7718  N N   . ALA A 1070 ? 0.2947 0.3558 0.2812 0.0382  -0.0544 -0.0299 1068 ALA A N   
7719  C CA  . ALA A 1070 ? 0.2921 0.3485 0.2749 0.0357  -0.0523 -0.0286 1068 ALA A CA  
7720  C C   . ALA A 1070 ? 0.2833 0.3365 0.2680 0.0331  -0.0489 -0.0277 1068 ALA A C   
7721  O O   . ALA A 1070 ? 0.3056 0.3533 0.2867 0.0322  -0.0470 -0.0253 1068 ALA A O   
7722  C CB  . ALA A 1070 ? 0.2877 0.3472 0.2711 0.0337  -0.0529 -0.0315 1068 ALA A CB  
7723  N N   . ALA A 1071 ? 0.2803 0.3376 0.2709 0.0317  -0.0482 -0.0297 1069 ALA A N   
7724  C CA  . ALA A 1071 ? 0.2766 0.3319 0.2693 0.0293  -0.0451 -0.0289 1069 ALA A CA  
7725  C C   . ALA A 1071 ? 0.2769 0.3277 0.2672 0.0314  -0.0444 -0.0263 1069 ALA A C   
7726  O O   . ALA A 1071 ? 0.2754 0.3212 0.2637 0.0299  -0.0421 -0.0242 1069 ALA A O   
7727  C CB  . ALA A 1071 ? 0.2739 0.3358 0.2733 0.0276  -0.0447 -0.0316 1069 ALA A CB  
7728  N N   . ARG A 1072 ? 0.2885 0.3409 0.2796 0.0348  -0.0465 -0.0263 1070 ARG A N   
7729  C CA  . ARG A 1072 ? 0.3134 0.3609 0.3025 0.0370  -0.0463 -0.0238 1070 ARG A CA  
7730  C C   . ARG A 1072 ? 0.2948 0.3356 0.2777 0.0371  -0.0460 -0.0204 1070 ARG A C   
7731  O O   . ARG A 1072 ? 0.2894 0.3251 0.2706 0.0366  -0.0442 -0.0182 1070 ARG A O   
7732  C CB  . ARG A 1072 ? 0.3114 0.3614 0.3025 0.0409  -0.0492 -0.0245 1070 ARG A CB  
7733  C CG  . ARG A 1072 ? 0.3236 0.3800 0.3211 0.0411  -0.0491 -0.0276 1070 ARG A CG  
7734  C CD  . ARG A 1072 ? 0.3642 0.4225 0.3638 0.0453  -0.0519 -0.0283 1070 ARG A CD  
7735  N NE  . ARG A 1072 ? 0.4044 0.4655 0.4032 0.0474  -0.0551 -0.0288 1070 ARG A NE  
7736  C CZ  . ARG A 1072 ? 0.3876 0.4561 0.3905 0.0475  -0.0565 -0.0319 1070 ARG A CZ  
7737  N NH1 . ARG A 1072 ? 0.4085 0.4827 0.4167 0.0457  -0.0549 -0.0347 1070 ARG A NH1 
7738  N NH2 . ARG A 1072 ? 0.3764 0.4470 0.3779 0.0495  -0.0595 -0.0321 1070 ARG A NH2 
7739  N N   . ASN A 1073 ? 0.2953 0.3365 0.2749 0.0377  -0.0476 -0.0201 1071 ASN A N   
7740  C CA  . ASN A 1073 ? 0.3021 0.3379 0.2757 0.0378  -0.0472 -0.0169 1071 ASN A CA  
7741  C C   . ASN A 1073 ? 0.3274 0.3600 0.2998 0.0344  -0.0440 -0.0164 1071 ASN A C   
7742  O O   . ASN A 1073 ? 0.3498 0.3771 0.3188 0.0341  -0.0426 -0.0135 1071 ASN A O   
7743  C CB  . ASN A 1073 ? 0.3806 0.4188 0.3509 0.0390  -0.0495 -0.0171 1071 ASN A CB  
7744  C CG  . ASN A 1073 ? 0.3674 0.4073 0.3373 0.0428  -0.0527 -0.0162 1071 ASN A CG  
7745  O OD1 . ASN A 1073 ? 0.4578 0.4956 0.4291 0.0446  -0.0532 -0.0147 1071 ASN A OD1 
7746  N ND2 . ASN A 1073 ? 0.4159 0.4596 0.3841 0.0441  -0.0551 -0.0172 1071 ASN A ND2 
7747  N N   . ALA A 1074 ? 0.2846 0.3204 0.2601 0.0317  -0.0430 -0.0192 1072 ALA A N   
7748  C CA  . ALA A 1074 ? 0.2972 0.3299 0.2722 0.0285  -0.0401 -0.0187 1072 ALA A CA  
7749  C C   . ALA A 1074 ? 0.2913 0.3210 0.2676 0.0278  -0.0380 -0.0172 1072 ALA A C   
7750  O O   . ALA A 1074 ? 0.3130 0.3379 0.2866 0.0266  -0.0360 -0.0151 1072 ALA A O   
7751  C CB  . ALA A 1074 ? 0.3205 0.3572 0.2995 0.0257  -0.0397 -0.0218 1072 ALA A CB  
7752  N N   . GLY A 1075 ? 0.3082 0.3411 0.2887 0.0287  -0.0383 -0.0184 1073 GLY A N   
7753  C CA  . GLY A 1075 ? 0.2727 0.3033 0.2544 0.0284  -0.0365 -0.0174 1073 GLY A CA  
7754  C C   . GLY A 1075 ? 0.3134 0.3379 0.2911 0.0302  -0.0366 -0.0143 1073 GLY A C   
7755  O O   . GLY A 1075 ? 0.3025 0.3232 0.2793 0.0290  -0.0345 -0.0128 1073 GLY A O   
7756  N N   . SER A 1076 ? 0.3054 0.3290 0.2808 0.0330  -0.0391 -0.0131 1074 SER A N   
7757  C CA  . SER A 1076 ? 0.3179 0.3358 0.2897 0.0346  -0.0394 -0.0097 1074 SER A CA  
7758  C C   . SER A 1076 ? 0.3394 0.3534 0.3063 0.0329  -0.0379 -0.0073 1074 SER A C   
7759  O O   . SER A 1076 ? 0.3644 0.3736 0.3296 0.0324  -0.0365 -0.0049 1074 SER A O   
7760  C CB  . SER A 1076 ? 0.3274 0.3458 0.2981 0.0381  -0.0427 -0.0087 1074 SER A CB  
7761  O OG  . SER A 1076 ? 0.4018 0.4222 0.3769 0.0402  -0.0440 -0.0103 1074 SER A OG  
7762  N N   . SER A 1077 ? 0.3051 0.3213 0.2702 0.0321  -0.0383 -0.0083 1075 SER A N   
7763  C CA  . SER A 1077 ? 0.3322 0.3454 0.2927 0.0309  -0.0370 -0.0064 1075 SER A CA  
7764  C C   . SER A 1077 ? 0.3412 0.3522 0.3025 0.0278  -0.0341 -0.0067 1075 SER A C   
7765  O O   . SER A 1077 ? 0.3245 0.3320 0.2824 0.0269  -0.0327 -0.0046 1075 SER A O   
7766  C CB  . SER A 1077 ? 0.3231 0.3398 0.2816 0.0311  -0.0384 -0.0078 1075 SER A CB  
7767  O OG  . SER A 1077 ? 0.4047 0.4233 0.3618 0.0341  -0.0413 -0.0071 1075 SER A OG  
7768  N N   . SER A 1078 ? 0.2947 0.3083 0.2605 0.0261  -0.0331 -0.0091 1076 SER A N   
7769  C CA  . SER A 1078 ? 0.2728 0.2844 0.2394 0.0232  -0.0304 -0.0091 1076 SER A CA  
7770  C C   . SER A 1078 ? 0.2981 0.3047 0.2628 0.0232  -0.0289 -0.0062 1076 SER A C   
7771  O O   . SER A 1078 ? 0.2865 0.2920 0.2518 0.0251  -0.0297 -0.0052 1076 SER A O   
7772  C CB  . SER A 1078 ? 0.3149 0.3305 0.2869 0.0216  -0.0297 -0.0115 1076 SER A CB  
7773  O OG  . SER A 1078 ? 0.2667 0.2804 0.2394 0.0188  -0.0271 -0.0109 1076 SER A OG  
7774  N N   . ALA A 1079 ? 0.2711 0.2747 0.2340 0.0212  -0.0269 -0.0051 1077 ALA A N   
7775  C CA  . ALA A 1079 ? 0.2703 0.2695 0.2319 0.0208  -0.0253 -0.0027 1077 ALA A CA  
7776  C C   . ALA A 1079 ? 0.2739 0.2732 0.2385 0.0186  -0.0232 -0.0036 1077 ALA A C   
7777  O O   . ALA A 1079 ? 0.2655 0.2614 0.2292 0.0178  -0.0216 -0.0019 1077 ALA A O   
7778  C CB  . ALA A 1079 ? 0.2916 0.2873 0.2487 0.0205  -0.0245 -0.0005 1077 ALA A CB  
7779  N N   . LEU A 1080 ? 0.2721 0.2757 0.2405 0.0175  -0.0232 -0.0060 1078 LEU A N   
7780  C CA  . LEU A 1080 ? 0.2645 0.2695 0.2361 0.0156  -0.0214 -0.0066 1078 LEU A CA  
7781  C C   . LEU A 1080 ? 0.2838 0.2873 0.2558 0.0169  -0.0211 -0.0058 1078 LEU A C   
7782  O O   . LEU A 1080 ? 0.2714 0.2758 0.2441 0.0193  -0.0228 -0.0062 1078 LEU A O   
7783  C CB  . LEU A 1080 ? 0.2886 0.2994 0.2645 0.0147  -0.0219 -0.0092 1078 LEU A CB  
7784  C CG  . LEU A 1080 ? 0.3329 0.3465 0.3123 0.0129  -0.0201 -0.0097 1078 LEU A CG  
7785  C CD1 . LEU A 1080 ? 0.2798 0.2914 0.2590 0.0098  -0.0181 -0.0086 1078 LEU A CD1 
7786  C CD2 . LEU A 1080 ? 0.2634 0.2837 0.2473 0.0126  -0.0209 -0.0121 1078 LEU A CD2 
7787  N N   . GLY A 1081 ? 0.2598 0.2611 0.2316 0.0153  -0.0191 -0.0047 1079 GLY A N   
7788  C CA  . GLY A 1081 ? 0.3055 0.3052 0.2778 0.0165  -0.0188 -0.0041 1079 GLY A CA  
7789  C C   . GLY A 1081 ? 0.2983 0.2922 0.2672 0.0173  -0.0189 -0.0016 1079 GLY A C   
7790  O O   . GLY A 1081 ? 0.2610 0.2529 0.2303 0.0180  -0.0186 -0.0011 1079 GLY A O   
7791  N N   . LEU A 1082 ? 0.2627 0.2541 0.2283 0.0173  -0.0192 -0.0001 1080 LEU A N   
7792  C CA  A LEU A 1082 ? 0.2659 0.2524 0.2283 0.0176  -0.0189 0.0027  1080 LEU A CA  
7793  C CA  B LEU A 1082 ? 0.2658 0.2523 0.2283 0.0176  -0.0189 0.0027  1080 LEU A CA  
7794  C C   . LEU A 1082 ? 0.2753 0.2597 0.2381 0.0158  -0.0168 0.0034  1080 LEU A C   
7795  O O   . LEU A 1082 ? 0.2840 0.2700 0.2477 0.0138  -0.0153 0.0026  1080 LEU A O   
7796  C CB  A LEU A 1082 ? 0.2659 0.2514 0.2249 0.0174  -0.0190 0.0039  1080 LEU A CB  
7797  C CB  B LEU A 1082 ? 0.2659 0.2513 0.2249 0.0174  -0.0190 0.0039  1080 LEU A CB  
7798  C CG  A LEU A 1082 ? 0.2729 0.2540 0.2283 0.0175  -0.0185 0.0069  1080 LEU A CG  
7799  C CG  B LEU A 1082 ? 0.2728 0.2538 0.2282 0.0174  -0.0184 0.0070  1080 LEU A CG  
7800  C CD1 A LEU A 1082 ? 0.2925 0.2714 0.2476 0.0196  -0.0202 0.0087  1080 LEU A CD1 
7801  C CD1 B LEU A 1082 ? 0.2707 0.2523 0.2229 0.0184  -0.0196 0.0080  1080 LEU A CD1 
7802  C CD2 A LEU A 1082 ? 0.2694 0.2511 0.2216 0.0173  -0.0186 0.0074  1080 LEU A CD2 
7803  C CD2 B LEU A 1082 ? 0.2653 0.2447 0.2202 0.0151  -0.0161 0.0075  1080 LEU A CD2 
7804  N N   . ASP A 1083 ? 0.2636 0.2445 0.2257 0.0166  -0.0169 0.0050  1081 ASP A N   
7805  C CA  . ASP A 1083 ? 0.2730 0.2521 0.2356 0.0151  -0.0151 0.0055  1081 ASP A CA  
7806  C C   . ASP A 1083 ? 0.3403 0.3145 0.3008 0.0156  -0.0152 0.0082  1081 ASP A C   
7807  O O   . ASP A 1083 ? 0.3501 0.3224 0.3116 0.0171  -0.0165 0.0086  1081 ASP A O   
7808  C CB  . ASP A 1083 ? 0.3284 0.3101 0.2944 0.0157  -0.0152 0.0033  1081 ASP A CB  
7809  C CG  . ASP A 1083 ? 0.3885 0.3698 0.3552 0.0140  -0.0133 0.0034  1081 ASP A CG  
7810  O OD1 . ASP A 1083 ? 0.4115 0.3904 0.3762 0.0124  -0.0119 0.0051  1081 ASP A OD1 
7811  O OD2 . ASP A 1083 ? 0.5046 0.4883 0.4737 0.0145  -0.0133 0.0016  1081 ASP A OD2 
7812  N N   . LEU A 1084 ? 0.2938 0.2661 0.2517 0.0142  -0.0139 0.0100  1082 LEU A N   
7813  C CA  . LEU A 1084 ? 0.2727 0.2410 0.2285 0.0144  -0.0140 0.0129  1082 LEU A CA  
7814  C C   . LEU A 1084 ? 0.2863 0.2526 0.2419 0.0126  -0.0121 0.0137  1082 LEU A C   
7815  O O   . LEU A 1084 ? 0.2798 0.2476 0.2356 0.0110  -0.0105 0.0128  1082 LEU A O   
7816  C CB  . LEU A 1084 ? 0.3176 0.2858 0.2700 0.0146  -0.0142 0.0145  1082 LEU A CB  
7817  C CG  . LEU A 1084 ? 0.3242 0.2941 0.2761 0.0165  -0.0163 0.0142  1082 LEU A CG  
7818  C CD1 . LEU A 1084 ? 0.3345 0.3046 0.2828 0.0166  -0.0163 0.0159  1082 LEU A CD1 
7819  C CD2 . LEU A 1084 ? 0.3598 0.3277 0.3132 0.0183  -0.0181 0.0152  1082 LEU A CD2 
7820  N N   . GLU A 1085 ? 0.3063 0.2692 0.2618 0.0129  -0.0123 0.0157  1083 GLU A N   
7821  C CA  . GLU A 1085 ? 0.3246 0.2855 0.2794 0.0112  -0.0106 0.0170  1083 GLU A CA  
7822  C C   . GLU A 1085 ? 0.3443 0.3035 0.2962 0.0110  -0.0103 0.0199  1083 GLU A C   
7823  O O   . GLU A 1085 ? 0.3746 0.3323 0.3256 0.0121  -0.0117 0.0218  1083 GLU A O   
7824  C CB  . GLU A 1085 ? 0.3582 0.3168 0.3152 0.0114  -0.0110 0.0170  1083 GLU A CB  
7825  C CG  . GLU A 1085 ? 0.4012 0.3578 0.3576 0.0097  -0.0094 0.0185  1083 GLU A CG  
7826  C CD  . GLU A 1085 ? 0.4228 0.3783 0.3818 0.0096  -0.0095 0.0176  1083 GLU A CD  
7827  O OE1 . GLU A 1085 ? 0.4972 0.4536 0.4584 0.0108  -0.0107 0.0155  1083 GLU A OE1 
7828  O OE2 . GLU A 1085 ? 0.4972 0.4512 0.4559 0.0083  -0.0084 0.0187  1083 GLU A OE2 
7829  N N   . LEU A 1086 ? 0.2964 0.2562 0.2467 0.0096  -0.0086 0.0202  1084 LEU A N   
7830  C CA  . LEU A 1086 ? 0.3064 0.2656 0.2538 0.0093  -0.0079 0.0224  1084 LEU A CA  
7831  C C   . LEU A 1086 ? 0.3723 0.3290 0.3198 0.0083  -0.0070 0.0246  1084 LEU A C   
7832  O O   . LEU A 1086 ? 0.3366 0.2926 0.2858 0.0072  -0.0060 0.0238  1084 LEU A O   
7833  C CB  . LEU A 1086 ? 0.2971 0.2587 0.2432 0.0085  -0.0068 0.0211  1084 LEU A CB  
7834  C CG  . LEU A 1086 ? 0.3201 0.2844 0.2666 0.0093  -0.0077 0.0186  1084 LEU A CG  
7835  C CD1 . LEU A 1086 ? 0.3089 0.2751 0.2543 0.0086  -0.0069 0.0172  1084 LEU A CD1 
7836  C CD2 . LEU A 1086 ? 0.3563 0.3212 0.3014 0.0110  -0.0095 0.0195  1084 LEU A CD2 
7837  N N   . PRO A 1087 ? 0.3481 0.3035 0.2939 0.0085  -0.0072 0.0276  1085 PRO A N   
7838  C CA  . PRO A 1087 ? 0.3394 0.2927 0.2855 0.0073  -0.0063 0.0299  1085 PRO A CA  
7839  C C   . PRO A 1087 ? 0.3908 0.3454 0.3361 0.0060  -0.0042 0.0294  1085 PRO A C   
7840  O O   . PRO A 1087 ? 0.3797 0.3366 0.3230 0.0061  -0.0035 0.0286  1085 PRO A O   
7841  C CB  . PRO A 1087 ? 0.4224 0.3752 0.3665 0.0078  -0.0070 0.0335  1085 PRO A CB  
7842  C CG  . PRO A 1087 ? 0.4547 0.4100 0.3966 0.0092  -0.0080 0.0328  1085 PRO A CG  
7843  C CD  . PRO A 1087 ? 0.3779 0.3340 0.3218 0.0099  -0.0087 0.0292  1085 PRO A CD  
7844  N N   . GLY A 1088 ? 0.3507 0.3037 0.2978 0.0048  -0.0034 0.0296  1086 GLY A N   
7845  C CA  . GLY A 1088 ? 0.3552 0.3090 0.3020 0.0036  -0.0016 0.0293  1086 GLY A CA  
7846  C C   . GLY A 1088 ? 0.3136 0.2654 0.2622 0.0025  -0.0012 0.0306  1086 GLY A C   
7847  O O   . GLY A 1088 ? 0.3086 0.2583 0.2582 0.0026  -0.0022 0.0324  1086 GLY A O   
7848  N N   . PRO A 1089 ? 0.3341 0.2864 0.2834 0.0015  0.0001  0.0297  1087 PRO A N   
7849  C CA  . PRO A 1089 ? 0.3163 0.2670 0.2674 0.0004  0.0005  0.0308  1087 PRO A CA  
7850  C C   . PRO A 1089 ? 0.3454 0.2946 0.2992 0.0006  -0.0007 0.0293  1087 PRO A C   
7851  O O   . PRO A 1089 ? 0.3464 0.2964 0.3006 0.0013  -0.0013 0.0272  1087 PRO A O   
7852  C CB  . PRO A 1089 ? 0.3268 0.2790 0.2778 -0.0004 0.0021  0.0299  1087 PRO A CB  
7853  C CG  . PRO A 1089 ? 0.3347 0.2884 0.2853 0.0001  0.0020  0.0275  1087 PRO A CG  
7854  C CD  . PRO A 1089 ? 0.3637 0.3179 0.3127 0.0013  0.0011  0.0277  1087 PRO A CD  
7855  N N   . VAL A 1090 ? 0.3162 0.2635 0.2717 -0.0002 -0.0009 0.0304  1088 VAL A N   
7856  C CA  . VAL A 1090 ? 0.3115 0.2580 0.2697 -0.0001 -0.0018 0.0285  1088 VAL A CA  
7857  C C   . VAL A 1090 ? 0.2924 0.2412 0.2506 -0.0004 -0.0008 0.0262  1088 VAL A C   
7858  O O   . VAL A 1090 ? 0.2690 0.2192 0.2259 -0.0011 0.0006  0.0266  1088 VAL A O   
7859  C CB  . VAL A 1090 ? 0.3546 0.2988 0.3150 -0.0010 -0.0023 0.0298  1088 VAL A CB  
7860  C CG1 . VAL A 1090 ? 0.3208 0.2625 0.2814 -0.0009 -0.0034 0.0326  1088 VAL A CG1 
7861  C CG2 . VAL A 1090 ? 0.3136 0.2588 0.2736 -0.0024 -0.0006 0.0307  1088 VAL A CG2 
7862  N N   . GLY A 1091 ? 0.2853 0.2347 0.2453 0.0000  -0.0016 0.0239  1089 GLY A N   
7863  C CA  . GLY A 1091 ? 0.3064 0.2583 0.2666 -0.0004 -0.0007 0.0222  1089 GLY A CA  
7864  C C   . GLY A 1091 ? 0.2946 0.2487 0.2534 -0.0003 -0.0001 0.0214  1089 GLY A C   
7865  O O   . GLY A 1091 ? 0.3139 0.2701 0.2727 -0.0010 0.0008  0.0207  1089 GLY A O   
7866  N N   . GLU A 1092 ? 0.2804 0.2343 0.2383 0.0007  -0.0008 0.0215  1090 GLU A N   
7867  C CA  . GLU A 1092 ? 0.3124 0.2685 0.2694 0.0008  -0.0005 0.0205  1090 GLU A CA  
7868  C C   . GLU A 1092 ? 0.2897 0.2458 0.2469 0.0023  -0.0019 0.0197  1090 GLU A C   
7869  O O   . GLU A 1092 ? 0.3204 0.2744 0.2774 0.0030  -0.0028 0.0209  1090 GLU A O   
7870  C CB  . GLU A 1092 ? 0.2801 0.2361 0.2352 0.0003  0.0005  0.0218  1090 GLU A CB  
7871  C CG  . GLU A 1092 ? 0.3230 0.2809 0.2777 0.0001  0.0010  0.0206  1090 GLU A CG  
7872  C CD  . GLU A 1092 ? 0.3319 0.2896 0.2852 -0.0003 0.0018  0.0215  1090 GLU A CD  
7873  O OE1 . GLU A 1092 ? 0.3286 0.2860 0.2803 0.0005  0.0015  0.0221  1090 GLU A OE1 
7874  O OE2 . GLU A 1092 ? 0.4206 0.3786 0.3743 -0.0012 0.0027  0.0215  1090 GLU A OE2 
7875  N N   . ARG A 1093 ? 0.2684 0.2271 0.2261 0.0026  -0.0021 0.0179  1091 ARG A N   
7876  C CA  . ARG A 1093 ? 0.2966 0.2560 0.2544 0.0040  -0.0034 0.0170  1091 ARG A CA  
7877  C C   . ARG A 1093 ? 0.2690 0.2301 0.2256 0.0037  -0.0030 0.0167  1091 ARG A C   
7878  O O   . ARG A 1093 ? 0.2614 0.2246 0.2186 0.0027  -0.0021 0.0158  1091 ARG A O   
7879  C CB  . ARG A 1093 ? 0.3753 0.3368 0.3353 0.0048  -0.0042 0.0147  1091 ARG A CB  
7880  C CG  . ARG A 1093 ? 0.5095 0.4690 0.4711 0.0057  -0.0054 0.0144  1091 ARG A CG  
7881  C CD  . ARG A 1093 ? 0.5922 0.5537 0.5558 0.0074  -0.0068 0.0119  1091 ARG A CD  
7882  N NE  . ARG A 1093 ? 0.6841 0.6501 0.6488 0.0069  -0.0060 0.0097  1091 ARG A NE  
7883  C CZ  . ARG A 1093 ? 0.6608 0.6283 0.6267 0.0067  -0.0057 0.0084  1091 ARG A CZ  
7884  N NH1 . ARG A 1093 ? 0.6891 0.6538 0.6558 0.0070  -0.0063 0.0085  1091 ARG A NH1 
7885  N NH2 . ARG A 1093 ? 0.5798 0.5520 0.5464 0.0062  -0.0048 0.0068  1091 ARG A NH2 
7886  N N   . ASN A 1094 ? 0.2843 0.2446 0.2393 0.0045  -0.0037 0.0175  1092 ASN A N   
7887  C CA  . ASN A 1094 ? 0.2752 0.2371 0.2291 0.0045  -0.0036 0.0170  1092 ASN A CA  
7888  C C   . ASN A 1094 ? 0.2595 0.2229 0.2138 0.0058  -0.0051 0.0158  1092 ASN A C   
7889  O O   . ASN A 1094 ? 0.3097 0.2718 0.2632 0.0071  -0.0062 0.0168  1092 ASN A O   
7890  C CB  . ASN A 1094 ? 0.2554 0.2159 0.2068 0.0044  -0.0030 0.0187  1092 ASN A CB  
7891  C CG  . ASN A 1094 ? 0.2856 0.2453 0.2370 0.0030  -0.0015 0.0195  1092 ASN A CG  
7892  O OD1 . ASN A 1094 ? 0.3114 0.2722 0.2635 0.0021  -0.0007 0.0186  1092 ASN A OD1 
7893  N ND2 . ASN A 1094 ? 0.2819 0.2397 0.2330 0.0029  -0.0012 0.0213  1092 ASN A ND2 
7894  N N   . LEU A 1095 ? 0.2679 0.2342 0.2236 0.0055  -0.0051 0.0139  1093 LEU A N   
7895  C CA  . LEU A 1095 ? 0.2741 0.2426 0.2308 0.0067  -0.0065 0.0123  1093 LEU A CA  
7896  C C   . LEU A 1095 ? 0.2857 0.2560 0.2419 0.0065  -0.0068 0.0115  1093 LEU A C   
7897  O O   . LEU A 1095 ? 0.2704 0.2412 0.2266 0.0051  -0.0058 0.0112  1093 LEU A O   
7898  C CB  . LEU A 1095 ? 0.2625 0.2337 0.2220 0.0065  -0.0064 0.0106  1093 LEU A CB  
7899  C CG  . LEU A 1095 ? 0.3631 0.3328 0.3234 0.0066  -0.0061 0.0109  1093 LEU A CG  
7900  C CD1 . LEU A 1095 ? 0.3805 0.3538 0.3432 0.0061  -0.0056 0.0091  1093 LEU A CD1 
7901  C CD2 . LEU A 1095 ? 0.3680 0.3355 0.3284 0.0085  -0.0077 0.0113  1093 LEU A CD2 
7902  N N   . TYR A 1096 ? 0.2566 0.2280 0.2124 0.0080  -0.0083 0.0109  1094 TYR A N   
7903  C CA  . TYR A 1096 ? 0.2800 0.2533 0.2351 0.0082  -0.0089 0.0098  1094 TYR A CA  
7904  C C   . TYR A 1096 ? 0.2807 0.2569 0.2378 0.0092  -0.0104 0.0080  1094 TYR A C   
7905  O O   . TYR A 1096 ? 0.2627 0.2385 0.2198 0.0109  -0.0116 0.0084  1094 TYR A O   
7906  C CB  . TYR A 1096 ? 0.2601 0.2319 0.2118 0.0092  -0.0094 0.0113  1094 TYR A CB  
7907  C CG  . TYR A 1096 ? 0.2652 0.2392 0.2159 0.0098  -0.0104 0.0100  1094 TYR A CG  
7908  C CD1 . TYR A 1096 ? 0.2612 0.2358 0.2114 0.0087  -0.0097 0.0090  1094 TYR A CD1 
7909  C CD2 . TYR A 1096 ? 0.2921 0.2677 0.2425 0.0115  -0.0122 0.0096  1094 TYR A CD2 
7910  C CE1 . TYR A 1096 ? 0.2824 0.2592 0.2319 0.0094  -0.0108 0.0074  1094 TYR A CE1 
7911  C CE2 . TYR A 1096 ? 0.2692 0.2473 0.2186 0.0121  -0.0133 0.0081  1094 TYR A CE2 
7912  C CZ  . TYR A 1096 ? 0.2647 0.2434 0.2137 0.0110  -0.0126 0.0069  1094 TYR A CZ  
7913  O OH  . TYR A 1096 ? 0.2665 0.2477 0.2146 0.0117  -0.0138 0.0051  1094 TYR A OH  
7914  N N   . THR A 1097 ? 0.2563 0.2356 0.2154 0.0082  -0.0103 0.0062  1095 THR A N   
7915  C CA  . THR A 1097 ? 0.2893 0.2722 0.2510 0.0089  -0.0114 0.0043  1095 THR A CA  
7916  C C   . THR A 1097 ? 0.2564 0.2420 0.2189 0.0084  -0.0121 0.0026  1095 THR A C   
7917  O O   . THR A 1097 ? 0.2580 0.2430 0.2203 0.0068  -0.0114 0.0026  1095 THR A O   
7918  C CB  . THR A 1097 ? 0.2882 0.2732 0.2528 0.0079  -0.0105 0.0035  1095 THR A CB  
7919  O OG1 . THR A 1097 ? 0.3476 0.3328 0.3129 0.0055  -0.0089 0.0038  1095 THR A OG1 
7920  C CG2 . THR A 1097 ? 0.3429 0.3257 0.3071 0.0087  -0.0101 0.0045  1095 THR A CG2 
7921  N N   . LEU A 1098 ? 0.2593 0.2479 0.2231 0.0097  -0.0137 0.0012  1096 LEU A N   
7922  C CA  . LEU A 1098 ? 0.2579 0.2494 0.2229 0.0093  -0.0147 -0.0007 1096 LEU A CA  
7923  C C   . LEU A 1098 ? 0.2561 0.2521 0.2253 0.0084  -0.0147 -0.0024 1096 LEU A C   
7924  O O   . LEU A 1098 ? 0.2560 0.2540 0.2266 0.0098  -0.0153 -0.0030 1096 LEU A O   
7925  C CB  . LEU A 1098 ? 0.2608 0.2529 0.2238 0.0116  -0.0167 -0.0010 1096 LEU A CB  
7926  C CG  . LEU A 1098 ? 0.2630 0.2519 0.2217 0.0125  -0.0168 0.0008  1096 LEU A CG  
7927  C CD1 . LEU A 1098 ? 0.2663 0.2566 0.2230 0.0148  -0.0190 0.0006  1096 LEU A CD1 
7928  C CD2 . LEU A 1098 ? 0.2627 0.2503 0.2202 0.0108  -0.0157 0.0006  1096 LEU A CD2 
7929  N N   . HIS A 1099 ? 0.2549 0.2525 0.2264 0.0060  -0.0140 -0.0032 1097 HIS A N   
7930  C CA  . HIS A 1099 ? 0.2533 0.2556 0.2290 0.0046  -0.0137 -0.0044 1097 HIS A CA  
7931  C C   . HIS A 1099 ? 0.2542 0.2594 0.2321 0.0038  -0.0151 -0.0063 1097 HIS A C   
7932  O O   . HIS A 1099 ? 0.2896 0.2929 0.2656 0.0043  -0.0161 -0.0068 1097 HIS A O   
7933  C CB  . HIS A 1099 ? 0.2806 0.2824 0.2576 0.0019  -0.0118 -0.0031 1097 HIS A CB  
7934  C CG  . HIS A 1099 ? 0.3229 0.3223 0.2981 0.0024  -0.0105 -0.0015 1097 HIS A CG  
7935  N ND1 . HIS A 1099 ? 0.3367 0.3390 0.3136 0.0024  -0.0097 -0.0016 1097 HIS A ND1 
7936  C CD2 . HIS A 1099 ? 0.3057 0.3003 0.2777 0.0029  -0.0099 0.0001  1097 HIS A CD2 
7937  C CE1 . HIS A 1099 ? 0.3374 0.3366 0.3123 0.0029  -0.0088 -0.0003 1097 HIS A CE1 
7938  N NE2 . HIS A 1099 ? 0.3239 0.3183 0.2958 0.0032  -0.0089 0.0009  1097 HIS A NE2 
7939  N N   . ALA A 1100 ? 0.2531 0.2632 0.2351 0.0026  -0.0151 -0.0074 1098 ALA A N   
7940  C CA  . ALA A 1100 ? 0.2851 0.2980 0.2700 0.0012  -0.0162 -0.0091 1098 ALA A CA  
7941  C C   . ALA A 1100 ? 0.3333 0.3431 0.3185 -0.0013 -0.0155 -0.0084 1098 ALA A C   
7942  O O   . ALA A 1100 ? 0.2886 0.2958 0.2732 -0.0026 -0.0138 -0.0065 1098 ALA A O   
7943  C CB  . ALA A 1100 ? 0.2635 0.2826 0.2532 -0.0001 -0.0160 -0.0101 1098 ALA A CB  
7944  N N   . ARG A 1101 ? 0.2828 0.2927 0.2690 -0.0018 -0.0170 -0.0101 1099 ARG A N   
7945  C CA  . ARG A 1101 ? 0.3003 0.3072 0.2875 -0.0040 -0.0167 -0.0099 1099 ARG A CA  
7946  C C   . ARG A 1101 ? 0.3032 0.3126 0.2956 -0.0073 -0.0161 -0.0094 1099 ARG A C   
7947  O O   . ARG A 1101 ? 0.3013 0.3080 0.2946 -0.0094 -0.0150 -0.0079 1099 ARG A O   
7948  C CB  . ARG A 1101 ? 0.2933 0.2995 0.2799 -0.0031 -0.0187 -0.0123 1099 ARG A CB  
7949  C CG  . ARG A 1101 ? 0.3276 0.3299 0.3090 -0.0010 -0.0188 -0.0121 1099 ARG A CG  
7950  C CD  . ARG A 1101 ? 0.3934 0.3960 0.3741 0.0000  -0.0209 -0.0147 1099 ARG A CD  
7951  N NE  . ARG A 1101 ? 0.4149 0.4143 0.3960 -0.0011 -0.0208 -0.0155 1099 ARG A NE  
7952  C CZ  . ARG A 1101 ? 0.4857 0.4818 0.4627 0.0002  -0.0204 -0.0151 1099 ARG A CZ  
7953  N NH1 . ARG A 1101 ? 0.4084 0.4037 0.3806 0.0025  -0.0198 -0.0135 1099 ARG A NH1 
7954  N NH2 . ARG A 1101 ? 0.4102 0.4040 0.3882 -0.0007 -0.0208 -0.0164 1099 ARG A NH2 
7955  N N   . GLY A 1102 ? 0.2550 0.2699 0.2512 -0.0080 -0.0167 -0.0105 1100 GLY A N   
7956  C CA  . GLY A 1102 ? 0.2596 0.2777 0.2611 -0.0114 -0.0162 -0.0099 1100 GLY A CA  
7957  C C   . GLY A 1102 ? 0.3312 0.3542 0.3369 -0.0120 -0.0180 -0.0123 1100 GLY A C   
7958  O O   . GLY A 1102 ? 0.2724 0.2993 0.2778 -0.0100 -0.0187 -0.0137 1100 GLY A O   
7959  N N   . ARG A 1103 ? 0.2570 0.2797 0.2667 -0.0147 -0.0189 -0.0129 1101 ARG A N   
7960  C CA  . ARG A 1103 ? 0.2781 0.3055 0.2923 -0.0156 -0.0208 -0.0153 1101 ARG A CA  
7961  C C   . ARG A 1103 ? 0.2608 0.2850 0.2738 -0.0144 -0.0231 -0.0181 1101 ARG A C   
7962  O O   . ARG A 1103 ? 0.2692 0.2887 0.2823 -0.0155 -0.0234 -0.0180 1101 ARG A O   
7963  C CB  . ARG A 1103 ? 0.3525 0.3828 0.3732 -0.0198 -0.0204 -0.0141 1101 ARG A CB  
7964  C CG  . ARG A 1103 ? 0.3254 0.3616 0.3513 -0.0209 -0.0222 -0.0165 1101 ARG A CG  
7965  C CD  . ARG A 1103 ? 0.3253 0.3654 0.3578 -0.0253 -0.0215 -0.0146 1101 ARG A CD  
7966  N NE  . ARG A 1103 ? 0.4191 0.4631 0.4516 -0.0261 -0.0190 -0.0117 1101 ARG A NE  
7967  C CZ  . ARG A 1103 ? 0.4380 0.4895 0.4722 -0.0257 -0.0183 -0.0121 1101 ARG A CZ  
7968  N NH1 . ARG A 1103 ? 0.3831 0.4391 0.4194 -0.0245 -0.0201 -0.0151 1101 ARG A NH1 
7969  N NH2 . ARG A 1103 ? 0.4682 0.5231 0.5021 -0.0263 -0.0159 -0.0096 1101 ARG A NH2 
7970  N N   . ILE A 1104 ? 0.2711 0.2983 0.2830 -0.0119 -0.0248 -0.0207 1102 ILE A N   
7971  C CA  . ILE A 1104 ? 0.2952 0.3206 0.3055 -0.0102 -0.0271 -0.0236 1102 ILE A CA  
7972  C C   . ILE A 1104 ? 0.2660 0.2949 0.2823 -0.0124 -0.0292 -0.0262 1102 ILE A C   
7973  O O   . ILE A 1104 ? 0.2651 0.2998 0.2852 -0.0132 -0.0295 -0.0266 1102 ILE A O   
7974  C CB  . ILE A 1104 ? 0.2647 0.2912 0.2699 -0.0061 -0.0280 -0.0246 1102 ILE A CB  
7975  C CG1 . ILE A 1104 ? 0.2630 0.2865 0.2630 -0.0042 -0.0260 -0.0219 1102 ILE A CG1 
7976  C CG2 . ILE A 1104 ? 0.2724 0.2972 0.2751 -0.0044 -0.0302 -0.0274 1102 ILE A CG2 
7977  C CD1 . ILE A 1104 ? 0.2634 0.2807 0.2600 -0.0043 -0.0249 -0.0205 1102 ILE A CD1 
7978  N N   . LEU A 1105 ? 0.2685 0.2942 0.2862 -0.0134 -0.0307 -0.0280 1103 LEU A N   
7979  C CA  . LEU A 1105 ? 0.2708 0.2992 0.2941 -0.0152 -0.0331 -0.0310 1103 LEU A CA  
7980  C C   . LEU A 1105 ? 0.2722 0.3040 0.2932 -0.0120 -0.0354 -0.0343 1103 LEU A C   
7981  O O   . LEU A 1105 ? 0.2736 0.3028 0.2891 -0.0090 -0.0360 -0.0355 1103 LEU A O   
7982  C CB  . LEU A 1105 ? 0.2734 0.2968 0.2989 -0.0170 -0.0342 -0.0322 1103 LEU A CB  
7983  C CG  . LEU A 1105 ? 0.2765 0.3016 0.3078 -0.0186 -0.0372 -0.0359 1103 LEU A CG  
7984  C CD1 . LEU A 1105 ? 0.2758 0.3054 0.3146 -0.0225 -0.0371 -0.0348 1103 LEU A CD1 
7985  C CD2 . LEU A 1105 ? 0.2793 0.2985 0.3116 -0.0195 -0.0382 -0.0373 1103 LEU A CD2 
7986  N N   . LEU A 1106 ? 0.2720 0.3099 0.2971 -0.0126 -0.0365 -0.0356 1104 LEU A N   
7987  C CA  . LEU A 1106 ? 0.2736 0.3154 0.2972 -0.0098 -0.0389 -0.0388 1104 LEU A CA  
7988  C C   . LEU A 1106 ? 0.2765 0.3200 0.3056 -0.0116 -0.0417 -0.0425 1104 LEU A C   
7989  O O   . LEU A 1106 ? 0.2940 0.3396 0.3299 -0.0152 -0.0418 -0.0424 1104 LEU A O   
7990  C CB  . LEU A 1106 ? 0.2716 0.3195 0.2960 -0.0086 -0.0386 -0.0382 1104 LEU A CB  
7991  C CG  . LEU A 1106 ? 0.2720 0.3188 0.2917 -0.0065 -0.0362 -0.0350 1104 LEU A CG  
7992  C CD1 . LEU A 1106 ? 0.2683 0.3211 0.2883 -0.0042 -0.0370 -0.0357 1104 LEU A CD1 
7993  C CD2 . LEU A 1106 ? 0.2699 0.3109 0.2824 -0.0038 -0.0358 -0.0342 1104 LEU A CD2 
7994  N N   . VAL A 1107 ? 0.2885 0.3312 0.3144 -0.0091 -0.0440 -0.0458 1105 VAL A N   
7995  C CA  . VAL A 1107 ? 0.2826 0.3273 0.3136 -0.0105 -0.0470 -0.0500 1105 VAL A CA  
7996  C C   . VAL A 1107 ? 0.2842 0.3340 0.3128 -0.0072 -0.0494 -0.0530 1105 VAL A C   
7997  O O   . VAL A 1107 ? 0.2947 0.3434 0.3186 -0.0044 -0.0510 -0.0554 1105 VAL A O   
7998  C CB  . VAL A 1107 ? 0.2855 0.3243 0.3159 -0.0109 -0.0479 -0.0519 1105 VAL A CB  
7999  C CG1 . VAL A 1107 ? 0.2889 0.3295 0.3257 -0.0128 -0.0511 -0.0563 1105 VAL A CG1 
8000  C CG2 . VAL A 1107 ? 0.2838 0.3173 0.3156 -0.0137 -0.0453 -0.0482 1105 VAL A CG2 
8001  N N   . PRO A 1108 ? 0.2853 0.3411 0.3168 -0.0073 -0.0497 -0.0528 1106 PRO A N   
8002  C CA  . PRO A 1108 ? 0.2843 0.3451 0.3135 -0.0039 -0.0521 -0.0554 1106 PRO A CA  
8003  C C   . PRO A 1108 ? 0.3134 0.3777 0.3476 -0.0049 -0.0555 -0.0601 1106 PRO A C   
8004  O O   . PRO A 1108 ? 0.3086 0.3723 0.3494 -0.0087 -0.0561 -0.0613 1106 PRO A O   
8005  C CB  . PRO A 1108 ? 0.3022 0.3681 0.3337 -0.0039 -0.0509 -0.0533 1106 PRO A CB  
8006  C CG  . PRO A 1108 ? 0.2794 0.3458 0.3182 -0.0086 -0.0494 -0.0519 1106 PRO A CG  
8007  C CD  . PRO A 1108 ? 0.2934 0.3521 0.3304 -0.0103 -0.0479 -0.0502 1106 PRO A CD  
8008  N N   . ALA A 1109 ? 0.2898 0.3577 0.3207 -0.0015 -0.0579 -0.0628 1107 ALA A N   
8009  C CA  . ALA A 1109 ? 0.2960 0.3687 0.3313 -0.0018 -0.0615 -0.0676 1107 ALA A CA  
8010  C C   . ALA A 1109 ? 0.3095 0.3897 0.3471 -0.0006 -0.0629 -0.0684 1107 ALA A C   
8011  O O   . ALA A 1109 ? 0.3365 0.4213 0.3809 -0.0026 -0.0651 -0.0714 1107 ALA A O   
8012  C CB  . ALA A 1109 ? 0.2969 0.3683 0.3266 0.0013  -0.0637 -0.0710 1107 ALA A CB  
8013  N N   . THR A 1110 ? 0.2907 0.3723 0.3232 0.0027  -0.0619 -0.0659 1108 THR A N   
8014  C CA  . THR A 1110 ? 0.2904 0.3790 0.3245 0.0045  -0.0634 -0.0666 1108 THR A CA  
8015  C C   . THR A 1110 ? 0.3017 0.3907 0.3359 0.0046  -0.0605 -0.0625 1108 THR A C   
8016  O O   . THR A 1110 ? 0.2845 0.3681 0.3155 0.0041  -0.0576 -0.0591 1108 THR A O   
8017  C CB  . THR A 1110 ? 0.3055 0.3958 0.3328 0.0093  -0.0657 -0.0679 1108 THR A CB  
8018  O OG1 . THR A 1110 ? 0.2934 0.3789 0.3132 0.0119  -0.0635 -0.0641 1108 THR A OG1 
8019  C CG2 . THR A 1110 ? 0.3165 0.4069 0.3429 0.0098  -0.0686 -0.0722 1108 THR A CG2 
8020  N N   . GLU A 1111 ? 0.3084 0.4041 0.3462 0.0053  -0.0614 -0.0631 1109 GLU A N   
8021  C CA  . GLU A 1111 ? 0.3212 0.4183 0.3596 0.0057  -0.0589 -0.0599 1109 GLU A CA  
8022  C C   . GLU A 1111 ? 0.2893 0.3819 0.3195 0.0096  -0.0578 -0.0570 1109 GLU A C   
8023  O O   . GLU A 1111 ? 0.2943 0.3833 0.3228 0.0091  -0.0549 -0.0537 1109 GLU A O   
8024  C CB  . GLU A 1111 ? 0.3751 0.4808 0.4190 0.0062  -0.0605 -0.0616 1109 GLU A CB  
8025  C CG  . GLU A 1111 ? 0.3509 0.4587 0.3942 0.0081  -0.0586 -0.0590 1109 GLU A CG  
8026  C CD  . GLU A 1111 ? 0.3976 0.5146 0.4472 0.0084  -0.0600 -0.0611 1109 GLU A CD  
8027  O OE1 . GLU A 1111 ? 0.3952 0.5165 0.4521 0.0045  -0.0592 -0.0616 1109 GLU A OE1 
8028  O OE2 . GLU A 1111 ? 0.3624 0.4825 0.4100 0.0124  -0.0621 -0.0620 1109 GLU A OE2 
8029  N N   . SER A 1112 ? 0.3112 0.4045 0.3364 0.0135  -0.0602 -0.0581 1110 SER A N   
8030  C CA  . SER A 1112 ? 0.3420 0.4310 0.3596 0.0171  -0.0594 -0.0551 1110 SER A CA  
8031  C C   . SER A 1112 ? 0.3121 0.3934 0.3252 0.0159  -0.0571 -0.0529 1110 SER A C   
8032  O O   . SER A 1112 ? 0.2960 0.3731 0.3054 0.0169  -0.0549 -0.0494 1110 SER A O   
8033  C CB  . SER A 1112 ? 0.3482 0.4393 0.3612 0.0210  -0.0627 -0.0565 1110 SER A CB  
8034  O OG  . SER A 1112 ? 0.3821 0.4692 0.3882 0.0243  -0.0620 -0.0532 1110 SER A OG  
8035  N N   . GLY A 1113 ? 0.2899 0.3692 0.3036 0.0138  -0.0576 -0.0549 1111 GLY A N   
8036  C CA  . GLY A 1113 ? 0.2860 0.3584 0.2962 0.0126  -0.0554 -0.0531 1111 GLY A CA  
8037  C C   . GLY A 1113 ? 0.2822 0.3517 0.2952 0.0097  -0.0521 -0.0502 1111 GLY A C   
8038  O O   . GLY A 1113 ? 0.2809 0.3452 0.2897 0.0101  -0.0498 -0.0471 1111 GLY A O   
8039  N N   . LEU A 1114 ? 0.2803 0.3538 0.3007 0.0066  -0.0519 -0.0510 1112 LEU A N   
8040  C CA  . LEU A 1114 ? 0.2768 0.3489 0.3001 0.0039  -0.0488 -0.0482 1112 LEU A CA  
8041  C C   . LEU A 1114 ? 0.2748 0.3469 0.2948 0.0065  -0.0472 -0.0454 1112 LEU A C   
8042  O O   . LEU A 1114 ? 0.2728 0.3405 0.2906 0.0059  -0.0445 -0.0424 1112 LEU A O   
8043  C CB  . LEU A 1114 ? 0.3017 0.3794 0.3336 0.0003  -0.0490 -0.0495 1112 LEU A CB  
8044  C CG  . LEU A 1114 ? 0.2835 0.3621 0.3188 -0.0024 -0.0459 -0.0466 1112 LEU A CG  
8045  C CD1 . LEU A 1114 ? 0.2860 0.3576 0.3191 -0.0045 -0.0434 -0.0438 1112 LEU A CD1 
8046  C CD2 . LEU A 1114 ? 0.3026 0.3876 0.3466 -0.0060 -0.0464 -0.0480 1112 LEU A CD2 
8047  N N   . TYR A 1115 ? 0.2756 0.3524 0.2955 0.0094  -0.0489 -0.0464 1113 TYR A N   
8048  C CA  . TYR A 1115 ? 0.2742 0.3509 0.2916 0.0121  -0.0478 -0.0440 1113 TYR A CA  
8049  C C   . TYR A 1115 ? 0.2750 0.3448 0.2849 0.0144  -0.0469 -0.0414 1113 TYR A C   
8050  O O   . TYR A 1115 ? 0.2731 0.3399 0.2812 0.0148  -0.0447 -0.0387 1113 TYR A O   
8051  C CB  . TYR A 1115 ? 0.2755 0.3583 0.2942 0.0153  -0.0504 -0.0458 1113 TYR A CB  
8052  C CG  . TYR A 1115 ? 0.2742 0.3649 0.3007 0.0134  -0.0510 -0.0480 1113 TYR A CG  
8053  C CD1 . TYR A 1115 ? 0.2811 0.3732 0.3128 0.0092  -0.0488 -0.0477 1113 TYR A CD1 
8054  C CD2 . TYR A 1115 ? 0.2916 0.3886 0.3202 0.0159  -0.0537 -0.0504 1113 TYR A CD2 
8055  C CE1 . TYR A 1115 ? 0.2707 0.3706 0.3098 0.0072  -0.0493 -0.0495 1113 TYR A CE1 
8056  C CE2 . TYR A 1115 ? 0.2746 0.3793 0.3105 0.0142  -0.0543 -0.0525 1113 TYR A CE2 
8057  C CZ  . TYR A 1115 ? 0.2905 0.3967 0.3317 0.0098  -0.0520 -0.0520 1113 TYR A CZ  
8058  O OH  . TYR A 1115 ? 0.3442 0.4587 0.3929 0.0078  -0.0524 -0.0539 1113 TYR A OH  
8059  N N   . HIS A 1116 ? 0.2781 0.3455 0.2835 0.0159  -0.0486 -0.0422 1114 HIS A N   
8060  C CA  . HIS A 1116 ? 0.2792 0.3405 0.2775 0.0178  -0.0477 -0.0396 1114 HIS A CA  
8061  C C   . HIS A 1116 ? 0.2771 0.3329 0.2749 0.0149  -0.0448 -0.0378 1114 HIS A C   
8062  O O   . HIS A 1116 ? 0.2760 0.3274 0.2702 0.0157  -0.0429 -0.0348 1114 HIS A O   
8063  C CB  . HIS A 1116 ? 0.2831 0.3444 0.2771 0.0198  -0.0500 -0.0411 1114 HIS A CB  
8064  C CG  . HIS A 1116 ? 0.2858 0.3504 0.2774 0.0237  -0.0526 -0.0412 1114 HIS A CG  
8065  N ND1 . HIS A 1116 ? 0.3747 0.4458 0.3699 0.0244  -0.0553 -0.0442 1114 HIS A ND1 
8066  C CD2 . HIS A 1116 ? 0.3005 0.3630 0.2867 0.0270  -0.0529 -0.0385 1114 HIS A CD2 
8067  C CE1 . HIS A 1116 ? 0.2897 0.3624 0.2816 0.0282  -0.0573 -0.0434 1114 HIS A CE1 
8068  N NE2 . HIS A 1116 ? 0.3397 0.4071 0.3261 0.0297  -0.0559 -0.0397 1114 HIS A NE2 
8069  N N   . GLN A 1117 ? 0.2767 0.3326 0.2783 0.0116  -0.0445 -0.0396 1115 GLN A N   
8070  C CA  . GLN A 1117 ? 0.2749 0.3257 0.2765 0.0088  -0.0420 -0.0378 1115 GLN A CA  
8071  C C   . GLN A 1117 ? 0.2714 0.3222 0.2752 0.0075  -0.0394 -0.0352 1115 GLN A C   
8072  O O   . GLN A 1117 ? 0.2700 0.3160 0.2709 0.0073  -0.0372 -0.0325 1115 GLN A O   
8073  C CB  . GLN A 1117 ? 0.2755 0.3266 0.2818 0.0055  -0.0426 -0.0402 1115 GLN A CB  
8074  C CG  . GLN A 1117 ? 0.2791 0.3295 0.2832 0.0065  -0.0449 -0.0431 1115 GLN A CG  
8075  C CD  . GLN A 1117 ? 0.2940 0.3446 0.3039 0.0030  -0.0458 -0.0457 1115 GLN A CD  
8076  O OE1 . GLN A 1117 ? 0.2924 0.3448 0.3084 -0.0001 -0.0450 -0.0453 1115 GLN A OE1 
8077  N NE2 . GLN A 1117 ? 0.2843 0.3333 0.2925 0.0036  -0.0475 -0.0484 1115 GLN A NE2 
8078  N N   . LEU A 1118 ? 0.2700 0.3265 0.2791 0.0067  -0.0397 -0.0361 1116 LEU A N   
8079  C CA  A LEU A 1118 ? 0.2669 0.3245 0.2782 0.0056  -0.0373 -0.0340 1116 LEU A CA  
8080  C CA  B LEU A 1118 ? 0.2669 0.3246 0.2783 0.0057  -0.0373 -0.0340 1116 LEU A CA  
8081  C C   . LEU A 1118 ? 0.2666 0.3217 0.2730 0.0090  -0.0366 -0.0319 1116 LEU A C   
8082  O O   . LEU A 1118 ? 0.2647 0.3167 0.2697 0.0084  -0.0342 -0.0296 1116 LEU A O   
8083  C CB  A LEU A 1118 ? 0.2659 0.3312 0.2838 0.0044  -0.0379 -0.0357 1116 LEU A CB  
8084  C CB  B LEU A 1118 ? 0.2660 0.3315 0.2837 0.0047  -0.0380 -0.0358 1116 LEU A CB  
8085  C CG  A LEU A 1118 ? 0.2629 0.3315 0.2843 0.0028  -0.0355 -0.0342 1116 LEU A CG  
8086  C CG  B LEU A 1118 ? 0.2655 0.3342 0.2897 0.0004  -0.0379 -0.0369 1116 LEU A CG  
8087  C CD1 A LEU A 1118 ? 0.2613 0.3256 0.2826 -0.0004 -0.0328 -0.0316 1116 LEU A CD1 
8088  C CD1 B LEU A 1118 ? 0.2652 0.3423 0.2952 0.0002  -0.0392 -0.0390 1116 LEU A CD1 
8089  C CD2 A LEU A 1118 ? 0.2625 0.3392 0.2910 0.0009  -0.0363 -0.0362 1116 LEU A CD2 
8090  C CD2 B LEU A 1118 ? 0.2632 0.3297 0.2888 -0.0028 -0.0349 -0.0341 1116 LEU A CD2 
8091  N N   . ALA A 1119 ? 0.2688 0.3251 0.2726 0.0125  -0.0388 -0.0328 1117 ALA A N   
8092  C CA  . ALA A 1119 ? 0.2991 0.3525 0.2984 0.0157  -0.0385 -0.0306 1117 ALA A CA  
8093  C C   . ALA A 1119 ? 0.2692 0.3154 0.2633 0.0155  -0.0368 -0.0281 1117 ALA A C   
8094  O O   . ALA A 1119 ? 0.2792 0.3223 0.2716 0.0159  -0.0351 -0.0258 1117 ALA A O   
8095  C CB  . ALA A 1119 ? 0.2723 0.3276 0.2694 0.0195  -0.0414 -0.0316 1117 ALA A CB  
8096  N N   . ALA A 1120 ? 0.2710 0.3146 0.2626 0.0148  -0.0374 -0.0286 1118 ALA A N   
8097  C CA  . ALA A 1120 ? 0.2712 0.3085 0.2580 0.0147  -0.0358 -0.0263 1118 ALA A CA  
8098  C C   . ALA A 1120 ? 0.2681 0.3029 0.2568 0.0118  -0.0330 -0.0248 1118 ALA A C   
8099  O O   . ALA A 1120 ? 0.2703 0.3010 0.2560 0.0123  -0.0313 -0.0222 1118 ALA A O   
8100  C CB  . ALA A 1120 ? 0.2737 0.3096 0.2582 0.0144  -0.0369 -0.0278 1118 ALA A CB  
8101  N N   . ALA A 1121 ? 0.2666 0.3042 0.2606 0.0088  -0.0326 -0.0261 1119 ALA A N   
8102  C CA  . ALA A 1121 ? 0.2641 0.2996 0.2599 0.0058  -0.0300 -0.0244 1119 ALA A CA  
8103  C C   . ALA A 1121 ? 0.2617 0.2988 0.2585 0.0063  -0.0284 -0.0228 1119 ALA A C   
8104  O O   . ALA A 1121 ? 0.2602 0.2938 0.2554 0.0056  -0.0263 -0.0206 1119 ALA A O   
8105  C CB  . ALA A 1121 ? 0.2637 0.3018 0.2651 0.0023  -0.0301 -0.0259 1119 ALA A CB  
8106  N N   . LEU A 1122 ? 0.2616 0.3042 0.2612 0.0076  -0.0295 -0.0242 1120 LEU A N   
8107  C CA  . LEU A 1122 ? 0.2596 0.3046 0.2606 0.0083  -0.0282 -0.0234 1120 LEU A CA  
8108  C C   . LEU A 1122 ? 0.2757 0.3163 0.2719 0.0113  -0.0280 -0.0217 1120 LEU A C   
8109  O O   . LEU A 1122 ? 0.2823 0.3215 0.2781 0.0112  -0.0262 -0.0202 1120 LEU A O   
8110  C CB  . LEU A 1122 ? 0.2898 0.3422 0.2953 0.0092  -0.0296 -0.0256 1120 LEU A CB  
8111  C CG  . LEU A 1122 ? 0.2587 0.3170 0.2702 0.0060  -0.0296 -0.0272 1120 LEU A CG  
8112  C CD1 . LEU A 1122 ? 0.2633 0.3291 0.2788 0.0075  -0.0311 -0.0295 1120 LEU A CD1 
8113  C CD2 . LEU A 1122 ? 0.2590 0.3178 0.2728 0.0027  -0.0268 -0.0254 1120 LEU A CD2 
8114  N N   . ALA A 1123 ? 0.2629 0.3011 0.2554 0.0140  -0.0300 -0.0218 1121 ALA A N   
8115  C CA  . ALA A 1123 ? 0.2640 0.2978 0.2522 0.0168  -0.0301 -0.0198 1121 ALA A CA  
8116  C C   . ALA A 1123 ? 0.3119 0.3397 0.2967 0.0154  -0.0279 -0.0173 1121 ALA A C   
8117  O O   . ALA A 1123 ? 0.2634 0.2878 0.2457 0.0170  -0.0274 -0.0155 1121 ALA A O   
8118  C CB  . ALA A 1123 ? 0.2831 0.3160 0.2678 0.0195  -0.0326 -0.0199 1121 ALA A CB  
8119  N N   . THR A 1124 ? 0.2623 0.2888 0.2474 0.0126  -0.0268 -0.0173 1122 THR A N   
8120  C CA  . THR A 1124 ? 0.2614 0.2827 0.2439 0.0112  -0.0248 -0.0152 1122 THR A CA  
8121  C C   . THR A 1124 ? 0.2618 0.2841 0.2475 0.0085  -0.0226 -0.0146 1122 THR A C   
8122  O O   . THR A 1124 ? 0.2697 0.2883 0.2541 0.0068  -0.0210 -0.0131 1122 THR A O   
8123  C CB  . THR A 1124 ? 0.2631 0.2816 0.2431 0.0104  -0.0253 -0.0154 1122 THR A CB  
8124  O OG1 . THR A 1124 ? 0.2634 0.2856 0.2471 0.0089  -0.0264 -0.0179 1122 THR A OG1 
8125  C CG2 . THR A 1124 ? 0.2742 0.2910 0.2496 0.0134  -0.0269 -0.0150 1122 THR A CG2 
8126  N N   . GLY A 1125 ? 0.2572 0.2848 0.2469 0.0081  -0.0226 -0.0157 1123 GLY A N   
8127  C CA  . GLY A 1125 ? 0.2547 0.2843 0.2472 0.0059  -0.0204 -0.0150 1123 GLY A CA  
8128  C C   . GLY A 1125 ? 0.2550 0.2868 0.2512 0.0022  -0.0197 -0.0151 1123 GLY A C   
8129  O O   . GLY A 1125 ? 0.2520 0.2856 0.2504 0.0001  -0.0178 -0.0140 1123 GLY A O   
8130  N N   . ASN A 1126 ? 0.2553 0.2870 0.2524 0.0014  -0.0211 -0.0164 1124 ASN A N   
8131  C CA  . ASN A 1126 ? 0.2552 0.2874 0.2557 -0.0021 -0.0207 -0.0165 1124 ASN A CA  
8132  C C   . ASN A 1126 ? 0.2658 0.3052 0.2721 -0.0038 -0.0212 -0.0178 1124 ASN A C   
8133  O O   . ASN A 1126 ? 0.2651 0.3091 0.2727 -0.0019 -0.0223 -0.0195 1124 ASN A O   
8134  C CB  . ASN A 1126 ? 0.2575 0.2863 0.2564 -0.0020 -0.0224 -0.0177 1124 ASN A CB  
8135  C CG  . ASN A 1126 ? 0.2688 0.2911 0.2622 -0.0006 -0.0218 -0.0163 1124 ASN A CG  
8136  O OD1 . ASN A 1126 ? 0.2635 0.2824 0.2563 -0.0022 -0.0201 -0.0144 1124 ASN A OD1 
8137  N ND2 . ASN A 1126 ? 0.2600 0.2811 0.2496 0.0024  -0.0232 -0.0170 1124 ASN A ND2 
8138  N N   . SER A 1127 ? 0.2759 0.3163 0.2860 -0.0075 -0.0202 -0.0170 1125 SER A N   
8139  C CA  . SER A 1127 ? 0.2806 0.3270 0.2967 -0.0099 -0.0209 -0.0182 1125 SER A CA  
8140  C C   . SER A 1127 ? 0.2567 0.3007 0.2739 -0.0109 -0.0230 -0.0200 1125 SER A C   
8141  O O   . SER A 1127 ? 0.2712 0.3093 0.2846 -0.0097 -0.0236 -0.0201 1125 SER A O   
8142  C CB  . SER A 1127 ? 0.3436 0.3925 0.3635 -0.0137 -0.0188 -0.0158 1125 SER A CB  
8143  O OG  . SER A 1127 ? 0.3224 0.3652 0.3413 -0.0157 -0.0182 -0.0140 1125 SER A OG  
8144  N N   . VAL A 1128 ? 0.2685 0.3175 0.2913 -0.0128 -0.0243 -0.0216 1126 VAL A N   
8145  C CA  . VAL A 1128 ? 0.2695 0.3168 0.2939 -0.0136 -0.0266 -0.0239 1126 VAL A CA  
8146  C C   . VAL A 1128 ? 0.2933 0.3433 0.3247 -0.0180 -0.0268 -0.0237 1126 VAL A C   
8147  O O   . VAL A 1128 ? 0.2939 0.3494 0.3294 -0.0201 -0.0256 -0.0223 1126 VAL A O   
8148  C CB  . VAL A 1128 ? 0.2613 0.3120 0.2851 -0.0106 -0.0291 -0.0271 1126 VAL A CB  
8149  C CG1 . VAL A 1128 ? 0.2612 0.3093 0.2783 -0.0063 -0.0292 -0.0269 1126 VAL A CG1 
8150  C CG2 . VAL A 1128 ? 0.2603 0.3195 0.2896 -0.0115 -0.0294 -0.0281 1126 VAL A CG2 
8151  N N   . ALA A 1129 ? 0.2856 0.3319 0.3185 -0.0194 -0.0285 -0.0251 1127 ALA A N   
8152  C CA  . ALA A 1129 ? 0.3017 0.3503 0.3418 -0.0232 -0.0297 -0.0259 1127 ALA A CA  
8153  C C   . ALA A 1129 ? 0.2671 0.3165 0.3079 -0.0217 -0.0329 -0.0301 1127 ALA A C   
8154  O O   . ALA A 1129 ? 0.2688 0.3133 0.3053 -0.0195 -0.0341 -0.0318 1127 ALA A O   
8155  C CB  . ALA A 1129 ? 0.2743 0.3172 0.3163 -0.0264 -0.0292 -0.0238 1127 ALA A CB  
8156  N N   . ILE A 1130 ? 0.2674 0.3236 0.3133 -0.0226 -0.0343 -0.0319 1128 ILE A N   
8157  C CA  . ILE A 1130 ? 0.2698 0.3279 0.3164 -0.0210 -0.0374 -0.0361 1128 ILE A CA  
8158  C C   . ILE A 1130 ? 0.3431 0.4008 0.3966 -0.0247 -0.0393 -0.0378 1128 ILE A C   
8159  O O   . ILE A 1130 ? 0.3149 0.3758 0.3749 -0.0287 -0.0387 -0.0361 1128 ILE A O   
8160  C CB  . ILE A 1130 ? 0.2686 0.3348 0.3167 -0.0193 -0.0380 -0.0375 1128 ILE A CB  
8161  C CG1 . ILE A 1130 ? 0.2724 0.3389 0.3145 -0.0157 -0.0362 -0.0358 1128 ILE A CG1 
8162  C CG2 . ILE A 1130 ? 0.2713 0.3392 0.3193 -0.0172 -0.0414 -0.0418 1128 ILE A CG2 
8163  C CD1 . ILE A 1130 ? 0.2779 0.3525 0.3224 -0.0142 -0.0367 -0.0370 1128 ILE A CD1 
8164  N N   . ASP A 1131 ? 0.2755 0.3296 0.3277 -0.0235 -0.0418 -0.0411 1129 ASP A N   
8165  C CA  . ASP A 1131 ? 0.3221 0.3754 0.3809 -0.0267 -0.0442 -0.0434 1129 ASP A CA  
8166  C C   . ASP A 1131 ? 0.3279 0.3890 0.3940 -0.0289 -0.0456 -0.0448 1129 ASP A C   
8167  O O   . ASP A 1131 ? 0.3113 0.3773 0.3765 -0.0264 -0.0472 -0.0477 1129 ASP A O   
8168  C CB  . ASP A 1131 ? 0.3230 0.3726 0.3786 -0.0240 -0.0469 -0.0477 1129 ASP A CB  
8169  C CG  . ASP A 1131 ? 0.3679 0.4165 0.4306 -0.0270 -0.0498 -0.0508 1129 ASP A CG  
8170  O OD1 . ASP A 1131 ? 0.3419 0.3892 0.4109 -0.0313 -0.0492 -0.0486 1129 ASP A OD1 
8171  O OD2 . ASP A 1131 ? 0.3846 0.4339 0.4466 -0.0250 -0.0527 -0.0554 1129 ASP A OD2 
8172  N N   . ALA A 1132 ? 0.3396 0.4020 0.4129 -0.0337 -0.0449 -0.0426 1130 ALA A N   
8173  C CA  . ALA A 1132 ? 0.3826 0.4528 0.4636 -0.0363 -0.0461 -0.0436 1130 ALA A CA  
8174  C C   . ALA A 1132 ? 0.3605 0.4313 0.4456 -0.0366 -0.0500 -0.0487 1130 ALA A C   
8175  O O   . ALA A 1132 ? 0.4579 0.5357 0.5479 -0.0374 -0.0516 -0.0507 1130 ALA A O   
8176  C CB  . ALA A 1132 ? 0.3569 0.4285 0.4448 -0.0417 -0.0443 -0.0396 1130 ALA A CB  
8177  N N   . ALA A 1133 ? 0.4009 0.4646 0.4840 -0.0358 -0.0518 -0.0510 1131 ALA A N   
8178  C CA  . ALA A 1133 ? 0.4123 0.4765 0.4991 -0.0357 -0.0558 -0.0563 1131 ALA A CA  
8179  C C   . ALA A 1133 ? 0.3988 0.4670 0.4804 -0.0310 -0.0575 -0.0601 1131 ALA A C   
8180  O O   . ALA A 1133 ? 0.4329 0.5033 0.5175 -0.0306 -0.0609 -0.0648 1131 ALA A O   
8181  C CB  . ALA A 1133 ? 0.3718 0.4277 0.4583 -0.0361 -0.0572 -0.0579 1131 ALA A CB  
8182  N N   . SER A 1134 ? 0.3818 0.4512 0.4560 -0.0273 -0.0554 -0.0582 1132 SER A N   
8183  C CA  . SER A 1134 ? 0.3633 0.4370 0.4329 -0.0228 -0.0570 -0.0611 1132 SER A CA  
8184  C C   . SER A 1134 ? 0.3832 0.4658 0.4587 -0.0238 -0.0584 -0.0626 1132 SER A C   
8185  O O   . SER A 1134 ? 0.3374 0.4239 0.4108 -0.0206 -0.0607 -0.0660 1132 SER A O   
8186  C CB  . SER A 1134 ? 0.4124 0.4849 0.4735 -0.0190 -0.0544 -0.0581 1132 SER A CB  
8187  O OG  . SER A 1134 ? 0.3757 0.4516 0.4389 -0.0206 -0.0517 -0.0543 1132 SER A OG  
8188  N N   . GLY A 1135 ? 0.3358 0.4220 0.4182 -0.0279 -0.0569 -0.0601 1133 GLY A N   
8189  C CA  . GLY A 1135 ? 0.3933 0.4887 0.4814 -0.0288 -0.0578 -0.0613 1133 GLY A CA  
8190  C C   . GLY A 1135 ? 0.3818 0.4823 0.4652 -0.0247 -0.0568 -0.0606 1133 GLY A C   
8191  O O   . GLY A 1135 ? 0.3886 0.4968 0.4755 -0.0240 -0.0584 -0.0628 1133 GLY A O   
8192  N N   . LEU A 1136 ? 0.3239 0.4206 0.3999 -0.0220 -0.0542 -0.0577 1134 LEU A N   
8193  C CA  . LEU A 1136 ? 0.3944 0.4951 0.4659 -0.0177 -0.0536 -0.0573 1134 LEU A CA  
8194  C C   . LEU A 1136 ? 0.3793 0.4842 0.4528 -0.0190 -0.0504 -0.0538 1134 LEU A C   
8195  O O   . LEU A 1136 ? 0.3716 0.4774 0.4403 -0.0155 -0.0492 -0.0526 1134 LEU A O   
8196  C CB  . LEU A 1136 ? 0.3605 0.4548 0.4222 -0.0133 -0.0533 -0.0568 1134 LEU A CB  
8197  C CG  . LEU A 1136 ? 0.3232 0.4153 0.3815 -0.0107 -0.0566 -0.0606 1134 LEU A CG  
8198  C CD1 . LEU A 1136 ? 0.3186 0.4036 0.3677 -0.0075 -0.0556 -0.0591 1134 LEU A CD1 
8199  C CD2 . LEU A 1136 ? 0.3691 0.4685 0.4282 -0.0079 -0.0594 -0.0637 1134 LEU A CD2 
8200  N N   . GLN A 1137 ? 0.3704 0.4778 0.4510 -0.0239 -0.0492 -0.0521 1135 GLN A N   
8201  C CA  . GLN A 1137 ? 0.3545 0.4665 0.4371 -0.0253 -0.0460 -0.0487 1135 GLN A CA  
8202  C C   . GLN A 1137 ? 0.3579 0.4787 0.4415 -0.0225 -0.0464 -0.0502 1135 GLN A C   
8203  O O   . GLN A 1137 ? 0.3692 0.4921 0.4501 -0.0206 -0.0441 -0.0483 1135 GLN A O   
8204  C CB  . GLN A 1137 ? 0.3771 0.4914 0.4678 -0.0313 -0.0450 -0.0467 1135 GLN A CB  
8205  C CG  . GLN A 1137 ? 0.3888 0.4945 0.4782 -0.0340 -0.0437 -0.0439 1135 GLN A CG  
8206  C CD  . GLN A 1137 ? 0.3514 0.4513 0.4426 -0.0353 -0.0467 -0.0466 1135 GLN A CD  
8207  O OE1 . GLN A 1137 ? 0.4252 0.5265 0.5163 -0.0332 -0.0497 -0.0508 1135 GLN A OE1 
8208  N NE2 . GLN A 1137 ? 0.4495 0.5434 0.5426 -0.0388 -0.0460 -0.0443 1135 GLN A NE2 
8209  N N   . ALA A 1138 ? 0.3186 0.4448 0.4063 -0.0220 -0.0494 -0.0539 1136 ALA A N   
8210  C CA  . ALA A 1138 ? 0.3358 0.4707 0.4249 -0.0193 -0.0498 -0.0553 1136 ALA A CA  
8211  C C   . ALA A 1138 ? 0.3498 0.4822 0.4308 -0.0133 -0.0502 -0.0557 1136 ALA A C   
8212  O O   . ALA A 1138 ? 0.3472 0.4859 0.4288 -0.0106 -0.0503 -0.0565 1136 ALA A O   
8213  C CB  . ALA A 1138 ? 0.3238 0.4653 0.4193 -0.0201 -0.0532 -0.0592 1136 ALA A CB  
8214  N N   . SER A 1139 ? 0.3926 0.5160 0.4664 -0.0113 -0.0504 -0.0551 1137 SER A N   
8215  C CA  . SER A 1139 ? 0.3684 0.4890 0.4346 -0.0059 -0.0508 -0.0550 1137 SER A CA  
8216  C C   . SER A 1139 ? 0.2841 0.4033 0.3471 -0.0046 -0.0476 -0.0518 1137 SER A C   
8217  O O   . SER A 1139 ? 0.3110 0.4290 0.3689 -0.0002 -0.0479 -0.0516 1137 SER A O   
8218  C CB  . SER A 1139 ? 0.3556 0.4679 0.4154 -0.0042 -0.0522 -0.0555 1137 SER A CB  
8219  O OG  . SER A 1139 ? 0.3991 0.5137 0.4601 -0.0033 -0.0558 -0.0593 1137 SER A OG  
8220  N N   . LEU A 1140 ? 0.3074 0.4271 0.3735 -0.0084 -0.0447 -0.0493 1138 LEU A N   
8221  C CA  . LEU A 1140 ? 0.3475 0.4660 0.4106 -0.0074 -0.0416 -0.0464 1138 LEU A CA  
8222  C C   . LEU A 1140 ? 0.3885 0.5161 0.4579 -0.0096 -0.0397 -0.0458 1138 LEU A C   
8223  O O   . LEU A 1140 ? 0.4086 0.5358 0.4784 -0.0120 -0.0368 -0.0430 1138 LEU A O   
8224  C CB  . LEU A 1140 ? 0.3379 0.4479 0.3973 -0.0095 -0.0395 -0.0434 1138 LEU A CB  
8225  C CG  . LEU A 1140 ? 0.3212 0.4220 0.3732 -0.0069 -0.0406 -0.0434 1138 LEU A CG  
8226  C CD1 . LEU A 1140 ? 0.3715 0.4651 0.4213 -0.0095 -0.0384 -0.0406 1138 LEU A CD1 
8227  C CD2 . LEU A 1140 ? 0.3503 0.4496 0.3964 -0.0017 -0.0408 -0.0432 1138 LEU A CD2 
8228  N N   . LYS A 1141 ? 0.3513 0.4875 0.4256 -0.0088 -0.0414 -0.0484 1139 LYS A N   
8229  C CA  . LYS A 1141 ? 0.4352 0.5812 0.5153 -0.0103 -0.0396 -0.0482 1139 LYS A CA  
8230  C C   . LYS A 1141 ? 0.4052 0.5526 0.4818 -0.0061 -0.0381 -0.0477 1139 LYS A C   
8231  O O   . LYS A 1141 ? 0.4107 0.5547 0.4824 -0.0014 -0.0397 -0.0489 1139 LYS A O   
8232  C CB  . LYS A 1141 ? 0.4351 0.5904 0.5220 -0.0106 -0.0420 -0.0514 1139 LYS A CB  
8233  N N   . ASN A 1142 ? 0.3963 0.5489 0.4755 -0.0080 -0.0351 -0.0460 1140 ASN A N   
8234  C CA  . ASN A 1142 ? 0.3625 0.5188 0.4401 -0.0044 -0.0338 -0.0463 1140 ASN A CA  
8235  C C   . ASN A 1142 ? 0.4005 0.5469 0.4700 -0.0010 -0.0333 -0.0450 1140 ASN A C   
8236  O O   . ASN A 1142 ? 0.3997 0.5460 0.4666 0.0038  -0.0344 -0.0464 1140 ASN A O   
8237  C CB  . ASN A 1142 ? 0.4568 0.6208 0.5374 -0.0006 -0.0361 -0.0499 1140 ASN A CB  
8238  C CG  . ASN A 1142 ? 0.4995 0.6734 0.5883 -0.0038 -0.0368 -0.0514 1140 ASN A CG  
8239  O OD1 . ASN A 1142 ? 0.4930 0.6688 0.5838 -0.0027 -0.0398 -0.0540 1140 ASN A OD1 
8240  N ND2 . ASN A 1142 ? 0.4845 0.6652 0.5782 -0.0079 -0.0340 -0.0498 1140 ASN A ND2 
8241  N N   . LEU A 1143 ? 0.4295 0.5678 0.4955 -0.0034 -0.0320 -0.0422 1141 LEU A N   
8242  C CA  . LEU A 1143 ? 0.3921 0.5216 0.4508 -0.0007 -0.0313 -0.0406 1141 LEU A CA  
8243  C C   . LEU A 1143 ? 0.3786 0.5114 0.4369 0.0004  -0.0287 -0.0397 1141 LEU A C   
8244  O O   . LEU A 1143 ? 0.3519 0.4917 0.4145 -0.0027 -0.0264 -0.0389 1141 LEU A O   
8245  C CB  . LEU A 1143 ? 0.3408 0.4614 0.3962 -0.0037 -0.0304 -0.0380 1141 LEU A CB  
8246  C CG  . LEU A 1143 ? 0.3768 0.4910 0.4302 -0.0039 -0.0328 -0.0388 1141 LEU A CG  
8247  C CD1 . LEU A 1143 ? 0.3672 0.4746 0.4192 -0.0076 -0.0313 -0.0361 1141 LEU A CD1 
8248  C CD2 . LEU A 1143 ? 0.3443 0.4527 0.3913 0.0011  -0.0348 -0.0397 1141 LEU A CD2 
8249  N N   . PRO A 1144 ? 0.3655 0.4936 0.4188 0.0046  -0.0289 -0.0399 1142 PRO A N   
8250  C CA  . PRO A 1144 ? 0.3671 0.4967 0.4193 0.0054  -0.0264 -0.0389 1142 PRO A CA  
8251  C C   . PRO A 1144 ? 0.3719 0.4982 0.4229 0.0010  -0.0236 -0.0356 1142 PRO A C   
8252  O O   . PRO A 1144 ? 0.3591 0.4781 0.4078 -0.0010 -0.0239 -0.0339 1142 PRO A O   
8253  C CB  . PRO A 1144 ? 0.3594 0.4816 0.4059 0.0102  -0.0277 -0.0393 1142 PRO A CB  
8254  C CG  . PRO A 1144 ? 0.3408 0.4602 0.3862 0.0125  -0.0310 -0.0407 1142 PRO A CG  
8255  C CD  . PRO A 1144 ? 0.3754 0.4959 0.4235 0.0085  -0.0314 -0.0405 1142 PRO A CD  
8256  N N   . GLN A 1145 ? 0.3393 0.4716 0.3923 -0.0003 -0.0210 -0.0348 1143 GLN A N   
8257  C CA  . GLN A 1145 ? 0.3607 0.4912 0.4133 -0.0046 -0.0183 -0.0314 1143 GLN A CA  
8258  C C   . GLN A 1145 ? 0.3771 0.4961 0.4232 -0.0039 -0.0181 -0.0293 1143 GLN A C   
8259  O O   . GLN A 1145 ? 0.3296 0.4439 0.3748 -0.0074 -0.0171 -0.0266 1143 GLN A O   
8260  C CB  . GLN A 1145 ? 0.4036 0.5428 0.4584 -0.0053 -0.0156 -0.0310 1143 GLN A CB  
8261  N N   . THR A 1146 ? 0.3555 0.4699 0.3972 0.0005  -0.0190 -0.0304 1144 THR A N   
8262  C CA  . THR A 1146 ? 0.3544 0.4582 0.3901 0.0014  -0.0188 -0.0285 1144 THR A CA  
8263  C C   . THR A 1146 ? 0.3379 0.4347 0.3719 -0.0002 -0.0203 -0.0276 1144 THR A C   
8264  O O   . THR A 1146 ? 0.3290 0.4192 0.3600 -0.0022 -0.0193 -0.0252 1144 THR A O   
8265  C CB  . THR A 1146 ? 0.3193 0.4197 0.3514 0.0065  -0.0202 -0.0301 1144 THR A CB  
8266  O OG1 . THR A 1146 ? 0.3506 0.4529 0.3842 0.0091  -0.0230 -0.0326 1144 THR A OG1 
8267  C CG2 . THR A 1146 ? 0.3906 0.4968 0.4239 0.0082  -0.0187 -0.0312 1144 THR A CG2 
8268  N N   . VAL A 1147 ? 0.2741 0.3726 0.3099 0.0008  -0.0227 -0.0297 1145 VAL A N   
8269  C CA  . VAL A 1147 ? 0.2996 0.3927 0.3343 -0.0005 -0.0244 -0.0295 1145 VAL A CA  
8270  C C   . VAL A 1147 ? 0.3094 0.4046 0.3483 -0.0055 -0.0234 -0.0283 1145 VAL A C   
8271  O O   . VAL A 1147 ? 0.3026 0.3915 0.3398 -0.0077 -0.0233 -0.0267 1145 VAL A O   
8272  C CB  . VAL A 1147 ? 0.2561 0.3509 0.2914 0.0025  -0.0275 -0.0323 1145 VAL A CB  
8273  C CG1 . VAL A 1147 ? 0.2587 0.3475 0.2918 0.0017  -0.0292 -0.0324 1145 VAL A CG1 
8274  C CG2 . VAL A 1147 ? 0.2536 0.3470 0.2855 0.0075  -0.0285 -0.0333 1145 VAL A CG2 
8275  N N   . GLY A 1148 ? 0.3203 0.4248 0.3653 -0.0076 -0.0229 -0.0290 1146 GLY A N   
8276  C CA  . GLY A 1148 ? 0.3242 0.4311 0.3739 -0.0127 -0.0220 -0.0275 1146 GLY A CA  
8277  C C   . GLY A 1148 ? 0.3006 0.4029 0.3485 -0.0155 -0.0196 -0.0240 1146 GLY A C   
8278  O O   . GLY A 1148 ? 0.3103 0.4094 0.3600 -0.0192 -0.0197 -0.0224 1146 GLY A O   
8279  N N   . LEU A 1149 ? 0.2916 0.3935 0.3361 -0.0139 -0.0176 -0.0227 1147 LEU A N   
8280  C CA  . LEU A 1149 ? 0.3391 0.4363 0.3813 -0.0162 -0.0155 -0.0194 1147 LEU A CA  
8281  C C   . LEU A 1149 ? 0.3007 0.3872 0.3386 -0.0161 -0.0165 -0.0186 1147 LEU A C   
8282  O O   . LEU A 1149 ? 0.3296 0.4119 0.3670 -0.0189 -0.0153 -0.0159 1147 LEU A O   
8283  C CB  . LEU A 1149 ? 0.3730 0.4712 0.4118 -0.0138 -0.0136 -0.0188 1147 LEU A CB  
8284  C CG  . LEU A 1149 ? 0.4441 0.5531 0.4863 -0.0138 -0.0120 -0.0195 1147 LEU A CG  
8285  C CD1 . LEU A 1149 ? 0.4625 0.5707 0.5006 -0.0106 -0.0107 -0.0197 1147 LEU A CD1 
8286  C CD2 . LEU A 1149 ? 0.4421 0.5574 0.4891 -0.0188 -0.0100 -0.0168 1147 LEU A CD2 
8287  N N   . ARG A 1150 ? 0.3119 0.3942 0.3469 -0.0128 -0.0187 -0.0208 1148 ARG A N   
8288  C CA  . ARG A 1150 ? 0.3228 0.3958 0.3535 -0.0123 -0.0196 -0.0202 1148 ARG A CA  
8289  C C   . ARG A 1150 ? 0.3009 0.3724 0.3344 -0.0145 -0.0216 -0.0213 1148 ARG A C   
8290  O O   . ARG A 1150 ? 0.2971 0.3614 0.3277 -0.0145 -0.0223 -0.0210 1148 ARG A O   
8291  C CB  . ARG A 1150 ? 0.2522 0.3213 0.2775 -0.0076 -0.0209 -0.0217 1148 ARG A CB  
8292  C CG  . ARG A 1150 ? 0.2968 0.3639 0.3183 -0.0056 -0.0191 -0.0202 1148 ARG A CG  
8293  C CD  . ARG A 1150 ? 0.3186 0.3771 0.3340 -0.0031 -0.0198 -0.0197 1148 ARG A CD  
8294  N NE  . ARG A 1150 ? 0.3166 0.3734 0.3286 -0.0006 -0.0187 -0.0189 1148 ARG A NE  
8295  C CZ  . ARG A 1150 ? 0.3408 0.3927 0.3484 0.0027  -0.0198 -0.0191 1148 ARG A CZ  
8296  N NH1 . ARG A 1150 ? 0.2670 0.3155 0.2725 0.0041  -0.0218 -0.0198 1148 ARG A NH1 
8297  N NH2 . ARG A 1150 ? 0.2923 0.3429 0.2977 0.0047  -0.0189 -0.0184 1148 ARG A NH2 
8298  N N   . VAL A 1151 ? 0.2980 0.3763 0.3373 -0.0162 -0.0226 -0.0228 1149 VAL A N   
8299  C CA  . VAL A 1151 ? 0.2555 0.3331 0.2978 -0.0177 -0.0249 -0.0247 1149 VAL A CA  
8300  C C   . VAL A 1151 ? 0.3538 0.4335 0.4022 -0.0229 -0.0242 -0.0229 1149 VAL A C   
8301  O O   . VAL A 1151 ? 0.3918 0.4786 0.4444 -0.0251 -0.0227 -0.0217 1149 VAL A O   
8302  C CB  . VAL A 1151 ? 0.3135 0.3972 0.3581 -0.0155 -0.0272 -0.0281 1149 VAL A CB  
8303  C CG1 . VAL A 1151 ? 0.3651 0.4492 0.4138 -0.0175 -0.0296 -0.0302 1149 VAL A CG1 
8304  C CG2 . VAL A 1151 ? 0.3139 0.3943 0.3524 -0.0105 -0.0283 -0.0294 1149 VAL A CG2 
8305  N N   . SER A 1152 ? 0.2986 0.3723 0.3475 -0.0249 -0.0252 -0.0227 1150 SER A N   
8306  C CA  . SER A 1152 ? 0.3878 0.4631 0.4435 -0.0298 -0.0255 -0.0216 1150 SER A CA  
8307  C C   . SER A 1152 ? 0.3418 0.4143 0.3995 -0.0301 -0.0286 -0.0248 1150 SER A C   
8308  O O   . SER A 1152 ? 0.3405 0.4089 0.3935 -0.0266 -0.0303 -0.0273 1150 SER A O   
8309  C CB  . SER A 1152 ? 0.3182 0.3885 0.3735 -0.0327 -0.0236 -0.0178 1150 SER A CB  
8310  O OG  . SER A 1152 ? 0.4750 0.5362 0.5255 -0.0311 -0.0243 -0.0182 1150 SER A OG  
8311  N N   . TRP A 1153 ? 0.3489 0.4240 0.4139 -0.0343 -0.0296 -0.0247 1151 TRP A N   
8312  C CA  . TRP A 1153 ? 0.3318 0.4047 0.3999 -0.0351 -0.0327 -0.0279 1151 TRP A CA  
8313  C C   . TRP A 1153 ? 0.3714 0.4381 0.4426 -0.0389 -0.0330 -0.0260 1151 TRP A C   
8314  O O   . TRP A 1153 ? 0.3991 0.4671 0.4740 -0.0426 -0.0312 -0.0223 1151 TRP A O   
8315  C CB  . TRP A 1153 ? 0.3653 0.4466 0.4402 -0.0366 -0.0343 -0.0301 1151 TRP A CB  
8316  C CG  . TRP A 1153 ? 0.3685 0.4554 0.4408 -0.0325 -0.0349 -0.0327 1151 TRP A CG  
8317  C CD1 . TRP A 1153 ? 0.3622 0.4554 0.4336 -0.0310 -0.0330 -0.0316 1151 TRP A CD1 
8318  C CD2 . TRP A 1153 ? 0.3208 0.4076 0.3910 -0.0291 -0.0379 -0.0369 1151 TRP A CD2 
8319  N NE1 . TRP A 1153 ? 0.3815 0.4781 0.4507 -0.0269 -0.0346 -0.0348 1151 TRP A NE1 
8320  C CE2 . TRP A 1153 ? 0.3393 0.4320 0.4075 -0.0257 -0.0376 -0.0379 1151 TRP A CE2 
8321  C CE3 . TRP A 1153 ? 0.2936 0.3759 0.3633 -0.0284 -0.0408 -0.0401 1151 TRP A CE3 
8322  C CZ2 . TRP A 1153 ? 0.3619 0.4561 0.4277 -0.0219 -0.0401 -0.0415 1151 TRP A CZ2 
8323  C CZ3 . TRP A 1153 ? 0.3462 0.4306 0.4133 -0.0246 -0.0432 -0.0438 1151 TRP A CZ3 
8324  C CH2 . TRP A 1153 ? 0.3626 0.4528 0.4278 -0.0214 -0.0429 -0.0442 1151 TRP A CH2 
8325  N N   . SER A 1154 ? 0.3300 0.3904 0.3999 -0.0378 -0.0353 -0.0287 1152 SER A N   
8326  C CA  . SER A 1154 ? 0.3702 0.4234 0.4421 -0.0405 -0.0357 -0.0274 1152 SER A CA  
8327  C C   . SER A 1154 ? 0.3854 0.4375 0.4629 -0.0421 -0.0392 -0.0311 1152 SER A C   
8328  O O   . SER A 1154 ? 0.3680 0.4191 0.4427 -0.0389 -0.0415 -0.0354 1152 SER A O   
8329  C CB  . SER A 1154 ? 0.3494 0.3949 0.4135 -0.0373 -0.0348 -0.0270 1152 SER A CB  
8330  O OG  . SER A 1154 ? 0.3679 0.4065 0.4341 -0.0397 -0.0352 -0.0256 1152 SER A OG  
8331  N N   . LYS A 1155 ? 0.3578 0.4103 0.4434 -0.0470 -0.0398 -0.0295 1153 LYS A N   
8332  C CA  . LYS A 1155 ? 0.3654 0.4150 0.4567 -0.0489 -0.0433 -0.0329 1153 LYS A CA  
8333  C C   . LYS A 1155 ? 0.3612 0.4012 0.4514 -0.0491 -0.0440 -0.0326 1153 LYS A C   
8334  O O   . LYS A 1155 ? 0.4423 0.4781 0.5325 -0.0476 -0.0468 -0.0369 1153 LYS A O   
8335  C CB  . LYS A 1155 ? 0.3739 0.4285 0.4753 -0.0543 -0.0440 -0.0313 1153 LYS A CB  
8336  N N   . ASP A 1156 ? 0.3706 0.4074 0.4597 -0.0507 -0.0414 -0.0277 1154 ASP A N   
8337  C CA  . ASP A 1156 ? 0.4123 0.4402 0.5006 -0.0511 -0.0417 -0.0266 1154 ASP A CA  
8338  C C   . ASP A 1156 ? 0.4021 0.4272 0.4809 -0.0470 -0.0392 -0.0253 1154 ASP A C   
8339  O O   . ASP A 1156 ? 0.3886 0.4143 0.4653 -0.0478 -0.0363 -0.0207 1154 ASP A O   
8340  C CB  . ASP A 1156 ? 0.3989 0.4257 0.4942 -0.0565 -0.0410 -0.0215 1154 ASP A CB  
8341  C CG  . ASP A 1156 ? 0.4960 0.5135 0.5919 -0.0572 -0.0418 -0.0205 1154 ASP A CG  
8342  O OD1 . ASP A 1156 ? 0.5040 0.5162 0.5935 -0.0533 -0.0419 -0.0226 1154 ASP A OD1 
8343  O OD2 . ASP A 1156 ? 0.4970 0.5126 0.6001 -0.0617 -0.0424 -0.0173 1154 ASP A OD2 
8344  N N   . TRP A 1157 ? 0.3926 0.4148 0.4656 -0.0427 -0.0404 -0.0294 1155 TRP A N   
8345  C CA  . TRP A 1157 ? 0.3713 0.3912 0.4353 -0.0388 -0.0382 -0.0284 1155 TRP A CA  
8346  C C   . TRP A 1157 ? 0.4106 0.4247 0.4735 -0.0400 -0.0363 -0.0243 1155 TRP A C   
8347  O O   . TRP A 1157 ? 0.3817 0.3962 0.4395 -0.0388 -0.0335 -0.0211 1155 TRP A O   
8348  C CB  . TRP A 1157 ? 0.3765 0.3937 0.4354 -0.0345 -0.0401 -0.0332 1155 TRP A CB  
8349  C CG  . TRP A 1157 ? 0.3718 0.3946 0.4308 -0.0327 -0.0421 -0.0374 1155 TRP A CG  
8350  C CD1 . TRP A 1157 ? 0.3615 0.3914 0.4239 -0.0340 -0.0422 -0.0373 1155 TRP A CD1 
8351  C CD2 . TRP A 1157 ? 0.3655 0.3875 0.4209 -0.0292 -0.0444 -0.0424 1155 TRP A CD2 
8352  N NE1 . TRP A 1157 ? 0.3757 0.4090 0.4370 -0.0314 -0.0445 -0.0418 1155 TRP A NE1 
8353  C CE2 . TRP A 1157 ? 0.3532 0.3819 0.4101 -0.0284 -0.0459 -0.0449 1155 TRP A CE2 
8354  C CE3 . TRP A 1157 ? 0.3596 0.3764 0.4107 -0.0265 -0.0454 -0.0449 1155 TRP A CE3 
8355  C CZ2 . TRP A 1157 ? 0.3506 0.3808 0.4046 -0.0252 -0.0484 -0.0498 1155 TRP A CZ2 
8356  C CZ3 . TRP A 1157 ? 0.3380 0.3566 0.3862 -0.0232 -0.0477 -0.0497 1155 TRP A CZ3 
8357  C CH2 . TRP A 1157 ? 0.3441 0.3692 0.3936 -0.0226 -0.0492 -0.0520 1155 TRP A CH2 
8358  N N   . ALA A 1158 ? 0.3814 0.3899 0.4490 -0.0424 -0.0380 -0.0245 1156 ALA A N   
8359  C CA  . ALA A 1158 ? 0.3996 0.4021 0.4659 -0.0431 -0.0365 -0.0209 1156 ALA A CA  
8360  C C   . ALA A 1158 ? 0.4519 0.4571 0.5207 -0.0466 -0.0340 -0.0149 1156 ALA A C   
8361  O O   . ALA A 1158 ? 0.4980 0.4995 0.5645 -0.0468 -0.0322 -0.0114 1156 ALA A O   
8362  C CB  . ALA A 1158 ? 0.4416 0.4375 0.5130 -0.0445 -0.0393 -0.0227 1156 ALA A CB  
8363  N N   . ALA A 1159 ? 0.4293 0.4412 0.5029 -0.0493 -0.0338 -0.0138 1157 ALA A N   
8364  C CA  . ALA A 1159 ? 0.4693 0.4851 0.5451 -0.0526 -0.0313 -0.0082 1157 ALA A CA  
8365  C C   . ALA A 1159 ? 0.4294 0.4508 0.4990 -0.0501 -0.0283 -0.0069 1157 ALA A C   
8366  O O   . ALA A 1159 ? 0.4927 0.5163 0.5616 -0.0517 -0.0258 -0.0023 1157 ALA A O   
8367  C CB  . ALA A 1159 ? 0.3779 0.3990 0.4626 -0.0572 -0.0325 -0.0073 1157 ALA A CB  
8368  N N   . ASP A 1160 ? 0.4447 0.4681 0.5095 -0.0462 -0.0287 -0.0108 1158 ASP A N   
8369  C CA  . ASP A 1160 ? 0.3834 0.4122 0.4431 -0.0437 -0.0264 -0.0101 1158 ASP A CA  
8370  C C   . ASP A 1160 ? 0.4137 0.4381 0.4651 -0.0396 -0.0252 -0.0103 1158 ASP A C   
8371  O O   . ASP A 1160 ? 0.4375 0.4654 0.4843 -0.0370 -0.0236 -0.0103 1158 ASP A O   
8372  C CB  . ASP A 1160 ? 0.4508 0.4859 0.5118 -0.0423 -0.0278 -0.0138 1158 ASP A CB  
8373  C CG  . ASP A 1160 ? 0.4510 0.4917 0.5205 -0.0466 -0.0288 -0.0133 1158 ASP A CG  
8374  O OD1 . ASP A 1160 ? 0.4759 0.5186 0.5490 -0.0502 -0.0271 -0.0090 1158 ASP A OD1 
8375  O OD2 . ASP A 1160 ? 0.4303 0.4735 0.5030 -0.0464 -0.0311 -0.0170 1158 ASP A OD2 
8376  N N   . GLY A 1161 ? 0.4064 0.4232 0.4561 -0.0390 -0.0259 -0.0106 1159 GLY A N   
8377  C CA  . GLY A 1161 ? 0.3657 0.3783 0.4079 -0.0354 -0.0247 -0.0107 1159 GLY A CA  
8378  C C   . GLY A 1161 ? 0.4647 0.4763 0.5050 -0.0364 -0.0220 -0.0061 1159 GLY A C   
8379  O O   . GLY A 1161 ? 0.4694 0.4844 0.5136 -0.0396 -0.0208 -0.0027 1159 GLY A O   
8380  N N   . PRO A 1162 ? 0.4204 0.4274 0.4546 -0.0336 -0.0210 -0.0057 1160 PRO A N   
8381  C CA  . PRO A 1162 ? 0.4308 0.4340 0.4601 -0.0299 -0.0221 -0.0091 1160 PRO A CA  
8382  C C   . PRO A 1162 ? 0.4259 0.4333 0.4512 -0.0267 -0.0219 -0.0113 1160 PRO A C   
8383  O O   . PRO A 1162 ? 0.3474 0.3592 0.3714 -0.0263 -0.0203 -0.0096 1160 PRO A O   
8384  C CB  . PRO A 1162 ? 0.4091 0.4072 0.4341 -0.0288 -0.0204 -0.0068 1160 PRO A CB  
8385  C CG  . PRO A 1162 ? 0.4693 0.4709 0.4942 -0.0303 -0.0180 -0.0028 1160 PRO A CG  
8386  C CD  . PRO A 1162 ? 0.4930 0.4991 0.5247 -0.0341 -0.0184 -0.0016 1160 PRO A CD  
8387  N N   . PHE A 1163 ? 0.3095 0.3157 0.3329 -0.0243 -0.0239 -0.0150 1161 PHE A N   
8388  C CA  . PHE A 1163 ? 0.3040 0.3131 0.3227 -0.0208 -0.0240 -0.0169 1161 PHE A CA  
8389  C C   . PHE A 1163 ? 0.3078 0.3126 0.3196 -0.0177 -0.0230 -0.0164 1161 PHE A C   
8390  O O   . PHE A 1163 ? 0.3513 0.3512 0.3621 -0.0180 -0.0225 -0.0154 1161 PHE A O   
8391  C CB  . PHE A 1163 ? 0.3140 0.3253 0.3346 -0.0200 -0.0268 -0.0210 1161 PHE A CB  
8392  C CG  . PHE A 1163 ? 0.2960 0.3113 0.3240 -0.0234 -0.0279 -0.0215 1161 PHE A CG  
8393  C CD1 . PHE A 1163 ? 0.3091 0.3302 0.3394 -0.0247 -0.0267 -0.0197 1161 PHE A CD1 
8394  C CD2 . PHE A 1163 ? 0.2963 0.3095 0.3292 -0.0253 -0.0301 -0.0237 1161 PHE A CD2 
8395  C CE1 . PHE A 1163 ? 0.3399 0.3652 0.3773 -0.0280 -0.0276 -0.0198 1161 PHE A CE1 
8396  C CE2 . PHE A 1163 ? 0.3091 0.3259 0.3493 -0.0288 -0.0312 -0.0238 1161 PHE A CE2 
8397  C CZ  . PHE A 1163 ? 0.3525 0.3755 0.3950 -0.0302 -0.0299 -0.0218 1161 PHE A CZ  
8398  N N   . ALA A 1164 ? 0.3257 0.3327 0.3331 -0.0147 -0.0227 -0.0170 1162 ALA A N   
8399  C CA  . ALA A 1164 ? 0.3347 0.3384 0.3357 -0.0118 -0.0218 -0.0163 1162 ALA A CA  
8400  C C   . ALA A 1164 ? 0.3339 0.3380 0.3313 -0.0087 -0.0235 -0.0193 1162 ALA A C   
8401  O O   . ALA A 1164 ? 0.3655 0.3678 0.3575 -0.0061 -0.0229 -0.0186 1162 ALA A O   
8402  C CB  . ALA A 1164 ? 0.3553 0.3606 0.3536 -0.0108 -0.0197 -0.0137 1162 ALA A CB  
8403  N N   . GLY A 1165 ? 0.2940 0.3005 0.2944 -0.0090 -0.0258 -0.0223 1163 GLY A N   
8404  C CA  . GLY A 1165 ? 0.3184 0.3263 0.3157 -0.0062 -0.0277 -0.0253 1163 GLY A CA  
8405  C C   . GLY A 1165 ? 0.3129 0.3251 0.3148 -0.0070 -0.0300 -0.0282 1163 GLY A C   
8406  O O   . GLY A 1165 ? 0.2705 0.2851 0.2779 -0.0098 -0.0299 -0.0277 1163 GLY A O   
8407  N N   . ALA A 1166 ? 0.2934 0.3072 0.2930 -0.0047 -0.0321 -0.0313 1164 ALA A N   
8408  C CA  . ALA A 1166 ? 0.2756 0.2937 0.2795 -0.0053 -0.0346 -0.0346 1164 ALA A CA  
8409  C C   . ALA A 1166 ? 0.2786 0.3000 0.2782 -0.0017 -0.0362 -0.0365 1164 ALA A C   
8410  O O   . ALA A 1166 ? 0.3053 0.3248 0.2989 0.0009  -0.0360 -0.0364 1164 ALA A O   
8411  C CB  . ALA A 1166 ? 0.2785 0.2946 0.2865 -0.0071 -0.0363 -0.0376 1164 ALA A CB  
8412  N N   . LEU A 1167 ? 0.2773 0.3039 0.2798 -0.0017 -0.0377 -0.0380 1165 LEU A N   
8413  C CA  . LEU A 1167 ? 0.2793 0.3097 0.2788 0.0014  -0.0398 -0.0401 1165 LEU A CA  
8414  C C   . LEU A 1167 ? 0.2817 0.3157 0.2863 0.0003  -0.0427 -0.0443 1165 LEU A C   
8415  O O   . LEU A 1167 ? 0.3164 0.3527 0.3274 -0.0026 -0.0429 -0.0447 1165 LEU A O   
8416  C CB  . LEU A 1167 ? 0.2773 0.3112 0.2757 0.0030  -0.0393 -0.0382 1165 LEU A CB  
8417  C CG  . LEU A 1167 ? 0.2749 0.3055 0.2691 0.0041  -0.0366 -0.0341 1165 LEU A CG  
8418  C CD1 . LEU A 1167 ? 0.2736 0.3079 0.2677 0.0057  -0.0367 -0.0329 1165 LEU A CD1 
8419  C CD2 . LEU A 1167 ? 0.2767 0.3037 0.2641 0.0066  -0.0364 -0.0334 1165 LEU A CD2 
8420  N N   . VAL A 1168 ? 0.2852 0.3198 0.2869 0.0024  -0.0448 -0.0476 1166 VAL A N   
8421  C CA  . VAL A 1168 ? 0.2881 0.3255 0.2943 0.0015  -0.0478 -0.0522 1166 VAL A CA  
8422  C C   . VAL A 1168 ? 0.2904 0.3330 0.2935 0.0048  -0.0502 -0.0546 1166 VAL A C   
8423  O O   . VAL A 1168 ? 0.2915 0.3337 0.2876 0.0080  -0.0499 -0.0536 1166 VAL A O   
8424  C CB  . VAL A 1168 ? 0.2908 0.3241 0.2972 0.0009  -0.0485 -0.0547 1166 VAL A CB  
8425  C CG1 . VAL A 1168 ? 0.3035 0.3396 0.3154 -0.0002 -0.0518 -0.0599 1166 VAL A CG1 
8426  C CG2 . VAL A 1168 ? 0.2887 0.3164 0.2976 -0.0020 -0.0461 -0.0518 1166 VAL A CG2 
8427  N N   . GLU A 1169 ? 0.2914 0.3388 0.2997 0.0039  -0.0526 -0.0575 1167 GLU A N   
8428  C CA  . GLU A 1169 ? 0.2942 0.3470 0.3003 0.0068  -0.0554 -0.0604 1167 GLU A CA  
8429  C C   . GLU A 1169 ? 0.2998 0.3544 0.3100 0.0058  -0.0585 -0.0658 1167 GLU A C   
8430  O O   . GLU A 1169 ? 0.2974 0.3515 0.3150 0.0023  -0.0589 -0.0671 1167 GLU A O   
8431  C CB  . GLU A 1169 ? 0.2923 0.3501 0.3007 0.0072  -0.0557 -0.0592 1167 GLU A CB  
8432  C CG  . GLU A 1169 ? 0.2951 0.3588 0.3014 0.0103  -0.0587 -0.0618 1167 GLU A CG  
8433  C CD  . GLU A 1169 ? 0.3153 0.3847 0.3267 0.0098  -0.0596 -0.0619 1167 GLU A CD  
8434  O OE1 . GLU A 1169 ? 0.3009 0.3700 0.3175 0.0069  -0.0578 -0.0601 1167 GLU A OE1 
8435  O OE2 . GLU A 1169 ? 0.3214 0.3960 0.3318 0.0123  -0.0621 -0.0638 1167 GLU A OE2 
8436  N N   . GLY A 1170 ? 0.3015 0.3582 0.3072 0.0089  -0.0606 -0.0689 1168 GLY A N   
8437  C CA  . GLY A 1170 ? 0.3349 0.3940 0.3445 0.0083  -0.0639 -0.0746 1168 GLY A CA  
8438  C C   . GLY A 1170 ? 0.3260 0.3863 0.3291 0.0119  -0.0656 -0.0776 1168 GLY A C   
8439  O O   . GLY A 1170 ? 0.3426 0.4017 0.3382 0.0145  -0.0640 -0.0749 1168 GLY A O   
8440  N N   . ASP A 1171 ? 0.3299 0.3931 0.3363 0.0118  -0.0689 -0.0833 1169 ASP A N   
8441  C CA  . ASP A 1171 ? 0.3492 0.4136 0.3502 0.0148  -0.0705 -0.0870 1169 ASP A CA  
8442  C C   . ASP A 1171 ? 0.3677 0.4258 0.3684 0.0138  -0.0689 -0.0873 1169 ASP A C   
8443  O O   . ASP A 1171 ? 0.3518 0.4046 0.3564 0.0108  -0.0667 -0.0845 1169 ASP A O   
8444  C CB  . ASP A 1171 ? 0.3600 0.4299 0.3644 0.0154  -0.0747 -0.0935 1169 ASP A CB  
8445  C CG  . ASP A 1171 ? 0.4120 0.4800 0.4265 0.0113  -0.0764 -0.0970 1169 ASP A CG  
8446  O OD1 . ASP A 1171 ? 0.3793 0.4413 0.3975 0.0085  -0.0746 -0.0956 1169 ASP A OD1 
8447  O OD2 . ASP A 1171 ? 0.4664 0.5394 0.4855 0.0109  -0.0796 -0.1012 1169 ASP A OD2 
8448  N N   . ALA A 1172 ? 0.3550 0.4142 0.3508 0.0166  -0.0701 -0.0908 1170 ALA A N   
8449  C CA  . ALA A 1172 ? 0.3499 0.4038 0.3443 0.0165  -0.0685 -0.0910 1170 ALA A CA  
8450  C C   . ALA A 1172 ? 0.3704 0.4196 0.3737 0.0127  -0.0693 -0.0935 1170 ALA A C   
8451  O O   . ALA A 1172 ? 0.3367 0.3798 0.3412 0.0110  -0.0669 -0.0908 1170 ALA A O   
8452  C CB  . ALA A 1172 ? 0.3597 0.4171 0.3477 0.0203  -0.0699 -0.0951 1170 ALA A CB  
8453  N N   . GLU A 1173 ? 0.3662 0.4180 0.3761 0.0114  -0.0727 -0.0985 1171 GLU A N   
8454  C CA  . GLU A 1173 ? 0.3535 0.4007 0.3726 0.0076  -0.0738 -0.1008 1171 GLU A CA  
8455  C C   . GLU A 1173 ? 0.3550 0.3985 0.3791 0.0036  -0.0713 -0.0952 1171 GLU A C   
8456  O O   . GLU A 1173 ? 0.3933 0.4308 0.4218 0.0009  -0.0703 -0.0939 1171 GLU A O   
8457  C CB  . GLU A 1173 ? 0.3835 0.4348 0.4087 0.0070  -0.0782 -0.1073 1171 GLU A CB  
8458  N N   . ARG A 1174 ? 0.3624 0.4097 0.3861 0.0033  -0.0705 -0.0919 1172 ARG A N   
8459  C CA  . ARG A 1174 ? 0.3493 0.3940 0.3772 -0.0002 -0.0679 -0.0865 1172 ARG A CA  
8460  C C   . ARG A 1174 ? 0.3422 0.3818 0.3652 0.0001  -0.0641 -0.0813 1172 ARG A C   
8461  O O   . ARG A 1174 ? 0.3652 0.4001 0.3924 -0.0031 -0.0623 -0.0783 1172 ARG A O   
8462  C CB  . ARG A 1174 ? 0.3351 0.3856 0.3633 0.0000  -0.0679 -0.0846 1172 ARG A CB  
8463  C CG  . ARG A 1174 ? 0.3337 0.3827 0.3650 -0.0030 -0.0649 -0.0789 1172 ARG A CG  
8464  C CD  . ARG A 1174 ? 0.3963 0.4431 0.4375 -0.0079 -0.0655 -0.0793 1172 ARG A CD  
8465  N NE  . ARG A 1174 ? 0.3849 0.4320 0.4293 -0.0108 -0.0629 -0.0742 1172 ARG A NE  
8466  C CZ  . ARG A 1174 ? 0.4242 0.4686 0.4758 -0.0152 -0.0622 -0.0724 1172 ARG A CZ  
8467  N NH1 . ARG A 1174 ? 0.4158 0.4563 0.4727 -0.0174 -0.0641 -0.0751 1172 ARG A NH1 
8468  N NH2 . ARG A 1174 ? 0.3768 0.4224 0.4303 -0.0174 -0.0596 -0.0676 1172 ARG A NH2 
8469  N N   . ILE A 1175 ? 0.3235 0.3640 0.3375 0.0039  -0.0628 -0.0800 1173 ILE A N   
8470  C CA  . ILE A 1175 ? 0.3391 0.3749 0.3482 0.0044  -0.0592 -0.0751 1173 ILE A CA  
8471  C C   . ILE A 1175 ? 0.3241 0.3540 0.3355 0.0031  -0.0589 -0.0764 1173 ILE A C   
8472  O O   . ILE A 1175 ? 0.3062 0.3313 0.3192 0.0009  -0.0564 -0.0725 1173 ILE A O   
8473  C CB  . ILE A 1175 ? 0.3144 0.3526 0.3139 0.0086  -0.0583 -0.0738 1173 ILE A CB  
8474  C CG1 . ILE A 1175 ? 0.3453 0.3882 0.3430 0.0097  -0.0582 -0.0712 1173 ILE A CG1 
8475  C CG2 . ILE A 1175 ? 0.3061 0.3392 0.3008 0.0092  -0.0550 -0.0698 1173 ILE A CG2 
8476  C CD1 . ILE A 1175 ? 0.3279 0.3738 0.3167 0.0139  -0.0581 -0.0701 1173 ILE A CD1 
8477  N N   . ARG A 1176 ? 0.3341 0.3645 0.3459 0.0044  -0.0615 -0.0820 1174 ARG A N   
8478  C CA  A ARG A 1176 ? 0.3309 0.3558 0.3453 0.0035  -0.0616 -0.0838 1174 ARG A CA  
8479  C CA  B ARG A 1176 ? 0.3309 0.3557 0.3452 0.0035  -0.0616 -0.0838 1174 ARG A CA  
8480  C C   . ARG A 1176 ? 0.3152 0.3357 0.3389 -0.0011 -0.0618 -0.0828 1174 ARG A C   
8481  O O   . ARG A 1176 ? 0.3621 0.3769 0.3873 -0.0027 -0.0600 -0.0801 1174 ARG A O   
8482  C CB  A ARG A 1176 ? 0.3240 0.3510 0.3379 0.0060  -0.0648 -0.0909 1174 ARG A CB  
8483  C CB  B ARG A 1176 ? 0.3242 0.3511 0.3380 0.0060  -0.0647 -0.0908 1174 ARG A CB  
8484  C CG  A ARG A 1176 ? 0.3500 0.3720 0.3643 0.0065  -0.0648 -0.0931 1174 ARG A CG  
8485  C CG  B ARG A 1176 ? 0.3525 0.3736 0.3696 0.0053  -0.0652 -0.0933 1174 ARG A CG  
8486  C CD  A ARG A 1176 ? 0.3548 0.3791 0.3708 0.0084  -0.0686 -0.1011 1174 ARG A CD  
8487  C CD  B ARG A 1176 ? 0.3545 0.3782 0.3712 0.0080  -0.0685 -0.1009 1174 ARG A CD  
8488  N NE  A ARG A 1176 ? 0.3447 0.3765 0.3544 0.0120  -0.0699 -0.1038 1174 ARG A NE  
8489  N NE  B ARG A 1176 ? 0.3525 0.3707 0.3742 0.0072  -0.0697 -0.1041 1174 ARG A NE  
8490  C CZ  A ARG A 1176 ? 0.3912 0.4258 0.3924 0.0159  -0.0689 -0.1044 1174 ARG A CZ  
8491  C CZ  B ARG A 1176 ? 0.4046 0.4199 0.4356 0.0044  -0.0726 -0.1076 1174 ARG A CZ  
8492  N NH1 A ARG A 1176 ? 0.3803 0.4111 0.3785 0.0168  -0.0666 -0.1028 1174 ARG A NH1 
8493  N NH1 B ARG A 1176 ? 0.3865 0.4043 0.4231 0.0019  -0.0745 -0.1082 1174 ARG A NH1 
8494  N NH2 A ARG A 1176 ? 0.3349 0.3766 0.3308 0.0189  -0.0702 -0.1064 1174 ARG A NH2 
8495  N NH2 B ARG A 1176 ? 0.4204 0.4304 0.4555 0.0040  -0.0737 -0.1104 1174 ARG A NH2 
8496  N N   . ALA A 1177 ? 0.3153 0.3388 0.3454 -0.0033 -0.0641 -0.0846 1175 ALA A N   
8497  C CA  . ALA A 1177 ? 0.3149 0.3350 0.3543 -0.0080 -0.0645 -0.0833 1175 ALA A CA  
8498  C C   . ALA A 1177 ? 0.3098 0.3277 0.3490 -0.0103 -0.0607 -0.0762 1175 ALA A C   
8499  O O   . ALA A 1177 ? 0.3322 0.3451 0.3759 -0.0133 -0.0598 -0.0737 1175 ALA A O   
8500  C CB  . ALA A 1177 ? 0.3164 0.3413 0.3625 -0.0099 -0.0675 -0.0864 1175 ALA A CB  
8501  N N   . VAL A 1178 ? 0.3200 0.3420 0.3541 -0.0088 -0.0588 -0.0730 1176 VAL A N   
8502  C CA  . VAL A 1178 ? 0.3015 0.3221 0.3348 -0.0105 -0.0553 -0.0667 1176 VAL A CA  
8503  C C   . VAL A 1178 ? 0.3091 0.3241 0.3376 -0.0094 -0.0527 -0.0639 1176 VAL A C   
8504  O O   . VAL A 1178 ? 0.3266 0.3377 0.3576 -0.0121 -0.0507 -0.0600 1176 VAL A O   
8505  C CB  . VAL A 1178 ? 0.3020 0.3280 0.3310 -0.0087 -0.0542 -0.0645 1176 VAL A CB  
8506  C CG1 . VAL A 1178 ? 0.2940 0.3185 0.3215 -0.0099 -0.0506 -0.0585 1176 VAL A CG1 
8507  C CG2 . VAL A 1178 ? 0.2994 0.3312 0.3340 -0.0100 -0.0566 -0.0669 1176 VAL A CG2 
8508  N N   . ASN A 1179 ? 0.3282 0.3431 0.3496 -0.0056 -0.0528 -0.0658 1177 ASN A N   
8509  C CA  . ASN A 1179 ? 0.3319 0.3420 0.3487 -0.0044 -0.0504 -0.0635 1177 ASN A CA  
8510  C C   . ASN A 1179 ? 0.3483 0.3526 0.3709 -0.0069 -0.0510 -0.0642 1177 ASN A C   
8511  O O   . ASN A 1179 ? 0.3393 0.3393 0.3617 -0.0081 -0.0486 -0.0603 1177 ASN A O   
8512  C CB  . ASN A 1179 ? 0.3745 0.3865 0.3839 -0.0001 -0.0510 -0.0663 1177 ASN A CB  
8513  C CG  . ASN A 1179 ? 0.4515 0.4610 0.4542 0.0017  -0.0478 -0.0625 1177 ASN A CG  
8514  O OD1 . ASN A 1179 ? 0.4445 0.4519 0.4466 0.0003  -0.0452 -0.0574 1177 ASN A OD1 
8515  N ND2 . ASN A 1179 ? 0.4623 0.4725 0.4597 0.0049  -0.0482 -0.0650 1177 ASN A ND2 
8516  N N   . LYS A 1180 ? 0.3319 0.3361 0.3601 -0.0077 -0.0543 -0.0693 1178 LYS A N   
8517  C CA  . LYS A 1180 ? 0.3494 0.3478 0.3840 -0.0101 -0.0553 -0.0702 1178 LYS A CA  
8518  C C   . LYS A 1180 ? 0.3431 0.3392 0.3842 -0.0147 -0.0542 -0.0656 1178 LYS A C   
8519  O O   . LYS A 1180 ? 0.3747 0.3655 0.4180 -0.0165 -0.0530 -0.0628 1178 LYS A O   
8520  C CB  . LYS A 1180 ? 0.3728 0.3718 0.4121 -0.0098 -0.0594 -0.0772 1178 LYS A CB  
8521  C CG  . LYS A 1180 ? 0.3685 0.3688 0.4015 -0.0052 -0.0603 -0.0818 1178 LYS A CG  
8522  C CD  . LYS A 1180 ? 0.4407 0.4430 0.4777 -0.0043 -0.0646 -0.0893 1178 LYS A CD  
8523  C CE  . LYS A 1180 ? 0.5038 0.4999 0.5479 -0.0059 -0.0667 -0.0924 1178 LYS A CE  
8524  N NZ  . LYS A 1180 ? 0.5375 0.5297 0.5774 -0.0035 -0.0651 -0.0922 1178 LYS A NZ  
8525  N N   . ALA A 1181 ? 0.3312 0.3319 0.3755 -0.0167 -0.0545 -0.0645 1179 ALA A N   
8526  C CA  . ALA A 1181 ? 0.3429 0.3427 0.3930 -0.0211 -0.0532 -0.0597 1179 ALA A CA  
8527  C C   . ALA A 1181 ? 0.3472 0.3455 0.3923 -0.0209 -0.0492 -0.0537 1179 ALA A C   
8528  O O   . ALA A 1181 ? 0.3553 0.3501 0.4040 -0.0239 -0.0478 -0.0498 1179 ALA A O   
8529  C CB  . ALA A 1181 ? 0.3301 0.3360 0.3841 -0.0228 -0.0542 -0.0601 1179 ALA A CB  
8530  N N   . ILE A 1182 ? 0.3428 0.3437 0.3798 -0.0175 -0.0474 -0.0529 1180 ILE A N   
8531  C CA  . ILE A 1182 ? 0.3275 0.3270 0.3600 -0.0173 -0.0438 -0.0475 1180 ILE A CA  
8532  C C   . ILE A 1182 ? 0.3340 0.3273 0.3649 -0.0169 -0.0428 -0.0464 1180 ILE A C   
8533  O O   . ILE A 1182 ? 0.3543 0.3449 0.3854 -0.0186 -0.0405 -0.0419 1180 ILE A O   
8534  C CB  . ILE A 1182 ? 0.3489 0.3524 0.3736 -0.0137 -0.0425 -0.0470 1180 ILE A CB  
8535  C CG1 . ILE A 1182 ? 0.3091 0.3187 0.3359 -0.0144 -0.0430 -0.0468 1180 ILE A CG1 
8536  C CG2 . ILE A 1182 ? 0.3343 0.3354 0.3535 -0.0128 -0.0391 -0.0424 1180 ILE A CG2 
8537  C CD1 . ILE A 1182 ? 0.3310 0.3447 0.3510 -0.0106 -0.0427 -0.0473 1180 ILE A CD1 
8538  N N   . ALA A 1183 ? 0.3272 0.3184 0.3567 -0.0146 -0.0446 -0.0507 1181 ALA A N   
8539  C CA  . ALA A 1183 ? 0.3937 0.3792 0.4220 -0.0140 -0.0438 -0.0502 1181 ALA A CA  
8540  C C   . ALA A 1183 ? 0.4163 0.3971 0.4524 -0.0179 -0.0444 -0.0484 1181 ALA A C   
8541  O O   . ALA A 1183 ? 0.4159 0.3921 0.4514 -0.0182 -0.0430 -0.0458 1181 ALA A O   
8542  C CB  . ALA A 1183 ? 0.3600 0.3451 0.3859 -0.0107 -0.0459 -0.0559 1181 ALA A CB  
8543  N N   . ALA A 1184 ? 0.3812 0.3632 0.4246 -0.0209 -0.0465 -0.0495 1182 ALA A N   
8544  C CA  . ALA A 1184 ? 0.3837 0.3615 0.4351 -0.0250 -0.0472 -0.0472 1182 ALA A CA  
8545  C C   . ALA A 1184 ? 0.4294 0.4081 0.4817 -0.0280 -0.0444 -0.0407 1182 ALA A C   
8546  O O   . ALA A 1184 ? 0.4448 0.4203 0.5031 -0.0315 -0.0446 -0.0378 1182 ALA A O   
8547  C CB  . ALA A 1184 ? 0.4470 0.4257 0.5064 -0.0273 -0.0508 -0.0510 1182 ALA A CB  
8548  N N   . LEU A 1185 ? 0.3592 0.3425 0.4060 -0.0268 -0.0419 -0.0383 1183 LEU A N   
8549  C CA  . LEU A 1185 ? 0.3961 0.3810 0.4437 -0.0295 -0.0393 -0.0325 1183 LEU A CA  
8550  C C   . LEU A 1185 ? 0.4127 0.3927 0.4580 -0.0295 -0.0372 -0.0288 1183 LEU A C   
8551  O O   . LEU A 1185 ? 0.4209 0.3988 0.4600 -0.0261 -0.0363 -0.0297 1183 LEU A O   
8552  C CB  . LEU A 1185 ? 0.3497 0.3407 0.3922 -0.0277 -0.0374 -0.0315 1183 LEU A CB  
8553  C CG  . LEU A 1185 ? 0.3725 0.3692 0.4173 -0.0277 -0.0392 -0.0346 1183 LEU A CG  
8554  C CD1 . LEU A 1185 ? 0.3564 0.3582 0.3952 -0.0251 -0.0375 -0.0338 1183 LEU A CD1 
8555  C CD2 . LEU A 1185 ? 0.3979 0.3968 0.4512 -0.0323 -0.0400 -0.0330 1183 LEU A CD2 
8556  N N   . PRO A 1186 ? 0.4309 0.4091 0.4809 -0.0331 -0.0364 -0.0244 1184 PRO A N   
8557  C CA  . PRO A 1186 ? 0.4261 0.3999 0.4737 -0.0331 -0.0344 -0.0207 1184 PRO A CA  
8558  C C   . PRO A 1186 ? 0.3834 0.3600 0.4237 -0.0311 -0.0312 -0.0179 1184 PRO A C   
8559  O O   . PRO A 1186 ? 0.3920 0.3741 0.4306 -0.0309 -0.0301 -0.0173 1184 PRO A O   
8560  C CB  . PRO A 1186 ? 0.4743 0.4469 0.5291 -0.0378 -0.0346 -0.0164 1184 PRO A CB  
8561  C CG  . PRO A 1186 ? 0.5158 0.4945 0.5746 -0.0401 -0.0350 -0.0165 1184 PRO A CG  
8562  C CD  . PRO A 1186 ? 0.4085 0.3891 0.4662 -0.0375 -0.0372 -0.0225 1184 PRO A CD  
8563  N N   . GLY A 1187 ? 0.3958 0.3686 0.4321 -0.0295 -0.0297 -0.0162 1185 GLY A N   
8564  C CA  . GLY A 1187 ? 0.4160 0.3907 0.4459 -0.0278 -0.0268 -0.0134 1185 GLY A CA  
8565  C C   . GLY A 1187 ? 0.3630 0.3379 0.3861 -0.0236 -0.0265 -0.0164 1185 GLY A C   
8566  O O   . GLY A 1187 ? 0.4256 0.3972 0.4477 -0.0217 -0.0279 -0.0195 1185 GLY A O   
8567  N N   . PRO A 1188 ? 0.3114 0.2902 0.3297 -0.0220 -0.0248 -0.0155 1186 PRO A N   
8568  C CA  . PRO A 1188 ? 0.3712 0.3500 0.3825 -0.0181 -0.0242 -0.0171 1186 PRO A CA  
8569  C C   . PRO A 1188 ? 0.3682 0.3482 0.3787 -0.0160 -0.0265 -0.0220 1186 PRO A C   
8570  O O   . PRO A 1188 ? 0.3581 0.3410 0.3725 -0.0171 -0.0283 -0.0241 1186 PRO A O   
8571  C CB  . PRO A 1188 ? 0.3987 0.3816 0.4066 -0.0175 -0.0222 -0.0147 1186 PRO A CB  
8572  C CG  . PRO A 1188 ? 0.4559 0.4427 0.4690 -0.0203 -0.0226 -0.0139 1186 PRO A CG  
8573  C CD  . PRO A 1188 ? 0.3930 0.3767 0.4122 -0.0236 -0.0234 -0.0128 1186 PRO A CD  
8574  N N   . LEU A 1189 ? 0.3595 0.3380 0.3650 -0.0129 -0.0264 -0.0238 1187 LEU A N   
8575  C CA  . LEU A 1189 ? 0.3748 0.3555 0.3780 -0.0103 -0.0282 -0.0281 1187 LEU A CA  
8576  C C   . LEU A 1189 ? 0.4189 0.4044 0.4186 -0.0089 -0.0277 -0.0276 1187 LEU A C   
8577  O O   . LEU A 1189 ? 0.4639 0.4498 0.4585 -0.0073 -0.0257 -0.0252 1187 LEU A O   
8578  C CB  . LEU A 1189 ? 0.3938 0.3723 0.3924 -0.0074 -0.0279 -0.0297 1187 LEU A CB  
8579  C CG  . LEU A 1189 ? 0.4052 0.3797 0.4070 -0.0076 -0.0295 -0.0324 1187 LEU A CG  
8580  C CD1 . LEU A 1189 ? 0.4047 0.3748 0.4107 -0.0104 -0.0287 -0.0292 1187 LEU A CD1 
8581  C CD2 . LEU A 1189 ? 0.4269 0.4009 0.4232 -0.0042 -0.0290 -0.0342 1187 LEU A CD2 
8582  N N   . LEU A 1190 ? 0.3817 0.3709 0.3844 -0.0095 -0.0296 -0.0299 1188 LEU A N   
8583  C CA  . LEU A 1190 ? 0.3883 0.3821 0.3884 -0.0082 -0.0293 -0.0294 1188 LEU A CA  
8584  C C   . LEU A 1190 ? 0.3944 0.3899 0.3885 -0.0045 -0.0300 -0.0315 1188 LEU A C   
8585  O O   . LEU A 1190 ? 0.3706 0.3661 0.3645 -0.0033 -0.0319 -0.0353 1188 LEU A O   
8586  C CB  . LEU A 1190 ? 0.3324 0.3301 0.3381 -0.0102 -0.0310 -0.0310 1188 LEU A CB  
8587  C CG  . LEU A 1190 ? 0.3687 0.3662 0.3809 -0.0142 -0.0305 -0.0287 1188 LEU A CG  
8588  C CD1 . LEU A 1190 ? 0.3878 0.3907 0.4043 -0.0155 -0.0318 -0.0299 1188 LEU A CD1 
8589  C CD2 . LEU A 1190 ? 0.3636 0.3599 0.3739 -0.0149 -0.0275 -0.0240 1188 LEU A CD2 
8590  N N   . LEU A 1191 ? 0.3315 0.3284 0.3207 -0.0027 -0.0285 -0.0291 1189 LEU A N   
8591  C CA  . LEU A 1191 ? 0.3678 0.3672 0.3516 0.0006  -0.0293 -0.0305 1189 LEU A CA  
8592  C C   . LEU A 1191 ? 0.3680 0.3722 0.3539 0.0009  -0.0314 -0.0328 1189 LEU A C   
8593  O O   . LEU A 1191 ? 0.3631 0.3696 0.3506 0.0001  -0.0310 -0.0312 1189 LEU A O   
8594  C CB  . LEU A 1191 ? 0.3371 0.3359 0.3156 0.0022  -0.0271 -0.0268 1189 LEU A CB  
8595  C CG  . LEU A 1191 ? 0.3600 0.3599 0.3320 0.0055  -0.0273 -0.0269 1189 LEU A CG  
8596  C CD1 . LEU A 1191 ? 0.3675 0.3654 0.3356 0.0063  -0.0249 -0.0227 1189 LEU A CD1 
8597  C CD2 . LEU A 1191 ? 0.3323 0.3369 0.3033 0.0073  -0.0293 -0.0287 1189 LEU A CD2 
8598  N N   . VAL A 1192 ? 0.3611 0.3670 0.3471 0.0020  -0.0338 -0.0370 1190 VAL A N   
8599  C CA  . VAL A 1192 ? 0.3321 0.3427 0.3207 0.0022  -0.0363 -0.0400 1190 VAL A CA  
8600  C C   . VAL A 1192 ? 0.3403 0.3544 0.3230 0.0058  -0.0372 -0.0406 1190 VAL A C   
8601  O O   . VAL A 1192 ? 0.3374 0.3508 0.3150 0.0080  -0.0371 -0.0412 1190 VAL A O   
8602  C CB  . VAL A 1192 ? 0.2917 0.3019 0.2851 0.0009  -0.0387 -0.0444 1190 VAL A CB  
8603  C CG1 . VAL A 1192 ? 0.3251 0.3405 0.3216 0.0010  -0.0414 -0.0477 1190 VAL A CG1 
8604  C CG2 . VAL A 1192 ? 0.3526 0.3589 0.3522 -0.0028 -0.0379 -0.0432 1190 VAL A CG2 
8605  N N   . GLN A 1193 ? 0.2949 0.3131 0.2783 0.0063  -0.0381 -0.0405 1191 GLN A N   
8606  C CA  . GLN A 1193 ? 0.2998 0.3218 0.2784 0.0096  -0.0395 -0.0413 1191 GLN A CA  
8607  C C   . GLN A 1193 ? 0.2889 0.3157 0.2713 0.0095  -0.0425 -0.0452 1191 GLN A C   
8608  O O   . GLN A 1193 ? 0.2872 0.3155 0.2755 0.0072  -0.0429 -0.0454 1191 GLN A O   
8609  C CB  . GLN A 1193 ? 0.3045 0.3271 0.2800 0.0109  -0.0382 -0.0373 1191 GLN A CB  
8610  C CG  . GLN A 1193 ? 0.2908 0.3092 0.2620 0.0114  -0.0356 -0.0335 1191 GLN A CG  
8611  C CD  . GLN A 1193 ? 0.3326 0.3516 0.3008 0.0131  -0.0348 -0.0301 1191 GLN A CD  
8612  O OE1 . GLN A 1193 ? 0.3379 0.3591 0.3018 0.0158  -0.0359 -0.0297 1191 GLN A OE1 
8613  N NE2 . GLN A 1193 ? 0.2980 0.3154 0.2688 0.0116  -0.0331 -0.0276 1191 GLN A NE2 
8614  N N   . ALA A 1194 ? 0.2925 0.3224 0.2716 0.0120  -0.0446 -0.0481 1192 ALA A N   
8615  C CA  . ALA A 1194 ? 0.2948 0.3294 0.2775 0.0120  -0.0477 -0.0523 1192 ALA A CA  
8616  C C   . ALA A 1194 ? 0.3209 0.3603 0.2985 0.0155  -0.0493 -0.0526 1192 ALA A C   
8617  O O   . ALA A 1194 ? 0.3006 0.3395 0.2714 0.0180  -0.0485 -0.0507 1192 ALA A O   
8618  C CB  . ALA A 1194 ? 0.2999 0.3338 0.2849 0.0113  -0.0494 -0.0570 1192 ALA A CB  
8619  N N   . ALA A 1195 ? 0.2978 0.3418 0.2787 0.0155  -0.0515 -0.0547 1193 ALA A N   
8620  C CA  . ALA A 1195 ? 0.3038 0.3529 0.2807 0.0188  -0.0536 -0.0552 1193 ALA A CA  
8621  C C   . ALA A 1195 ? 0.3514 0.4057 0.3333 0.0183  -0.0568 -0.0599 1193 ALA A C   
8622  O O   . ALA A 1195 ? 0.3229 0.3771 0.3119 0.0153  -0.0570 -0.0611 1193 ALA A O   
8623  C CB  . ALA A 1195 ? 0.3199 0.3693 0.2946 0.0201  -0.0524 -0.0507 1193 ALA A CB  
8624  N N   . SER A 1196 ? 0.3062 0.3651 0.2843 0.0212  -0.0593 -0.0623 1194 SER A N   
8625  C CA  . SER A 1196 ? 0.3423 0.4068 0.3248 0.0212  -0.0626 -0.0664 1194 SER A CA  
8626  C C   . SER A 1196 ? 0.3312 0.3987 0.3156 0.0216  -0.0628 -0.0640 1194 SER A C   
8627  O O   . SER A 1196 ? 0.3119 0.3776 0.2930 0.0228  -0.0609 -0.0594 1194 SER A O   
8628  C CB  . SER A 1196 ? 0.3886 0.4578 0.3662 0.0244  -0.0653 -0.0698 1194 SER A CB  
8629  O OG  . SER A 1196 ? 0.3734 0.4444 0.3439 0.0278  -0.0651 -0.0662 1194 SER A OG  
8630  N N   . SER A 1197 ? 0.3629 0.4352 0.3531 0.0207  -0.0652 -0.0673 1195 SER A N   
8631  C CA  . SER A 1197 ? 0.3594 0.4356 0.3514 0.0216  -0.0659 -0.0657 1195 SER A CA  
8632  C C   . SER A 1197 ? 0.3603 0.4389 0.3449 0.0259  -0.0669 -0.0637 1195 SER A C   
8633  O O   . SER A 1197 ? 0.3058 0.3845 0.2893 0.0273  -0.0661 -0.0601 1195 SER A O   
8634  C CB  . SER A 1197 ? 0.3677 0.4496 0.3669 0.0202  -0.0688 -0.0701 1195 SER A CB  
8635  O OG  . SER A 1197 ? 0.3743 0.4540 0.3808 0.0159  -0.0678 -0.0712 1195 SER A OG  
8636  N N   . GLY A 1198 ? 0.3584 0.4391 0.3381 0.0282  -0.0688 -0.0660 1196 GLY A N   
8637  C CA  . GLY A 1198 ? 0.3479 0.4312 0.3205 0.0323  -0.0700 -0.0638 1196 GLY A CA  
8638  C C   . GLY A 1198 ? 0.3667 0.4450 0.3334 0.0333  -0.0671 -0.0583 1196 GLY A C   
8639  O O   . GLY A 1198 ? 0.3246 0.4036 0.2878 0.0358  -0.0673 -0.0546 1196 GLY A O   
8640  N N   . GLU A 1199 ? 0.3163 0.3894 0.2821 0.0315  -0.0645 -0.0576 1197 GLU A N   
8641  C CA  . GLU A 1199 ? 0.3299 0.3979 0.2907 0.0321  -0.0616 -0.0523 1197 GLU A CA  
8642  C C   . GLU A 1199 ? 0.3827 0.4480 0.3465 0.0312  -0.0599 -0.0486 1197 GLU A C   
8643  O O   . GLU A 1199 ? 0.3221 0.3853 0.2820 0.0328  -0.0588 -0.0442 1197 GLU A O   
8644  C CB  . GLU A 1199 ? 0.3445 0.4077 0.3047 0.0301  -0.0593 -0.0528 1197 GLU A CB  
8645  C CG  . GLU A 1199 ? 0.4251 0.4837 0.3796 0.0309  -0.0565 -0.0478 1197 GLU A CG  
8646  C CD  . GLU A 1199 ? 0.4882 0.5494 0.4349 0.0341  -0.0573 -0.0467 1197 GLU A CD  
8647  O OE1 . GLU A 1199 ? 0.4733 0.5401 0.4185 0.0360  -0.0601 -0.0498 1197 GLU A OE1 
8648  O OE2 . GLU A 1199 ? 0.6000 0.6580 0.5419 0.0347  -0.0551 -0.0428 1197 GLU A OE2 
8649  N N   . ILE A 1200 ? 0.3210 0.3867 0.2922 0.0284  -0.0597 -0.0504 1198 ILE A N   
8650  C CA  . ILE A 1200 ? 0.3156 0.3800 0.2899 0.0278  -0.0582 -0.0474 1198 ILE A CA  
8651  C C   . ILE A 1200 ? 0.3079 0.3763 0.2807 0.0310  -0.0603 -0.0462 1198 ILE A C   
8652  O O   . ILE A 1200 ? 0.3413 0.4076 0.3131 0.0321  -0.0592 -0.0425 1198 ILE A O   
8653  C CB  . ILE A 1200 ? 0.3268 0.3919 0.3092 0.0242  -0.0577 -0.0497 1198 ILE A CB  
8654  C CG1 . ILE A 1200 ? 0.2948 0.3548 0.2786 0.0210  -0.0553 -0.0497 1198 ILE A CG1 
8655  C CG2 . ILE A 1200 ? 0.3027 0.3687 0.2887 0.0240  -0.0566 -0.0474 1198 ILE A CG2 
8656  C CD1 . ILE A 1200 ? 0.2925 0.3532 0.2843 0.0172  -0.0549 -0.0515 1198 ILE A CD1 
8657  N N   . ALA A 1201 ? 0.3146 0.3886 0.2875 0.0326  -0.0635 -0.0494 1199 ALA A N   
8658  C CA  . ALA A 1201 ? 0.3356 0.4137 0.3074 0.0358  -0.0659 -0.0483 1199 ALA A CA  
8659  C C   . ALA A 1201 ? 0.3287 0.4049 0.2924 0.0390  -0.0660 -0.0443 1199 ALA A C   
8660  O O   . ALA A 1201 ? 0.3213 0.3975 0.2838 0.0413  -0.0665 -0.0412 1199 ALA A O   
8661  C CB  . ALA A 1201 ? 0.3235 0.4085 0.2978 0.0366  -0.0694 -0.0530 1199 ALA A CB  
8662  N N   . ARG A 1202 ? 0.3130 0.3879 0.2715 0.0393  -0.0655 -0.0443 1200 ARG A N   
8663  C CA  . ARG A 1202 ? 0.3502 0.4246 0.3009 0.0422  -0.0658 -0.0406 1200 ARG A CA  
8664  C C   . ARG A 1202 ? 0.3686 0.4364 0.3165 0.0417  -0.0626 -0.0356 1200 ARG A C   
8665  O O   . ARG A 1202 ? 0.3762 0.4428 0.3203 0.0439  -0.0629 -0.0313 1200 ARG A O   
8666  C CB  . ARG A 1202 ? 0.3208 0.3980 0.2670 0.0429  -0.0668 -0.0432 1200 ARG A CB  
8667  C CG  . ARG A 1202 ? 0.3621 0.4466 0.3093 0.0444  -0.0705 -0.0477 1200 ARG A CG  
8668  C CD  . ARG A 1202 ? 0.3651 0.4526 0.3067 0.0457  -0.0714 -0.0499 1200 ARG A CD  
8669  N NE  . ARG A 1202 ? 0.3349 0.4190 0.2779 0.0430  -0.0693 -0.0523 1200 ARG A NE  
8670  C CZ  . ARG A 1202 ? 0.3641 0.4495 0.3121 0.0411  -0.0703 -0.0579 1200 ARG A CZ  
8671  N NH1 . ARG A 1202 ? 0.3302 0.4212 0.2818 0.0415  -0.0734 -0.0621 1200 ARG A NH1 
8672  N NH2 . ARG A 1202 ? 0.3696 0.4507 0.3192 0.0386  -0.0681 -0.0593 1200 ARG A NH2 
8673  N N   . ASN A 1203 ? 0.3508 0.4142 0.3007 0.0388  -0.0598 -0.0360 1201 ASN A N   
8674  C CA  . ASN A 1203 ? 0.3583 0.4158 0.3049 0.0382  -0.0568 -0.0318 1201 ASN A CA  
8675  C C   . ASN A 1203 ? 0.4187 0.4720 0.3700 0.0363  -0.0547 -0.0300 1201 ASN A C   
8676  O O   . ASN A 1203 ? 0.3694 0.4218 0.3257 0.0335  -0.0535 -0.0325 1201 ASN A O   
8677  C CB  . ASN A 1203 ? 0.3552 0.4110 0.2996 0.0366  -0.0552 -0.0334 1201 ASN A CB  
8678  C CG  . ASN A 1203 ? 0.4273 0.4776 0.3683 0.0361  -0.0522 -0.0292 1201 ASN A CG  
8679  O OD1 . ASN A 1203 ? 0.3930 0.4405 0.3328 0.0369  -0.0514 -0.0249 1201 ASN A OD1 
8680  N ND2 . ASN A 1203 ? 0.4634 0.5119 0.4030 0.0347  -0.0506 -0.0306 1201 ASN A ND2 
8681  N N   . PRO A 1204 ? 0.3940 0.4447 0.3439 0.0377  -0.0543 -0.0258 1202 PRO A N   
8682  C CA  . PRO A 1204 ? 0.3786 0.4256 0.3327 0.0361  -0.0522 -0.0244 1202 PRO A CA  
8683  C C   . PRO A 1204 ? 0.3959 0.4380 0.3499 0.0333  -0.0490 -0.0238 1202 PRO A C   
8684  O O   . PRO A 1204 ? 0.3905 0.4305 0.3488 0.0313  -0.0472 -0.0239 1202 PRO A O   
8685  C CB  . PRO A 1204 ? 0.4087 0.4535 0.3603 0.0386  -0.0527 -0.0201 1202 PRO A CB  
8686  C CG  . PRO A 1204 ? 0.4711 0.5171 0.4162 0.0409  -0.0541 -0.0180 1202 PRO A CG  
8687  C CD  . PRO A 1204 ? 0.3737 0.4250 0.3185 0.0409  -0.0559 -0.0223 1202 PRO A CD  
8688  N N   . ASP A 1205 ? 0.3805 0.4211 0.3298 0.0333  -0.0481 -0.0231 1203 ASP A N   
8689  C CA  . ASP A 1205 ? 0.3973 0.4336 0.3464 0.0308  -0.0453 -0.0227 1203 ASP A CA  
8690  C C   . ASP A 1205 ? 0.3943 0.4322 0.3454 0.0290  -0.0455 -0.0271 1203 ASP A C   
8691  O O   . ASP A 1205 ? 0.3853 0.4205 0.3346 0.0278  -0.0437 -0.0271 1203 ASP A O   
8692  C CB  . ASP A 1205 ? 0.4103 0.4436 0.3532 0.0320  -0.0440 -0.0189 1203 ASP A CB  
8693  C CG  . ASP A 1205 ? 0.4486 0.4800 0.3898 0.0338  -0.0443 -0.0144 1203 ASP A CG  
8694  O OD1 . ASP A 1205 ? 0.4635 0.4926 0.4084 0.0331  -0.0435 -0.0135 1203 ASP A OD1 
8695  O OD2 . ASP A 1205 ? 0.5371 0.5694 0.4733 0.0359  -0.0453 -0.0118 1203 ASP A OD2 
8696  N N   . ALA A 1206 ? 0.3262 0.3686 0.2811 0.0289  -0.0477 -0.0309 1204 ALA A N   
8697  C CA  . ALA A 1206 ? 0.3281 0.3717 0.2860 0.0269  -0.0481 -0.0352 1204 ALA A CA  
8698  C C   . ALA A 1206 ? 0.3789 0.4177 0.3397 0.0238  -0.0454 -0.0348 1204 ALA A C   
8699  O O   . ALA A 1206 ? 0.3233 0.3605 0.2835 0.0227  -0.0448 -0.0365 1204 ALA A O   
8700  C CB  . ALA A 1206 ? 0.3047 0.3531 0.2681 0.0264  -0.0505 -0.0389 1204 ALA A CB  
8701  N N   . TYR A 1207 ? 0.3415 0.3782 0.3055 0.0224  -0.0438 -0.0326 1205 TYR A N   
8702  C CA  . TYR A 1207 ? 0.2867 0.3187 0.2527 0.0198  -0.0410 -0.0312 1205 TYR A CA  
8703  C C   . TYR A 1207 ? 0.3734 0.4016 0.3352 0.0209  -0.0391 -0.0268 1205 TYR A C   
8704  O O   . TYR A 1207 ? 0.4031 0.4321 0.3633 0.0229  -0.0397 -0.0247 1205 TYR A O   
8705  C CB  . TYR A 1207 ? 0.3237 0.3567 0.2965 0.0172  -0.0405 -0.0320 1205 TYR A CB  
8706  C CG  . TYR A 1207 ? 0.3116 0.3482 0.2891 0.0158  -0.0425 -0.0362 1205 TYR A CG  
8707  C CD1 . TYR A 1207 ? 0.3263 0.3615 0.3048 0.0142  -0.0427 -0.0387 1205 TYR A CD1 
8708  C CD2 . TYR A 1207 ? 0.3332 0.3750 0.3144 0.0162  -0.0444 -0.0379 1205 TYR A CD2 
8709  C CE1 . TYR A 1207 ? 0.2868 0.3250 0.2701 0.0128  -0.0448 -0.0427 1205 TYR A CE1 
8710  C CE2 . TYR A 1207 ? 0.3128 0.3582 0.2987 0.0147  -0.0464 -0.0418 1205 TYR A CE2 
8711  C CZ  . TYR A 1207 ? 0.2903 0.3337 0.2773 0.0129  -0.0466 -0.0442 1205 TYR A CZ  
8712  O OH  . TYR A 1207 ? 0.2882 0.3347 0.2803 0.0114  -0.0488 -0.0482 1205 TYR A OH  
8713  N N   . CYS A 1208 ? 0.2980 0.3220 0.2581 0.0197  -0.0369 -0.0254 1206 CYS A N   
8714  C CA  . CYS A 1208 ? 0.3343 0.3546 0.2905 0.0205  -0.0351 -0.0213 1206 CYS A CA  
8715  C C   . CYS A 1208 ? 0.3174 0.3347 0.2772 0.0184  -0.0329 -0.0197 1206 CYS A C   
8716  O O   . CYS A 1208 ? 0.3054 0.3214 0.2685 0.0158  -0.0318 -0.0209 1206 CYS A O   
8717  C CB  . CYS A 1208 ? 0.3781 0.3963 0.3298 0.0209  -0.0341 -0.0206 1206 CYS A CB  
8718  S SG  . CYS A 1208 ? 0.4080 0.4215 0.3555 0.0214  -0.0317 -0.0155 1206 CYS A SG  
8719  N N   . LEU A 1209 ? 0.2794 0.2958 0.2387 0.0195  -0.0325 -0.0170 1207 LEU A N   
8720  C CA  . LEU A 1209 ? 0.2758 0.2902 0.2384 0.0177  -0.0307 -0.0158 1207 LEU A CA  
8721  C C   . LEU A 1209 ? 0.2842 0.2938 0.2448 0.0165  -0.0282 -0.0134 1207 LEU A C   
8722  O O   . LEU A 1209 ? 0.2795 0.2876 0.2428 0.0147  -0.0265 -0.0127 1207 LEU A O   
8723  C CB  . LEU A 1209 ? 0.2756 0.2910 0.2388 0.0196  -0.0313 -0.0143 1207 LEU A CB  
8724  C CG  . LEU A 1209 ? 0.2768 0.2972 0.2425 0.0210  -0.0338 -0.0165 1207 LEU A CG  
8725  C CD1 . LEU A 1209 ? 0.2874 0.3081 0.2542 0.0227  -0.0342 -0.0150 1207 LEU A CD1 
8726  C CD2 . LEU A 1209 ? 0.2750 0.2989 0.2459 0.0187  -0.0340 -0.0196 1207 LEU A CD2 
8727  N N   . ASN A 1210 ? 0.2849 0.2925 0.2408 0.0175  -0.0279 -0.0122 1208 ASN A N   
8728  C CA  . ASN A 1210 ? 0.2964 0.2998 0.2508 0.0162  -0.0256 -0.0103 1208 ASN A CA  
8729  C C   . ASN A 1210 ? 0.3051 0.3077 0.2632 0.0135  -0.0245 -0.0122 1208 ASN A C   
8730  O O   . ASN A 1210 ? 0.2888 0.2885 0.2478 0.0119  -0.0226 -0.0106 1208 ASN A O   
8731  C CB  . ASN A 1210 ? 0.3247 0.3273 0.2740 0.0175  -0.0255 -0.0094 1208 ASN A CB  
8732  C CG  . ASN A 1210 ? 0.4347 0.4377 0.3800 0.0200  -0.0264 -0.0067 1208 ASN A CG  
8733  O OD1 . ASN A 1210 ? 0.4969 0.5004 0.4432 0.0210  -0.0273 -0.0057 1208 ASN A OD1 
8734  N ND2 . ASN A 1210 ? 0.5011 0.5042 0.4418 0.0210  -0.0262 -0.0056 1208 ASN A ND2 
8735  N N   . TRP A 1211 ? 0.2783 0.2835 0.2386 0.0129  -0.0260 -0.0154 1209 TRP A N   
8736  C CA  . TRP A 1211 ? 0.3107 0.3147 0.2745 0.0103  -0.0253 -0.0170 1209 TRP A CA  
8737  C C   . TRP A 1211 ? 0.3061 0.3116 0.2755 0.0081  -0.0251 -0.0176 1209 TRP A C   
8738  O O   . TRP A 1211 ? 0.3604 0.3653 0.3335 0.0058  -0.0249 -0.0188 1209 TRP A O   
8739  C CB  . TRP A 1211 ? 0.3068 0.3123 0.2704 0.0107  -0.0269 -0.0204 1209 TRP A CB  
8740  C CG  . TRP A 1211 ? 0.3099 0.3161 0.2677 0.0133  -0.0275 -0.0202 1209 TRP A CG  
8741  C CD1 . TRP A 1211 ? 0.3552 0.3652 0.3111 0.0153  -0.0297 -0.0223 1209 TRP A CD1 
8742  C CD2 . TRP A 1211 ? 0.3306 0.3342 0.2838 0.0143  -0.0259 -0.0174 1209 TRP A CD2 
8743  N NE1 . TRP A 1211 ? 0.3538 0.3639 0.3040 0.0174  -0.0295 -0.0209 1209 TRP A NE1 
8744  C CE2 . TRP A 1211 ? 0.3187 0.3249 0.2673 0.0168  -0.0271 -0.0178 1209 TRP A CE2 
8745  C CE3 . TRP A 1211 ? 0.3364 0.3360 0.2890 0.0133  -0.0236 -0.0146 1209 TRP A CE3 
8746  C CZ2 . TRP A 1211 ? 0.3379 0.3430 0.2815 0.0181  -0.0260 -0.0154 1209 TRP A CZ2 
8747  C CZ3 . TRP A 1211 ? 0.3272 0.3255 0.2750 0.0146  -0.0225 -0.0124 1209 TRP A CZ3 
8748  C CH2 . TRP A 1211 ? 0.2986 0.2997 0.2421 0.0169  -0.0236 -0.0127 1209 TRP A CH2 
8749  N N   . LEU A 1212 ? 0.2690 0.2766 0.2394 0.0088  -0.0253 -0.0166 1210 LEU A N   
8750  C CA  . LEU A 1212 ? 0.2666 0.2767 0.2422 0.0069  -0.0250 -0.0170 1210 LEU A CA  
8751  C C   . LEU A 1212 ? 0.2639 0.2724 0.2398 0.0063  -0.0229 -0.0143 1210 LEU A C   
8752  O O   . LEU A 1212 ? 0.2620 0.2731 0.2417 0.0049  -0.0224 -0.0144 1210 LEU A O   
8753  C CB  . LEU A 1212 ? 0.2701 0.2852 0.2476 0.0082  -0.0270 -0.0188 1210 LEU A CB  
8754  C CG  . LEU A 1212 ? 0.2698 0.2875 0.2488 0.0081  -0.0292 -0.0220 1210 LEU A CG  
8755  C CD1 . LEU A 1212 ? 0.3012 0.3237 0.2807 0.0102  -0.0314 -0.0236 1210 LEU A CD1 
8756  C CD2 . LEU A 1212 ? 0.2687 0.2871 0.2533 0.0047  -0.0289 -0.0234 1210 LEU A CD2 
8757  N N   . VAL A 1213 ? 0.2639 0.2685 0.2357 0.0073  -0.0217 -0.0121 1211 VAL A N   
8758  C CA  . VAL A 1213 ? 0.2801 0.2828 0.2521 0.0066  -0.0197 -0.0097 1211 VAL A CA  
8759  C C   . VAL A 1213 ? 0.2854 0.2841 0.2563 0.0050  -0.0181 -0.0086 1211 VAL A C   
8760  O O   . VAL A 1213 ? 0.2656 0.2628 0.2349 0.0051  -0.0185 -0.0094 1211 VAL A O   
8761  C CB  . VAL A 1213 ? 0.2940 0.2953 0.2627 0.0092  -0.0197 -0.0079 1211 VAL A CB  
8762  C CG1 . VAL A 1213 ? 0.3204 0.3256 0.2907 0.0109  -0.0214 -0.0091 1211 VAL A CG1 
8763  C CG2 . VAL A 1213 ? 0.2645 0.2630 0.2283 0.0108  -0.0201 -0.0068 1211 VAL A CG2 
8764  N N   . GLU A 1214 ? 0.2789 0.2762 0.2507 0.0038  -0.0163 -0.0068 1212 GLU A N   
8765  C CA  . GLU A 1214 ? 0.3244 0.3182 0.2956 0.0022  -0.0147 -0.0054 1212 GLU A CA  
8766  C C   . GLU A 1214 ? 0.2573 0.2481 0.2251 0.0034  -0.0135 -0.0031 1212 GLU A C   
8767  O O   . GLU A 1214 ? 0.2562 0.2480 0.2244 0.0041  -0.0132 -0.0023 1212 GLU A O   
8768  C CB  . GLU A 1214 ? 0.2898 0.2847 0.2652 -0.0006 -0.0136 -0.0050 1212 GLU A CB  
8769  N N   . GLU A 1215 ? 0.2708 0.2583 0.2355 0.0038  -0.0130 -0.0022 1213 GLU A N   
8770  C CA  . GLU A 1215 ? 0.2733 0.2579 0.2351 0.0046  -0.0118 0.0001  1213 GLU A CA  
8771  C C   . GLU A 1215 ? 0.2668 0.2498 0.2301 0.0027  -0.0101 0.0014  1213 GLU A C   
8772  O O   . GLU A 1215 ? 0.2794 0.2618 0.2444 0.0010  -0.0097 0.0010  1213 GLU A O   
8773  C CB  . GLU A 1215 ? 0.2613 0.2438 0.2194 0.0057  -0.0119 0.0006  1213 GLU A CB  
8774  C CG  . GLU A 1215 ? 0.2630 0.2472 0.2188 0.0078  -0.0135 -0.0004 1213 GLU A CG  
8775  C CD  . GLU A 1215 ? 0.2648 0.2480 0.2173 0.0085  -0.0134 -0.0003 1213 GLU A CD  
8776  O OE1 . GLU A 1215 ? 0.2901 0.2737 0.2435 0.0078  -0.0137 -0.0023 1213 GLU A OE1 
8777  O OE2 . GLU A 1215 ? 0.2695 0.2516 0.2186 0.0098  -0.0131 0.0017  1213 GLU A OE2 
8778  N N   . VAL A 1216 ? 0.2545 0.2368 0.2174 0.0030  -0.0093 0.0029  1214 VAL A N   
8779  C CA  . VAL A 1216 ? 0.2525 0.2335 0.2164 0.0015  -0.0076 0.0043  1214 VAL A CA  
8780  C C   . VAL A 1216 ? 0.2553 0.2332 0.2162 0.0025  -0.0069 0.0061  1214 VAL A C   
8781  O O   . VAL A 1216 ? 0.2535 0.2313 0.2133 0.0042  -0.0075 0.0065  1214 VAL A O   
8782  C CB  . VAL A 1216 ? 0.2696 0.2538 0.2365 0.0005  -0.0072 0.0040  1214 VAL A CB  
8783  C CG1 . VAL A 1216 ? 0.2957 0.2789 0.2631 -0.0010 -0.0056 0.0056  1214 VAL A CG1 
8784  C CG2 . VAL A 1216 ? 0.2975 0.2849 0.2676 -0.0009 -0.0079 0.0025  1214 VAL A CG2 
8785  N N   . SER A 1217 ? 0.2611 0.2367 0.2214 0.0015  -0.0057 0.0073  1215 SER A N   
8786  C CA  . SER A 1217 ? 0.2694 0.2423 0.2275 0.0021  -0.0049 0.0091  1215 SER A CA  
8787  C C   . SER A 1217 ? 0.2732 0.2460 0.2330 0.0007  -0.0037 0.0100  1215 SER A C   
8788  O O   . SER A 1217 ? 0.2549 0.2285 0.2165 -0.0010 -0.0031 0.0098  1215 SER A O   
8789  C CB  . SER A 1217 ? 0.2759 0.2466 0.2317 0.0022  -0.0045 0.0097  1215 SER A CB  
8790  O OG  . SER A 1217 ? 0.3326 0.3011 0.2872 0.0021  -0.0034 0.0115  1215 SER A OG  
8791  N N   . ALA A 1218 ? 0.2541 0.2264 0.2135 0.0013  -0.0034 0.0108  1216 ALA A N   
8792  C CA  . ALA A 1218 ? 0.2661 0.2385 0.2266 0.0002  -0.0023 0.0115  1216 ALA A CA  
8793  C C   . ALA A 1218 ? 0.2482 0.2177 0.2069 0.0007  -0.0018 0.0130  1216 ALA A C   
8794  O O   . ALA A 1218 ? 0.2605 0.2287 0.2181 0.0021  -0.0026 0.0133  1216 ALA A O   
8795  C CB  . ALA A 1218 ? 0.2487 0.2243 0.2111 0.0005  -0.0026 0.0104  1216 ALA A CB  
8796  N N   . SER A 1219 ? 0.2588 0.2271 0.2175 -0.0005 -0.0007 0.0140  1217 SER A N   
8797  C CA  . SER A 1219 ? 0.2559 0.2216 0.2132 -0.0002 -0.0002 0.0154  1217 SER A CA  
8798  C C   . SER A 1219 ? 0.2560 0.2226 0.2146 -0.0011 0.0005  0.0157  1217 SER A C   
8799  O O   . SER A 1219 ? 0.2782 0.2459 0.2378 -0.0024 0.0012  0.0159  1217 SER A O   
8800  C CB  . SER A 1219 ? 0.2756 0.2395 0.2316 -0.0006 0.0005  0.0164  1217 SER A CB  
8801  O OG  . SER A 1219 ? 0.2809 0.2429 0.2359 -0.0005 0.0010  0.0178  1217 SER A OG  
8802  N N   . ILE A 1220 ? 0.2517 0.2180 0.2105 -0.0003 0.0001  0.0155  1218 ILE A N   
8803  C CA  . ILE A 1220 ? 0.2682 0.2359 0.2282 -0.0008 0.0006  0.0152  1218 ILE A CA  
8804  C C   . ILE A 1220 ? 0.2522 0.2173 0.2115 -0.0008 0.0009  0.0164  1218 ILE A C   
8805  O O   . ILE A 1220 ? 0.2891 0.2518 0.2479 0.0001  0.0002  0.0168  1218 ILE A O   
8806  C CB  . ILE A 1220 ? 0.2654 0.2355 0.2268 0.0003  -0.0003 0.0134  1218 ILE A CB  
8807  C CG1 . ILE A 1220 ? 0.3482 0.3215 0.3106 0.0003  -0.0006 0.0122  1218 ILE A CG1 
8808  C CG2 . ILE A 1220 ? 0.3034 0.2757 0.2659 -0.0001 0.0002  0.0128  1218 ILE A CG2 
8809  C CD1 . ILE A 1220 ? 0.3705 0.3430 0.3325 0.0018  -0.0019 0.0115  1218 ILE A CD1 
8810  N N   . ASN A 1221 ? 0.2872 0.2528 0.2468 -0.0020 0.0018  0.0171  1219 ASN A N   
8811  C CA  . ASN A 1221 ? 0.2961 0.2599 0.2555 -0.0022 0.0021  0.0180  1219 ASN A CA  
8812  C C   . ASN A 1221 ? 0.3146 0.2795 0.2752 -0.0016 0.0015  0.0167  1219 ASN A C   
8813  O O   . ASN A 1221 ? 0.3367 0.3047 0.2981 -0.0020 0.0018  0.0158  1219 ASN A O   
8814  C CB  . ASN A 1221 ? 0.3048 0.2689 0.2641 -0.0035 0.0032  0.0191  1219 ASN A CB  
8815  C CG  . ASN A 1221 ? 0.3349 0.2978 0.2943 -0.0038 0.0035  0.0200  1219 ASN A CG  
8816  O OD1 . ASN A 1221 ? 0.3090 0.2702 0.2684 -0.0032 0.0029  0.0200  1219 ASN A OD1 
8817  N ND2 . ASN A 1221 ? 0.3377 0.3013 0.2973 -0.0047 0.0042  0.0208  1219 ASN A ND2 
8818  N N   . THR A 1222 ? 0.3077 0.2703 0.2685 -0.0006 0.0005  0.0165  1220 THR A N   
8819  C CA  . THR A 1222 ? 0.3487 0.3119 0.3111 0.0002  -0.0005 0.0149  1220 THR A CA  
8820  C C   . THR A 1222 ? 0.4216 0.3833 0.3846 -0.0004 -0.0004 0.0154  1220 THR A C   
8821  O O   . THR A 1222 ? 0.3902 0.3518 0.3547 0.0003  -0.0014 0.0140  1220 THR A O   
8822  C CB  . THR A 1222 ? 0.3804 0.3417 0.3434 0.0017  -0.0020 0.0142  1220 THR A CB  
8823  O OG1 . THR A 1222 ? 0.3299 0.2875 0.2920 0.0016  -0.0022 0.0164  1220 THR A OG1 
8824  C CG2 . THR A 1222 ? 0.3486 0.3121 0.3114 0.0024  -0.0022 0.0133  1220 THR A CG2 
8825  N N   . ALA A 1223 ? 0.3187 0.2793 0.2807 -0.0015 0.0007  0.0173  1221 ALA A N   
8826  C CA  . ALA A 1223 ? 0.3907 0.3509 0.3534 -0.0022 0.0009  0.0177  1221 ALA A CA  
8827  C C   . ALA A 1223 ? 0.5216 0.4851 0.4842 -0.0029 0.0016  0.0172  1221 ALA A C   
8828  O O   . ALA A 1223 ? 0.6217 0.5856 0.5850 -0.0034 0.0017  0.0173  1221 ALA A O   
8829  C CB  . ALA A 1223 ? 0.3617 0.3193 0.3236 -0.0029 0.0015  0.0201  1221 ALA A CB  
8830  N N   . ALA A 1224 ? 0.7130 0.6793 0.6751 -0.0030 0.0021  0.0168  1222 ALA A N   
8831  C CA  . ALA A 1224 ? 0.7132 0.6831 0.6753 -0.0040 0.0030  0.0170  1222 ALA A CA  
8832  C C   . ALA A 1224 ? 0.8341 0.8075 0.7970 -0.0037 0.0026  0.0153  1222 ALA A C   
8833  O O   . ALA A 1224 ? 0.8759 0.8529 0.8384 -0.0045 0.0033  0.0157  1222 ALA A O   
8834  C CB  . ALA A 1224 ? 0.6372 0.6089 0.5990 -0.0042 0.0033  0.0171  1222 ALA A CB  
8835  N N   . ALA A 1225 ? 0.7256 0.6982 0.6894 -0.0027 0.0016  0.0135  1223 ALA A N   
8836  C CA  . ALA A 1225 ? 0.7244 0.7006 0.6890 -0.0024 0.0011  0.0116  1223 ALA A CA  
8837  C C   . ALA A 1225 ? 0.7697 0.7430 0.7355 -0.0021 0.0001  0.0110  1223 ALA A C   
8838  O O   . ALA A 1225 ? 0.8337 0.8060 0.7993 -0.0030 0.0005  0.0123  1223 ALA A O   
8839  C CB  . ALA A 1225 ? 0.6027 0.5825 0.5681 -0.0012 0.0005  0.0089  1223 ALA A CB  
8840  N N   . ALA B 16   ? 0.7269 0.5456 0.6443 0.1379  -0.1154 -0.0979 14   ALA B N   
8841  C CA  . ALA B 16   ? 0.7884 0.6165 0.7108 0.1274  -0.1104 -0.0933 14   ALA B CA  
8842  C C   . ALA B 16   ? 0.8303 0.6429 0.7424 0.1187  -0.1134 -0.0903 14   ALA B C   
8843  O O   . ALA B 16   ? 0.8660 0.6675 0.7696 0.1204  -0.1158 -0.0933 14   ALA B O   
8844  C CB  . ALA B 16   ? 0.7217 0.5685 0.6528 0.1284  -0.1027 -0.0953 14   ALA B CB  
8845  N N   . PRO B 17   ? 0.7595 0.5717 0.6723 0.1094  -0.1133 -0.0846 15   PRO B N   
8846  C CA  . PRO B 17   ? 0.7291 0.5287 0.6331 0.1003  -0.1158 -0.0812 15   PRO B CA  
8847  C C   . PRO B 17   ? 0.7209 0.5265 0.6255 0.0972  -0.1114 -0.0825 15   PRO B C   
8848  O O   . PRO B 17   ? 0.7124 0.5355 0.6264 0.0977  -0.1048 -0.0832 15   PRO B O   
8849  C CB  . PRO B 17   ? 0.7316 0.5358 0.6394 0.0918  -0.1147 -0.0750 15   PRO B CB  
8850  C CG  . PRO B 17   ? 0.7215 0.5344 0.6368 0.0973  -0.1141 -0.0754 15   PRO B CG  
8851  C CD  . PRO B 17   ? 0.7100 0.5339 0.6317 0.1066  -0.1108 -0.0809 15   PRO B CD  
8852  N N   . ALA B 18   ? 0.6353 0.4257 0.5294 0.0939  -0.1154 -0.0827 16   ALA B N   
8853  C CA  . ALA B 18   ? 0.6152 0.4098 0.5087 0.0901  -0.1120 -0.0834 16   ALA B CA  
8854  C C   . ALA B 18   ? 0.5949 0.4017 0.4951 0.0804  -0.1070 -0.0781 16   ALA B C   
8855  O O   . ALA B 18   ? 0.5765 0.3796 0.4757 0.0738  -0.1088 -0.0732 16   ALA B O   
8856  C CB  . ALA B 18   ? 0.6347 0.4092 0.5149 0.0877  -0.1181 -0.0843 16   ALA B CB  
8857  N N   . PRO B 19   ? 0.5593 0.3806 0.4660 0.0795  -0.1007 -0.0790 17   PRO B N   
8858  C CA  . PRO B 19   ? 0.5265 0.3601 0.4400 0.0711  -0.0958 -0.0742 17   PRO B CA  
8859  C C   . PRO B 19   ? 0.4940 0.3175 0.4005 0.0614  -0.0989 -0.0698 17   PRO B C   
8860  O O   . PRO B 19   ? 0.4959 0.3084 0.3941 0.0597  -0.1021 -0.0709 17   PRO B O   
8861  C CB  . PRO B 19   ? 0.4938 0.3409 0.4128 0.0728  -0.0898 -0.0768 17   PRO B CB  
8862  C CG  . PRO B 19   ? 0.5581 0.4046 0.4764 0.0832  -0.0903 -0.0828 17   PRO B CG  
8863  C CD  . PRO B 19   ? 0.5299 0.3566 0.4375 0.0862  -0.0979 -0.0844 17   PRO B CD  
8864  N N   . PHE B 20   ? 0.4513 0.2792 0.3613 0.0550  -0.0978 -0.0646 18   PHE B N   
8865  C CA  . PHE B 20   ? 0.4646 0.2876 0.3705 0.0451  -0.0995 -0.0595 18   PHE B CA  
8866  C C   . PHE B 20   ? 0.5438 0.3466 0.4381 0.0429  -0.1073 -0.0584 18   PHE B C   
8867  O O   . PHE B 20   ? 0.5053 0.3026 0.3949 0.0344  -0.1093 -0.0542 18   PHE B O   
8868  C CB  . PHE B 20   ? 0.4156 0.2448 0.3224 0.0404  -0.0961 -0.0591 18   PHE B CB  
8869  C CG  . PHE B 20   ? 0.4146 0.2629 0.3322 0.0415  -0.0887 -0.0595 18   PHE B CG  
8870  C CD1 . PHE B 20   ? 0.3565 0.2160 0.2811 0.0368  -0.0849 -0.0553 18   PHE B CD1 
8871  C CD2 . PHE B 20   ? 0.4035 0.2584 0.3239 0.0471  -0.0855 -0.0640 18   PHE B CD2 
8872  C CE1 . PHE B 20   ? 0.4031 0.2791 0.3372 0.0377  -0.0785 -0.0556 18   PHE B CE1 
8873  C CE2 . PHE B 20   ? 0.3656 0.2376 0.2957 0.0477  -0.0789 -0.0639 18   PHE B CE2 
8874  C CZ  . PHE B 20   ? 0.3903 0.2724 0.3271 0.0430  -0.0755 -0.0598 18   PHE B CZ  
8875  N N   . ALA B 21   ? 0.5585 0.3504 0.4482 0.0503  -0.1117 -0.0617 19   ALA B N   
8876  C CA  . ALA B 21   ? 0.6170 0.3883 0.4950 0.0487  -0.1197 -0.0608 19   ALA B CA  
8877  C C   . ALA B 21   ? 0.6068 0.3747 0.4832 0.0410  -0.1219 -0.0545 19   ALA B C   
8878  O O   . ALA B 21   ? 0.6322 0.3849 0.4991 0.0355  -0.1276 -0.0517 19   ALA B O   
8879  C CB  . ALA B 21   ? 0.5844 0.3465 0.4590 0.0592  -0.1236 -0.0657 19   ALA B CB  
8880  N N   . ASP B 22   ? 0.5601 0.3415 0.4452 0.0405  -0.1175 -0.0521 20   ASP B N   
8881  C CA  . ASP B 22   ? 0.5570 0.3371 0.4410 0.0336  -0.1188 -0.0462 20   ASP B CA  
8882  C C   . ASP B 22   ? 0.4805 0.2786 0.3735 0.0281  -0.1120 -0.0429 20   ASP B C   
8883  O O   . ASP B 22   ? 0.4863 0.2922 0.3842 0.0273  -0.1098 -0.0404 20   ASP B O   
8884  C CB  . ASP B 22   ? 0.6054 0.3815 0.4894 0.0389  -0.1217 -0.0464 20   ASP B CB  
8885  N N   . PHE B 23   ? 0.4412 0.2459 0.3362 0.0243  -0.1086 -0.0430 21   PHE B N   
8886  C CA  . PHE B 23   ? 0.4308 0.2532 0.3349 0.0205  -0.1018 -0.0407 21   PHE B CA  
8887  C C   . PHE B 23   ? 0.4081 0.2321 0.3114 0.0124  -0.1019 -0.0345 21   PHE B C   
8888  O O   . PHE B 23   ? 0.4159 0.2501 0.3253 0.0126  -0.0985 -0.0328 21   PHE B O   
8889  C CB  . PHE B 23   ? 0.3733 0.2014 0.2788 0.0180  -0.0988 -0.0417 21   PHE B CB  
8890  C CG  . PHE B 23   ? 0.4186 0.2641 0.3330 0.0142  -0.0922 -0.0393 21   PHE B CG  
8891  C CD1 . PHE B 23   ? 0.3889 0.2475 0.3123 0.0191  -0.0872 -0.0410 21   PHE B CD1 
8892  C CD2 . PHE B 23   ? 0.4105 0.2591 0.3241 0.0059  -0.0912 -0.0352 21   PHE B CD2 
8893  C CE1 . PHE B 23   ? 0.3679 0.2412 0.2989 0.0159  -0.0815 -0.0388 21   PHE B CE1 
8894  C CE2 . PHE B 23   ? 0.4523 0.3165 0.3737 0.0032  -0.0853 -0.0331 21   PHE B CE2 
8895  C CZ  . PHE B 23   ? 0.4092 0.2851 0.3390 0.0082  -0.0806 -0.0350 21   PHE B CZ  
8896  N N   . ALA B 24   ? 0.3936 0.2081 0.2894 0.0052  -0.1057 -0.0311 22   ALA B N   
8897  C CA  . ALA B 24   ? 0.4604 0.2767 0.3549 -0.0031 -0.1058 -0.0249 22   ALA B CA  
8898  C C   . ALA B 24   ? 0.4470 0.2466 0.3305 -0.0091 -0.1127 -0.0218 22   ALA B C   
8899  O O   . ALA B 24   ? 0.4619 0.2627 0.3434 -0.0172 -0.1127 -0.0182 22   ALA B O   
8900  C CB  . ALA B 24   ? 0.4273 0.2595 0.3286 -0.0082 -0.0998 -0.0226 22   ALA B CB  
8901  N N   . PRO B 25   ? 0.4935 0.2773 0.3696 -0.0057 -0.1188 -0.0229 23   PRO B N   
8902  C CA  . PRO B 25   ? 0.5369 0.3035 0.4019 -0.0118 -0.1258 -0.0197 23   PRO B CA  
8903  C C   . PRO B 25   ? 0.5044 0.2743 0.3682 -0.0210 -0.1256 -0.0126 23   PRO B C   
8904  O O   . PRO B 25   ? 0.4995 0.2770 0.3674 -0.0200 -0.1231 -0.0108 23   PRO B O   
8905  C CB  . PRO B 25   ? 0.5198 0.2709 0.3786 -0.0046 -0.1316 -0.0226 23   PRO B CB  
8906  C CG  . PRO B 25   ? 0.5262 0.2887 0.3934 0.0023  -0.1275 -0.0245 23   PRO B CG  
8907  C CD  . PRO B 25   ? 0.4862 0.2676 0.3639 0.0035  -0.1197 -0.0266 23   PRO B CD  
8908  N N   . PRO B 26   ? 0.5136 0.2786 0.3720 -0.0301 -0.1282 -0.0085 24   PRO B N   
8909  C CA  . PRO B 26   ? 0.4964 0.2652 0.3535 -0.0393 -0.1280 -0.0014 24   PRO B CA  
8910  C C   . PRO B 26   ? 0.5206 0.2763 0.3702 -0.0397 -0.1334 0.0014  24   PRO B C   
8911  O O   . PRO B 26   ? 0.5263 0.2662 0.3696 -0.0344 -0.1389 -0.0015 24   PRO B O   
8912  C CB  . PRO B 26   ? 0.5094 0.2737 0.3616 -0.0484 -0.1306 0.0017  24   PRO B CB  
8913  C CG  . PRO B 26   ? 0.5557 0.3044 0.4017 -0.0439 -0.1357 -0.0034 24   PRO B CG  
8914  C CD  . PRO B 26   ? 0.5172 0.2728 0.3702 -0.0326 -0.1317 -0.0101 24   PRO B CD  
8915  N N   . VAL B 27   ? 0.5022 0.2648 0.3523 -0.0459 -0.1317 0.0072  25   VAL B N   
8916  C CA  . VAL B 27   ? 0.5388 0.2899 0.3815 -0.0473 -0.1367 0.0107  25   VAL B CA  
8917  C C   . VAL B 27   ? 0.5081 0.2379 0.3388 -0.0521 -0.1451 0.0128  25   VAL B C   
8918  O O   . VAL B 27   ? 0.5579 0.2717 0.3810 -0.0490 -0.1512 0.0125  25   VAL B O   
8919  C CB  . VAL B 27   ? 0.5264 0.2899 0.3715 -0.0540 -0.1330 0.0169  25   VAL B CB  
8920  C CG1 . VAL B 27   ? 0.5182 0.2690 0.3542 -0.0572 -0.1386 0.0215  25   VAL B CG1 
8921  C CG2 . VAL B 27   ? 0.4576 0.2390 0.3133 -0.0480 -0.1257 0.0143  25   VAL B CG2 
8922  N N   . ARG B 28   ? 0.5174 0.2464 0.3460 -0.0594 -0.1460 0.0147  26   ARG B N   
8923  C CA  . ARG B 28   ? 0.5476 0.2569 0.3646 -0.0657 -0.1541 0.0174  26   ARG B CA  
8924  C C   . ARG B 28   ? 0.5641 0.2742 0.3815 -0.0692 -0.1541 0.0158  26   ARG B C   
8925  O O   . ARG B 28   ? 0.5561 0.2842 0.3828 -0.0695 -0.1474 0.0148  26   ARG B O   
8926  C CB  . ARG B 28   ? 0.5919 0.2999 0.4037 -0.0765 -0.1563 0.0259  26   ARG B CB  
8927  C CG  . ARG B 28   ? 0.5812 0.3076 0.3991 -0.0856 -0.1507 0.0307  26   ARG B CG  
8928  C CD  . ARG B 28   ? 0.6179 0.3446 0.4309 -0.0954 -0.1522 0.0391  26   ARG B CD  
8929  N NE  . ARG B 28   ? 0.6293 0.3619 0.4445 -0.0913 -0.1495 0.0400  26   ARG B NE  
8930  C CZ  . ARG B 28   ? 0.7085 0.4265 0.5157 -0.0899 -0.1549 0.0416  26   ARG B CZ  
8931  N NH1 . ARG B 28   ? 0.7303 0.4261 0.5266 -0.0919 -0.1634 0.0423  26   ARG B NH1 
8932  N NH2 . ARG B 28   ? 0.6453 0.3709 0.4553 -0.0864 -0.1519 0.0424  26   ARG B NH2 
8933  N N   . PRO B 29   ? 0.6195 0.3100 0.4268 -0.0717 -0.1616 0.0154  27   PRO B N   
8934  C CA  . PRO B 29   ? 0.6198 0.3103 0.4264 -0.0767 -0.1623 0.0148  27   PRO B CA  
8935  C C   . PRO B 29   ? 0.6131 0.3180 0.4234 -0.0883 -0.1590 0.0216  27   PRO B C   
8936  O O   . PRO B 29   ? 0.6059 0.3097 0.4127 -0.0959 -0.1608 0.0283  27   PRO B O   
8937  C CB  . PRO B 29   ? 0.6106 0.2748 0.4036 -0.0785 -0.1723 0.0144  27   PRO B CB  
8938  C CG  . PRO B 29   ? 0.6736 0.3254 0.4623 -0.0695 -0.1756 0.0116  27   PRO B CG  
8939  C CD  . PRO B 29   ? 0.6220 0.2888 0.4177 -0.0693 -0.1702 0.0150  27   PRO B CD  
8940  N N   . GLN B 30   ? 0.6312 0.3504 0.4489 -0.0894 -0.1542 0.0201  28   GLN B N   
8941  C CA  . GLN B 30   ? 0.6229 0.3594 0.4463 -0.0988 -0.1498 0.0260  28   GLN B CA  
8942  C C   . GLN B 30   ? 0.6342 0.3602 0.4494 -0.1104 -0.1562 0.0310  28   GLN B C   
8943  O O   . GLN B 30   ? 0.6028 0.3204 0.4145 -0.1112 -0.1597 0.0282  28   GLN B O   
8944  C CB  . GLN B 30   ? 0.6149 0.3709 0.4496 -0.0950 -0.1423 0.0224  28   GLN B CB  
8945  C CG  . GLN B 30   ? 0.5287 0.2951 0.3716 -0.0839 -0.1361 0.0175  28   GLN B CG  
8946  C CD  . GLN B 30   ? 0.5187 0.2975 0.3662 -0.0852 -0.1317 0.0216  28   GLN B CD  
8947  O OE1 . GLN B 30   ? 0.4827 0.2785 0.3366 -0.0903 -0.1266 0.0253  28   GLN B OE1 
8948  N NE2 . GLN B 30   ? 0.5365 0.3070 0.3808 -0.0802 -0.1336 0.0209  28   GLN B NE2 
8949  N N   . SER B 31   ? 0.5994 0.3262 0.4115 -0.1197 -0.1578 0.0386  29   SER B N   
8950  C CA  . SER B 31   ? 0.6452 0.3639 0.4501 -0.1321 -0.1636 0.0444  29   SER B CA  
8951  C C   . SER B 31   ? 0.6167 0.3518 0.4287 -0.1378 -0.1598 0.0456  29   SER B C   
8952  O O   . SER B 31   ? 0.5586 0.3123 0.3812 -0.1326 -0.1523 0.0425  29   SER B O   
8953  C CB  . SER B 31   ? 0.6497 0.3693 0.4510 -0.1407 -0.1649 0.0527  29   SER B CB  
8954  O OG  . SER B 31   ? 0.5688 0.3133 0.3801 -0.1447 -0.1571 0.0567  29   SER B OG  
8955  N N   . THR B 32   ? 0.6183 0.3466 0.4243 -0.1491 -0.1653 0.0505  30   THR B N   
8956  C CA  . THR B 32   ? 0.6049 0.3492 0.4174 -0.1560 -0.1623 0.0527  30   THR B CA  
8957  C C   . THR B 32   ? 0.5933 0.3637 0.4165 -0.1588 -0.1540 0.0573  30   THR B C   
8958  O O   . THR B 32   ? 0.5855 0.3747 0.4186 -0.1566 -0.1477 0.0554  30   THR B O   
8959  C CB  . THR B 32   ? 0.7022 0.4339 0.5058 -0.1685 -0.1704 0.0578  30   THR B CB  
8960  O OG1 . THR B 32   ? 0.6906 0.4047 0.4871 -0.1629 -0.1754 0.0523  30   THR B OG1 
8961  C CG2 . THR B 32   ? 0.6739 0.4256 0.4850 -0.1776 -0.1670 0.0622  30   THR B CG2 
8962  N N   . LEU B 33   ? 0.5389 0.3107 0.3599 -0.1631 -0.1540 0.0631  31   LEU B N   
8963  C CA  . LEU B 33   ? 0.5752 0.3713 0.4054 -0.1654 -0.1462 0.0673  31   LEU B CA  
8964  C C   . LEU B 33   ? 0.5500 0.3589 0.3894 -0.1532 -0.1383 0.0616  31   LEU B C   
8965  O O   . LEU B 33   ? 0.5360 0.3667 0.3854 -0.1525 -0.1311 0.0620  31   LEU B O   
8966  C CB  . LEU B 33   ? 0.5868 0.3803 0.4115 -0.1728 -0.1482 0.0748  31   LEU B CB  
8967  C CG  . LEU B 33   ? 0.6249 0.4097 0.4419 -0.1866 -0.1552 0.0817  31   LEU B CG  
8968  C CD1 . LEU B 33   ? 0.5548 0.3289 0.3629 -0.1928 -0.1595 0.0881  31   LEU B CD1 
8969  C CD2 . LEU B 33   ? 0.6185 0.4259 0.4438 -0.1949 -0.1508 0.0863  31   LEU B CD2 
8970  N N   . ARG B 34   ? 0.5498 0.3455 0.3860 -0.1435 -0.1398 0.0561  32   ARG B N   
8971  C CA  . ARG B 34   ? 0.5204 0.3275 0.3652 -0.1321 -0.1329 0.0504  32   ARG B CA  
8972  C C   . ARG B 34   ? 0.5144 0.3310 0.3666 -0.1278 -0.1292 0.0452  32   ARG B C   
8973  O O   . ARG B 34   ? 0.4857 0.3203 0.3477 -0.1229 -0.1218 0.0433  32   ARG B O   
8974  C CB  . ARG B 34   ? 0.5355 0.3262 0.3751 -0.1230 -0.1359 0.0457  32   ARG B CB  
8975  C CG  . ARG B 34   ? 0.4697 0.2552 0.3041 -0.1251 -0.1377 0.0503  32   ARG B CG  
8976  C CD  . ARG B 34   ? 0.4757 0.2818 0.3188 -0.1224 -0.1296 0.0515  32   ARG B CD  
8977  N NE  . ARG B 34   ? 0.5275 0.3394 0.3776 -0.1105 -0.1248 0.0445  32   ARG B NE  
8978  C CZ  . ARG B 34   ? 0.5229 0.3277 0.3714 -0.1029 -0.1255 0.0417  32   ARG B CZ  
8979  N NH1 . ARG B 34   ? 0.5070 0.2980 0.3467 -0.1052 -0.1307 0.0449  32   ARG B NH1 
8980  N NH2 . ARG B 34   ? 0.4997 0.3114 0.3553 -0.0929 -0.1209 0.0356  32   ARG B NH2 
8981  N N   . ARG B 35   ? 0.4980 0.3023 0.3453 -0.1295 -0.1344 0.0430  33   ARG B N   
8982  C CA  . ARG B 35   ? 0.5201 0.3329 0.3737 -0.1259 -0.1312 0.0384  33   ARG B CA  
8983  C C   . ARG B 35   ? 0.5043 0.3385 0.3661 -0.1325 -0.1263 0.0426  33   ARG B C   
8984  O O   . ARG B 35   ? 0.4745 0.3231 0.3450 -0.1275 -0.1206 0.0393  33   ARG B O   
8985  C CB  . ARG B 35   ? 0.5412 0.3354 0.3865 -0.1270 -0.1384 0.0353  33   ARG B CB  
8986  C CG  . ARG B 35   ? 0.6117 0.3871 0.4506 -0.1177 -0.1421 0.0293  33   ARG B CG  
8987  C CD  . ARG B 35   ? 0.7227 0.4790 0.5525 -0.1189 -0.1495 0.0264  33   ARG B CD  
8988  N NE  . ARG B 35   ? 0.8053 0.5431 0.6282 -0.1100 -0.1535 0.0210  33   ARG B NE  
8989  C CZ  . ARG B 35   ? 0.8498 0.5896 0.6768 -0.0986 -0.1501 0.0139  33   ARG B CZ  
8990  N NH1 . ARG B 35   ? 0.8017 0.5597 0.6387 -0.0948 -0.1430 0.0113  33   ARG B NH1 
8991  N NH2 . ARG B 35   ? 0.8489 0.5722 0.6695 -0.0907 -0.1539 0.0095  33   ARG B NH2 
8992  N N   . ALA B 36   ? 0.4792 0.3164 0.3385 -0.1436 -0.1285 0.0500  34   ALA B N   
8993  C CA  . ALA B 36   ? 0.4716 0.3300 0.3388 -0.1500 -0.1241 0.0542  34   ALA B CA  
8994  C C   . ALA B 36   ? 0.4493 0.3281 0.3262 -0.1450 -0.1155 0.0545  34   ALA B C   
8995  O O   . ALA B 36   ? 0.4172 0.3145 0.3031 -0.1441 -0.1099 0.0542  34   ALA B O   
8996  C CB  . ALA B 36   ? 0.5142 0.3710 0.3764 -0.1633 -0.1286 0.0623  34   ALA B CB  
8997  N N   . ILE B 37   ? 0.4631 0.3385 0.3379 -0.1415 -0.1145 0.0550  35   ILE B N   
8998  C CA  . ILE B 37   ? 0.4018 0.2937 0.2847 -0.1350 -0.1067 0.0538  35   ILE B CA  
8999  C C   . ILE B 37   ? 0.3807 0.2775 0.2705 -0.1249 -0.1025 0.0466  35   ILE B C   
9000  O O   . ILE B 37   ? 0.3859 0.3010 0.2847 -0.1226 -0.0962 0.0460  35   ILE B O   
9001  C CB  . ILE B 37   ? 0.3928 0.2764 0.2710 -0.1321 -0.1076 0.0545  35   ILE B CB  
9002  C CG1 . ILE B 37   ? 0.4056 0.2871 0.2775 -0.1426 -0.1109 0.0625  35   ILE B CG1 
9003  C CG2 . ILE B 37   ? 0.3934 0.2914 0.2794 -0.1239 -0.1001 0.0518  35   ILE B CG2 
9004  C CD1 . ILE B 37   ? 0.4152 0.2829 0.2796 -0.1406 -0.1139 0.0633  35   ILE B CD1 
9005  N N   . THR B 38   ? 0.3799 0.2605 0.2654 -0.1184 -0.1060 0.0410  36   THR B N   
9006  C CA  . THR B 38   ? 0.3711 0.2558 0.2626 -0.1083 -0.1019 0.0341  36   THR B CA  
9007  C C   . THR B 38   ? 0.3810 0.2763 0.2780 -0.1098 -0.0998 0.0331  36   THR B C   
9008  O O   . THR B 38   ? 0.3641 0.2727 0.2694 -0.1040 -0.0939 0.0301  36   THR B O   
9009  C CB  . THR B 38   ? 0.4019 0.2671 0.2871 -0.1017 -0.1065 0.0287  36   THR B CB  
9010  O OG1 . THR B 38   ? 0.4419 0.2981 0.3223 -0.1000 -0.1085 0.0298  36   THR B OG1 
9011  C CG2 . THR B 38   ? 0.4179 0.2882 0.3094 -0.0914 -0.1021 0.0219  36   THR B CG2 
9012  N N   . ALA B 39   ? 0.4396 0.3292 0.3320 -0.1180 -0.1047 0.0360  37   ALA B N   
9013  C CA  . ALA B 39   ? 0.4072 0.3062 0.3042 -0.1204 -0.1036 0.0355  37   ALA B CA  
9014  C C   . ALA B 39   ? 0.4007 0.3232 0.3073 -0.1226 -0.0970 0.0389  37   ALA B C   
9015  O O   . ALA B 39   ? 0.4375 0.3711 0.3503 -0.1210 -0.0940 0.0372  37   ALA B O   
9016  C CB  . ALA B 39   ? 0.3845 0.2720 0.2738 -0.1299 -0.1109 0.0386  37   ALA B CB  
9017  N N   . ALA B 40   ? 0.4051 0.3356 0.3129 -0.1261 -0.0949 0.0439  38   ALA B N   
9018  C CA  . ALA B 40   ? 0.3847 0.3374 0.3009 -0.1283 -0.0889 0.0475  38   ALA B CA  
9019  C C   . ALA B 40   ? 0.3739 0.3379 0.2973 -0.1189 -0.0818 0.0441  38   ALA B C   
9020  O O   . ALA B 40   ? 0.3642 0.3467 0.2948 -0.1193 -0.0765 0.0463  38   ALA B O   
9021  C CB  . ALA B 40   ? 0.3781 0.3349 0.2915 -0.1377 -0.0902 0.0549  38   ALA B CB  
9022  N N   . TYR B 41   ? 0.3956 0.3490 0.3173 -0.1105 -0.0818 0.0386  39   TYR B N   
9023  C CA  . TYR B 41   ? 0.3448 0.3059 0.2718 -0.1022 -0.0761 0.0358  39   TYR B CA  
9024  C C   . TYR B 41   ? 0.3646 0.3445 0.3011 -0.0990 -0.0698 0.0348  39   TYR B C   
9025  O O   . TYR B 41   ? 0.3228 0.3159 0.2640 -0.0975 -0.0649 0.0365  39   TYR B O   
9026  C CB  . TYR B 41   ? 0.3408 0.2877 0.2650 -0.0938 -0.0777 0.0297  39   TYR B CB  
9027  C CG  . TYR B 41   ? 0.3223 0.2706 0.2487 -0.0865 -0.0743 0.0273  39   TYR B CG  
9028  C CD1 . TYR B 41   ? 0.3240 0.2883 0.2569 -0.0844 -0.0683 0.0284  39   TYR B CD1 
9029  C CD2 . TYR B 41   ? 0.3779 0.3113 0.2996 -0.0813 -0.0773 0.0237  39   TYR B CD2 
9030  C CE1 . TYR B 41   ? 0.3250 0.2899 0.2594 -0.0778 -0.0655 0.0260  39   TYR B CE1 
9031  C CE2 . TYR B 41   ? 0.3344 0.2692 0.2581 -0.0748 -0.0745 0.0215  39   TYR B CE2 
9032  C CZ  . TYR B 41   ? 0.3377 0.2880 0.2677 -0.0732 -0.0687 0.0227  39   TYR B CZ  
9033  O OH  . TYR B 41   ? 0.3285 0.2798 0.2602 -0.0670 -0.0663 0.0205  39   TYR B OH  
9034  N N   . ARG B 42   ? 0.3028 0.2840 0.2419 -0.0979 -0.0700 0.0322  40   ARG B N   
9035  C CA  . ARG B 42   ? 0.2937 0.2916 0.2416 -0.0945 -0.0645 0.0312  40   ARG B CA  
9036  C C   . ARG B 42   ? 0.2948 0.2992 0.2442 -0.1008 -0.0660 0.0336  40   ARG B C   
9037  O O   . ARG B 42   ? 0.3796 0.3908 0.3339 -0.0977 -0.0639 0.0312  40   ARG B O   
9038  C CB  . ARG B 42   ? 0.2985 0.2937 0.2493 -0.0850 -0.0620 0.0248  40   ARG B CB  
9039  C CG  . ARG B 42   ? 0.3288 0.3235 0.2806 -0.0786 -0.0590 0.0229  40   ARG B CG  
9040  C CD  . ARG B 42   ? 0.3057 0.2926 0.2580 -0.0703 -0.0585 0.0168  40   ARG B CD  
9041  N NE  . ARG B 42   ? 0.3002 0.2803 0.2500 -0.0666 -0.0586 0.0157  40   ARG B NE  
9042  C CZ  . ARG B 42   ? 0.2986 0.2869 0.2520 -0.0633 -0.0545 0.0160  40   ARG B CZ  
9043  N NH1 . ARG B 42   ? 0.3071 0.3106 0.2669 -0.0625 -0.0496 0.0170  40   ARG B NH1 
9044  N NH2 . ARG B 42   ? 0.2983 0.2790 0.2486 -0.0605 -0.0555 0.0150  40   ARG B NH2 
9045  N N   . ARG B 43   ? 0.2882 0.2910 0.2336 -0.1101 -0.0698 0.0389  41   ARG B N   
9046  C CA  . ARG B 43   ? 0.3419 0.3502 0.2884 -0.1171 -0.0721 0.0416  41   ARG B CA  
9047  C C   . ARG B 43   ? 0.3527 0.3829 0.3087 -0.1161 -0.0664 0.0432  41   ARG B C   
9048  O O   . ARG B 43   ? 0.3396 0.3814 0.2996 -0.1140 -0.0617 0.0449  41   ARG B O   
9049  C CB  . ARG B 43   ? 0.3903 0.3938 0.3309 -0.1277 -0.0771 0.0476  41   ARG B CB  
9050  C CG  . ARG B 43   ? 0.3720 0.3828 0.3139 -0.1365 -0.0797 0.0516  41   ARG B CG  
9051  C CD  . ARG B 43   ? 0.3847 0.3845 0.3185 -0.1468 -0.0862 0.0566  41   ARG B CD  
9052  N NE  . ARG B 43   ? 0.4038 0.3800 0.3285 -0.1451 -0.0920 0.0529  41   ARG B NE  
9053  C CZ  . ARG B 43   ? 0.4228 0.3839 0.3388 -0.1501 -0.0972 0.0554  41   ARG B CZ  
9054  N NH1 . ARG B 43   ? 0.4054 0.3723 0.3205 -0.1574 -0.0973 0.0618  41   ARG B NH1 
9055  N NH2 . ARG B 43   ? 0.4321 0.3718 0.3399 -0.1477 -0.1026 0.0514  41   ARG B NH2 
9056  N N   . PRO B 44   ? 0.3613 0.3975 0.3208 -0.1169 -0.0666 0.0424  42   PRO B N   
9057  C CA  . PRO B 44   ? 0.3376 0.3946 0.3062 -0.1155 -0.0615 0.0440  42   PRO B CA  
9058  C C   . PRO B 44   ? 0.2768 0.3479 0.2478 -0.1221 -0.0600 0.0504  42   PRO B C   
9059  O O   . PRO B 44   ? 0.3003 0.3672 0.2667 -0.1310 -0.0642 0.0548  42   PRO B O   
9060  C CB  . PRO B 44   ? 0.3457 0.4035 0.3152 -0.1180 -0.0641 0.0432  42   PRO B CB  
9061  C CG  . PRO B 44   ? 0.3909 0.4288 0.3537 -0.1148 -0.0681 0.0381  42   PRO B CG  
9062  C CD  . PRO B 44   ? 0.3774 0.4010 0.3328 -0.1171 -0.0712 0.0391  42   PRO B CD  
9063  N N   . GLU B 45   ? 0.3090 0.3969 0.2871 -0.1178 -0.0539 0.0509  43   GLU B N   
9064  C CA  . GLU B 45   ? 0.3257 0.4288 0.3066 -0.1230 -0.0516 0.0567  43   GLU B CA  
9065  C C   . GLU B 45   ? 0.3434 0.4561 0.3264 -0.1323 -0.0543 0.0617  43   GLU B C   
9066  O O   . GLU B 45   ? 0.3262 0.4441 0.3077 -0.1403 -0.0556 0.0674  43   GLU B O   
9067  C CB  . GLU B 45   ? 0.3347 0.4540 0.3228 -0.1154 -0.0446 0.0556  43   GLU B CB  
9068  C CG  . GLU B 45   ? 0.3687 0.4891 0.3547 -0.1139 -0.0419 0.0569  43   GLU B CG  
9069  C CD  . GLU B 45   ? 0.2677 0.4009 0.2596 -0.1053 -0.0353 0.0547  43   GLU B CD  
9070  O OE1 . GLU B 45   ? 0.3000 0.4304 0.2946 -0.0975 -0.0335 0.0496  43   GLU B OE1 
9071  O OE2 . GLU B 45   ? 0.3107 0.4565 0.3043 -0.1064 -0.0320 0.0580  43   GLU B OE2 
9072  N N   . THR B 46   ? 0.3680 0.4830 0.3540 -0.1317 -0.0555 0.0599  44   THR B N   
9073  C CA  . THR B 46   ? 0.3382 0.4614 0.3259 -0.1408 -0.0587 0.0645  44   THR B CA  
9074  C C   . THR B 46   ? 0.3872 0.4943 0.3663 -0.1503 -0.0660 0.0670  44   THR B C   
9075  O O   . THR B 46   ? 0.3659 0.4797 0.3455 -0.1598 -0.0691 0.0722  44   THR B O   
9076  C CB  . THR B 46   ? 0.3203 0.4484 0.3126 -0.1378 -0.0587 0.0617  44   THR B CB  
9077  O OG1 . THR B 46   ? 0.3618 0.4720 0.3494 -0.1320 -0.0606 0.0556  44   THR B OG1 
9078  C CG2 . THR B 46   ? 0.3373 0.4850 0.3389 -0.1307 -0.0521 0.0611  44   THR B CG2 
9079  N N   . GLU B 47   ? 0.3444 0.4304 0.3156 -0.1479 -0.0691 0.0635  45   GLU B N   
9080  C CA  . GLU B 47   ? 0.3646 0.4342 0.3268 -0.1565 -0.0762 0.0660  45   GLU B CA  
9081  C C   . GLU B 47   ? 0.3370 0.4049 0.2953 -0.1610 -0.0764 0.0705  45   GLU B C   
9082  O O   . GLU B 47   ? 0.3823 0.4435 0.3350 -0.1709 -0.0817 0.0751  45   GLU B O   
9083  C CB  . GLU B 47   ? 0.4068 0.4535 0.3616 -0.1519 -0.0802 0.0600  45   GLU B CB  
9084  C CG  . GLU B 47   ? 0.4596 0.5056 0.4165 -0.1483 -0.0809 0.0556  45   GLU B CG  
9085  C CD  . GLU B 47   ? 0.5565 0.5809 0.5060 -0.1429 -0.0843 0.0494  45   GLU B CD  
9086  O OE1 . GLU B 47   ? 0.5489 0.5576 0.4910 -0.1437 -0.0875 0.0492  45   GLU B OE1 
9087  O OE2 . GLU B 47   ? 0.6434 0.6668 0.5945 -0.1377 -0.0838 0.0449  45   GLU B OE2 
9088  N N   . CYS B 48   ? 0.3612 0.4350 0.3221 -0.1543 -0.0708 0.0694  46   CYS B N   
9089  C CA  . CYS B 48   ? 0.3603 0.4323 0.3170 -0.1579 -0.0707 0.0734  46   CYS B CA  
9090  C C   . CYS B 48   ? 0.3641 0.4555 0.3250 -0.1662 -0.0690 0.0807  46   CYS B C   
9091  O O   . CYS B 48   ? 0.3564 0.4444 0.3121 -0.1745 -0.0719 0.0860  46   CYS B O   
9092  C CB  . CYS B 48   ? 0.3027 0.3755 0.2609 -0.1479 -0.0654 0.0697  46   CYS B CB  
9093  S SG  . CYS B 48   ? 0.3477 0.3982 0.3006 -0.1383 -0.0671 0.0618  46   CYS B SG  
9094  N N   . LEU B 49   ? 0.3198 0.4320 0.2899 -0.1639 -0.0642 0.0812  47   LEU B N   
9095  C CA  . LEU B 49   ? 0.3620 0.4955 0.3372 -0.1693 -0.0608 0.0875  47   LEU B CA  
9096  C C   . LEU B 49   ? 0.3390 0.4767 0.3131 -0.1824 -0.0655 0.0943  47   LEU B C   
9097  O O   . LEU B 49   ? 0.3592 0.5041 0.3320 -0.1894 -0.0653 0.1004  47   LEU B O   
9098  C CB  . LEU B 49   ? 0.3166 0.4714 0.3021 -0.1620 -0.0540 0.0858  47   LEU B CB  
9099  C CG  . LEU B 49   ? 0.3416 0.5032 0.3287 -0.1538 -0.0477 0.0841  47   LEU B CG  
9100  C CD1 . LEU B 49   ? 0.3300 0.4990 0.3146 -0.1608 -0.0469 0.0905  47   LEU B CD1 
9101  C CD2 . LEU B 49   ? 0.3417 0.4836 0.3234 -0.1457 -0.0481 0.0779  47   LEU B CD2 
9102  N N   . PRO B 50   ? 0.3502 0.4841 0.3246 -0.1865 -0.0701 0.0938  48   PRO B N   
9103  C CA  . PRO B 50   ? 0.3860 0.5261 0.3602 -0.1995 -0.0746 0.1007  48   PRO B CA  
9104  C C   . PRO B 50   ? 0.4148 0.5412 0.3797 -0.2089 -0.0797 0.1055  48   PRO B C   
9105  O O   . PRO B 50   ? 0.4109 0.5501 0.3772 -0.2183 -0.0798 0.1128  48   PRO B O   
9106  C CB  . PRO B 50   ? 0.3184 0.4500 0.2921 -0.2005 -0.0795 0.0976  48   PRO B CB  
9107  C CG  . PRO B 50   ? 0.3091 0.4443 0.2882 -0.1878 -0.0745 0.0907  48   PRO B CG  
9108  C CD  . PRO B 50   ? 0.3441 0.4710 0.3201 -0.1795 -0.0708 0.0873  48   PRO B CD  
9109  N N   . PRO B 51   ? 0.3884 0.4896 0.3437 -0.2070 -0.0841 0.1021  49   PRO B N   
9110  C CA  . PRO B 51   ? 0.4203 0.5089 0.3666 -0.2159 -0.0888 0.1072  49   PRO B CA  
9111  C C   . PRO B 51   ? 0.4390 0.5384 0.3861 -0.2153 -0.0837 0.1108  49   PRO B C   
9112  O O   . PRO B 51   ? 0.4565 0.5553 0.3990 -0.2251 -0.0863 0.1175  49   PRO B O   
9113  C CB  . PRO B 51   ? 0.4940 0.5539 0.4306 -0.2114 -0.0939 0.1015  49   PRO B CB  
9114  C CG  . PRO B 51   ? 0.4767 0.5375 0.4181 -0.1983 -0.0893 0.0936  49   PRO B CG  
9115  C CD  . PRO B 51   ? 0.4142 0.4965 0.3657 -0.1981 -0.0858 0.0941  49   PRO B CD  
9116  N N   . LEU B 52   ? 0.3973 0.5066 0.3498 -0.2042 -0.0765 0.1067  50   LEU B N   
9117  C CA  . LEU B 52   ? 0.4281 0.5488 0.3813 -0.2033 -0.0713 0.1100  50   LEU B CA  
9118  C C   . LEU B 52   ? 0.4159 0.5634 0.3767 -0.2099 -0.0677 0.1166  50   LEU B C   
9119  O O   . LEU B 52   ? 0.3967 0.5509 0.3551 -0.2167 -0.0671 0.1229  50   LEU B O   
9120  C CB  . LEU B 52   ? 0.3947 0.5177 0.3513 -0.1895 -0.0651 0.1034  50   LEU B CB  
9121  C CG  . LEU B 52   ? 0.3979 0.4969 0.3479 -0.1820 -0.0676 0.0970  50   LEU B CG  
9122  C CD1 . LEU B 52   ? 0.3746 0.4792 0.3297 -0.1689 -0.0612 0.0906  50   LEU B CD1 
9123  C CD2 . LEU B 52   ? 0.3985 0.4829 0.3388 -0.1865 -0.0711 0.1001  50   LEU B CD2 
9124  N N   . VAL B 53   ? 0.4037 0.5671 0.3736 -0.2079 -0.0653 0.1154  51   VAL B N   
9125  C CA  . VAL B 53   ? 0.3619 0.5517 0.3397 -0.2140 -0.0622 0.1216  51   VAL B CA  
9126  C C   . VAL B 53   ? 0.4139 0.5988 0.3852 -0.2250 -0.0680 0.1279  51   VAL B C   
9127  O O   . VAL B 53   ? 0.4059 0.6051 0.3777 -0.2282 -0.0658 0.1330  51   VAL B O   
9128  C CB  . VAL B 53   ? 0.3692 0.5726 0.3565 -0.2098 -0.0602 0.1187  51   VAL B CB  
9129  C CG1 . VAL B 53   ? 0.4216 0.6461 0.4137 -0.2132 -0.0587 0.1237  51   VAL B CG1 
9130  C CG2 . VAL B 53   ? 0.3285 0.5386 0.3212 -0.1955 -0.0534 0.1123  51   VAL B CG2 
9131  N N   . GLU B 54   ? 0.4255 0.5893 0.3897 -0.2298 -0.0756 0.1270  52   GLU B N   
9132  C CA  . GLU B 54   ? 0.4783 0.6354 0.4353 -0.2393 -0.0816 0.1324  52   GLU B CA  
9133  C C   . GLU B 54   ? 0.4445 0.5944 0.3937 -0.2438 -0.0828 0.1366  52   GLU B C   
9134  O O   . GLU B 54   ? 0.5469 0.7049 0.4941 -0.2503 -0.0839 0.1425  52   GLU B O   
9135  C CB  . GLU B 54   ? 0.4711 0.6052 0.4214 -0.2423 -0.0895 0.1298  52   GLU B CB  
9136  N N   . ALA B 55   ? 0.4805 0.6151 0.4249 -0.2405 -0.0828 0.1338  53   ALA B N   
9137  C CA  . ALA B 55   ? 0.4886 0.6143 0.4247 -0.2442 -0.0842 0.1375  53   ALA B CA  
9138  C C   . ALA B 55   ? 0.4580 0.6068 0.3992 -0.2423 -0.0768 0.1408  53   ALA B C   
9139  O O   . ALA B 55   ? 0.4931 0.6420 0.4288 -0.2474 -0.0779 0.1457  53   ALA B O   
9140  C CB  . ALA B 55   ? 0.4921 0.5945 0.4218 -0.2405 -0.0864 0.1332  53   ALA B CB  
9141  N N   . ALA B 56   ? 0.4583 0.6263 0.4095 -0.2347 -0.0693 0.1380  54   ALA B N   
9142  C CA  . ALA B 56   ? 0.4355 0.6258 0.3918 -0.2310 -0.0618 0.1400  54   ALA B CA  
9143  C C   . ALA B 56   ? 0.4920 0.7065 0.4551 -0.2331 -0.0595 0.1435  54   ALA B C   
9144  O O   . ALA B 56   ? 0.4660 0.7007 0.4342 -0.2290 -0.0530 0.1446  54   ALA B O   
9145  C CB  . ALA B 56   ? 0.4405 0.6380 0.4032 -0.2206 -0.0549 0.1346  54   ALA B CB  
9146  N N   . THR B 57   ? 0.4743 0.6870 0.4375 -0.2389 -0.0646 0.1453  55   THR B N   
9147  C CA  . THR B 57   ? 0.4921 0.7270 0.4615 -0.2413 -0.0630 0.1489  55   THR B CA  
9148  C C   . THR B 57   ? 0.5270 0.7674 0.4918 -0.2487 -0.0643 0.1554  55   THR B C   
9149  O O   . THR B 57   ? 0.5638 0.7863 0.5193 -0.2564 -0.0707 0.1583  55   THR B O   
9150  C CB  . THR B 57   ? 0.4978 0.7278 0.4679 -0.2455 -0.0683 0.1488  55   THR B CB  
9151  O OG1 . THR B 57   ? 0.4323 0.6646 0.4093 -0.2377 -0.0656 0.1431  55   THR B OG1 
9152  C CG2 . THR B 57   ? 0.5851 0.8348 0.5592 -0.2505 -0.0683 0.1541  55   THR B CG2 
9153  N N   . GLN B 58   ? 0.5270 0.7921 0.4983 -0.2463 -0.0584 0.1576  56   GLN B N   
9154  C CA  . GLN B 58   ? 0.5346 0.8085 0.5028 -0.2531 -0.0591 0.1638  56   GLN B CA  
9155  C C   . GLN B 58   ? 0.5377 0.8338 0.5129 -0.2558 -0.0583 0.1673  56   GLN B C   
9156  O O   . GLN B 58   ? 0.5785 0.8880 0.5622 -0.2499 -0.0549 0.1645  56   GLN B O   
9157  C CB  . GLN B 58   ? 0.5562 0.8392 0.5246 -0.2480 -0.0529 0.1637  56   GLN B CB  
9158  C CG  . GLN B 58   ? 0.4696 0.7333 0.4324 -0.2435 -0.0525 0.1597  56   GLN B CG  
9159  C CD  . GLN B 58   ? 0.5991 0.8603 0.5554 -0.2450 -0.0513 0.1624  56   GLN B CD  
9160  O OE1 . GLN B 58   ? 0.6801 0.9347 0.6297 -0.2538 -0.0561 0.1674  56   GLN B OE1 
9161  N NE2 . GLN B 58   ? 0.6298 0.8959 0.5877 -0.2364 -0.0449 0.1590  56   GLN B NE2 
9162  N N   . SER B 59   ? 0.5675 0.8673 0.5388 -0.2648 -0.0616 0.1735  57   SER B N   
9163  C CA  . SER B 59   ? 0.5846 0.9053 0.5617 -0.2687 -0.0614 0.1777  57   SER B CA  
9164  C C   . SER B 59   ? 0.6002 0.9478 0.5869 -0.2601 -0.0528 0.1765  57   SER B C   
9165  O O   . SER B 59   ? 0.5601 0.9108 0.5477 -0.2528 -0.0473 0.1736  57   SER B O   
9166  C CB  . SER B 59   ? 0.6029 0.9222 0.5735 -0.2801 -0.0663 0.1848  57   SER B CB  
9167  O OG  . SER B 59   ? 0.6450 0.9677 0.6126 -0.2797 -0.0633 0.1866  57   SER B OG  
9168  N N   . LYS B 60   ? 0.6069 0.9740 0.6005 -0.2610 -0.0518 0.1787  58   LYS B N   
9169  C CA  . LYS B 60   ? 0.6067 1.0002 0.6094 -0.2530 -0.0443 0.1778  58   LYS B CA  
9170  C C   . LYS B 60   ? 0.6140 1.0184 0.6148 -0.2543 -0.0411 0.1814  58   LYS B C   
9171  O O   . LYS B 60   ? 0.6315 1.0506 0.6370 -0.2455 -0.0341 0.1789  58   LYS B O   
9172  C CB  . LYS B 60   ? 0.6681 1.0791 0.6777 -0.2548 -0.0448 0.1802  58   LYS B CB  
9173  C CG  . LYS B 60   ? 0.7288 1.1678 0.7475 -0.2470 -0.0376 0.1799  58   LYS B CG  
9174  C CD  . LYS B 60   ? 0.7066 1.1486 0.7312 -0.2338 -0.0318 0.1727  58   LYS B CD  
9175  C CE  . LYS B 60   ? 0.6972 1.1662 0.7307 -0.2259 -0.0255 0.1722  58   LYS B CE  
9176  N NZ  . LYS B 60   ? 0.7321 1.2033 0.7708 -0.2128 -0.0201 0.1652  58   LYS B NZ  
9177  N N   . GLU B 61   ? 0.5911 0.9882 0.5847 -0.2651 -0.0462 0.1871  59   GLU B N   
9178  C CA  . GLU B 61   ? 0.5358 0.9417 0.5269 -0.2669 -0.0435 0.1905  59   GLU B CA  
9179  C C   . GLU B 61   ? 0.5956 0.9903 0.5829 -0.2601 -0.0400 0.1863  59   GLU B C   
9180  O O   . GLU B 61   ? 0.5986 1.0075 0.5890 -0.2529 -0.0333 0.1848  59   GLU B O   
9181  C CB  . GLU B 61   ? 0.6077 1.0053 0.5911 -0.2803 -0.0504 0.1974  59   GLU B CB  
9182  N N   . ILE B 62   ? 0.5999 0.9688 0.5801 -0.2619 -0.0445 0.1841  60   ILE B N   
9183  C CA  . ILE B 62   ? 0.5641 0.9206 0.5400 -0.2559 -0.0417 0.1802  60   ILE B CA  
9184  C C   . ILE B 62   ? 0.5428 0.9092 0.5261 -0.2429 -0.0345 0.1738  60   ILE B C   
9185  O O   . ILE B 62   ? 0.5455 0.9165 0.5287 -0.2360 -0.0289 0.1715  60   ILE B O   
9186  C CB  . ILE B 62   ? 0.5747 0.9010 0.5416 -0.2606 -0.0486 0.1792  60   ILE B CB  
9187  C CG1 . ILE B 62   ? 0.5801 0.8962 0.5385 -0.2729 -0.0556 0.1856  60   ILE B CG1 
9188  C CG2 . ILE B 62   ? 0.6006 0.9137 0.5637 -0.2535 -0.0457 0.1746  60   ILE B CG2 
9189  C CD1 . ILE B 62   ? 0.6167 0.9023 0.5653 -0.2776 -0.0629 0.1848  60   ILE B CD1 
9190  N N   . ARG B 63   ? 0.4822 0.8523 0.4720 -0.2393 -0.0344 0.1708  61   ARG B N   
9191  C CA  . ARG B 63   ? 0.5129 0.8914 0.5096 -0.2269 -0.0280 0.1646  61   ARG B CA  
9192  C C   . ARG B 63   ? 0.5365 0.9406 0.5394 -0.2203 -0.0210 0.1648  61   ARG B C   
9193  O O   . ARG B 63   ? 0.5312 0.9394 0.5358 -0.2104 -0.0151 0.1604  61   ARG B O   
9194  C CB  . ARG B 63   ? 0.5247 0.9025 0.5270 -0.2250 -0.0299 0.1618  61   ARG B CB  
9195  C CG  . ARG B 63   ? 0.5701 0.9220 0.5671 -0.2273 -0.0350 0.1592  61   ARG B CG  
9196  C CD  . ARG B 63   ? 0.6127 0.9650 0.6158 -0.2236 -0.0357 0.1555  61   ARG B CD  
9197  N NE  . ARG B 63   ? 0.5679 0.9254 0.5725 -0.2310 -0.0402 0.1595  61   ARG B NE  
9198  C CZ  . ARG B 63   ? 0.5872 0.9633 0.6000 -0.2278 -0.0379 0.1594  61   ARG B CZ  
9199  N NH1 . ARG B 63   ? 0.5704 0.9620 0.5907 -0.2170 -0.0312 0.1555  61   ARG B NH1 
9200  N NH2 . ARG B 63   ? 0.5713 0.9502 0.5845 -0.2355 -0.0426 0.1633  61   ARG B NH2 
9201  N N   . ASP B 64   ? 0.5249 0.9462 0.5309 -0.2255 -0.0215 0.1698  62   ASP B N   
9202  C CA  . ASP B 64   ? 0.5315 0.9774 0.5430 -0.2195 -0.0151 0.1702  62   ASP B CA  
9203  C C   . ASP B 64   ? 0.4586 0.9041 0.4647 -0.2186 -0.0121 0.1711  62   ASP B C   
9204  O O   . ASP B 64   ? 0.4752 0.9317 0.4841 -0.2088 -0.0056 0.1677  62   ASP B O   
9205  C CB  . ASP B 64   ? 0.5387 1.0024 0.5542 -0.2264 -0.0170 0.1760  62   ASP B CB  
9206  C CG  . ASP B 64   ? 0.5753 1.0453 0.5977 -0.2246 -0.0181 0.1746  62   ASP B CG  
9207  O OD1 . ASP B 64   ? 0.5626 1.0209 0.5862 -0.2194 -0.0185 0.1695  62   ASP B OD1 
9208  O OD2 . ASP B 64   ? 0.6558 1.1429 0.6827 -0.2283 -0.0187 0.1786  62   ASP B OD2 
9209  N N   . ALA B 65   ? 0.4750 0.9075 0.4729 -0.2287 -0.0168 0.1757  63   ALA B N   
9210  C CA  . ALA B 65   ? 0.4878 0.9184 0.4798 -0.2284 -0.0144 0.1767  63   ALA B CA  
9211  C C   . ALA B 65   ? 0.5339 0.9500 0.5225 -0.2199 -0.0115 0.1708  63   ALA B C   
9212  O O   . ALA B 65   ? 0.5239 0.9434 0.5098 -0.2151 -0.0070 0.1697  63   ALA B O   
9213  C CB  . ALA B 65   ? 0.5303 0.9481 0.5139 -0.2413 -0.0209 0.1829  63   ALA B CB  
9214  N N   . ALA B 66   ? 0.5005 0.9006 0.4891 -0.2179 -0.0140 0.1668  64   ALA B N   
9215  C CA  . ALA B 66   ? 0.5200 0.9062 0.5053 -0.2101 -0.0115 0.1613  64   ALA B CA  
9216  C C   . ALA B 66   ? 0.5193 0.9211 0.5115 -0.1970 -0.0038 0.1559  64   ALA B C   
9217  O O   . ALA B 66   ? 0.4709 0.8709 0.4601 -0.1901 0.0005  0.1529  64   ALA B O   
9218  C CB  . ALA B 66   ? 0.5188 0.8832 0.5019 -0.2123 -0.0166 0.1590  64   ALA B CB  
9219  N N   . ALA B 67   ? 0.4751 0.8915 0.4760 -0.1932 -0.0023 0.1545  65   ALA B N   
9220  C CA  . ALA B 67   ? 0.4297 0.8605 0.4371 -0.1804 0.0045  0.1492  65   ALA B CA  
9221  C C   . ALA B 67   ? 0.5026 0.9512 0.5102 -0.1767 0.0096  0.1506  65   ALA B C   
9222  O O   . ALA B 67   ? 0.5434 0.9995 0.5531 -0.1657 0.0154  0.1459  65   ALA B O   
9223  C CB  . ALA B 67   ? 0.4739 0.9161 0.4901 -0.1777 0.0043  0.1480  65   ALA B CB  
9224  N N   . SER B 68   ? 0.5025 0.9581 0.5079 -0.1858 0.0075  0.1569  66   SER B N   
9225  C CA  . SER B 68   ? 0.5157 0.9883 0.5209 -0.1832 0.0122  0.1586  66   SER B CA  
9226  C C   . SER B 68   ? 0.5045 0.9656 0.5013 -0.1818 0.0139  0.1577  66   SER B C   
9227  O O   . SER B 68   ? 0.5309 1.0004 0.5275 -0.1726 0.0197  0.1544  66   SER B O   
9228  C CB  . SER B 68   ? 0.4637 0.9484 0.4697 -0.1938 0.0092  0.1659  66   SER B CB  
9229  N N   . THR B 69   ? 0.5385 0.9798 0.5275 -0.1907 0.0086  0.1605  67   THR B N   
9230  C CA  . THR B 69   ? 0.4898 0.9162 0.4701 -0.1890 0.0095  0.1590  67   THR B CA  
9231  C C   . THR B 69   ? 0.5127 0.9337 0.4939 -0.1768 0.0137  0.1516  67   THR B C   
9232  O O   . THR B 69   ? 0.5079 0.9305 0.4856 -0.1697 0.0183  0.1489  67   THR B O   
9233  C CB  . THR B 69   ? 0.5652 0.9682 0.5377 -0.1997 0.0023  0.1624  67   THR B CB  
9234  O OG1 . THR B 69   ? 0.5022 0.9098 0.4729 -0.2110 -0.0017 0.1694  67   THR B OG1 
9235  C CG2 . THR B 69   ? 0.4975 0.8833 0.4605 -0.1974 0.0028  0.1606  67   THR B CG2 
9236  N N   . ALA B 70   ? 0.4625 0.8770 0.4481 -0.1742 0.0122  0.1481  68   ALA B N   
9237  C CA  . ALA B 70   ? 0.5032 0.9132 0.4901 -0.1627 0.0161  0.1411  68   ALA B CA  
9238  C C   . ALA B 70   ? 0.5378 0.9682 0.5304 -0.1515 0.0229  0.1375  68   ALA B C   
9239  O O   . ALA B 70   ? 0.5450 0.9729 0.5358 -0.1416 0.0271  0.1322  68   ALA B O   
9240  C CB  . ALA B 70   ? 0.4804 0.8810 0.4715 -0.1626 0.0130  0.1385  68   ALA B CB  
9241  N N   . ARG B 71   ? 0.4621 0.9121 0.4612 -0.1527 0.0238  0.1402  69   ARG B N   
9242  C CA  . ARG B 71   ? 0.5459 1.0157 0.5502 -0.1423 0.0299  0.1372  69   ARG B CA  
9243  C C   . ARG B 71   ? 0.5094 0.9827 0.5076 -0.1387 0.0339  0.1369  69   ARG B C   
9244  O O   . ARG B 71   ? 0.4805 0.9566 0.4784 -0.1274 0.0388  0.1315  69   ARG B O   
9245  C CB  . ARG B 71   ? 0.5276 1.0173 0.5391 -0.1458 0.0294  0.1411  69   ARG B CB  
9246  N N   . LYS B 72   ? 0.5137 0.9864 0.5066 -0.1482 0.0319  0.1428  70   LYS B N   
9247  C CA  . LYS B 72   ? 0.5089 0.9856 0.4958 -0.1454 0.0356  0.1430  70   LYS B CA  
9248  C C   . LYS B 72   ? 0.5371 0.9962 0.5165 -0.1394 0.0369  0.1382  70   LYS B C   
9249  O O   . LYS B 72   ? 0.5600 1.0235 0.5358 -0.1319 0.0415  0.1354  70   LYS B O   
9250  C CB  . LYS B 72   ? 0.5368 1.0138 0.5189 -0.1578 0.0323  0.1506  70   LYS B CB  
9251  N N   . LEU B 73   ? 0.5755 1.0148 0.5523 -0.1423 0.0329  0.1371  71   LEU B N   
9252  C CA  . LEU B 73   ? 0.5266 0.9486 0.4959 -0.1371 0.0337  0.1328  71   LEU B CA  
9253  C C   . LEU B 73   ? 0.5171 0.9434 0.4900 -0.1233 0.0386  0.1252  71   LEU B C   
9254  O O   . LEU B 73   ? 0.4895 0.9139 0.4572 -0.1156 0.0423  0.1215  71   LEU B O   
9255  C CB  . LEU B 73   ? 0.5266 0.9266 0.4921 -0.1444 0.0278  0.1340  71   LEU B CB  
9256  C CG  . LEU B 73   ? 0.4945 0.8860 0.4542 -0.1576 0.0224  0.1411  71   LEU B CG  
9257  C CD1 . LEU B 73   ? 0.5137 0.8831 0.4699 -0.1644 0.0161  0.1420  71   LEU B CD1 
9258  C CD2 . LEU B 73   ? 0.5192 0.9077 0.4697 -0.1577 0.0240  0.1425  71   LEU B CD2 
9259  N N   . ILE B 74   ? 0.5114 0.9431 0.4929 -0.1199 0.0386  0.1228  72   ILE B N   
9260  C CA  . ILE B 74   ? 0.5373 0.9720 0.5224 -0.1069 0.0427  0.1156  72   ILE B CA  
9261  C C   . ILE B 74   ? 0.5290 0.9812 0.5155 -0.0982 0.0481  0.1135  72   ILE B C   
9262  O O   . ILE B 74   ? 0.5409 0.9918 0.5256 -0.0872 0.0519  0.1075  72   ILE B O   
9263  C CB  . ILE B 74   ? 0.4298 0.8668 0.4238 -0.1058 0.0411  0.1140  72   ILE B CB  
9264  N N   . GLU B 75   ? 0.5346 1.0033 0.5241 -0.1029 0.0486  0.1183  73   GLU B N   
9265  C CA  . GLU B 75   ? 0.5410 1.0269 0.5316 -0.0949 0.0537  0.1167  73   GLU B CA  
9266  C C   . GLU B 75   ? 0.5044 0.9850 0.4853 -0.0934 0.0559  0.1163  73   GLU B C   
9267  O O   . GLU B 75   ? 0.4928 0.9767 0.4715 -0.0827 0.0602  0.1111  73   GLU B O   
9268  C CB  . GLU B 75   ? 0.5024 1.0081 0.4989 -0.1007 0.0534  0.1223  73   GLU B CB  
9269  N N   . ALA B 76   ? 0.4977 0.9691 0.4721 -0.1041 0.0527  0.1215  74   ALA B N   
9270  C CA  . ALA B 76   ? 0.5305 0.9941 0.4948 -0.1032 0.0541  0.1212  74   ALA B CA  
9271  C C   . ALA B 76   ? 0.5430 0.9907 0.5021 -0.0944 0.0552  0.1145  74   ALA B C   
9272  O O   . ALA B 76   ? 0.5669 1.0150 0.5205 -0.0864 0.0588  0.1107  74   ALA B O   
9273  C CB  . ALA B 76   ? 0.5290 0.9825 0.4872 -0.1165 0.0495  0.1281  74   ALA B CB  
9274  N N   . LEU B 77   ? 0.5634 0.9971 0.5239 -0.0957 0.0520  0.1128  75   LEU B N   
9275  C CA  . LEU B 77   ? 0.5436 0.9620 0.4991 -0.0878 0.0527  0.1066  75   LEU B CA  
9276  C C   . LEU B 77   ? 0.5222 0.9497 0.4815 -0.0741 0.0575  0.0996  75   LEU B C   
9277  O O   . LEU B 77   ? 0.5589 0.9796 0.5120 -0.0659 0.0597  0.0946  75   LEU B O   
9278  C CB  . LEU B 77   ? 0.4717 0.8747 0.4286 -0.0923 0.0483  0.1065  75   LEU B CB  
9279  N N   . ARG B 78   ? 0.5124 0.9545 0.4816 -0.0712 0.0587  0.0991  76   ARG B N   
9280  C CA  . ARG B 78   ? 0.5251 0.9752 0.4980 -0.0580 0.0627  0.0926  76   ARG B CA  
9281  C C   . ARG B 78   ? 0.5641 1.0279 0.5345 -0.0524 0.0669  0.0919  76   ARG B C   
9282  O O   . ARG B 78   ? 0.5455 1.0137 0.5169 -0.0408 0.0702  0.0861  76   ARG B O   
9283  C CB  . ARG B 78   ? 0.5167 0.9767 0.5005 -0.0567 0.0621  0.0923  76   ARG B CB  
9284  C CG  . ARG B 78   ? 0.5345 0.9808 0.5209 -0.0562 0.0595  0.0895  76   ARG B CG  
9285  C CD  . ARG B 78   ? 0.5570 1.0131 0.5538 -0.0528 0.0593  0.0883  76   ARG B CD  
9286  N NE  . ARG B 78   ? 0.5686 1.0119 0.5671 -0.0487 0.0580  0.0837  76   ARG B NE  
9287  C CZ  . ARG B 78   ? 0.6108 1.0585 0.6173 -0.0446 0.0576  0.0816  76   ARG B CZ  
9288  N NH1 . ARG B 78   ? 0.5511 1.0155 0.5645 -0.0439 0.0583  0.0835  76   ARG B NH1 
9289  N NH2 . ARG B 78   ? 0.5898 1.0250 0.5971 -0.0409 0.0565  0.0774  76   ARG B NH2 
9290  N N   . GLY B 79   ? 0.5080 0.9782 0.4752 -0.0603 0.0668  0.0978  77   GLY B N   
9291  C CA  . GLY B 79   ? 0.5314 1.0142 0.4954 -0.0558 0.0708  0.0975  77   GLY B CA  
9292  C C   . GLY B 79   ? 0.5293 1.0002 0.4817 -0.0548 0.0715  0.0963  77   GLY B C   
9293  O O   . GLY B 79   ? 0.5213 1.0001 0.4692 -0.0561 0.0735  0.0987  77   GLY B O   
9294  N N   . LYS B 80   ? 0.5952 1.0471 0.5425 -0.0526 0.0698  0.0925  78   LYS B N   
9295  C CA  . LYS B 80   ? 0.5707 1.0091 0.5064 -0.0508 0.0700  0.0905  78   LYS B CA  
9296  C C   . LYS B 80   ? 0.6082 1.0354 0.5413 -0.0394 0.0710  0.0823  78   LYS B C   
9297  O O   . LYS B 80   ? 0.6090 1.0345 0.5486 -0.0354 0.0705  0.0790  78   LYS B O   
9298  C CB  . LYS B 80   ? 0.5641 0.9869 0.4937 -0.0622 0.0653  0.0956  78   LYS B CB  
9299  C CG  . LYS B 80   ? 0.5655 0.9954 0.4962 -0.0747 0.0633  0.1040  78   LYS B CG  
9300  C CD  . LYS B 80   ? 0.6168 1.0282 0.5427 -0.0849 0.0578  0.1079  78   LYS B CD  
9301  C CE  . LYS B 80   ? 0.6755 1.0903 0.6006 -0.0978 0.0549  0.1163  78   LYS B CE  
9302  N NZ  . LYS B 80   ? 0.6302 1.0254 0.5508 -0.1072 0.0490  0.1197  78   LYS B NZ  
9303  N N   . HIS B 81   ? 0.6371 1.0559 0.5601 -0.0346 0.0722  0.0790  79   HIS B N   
9304  C CA  . HIS B 81   ? 0.6714 1.0777 0.5903 -0.0244 0.0726  0.0712  79   HIS B CA  
9305  C C   . HIS B 81   ? 0.7219 1.1111 0.6402 -0.0279 0.0685  0.0707  79   HIS B C   
9306  O O   . HIS B 81   ? 0.6858 1.0616 0.5965 -0.0345 0.0655  0.0733  79   HIS B O   
9307  C CB  . HIS B 81   ? 0.6617 1.0618 0.5689 -0.0199 0.0740  0.0685  79   HIS B CB  
9308  N N   . GLY B 85   ? 0.5776 0.8799 0.4583 0.0108  0.0608  0.0352  83   GLY B N   
9309  C CA  . GLY B 85   ? 0.5912 0.8928 0.4632 0.0201  0.0630  0.0296  83   GLY B CA  
9310  C C   . GLY B 85   ? 0.6228 0.9129 0.4970 0.0301  0.0617  0.0211  83   GLY B C   
9311  O O   . GLY B 85   ? 0.5992 0.8914 0.4679 0.0394  0.0642  0.0157  83   GLY B O   
9312  N N   . VAL B 86   ? 0.6274 0.9048 0.5092 0.0281  0.0576  0.0200  84   VAL B N   
9313  C CA  . VAL B 86   ? 0.6200 0.8864 0.5046 0.0368  0.0561  0.0125  84   VAL B CA  
9314  C C   . VAL B 86   ? 0.5943 0.8766 0.4846 0.0444  0.0609  0.0102  84   VAL B C   
9315  O O   . VAL B 86   ? 0.5853 0.8635 0.4734 0.0542  0.0616  0.0036  84   VAL B O   
9316  C CB  . VAL B 86   ? 0.6005 0.8506 0.4918 0.0322  0.0507  0.0124  84   VAL B CB  
9317  C CG1 . VAL B 86   ? 0.6028 0.8508 0.5021 0.0389  0.0508  0.0076  84   VAL B CG1 
9318  C CG2 . VAL B 86   ? 0.5985 0.8283 0.4830 0.0313  0.0457  0.0099  84   VAL B CG2 
9319  N N   . GLU B 87   ? 0.6309 0.9314 0.5280 0.0402  0.0641  0.0156  85   GLU B N   
9320  C CA  . GLU B 87   ? 0.5932 0.9107 0.4957 0.0474  0.0688  0.0138  85   GLU B CA  
9321  C C   . GLU B 87   ? 0.5599 0.8819 0.4568 0.0556  0.0714  0.0101  85   GLU B C   
9322  O O   . GLU B 87   ? 0.5468 0.8696 0.4463 0.0650  0.0725  0.0049  85   GLU B O   
9323  C CB  . GLU B 87   ? 0.6161 0.9504 0.5279 0.0399  0.0704  0.0209  85   GLU B CB  
9324  N N   . GLY B 88   ? 0.5873 0.9112 0.4764 0.0520  0.0720  0.0128  86   GLY B N   
9325  C CA  . GLY B 88   ? 0.5683 0.8960 0.4517 0.0594  0.0744  0.0094  86   GLY B CA  
9326  C C   . GLY B 88   ? 0.5615 0.8729 0.4360 0.0679  0.0726  0.0016  86   GLY B C   
9327  O O   . GLY B 88   ? 0.5305 0.8431 0.4026 0.0769  0.0741  -0.0033 86   GLY B O   
9328  N N   . LEU B 89   ? 0.5538 0.8495 0.4231 0.0652  0.0690  0.0004  87   LEU B N   
9329  C CA  . LEU B 89   ? 0.5774 0.8565 0.4390 0.0729  0.0665  -0.0072 87   LEU B CA  
9330  C C   . LEU B 89   ? 0.4904 0.7661 0.3585 0.0813  0.0664  -0.0129 87   LEU B C   
9331  O O   . LEU B 89   ? 0.4675 0.7381 0.3319 0.0904  0.0664  -0.0189 87   LEU B O   
9332  C CB  . LEU B 89   ? 0.5563 0.8163 0.4151 0.0664  0.0609  -0.0066 87   LEU B CB  
9333  C CG  . LEU B 89   ? 0.6030 0.8452 0.4515 0.0700  0.0573  -0.0119 87   LEU B CG  
9334  C CD1 . LEU B 89   ? 0.6034 0.8286 0.4527 0.0617  0.0513  -0.0095 87   LEU B CD1 
9335  C CD2 . LEU B 89   ? 0.5631 0.7958 0.4109 0.0804  0.0563  -0.0201 87   LEU B CD2 
9336  N N   . VAL B 90   ? 0.5152 0.7928 0.3931 0.0781  0.0657  -0.0108 88   VAL B N   
9337  C CA  . VAL B 90   ? 0.4895 0.7645 0.3739 0.0854  0.0655  -0.0154 88   VAL B CA  
9338  C C   . VAL B 90   ? 0.5339 0.8208 0.4216 0.0926  0.0686  -0.0169 88   VAL B C   
9339  O O   . VAL B 90   ? 0.5202 0.8004 0.4071 0.1018  0.0680  -0.0229 88   VAL B O   
9340  C CB  . VAL B 90   ? 0.4571 0.7316 0.3534 0.0787  0.0635  -0.0116 88   VAL B CB  
9341  C CG1 . VAL B 90   ? 0.4384 0.7138 0.3417 0.0862  0.0641  -0.0155 88   VAL B CG1 
9342  C CG2 . VAL B 90   ? 0.4930 0.7472 0.3894 0.0718  0.0577  -0.0111 88   VAL B CG2 
9343  N N   . GLN B 91   ? 0.5143 0.8184 0.4054 0.0885  0.0717  -0.0113 89   GLN B N   
9344  C CA  . GLN B 91   ? 0.4904 0.8071 0.3845 0.0952  0.0746  -0.0124 89   GLN B CA  
9345  C C   . GLN B 91   ? 0.4986 0.8102 0.3825 0.1025  0.0751  -0.0173 89   GLN B C   
9346  O O   . GLN B 91   ? 0.5014 0.8125 0.3853 0.1119  0.0755  -0.0221 89   GLN B O   
9347  C CB  . GLN B 91   ? 0.5338 0.8704 0.4341 0.0882  0.0774  -0.0050 89   GLN B CB  
9348  N N   . GLU B 92   ? 0.4966 0.8038 0.3713 0.0985  0.0748  -0.0162 90   GLU B N   
9349  C CA  . GLU B 92   ? 0.5364 0.8395 0.4010 0.1049  0.0753  -0.0205 90   GLU B CA  
9350  C C   . GLU B 92   ? 0.4938 0.7794 0.3537 0.1140  0.0724  -0.0286 90   GLU B C   
9351  O O   . GLU B 92   ? 0.4467 0.7317 0.3024 0.1225  0.0731  -0.0332 90   GLU B O   
9352  C CB  . GLU B 92   ? 0.4933 0.7927 0.3485 0.0983  0.0747  -0.0177 90   GLU B CB  
9353  C CG  . GLU B 92   ? 0.6134 0.9088 0.4575 0.1043  0.0753  -0.0218 90   GLU B CG  
9354  C CD  . GLU B 92   ? 0.6000 0.8895 0.4342 0.0980  0.0741  -0.0194 90   GLU B CD  
9355  O OE1 . GLU B 92   ? 0.6909 0.9796 0.5266 0.0887  0.0727  -0.0142 90   GLU B OE1 
9356  O OE2 . GLU B 92   ? 0.6267 0.9117 0.4510 0.1022  0.0742  -0.0227 90   GLU B OE2 
9357  N N   . TYR B 93   ? 0.4824 0.7534 0.3424 0.1124  0.0689  -0.0306 91   TYR B N   
9358  C CA  . TYR B 93   ? 0.4582 0.7115 0.3136 0.1201  0.0656  -0.0381 91   TYR B CA  
9359  C C   . TYR B 93   ? 0.4738 0.7247 0.3379 0.1244  0.0647  -0.0403 91   TYR B C   
9360  O O   . TYR B 93   ? 0.4884 0.7232 0.3498 0.1294  0.0614  -0.0459 91   TYR B O   
9361  C CB  . TYR B 93   ? 0.4602 0.6967 0.3080 0.1162  0.0617  -0.0396 91   TYR B CB  
9362  C CG  . TYR B 93   ? 0.4500 0.6845 0.2865 0.1149  0.0617  -0.0396 91   TYR B CG  
9363  C CD1 . TYR B 93   ? 0.4670 0.6908 0.2944 0.1222  0.0601  -0.0457 91   TYR B CD1 
9364  C CD2 . TYR B 93   ? 0.4922 0.7358 0.3272 0.1063  0.0633  -0.0332 91   TYR B CD2 
9365  C CE1 . TYR B 93   ? 0.5163 0.7386 0.3334 0.1211  0.0602  -0.0457 91   TYR B CE1 
9366  C CE2 . TYR B 93   ? 0.4928 0.7347 0.3175 0.1051  0.0633  -0.0329 91   TYR B CE2 
9367  C CZ  . TYR B 93   ? 0.5092 0.7406 0.3249 0.1126  0.0618  -0.0392 91   TYR B CZ  
9368  O OH  . TYR B 93   ? 0.5834 0.8132 0.3886 0.1113  0.0617  -0.0389 91   TYR B OH  
9369  N N   . SER B 94   ? 0.4234 0.6898 0.2979 0.1224  0.0673  -0.0360 92   SER B N   
9370  C CA  . SER B 94   ? 0.4111 0.6771 0.2945 0.1259  0.0665  -0.0373 92   SER B CA  
9371  C C   . SER B 94   ? 0.4607 0.7098 0.3445 0.1244  0.0627  -0.0398 92   SER B C   
9372  O O   . SER B 94   ? 0.4514 0.6884 0.3349 0.1308  0.0602  -0.0449 92   SER B O   
9373  C CB  . SER B 94   ? 0.4333 0.6985 0.3156 0.1366  0.0667  -0.0422 92   SER B CB  
9374  O OG  . SER B 94   ? 0.4854 0.7648 0.3656 0.1388  0.0700  -0.0408 92   SER B OG  
9375  N N   . LEU B 95   ? 0.3871 0.6354 0.2712 0.1156  0.0621  -0.0359 93   LEU B N   
9376  C CA  . LEU B 95   ? 0.4013 0.6342 0.2857 0.1133  0.0583  -0.0379 93   LEU B CA  
9377  C C   . LEU B 95   ? 0.4120 0.6483 0.3087 0.1107  0.0579  -0.0352 93   LEU B C   
9378  O O   . LEU B 95   ? 0.4265 0.6795 0.3299 0.1065  0.0609  -0.0299 93   LEU B O   
9379  C CB  . LEU B 95   ? 0.4150 0.6400 0.2968 0.1032  0.0554  -0.0340 93   LEU B CB  
9380  C CG  . LEU B 95   ? 0.4273 0.6481 0.2966 0.1044  0.0553  -0.0359 93   LEU B CG  
9381  C CD1 . LEU B 95   ? 0.3954 0.6080 0.2632 0.0942  0.0519  -0.0317 93   LEU B CD1 
9382  C CD2 . LEU B 95   ? 0.4055 0.6110 0.2676 0.1131  0.0527  -0.0437 93   LEU B CD2 
9383  N N   . SER B 96   ? 0.3532 0.5738 0.2526 0.1129  0.0541  -0.0389 94   SER B N   
9384  C CA  . SER B 96   ? 0.3458 0.5657 0.2562 0.1083  0.0525  -0.0360 94   SER B CA  
9385  C C   . SER B 96   ? 0.3166 0.5325 0.2299 0.0967  0.0501  -0.0307 94   SER B C   
9386  O O   . SER B 96   ? 0.3325 0.5429 0.2392 0.0929  0.0488  -0.0301 94   SER B O   
9387  C CB  . SER B 96   ? 0.3521 0.5551 0.2637 0.1130  0.0487  -0.0410 94   SER B CB  
9388  O OG  . SER B 96   ? 0.3199 0.5040 0.2274 0.1094  0.0441  -0.0428 94   SER B OG  
9389  N N   . SER B 97   ? 0.2837 0.5022 0.2067 0.0913  0.0493  -0.0271 95   SER B N   
9390  C CA  . SER B 97   ? 0.3298 0.5423 0.2558 0.0809  0.0464  -0.0227 95   SER B CA  
9391  C C   . SER B 97   ? 0.3381 0.5295 0.2602 0.0796  0.0415  -0.0259 95   SER B C   
9392  O O   . SER B 97   ? 0.3163 0.5019 0.2344 0.0737  0.0395  -0.0239 95   SER B O   
9393  C CB  . SER B 97   ? 0.3129 0.5303 0.2495 0.0765  0.0461  -0.0191 95   SER B CB  
9394  O OG  . SER B 97   ? 0.4160 0.6540 0.3562 0.0766  0.0505  -0.0155 95   SER B OG  
9395  N N   . GLN B 98   ? 0.2942 0.4739 0.2174 0.0849  0.0392  -0.0306 96   GLN B N   
9396  C CA  . GLN B 98   ? 0.3144 0.4749 0.2343 0.0836  0.0345  -0.0336 96   GLN B CA  
9397  C C   . GLN B 98   ? 0.3279 0.4835 0.2372 0.0858  0.0340  -0.0362 96   GLN B C   
9398  O O   . GLN B 98   ? 0.3130 0.4572 0.2192 0.0815  0.0305  -0.0362 96   GLN B O   
9399  C CB  . GLN B 98   ? 0.3125 0.4624 0.2350 0.0892  0.0324  -0.0382 96   GLN B CB  
9400  C CG  . GLN B 98   ? 0.3034 0.4522 0.2359 0.0855  0.0312  -0.0359 96   GLN B CG  
9401  C CD  . GLN B 98   ? 0.3017 0.4420 0.2372 0.0768  0.0278  -0.0331 96   GLN B CD  
9402  O OE1 . GLN B 98   ? 0.3721 0.5194 0.3092 0.0703  0.0286  -0.0285 96   GLN B OE1 
9403  N NE2 . GLN B 98   ? 0.2947 0.4197 0.2307 0.0766  0.0239  -0.0358 96   GLN B NE2 
9404  N N   . GLU B 99   ? 0.3223 0.4867 0.2258 0.0927  0.0375  -0.0384 97   GLU B N   
9405  C CA  . GLU B 99   ? 0.3357 0.4963 0.2283 0.0948  0.0372  -0.0407 97   GLU B CA  
9406  C C   . GLU B 99   ? 0.3392 0.5063 0.2296 0.0869  0.0380  -0.0354 97   GLU B C   
9407  O O   . GLU B 99   ? 0.3253 0.4833 0.2088 0.0846  0.0354  -0.0361 97   GLU B O   
9408  C CB  . GLU B 99   ? 0.3189 0.4881 0.2055 0.1045  0.0409  -0.0445 97   GLU B CB  
9409  C CG  . GLU B 99   ? 0.3037 0.4609 0.1884 0.1128  0.0389  -0.0510 97   GLU B CG  
9410  C CD  . GLU B 99   ? 0.3501 0.5173 0.2304 0.1231  0.0428  -0.0545 97   GLU B CD  
9411  O OE1 . GLU B 99   ? 0.3432 0.5283 0.2233 0.1236  0.0476  -0.0516 97   GLU B OE1 
9412  O OE2 . GLU B 99   ? 0.3739 0.5311 0.2511 0.1306  0.0411  -0.0601 97   GLU B OE2 
9413  N N   . GLY B 100  ? 0.3407 0.5232 0.2367 0.0826  0.0411  -0.0300 98   GLY B N   
9414  C CA  . GLY B 100  ? 0.3794 0.5674 0.2734 0.0745  0.0415  -0.0244 98   GLY B CA  
9415  C C   . GLY B 100  ? 0.3370 0.5107 0.2329 0.0668  0.0365  -0.0226 98   GLY B C   
9416  O O   . GLY B 100  ? 0.3347 0.5033 0.2243 0.0628  0.0347  -0.0212 98   GLY B O   
9417  N N   . VAL B 101  ? 0.3155 0.4825 0.2197 0.0649  0.0342  -0.0227 99   VAL B N   
9418  C CA  . VAL B 101  ? 0.3587 0.5122 0.2652 0.0585  0.0294  -0.0214 99   VAL B CA  
9419  C C   . VAL B 101  ? 0.3473 0.4852 0.2471 0.0611  0.0257  -0.0260 99   VAL B C   
9420  O O   . VAL B 101  ? 0.3099 0.4398 0.2064 0.0562  0.0226  -0.0245 99   VAL B O   
9421  C CB  . VAL B 101  ? 0.3063 0.4567 0.2229 0.0570  0.0281  -0.0211 99   VAL B CB  
9422  C CG1 . VAL B 101  ? 0.2951 0.4310 0.2138 0.0515  0.0232  -0.0206 99   VAL B CG1 
9423  C CG2 . VAL B 101  ? 0.3192 0.4850 0.2424 0.0534  0.0312  -0.0161 99   VAL B CG2 
9424  N N   . ALA B 102  ? 0.3233 0.4563 0.2208 0.0688  0.0257  -0.0316 100  ALA B N   
9425  C CA  . ALA B 102  ? 0.3198 0.4379 0.2109 0.0713  0.0219  -0.0361 100  ALA B CA  
9426  C C   . ALA B 102  ? 0.3433 0.4623 0.2241 0.0709  0.0221  -0.0358 100  ALA B C   
9427  O O   . ALA B 102  ? 0.3658 0.4734 0.2425 0.0685  0.0182  -0.0367 100  ALA B O   
9428  C CB  . ALA B 102  ? 0.3198 0.4330 0.2096 0.0798  0.0220  -0.0420 100  ALA B CB  
9429  N N   . LEU B 103  ? 0.3118 0.4448 0.1885 0.0734  0.0267  -0.0346 101  LEU B N   
9430  C CA  . LEU B 103  ? 0.3834 0.5184 0.2497 0.0732  0.0273  -0.0341 101  LEU B CA  
9431  C C   . LEU B 103  ? 0.3511 0.4847 0.2173 0.0641  0.0252  -0.0286 101  LEU B C   
9432  O O   . LEU B 103  ? 0.3416 0.4670 0.2005 0.0625  0.0223  -0.0291 101  LEU B O   
9433  C CB  . LEU B 103  ? 0.3736 0.5258 0.2364 0.0776  0.0331  -0.0334 101  LEU B CB  
9434  C CG  . LEU B 103  ? 0.3487 0.5062 0.2007 0.0771  0.0347  -0.0321 101  LEU B CG  
9435  C CD1 . LEU B 103  ? 0.3448 0.4900 0.1868 0.0828  0.0320  -0.0382 101  LEU B CD1 
9436  C CD2 . LEU B 103  ? 0.3784 0.5558 0.2297 0.0803  0.0409  -0.0303 101  LEU B CD2 
9437  N N   . MET B 104  ? 0.3240 0.4652 0.1979 0.0582  0.0264  -0.0233 102  MET B N   
9438  C CA  . MET B 104  ? 0.3753 0.5142 0.2492 0.0495  0.0240  -0.0180 102  MET B CA  
9439  C C   . MET B 104  ? 0.3579 0.4793 0.2329 0.0470  0.0182  -0.0197 102  MET B C   
9440  O O   . MET B 104  ? 0.3926 0.5081 0.2629 0.0424  0.0154  -0.0174 102  MET B O   
9441  C CB  . MET B 104  ? 0.3470 0.4965 0.2290 0.0438  0.0261  -0.0123 102  MET B CB  
9442  C CG  . MET B 104  ? 0.3451 0.5138 0.2264 0.0455  0.0319  -0.0100 102  MET B CG  
9443  S SD  . MET B 104  ? 0.4799 0.6554 0.3487 0.0451  0.0341  -0.0080 102  MET B SD  
9444  C CE  . MET B 104  ? 0.5368 0.7089 0.4058 0.0335  0.0309  -0.0007 102  MET B CE  
9445  N N   . CYS B 105  ? 0.2857 0.3991 0.1667 0.0500  0.0163  -0.0235 103  CYS B N   
9446  C CA  . CYS B 105  ? 0.3505 0.4482 0.2327 0.0483  0.0110  -0.0255 103  CYS B CA  
9447  C C   . CYS B 105  ? 0.3897 0.4791 0.2623 0.0512  0.0086  -0.0290 103  CYS B C   
9448  O O   . CYS B 105  ? 0.3940 0.4744 0.2639 0.0476  0.0045  -0.0282 103  CYS B O   
9449  C CB  . CYS B 105  ? 0.2898 0.3816 0.1798 0.0513  0.0099  -0.0290 103  CYS B CB  
9450  S SG  . CYS B 105  ? 0.3382 0.4366 0.2397 0.0470  0.0113  -0.0250 103  CYS B SG  
9451  N N   . LEU B 106  ? 0.3326 0.4246 0.1996 0.0581  0.0108  -0.0331 104  LEU B N   
9452  C CA  . LEU B 106  ? 0.3548 0.4396 0.2115 0.0612  0.0087  -0.0366 104  LEU B CA  
9453  C C   . LEU B 106  ? 0.3996 0.4887 0.2487 0.0570  0.0090  -0.0325 104  LEU B C   
9454  O O   . LEU B 106  ? 0.3791 0.4590 0.2221 0.0556  0.0052  -0.0333 104  LEU B O   
9455  C CB  . LEU B 106  ? 0.3680 0.4559 0.2195 0.0696  0.0114  -0.0416 104  LEU B CB  
9456  C CG  . LEU B 106  ? 0.3817 0.4629 0.2212 0.0731  0.0095  -0.0454 104  LEU B CG  
9457  C CD1 . LEU B 106  ? 0.4428 0.5074 0.2827 0.0727  0.0035  -0.0489 104  LEU B CD1 
9458  C CD2 . LEU B 106  ? 0.3905 0.4775 0.2233 0.0816  0.0131  -0.0497 104  LEU B CD2 
9459  N N   . ALA B 107  ? 0.3501 0.4534 0.1993 0.0550  0.0135  -0.0281 105  ALA B N   
9460  C CA  . ALA B 107  ? 0.4082 0.5162 0.2500 0.0506  0.0140  -0.0237 105  ALA B CA  
9461  C C   . ALA B 107  ? 0.4025 0.5018 0.2466 0.0429  0.0094  -0.0197 105  ALA B C   
9462  O O   . ALA B 107  ? 0.4329 0.5276 0.2693 0.0404  0.0070  -0.0182 105  ALA B O   
9463  C CB  . ALA B 107  ? 0.3987 0.5245 0.2412 0.0493  0.0197  -0.0192 105  ALA B CB  
9464  N N   . GLU B 108  ? 0.4116 0.5083 0.2658 0.0396  0.0081  -0.0182 106  GLU B N   
9465  C CA  . GLU B 108  ? 0.4718 0.5593 0.3287 0.0332  0.0035  -0.0151 106  GLU B CA  
9466  C C   . GLU B 108  ? 0.4892 0.5622 0.3429 0.0349  -0.0018 -0.0190 106  GLU B C   
9467  O O   . GLU B 108  ? 0.4823 0.5490 0.3312 0.0312  -0.0053 -0.0169 106  GLU B O   
9468  C CB  . GLU B 108  ? 0.3960 0.4839 0.2644 0.0304  0.0034  -0.0135 106  GLU B CB  
9469  C CG  . GLU B 108  ? 0.4984 0.5748 0.3706 0.0256  -0.0018 -0.0120 106  GLU B CG  
9470  C CD  . GLU B 108  ? 0.5091 0.5841 0.3922 0.0245  -0.0022 -0.0122 106  GLU B CD  
9471  O OE1 . GLU B 108  ? 0.4779 0.5622 0.3660 0.0259  0.0017  -0.0119 106  GLU B OE1 
9472  O OE2 . GLU B 108  ? 0.6039 0.6687 0.4907 0.0224  -0.0064 -0.0126 106  GLU B OE2 
9473  N N   . ALA B 109  ? 0.4616 0.5291 0.3176 0.0403  -0.0026 -0.0247 107  ALA B N   
9474  C CA  . ALA B 109  ? 0.4842 0.5386 0.3371 0.0420  -0.0076 -0.0286 107  ALA B CA  
9475  C C   . ALA B 109  ? 0.4850 0.5381 0.3259 0.0433  -0.0085 -0.0293 107  ALA B C   
9476  O O   . ALA B 109  ? 0.4882 0.5322 0.3256 0.0411  -0.0131 -0.0292 107  ALA B O   
9477  C CB  . ALA B 109  ? 0.4995 0.5493 0.3562 0.0476  -0.0079 -0.0343 107  ALA B CB  
9478  N N   . LEU B 110  ? 0.4062 0.4685 0.2405 0.0469  -0.0041 -0.0299 108  LEU B N   
9479  C CA  . LEU B 110  ? 0.4872 0.5487 0.3092 0.0485  -0.0046 -0.0308 108  LEU B CA  
9480  C C   . LEU B 110  ? 0.5059 0.5689 0.3237 0.0420  -0.0058 -0.0248 108  LEU B C   
9481  O O   . LEU B 110  ? 0.4994 0.5565 0.3083 0.0417  -0.0088 -0.0251 108  LEU B O   
9482  C CB  . LEU B 110  ? 0.4841 0.5563 0.3001 0.0542  0.0008  -0.0328 108  LEU B CB  
9483  C CG  . LEU B 110  ? 0.5099 0.5787 0.3264 0.0619  0.0013  -0.0396 108  LEU B CG  
9484  C CD1 . LEU B 110  ? 0.4167 0.4984 0.2287 0.0674  0.0073  -0.0408 108  LEU B CD1 
9485  C CD2 . LEU B 110  ? 0.5089 0.5641 0.3185 0.0647  -0.0037 -0.0447 108  LEU B CD2 
9486  N N   . LEU B 111  ? 0.4830 0.5531 0.3064 0.0368  -0.0038 -0.0192 109  LEU B N   
9487  C CA  . LEU B 111  ? 0.5548 0.6249 0.3745 0.0301  -0.0055 -0.0132 109  LEU B CA  
9488  C C   . LEU B 111  ? 0.5729 0.6295 0.3955 0.0265  -0.0118 -0.0126 109  LEU B C   
9489  O O   . LEU B 111  ? 0.5756 0.6295 0.3939 0.0216  -0.0143 -0.0082 109  LEU B O   
9490  C CB  . LEU B 111  ? 0.5214 0.6032 0.3461 0.0254  -0.0016 -0.0075 109  LEU B CB  
9491  C CG  . LEU B 111  ? 0.4843 0.5814 0.3049 0.0284  0.0048  -0.0070 109  LEU B CG  
9492  C CD1 . LEU B 111  ? 0.5250 0.6339 0.3533 0.0245  0.0085  -0.0024 109  LEU B CD1 
9493  C CD2 . LEU B 111  ? 0.5354 0.6357 0.3436 0.0273  0.0054  -0.0047 109  LEU B CD2 
9494  N N   . ARG B 112  ? 0.5805 0.6289 0.4104 0.0289  -0.0146 -0.0168 110  ARG B N   
9495  C CA  . ARG B 112  ? 0.5993 0.6353 0.4309 0.0266  -0.0207 -0.0171 110  ARG B CA  
9496  C C   . ARG B 112  ? 0.6074 0.6361 0.4294 0.0289  -0.0243 -0.0198 110  ARG B C   
9497  O O   . ARG B 112  ? 0.6478 0.6667 0.4701 0.0272  -0.0297 -0.0199 110  ARG B O   
9498  C CB  . ARG B 112  ? 0.5532 0.5838 0.3958 0.0282  -0.0224 -0.0204 110  ARG B CB  
9499  C CG  . ARG B 112  ? 0.5877 0.6244 0.4397 0.0256  -0.0194 -0.0176 110  ARG B CG  
9500  C CD  . ARG B 112  ? 0.7046 0.7349 0.5673 0.0258  -0.0218 -0.0198 110  ARG B CD  
9501  N NE  . ARG B 112  ? 0.6941 0.7244 0.5605 0.0309  -0.0204 -0.0249 110  ARG B NE  
9502  C CZ  . ARG B 112  ? 0.7227 0.7589 0.5961 0.0322  -0.0168 -0.0254 110  ARG B CZ  
9503  N NH1 . ARG B 112  ? 0.7001 0.7433 0.5779 0.0287  -0.0143 -0.0212 110  ARG B NH1 
9504  N NH2 . ARG B 112  ? 0.7687 0.8033 0.6444 0.0371  -0.0161 -0.0301 110  ARG B NH2 
9505  N N   . ILE B 113  ? 0.5926 0.6262 0.4059 0.0327  -0.0215 -0.0219 111  ILE B N   
9506  C CA  . ILE B 113  ? 0.5746 0.6025 0.3768 0.0346  -0.0245 -0.0240 111  ILE B CA  
9507  C C   . ILE B 113  ? 0.6728 0.7065 0.4659 0.0309  -0.0231 -0.0186 111  ILE B C   
9508  O O   . ILE B 113  ? 0.6367 0.6815 0.4254 0.0321  -0.0178 -0.0174 111  ILE B O   
9509  C CB  . ILE B 113  ? 0.5637 0.5925 0.3610 0.0415  -0.0225 -0.0302 111  ILE B CB  
9510  C CG1 . ILE B 113  ? 0.6006 0.6244 0.4074 0.0446  -0.0235 -0.0349 111  ILE B CG1 
9511  C CG2 . ILE B 113  ? 0.5701 0.5921 0.3560 0.0434  -0.0262 -0.0327 111  ILE B CG2 
9512  C CD1 . ILE B 113  ? 0.6200 0.6437 0.4224 0.0515  -0.0218 -0.0410 111  ILE B CD1 
9513  N N   . PRO B 114  ? 0.7294 0.7563 0.5194 0.0265  -0.0277 -0.0151 112  PRO B N   
9514  C CA  . PRO B 114  ? 0.6478 0.6800 0.4305 0.0216  -0.0265 -0.0086 112  PRO B CA  
9515  C C   . PRO B 114  ? 0.6226 0.6587 0.3917 0.0236  -0.0250 -0.0089 112  PRO B C   
9516  O O   . PRO B 114  ? 0.6322 0.6768 0.3957 0.0204  -0.0217 -0.0038 112  PRO B O   
9517  C CB  . PRO B 114  ? 0.6757 0.6973 0.4598 0.0169  -0.0327 -0.0054 112  PRO B CB  
9518  C CG  . PRO B 114  ? 0.6711 0.6821 0.4584 0.0206  -0.0376 -0.0111 112  PRO B CG  
9519  C CD  . PRO B 114  ? 0.6668 0.6815 0.4614 0.0252  -0.0342 -0.0162 112  PRO B CD  
9520  N N   . ASP B 115  ? 0.6198 0.6499 0.3828 0.0287  -0.0272 -0.0145 113  ASP B N   
9521  C CA  . ASP B 115  ? 0.6821 0.7157 0.4314 0.0309  -0.0258 -0.0151 113  ASP B CA  
9522  C C   . ASP B 115  ? 0.6824 0.7273 0.4299 0.0361  -0.0191 -0.0181 113  ASP B C   
9523  O O   . ASP B 115  ? 0.6468 0.6900 0.3994 0.0412  -0.0184 -0.0238 113  ASP B O   
9524  C CB  . ASP B 115  ? 0.6534 0.6754 0.3960 0.0339  -0.0315 -0.0198 113  ASP B CB  
9525  C CG  . ASP B 115  ? 0.7299 0.7552 0.4576 0.0367  -0.0300 -0.0209 113  ASP B CG  
9526  O OD1 . ASP B 115  ? 0.8267 0.8568 0.5468 0.0328  -0.0289 -0.0153 113  ASP B OD1 
9527  O OD2 . ASP B 115  ? 0.7611 0.7840 0.4842 0.0427  -0.0301 -0.0272 113  ASP B OD2 
9528  N N   . THR B 116  ? 0.6674 0.7239 0.4075 0.0349  -0.0144 -0.0143 114  THR B N   
9529  C CA  . THR B 116  ? 0.6938 0.7630 0.4322 0.0400  -0.0077 -0.0166 114  THR B CA  
9530  C C   . THR B 116  ? 0.6916 0.7560 0.4231 0.0480  -0.0082 -0.0245 114  THR B C   
9531  O O   . THR B 116  ? 0.6663 0.7341 0.4019 0.0536  -0.0052 -0.0291 114  THR B O   
9532  C CB  . THR B 116  ? 0.7177 0.8003 0.4481 0.0370  -0.0029 -0.0108 114  THR B CB  
9533  O OG1 . THR B 116  ? 0.7466 0.8340 0.4843 0.0294  -0.0021 -0.0035 114  THR B OG1 
9534  C CG2 . THR B 116  ? 0.7486 0.8452 0.4764 0.0430  0.0041  -0.0135 114  THR B CG2 
9535  N N   . ALA B 117  ? 0.7241 0.7800 0.4449 0.0486  -0.0125 -0.0261 115  ALA B N   
9536  C CA  . ALA B 117  ? 0.6801 0.7308 0.3929 0.0560  -0.0135 -0.0336 115  ALA B CA  
9537  C C   . ALA B 117  ? 0.6713 0.7111 0.3929 0.0592  -0.0172 -0.0395 115  ALA B C   
9538  O O   . ALA B 117  ? 0.6883 0.7274 0.4080 0.0658  -0.0157 -0.0457 115  ALA B O   
9539  C CB  . ALA B 117  ? 0.7403 0.7838 0.4398 0.0553  -0.0179 -0.0337 115  ALA B CB  
9540  N N   . THR B 118  ? 0.6667 0.6980 0.3975 0.0545  -0.0220 -0.0376 116  THR B N   
9541  C CA  . THR B 118  ? 0.6799 0.7018 0.4198 0.0568  -0.0253 -0.0426 116  THR B CA  
9542  C C   . THR B 118  ? 0.6153 0.6446 0.3649 0.0593  -0.0203 -0.0437 116  THR B C   
9543  O O   . THR B 118  ? 0.6194 0.6449 0.3708 0.0646  -0.0203 -0.0495 116  THR B O   
9544  C CB  . THR B 118  ? 0.6197 0.6327 0.3678 0.0512  -0.0311 -0.0398 116  THR B CB  
9545  O OG1 . THR B 118  ? 0.7053 0.7116 0.4443 0.0489  -0.0360 -0.0385 116  THR B OG1 
9546  C CG2 . THR B 118  ? 0.6410 0.6449 0.3979 0.0534  -0.0346 -0.0448 116  THR B CG2 
9547  N N   . ARG B 119  ? 0.6309 0.6705 0.3867 0.0554  -0.0162 -0.0381 117  ARG B N   
9548  C CA  . ARG B 119  ? 0.5883 0.6360 0.3533 0.0575  -0.0113 -0.0386 117  ARG B CA  
9549  C C   . ARG B 119  ? 0.5874 0.6429 0.3456 0.0648  -0.0064 -0.0427 117  ARG B C   
9550  O O   . ARG B 119  ? 0.5669 0.6215 0.3297 0.0699  -0.0051 -0.0474 117  ARG B O   
9551  C CB  . ARG B 119  ? 0.5961 0.6539 0.3676 0.0514  -0.0082 -0.0314 117  ARG B CB  
9552  C CG  . ARG B 119  ? 0.5001 0.5668 0.2815 0.0530  -0.0034 -0.0314 117  ARG B CG  
9553  C CD  . ARG B 119  ? 0.5872 0.6654 0.3727 0.0471  0.0001  -0.0241 117  ARG B CD  
9554  N NE  . ARG B 119  ? 0.6189 0.6916 0.4035 0.0398  -0.0039 -0.0189 117  ARG B NE  
9555  C CZ  . ARG B 119  ? 0.6763 0.7551 0.4540 0.0354  -0.0027 -0.0133 117  ARG B CZ  
9556  N NH1 . ARG B 119  ? 0.5958 0.6878 0.3671 0.0371  0.0028  -0.0120 117  ARG B NH1 
9557  N NH2 . ARG B 119  ? 0.6842 0.7560 0.4612 0.0291  -0.0070 -0.0088 117  ARG B NH2 
9558  N N   . ASP B 120  ? 0.6277 0.6907 0.3745 0.0656  -0.0036 -0.0412 118  ASP B N   
9559  C CA  . ASP B 120  ? 0.6502 0.7219 0.3898 0.0729  0.0014  -0.0450 118  ASP B CA  
9560  C C   . ASP B 120  ? 0.6336 0.6937 0.3672 0.0799  -0.0018 -0.0532 118  ASP B C   
9561  O O   . ASP B 120  ? 0.6142 0.6781 0.3461 0.0871  0.0015  -0.0579 118  ASP B O   
9562  C CB  . ASP B 120  ? 0.6704 0.7524 0.3984 0.0719  0.0048  -0.0414 118  ASP B CB  
9563  C CG  . ASP B 120  ? 0.6926 0.7891 0.4260 0.0661  0.0094  -0.0337 118  ASP B CG  
9564  O OD1 . ASP B 120  ? 0.7124 0.8099 0.4585 0.0625  0.0095  -0.0311 118  ASP B OD1 
9565  O OD2 . ASP B 120  ? 0.7375 0.8444 0.4624 0.0649  0.0129  -0.0302 118  ASP B OD2 
9566  N N   . ALA B 121  ? 0.6727 0.7187 0.4027 0.0781  -0.0084 -0.0550 119  ALA B N   
9567  C CA  . ALA B 121  ? 0.6422 0.6762 0.3667 0.0840  -0.0122 -0.0626 119  ALA B CA  
9568  C C   . ALA B 121  ? 0.6616 0.6891 0.3977 0.0857  -0.0138 -0.0660 119  ALA B C   
9569  O O   . ALA B 121  ? 0.6737 0.6966 0.4069 0.0922  -0.0138 -0.0722 119  ALA B O   
9570  C CB  . ALA B 121  ? 0.6852 0.7070 0.4027 0.0812  -0.0190 -0.0633 119  ALA B CB  
9571  N N   . LEU B 122  ? 0.6069 0.6333 0.3556 0.0799  -0.0152 -0.0620 120  LEU B N   
9572  C CA  . LEU B 122  ? 0.6187 0.6404 0.3786 0.0812  -0.0161 -0.0646 120  LEU B CA  
9573  C C   . LEU B 122  ? 0.6053 0.6374 0.3679 0.0864  -0.0098 -0.0659 120  LEU B C   
9574  O O   . LEU B 122  ? 0.5962 0.6231 0.3615 0.0912  -0.0103 -0.0707 120  LEU B O   
9575  C CB  . LEU B 122  ? 0.6053 0.6257 0.3778 0.0741  -0.0181 -0.0597 120  LEU B CB  
9576  C CG  . LEU B 122  ? 0.6234 0.6396 0.4079 0.0748  -0.0189 -0.0617 120  LEU B CG  
9577  C CD1 . LEU B 122  ? 0.6282 0.6299 0.4115 0.0767  -0.0248 -0.0672 120  LEU B CD1 
9578  C CD2 . LEU B 122  ? 0.5851 0.6040 0.3819 0.0684  -0.0189 -0.0563 120  LEU B CD2 
9579  N N   . ILE B 123  ? 0.5598 0.6066 0.3216 0.0855  -0.0041 -0.0614 121  ILE B N   
9580  C CA  . ILE B 123  ? 0.5992 0.6578 0.3638 0.0904  0.0020  -0.0622 121  ILE B CA  
9581  C C   . ILE B 123  ? 0.6617 0.7187 0.4156 0.0995  0.0033  -0.0689 121  ILE B C   
9582  O O   . ILE B 123  ? 0.6674 0.7231 0.4242 0.1053  0.0044  -0.0732 121  ILE B O   
9583  C CB  . ILE B 123  ? 0.5384 0.6138 0.3040 0.0868  0.0076  -0.0555 121  ILE B CB  
9584  C CG1 . ILE B 123  ? 0.4872 0.5637 0.2644 0.0784  0.0065  -0.0493 121  ILE B CG1 
9585  C CG2 . ILE B 123  ? 0.5638 0.6530 0.3302 0.0929  0.0142  -0.0568 121  ILE B CG2 
9586  C CD1 . ILE B 123  ? 0.4961 0.5870 0.2732 0.0733  0.0107  -0.0422 121  ILE B CD1 
9587  N N   . ARG B 124  ? 0.6059 0.6627 0.3466 0.1009  0.0029  -0.0700 122  ARG B N   
9588  C CA  . ARG B 124  ? 0.7036 0.7601 0.4327 0.1099  0.0045  -0.0763 122  ARG B CA  
9589  C C   . ARG B 124  ? 0.7448 0.7838 0.4716 0.1140  -0.0012 -0.0834 122  ARG B C   
9590  O O   . ARG B 124  ? 0.8301 0.8670 0.5533 0.1214  0.0000  -0.0887 122  ARG B O   
9591  C CB  . ARG B 124  ? 0.6699 0.7306 0.3851 0.1100  0.0054  -0.0754 122  ARG B CB  
9592  N N   . ASP B 125  ? 0.7155 0.7415 0.4463 0.1086  -0.0076 -0.0830 123  ASP B N   
9593  C CA  . ASP B 125  ? 0.7502 0.7595 0.4773 0.1114  -0.0137 -0.0893 123  ASP B CA  
9594  C C   . ASP B 125  ? 0.7197 0.7207 0.4594 0.1097  -0.0166 -0.0902 123  ASP B C   
9595  O O   . ASP B 125  ? 0.7937 0.7812 0.5309 0.1123  -0.0214 -0.0956 123  ASP B O   
9596  C CB  . ASP B 125  ? 0.7279 0.7278 0.4479 0.1071  -0.0195 -0.0890 123  ASP B CB  
9597  C CG  . ASP B 125  ? 0.7933 0.8004 0.4998 0.1084  -0.0171 -0.0880 123  ASP B CG  
9598  O OD1 . ASP B 125  ? 0.8160 0.8293 0.5168 0.1144  -0.0126 -0.0904 123  ASP B OD1 
9599  O OD2 . ASP B 125  ? 0.8224 0.8289 0.5265 0.1026  -0.0195 -0.0840 123  ASP B OD2 
9600  N N   . LYS B 126  ? 0.6858 0.6944 0.4385 0.1054  -0.0141 -0.0852 124  LYS B N   
9601  C CA  . LYS B 126  ? 0.6666 0.6672 0.4308 0.1033  -0.0171 -0.0858 124  LYS B CA  
9602  C C   . LYS B 126  ? 0.7020 0.7129 0.4768 0.1042  -0.0119 -0.0834 124  LYS B C   
9603  O O   . LYS B 126  ? 0.7329 0.7392 0.5119 0.1079  -0.0122 -0.0867 124  LYS B O   
9604  C CB  . LYS B 126  ? 0.7089 0.7036 0.4797 0.0952  -0.0219 -0.0821 124  LYS B CB  
9605  N N   . ILE B 127  ? 0.6581 0.6826 0.4372 0.1005  -0.0075 -0.0775 125  ILE B N   
9606  C CA  . ILE B 127  ? 0.6193 0.6538 0.4094 0.1001  -0.0031 -0.0745 125  ILE B CA  
9607  C C   . ILE B 127  ? 0.6594 0.7027 0.4456 0.1082  0.0021  -0.0774 125  ILE B C   
9608  O O   . ILE B 127  ? 0.6180 0.6621 0.4109 0.1114  0.0035  -0.0789 125  ILE B O   
9609  C CB  . ILE B 127  ? 0.5995 0.6448 0.3953 0.0928  -0.0007 -0.0671 125  ILE B CB  
9610  C CG1 . ILE B 127  ? 0.5909 0.6269 0.3896 0.0856  -0.0062 -0.0645 125  ILE B CG1 
9611  C CG2 . ILE B 127  ? 0.5752 0.6304 0.3827 0.0919  0.0033  -0.0640 125  ILE B CG2 
9612  C CD1 . ILE B 127  ? 0.6534 0.6782 0.4610 0.0841  -0.0105 -0.0665 125  ILE B CD1 
9613  N N   . ALA B 128  ? 0.6030 0.6537 0.3783 0.1118  0.0051  -0.0782 126  ALA B N   
9614  C CA  . ALA B 128  ? 0.6524 0.7134 0.4239 0.1200  0.0105  -0.0808 126  ALA B CA  
9615  C C   . ALA B 128  ? 0.7173 0.7668 0.4846 0.1281  0.0082  -0.0883 126  ALA B C   
9616  O O   . ALA B 128  ? 0.6762 0.7325 0.4419 0.1353  0.0121  -0.0907 126  ALA B O   
9617  C CB  . ALA B 128  ? 0.6004 0.6717 0.3604 0.1220  0.0141  -0.0800 126  ALA B CB  
9618  N N   . ASP B 129  ? 0.7665 0.7986 0.5330 0.1266  0.0017  -0.0915 127  ASP B N   
9619  C CA  . ASP B 129  ? 0.7970 0.8161 0.5607 0.1329  -0.0014 -0.0981 127  ASP B CA  
9620  C C   . ASP B 129  ? 0.7824 0.7954 0.5588 0.1301  -0.0036 -0.0972 127  ASP B C   
9621  O O   . ASP B 129  ? 0.8763 0.8745 0.6518 0.1318  -0.0084 -0.1015 127  ASP B O   
9622  C CB  . ASP B 129  ? 0.8386 0.8422 0.5913 0.1335  -0.0074 -0.1028 127  ASP B CB  
9623  C CG  . ASP B 129  ? 0.8970 0.9051 0.6398 0.1362  -0.0054 -0.1032 127  ASP B CG  
9624  O OD1 . ASP B 129  ? 0.9258 0.9444 0.6686 0.1412  -0.0002 -0.1031 127  ASP B OD1 
9625  O OD2 . ASP B 129  ? 0.9816 0.9831 0.7168 0.1332  -0.0090 -0.1037 127  ASP B OD2 
9626  N N   . GLY B 130  ? 0.7491 0.7731 0.5372 0.1255  -0.0003 -0.0915 128  GLY B N   
9627  C CA  . GLY B 130  ? 0.7376 0.7576 0.5379 0.1228  -0.0017 -0.0902 128  GLY B CA  
9628  C C   . GLY B 130  ? 0.7978 0.8059 0.6034 0.1155  -0.0075 -0.0889 128  GLY B C   
9629  O O   . GLY B 130  ? 0.7249 0.7315 0.5415 0.1120  -0.0083 -0.0868 128  GLY B O   
9630  N N   . ASN B 131  ? 0.9095 0.9094 0.7079 0.1131  -0.0116 -0.0902 129  ASN B N   
9631  C CA  . ASN B 131  ? 0.8933 0.8828 0.6966 0.1063  -0.0173 -0.0890 129  ASN B CA  
9632  C C   . ASN B 131  ? 0.9021 0.9007 0.7124 0.0989  -0.0157 -0.0823 129  ASN B C   
9633  O O   . ASN B 131  ? 0.9553 0.9541 0.7609 0.0954  -0.0172 -0.0805 129  ASN B O   
9634  C CB  . ASN B 131  ? 0.8464 0.8238 0.6390 0.1070  -0.0226 -0.0931 129  ASN B CB  
9635  N N   . TRP B 132  ? 0.7906 0.7966 0.6121 0.0965  -0.0129 -0.0787 130  TRP B N   
9636  C CA  . TRP B 132  ? 0.7549 0.7686 0.5835 0.0896  -0.0116 -0.0725 130  TRP B CA  
9637  C C   . TRP B 132  ? 0.8037 0.8108 0.6430 0.0839  -0.0152 -0.0706 130  TRP B C   
9638  O O   . TRP B 132  ? 0.8183 0.8268 0.6611 0.0779  -0.0165 -0.0666 130  TRP B O   
9639  C CB  . TRP B 132  ? 0.6888 0.7179 0.5220 0.0904  -0.0053 -0.0689 130  TRP B CB  
9640  C CG  . TRP B 132  ? 0.6194 0.6502 0.4609 0.0931  -0.0034 -0.0697 130  TRP B CG  
9641  C CD1 . TRP B 132  ? 0.6158 0.6489 0.4546 0.1005  -0.0008 -0.0733 130  TRP B CD1 
9642  C CD2 . TRP B 132  ? 0.5897 0.6202 0.4432 0.0886  -0.0040 -0.0668 130  TRP B CD2 
9643  N NE1 . TRP B 132  ? 0.5615 0.5955 0.4099 0.1007  0.0001  -0.0726 130  TRP B NE1 
9644  C CE2 . TRP B 132  ? 0.5839 0.6164 0.4413 0.0933  -0.0018 -0.0686 130  TRP B CE2 
9645  C CE3 . TRP B 132  ? 0.5868 0.6154 0.4478 0.0813  -0.0063 -0.0629 130  TRP B CE3 
9646  C CZ2 . TRP B 132  ? 0.4937 0.5264 0.3620 0.0907  -0.0018 -0.0666 130  TRP B CZ2 
9647  C CZ3 . TRP B 132  ? 0.5744 0.6034 0.4461 0.0789  -0.0062 -0.0612 130  TRP B CZ3 
9648  C CH2 . TRP B 132  ? 0.4810 0.5122 0.3563 0.0835  -0.0039 -0.0629 130  TRP B CH2 
9649  N N   . LYS B 133  ? 0.8544 0.8541 0.6985 0.0857  -0.0171 -0.0735 131  LYS B N   
9650  C CA  . LYS B 133  ? 0.9102 0.9046 0.7646 0.0805  -0.0202 -0.0717 131  LYS B CA  
9651  C C   . LYS B 133  ? 0.9510 0.9364 0.8033 0.0764  -0.0258 -0.0721 131  LYS B C   
9652  O O   . LYS B 133  ? 0.9832 0.9691 0.8423 0.0708  -0.0273 -0.0686 131  LYS B O   
9653  C CB  . LYS B 133  ? 0.9013 0.8894 0.7602 0.0833  -0.0211 -0.0747 131  LYS B CB  
9654  N N   . SER B 134  ? 0.9910 0.9681 0.8339 0.0794  -0.0289 -0.0764 132  SER B N   
9655  C CA  . SER B 134  ? 1.0029 0.9712 0.8438 0.0759  -0.0347 -0.0771 132  SER B CA  
9656  C C   . SER B 134  ? 1.0058 0.9795 0.8439 0.0722  -0.0345 -0.0733 132  SER B C   
9657  O O   . SER B 134  ? 0.9826 0.9545 0.8263 0.0670  -0.0374 -0.0705 132  SER B O   
9658  C CB  . SER B 134  ? 0.9429 0.9010 0.7734 0.0801  -0.0382 -0.0827 132  SER B CB  
9659  N N   . HIS B 135  ? 0.9827 0.9630 0.8120 0.0749  -0.0310 -0.0729 133  HIS B N   
9660  C CA  . HIS B 135  ? 0.9921 0.9765 0.8169 0.0715  -0.0312 -0.0693 133  HIS B CA  
9661  C C   . HIS B 135  ? 0.9784 0.9710 0.8120 0.0663  -0.0289 -0.0633 133  HIS B C   
9662  O O   . HIS B 135  ? 0.9506 0.9440 0.7825 0.0623  -0.0304 -0.0600 133  HIS B O   
9663  C CB  . HIS B 135  ? 0.9212 0.9114 0.7341 0.0758  -0.0278 -0.0704 133  HIS B CB  
9664  N N   . LEU B 136  ? 0.9585 0.9566 0.8008 0.0664  -0.0254 -0.0619 134  LEU B N   
9665  C CA  . LEU B 136  ? 0.9319 0.9370 0.7825 0.0615  -0.0235 -0.0565 134  LEU B CA  
9666  C C   . LEU B 136  ? 0.9504 0.9545 0.8127 0.0606  -0.0233 -0.0565 134  LEU B C   
9667  O O   . LEU B 136  ? 0.9796 0.9786 0.8486 0.0569  -0.0267 -0.0555 134  LEU B O   
9668  C CB  . LEU B 136  ? 0.8401 0.8578 0.6879 0.0620  -0.0178 -0.0533 134  LEU B CB  
9669  C CG  . LEU B 136  ? 0.7806 0.8017 0.6165 0.0632  -0.0168 -0.0529 134  LEU B CG  
9670  C CD1 . LEU B 136  ? 0.6602 0.6947 0.4942 0.0652  -0.0105 -0.0508 134  LEU B CD1 
9671  C CD2 . LEU B 136  ? 0.7499 0.7688 0.5837 0.0576  -0.0199 -0.0490 134  LEU B CD2 
9672  N N   . ARG B 140  ? 0.6033 0.5991 0.5110 0.0416  -0.0321 -0.0465 138  ARG B N   
9673  C CA  . ARG B 140  ? 0.6770 0.6808 0.5887 0.0405  -0.0278 -0.0434 138  ARG B CA  
9674  C C   . ARG B 140  ? 0.6251 0.6347 0.5326 0.0443  -0.0235 -0.0444 138  ARG B C   
9675  O O   . ARG B 140  ? 0.5131 0.5227 0.4120 0.0469  -0.0231 -0.0460 138  ARG B O   
9676  C CB  . ARG B 140  ? 0.5883 0.5951 0.4984 0.0367  -0.0278 -0.0390 138  ARG B CB  
9677  N N   . SER B 141  ? 0.5042 0.5189 0.4177 0.0448  -0.0203 -0.0436 139  SER B N   
9678  C CA  . SER B 141  ? 0.4730 0.4942 0.3837 0.0487  -0.0161 -0.0444 139  SER B CA  
9679  C C   . SER B 141  ? 0.4700 0.4988 0.3740 0.0483  -0.0135 -0.0419 139  SER B C   
9680  O O   . SER B 141  ? 0.4639 0.4952 0.3681 0.0439  -0.0138 -0.0381 139  SER B O   
9681  C CB  . SER B 141  ? 0.4344 0.4609 0.3535 0.0485  -0.0132 -0.0430 139  SER B CB  
9682  O OG  . SER B 141  ? 0.4544 0.4891 0.3713 0.0520  -0.0090 -0.0431 139  SER B OG  
9683  N N   . LEU B 142  ? 0.4211 0.4534 0.3187 0.0530  -0.0110 -0.0441 140  LEU B N   
9684  C CA  . LEU B 142  ? 0.4141 0.4559 0.3058 0.0529  -0.0076 -0.0415 140  LEU B CA  
9685  C C   . LEU B 142  ? 0.4084 0.4605 0.3062 0.0499  -0.0040 -0.0371 140  LEU B C   
9686  O O   . LEU B 142  ? 0.3206 0.3805 0.2152 0.0475  -0.0019 -0.0335 140  LEU B O   
9687  C CB  . LEU B 142  ? 0.3946 0.4393 0.2793 0.0594  -0.0050 -0.0451 140  LEU B CB  
9688  C CG  . LEU B 142  ? 0.4335 0.4844 0.3088 0.0597  -0.0031 -0.0437 140  LEU B CG  
9689  C CD1 . LEU B 142  ? 0.5041 0.5454 0.3723 0.0588  -0.0075 -0.0453 140  LEU B CD1 
9690  C CD2 . LEU B 142  ? 0.4684 0.5258 0.3387 0.0663  0.0007  -0.0465 140  LEU B CD2 
9691  N N   . PHE B 143  ? 0.3553 0.4077 0.2618 0.0499  -0.0035 -0.0372 141  PHE B N   
9692  C CA  . PHE B 143  ? 0.3528 0.4155 0.2649 0.0483  0.0001  -0.0338 141  PHE B CA  
9693  C C   . PHE B 143  ? 0.3415 0.4030 0.2604 0.0422  -0.0015 -0.0302 141  PHE B C   
9694  O O   . PHE B 143  ? 0.3242 0.3922 0.2491 0.0407  0.0006  -0.0278 141  PHE B O   
9695  C CB  . PHE B 143  ? 0.3200 0.3849 0.2359 0.0533  0.0022  -0.0366 141  PHE B CB  
9696  C CG  . PHE B 143  ? 0.2720 0.3369 0.1806 0.0599  0.0035  -0.0406 141  PHE B CG  
9697  C CD1 . PHE B 143  ? 0.2674 0.3413 0.1693 0.0616  0.0066  -0.0396 141  PHE B CD1 
9698  C CD2 . PHE B 143  ? 0.2847 0.3405 0.1926 0.0642  0.0014  -0.0453 141  PHE B CD2 
9699  C CE1 . PHE B 143  ? 0.3072 0.3810 0.2017 0.0681  0.0078  -0.0436 141  PHE B CE1 
9700  C CE2 . PHE B 143  ? 0.3023 0.3571 0.2028 0.0705  0.0022  -0.0493 141  PHE B CE2 
9701  C CZ  . PHE B 143  ? 0.3005 0.3641 0.1941 0.0727  0.0054  -0.0486 141  PHE B CZ  
9702  N N   . VAL B 144  ? 0.3779 0.4313 0.2955 0.0388  -0.0054 -0.0295 142  VAL B N   
9703  C CA  . VAL B 144  ? 0.4231 0.4740 0.3468 0.0337  -0.0074 -0.0266 142  VAL B CA  
9704  C C   . VAL B 144  ? 0.3777 0.4376 0.3023 0.0296  -0.0049 -0.0217 142  VAL B C   
9705  O O   . VAL B 144  ? 0.3909 0.4521 0.3220 0.0266  -0.0049 -0.0197 142  VAL B O   
9706  C CB  . VAL B 144  ? 0.4160 0.4573 0.3369 0.0314  -0.0120 -0.0268 142  VAL B CB  
9707  C CG1 . VAL B 144  ? 0.4900 0.5292 0.4155 0.0263  -0.0140 -0.0235 142  VAL B CG1 
9708  C CG2 . VAL B 144  ? 0.5037 0.5364 0.4260 0.0344  -0.0148 -0.0313 142  VAL B CG2 
9709  N N   . ASN B 145  ? 0.4208 0.4876 0.3390 0.0292  -0.0028 -0.0197 143  ASN B N   
9710  C CA  . ASN B 145  ? 0.4080 0.4839 0.3267 0.0247  -0.0006 -0.0146 143  ASN B CA  
9711  C C   . ASN B 145  ? 0.3921 0.4808 0.3124 0.0273  0.0043  -0.0141 143  ASN B C   
9712  O O   . ASN B 145  ? 0.3742 0.4726 0.2931 0.0242  0.0067  -0.0100 143  ASN B O   
9713  C CB  . ASN B 145  ? 0.4516 0.5276 0.3623 0.0214  -0.0015 -0.0116 143  ASN B CB  
9714  C CG  . ASN B 145  ? 0.4873 0.5522 0.3975 0.0176  -0.0064 -0.0105 143  ASN B CG  
9715  O OD1 . ASN B 145  ? 0.5653 0.6264 0.4816 0.0149  -0.0083 -0.0095 143  ASN B OD1 
9716  N ND2 . ASN B 145  ? 0.5273 0.5870 0.4300 0.0177  -0.0087 -0.0109 143  ASN B ND2 
9717  N N   . ALA B 146  ? 0.3432 0.4322 0.2663 0.0328  0.0057  -0.0181 144  ALA B N   
9718  C CA  . ALA B 146  ? 0.3323 0.4335 0.2560 0.0364  0.0103  -0.0181 144  ALA B CA  
9719  C C   . ALA B 146  ? 0.3284 0.4388 0.2591 0.0328  0.0123  -0.0142 144  ALA B C   
9720  O O   . ALA B 146  ? 0.3583 0.4815 0.2892 0.0339  0.0161  -0.0124 144  ALA B O   
9721  C CB  . ALA B 146  ? 0.3614 0.4595 0.2859 0.0436  0.0109  -0.0234 144  ALA B CB  
9722  N N   . ALA B 147  ? 0.3534 0.4581 0.2900 0.0287  0.0097  -0.0129 145  ALA B N   
9723  C CA  . ALA B 147  ? 0.3392 0.4521 0.2817 0.0246  0.0112  -0.0090 145  ALA B CA  
9724  C C   . ALA B 147  ? 0.3672 0.4885 0.3061 0.0194  0.0125  -0.0039 145  ALA B C   
9725  O O   . ALA B 147  ? 0.3720 0.5057 0.3136 0.0180  0.0154  -0.0009 145  ALA B O   
9726  C CB  . ALA B 147  ? 0.3085 0.4127 0.2566 0.0211  0.0079  -0.0086 145  ALA B CB  
9727  N N   . THR B 148  ? 0.3400 0.4551 0.2725 0.0166  0.0102  -0.0027 146  THR B N   
9728  C CA  . THR B 148  ? 0.3400 0.4623 0.2681 0.0114  0.0111  0.0023  146  THR B CA  
9729  C C   . THR B 148  ? 0.4133 0.5492 0.3379 0.0148  0.0158  0.0026  146  THR B C   
9730  O O   . THR B 148  ? 0.4099 0.5586 0.3359 0.0117  0.0186  0.0068  146  THR B O   
9731  C CB  . THR B 148  ? 0.4374 0.5491 0.3588 0.0085  0.0074  0.0031  146  THR B CB  
9732  O OG1 . THR B 148  ? 0.5150 0.6153 0.4399 0.0052  0.0031  0.0033  146  THR B OG1 
9733  C CG2 . THR B 148  ? 0.4594 0.5782 0.3751 0.0033  0.0084  0.0084  146  THR B CG2 
9734  N N   . TRP B 149  ? 0.3361 0.4698 0.2559 0.0212  0.0166  -0.0018 147  TRP B N   
9735  C CA  . TRP B 149  ? 0.3534 0.4998 0.2695 0.0255  0.0211  -0.0021 147  TRP B CA  
9736  C C   . TRP B 149  ? 0.3163 0.4741 0.2393 0.0288  0.0246  -0.0026 147  TRP B C   
9737  O O   . TRP B 149  ? 0.3485 0.5212 0.2708 0.0297  0.0287  -0.0005 147  TRP B O   
9738  C CB  . TRP B 149  ? 0.3195 0.4593 0.2287 0.0322  0.0207  -0.0074 147  TRP B CB  
9739  C CG  . TRP B 149  ? 0.3373 0.4686 0.2388 0.0292  0.0177  -0.0066 147  TRP B CG  
9740  C CD1 . TRP B 149  ? 0.3309 0.4472 0.2304 0.0296  0.0133  -0.0095 147  TRP B CD1 
9741  C CD2 . TRP B 149  ? 0.3667 0.5043 0.2616 0.0249  0.0188  -0.0021 147  TRP B CD2 
9742  N NE1 . TRP B 149  ? 0.3371 0.4497 0.2290 0.0263  0.0114  -0.0074 147  TRP B NE1 
9743  C CE2 . TRP B 149  ? 0.3876 0.5128 0.2763 0.0233  0.0147  -0.0028 147  TRP B CE2 
9744  C CE3 . TRP B 149  ? 0.4160 0.5691 0.3097 0.0222  0.0227  0.0025  147  TRP B CE3 
9745  C CZ2 . TRP B 149  ? 0.4297 0.5565 0.3105 0.0192  0.0143  0.0010  147  TRP B CZ2 
9746  C CZ3 . TRP B 149  ? 0.4517 0.6067 0.3376 0.0178  0.0225  0.0064  147  TRP B CZ3 
9747  C CH2 . TRP B 149  ? 0.4508 0.5924 0.3301 0.0164  0.0183  0.0057  147  TRP B CH2 
9748  N N   . GLY B 150  ? 0.3239 0.4754 0.2534 0.0308  0.0232  -0.0052 148  GLY B N   
9749  C CA  . GLY B 150  ? 0.3535 0.5153 0.2900 0.0333  0.0260  -0.0052 148  GLY B CA  
9750  C C   . GLY B 150  ? 0.4014 0.5758 0.3419 0.0269  0.0277  0.0008  148  GLY B C   
9751  O O   . GLY B 150  ? 0.3941 0.5834 0.3371 0.0288  0.0315  0.0022  148  GLY B O   
9752  N N   . LEU B 151  ? 0.4058 0.5742 0.3468 0.0192  0.0246  0.0044  149  LEU B N   
9753  C CA  . LEU B 151  ? 0.4055 0.5843 0.3491 0.0120  0.0255  0.0105  149  LEU B CA  
9754  C C   . LEU B 151  ? 0.3987 0.5903 0.3368 0.0108  0.0288  0.0137  149  LEU B C   
9755  O O   . LEU B 151  ? 0.4012 0.6083 0.3424 0.0086  0.0319  0.0174  149  LEU B O   
9756  C CB  . LEU B 151  ? 0.4274 0.5944 0.3710 0.0045  0.0209  0.0131  149  LEU B CB  
9757  C CG  . LEU B 151  ? 0.5146 0.6880 0.4617 -0.0037 0.0204  0.0190  149  LEU B CG  
9758  C CD1 . LEU B 151  ? 0.4559 0.6416 0.4107 -0.0022 0.0232  0.0194  149  LEU B CD1 
9759  C CD2 . LEU B 151  ? 0.5137 0.6722 0.4617 -0.0087 0.0154  0.0196  149  LEU B CD2 
9760  N N   . VAL B 152  ? 0.4286 0.6147 0.3584 0.0125  0.0283  0.0123  150  VAL B N   
9761  C CA  . VAL B 152  ? 0.4097 0.6076 0.3333 0.0115  0.0315  0.0152  150  VAL B CA  
9762  C C   . VAL B 152  ? 0.4347 0.6478 0.3592 0.0187  0.0367  0.0132  150  VAL B C   
9763  O O   . VAL B 152  ? 0.4618 0.6913 0.3860 0.0169  0.0404  0.0171  150  VAL B O   
9764  C CB  . VAL B 152  ? 0.3952 0.5821 0.3092 0.0120  0.0293  0.0137  150  VAL B CB  
9765  C CG1 . VAL B 152  ? 0.4610 0.6603 0.3678 0.0123  0.0330  0.0160  150  VAL B CG1 
9766  C CG2 . VAL B 152  ? 0.4473 0.6212 0.3602 0.0045  0.0243  0.0166  150  VAL B CG2 
9767  N N   . VAL B 153  ? 0.3819 0.5900 0.3076 0.0271  0.0370  0.0071  151  VAL B N   
9768  C CA  . VAL B 153  ? 0.4085 0.6288 0.3336 0.0353  0.0415  0.0042  151  VAL B CA  
9769  C C   . VAL B 153  ? 0.3825 0.6157 0.3168 0.0364  0.0440  0.0055  151  VAL B C   
9770  O O   . VAL B 153  ? 0.3476 0.5980 0.2826 0.0394  0.0484  0.0067  151  VAL B O   
9771  C CB  . VAL B 153  ? 0.4025 0.6104 0.3236 0.0439  0.0402  -0.0029 151  VAL B CB  
9772  C CG1 . VAL B 153  ? 0.3990 0.6179 0.3203 0.0532  0.0444  -0.0065 151  VAL B CG1 
9773  C CG2 . VAL B 153  ? 0.3787 0.5770 0.2899 0.0435  0.0384  -0.0042 151  VAL B CG2 
9774  N N   . THR B 154  ? 0.3782 0.6038 0.3196 0.0344  0.0412  0.0052  152  THR B N   
9775  C CA  . THR B 154  ? 0.3788 0.6147 0.3288 0.0362  0.0431  0.0058  152  THR B CA  
9776  C C   . THR B 154  ? 0.3861 0.6267 0.3425 0.0271  0.0418  0.0115  152  THR B C   
9777  O O   . THR B 154  ? 0.4410 0.6927 0.4045 0.0275  0.0434  0.0130  152  THR B O   
9778  C CB  . THR B 154  ? 0.3606 0.5847 0.3140 0.0423  0.0411  0.0004  152  THR B CB  
9779  O OG1 . THR B 154  ? 0.4170 0.6260 0.3725 0.0369  0.0366  0.0007  152  THR B OG1 
9780  C CG2 . THR B 154  ? 0.4654 0.6818 0.4120 0.0507  0.0413  -0.0055 152  THR B CG2 
9781  N N   . GLY B 155  ? 0.3845 0.6163 0.3382 0.0191  0.0386  0.0147  153  GLY B N   
9782  C CA  . GLY B 155  ? 0.3955 0.6289 0.3547 0.0106  0.0366  0.0196  153  GLY B CA  
9783  C C   . GLY B 155  ? 0.4287 0.6514 0.3940 0.0107  0.0335  0.0174  153  GLY B C   
9784  O O   . GLY B 155  ? 0.4941 0.7190 0.4645 0.0045  0.0320  0.0209  153  GLY B O   
9785  N N   . LYS B 156  ? 0.3879 0.5990 0.3527 0.0173  0.0324  0.0117  154  LYS B N   
9786  C CA  . LYS B 156  ? 0.4196 0.6208 0.3899 0.0179  0.0297  0.0095  154  LYS B CA  
9787  C C   . LYS B 156  ? 0.4225 0.6049 0.3891 0.0174  0.0257  0.0066  154  LYS B C   
9788  O O   . LYS B 156  ? 0.3808 0.5573 0.3413 0.0210  0.0257  0.0038  154  LYS B O   
9789  C CB  . LYS B 156  ? 0.4763 0.6817 0.4505 0.0263  0.0318  0.0056  154  LYS B CB  
9790  N N   . LEU B 157  ? 0.3614 0.5346 0.3316 0.0130  0.0224  0.0074  155  LEU B N   
9791  C CA  . LEU B 157  ? 0.4505 0.6068 0.4181 0.0122  0.0185  0.0050  155  LEU B CA  
9792  C C   . LEU B 157  ? 0.4600 0.6086 0.4322 0.0165  0.0174  0.0009  155  LEU B C   
9793  O O   . LEU B 157  ? 0.4705 0.6234 0.4487 0.0160  0.0178  0.0017  155  LEU B O   
9794  C CB  . LEU B 157  ? 0.4713 0.6222 0.4385 0.0039  0.0153  0.0089  155  LEU B CB  
9795  N N   . THR B 158  ? 0.4460 0.5834 0.4153 0.0206  0.0158  -0.0032 156  THR B N   
9796  C CA  . THR B 158  ? 0.4557 0.5833 0.4288 0.0232  0.0139  -0.0066 156  THR B CA  
9797  C C   . THR B 158  ? 0.4248 0.5387 0.3956 0.0206  0.0101  -0.0077 156  THR B C   
9798  O O   . THR B 158  ? 0.4738 0.5846 0.4390 0.0188  0.0090  -0.0069 156  THR B O   
9799  C CB  . THR B 158  ? 0.4530 0.5800 0.4256 0.0310  0.0154  -0.0110 156  THR B CB  
9800  O OG1 . THR B 158  ? 0.4159 0.5369 0.3818 0.0334  0.0147  -0.0134 156  THR B OG1 
9801  C CG2 . THR B 158  ? 0.4524 0.5936 0.4265 0.0344  0.0193  -0.0101 156  THR B CG2 
9802  N N   . SER B 159  ? 0.4055 0.5114 0.3806 0.0204  0.0079  -0.0093 157  SER B N   
9803  C CA  . SER B 159  ? 0.4185 0.5122 0.3921 0.0184  0.0043  -0.0104 157  SER B CA  
9804  C C   . SER B 159  ? 0.3658 0.4520 0.3363 0.0230  0.0034  -0.0145 157  SER B C   
9805  O O   . SER B 159  ? 0.4088 0.4870 0.3760 0.0217  0.0007  -0.0151 157  SER B O   
9806  C CB  . SER B 159  ? 0.4066 0.4952 0.3857 0.0163  0.0024  -0.0104 157  SER B CB  
9807  O OG  . SER B 159  ? 0.4838 0.5723 0.4671 0.0204  0.0034  -0.0131 157  SER B OG  
9808  N N   . THR B 160  ? 0.3992 0.4875 0.3705 0.0284  0.0052  -0.0172 158  THR B N   
9809  C CA  . THR B 160  ? 0.3530 0.4338 0.3208 0.0327  0.0041  -0.0212 158  THR B CA  
9810  C C   . THR B 160  ? 0.3352 0.4226 0.2991 0.0377  0.0070  -0.0226 158  THR B C   
9811  O O   . THR B 160  ? 0.3403 0.4385 0.3053 0.0385  0.0100  -0.0208 158  THR B O   
9812  C CB  . THR B 160  ? 0.3260 0.3993 0.2983 0.0347  0.0025  -0.0240 158  THR B CB  
9813  O OG1 . THR B 160  ? 0.3167 0.3958 0.2932 0.0372  0.0048  -0.0241 158  THR B OG1 
9814  C CG2 . THR B 160  ? 0.3735 0.4406 0.3494 0.0302  -0.0003 -0.0230 158  THR B CG2 
9815  N N   . VAL B 161  ? 0.2807 0.3613 0.2399 0.0414  0.0058  -0.0260 159  VAL B N   
9816  C CA  . VAL B 161  ? 0.3239 0.4084 0.2769 0.0459  0.0078  -0.0278 159  VAL B CA  
9817  C C   . VAL B 161  ? 0.3137 0.3931 0.2667 0.0520  0.0075  -0.0321 159  VAL B C   
9818  O O   . VAL B 161  ? 0.3016 0.3707 0.2561 0.0519  0.0046  -0.0343 159  VAL B O   
9819  C CB  . VAL B 161  ? 0.3320 0.4117 0.2780 0.0444  0.0059  -0.0280 159  VAL B CB  
9820  C CG1 . VAL B 161  ? 0.3794 0.4568 0.3186 0.0500  0.0063  -0.0317 159  VAL B CG1 
9821  C CG2 . VAL B 161  ? 0.4497 0.5375 0.3940 0.0397  0.0072  -0.0234 159  VAL B CG2 
9822  N N   . ASN B 162  ? 0.2700 0.3565 0.2214 0.0572  0.0105  -0.0333 160  ASN B N   
9823  C CA  . ASN B 162  ? 0.2804 0.3608 0.2302 0.0634  0.0100  -0.0376 160  ASN B CA  
9824  C C   . ASN B 162  ? 0.2748 0.3498 0.2161 0.0663  0.0089  -0.0407 160  ASN B C   
9825  O O   . ASN B 162  ? 0.2567 0.3381 0.1926 0.0704  0.0114  -0.0416 160  ASN B O   
9826  C CB  . ASN B 162  ? 0.3231 0.4124 0.2750 0.0683  0.0132  -0.0378 160  ASN B CB  
9827  C CG  . ASN B 162  ? 0.3654 0.4466 0.3158 0.0746  0.0120  -0.0422 160  ASN B CG  
9828  O OD1 . ASN B 162  ? 0.3134 0.3834 0.2593 0.0759  0.0092  -0.0454 160  ASN B OD1 
9829  N ND2 . ASN B 162  ? 0.2861 0.3725 0.2400 0.0784  0.0139  -0.0423 160  ASN B ND2 
9830  N N   . ASP B 163  ? 0.2662 0.3296 0.2061 0.0643  0.0051  -0.0423 161  ASP B N   
9831  C CA  . ASP B 163  ? 0.2423 0.2999 0.1739 0.0661  0.0034  -0.0450 161  ASP B CA  
9832  C C   . ASP B 163  ? 0.2639 0.3164 0.1905 0.0731  0.0032  -0.0497 161  ASP B C   
9833  O O   . ASP B 163  ? 0.2856 0.3360 0.2041 0.0759  0.0028  -0.0521 161  ASP B O   
9834  C CB  . ASP B 163  ? 0.2859 0.3334 0.2179 0.0616  -0.0008 -0.0451 161  ASP B CB  
9835  C CG  . ASP B 163  ? 0.3359 0.3752 0.2742 0.0606  -0.0035 -0.0463 161  ASP B CG  
9836  O OD1 . ASP B 163  ? 0.2884 0.3314 0.2333 0.0600  -0.0020 -0.0448 161  ASP B OD1 
9837  O OD2 . ASP B 163  ? 0.3667 0.3961 0.3034 0.0600  -0.0071 -0.0485 161  ASP B OD2 
9838  N N   . ARG B 164  ? 0.2900 0.3400 0.2206 0.0760  0.0032  -0.0512 162  ARG B N   
9839  C CA  . ARG B 164  ? 0.2994 0.3448 0.2247 0.0831  0.0030  -0.0556 162  ARG B CA  
9840  C C   . ARG B 164  ? 0.2977 0.3548 0.2193 0.0884  0.0074  -0.0557 162  ARG B C   
9841  O O   . ARG B 164  ? 0.2721 0.3271 0.1858 0.0940  0.0076  -0.0592 162  ARG B O   
9842  C CB  . ARG B 164  ? 0.2616 0.3006 0.1919 0.0846  0.0016  -0.0568 162  ARG B CB  
9843  C CG  . ARG B 164  ? 0.3149 0.3421 0.2483 0.0803  -0.0027 -0.0572 162  ARG B CG  
9844  C CD  . ARG B 164  ? 0.3635 0.3814 0.2901 0.0798  -0.0061 -0.0600 162  ARG B CD  
9845  N NE  . ARG B 164  ? 0.4399 0.4541 0.3577 0.0863  -0.0062 -0.0641 162  ARG B NE  
9846  C CZ  . ARG B 164  ? 0.4612 0.4710 0.3711 0.0871  -0.0079 -0.0664 162  ARG B CZ  
9847  N NH1 . ARG B 164  ? 0.5272 0.5359 0.4370 0.0819  -0.0097 -0.0648 162  ARG B NH1 
9848  N NH2 . ARG B 164  ? 0.4713 0.4776 0.3728 0.0936  -0.0079 -0.0704 162  ARG B NH2 
9849  N N   . SER B 165  ? 0.2790 0.3485 0.2065 0.0870  0.0107  -0.0520 163  SER B N   
9850  C CA  . SER B 165  ? 0.2856 0.3685 0.2106 0.0912  0.0151  -0.0514 163  SER B CA  
9851  C C   . SER B 165  ? 0.2643 0.3514 0.1822 0.0902  0.0161  -0.0508 163  SER B C   
9852  O O   . SER B 165  ? 0.2722 0.3643 0.1835 0.0959  0.0184  -0.0530 163  SER B O   
9853  C CB  . SER B 165  ? 0.2588 0.3544 0.1922 0.0882  0.0179  -0.0468 163  SER B CB  
9854  O OG  . SER B 165  ? 0.2672 0.3777 0.1988 0.0908  0.0222  -0.0453 163  SER B OG  
9855  N N   . LEU B 166  ? 0.2668 0.3515 0.1854 0.0832  0.0144  -0.0481 164  LEU B N   
9856  C CA  . LEU B 166  ? 0.2719 0.3604 0.1835 0.0816  0.0152  -0.0471 164  LEU B CA  
9857  C C   . LEU B 166  ? 0.2828 0.3610 0.1851 0.0858  0.0128  -0.0519 164  LEU B C   
9858  O O   . LEU B 166  ? 0.2855 0.3687 0.1799 0.0888  0.0147  -0.0529 164  LEU B O   
9859  C CB  . LEU B 166  ? 0.2592 0.3467 0.1739 0.0732  0.0134  -0.0429 164  LEU B CB  
9860  C CG  . LEU B 166  ? 0.2726 0.3723 0.1943 0.0688  0.0161  -0.0377 164  LEU B CG  
9861  C CD1 . LEU B 166  ? 0.2967 0.3923 0.2214 0.0608  0.0136  -0.0341 164  LEU B CD1 
9862  C CD2 . LEU B 166  ? 0.2671 0.3816 0.1850 0.0703  0.0206  -0.0356 164  LEU B CD2 
9863  N N   . ALA B 167  ? 0.2910 0.3550 0.1936 0.0858  0.0086  -0.0549 165  ALA B N   
9864  C CA  . ALA B 167  ? 0.3057 0.3592 0.1994 0.0897  0.0058  -0.0596 165  ALA B CA  
9865  C C   . ALA B 167  ? 0.2966 0.3522 0.1847 0.0984  0.0080  -0.0636 165  ALA B C   
9866  O O   . ALA B 167  ? 0.3086 0.3626 0.1872 0.1025  0.0081  -0.0667 165  ALA B O   
9867  C CB  . ALA B 167  ? 0.2996 0.3382 0.1958 0.0874  0.0007  -0.0617 165  ALA B CB  
9868  N N   . ALA B 168  ? 0.2931 0.3525 0.1867 0.1017  0.0099  -0.0637 166  ALA B N   
9869  C CA  . ALA B 168  ? 0.3018 0.3643 0.1905 0.1106  0.0122  -0.0674 166  ALA B CA  
9870  C C   . ALA B 168  ? 0.3053 0.3833 0.1898 0.1131  0.0171  -0.0659 166  ALA B C   
9871  O O   . ALA B 168  ? 0.3164 0.3950 0.1923 0.1200  0.0182  -0.0697 166  ALA B O   
9872  C CB  . ALA B 168  ? 0.2967 0.3608 0.1928 0.1132  0.0130  -0.0671 166  ALA B CB  
9873  N N   . ALA B 169  ? 0.2964 0.3872 0.1868 0.1076  0.0199  -0.0605 167  ALA B N   
9874  C CA  . ALA B 169  ? 0.2992 0.4059 0.1865 0.1088  0.0246  -0.0583 167  ALA B CA  
9875  C C   . ALA B 169  ? 0.3113 0.4152 0.1884 0.1084  0.0239  -0.0595 167  ALA B C   
9876  O O   . ALA B 169  ? 0.3167 0.4287 0.1867 0.1135  0.0270  -0.0609 167  ALA B O   
9877  C CB  . ALA B 169  ? 0.2959 0.4148 0.1917 0.1015  0.0268  -0.0518 167  ALA B CB  
9878  N N   . LEU B 170  ? 0.3063 0.3993 0.1827 0.1023  0.0198  -0.0587 168  LEU B N   
9879  C CA  . LEU B 170  ? 0.3145 0.4047 0.1814 0.1013  0.0187  -0.0594 168  LEU B CA  
9880  C C   . LEU B 170  ? 0.3276 0.4092 0.1844 0.1091  0.0173  -0.0659 168  LEU B C   
9881  O O   . LEU B 170  ? 0.3575 0.4439 0.2051 0.1125  0.0193  -0.0672 168  LEU B O   
9882  C CB  . LEU B 170  ? 0.3548 0.4349 0.2238 0.0934  0.0142  -0.0573 168  LEU B CB  
9883  C CG  . LEU B 170  ? 0.3682 0.4451 0.2278 0.0915  0.0126  -0.0574 168  LEU B CG  
9884  C CD1 . LEU B 170  ? 0.3561 0.4483 0.2115 0.0913  0.0174  -0.0541 168  LEU B CD1 
9885  C CD2 . LEU B 170  ? 0.3875 0.4566 0.2512 0.0836  0.0086  -0.0545 168  LEU B CD2 
9886  N N   . THR B 171  ? 0.3464 0.4149 0.2044 0.1120  0.0139  -0.0699 169  THR B N   
9887  C CA  . THR B 171  ? 0.3528 0.4122 0.2011 0.1199  0.0123  -0.0763 169  THR B CA  
9888  C C   . THR B 171  ? 0.3491 0.4202 0.1933 0.1283  0.0172  -0.0781 169  THR B C   
9889  O O   . THR B 171  ? 0.3758 0.4465 0.2093 0.1340  0.0179  -0.0819 169  THR B O   
9890  C CB  . THR B 171  ? 0.3870 0.4312 0.2384 0.1212  0.0079  -0.0796 169  THR B CB  
9891  O OG1 . THR B 171  ? 0.4263 0.4603 0.2812 0.1137  0.0033  -0.0781 169  THR B OG1 
9892  C CG2 . THR B 171  ? 0.4048 0.4385 0.2456 0.1295  0.0059  -0.0864 169  THR B CG2 
9893  N N   . ARG B 172  ? 0.3421 0.4242 0.1947 0.1294  0.0207  -0.0756 170  ARG B N   
9894  C CA  . ARG B 172  ? 0.3473 0.4417 0.1972 0.1378  0.0254  -0.0773 170  ARG B CA  
9895  C C   . ARG B 172  ? 0.3518 0.4605 0.1957 0.1378  0.0297  -0.0753 170  ARG B C   
9896  O O   . ARG B 172  ? 0.3635 0.4759 0.1985 0.1455  0.0319  -0.0791 170  ARG B O   
9897  C CB  . ARG B 172  ? 0.3370 0.4416 0.1981 0.1378  0.0281  -0.0742 170  ARG B CB  
9898  C CG  . ARG B 172  ? 0.3437 0.4578 0.2028 0.1478  0.0319  -0.0770 170  ARG B CG  
9899  C CD  . ARG B 172  ? 0.3329 0.4592 0.2036 0.1472  0.0347  -0.0733 170  ARG B CD  
9900  N NE  . ARG B 172  ? 0.3242 0.4390 0.2028 0.1427  0.0308  -0.0723 170  ARG B NE  
9901  C CZ  . ARG B 172  ? 0.3115 0.4291 0.1990 0.1337  0.0303  -0.0670 170  ARG B CZ  
9902  N NH1 . ARG B 172  ? 0.3062 0.4361 0.1956 0.1276  0.0330  -0.0621 170  ARG B NH1 
9903  N NH2 . ARG B 172  ? 0.3048 0.4120 0.1987 0.1306  0.0270  -0.0666 170  ARG B NH2 
9904  N N   . LEU B 173  ? 0.3433 0.4601 0.1916 0.1292  0.0308  -0.0693 171  LEU B N   
9905  C CA  . LEU B 173  ? 0.3470 0.4791 0.1906 0.1285  0.0352  -0.0665 171  LEU B CA  
9906  C C   . LEU B 173  ? 0.3650 0.4895 0.1958 0.1300  0.0334  -0.0697 171  LEU B C   
9907  O O   . LEU B 173  ? 0.3683 0.5029 0.1912 0.1346  0.0371  -0.0706 171  LEU B O   
9908  C CB  . LEU B 173  ? 0.3788 0.5205 0.2304 0.1184  0.0364  -0.0590 171  LEU B CB  
9909  C CG  . LEU B 173  ? 0.3454 0.4773 0.1970 0.1092  0.0323  -0.0560 171  LEU B CG  
9910  C CD1 . LEU B 173  ? 0.3892 0.5270 0.2319 0.1068  0.0338  -0.0539 171  LEU B CD1 
9911  C CD2 . LEU B 173  ? 0.3191 0.4548 0.1823 0.1012  0.0320  -0.0504 171  LEU B CD2 
9912  N N   . ILE B 174  ? 0.3600 0.4671 0.1885 0.1265  0.0278  -0.0714 172  ILE B N   
9913  C CA  . ILE B 174  ? 0.3723 0.4712 0.1884 0.1279  0.0255  -0.0747 172  ILE B CA  
9914  C C   . ILE B 174  ? 0.3859 0.4799 0.1926 0.1387  0.0256  -0.0819 172  ILE B C   
9915  O O   . ILE B 174  ? 0.3971 0.4940 0.1954 0.1417  0.0270  -0.0831 172  ILE B O   
9916  C CB  . ILE B 174  ? 0.3695 0.4513 0.1862 0.1215  0.0190  -0.0748 172  ILE B CB  
9917  C CG1 . ILE B 174  ? 0.3580 0.4448 0.1821 0.1114  0.0189  -0.0679 172  ILE B CG1 
9918  C CG2 . ILE B 174  ? 0.4150 0.4864 0.2186 0.1242  0.0159  -0.0792 172  ILE B CG2 
9919  C CD1 . ILE B 174  ? 0.4386 0.5102 0.2656 0.1053  0.0129  -0.0677 172  ILE B CD1 
9920  N N   . SER B 175  ? 0.4024 0.4871 0.2127 0.1431  0.0235  -0.0856 173  SER B N   
9921  C CA  . SER B 175  ? 0.4006 0.4778 0.2060 0.1510  0.0223  -0.0906 173  SER B CA  
9922  C C   . SER B 175  ? 0.4028 0.4963 0.2097 0.1558  0.0277  -0.0889 173  SER B C   
9923  O O   . SER B 175  ? 0.4161 0.5068 0.2163 0.1617  0.0275  -0.0922 173  SER B O   
9924  C CB  . SER B 175  ? 0.4344 0.4986 0.2444 0.1538  0.0188  -0.0938 173  SER B CB  
9925  O OG  . SER B 175  ? 0.4824 0.5305 0.2905 0.1499  0.0133  -0.0959 173  SER B OG  
9926  N N   . ARG B 176  ? 0.3993 0.5097 0.2149 0.1535  0.0323  -0.0840 174  ARG B N   
9927  C CA  . ARG B 176  ? 0.3956 0.5227 0.2137 0.1576  0.0373  -0.0820 174  ARG B CA  
9928  C C   . ARG B 176  ? 0.4014 0.5399 0.2137 0.1551  0.0405  -0.0793 174  ARG B C   
9929  O O   . ARG B 176  ? 0.4256 0.5697 0.2334 0.1604  0.0425  -0.0807 174  ARG B O   
9930  C CB  . ARG B 176  ? 0.3823 0.5231 0.2126 0.1555  0.0405  -0.0775 174  ARG B CB  
9931  C CG  . ARG B 176  ? 0.4017 0.5588 0.2364 0.1605  0.0449  -0.0760 174  ARG B CG  
9932  C CD  . ARG B 176  ? 0.3770 0.5454 0.2240 0.1585  0.0471  -0.0719 174  ARG B CD  
9933  N NE  . ARG B 176  ? 0.3630 0.5438 0.2147 0.1498  0.0497  -0.0658 174  ARG B NE  
9934  C CZ  . ARG B 176  ? 0.3950 0.5730 0.2520 0.1437  0.0485  -0.0635 174  ARG B CZ  
9935  N NH1 . ARG B 176  ? 0.3711 0.5353 0.2306 0.1451  0.0449  -0.0666 174  ARG B NH1 
9936  N NH2 . ARG B 176  ? 0.4326 0.6220 0.2926 0.1358  0.0508  -0.0579 174  ARG B NH2 
9937  N N   . CYS B 177  ? 0.4072 0.5485 0.2188 0.1472  0.0406  -0.0754 175  CYS B N   
9938  C CA  . CYS B 177  ? 0.4049 0.5596 0.2129 0.1434  0.0441  -0.0711 175  CYS B CA  
9939  C C   . CYS B 177  ? 0.4119 0.5567 0.2089 0.1403  0.0412  -0.0722 175  CYS B C   
9940  O O   . CYS B 177  ? 0.4787 0.6327 0.2706 0.1387  0.0438  -0.0697 175  CYS B O   
9941  C CB  . CYS B 177  ? 0.3957 0.5652 0.2122 0.1358  0.0473  -0.0641 175  CYS B CB  
9942  S SG  . CYS B 177  ? 0.4976 0.6819 0.3277 0.1385  0.0510  -0.0617 175  CYS B SG  
9943  N N   . GLY B 178  ? 0.4187 0.5457 0.2122 0.1391  0.0358  -0.0756 176  GLY B N   
9944  C CA  . GLY B 178  ? 0.4726 0.5892 0.2548 0.1375  0.0325  -0.0775 176  GLY B CA  
9945  C C   . GLY B 178  ? 0.4708 0.5938 0.2505 0.1292  0.0331  -0.0720 176  GLY B C   
9946  O O   . GLY B 178  ? 0.4402 0.5722 0.2269 0.1236  0.0349  -0.0669 176  GLY B O   
9947  N N   . GLU B 179  ? 0.4947 0.6122 0.2639 0.1284  0.0312  -0.0730 177  GLU B N   
9948  C CA  . GLU B 179  ? 0.5063 0.6281 0.2715 0.1207  0.0311  -0.0678 177  GLU B CA  
9949  C C   . GLU B 179  ? 0.4792 0.6213 0.2495 0.1163  0.0369  -0.0606 177  GLU B C   
9950  O O   . GLU B 179  ? 0.4671 0.6118 0.2405 0.1083  0.0362  -0.0551 177  GLU B O   
9951  C CB  . GLU B 179  ? 0.5144 0.6287 0.2671 0.1215  0.0288  -0.0700 177  GLU B CB  
9952  C CG  . GLU B 179  ? 0.5701 0.6858 0.3178 0.1136  0.0274  -0.0649 177  GLU B CG  
9953  C CD  . GLU B 179  ? 0.6675 0.7754 0.4027 0.1141  0.0248  -0.0670 177  GLU B CD  
9954  O OE1 . GLU B 179  ? 0.6752 0.7790 0.4054 0.1207  0.0249  -0.0720 177  GLU B OE1 
9955  O OE2 . GLU B 179  ? 0.7184 0.8242 0.4488 0.1079  0.0223  -0.0634 177  GLU B OE2 
9956  N N   . PRO B 180  ? 0.4484 0.6043 0.2210 0.1202  0.0421  -0.0598 178  PRO B N   
9957  C CA  . PRO B 180  ? 0.4540 0.6290 0.2310 0.1148  0.0471  -0.0525 178  PRO B CA  
9958  C C   . PRO B 180  ? 0.5075 0.6894 0.2955 0.1094  0.0480  -0.0478 178  PRO B C   
9959  O O   . PRO B 180  ? 0.4698 0.6621 0.2598 0.1018  0.0499  -0.0410 178  PRO B O   
9960  C CB  . PRO B 180  ? 0.5087 0.6957 0.2871 0.1214  0.0518  -0.0538 178  PRO B CB  
9961  C CG  . PRO B 180  ? 0.4835 0.6571 0.2531 0.1289  0.0490  -0.0610 178  PRO B CG  
9962  C CD  . PRO B 180  ? 0.4836 0.6384 0.2532 0.1292  0.0433  -0.0652 178  PRO B CD  
9963  N N   . VAL B 181  ? 0.4070 0.5833 0.2022 0.1127  0.0467  -0.0510 179  VAL B N   
9964  C CA  . VAL B 181  ? 0.4310 0.6134 0.2372 0.1069  0.0473  -0.0462 179  VAL B CA  
9965  C C   . VAL B 181  ? 0.4472 0.6155 0.2561 0.0977  0.0417  -0.0432 179  VAL B C   
9966  O O   . VAL B 181  ? 0.3878 0.5615 0.2043 0.0895  0.0418  -0.0369 179  VAL B O   
9967  C CB  . VAL B 181  ? 0.4666 0.6476 0.2817 0.1124  0.0476  -0.0496 179  VAL B CB  
9968  C CG1 . VAL B 181  ? 0.4089 0.5680 0.2242 0.1141  0.0414  -0.0549 179  VAL B CG1 
9969  C CG2 . VAL B 181  ? 0.4650 0.6560 0.2933 0.1059  0.0492  -0.0435 179  VAL B CG2 
9970  N N   . ILE B 182  ? 0.4348 0.5854 0.2376 0.0989  0.0365  -0.0476 180  ILE B N   
9971  C CA  . ILE B 182  ? 0.4803 0.6182 0.2849 0.0908  0.0311  -0.0449 180  ILE B CA  
9972  C C   . ILE B 182  ? 0.4674 0.6126 0.2671 0.0839  0.0321  -0.0388 180  ILE B C   
9973  O O   . ILE B 182  ? 0.4827 0.6270 0.2884 0.0754  0.0303  -0.0332 180  ILE B O   
9974  C CB  . ILE B 182  ? 0.4548 0.5736 0.2534 0.0939  0.0254  -0.0510 180  ILE B CB  
9975  C CG1 . ILE B 182  ? 0.4260 0.5366 0.2303 0.0995  0.0239  -0.0563 180  ILE B CG1 
9976  C CG2 . ILE B 182  ? 0.4552 0.5621 0.2558 0.0858  0.0199  -0.0481 180  ILE B CG2 
9977  C CD1 . ILE B 182  ? 0.4274 0.5228 0.2230 0.1052  0.0198  -0.0633 180  ILE B CD1 
9978  N N   . ARG B 183  ? 0.4684 0.6208 0.2568 0.0873  0.0350  -0.0396 181  ARG B N   
9979  C CA  . ARG B 183  ? 0.4316 0.5910 0.2142 0.0808  0.0360  -0.0336 181  ARG B CA  
9980  C C   . ARG B 183  ? 0.5001 0.6755 0.2910 0.0746  0.0400  -0.0262 181  ARG B C   
9981  O O   . ARG B 183  ? 0.5009 0.6763 0.2928 0.0658  0.0384  -0.0200 181  ARG B O   
9982  C CB  . ARG B 183  ? 0.4699 0.6357 0.2387 0.0863  0.0390  -0.0359 181  ARG B CB  
9983  C CG  . ARG B 183  ? 0.5907 0.7417 0.3498 0.0933  0.0353  -0.0437 181  ARG B CG  
9984  C CD  . ARG B 183  ? 0.6128 0.7691 0.3600 0.0965  0.0378  -0.0446 181  ARG B CD  
9985  N NE  . ARG B 183  ? 0.7577 0.9091 0.5021 0.1057  0.0382  -0.0518 181  ARG B NE  
9986  C CZ  . ARG B 183  ? 0.6623 0.8252 0.4088 0.1109  0.0433  -0.0526 181  ARG B CZ  
9987  N NH1 . ARG B 183  ? 0.6370 0.8181 0.3892 0.1077  0.0486  -0.0467 181  ARG B NH1 
9988  N NH2 . ARG B 183  ? 0.6401 0.7962 0.3830 0.1192  0.0426  -0.0593 181  ARG B NH2 
9989  N N   . ARG B 184  ? 0.4739 0.6631 0.2708 0.0790  0.0449  -0.0268 182  ARG B N   
9990  C CA  . ARG B 184  ? 0.4948 0.7000 0.3000 0.0732  0.0487  -0.0199 182  ARG B CA  
9991  C C   . ARG B 184  ? 0.4866 0.6837 0.3030 0.0657  0.0448  -0.0165 182  ARG B C   
9992  O O   . ARG B 184  ? 0.5153 0.7183 0.3352 0.0571  0.0450  -0.0096 182  ARG B O   
9993  C CB  . ARG B 184  ? 0.5121 0.7335 0.3217 0.0804  0.0545  -0.0219 182  ARG B CB  
9994  C CG  . ARG B 184  ? 0.5982 0.8304 0.4020 0.0845  0.0586  -0.0222 182  ARG B CG  
9995  C CD  . ARG B 184  ? 0.6182 0.8672 0.4246 0.0768  0.0622  -0.0140 182  ARG B CD  
9996  N NE  . ARG B 184  ? 0.6186 0.8832 0.4369 0.0767  0.0660  -0.0112 182  ARG B NE  
9997  C CZ  . ARG B 184  ? 0.6753 0.9467 0.5022 0.0693  0.0662  -0.0055 182  ARG B CZ  
9998  N NH1 . ARG B 184  ? 0.6850 0.9494 0.5099 0.0609  0.0630  -0.0015 182  ARG B NH1 
9999  N NH2 . ARG B 184  ? 0.6254 0.9109 0.4631 0.0701  0.0694  -0.0036 182  ARG B NH2 
10000 N N   . GLY B 185  ? 0.4577 0.6410 0.2794 0.0687  0.0412  -0.0213 183  GLY B N   
10001 C CA  . GLY B 185  ? 0.4603 0.6354 0.2921 0.0622  0.0375  -0.0186 183  GLY B CA  
10002 C C   . GLY B 185  ? 0.4956 0.6598 0.3243 0.0542  0.0328  -0.0150 183  GLY B C   
10003 O O   . GLY B 185  ? 0.4377 0.6024 0.2726 0.0465  0.0315  -0.0096 183  GLY B O   
10004 N N   . VAL B 186  ? 0.4370 0.5910 0.2558 0.0562  0.0299  -0.0180 184  VAL B N   
10005 C CA  . VAL B 186  ? 0.4985 0.6425 0.3131 0.0493  0.0253  -0.0146 184  VAL B CA  
10006 C C   . VAL B 186  ? 0.5088 0.6649 0.3208 0.0423  0.0279  -0.0070 184  VAL B C   
10007 O O   . VAL B 186  ? 0.5113 0.6635 0.3266 0.0343  0.0251  -0.0018 184  VAL B O   
10008 C CB  . VAL B 186  ? 0.4963 0.6290 0.2999 0.0533  0.0222  -0.0193 184  VAL B CB  
10009 C CG1 . VAL B 186  ? 0.4855 0.6110 0.2832 0.0464  0.0182  -0.0151 184  VAL B CG1 
10010 C CG2 . VAL B 186  ? 0.4688 0.5871 0.2759 0.0580  0.0182  -0.0259 184  VAL B CG2 
10011 N N   . ASP B 187  ? 0.5081 0.6790 0.3139 0.0451  0.0332  -0.0062 185  ASP B N   
10012 C CA  . ASP B 187  ? 0.5229 0.7067 0.3260 0.0382  0.0360  0.0014  185  ASP B CA  
10013 C C   . ASP B 187  ? 0.5640 0.7555 0.3786 0.0318  0.0371  0.0068  185  ASP B C   
10014 O O   . ASP B 187  ? 0.5679 0.7610 0.3825 0.0231  0.0359  0.0136  185  ASP B O   
10015 C CB  . ASP B 187  ? 0.5330 0.7335 0.3286 0.0433  0.0421  0.0009  185  ASP B CB  
10016 C CG  . ASP B 187  ? 0.6503 0.8440 0.4323 0.0477  0.0409  -0.0030 185  ASP B CG  
10017 O OD1 . ASP B 187  ? 0.6956 0.8722 0.4740 0.0460  0.0351  -0.0045 185  ASP B OD1 
10018 O OD2 . ASP B 187  ? 0.6358 0.8415 0.4105 0.0531  0.0457  -0.0045 185  ASP B OD2 
10019 N N   . MET B 188  ? 0.5536 0.7490 0.3776 0.0360  0.0389  0.0039  186  MET B N   
10020 C CA  . MET B 188  ? 0.5084 0.7113 0.3434 0.0304  0.0400  0.0085  186  MET B CA  
10021 C C   . MET B 188  ? 0.5147 0.7022 0.3549 0.0238  0.0340  0.0104  186  MET B C   
10022 O O   . MET B 188  ? 0.5860 0.7760 0.4289 0.0154  0.0331  0.0168  186  MET B O   
10023 C CB  . MET B 188  ? 0.5582 0.7686 0.4013 0.0374  0.0432  0.0045  186  MET B CB  
10024 C CG  . MET B 188  ? 0.6010 0.8199 0.4557 0.0323  0.0443  0.0088  186  MET B CG  
10025 S SD  . MET B 188  ? 0.6606 0.9006 0.5147 0.0246  0.0487  0.0177  186  MET B SD  
10026 C CE  . MET B 188  ? 0.6381 0.8934 0.4833 0.0333  0.0549  0.0147  186  MET B CE  
10027 N N   . ALA B 189  ? 0.5291 0.7006 0.3706 0.0276  0.0299  0.0049  187  ALA B N   
10028 C CA  . ALA B 189  ? 0.5467 0.7036 0.3929 0.0222  0.0244  0.0062  187  ALA B CA  
10029 C C   . ALA B 189  ? 0.5800 0.7314 0.4192 0.0150  0.0212  0.0113  187  ALA B C   
10030 O O   . ALA B 189  ? 0.5610 0.7078 0.4043 0.0079  0.0183  0.0157  187  ALA B O   
10031 C CB  . ALA B 189  ? 0.5026 0.6442 0.3501 0.0278  0.0206  -0.0006 187  ALA B CB  
10032 N N   . MET B 190  ? 0.5569 0.7084 0.3852 0.0168  0.0215  0.0107  188  MET B N   
10033 C CA  . MET B 190  ? 0.6185 0.7644 0.4392 0.0103  0.0184  0.0156  188  MET B CA  
10034 C C   . MET B 190  ? 0.6121 0.7695 0.4340 0.0020  0.0205  0.0237  188  MET B C   
10035 O O   . MET B 190  ? 0.6445 0.7946 0.4667 -0.0054 0.0166  0.0285  188  MET B O   
10036 C CB  . MET B 190  ? 0.5792 0.7248 0.3874 0.0142  0.0189  0.0134  188  MET B CB  
10037 C CG  . MET B 190  ? 0.6906 0.8198 0.4922 0.0123  0.0127  0.0130  188  MET B CG  
10038 S SD  . MET B 190  ? 0.8925 1.0235 0.6780 0.0141  0.0134  0.0130  188  MET B SD  
10039 C CE  . MET B 190  ? 0.6275 0.7646 0.4106 0.0254  0.0178  0.0048  188  MET B CE  
10040 N N   . ARG B 191  ? 0.5693 0.7449 0.3921 0.0032  0.0266  0.0253  189  ARG B N   
10041 C CA  . ARG B 191  ? 0.6232 0.8113 0.4479 -0.0049 0.0288  0.0332  189  ARG B CA  
10042 C C   . ARG B 191  ? 0.6479 0.8318 0.4834 -0.0103 0.0263  0.0357  189  ARG B C   
10043 O O   . ARG B 191  ? 0.6599 0.8402 0.4950 -0.0189 0.0235  0.0417  189  ARG B O   
10044 C CB  . ARG B 191  ? 0.5847 0.7944 0.4096 -0.0017 0.0360  0.0339  189  ARG B CB  
10045 N N   . MET B 192  ? 0.5889 0.7723 0.4335 -0.0052 0.0270  0.0309  190  MET B N   
10046 C CA  . MET B 192  ? 0.5574 0.7370 0.4120 -0.0098 0.0248  0.0328  190  MET B CA  
10047 C C   . MET B 192  ? 0.6147 0.7750 0.4685 -0.0139 0.0180  0.0332  190  MET B C   
10048 O O   . MET B 192  ? 0.6374 0.7948 0.4922 -0.0220 0.0154  0.0388  190  MET B O   
10049 C CB  . MET B 192  ? 0.6057 0.7874 0.4693 -0.0028 0.0266  0.0272  190  MET B CB  
10050 C CG  . MET B 192  ? 0.5805 0.7810 0.4457 0.0023  0.0330  0.0262  190  MET B CG  
10051 S SD  . MET B 192  ? 0.6596 0.8605 0.5359 0.0094  0.0342  0.0204  190  MET B SD  
10052 C CE  . MET B 192  ? 0.4963 0.7014 0.3824 0.0005  0.0331  0.0264  190  MET B CE  
10053 N N   . MET B 193  ? 0.5501 0.6969 0.4020 -0.0083 0.0150  0.0274  191  MET B N   
10054 C CA  . MET B 193  ? 0.6208 0.7500 0.4735 -0.0111 0.0087  0.0270  191  MET B CA  
10055 C C   . MET B 193  ? 0.6136 0.7366 0.4580 -0.0177 0.0053  0.0323  191  MET B C   
10056 O O   . MET B 193  ? 0.6348 0.7454 0.4805 -0.0219 0.0002  0.0339  191  MET B O   
10057 C CB  . MET B 193  ? 0.6368 0.7543 0.4889 -0.0038 0.0063  0.0198  191  MET B CB  
10058 C CG  . MET B 193  ? 0.6139 0.7321 0.4751 0.0018  0.0078  0.0146  191  MET B CG  
10059 S SD  . MET B 193  ? 0.7288 0.8291 0.5913 0.0067  0.0026  0.0079  191  MET B SD  
10060 C CE  . MET B 193  ? 0.5625 0.6628 0.4144 0.0130  0.0037  0.0038  191  MET B CE  
10061 N N   . GLY B 194  ? 0.6120 0.7432 0.4475 -0.0186 0.0078  0.0350  192  GLY B N   
10062 C CA  . GLY B 194  ? 0.6441 0.7687 0.4707 -0.0245 0.0043  0.0399  192  GLY B CA  
10063 C C   . GLY B 194  ? 0.6521 0.7867 0.4766 -0.0331 0.0060  0.0482  192  GLY B C   
10064 O O   . GLY B 194  ? 0.6661 0.7934 0.4844 -0.0394 0.0022  0.0532  192  GLY B O   
10065 N N   . GLU B 195  ? 0.6023 0.7538 0.4320 -0.0335 0.0114  0.0498  193  GLU B N   
10066 C CA  . GLU B 195  ? 0.6262 0.7900 0.4541 -0.0417 0.0137  0.0578  193  GLU B CA  
10067 C C   . GLU B 195  ? 0.6090 0.7825 0.4474 -0.0452 0.0158  0.0602  193  GLU B C   
10068 O O   . GLU B 195  ? 0.5636 0.7423 0.4016 -0.0540 0.0154  0.0674  193  GLU B O   
10069 C CB  . GLU B 195  ? 0.6472 0.8272 0.4679 -0.0395 0.0193  0.0590  193  GLU B CB  
10070 C CG  . GLU B 195  ? 0.7504 0.9221 0.5596 -0.0360 0.0176  0.0567  193  GLU B CG  
10071 C CD  . GLU B 195  ? 0.7805 0.9685 0.5821 -0.0334 0.0234  0.0576  193  GLU B CD  
10072 O OE1 . GLU B 195  ? 0.7036 0.9096 0.5079 -0.0363 0.0284  0.0617  193  GLU B OE1 
10073 O OE2 . GLU B 195  ? 0.8490 1.0320 0.6417 -0.0283 0.0230  0.0540  193  GLU B OE2 
10074 N N   . GLN B 196  ? 0.5807 0.7568 0.4281 -0.0390 0.0176  0.0548  194  GLN B N   
10075 C CA  . GLN B 196  ? 0.5309 0.7158 0.3886 -0.0418 0.0194  0.0566  194  GLN B CA  
10076 C C   . GLN B 196  ? 0.5333 0.7030 0.3974 -0.0441 0.0141  0.0554  194  GLN B C   
10077 O O   . GLN B 196  ? 0.5768 0.7473 0.4446 -0.0515 0.0125  0.0603  194  GLN B O   
10078 C CB  . GLN B 196  ? 0.5902 0.7885 0.4537 -0.0334 0.0249  0.0516  194  GLN B CB  
10079 N N   . PHE B 197  ? 0.5135 0.6693 0.3787 -0.0379 0.0112  0.0491  195  PHE B N   
10080 C CA  . PHE B 197  ? 0.5622 0.7037 0.4333 -0.0395 0.0064  0.0477  195  PHE B CA  
10081 C C   . PHE B 197  ? 0.5282 0.6559 0.3935 -0.0464 0.0006  0.0519  195  PHE B C   
10082 O O   . PHE B 197  ? 0.5421 0.6626 0.4113 -0.0514 -0.0029 0.0541  195  PHE B O   
10083 C CB  . PHE B 197  ? 0.5735 0.7052 0.4475 -0.0309 0.0052  0.0398  195  PHE B CB  
10084 C CG  . PHE B 197  ? 0.6006 0.7434 0.4804 -0.0238 0.0101  0.0353  195  PHE B CG  
10085 C CD1 . PHE B 197  ? 0.5903 0.7485 0.4759 -0.0256 0.0142  0.0379  195  PHE B CD1 
10086 C CD2 . PHE B 197  ? 0.6134 0.7511 0.4927 -0.0155 0.0104  0.0285  195  PHE B CD2 
10087 C CE1 . PHE B 197  ? 0.5994 0.7676 0.4902 -0.0186 0.0185  0.0337  195  PHE B CE1 
10088 C CE2 . PHE B 197  ? 0.5859 0.7327 0.4700 -0.0088 0.0145  0.0244  195  PHE B CE2 
10089 C CZ  . PHE B 197  ? 0.5904 0.7523 0.4801 -0.0101 0.0186  0.0269  195  PHE B CZ  
10090 N N   . VAL B 198  ? 0.4833 0.6066 0.3391 -0.0466 -0.0007 0.0530  196  VAL B N   
10091 C CA  . VAL B 198  ? 0.4706 0.5808 0.3199 -0.0530 -0.0063 0.0573  196  VAL B CA  
10092 C C   . VAL B 198  ? 0.5261 0.6450 0.3665 -0.0584 -0.0045 0.0637  196  VAL B C   
10093 O O   . VAL B 198  ? 0.5198 0.6519 0.3571 -0.0553 0.0005  0.0632  196  VAL B O   
10094 C CB  . VAL B 198  ? 0.4580 0.5512 0.3037 -0.0484 -0.0111 0.0528  196  VAL B CB  
10095 C CG1 . VAL B 198  ? 0.4969 0.5819 0.3516 -0.0435 -0.0129 0.0469  196  VAL B CG1 
10096 C CG2 . VAL B 198  ? 0.5210 0.6179 0.3600 -0.0424 -0.0087 0.0496  196  VAL B CG2 
10097 N N   . THR B 199  ? 0.5262 0.6374 0.3621 -0.0667 -0.0088 0.0699  197  THR B N   
10098 C CA  . THR B 199  ? 0.4279 0.5448 0.2540 -0.0723 -0.0080 0.0762  197  THR B CA  
10099 C C   . THR B 199  ? 0.5387 0.6465 0.3553 -0.0684 -0.0102 0.0741  197  THR B C   
10100 O O   . THR B 199  ? 0.5452 0.6615 0.3538 -0.0691 -0.0074 0.0767  197  THR B O   
10101 C CB  . THR B 199  ? 0.4640 0.5751 0.2881 -0.0829 -0.0121 0.0838  197  THR B CB  
10102 O OG1 . THR B 199  ? 0.5006 0.6158 0.3346 -0.0855 -0.0115 0.0843  197  THR B OG1 
10103 C CG2 . THR B 199  ? 0.4890 0.6121 0.3053 -0.0899 -0.0096 0.0915  197  THR B CG2 
10104 N N   . GLY B 200  ? 0.4761 0.5673 0.2935 -0.0641 -0.0150 0.0693  198  GLY B N   
10105 C CA  . GLY B 200  ? 0.5239 0.6061 0.3332 -0.0598 -0.0175 0.0665  198  GLY B CA  
10106 C C   . GLY B 200  ? 0.5381 0.6059 0.3522 -0.0538 -0.0216 0.0598  198  GLY B C   
10107 O O   . GLY B 200  ? 0.4703 0.5320 0.2924 -0.0545 -0.0238 0.0587  198  GLY B O   
10108 N N   . GLU B 201  ? 0.5747 0.6377 0.3839 -0.0478 -0.0226 0.0554  199  GLU B N   
10109 C CA  . GLU B 201  ? 0.5756 0.6255 0.3890 -0.0422 -0.0267 0.0493  199  GLU B CA  
10110 C C   . GLU B 201  ? 0.5453 0.5785 0.3547 -0.0456 -0.0340 0.0518  199  GLU B C   
10111 O O   . GLU B 201  ? 0.5898 0.6121 0.4043 -0.0423 -0.0379 0.0477  199  GLU B O   
10112 C CB  . GLU B 201  ? 0.6102 0.6617 0.4202 -0.0345 -0.0251 0.0434  199  GLU B CB  
10113 C CG  . GLU B 201  ? 0.6992 0.7655 0.5136 -0.0299 -0.0183 0.0400  199  GLU B CG  
10114 C CD  . GLU B 201  ? 0.8196 0.8856 0.6312 -0.0219 -0.0172 0.0334  199  GLU B CD  
10115 O OE1 . GLU B 201  ? 0.8010 0.8613 0.6035 -0.0210 -0.0198 0.0333  199  GLU B OE1 
10116 O OE2 . GLU B 201  ? 0.8662 0.9374 0.6845 -0.0165 -0.0140 0.0284  199  GLU B OE2 
10117 N N   . THR B 202  ? 0.5302 0.5616 0.3304 -0.0518 -0.0359 0.0583  200  THR B N   
10118 C CA  . THR B 202  ? 0.5286 0.5444 0.3243 -0.0559 -0.0429 0.0617  200  THR B CA  
10119 C C   . THR B 202  ? 0.5399 0.5580 0.3326 -0.0652 -0.0432 0.0698  200  THR B C   
10120 O O   . THR B 202  ? 0.5096 0.5420 0.3008 -0.0686 -0.0381 0.0734  200  THR B O   
10121 C CB  . THR B 202  ? 0.5481 0.5567 0.3332 -0.0543 -0.0463 0.0620  200  THR B CB  
10122 O OG1 . THR B 202  ? 0.5415 0.5607 0.3176 -0.0580 -0.0427 0.0669  200  THR B OG1 
10123 C CG2 . THR B 202  ? 0.5650 0.5720 0.3524 -0.0455 -0.0461 0.0542  200  THR B CG2 
10124 N N   . ILE B 203  ? 0.5076 0.5116 0.2993 -0.0693 -0.0494 0.0728  201  ILE B N   
10125 C CA  . ILE B 203  ? 0.5083 0.5125 0.2963 -0.0788 -0.0505 0.0807  201  ILE B CA  
10126 C C   . ILE B 203  ? 0.5120 0.5213 0.2884 -0.0834 -0.0495 0.0867  201  ILE B C   
10127 O O   . ILE B 203  ? 0.4974 0.5164 0.2715 -0.0906 -0.0468 0.0930  201  ILE B O   
10128 C CB  . ILE B 203  ? 0.4852 0.4710 0.2730 -0.0818 -0.0580 0.0824  201  ILE B CB  
10129 C CG1 . ILE B 203  ? 0.4330 0.4186 0.2177 -0.0919 -0.0593 0.0904  201  ILE B CG1 
10130 C CG2 . ILE B 203  ? 0.4750 0.4461 0.2546 -0.0797 -0.0642 0.0822  201  ILE B CG2 
10131 C CD1 . ILE B 203  ? 0.4216 0.4191 0.2155 -0.0944 -0.0548 0.0905  201  ILE B CD1 
10132 N N   . ARG B 204  ? 0.5059 0.5098 0.2748 -0.0793 -0.0515 0.0848  202  ARG B N   
10133 C CA  . ARG B 204  ? 0.5148 0.5240 0.2721 -0.0828 -0.0502 0.0899  202  ARG B CA  
10134 C C   . ARG B 204  ? 0.5234 0.5537 0.2817 -0.0830 -0.0419 0.0906  202  ARG B C   
10135 O O   . ARG B 204  ? 0.5197 0.5588 0.2722 -0.0900 -0.0396 0.0976  202  ARG B O   
10136 C CB  . ARG B 204  ? 0.5827 0.5834 0.3333 -0.0767 -0.0534 0.0861  202  ARG B CB  
10137 C CG  . ARG B 204  ? 0.6114 0.6146 0.3489 -0.0799 -0.0533 0.0912  202  ARG B CG  
10138 C CD  . ARG B 204  ? 0.5989 0.5919 0.3302 -0.0738 -0.0575 0.0871  202  ARG B CD  
10139 N NE  . ARG B 204  ? 0.5725 0.5746 0.3064 -0.0657 -0.0529 0.0799  202  ARG B NE  
10140 C CZ  . ARG B 204  ? 0.6015 0.6153 0.3281 -0.0646 -0.0482 0.0803  202  ARG B CZ  
10141 N NH1 . ARG B 204  ? 0.6376 0.6574 0.3548 -0.0712 -0.0467 0.0877  202  ARG B NH1 
10142 N NH2 . ARG B 204  ? 0.6208 0.6402 0.3494 -0.0566 -0.0450 0.0731  202  ARG B NH2 
10143 N N   . GLU B 205  ? 0.5009 0.5397 0.2666 -0.0753 -0.0373 0.0835  203  GLU B N   
10144 C CA  . GLU B 205  ? 0.5155 0.5744 0.2827 -0.0740 -0.0294 0.0833  203  GLU B CA  
10145 C C   . GLU B 205  ? 0.5235 0.5931 0.2978 -0.0801 -0.0262 0.0875  203  GLU B C   
10146 O O   . GLU B 205  ? 0.4627 0.5479 0.2344 -0.0841 -0.0212 0.0921  203  GLU B O   
10147 C CB  . GLU B 205  ? 0.5698 0.6326 0.3430 -0.0639 -0.0262 0.0742  203  GLU B CB  
10148 C CG  . GLU B 205  ? 0.6120 0.6947 0.3873 -0.0611 -0.0182 0.0730  203  GLU B CG  
10149 C CD  . GLU B 205  ? 0.6988 0.7831 0.4784 -0.0510 -0.0158 0.0640  203  GLU B CD  
10150 O OE1 . GLU B 205  ? 0.6990 0.7727 0.4857 -0.0471 -0.0191 0.0590  203  GLU B OE1 
10151 O OE2 . GLU B 205  ? 0.8091 0.9052 0.5847 -0.0469 -0.0108 0.0621  203  GLU B OE2 
10152 N N   . ALA B 206  ? 0.4598 0.5220 0.2432 -0.0807 -0.0289 0.0859  204  ALA B N   
10153 C CA  . ALA B 206  ? 0.4923 0.5635 0.2822 -0.0868 -0.0265 0.0899  204  ALA B CA  
10154 C C   . ALA B 206  ? 0.4965 0.5690 0.2787 -0.0975 -0.0281 0.0995  204  ALA B C   
10155 O O   . ALA B 206  ? 0.5054 0.5937 0.2892 -0.1026 -0.0235 0.1041  204  ALA B O   
10156 C CB  . ALA B 206  ? 0.4498 0.5097 0.2490 -0.0860 -0.0303 0.0868  204  ALA B CB  
10157 N N   . LEU B 207  ? 0.4495 0.5058 0.2231 -0.1010 -0.0346 0.1028  205  LEU B N   
10158 C CA  . LEU B 207  ? 0.5237 0.5789 0.2893 -0.1117 -0.0368 0.1123  205  LEU B CA  
10159 C C   . LEU B 207  ? 0.5636 0.6353 0.3215 -0.1140 -0.0314 0.1166  205  LEU B C   
10160 O O   . LEU B 207  ? 0.5612 0.6449 0.3182 -0.1220 -0.0287 0.1235  205  LEU B O   
10161 C CB  . LEU B 207  ? 0.5280 0.5610 0.2857 -0.1140 -0.0453 0.1144  205  LEU B CB  
10162 C CG  . LEU B 207  ? 0.4962 0.5119 0.2598 -0.1136 -0.0516 0.1120  205  LEU B CG  
10163 C CD1 . LEU B 207  ? 0.4702 0.4650 0.2257 -0.1125 -0.0594 0.1121  205  LEU B CD1 
10164 C CD2 . LEU B 207  ? 0.4627 0.4788 0.2290 -0.1231 -0.0528 0.1180  205  LEU B CD2 
10165 N N   . LYS B 208  ? 0.4946 0.5673 0.2467 -0.1071 -0.0299 0.1126  206  LYS B N   
10166 C CA  . LYS B 208  ? 0.5343 0.6237 0.2793 -0.1080 -0.0241 0.1157  206  LYS B CA  
10167 C C   . LYS B 208  ? 0.5484 0.6603 0.3016 -0.1074 -0.0162 0.1153  206  LYS B C   
10168 O O   . LYS B 208  ? 0.5818 0.7093 0.3311 -0.1131 -0.0119 0.1214  206  LYS B O   
10169 C CB  . LYS B 208  ? 0.5709 0.6576 0.3095 -0.0992 -0.0237 0.1099  206  LYS B CB  
10170 N N   . ARG B 209  ? 0.5307 0.6450 0.2951 -0.1007 -0.0141 0.1083  207  ARG B N   
10171 C CA  . ARG B 209  ? 0.5446 0.6800 0.3171 -0.0994 -0.0067 0.1076  207  ARG B CA  
10172 C C   . ARG B 209  ? 0.6052 0.7468 0.3832 -0.1090 -0.0067 0.1142  207  ARG B C   
10173 O O   . ARG B 209  ? 0.6017 0.7629 0.3855 -0.1097 -0.0007 0.1154  207  ARG B O   
10174 C CB  . ARG B 209  ? 0.5654 0.7011 0.3477 -0.0891 -0.0047 0.0981  207  ARG B CB  
10175 C CG  . ARG B 209  ? 0.5927 0.7291 0.3701 -0.0794 -0.0025 0.0915  207  ARG B CG  
10176 C CD  . ARG B 209  ? 0.6288 0.7673 0.4159 -0.0699 0.0001  0.0827  207  ARG B CD  
10177 N NE  . ARG B 209  ? 0.7277 0.8662 0.5097 -0.0609 0.0018  0.0764  207  ARG B NE  
10178 C CZ  . ARG B 209  ? 0.7650 0.8998 0.5527 -0.0520 0.0023  0.0682  207  ARG B CZ  
10179 N NH1 . ARG B 209  ? 0.6832 0.8142 0.4820 -0.0506 0.0013  0.0651  207  ARG B NH1 
10180 N NH2 . ARG B 209  ? 0.7797 0.9145 0.5615 -0.0446 0.0036  0.0629  207  ARG B NH2 
10181 N N   . SER B 210  ? 0.5744 0.7000 0.3507 -0.1163 -0.0135 0.1185  208  SER B N   
10182 C CA  . SER B 210  ? 0.5422 0.6721 0.3236 -0.1257 -0.0142 0.1247  208  SER B CA  
10183 C C   . SER B 210  ? 0.5283 0.6692 0.3028 -0.1357 -0.0126 0.1343  208  SER B C   
10184 O O   . SER B 210  ? 0.5247 0.6738 0.3062 -0.1425 -0.0116 0.1383  208  SER B O   
10185 C CB  . SER B 210  ? 0.4713 0.5787 0.2537 -0.1290 -0.0224 0.1250  208  SER B CB  
10186 O OG  . SER B 210  ? 0.4892 0.5882 0.2798 -0.1201 -0.0234 0.1162  208  SER B OG  
10187 N N   . LYS B 211  ? 0.5815 0.7210 0.3472 -0.1348 -0.0124 0.1354  209  LYS B N   
10188 C CA  . LYS B 211  ? 0.5333 0.6793 0.2966 -0.1424 -0.0115 0.1420  209  LYS B CA  
10189 C C   . LYS B 211  ? 0.5948 0.7660 0.3670 -0.1433 -0.0040 0.1431  209  LYS B C   
10190 O O   . LYS B 211  ? 0.5772 0.7548 0.3520 -0.1519 -0.0040 0.1492  209  LYS B O   
10191 C CB  . LYS B 211  ? 0.5634 0.7047 0.3154 -0.1397 -0.0120 0.1421  209  LYS B CB  
10192 C CG  . LYS B 211  ? 0.6982 0.8150 0.4414 -0.1386 -0.0198 0.1411  209  LYS B CG  
10193 C CD  . LYS B 211  ? 0.7535 0.8543 0.4949 -0.1484 -0.0271 0.1474  209  LYS B CD  
10194 C CE  . LYS B 211  ? 0.7873 0.8654 0.5182 -0.1474 -0.0346 0.1474  209  LYS B CE  
10195 N NZ  . LYS B 211  ? 0.7888 0.8550 0.5197 -0.1397 -0.0378 0.1410  209  LYS B NZ  
10196 N N   . GLU B 212  ? 0.5717 0.7569 0.3488 -0.1343 0.0023  0.1371  210  GLU B N   
10197 C CA  . GLU B 212  ? 0.5487 0.7582 0.3342 -0.1335 0.0096  0.1373  210  GLU B CA  
10198 C C   . GLU B 212  ? 0.5522 0.7678 0.3481 -0.1409 0.0089  0.1410  210  GLU B C   
10199 O O   . GLU B 212  ? 0.5617 0.7884 0.3608 -0.1481 0.0101  0.1465  210  GLU B O   
10200 C CB  . GLU B 212  ? 0.5422 0.7625 0.3308 -0.1216 0.0155  0.1294  210  GLU B CB  
10201 N N   . LEU B 213  ? 0.5219 0.7304 0.3232 -0.1394 0.0066  0.1381  211  LEU B N   
10202 C CA  . LEU B 213  ? 0.5634 0.7778 0.3746 -0.1460 0.0059  0.1411  211  LEU B CA  
10203 C C   . LEU B 213  ? 0.5743 0.7743 0.3822 -0.1575 -0.0012 0.1480  211  LEU B C   
10204 O O   . LEU B 213  ? 0.5570 0.7645 0.3717 -0.1651 -0.0017 0.1522  211  LEU B O   
10205 C CB  . LEU B 213  ? 0.5275 0.7391 0.3453 -0.1406 0.0059  0.1358  211  LEU B CB  
10206 C CG  . LEU B 213  ? 0.5546 0.7807 0.3764 -0.1290 0.0128  0.1288  211  LEU B CG  
10207 C CD1 . LEU B 213  ? 0.5544 0.7818 0.3849 -0.1253 0.0134  0.1247  211  LEU B CD1 
10208 C CD2 . LEU B 213  ? 0.6200 0.8694 0.4466 -0.1279 0.0195  0.1299  211  LEU B CD2 
10209 N N   . GLU B 214  ? 0.5498 0.7288 0.3473 -0.1589 -0.0071 0.1490  212  GLU B N   
10210 C CA  . GLU B 214  ? 0.5577 0.7223 0.3513 -0.1695 -0.0141 0.1554  212  GLU B CA  
10211 C C   . GLU B 214  ? 0.5787 0.7561 0.3719 -0.1768 -0.0121 0.1616  212  GLU B C   
10212 O O   . GLU B 214  ? 0.5882 0.7647 0.3843 -0.1865 -0.0155 0.1669  212  GLU B O   
10213 C CB  . GLU B 214  ? 0.5860 0.7259 0.3685 -0.1685 -0.0207 0.1550  212  GLU B CB  
10214 C CG  . GLU B 214  ? 0.5550 0.6777 0.3380 -0.1650 -0.0255 0.1509  212  GLU B CG  
10215 C CD  . GLU B 214  ? 0.5483 0.6460 0.3207 -0.1644 -0.0330 0.1508  212  GLU B CD  
10216 O OE1 . GLU B 214  ? 0.6363 0.7310 0.4006 -0.1652 -0.0337 0.1530  212  GLU B OE1 
10217 O OE2 . GLU B 214  ? 0.5756 0.6568 0.3477 -0.1629 -0.0382 0.1484  212  GLU B OE2 
10218 N N   . GLU B 215  ? 0.5604 0.7503 0.3503 -0.1723 -0.0068 0.1608  213  GLU B N   
10219 C CA  . GLU B 215  ? 0.5481 0.7522 0.3379 -0.1787 -0.0044 0.1665  213  GLU B CA  
10220 C C   . GLU B 215  ? 0.6149 0.8405 0.4169 -0.1817 -0.0002 0.1679  213  GLU B C   
10221 O O   . GLU B 215  ? 0.6349 0.8694 0.4385 -0.1901 -0.0005 0.1738  213  GLU B O   
10222 C CB  . GLU B 215  ? 0.6028 0.8158 0.3861 -0.1724 0.0007  0.1647  213  GLU B CB  
10223 N N   . LYS B 216  ? 0.5892 0.8232 0.3999 -0.1751 0.0033  0.1626  214  LYS B N   
10224 C CA  . LYS B 216  ? 0.6092 0.8621 0.4319 -0.1777 0.0064  0.1637  214  LYS B CA  
10225 C C   . LYS B 216  ? 0.5747 0.8177 0.4021 -0.1860 0.0004  0.1666  214  LYS B C   
10226 O O   . LYS B 216  ? 0.6030 0.8605 0.4401 -0.1894 0.0019  0.1681  214  LYS B O   
10227 C CB  . LYS B 216  ? 0.5634 0.8305 0.3936 -0.1666 0.0129  0.1567  214  LYS B CB  
10228 C CG  . LYS B 216  ? 0.6444 0.9243 0.4714 -0.1577 0.0195  0.1532  214  LYS B CG  
10229 C CD  . LYS B 216  ? 0.6556 0.9555 0.4930 -0.1494 0.0261  0.1481  214  LYS B CD  
10230 C CE  . LYS B 216  ? 0.7053 1.0123 0.5387 -0.1379 0.0318  0.1423  214  LYS B CE  
10231 N NZ  . LYS B 216  ? 0.7291 1.0216 0.5589 -0.1295 0.0307  0.1356  214  LYS B NZ  
10232 N N   . GLY B 217  ? 0.5549 0.7733 0.3755 -0.1890 -0.0067 0.1671  215  GLY B N   
10233 C CA  . GLY B 217  ? 0.5622 0.7685 0.3855 -0.1971 -0.0132 0.1700  215  GLY B CA  
10234 C C   . GLY B 217  ? 0.5816 0.7748 0.4072 -0.1925 -0.0156 0.1650  215  GLY B C   
10235 O O   . GLY B 217  ? 0.5958 0.7779 0.4234 -0.1987 -0.0211 0.1669  215  GLY B O   
10236 N N   . PHE B 218  ? 0.5230 0.7173 0.3483 -0.1818 -0.0117 0.1587  216  PHE B N   
10237 C CA  . PHE B 218  ? 0.5375 0.7173 0.3634 -0.1773 -0.0146 0.1542  216  PHE B CA  
10238 C C   . PHE B 218  ? 0.5452 0.6980 0.3601 -0.1789 -0.0221 0.1549  216  PHE B C   
10239 O O   . PHE B 218  ? 0.5252 0.6716 0.3316 -0.1806 -0.0238 0.1575  216  PHE B O   
10240 C CB  . PHE B 218  ? 0.5434 0.7324 0.3718 -0.1653 -0.0085 0.1471  216  PHE B CB  
10241 C CG  . PHE B 218  ? 0.5533 0.7670 0.3931 -0.1620 -0.0015 0.1452  216  PHE B CG  
10242 C CD1 . PHE B 218  ? 0.5599 0.7935 0.4017 -0.1609 0.0042  0.1465  216  PHE B CD1 
10243 C CD2 . PHE B 218  ? 0.5237 0.7405 0.3722 -0.1597 -0.0008 0.1422  216  PHE B CD2 
10244 C CE1 . PHE B 218  ? 0.5563 0.8121 0.4085 -0.1572 0.0102  0.1446  216  PHE B CE1 
10245 C CE2 . PHE B 218  ? 0.5441 0.7832 0.4031 -0.1562 0.0053  0.1403  216  PHE B CE2 
10246 C CZ  . PHE B 218  ? 0.5201 0.7786 0.3810 -0.1548 0.0107  0.1415  216  PHE B CZ  
10247 N N   . SER B 219  ? 0.5177 0.6548 0.3331 -0.1779 -0.0266 0.1525  217  SER B N   
10248 C CA  . SER B 219  ? 0.4852 0.5968 0.2910 -0.1765 -0.0334 0.1513  217  SER B CA  
10249 C C   . SER B 219  ? 0.4884 0.5948 0.3008 -0.1640 -0.0323 0.1411  217  SER B C   
10250 O O   . SER B 219  ? 0.5004 0.6225 0.3221 -0.1582 -0.0264 0.1367  217  SER B O   
10251 C CB  . SER B 219  ? 0.5210 0.6136 0.3246 -0.1853 -0.0417 0.1554  217  SER B CB  
10252 O OG  . SER B 219  ? 0.5417 0.6343 0.3537 -0.1860 -0.0425 0.1534  217  SER B OG  
10253 N N   . TYR B 220  ? 0.4782 0.5626 0.2863 -0.1594 -0.0380 0.1370  218  TYR B N   
10254 C CA  . TYR B 220  ? 0.4538 0.5331 0.2675 -0.1473 -0.0369 0.1273  218  TYR B CA  
10255 C C   . TYR B 220  ? 0.4356 0.4921 0.2503 -0.1457 -0.0441 0.1237  218  TYR B C   
10256 O O   . TYR B 220  ? 0.4932 0.5334 0.3008 -0.1521 -0.0508 0.1281  218  TYR B O   
10257 C CB  . TYR B 220  ? 0.4271 0.5062 0.2343 -0.1401 -0.0350 0.1243  218  TYR B CB  
10258 C CG  . TYR B 220  ? 0.4437 0.5461 0.2532 -0.1365 -0.0266 0.1235  218  TYR B CG  
10259 C CD1 . TYR B 220  ? 0.4622 0.5788 0.2656 -0.1432 -0.0233 0.1308  218  TYR B CD1 
10260 C CD2 . TYR B 220  ? 0.4294 0.5396 0.2467 -0.1261 -0.0219 0.1155  218  TYR B CD2 
10261 C CE1 . TYR B 220  ? 0.4433 0.5818 0.2487 -0.1390 -0.0154 0.1297  218  TYR B CE1 
10262 C CE2 . TYR B 220  ? 0.4364 0.5671 0.2553 -0.1220 -0.0145 0.1144  218  TYR B CE2 
10263 C CZ  . TYR B 220  ? 0.4447 0.5897 0.2577 -0.1282 -0.0112 0.1213  218  TYR B CZ  
10264 O OH  . TYR B 220  ? 0.4683 0.6339 0.2830 -0.1232 -0.0036 0.1196  218  TYR B OH  
10265 N N   . SER B 221  ? 0.4417 0.4972 0.2651 -0.1369 -0.0427 0.1157  219  SER B N   
10266 C CA  . SER B 221  ? 0.4092 0.4447 0.2341 -0.1325 -0.0484 0.1105  219  SER B CA  
10267 C C   . SER B 221  ? 0.4294 0.4660 0.2585 -0.1206 -0.0454 0.1020  219  SER B C   
10268 O O   . SER B 221  ? 0.4114 0.4622 0.2488 -0.1157 -0.0398 0.0980  219  SER B O   
10269 C CB  . SER B 221  ? 0.4041 0.4374 0.2366 -0.1355 -0.0502 0.1099  219  SER B CB  
10270 O OG  . SER B 221  ? 0.4187 0.4348 0.2535 -0.1295 -0.0546 0.1038  219  SER B OG  
10271 N N   . TYR B 222  ? 0.4160 0.4381 0.2394 -0.1161 -0.0494 0.0994  220  TYR B N   
10272 C CA  . TYR B 222  ? 0.4092 0.4329 0.2353 -0.1057 -0.0467 0.0921  220  TYR B CA  
10273 C C   . TYR B 222  ? 0.3877 0.4012 0.2212 -0.0991 -0.0490 0.0850  220  TYR B C   
10274 O O   . TYR B 222  ? 0.4067 0.4043 0.2391 -0.1010 -0.0550 0.0853  220  TYR B O   
10275 C CB  . TYR B 222  ? 0.4028 0.4181 0.2189 -0.1040 -0.0493 0.0928  220  TYR B CB  
10276 C CG  . TYR B 222  ? 0.4123 0.4390 0.2207 -0.1100 -0.0464 0.0995  220  TYR B CG  
10277 C CD1 . TYR B 222  ? 0.4070 0.4515 0.2166 -0.1063 -0.0395 0.0980  220  TYR B CD1 
10278 C CD2 . TYR B 222  ? 0.4272 0.4470 0.2271 -0.1194 -0.0507 0.1075  220  TYR B CD2 
10279 C CE1 . TYR B 222  ? 0.4157 0.4718 0.2184 -0.1114 -0.0364 0.1041  220  TYR B CE1 
10280 C CE2 . TYR B 222  ? 0.4463 0.4775 0.2392 -0.1252 -0.0478 0.1140  220  TYR B CE2 
10281 C CZ  . TYR B 222  ? 0.4301 0.4800 0.2246 -0.1211 -0.0404 0.1122  220  TYR B CZ  
10282 O OH  . TYR B 222  ? 0.4542 0.5166 0.2418 -0.1265 -0.0372 0.1184  220  TYR B OH  
10283 N N   . ASP B 223  ? 0.3898 0.4126 0.2309 -0.0914 -0.0442 0.0788  221  ASP B N   
10284 C CA  . ASP B 223  ? 0.4306 0.4470 0.2797 -0.0845 -0.0452 0.0718  221  ASP B CA  
10285 C C   . ASP B 223  ? 0.5008 0.5134 0.3488 -0.0760 -0.0450 0.0661  221  ASP B C   
10286 O O   . ASP B 223  ? 0.4986 0.5230 0.3491 -0.0711 -0.0398 0.0631  221  ASP B O   
10287 C CB  . ASP B 223  ? 0.4436 0.4740 0.3026 -0.0831 -0.0399 0.0696  221  ASP B CB  
10288 C CG  . ASP B 223  ? 0.5202 0.5466 0.3872 -0.0749 -0.0397 0.0620  221  ASP B CG  
10289 O OD1 . ASP B 223  ? 0.5247 0.5360 0.3916 -0.0732 -0.0447 0.0596  221  ASP B OD1 
10290 O OD2 . ASP B 223  ? 0.5469 0.5853 0.4203 -0.0702 -0.0345 0.0584  221  ASP B OD2 
10291 N N   . MET B 224  ? 0.4654 0.4617 0.3097 -0.0742 -0.0509 0.0648  222  MET B N   
10292 C CA  . MET B 224  ? 0.5227 0.5142 0.3676 -0.0661 -0.0515 0.0588  222  MET B CA  
10293 C C   . MET B 224  ? 0.5190 0.5139 0.3746 -0.0600 -0.0490 0.0524  222  MET B C   
10294 O O   . MET B 224  ? 0.5840 0.5714 0.4443 -0.0602 -0.0517 0.0510  222  MET B O   
10295 C CB  . MET B 224  ? 0.4835 0.4571 0.3228 -0.0659 -0.0587 0.0592  222  MET B CB  
10296 C CG  . MET B 224  ? 0.4540 0.4229 0.2822 -0.0726 -0.0618 0.0661  222  MET B CG  
10297 S SD  . MET B 224  ? 0.5500 0.5314 0.3709 -0.0725 -0.0573 0.0683  222  MET B SD  
10298 C CE  . MET B 224  ? 0.4557 0.4273 0.2746 -0.0639 -0.0605 0.0623  222  MET B CE  
10299 N N   . LEU B 225  ? 0.5171 0.5235 0.3762 -0.0550 -0.0438 0.0488  223  LEU B N   
10300 C CA  . LEU B 225  ? 0.5548 0.5658 0.4238 -0.0496 -0.0409 0.0432  223  LEU B CA  
10301 C C   . LEU B 225  ? 0.6392 0.6369 0.5118 -0.0454 -0.0454 0.0387  223  LEU B C   
10302 O O   . LEU B 225  ? 0.6126 0.6033 0.4823 -0.0415 -0.0480 0.0361  223  LEU B O   
10303 C CB  . LEU B 225  ? 0.5945 0.6164 0.4646 -0.0440 -0.0358 0.0396  223  LEU B CB  
10304 C CG  . LEU B 225  ? 0.6091 0.6465 0.4774 -0.0472 -0.0305 0.0433  223  LEU B CG  
10305 C CD1 . LEU B 225  ? 0.6181 0.6642 0.4852 -0.0410 -0.0262 0.0396  223  LEU B CD1 
10306 C CD2 . LEU B 225  ? 0.5628 0.6085 0.4389 -0.0497 -0.0278 0.0443  223  LEU B CD2 
10307 N N   . GLY B 226  ? 0.5560 0.5507 0.4347 -0.0464 -0.0464 0.0379  224  GLY B N   
10308 C CA  . GLY B 226  ? 0.5909 0.5731 0.4726 -0.0431 -0.0508 0.0343  224  GLY B CA  
10309 C C   . GLY B 226  ? 0.5244 0.5038 0.4114 -0.0452 -0.0518 0.0343  224  GLY B C   
10310 O O   . GLY B 226  ? 0.5076 0.4870 0.3921 -0.0517 -0.0527 0.0390  224  GLY B O   
10311 N N   . GLU B 227  ? 0.5290 0.5062 0.4232 -0.0400 -0.0518 0.0291  225  GLU B N   
10312 C CA  . GLU B 227  ? 0.4612 0.4361 0.3609 -0.0410 -0.0525 0.0282  225  GLU B CA  
10313 C C   . GLU B 227  ? 0.4300 0.4022 0.3367 -0.0342 -0.0525 0.0220  225  GLU B C   
10314 O O   . GLU B 227  ? 0.4517 0.4270 0.3603 -0.0292 -0.0508 0.0186  225  GLU B O   
10315 C CB  . GLU B 227  ? 0.5079 0.4952 0.4114 -0.0444 -0.0478 0.0302  225  GLU B CB  
10316 C CG  . GLU B 227  ? 0.5259 0.5264 0.4340 -0.0403 -0.0420 0.0275  225  GLU B CG  
10317 C CD  . GLU B 227  ? 0.5750 0.5876 0.4873 -0.0433 -0.0379 0.0294  225  GLU B CD  
10318 O OE1 . GLU B 227  ? 0.5815 0.5942 0.5000 -0.0426 -0.0376 0.0275  225  GLU B OE1 
10319 O OE2 . GLU B 227  ? 0.5978 0.6203 0.5074 -0.0463 -0.0349 0.0329  225  GLU B OE2 
10320 N N   . ALA B 228  ? 0.3986 0.3653 0.3089 -0.0343 -0.0544 0.0208  226  ALA B N   
10321 C CA  . ALA B 228  ? 0.4136 0.3786 0.3310 -0.0286 -0.0543 0.0153  226  ALA B CA  
10322 C C   . ALA B 228  ? 0.3948 0.3545 0.3117 -0.0233 -0.0565 0.0121  226  ALA B C   
10323 O O   . ALA B 228  ? 0.3936 0.3589 0.3150 -0.0188 -0.0538 0.0085  226  ALA B O   
10324 C CB  . ALA B 228  ? 0.4181 0.3954 0.3428 -0.0266 -0.0487 0.0131  226  ALA B CB  
10325 N N   . ALA B 229  ? 0.3426 0.2913 0.2536 -0.0241 -0.0616 0.0137  227  ALA B N   
10326 C CA  . ALA B 229  ? 0.3716 0.3143 0.2826 -0.0191 -0.0646 0.0106  227  ALA B CA  
10327 C C   . ALA B 229  ? 0.3557 0.2990 0.2751 -0.0137 -0.0640 0.0054  227  ALA B C   
10328 O O   . ALA B 229  ? 0.3838 0.3248 0.3063 -0.0141 -0.0643 0.0046  227  ALA B O   
10329 C CB  . ALA B 229  ? 0.3187 0.2486 0.2226 -0.0206 -0.0707 0.0130  227  ALA B CB  
10330 N N   . THR B 230  ? 0.3632 0.3099 0.2862 -0.0091 -0.0629 0.0019  228  THR B N   
10331 C CA  . THR B 230  ? 0.3769 0.3251 0.3080 -0.0041 -0.0622 -0.0028 228  THR B CA  
10332 C C   . THR B 230  ? 0.3709 0.3106 0.3021 -0.0004 -0.0671 -0.0049 228  THR B C   
10333 O O   . THR B 230  ? 0.3306 0.2692 0.2675 0.0028  -0.0676 -0.0080 228  THR B O   
10334 C CB  . THR B 230  ? 0.4311 0.3885 0.3666 -0.0014 -0.0582 -0.0054 228  THR B CB  
10335 O OG1 . THR B 230  ? 0.4656 0.4312 0.4009 -0.0043 -0.0536 -0.0036 228  THR B OG1 
10336 C CG2 . THR B 230  ? 0.3979 0.3575 0.3419 0.0029  -0.0572 -0.0098 228  THR B CG2 
10337 N N   . THR B 231  ? 0.3791 0.3134 0.3042 -0.0004 -0.0706 -0.0033 229  THR B N   
10338 C CA  . THR B 231  ? 0.3735 0.3002 0.2984 0.0034  -0.0755 -0.0051 229  THR B CA  
10339 C C   . THR B 231  ? 0.3852 0.3013 0.3012 0.0007  -0.0805 -0.0013 229  THR B C   
10340 O O   . THR B 231  ? 0.3806 0.2964 0.2903 -0.0043 -0.0799 0.0028  229  THR B O   
10341 C CB  . THR B 231  ? 0.3547 0.2847 0.2810 0.0067  -0.0758 -0.0072 229  THR B CB  
10342 O OG1 . THR B 231  ? 0.4062 0.3353 0.3244 0.0038  -0.0764 -0.0039 229  THR B OG1 
10343 C CG2 . THR B 231  ? 0.3351 0.2753 0.2689 0.0085  -0.0709 -0.0104 229  THR B CG2 
10344 N N   . ALA B 232  ? 0.3493 0.2572 0.2650 0.0043  -0.0854 -0.0027 230  ALA B N   
10345 C CA  . ALA B 232  ? 0.4097 0.3062 0.3165 0.0025  -0.0909 0.0007  230  ALA B CA  
10346 C C   . ALA B 232  ? 0.4255 0.3226 0.3253 -0.0001 -0.0914 0.0039  230  ALA B C   
10347 O O   . ALA B 232  ? 0.3783 0.2693 0.2696 -0.0047 -0.0937 0.0084  230  ALA B O   
10348 C CB  . ALA B 232  ? 0.4390 0.3276 0.3472 0.0080  -0.0961 -0.0020 230  ALA B CB  
10349 N N   . ALA B 233  ? 0.4127 0.3169 0.3156 0.0026  -0.0895 0.0016  231  ALA B N   
10350 C CA  . ALA B 233  ? 0.4047 0.3096 0.3007 0.0007  -0.0901 0.0041  231  ALA B CA  
10351 C C   . ALA B 233  ? 0.4123 0.3235 0.3044 -0.0048 -0.0856 0.0075  231  ALA B C   
10352 O O   . ALA B 233  ? 0.3794 0.2885 0.2630 -0.0082 -0.0867 0.0115  231  ALA B O   
10353 C CB  . ALA B 233  ? 0.3692 0.2799 0.2694 0.0050  -0.0893 0.0004  231  ALA B CB  
10354 N N   . ASP B 234  ? 0.3095 0.2288 0.2076 -0.0056 -0.0805 0.0062  232  ASP B N   
10355 C CA  . ASP B 234  ? 0.3927 0.3185 0.2878 -0.0106 -0.0763 0.0096  232  ASP B CA  
10356 C C   . ASP B 234  ? 0.3809 0.2996 0.2689 -0.0161 -0.0790 0.0147  232  ASP B C   
10357 O O   . ASP B 234  ? 0.3407 0.2611 0.2218 -0.0207 -0.0782 0.0190  232  ASP B O   
10358 C CB  . ASP B 234  ? 0.3563 0.2908 0.2595 -0.0102 -0.0712 0.0073  232  ASP B CB  
10359 C CG  . ASP B 234  ? 0.4399 0.3830 0.3489 -0.0062 -0.0675 0.0032  232  ASP B CG  
10360 O OD1 . ASP B 234  ? 0.4557 0.3995 0.3616 -0.0046 -0.0682 0.0026  232  ASP B OD1 
10361 O OD2 . ASP B 234  ? 0.4480 0.3967 0.3644 -0.0048 -0.0642 0.0007  232  ASP B OD2 
10362 N N   . ALA B 235  ? 0.3507 0.2616 0.2403 -0.0160 -0.0820 0.0143  233  ALA B N   
10363 C CA  . ALA B 235  ? 0.3702 0.2731 0.2533 -0.0214 -0.0849 0.0189  233  ALA B CA  
10364 C C   . ALA B 235  ? 0.3752 0.2687 0.2487 -0.0231 -0.0900 0.0225  233  ALA B C   
10365 O O   . ALA B 235  ? 0.3811 0.2723 0.2471 -0.0293 -0.0908 0.0278  233  ALA B O   
10366 C CB  . ALA B 235  ? 0.4043 0.2997 0.2909 -0.0198 -0.0875 0.0168  233  ALA B CB  
10367 N N   . GLU B 236  ? 0.3712 0.2594 0.2446 -0.0179 -0.0936 0.0199  234  GLU B N   
10368 C CA  . GLU B 236  ? 0.3674 0.2464 0.2315 -0.0191 -0.0988 0.0233  234  GLU B CA  
10369 C C   . GLU B 236  ? 0.4136 0.2997 0.2720 -0.0227 -0.0960 0.0266  234  GLU B C   
10370 O O   . GLU B 236  ? 0.4172 0.2978 0.2662 -0.0274 -0.0986 0.0318  234  GLU B O   
10371 C CB  . GLU B 236  ? 0.3974 0.2712 0.2639 -0.0122 -0.1029 0.0194  234  GLU B CB  
10372 C CG  . GLU B 236  ? 0.4765 0.3391 0.3339 -0.0125 -0.1093 0.0225  234  GLU B CG  
10373 C CD  . GLU B 236  ? 0.5640 0.4226 0.4247 -0.0053 -0.1134 0.0184  234  GLU B CD  
10374 O OE1 . GLU B 236  ? 0.6039 0.4673 0.4741 -0.0004 -0.1117 0.0134  234  GLU B OE1 
10375 O OE2 . GLU B 236  ? 0.6004 0.4512 0.4541 -0.0048 -0.1184 0.0205  234  GLU B OE2 
10376 N N   . ARG B 237  ? 0.3666 0.2648 0.2302 -0.0205 -0.0907 0.0237  235  ARG B N   
10377 C CA  . ARG B 237  ? 0.3761 0.2820 0.2343 -0.0233 -0.0875 0.0264  235  ARG B CA  
10378 C C   . ARG B 237  ? 0.3800 0.2902 0.2346 -0.0304 -0.0846 0.0314  235  ARG B C   
10379 O O   . ARG B 237  ? 0.3907 0.3005 0.2366 -0.0349 -0.0852 0.0363  235  ARG B O   
10380 C CB  . ARG B 237  ? 0.4089 0.3261 0.2735 -0.0191 -0.0826 0.0218  235  ARG B CB  
10381 C CG  . ARG B 237  ? 0.4575 0.3823 0.3162 -0.0211 -0.0794 0.0238  235  ARG B CG  
10382 C CD  . ARG B 237  ? 0.5648 0.5023 0.4296 -0.0191 -0.0730 0.0206  235  ARG B CD  
10383 N NE  . ARG B 237  ? 0.6671 0.6113 0.5252 -0.0203 -0.0702 0.0223  235  ARG B NE  
10384 C CZ  . ARG B 237  ? 0.6185 0.5673 0.4770 -0.0162 -0.0686 0.0187  235  ARG B CZ  
10385 N NH1 . ARG B 237  ? 0.6272 0.5756 0.4930 -0.0110 -0.0690 0.0133  235  ARG B NH1 
10386 N NH2 . ARG B 237  ? 0.5854 0.5396 0.4365 -0.0174 -0.0664 0.0205  235  ARG B NH2 
10387 N N   . TYR B 238  ? 0.3608 0.2756 0.2219 -0.0316 -0.0815 0.0305  236  TYR B N   
10388 C CA  . TYR B 238  ? 0.3693 0.2889 0.2276 -0.0385 -0.0789 0.0354  236  TYR B CA  
10389 C C   . TYR B 238  ? 0.3706 0.2783 0.2201 -0.0441 -0.0844 0.0410  236  TYR B C   
10390 O O   . TYR B 238  ? 0.3744 0.2850 0.2175 -0.0505 -0.0834 0.0465  236  TYR B O   
10391 C CB  . TYR B 238  ? 0.3448 0.2698 0.2116 -0.0387 -0.0756 0.0333  236  TYR B CB  
10392 C CG  . TYR B 238  ? 0.3854 0.3236 0.2602 -0.0347 -0.0695 0.0291  236  TYR B CG  
10393 C CD1 . TYR B 238  ? 0.4988 0.4465 0.3713 -0.0342 -0.0657 0.0294  236  TYR B CD1 
10394 C CD2 . TYR B 238  ? 0.3911 0.3315 0.2749 -0.0313 -0.0678 0.0247  236  TYR B CD2 
10395 C CE1 . TYR B 238  ? 0.5092 0.4677 0.3884 -0.0303 -0.0605 0.0254  236  TYR B CE1 
10396 C CE2 . TYR B 238  ? 0.4427 0.3940 0.3332 -0.0277 -0.0626 0.0211  236  TYR B CE2 
10397 C CZ  . TYR B 238  ? 0.5248 0.4848 0.4130 -0.0272 -0.0591 0.0214  236  TYR B CZ  
10398 O OH  . TYR B 238  ? 0.5580 0.5278 0.4524 -0.0234 -0.0543 0.0176  236  TYR B OH  
10399 N N   . TYR B 239  ? 0.3725 0.2667 0.2213 -0.0418 -0.0902 0.0397  237  TYR B N   
10400 C CA  . TYR B 239  ? 0.3881 0.2693 0.2277 -0.0466 -0.0961 0.0448  237  TYR B CA  
10401 C C   . TYR B 239  ? 0.4194 0.2993 0.2496 -0.0487 -0.0977 0.0488  237  TYR B C   
10402 O O   . TYR B 239  ? 0.4206 0.2983 0.2427 -0.0557 -0.0988 0.0550  237  TYR B O   
10403 C CB  . TYR B 239  ? 0.3935 0.2604 0.2339 -0.0422 -0.1022 0.0420  237  TYR B CB  
10404 C CG  . TYR B 239  ? 0.4334 0.2849 0.2635 -0.0462 -0.1091 0.0469  237  TYR B CG  
10405 C CD1 . TYR B 239  ? 0.4486 0.2931 0.2754 -0.0522 -0.1113 0.0505  237  TYR B CD1 
10406 C CD2 . TYR B 239  ? 0.4198 0.2633 0.2431 -0.0441 -0.1137 0.0481  237  TYR B CD2 
10407 C CE1 . TYR B 239  ? 0.4707 0.3001 0.2874 -0.0561 -0.1180 0.0552  237  TYR B CE1 
10408 C CE2 . TYR B 239  ? 0.5196 0.3483 0.3330 -0.0478 -0.1203 0.0528  237  TYR B CE2 
10409 C CZ  . TYR B 239  ? 0.4758 0.2972 0.2859 -0.0538 -0.1225 0.0564  237  TYR B CZ  
10410 O OH  . TYR B 239  ? 0.5793 0.3848 0.3790 -0.0576 -0.1294 0.0612  237  TYR B OH  
10411 N N   . ARG B 240  ? 0.4120 0.2932 0.2429 -0.0429 -0.0980 0.0454  238  ARG B N   
10412 C CA  . ARG B 240  ? 0.4350 0.3143 0.2565 -0.0445 -0.0998 0.0489  238  ARG B CA  
10413 C C   . ARG B 240  ? 0.4112 0.3035 0.2294 -0.0495 -0.0942 0.0526  238  ARG B C   
10414 O O   . ARG B 240  ? 0.4306 0.3206 0.2391 -0.0543 -0.0958 0.0581  238  ARG B O   
10415 C CB  . ARG B 240  ? 0.4422 0.3210 0.2655 -0.0372 -0.1014 0.0442  238  ARG B CB  
10416 C CG  . ARG B 240  ? 0.4587 0.3247 0.2841 -0.0322 -0.1076 0.0413  238  ARG B CG  
10417 C CD  . ARG B 240  ? 0.4347 0.2858 0.2500 -0.0358 -0.1145 0.0464  238  ARG B CD  
10418 N NE  . ARG B 240  ? 0.5515 0.3908 0.3692 -0.0303 -0.1203 0.0433  238  ARG B NE  
10419 C CZ  . ARG B 240  ? 0.6338 0.4581 0.4443 -0.0316 -0.1271 0.0464  238  ARG B CZ  
10420 N NH1 . ARG B 240  ? 0.5520 0.3704 0.3521 -0.0386 -0.1293 0.0531  238  ARG B NH1 
10421 N NH2 . ARG B 240  ? 0.6548 0.4698 0.4684 -0.0255 -0.1320 0.0427  238  ARG B NH2 
10422 N N   . ASP B 241  ? 0.4085 0.3143 0.2344 -0.0483 -0.0876 0.0497  239  ASP B N   
10423 C CA  . ASP B 241  ? 0.4173 0.3365 0.2409 -0.0527 -0.0819 0.0530  239  ASP B CA  
10424 C C   . ASP B 241  ? 0.4037 0.3217 0.2226 -0.0614 -0.0825 0.0598  239  ASP B C   
10425 O O   . ASP B 241  ? 0.4076 0.3302 0.2191 -0.0667 -0.0812 0.0652  239  ASP B O   
10426 C CB  . ASP B 241  ? 0.4150 0.3480 0.2484 -0.0491 -0.0752 0.0483  239  ASP B CB  
10427 C CG  . ASP B 241  ? 0.5136 0.4499 0.3505 -0.0416 -0.0738 0.0423  239  ASP B CG  
10428 O OD1 . ASP B 241  ? 0.5571 0.4882 0.3881 -0.0395 -0.0769 0.0421  239  ASP B OD1 
10429 O OD2 . ASP B 241  ? 0.5497 0.4939 0.3952 -0.0378 -0.0697 0.0377  239  ASP B OD2 
10430 N N   . TYR B 242  ? 0.4136 0.3259 0.2369 -0.0631 -0.0844 0.0596  240  TYR B N   
10431 C CA  . TYR B 242  ? 0.4078 0.3172 0.2265 -0.0717 -0.0859 0.0661  240  TYR B CA  
10432 C C   . TYR B 242  ? 0.4246 0.3215 0.2315 -0.0761 -0.0919 0.0717  240  TYR B C   
10433 O O   . TYR B 242  ? 0.4337 0.3336 0.2338 -0.0837 -0.0914 0.0783  240  TYR B O   
10434 C CB  . TYR B 242  ? 0.4040 0.3066 0.2284 -0.0720 -0.0880 0.0643  240  TYR B CB  
10435 C CG  . TYR B 242  ? 0.3888 0.3042 0.2237 -0.0703 -0.0821 0.0606  240  TYR B CG  
10436 C CD1 . TYR B 242  ? 0.4029 0.3352 0.2403 -0.0720 -0.0755 0.0617  240  TYR B CD1 
10437 C CD2 . TYR B 242  ? 0.4103 0.3206 0.2522 -0.0668 -0.0834 0.0562  240  TYR B CD2 
10438 C CE1 . TYR B 242  ? 0.4097 0.3533 0.2566 -0.0702 -0.0703 0.0585  240  TYR B CE1 
10439 C CE2 . TYR B 242  ? 0.4379 0.3592 0.2890 -0.0653 -0.0783 0.0531  240  TYR B CE2 
10440 C CZ  . TYR B 242  ? 0.3941 0.3318 0.2478 -0.0670 -0.0719 0.0543  240  TYR B CZ  
10441 O OH  . TYR B 242  ? 0.3851 0.3331 0.2478 -0.0653 -0.0673 0.0512  240  TYR B OH  
10442 N N   . GLU B 243  ? 0.4340 0.3171 0.2385 -0.0713 -0.0977 0.0693  241  GLU B N   
10443 C CA  . GLU B 243  ? 0.4471 0.3163 0.2404 -0.0746 -0.1043 0.0743  241  GLU B CA  
10444 C C   . GLU B 243  ? 0.4613 0.3373 0.2465 -0.0772 -0.1023 0.0783  241  GLU B C   
10445 O O   . GLU B 243  ? 0.4671 0.3392 0.2429 -0.0845 -0.1046 0.0853  241  GLU B O   
10446 C CB  . GLU B 243  ? 0.4580 0.3133 0.2517 -0.0674 -0.1103 0.0699  241  GLU B CB  
10447 C CG  . GLU B 243  ? 0.5139 0.3542 0.2963 -0.0693 -0.1175 0.0743  241  GLU B CG  
10448 C CD  . GLU B 243  ? 0.5642 0.3940 0.3484 -0.0608 -0.1226 0.0692  241  GLU B CD  
10449 O OE1 . GLU B 243  ? 0.5133 0.3513 0.3043 -0.0541 -0.1195 0.0635  241  GLU B OE1 
10450 O OE2 . GLU B 243  ? 0.6067 0.4202 0.3855 -0.0608 -0.1297 0.0708  241  GLU B OE2 
10451 N N   . SER B 244  ? 0.4443 0.3301 0.2328 -0.0712 -0.0984 0.0739  242  SER B N   
10452 C CA  A SER B 244  ? 0.4554 0.3489 0.2364 -0.0731 -0.0959 0.0770  242  SER B CA  
10453 C CA  B SER B 244  ? 0.4554 0.3489 0.2364 -0.0731 -0.0959 0.0770  242  SER B CA  
10454 C CA  C SER B 244  ? 0.4554 0.3489 0.2364 -0.0731 -0.0959 0.0770  242  SER B CA  
10455 C C   . SER B 244  ? 0.4506 0.3571 0.2297 -0.0806 -0.0905 0.0823  242  SER B C   
10456 O O   . SER B 244  ? 0.4622 0.3700 0.2317 -0.0863 -0.0909 0.0885  242  SER B O   
10457 C CB  A SER B 244  ? 0.4584 0.3605 0.2442 -0.0651 -0.0923 0.0705  242  SER B CB  
10458 C CB  B SER B 244  ? 0.4520 0.3540 0.2376 -0.0651 -0.0924 0.0705  242  SER B CB  
10459 C CB  C SER B 244  ? 0.4519 0.3541 0.2376 -0.0651 -0.0923 0.0705  242  SER B CB  
10460 O OG  A SER B 244  ? 0.4594 0.3713 0.2386 -0.0666 -0.0887 0.0729  242  SER B OG  
10461 O OG  B SER B 244  ? 0.4656 0.3567 0.2539 -0.0584 -0.0973 0.0657  242  SER B OG  
10462 O OG  C SER B 244  ? 0.4589 0.3734 0.2551 -0.0626 -0.0861 0.0661  242  SER B OG  
10463 N N   . ALA B 245  ? 0.4386 0.3554 0.2269 -0.0809 -0.0856 0.0803  243  ALA B N   
10464 C CA  . ALA B 245  ? 0.4633 0.3940 0.2510 -0.0878 -0.0803 0.0852  243  ALA B CA  
10465 C C   . ALA B 245  ? 0.4529 0.3758 0.2334 -0.0976 -0.0844 0.0932  243  ALA B C   
10466 O O   . ALA B 245  ? 0.4605 0.3913 0.2347 -0.1043 -0.0822 0.0995  243  ALA B O   
10467 C CB  . ALA B 245  ? 0.4628 0.4051 0.2623 -0.0857 -0.0749 0.0811  243  ALA B CB  
10468 N N   . ILE B 246  ? 0.4572 0.3646 0.2382 -0.0985 -0.0904 0.0931  244  ILE B N   
10469 C CA  . ILE B 246  ? 0.4722 0.3699 0.2457 -0.1079 -0.0952 0.1006  244  ILE B CA  
10470 C C   . ILE B 246  ? 0.4884 0.3797 0.2493 -0.1117 -0.0987 0.1065  244  ILE B C   
10471 O O   . ILE B 246  ? 0.5102 0.4040 0.2641 -0.1208 -0.0988 0.1142  244  ILE B O   
10472 C CB  . ILE B 246  ? 0.4750 0.3552 0.2506 -0.1068 -0.1017 0.0985  244  ILE B CB  
10473 C CG1 . ILE B 246  ? 0.4608 0.3485 0.2479 -0.1052 -0.0980 0.0942  244  ILE B CG1 
10474 C CG2 . ILE B 246  ? 0.4937 0.3603 0.2594 -0.1162 -0.1080 0.1063  244  ILE B CG2 
10475 C CD1 . ILE B 246  ? 0.4624 0.3339 0.2520 -0.1028 -0.1037 0.0910  244  ILE B CD1 
10476 N N   . HIS B 247  ? 0.5001 0.3833 0.2576 -0.1051 -0.1018 0.1032  245  HIS B N   
10477 C CA  . HIS B 247  ? 0.5063 0.3836 0.2514 -0.1083 -0.1052 0.1088  245  HIS B CA  
10478 C C   . HIS B 247  ? 0.5065 0.4018 0.2480 -0.1126 -0.0986 0.1128  245  HIS B C   
10479 O O   . HIS B 247  ? 0.5204 0.4149 0.2524 -0.1207 -0.0999 0.1207  245  HIS B O   
10480 C CB  . HIS B 247  ? 0.5265 0.3944 0.2696 -0.0998 -0.1091 0.1040  245  HIS B CB  
10481 C CG  . HIS B 247  ? 0.5291 0.3771 0.2718 -0.0970 -0.1171 0.1022  245  HIS B CG  
10482 N ND1 . HIS B 247  ? 0.5339 0.3658 0.2670 -0.1030 -0.1242 0.1084  245  HIS B ND1 
10483 C CD2 . HIS B 247  ? 0.5365 0.3783 0.2872 -0.0888 -0.1192 0.0950  245  HIS B CD2 
10484 C CE1 . HIS B 247  ? 0.5892 0.4055 0.3243 -0.0980 -0.1303 0.1048  245  HIS B CE1 
10485 N NE2 . HIS B 247  ? 0.5841 0.4066 0.3299 -0.0894 -0.1272 0.0967  245  HIS B NE2 
10486 N N   . ALA B 248  ? 0.4918 0.4033 0.2407 -0.1070 -0.0914 0.1076  246  ALA B N   
10487 C CA  . ALA B 248  ? 0.4916 0.4210 0.2374 -0.1098 -0.0848 0.1105  246  ALA B CA  
10488 C C   . ALA B 248  ? 0.4942 0.4335 0.2403 -0.1193 -0.0816 0.1171  246  ALA B C   
10489 O O   . ALA B 248  ? 0.5049 0.4504 0.2428 -0.1263 -0.0803 0.1241  246  ALA B O   
10490 C CB  . ALA B 248  ? 0.4753 0.4187 0.2295 -0.1012 -0.0782 0.1029  246  ALA B CB  
10491 N N   . ILE B 249  ? 0.4842 0.4263 0.2402 -0.1198 -0.0802 0.1149  247  ILE B N   
10492 C CA  . ILE B 249  ? 0.5060 0.4580 0.2634 -0.1289 -0.0774 0.1209  247  ILE B CA  
10493 C C   . ILE B 249  ? 0.5061 0.4447 0.2535 -0.1388 -0.0840 0.1294  247  ILE B C   
10494 O O   . ILE B 249  ? 0.5134 0.4606 0.2553 -0.1475 -0.0821 0.1370  247  ILE B O   
10495 C CB  . ILE B 249  ? 0.4722 0.4277 0.2419 -0.1270 -0.0756 0.1164  247  ILE B CB  
10496 C CG1 . ILE B 249  ? 0.4549 0.4238 0.2338 -0.1175 -0.0691 0.1085  247  ILE B CG1 
10497 C CG2 . ILE B 249  ? 0.4746 0.4399 0.2460 -0.1369 -0.0734 0.1228  247  ILE B CG2 
10498 C CD1 . ILE B 249  ? 0.4416 0.4076 0.2317 -0.1125 -0.0691 0.1021  247  ILE B CD1 
10499 N N   . GLY B 250  ? 0.5306 0.4479 0.2753 -0.1373 -0.0918 0.1282  248  GLY B N   
10500 C CA  . GLY B 250  ? 0.5304 0.4322 0.2648 -0.1461 -0.0990 0.1359  248  GLY B CA  
10501 C C   . GLY B 250  ? 0.5710 0.4745 0.2932 -0.1509 -0.0993 0.1427  248  GLY B C   
10502 O O   . GLY B 250  ? 0.5899 0.4942 0.3059 -0.1612 -0.1003 0.1509  248  GLY B O   
10503 N N   . LYS B 251  ? 0.5602 0.4646 0.2793 -0.1436 -0.0984 0.1391  249  LYS B N   
10504 C CA  . LYS B 251  ? 0.5566 0.4633 0.2637 -0.1478 -0.0985 0.1453  249  LYS B CA  
10505 C C   . LYS B 251  ? 0.5535 0.4836 0.2625 -0.1529 -0.0900 0.1489  249  LYS B C   
10506 O O   . LYS B 251  ? 0.5652 0.4990 0.2705 -0.1598 -0.0893 0.1546  249  LYS B O   
10507 C CB  . LYS B 251  ? 0.5550 0.4582 0.2590 -0.1383 -0.0993 0.1400  249  LYS B CB  
10508 N N   . ALA B 252  ? 0.5368 0.4840 0.2551 -0.1484 -0.0829 0.1441  250  ALA B N   
10509 C CA  . ALA B 252  ? 0.5498 0.5202 0.2695 -0.1528 -0.0748 0.1477  250  ALA B CA  
10510 C C   . ALA B 252  ? 0.5937 0.5683 0.3180 -0.1628 -0.0745 0.1533  250  ALA B C   
10511 O O   . ALA B 252  ? 0.5887 0.5780 0.3135 -0.1684 -0.0699 0.1577  250  ALA B O   
10512 C CB  . ALA B 252  ? 0.5375 0.5240 0.2690 -0.1440 -0.0674 0.1395  250  ALA B CB  
10513 N N   . SER B 253  ? 0.5803 0.5425 0.3082 -0.1650 -0.0794 0.1530  251  SER B N   
10514 C CA  . SER B 253  ? 0.5476 0.5116 0.2794 -0.1747 -0.0803 0.1581  251  SER B CA  
10515 C C   . SER B 253  ? 0.6088 0.5675 0.3338 -0.1826 -0.0834 0.1645  251  SER B C   
10516 O O   . SER B 253  ? 0.6311 0.6018 0.3589 -0.1907 -0.0807 0.1693  251  SER B O   
10517 C CB  . SER B 253  ? 0.5682 0.5148 0.3025 -0.1751 -0.0866 0.1563  251  SER B CB  
10518 O OG  . SER B 253  ? 0.6011 0.5488 0.3389 -0.1847 -0.0879 0.1609  251  SER B OG  
10519 N N   . ALA B 254  ? 0.6106 0.5518 0.3269 -0.1802 -0.0892 0.1644  252  ALA B N   
10520 C CA  . ALA B 254  ? 0.6173 0.5526 0.3259 -0.1866 -0.0923 0.1702  252  ALA B CA  
10521 C C   . ALA B 254  ? 0.6685 0.5988 0.3784 -0.1974 -0.0961 0.1756  252  ALA B C   
10522 O O   . ALA B 254  ? 0.6376 0.5749 0.3451 -0.2051 -0.0951 0.1813  252  ALA B O   
10523 C CB  . ALA B 254  ? 0.6181 0.5732 0.3247 -0.1868 -0.0851 0.1722  252  ALA B CB  
10524 N N   . GLY B 255  ? 0.6449 0.5629 0.3584 -0.1978 -0.1007 0.1737  253  GLY B N   
10525 C CA  . GLY B 255  ? 0.6624 0.5721 0.3761 -0.2075 -0.1057 0.1780  253  GLY B CA  
10526 C C   . GLY B 255  ? 0.6870 0.6163 0.4089 -0.2147 -0.1006 0.1809  253  GLY B C   
10527 O O   . GLY B 255  ? 0.7295 0.6554 0.4510 -0.2241 -0.1042 0.1856  253  GLY B O   
10528 N N   . ARG B 256  ? 0.6339 0.5840 0.3636 -0.2105 -0.0925 0.1782  254  ARG B N   
10529 C CA  . ARG B 256  ? 0.6549 0.6249 0.3932 -0.2167 -0.0874 0.1806  254  ARG B CA  
10530 C C   . ARG B 256  ? 0.6718 0.6337 0.4156 -0.2197 -0.0914 0.1795  254  ARG B C   
10531 O O   . ARG B 256  ? 0.6344 0.6102 0.3851 -0.2261 -0.0888 0.1820  254  ARG B O   
10532 C CB  . ARG B 256  ? 0.6213 0.6159 0.3661 -0.2105 -0.0776 0.1776  254  ARG B CB  
10533 C CG  . ARG B 256  ? 0.6653 0.6757 0.4069 -0.2110 -0.0722 0.1804  254  ARG B CG  
10534 C CD  . ARG B 256  ? 0.6502 0.6826 0.3974 -0.2033 -0.0629 0.1763  254  ARG B CD  
10535 N NE  . ARG B 256  ? 0.6669 0.6905 0.4104 -0.1928 -0.0632 0.1703  254  ARG B NE  
10536 C CZ  . ARG B 256  ? 0.6333 0.6694 0.3814 -0.1845 -0.0572 0.1649  254  ARG B CZ  
10537 N NH1 . ARG B 256  ? 0.5720 0.6303 0.3291 -0.1846 -0.0500 0.1644  254  ARG B NH1 
10538 N NH2 . ARG B 256  ? 0.6582 0.6843 0.4021 -0.1757 -0.0586 0.1597  254  ARG B NH2 
10539 N N   . GLY B 257  ? 0.6532 0.5932 0.3940 -0.2152 -0.0976 0.1758  255  GLY B N   
10540 C CA  . GLY B 257  ? 0.5855 0.5157 0.3304 -0.2176 -0.1019 0.1744  255  GLY B CA  
10541 C C   . GLY B 257  ? 0.5938 0.5359 0.3475 -0.2118 -0.0965 0.1697  255  GLY B C   
10542 O O   . GLY B 257  ? 0.5959 0.5552 0.3532 -0.2060 -0.0891 0.1674  255  GLY B O   
10543 N N   . ILE B 258  ? 0.5757 0.5087 0.3330 -0.2135 -0.1003 0.1682  256  ILE B N   
10544 C CA  . ILE B 258  ? 0.6044 0.5442 0.3692 -0.2073 -0.0965 0.1633  256  ILE B CA  
10545 C C   . ILE B 258  ? 0.5694 0.5362 0.3441 -0.2103 -0.0885 0.1645  256  ILE B C   
10546 O O   . ILE B 258  ? 0.5074 0.4841 0.2886 -0.2041 -0.0837 0.1602  256  ILE B O   
10547 C CB  . ILE B 258  ? 0.5871 0.5066 0.3517 -0.2075 -0.1035 0.1609  256  ILE B CB  
10548 C CG1 . ILE B 258  ? 0.6231 0.5401 0.3886 -0.2184 -0.1075 0.1653  256  ILE B CG1 
10549 C CG2 . ILE B 258  ? 0.5983 0.4921 0.3543 -0.2018 -0.1108 0.1582  256  ILE B CG2 
10550 C CD1 . ILE B 258  ? 0.6468 0.5432 0.4114 -0.2187 -0.1148 0.1628  256  ILE B CD1 
10551 N N   . TYR B 259  ? 0.5816 0.5610 0.3581 -0.2191 -0.0870 0.1698  257  TYR B N   
10552 C CA  . TYR B 259  ? 0.6114 0.6169 0.3980 -0.2217 -0.0798 0.1709  257  TYR B CA  
10553 C C   . TYR B 259  ? 0.5610 0.5890 0.3493 -0.2189 -0.0716 0.1716  257  TYR B C   
10554 O O   . TYR B 259  ? 0.6448 0.6924 0.4409 -0.2143 -0.0644 0.1690  257  TYR B O   
10555 C CB  . TYR B 259  ? 0.5686 0.5763 0.3576 -0.2331 -0.0833 0.1759  257  TYR B CB  
10556 C CG  . TYR B 259  ? 0.6073 0.5922 0.3940 -0.2361 -0.0918 0.1749  257  TYR B CG  
10557 C CD1 . TYR B 259  ? 0.5751 0.5573 0.3673 -0.2319 -0.0916 0.1705  257  TYR B CD1 
10558 C CD2 . TYR B 259  ? 0.6420 0.6075 0.4205 -0.2426 -0.1001 0.1782  257  TYR B CD2 
10559 C CE1 . TYR B 259  ? 0.6071 0.5678 0.3966 -0.2339 -0.0993 0.1692  257  TYR B CE1 
10560 C CE2 . TYR B 259  ? 0.6083 0.5523 0.3841 -0.2445 -0.1080 0.1767  257  TYR B CE2 
10561 C CZ  . TYR B 259  ? 0.6233 0.5650 0.4047 -0.2400 -0.1075 0.1721  257  TYR B CZ  
10562 O OH  . TYR B 259  ? 0.6371 0.5570 0.4153 -0.2414 -0.1154 0.1703  257  TYR B OH  
10563 N N   . GLU B 260  ? 0.5752 0.6007 0.3562 -0.2211 -0.0726 0.1750  258  GLU B N   
10564 C CA  . GLU B 260  ? 0.5939 0.6392 0.3753 -0.2177 -0.0651 0.1753  258  GLU B CA  
10565 C C   . GLU B 260  ? 0.6450 0.6850 0.4216 -0.2070 -0.0632 0.1703  258  GLU B C   
10566 O O   . GLU B 260  ? 0.6494 0.7074 0.4288 -0.2011 -0.0557 0.1680  258  GLU B O   
10567 C CB  . GLU B 260  ? 0.6167 0.6634 0.3923 -0.2255 -0.0667 0.1815  258  GLU B CB  
10568 N N   . GLY B 261  ? 0.5964 0.6121 0.3659 -0.2040 -0.0700 0.1683  259  GLY B N   
10569 C CA  . GLY B 261  ? 0.6056 0.6150 0.3699 -0.1943 -0.0693 0.1637  259  GLY B CA  
10570 C C   . GLY B 261  ? 0.5726 0.5825 0.3419 -0.1859 -0.0674 0.1574  259  GLY B C   
10571 O O   . GLY B 261  ? 0.5239 0.5345 0.3011 -0.1869 -0.0677 0.1556  259  GLY B O   
10572 N N   . PRO B 262  ? 0.5188 0.5284 0.2878 -0.1753 -0.0651 0.1510  260  PRO B N   
10573 C CA  . PRO B 262  ? 0.4897 0.5012 0.2692 -0.1642 -0.0623 0.1411  260  PRO B CA  
10574 C C   . PRO B 262  ? 0.4861 0.4755 0.2674 -0.1611 -0.0694 0.1367  260  PRO B C   
10575 O O   . PRO B 262  ? 0.5341 0.5042 0.3072 -0.1649 -0.0768 0.1399  260  PRO B O   
10576 C CB  . PRO B 262  ? 0.5003 0.5157 0.2769 -0.1551 -0.0590 0.1366  260  PRO B CB  
10577 C CG  . PRO B 262  ? 0.4959 0.4992 0.2593 -0.1600 -0.0640 0.1425  260  PRO B CG  
10578 C CD  . PRO B 262  ? 0.5276 0.5345 0.2865 -0.1732 -0.0654 0.1524  260  PRO B CD  
10579 N N   . GLY B 263  ? 0.4605 0.4532 0.2525 -0.1538 -0.0669 0.1292  261  GLY B N   
10580 C CA  . GLY B 263  ? 0.4577 0.4318 0.2525 -0.1486 -0.0724 0.1235  261  GLY B CA  
10581 C C   . GLY B 263  ? 0.4420 0.4185 0.2446 -0.1364 -0.0692 0.1140  261  GLY B C   
10582 O O   . GLY B 263  ? 0.4395 0.4303 0.2443 -0.1313 -0.0632 0.1115  261  GLY B O   
10583 N N   . ILE B 264  ? 0.4387 0.4011 0.2453 -0.1315 -0.0733 0.1086  262  ILE B N   
10584 C CA  . ILE B 264  ? 0.4234 0.3870 0.2377 -0.1205 -0.0709 0.0997  262  ILE B CA  
10585 C C   . ILE B 264  ? 0.4233 0.3870 0.2472 -0.1191 -0.0705 0.0959  262  ILE B C   
10586 O O   . ILE B 264  ? 0.4202 0.3751 0.2428 -0.1252 -0.0748 0.0989  262  ILE B O   
10587 C CB  . ILE B 264  ? 0.4924 0.4382 0.3018 -0.1143 -0.0763 0.0962  262  ILE B CB  
10588 C CG1 . ILE B 264  ? 0.4564 0.4063 0.2732 -0.1033 -0.0731 0.0877  262  ILE B CG1 
10589 C CG2 . ILE B 264  ? 0.4418 0.3676 0.2489 -0.1165 -0.0840 0.0966  262  ILE B CG2 
10590 C CD1 . ILE B 264  ? 0.4475 0.3841 0.2592 -0.0975 -0.0775 0.0848  262  ILE B CD1 
10591 N N   . SER B 265  ? 0.4157 0.3894 0.2486 -0.1112 -0.0655 0.0893  263  SER B N   
10592 C CA  . SER B 265  ? 0.3926 0.3660 0.2348 -0.1081 -0.0650 0.0846  263  SER B CA  
10593 C C   . SER B 265  ? 0.4231 0.3874 0.2687 -0.0981 -0.0664 0.0768  263  SER B C   
10594 O O   . SER B 265  ? 0.4382 0.4056 0.2833 -0.0922 -0.0642 0.0738  263  SER B O   
10595 C CB  . SER B 265  ? 0.4419 0.4359 0.2926 -0.1078 -0.0578 0.0838  263  SER B CB  
10596 O OG  . SER B 265  ? 0.4430 0.4455 0.2922 -0.1173 -0.0569 0.0907  263  SER B OG  
10597 N N   . ILE B 266  ? 0.3781 0.3312 0.2272 -0.0964 -0.0701 0.0737  264  ILE B N   
10598 C CA  . ILE B 266  ? 0.4061 0.3514 0.2592 -0.0873 -0.0714 0.0665  264  ILE B CA  
10599 C C   . ILE B 266  ? 0.3937 0.3422 0.2562 -0.0845 -0.0695 0.0620  264  ILE B C   
10600 O O   . ILE B 266  ? 0.4153 0.3667 0.2797 -0.0901 -0.0694 0.0646  264  ILE B O   
10601 C CB  . ILE B 266  ? 0.3995 0.3245 0.2460 -0.0864 -0.0790 0.0664  264  ILE B CB  
10602 C CG1 . ILE B 266  ? 0.4609 0.3746 0.3057 -0.0917 -0.0839 0.0685  264  ILE B CG1 
10603 C CG2 . ILE B 266  ? 0.3950 0.3158 0.2315 -0.0894 -0.0814 0.0711  264  ILE B CG2 
10604 C CD1 . ILE B 266  ? 0.5409 0.4340 0.3797 -0.0897 -0.0915 0.0677  264  ILE B CD1 
10605 N N   . LYS B 267  ? 0.3704 0.3181 0.2387 -0.0760 -0.0684 0.0553  265  LYS B N   
10606 C CA  . LYS B 267  ? 0.3639 0.3126 0.2407 -0.0722 -0.0672 0.0505  265  LYS B CA  
10607 C C   . LYS B 267  ? 0.3537 0.2862 0.2297 -0.0675 -0.0726 0.0466  265  LYS B C   
10608 O O   . LYS B 267  ? 0.3571 0.2844 0.2313 -0.0624 -0.0741 0.0441  265  LYS B O   
10609 C CB  . LYS B 267  ? 0.3687 0.3314 0.2535 -0.0661 -0.0609 0.0460  265  LYS B CB  
10610 C CG  . LYS B 267  ? 0.4116 0.3913 0.2979 -0.0698 -0.0552 0.0493  265  LYS B CG  
10611 C CD  . LYS B 267  ? 0.4815 0.4738 0.3766 -0.0638 -0.0494 0.0445  265  LYS B CD  
10612 C CE  . LYS B 267  ? 0.5404 0.5498 0.4374 -0.0673 -0.0441 0.0478  265  LYS B CE  
10613 N NZ  . LYS B 267  ? 0.5404 0.5528 0.4294 -0.0721 -0.0440 0.0532  265  LYS B NZ  
10614 N N   . LEU B 268  ? 0.3458 0.2708 0.2232 -0.0691 -0.0755 0.0459  266  LEU B N   
10615 C CA  . LEU B 268  ? 0.3719 0.2822 0.2488 -0.0641 -0.0804 0.0419  266  LEU B CA  
10616 C C   . LEU B 268  ? 0.3610 0.2755 0.2454 -0.0550 -0.0777 0.0352  266  LEU B C   
10617 O O   . LEU B 268  ? 0.3652 0.2702 0.2485 -0.0498 -0.0811 0.0322  266  LEU B O   
10618 C CB  . LEU B 268  ? 0.3515 0.2542 0.2285 -0.0672 -0.0835 0.0420  266  LEU B CB  
10619 C CG  . LEU B 268  ? 0.3666 0.2615 0.2349 -0.0764 -0.0878 0.0487  266  LEU B CG  
10620 C CD1 . LEU B 268  ? 0.3794 0.2644 0.2468 -0.0792 -0.0918 0.0485  266  LEU B CD1 
10621 C CD2 . LEU B 268  ? 0.3859 0.2686 0.2452 -0.0768 -0.0928 0.0513  266  LEU B CD2 
10622 N N   . SER B 269  ? 0.3220 0.2507 0.2140 -0.0530 -0.0716 0.0330  267  SER B N   
10623 C CA  . SER B 269  ? 0.3107 0.2433 0.2098 -0.0451 -0.0691 0.0270  267  SER B CA  
10624 C C   . SER B 269  ? 0.3192 0.2520 0.2160 -0.0413 -0.0691 0.0260  267  SER B C   
10625 O O   . SER B 269  ? 0.3336 0.2662 0.2349 -0.0348 -0.0687 0.0212  267  SER B O   
10626 C CB  . SER B 269  ? 0.3575 0.3047 0.2645 -0.0442 -0.0629 0.0252  267  SER B CB  
10627 O OG  . SER B 269  ? 0.3190 0.2779 0.2250 -0.0466 -0.0588 0.0281  267  SER B OG  
10628 N N   . ALA B 270  ? 0.3194 0.2528 0.2093 -0.0455 -0.0697 0.0306  268  ALA B N   
10629 C CA  . ALA B 270  ? 0.3280 0.2606 0.2144 -0.0423 -0.0702 0.0300  268  ALA B CA  
10630 C C   . ALA B 270  ? 0.3540 0.2717 0.2359 -0.0399 -0.0766 0.0292  268  ALA B C   
10631 O O   . ALA B 270  ? 0.3481 0.2647 0.2295 -0.0354 -0.0775 0.0270  268  ALA B O   
10632 C CB  . ALA B 270  ? 0.3566 0.2953 0.2364 -0.0477 -0.0686 0.0354  268  ALA B CB  
10633 N N   . LEU B 271  ? 0.3505 0.2567 0.2292 -0.0425 -0.0813 0.0308  269  LEU B N   
10634 C CA  . LEU B 271  ? 0.3567 0.2478 0.2295 -0.0409 -0.0880 0.0311  269  LEU B CA  
10635 C C   . LEU B 271  ? 0.3939 0.2783 0.2720 -0.0342 -0.0904 0.0255  269  LEU B C   
10636 O O   . LEU B 271  ? 0.4009 0.2732 0.2749 -0.0316 -0.0959 0.0250  269  LEU B O   
10637 C CB  . LEU B 271  ? 0.3650 0.2458 0.2294 -0.0482 -0.0924 0.0367  269  LEU B CB  
10638 C CG  . LEU B 271  ? 0.3769 0.2640 0.2352 -0.0553 -0.0906 0.0429  269  LEU B CG  
10639 C CD1 . LEU B 271  ? 0.4471 0.3243 0.2974 -0.0633 -0.0951 0.0488  269  LEU B CD1 
10640 C CD2 . LEU B 271  ? 0.4043 0.2911 0.2581 -0.0527 -0.0914 0.0434  269  LEU B CD2 
10641 N N   . HIS B 272  ? 0.3348 0.2268 0.2216 -0.0313 -0.0864 0.0215  270  HIS B N   
10642 C CA  . HIS B 272  ? 0.3602 0.2477 0.2524 -0.0247 -0.0881 0.0161  270  HIS B CA  
10643 C C   . HIS B 272  ? 0.3586 0.2589 0.2605 -0.0213 -0.0822 0.0120  270  HIS B C   
10644 O O   . HIS B 272  ? 0.3647 0.2740 0.2691 -0.0248 -0.0779 0.0134  270  HIS B O   
10645 C CB  . HIS B 272  ? 0.3990 0.2755 0.2887 -0.0262 -0.0920 0.0163  270  HIS B CB  
10646 C CG  . HIS B 272  ? 0.4298 0.2986 0.3223 -0.0192 -0.0953 0.0115  270  HIS B CG  
10647 N ND1 . HIS B 272  ? 0.3930 0.2684 0.2943 -0.0141 -0.0921 0.0064  270  HIS B ND1 
10648 C CD2 . HIS B 272  ? 0.4299 0.2856 0.3175 -0.0162 -0.1014 0.0110  270  HIS B CD2 
10649 C CE1 . HIS B 272  ? 0.4556 0.3230 0.3576 -0.0083 -0.0959 0.0030  270  HIS B CE1 
10650 N NE2 . HIS B 272  ? 0.4985 0.3538 0.3923 -0.0092 -0.1016 0.0055  270  HIS B NE2 
10651 N N   . PRO B 273  ? 0.3355 0.2372 0.2433 -0.0145 -0.0819 0.0072  271  PRO B N   
10652 C CA  . PRO B 273  ? 0.3502 0.2634 0.2670 -0.0115 -0.0766 0.0035  271  PRO B CA  
10653 C C   . PRO B 273  ? 0.3682 0.2821 0.2899 -0.0111 -0.0753 0.0014  271  PRO B C   
10654 O O   . PRO B 273  ? 0.3472 0.2708 0.2757 -0.0097 -0.0707 -0.0008 271  PRO B O   
10655 C CB  . PRO B 273  ? 0.3872 0.3006 0.3080 -0.0050 -0.0776 -0.0005 271  PRO B CB  
10656 C CG  . PRO B 273  ? 0.4045 0.3053 0.3196 -0.0036 -0.0839 0.0001  271  PRO B CG  
10657 C CD  . PRO B 273  ? 0.3757 0.2701 0.2816 -0.0099 -0.0863 0.0056  271  PRO B CD  
10658 N N   . ARG B 274  ? 0.3557 0.2590 0.2735 -0.0122 -0.0795 0.0020  272  ARG B N   
10659 C CA  . ARG B 274  ? 0.3339 0.2367 0.2553 -0.0117 -0.0788 -0.0001 272  ARG B CA  
10660 C C   . ARG B 274  ? 0.3785 0.2751 0.2936 -0.0183 -0.0809 0.0039  272  ARG B C   
10661 O O   . ARG B 274  ? 0.3948 0.2812 0.3069 -0.0183 -0.0848 0.0033  272  ARG B O   
10662 C CB  . ARG B 274  ? 0.3552 0.2508 0.2788 -0.0053 -0.0819 -0.0045 272  ARG B CB  
10663 C CG  . ARG B 274  ? 0.3612 0.2637 0.2919 0.0010  -0.0799 -0.0085 272  ARG B CG  
10664 C CD  . ARG B 274  ? 0.3537 0.2698 0.2922 0.0013  -0.0736 -0.0102 272  ARG B CD  
10665 N NE  . ARG B 274  ? 0.3193 0.2370 0.2607 0.0006  -0.0718 -0.0114 272  ARG B NE  
10666 C CZ  . ARG B 274  ? 0.3533 0.2691 0.2983 0.0050  -0.0724 -0.0151 272  ARG B CZ  
10667 N NH1 . ARG B 274  ? 0.3460 0.2587 0.2929 0.0105  -0.0747 -0.0181 272  ARG B NH1 
10668 N NH2 . ARG B 274  ? 0.3207 0.2381 0.2676 0.0038  -0.0707 -0.0159 272  ARG B NH2 
10669 N N   . TYR B 275  ? 0.3345 0.2377 0.2476 -0.0241 -0.0784 0.0081  273  TYR B N   
10670 C CA  . TYR B 275  ? 0.3635 0.2630 0.2714 -0.0313 -0.0800 0.0124  273  TYR B CA  
10671 C C   . TYR B 275  ? 0.3595 0.2651 0.2727 -0.0323 -0.0770 0.0109  273  TYR B C   
10672 O O   . TYR B 275  ? 0.3323 0.2505 0.2500 -0.0340 -0.0720 0.0117  273  TYR B O   
10673 C CB  . TYR B 275  ? 0.3719 0.2776 0.2760 -0.0371 -0.0783 0.0176  273  TYR B CB  
10674 C CG  . TYR B 275  ? 0.3346 0.2387 0.2342 -0.0452 -0.0795 0.0225  273  TYR B CG  
10675 C CD1 . TYR B 275  ? 0.4216 0.3114 0.3151 -0.0478 -0.0853 0.0238  273  TYR B CD1 
10676 C CD2 . TYR B 275  ? 0.3260 0.2428 0.2271 -0.0501 -0.0751 0.0259  273  TYR B CD2 
10677 C CE1 . TYR B 275  ? 0.4209 0.3090 0.3101 -0.0559 -0.0868 0.0285  273  TYR B CE1 
10678 C CE2 . TYR B 275  ? 0.3669 0.2832 0.2642 -0.0580 -0.0763 0.0307  273  TYR B CE2 
10679 C CZ  . TYR B 275  ? 0.4099 0.3117 0.3013 -0.0611 -0.0822 0.0320  273  TYR B CZ  
10680 O OH  . TYR B 275  ? 0.3691 0.2701 0.2567 -0.0695 -0.0838 0.0370  273  TYR B OH  
10681 N N   . SER B 276  ? 0.3209 0.2173 0.2332 -0.0310 -0.0802 0.0087  274  SER B N   
10682 C CA  . SER B 276  ? 0.3514 0.2527 0.2683 -0.0316 -0.0778 0.0070  274  SER B CA  
10683 C C   . SER B 276  ? 0.3493 0.2371 0.2618 -0.0315 -0.0829 0.0056  274  SER B C   
10684 O O   . SER B 276  ? 0.3403 0.2162 0.2484 -0.0283 -0.0876 0.0043  274  SER B O   
10685 C CB  . SER B 276  ? 0.4397 0.3512 0.3657 -0.0253 -0.0730 0.0022  274  SER B CB  
10686 O OG  . SER B 276  ? 0.4013 0.3058 0.3284 -0.0187 -0.0754 -0.0022 274  SER B OG  
10687 N N   . ARG B 277  ? 0.3117 0.2013 0.2252 -0.0347 -0.0822 0.0058  275  ARG B N   
10688 C CA  . ARG B 277  ? 0.3588 0.2357 0.2679 -0.0346 -0.0869 0.0042  275  ARG B CA  
10689 C C   . ARG B 277  ? 0.3454 0.2175 0.2570 -0.0258 -0.0878 -0.0018 275  ARG B C   
10690 O O   . ARG B 277  ? 0.3509 0.2091 0.2568 -0.0238 -0.0931 -0.0033 275  ARG B O   
10691 C CB  . ARG B 277  ? 0.3390 0.2209 0.2499 -0.0388 -0.0852 0.0047  275  ARG B CB  
10692 C CG  . ARG B 277  ? 0.3729 0.2423 0.2795 -0.0381 -0.0897 0.0022  275  ARG B CG  
10693 C CD  . ARG B 277  ? 0.3651 0.2180 0.2615 -0.0423 -0.0967 0.0052  275  ARG B CD  
10694 N NE  . ARG B 277  ? 0.3757 0.2159 0.2675 -0.0411 -0.1012 0.0023  275  ARG B NE  
10695 C CZ  . ARG B 277  ? 0.3845 0.2157 0.2750 -0.0335 -0.1036 -0.0028 275  ARG B CZ  
10696 N NH1 . ARG B 277  ? 0.4111 0.2445 0.3050 -0.0266 -0.1023 -0.0053 275  ARG B NH1 
10697 N NH2 . ARG B 277  ? 0.4483 0.2684 0.3342 -0.0326 -0.1075 -0.0054 275  ARG B NH2 
10698 N N   . ALA B 278  ? 0.3498 0.2333 0.2697 -0.0206 -0.0828 -0.0051 276  ALA B N   
10699 C CA  . ALA B 278  ? 0.3680 0.2486 0.2909 -0.0126 -0.0833 -0.0105 276  ALA B CA  
10700 C C   . ALA B 278  ? 0.3708 0.2419 0.2898 -0.0088 -0.0876 -0.0111 276  ALA B C   
10701 O O   . ALA B 278  ? 0.3894 0.2528 0.3075 -0.0031 -0.0905 -0.0148 276  ALA B O   
10702 C CB  . ALA B 278  ? 0.3627 0.2577 0.2952 -0.0085 -0.0773 -0.0133 276  ALA B CB  
10703 N N   . GLN B 279  ? 0.3531 0.2243 0.2693 -0.0119 -0.0883 -0.0073 277  GLN B N   
10704 C CA  . GLN B 279  ? 0.3378 0.2003 0.2499 -0.0088 -0.0925 -0.0073 277  GLN B CA  
10705 C C   . GLN B 279  ? 0.3653 0.2139 0.2670 -0.0141 -0.0983 -0.0031 277  GLN B C   
10706 O O   . GLN B 279  ? 0.4065 0.2501 0.3039 -0.0144 -0.1011 -0.0008 277  GLN B O   
10707 C CB  . GLN B 279  ? 0.3851 0.2576 0.3013 -0.0076 -0.0892 -0.0065 277  GLN B CB  
10708 C CG  . GLN B 279  ? 0.4063 0.2914 0.3323 -0.0025 -0.0839 -0.0106 277  GLN B CG  
10709 C CD  . GLN B 279  ? 0.4431 0.3244 0.3721 0.0052  -0.0857 -0.0156 277  GLN B CD  
10710 O OE1 . GLN B 279  ? 0.5040 0.3753 0.4288 0.0082  -0.0905 -0.0162 277  GLN B OE1 
10711 N NE2 . GLN B 279  ? 0.3711 0.2606 0.3073 0.0084  -0.0819 -0.0191 277  GLN B NE2 
10712 N N   . ALA B 280  ? 0.3707 0.2126 0.2681 -0.0184 -0.1006 -0.0019 278  ALA B N   
10713 C CA  . ALA B 280  ? 0.3936 0.2228 0.2811 -0.0250 -0.1060 0.0028  278  ALA B CA  
10714 C C   . ALA B 280  ? 0.4370 0.2514 0.3178 -0.0213 -0.1123 0.0024  278  ALA B C   
10715 O O   . ALA B 280  ? 0.4258 0.2331 0.2995 -0.0259 -0.1157 0.0071  278  ALA B O   
10716 C CB  . ALA B 280  ? 0.3929 0.2156 0.2769 -0.0290 -0.1082 0.0030  278  ALA B CB  
10717 N N   . ALA B 281  ? 0.4259 0.2353 0.3085 -0.0129 -0.1140 -0.0029 279  ALA B N   
10718 C CA  . ALA B 281  ? 0.4825 0.2776 0.3588 -0.0087 -0.1203 -0.0035 279  ALA B CA  
10719 C C   . ALA B 281  ? 0.4705 0.2699 0.3474 -0.0081 -0.1197 -0.0013 279  ALA B C   
10720 O O   . ALA B 281  ? 0.4810 0.2690 0.3500 -0.0096 -0.1250 0.0018  279  ALA B O   
10721 C CB  . ALA B 281  ? 0.5153 0.3068 0.3946 0.0009  -0.1215 -0.0100 279  ALA B CB  
10722 N N   . ARG B 282  ? 0.4056 0.2210 0.2913 -0.0060 -0.1137 -0.0026 280  ARG B N   
10723 C CA  . ARG B 282  ? 0.4365 0.2565 0.3225 -0.0060 -0.1130 -0.0004 280  ARG B CA  
10724 C C   . ARG B 282  ? 0.4109 0.2316 0.2912 -0.0150 -0.1128 0.0060  280  ARG B C   
10725 O O   . ARG B 282  ? 0.4808 0.2972 0.3559 -0.0165 -0.1154 0.0092  280  ARG B O   
10726 C CB  . ARG B 282  ? 0.4519 0.2883 0.3484 -0.0018 -0.1068 -0.0036 280  ARG B CB  
10727 C CG  . ARG B 282  ? 0.4425 0.2796 0.3449 0.0073  -0.1071 -0.0095 280  ARG B CG  
10728 C CD  . ARG B 282  ? 0.4320 0.2838 0.3434 0.0105  -0.1020 -0.0116 280  ARG B CD  
10729 N NE  . ARG B 282  ? 0.4328 0.2844 0.3415 0.0101  -0.1036 -0.0091 280  ARG B NE  
10730 C CZ  . ARG B 282  ? 0.4626 0.3258 0.3766 0.0105  -0.0996 -0.0093 280  ARG B CZ  
10731 N NH1 . ARG B 282  ? 0.4230 0.2986 0.3453 0.0115  -0.0940 -0.0117 280  ARG B NH1 
10732 N NH2 . ARG B 282  ? 0.4605 0.3222 0.3709 0.0099  -0.1016 -0.0070 280  ARG B NH2 
10733 N N   . VAL B 283  ? 0.4126 0.2392 0.2939 -0.0211 -0.1096 0.0081  281  VAL B N   
10734 C CA  . VAL B 283  ? 0.3737 0.2025 0.2501 -0.0300 -0.1091 0.0144  281  VAL B CA  
10735 C C   . VAL B 283  ? 0.4037 0.2153 0.2688 -0.0341 -0.1163 0.0184  281  VAL B C   
10736 O O   . VAL B 283  ? 0.4588 0.2682 0.3185 -0.0376 -0.1180 0.0228  281  VAL B O   
10737 C CB  . VAL B 283  ? 0.3800 0.2181 0.2600 -0.0354 -0.1048 0.0156  281  VAL B CB  
10738 C CG1 . VAL B 283  ? 0.3727 0.2124 0.2470 -0.0449 -0.1049 0.0225  281  VAL B CG1 
10739 C CG2 . VAL B 283  ? 0.4033 0.2587 0.2938 -0.0317 -0.0976 0.0123  281  VAL B CG2 
10740 N N   . MET B 284  ? 0.4028 0.2014 0.2639 -0.0336 -0.1209 0.0169  282  MET B N   
10741 C CA  . MET B 284  ? 0.4225 0.2030 0.2724 -0.0375 -0.1284 0.0206  282  MET B CA  
10742 C C   . MET B 284  ? 0.4879 0.2590 0.3334 -0.0323 -0.1330 0.0202  282  MET B C   
10743 O O   . MET B 284  ? 0.4878 0.2491 0.3245 -0.0369 -0.1375 0.0252  282  MET B O   
10744 C CB  . MET B 284  ? 0.4448 0.2129 0.2914 -0.0369 -0.1325 0.0181  282  MET B CB  
10745 C CG  . MET B 284  ? 0.4425 0.2186 0.2922 -0.0429 -0.1290 0.0190  282  MET B CG  
10746 S SD  . MET B 284  ? 0.5205 0.3022 0.3660 -0.0555 -0.1278 0.0277  282  MET B SD  
10747 C CE  . MET B 284  ? 0.5062 0.2638 0.3376 -0.0610 -0.1377 0.0318  282  MET B CE  
10748 N N   . GLY B 285  ? 0.4606 0.2347 0.3123 -0.0228 -0.1320 0.0145  283  GLY B N   
10749 C CA  . GLY B 285  ? 0.4623 0.2270 0.3103 -0.0170 -0.1368 0.0136  283  GLY B CA  
10750 C C   . GLY B 285  ? 0.5272 0.3009 0.3768 -0.0172 -0.1345 0.0159  283  GLY B C   
10751 O O   . GLY B 285  ? 0.5327 0.2972 0.3763 -0.0155 -0.1393 0.0175  283  GLY B O   
10752 N N   . GLU B 286  ? 0.4716 0.2626 0.3285 -0.0191 -0.1274 0.0160  284  GLU B N   
10753 C CA  . GLU B 286  ? 0.4739 0.2742 0.3328 -0.0183 -0.1248 0.0172  284  GLU B CA  
10754 C C   . GLU B 286  ? 0.4693 0.2783 0.3260 -0.0267 -0.1211 0.0226  284  GLU B C   
10755 O O   . GLU B 286  ? 0.4834 0.2920 0.3351 -0.0288 -0.1222 0.0262  284  GLU B O   
10756 C CB  . GLU B 286  ? 0.4979 0.3116 0.3679 -0.0112 -0.1197 0.0115  284  GLU B CB  
10757 C CG  . GLU B 286  ? 0.5042 0.3120 0.3776 -0.0021 -0.1228 0.0059  284  GLU B CG  
10758 C CD  . GLU B 286  ? 0.5284 0.3504 0.4134 0.0034  -0.1172 0.0006  284  GLU B CD  
10759 O OE1 . GLU B 286  ? 0.4943 0.3293 0.3842 0.0020  -0.1121 0.0011  284  GLU B OE1 
10760 O OE2 . GLU B 286  ? 0.5457 0.3657 0.4347 0.0092  -0.1179 -0.0039 284  GLU B OE2 
10761 N N   . LEU B 287  ? 0.4854 0.3031 0.3457 -0.0312 -0.1166 0.0233  285  LEU B N   
10762 C CA  . LEU B 287  ? 0.4322 0.2599 0.2912 -0.0388 -0.1127 0.0284  285  LEU B CA  
10763 C C   . LEU B 287  ? 0.4616 0.2782 0.3099 -0.0470 -0.1174 0.0349  285  LEU B C   
10764 O O   . LEU B 287  ? 0.4556 0.2744 0.2988 -0.0516 -0.1172 0.0397  285  LEU B O   
10765 C CB  . LEU B 287  ? 0.3979 0.2387 0.2646 -0.0406 -0.1065 0.0269  285  LEU B CB  
10766 C CG  . LEU B 287  ? 0.4432 0.3000 0.3126 -0.0455 -0.1003 0.0300  285  LEU B CG  
10767 C CD1 . LEU B 287  ? 0.3728 0.2417 0.2510 -0.0449 -0.0947 0.0272  285  LEU B CD1 
10768 C CD2 . LEU B 287  ? 0.4222 0.2765 0.2835 -0.0549 -0.1020 0.0372  285  LEU B CD2 
10769 N N   . LEU B 288  ? 0.4686 0.2730 0.3130 -0.0492 -0.1218 0.0352  286  LEU B N   
10770 C CA  . LEU B 288  ? 0.4655 0.2583 0.2995 -0.0577 -0.1268 0.0415  286  LEU B CA  
10771 C C   . LEU B 288  ? 0.4883 0.2709 0.3134 -0.0583 -0.1318 0.0452  286  LEU B C   
10772 O O   . LEU B 288  ? 0.4728 0.2563 0.2917 -0.0663 -0.1321 0.0517  286  LEU B O   
10773 C CB  . LEU B 288  ? 0.5159 0.2943 0.3465 -0.0582 -0.1319 0.0401  286  LEU B CB  
10774 C CG  . LEU B 288  ? 0.6093 0.3722 0.4283 -0.0665 -0.1385 0.0463  286  LEU B CG  
10775 C CD1 . LEU B 288  ? 0.5192 0.2924 0.3369 -0.0772 -0.1352 0.0530  286  LEU B CD1 
10776 C CD2 . LEU B 288  ? 0.6378 0.3853 0.4533 -0.0657 -0.1439 0.0438  286  LEU B CD2 
10777 N N   . PRO B 289  ? 0.5311 0.3046 0.3551 -0.0505 -0.1357 0.0417  287  PRO B N   
10778 C CA  . PRO B 289  ? 0.4897 0.2536 0.3047 -0.0514 -0.1406 0.0457  287  PRO B CA  
10779 C C   . PRO B 289  ? 0.5011 0.2785 0.3166 -0.0542 -0.1360 0.0489  287  PRO B C   
10780 O O   . PRO B 289  ? 0.5214 0.2929 0.3280 -0.0588 -0.1392 0.0544  287  PRO B O   
10781 C CB  . PRO B 289  ? 0.5433 0.2991 0.3601 -0.0410 -0.1444 0.0400  287  PRO B CB  
10782 C CG  . PRO B 289  ? 0.5575 0.3107 0.3795 -0.0369 -0.1443 0.0348  287  PRO B CG  
10783 C CD  . PRO B 289  ? 0.5366 0.3064 0.3663 -0.0409 -0.1368 0.0345  287  PRO B CD  
10784 N N   . ARG B 290  ? 0.4759 0.2709 0.3010 -0.0514 -0.1287 0.0456  288  ARG B N   
10785 C CA  . ARG B 290  ? 0.4727 0.2808 0.2978 -0.0541 -0.1241 0.0485  288  ARG B CA  
10786 C C   . ARG B 290  ? 0.4695 0.2831 0.2905 -0.0644 -0.1218 0.0551  288  ARG B C   
10787 O O   . ARG B 290  ? 0.4859 0.3011 0.3004 -0.0690 -0.1220 0.0603  288  ARG B O   
10788 C CB  . ARG B 290  ? 0.4526 0.2769 0.2888 -0.0481 -0.1173 0.0430  288  ARG B CB  
10789 C CG  . ARG B 290  ? 0.5392 0.3600 0.3786 -0.0389 -0.1194 0.0378  288  ARG B CG  
10790 C CD  . ARG B 290  ? 0.5371 0.3707 0.3882 -0.0329 -0.1138 0.0317  288  ARG B CD  
10791 N NE  . ARG B 290  ? 0.5843 0.4212 0.4384 -0.0263 -0.1138 0.0283  288  ARG B NE  
10792 C CZ  . ARG B 290  ? 0.5403 0.3882 0.4038 -0.0210 -0.1093 0.0233  288  ARG B CZ  
10793 N NH1 . ARG B 290  ? 0.5600 0.4168 0.4310 -0.0211 -0.1044 0.0209  288  ARG B NH1 
10794 N NH2 . ARG B 290  ? 0.5319 0.3821 0.3973 -0.0158 -0.1099 0.0208  288  ARG B NH2 
10795 N N   . VAL B 291  ? 0.4386 0.2558 0.2633 -0.0682 -0.1198 0.0551  289  VAL B N   
10796 C CA  . VAL B 291  ? 0.4403 0.2629 0.2612 -0.0783 -0.1181 0.0617  289  VAL B CA  
10797 C C   . VAL B 291  ? 0.4800 0.2865 0.2888 -0.0849 -0.1252 0.0680  289  VAL B C   
10798 O O   . VAL B 291  ? 0.4848 0.2952 0.2878 -0.0926 -0.1246 0.0745  289  VAL B O   
10799 C CB  . VAL B 291  ? 0.4331 0.2613 0.2602 -0.0811 -0.1154 0.0604  289  VAL B CB  
10800 C CG1 . VAL B 291  ? 0.4429 0.2799 0.2674 -0.0915 -0.1130 0.0672  289  VAL B CG1 
10801 C CG2 . VAL B 291  ? 0.4868 0.3289 0.3253 -0.0741 -0.1091 0.0541  289  VAL B CG2 
10802 N N   . LYS B 292  ? 0.5031 0.2911 0.3076 -0.0820 -0.1322 0.0662  290  LYS B N   
10803 C CA  . LYS B 292  ? 0.4930 0.2634 0.2853 -0.0880 -0.1398 0.0720  290  LYS B CA  
10804 C C   . LYS B 292  ? 0.5210 0.2906 0.3066 -0.0885 -0.1410 0.0758  290  LYS B C   
10805 O O   . LYS B 292  ? 0.5398 0.3057 0.3165 -0.0971 -0.1433 0.0832  290  LYS B O   
10806 C CB  . LYS B 292  ? 0.5801 0.3310 0.3696 -0.0826 -0.1469 0.0682  290  LYS B CB  
10807 C CG  . LYS B 292  ? 0.6430 0.3735 0.4203 -0.0841 -0.1556 0.0720  290  LYS B CG  
10808 C CD  . LYS B 292  ? 0.6350 0.3571 0.4029 -0.0959 -0.1593 0.0798  290  LYS B CD  
10809 C CE  . LYS B 292  ? 0.7229 0.4229 0.4779 -0.0971 -0.1686 0.0837  290  LYS B CE  
10810 N NZ  . LYS B 292  ? 0.7194 0.4009 0.4727 -0.0895 -0.1751 0.0783  290  LYS B NZ  
10811 N N   . ALA B 293  ? 0.5313 0.3050 0.3210 -0.0798 -0.1395 0.0711  291  ALA B N   
10812 C CA  . ALA B 293  ? 0.5852 0.3581 0.3685 -0.0796 -0.1408 0.0742  291  ALA B CA  
10813 C C   . ALA B 293  ? 0.5231 0.3123 0.3057 -0.0864 -0.1348 0.0792  291  ALA B C   
10814 O O   . ALA B 293  ? 0.5629 0.3489 0.3362 -0.0919 -0.1370 0.0854  291  ALA B O   
10815 C CB  . ALA B 293  ? 0.5191 0.2944 0.3081 -0.0687 -0.1402 0.0677  291  ALA B CB  
10816 N N   . LEU B 294  ? 0.5338 0.3406 0.3258 -0.0861 -0.1272 0.0767  292  LEU B N   
10817 C CA  . LEU B 294  ? 0.4848 0.3083 0.2768 -0.0920 -0.1211 0.0810  292  LEU B CA  
10818 C C   . LEU B 294  ? 0.5086 0.3298 0.2939 -0.1034 -0.1227 0.0888  292  LEU B C   
10819 O O   . LEU B 294  ? 0.4908 0.3183 0.2703 -0.1097 -0.1211 0.0948  292  LEU B O   
10820 C CB  . LEU B 294  ? 0.4526 0.2948 0.2566 -0.0885 -0.1130 0.0761  292  LEU B CB  
10821 C CG  . LEU B 294  ? 0.4391 0.2873 0.2505 -0.0782 -0.1101 0.0688  292  LEU B CG  
10822 C CD1 . LEU B 294  ? 0.4209 0.2857 0.2434 -0.0755 -0.1026 0.0645  292  LEU B CD1 
10823 C CD2 . LEU B 294  ? 0.4421 0.2937 0.2483 -0.0767 -0.1094 0.0703  292  LEU B CD2 
10824 N N   . ALA B 295  ? 0.4885 0.3013 0.2747 -0.1064 -0.1258 0.0888  293  ALA B N   
10825 C CA  . ALA B 295  ? 0.5258 0.3352 0.3055 -0.1178 -0.1281 0.0963  293  ALA B CA  
10826 C C   . ALA B 295  ? 0.5309 0.3232 0.2975 -0.1225 -0.1355 0.1023  293  ALA B C   
10827 O O   . ALA B 295  ? 0.5504 0.3448 0.3103 -0.1323 -0.1359 0.1101  293  ALA B O   
10828 C CB  . ALA B 295  ? 0.5005 0.3037 0.2839 -0.1193 -0.1301 0.0942  293  ALA B CB  
10829 N N   . LEU B 296  ? 0.5589 0.3351 0.3218 -0.1155 -0.1413 0.0990  294  LEU B N   
10830 C CA  . LEU B 296  ? 0.5492 0.3090 0.2993 -0.1188 -0.1486 0.1045  294  LEU B CA  
10831 C C   . LEU B 296  ? 0.6031 0.3737 0.3487 -0.1219 -0.1453 0.1093  294  LEU B C   
10832 O O   . LEU B 296  ? 0.6238 0.3880 0.3590 -0.1303 -0.1487 0.1171  294  LEU B O   
10833 C CB  . LEU B 296  ? 0.6282 0.3710 0.3766 -0.1092 -0.1548 0.0993  294  LEU B CB  
10834 C CG  . LEU B 296  ? 0.7037 0.4241 0.4387 -0.1124 -0.1642 0.1043  294  LEU B CG  
10835 C CD1 . LEU B 296  ? 0.7688 0.4758 0.4988 -0.1200 -0.1693 0.1078  294  LEU B CD1 
10836 C CD2 . LEU B 296  ? 0.7670 0.4742 0.5014 -0.1015 -0.1695 0.0988  294  LEU B CD2 
10837 N N   . LEU B 297  ? 0.5398 0.3262 0.2926 -0.1153 -0.1388 0.1048  295  LEU B N   
10838 C CA  . LEU B 297  ? 0.5381 0.3361 0.2867 -0.1180 -0.1350 0.1090  295  LEU B CA  
10839 C C   . LEU B 297  ? 0.5582 0.3707 0.3063 -0.1282 -0.1300 0.1153  295  LEU B C   
10840 O O   . LEU B 297  ? 0.5513 0.3658 0.2908 -0.1352 -0.1303 0.1224  295  LEU B O   
10841 C CB  . LEU B 297  ? 0.5185 0.3300 0.2750 -0.1086 -0.1292 0.1023  295  LEU B CB  
10842 C CG  . LEU B 297  ? 0.5956 0.3963 0.3523 -0.0986 -0.1335 0.0967  295  LEU B CG  
10843 C CD1 . LEU B 297  ? 0.6154 0.4316 0.3807 -0.0907 -0.1271 0.0904  295  LEU B CD1 
10844 C CD2 . LEU B 297  ? 0.6050 0.3926 0.3491 -0.1007 -0.1398 0.1018  295  LEU B CD2 
10845 N N   . ALA B 298  ? 0.5298 0.3533 0.2873 -0.1292 -0.1253 0.1130  296  ALA B N   
10846 C CA  . ALA B 298  ? 0.5221 0.3605 0.2802 -0.1388 -0.1206 0.1189  296  ALA B CA  
10847 C C   . ALA B 298  ? 0.5422 0.3681 0.2899 -0.1501 -0.1267 0.1275  296  ALA B C   
10848 O O   . ALA B 298  ? 0.5534 0.3884 0.2961 -0.1588 -0.1246 0.1348  296  ALA B O   
10849 C CB  . ALA B 298  ? 0.5061 0.3564 0.2761 -0.1375 -0.1155 0.1146  296  ALA B CB  
10850 N N   . LYS B 299  ? 0.5642 0.3692 0.3083 -0.1500 -0.1345 0.1267  297  LYS B N   
10851 C CA  . LYS B 299  ? 0.6077 0.3978 0.3410 -0.1606 -0.1415 0.1347  297  LYS B CA  
10852 C C   . LYS B 299  ? 0.5892 0.3724 0.3105 -0.1637 -0.1448 0.1409  297  LYS B C   
10853 O O   . LYS B 299  ? 0.6183 0.4034 0.3345 -0.1737 -0.1454 0.1478  297  LYS B O   
10854 C CB  . LYS B 299  ? 0.6048 0.3722 0.3361 -0.1581 -0.1494 0.1315  297  LYS B CB  
10855 C CG  . LYS B 299  ? 0.6932 0.4399 0.4111 -0.1669 -0.1584 0.1391  297  LYS B CG  
10856 C CD  . LYS B 299  ? 0.7492 0.4715 0.4639 -0.1615 -0.1668 0.1347  297  LYS B CD  
10857 C CE  . LYS B 299  ? 0.8538 0.5606 0.5603 -0.1680 -0.1739 0.1382  297  LYS B CE  
10858 N NZ  . LYS B 299  ? 0.9019 0.5848 0.6045 -0.1618 -0.1823 0.1334  297  LYS B NZ  
10859 N N   . ASN B 300  ? 0.6099 0.3875 0.3297 -0.1544 -0.1462 0.1366  298  ASN B N   
10860 C CA  . ASN B 300  ? 0.6030 0.3732 0.3117 -0.1568 -0.1498 0.1417  298  ASN B CA  
10861 C C   . ASN B 300  ? 0.6001 0.3912 0.3087 -0.1624 -0.1426 0.1464  298  ASN B C   
10862 O O   . ASN B 300  ? 0.6485 0.4380 0.3512 -0.1682 -0.1439 0.1512  298  ASN B O   
10863 C CB  . ASN B 300  ? 0.7087 0.4702 0.4164 -0.1453 -0.1526 0.1360  298  ASN B CB  
10864 C CG  . ASN B 300  ? 0.7673 0.5075 0.4748 -0.1395 -0.1602 0.1314  298  ASN B CG  
10865 O OD1 . ASN B 300  ? 0.8021 0.5288 0.5059 -0.1452 -0.1655 0.1339  298  ASN B OD1 
10866 N ND2 . ASN B 300  ? 0.7568 0.4951 0.4698 -0.1279 -0.1604 0.1236  298  ASN B ND2 
10867 N N   . TYR B 301  ? 0.5824 0.3941 0.2987 -0.1601 -0.1344 0.1441  299  TYR B N   
10868 C CA  . TYR B 301  ? 0.5794 0.4120 0.2951 -0.1654 -0.1273 0.1488  299  TYR B CA  
10869 C C   . TYR B 301  ? 0.5787 0.4235 0.2992 -0.1753 -0.1237 0.1531  299  TYR B C   
10870 O O   . TYR B 301  ? 0.5807 0.4438 0.3022 -0.1803 -0.1177 0.1569  299  TYR B O   
10871 C CB  . TYR B 301  ? 0.5595 0.4103 0.2844 -0.1559 -0.1192 0.1416  299  TYR B CB  
10872 C CG  . TYR B 301  ? 0.5599 0.4039 0.2812 -0.1467 -0.1212 0.1374  299  TYR B CG  
10873 C CD1 . TYR B 301  ? 0.6207 0.4646 0.3315 -0.1493 -0.1220 0.1425  299  TYR B CD1 
10874 C CD2 . TYR B 301  ? 0.5486 0.3872 0.2774 -0.1357 -0.1221 0.1284  299  TYR B CD2 
10875 C CE1 . TYR B 301  ? 0.6183 0.4563 0.3259 -0.1412 -0.1241 0.1386  299  TYR B CE1 
10876 C CE2 . TYR B 301  ? 0.5547 0.3880 0.2808 -0.1277 -0.1240 0.1246  299  TYR B CE2 
10877 C CZ  . TYR B 301  ? 0.5606 0.3935 0.2761 -0.1304 -0.1251 0.1297  299  TYR B CZ  
10878 O OH  . TYR B 301  ? 0.5711 0.3988 0.2839 -0.1226 -0.1273 0.1260  299  TYR B OH  
10879 N N   . ASP B 302  ? 0.5798 0.4150 0.3031 -0.1779 -0.1275 0.1524  300  ASP B N   
10880 C CA  . ASP B 302  ? 0.5829 0.4291 0.3116 -0.1868 -0.1248 0.1559  300  ASP B CA  
10881 C C   . ASP B 302  ? 0.5607 0.4329 0.2973 -0.1860 -0.1152 0.1553  300  ASP B C   
10882 O O   . ASP B 302  ? 0.5606 0.4507 0.2998 -0.1927 -0.1100 0.1595  300  ASP B O   
10883 C CB  . ASP B 302  ? 0.5951 0.4406 0.3194 -0.1974 -0.1270 0.1625  300  ASP B CB  
10884 C CG  . ASP B 302  ? 0.6681 0.5166 0.3969 -0.2063 -0.1278 0.1651  300  ASP B CG  
10885 O OD1 . ASP B 302  ? 0.5942 0.4315 0.3254 -0.2040 -0.1313 0.1616  300  ASP B OD1 
10886 O OD2 . ASP B 302  ? 0.6351 0.4975 0.3652 -0.2150 -0.1249 0.1704  300  ASP B OD2 
10887 N N   . ILE B 303  ? 0.5438 0.4209 0.2897 -0.1750 -0.1116 0.1464  301  ILE B N   
10888 C CA  . ILE B 303  ? 0.5622 0.4631 0.3193 -0.1720 -0.1025 0.1429  301  ILE B CA  
10889 C C   . ILE B 303  ? 0.5140 0.4128 0.2809 -0.1691 -0.1027 0.1374  301  ILE B C   
10890 O O   . ILE B 303  ? 0.5188 0.3985 0.2844 -0.1669 -0.1092 0.1345  301  ILE B O   
10891 C CB  . ILE B 303  ? 0.5126 0.4232 0.2728 -0.1614 -0.0972 0.1368  301  ILE B CB  
10892 C CG1 . ILE B 303  ? 0.5056 0.4025 0.2697 -0.1504 -0.1004 0.1280  301  ILE B CG1 
10893 C CG2 . ILE B 303  ? 0.5248 0.4346 0.2740 -0.1637 -0.0980 0.1419  301  ILE B CG2 
10894 C CD1 . ILE B 303  ? 0.4909 0.3991 0.2607 -0.1399 -0.0947 0.1211  301  ILE B CD1 
10895 N N   . GLY B 304  ? 0.5281 0.4473 0.3048 -0.1689 -0.0956 0.1358  302  GLY B N   
10896 C CA  . GLY B 304  ? 0.4878 0.4075 0.2745 -0.1655 -0.0949 0.1301  302  GLY B CA  
10897 C C   . GLY B 304  ? 0.4883 0.4068 0.2818 -0.1525 -0.0928 0.1204  302  GLY B C   
10898 O O   . GLY B 304  ? 0.4974 0.4244 0.2918 -0.1461 -0.0886 0.1176  302  GLY B O   
10899 N N   . LEU B 305  ? 0.4869 0.3945 0.2851 -0.1486 -0.0960 0.1152  303  LEU B N   
10900 C CA  . LEU B 305  ? 0.4693 0.3769 0.2755 -0.1369 -0.0939 0.1061  303  LEU B CA  
10901 C C   . LEU B 305  ? 0.4540 0.3678 0.2698 -0.1365 -0.0917 0.1027  303  LEU B C   
10902 O O   . LEU B 305  ? 0.4829 0.3844 0.2972 -0.1404 -0.0968 0.1036  303  LEU B O   
10903 C CB  . LEU B 305  ? 0.4961 0.3818 0.2974 -0.1312 -0.1009 0.1025  303  LEU B CB  
10904 C CG  . LEU B 305  ? 0.4724 0.3570 0.2816 -0.1194 -0.0994 0.0932  303  LEU B CG  
10905 C CD1 . LEU B 305  ? 0.4586 0.3308 0.2622 -0.1133 -0.1034 0.0911  303  LEU B CD1 
10906 C CD2 . LEU B 305  ? 0.5357 0.4115 0.3499 -0.1175 -0.1022 0.0891  303  LEU B CD2 
10907 N N   . ASN B 306  ? 0.4273 0.3593 0.2523 -0.1318 -0.0843 0.0990  304  ASN B N   
10908 C CA  . ASN B 306  ? 0.4397 0.3806 0.2741 -0.1318 -0.0813 0.0964  304  ASN B CA  
10909 C C   . ASN B 306  ? 0.4036 0.3420 0.2457 -0.1210 -0.0801 0.0875  304  ASN B C   
10910 O O   . ASN B 306  ? 0.4184 0.3613 0.2626 -0.1134 -0.0769 0.0833  304  ASN B O   
10911 C CB  . ASN B 306  ? 0.4078 0.3724 0.2476 -0.1348 -0.0739 0.0990  304  ASN B CB  
10912 C CG  . ASN B 306  ? 0.4461 0.4208 0.2963 -0.1329 -0.0704 0.0955  304  ASN B CG  
10913 O OD1 . ASN B 306  ? 0.4637 0.4463 0.3214 -0.1245 -0.0659 0.0893  304  ASN B OD1 
10914 N ND2 . ASN B 306  ? 0.4332 0.4068 0.2836 -0.1409 -0.0728 0.0993  304  ASN B ND2 
10915 N N   . ILE B 307  ? 0.4032 0.3348 0.2492 -0.1206 -0.0825 0.0847  305  ILE B N   
10916 C CA  . ILE B 307  ? 0.3988 0.3293 0.2527 -0.1113 -0.0810 0.0766  305  ILE B CA  
10917 C C   . ILE B 307  ? 0.3965 0.3458 0.2602 -0.1106 -0.0744 0.0750  305  ILE B C   
10918 O O   . ILE B 307  ? 0.3754 0.3276 0.2415 -0.1160 -0.0748 0.0770  305  ILE B O   
10919 C CB  . ILE B 307  ? 0.4150 0.3270 0.2670 -0.1107 -0.0875 0.0742  305  ILE B CB  
10920 C CG1 . ILE B 307  ? 0.4536 0.3467 0.2964 -0.1097 -0.0942 0.0750  305  ILE B CG1 
10921 C CG2 . ILE B 307  ? 0.3972 0.3109 0.2580 -0.1020 -0.0853 0.0665  305  ILE B CG2 
10922 C CD1 . ILE B 307  ? 0.5051 0.3788 0.3443 -0.1098 -0.1012 0.0734  305  ILE B CD1 
10923 N N   . ASP B 308  ? 0.3706 0.3320 0.2397 -0.1036 -0.0686 0.0711  306  ASP B N   
10924 C CA  . ASP B 308  ? 0.3474 0.3259 0.2258 -0.1014 -0.0624 0.0688  306  ASP B CA  
10925 C C   . ASP B 308  ? 0.3780 0.3517 0.2626 -0.0983 -0.0636 0.0641  306  ASP B C   
10926 O O   . ASP B 308  ? 0.3794 0.3384 0.2627 -0.0942 -0.0677 0.0603  306  ASP B O   
10927 C CB  . ASP B 308  ? 0.3539 0.3430 0.2360 -0.0935 -0.0569 0.0648  306  ASP B CB  
10928 C CG  . ASP B 308  ? 0.4287 0.4268 0.3056 -0.0963 -0.0543 0.0692  306  ASP B CG  
10929 O OD1 . ASP B 308  ? 0.3735 0.3716 0.2446 -0.1048 -0.0562 0.0759  306  ASP B OD1 
10930 O OD2 . ASP B 308  ? 0.4226 0.4276 0.3009 -0.0900 -0.0505 0.0661  306  ASP B OD2 
10931 N N   . ALA B 309  ? 0.3573 0.3441 0.2487 -0.0999 -0.0598 0.0642  307  ALA B N   
10932 C CA  . ALA B 309  ? 0.3254 0.3097 0.2229 -0.0970 -0.0602 0.0599  307  ALA B CA  
10933 C C   . ALA B 309  ? 0.3294 0.3234 0.2350 -0.0880 -0.0548 0.0539  307  ALA B C   
10934 O O   . ALA B 309  ? 0.3304 0.3387 0.2388 -0.0863 -0.0495 0.0543  307  ALA B O   
10935 C CB  . ALA B 309  ? 0.3265 0.3181 0.2264 -0.1046 -0.0601 0.0637  307  ALA B CB  
10936 N N   . GLU B 310  ? 0.3054 0.2910 0.2143 -0.0822 -0.0563 0.0483  308  GLU B N   
10937 C CA  . GLU B 310  ? 0.3302 0.3223 0.2460 -0.0737 -0.0520 0.0426  308  GLU B CA  
10938 C C   . GLU B 310  ? 0.3161 0.3118 0.2388 -0.0722 -0.0507 0.0396  308  GLU B C   
10939 O O   . GLU B 310  ? 0.3191 0.3223 0.2436 -0.0776 -0.0498 0.0428  308  GLU B O   
10940 C CB  . GLU B 310  ? 0.3390 0.3192 0.2525 -0.0673 -0.0545 0.0385  308  GLU B CB  
10941 C CG  . GLU B 310  ? 0.3624 0.3390 0.2685 -0.0691 -0.0561 0.0417  308  GLU B CG  
10942 C CD  . GLU B 310  ? 0.3512 0.3185 0.2557 -0.0624 -0.0581 0.0377  308  GLU B CD  
10943 O OE1 . GLU B 310  ? 0.3883 0.3621 0.2973 -0.0562 -0.0545 0.0338  308  GLU B OE1 
10944 O OE2 . GLU B 310  ? 0.3370 0.2904 0.2354 -0.0635 -0.0635 0.0386  308  GLU B OE2 
10945 N N   . GLU B 311  ? 0.3007 0.2914 0.2273 -0.0652 -0.0506 0.0339  309  GLU B N   
10946 C CA  . GLU B 311  ? 0.3229 0.3178 0.2561 -0.0632 -0.0490 0.0309  309  GLU B CA  
10947 C C   . GLU B 311  ? 0.3285 0.3147 0.2591 -0.0685 -0.0535 0.0325  309  GLU B C   
10948 O O   . GLU B 311  ? 0.3043 0.2775 0.2280 -0.0718 -0.0587 0.0344  309  GLU B O   
10949 C CB  . GLU B 311  ? 0.3184 0.3099 0.2559 -0.0547 -0.0480 0.0246  309  GLU B CB  
10950 C CG  . GLU B 311  ? 0.3263 0.3265 0.2672 -0.0491 -0.0435 0.0224  309  GLU B CG  
10951 C CD  . GLU B 311  ? 0.3651 0.3584 0.3009 -0.0472 -0.0454 0.0223  309  GLU B CD  
10952 O OE1 . GLU B 311  ? 0.3278 0.3104 0.2572 -0.0506 -0.0500 0.0246  309  GLU B OE1 
10953 O OE2 . GLU B 311  ? 0.3736 0.3721 0.3116 -0.0424 -0.0424 0.0200  309  GLU B OE2 
10954 N N   . ALA B 312  ? 0.2752 0.2681 0.2109 -0.0693 -0.0518 0.0318  310  ALA B N   
10955 C CA  . ALA B 312  ? 0.2782 0.2637 0.2114 -0.0745 -0.0560 0.0332  310  ALA B CA  
10956 C C   . ALA B 312  ? 0.3134 0.2813 0.2427 -0.0714 -0.0609 0.0295  310  ALA B C   
10957 O O   . ALA B 312  ? 0.3316 0.2883 0.2550 -0.0763 -0.0661 0.0315  310  ALA B O   
10958 C CB  . ALA B 312  ? 0.2810 0.2769 0.2208 -0.0748 -0.0532 0.0323  310  ALA B CB  
10959 N N   . ASP B 313  ? 0.3265 0.2920 0.2589 -0.0633 -0.0596 0.0242  311  ASP B N   
10960 C CA  . ASP B 313  ? 0.2974 0.2476 0.2266 -0.0598 -0.0640 0.0206  311  ASP B CA  
10961 C C   . ASP B 313  ? 0.3194 0.2569 0.2412 -0.0602 -0.0685 0.0219  311  ASP B C   
10962 O O   . ASP B 313  ? 0.3527 0.2773 0.2715 -0.0568 -0.0724 0.0189  311  ASP B O   
10963 C CB  . ASP B 313  ? 0.3004 0.2529 0.2358 -0.0512 -0.0612 0.0146  311  ASP B CB  
10964 C CG  . ASP B 313  ? 0.3951 0.3535 0.3336 -0.0461 -0.0578 0.0130  311  ASP B CG  
10965 O OD1 . ASP B 313  ? 0.3216 0.2803 0.2566 -0.0481 -0.0581 0.0159  311  ASP B OD1 
10966 O OD2 . ASP B 313  ? 0.3808 0.3435 0.3250 -0.0401 -0.0549 0.0088  311  ASP B OD2 
10967 N N   . ARG B 314  ? 0.3298 0.2708 0.2484 -0.0643 -0.0681 0.0264  312  ARG B N   
10968 C CA  . ARG B 314  ? 0.3139 0.2427 0.2246 -0.0659 -0.0728 0.0286  312  ARG B CA  
10969 C C   . ARG B 314  ? 0.3467 0.2700 0.2503 -0.0753 -0.0768 0.0346  312  ARG B C   
10970 O O   . ARG B 314  ? 0.3356 0.2470 0.2317 -0.0775 -0.0815 0.0369  312  ARG B O   
10971 C CB  . ARG B 314  ? 0.3136 0.2491 0.2247 -0.0634 -0.0698 0.0293  312  ARG B CB  
10972 C CG  . ARG B 314  ? 0.3613 0.2964 0.2768 -0.0544 -0.0682 0.0235  312  ARG B CG  
10973 C CD  . ARG B 314  ? 0.3429 0.2891 0.2612 -0.0517 -0.0636 0.0235  312  ARG B CD  
10974 N NE  . ARG B 314  ? 0.3364 0.2788 0.2568 -0.0441 -0.0637 0.0187  312  ARG B NE  
10975 C CZ  . ARG B 314  ? 0.3461 0.2959 0.2692 -0.0402 -0.0604 0.0173  312  ARG B CZ  
10976 N NH1 . ARG B 314  ? 0.2914 0.2531 0.2155 -0.0424 -0.0562 0.0197  312  ARG B NH1 
10977 N NH2 . ARG B 314  ? 0.3190 0.2641 0.2435 -0.0340 -0.0615 0.0134  312  ARG B NH2 
10978 N N   . LEU B 315  ? 0.3743 0.3058 0.2802 -0.0810 -0.0754 0.0373  313  LEU B N   
10979 C CA  . LEU B 315  ? 0.3396 0.2680 0.2394 -0.0908 -0.0788 0.0436  313  LEU B CA  
10980 C C   . LEU B 315  ? 0.3829 0.2909 0.2745 -0.0929 -0.0864 0.0436  313  LEU B C   
10981 O O   . LEU B 315  ? 0.3912 0.2894 0.2750 -0.0972 -0.0906 0.0475  313  LEU B O   
10982 C CB  . LEU B 315  ? 0.3475 0.2889 0.2522 -0.0961 -0.0761 0.0459  313  LEU B CB  
10983 C CG  . LEU B 315  ? 0.3513 0.2982 0.2527 -0.1066 -0.0771 0.0533  313  LEU B CG  
10984 C CD1 . LEU B 315  ? 0.3293 0.2904 0.2374 -0.1100 -0.0740 0.0543  313  LEU B CD1 
10985 C CD2 . LEU B 315  ? 0.3795 0.3088 0.2714 -0.1135 -0.0847 0.0567  313  LEU B CD2 
10986 N N   . GLU B 316  ? 0.3527 0.2537 0.2456 -0.0901 -0.0884 0.0394  314  GLU B N   
10987 C CA  . GLU B 316  ? 0.3837 0.2651 0.2682 -0.0924 -0.0958 0.0394  314  GLU B CA  
10988 C C   . GLU B 316  ? 0.4349 0.3023 0.3142 -0.0867 -0.0994 0.0371  314  GLU B C   
10989 O O   . GLU B 316  ? 0.4684 0.3201 0.3389 -0.0902 -0.1058 0.0395  314  GLU B O   
10990 C CB  . GLU B 316  ? 0.4307 0.3087 0.3175 -0.0902 -0.0968 0.0351  314  GLU B CB  
10991 C CG  . GLU B 316  ? 0.3826 0.2722 0.2728 -0.0975 -0.0949 0.0384  314  GLU B CG  
10992 C CD  . GLU B 316  ? 0.4348 0.3209 0.3264 -0.0963 -0.0963 0.0346  314  GLU B CD  
10993 O OE1 . GLU B 316  ? 0.4569 0.3257 0.3421 -0.0949 -0.1020 0.0321  314  GLU B OE1 
10994 O OE2 . GLU B 316  ? 0.4309 0.3315 0.3298 -0.0964 -0.0918 0.0341  314  GLU B OE2 
10995 N N   . LEU B 317  ? 0.4128 0.2859 0.2975 -0.0782 -0.0956 0.0328  315  LEU B N   
10996 C CA  . LEU B 317  ? 0.4382 0.3001 0.3188 -0.0727 -0.0986 0.0309  315  LEU B CA  
10997 C C   . LEU B 317  ? 0.4378 0.2963 0.3115 -0.0783 -0.1009 0.0368  315  LEU B C   
10998 O O   . LEU B 317  ? 0.4580 0.3007 0.3238 -0.0781 -0.1068 0.0376  315  LEU B O   
10999 C CB  . LEU B 317  ? 0.3815 0.2529 0.2699 -0.0637 -0.0936 0.0259  315  LEU B CB  
11000 C CG  . LEU B 317  ? 0.3983 0.2616 0.2840 -0.0577 -0.0959 0.0240  315  LEU B CG  
11001 C CD1 . LEU B 317  ? 0.4570 0.3014 0.3363 -0.0551 -0.1027 0.0217  315  LEU B CD1 
11002 C CD2 . LEU B 317  ? 0.4166 0.2907 0.3110 -0.0495 -0.0907 0.0190  315  LEU B CD2 
11003 N N   . SER B 318  ? 0.3949 0.2680 0.2711 -0.0831 -0.0964 0.0411  316  SER B N   
11004 C CA  . SER B 318  ? 0.4035 0.2749 0.2730 -0.0886 -0.0981 0.0470  316  SER B CA  
11005 C C   . SER B 318  ? 0.4404 0.2987 0.3008 -0.0975 -0.1045 0.0523  316  SER B C   
11006 O O   . SER B 318  ? 0.4620 0.3114 0.3145 -0.1009 -0.1084 0.0564  316  SER B O   
11007 C CB  . SER B 318  ? 0.3698 0.2610 0.2441 -0.0916 -0.0915 0.0503  316  SER B CB  
11008 O OG  . SER B 318  ? 0.4182 0.3182 0.2950 -0.0986 -0.0899 0.0534  316  SER B OG  
11009 N N   . LEU B 319  ? 0.4249 0.2817 0.2860 -0.1017 -0.1060 0.0524  317  LEU B N   
11010 C CA  . LEU B 319  ? 0.4228 0.2658 0.2749 -0.1104 -0.1127 0.0572  317  LEU B CA  
11011 C C   . LEU B 319  ? 0.4359 0.2560 0.2796 -0.1068 -0.1202 0.0550  317  LEU B C   
11012 O O   . LEU B 319  ? 0.4592 0.2658 0.2935 -0.1134 -0.1263 0.0598  317  LEU B O   
11013 C CB  . LEU B 319  ? 0.4203 0.2661 0.2752 -0.1148 -0.1129 0.0570  317  LEU B CB  
11014 C CG  . LEU B 319  ? 0.4311 0.2993 0.2942 -0.1190 -0.1062 0.0596  317  LEU B CG  
11015 C CD1 . LEU B 319  ? 0.4049 0.2746 0.2708 -0.1224 -0.1070 0.0586  317  LEU B CD1 
11016 C CD2 . LEU B 319  ? 0.4572 0.3324 0.3167 -0.1283 -0.1058 0.0676  317  LEU B CD2 
11017 N N   . ASP B 320  ? 0.4731 0.2887 0.3200 -0.0966 -0.1199 0.0480  318  ASP B N   
11018 C CA  . ASP B 320  ? 0.4947 0.2897 0.3341 -0.0920 -0.1267 0.0455  318  ASP B CA  
11019 C C   . ASP B 320  ? 0.5164 0.3068 0.3505 -0.0916 -0.1286 0.0486  318  ASP B C   
11020 O O   . ASP B 320  ? 0.5133 0.2854 0.3378 -0.0929 -0.1356 0.0504  318  ASP B O   
11021 C CB  . ASP B 320  ? 0.4591 0.2531 0.3042 -0.0808 -0.1253 0.0373  318  ASP B CB  
11022 C CG  . ASP B 320  ? 0.5060 0.2969 0.3524 -0.0810 -0.1263 0.0341  318  ASP B CG  
11023 O OD1 . ASP B 320  ? 0.5381 0.3133 0.3761 -0.0857 -0.1328 0.0358  318  ASP B OD1 
11024 O OD2 . ASP B 320  ? 0.4563 0.2597 0.3115 -0.0766 -0.1209 0.0300  318  ASP B OD2 
11025 N N   . LEU B 321  ? 0.4532 0.2592 0.2927 -0.0899 -0.1226 0.0494  319  LEU B N   
11026 C CA  . LEU B 321  ? 0.4764 0.2789 0.3104 -0.0905 -0.1242 0.0529  319  LEU B CA  
11027 C C   . LEU B 321  ? 0.4887 0.2885 0.3148 -0.1019 -0.1270 0.0612  319  LEU B C   
11028 O O   . LEU B 321  ? 0.4986 0.2844 0.3153 -0.1044 -0.1327 0.0648  319  LEU B O   
11029 C CB  . LEU B 321  ? 0.4561 0.2759 0.2975 -0.0856 -0.1172 0.0512  319  LEU B CB  
11030 C CG  . LEU B 321  ? 0.4589 0.2783 0.3058 -0.0742 -0.1160 0.0440  319  LEU B CG  
11031 C CD1 . LEU B 321  ? 0.4758 0.3061 0.3325 -0.0701 -0.1110 0.0389  319  LEU B CD1 
11032 C CD2 . LEU B 321  ? 0.4576 0.2853 0.3058 -0.0710 -0.1129 0.0444  319  LEU B CD2 
11033 N N   . LEU B 322  ? 0.4523 0.2658 0.2821 -0.1092 -0.1230 0.0647  320  LEU B N   
11034 C CA  . LEU B 322  ? 0.4675 0.2803 0.2906 -0.1208 -0.1253 0.0730  320  LEU B CA  
11035 C C   . LEU B 322  ? 0.4985 0.2886 0.3113 -0.1256 -0.1343 0.0751  320  LEU B C   
11036 O O   . LEU B 322  ? 0.5249 0.3054 0.3284 -0.1323 -0.1390 0.0813  320  LEU B O   
11037 C CB  . LEU B 322  ? 0.4563 0.2874 0.2861 -0.1271 -0.1199 0.0754  320  LEU B CB  
11038 C CG  . LEU B 322  ? 0.4768 0.3109 0.3011 -0.1397 -0.1214 0.0844  320  LEU B CG  
11039 C CD1 . LEU B 322  ? 0.4887 0.3314 0.3107 -0.1410 -0.1184 0.0886  320  LEU B CD1 
11040 C CD2 . LEU B 322  ? 0.4726 0.3226 0.3037 -0.1457 -0.1174 0.0863  320  LEU B CD2 
11041 N N   . GLU B 323  ? 0.4835 0.2645 0.2975 -0.1220 -0.1371 0.0701  321  GLU B N   
11042 C CA  . GLU B 323  ? 0.5446 0.3028 0.3486 -0.1256 -0.1460 0.0711  321  GLU B CA  
11043 C C   . GLU B 323  ? 0.5530 0.2929 0.3478 -0.1220 -0.1521 0.0715  321  GLU B C   
11044 O O   . GLU B 323  ? 0.6156 0.3407 0.3999 -0.1293 -0.1587 0.0771  321  GLU B O   
11045 C CB  . GLU B 323  ? 0.5917 0.3441 0.3990 -0.1199 -0.1471 0.0642  321  GLU B CB  
11046 C CG  . GLU B 323  ? 0.5943 0.3213 0.3909 -0.1211 -0.1565 0.0637  321  GLU B CG  
11047 C CD  . GLU B 323  ? 0.6677 0.3907 0.4610 -0.1313 -0.1598 0.0671  321  GLU B CD  
11048 O OE1 . GLU B 323  ? 0.6446 0.3849 0.4456 -0.1351 -0.1544 0.0678  321  GLU B OE1 
11049 O OE2 . GLU B 323  ? 0.6669 0.3687 0.4493 -0.1355 -0.1682 0.0691  321  GLU B OE2 
11050 N N   . VAL B 324  ? 0.5228 0.2635 0.3215 -0.1110 -0.1502 0.0658  322  VAL B N   
11051 C CA  . VAL B 324  ? 0.5408 0.2648 0.3315 -0.1066 -0.1560 0.0657  322  VAL B CA  
11052 C C   . VAL B 324  ? 0.5944 0.3208 0.3794 -0.1133 -0.1563 0.0732  322  VAL B C   
11053 O O   . VAL B 324  ? 0.6194 0.3284 0.3935 -0.1164 -0.1634 0.0771  322  VAL B O   
11054 C CB  . VAL B 324  ? 0.5747 0.3018 0.3720 -0.0934 -0.1534 0.0580  322  VAL B CB  
11055 C CG1 . VAL B 324  ? 0.6135 0.3261 0.4033 -0.0890 -0.1590 0.0585  322  VAL B CG1 
11056 C CG2 . VAL B 324  ? 0.5887 0.3106 0.3898 -0.0867 -0.1542 0.0508  322  VAL B CG2 
11057 N N   . LEU B 325  ? 0.5579 0.3056 0.3495 -0.1155 -0.1487 0.0754  323  LEU B N   
11058 C CA  . LEU B 325  ? 0.5677 0.3192 0.3540 -0.1216 -0.1484 0.0824  323  LEU B CA  
11059 C C   . LEU B 325  ? 0.5921 0.3352 0.3691 -0.1343 -0.1532 0.0906  323  LEU B C   
11060 O O   . LEU B 325  ? 0.5528 0.2841 0.3199 -0.1385 -0.1584 0.0959  323  LEU B O   
11061 C CB  . LEU B 325  ? 0.5032 0.2797 0.2985 -0.1211 -0.1390 0.0826  323  LEU B CB  
11062 C CG  . LEU B 325  ? 0.5653 0.3502 0.3689 -0.1092 -0.1344 0.0753  323  LEU B CG  
11063 C CD1 . LEU B 325  ? 0.5216 0.3306 0.3351 -0.1088 -0.1252 0.0745  323  LEU B CD1 
11064 C CD2 . LEU B 325  ? 0.4939 0.2704 0.2916 -0.1047 -0.1374 0.0756  323  LEU B CD2 
11065 N N   . CYS B 326  ? 0.5576 0.3062 0.3376 -0.1409 -0.1521 0.0920  324  CYS B N   
11066 C CA  . CYS B 326  ? 0.5632 0.3054 0.3350 -0.1540 -0.1566 0.1002  324  CYS B CA  
11067 C C   . CYS B 326  ? 0.5955 0.3097 0.3554 -0.1558 -0.1671 0.1013  324  CYS B C   
11068 O O   . CYS B 326  ? 0.6192 0.3242 0.3696 -0.1659 -0.1720 0.1090  324  CYS B O   
11069 C CB  . CYS B 326  ? 0.5717 0.3270 0.3502 -0.1604 -0.1531 0.1012  324  CYS B CB  
11070 S SG  . CYS B 326  ? 0.5806 0.3687 0.3710 -0.1608 -0.1415 0.1023  324  CYS B SG  
11071 N N   . LEU B 327  ? 0.5904 0.2907 0.3502 -0.1460 -0.1705 0.0939  325  LEU B N   
11072 C CA  . LEU B 327  ? 0.6277 0.3004 0.3761 -0.1457 -0.1806 0.0938  325  LEU B CA  
11073 C C   . LEU B 327  ? 0.6855 0.3460 0.4281 -0.1383 -0.1843 0.0927  325  LEU B C   
11074 O O   . LEU B 327  ? 0.7002 0.3370 0.4329 -0.1367 -0.1929 0.0923  325  LEU B O   
11075 C CB  . LEU B 327  ? 0.6274 0.2916 0.3785 -0.1394 -0.1827 0.0862  325  LEU B CB  
11076 C CG  . LEU B 327  ? 0.6656 0.3376 0.4205 -0.1473 -0.1809 0.0875  325  LEU B CG  
11077 C CD1 . LEU B 327  ? 0.7084 0.3766 0.4680 -0.1391 -0.1809 0.0789  325  LEU B CD1 
11078 C CD2 . LEU B 327  ? 0.6829 0.3393 0.4263 -0.1601 -0.1887 0.0951  325  LEU B CD2 
11079 N N   . ASP B 328  ? 0.6351 0.3106 0.3831 -0.1337 -0.1783 0.0921  326  ASP B N   
11080 C CA  . ASP B 328  ? 0.5987 0.2641 0.3416 -0.1268 -0.1817 0.0913  326  ASP B CA  
11081 C C   . ASP B 328  ? 0.6911 0.3449 0.4215 -0.1362 -0.1875 0.1003  326  ASP B C   
11082 O O   . ASP B 328  ? 0.7197 0.3870 0.4500 -0.1446 -0.1835 0.1068  326  ASP B O   
11083 C CB  . ASP B 328  ? 0.6446 0.3302 0.3972 -0.1195 -0.1736 0.0880  326  ASP B CB  
11084 C CG  . ASP B 328  ? 0.7164 0.3925 0.4658 -0.1101 -0.1769 0.0851  326  ASP B CG  
11085 O OD1 . ASP B 328  ? 0.7163 0.3750 0.4544 -0.1129 -0.1842 0.0895  326  ASP B OD1 
11086 O OD2 . ASP B 328  ? 0.7622 0.4482 0.5205 -0.1001 -0.1724 0.0786  326  ASP B OD2 
11087 N N   . GLY B 329  ? 0.7113 0.3399 0.4308 -0.1348 -0.1969 0.1007  327  GLY B N   
11088 C CA  . GLY B 329  ? 0.6947 0.3161 0.4050 -0.1421 -0.2015 0.1064  327  GLY B CA  
11089 C C   . GLY B 329  ? 0.7257 0.3552 0.4346 -0.1416 -0.1988 0.1102  327  GLY B C   
11090 O O   . GLY B 329  ? 0.7885 0.4193 0.4920 -0.1500 -0.1999 0.1161  327  GLY B O   
11091 N N   . ASP B 330  ? 0.7023 0.3377 0.4160 -0.1319 -0.1953 0.1067  328  ASP B N   
11092 C CA  . ASP B 330  ? 0.7539 0.3988 0.4665 -0.1311 -0.1923 0.1097  328  ASP B CA  
11093 C C   . ASP B 330  ? 0.7189 0.3860 0.4352 -0.1402 -0.1846 0.1154  328  ASP B C   
11094 O O   . ASP B 330  ? 0.7093 0.3813 0.4208 -0.1438 -0.1836 0.1207  328  ASP B O   
11095 C CB  . ASP B 330  ? 0.7624 0.4155 0.4838 -0.1175 -0.1885 0.1015  328  ASP B CB  
11096 C CG  . ASP B 330  ? 0.8845 0.5170 0.6022 -0.1076 -0.1960 0.0962  328  ASP B CG  
11097 O OD1 . ASP B 330  ? 0.8887 0.5019 0.5964 -0.1107 -0.2039 0.0987  328  ASP B OD1 
11098 O OD2 . ASP B 330  ? 0.7825 0.4208 0.5089 -0.0965 -0.1932 0.0884  328  ASP B OD2 
11099 N N   . LEU B 331  ? 0.7212 0.4022 0.4457 -0.1440 -0.1793 0.1143  329  LEU B N   
11100 C CA  . LEU B 331  ? 0.6627 0.3653 0.3910 -0.1525 -0.1721 0.1196  329  LEU B CA  
11101 C C   . LEU B 331  ? 0.7114 0.4084 0.4319 -0.1667 -0.1759 0.1284  329  LEU B C   
11102 O O   . LEU B 331  ? 0.7007 0.4161 0.4249 -0.1747 -0.1701 0.1330  329  LEU B O   
11103 C CB  . LEU B 331  ? 0.6342 0.3572 0.3767 -0.1481 -0.1636 0.1136  329  LEU B CB  
11104 C CG  . LEU B 331  ? 0.6495 0.3819 0.4007 -0.1353 -0.1587 0.1057  329  LEU B CG  
11105 C CD1 . LEU B 331  ? 0.5458 0.2924 0.3099 -0.1301 -0.1523 0.0988  329  LEU B CD1 
11106 C CD2 . LEU B 331  ? 0.6177 0.3645 0.3686 -0.1357 -0.1537 0.1088  329  LEU B CD2 
11107 N N   . SER B 332  ? 0.6870 0.3643 0.4009 -0.1683 -0.1840 0.1277  330  SER B N   
11108 C CA  . SER B 332  ? 0.7378 0.4131 0.4482 -0.1799 -0.1871 0.1323  330  SER B CA  
11109 C C   . SER B 332  ? 0.7274 0.4174 0.4363 -0.1891 -0.1835 0.1396  330  SER B C   
11110 O O   . SER B 332  ? 0.7923 0.4810 0.4968 -0.1872 -0.1838 0.1413  330  SER B O   
11111 C CB  . SER B 332  ? 0.7577 0.4086 0.4595 -0.1786 -0.1969 0.1301  330  SER B CB  
11112 O OG  . SER B 332  ? 0.8141 0.4612 0.5125 -0.1887 -0.2008 0.1334  330  SER B OG  
11113 N N   . GLY B 333  ? 0.7215 0.4262 0.4342 -0.1989 -0.1799 0.1439  331  GLY B N   
11114 C CA  . GLY B 333  ? 0.7497 0.4702 0.4619 -0.2081 -0.1761 0.1509  331  GLY B CA  
11115 C C   . GLY B 333  ? 0.8074 0.5536 0.5275 -0.2076 -0.1660 0.1524  331  GLY B C   
11116 O O   . GLY B 333  ? 0.8531 0.6159 0.5745 -0.2156 -0.1619 0.1579  331  GLY B O   
11117 N N   . TRP B 334  ? 0.6857 0.4359 0.4110 -0.1983 -0.1620 0.1475  332  TRP B N   
11118 C CA  . TRP B 334  ? 0.6718 0.4456 0.4038 -0.1963 -0.1526 0.1481  332  TRP B CA  
11119 C C   . TRP B 334  ? 0.7037 0.4918 0.4444 -0.1997 -0.1480 0.1478  332  TRP B C   
11120 O O   . TRP B 334  ? 0.6992 0.4795 0.4439 -0.1952 -0.1499 0.1423  332  TRP B O   
11121 C CB  . TRP B 334  ? 0.6556 0.4272 0.3892 -0.1835 -0.1510 0.1419  332  TRP B CB  
11122 C CG  . TRP B 334  ? 0.6332 0.4304 0.3772 -0.1782 -0.1408 0.1385  332  TRP B CG  
11123 C CD1 . TRP B 334  ? 0.6412 0.4566 0.3848 -0.1823 -0.1349 0.1434  332  TRP B CD1 
11124 C CD2 . TRP B 334  ? 0.6250 0.4319 0.3808 -0.1674 -0.1356 0.1293  332  TRP B CD2 
11125 N NE1 . TRP B 334  ? 0.6028 0.4380 0.3571 -0.1745 -0.1265 0.1375  332  TRP B NE1 
11126 C CE2 . TRP B 334  ? 0.5461 0.3762 0.3080 -0.1655 -0.1268 0.1291  332  TRP B CE2 
11127 C CE3 . TRP B 334  ? 0.5862 0.3843 0.3477 -0.1592 -0.1374 0.1214  332  TRP B CE3 
11128 C CZ2 . TRP B 334  ? 0.5179 0.3615 0.2912 -0.1560 -0.1203 0.1213  332  TRP B CZ2 
11129 C CZ3 . TRP B 334  ? 0.5721 0.3844 0.3450 -0.1501 -0.1307 0.1140  332  TRP B CZ3 
11130 C CH2 . TRP B 334  ? 0.5366 0.3710 0.3152 -0.1486 -0.1225 0.1140  332  TRP B CH2 
11131 N N   . ASN B 335  ? 0.5958 0.4069 0.3413 -0.2065 -0.1413 0.1522  333  ASN B N   
11132 C CA  . ASN B 335  ? 0.6449 0.4730 0.3995 -0.2097 -0.1361 0.1523  333  ASN B CA  
11133 C C   . ASN B 335  ? 0.5886 0.4404 0.3540 -0.2014 -0.1261 0.1474  333  ASN B C   
11134 O O   . ASN B 335  ? 0.5668 0.4380 0.3409 -0.2039 -0.1202 0.1476  333  ASN B O   
11135 C CB  . ASN B 335  ? 0.6167 0.4573 0.3731 -0.2217 -0.1353 0.1582  333  ASN B CB  
11136 C CG  . ASN B 335  ? 0.6996 0.5203 0.4494 -0.2282 -0.1446 0.1598  333  ASN B CG  
11137 O OD1 . ASN B 335  ? 0.7050 0.5092 0.4537 -0.2259 -0.1500 0.1560  333  ASN B OD1 
11138 N ND2 . ASN B 335  ? 0.7432 0.5655 0.4882 -0.2360 -0.1467 0.1652  333  ASN B ND2 
11139 N N   . GLY B 336  ? 0.5955 0.4461 0.3607 -0.1915 -0.1243 0.1427  334  GLY B N   
11140 C CA  . GLY B 336  ? 0.5333 0.4060 0.3081 -0.1840 -0.1152 0.1381  334  GLY B CA  
11141 C C   . GLY B 336  ? 0.5457 0.4213 0.3313 -0.1736 -0.1122 0.1286  334  GLY B C   
11142 O O   . GLY B 336  ? 0.4889 0.3819 0.2825 -0.1670 -0.1049 0.1244  334  GLY B O   
11143 N N   . MET B 337  ? 0.5318 0.3909 0.3176 -0.1718 -0.1178 0.1250  335  MET B N   
11144 C CA  . MET B 337  ? 0.5358 0.3972 0.3314 -0.1620 -0.1152 0.1160  335  MET B CA  
11145 C C   . MET B 337  ? 0.5683 0.4505 0.3740 -0.1647 -0.1087 0.1159  335  MET B C   
11146 O O   . MET B 337  ? 0.5075 0.3910 0.3121 -0.1743 -0.1105 0.1209  335  MET B O   
11147 C CB  . MET B 337  ? 0.5991 0.4378 0.3915 -0.1599 -0.1229 0.1126  335  MET B CB  
11148 C CG  . MET B 337  ? 0.5328 0.3731 0.3349 -0.1496 -0.1205 0.1033  335  MET B CG  
11149 S SD  . MET B 337  ? 0.7615 0.6067 0.5681 -0.1362 -0.1163 0.0963  335  MET B SD  
11150 C CE  . MET B 337  ? 0.5596 0.3780 0.3557 -0.1325 -0.1255 0.0954  335  MET B CE  
11151 N N   . GLY B 338  ? 0.5361 0.4341 0.3510 -0.1564 -0.1015 0.1103  336  GLY B N   
11152 C CA  . GLY B 338  ? 0.4904 0.4092 0.3152 -0.1577 -0.0949 0.1098  336  GLY B CA  
11153 C C   . GLY B 338  ? 0.4411 0.3620 0.2755 -0.1484 -0.0924 0.1013  336  GLY B C   
11154 O O   . GLY B 338  ? 0.4453 0.3578 0.2805 -0.1390 -0.0931 0.0951  336  GLY B O   
11155 N N   . PHE B 339  ? 0.4237 0.3564 0.2654 -0.1511 -0.0894 0.1012  337  PHE B N   
11156 C CA  . PHE B 339  ? 0.4343 0.3682 0.2847 -0.1438 -0.0876 0.0939  337  PHE B CA  
11157 C C   . PHE B 339  ? 0.4275 0.3842 0.2872 -0.1452 -0.0807 0.0944  337  PHE B C   
11158 O O   . PHE B 339  ? 0.4396 0.4047 0.2989 -0.1545 -0.0805 0.1005  337  PHE B O   
11159 C CB  . PHE B 339  ? 0.4199 0.3356 0.2671 -0.1465 -0.0947 0.0930  337  PHE B CB  
11160 C CG  . PHE B 339  ? 0.4515 0.3627 0.3049 -0.1374 -0.0943 0.0848  337  PHE B CG  
11161 C CD1 . PHE B 339  ? 0.4793 0.3780 0.3312 -0.1284 -0.0964 0.0792  337  PHE B CD1 
11162 C CD2 . PHE B 339  ? 0.4480 0.3678 0.3088 -0.1380 -0.0920 0.0828  337  PHE B CD2 
11163 C CE1 . PHE B 339  ? 0.4645 0.3601 0.3224 -0.1203 -0.0958 0.0718  337  PHE B CE1 
11164 C CE2 . PHE B 339  ? 0.4665 0.3824 0.3327 -0.1299 -0.0916 0.0755  337  PHE B CE2 
11165 C CZ  . PHE B 339  ? 0.4640 0.3679 0.3287 -0.1211 -0.0934 0.0701  337  PHE B CZ  
11166 N N   . VAL B 340  ? 0.4015 0.3681 0.2695 -0.1360 -0.0753 0.0881  338  VAL B N   
11167 C CA  . VAL B 340  ? 0.3912 0.3787 0.2685 -0.1355 -0.0688 0.0875  338  VAL B CA  
11168 C C   . VAL B 340  ? 0.3711 0.3557 0.2537 -0.1354 -0.0704 0.0845  338  VAL B C   
11169 O O   . VAL B 340  ? 0.3802 0.3506 0.2626 -0.1300 -0.0737 0.0792  338  VAL B O   
11170 C CB  . VAL B 340  ? 0.3771 0.3756 0.2600 -0.1255 -0.0624 0.0823  338  VAL B CB  
11171 C CG1 . VAL B 340  ? 0.3588 0.3776 0.2514 -0.1241 -0.0561 0.0812  338  VAL B CG1 
11172 C CG2 . VAL B 340  ? 0.3613 0.3633 0.2386 -0.1256 -0.0608 0.0852  338  VAL B CG2 
11173 N N   . VAL B 341  ? 0.3612 0.3601 0.2487 -0.1413 -0.0680 0.0878  339  VAL B N   
11174 C CA  . VAL B 341  ? 0.3551 0.3552 0.2487 -0.1409 -0.0684 0.0849  339  VAL B CA  
11175 C C   . VAL B 341  ? 0.3405 0.3637 0.2439 -0.1380 -0.0610 0.0839  339  VAL B C   
11176 O O   . VAL B 341  ? 0.3426 0.3816 0.2470 -0.1422 -0.0572 0.0887  339  VAL B O   
11177 C CB  . VAL B 341  ? 0.4180 0.4109 0.3074 -0.1517 -0.0742 0.0901  339  VAL B CB  
11178 C CG1 . VAL B 341  ? 0.4459 0.4142 0.3251 -0.1536 -0.0819 0.0905  339  VAL B CG1 
11179 C CG2 . VAL B 341  ? 0.4528 0.4608 0.3416 -0.1617 -0.0723 0.0983  339  VAL B CG2 
11180 N N   . GLN B 342  ? 0.3287 0.3538 0.2390 -0.1305 -0.0587 0.0777  340  GLN B N   
11181 C CA  . GLN B 342  ? 0.3145 0.3596 0.2340 -0.1259 -0.0518 0.0757  340  GLN B CA  
11182 C C   . GLN B 342  ? 0.3445 0.3985 0.2694 -0.1309 -0.0519 0.0775  340  GLN B C   
11183 O O   . GLN B 342  ? 0.3118 0.3562 0.2377 -0.1301 -0.0551 0.0744  340  GLN B O   
11184 C CB  . GLN B 342  ? 0.3097 0.3520 0.2335 -0.1145 -0.0492 0.0679  340  GLN B CB  
11185 C CG  . GLN B 342  ? 0.3047 0.3393 0.2238 -0.1091 -0.0491 0.0659  340  GLN B CG  
11186 C CD  . GLN B 342  ? 0.3298 0.3521 0.2502 -0.1004 -0.0504 0.0588  340  GLN B CD  
11187 O OE1 . GLN B 342  ? 0.3157 0.3249 0.2347 -0.1008 -0.0548 0.0569  340  GLN B OE1 
11188 N NE2 . GLN B 342  ? 0.2984 0.3250 0.2212 -0.0925 -0.0465 0.0549  340  GLN B NE2 
11189 N N   . ALA B 343  ? 0.3105 0.3835 0.2389 -0.1358 -0.0482 0.0824  341  ALA B N   
11190 C CA  . ALA B 343  ? 0.3114 0.3946 0.2449 -0.1418 -0.0485 0.0851  341  ALA B CA  
11191 C C   . ALA B 343  ? 0.3233 0.4144 0.2655 -0.1343 -0.0450 0.0796  341  ALA B C   
11192 O O   . ALA B 343  ? 0.2950 0.3897 0.2410 -0.1380 -0.0465 0.0804  341  ALA B O   
11193 C CB  . ALA B 343  ? 0.3319 0.4350 0.2672 -0.1488 -0.0452 0.0920  341  ALA B CB  
11194 N N   . TYR B 344  ? 0.3125 0.4065 0.2579 -0.1242 -0.0406 0.0743  342  TYR B N   
11195 C CA  . TYR B 344  ? 0.3022 0.4010 0.2551 -0.1172 -0.0380 0.0691  342  TYR B CA  
11196 C C   . TYR B 344  ? 0.3098 0.3907 0.2609 -0.1152 -0.0427 0.0647  342  TYR B C   
11197 O O   . TYR B 344  ? 0.3135 0.3972 0.2702 -0.1103 -0.0411 0.0606  342  TYR B O   
11198 C CB  . TYR B 344  ? 0.2663 0.3732 0.2231 -0.1072 -0.0321 0.0647  342  TYR B CB  
11199 C CG  . TYR B 344  ? 0.2816 0.3747 0.2348 -0.0997 -0.0326 0.0596  342  TYR B CG  
11200 C CD1 . TYR B 344  ? 0.3101 0.3839 0.2563 -0.1013 -0.0379 0.0590  342  TYR B CD1 
11201 C CD2 . TYR B 344  ? 0.2836 0.3836 0.2406 -0.0908 -0.0277 0.0554  342  TYR B CD2 
11202 C CE1 . TYR B 344  ? 0.2888 0.3518 0.2326 -0.0942 -0.0382 0.0545  342  TYR B CE1 
11203 C CE2 . TYR B 344  ? 0.2826 0.3714 0.2369 -0.0843 -0.0280 0.0510  342  TYR B CE2 
11204 C CZ  . TYR B 344  ? 0.2817 0.3526 0.2296 -0.0860 -0.0332 0.0506  342  TYR B CZ  
11205 O OH  . TYR B 344  ? 0.2698 0.3311 0.2157 -0.0794 -0.0334 0.0463  342  TYR B OH  
11206 N N   . GLY B 345  ? 0.3104 0.3733 0.2537 -0.1189 -0.0483 0.0655  343  GLY B N   
11207 C CA  . GLY B 345  ? 0.2930 0.3384 0.2339 -0.1165 -0.0529 0.0611  343  GLY B CA  
11208 C C   . GLY B 345  ? 0.2964 0.3377 0.2358 -0.1247 -0.0576 0.0639  343  GLY B C   
11209 O O   . GLY B 345  ? 0.3094 0.3523 0.2454 -0.1339 -0.0601 0.0699  343  GLY B O   
11210 N N   . LYS B 346  ? 0.2929 0.3282 0.2345 -0.1212 -0.0591 0.0594  344  LYS B N   
11211 C CA  . LYS B 346  ? 0.2997 0.3307 0.2400 -0.1280 -0.0637 0.0611  344  LYS B CA  
11212 C C   . LYS B 346  ? 0.3463 0.3577 0.2768 -0.1342 -0.0709 0.0632  344  LYS B C   
11213 O O   . LYS B 346  ? 0.3500 0.3581 0.2780 -0.1423 -0.0754 0.0664  344  LYS B O   
11214 C CB  . LYS B 346  ? 0.3085 0.3370 0.2528 -0.1218 -0.0633 0.0552  344  LYS B CB  
11215 C CG  . LYS B 346  ? 0.3112 0.3585 0.2650 -0.1163 -0.0567 0.0535  344  LYS B CG  
11216 C CD  . LYS B 346  ? 0.2797 0.3234 0.2367 -0.1100 -0.0564 0.0478  344  LYS B CD  
11217 C CE  . LYS B 346  ? 0.3448 0.4074 0.3108 -0.1065 -0.0509 0.0472  344  LYS B CE  
11218 N NZ  . LYS B 346  ? 0.3133 0.3728 0.2825 -0.0993 -0.0498 0.0415  344  LYS B NZ  
11219 N N   . ARG B 347  ? 0.3377 0.3359 0.2625 -0.1306 -0.0726 0.0615  345  ARG B N   
11220 C CA  . ARG B 347  ? 0.3537 0.3318 0.2688 -0.1355 -0.0798 0.0630  345  ARG B CA  
11221 C C   . ARG B 347  ? 0.3767 0.3559 0.2866 -0.1444 -0.0816 0.0703  345  ARG B C   
11222 O O   . ARG B 347  ? 0.3626 0.3255 0.2640 -0.1501 -0.0881 0.0727  345  ARG B O   
11223 C CB  . ARG B 347  ? 0.3807 0.3427 0.2919 -0.1269 -0.0814 0.0574  345  ARG B CB  
11224 C CG  . ARG B 347  ? 0.3313 0.2884 0.2457 -0.1193 -0.0812 0.0504  345  ARG B CG  
11225 C CD  . ARG B 347  ? 0.3561 0.3030 0.2691 -0.1099 -0.0809 0.0449  345  ARG B CD  
11226 N NE  . ARG B 347  ? 0.3161 0.2761 0.2351 -0.1040 -0.0745 0.0438  345  ARG B NE  
11227 C CZ  . ARG B 347  ? 0.3502 0.3048 0.2688 -0.0965 -0.0736 0.0401  345  ARG B CZ  
11228 N NH1 . ARG B 347  ? 0.3464 0.2834 0.2591 -0.0936 -0.0783 0.0373  345  ARG B NH1 
11229 N NH2 . ARG B 347  ? 0.3018 0.2690 0.2258 -0.0917 -0.0678 0.0391  345  ARG B NH2 
11230 N N   . CYS B 348  ? 0.3406 0.3385 0.2551 -0.1457 -0.0761 0.0740  346  CYS B N   
11231 C CA  . CYS B 348  ? 0.3723 0.3731 0.2821 -0.1527 -0.0765 0.0806  346  CYS B CA  
11232 C C   . CYS B 348  ? 0.4142 0.4060 0.3171 -0.1647 -0.0832 0.0867  346  CYS B C   
11233 O O   . CYS B 348  ? 0.4025 0.3799 0.2967 -0.1682 -0.0877 0.0893  346  CYS B O   
11234 C CB  . CYS B 348  ? 0.3756 0.4013 0.2928 -0.1529 -0.0693 0.0835  346  CYS B CB  
11235 S SG  . CYS B 348  ? 0.4779 0.5089 0.3898 -0.1576 -0.0678 0.0900  346  CYS B SG  
11236 N N   . PRO B 349  ? 0.3667 0.3658 0.2728 -0.1715 -0.0844 0.0893  347  PRO B N   
11237 C CA  . PRO B 349  ? 0.3837 0.3736 0.2827 -0.1836 -0.0911 0.0955  347  PRO B CA  
11238 C C   . PRO B 349  ? 0.4056 0.3681 0.2948 -0.1835 -0.0990 0.0930  347  PRO B C   
11239 O O   . PRO B 349  ? 0.4274 0.3776 0.3079 -0.1917 -0.1048 0.0980  347  PRO B O   
11240 C CB  . PRO B 349  ? 0.3885 0.3918 0.2940 -0.1891 -0.0907 0.0973  347  PRO B CB  
11241 C CG  . PRO B 349  ? 0.3751 0.3862 0.2888 -0.1785 -0.0858 0.0903  347  PRO B CG  
11242 C CD  . PRO B 349  ? 0.3769 0.3919 0.2927 -0.1689 -0.0803 0.0869  347  PRO B CD  
11243 N N   . PHE B 350  ? 0.3924 0.3449 0.2826 -0.1744 -0.0996 0.0853  348  PHE B N   
11244 C CA  . PHE B 350  ? 0.4234 0.3501 0.3043 -0.1732 -0.1069 0.0823  348  PHE B CA  
11245 C C   . PHE B 350  ? 0.4254 0.3403 0.3003 -0.1686 -0.1079 0.0815  348  PHE B C   
11246 O O   . PHE B 350  ? 0.4271 0.3216 0.2921 -0.1717 -0.1148 0.0827  348  PHE B O   
11247 C CB  . PHE B 350  ? 0.3988 0.3202 0.2829 -0.1650 -0.1069 0.0745  348  PHE B CB  
11248 C CG  . PHE B 350  ? 0.4260 0.3614 0.3170 -0.1684 -0.1051 0.0750  348  PHE B CG  
11249 C CD1 . PHE B 350  ? 0.4831 0.4114 0.3699 -0.1778 -0.1112 0.0780  348  PHE B CD1 
11250 C CD2 . PHE B 350  ? 0.4208 0.3765 0.3224 -0.1627 -0.0976 0.0727  348  PHE B CD2 
11251 C CE1 . PHE B 350  ? 0.4308 0.3726 0.3240 -0.1813 -0.1098 0.0787  348  PHE B CE1 
11252 C CE2 . PHE B 350  ? 0.4335 0.4024 0.3416 -0.1658 -0.0961 0.0734  348  PHE B CE2 
11253 C CZ  . PHE B 350  ? 0.4445 0.4067 0.3484 -0.1752 -0.1022 0.0764  348  PHE B CZ  
11254 N N   . VAL B 351  ? 0.4287 0.3559 0.3090 -0.1615 -0.1013 0.0799  349  VAL B N   
11255 C CA  . VAL B 351  ? 0.4026 0.3206 0.2772 -0.1581 -0.1021 0.0800  349  VAL B CA  
11256 C C   . VAL B 351  ? 0.4557 0.3717 0.3231 -0.1687 -0.1052 0.0884  349  VAL B C   
11257 O O   . VAL B 351  ? 0.4462 0.3444 0.3044 -0.1700 -0.1106 0.0897  349  VAL B O   
11258 C CB  . VAL B 351  ? 0.4269 0.3596 0.3089 -0.1488 -0.0943 0.0766  349  VAL B CB  
11259 C CG1 . VAL B 351  ? 0.3942 0.3181 0.2700 -0.1458 -0.0953 0.0772  349  VAL B CG1 
11260 C CG2 . VAL B 351  ? 0.3908 0.3238 0.2791 -0.1386 -0.0917 0.0686  349  VAL B CG2 
11261 N N   . LEU B 352  ? 0.4139 0.3485 0.2855 -0.1764 -0.1018 0.0942  350  LEU B N   
11262 C CA  . LEU B 352  ? 0.4277 0.3620 0.2929 -0.1877 -0.1048 0.1028  350  LEU B CA  
11263 C C   . LEU B 352  ? 0.4726 0.3857 0.3284 -0.1960 -0.1141 0.1055  350  LEU B C   
11264 O O   . LEU B 352  ? 0.5076 0.4079 0.3540 -0.2018 -0.1190 0.1102  350  LEU B O   
11265 C CB  . LEU B 352  ? 0.4478 0.4075 0.3203 -0.1944 -0.0994 0.1082  350  LEU B CB  
11266 C CG  . LEU B 352  ? 0.4623 0.4426 0.3423 -0.1873 -0.0905 0.1068  350  LEU B CG  
11267 C CD1 . LEU B 352  ? 0.4438 0.4489 0.3312 -0.1932 -0.0855 0.1117  350  LEU B CD1 
11268 C CD2 . LEU B 352  ? 0.4244 0.3995 0.2976 -0.1867 -0.0905 0.1094  350  LEU B CD2 
11269 N N   . ASP B 353  ? 0.4641 0.3730 0.3217 -0.1971 -0.1169 0.1028  351  ASP B N   
11270 C CA  . ASP B 353  ? 0.5484 0.4346 0.3964 -0.2036 -0.1262 0.1041  351  ASP B CA  
11271 C C   . ASP B 353  ? 0.5292 0.3912 0.3679 -0.1976 -0.1313 0.1007  351  ASP B C   
11272 O O   . ASP B 353  ? 0.5445 0.3891 0.3727 -0.2044 -0.1384 0.1049  351  ASP B O   
11273 C CB  . ASP B 353  ? 0.4860 0.3701 0.3374 -0.2026 -0.1279 0.0996  351  ASP B CB  
11274 C CG  . ASP B 353  ? 0.5572 0.4606 0.4153 -0.2113 -0.1257 0.1042  351  ASP B CG  
11275 O OD1 . ASP B 353  ? 0.5441 0.4589 0.4023 -0.2207 -0.1248 0.1120  351  ASP B OD1 
11276 O OD2 . ASP B 353  ? 0.5348 0.4422 0.3982 -0.2087 -0.1250 0.1001  351  ASP B OD2 
11277 N N   . PHE B 354  ? 0.4966 0.3573 0.3391 -0.1849 -0.1279 0.0930  352  PHE B N   
11278 C CA  . PHE B 354  ? 0.5373 0.3766 0.3720 -0.1780 -0.1324 0.0892  352  PHE B CA  
11279 C C   . PHE B 354  ? 0.5418 0.3785 0.3706 -0.1808 -0.1330 0.0944  352  PHE B C   
11280 O O   . PHE B 354  ? 0.5515 0.3673 0.3698 -0.1829 -0.1402 0.0961  352  PHE B O   
11281 C CB  . PHE B 354  ? 0.4943 0.3362 0.3356 -0.1642 -0.1279 0.0803  352  PHE B CB  
11282 C CG  . PHE B 354  ? 0.4793 0.3052 0.3148 -0.1563 -0.1306 0.0770  352  PHE B CG  
11283 C CD1 . PHE B 354  ? 0.5598 0.3621 0.3870 -0.1539 -0.1380 0.0737  352  PHE B CD1 
11284 C CD2 . PHE B 354  ? 0.5028 0.3370 0.3406 -0.1516 -0.1260 0.0772  352  PHE B CD2 
11285 C CE1 . PHE B 354  ? 0.5779 0.3659 0.3999 -0.1466 -0.1408 0.0708  352  PHE B CE1 
11286 C CE2 . PHE B 354  ? 0.5582 0.3781 0.3907 -0.1448 -0.1289 0.0745  352  PHE B CE2 
11287 C CZ  . PHE B 354  ? 0.5559 0.3529 0.3807 -0.1421 -0.1363 0.0713  352  PHE B CZ  
11288 N N   . ILE B 355  ? 0.5053 0.3628 0.3403 -0.1809 -0.1258 0.0972  353  ILE B N   
11289 C CA  . ILE B 355  ? 0.5164 0.3729 0.3458 -0.1829 -0.1258 0.1020  353  ILE B CA  
11290 C C   . ILE B 355  ? 0.5555 0.4057 0.3764 -0.1967 -0.1314 0.1111  353  ILE B C   
11291 O O   . ILE B 355  ? 0.5188 0.3546 0.3301 -0.1992 -0.1361 0.1145  353  ILE B O   
11292 C CB  . ILE B 355  ? 0.4601 0.3411 0.2982 -0.1792 -0.1165 0.1023  353  ILE B CB  
11293 C CG1 . ILE B 355  ? 0.4429 0.3273 0.2881 -0.1656 -0.1119 0.0935  353  ILE B CG1 
11294 C CG2 . ILE B 355  ? 0.5020 0.3833 0.3338 -0.1826 -0.1165 0.1080  353  ILE B CG2 
11295 C CD1 . ILE B 355  ? 0.4314 0.3387 0.2850 -0.1612 -0.1030 0.0929  353  ILE B CD1 
11296 N N   . ILE B 356  ? 0.5023 0.3632 0.3264 -0.2061 -0.1310 0.1154  354  ILE B N   
11297 C CA  . ILE B 356  ? 0.5515 0.4066 0.3676 -0.2200 -0.1366 0.1244  354  ILE B CA  
11298 C C   . ILE B 356  ? 0.5514 0.3765 0.3559 -0.2222 -0.1469 0.1237  354  ILE B C   
11299 O O   . ILE B 356  ? 0.5939 0.4052 0.3881 -0.2292 -0.1526 0.1296  354  ILE B O   
11300 C CB  . ILE B 356  ? 0.5773 0.4508 0.4001 -0.2295 -0.1343 0.1288  354  ILE B CB  
11301 C CG1 . ILE B 356  ? 0.5372 0.4399 0.3692 -0.2293 -0.1249 0.1316  354  ILE B CG1 
11302 C CG2 . ILE B 356  ? 0.5975 0.4616 0.4120 -0.2424 -0.1417 0.1360  354  ILE B CG2 
11303 C CD1 . ILE B 356  ? 0.5767 0.5008 0.4189 -0.2332 -0.1206 0.1326  354  ILE B CD1 
11304 N N   . ASP B 357  ? 0.5564 0.3705 0.3620 -0.2161 -0.1495 0.1166  355  ASP B N   
11305 C CA  . ASP B 357  ? 0.6081 0.3929 0.4024 -0.2163 -0.1592 0.1148  355  ASP B CA  
11306 C C   . ASP B 357  ? 0.6197 0.3890 0.4070 -0.2088 -0.1616 0.1128  355  ASP B C   
11307 O O   . ASP B 357  ? 0.5994 0.3478 0.3753 -0.2126 -0.1694 0.1157  355  ASP B O   
11308 C CB  . ASP B 357  ? 0.6247 0.4031 0.4222 -0.2095 -0.1605 0.1068  355  ASP B CB  
11309 C CG  . ASP B 357  ? 0.6368 0.3850 0.4228 -0.2073 -0.1699 0.1035  355  ASP B CG  
11310 O OD1 . ASP B 357  ? 0.6953 0.4352 0.4737 -0.2131 -0.1758 0.1069  355  ASP B OD1 
11311 O OD2 . ASP B 357  ? 0.6751 0.4139 0.4611 -0.1953 -0.1699 0.0959  355  ASP B OD2 
11312 N N   . LEU B 358  ? 0.5736 0.3534 0.3678 -0.1975 -0.1549 0.1076  356  LEU B N   
11313 C CA  . LEU B 358  ? 0.5898 0.3565 0.3782 -0.1900 -0.1569 0.1056  356  LEU B CA  
11314 C C   . LEU B 358  ? 0.6013 0.3663 0.3821 -0.1984 -0.1589 0.1142  356  LEU B C   
11315 O O   . LEU B 358  ? 0.6673 0.4118 0.4377 -0.1979 -0.1655 0.1154  356  LEU B O   
11316 C CB  . LEU B 358  ? 0.5280 0.3091 0.3261 -0.1774 -0.1490 0.0989  356  LEU B CB  
11317 C CG  . LEU B 358  ? 0.5547 0.3285 0.3492 -0.1695 -0.1492 0.0971  356  LEU B CG  
11318 C CD1 . LEU B 358  ? 0.5533 0.2996 0.3381 -0.1655 -0.1579 0.0941  356  LEU B CD1 
11319 C CD2 . LEU B 358  ? 0.5137 0.3032 0.3191 -0.1577 -0.1412 0.0902  356  LEU B CD2 
11320 N N   . ALA B 359  ? 0.5531 0.3395 0.3386 -0.2060 -0.1534 0.1203  357  ALA B N   
11321 C CA  . ALA B 359  ? 0.6176 0.4045 0.3960 -0.2148 -0.1547 0.1291  357  ALA B CA  
11322 C C   . ALA B 359  ? 0.6723 0.4428 0.4410 -0.2238 -0.1637 0.1332  357  ALA B C   
11323 O O   . ALA B 359  ? 0.6647 0.4256 0.4250 -0.2258 -0.1679 0.1362  357  ALA B O   
11324 C CB  . ALA B 359  ? 0.5920 0.4080 0.3787 -0.2203 -0.1464 0.1340  357  ALA B CB  
11325 N N   . ARG B 360  ? 0.6046 0.3738 0.3750 -0.2274 -0.1664 0.1317  358  ARG B N   
11326 C CA  . ARG B 360  ? 0.6745 0.4311 0.4365 -0.2339 -0.1745 0.1342  358  ARG B CA  
11327 C C   . ARG B 360  ? 0.6315 0.3600 0.3829 -0.2276 -0.1826 0.1300  358  ARG B C   
11328 O O   . ARG B 360  ? 0.7083 0.4256 0.4507 -0.2317 -0.1886 0.1334  358  ARG B O   
11329 C CB  . ARG B 360  ? 0.6432 0.4052 0.4092 -0.2383 -0.1753 0.1334  358  ARG B CB  
11330 C CG  . ARG B 360  ? 0.6614 0.4502 0.4357 -0.2469 -0.1695 0.1391  358  ARG B CG  
11331 C CD  . ARG B 360  ? 0.7434 0.5350 0.5200 -0.2515 -0.1718 0.1387  358  ARG B CD  
11332 N NE  . ARG B 360  ? 0.7680 0.5862 0.5530 -0.2593 -0.1662 0.1440  358  ARG B NE  
11333 C CZ  . ARG B 360  ? 0.7597 0.5947 0.5549 -0.2588 -0.1610 0.1423  358  ARG B CZ  
11334 N NH1 . ARG B 360  ? 0.7900 0.6182 0.5884 -0.2515 -0.1605 0.1355  358  ARG B NH1 
11335 N NH2 . ARG B 360  ? 0.7986 0.6582 0.6011 -0.2655 -0.1563 0.1473  358  ARG B NH2 
11336 N N   . ARG B 361  ? 0.6466 0.3640 0.3993 -0.2173 -0.1829 0.1226  359  ARG B N   
11337 C CA  . ARG B 361  ? 0.7617 0.4533 0.5049 -0.2104 -0.1907 0.1181  359  ARG B CA  
11338 C C   . ARG B 361  ? 0.7492 0.4330 0.4883 -0.2042 -0.1910 0.1177  359  ARG B C   
11339 O O   . ARG B 361  ? 0.7234 0.3870 0.4534 -0.2002 -0.1980 0.1157  359  ARG B O   
11340 C CB  . ARG B 361  ? 0.7713 0.4537 0.5170 -0.2015 -0.1916 0.1097  359  ARG B CB  
11341 C CG  . ARG B 361  ? 0.7326 0.4279 0.4892 -0.1953 -0.1838 0.1056  359  ARG B CG  
11342 C CD  . ARG B 361  ? 0.6963 0.3865 0.4564 -0.1893 -0.1845 0.0979  359  ARG B CD  
11343 N NE  . ARG B 361  ? 0.6523 0.3609 0.4249 -0.1819 -0.1759 0.0929  359  ARG B NE  
11344 C CZ  . ARG B 361  ? 0.6338 0.3432 0.4102 -0.1691 -0.1726 0.0863  359  ARG B CZ  
11345 N NH1 . ARG B 361  ? 0.6100 0.3001 0.3785 -0.1631 -0.1778 0.0841  359  ARG B NH1 
11346 N NH2 . ARG B 361  ? 0.5760 0.3062 0.3645 -0.1623 -0.1639 0.0819  359  ARG B NH2 
11347 N N   . SER B 362  ? 0.6555 0.3550 0.4009 -0.2032 -0.1837 0.1198  360  SER B N   
11348 C CA  . SER B 362  ? 0.6627 0.3566 0.4041 -0.1977 -0.1837 0.1202  360  SER B CA  
11349 C C   . SER B 362  ? 0.7025 0.4015 0.4389 -0.2060 -0.1844 0.1276  360  SER B C   
11350 O O   . SER B 362  ? 0.7266 0.4172 0.4574 -0.2022 -0.1864 0.1280  360  SER B O   
11351 C CB  . SER B 362  ? 0.6557 0.3655 0.4065 -0.1902 -0.1750 0.1174  360  SER B CB  
11352 O OG  . SER B 362  ? 0.6242 0.3596 0.3826 -0.1968 -0.1674 0.1220  360  SER B OG  
11353 N N   . GLY B 363  ? 0.6366 0.3500 0.3750 -0.2169 -0.1827 0.1333  361  GLY B N   
11354 C CA  . GLY B 363  ? 0.6514 0.3731 0.3866 -0.2248 -0.1821 0.1404  361  GLY B CA  
11355 C C   . GLY B 363  ? 0.6414 0.3803 0.3812 -0.2225 -0.1741 0.1426  361  GLY B C   
11356 O O   . GLY B 363  ? 0.7051 0.4448 0.4402 -0.2250 -0.1745 0.1466  361  GLY B O   
11357 N N   . ARG B 364  ? 0.6808 0.4331 0.4294 -0.2175 -0.1670 0.1399  362  ARG B N   
11358 C CA  . ARG B 364  ? 0.7025 0.4741 0.4561 -0.2151 -0.1586 0.1420  362  ARG B CA  
11359 C C   . ARG B 364  ? 0.6633 0.4608 0.4261 -0.2219 -0.1514 0.1453  362  ARG B C   
11360 O O   . ARG B 364  ? 0.6632 0.4643 0.4319 -0.2222 -0.1504 0.1428  362  ARG B O   
11361 C CB  . ARG B 364  ? 0.6486 0.4205 0.4079 -0.2012 -0.1549 0.1337  362  ARG B CB  
11362 C CG  . ARG B 364  ? 0.6748 0.4228 0.4269 -0.1925 -0.1614 0.1290  362  ARG B CG  
11363 C CD  . ARG B 364  ? 0.6681 0.4126 0.4129 -0.1918 -0.1623 0.1329  362  ARG B CD  
11364 N NE  . ARG B 364  ? 0.6658 0.3843 0.4017 -0.1861 -0.1705 0.1302  362  ARG B NE  
11365 C CZ  . ARG B 364  ? 0.6478 0.3614 0.3873 -0.1730 -0.1701 0.1219  362  ARG B CZ  
11366 N NH1 . ARG B 364  ? 0.6266 0.3585 0.3779 -0.1646 -0.1622 0.1157  362  ARG B NH1 
11367 N NH2 . ARG B 364  ? 0.7140 0.4038 0.4450 -0.1684 -0.1782 0.1200  362  ARG B NH2 
11368 N N   . ARG B 365  ? 0.6035 0.4193 0.3676 -0.2269 -0.1465 0.1506  363  ARG B N   
11369 C CA  . ARG B 365  ? 0.5663 0.4093 0.3402 -0.2312 -0.1386 0.1531  363  ARG B CA  
11370 C C   . ARG B 365  ? 0.5593 0.4161 0.3409 -0.2209 -0.1305 0.1482  363  ARG B C   
11371 O O   . ARG B 365  ? 0.6188 0.4848 0.4000 -0.2172 -0.1261 0.1489  363  ARG B O   
11372 C CB  . ARG B 365  ? 0.6330 0.4920 0.4066 -0.2396 -0.1363 0.1597  363  ARG B CB  
11373 C CG  . ARG B 365  ? 0.5995 0.4878 0.3837 -0.2433 -0.1280 0.1619  363  ARG B CG  
11374 C CD  . ARG B 365  ? 0.6980 0.5976 0.4821 -0.2542 -0.1289 0.1682  363  ARG B CD  
11375 N NE  . ARG B 365  ? 0.6710 0.5988 0.4657 -0.2572 -0.1215 0.1700  363  ARG B NE  
11376 C CZ  . ARG B 365  ? 0.6625 0.6129 0.4617 -0.2565 -0.1137 0.1723  363  ARG B CZ  
11377 N NH1 . ARG B 365  ? 0.6186 0.5670 0.4123 -0.2535 -0.1122 0.1734  363  ARG B NH1 
11378 N NH2 . ARG B 365  ? 0.6228 0.5982 0.4320 -0.2585 -0.1074 0.1734  363  ARG B NH2 
11379 N N   . ILE B 366  ? 0.5602 0.4205 0.3508 -0.2142 -0.1284 0.1410  364  ILE B N   
11380 C CA  . ILE B 366  ? 0.5437 0.4160 0.3437 -0.2014 -0.1213 0.1329  364  ILE B CA  
11381 C C   . ILE B 366  ? 0.5553 0.4566 0.3640 -0.2028 -0.1121 0.1351  364  ILE B C   
11382 O O   . ILE B 366  ? 0.5313 0.4456 0.3443 -0.2106 -0.1103 0.1390  364  ILE B O   
11383 C CB  . ILE B 366  ? 0.5026 0.3680 0.3086 -0.1941 -0.1225 0.1247  364  ILE B CB  
11384 C CG1 . ILE B 366  ? 0.5660 0.4027 0.3630 -0.1916 -0.1314 0.1221  364  ILE B CG1 
11385 C CG2 . ILE B 366  ? 0.4809 0.3605 0.2974 -0.1818 -0.1148 0.1169  364  ILE B CG2 
11386 C CD1 . ILE B 366  ? 0.5481 0.3761 0.3493 -0.1852 -0.1334 0.1146  364  ILE B CD1 
11387 N N   . MET B 367  ? 0.4869 0.3985 0.2978 -0.1952 -0.1065 0.1326  365  MET B N   
11388 C CA  . MET B 367  ? 0.4722 0.4110 0.2916 -0.1941 -0.0974 0.1332  365  MET B CA  
11389 C C   . MET B 367  ? 0.4723 0.4205 0.3033 -0.1857 -0.0928 0.1253  365  MET B C   
11390 O O   . MET B 367  ? 0.4595 0.3992 0.2926 -0.1753 -0.0929 0.1178  365  MET B O   
11391 C CB  . MET B 367  ? 0.4955 0.4399 0.3119 -0.1890 -0.0936 0.1331  365  MET B CB  
11392 C CG  . MET B 367  ? 0.4976 0.4300 0.3016 -0.1964 -0.0987 0.1404  365  MET B CG  
11393 S SD  . MET B 367  ? 0.6227 0.5585 0.4218 -0.1897 -0.0954 0.1397  365  MET B SD  
11394 C CE  . MET B 367  ? 0.5650 0.5327 0.3696 -0.1937 -0.0857 0.1442  365  MET B CE  
11395 N N   . VAL B 368  ? 0.4513 0.4167 0.2897 -0.1903 -0.0890 0.1272  366  VAL B N   
11396 C CA  . VAL B 368  ? 0.4302 0.4043 0.2793 -0.1833 -0.0852 0.1205  366  VAL B CA  
11397 C C   . VAL B 368  ? 0.4384 0.4391 0.2960 -0.1803 -0.0762 0.1204  366  VAL B C   
11398 O O   . VAL B 368  ? 0.4568 0.4739 0.3164 -0.1883 -0.0735 0.1265  366  VAL B O   
11399 C CB  . VAL B 368  ? 0.4337 0.4044 0.2851 -0.1901 -0.0890 0.1218  366  VAL B CB  
11400 C CG1 . VAL B 368  ? 0.4221 0.3996 0.2837 -0.1817 -0.0854 0.1143  366  VAL B CG1 
11401 C CG2 . VAL B 368  ? 0.5031 0.4472 0.3449 -0.1939 -0.0984 0.1226  366  VAL B CG2 
11402 N N   . ARG B 369  ? 0.4024 0.4075 0.2648 -0.1688 -0.0715 0.1135  367  ARG B N   
11403 C CA  . ARG B 369  ? 0.3886 0.4176 0.2590 -0.1646 -0.0631 0.1123  367  ARG B CA  
11404 C C   . ARG B 369  ? 0.3758 0.4126 0.2564 -0.1611 -0.0608 0.1078  367  ARG B C   
11405 O O   . ARG B 369  ? 0.3862 0.4133 0.2696 -0.1532 -0.0618 0.1009  367  ARG B O   
11406 C CB  . ARG B 369  ? 0.4035 0.4337 0.2735 -0.1545 -0.0594 0.1075  367  ARG B CB  
11407 C CG  . ARG B 369  ? 0.3682 0.4222 0.2461 -0.1495 -0.0508 0.1058  367  ARG B CG  
11408 C CD  . ARG B 369  ? 0.3821 0.4351 0.2615 -0.1377 -0.0476 0.0987  367  ARG B CD  
11409 N NE  . ARG B 369  ? 0.3853 0.4302 0.2557 -0.1373 -0.0493 0.1004  367  ARG B NE  
11410 C CZ  . ARG B 369  ? 0.4046 0.4398 0.2732 -0.1288 -0.0498 0.0949  367  ARG B CZ  
11411 N NH1 . ARG B 369  ? 0.3821 0.4141 0.2572 -0.1202 -0.0490 0.0876  367  ARG B NH1 
11412 N NH2 . ARG B 369  ? 0.3794 0.4083 0.2396 -0.1291 -0.0514 0.0971  367  ARG B NH2 
11413 N N   . LEU B 370  ? 0.3731 0.4277 0.2590 -0.1671 -0.0577 0.1118  368  LEU B N   
11414 C CA  . LEU B 370  ? 0.3668 0.4313 0.2625 -0.1641 -0.0551 0.1082  368  LEU B CA  
11415 C C   . LEU B 370  ? 0.3463 0.4299 0.2495 -0.1554 -0.0470 0.1044  368  LEU B C   
11416 O O   . LEU B 370  ? 0.3614 0.4617 0.2650 -0.1575 -0.0425 0.1084  368  LEU B O   
11417 C CB  . LEU B 370  ? 0.3658 0.4402 0.2639 -0.1751 -0.0563 0.1145  368  LEU B CB  
11418 C CG  . LEU B 370  ? 0.3958 0.4814 0.3038 -0.1735 -0.0541 0.1118  368  LEU B CG  
11419 C CD1 . LEU B 370  ? 0.3755 0.4423 0.2832 -0.1706 -0.0593 0.1065  368  LEU B CD1 
11420 C CD2 . LEU B 370  ? 0.3943 0.4940 0.3042 -0.1850 -0.0544 0.1194  368  LEU B CD2 
11421 N N   . VAL B 371  ? 0.3347 0.4155 0.2433 -0.1455 -0.0453 0.0969  369  VAL B N   
11422 C CA  . VAL B 371  ? 0.3212 0.4179 0.2367 -0.1367 -0.0382 0.0927  369  VAL B CA  
11423 C C   . VAL B 371  ? 0.3311 0.4346 0.2556 -0.1338 -0.0367 0.0892  369  VAL B C   
11424 O O   . VAL B 371  ? 0.3572 0.4520 0.2821 -0.1380 -0.0411 0.0894  369  VAL B O   
11425 C CB  . VAL B 371  ? 0.3172 0.4042 0.2303 -0.1268 -0.0374 0.0866  369  VAL B CB  
11426 C CG1 . VAL B 371  ? 0.3290 0.4064 0.2324 -0.1298 -0.0401 0.0900  369  VAL B CG1 
11427 C CG2 . VAL B 371  ? 0.3129 0.3837 0.2279 -0.1212 -0.0409 0.0803  369  VAL B CG2 
11428 N N   . LYS B 372  ? 0.2986 0.4171 0.2300 -0.1263 -0.0305 0.0857  370  LYS B N   
11429 C CA  . LYS B 372  ? 0.3143 0.4368 0.2539 -0.1220 -0.0293 0.0814  370  LYS B CA  
11430 C C   . LYS B 372  ? 0.2826 0.3898 0.2223 -0.1132 -0.0307 0.0740  370  LYS B C   
11431 O O   . LYS B 372  ? 0.3086 0.4027 0.2480 -0.1140 -0.0350 0.0720  370  LYS B O   
11432 C CB  . LYS B 372  ? 0.2966 0.4426 0.2438 -0.1189 -0.0226 0.0816  370  LYS B CB  
11433 C CG  . LYS B 372  ? 0.3278 0.4893 0.2756 -0.1287 -0.0218 0.0894  370  LYS B CG  
11434 C CD  . LYS B 372  ? 0.3310 0.5165 0.2874 -0.1263 -0.0159 0.0900  370  LYS B CD  
11435 C CE  . LYS B 372  ? 0.4031 0.6045 0.3593 -0.1364 -0.0150 0.0982  370  LYS B CE  
11436 N NZ  . LYS B 372  ? 0.2874 0.5140 0.2505 -0.1327 -0.0082 0.0989  370  LYS B NZ  
11437 N N   . GLY B 373  ? 0.3087 0.4164 0.2481 -0.1050 -0.0274 0.0700  371  GLY B N   
11438 C CA  . GLY B 373  ? 0.3004 0.3931 0.2394 -0.0975 -0.0292 0.0636  371  GLY B CA  
11439 C C   . GLY B 373  ? 0.3111 0.4099 0.2537 -0.0876 -0.0243 0.0583  371  GLY B C   
11440 O O   . GLY B 373  ? 0.3273 0.4416 0.2760 -0.0847 -0.0196 0.0577  371  GLY B O   
11441 N N   . ALA B 374  ? 0.2803 0.3668 0.2192 -0.0823 -0.0257 0.0545  372  ALA B N   
11442 C CA  . ALA B 374  ? 0.2754 0.3667 0.2160 -0.0739 -0.0216 0.0503  372  ALA B CA  
11443 C C   . ALA B 374  ? 0.3069 0.3930 0.2527 -0.0661 -0.0211 0.0437  372  ALA B C   
11444 O O   . ALA B 374  ? 0.2976 0.3864 0.2449 -0.0591 -0.0181 0.0399  372  ALA B O   
11445 C CB  . ALA B 374  ? 0.3263 0.4088 0.2592 -0.0732 -0.0232 0.0507  372  ALA B CB  
11446 N N   . TYR B 375  ? 0.2672 0.3459 0.2157 -0.0672 -0.0240 0.0423  373  TYR B N   
11447 C CA  . TYR B 375  ? 0.2701 0.3417 0.2225 -0.0603 -0.0242 0.0363  373  TYR B CA  
11448 C C   . TYR B 375  ? 0.2402 0.3193 0.1997 -0.0593 -0.0224 0.0350  373  TYR B C   
11449 O O   . TYR B 375  ? 0.2569 0.3287 0.2191 -0.0559 -0.0237 0.0311  373  TYR B O   
11450 C CB  . TYR B 375  ? 0.2446 0.2982 0.1930 -0.0608 -0.0296 0.0347  373  TYR B CB  
11451 C CG  . TYR B 375  ? 0.2829 0.3272 0.2240 -0.0614 -0.0322 0.0359  373  TYR B CG  
11452 C CD1 . TYR B 375  ? 0.2762 0.3187 0.2111 -0.0688 -0.0347 0.0414  373  TYR B CD1 
11453 C CD2 . TYR B 375  ? 0.3284 0.3659 0.2688 -0.0550 -0.0324 0.0316  373  TYR B CD2 
11454 C CE1 . TYR B 375  ? 0.3097 0.3434 0.2376 -0.0694 -0.0372 0.0427  373  TYR B CE1 
11455 C CE2 . TYR B 375  ? 0.3526 0.3817 0.2863 -0.0555 -0.0350 0.0327  373  TYR B CE2 
11456 C CZ  . TYR B 375  ? 0.3536 0.3808 0.2810 -0.0626 -0.0374 0.0382  373  TYR B CZ  
11457 O OH  . TYR B 375  ? 0.3442 0.3627 0.2644 -0.0631 -0.0402 0.0395  373  TYR B OH  
11458 N N   . TRP B 376  ? 0.2297 0.3240 0.1924 -0.0620 -0.0193 0.0382  374  TRP B N   
11459 C CA  . TRP B 376  ? 0.2323 0.3330 0.2011 -0.0628 -0.0186 0.0380  374  TRP B CA  
11460 C C   . TRP B 376  ? 0.2217 0.3221 0.1957 -0.0547 -0.0165 0.0323  374  TRP B C   
11461 O O   . TRP B 376  ? 0.2441 0.3386 0.2205 -0.0542 -0.0184 0.0302  374  TRP B O   
11462 C CB  . TRP B 376  ? 0.2239 0.3426 0.1955 -0.0665 -0.0154 0.0424  374  TRP B CB  
11463 C CG  . TRP B 376  ? 0.2499 0.3757 0.2278 -0.0677 -0.0151 0.0426  374  TRP B CG  
11464 C CD1 . TRP B 376  ? 0.2435 0.3666 0.2211 -0.0747 -0.0187 0.0454  374  TRP B CD1 
11465 C CD2 . TRP B 376  ? 0.2744 0.4102 0.2590 -0.0617 -0.0114 0.0397  374  TRP B CD2 
11466 N NE1 . TRP B 376  ? 0.2319 0.3635 0.2160 -0.0734 -0.0173 0.0445  374  TRP B NE1 
11467 C CE2 . TRP B 376  ? 0.2542 0.3937 0.2427 -0.0654 -0.0128 0.0411  374  TRP B CE2 
11468 C CE3 . TRP B 376  ? 0.2772 0.4188 0.2646 -0.0535 -0.0072 0.0361  374  TRP B CE3 
11469 C CZ2 . TRP B 376  ? 0.2420 0.3910 0.2371 -0.0612 -0.0102 0.0392  374  TRP B CZ2 
11470 C CZ3 . TRP B 376  ? 0.2949 0.4452 0.2887 -0.0493 -0.0047 0.0341  374  TRP B CZ3 
11471 C CH2 . TRP B 376  ? 0.2658 0.4200 0.2636 -0.0531 -0.0061 0.0358  374  TRP B CH2 
11472 N N   . ASP B 377  ? 0.2431 0.3495 0.2186 -0.0484 -0.0126 0.0299  375  ASP B N   
11473 C CA  . ASP B 377  ? 0.2646 0.3706 0.2449 -0.0411 -0.0107 0.0249  375  ASP B CA  
11474 C C   . ASP B 377  ? 0.3122 0.4026 0.2913 -0.0389 -0.0140 0.0211  375  ASP B C   
11475 O O   . ASP B 377  ? 0.2463 0.3348 0.2295 -0.0360 -0.0140 0.0182  375  ASP B O   
11476 C CB  . ASP B 377  ? 0.3850 0.4974 0.3655 -0.0350 -0.0068 0.0228  375  ASP B CB  
11477 C CG  . ASP B 377  ? 0.3826 0.5120 0.3660 -0.0349 -0.0028 0.0252  375  ASP B CG  
11478 O OD1 . ASP B 377  ? 0.4611 0.5979 0.4499 -0.0341 -0.0015 0.0251  375  ASP B OD1 
11479 O OD2 . ASP B 377  ? 0.4741 0.6099 0.4542 -0.0354 -0.0009 0.0272  375  ASP B OD2 
11480 N N   . ALA B 378  ? 0.2849 0.3648 0.2585 -0.0399 -0.0168 0.0212  376  ALA B N   
11481 C CA  . ALA B 378  ? 0.2900 0.3561 0.2627 -0.0374 -0.0199 0.0176  376  ALA B CA  
11482 C C   . ALA B 378  ? 0.2693 0.3286 0.2420 -0.0413 -0.0233 0.0182  376  ALA B C   
11483 O O   . ALA B 378  ? 0.2486 0.3006 0.2232 -0.0381 -0.0246 0.0146  376  ALA B O   
11484 C CB  . ALA B 378  ? 0.2952 0.3521 0.2618 -0.0375 -0.0222 0.0178  376  ALA B CB  
11485 N N   . GLU B 379  ? 0.2520 0.3137 0.2226 -0.0482 -0.0250 0.0227  377  GLU B N   
11486 C CA  . GLU B 379  ? 0.2526 0.3071 0.2224 -0.0522 -0.0287 0.0232  377  GLU B CA  
11487 C C   . GLU B 379  ? 0.2524 0.3135 0.2284 -0.0502 -0.0268 0.0214  377  GLU B C   
11488 O O   . GLU B 379  ? 0.2523 0.3055 0.2286 -0.0496 -0.0291 0.0190  377  GLU B O   
11489 C CB  . GLU B 379  ? 0.2376 0.2930 0.2034 -0.0607 -0.0312 0.0287  377  GLU B CB  
11490 C CG  . GLU B 379  ? 0.2528 0.3008 0.2116 -0.0637 -0.0337 0.0312  377  GLU B CG  
11491 C CD  . GLU B 379  ? 0.3310 0.3612 0.2852 -0.0623 -0.0384 0.0287  377  GLU B CD  
11492 O OE1 . GLU B 379  ? 0.2914 0.3152 0.2476 -0.0592 -0.0398 0.0250  377  GLU B OE1 
11493 O OE2 . GLU B 379  ? 0.3179 0.3408 0.2661 -0.0642 -0.0409 0.0305  377  GLU B OE2 
11494 N N   . ILE B 380  ? 0.2349 0.3103 0.2154 -0.0491 -0.0227 0.0224  378  ILE B N   
11495 C CA  . ILE B 380  ? 0.2162 0.2981 0.2025 -0.0467 -0.0208 0.0208  378  ILE B CA  
11496 C C   . ILE B 380  ? 0.2208 0.2964 0.2094 -0.0398 -0.0201 0.0155  378  ILE B C   
11497 O O   . ILE B 380  ? 0.2376 0.3084 0.2277 -0.0390 -0.0215 0.0135  378  ILE B O   
11498 C CB  . ILE B 380  ? 0.2171 0.3158 0.2078 -0.0460 -0.0165 0.0228  378  ILE B CB  
11499 C CG1 . ILE B 380  ? 0.2648 0.3715 0.2538 -0.0534 -0.0171 0.0284  378  ILE B CG1 
11500 C CG2 . ILE B 380  ? 0.2137 0.3189 0.2104 -0.0429 -0.0147 0.0209  378  ILE B CG2 
11501 C CD1 . ILE B 380  ? 0.2312 0.3360 0.2199 -0.0602 -0.0206 0.0310  378  ILE B CD1 
11502 N N   . LYS B 381  ? 0.2257 0.3010 0.2142 -0.0348 -0.0180 0.0134  379  LYS B N   
11503 C CA  . LYS B 381  ? 0.2345 0.3041 0.2251 -0.0286 -0.0174 0.0087  379  LYS B CA  
11504 C C   . LYS B 381  ? 0.2100 0.2663 0.1981 -0.0291 -0.0213 0.0067  379  LYS B C   
11505 O O   . LYS B 381  ? 0.2109 0.2643 0.2018 -0.0261 -0.0213 0.0038  379  LYS B O   
11506 C CB  . LYS B 381  ? 0.2215 0.2915 0.2113 -0.0243 -0.0155 0.0071  379  LYS B CB  
11507 C CG  . LYS B 381  ? 0.2760 0.3407 0.2682 -0.0184 -0.0150 0.0026  379  LYS B CG  
11508 C CD  . LYS B 381  ? 0.2485 0.3142 0.2398 -0.0143 -0.0131 0.0011  379  LYS B CD  
11509 C CE  . LYS B 381  ? 0.2736 0.3350 0.2679 -0.0089 -0.0125 -0.0031 379  LYS B CE  
11510 N NZ  . LYS B 381  ? 0.2316 0.2932 0.2245 -0.0052 -0.0112 -0.0047 379  LYS B NZ  
11511 N N   . ARG B 382  ? 0.2186 0.2669 0.2015 -0.0325 -0.0245 0.0083  380  ARG B N   
11512 C CA  . ARG B 382  ? 0.2691 0.3042 0.2490 -0.0321 -0.0284 0.0062  380  ARG B CA  
11513 C C   . ARG B 382  ? 0.2413 0.2736 0.2217 -0.0344 -0.0303 0.0059  380  ARG B C   
11514 O O   . ARG B 382  ? 0.2328 0.2586 0.2140 -0.0313 -0.0314 0.0025  380  ARG B O   
11515 C CB  . ARG B 382  ? 0.3093 0.3364 0.2829 -0.0356 -0.0318 0.0084  380  ARG B CB  
11516 C CG  . ARG B 382  ? 0.3782 0.3912 0.3483 -0.0341 -0.0358 0.0059  380  ARG B CG  
11517 C CD  . ARG B 382  ? 0.3978 0.4080 0.3699 -0.0276 -0.0348 0.0020  380  ARG B CD  
11518 N NE  . ARG B 382  ? 0.4420 0.4519 0.4186 -0.0234 -0.0338 -0.0018 380  ARG B NE  
11519 C CZ  . ARG B 382  ? 0.4906 0.5007 0.4706 -0.0180 -0.0322 -0.0052 380  ARG B CZ  
11520 N NH1 . ARG B 382  ? 0.5339 0.5445 0.5134 -0.0158 -0.0314 -0.0056 380  ARG B NH1 
11521 N NH2 . ARG B 382  ? 0.4132 0.4232 0.3969 -0.0149 -0.0314 -0.0082 380  ARG B NH2 
11522 N N   . ALA B 383  ? 0.2092 0.2464 0.1889 -0.0401 -0.0310 0.0096  381  ALA B N   
11523 C CA  . ALA B 383  ? 0.2482 0.2828 0.2280 -0.0427 -0.0332 0.0094  381  ALA B CA  
11524 C C   . ALA B 383  ? 0.2342 0.2744 0.2196 -0.0382 -0.0303 0.0065  381  ALA B C   
11525 O O   . ALA B 383  ? 0.2239 0.2585 0.2091 -0.0374 -0.0320 0.0042  381  ALA B O   
11526 C CB  . ALA B 383  ? 0.2581 0.2986 0.2367 -0.0499 -0.0342 0.0142  381  ALA B CB  
11527 N N   . GLN B 384  ? 0.2179 0.2688 0.2078 -0.0352 -0.0261 0.0066  382  GLN B N   
11528 C CA  . GLN B 384  ? 0.2224 0.2786 0.2175 -0.0309 -0.0235 0.0041  382  GLN B CA  
11529 C C   . GLN B 384  ? 0.2361 0.2845 0.2317 -0.0255 -0.0235 -0.0002 382  GLN B C   
11530 O O   . GLN B 384  ? 0.2418 0.2880 0.2389 -0.0238 -0.0237 -0.0024 382  GLN B O   
11531 C CB  . GLN B 384  ? 0.2130 0.2816 0.2122 -0.0288 -0.0194 0.0052  382  GLN B CB  
11532 C CG  . GLN B 384  ? 0.1786 0.2578 0.1787 -0.0337 -0.0189 0.0095  382  GLN B CG  
11533 C CD  . GLN B 384  ? 0.2236 0.3155 0.2281 -0.0304 -0.0146 0.0100  382  GLN B CD  
11534 O OE1 . GLN B 384  ? 0.2389 0.3308 0.2441 -0.0256 -0.0124 0.0080  382  GLN B OE1 
11535 N NE2 . GLN B 384  ? 0.2136 0.3163 0.2211 -0.0327 -0.0136 0.0126  382  GLN B NE2 
11536 N N   . LEU B 385  ? 0.2028 0.2471 0.1970 -0.0230 -0.0233 -0.0014 383  LEU B N   
11537 C CA  . LEU B 385  ? 0.2242 0.2616 0.2191 -0.0183 -0.0236 -0.0052 383  LEU B CA  
11538 C C   . LEU B 385  ? 0.2282 0.2557 0.2202 -0.0190 -0.0270 -0.0068 383  LEU B C   
11539 O O   . LEU B 385  ? 0.2485 0.2733 0.2425 -0.0154 -0.0267 -0.0100 383  LEU B O   
11540 C CB  . LEU B 385  ? 0.2178 0.2521 0.2110 -0.0163 -0.0236 -0.0057 383  LEU B CB  
11541 C CG  . LEU B 385  ? 0.2873 0.3300 0.2833 -0.0137 -0.0200 -0.0056 383  LEU B CG  
11542 C CD1 . LEU B 385  ? 0.2640 0.3027 0.2575 -0.0121 -0.0206 -0.0062 383  LEU B CD1 
11543 C CD2 . LEU B 385  ? 0.2968 0.3426 0.2977 -0.0094 -0.0176 -0.0083 383  LEU B CD2 
11544 N N   . ASP B 386  ? 0.2433 0.2650 0.2304 -0.0235 -0.0305 -0.0048 384  ASP B N   
11545 C CA  . ASP B 386  ? 0.2631 0.2738 0.2464 -0.0238 -0.0343 -0.0066 384  ASP B CA  
11546 C C   . ASP B 386  ? 0.2583 0.2694 0.2414 -0.0261 -0.0353 -0.0065 384  ASP B C   
11547 O O   . ASP B 386  ? 0.2933 0.2951 0.2727 -0.0264 -0.0386 -0.0081 384  ASP B O   
11548 C CB  . ASP B 386  ? 0.2598 0.2621 0.2370 -0.0274 -0.0381 -0.0045 384  ASP B CB  
11549 C CG  . ASP B 386  ? 0.3376 0.3375 0.3141 -0.0245 -0.0379 -0.0051 384  ASP B CG  
11550 O OD1 . ASP B 386  ? 0.3598 0.3635 0.3405 -0.0197 -0.0351 -0.0076 384  ASP B OD1 
11551 O OD2 . ASP B 386  ? 0.3410 0.3350 0.3127 -0.0273 -0.0407 -0.0031 384  ASP B OD2 
11552 N N   . GLY B 387  ? 0.2393 0.2607 0.2262 -0.0274 -0.0326 -0.0049 385  GLY B N   
11553 C CA  . GLY B 387  ? 0.2362 0.2586 0.2230 -0.0297 -0.0337 -0.0047 385  GLY B CA  
11554 C C   . GLY B 387  ? 0.3055 0.3205 0.2866 -0.0353 -0.0383 -0.0029 385  GLY B C   
11555 O O   . GLY B 387  ? 0.2936 0.3027 0.2722 -0.0358 -0.0406 -0.0045 385  GLY B O   
11556 N N   . LEU B 388  ? 0.2509 0.2655 0.2292 -0.0398 -0.0397 0.0006  386  LEU B N   
11557 C CA  . LEU B 388  ? 0.2874 0.2934 0.2596 -0.0456 -0.0446 0.0025  386  LEU B CA  
11558 C C   . LEU B 388  ? 0.3061 0.3195 0.2793 -0.0514 -0.0451 0.0057  386  LEU B C   
11559 O O   . LEU B 388  ? 0.2849 0.3110 0.2636 -0.0508 -0.0415 0.0068  386  LEU B O   
11560 C CB  . LEU B 388  ? 0.3365 0.3372 0.3044 -0.0483 -0.0466 0.0050  386  LEU B CB  
11561 C CG  . LEU B 388  ? 0.3136 0.3063 0.2804 -0.0425 -0.0468 0.0015  386  LEU B CG  
11562 C CD1 . LEU B 388  ? 0.3032 0.2894 0.2651 -0.0451 -0.0493 0.0039  386  LEU B CD1 
11563 C CD2 . LEU B 388  ? 0.3443 0.3263 0.3087 -0.0390 -0.0494 -0.0028 386  LEU B CD2 
11564 N N   . ALA B 389  ? 0.3310 0.3362 0.2986 -0.0569 -0.0499 0.0071  387  ALA B N   
11565 C CA  . ALA B 389  ? 0.3301 0.3408 0.2983 -0.0622 -0.0511 0.0095  387  ALA B CA  
11566 C C   . ALA B 389  ? 0.3059 0.3312 0.2784 -0.0664 -0.0485 0.0143  387  ALA B C   
11567 O O   . ALA B 389  ? 0.3080 0.3442 0.2849 -0.0677 -0.0468 0.0156  387  ALA B O   
11568 C CB  . ALA B 389  ? 0.3988 0.3965 0.3594 -0.0679 -0.0573 0.0104  387  ALA B CB  
11569 N N   . ASP B 390  ? 0.2915 0.3175 0.2626 -0.0685 -0.0483 0.0171  388  ASP B N   
11570 C CA  . ASP B 390  ? 0.2379 0.2776 0.2122 -0.0728 -0.0460 0.0219  388  ASP B CA  
11571 C C   . ASP B 390  ? 0.2476 0.2867 0.2205 -0.0715 -0.0446 0.0229  388  ASP B C   
11572 O O   . ASP B 390  ? 0.2896 0.3181 0.2596 -0.0672 -0.0454 0.0199  388  ASP B O   
11573 C CB  . ASP B 390  ? 0.3077 0.3475 0.2790 -0.0819 -0.0501 0.0263  388  ASP B CB  
11574 C CG  . ASP B 390  ? 0.3566 0.4144 0.3335 -0.0857 -0.0472 0.0306  388  ASP B CG  
11575 O OD1 . ASP B 390  ? 0.3148 0.3831 0.2951 -0.0838 -0.0431 0.0321  388  ASP B OD1 
11576 O OD2 . ASP B 390  ? 0.3183 0.3800 0.2961 -0.0904 -0.0492 0.0324  388  ASP B OD2 
11577 N N   . PHE B 391  ? 0.2475 0.2980 0.2223 -0.0748 -0.0424 0.0271  389  PHE B N   
11578 C CA  . PHE B 391  ? 0.2600 0.3107 0.2329 -0.0740 -0.0410 0.0284  389  PHE B CA  
11579 C C   . PHE B 391  ? 0.2484 0.2892 0.2140 -0.0810 -0.0458 0.0319  389  PHE B C   
11580 O O   . PHE B 391  ? 0.2672 0.3060 0.2305 -0.0878 -0.0493 0.0347  389  PHE B O   
11581 C CB  . PHE B 391  ? 0.2786 0.3472 0.2567 -0.0739 -0.0361 0.0312  389  PHE B CB  
11582 C CG  . PHE B 391  ? 0.2416 0.3192 0.2263 -0.0667 -0.0316 0.0278  389  PHE B CG  
11583 C CD1 . PHE B 391  ? 0.2164 0.2905 0.2019 -0.0594 -0.0292 0.0239  389  PHE B CD1 
11584 C CD2 . PHE B 391  ? 0.2147 0.3035 0.2046 -0.0675 -0.0301 0.0287  389  PHE B CD2 
11585 C CE1 . PHE B 391  ? 0.2203 0.3013 0.2114 -0.0531 -0.0255 0.0209  389  PHE B CE1 
11586 C CE2 . PHE B 391  ? 0.2356 0.3315 0.2311 -0.0607 -0.0262 0.0257  389  PHE B CE2 
11587 C CZ  . PHE B 391  ? 0.2114 0.3030 0.2073 -0.0536 -0.0240 0.0218  389  PHE B CZ  
11588 N N   . PRO B 392  ? 0.2478 0.2814 0.2094 -0.0796 -0.0464 0.0318  390  PRO B N   
11589 C CA  . PRO B 392  ? 0.2784 0.3033 0.2327 -0.0865 -0.0508 0.0358  390  PRO B CA  
11590 C C   . PRO B 392  ? 0.2604 0.2979 0.2152 -0.0920 -0.0487 0.0416  390  PRO B C   
11591 O O   . PRO B 392  ? 0.3023 0.3337 0.2510 -0.0980 -0.0519 0.0455  390  PRO B O   
11592 C CB  . PRO B 392  ? 0.2614 0.2738 0.2117 -0.0813 -0.0520 0.0328  390  PRO B CB  
11593 C CG  . PRO B 392  ? 0.2494 0.2720 0.2056 -0.0739 -0.0463 0.0299  390  PRO B CG  
11594 C CD  . PRO B 392  ? 0.2402 0.2728 0.2033 -0.0717 -0.0434 0.0281  390  PRO B CD  
11595 N N   . VAL B 393  ? 0.2703 0.3249 0.2318 -0.0897 -0.0433 0.0420  391  VAL B N   
11596 C CA  . VAL B 393  ? 0.2865 0.3561 0.2495 -0.0940 -0.0405 0.0471  391  VAL B CA  
11597 C C   . VAL B 393  ? 0.2698 0.3550 0.2398 -0.0955 -0.0379 0.0484  391  VAL B C   
11598 O O   . VAL B 393  ? 0.2833 0.3688 0.2573 -0.0914 -0.0373 0.0448  391  VAL B O   
11599 C CB  . VAL B 393  ? 0.2452 0.3213 0.2093 -0.0881 -0.0358 0.0459  391  VAL B CB  
11600 C CG1 . VAL B 393  ? 0.2771 0.3385 0.2344 -0.0869 -0.0385 0.0450  391  VAL B CG1 
11601 C CG2 . VAL B 393  ? 0.2352 0.3168 0.2057 -0.0791 -0.0316 0.0407  391  VAL B CG2 
11602 N N   . PHE B 394  ? 0.2847 0.3839 0.2561 -0.1012 -0.0363 0.0538  392  PHE B N   
11603 C CA  . PHE B 394  ? 0.2397 0.3562 0.2184 -0.1019 -0.0334 0.0553  392  PHE B CA  
11604 C C   . PHE B 394  ? 0.2504 0.3777 0.2352 -0.0925 -0.0276 0.0515  392  PHE B C   
11605 O O   . PHE B 394  ? 0.2534 0.3774 0.2367 -0.0867 -0.0253 0.0489  392  PHE B O   
11606 C CB  . PHE B 394  ? 0.2759 0.4055 0.2548 -0.1105 -0.0332 0.0622  392  PHE B CB  
11607 C CG  . PHE B 394  ? 0.3207 0.4392 0.2933 -0.1203 -0.0393 0.0662  392  PHE B CG  
11608 C CD1 . PHE B 394  ? 0.2845 0.3967 0.2570 -0.1244 -0.0437 0.0660  392  PHE B CD1 
11609 C CD2 . PHE B 394  ? 0.2857 0.3993 0.2519 -0.1255 -0.0411 0.0701  392  PHE B CD2 
11610 C CE1 . PHE B 394  ? 0.3156 0.4161 0.2817 -0.1334 -0.0498 0.0694  392  PHE B CE1 
11611 C CE2 . PHE B 394  ? 0.2884 0.3904 0.2483 -0.1345 -0.0471 0.0738  392  PHE B CE2 
11612 C CZ  . PHE B 394  ? 0.3157 0.4109 0.2755 -0.1385 -0.0516 0.0734  392  PHE B CZ  
11613 N N   . THR B 395  ? 0.2312 0.3709 0.2228 -0.0911 -0.0254 0.0513  393  THR B N   
11614 C CA  . THR B 395  ? 0.2671 0.4168 0.2644 -0.0824 -0.0202 0.0479  393  THR B CA  
11615 C C   . THR B 395  ? 0.2783 0.4494 0.2809 -0.0829 -0.0160 0.0514  393  THR B C   
11616 O O   . THR B 395  ? 0.2663 0.4459 0.2729 -0.0754 -0.0116 0.0488  393  THR B O   
11617 C CB  . THR B 395  ? 0.2713 0.4177 0.2724 -0.0782 -0.0208 0.0439  393  THR B CB  
11618 O OG1 . THR B 395  ? 0.2930 0.4475 0.2973 -0.0838 -0.0225 0.0469  393  THR B OG1 
11619 C CG2 . THR B 395  ? 0.3058 0.4321 0.3019 -0.0769 -0.0246 0.0401  393  THR B CG2 
11620 N N   . ARG B 396  ? 0.2898 0.4699 0.2927 -0.0914 -0.0173 0.0571  394  ARG B N   
11621 C CA  . ARG B 396  ? 0.2363 0.4375 0.2436 -0.0924 -0.0132 0.0609  394  ARG B CA  
11622 C C   . ARG B 396  ? 0.2764 0.4786 0.2785 -0.0976 -0.0131 0.0652  394  ARG B C   
11623 O O   . ARG B 396  ? 0.2506 0.4423 0.2472 -0.1054 -0.0176 0.0681  394  ARG B O   
11624 C CB  . ARG B 396  ? 0.2649 0.4789 0.2776 -0.0984 -0.0144 0.0647  394  ARG B CB  
11625 C CG  . ARG B 396  ? 0.2538 0.4691 0.2719 -0.0931 -0.0141 0.0610  394  ARG B CG  
11626 C CD  . ARG B 396  ? 0.2737 0.5042 0.2975 -0.0989 -0.0150 0.0651  394  ARG B CD  
11627 N NE  . ARG B 396  ? 0.4284 0.6581 0.4564 -0.0946 -0.0156 0.0617  394  ARG B NE  
11628 C CZ  . ARG B 396  ? 0.4623 0.7086 0.4977 -0.0915 -0.0130 0.0622  394  ARG B CZ  
11629 N NH1 . ARG B 396  ? 0.5157 0.7819 0.5557 -0.0920 -0.0094 0.0658  394  ARG B NH1 
11630 N NH2 . ARG B 396  ? 0.3864 0.6295 0.4245 -0.0876 -0.0139 0.0589  394  ARG B NH2 
11631 N N   . LYS B 397  ? 0.2994 0.5142 0.3029 -0.0932 -0.0081 0.0655  395  LYS B N   
11632 C CA  . LYS B 397  ? 0.3117 0.5279 0.3098 -0.0975 -0.0076 0.0693  395  LYS B CA  
11633 C C   . LYS B 397  ? 0.3207 0.5459 0.3186 -0.1088 -0.0096 0.0766  395  LYS B C   
11634 O O   . LYS B 397  ? 0.3142 0.5330 0.3057 -0.1155 -0.0120 0.0804  395  LYS B O   
11635 C CB  . LYS B 397  ? 0.3276 0.5573 0.3273 -0.0902 -0.0015 0.0681  395  LYS B CB  
11636 C CG  . LYS B 397  ? 0.3608 0.5884 0.3536 -0.0921 -0.0007 0.0704  395  LYS B CG  
11637 C CD  . LYS B 397  ? 0.3877 0.6328 0.3811 -0.0997 0.0010  0.0773  395  LYS B CD  
11638 C CE  . LYS B 397  ? 0.3683 0.6123 0.3546 -0.1013 0.0021  0.0797  395  LYS B CE  
11639 N NZ  . LYS B 397  ? 0.3915 0.6543 0.3788 -0.1091 0.0040  0.0869  395  LYS B NZ  
11640 N N   . ILE B 398  ? 0.2729 0.5125 0.2776 -0.1114 -0.0091 0.0788  396  ILE B N   
11641 C CA  . ILE B 398  ? 0.2879 0.5366 0.2929 -0.1227 -0.0113 0.0859  396  ILE B CA  
11642 C C   . ILE B 398  ? 0.2517 0.4810 0.2506 -0.1310 -0.0184 0.0874  396  ILE B C   
11643 O O   . ILE B 398  ? 0.2873 0.5170 0.2827 -0.1411 -0.0212 0.0933  396  ILE B O   
11644 C CB  . ILE B 398  ? 0.2896 0.5590 0.3038 -0.1232 -0.0092 0.0878  396  ILE B CB  
11645 C CG1 . ILE B 398  ? 0.3681 0.6516 0.3835 -0.1346 -0.0103 0.0957  396  ILE B CG1 
11646 C CG2 . ILE B 398  ? 0.3250 0.5857 0.3423 -0.1215 -0.0125 0.0841  396  ILE B CG2 
11647 C CD1 . ILE B 398  ? 0.4167 0.7250 0.4418 -0.1341 -0.0070 0.0980  396  ILE B CD1 
11648 N N   . HIS B 399  ? 0.2422 0.4538 0.2394 -0.1269 -0.0214 0.0821  397  HIS B N   
11649 C CA  . HIS B 399  ? 0.3081 0.4999 0.2988 -0.1337 -0.0282 0.0828  397  HIS B CA  
11650 C C   . HIS B 399  ? 0.2958 0.4741 0.2777 -0.1363 -0.0302 0.0842  397  HIS B C   
11651 O O   . HIS B 399  ? 0.2974 0.4666 0.2737 -0.1456 -0.0353 0.0884  397  HIS B O   
11652 C CB  . HIS B 399  ? 0.3143 0.4915 0.3053 -0.1277 -0.0304 0.0764  397  HIS B CB  
11653 C CG  . HIS B 399  ? 0.2756 0.4633 0.2739 -0.1271 -0.0300 0.0757  397  HIS B CG  
11654 N ND1 . HIS B 399  ? 0.2712 0.4512 0.2715 -0.1204 -0.0304 0.0700  397  HIS B ND1 
11655 C CD2 . HIS B 399  ? 0.2933 0.4994 0.2975 -0.1322 -0.0291 0.0801  397  HIS B CD2 
11656 C CE1 . HIS B 399  ? 0.2892 0.4817 0.2960 -0.1214 -0.0300 0.0709  397  HIS B CE1 
11657 N NE2 . HIS B 399  ? 0.2801 0.4886 0.2895 -0.1285 -0.0293 0.0770  397  HIS B NE2 
11658 N N   . THR B 400  ? 0.3238 0.5000 0.3043 -0.1282 -0.0266 0.0807  398  THR B N   
11659 C CA  . THR B 400  ? 0.2969 0.4619 0.2691 -0.1303 -0.0282 0.0822  398  THR B CA  
11660 C C   . THR B 400  ? 0.3005 0.4774 0.2708 -0.1395 -0.0278 0.0900  398  THR B C   
11661 O O   . THR B 400  ? 0.3416 0.5070 0.3045 -0.1470 -0.0322 0.0937  398  THR B O   
11662 C CB  . THR B 400  ? 0.2785 0.4423 0.2503 -0.1198 -0.0239 0.0773  398  THR B CB  
11663 O OG1 . THR B 400  ? 0.2621 0.4124 0.2347 -0.1124 -0.0251 0.0706  398  THR B OG1 
11664 C CG2 . THR B 400  ? 0.2787 0.4334 0.2423 -0.1218 -0.0251 0.0793  398  THR B CG2 
11665 N N   . ASP B 401  ? 0.3082 0.5082 0.2850 -0.1392 -0.0227 0.0925  399  ASP B N   
11666 C CA  . ASP B 401  ? 0.3416 0.5553 0.3172 -0.1481 -0.0218 0.1001  399  ASP B CA  
11667 C C   . ASP B 401  ? 0.2874 0.4967 0.2611 -0.1604 -0.0277 0.1057  399  ASP B C   
11668 O O   . ASP B 401  ? 0.3258 0.5320 0.2934 -0.1693 -0.0303 0.1115  399  ASP B O   
11669 C CB  . ASP B 401  ? 0.3389 0.5796 0.3227 -0.1450 -0.0151 0.1015  399  ASP B CB  
11670 C CG  . ASP B 401  ? 0.4057 0.6514 0.3899 -0.1338 -0.0093 0.0970  399  ASP B CG  
11671 O OD1 . ASP B 401  ? 0.3653 0.5967 0.3426 -0.1308 -0.0100 0.0947  399  ASP B OD1 
11672 O OD2 . ASP B 401  ? 0.3826 0.6466 0.3740 -0.1279 -0.0041 0.0956  399  ASP B OD2 
11673 N N   . VAL B 402  ? 0.3332 0.5418 0.3116 -0.1614 -0.0302 0.1042  400  VAL B N   
11674 C CA  . VAL B 402  ? 0.2941 0.4968 0.2702 -0.1731 -0.0364 0.1090  400  VAL B CA  
11675 C C   . VAL B 402  ? 0.3211 0.4970 0.2868 -0.1764 -0.0429 0.1084  400  VAL B C   
11676 O O   . VAL B 402  ? 0.3416 0.5118 0.3014 -0.1870 -0.0473 0.1143  400  VAL B O   
11677 C CB  . VAL B 402  ? 0.3300 0.5367 0.3129 -0.1724 -0.0377 0.1067  400  VAL B CB  
11678 C CG1 . VAL B 402  ? 0.3597 0.5573 0.3392 -0.1841 -0.0450 0.1109  400  VAL B CG1 
11679 C CG2 . VAL B 402  ? 0.3488 0.5832 0.3418 -0.1701 -0.0318 0.1083  400  VAL B CG2 
11680 N N   . SER B 403  ? 0.3301 0.4892 0.2933 -0.1675 -0.0437 0.1013  401  SER B N   
11681 C CA  . SER B 403  ? 0.3558 0.4897 0.3095 -0.1688 -0.0494 0.0999  401  SER B CA  
11682 C C   . SER B 403  ? 0.3906 0.5222 0.3372 -0.1738 -0.0498 0.1050  401  SER B C   
11683 O O   . SER B 403  ? 0.3784 0.4966 0.3174 -0.1824 -0.0557 0.1090  401  SER B O   
11684 C CB  . SER B 403  ? 0.3414 0.4628 0.2950 -0.1569 -0.0483 0.0916  401  SER B CB  
11685 O OG  . SER B 403  ? 0.3969 0.4948 0.3416 -0.1571 -0.0535 0.0899  401  SER B OG  
11686 N N   . TYR B 404  ? 0.3679 0.5128 0.3166 -0.1685 -0.0436 0.1049  402  TYR B N   
11687 C CA  . TYR B 404  ? 0.3934 0.5370 0.3352 -0.1722 -0.0434 0.1093  402  TYR B CA  
11688 C C   . TYR B 404  ? 0.4123 0.5634 0.3519 -0.1857 -0.0459 0.1182  402  TYR B C   
11689 O O   . TYR B 404  ? 0.4044 0.5417 0.3352 -0.1929 -0.0509 0.1223  402  TYR B O   
11690 C CB  . TYR B 404  ? 0.3403 0.4997 0.2856 -0.1639 -0.0358 0.1074  402  TYR B CB  
11691 C CG  . TYR B 404  ? 0.3745 0.5309 0.3120 -0.1653 -0.0352 0.1104  402  TYR B CG  
11692 C CD1 . TYR B 404  ? 0.3887 0.5563 0.3237 -0.1749 -0.0348 0.1184  402  TYR B CD1 
11693 C CD2 . TYR B 404  ? 0.3870 0.5305 0.3200 -0.1570 -0.0348 0.1054  402  TYR B CD2 
11694 C CE1 . TYR B 404  ? 0.3787 0.5436 0.3061 -0.1763 -0.0342 0.1214  402  TYR B CE1 
11695 C CE2 . TYR B 404  ? 0.3364 0.4771 0.2620 -0.1583 -0.0344 0.1082  402  TYR B CE2 
11696 C CZ  . TYR B 404  ? 0.3993 0.5505 0.3220 -0.1678 -0.0341 0.1162  402  TYR B CZ  
11697 O OH  . TYR B 404  ? 0.4103 0.5590 0.3252 -0.1692 -0.0337 0.1192  402  TYR B OH  
11698 N N   . ILE B 405  ? 0.4080 0.5806 0.3555 -0.1894 -0.0430 0.1215  403  ILE B N   
11699 C CA  . ILE B 405  ? 0.4192 0.6015 0.3656 -0.2026 -0.0450 0.1304  403  ILE B CA  
11700 C C   . ILE B 405  ? 0.3689 0.5313 0.3093 -0.2120 -0.0538 0.1326  403  ILE B C   
11701 O O   . ILE B 405  ? 0.3975 0.5548 0.3313 -0.2228 -0.0579 0.1394  403  ILE B O   
11702 C CB  . ILE B 405  ? 0.4181 0.6286 0.3753 -0.2036 -0.0399 0.1328  403  ILE B CB  
11703 C CG1 . ILE B 405  ? 0.4297 0.6590 0.3913 -0.1945 -0.0315 0.1309  403  ILE B CG1 
11704 C CG2 . ILE B 405  ? 0.4089 0.6291 0.3659 -0.2156 -0.0428 0.1405  403  ILE B CG2 
11705 C CD1 . ILE B 405  ? 0.4867 0.7438 0.4594 -0.1930 -0.0260 0.1321  403  ILE B CD1 
11706 N N   . ALA B 406  ? 0.4331 0.5831 0.3751 -0.2078 -0.0569 0.1269  404  ALA B N   
11707 C CA  . ALA B 406  ? 0.4349 0.5649 0.3707 -0.2158 -0.0654 0.1282  404  ALA B CA  
11708 C C   . ALA B 406  ? 0.4526 0.5577 0.3769 -0.2166 -0.0705 0.1280  404  ALA B C   
11709 O O   . ALA B 406  ? 0.4548 0.5476 0.3717 -0.2270 -0.0771 0.1331  404  ALA B O   
11710 C CB  . ALA B 406  ? 0.4257 0.5487 0.3657 -0.2101 -0.0671 0.1215  404  ALA B CB  
11711 N N   . CYS B 407  ? 0.4162 0.5133 0.3387 -0.2058 -0.0679 0.1222  405  CYS B N   
11712 C CA  . CYS B 407  ? 0.4729 0.5471 0.3848 -0.2056 -0.0726 0.1217  405  CYS B CA  
11713 C C   . CYS B 407  ? 0.4782 0.5567 0.3843 -0.2135 -0.0725 0.1294  405  CYS B C   
11714 O O   . CYS B 407  ? 0.4571 0.5170 0.3533 -0.2194 -0.0787 0.1325  405  CYS B O   
11715 C CB  . CYS B 407  ? 0.4598 0.5265 0.3722 -0.1920 -0.0696 0.1136  405  CYS B CB  
11716 S SG  . CYS B 407  ? 0.4823 0.5390 0.3994 -0.1833 -0.0710 0.1046  405  CYS B SG  
11717 N N   . ALA B 408  ? 0.4239 0.5268 0.3356 -0.2137 -0.0656 0.1327  406  ALA B N   
11718 C CA  . ALA B 408  ? 0.4788 0.5889 0.3855 -0.2225 -0.0652 0.1409  406  ALA B CA  
11719 C C   . ALA B 408  ? 0.4546 0.5608 0.3574 -0.2373 -0.0716 0.1486  406  ALA B C   
11720 O O   . ALA B 408  ? 0.4680 0.5641 0.3624 -0.2428 -0.0759 0.1526  406  ALA B O   
11721 C CB  . ALA B 408  ? 0.4814 0.6207 0.3960 -0.2198 -0.0564 0.1427  406  ALA B CB  
11722 N N   . ALA B 409  ? 0.4448 0.5582 0.3542 -0.2399 -0.0730 0.1480  407  ALA B N   
11723 C CA  . ALA B 409  ? 0.4785 0.5858 0.3841 -0.2491 -0.0801 0.1519  407  ALA B CA  
11724 C C   . ALA B 409  ? 0.4407 0.5167 0.3350 -0.2524 -0.0889 0.1511  407  ALA B C   
11725 O O   . ALA B 409  ? 0.5079 0.5744 0.3946 -0.2597 -0.0949 0.1553  407  ALA B O   
11726 C CB  . ALA B 409  ? 0.4701 0.5896 0.3842 -0.2501 -0.0801 0.1508  407  ALA B CB  
11727 N N   . LYS B 410  ? 0.4905 0.5501 0.3835 -0.2467 -0.0901 0.1456  408  LYS B N   
11728 C CA  . LYS B 410  ? 0.4619 0.4909 0.3441 -0.2480 -0.0983 0.1439  408  LYS B CA  
11729 C C   . LYS B 410  ? 0.5291 0.5468 0.4018 -0.2486 -0.0998 0.1468  408  LYS B C   
11730 O O   . LYS B 410  ? 0.5376 0.5367 0.4006 -0.2535 -0.1073 0.1489  408  LYS B O   
11731 C CB  . LYS B 410  ? 0.4689 0.4863 0.3535 -0.2357 -0.0982 0.1340  408  LYS B CB  
11732 C CG  . LYS B 410  ? 0.5038 0.4903 0.3780 -0.2341 -0.1062 0.1306  408  LYS B CG  
11733 C CD  . LYS B 410  ? 0.5228 0.5006 0.4002 -0.2213 -0.1052 0.1206  408  LYS B CD  
11734 C CE  . LYS B 410  ? 0.5340 0.5167 0.4176 -0.2220 -0.1059 0.1180  408  LYS B CE  
11735 N NZ  . LYS B 410  ? 0.5278 0.4902 0.4036 -0.2298 -0.1151 0.1191  408  LYS B NZ  
11736 N N   . LEU B 411  ? 0.4799 0.5096 0.3554 -0.2414 -0.0928 0.1456  409  LEU B N   
11737 C CA  . LEU B 411  ? 0.4727 0.4931 0.3394 -0.2415 -0.0937 0.1482  409  LEU B CA  
11738 C C   . LEU B 411  ? 0.4990 0.5270 0.3621 -0.2514 -0.0955 0.1557  409  LEU B C   
11739 O O   . LEU B 411  ? 0.4981 0.5086 0.3513 -0.2553 -0.1016 0.1581  409  LEU B O   
11740 C CB  . LEU B 411  ? 0.4670 0.5006 0.3385 -0.2299 -0.0855 0.1437  409  LEU B CB  
11741 C CG  . LEU B 411  ? 0.5417 0.5607 0.4135 -0.2165 -0.0856 0.1341  409  LEU B CG  
11742 C CD1 . LEU B 411  ? 0.4922 0.5278 0.3710 -0.2055 -0.0771 0.1294  409  LEU B CD1 
11743 C CD2 . LEU B 411  ? 0.5045 0.4975 0.3646 -0.2165 -0.0923 0.1340  409  LEU B CD2 
11744 N N   . LEU B 412  ? 0.5451 0.5993 0.4168 -0.2541 -0.0906 0.1584  410  LEU B N   
11745 C CA  . LEU B 412  ? 0.5592 0.6234 0.4290 -0.2620 -0.0919 0.1645  410  LEU B CA  
11746 C C   . LEU B 412  ? 0.5777 0.6252 0.4405 -0.2708 -0.1014 0.1673  410  LEU B C   
11747 O O   . LEU B 412  ? 0.5947 0.6434 0.4527 -0.2778 -0.1042 0.1725  410  LEU B O   
11748 C CB  . LEU B 412  ? 0.5008 0.5964 0.3819 -0.2623 -0.0850 0.1662  410  LEU B CB  
11749 C CG  . LEU B 412  ? 0.5495 0.6640 0.4362 -0.2544 -0.0755 0.1647  410  LEU B CG  
11750 C CD1 . LEU B 412  ? 0.4946 0.6390 0.3927 -0.2533 -0.0690 0.1654  410  LEU B CD1 
11751 C CD2 . LEU B 412  ? 0.5384 0.6506 0.4177 -0.2555 -0.0750 0.1679  410  LEU B CD2 
11752 N N   . ALA B 413  ? 0.5653 0.5974 0.4269 -0.2705 -0.1064 0.1638  411  ALA B N   
11753 C CA  . ALA B 413  ? 0.5259 0.5404 0.3796 -0.2780 -0.1157 0.1660  411  ALA B CA  
11754 C C   . ALA B 413  ? 0.6378 0.6227 0.4790 -0.2776 -0.1228 0.1650  411  ALA B C   
11755 O O   . ALA B 413  ? 0.6170 0.5862 0.4502 -0.2838 -0.1309 0.1672  411  ALA B O   
11756 C CB  . ALA B 413  ? 0.6016 0.6128 0.4591 -0.2777 -0.1183 0.1626  411  ALA B CB  
11757 N N   . ALA B 414  ? 0.5848 0.5616 0.4238 -0.2704 -0.1203 0.1620  412  ALA B N   
11758 C CA  . ALA B 414  ? 0.5774 0.5256 0.4050 -0.2684 -0.1269 0.1604  412  ALA B CA  
11759 C C   . ALA B 414  ? 0.6184 0.5668 0.4411 -0.2672 -0.1247 0.1630  412  ALA B C   
11760 O O   . ALA B 414  ? 0.6149 0.5437 0.4305 -0.2621 -0.1275 0.1605  412  ALA B O   
11761 C CB  . ALA B 414  ? 0.5617 0.4942 0.3894 -0.2598 -0.1276 0.1533  412  ALA B CB  
11762 N N   . THR B 415  ? 0.5773 0.5477 0.4038 -0.2715 -0.1199 0.1680  413  THR B N   
11763 C CA  . THR B 415  ? 0.5822 0.5560 0.4051 -0.2697 -0.1167 0.1702  413  THR B CA  
11764 C C   . THR B 415  ? 0.6405 0.5907 0.4510 -0.2729 -0.1247 0.1723  413  THR B C   
11765 O O   . THR B 415  ? 0.6197 0.5676 0.4257 -0.2702 -0.1230 0.1732  413  THR B O   
11766 C CB  . THR B 415  ? 0.5733 0.5757 0.4027 -0.2739 -0.1103 0.1750  413  THR B CB  
11767 O OG1 . THR B 415  ? 0.6580 0.6633 0.4865 -0.2839 -0.1152 0.1796  413  THR B OG1 
11768 C CG2 . THR B 415  ? 0.5112 0.5374 0.3527 -0.2685 -0.1016 0.1723  413  THR B CG2 
11769 N N   . ASP B 416  ? 0.6391 0.5717 0.4434 -0.2784 -0.1334 0.1729  414  ASP B N   
11770 C CA  . ASP B 416  ? 0.6266 0.5349 0.4187 -0.2804 -0.1413 0.1742  414  ASP B CA  
11771 C C   . ASP B 416  ? 0.6607 0.5477 0.4477 -0.2708 -0.1431 0.1686  414  ASP B C   
11772 O O   . ASP B 416  ? 0.7629 0.6367 0.5419 -0.2692 -0.1459 0.1693  414  ASP B O   
11773 C CB  . ASP B 416  ? 0.7205 0.6145 0.5067 -0.2879 -0.1504 0.1758  414  ASP B CB  
11774 C CG  . ASP B 416  ? 0.8166 0.7262 0.6036 -0.2987 -0.1509 0.1828  414  ASP B CG  
11775 O OD1 . ASP B 416  ? 0.7758 0.7075 0.5681 -0.3003 -0.1442 0.1863  414  ASP B OD1 
11776 O OD2 . ASP B 416  ? 0.9147 0.8142 0.6966 -0.3055 -0.1582 0.1849  414  ASP B OD2 
11777 N N   . VAL B 417  ? 0.6081 0.4918 0.3998 -0.2642 -0.1416 0.1630  415  VAL B N   
11778 C CA  . VAL B 417  ? 0.6471 0.5098 0.4341 -0.2549 -0.1439 0.1574  415  VAL B CA  
11779 C C   . VAL B 417  ? 0.6174 0.4920 0.4112 -0.2462 -0.1356 0.1543  415  VAL B C   
11780 O O   . VAL B 417  ? 0.6753 0.5340 0.4654 -0.2380 -0.1370 0.1499  415  VAL B O   
11781 C CB  . VAL B 417  ? 0.6451 0.4879 0.4295 -0.2531 -0.1507 0.1527  415  VAL B CB  
11782 C CG1 . VAL B 417  ? 0.6560 0.4837 0.4312 -0.2607 -0.1598 0.1557  415  VAL B CG1 
11783 C CG2 . VAL B 417  ? 0.6747 0.5326 0.4694 -0.2532 -0.1464 0.1505  415  VAL B CG2 
11784 N N   . VAL B 418  ? 0.5968 0.4984 0.4002 -0.2473 -0.1272 0.1561  416  VAL B N   
11785 C CA  . VAL B 418  ? 0.5805 0.4946 0.3894 -0.2391 -0.1191 0.1535  416  VAL B CA  
11786 C C   . VAL B 418  ? 0.6146 0.5557 0.4285 -0.2416 -0.1114 0.1578  416  VAL B C   
11787 O O   . VAL B 418  ? 0.5699 0.5262 0.3879 -0.2492 -0.1106 0.1617  416  VAL B O   
11788 C CB  . VAL B 418  ? 0.5519 0.4740 0.3719 -0.2314 -0.1155 0.1458  416  VAL B CB  
11789 C CG1 . VAL B 418  ? 0.5628 0.4601 0.3793 -0.2258 -0.1222 0.1392  416  VAL B CG1 
11790 C CG2 . VAL B 418  ? 0.5304 0.4711 0.3576 -0.2400 -0.1130 0.1499  416  VAL B CG2 
11791 N N   . PHE B 419  ? 0.5434 0.4908 0.3573 -0.2340 -0.1060 0.1562  417  PHE B N   
11792 C CA  . PHE B 419  ? 0.5579 0.5303 0.3757 -0.2348 -0.0982 0.1596  417  PHE B CA  
11793 C C   . PHE B 419  ? 0.5583 0.5512 0.3886 -0.2259 -0.0898 0.1536  417  PHE B C   
11794 O O   . PHE B 419  ? 0.5166 0.5072 0.3494 -0.2138 -0.0871 0.1461  417  PHE B O   
11795 C CB  . PHE B 419  ? 0.5422 0.5084 0.3520 -0.2311 -0.0979 0.1605  417  PHE B CB  
11796 C CG  . PHE B 419  ? 0.5078 0.4989 0.3215 -0.2298 -0.0896 0.1625  417  PHE B CG  
11797 C CD1 . PHE B 419  ? 0.5486 0.5581 0.3662 -0.2375 -0.0873 0.1673  417  PHE B CD1 
11798 C CD2 . PHE B 419  ? 0.5526 0.5490 0.3671 -0.2194 -0.0843 0.1580  417  PHE B CD2 
11799 C CE1 . PHE B 419  ? 0.5492 0.5815 0.3704 -0.2357 -0.0796 0.1688  417  PHE B CE1 
11800 C CE2 . PHE B 419  ? 0.5265 0.5449 0.3429 -0.2186 -0.0768 0.1604  417  PHE B CE2 
11801 C CZ  . PHE B 419  ? 0.5577 0.5941 0.3779 -0.2263 -0.0743 0.1654  417  PHE B CZ  
11802 N N   . PRO B 420  ? 0.5079 0.5209 0.3464 -0.2308 -0.0859 0.1560  418  PRO B N   
11803 C CA  . PRO B 420  ? 0.5079 0.5394 0.3586 -0.2216 -0.0785 0.1496  418  PRO B CA  
11804 C C   . PRO B 420  ? 0.5175 0.5679 0.3708 -0.2155 -0.0704 0.1490  418  PRO B C   
11805 O O   . PRO B 420  ? 0.4976 0.5591 0.3471 -0.2220 -0.0683 0.1560  418  PRO B O   
11806 C CB  . PRO B 420  ? 0.4679 0.5148 0.3254 -0.2304 -0.0777 0.1539  418  PRO B CB  
11807 C CG  . PRO B 420  ? 0.4704 0.5010 0.3205 -0.2413 -0.0864 0.1589  418  PRO B CG  
11808 C CD  . PRO B 420  ? 0.5213 0.5391 0.3609 -0.2421 -0.0894 0.1614  418  PRO B CD  
11809 N N   . GLN B 421  ? 0.4886 0.5429 0.3482 -0.2029 -0.0659 0.1407  419  GLN B N   
11810 C CA  . GLN B 421  ? 0.4479 0.5185 0.3102 -0.1953 -0.0583 0.1386  419  GLN B CA  
11811 C C   . GLN B 421  ? 0.4226 0.5105 0.2970 -0.1877 -0.0520 0.1330  419  GLN B C   
11812 O O   . GLN B 421  ? 0.3860 0.4653 0.2643 -0.1789 -0.0524 0.1253  419  GLN B O   
11813 C CB  . GLN B 421  ? 0.4508 0.5054 0.3069 -0.1866 -0.0598 0.1337  419  GLN B CB  
11814 C CG  . GLN B 421  ? 0.4378 0.4728 0.2817 -0.1933 -0.0668 0.1388  419  GLN B CG  
11815 C CD  . GLN B 421  ? 0.4696 0.4855 0.3081 -0.1844 -0.0699 0.1332  419  GLN B CD  
11816 O OE1 . GLN B 421  ? 0.4838 0.4967 0.3150 -0.1838 -0.0699 0.1352  419  GLN B OE1 
11817 N NE2 . GLN B 421  ? 0.4281 0.4308 0.2699 -0.1778 -0.0727 0.1263  419  GLN B NE2 
11818 N N   . PHE B 422  ? 0.4163 0.5287 0.2964 -0.1909 -0.0462 0.1367  420  PHE B N   
11819 C CA  . PHE B 422  ? 0.4381 0.5675 0.3297 -0.1854 -0.0410 0.1326  420  PHE B CA  
11820 C C   . PHE B 422  ? 0.3873 0.5292 0.2823 -0.1741 -0.0337 0.1274  420  PHE B C   
11821 O O   . PHE B 422  ? 0.4369 0.5975 0.3323 -0.1750 -0.0284 0.1309  420  PHE B O   
11822 C CB  . PHE B 422  ? 0.4339 0.5828 0.3304 -0.1953 -0.0393 0.1394  420  PHE B CB  
11823 C CG  . PHE B 422  ? 0.4604 0.5965 0.3535 -0.2066 -0.0468 0.1443  420  PHE B CG  
11824 C CD1 . PHE B 422  ? 0.4321 0.5557 0.3284 -0.2052 -0.0511 0.1400  420  PHE B CD1 
11825 C CD2 . PHE B 422  ? 0.4607 0.5968 0.3469 -0.2188 -0.0498 0.1533  420  PHE B CD2 
11826 C CE1 . PHE B 422  ? 0.4763 0.5871 0.3688 -0.2155 -0.0583 0.1441  420  PHE B CE1 
11827 C CE2 . PHE B 422  ? 0.5368 0.6596 0.4202 -0.2282 -0.0575 0.1565  420  PHE B CE2 
11828 C CZ  . PHE B 422  ? 0.4657 0.5758 0.3513 -0.2277 -0.0616 0.1530  420  PHE B CZ  
11829 N N   . ALA B 423  ? 0.4037 0.5356 0.3013 -0.1635 -0.0336 0.1191  421  ALA B N   
11830 C CA  . ALA B 423  ? 0.3909 0.5308 0.2911 -0.1522 -0.0277 0.1134  421  ALA B CA  
11831 C C   . ALA B 423  ? 0.4121 0.5701 0.3233 -0.1470 -0.0223 0.1100  421  ALA B C   
11832 O O   . ALA B 423  ? 0.4180 0.5699 0.3347 -0.1434 -0.0238 0.1053  421  ALA B O   
11833 C CB  . ALA B 423  ? 0.3766 0.4957 0.2735 -0.1440 -0.0308 0.1066  421  ALA B CB  
11834 N N   . THR B 424  ? 0.4485 0.6287 0.3628 -0.1459 -0.0159 0.1120  422  THR B N   
11835 C CA  . THR B 424  ? 0.3619 0.5597 0.2862 -0.1397 -0.0105 0.1086  422  THR B CA  
11836 C C   . THR B 424  ? 0.3891 0.6076 0.3140 -0.1359 -0.0034 0.1095  422  THR B C   
11837 O O   . THR B 424  ? 0.4298 0.6547 0.3489 -0.1418 -0.0025 0.1154  422  THR B O   
11838 C CB  . THR B 424  ? 0.4074 0.6145 0.3384 -0.1473 -0.0117 0.1124  422  THR B CB  
11839 O OG1 . THR B 424  ? 0.3335 0.5586 0.2742 -0.1407 -0.0063 0.1092  422  THR B OG1 
11840 C CG2 . THR B 424  ? 0.3846 0.6024 0.3125 -0.1593 -0.0122 0.1217  422  THR B CG2 
11841 N N   . HIS B 425  ? 0.3552 0.5836 0.2866 -0.1258 0.0015  0.1037  423  HIS B N   
11842 C CA  . HIS B 425  ? 0.3702 0.6202 0.3036 -0.1209 0.0086  0.1037  423  HIS B CA  
11843 C C   . HIS B 425  ? 0.4713 0.7436 0.4144 -0.1223 0.0123  0.1059  423  HIS B C   
11844 O O   . HIS B 425  ? 0.4708 0.7619 0.4173 -0.1164 0.0185  0.1047  423  HIS B O   
11845 C CB  . HIS B 425  ? 0.3580 0.6038 0.2915 -0.1081 0.0115  0.0956  423  HIS B CB  
11846 C CG  . HIS B 425  ? 0.4338 0.6607 0.3580 -0.1060 0.0085  0.0934  423  HIS B CG  
11847 N ND1 . HIS B 425  ? 0.4841 0.6982 0.4080 -0.0964 0.0080  0.0859  423  HIS B ND1 
11848 C CD2 . HIS B 425  ? 0.4401 0.6590 0.3552 -0.1123 0.0058  0.0980  423  HIS B CD2 
11849 C CE1 . HIS B 425  ? 0.4743 0.6738 0.3895 -0.0968 0.0050  0.0858  423  HIS B CE1 
11850 N NE2 . HIS B 425  ? 0.4113 0.6131 0.3209 -0.1062 0.0036  0.0931  423  HIS B NE2 
11851 N N   . ASN B 426  ? 0.4247 0.6952 0.3722 -0.1294 0.0086  0.1086  424  ASN B N   
11852 C CA  . ASN B 426  ? 0.4338 0.7236 0.3913 -0.1301 0.0114  0.1099  424  ASN B CA  
11853 C C   . ASN B 426  ? 0.3848 0.6913 0.3424 -0.1415 0.0120  0.1190  424  ASN B C   
11854 O O   . ASN B 426  ? 0.4694 0.7663 0.4232 -0.1523 0.0066  0.1242  424  ASN B O   
11855 C CB  . ASN B 426  ? 0.3896 0.6674 0.3521 -0.1305 0.0069  0.1069  424  ASN B CB  
11856 C CG  . ASN B 426  ? 0.3823 0.6792 0.3553 -0.1299 0.0095  0.1074  424  ASN B CG  
11857 O OD1 . ASN B 426  ? 0.4114 0.7286 0.3877 -0.1357 0.0121  0.1132  424  ASN B OD1 
11858 N ND2 . ASN B 426  ? 0.3714 0.6623 0.3498 -0.1230 0.0089  0.1014  424  ASN B ND2 
11859 N N   . ALA B 427  ? 0.4456 0.7755 0.4079 -0.1381 0.0178  0.1199  425  ALA B N   
11860 C CA  . ALA B 427  ? 0.4673 0.8095 0.4312 -0.1451 0.0170  0.1254  425  ALA B CA  
11861 C C   . ALA B 427  ? 0.4400 0.7833 0.4094 -0.1540 0.0122  0.1291  425  ALA B C   
11862 O O   . ALA B 427  ? 0.3662 0.7090 0.3332 -0.1639 0.0084  0.1349  425  ALA B O   
11863 C CB  . ALA B 427  ? 0.4310 0.7957 0.4004 -0.1370 0.0232  0.1234  425  ALA B CB  
11864 N N   . GLN B 428  ? 0.4220 0.7666 0.3986 -0.1507 0.0121  0.1259  426  GLN B N   
11865 C CA  . GLN B 428  ? 0.4032 0.7481 0.3847 -0.1587 0.0073  0.1290  426  GLN B CA  
11866 C C   . GLN B 428  ? 0.4467 0.7688 0.4208 -0.1686 0.0003  0.1320  426  GLN B C   
11867 O O   . GLN B 428  ? 0.4429 0.7632 0.4160 -0.1785 -0.0046 0.1370  426  GLN B O   
11868 C CB  . GLN B 428  ? 0.4216 0.7726 0.4120 -0.1520 0.0090  0.1244  426  GLN B CB  
11869 C CG  . GLN B 428  ? 0.4275 0.7856 0.4245 -0.1582 0.0053  0.1272  426  GLN B CG  
11870 C CD  . GLN B 428  ? 0.4643 0.8032 0.4575 -0.1681 -0.0019 0.1296  426  GLN B CD  
11871 O OE1 . GLN B 428  ? 0.4654 0.7867 0.4546 -0.1672 -0.0035 0.1270  426  GLN B OE1 
11872 N NE2 . GLN B 428  ? 0.4157 0.7573 0.4094 -0.1774 -0.0064 0.1346  426  GLN B NE2 
11873 N N   . THR B 429  ? 0.4376 0.7417 0.4062 -0.1658 -0.0004 0.1289  427  THR B N   
11874 C CA  . THR B 429  ? 0.4496 0.7293 0.4102 -0.1734 -0.0075 0.1307  427  THR B CA  
11875 C C   . THR B 429  ? 0.4462 0.7226 0.3988 -0.1822 -0.0101 0.1370  427  THR B C   
11876 O O   . THR B 429  ? 0.4401 0.7063 0.3895 -0.1920 -0.0165 0.1412  427  THR B O   
11877 C CB  . THR B 429  ? 0.4270 0.6844 0.3832 -0.1635 -0.0091 0.1227  427  THR B CB  
11878 O OG1 . THR B 429  ? 0.4517 0.7110 0.4156 -0.1540 -0.0070 0.1158  427  THR B OG1 
11879 C CG2 . THR B 429  ? 0.3917 0.6228 0.3405 -0.1697 -0.0170 0.1233  427  THR B CG2 
11880 N N   . LEU B 430  ? 0.4514 0.7349 0.4005 -0.1778 -0.0058 0.1369  428  LEU B N   
11881 C CA  . LEU B 430  ? 0.4669 0.7468 0.4084 -0.1847 -0.0082 0.1420  428  LEU B CA  
11882 C C   . LEU B 430  ? 0.4692 0.7620 0.4150 -0.1931 -0.0104 0.1473  428  LEU B C   
11883 O O   . LEU B 430  ? 0.4390 0.7210 0.3792 -0.2030 -0.0163 0.1521  428  LEU B O   
11884 C CB  . LEU B 430  ? 0.4759 0.7644 0.4142 -0.1772 -0.0022 0.1404  428  LEU B CB  
11885 C CG  . LEU B 430  ? 0.4490 0.7321 0.3780 -0.1816 -0.0035 0.1443  428  LEU B CG  
11886 C CD1 . LEU B 430  ? 0.4443 0.7356 0.3709 -0.1716 0.0030  0.1407  428  LEU B CD1 
11887 C CD2 . LEU B 430  ? 0.5113 0.8054 0.4417 -0.1906 -0.0053 0.1505  428  LEU B CD2 
11888 N N   . ALA B 431  ? 0.4701 0.7858 0.4253 -0.1890 -0.0058 0.1464  429  ALA B N   
11889 C CA  . ALA B 431  ? 0.4923 0.8220 0.4515 -0.1965 -0.0076 0.1516  429  ALA B CA  
11890 C C   . ALA B 431  ? 0.4946 0.8128 0.4541 -0.2056 -0.0149 0.1541  429  ALA B C   
11891 O O   . ALA B 431  ? 0.4584 0.7756 0.4151 -0.2155 -0.0195 0.1596  429  ALA B O   
11892 C CB  . ALA B 431  ? 0.4298 0.7851 0.3992 -0.1893 -0.0017 0.1496  429  ALA B CB  
11893 N N   . ALA B 432  ? 0.4812 0.7903 0.4436 -0.2024 -0.0161 0.1500  430  ALA B N   
11894 C CA  . ALA B 432  ? 0.4633 0.7597 0.4252 -0.2104 -0.0232 0.1517  430  ALA B CA  
11895 C C   . ALA B 432  ? 0.5203 0.7938 0.4712 -0.2193 -0.0301 0.1552  430  ALA B C   
11896 O O   . ALA B 432  ? 0.4809 0.7493 0.4296 -0.2288 -0.0361 0.1595  430  ALA B O   
11897 C CB  . ALA B 432  ? 0.4885 0.7774 0.4544 -0.2046 -0.0230 0.1462  430  ALA B CB  
11898 N N   . ILE B 433  ? 0.4716 0.7304 0.4151 -0.2162 -0.0295 0.1535  431  ILE B N   
11899 C CA  . ILE B 433  ? 0.5169 0.7523 0.4495 -0.2237 -0.0364 0.1565  431  ILE B CA  
11900 C C   . ILE B 433  ? 0.5061 0.7480 0.4347 -0.2305 -0.0374 0.1623  431  ILE B C   
11901 O O   . ILE B 433  ? 0.4964 0.7259 0.4190 -0.2399 -0.0443 0.1665  431  ILE B O   
11902 C CB  . ILE B 433  ? 0.4618 0.6794 0.3874 -0.2178 -0.0356 0.1530  431  ILE B CB  
11903 C CG1 . ILE B 433  ? 0.5380 0.7473 0.4672 -0.2125 -0.0356 0.1477  431  ILE B CG1 
11904 C CG2 . ILE B 433  ? 0.4618 0.6559 0.3756 -0.2248 -0.0426 0.1562  431  ILE B CG2 
11905 C CD1 . ILE B 433  ? 0.4911 0.6783 0.4130 -0.2062 -0.0374 0.1430  431  ILE B CD1 
11906 N N   . TYR B 434  ? 0.5234 0.7844 0.4548 -0.2256 -0.0307 0.1625  432  TYR B N   
11907 C CA  . TYR B 434  ? 0.5069 0.7762 0.4350 -0.2316 -0.0310 0.1679  432  TYR B CA  
11908 C C   . TYR B 434  ? 0.5641 0.8396 0.4947 -0.2416 -0.0357 0.1730  432  TYR B C   
11909 O O   . TYR B 434  ? 0.5750 0.8416 0.4989 -0.2507 -0.0411 0.1780  432  TYR B O   
11910 C CB  . TYR B 434  ? 0.5084 0.8009 0.4413 -0.2236 -0.0224 0.1665  432  TYR B CB  
11911 C CG  . TYR B 434  ? 0.5217 0.8279 0.4533 -0.2290 -0.0216 0.1720  432  TYR B CG  
11912 C CD1 . TYR B 434  ? 0.5351 0.8295 0.4569 -0.2339 -0.0242 0.1754  432  TYR B CD1 
11913 C CD2 . TYR B 434  ? 0.5246 0.8558 0.4647 -0.2290 -0.0181 0.1737  432  TYR B CD2 
11914 C CE1 . TYR B 434  ? 0.6036 0.9109 0.5241 -0.2390 -0.0232 0.1805  432  TYR B CE1 
11915 C CE2 . TYR B 434  ? 0.5069 0.8515 0.4458 -0.2340 -0.0172 0.1789  432  TYR B CE2 
11916 C CZ  . TYR B 434  ? 0.5381 0.8708 0.4673 -0.2392 -0.0196 0.1823  432  TYR B CZ  
11917 O OH  . TYR B 434  ? 0.6373 0.9835 0.5653 -0.2443 -0.0186 0.1875  432  TYR B OH  
11918 N N   . HIS B 435  ? 0.5363 0.8260 0.4762 -0.2400 -0.0343 0.1717  433  HIS B N   
11919 C CA  . HIS B 435  ? 0.5887 0.8853 0.5310 -0.2491 -0.0387 0.1766  433  HIS B CA  
11920 C C   . HIS B 435  ? 0.6113 0.8848 0.5483 -0.2565 -0.0473 0.1774  433  HIS B C   
11921 O O   . HIS B 435  ? 0.5737 0.8437 0.5070 -0.2665 -0.0531 0.1825  433  HIS B O   
11922 C CB  . HIS B 435  ? 0.5150 0.8358 0.4687 -0.2444 -0.0340 0.1751  433  HIS B CB  
11923 C CG  . HIS B 435  ? 0.5617 0.9066 0.5201 -0.2390 -0.0267 0.1756  433  HIS B CG  
11924 N ND1 . HIS B 435  ? 0.5608 0.9189 0.5185 -0.2453 -0.0268 0.1813  433  HIS B ND1 
11925 C CD2 . HIS B 435  ? 0.5298 0.8873 0.4931 -0.2276 -0.0191 0.1709  433  HIS B CD2 
11926 C CE1 . HIS B 435  ? 0.5159 0.8940 0.4780 -0.2380 -0.0195 0.1801  433  HIS B CE1 
11927 N NE2 . HIS B 435  ? 0.5320 0.9099 0.4975 -0.2270 -0.0148 0.1736  433  HIS B NE2 
11928 N N   . MET B 436  ? 0.5886 0.8460 0.5247 -0.2518 -0.0485 0.1724  434  MET B N   
11929 C CA  . MET B 436  ? 0.5655 0.7989 0.4956 -0.2580 -0.0568 0.1725  434  MET B CA  
11930 C C   . MET B 436  ? 0.6208 0.8345 0.5392 -0.2652 -0.0628 0.1763  434  MET B C   
11931 O O   . MET B 436  ? 0.6008 0.8010 0.5138 -0.2737 -0.0704 0.1793  434  MET B O   
11932 C CB  . MET B 436  ? 0.5853 0.8052 0.5162 -0.2506 -0.0562 0.1662  434  MET B CB  
11933 C CG  . MET B 436  ? 0.6116 0.8037 0.5351 -0.2553 -0.0646 0.1653  434  MET B CG  
11934 S SD  . MET B 436  ? 0.6428 0.8197 0.5671 -0.2459 -0.0630 0.1578  434  MET B SD  
11935 C CE  . MET B 436  ? 0.5358 0.7403 0.4743 -0.2380 -0.0550 0.1544  434  MET B CE  
11936 N N   . ALA B 437  ? 0.5874 0.7994 0.5014 -0.2618 -0.0596 0.1762  435  ALA B N   
11937 C CA  . ALA B 437  ? 0.6388 0.8311 0.5414 -0.2676 -0.0651 0.1794  435  ALA B CA  
11938 C C   . ALA B 437  ? 0.7021 0.9011 0.6023 -0.2780 -0.0687 0.1862  435  ALA B C   
11939 O O   . ALA B 437  ? 0.7058 0.8856 0.5965 -0.2851 -0.0759 0.1892  435  ALA B O   
11940 C CB  . ALA B 437  ? 0.6123 0.8034 0.5111 -0.2610 -0.0602 0.1777  435  ALA B CB  
11941 N N   . GLY B 438  ? 0.7443 0.9697 0.6525 -0.2787 -0.0642 0.1887  436  GLY B N   
11942 C CA  . GLY B 438  ? 0.7283 0.9616 0.6348 -0.2888 -0.0676 0.1954  436  GLY B CA  
11943 C C   . GLY B 438  ? 0.7857 1.0300 0.6898 -0.2898 -0.0639 0.1990  436  GLY B C   
11944 O O   . GLY B 438  ? 0.8340 1.0902 0.7414 -0.2815 -0.0565 0.1962  436  GLY B O   
11945 N N   . LYS B 439  ? 0.7400 0.9799 0.6377 -0.3000 -0.0693 0.2051  437  LYS B N   
11946 C CA  . LYS B 439  ? 0.7302 0.9822 0.6257 -0.3024 -0.0662 0.2094  437  LYS B CA  
11947 C C   . LYS B 439  ? 0.7616 0.9915 0.6450 -0.3067 -0.0711 0.2117  437  LYS B C   
11948 O O   . LYS B 439  ? 0.7665 1.0026 0.6475 -0.3045 -0.0669 0.2128  437  LYS B O   
11949 C CB  . LYS B 439  ? 0.7460 1.0175 0.6455 -0.3111 -0.0672 0.2156  437  LYS B CB  
11950 N N   . ASP B 440  ? 0.7692 0.9735 0.6447 -0.3125 -0.0798 0.2123  438  ASP B N   
11951 C CA  . ASP B 440  ? 0.7703 0.9529 0.6339 -0.3170 -0.0854 0.2148  438  ASP B CA  
11952 C C   . ASP B 440  ? 0.8300 0.9971 0.6895 -0.3077 -0.0832 0.2094  438  ASP B C   
11953 O O   . ASP B 440  ? 0.8689 1.0182 0.7269 -0.3039 -0.0862 0.2049  438  ASP B O   
11954 C CB  . ASP B 440  ? 0.8354 0.9961 0.6917 -0.3260 -0.0958 0.2172  438  ASP B CB  
11955 N N   . PHE B 441  ? 0.7217 0.8953 0.5791 -0.3039 -0.0781 0.2099  439  PHE B N   
11956 C CA  . PHE B 441  ? 0.7519 0.9138 0.6059 -0.2945 -0.0752 0.2049  439  PHE B CA  
11957 C C   . PHE B 441  ? 0.7934 0.9418 0.6365 -0.2967 -0.0777 0.2076  439  PHE B C   
11958 O O   . PHE B 441  ? 0.7610 0.9196 0.6022 -0.3026 -0.0772 0.2130  439  PHE B O   
11959 C CB  . PHE B 441  ? 0.6831 0.8675 0.5458 -0.2843 -0.0650 0.2009  439  PHE B CB  
11960 C CG  . PHE B 441  ? 0.7344 0.9066 0.5936 -0.2742 -0.0623 0.1954  439  PHE B CG  
11961 C CD1 . PHE B 441  ? 0.6527 0.8159 0.5149 -0.2680 -0.0624 0.1898  439  PHE B CD1 
11962 C CD2 . PHE B 441  ? 0.7027 0.8724 0.5554 -0.2710 -0.0597 0.1958  439  PHE B CD2 
11963 C CE1 . PHE B 441  ? 0.5985 0.7507 0.4573 -0.2590 -0.0601 0.1850  439  PHE B CE1 
11964 C CE2 . PHE B 441  ? 0.6731 0.8314 0.5221 -0.2618 -0.0576 0.1909  439  PHE B CE2 
11965 C CZ  . PHE B 441  ? 0.6875 0.8371 0.5395 -0.2558 -0.0579 0.1855  439  PHE B CZ  
11966 N N   . HIS B 442  ? 0.7595 0.8850 0.5956 -0.2915 -0.0803 0.2039  440  HIS B N   
11967 C CA  . HIS B 442  ? 0.7276 0.8404 0.5540 -0.2903 -0.0813 0.2050  440  HIS B CA  
11968 C C   . HIS B 442  ? 0.6981 0.8007 0.5230 -0.2791 -0.0784 0.1987  440  HIS B C   
11969 O O   . HIS B 442  ? 0.6608 0.7551 0.4887 -0.2748 -0.0795 0.1942  440  HIS B O   
11970 C CB  . HIS B 442  ? 0.7708 0.8586 0.5865 -0.2987 -0.0915 0.2086  440  HIS B CB  
11971 C CG  . HIS B 442  ? 0.7883 0.8522 0.6010 -0.2982 -0.0986 0.2052  440  HIS B CG  
11972 N ND1 . HIS B 442  ? 0.7641 0.8055 0.5707 -0.2914 -0.1012 0.2007  440  HIS B ND1 
11973 C CD2 . HIS B 442  ? 0.7579 0.8170 0.5729 -0.3034 -0.1038 0.2054  440  HIS B CD2 
11974 C CE1 . HIS B 442  ? 0.7746 0.7983 0.5797 -0.2923 -0.1075 0.1982  440  HIS B CE1 
11975 N NE2 . HIS B 442  ? 0.8332 0.8669 0.6431 -0.2996 -0.1092 0.2010  440  HIS B NE2 
11976 N N   . VAL B 443  ? 0.6995 0.8032 0.5198 -0.2743 -0.0747 0.1985  441  VAL B N   
11977 C CA  . VAL B 443  ? 0.6367 0.7293 0.4542 -0.2639 -0.0727 0.1928  441  VAL B CA  
11978 C C   . VAL B 443  ? 0.6734 0.7352 0.4832 -0.2647 -0.0816 0.1912  441  VAL B C   
11979 O O   . VAL B 443  ? 0.6767 0.7227 0.4788 -0.2719 -0.0889 0.1949  441  VAL B O   
11980 C CB  . VAL B 443  ? 0.7199 0.8174 0.5321 -0.2594 -0.0682 0.1933  441  VAL B CB  
11981 C CG1 . VAL B 443  ? 0.6255 0.7075 0.4327 -0.2495 -0.0680 0.1879  441  VAL B CG1 
11982 C CG2 . VAL B 443  ? 0.6966 0.8248 0.5171 -0.2564 -0.0588 0.1935  441  VAL B CG2 
11983 N N   . GLY B 444  ? 0.6447 0.6980 0.4566 -0.2573 -0.0813 0.1856  442  GLY B N   
11984 C CA  . GLY B 444  ? 0.6134 0.6392 0.4195 -0.2574 -0.0894 0.1834  442  GLY B CA  
11985 C C   . GLY B 444  ? 0.6504 0.6747 0.4623 -0.2609 -0.0924 0.1823  442  GLY B C   
11986 O O   . GLY B 444  ? 0.6222 0.6251 0.4305 -0.2591 -0.0982 0.1792  442  GLY B O   
11987 N N   . LYS B 445  ? 0.6248 0.6714 0.4453 -0.2656 -0.0888 0.1847  443  LYS B N   
11988 C CA  . LYS B 445  ? 0.6363 0.6842 0.4632 -0.2682 -0.0910 0.1834  443  LYS B CA  
11989 C C   . LYS B 445  ? 0.6210 0.6731 0.4546 -0.2589 -0.0860 0.1773  443  LYS B C   
11990 O O   . LYS B 445  ? 0.6148 0.6492 0.4469 -0.2567 -0.0903 0.1738  443  LYS B O   
11991 C CB  . LYS B 445  ? 0.6048 0.6765 0.4389 -0.2755 -0.0885 0.1878  443  LYS B CB  
11992 N N   . TYR B 446  ? 0.5879 0.6633 0.4288 -0.2532 -0.0770 0.1760  444  TYR B N   
11993 C CA  . TYR B 446  ? 0.5645 0.6442 0.4106 -0.2433 -0.0717 0.1703  444  TYR B CA  
11994 C C   . TYR B 446  ? 0.5952 0.6931 0.4431 -0.2366 -0.0633 0.1695  444  TYR B C   
11995 O O   . TYR B 446  ? 0.5427 0.6492 0.3881 -0.2398 -0.0618 0.1733  444  TYR B O   
11996 C CB  . TYR B 446  ? 0.4990 0.5913 0.3557 -0.2437 -0.0698 0.1685  444  TYR B CB  
11997 C CG  . TYR B 446  ? 0.5555 0.6772 0.4214 -0.2459 -0.0638 0.1710  444  TYR B CG  
11998 C CD1 . TYR B 446  ? 0.5673 0.6952 0.4343 -0.2555 -0.0673 0.1760  444  TYR B CD1 
11999 C CD2 . TYR B 446  ? 0.5206 0.6637 0.3939 -0.2378 -0.0549 0.1682  444  TYR B CD2 
12000 C CE1 . TYR B 446  ? 0.5810 0.7360 0.4565 -0.2571 -0.0621 0.1783  444  TYR B CE1 
12001 C CE2 . TYR B 446  ? 0.5334 0.7033 0.4152 -0.2389 -0.0497 0.1701  444  TYR B CE2 
12002 C CZ  . TYR B 446  ? 0.5897 0.7656 0.4727 -0.2486 -0.0533 0.1753  444  TYR B CZ  
12003 O OH  . TYR B 446  ? 0.5984 0.8011 0.4898 -0.2495 -0.0483 0.1773  444  TYR B OH  
12004 N N   . GLU B 447  ? 0.5187 0.6221 0.3707 -0.2271 -0.0579 0.1643  445  GLU B N   
12005 C CA  . GLU B 447  ? 0.4620 0.5829 0.3159 -0.2196 -0.0498 0.1626  445  GLU B CA  
12006 C C   . GLU B 447  ? 0.4523 0.5855 0.3147 -0.2113 -0.0438 0.1573  445  GLU B C   
12007 O O   . GLU B 447  ? 0.4793 0.6035 0.3453 -0.2097 -0.0464 0.1539  445  GLU B O   
12008 C CB  . GLU B 447  ? 0.4941 0.5996 0.3374 -0.2151 -0.0512 0.1616  445  GLU B CB  
12009 C CG  . GLU B 447  ? 0.4665 0.5553 0.3084 -0.2058 -0.0528 0.1547  445  GLU B CG  
12010 C CD  . GLU B 447  ? 0.5138 0.5879 0.3470 -0.1997 -0.0546 0.1522  445  GLU B CD  
12011 O OE1 . GLU B 447  ? 0.4790 0.5529 0.3032 -0.2053 -0.0553 0.1584  445  GLU B OE1 
12012 O OE2 . GLU B 447  ? 0.4596 0.5225 0.2949 -0.1894 -0.0554 0.1441  445  GLU B OE2 
12013 N N   . PHE B 448  ? 0.4812 0.6346 0.3476 -0.2047 -0.0360 0.1555  446  PHE B N   
12014 C CA  . PHE B 448  ? 0.4419 0.6060 0.3162 -0.1941 -0.0302 0.1488  446  PHE B CA  
12015 C C   . PHE B 448  ? 0.4111 0.5635 0.2815 -0.1826 -0.0294 0.1417  446  PHE B C   
12016 O O   . PHE B 448  ? 0.4436 0.5860 0.3045 -0.1837 -0.0315 0.1438  446  PHE B O   
12017 C CB  . PHE B 448  ? 0.4655 0.6591 0.3479 -0.1925 -0.0223 0.1498  446  PHE B CB  
12018 C CG  . PHE B 448  ? 0.4244 0.6307 0.3158 -0.1993 -0.0231 0.1527  446  PHE B CG  
12019 C CD1 . PHE B 448  ? 0.4452 0.6541 0.3445 -0.1977 -0.0229 0.1499  446  PHE B CD1 
12020 C CD2 . PHE B 448  ? 0.4819 0.6975 0.3735 -0.2072 -0.0242 0.1582  446  PHE B CD2 
12021 C CE1 . PHE B 448  ? 0.4732 0.6936 0.3803 -0.2038 -0.0241 0.1525  446  PHE B CE1 
12022 C CE2 . PHE B 448  ? 0.5931 0.8203 0.4924 -0.2133 -0.0254 0.1609  446  PHE B CE2 
12023 C CZ  . PHE B 448  ? 0.5087 0.7382 0.4157 -0.2115 -0.0255 0.1579  446  PHE B CZ  
12024 N N   . GLN B 449  ? 0.4389 0.5931 0.3169 -0.1716 -0.0264 0.1333  447  GLN B N   
12025 C CA  . GLN B 449  ? 0.4189 0.5644 0.2941 -0.1605 -0.0251 0.1264  447  GLN B CA  
12026 C C   . GLN B 449  ? 0.4422 0.6042 0.3261 -0.1501 -0.0180 0.1202  447  GLN B C   
12027 O O   . GLN B 449  ? 0.4425 0.6166 0.3354 -0.1498 -0.0156 0.1193  447  GLN B O   
12028 C CB  . GLN B 449  ? 0.3734 0.4930 0.2463 -0.1569 -0.0317 0.1214  447  GLN B CB  
12029 C CG  . GLN B 449  ? 0.4403 0.5405 0.3036 -0.1656 -0.0393 0.1266  447  GLN B CG  
12030 C CD  . GLN B 449  ? 0.4500 0.5259 0.3094 -0.1597 -0.0448 0.1210  447  GLN B CD  
12031 O OE1 . GLN B 449  ? 0.4065 0.4798 0.2714 -0.1499 -0.0433 0.1133  447  GLN B OE1 
12032 N NE2 . GLN B 449  ? 0.4425 0.5004 0.2922 -0.1655 -0.0514 0.1250  447  GLN B NE2 
12033 N N   . CYS B 450  ? 0.4020 0.5639 0.2827 -0.1416 -0.0150 0.1159  448  CYS B N   
12034 C CA  . CYS B 450  ? 0.3917 0.5667 0.2792 -0.1309 -0.0088 0.1095  448  CYS B CA  
12035 C C   . CYS B 450  ? 0.4217 0.5839 0.3047 -0.1215 -0.0092 0.1031  448  CYS B C   
12036 O O   . CYS B 450  ? 0.3664 0.5130 0.2409 -0.1234 -0.0136 0.1044  448  CYS B O   
12037 C CB  . CYS B 450  ? 0.4220 0.6225 0.3110 -0.1318 -0.0018 0.1132  448  CYS B CB  
12038 S SG  . CYS B 450  ? 0.4788 0.6827 0.3565 -0.1310 0.0007  0.1157  448  CYS B SG  
12039 N N   . LEU B 451  ? 0.4066 0.5757 0.2953 -0.1113 -0.0049 0.0963  449  LEU B N   
12040 C CA  . LEU B 451  ? 0.3974 0.5559 0.2827 -0.1020 -0.0050 0.0899  449  LEU B CA  
12041 C C   . LEU B 451  ? 0.4307 0.6010 0.3105 -0.0988 -0.0002 0.0905  449  LEU B C   
12042 O O   . LEU B 451  ? 0.4340 0.6244 0.3163 -0.0993 0.0053  0.0928  449  LEU B O   
12043 C CB  . LEU B 451  ? 0.4436 0.6013 0.3375 -0.0927 -0.0034 0.0820  449  LEU B CB  
12044 N N   . HIS B 452  ? 0.4227 0.5804 0.2948 -0.0954 -0.0024 0.0882  450  HIS B N   
12045 C CA  . HIS B 452  ? 0.5109 0.6775 0.3767 -0.0914 0.0017  0.0879  450  HIS B CA  
12046 C C   . HIS B 452  ? 0.4256 0.6074 0.2975 -0.0824 0.0080  0.0824  450  HIS B C   
12047 O O   . HIS B 452  ? 0.4354 0.6129 0.3142 -0.0759 0.0080  0.0763  450  HIS B O   
12048 C CB  . HIS B 452  ? 0.4532 0.6022 0.3111 -0.0875 -0.0022 0.0847  450  HIS B CB  
12049 C CG  . HIS B 452  ? 0.4658 0.6223 0.3179 -0.0813 0.0019  0.0823  450  HIS B CG  
12050 N ND1 . HIS B 452  ? 0.5230 0.6885 0.3668 -0.0857 0.0039  0.0878  450  HIS B ND1 
12051 C CD2 . HIS B 452  ? 0.5251 0.6817 0.3783 -0.0712 0.0043  0.0750  450  HIS B CD2 
12052 C CE1 . HIS B 452  ? 0.5297 0.7003 0.3695 -0.0781 0.0074  0.0837  450  HIS B CE1 
12053 N NE2 . HIS B 452  ? 0.4805 0.6455 0.3257 -0.0693 0.0076  0.0759  450  HIS B NE2 
12054 N N   . GLY B 453  ? 0.4776 0.6771 0.3467 -0.0819 0.0134  0.0848  451  GLY B N   
12055 C CA  . GLY B 453  ? 0.4775 0.6921 0.3512 -0.0729 0.0197  0.0799  451  GLY B CA  
12056 C C   . GLY B 453  ? 0.5355 0.7661 0.4195 -0.0738 0.0230  0.0809  451  GLY B C   
12057 O O   . GLY B 453  ? 0.6127 0.8635 0.4981 -0.0727 0.0287  0.0827  451  GLY B O   
12058 N N   . MET B 454  ? 0.4871 0.7092 0.3781 -0.0760 0.0196  0.0801  452  MET B N   
12059 C CA  . MET B 454  ? 0.5201 0.7561 0.4213 -0.0763 0.0223  0.0805  452  MET B CA  
12060 C C   . MET B 454  ? 0.4988 0.7475 0.4010 -0.0872 0.0226  0.0891  452  MET B C   
12061 O O   . MET B 454  ? 0.5510 0.8204 0.4588 -0.0872 0.0274  0.0910  452  MET B O   
12062 C CB  . MET B 454  ? 0.5380 0.7598 0.4458 -0.0744 0.0183  0.0763  452  MET B CB  
12063 C CG  . MET B 454  ? 0.5522 0.7867 0.4707 -0.0727 0.0209  0.0752  452  MET B CG  
12064 S SD  . MET B 454  ? 0.7859 1.0316 0.7083 -0.0594 0.0270  0.0679  452  MET B SD  
12065 C CE  . MET B 454  ? 0.7144 0.9371 0.6315 -0.0521 0.0235  0.0607  452  MET B CE  
12066 N N   . GLY B 455  ? 0.4947 0.7315 0.3916 -0.0965 0.0175  0.0944  453  GLY B N   
12067 C CA  . GLY B 455  ? 0.4965 0.7415 0.3949 -0.1079 0.0163  0.1024  453  GLY B CA  
12068 C C   . GLY B 455  ? 0.5661 0.8271 0.4592 -0.1140 0.0197  0.1095  453  GLY B C   
12069 O O   . GLY B 455  ? 0.5288 0.8015 0.4248 -0.1231 0.0199  0.1162  453  GLY B O   
12070 N N   . GLU B 456  ? 0.5739 0.8363 0.4592 -0.1096 0.0222  0.1083  454  GLU B N   
12071 C CA  . GLU B 456  ? 0.6028 0.8797 0.4817 -0.1155 0.0253  0.1152  454  GLU B CA  
12072 C C   . GLU B 456  ? 0.5794 0.8809 0.4679 -0.1138 0.0309  0.1158  454  GLU B C   
12073 O O   . GLU B 456  ? 0.5863 0.8964 0.4765 -0.1213 0.0305  0.1214  454  GLU B O   
12074 C CB  . GLU B 456  ? 0.6409 0.9128 0.5097 -0.1095 0.0266  0.1125  454  GLU B CB  
12075 C CG  . GLU B 456  ? 0.6732 0.9199 0.5334 -0.1119 0.0199  0.1124  454  GLU B CG  
12076 C CD  . GLU B 456  ? 0.6412 0.8704 0.5039 -0.1025 0.0171  0.1035  454  GLU B CD  
12077 O OE1 . GLU B 456  ? 0.6486 0.8802 0.5208 -0.0981 0.0181  0.0992  454  GLU B OE1 
12078 O OE2 . GLU B 456  ? 0.5992 0.8128 0.4541 -0.0996 0.0140  0.1010  454  GLU B OE2 
12079 N N   . PRO B 457  ? 0.5258 0.8386 0.4209 -0.1038 0.0357  0.1098  455  PRO B N   
12080 C CA  . PRO B 457  ? 0.5939 0.9292 0.4988 -0.1019 0.0402  0.1102  455  PRO B CA  
12081 C C   . PRO B 457  ? 0.5877 0.9292 0.5005 -0.1118 0.0375  0.1159  455  PRO B C   
12082 O O   . PRO B 457  ? 0.5817 0.9404 0.4997 -0.1141 0.0397  0.1189  455  PRO B O   
12083 C CB  . PRO B 457  ? 0.5873 0.9278 0.4980 -0.0901 0.0440  0.1027  455  PRO B CB  
12084 C CG  . PRO B 457  ? 0.5488 0.8738 0.4501 -0.0839 0.0434  0.0979  455  PRO B CG  
12085 C CD  . PRO B 457  ? 0.5736 0.8786 0.4679 -0.0929 0.0369  0.1019  455  PRO B CD  
12086 N N   . LEU B 458  ? 0.5612 0.8889 0.4745 -0.1178 0.0326  0.1175  456  LEU B N   
12087 C CA  . LEU B 458  ? 0.5234 0.8550 0.4434 -0.1275 0.0293  0.1226  456  LEU B CA  
12088 C C   . LEU B 458  ? 0.5261 0.8503 0.4399 -0.1392 0.0247  0.1298  456  LEU B C   
12089 O O   . LEU B 458  ? 0.4840 0.8203 0.4022 -0.1458 0.0243  0.1346  456  LEU B O   
12090 C CB  . LEU B 458  ? 0.5098 0.8298 0.4333 -0.1285 0.0259  0.1209  456  LEU B CB  
12091 C CG  . LEU B 458  ? 0.4907 0.8108 0.4198 -0.1391 0.0214  0.1260  456  LEU B CG  
12092 C CD1 . LEU B 458  ? 0.4550 0.7983 0.3946 -0.1385 0.0246  0.1270  456  LEU B CD1 
12093 C CD2 . LEU B 458  ? 0.4914 0.7975 0.4223 -0.1399 0.0178  0.1240  456  LEU B CD2 
12094 N N   . TYR B 459  ? 0.5288 0.8331 0.4321 -0.1416 0.0209  0.1305  457  TYR B N   
12095 C CA  . TYR B 459  ? 0.5350 0.8287 0.4325 -0.1532 0.0153  0.1372  457  TYR B CA  
12096 C C   . TYR B 459  ? 0.5483 0.8505 0.4410 -0.1555 0.0172  0.1408  457  TYR B C   
12097 O O   . TYR B 459  ? 0.5429 0.8384 0.4311 -0.1653 0.0128  0.1467  457  TYR B O   
12098 C CB  . TYR B 459  ? 0.4851 0.7527 0.3735 -0.1552 0.0095  0.1368  457  TYR B CB  
12099 C CG  . TYR B 459  ? 0.4854 0.7439 0.3786 -0.1582 0.0057  0.1363  457  TYR B CG  
12100 C CD1 . TYR B 459  ? 0.4752 0.7269 0.3692 -0.1691 -0.0001 0.1416  457  TYR B CD1 
12101 C CD2 . TYR B 459  ? 0.5023 0.7589 0.4005 -0.1492 0.0074  0.1296  457  TYR B CD2 
12102 C CE1 . TYR B 459  ? 0.4902 0.7338 0.3885 -0.1718 -0.0037 0.1410  457  TYR B CE1 
12103 C CE2 . TYR B 459  ? 0.4484 0.6953 0.3528 -0.1505 0.0033  0.1275  457  TYR B CE2 
12104 C CZ  . TYR B 459  ? 0.4494 0.6905 0.3529 -0.1624 -0.0019 0.1338  457  TYR B CZ  
12105 O OH  . TYR B 459  ? 0.4771 0.7084 0.3861 -0.1639 -0.0062 0.1318  457  TYR B OH  
12106 N N   . GLU B 460  ? 0.4915 0.8081 0.3848 -0.1468 0.0235  0.1374  458  GLU B N   
12107 C CA  . GLU B 460  ? 0.6465 0.9744 0.5368 -0.1496 0.0256  0.1413  458  GLU B CA  
12108 C C   . GLU B 460  ? 0.6349 0.9812 0.5340 -0.1561 0.0261  0.1460  458  GLU B C   
12109 O O   . GLU B 460  ? 0.6387 0.9936 0.5354 -0.1611 0.0267  0.1506  458  GLU B O   
12110 C CB  . GLU B 460  ? 0.6726 1.0106 0.5607 -0.1382 0.0320  0.1361  458  GLU B CB  
12111 C CG  . GLU B 460  ? 0.6582 1.0092 0.5553 -0.1278 0.0370  0.1299  458  GLU B CG  
12112 C CD  . GLU B 460  ? 0.7252 1.0794 0.6177 -0.1159 0.0420  0.1238  458  GLU B CD  
12113 O OE1 . GLU B 460  ? 0.7238 1.0678 0.6058 -0.1158 0.0412  0.1240  458  GLU B OE1 
12114 O OE2 . GLU B 460  ? 0.7726 1.1390 0.6718 -0.1067 0.0465  0.1186  458  GLU B OE2 
12115 N N   . GLU B 461  ? 0.6038 0.9560 0.5126 -0.1564 0.0256  0.1450  459  GLU B N   
12116 C CA  . GLU B 461  ? 0.6567 1.0246 0.5738 -0.1632 0.0249  0.1495  459  GLU B CA  
12117 C C   . GLU B 461  ? 0.6645 1.0191 0.5798 -0.1760 0.0175  0.1553  459  GLU B C   
12118 O O   . GLU B 461  ? 0.6332 0.9986 0.5550 -0.1827 0.0158  0.1592  459  GLU B O   
12119 C CB  . GLU B 461  ? 0.5703 0.9520 0.4987 -0.1564 0.0281  0.1453  459  GLU B CB  
12120 C CG  . GLU B 461  ? 0.5521 0.9410 0.4816 -0.1424 0.0344  0.1381  459  GLU B CG  
12121 C CD  . GLU B 461  ? 0.7202 1.1264 0.6487 -0.1382 0.0397  0.1384  459  GLU B CD  
12122 O OE1 . GLU B 461  ? 0.6631 1.0797 0.5922 -0.1458 0.0390  0.1443  459  GLU B OE1 
12123 O OE2 . GLU B 461  ? 0.7423 1.1518 0.6692 -0.1271 0.0444  0.1327  459  GLU B OE2 
12124 N N   . VAL B 462  ? 0.6327 0.9638 0.5391 -0.1794 0.0127  0.1558  460  VAL B N   
12125 C CA  . VAL B 462  ? 0.6226 0.9373 0.5265 -0.1903 0.0050  0.1602  460  VAL B CA  
12126 C C   . VAL B 462  ? 0.6302 0.9316 0.5233 -0.1978 0.0008  0.1652  460  VAL B C   
12127 O O   . VAL B 462  ? 0.5396 0.8391 0.4318 -0.2084 -0.0039 0.1710  460  VAL B O   
12128 C CB  . VAL B 462  ? 0.5504 0.8463 0.4537 -0.1876 0.0018  0.1561  460  VAL B CB  
12129 C CG1 . VAL B 462  ? 0.5228 0.8012 0.4233 -0.1986 -0.0064 0.1604  460  VAL B CG1 
12130 C CG2 . VAL B 462  ? 0.5232 0.8321 0.4370 -0.1798 0.0060  0.1511  460  VAL B CG2 
12131 N N   . VAL B 463  ? 0.5658 0.8572 0.4503 -0.1925 0.0021  0.1629  461  VAL B N   
12132 C CA  . VAL B 463  ? 0.5960 0.8721 0.4695 -0.1986 -0.0022 0.1670  461  VAL B CA  
12133 C C   . VAL B 463  ? 0.6196 0.9124 0.4925 -0.2025 0.0006  0.1717  461  VAL B C   
12134 O O   . VAL B 463  ? 0.6374 0.9495 0.5140 -0.1956 0.0074  0.1694  461  VAL B O   
12135 C CB  . VAL B 463  ? 0.4924 0.7529 0.3568 -0.1910 -0.0018 0.1628  461  VAL B CB  
12136 C CG1 . VAL B 463  ? 0.6355 0.8789 0.4885 -0.1973 -0.0070 0.1671  461  VAL B CG1 
12137 C CG2 . VAL B 463  ? 0.5612 0.8072 0.4268 -0.1864 -0.0040 0.1579  461  VAL B CG2 
12138 N N   . GLY B 464  ? 0.6044 0.8897 0.4725 -0.2134 -0.0048 0.1781  462  GLY B N   
12139 C CA  . GLY B 464  ? 0.6741 0.9712 0.5391 -0.2178 -0.0030 0.1830  462  GLY B CA  
12140 C C   . GLY B 464  ? 0.7495 1.0617 0.6214 -0.2270 -0.0044 0.1885  462  GLY B C   
12141 O O   . GLY B 464  ? 0.7201 1.0421 0.6015 -0.2269 -0.0040 0.1874  462  GLY B O   
12142 N N   . ARG B 465  ? 0.7604 1.0751 0.6272 -0.2351 -0.0062 0.1947  463  ARG B N   
12143 C CA  . ARG B 465  ? 0.8089 1.1393 0.6815 -0.2441 -0.0074 0.2004  463  ARG B CA  
12144 C C   . ARG B 465  ? 0.8346 1.1938 0.7178 -0.2381 -0.0001 0.1985  463  ARG B C   
12145 O O   . ARG B 465  ? 0.8133 1.1863 0.7038 -0.2438 -0.0011 0.2018  463  ARG B O   
12146 C CB  . ARG B 465  ? 0.8002 1.1293 0.6648 -0.2529 -0.0098 0.2072  463  ARG B CB  
12147 N N   . GLY B 466  ? 0.8066 1.1748 0.6905 -0.2265 0.0070  0.1932  464  GLY B N   
12148 C CA  . GLY B 466  ? 0.7632 1.1572 0.6568 -0.2193 0.0138  0.1905  464  GLY B CA  
12149 C C   . GLY B 466  ? 0.8666 1.2635 0.7695 -0.2133 0.0147  0.1854  464  GLY B C   
12150 O O   . GLY B 466  ? 0.8264 1.2447 0.7383 -0.2087 0.0193  0.1839  464  GLY B O   
12151 N N   . LYS B 467  ? 0.8354 1.2112 0.7362 -0.2131 0.0105  0.1827  465  LYS B N   
12152 C CA  . LYS B 467  ? 0.8013 1.1781 0.7102 -0.2074 0.0111  0.1777  465  LYS B CA  
12153 C C   . LYS B 467  ? 0.8358 1.2036 0.7476 -0.2171 0.0042  0.1810  465  LYS B C   
12154 O O   . LYS B 467  ? 0.8457 1.2243 0.7610 -0.2254 0.0020  0.1863  465  LYS B O   
12155 C CB  . LYS B 467  ? 0.7861 1.1472 0.6909 -0.1980 0.0124  0.1711  465  LYS B CB  
12156 C CG  . LYS B 467  ? 0.7991 1.1701 0.7020 -0.1869 0.0195  0.1666  465  LYS B CG  
12157 C CD  . LYS B 467  ? 0.8037 1.2006 0.7169 -0.1802 0.0256  0.1644  465  LYS B CD  
12158 C CE  . LYS B 467  ? 0.7940 1.1992 0.7049 -0.1682 0.0325  0.1591  465  LYS B CE  
12159 N NZ  . LYS B 467  ? 0.7167 1.1426 0.6376 -0.1593 0.0379  0.1550  465  LYS B NZ  
12160 N N   . LEU B 468  ? 0.6151 0.9632 0.5253 -0.2159 0.0005  0.1777  466  LEU B N   
12161 C CA  . LEU B 468  ? 0.5544 0.8901 0.4654 -0.2249 -0.0068 0.1804  466  LEU B CA  
12162 C C   . LEU B 468  ? 0.6400 0.9526 0.5402 -0.2339 -0.0139 0.1846  466  LEU B C   
12163 O O   . LEU B 468  ? 0.6302 0.9306 0.5296 -0.2421 -0.0207 0.1873  466  LEU B O   
12164 C CB  . LEU B 468  ? 0.6193 0.9464 0.5347 -0.2190 -0.0072 0.1748  466  LEU B CB  
12165 N N   . ASP B 469  ? 0.6225 0.9284 0.5141 -0.2322 -0.0127 0.1851  467  ASP B N   
12166 C CA  . ASP B 469  ? 0.6609 0.9443 0.5415 -0.2398 -0.0194 0.1889  467  ASP B CA  
12167 C C   . ASP B 469  ? 0.5694 0.8272 0.4464 -0.2400 -0.0253 0.1862  467  ASP B C   
12168 O O   . ASP B 469  ? 0.6658 0.9065 0.5379 -0.2487 -0.0329 0.1896  467  ASP B O   
12169 C CB  . ASP B 469  ? 0.6164 0.9040 0.4960 -0.2522 -0.0239 0.1964  467  ASP B CB  
12170 N N   . ARG B 470  ? 0.5983 0.8531 0.4774 -0.2300 -0.0220 0.1798  468  ARG B N   
12171 C CA  . ARG B 470  ? 0.6188 0.8501 0.4944 -0.2289 -0.0269 0.1768  468  ARG B CA  
12172 C C   . ARG B 470  ? 0.5151 0.7363 0.3843 -0.2195 -0.0243 0.1722  468  ARG B C   
12173 O O   . ARG B 470  ? 0.5362 0.7725 0.4090 -0.2105 -0.0171 0.1684  468  ARG B O   
12174 C CB  . ARG B 470  ? 0.6052 0.8421 0.4905 -0.2267 -0.0264 0.1736  468  ARG B CB  
12175 C CG  . ARG B 470  ? 0.5360 0.7817 0.4272 -0.2361 -0.0298 0.1780  468  ARG B CG  
12176 C CD  . ARG B 470  ? 0.5761 0.8006 0.4591 -0.2470 -0.0390 0.1826  468  ARG B CD  
12177 N NE  . ARG B 470  ? 0.6184 0.8498 0.5061 -0.2560 -0.0429 0.1867  468  ARG B NE  
12178 C CZ  . ARG B 470  ? 0.6346 0.8786 0.5225 -0.2635 -0.0435 0.1924  468  ARG B CZ  
12179 N NH1 . ARG B 470  ? 0.6313 0.8830 0.5154 -0.2633 -0.0402 0.1949  468  ARG B NH1 
12180 N NH2 . ARG B 470  ? 0.5850 0.8337 0.4766 -0.2715 -0.0475 0.1958  468  ARG B NH2 
12181 N N   . PRO B 471  ? 0.5709 0.7670 0.4305 -0.2209 -0.0301 0.1722  469  PRO B N   
12182 C CA  . PRO B 471  ? 0.5415 0.7277 0.3942 -0.2123 -0.0282 0.1682  469  PRO B CA  
12183 C C   . PRO B 471  ? 0.5621 0.7449 0.4185 -0.2034 -0.0261 0.1617  469  PRO B C   
12184 O O   . PRO B 471  ? 0.5419 0.7220 0.4040 -0.2049 -0.0282 0.1606  469  PRO B O   
12185 C CB  . PRO B 471  ? 0.5738 0.7337 0.4152 -0.2178 -0.0363 0.1710  469  PRO B CB  
12186 C CG  . PRO B 471  ? 0.5932 0.7441 0.4367 -0.2268 -0.0428 0.1739  469  PRO B CG  
12187 C CD  . PRO B 471  ? 0.5667 0.7421 0.4204 -0.2307 -0.0390 0.1762  469  PRO B CD  
12188 N N   . CYS B 472  ? 0.5148 0.6985 0.3678 -0.1939 -0.0219 0.1574  470  CYS B N   
12189 C CA  . CYS B 472  ? 0.5406 0.7205 0.3957 -0.1848 -0.0199 0.1512  470  CYS B CA  
12190 C C   . CYS B 472  ? 0.5336 0.6943 0.3779 -0.1797 -0.0226 0.1487  470  CYS B C   
12191 O O   . CYS B 472  ? 0.5082 0.6710 0.3464 -0.1775 -0.0207 0.1492  470  CYS B O   
12192 C CB  . CYS B 472  ? 0.4633 0.6672 0.3267 -0.1763 -0.0113 0.1471  470  CYS B CB  
12193 S SG  . CYS B 472  ? 0.5091 0.7077 0.3786 -0.1641 -0.0096 0.1375  470  CYS B SG  
12194 N N   . ARG B 473  ? 0.4714 0.6121 0.3173 -0.1752 -0.0276 0.1429  471  ARG B N   
12195 C CA  . ARG B 473  ? 0.4846 0.6063 0.3248 -0.1674 -0.0306 0.1374  471  ARG B CA  
12196 C C   . ARG B 473  ? 0.4866 0.6138 0.3342 -0.1543 -0.0259 0.1280  471  ARG B C   
12197 O O   . ARG B 473  ? 0.4089 0.5389 0.2658 -0.1511 -0.0249 0.1238  471  ARG B O   
12198 C CB  . ARG B 473  ? 0.4864 0.5822 0.3232 -0.1701 -0.0393 0.1368  471  ARG B CB  
12199 C CG  . ARG B 473  ? 0.4476 0.5239 0.2782 -0.1625 -0.0429 0.1316  471  ARG B CG  
12200 C CD  . ARG B 473  ? 0.4518 0.5035 0.2787 -0.1656 -0.0515 0.1317  471  ARG B CD  
12201 N NE  . ARG B 473  ? 0.4769 0.5246 0.2975 -0.1784 -0.0558 0.1408  471  ARG B NE  
12202 C CZ  . ARG B 473  ? 0.5070 0.5463 0.3166 -0.1842 -0.0593 0.1467  471  ARG B CZ  
12203 N NH1 . ARG B 473  ? 0.4937 0.5271 0.2970 -0.1781 -0.0592 0.1444  471  ARG B NH1 
12204 N NH2 . ARG B 473  ? 0.5042 0.5405 0.3086 -0.1964 -0.0632 0.1551  471  ARG B NH2 
12205 N N   . ILE B 474  ? 0.4536 0.5818 0.2967 -0.1472 -0.0232 0.1249  472  ILE B N   
12206 C CA  . ILE B 474  ? 0.4473 0.5818 0.2962 -0.1351 -0.0184 0.1165  472  ILE B CA  
12207 C C   . ILE B 474  ? 0.4477 0.5607 0.2960 -0.1281 -0.0232 0.1097  472  ILE B C   
12208 O O   . ILE B 474  ? 0.4057 0.5039 0.2454 -0.1281 -0.0274 0.1102  472  ILE B O   
12209 C CB  . ILE B 474  ? 0.4231 0.5714 0.2673 -0.1311 -0.0127 0.1166  472  ILE B CB  
12210 C CG1 . ILE B 474  ? 0.4705 0.6428 0.3166 -0.1373 -0.0073 0.1230  472  ILE B CG1 
12211 C CG2 . ILE B 474  ? 0.4582 0.6094 0.3070 -0.1184 -0.0089 0.1076  472  ILE B CG2 
12212 C CD1 . ILE B 474  ? 0.4809 0.6695 0.3236 -0.1320 -0.0007 0.1222  472  ILE B CD1 
12213 N N   . TYR B 475  ? 0.4370 0.5487 0.2943 -0.1220 -0.0226 0.1035  473  TYR B N   
12214 C CA  . TYR B 475  ? 0.3975 0.4920 0.2558 -0.1143 -0.0260 0.0963  473  TYR B CA  
12215 C C   . TYR B 475  ? 0.4370 0.5354 0.2939 -0.1048 -0.0223 0.0910  473  TYR B C   
12216 O O   . TYR B 475  ? 0.4369 0.5499 0.2996 -0.0991 -0.0165 0.0875  473  TYR B O   
12217 C CB  . TYR B 475  ? 0.3821 0.4761 0.2506 -0.1115 -0.0260 0.0920  473  TYR B CB  
12218 C CG  . TYR B 475  ? 0.4214 0.4977 0.2917 -0.1049 -0.0300 0.0853  473  TYR B CG  
12219 C CD1 . TYR B 475  ? 0.4538 0.5316 0.3282 -0.0947 -0.0271 0.0781  473  TYR B CD1 
12220 C CD2 . TYR B 475  ? 0.3504 0.4089 0.2184 -0.1087 -0.0367 0.0863  473  TYR B CD2 
12221 C CE1 . TYR B 475  ? 0.4895 0.5524 0.3660 -0.0890 -0.0306 0.0723  473  TYR B CE1 
12222 C CE2 . TYR B 475  ? 0.4062 0.4498 0.2762 -0.1024 -0.0401 0.0802  473  TYR B CE2 
12223 C CZ  . TYR B 475  ? 0.4616 0.5080 0.3361 -0.0927 -0.0369 0.0733  473  TYR B CZ  
12224 O OH  . TYR B 475  ? 0.4958 0.5286 0.3727 -0.0867 -0.0401 0.0676  473  TYR B OH  
12225 N N   . ALA B 476  ? 0.3968 0.4818 0.2456 -0.1031 -0.0258 0.0904  474  ALA B N   
12226 C CA  . ALA B 476  ? 0.4497 0.5386 0.2944 -0.0961 -0.0228 0.0870  474  ALA B CA  
12227 C C   . ALA B 476  ? 0.4609 0.5355 0.3070 -0.0876 -0.0256 0.0795  474  ALA B C   
12228 O O   . ALA B 476  ? 0.3902 0.4480 0.2306 -0.0884 -0.0314 0.0798  474  ALA B O   
12229 C CB  . ALA B 476  ? 0.4056 0.4929 0.2389 -0.1016 -0.0243 0.0931  474  ALA B CB  
12230 N N   . PRO B 477  ? 0.4126 0.4931 0.2659 -0.0794 -0.0220 0.0729  475  PRO B N   
12231 C CA  . PRO B 477  ? 0.4018 0.4699 0.2565 -0.0715 -0.0244 0.0659  475  PRO B CA  
12232 C C   . PRO B 477  ? 0.4259 0.4898 0.2719 -0.0683 -0.0252 0.0650  475  PRO B C   
12233 O O   . PRO B 477  ? 0.4354 0.5106 0.2764 -0.0686 -0.0214 0.0671  475  PRO B O   
12234 C CB  . PRO B 477  ? 0.4253 0.5038 0.2892 -0.0645 -0.0195 0.0601  475  PRO B CB  
12235 C CG  . PRO B 477  ? 0.4249 0.5184 0.2937 -0.0695 -0.0157 0.0642  475  PRO B CG  
12236 C CD  . PRO B 477  ? 0.4371 0.5358 0.2979 -0.0771 -0.0156 0.0715  475  PRO B CD  
12237 N N   . VAL B 478  ? 0.3756 0.4234 0.2197 -0.0653 -0.0304 0.0619  476  VAL B N   
12238 C CA  . VAL B 478  ? 0.4101 0.4515 0.2458 -0.0625 -0.0324 0.0610  476  VAL B CA  
12239 C C   . VAL B 478  ? 0.4726 0.5043 0.3124 -0.0546 -0.0347 0.0537  476  VAL B C   
12240 O O   . VAL B 478  ? 0.4618 0.4819 0.3055 -0.0544 -0.0390 0.0522  476  VAL B O   
12241 C CB  . VAL B 478  ? 0.3954 0.4254 0.2219 -0.0692 -0.0379 0.0670  476  VAL B CB  
12242 C CG1 . VAL B 478  ? 0.4586 0.4824 0.2765 -0.0659 -0.0401 0.0659  476  VAL B CG1 
12243 C CG2 . VAL B 478  ? 0.4360 0.4758 0.2585 -0.0778 -0.0359 0.0748  476  VAL B CG2 
12244 N N   . GLY B 479  ? 0.5110 0.5473 0.3497 -0.0482 -0.0320 0.0492  477  GLY B N   
12245 C CA  . GLY B 479  ? 0.5716 0.5994 0.4137 -0.0411 -0.0342 0.0426  477  GLY B CA  
12246 C C   . GLY B 479  ? 0.6376 0.6745 0.4813 -0.0343 -0.0295 0.0374  477  GLY B C   
12247 O O   . GLY B 479  ? 0.5240 0.5737 0.3651 -0.0344 -0.0246 0.0388  477  GLY B O   
12248 N N   . THR B 480  ? 0.6470 0.6769 0.4950 -0.0282 -0.0314 0.0313  478  THR B N   
12249 C CA  . THR B 480  ? 0.7017 0.7373 0.5515 -0.0213 -0.0280 0.0255  478  THR B CA  
12250 C C   . THR B 480  ? 0.7557 0.7881 0.6155 -0.0166 -0.0282 0.0200  478  THR B C   
12251 O O   . THR B 480  ? 0.7608 0.7980 0.6227 -0.0112 -0.0253 0.0154  478  THR B O   
12252 C CB  . THR B 480  ? 0.7280 0.7579 0.5696 -0.0182 -0.0304 0.0235  478  THR B CB  
12253 O OG1 . THR B 480  ? 0.6604 0.6764 0.5018 -0.0186 -0.0367 0.0231  478  THR B OG1 
12254 C CG2 . THR B 480  ? 0.7135 0.7491 0.5446 -0.0216 -0.0289 0.0283  478  THR B CG2 
12255 N N   . HIS B 481  ? 0.7497 0.7741 0.6152 -0.0184 -0.0316 0.0202  479  HIS B N   
12256 C CA  . HIS B 481  ? 0.7112 0.7313 0.5852 -0.0140 -0.0325 0.0149  479  HIS B CA  
12257 C C   . HIS B 481  ? 0.7404 0.7710 0.6213 -0.0115 -0.0272 0.0126  479  HIS B C   
12258 O O   . HIS B 481  ? 0.7340 0.7712 0.6182 -0.0149 -0.0248 0.0156  479  HIS B O   
12259 C CB  . HIS B 481  ? 0.7270 0.7376 0.6052 -0.0167 -0.0367 0.0161  479  HIS B CB  
12260 N N   . GLU B 482  ? 0.6952 0.7268 0.5782 -0.0056 -0.0258 0.0073  480  GLU B N   
12261 C CA  . GLU B 482  ? 0.7184 0.7594 0.6070 -0.0023 -0.0210 0.0048  480  GLU B CA  
12262 C C   . GLU B 482  ? 0.7318 0.7736 0.6293 -0.0041 -0.0205 0.0053  480  GLU B C   
12263 O O   . GLU B 482  ? 0.7556 0.8073 0.6564 -0.0048 -0.0165 0.0066  480  GLU B O   
12264 C CB  . GLU B 482  ? 0.6991 0.7375 0.5887 0.0041  -0.0210 -0.0012 480  GLU B CB  
12265 N N   . THR B 483  ? 0.7148 0.7469 0.6163 -0.0046 -0.0245 0.0043  481  THR B N   
12266 C CA  . THR B 483  ? 0.7480 0.7802 0.6574 -0.0061 -0.0243 0.0045  481  THR B CA  
12267 C C   . THR B 483  ? 0.7258 0.7627 0.6342 -0.0122 -0.0234 0.0100  481  THR B C   
12268 O O   . THR B 483  ? 0.6907 0.7358 0.6039 -0.0131 -0.0202 0.0109  481  THR B O   
12269 C CB  . THR B 483  ? 0.6728 0.6936 0.5855 -0.0055 -0.0290 0.0026  481  THR B CB  
12270 O OG1 . THR B 483  ? 0.7318 0.7501 0.6476 -0.0002 -0.0293 -0.0025 481  THR B OG1 
12271 C CG2 . THR B 483  ? 0.6825 0.7027 0.6018 -0.0078 -0.0292 0.0035  481  THR B CG2 
12272 N N   . LEU B 484  ? 0.7955 0.8270 0.6975 -0.0165 -0.0266 0.0139  482  LEU B N   
12273 C CA  . LEU B 484  ? 0.8191 0.8539 0.7192 -0.0231 -0.0265 0.0195  482  LEU B CA  
12274 C C   . LEU B 484  ? 0.8016 0.8503 0.6994 -0.0245 -0.0215 0.0223  482  LEU B C   
12275 O O   . LEU B 484  ? 0.7671 0.8224 0.6664 -0.0294 -0.0200 0.0263  482  LEU B O   
12276 C CB  . LEU B 484  ? 0.7447 0.7691 0.6376 -0.0271 -0.0314 0.0230  482  LEU B CB  
12277 C CG  . LEU B 484  ? 0.7241 0.7351 0.6189 -0.0247 -0.0365 0.0200  482  LEU B CG  
12278 C CD1 . LEU B 484  ? 0.6604 0.6610 0.5475 -0.0278 -0.0416 0.0231  482  LEU B CD1 
12279 C CD2 . LEU B 484  ? 0.7146 0.7229 0.6171 -0.0253 -0.0373 0.0189  482  LEU B CD2 
12280 N N   . LEU B 485  ? 0.7459 0.7997 0.6402 -0.0203 -0.0188 0.0200  483  LEU B N   
12281 C CA  . LEU B 485  ? 0.7000 0.7683 0.5926 -0.0206 -0.0137 0.0220  483  LEU B CA  
12282 C C   . LEU B 485  ? 0.7122 0.7899 0.6131 -0.0177 -0.0096 0.0197  483  LEU B C   
12283 O O   . LEU B 485  ? 0.7127 0.8024 0.6150 -0.0202 -0.0061 0.0229  483  LEU B O   
12284 C CB  . LEU B 485  ? 0.7267 0.7968 0.6122 -0.0164 -0.0123 0.0199  483  LEU B CB  
12285 C CG  . LEU B 485  ? 0.7520 0.8185 0.6279 -0.0209 -0.0147 0.0243  483  LEU B CG  
12286 C CD1 . LEU B 485  ? 0.7067 0.7741 0.5751 -0.0165 -0.0138 0.0219  483  LEU B CD1 
12287 C CD2 . LEU B 485  ? 0.6828 0.7595 0.5570 -0.0274 -0.0123 0.0307  483  LEU B CD2 
12288 N N   . ALA B 486  ? 0.7045 0.7772 0.6108 -0.0124 -0.0102 0.0144  484  ALA B N   
12289 C CA  . ALA B 486  ? 0.6810 0.7610 0.5953 -0.0100 -0.0070 0.0126  484  ALA B CA  
12290 C C   . ALA B 486  ? 0.6484 0.7303 0.5673 -0.0157 -0.0076 0.0164  484  ALA B C   
12291 O O   . ALA B 486  ? 0.6357 0.7288 0.5587 -0.0165 -0.0042 0.0179  484  ALA B O   
12292 C CB  . ALA B 486  ? 0.6555 0.7281 0.5746 -0.0044 -0.0082 0.0068  484  ALA B CB  
12293 N N   . TYR B 487  ? 0.6708 0.7418 0.5889 -0.0197 -0.0122 0.0180  485  TYR B N   
12294 C CA  . TYR B 487  ? 0.6150 0.6861 0.5362 -0.0255 -0.0134 0.0216  485  TYR B CA  
12295 C C   . TYR B 487  ? 0.6959 0.7774 0.6137 -0.0313 -0.0114 0.0275  485  TYR B C   
12296 O O   . TYR B 487  ? 0.6193 0.7088 0.5416 -0.0345 -0.0096 0.0299  485  TYR B O   
12297 C CB  . TYR B 487  ? 0.6992 0.7555 0.6187 -0.0281 -0.0190 0.0221  485  TYR B CB  
12298 N N   . LEU B 488  ? 0.6423 0.7243 0.5523 -0.0330 -0.0115 0.0300  486  LEU B N   
12299 C CA  . LEU B 488  ? 0.6974 0.7895 0.6037 -0.0391 -0.0097 0.0361  486  LEU B CA  
12300 C C   . LEU B 488  ? 0.6857 0.7953 0.5960 -0.0370 -0.0038 0.0361  486  LEU B C   
12301 O O   . LEU B 488  ? 0.6956 0.8151 0.6082 -0.0421 -0.0022 0.0405  486  LEU B O   
12302 C CB  . LEU B 488  ? 0.6363 0.7254 0.5329 -0.0407 -0.0109 0.0385  486  LEU B CB  
12303 N N   . VAL B 489  ? 0.6394 0.7530 0.5505 -0.0294 -0.0008 0.0313  487  VAL B N   
12304 C CA  . VAL B 489  ? 0.6672 0.7971 0.5815 -0.0263 0.0048  0.0309  487  VAL B CA  
12305 C C   . VAL B 489  ? 0.6583 0.7930 0.5818 -0.0267 0.0058  0.0306  487  VAL B C   
12306 O O   . VAL B 489  ? 0.6191 0.7684 0.5458 -0.0284 0.0093  0.0333  487  VAL B O   
12307 C CB  . VAL B 489  ? 0.6712 0.8017 0.5837 -0.0176 0.0071  0.0252  487  VAL B CB  
12308 C CG1 . VAL B 489  ? 0.6449 0.7915 0.5612 -0.0133 0.0126  0.0242  487  VAL B CG1 
12309 C CG2 . VAL B 489  ? 0.6395 0.7668 0.5422 -0.0175 0.0064  0.0259  487  VAL B CG2 
12310 N N   . ARG B 490  ? 0.5901 0.7135 0.5180 -0.0251 0.0027  0.0273  488  ARG B N   
12311 C CA  . ARG B 490  ? 0.6381 0.7649 0.5742 -0.0256 0.0033  0.0270  488  ARG B CA  
12312 C C   . ARG B 490  ? 0.7340 0.8646 0.6709 -0.0342 0.0020  0.0329  488  ARG B C   
12313 O O   . ARG B 490  ? 0.7140 0.8543 0.6569 -0.0356 0.0039  0.0343  488  ARG B O   
12314 C CB  . ARG B 490  ? 0.5753 0.6887 0.5151 -0.0225 0.0001  0.0225  488  ARG B CB  
12315 N N   . ARG B 491  ? 0.6112 0.7341 0.5421 -0.0401 -0.0015 0.0366  489  ARG B N   
12316 C CA  . ARG B 491  ? 0.6515 0.7773 0.5821 -0.0488 -0.0031 0.0427  489  ARG B CA  
12317 C C   . ARG B 491  ? 0.6813 0.8236 0.6096 -0.0522 0.0008  0.0475  489  ARG B C   
12318 O O   . ARG B 491  ? 0.6799 0.8321 0.6115 -0.0576 0.0018  0.0517  489  ARG B O   
12319 C CB  . ARG B 491  ? 0.6632 0.7731 0.5878 -0.0538 -0.0087 0.0448  489  ARG B CB  
12320 C CG  . ARG B 491  ? 0.6642 0.7591 0.5917 -0.0518 -0.0128 0.0409  489  ARG B CG  
12321 C CD  . ARG B 491  ? 0.6411 0.7216 0.5631 -0.0577 -0.0186 0.0439  489  ARG B CD  
12322 N NE  . ARG B 491  ? 0.6390 0.7059 0.5637 -0.0553 -0.0223 0.0400  489  ARG B NE  
12323 C CZ  . ARG B 491  ? 0.6473 0.7013 0.5691 -0.0517 -0.0254 0.0369  489  ARG B CZ  
12324 N NH1 . ARG B 491  ? 0.6144 0.6660 0.5300 -0.0507 -0.0259 0.0374  489  ARG B NH1 
12325 N NH2 . ARG B 491  ? 0.5472 0.5911 0.4724 -0.0492 -0.0282 0.0333  489  ARG B NH2 
12326 N N   . LEU B 492  ? 0.7316 0.8772 0.6541 -0.0491 0.0030  0.0470  490  LEU B N   
12327 C CA  . LEU B 492  ? 0.7259 0.8886 0.6461 -0.0513 0.0073  0.0511  490  LEU B CA  
12328 C C   . LEU B 492  ? 0.7301 0.9097 0.6582 -0.0485 0.0120  0.0505  490  LEU B C   
12329 O O   . LEU B 492  ? 0.6970 0.8909 0.6268 -0.0536 0.0143  0.0556  490  LEU B O   
12330 C CB  . LEU B 492  ? 0.7142 0.8776 0.6273 -0.0463 0.0093  0.0491  490  LEU B CB  
12331 C CG  . LEU B 492  ? 0.7130 0.8751 0.6165 -0.0514 0.0083  0.0538  490  LEU B CG  
12332 C CD1 . LEU B 492  ? 0.6986 0.8682 0.6014 -0.0616 0.0078  0.0617  490  LEU B CD1 
12333 C CD2 . LEU B 492  ? 0.7070 0.8494 0.6046 -0.0512 0.0029  0.0520  490  LEU B CD2 
12334 N N   . LEU B 493  ? 0.7066 0.8848 0.6397 -0.0405 0.0134  0.0445  491  LEU B N   
12335 C CA  . LEU B 493  ? 0.6828 0.8761 0.6229 -0.0363 0.0178  0.0432  491  LEU B CA  
12336 C C   . LEU B 493  ? 0.6721 0.8640 0.6203 -0.0383 0.0161  0.0430  491  LEU B C   
12337 O O   . LEU B 493  ? 0.6776 0.8792 0.6321 -0.0338 0.0190  0.0410  491  LEU B O   
12338 C CB  . LEU B 493  ? 0.6071 0.8006 0.5470 -0.0260 0.0205  0.0368  491  LEU B CB  
12339 C CG  . LEU B 493  ? 0.6085 0.8045 0.5399 -0.0237 0.0225  0.0367  491  LEU B CG  
12340 C CD1 . LEU B 493  ? 0.5450 0.7402 0.4754 -0.0135 0.0248  0.0302  491  LEU B CD1 
12341 C CD2 . LEU B 493  ? 0.6854 0.8999 0.6155 -0.0280 0.0263  0.0424  491  LEU B CD2 
12342 N N   . GLU B 494  ? 0.7351 0.9150 0.6827 -0.0447 0.0113  0.0452  492  GLU B N   
12343 C CA  . GLU B 494  ? 0.6962 0.8745 0.6504 -0.0478 0.0093  0.0457  492  GLU B CA  
12344 C C   . GLU B 494  ? 0.6622 0.8374 0.6222 -0.0399 0.0101  0.0397  492  GLU B C   
12345 O O   . GLU B 494  ? 0.6855 0.8679 0.6522 -0.0397 0.0111  0.0397  492  GLU B O   
12346 C CB  . GLU B 494  ? 0.6958 0.8914 0.6539 -0.0534 0.0115  0.0511  492  GLU B CB  
12347 C CG  . GLU B 494  ? 0.7037 0.9052 0.6561 -0.0612 0.0114  0.0575  492  GLU B CG  
12348 C CD  . GLU B 494  ? 0.7364 0.9220 0.6839 -0.0690 0.0056  0.0606  492  GLU B CD  
12349 O OE1 . GLU B 494  ? 0.7199 0.8959 0.6706 -0.0709 0.0020  0.0595  492  GLU B OE1 
12350 O OE2 . GLU B 494  ? 0.7269 0.9095 0.6670 -0.0731 0.0045  0.0640  492  GLU B OE2 
12351 N N   . ASN B 495  ? 0.6369 0.8016 0.5942 -0.0336 0.0095  0.0347  493  ASN B N   
12352 C CA  . ASN B 495  ? 0.6718 0.8325 0.6337 -0.0261 0.0102  0.0289  493  ASN B CA  
12353 C C   . ASN B 495  ? 0.6622 0.8384 0.6290 -0.0208 0.0150  0.0277  493  ASN B C   
12354 O O   . ASN B 495  ? 0.6742 0.8495 0.6463 -0.0162 0.0154  0.0243  493  ASN B O   
12355 C CB  . ASN B 495  ? 0.6514 0.8022 0.6177 -0.0282 0.0067  0.0279  493  ASN B CB  
12356 C CG  . ASN B 495  ? 0.6645 0.7976 0.6275 -0.0274 0.0027  0.0251  493  ASN B CG  
12357 O OD1 . ASN B 495  ? 0.7170 0.8445 0.6742 -0.0265 0.0020  0.0246  493  ASN B OD1 
12358 N ND2 . ASN B 495  ? 0.6638 0.7883 0.6306 -0.0275 0.0002  0.0232  493  ASN B ND2 
12359 N N   . GLY B 496  ? 0.6797 0.8702 0.6446 -0.0212 0.0185  0.0305  494  GLY B N   
12360 C CA  . GLY B 496  ? 0.7305 0.9367 0.7000 -0.0161 0.0230  0.0296  494  GLY B CA  
12361 C C   . GLY B 496  ? 0.7937 1.0073 0.7711 -0.0186 0.0229  0.0315  494  GLY B C   
12362 O O   . GLY B 496  ? 0.8692 1.0885 0.8517 -0.0126 0.0250  0.0286  494  GLY B O   
12363 N N   . ALA B 497  ? 0.7405 0.9537 0.7186 -0.0274 0.0203  0.0362  495  ALA B N   
12364 C CA  . ALA B 497  ? 0.6667 0.8866 0.6519 -0.0307 0.0198  0.0383  495  ALA B CA  
12365 C C   . ALA B 497  ? 0.6151 0.8567 0.6037 -0.0317 0.0238  0.0421  495  ALA B C   
12366 O O   . ALA B 497  ? 0.6140 0.8638 0.5993 -0.0367 0.0249  0.0465  495  ALA B O   
12367 C CB  . ALA B 497  ? 0.6563 0.8662 0.6403 -0.0397 0.0150  0.0417  495  ALA B CB  
12368 N N   . ASN B 498  ? 0.6224 0.8738 0.6178 -0.0270 0.0259  0.0404  496  ASN B N   
12369 C CA  . ASN B 498  ? 0.6195 0.8929 0.6194 -0.0273 0.0297  0.0438  496  ASN B CA  
12370 C C   . ASN B 498  ? 0.5528 0.8337 0.5548 -0.0380 0.0279  0.0504  496  ASN B C   
12371 O O   . ASN B 498  ? 0.5791 0.8782 0.5829 -0.0408 0.0308  0.0547  496  ASN B O   
12372 C CB  . ASN B 498  ? 0.6287 0.9094 0.6355 -0.0198 0.0317  0.0405  496  ASN B CB  
12373 N N   . SER B 499  ? 0.5552 0.8225 0.5569 -0.0442 0.0231  0.0513  497  SER B N   
12374 C CA  . SER B 499  ? 0.5427 0.8148 0.5456 -0.0549 0.0206  0.0575  497  SER B CA  
12375 C C   . SER B 499  ? 0.5204 0.7909 0.5164 -0.0621 0.0197  0.0621  497  SER B C   
12376 O O   . SER B 499  ? 0.4793 0.7556 0.4757 -0.0715 0.0180  0.0679  497  SER B O   
12377 C CB  . SER B 499  ? 0.5287 0.7855 0.5327 -0.0587 0.0155  0.0566  497  SER B CB  
12378 O OG  . SER B 499  ? 0.4202 0.6566 0.4181 -0.0577 0.0125  0.0535  497  SER B OG  
12379 N N   . SER B 500  ? 0.4809 0.7431 0.4703 -0.0583 0.0205  0.0597  498  SER B N   
12380 C CA  . SER B 500  ? 0.4988 0.7575 0.4808 -0.0651 0.0191  0.0639  498  SER B CA  
12381 C C   . SER B 500  ? 0.5396 0.8198 0.5219 -0.0674 0.0235  0.0688  498  SER B C   
12382 O O   . SER B 500  ? 0.5260 0.8209 0.5117 -0.0603 0.0284  0.0668  498  SER B O   
12383 C CB  . SER B 500  ? 0.5436 0.7867 0.5184 -0.0599 0.0184  0.0597  498  SER B CB  
12384 O OG  . SER B 500  ? 0.6166 0.8666 0.5921 -0.0500 0.0229  0.0552  498  SER B OG  
12385 N N   . PHE B 501  ? 0.4602 0.7422 0.4388 -0.0775 0.0217  0.0752  499  PHE B N   
12386 C CA  . PHE B 501  ? 0.5129 0.8146 0.4905 -0.0807 0.0257  0.0804  499  PHE B CA  
12387 C C   . PHE B 501  ? 0.5431 0.8479 0.5158 -0.0724 0.0300  0.0771  499  PHE B C   
12388 O O   . PHE B 501  ? 0.5328 0.8571 0.5076 -0.0686 0.0353  0.0778  499  PHE B O   
12389 C CB  . PHE B 501  ? 0.4563 0.7544 0.4287 -0.0930 0.0222  0.0876  499  PHE B CB  
12390 C CG  . PHE B 501  ? 0.4750 0.7949 0.4474 -0.0984 0.0259  0.0941  499  PHE B CG  
12391 C CD1 . PHE B 501  ? 0.5278 0.8544 0.4944 -0.0951 0.0299  0.0944  499  PHE B CD1 
12392 C CD2 . PHE B 501  ? 0.4639 0.7978 0.4419 -0.1070 0.0254  0.1001  499  PHE B CD2 
12393 C CE1 . PHE B 501  ? 0.5239 0.8714 0.4903 -0.1000 0.0336  0.1005  499  PHE B CE1 
12394 C CE2 . PHE B 501  ? 0.5115 0.8664 0.4899 -0.1123 0.0289  0.1064  499  PHE B CE2 
12395 C CZ  . PHE B 501  ? 0.4875 0.8472 0.4605 -0.1079 0.0324  0.1058  499  PHE B CZ  
12396 N N   . VAL B 502  ? 0.5894 0.8750 0.5552 -0.0692 0.0276  0.0732  500  VAL B N   
12397 C CA  . VAL B 502  ? 0.6295 0.9157 0.5896 -0.0616 0.0310  0.0699  500  VAL B CA  
12398 C C   . VAL B 502  ? 0.6316 0.9304 0.5969 -0.0510 0.0360  0.0650  500  VAL B C   
12399 O O   . VAL B 502  ? 0.6612 0.9744 0.6247 -0.0467 0.0407  0.0650  500  VAL B O   
12400 C CB  . VAL B 502  ? 0.5785 0.8409 0.5321 -0.0590 0.0270  0.0656  500  VAL B CB  
12401 N N   . HIS B 503  ? 0.5426 0.8363 0.5143 -0.0464 0.0348  0.0607  501  HIS B N   
12402 C CA  . HIS B 503  ? 0.5696 0.8735 0.5462 -0.0361 0.0390  0.0560  501  HIS B CA  
12403 C C   . HIS B 503  ? 0.6105 0.9385 0.5941 -0.0373 0.0427  0.0598  501  HIS B C   
12404 O O   . HIS B 503  ? 0.6061 0.9481 0.5914 -0.0293 0.0474  0.0575  501  HIS B O   
12405 C CB  . HIS B 503  ? 0.5936 0.8834 0.5742 -0.0310 0.0363  0.0505  501  HIS B CB  
12406 C CG  . HIS B 503  ? 0.6675 0.9683 0.6547 -0.0224 0.0397  0.0469  501  HIS B CG  
12407 N ND1 . HIS B 503  ? 0.6550 0.9689 0.6504 -0.0244 0.0403  0.0494  501  HIS B ND1 
12408 C CD2 . HIS B 503  ? 0.6840 0.9842 0.6706 -0.0117 0.0422  0.0411  501  HIS B CD2 
12409 C CE1 . HIS B 503  ? 0.6611 0.9822 0.6607 -0.0151 0.0432  0.0453  501  HIS B CE1 
12410 N NE2 . HIS B 503  ? 0.7441 1.0566 0.7383 -0.0073 0.0443  0.0402  501  HIS B NE2 
12411 N N   . ARG B 504  ? 0.5912 0.9247 0.5790 -0.0469 0.0406  0.0655  502  ARG B N   
12412 C CA  . ARG B 504  ? 0.5257 0.8818 0.5216 -0.0482 0.0435  0.0689  502  ARG B CA  
12413 C C   . ARG B 504  ? 0.5599 0.9368 0.5540 -0.0504 0.0481  0.0737  502  ARG B C   
12414 O O   . ARG B 504  ? 0.5495 0.9439 0.5493 -0.0455 0.0514  0.0734  502  ARG B O   
12415 C CB  . ARG B 504  ? 0.4727 0.8266 0.4735 -0.0580 0.0392  0.0732  502  ARG B CB  
12416 C CG  . ARG B 504  ? 0.5119 0.8527 0.5171 -0.0542 0.0361  0.0685  502  ARG B CG  
12417 C CD  . ARG B 504  ? 0.5021 0.8343 0.5091 -0.0643 0.0307  0.0721  502  ARG B CD  
12418 N NE  . ARG B 504  ? 0.4702 0.8206 0.4819 -0.0728 0.0310  0.0789  502  ARG B NE  
12419 C CZ  . ARG B 504  ? 0.5062 0.8726 0.5265 -0.0718 0.0326  0.0798  502  ARG B CZ  
12420 N NH1 . ARG B 504  ? 0.5517 0.9193 0.5768 -0.0619 0.0343  0.0744  502  ARG B NH1 
12421 N NH2 . ARG B 504  ? 0.4439 0.8253 0.4681 -0.0810 0.0321  0.0865  502  ARG B NH2 
12422 N N   . ILE B 505  ? 0.5527 0.9249 0.5391 -0.0571 0.0470  0.0775  503  ILE B N   
12423 C CA  . ILE B 505  ? 0.5682 0.9557 0.5523 -0.0585 0.0501  0.0811  503  ILE B CA  
12424 C C   . ILE B 505  ? 0.5944 0.9881 0.5770 -0.0460 0.0547  0.0754  503  ILE B C   
12425 O O   . ILE B 505  ? 0.5643 0.9719 0.5481 -0.0441 0.0571  0.0766  503  ILE B O   
12426 C CB  . ILE B 505  ? 0.5371 0.9158 0.5121 -0.0678 0.0479  0.0860  503  ILE B CB  
12427 N N   . ASN B 506  ? 0.5551 0.9385 0.5350 -0.0374 0.0557  0.0691  504  ASN B N   
12428 C CA  . ASN B 506  ? 0.6409 1.0270 0.6183 -0.0252 0.0594  0.0631  504  ASN B CA  
12429 C C   . ASN B 506  ? 0.6428 1.0344 0.6281 -0.0157 0.0608  0.0582  504  ASN B C   
12430 O O   . ASN B 506  ? 0.6248 1.0185 0.6085 -0.0051 0.0635  0.0530  504  ASN B O   
12431 C CB  . ASN B 506  ? 0.6429 1.0094 0.6110 -0.0213 0.0581  0.0584  504  ASN B CB  
12432 N N   . ASP B 507  ? 0.5822 0.9753 0.5755 -0.0190 0.0588  0.0596  505  ASP B N   
12433 C CA  . ASP B 507  ? 0.6403 1.0389 0.6412 -0.0104 0.0597  0.0555  505  ASP B CA  
12434 C C   . ASP B 507  ? 0.6875 1.1046 0.6942 -0.0101 0.0610  0.0583  505  ASP B C   
12435 O O   . ASP B 507  ? 0.6472 1.0720 0.6576 -0.0196 0.0592  0.0643  505  ASP B O   
12436 C CB  . ASP B 507  ? 0.6379 1.0299 0.6445 -0.0139 0.0568  0.0557  505  ASP B CB  
12437 C CG  . ASP B 507  ? 0.6954 1.0876 0.7076 -0.0036 0.0576  0.0502  505  ASP B CG  
12438 O OD1 . ASP B 507  ? 0.7489 1.1524 0.7645 0.0029  0.0593  0.0490  505  ASP B OD1 
12439 O OD2 . ASP B 507  ? 0.7441 1.1200 0.7567 -0.0018 0.0547  0.0466  505  ASP B OD2 
12440 N N   . PRO B 508  ? 0.7172 1.1417 0.7245 0.0005  0.0638  0.0543  506  PRO B N   
12441 C CA  . PRO B 508  ? 0.6889 1.1318 0.7018 0.0013  0.0650  0.0569  506  PRO B CA  
12442 C C   . PRO B 508  ? 0.6864 1.1356 0.7085 -0.0008 0.0629  0.0587  506  PRO B C   
12443 O O   . PRO B 508  ? 0.6541 1.1188 0.6810 -0.0035 0.0631  0.0625  506  PRO B O   
12444 C CB  . PRO B 508  ? 0.6902 1.1359 0.7006 0.0144  0.0682  0.0510  506  PRO B CB  
12445 C CG  . PRO B 508  ? 0.6970 1.1272 0.6985 0.0179  0.0688  0.0468  506  PRO B CG  
12446 C CD  . PRO B 508  ? 0.6927 1.1090 0.6944 0.0117  0.0659  0.0474  506  PRO B CD  
12447 N N   . LYS B 509  ? 0.6891 1.1272 0.7138 0.0002  0.0609  0.0562  507  LYS B N   
12448 C CA  . LYS B 509  ? 0.6507 1.0940 0.6838 -0.0021 0.0587  0.0579  507  LYS B CA  
12449 C C   . LYS B 509  ? 0.7045 1.1517 0.7399 -0.0157 0.0558  0.0649  507  LYS B C   
12450 O O   . LYS B 509  ? 0.7336 1.1936 0.7747 -0.0189 0.0549  0.0685  507  LYS B O   
12451 C CB  . LYS B 509  ? 0.6779 1.1075 0.7125 0.0021  0.0572  0.0534  507  LYS B CB  
12452 N N   . VAL B 510  ? 0.7042 1.1403 0.7347 -0.0237 0.0542  0.0671  508  VAL B N   
12453 C CA  . VAL B 510  ? 0.6597 1.0966 0.6915 -0.0369 0.0508  0.0736  508  VAL B CA  
12454 C C   . VAL B 510  ? 0.6121 1.0632 0.6432 -0.0418 0.0517  0.0786  508  VAL B C   
12455 O O   . VAL B 510  ? 0.6083 1.0611 0.6337 -0.0397 0.0542  0.0783  508  VAL B O   
12456 C CB  . VAL B 510  ? 0.5862 1.0061 0.6118 -0.0437 0.0487  0.0744  508  VAL B CB  
12457 C CG1 . VAL B 510  ? 0.5716 0.9913 0.5969 -0.0576 0.0450  0.0814  508  VAL B CG1 
12458 C CG2 . VAL B 510  ? 0.6078 1.0152 0.6353 -0.0402 0.0475  0.0702  508  VAL B CG2 
12459 N N   . SER B 511  ? 0.6166 1.0783 0.6534 -0.0484 0.0495  0.0833  509  SER B N   
12460 C CA  . SER B 511  ? 0.5509 1.0273 0.5881 -0.0541 0.0498  0.0887  509  SER B CA  
12461 C C   . SER B 511  ? 0.5568 1.0266 0.5900 -0.0677 0.0464  0.0947  509  SER B C   
12462 O O   . SER B 511  ? 0.5845 1.0395 0.6159 -0.0734 0.0431  0.0951  509  SER B O   
12463 C CB  . SER B 511  ? 0.5557 1.0473 0.6010 -0.0539 0.0491  0.0906  509  SER B CB  
12464 O OG  . SER B 511  ? 0.5543 1.0392 0.6032 -0.0604 0.0449  0.0923  509  SER B OG  
12465 N N   . ILE B 512  ? 0.4792 0.9602 0.5109 -0.0729 0.0469  0.0994  510  ILE B N   
12466 C CA  . ILE B 512  ? 0.5664 1.0413 0.5937 -0.0859 0.0434  0.1054  510  ILE B CA  
12467 C C   . ILE B 512  ? 0.5669 1.0393 0.5985 -0.0953 0.0384  0.1092  510  ILE B C   
12468 O O   . ILE B 512  ? 0.5370 0.9966 0.5646 -0.1052 0.0343  0.1125  510  ILE B O   
12469 C CB  . ILE B 512  ? 0.4588 0.9475 0.4840 -0.0892 0.0452  0.1098  510  ILE B CB  
12470 N N   . ASP B 513  ? 0.5314 1.0154 0.5707 -0.0922 0.0383  0.1087  511  ASP B N   
12471 C CA  . ASP B 513  ? 0.5227 1.0037 0.5659 -0.1001 0.0335  0.1116  511  ASP B CA  
12472 C C   . ASP B 513  ? 0.4977 0.9589 0.5392 -0.1008 0.0309  0.1086  511  ASP B C   
12473 O O   . ASP B 513  ? 0.5054 0.9558 0.5449 -0.1109 0.0262  0.1119  511  ASP B O   
12474 C CB  . ASP B 513  ? 0.4989 0.9953 0.5503 -0.0949 0.0343  0.1108  511  ASP B CB  
12475 C CG  . ASP B 513  ? 0.6096 1.1258 0.6634 -0.0978 0.0353  0.1155  511  ASP B CG  
12476 O OD1 . ASP B 513  ? 0.6313 1.1484 0.6827 -0.1090 0.0324  0.1214  511  ASP B OD1 
12477 O OD2 . ASP B 513  ? 0.6316 1.1622 0.6894 -0.0888 0.0389  0.1133  511  ASP B OD2 
12478 N N   . GLU B 514  ? 0.4643 0.9204 0.5063 -0.0900 0.0339  0.1023  512  GLU B N   
12479 C CA  . GLU B 514  ? 0.5197 0.9577 0.5600 -0.0899 0.0319  0.0991  512  GLU B CA  
12480 C C   . GLU B 514  ? 0.5295 0.9522 0.5616 -0.0978 0.0299  0.1014  512  GLU B C   
12481 O O   . GLU B 514  ? 0.4619 0.8713 0.4925 -0.1053 0.0256  0.1029  512  GLU B O   
12482 C CB  . GLU B 514  ? 0.5445 0.9802 0.5858 -0.0767 0.0359  0.0920  512  GLU B CB  
12483 C CG  . GLU B 514  ? 0.5955 1.0448 0.6440 -0.0678 0.0379  0.0894  512  GLU B CG  
12484 C CD  . GLU B 514  ? 0.6470 1.0912 0.6958 -0.0551 0.0410  0.0823  512  GLU B CD  
12485 O OE1 . GLU B 514  ? 0.6393 1.0689 0.6867 -0.0546 0.0397  0.0795  512  GLU B OE1 
12486 O OE2 . GLU B 514  ? 0.6185 1.0729 0.6687 -0.0457 0.0444  0.0796  512  GLU B OE2 
12487 N N   . LEU B 515  ? 0.4836 0.9077 0.5100 -0.0960 0.0327  0.1016  513  LEU B N   
12488 C CA  . LEU B 515  ? 0.4917 0.9009 0.5095 -0.1027 0.0308  0.1037  513  LEU B CA  
12489 C C   . LEU B 515  ? 0.4937 0.9000 0.5095 -0.1165 0.0258  0.1107  513  LEU B C   
12490 O O   . LEU B 515  ? 0.4492 0.8391 0.4585 -0.1235 0.0224  0.1125  513  LEU B O   
12491 C CB  . LEU B 515  ? 0.4002 0.8125 0.4121 -0.0974 0.0350  0.1025  513  LEU B CB  
12492 N N   . ILE B 516  ? 0.4509 0.8720 0.4717 -0.1205 0.0248  0.1145  514  ILE B N   
12493 C CA  . ILE B 516  ? 0.4437 0.8630 0.4621 -0.1335 0.0199  0.1212  514  ILE B CA  
12494 C C   . ILE B 516  ? 0.4783 0.8913 0.5002 -0.1402 0.0146  0.1227  514  ILE B C   
12495 O O   . ILE B 516  ? 0.4650 0.8740 0.4843 -0.1513 0.0097  0.1280  514  ILE B O   
12496 C CB  . ILE B 516  ? 0.5152 0.9544 0.5358 -0.1352 0.0217  0.1253  514  ILE B CB  
12497 N N   . ALA B 517  ? 0.4112 0.8225 0.4383 -0.1338 0.0152  0.1181  515  ALA B N   
12498 C CA  . ALA B 517  ? 0.4789 0.8845 0.5093 -0.1394 0.0103  0.1191  515  ALA B CA  
12499 C C   . ALA B 517  ? 0.4854 0.8701 0.5089 -0.1495 0.0046  0.1215  515  ALA B C   
12500 O O   . ALA B 517  ? 0.4513 0.8219 0.4689 -0.1485 0.0049  0.1197  515  ALA B O   
12501 C CB  . ALA B 517  ? 0.3870 0.7920 0.4232 -0.1300 0.0121  0.1132  515  ALA B CB  
12502 N N   . ASP B 518  ? 0.4099 0.7920 0.4337 -0.1592 -0.0010 0.1256  516  ASP B N   
12503 C CA  . ASP B 518  ? 0.4283 0.7900 0.4452 -0.1693 -0.0073 0.1281  516  ASP B CA  
12504 C C   . ASP B 518  ? 0.4053 0.7520 0.4231 -0.1671 -0.0094 0.1237  516  ASP B C   
12505 O O   . ASP B 518  ? 0.4332 0.7836 0.4567 -0.1664 -0.0109 0.1224  516  ASP B O   
12506 C CB  . ASP B 518  ? 0.4314 0.7956 0.4476 -0.1802 -0.0127 0.1340  516  ASP B CB  
12507 C CG  . ASP B 518  ? 0.4873 0.8299 0.4947 -0.1909 -0.0194 0.1371  516  ASP B CG  
12508 O OD1 . ASP B 518  ? 0.4877 0.8117 0.4909 -0.1900 -0.0211 0.1341  516  ASP B OD1 
12509 O OD2 . ASP B 518  ? 0.5301 0.8739 0.5343 -0.2000 -0.0233 0.1426  516  ASP B OD2 
12510 N N   . PRO B 519  ? 0.3495 0.6793 0.3618 -0.1662 -0.0097 0.1214  517  PRO B N   
12511 C CA  . PRO B 519  ? 0.3752 0.6905 0.3885 -0.1635 -0.0119 0.1167  517  PRO B CA  
12512 C C   . PRO B 519  ? 0.3834 0.6882 0.3961 -0.1728 -0.0190 0.1188  517  PRO B C   
12513 O O   . PRO B 519  ? 0.3970 0.6967 0.4133 -0.1690 -0.0206 0.1146  517  PRO B O   
12514 C CB  . PRO B 519  ? 0.3948 0.6881 0.3990 -0.1587 -0.0127 0.1126  517  PRO B CB  
12515 C CG  . PRO B 519  ? 0.4650 0.7605 0.4630 -0.1667 -0.0128 0.1189  517  PRO B CG  
12516 C CD  . PRO B 519  ? 0.3957 0.7174 0.3998 -0.1674 -0.0086 0.1228  517  PRO B CD  
12517 N N   . VAL B 520  ? 0.4093 0.7077 0.4159 -0.1829 -0.0238 0.1241  518  VAL B N   
12518 C CA  . VAL B 520  ? 0.3958 0.6818 0.4001 -0.1914 -0.0312 0.1257  518  VAL B CA  
12519 C C   . VAL B 520  ? 0.4441 0.7448 0.4563 -0.1902 -0.0312 0.1256  518  VAL B C   
12520 O O   . VAL B 520  ? 0.4151 0.7073 0.4286 -0.1913 -0.0350 0.1235  518  VAL B O   
12521 C CB  . VAL B 520  ? 0.4233 0.7009 0.4192 -0.2020 -0.0363 0.1317  518  VAL B CB  
12522 C CG1 . VAL B 520  ? 0.4711 0.7330 0.4632 -0.2102 -0.0443 0.1329  518  VAL B CG1 
12523 C CG2 . VAL B 520  ? 0.3607 0.6245 0.3485 -0.2025 -0.0360 0.1320  518  VAL B CG2 
12524 N N   . GLU B 521  ? 0.3831 0.7055 0.4003 -0.1876 -0.0270 0.1278  519  GLU B N   
12525 C CA  . GLU B 521  ? 0.4327 0.7695 0.4570 -0.1866 -0.0271 0.1282  519  GLU B CA  
12526 C C   . GLU B 521  ? 0.4311 0.7750 0.4630 -0.1756 -0.0227 0.1224  519  GLU B C   
12527 O O   . GLU B 521  ? 0.4167 0.7641 0.4532 -0.1749 -0.0245 0.1214  519  GLU B O   
12528 C CB  . GLU B 521  ? 0.4062 0.7639 0.4331 -0.1881 -0.0246 0.1328  519  GLU B CB  
12529 C CG  . GLU B 521  ? 0.4289 0.7817 0.4488 -0.1994 -0.0291 0.1391  519  GLU B CG  
12530 C CD  . GLU B 521  ? 0.5154 0.8529 0.5311 -0.2089 -0.0369 0.1412  519  GLU B CD  
12531 O OE1 . GLU B 521  ? 0.4442 0.7827 0.4641 -0.2076 -0.0385 0.1393  519  GLU B OE1 
12532 O OE2 . GLU B 521  ? 0.5402 0.8640 0.5478 -0.2175 -0.0417 0.1447  519  GLU B OE2 
12533 N N   . VAL B 522  ? 0.3744 0.7205 0.4075 -0.1668 -0.0173 0.1187  520  VAL B N   
12534 C CA  . VAL B 522  ? 0.3813 0.7317 0.4208 -0.1563 -0.0137 0.1129  520  VAL B CA  
12535 C C   . VAL B 522  ? 0.4372 0.7698 0.4758 -0.1580 -0.0182 0.1097  520  VAL B C   
12536 O O   . VAL B 522  ? 0.4569 0.7926 0.5010 -0.1537 -0.0184 0.1067  520  VAL B O   
12537 C CB  . VAL B 522  ? 0.3726 0.7273 0.4125 -0.1468 -0.0073 0.1095  520  VAL B CB  
12538 C CG1 . VAL B 522  ? 0.4309 0.7888 0.4770 -0.1360 -0.0040 0.1036  520  VAL B CG1 
12539 C CG2 . VAL B 522  ? 0.4265 0.7989 0.4671 -0.1446 -0.0031 0.1123  520  VAL B CG2 
12540 N N   . VAL B 523  ? 0.3789 0.6923 0.4103 -0.1640 -0.0220 0.1102  521  VAL B N   
12541 C CA  . VAL B 523  ? 0.4192 0.7102 0.4468 -0.1629 -0.0272 0.1055  521  VAL B CA  
12542 C C   . VAL B 523  ? 0.4186 0.7114 0.4485 -0.1724 -0.0326 0.1088  521  VAL B C   
12543 O O   . VAL B 523  ? 0.3997 0.6865 0.4315 -0.1692 -0.0348 0.1049  521  VAL B O   
12544 C CB  . VAL B 523  ? 0.4366 0.7024 0.4534 -0.1644 -0.0306 0.1039  521  VAL B CB  
12545 C CG1 . VAL B 523  ? 0.3725 0.6162 0.3849 -0.1658 -0.0369 0.1004  521  VAL B CG1 
12546 C CG2 . VAL B 523  ? 0.3116 0.5731 0.3266 -0.1531 -0.0257 0.0988  521  VAL B CG2 
12547 N N   . ARG B 524  ? 0.4271 0.7229 0.4535 -0.1808 -0.0353 0.1145  522  ARG B N   
12548 C CA  . ARG B 524  ? 0.4075 0.7001 0.4328 -0.1878 -0.0410 0.1169  522  ARG B CA  
12549 C C   . ARG B 524  ? 0.4742 0.7824 0.5080 -0.1824 -0.0389 0.1153  522  ARG B C   
12550 O O   . ARG B 524  ? 0.4670 0.7691 0.5007 -0.1852 -0.0433 0.1147  522  ARG B O   
12551 C CB  . ARG B 524  ? 0.4369 0.7329 0.4576 -0.1970 -0.0435 0.1236  522  ARG B CB  
12552 C CG  . ARG B 524  ? 0.4619 0.7516 0.4798 -0.2054 -0.0502 0.1264  522  ARG B CG  
12553 C CD  . ARG B 524  ? 0.5154 0.8160 0.5318 -0.2129 -0.0513 0.1331  522  ARG B CD  
12554 N NE  . ARG B 524  ? 0.4364 0.7313 0.4462 -0.2172 -0.0516 0.1363  522  ARG B NE  
12555 C CZ  . ARG B 524  ? 0.5461 0.8191 0.5466 -0.2240 -0.0572 0.1373  522  ARG B CZ  
12556 N NH1 . ARG B 524  ? 0.6040 0.8580 0.6002 -0.2269 -0.0631 0.1351  522  ARG B NH1 
12557 N NH2 . ARG B 524  ? 0.5761 0.8459 0.5710 -0.2275 -0.0571 0.1405  522  ARG B NH2 
12558 N N   . ALA B 525  ? 0.4431 0.7704 0.4835 -0.1742 -0.0323 0.1145  523  ALA B N   
12559 C CA  . ALA B 525  ? 0.4381 0.7812 0.4864 -0.1686 -0.0302 0.1134  523  ALA B CA  
12560 C C   . ALA B 525  ? 0.4508 0.7902 0.5033 -0.1598 -0.0286 0.1072  523  ALA B C   
12561 O O   . ALA B 525  ? 0.4209 0.7705 0.4793 -0.1552 -0.0276 0.1059  523  ALA B O   
12562 C CB  . ALA B 525  ? 0.4011 0.7662 0.4540 -0.1634 -0.0242 0.1152  523  ALA B CB  
12563 N N   . MET B 526  ? 0.4180 0.7433 0.4678 -0.1575 -0.0286 0.1034  524  MET B N   
12564 C CA  . MET B 526  ? 0.4110 0.7338 0.4651 -0.1488 -0.0269 0.0975  524  MET B CA  
12565 C C   . MET B 526  ? 0.4160 0.7296 0.4699 -0.1519 -0.0325 0.0961  524  MET B C   
12566 O O   . MET B 526  ? 0.4074 0.7102 0.4558 -0.1611 -0.0382 0.0987  524  MET B O   
12567 C CB  . MET B 526  ? 0.4425 0.7458 0.4896 -0.1425 -0.0258 0.0926  524  MET B CB  
12568 C CG  . MET B 526  ? 0.4249 0.7383 0.4727 -0.1371 -0.0196 0.0929  524  MET B CG  
12569 S SD  . MET B 526  ? 0.5805 0.8714 0.6200 -0.1291 -0.0184 0.0870  524  MET B SD  
12570 C CE  . MET B 526  ? 0.5166 0.8003 0.5591 -0.1174 -0.0173 0.0794  524  MET B CE  
12571 N N   . PRO B 527  ? 0.4553 0.7718 0.5141 -0.1437 -0.0310 0.0917  525  PRO B N   
12572 C CA  . PRO B 527  ? 0.4364 0.7462 0.4954 -0.1466 -0.0361 0.0905  525  PRO B CA  
12573 C C   . PRO B 527  ? 0.4201 0.7025 0.4693 -0.1492 -0.0414 0.0873  525  PRO B C   
12574 O O   . PRO B 527  ? 0.3607 0.6361 0.4072 -0.1572 -0.0473 0.0889  525  PRO B O   
12575 C CB  . PRO B 527  ? 0.3884 0.7053 0.4533 -0.1351 -0.0324 0.0860  525  PRO B CB  
12576 C CG  . PRO B 527  ? 0.4423 0.7564 0.5059 -0.1255 -0.0269 0.0824  525  PRO B CG  
12577 C CD  . PRO B 527  ? 0.4536 0.7758 0.5162 -0.1307 -0.0249 0.0871  525  PRO B CD  
12578 N N   . VAL B 528  ? 0.4050 0.6719 0.4487 -0.1426 -0.0395 0.0829  526  VAL B N   
12579 C CA  . VAL B 528  ? 0.3671 0.6084 0.4014 -0.1443 -0.0440 0.0798  526  VAL B CA  
12580 C C   . VAL B 528  ? 0.3564 0.5907 0.3852 -0.1462 -0.0431 0.0813  526  VAL B C   
12581 O O   . VAL B 528  ? 0.4018 0.6364 0.4309 -0.1382 -0.0382 0.0787  526  VAL B O   
12582 C CB  . VAL B 528  ? 0.3587 0.5872 0.3916 -0.1340 -0.0429 0.0726  526  VAL B CB  
12583 C CG1 . VAL B 528  ? 0.3815 0.5848 0.4047 -0.1345 -0.0466 0.0693  526  VAL B CG1 
12584 C CG2 . VAL B 528  ? 0.3684 0.6012 0.4052 -0.1333 -0.0449 0.0713  526  VAL B CG2 
12585 N N   . VAL B 529  ? 0.3727 0.6001 0.3961 -0.1569 -0.0479 0.0857  527  VAL B N   
12586 C CA  . VAL B 529  ? 0.3322 0.5526 0.3499 -0.1595 -0.0475 0.0877  527  VAL B CA  
12587 C C   . VAL B 529  ? 0.3525 0.5507 0.3633 -0.1523 -0.0479 0.0816  527  VAL B C   
12588 O O   . VAL B 529  ? 0.3729 0.5535 0.3788 -0.1522 -0.0524 0.0781  527  VAL B O   
12589 C CB  . VAL B 529  ? 0.3292 0.5454 0.3420 -0.1730 -0.0533 0.0938  527  VAL B CB  
12590 C CG1 . VAL B 529  ? 0.3671 0.5715 0.3722 -0.1754 -0.0538 0.0953  527  VAL B CG1 
12591 C CG2 . VAL B 529  ? 0.4080 0.6494 0.4285 -0.1803 -0.0521 0.1005  527  VAL B CG2 
12592 N N   . GLY B 530  ? 0.3520 0.5514 0.3624 -0.1459 -0.0432 0.0801  528  GLY B N   
12593 C CA  . GLY B 530  ? 0.3166 0.4965 0.3210 -0.1394 -0.0434 0.0748  528  GLY B CA  
12594 C C   . GLY B 530  ? 0.3513 0.5286 0.3588 -0.1283 -0.0405 0.0682  528  GLY B C   
12595 O O   . GLY B 530  ? 0.3343 0.4948 0.3370 -0.1231 -0.0412 0.0636  528  GLY B O   
12596 N N   . ALA B 531  ? 0.3032 0.4967 0.3186 -0.1245 -0.0372 0.0678  529  ALA B N   
12597 C CA  . ALA B 531  ? 0.3197 0.5115 0.3381 -0.1140 -0.0343 0.0620  529  ALA B CA  
12598 C C   . ALA B 531  ? 0.3116 0.4989 0.3285 -0.1059 -0.0301 0.0586  529  ALA B C   
12599 O O   . ALA B 531  ? 0.3260 0.5230 0.3439 -0.1056 -0.0268 0.0610  529  ALA B O   
12600 C CB  . ALA B 531  ? 0.3458 0.5579 0.3731 -0.1112 -0.0310 0.0630  529  ALA B CB  
12601 N N   . LYS B 532  ? 0.2742 0.4471 0.2886 -0.0993 -0.0305 0.0531  530  LYS B N   
12602 C CA  . LYS B 532  ? 0.3130 0.4806 0.3263 -0.0910 -0.0270 0.0492  530  LYS B CA  
12603 C C   . LYS B 532  ? 0.3399 0.5250 0.3598 -0.0849 -0.0212 0.0492  530  LYS B C   
12604 O O   . LYS B 532  ? 0.2933 0.4922 0.3191 -0.0844 -0.0198 0.0504  530  LYS B O   
12605 C CB  . LYS B 532  ? 0.3150 0.4677 0.3264 -0.0850 -0.0281 0.0433  530  LYS B CB  
12606 C CG  . LYS B 532  ? 0.3658 0.5130 0.3766 -0.0764 -0.0247 0.0390  530  LYS B CG  
12607 C CD  . LYS B 532  ? 0.3449 0.4792 0.3545 -0.0709 -0.0258 0.0337  530  LYS B CD  
12608 C CE  . LYS B 532  ? 0.3248 0.4668 0.3396 -0.0681 -0.0247 0.0325  530  LYS B CE  
12609 N NZ  . LYS B 532  ? 0.3277 0.4830 0.3485 -0.0616 -0.0197 0.0319  530  LYS B NZ  
12610 N N   . HIS B 533  ? 0.2823 0.4665 0.3007 -0.0799 -0.0179 0.0477  531  HIS B N   
12611 C CA  . HIS B 533  ? 0.2643 0.4623 0.2879 -0.0726 -0.0125 0.0466  531  HIS B CA  
12612 C C   . HIS B 533  ? 0.3460 0.5438 0.3737 -0.0656 -0.0114 0.0425  531  HIS B C   
12613 O O   . HIS B 533  ? 0.2890 0.4724 0.3142 -0.0627 -0.0131 0.0386  531  HIS B O   
12614 C CB  . HIS B 533  ? 0.2833 0.4766 0.3035 -0.0678 -0.0099 0.0447  531  HIS B CB  
12615 C CG  . HIS B 533  ? 0.3594 0.5679 0.3836 -0.0618 -0.0047 0.0445  531  HIS B CG  
12616 N ND1 . HIS B 533  ? 0.3715 0.5838 0.3999 -0.0535 -0.0019 0.0409  531  HIS B ND1 
12617 C CD2 . HIS B 533  ? 0.3790 0.5997 0.4033 -0.0628 -0.0018 0.0476  531  HIS B CD2 
12618 C CE1 . HIS B 533  ? 0.4207 0.6464 0.4516 -0.0492 0.0024  0.0414  531  HIS B CE1 
12619 N NE2 . HIS B 533  ? 0.4104 0.6419 0.4388 -0.0547 0.0027  0.0454  531  HIS B NE2 
12620 N N   . ASP B 534  ? 0.3441 0.5584 0.3782 -0.0627 -0.0085 0.0436  532  ASP B N   
12621 C CA  . ASP B 534  ? 0.3876 0.6031 0.4257 -0.0566 -0.0077 0.0404  532  ASP B CA  
12622 C C   . ASP B 534  ? 0.3368 0.5435 0.3738 -0.0477 -0.0053 0.0353  532  ASP B C   
12623 O O   . ASP B 534  ? 0.3409 0.5425 0.3792 -0.0435 -0.0056 0.0323  532  ASP B O   
12624 C CB  . ASP B 534  ? 0.3805 0.6163 0.4256 -0.0550 -0.0050 0.0428  532  ASP B CB  
12625 C CG  . ASP B 534  ? 0.5371 0.7820 0.5846 -0.0635 -0.0079 0.0475  532  ASP B CG  
12626 O OD1 . ASP B 534  ? 0.5620 0.7964 0.6069 -0.0684 -0.0122 0.0474  532  ASP B OD1 
12627 O OD2 . ASP B 534  ? 0.6315 0.8941 0.6833 -0.0653 -0.0059 0.0513  532  ASP B OD2 
12628 N N   . ARG B 535  ? 0.2929 0.4981 0.3274 -0.0449 -0.0030 0.0345  533  ARG B N   
12629 C CA  . ARG B 535  ? 0.3028 0.5009 0.3364 -0.0366 -0.0007 0.0299  533  ARG B CA  
12630 C C   . ARG B 535  ? 0.3306 0.5106 0.3584 -0.0370 -0.0029 0.0272  533  ARG B C   
12631 O O   . ARG B 535  ? 0.3353 0.5088 0.3620 -0.0309 -0.0013 0.0236  533  ARG B O   
12632 C CB  . ARG B 535  ? 0.3754 0.5842 0.4100 -0.0320 0.0035  0.0302  533  ARG B CB  
12633 N N   . ILE B 536  ? 0.2518 0.4235 0.2760 -0.0439 -0.0067 0.0289  534  ILE B N   
12634 C CA  . ILE B 536  ? 0.3038 0.4585 0.3226 -0.0440 -0.0090 0.0264  534  ILE B CA  
12635 C C   . ILE B 536  ? 0.2783 0.4231 0.2964 -0.0455 -0.0124 0.0246  534  ILE B C   
12636 O O   . ILE B 536  ? 0.2822 0.4280 0.2999 -0.0516 -0.0152 0.0272  534  ILE B O   
12637 C CB  . ILE B 536  ? 0.2724 0.4233 0.2861 -0.0501 -0.0109 0.0293  534  ILE B CB  
12638 C CG1 . ILE B 536  ? 0.3396 0.5020 0.3539 -0.0487 -0.0073 0.0313  534  ILE B CG1 
12639 C CG2 . ILE B 536  ? 0.3119 0.4455 0.3203 -0.0491 -0.0133 0.0264  534  ILE B CG2 
12640 C CD1 . ILE B 536  ? 0.3210 0.4791 0.3299 -0.0538 -0.0087 0.0340  534  ILE B CD1 
12641 N N   . ALA B 537  ? 0.2745 0.4097 0.2921 -0.0400 -0.0121 0.0203  535  ALA B N   
12642 C CA  . ALA B 537  ? 0.2747 0.4008 0.2915 -0.0405 -0.0148 0.0182  535  ALA B CA  
12643 C C   . ALA B 537  ? 0.2508 0.3631 0.2617 -0.0447 -0.0188 0.0179  535  ALA B C   
12644 O O   . ALA B 537  ? 0.2306 0.3354 0.2383 -0.0433 -0.0188 0.0167  535  ALA B O   
12645 C CB  . ALA B 537  ? 0.2794 0.4013 0.2980 -0.0332 -0.0129 0.0139  535  ALA B CB  
12646 N N   . LEU B 538  ? 0.2628 0.3714 0.2718 -0.0498 -0.0223 0.0190  536  LEU B N   
12647 C CA  . LEU B 538  ? 0.2676 0.3609 0.2708 -0.0522 -0.0264 0.0175  536  LEU B CA  
12648 C C   . LEU B 538  ? 0.2739 0.3581 0.2768 -0.0455 -0.0255 0.0127  536  LEU B C   
12649 O O   . LEU B 538  ? 0.2449 0.3337 0.2518 -0.0406 -0.0228 0.0107  536  LEU B O   
12650 C CB  . LEU B 538  ? 0.3018 0.3924 0.3035 -0.0572 -0.0301 0.0185  536  LEU B CB  
12651 C CG  . LEU B 538  ? 0.3382 0.4338 0.3386 -0.0655 -0.0326 0.0234  536  LEU B CG  
12652 C CD1 . LEU B 538  ? 0.3227 0.4166 0.3222 -0.0697 -0.0361 0.0238  536  LEU B CD1 
12653 C CD2 . LEU B 538  ? 0.3169 0.4019 0.3111 -0.0693 -0.0355 0.0246  536  LEU B CD2 
12654 N N   . PRO B 539  ? 0.2520 0.3237 0.2502 -0.0451 -0.0276 0.0109  537  PRO B N   
12655 C CA  . PRO B 539  ? 0.2506 0.3150 0.2490 -0.0388 -0.0266 0.0064  537  PRO B CA  
12656 C C   . PRO B 539  ? 0.2296 0.2934 0.2299 -0.0365 -0.0266 0.0039  537  PRO B C   
12657 O O   . PRO B 539  ? 0.2550 0.3205 0.2585 -0.0310 -0.0238 0.0014  537  PRO B O   
12658 C CB  . PRO B 539  ? 0.2193 0.2702 0.2118 -0.0402 -0.0302 0.0055  537  PRO B CB  
12659 C CG  . PRO B 539  ? 0.2376 0.2911 0.2277 -0.0458 -0.0313 0.0097  537  PRO B CG  
12660 C CD  . PRO B 539  ? 0.2430 0.3073 0.2357 -0.0503 -0.0310 0.0130  537  PRO B CD  
12661 N N   . ALA B 540  ? 0.2288 0.2908 0.2271 -0.0407 -0.0295 0.0049  538  ALA B N   
12662 C CA  . ALA B 540  ? 0.2802 0.3419 0.2797 -0.0386 -0.0295 0.0027  538  ALA B CA  
12663 C C   . ALA B 540  ? 0.3110 0.3852 0.3164 -0.0359 -0.0258 0.0034  538  ALA B C   
12664 O O   . ALA B 540  ? 0.2628 0.3370 0.2699 -0.0323 -0.0247 0.0011  538  ALA B O   
12665 C CB  . ALA B 540  ? 0.2446 0.3019 0.2401 -0.0441 -0.0337 0.0037  538  ALA B CB  
12666 N N   . GLU B 541  ? 0.2947 0.3795 0.3032 -0.0374 -0.0240 0.0066  539  GLU B N   
12667 C CA  . GLU B 541  ? 0.2970 0.3942 0.3109 -0.0352 -0.0211 0.0077  539  GLU B CA  
12668 C C   . GLU B 541  ? 0.2796 0.3813 0.2968 -0.0295 -0.0171 0.0067  539  GLU B C   
12669 O O   . GLU B 541  ? 0.2777 0.3900 0.2990 -0.0274 -0.0146 0.0079  539  GLU B O   
12670 C CB  . GLU B 541  ? 0.2670 0.3744 0.2823 -0.0408 -0.0220 0.0120  539  GLU B CB  
12671 C CG  . GLU B 541  ? 0.3361 0.4388 0.3483 -0.0464 -0.0263 0.0128  539  GLU B CG  
12672 C CD  . GLU B 541  ? 0.4964 0.6076 0.5093 -0.0534 -0.0281 0.0173  539  GLU B CD  
12673 O OE1 . GLU B 541  ? 0.4866 0.6092 0.5030 -0.0538 -0.0257 0.0201  539  GLU B OE1 
12674 O OE2 . GLU B 541  ? 0.5306 0.6370 0.5402 -0.0586 -0.0321 0.0181  539  GLU B OE2 
12675 N N   . LEU B 542  ? 0.2391 0.3324 0.2542 -0.0267 -0.0168 0.0042  540  LEU B N   
12676 C CA  . LEU B 542  ? 0.2158 0.3118 0.2331 -0.0217 -0.0135 0.0031  540  LEU B CA  
12677 C C   . LEU B 542  ? 0.2661 0.3669 0.2875 -0.0167 -0.0110 0.0017  540  LEU B C   
12678 O O   . LEU B 542  ? 0.2421 0.3482 0.2659 -0.0130 -0.0083 0.0016  540  LEU B O   
12679 C CB  . LEU B 542  ? 0.2674 0.3526 0.2819 -0.0195 -0.0141 0.0004  540  LEU B CB  
12680 C CG  . LEU B 542  ? 0.3316 0.4130 0.3431 -0.0209 -0.0149 0.0010  540  LEU B CG  
12681 C CD1 . LEU B 542  ? 0.2811 0.3547 0.2920 -0.0164 -0.0143 -0.0024 540  LEU B CD1 
12682 C CD2 . LEU B 542  ? 0.2438 0.3350 0.2565 -0.0215 -0.0127 0.0037  540  LEU B CD2 
12683 N N   . PHE B 543  ? 0.2413 0.3396 0.2630 -0.0164 -0.0119 0.0005  541  PHE B N   
12684 C CA  . PHE B 543  ? 0.2399 0.3416 0.2648 -0.0119 -0.0098 -0.0007 541  PHE B CA  
12685 C C   . PHE B 543  ? 0.2838 0.3948 0.3113 -0.0131 -0.0098 0.0016  541  PHE B C   
12686 O O   . PHE B 543  ? 0.2750 0.3881 0.3047 -0.0099 -0.0086 0.0008  541  PHE B O   
12687 C CB  . PHE B 543  ? 0.1975 0.2903 0.2210 -0.0099 -0.0104 -0.0037 541  PHE B CB  
12688 C CG  . PHE B 543  ? 0.2295 0.3138 0.2509 -0.0087 -0.0107 -0.0058 541  PHE B CG  
12689 C CD1 . PHE B 543  ? 0.2882 0.3736 0.3107 -0.0059 -0.0088 -0.0062 541  PHE B CD1 
12690 C CD2 . PHE B 543  ? 0.1898 0.2653 0.2077 -0.0103 -0.0131 -0.0074 541  PHE B CD2 
12691 C CE1 . PHE B 543  ? 0.2579 0.3359 0.2785 -0.0049 -0.0093 -0.0080 541  PHE B CE1 
12692 C CE2 . PHE B 543  ? 0.2481 0.3164 0.2642 -0.0090 -0.0135 -0.0093 541  PHE B CE2 
12693 C CZ  . PHE B 543  ? 0.2865 0.3563 0.3042 -0.0064 -0.0116 -0.0095 541  PHE B CZ  
12694 N N   . GLY B 544  ? 0.2718 0.3885 0.2992 -0.0178 -0.0112 0.0044  542  GLY B N   
12695 C CA  . GLY B 544  ? 0.2743 0.4013 0.3047 -0.0191 -0.0112 0.0068  542  GLY B CA  
12696 C C   . GLY B 544  ? 0.3526 0.4760 0.3820 -0.0199 -0.0131 0.0059  542  GLY B C   
12697 O O   . GLY B 544  ? 0.2742 0.3881 0.2997 -0.0221 -0.0154 0.0044  542  GLY B O   
12698 N N   . ASP B 545  ? 0.2944 0.4255 0.3271 -0.0178 -0.0122 0.0068  543  ASP B N   
12699 C CA  . ASP B 545  ? 0.3880 0.5169 0.4197 -0.0185 -0.0139 0.0062  543  ASP B CA  
12700 C C   . ASP B 545  ? 0.3454 0.4654 0.3754 -0.0144 -0.0130 0.0029  543  ASP B C   
12701 O O   . ASP B 545  ? 0.3525 0.4692 0.3806 -0.0150 -0.0145 0.0021  543  ASP B O   
12702 C CB  . ASP B 545  ? 0.4067 0.5472 0.4424 -0.0175 -0.0134 0.0085  543  ASP B CB  
12703 C CG  . ASP B 545  ? 0.5061 0.6574 0.5443 -0.0213 -0.0140 0.0119  543  ASP B CG  
12704 O OD1 . ASP B 545  ? 0.5017 0.6505 0.5373 -0.0271 -0.0165 0.0129  543  ASP B OD1 
12705 O OD2 . ASP B 545  ? 0.6503 0.8124 0.6929 -0.0185 -0.0120 0.0135  543  ASP B OD2 
12706 N N   . ALA B 546  ? 0.3014 0.4177 0.3319 -0.0106 -0.0108 0.0012  544  ALA B N   
12707 C CA  . ALA B 546  ? 0.3219 0.4308 0.3513 -0.0071 -0.0099 -0.0015 544  ALA B CA  
12708 C C   . ALA B 546  ? 0.3297 0.4294 0.3549 -0.0094 -0.0121 -0.0035 544  ALA B C   
12709 O O   . ALA B 546  ? 0.3050 0.4015 0.3288 -0.0083 -0.0123 -0.0049 544  ALA B O   
12710 C CB  . ALA B 546  ? 0.3048 0.4113 0.3353 -0.0033 -0.0076 -0.0028 544  ALA B CB  
12711 N N   . ARG B 547  ? 0.2838 0.3789 0.3063 -0.0124 -0.0137 -0.0037 545  ARG B N   
12712 C CA  . ARG B 547  ? 0.2867 0.3722 0.3048 -0.0140 -0.0159 -0.0059 545  ARG B CA  
12713 C C   . ARG B 547  ? 0.2745 0.3564 0.2900 -0.0178 -0.0180 -0.0051 545  ARG B C   
12714 O O   . ARG B 547  ? 0.2498 0.3361 0.2672 -0.0184 -0.0171 -0.0033 545  ARG B O   
12715 C CB  . ARG B 547  ? 0.3282 0.4073 0.3460 -0.0098 -0.0144 -0.0089 545  ARG B CB  
12716 C CG  . ARG B 547  ? 0.2684 0.3468 0.2880 -0.0077 -0.0127 -0.0092 545  ARG B CG  
12717 C CD  . ARG B 547  ? 0.3093 0.3823 0.3290 -0.0040 -0.0114 -0.0120 545  ARG B CD  
12718 N NE  . ARG B 547  ? 0.2951 0.3694 0.3173 -0.0015 -0.0094 -0.0120 545  ARG B NE  
12719 C CZ  . ARG B 547  ? 0.2962 0.3658 0.3174 -0.0012 -0.0098 -0.0131 545  ARG B CZ  
12720 N NH1 . ARG B 547  ? 0.2565 0.3194 0.2745 -0.0028 -0.0120 -0.0144 545  ARG B NH1 
12721 N NH2 . ARG B 547  ? 0.2821 0.3535 0.3054 0.0010  -0.0081 -0.0130 545  ARG B NH2 
12722 N N   . THR B 548  ? 0.2376 0.3113 0.2486 -0.0201 -0.0209 -0.0065 546  THR B N   
12723 C CA  . THR B 548  ? 0.2152 0.2831 0.2225 -0.0239 -0.0236 -0.0059 546  THR B CA  
12724 C C   . THR B 548  ? 0.2427 0.3033 0.2490 -0.0208 -0.0229 -0.0082 546  THR B C   
12725 O O   . THR B 548  ? 0.2079 0.2631 0.2133 -0.0175 -0.0226 -0.0112 546  THR B O   
12726 C CB  . THR B 548  ? 0.2444 0.3057 0.2467 -0.0275 -0.0275 -0.0065 546  THR B CB  
12727 O OG1 . THR B 548  ? 0.2814 0.3501 0.2851 -0.0301 -0.0281 -0.0044 546  THR B OG1 
12728 C CG2 . THR B 548  ? 0.2478 0.3029 0.2460 -0.0320 -0.0307 -0.0054 546  THR B CG2 
12729 N N   . ASN B 549  ? 0.2104 0.2716 0.2169 -0.0220 -0.0228 -0.0068 547  ASN B N   
12730 C CA  . ASN B 549  ? 0.2460 0.3003 0.2512 -0.0196 -0.0226 -0.0087 547  ASN B CA  
12731 C C   . ASN B 549  ? 0.2382 0.2813 0.2381 -0.0207 -0.0261 -0.0107 547  ASN B C   
12732 O O   . ASN B 549  ? 0.2778 0.3178 0.2741 -0.0250 -0.0293 -0.0096 547  ASN B O   
12733 C CB  . ASN B 549  ? 0.2338 0.2912 0.2395 -0.0214 -0.0222 -0.0063 547  ASN B CB  
12734 C CG  . ASN B 549  ? 0.1976 0.2493 0.2026 -0.0183 -0.0216 -0.0081 547  ASN B CG  
12735 O OD1 . ASN B 549  ? 0.2304 0.2783 0.2362 -0.0143 -0.0208 -0.0110 547  ASN B OD1 
12736 N ND2 . ASN B 549  ? 0.2493 0.3010 0.2528 -0.0205 -0.0222 -0.0061 547  ASN B ND2 
12737 N N   . SER B 550  ? 0.2505 0.2873 0.2499 -0.0168 -0.0258 -0.0137 548  SER B N   
12738 C CA  . SER B 550  ? 0.2351 0.2610 0.2293 -0.0169 -0.0291 -0.0159 548  SER B CA  
12739 C C   . SER B 550  ? 0.2310 0.2521 0.2215 -0.0209 -0.0320 -0.0138 548  SER B C   
12740 O O   . SER B 550  ? 0.2795 0.3052 0.2719 -0.0221 -0.0308 -0.0115 548  SER B O   
12741 C CB  . SER B 550  ? 0.2453 0.2672 0.2405 -0.0116 -0.0279 -0.0193 548  SER B CB  
12742 O OG  . SER B 550  ? 0.2435 0.2680 0.2416 -0.0100 -0.0260 -0.0187 548  SER B OG  
12743 N N   . ALA B 551  ? 0.2349 0.2462 0.2197 -0.0229 -0.0360 -0.0147 549  ALA B N   
12744 C CA  . ALA B 551  ? 0.2559 0.2607 0.2361 -0.0271 -0.0395 -0.0127 549  ALA B CA  
12745 C C   . ALA B 551  ? 0.2731 0.2676 0.2501 -0.0238 -0.0414 -0.0154 549  ALA B C   
12746 O O   . ALA B 551  ? 0.2479 0.2371 0.2237 -0.0198 -0.0418 -0.0190 549  ALA B O   
12747 C CB  . ALA B 551  ? 0.2860 0.2862 0.2613 -0.0325 -0.0435 -0.0113 549  ALA B CB  
12748 N N   . GLY B 552  ? 0.2886 0.2806 0.2642 -0.0254 -0.0424 -0.0135 550  GLY B N   
12749 C CA  . GLY B 552  ? 0.3095 0.2914 0.2816 -0.0228 -0.0448 -0.0154 550  GLY B CA  
12750 C C   . GLY B 552  ? 0.2973 0.2676 0.2620 -0.0269 -0.0502 -0.0145 550  GLY B C   
12751 O O   . GLY B 552  ? 0.3187 0.2874 0.2804 -0.0313 -0.0524 -0.0131 550  GLY B O   
12752 N N   . LEU B 553  ? 0.3189 0.2804 0.2801 -0.0254 -0.0526 -0.0151 551  LEU B N   
12753 C CA  . LEU B 553  ? 0.3627 0.3117 0.3161 -0.0291 -0.0582 -0.0140 551  LEU B CA  
12754 C C   . LEU B 553  ? 0.3119 0.2589 0.2637 -0.0309 -0.0591 -0.0112 551  LEU B C   
12755 O O   . LEU B 553  ? 0.3385 0.2891 0.2939 -0.0268 -0.0566 -0.0122 551  LEU B O   
12756 C CB  . LEU B 553  ? 0.3827 0.3198 0.3317 -0.0245 -0.0614 -0.0185 551  LEU B CB  
12757 C CG  . LEU B 553  ? 0.3958 0.3328 0.3445 -0.0228 -0.0612 -0.0215 551  LEU B CG  
12758 C CD1 . LEU B 553  ? 0.4006 0.3283 0.3465 -0.0163 -0.0630 -0.0265 551  LEU B CD1 
12759 C CD2 . LEU B 553  ? 0.3763 0.3095 0.3201 -0.0295 -0.0646 -0.0193 551  LEU B CD2 
12760 N N   . ASP B 554  ? 0.3650 0.3067 0.3114 -0.0374 -0.0628 -0.0075 552  ASP B N   
12761 C CA  . ASP B 554  ? 0.3815 0.3225 0.3261 -0.0401 -0.0635 -0.0040 552  ASP B CA  
12762 C C   . ASP B 554  ? 0.3705 0.2964 0.3087 -0.0378 -0.0682 -0.0056 552  ASP B C   
12763 O O   . ASP B 554  ? 0.3521 0.2663 0.2833 -0.0413 -0.0734 -0.0048 552  ASP B O   
12764 C CB  . ASP B 554  ? 0.3655 0.3095 0.3077 -0.0486 -0.0648 0.0014  552  ASP B CB  
12765 C CG  . ASP B 554  ? 0.3858 0.3304 0.3260 -0.0517 -0.0652 0.0053  552  ASP B CG  
12766 O OD1 . ASP B 554  ? 0.3626 0.3040 0.3026 -0.0472 -0.0648 0.0038  552  ASP B OD1 
12767 O OD2 . ASP B 554  ? 0.4002 0.3490 0.3389 -0.0588 -0.0657 0.0101  552  ASP B OD2 
12768 N N   . LEU B 555  ? 0.3482 0.2743 0.2888 -0.0320 -0.0668 -0.0079 553  LEU B N   
12769 C CA  . LEU B 555  ? 0.3848 0.2975 0.3200 -0.0289 -0.0711 -0.0097 553  LEU B CA  
12770 C C   . LEU B 555  ? 0.4010 0.3073 0.3304 -0.0337 -0.0745 -0.0054 553  LEU B C   
12771 O O   . LEU B 555  ? 0.3923 0.2879 0.3173 -0.0310 -0.0781 -0.0065 553  LEU B O   
12772 C CB  . LEU B 555  ? 0.3769 0.2928 0.3172 -0.0209 -0.0685 -0.0137 553  LEU B CB  
12773 C CG  . LEU B 555  ? 0.4013 0.3219 0.3466 -0.0155 -0.0657 -0.0182 553  LEU B CG  
12774 C CD1 . LEU B 555  ? 0.3975 0.3201 0.3471 -0.0082 -0.0640 -0.0218 553  LEU B CD1 
12775 C CD2 . LEU B 555  ? 0.4323 0.3429 0.3724 -0.0153 -0.0694 -0.0205 553  LEU B CD2 
12776 N N   . SER B 556  ? 0.3567 0.2695 0.2859 -0.0406 -0.0735 -0.0005 554  SER B N   
12777 C CA  . SER B 556  ? 0.3500 0.2566 0.2729 -0.0465 -0.0770 0.0042  554  SER B CA  
12778 C C   . SER B 556  ? 0.3827 0.2812 0.2992 -0.0537 -0.0816 0.0071  554  SER B C   
12779 O O   . SER B 556  ? 0.4091 0.3003 0.3192 -0.0593 -0.0854 0.0112  554  SER B O   
12780 C CB  . SER B 556  ? 0.3659 0.2859 0.2924 -0.0496 -0.0727 0.0082  554  SER B CB  
12781 O OG  . SER B 556  ? 0.3889 0.3200 0.3189 -0.0542 -0.0699 0.0105  554  SER B OG  
12782 N N   . ASN B 557  ? 0.3742 0.2735 0.2921 -0.0538 -0.0815 0.0050  555  ASN B N   
12783 C CA  . ASN B 557  ? 0.4030 0.2956 0.3155 -0.0607 -0.0858 0.0073  555  ASN B CA  
12784 C C   . ASN B 557  ? 0.3828 0.2566 0.2876 -0.0582 -0.0920 0.0040  555  ASN B C   
12785 O O   . ASN B 557  ? 0.3923 0.2634 0.2986 -0.0511 -0.0914 -0.0014 555  ASN B O   
12786 C CB  . ASN B 557  ? 0.3765 0.2806 0.2947 -0.0618 -0.0824 0.0066  555  ASN B CB  
12787 C CG  . ASN B 557  ? 0.4068 0.3058 0.3201 -0.0695 -0.0866 0.0092  555  ASN B CG  
12788 O OD1 . ASN B 557  ? 0.4085 0.2917 0.3142 -0.0704 -0.0924 0.0079  555  ASN B OD1 
12789 N ND2 . ASN B 557  ? 0.3620 0.2743 0.2796 -0.0753 -0.0839 0.0130  555  ASN B ND2 
12790 N N   . GLU B 558  ? 0.4456 0.3063 0.3417 -0.0637 -0.0979 0.0073  556  GLU B N   
12791 C CA  . GLU B 558  ? 0.4552 0.2965 0.3431 -0.0609 -0.1043 0.0043  556  GLU B CA  
12792 C C   . GLU B 558  ? 0.4598 0.2957 0.3455 -0.0606 -0.1064 0.0009  556  GLU B C   
12793 O O   . GLU B 558  ? 0.5024 0.3269 0.3844 -0.0543 -0.1092 -0.0041 556  GLU B O   
12794 C CB  . GLU B 558  ? 0.4571 0.2848 0.3357 -0.0675 -0.1105 0.0090  556  GLU B CB  
12795 C CG  . GLU B 558  ? 0.4352 0.2651 0.3141 -0.0669 -0.1094 0.0118  556  GLU B CG  
12796 C CD  . GLU B 558  ? 0.4768 0.2993 0.3552 -0.0574 -0.1103 0.0071  556  GLU B CD  
12797 O OE1 . GLU B 558  ? 0.4996 0.3144 0.3770 -0.0509 -0.1120 0.0016  556  GLU B OE1 
12798 O OE2 . GLU B 558  ? 0.4784 0.3033 0.3574 -0.0564 -0.1093 0.0090  556  GLU B OE2 
12799 N N   . GLU B 559  ? 0.4565 0.3002 0.3440 -0.0672 -0.1054 0.0036  557  GLU B N   
12800 C CA  . GLU B 559  ? 0.4659 0.3066 0.3522 -0.0665 -0.1067 0.0002  557  GLU B CA  
12801 C C   . GLU B 559  ? 0.4281 0.2755 0.3206 -0.0568 -0.1020 -0.0059 557  GLU B C   
12802 O O   . GLU B 559  ? 0.4149 0.2528 0.3038 -0.0517 -0.1043 -0.0109 557  GLU B O   
12803 C CB  . GLU B 559  ? 0.5076 0.3596 0.3971 -0.0746 -0.1052 0.0041  557  GLU B CB  
12804 C CG  . GLU B 559  ? 0.5686 0.4146 0.4519 -0.0854 -0.1102 0.0101  557  GLU B CG  
12805 C CD  . GLU B 559  ? 0.6416 0.5010 0.5294 -0.0924 -0.1083 0.0132  557  GLU B CD  
12806 O OE1 . GLU B 559  ? 0.6851 0.5525 0.5778 -0.0887 -0.1050 0.0098  557  GLU B OE1 
12807 O OE2 . GLU B 559  ? 0.6240 0.4863 0.5103 -0.1017 -0.1100 0.0193  557  GLU B OE2 
12808 N N   . THR B 560  ? 0.3924 0.2564 0.2942 -0.0542 -0.0953 -0.0055 558  THR B N   
12809 C CA  . THR B 560  ? 0.4079 0.2796 0.3162 -0.0457 -0.0905 -0.0105 558  THR B CA  
12810 C C   . THR B 560  ? 0.4153 0.2769 0.3211 -0.0376 -0.0922 -0.0150 558  THR B C   
12811 O O   . THR B 560  ? 0.4028 0.2619 0.3088 -0.0312 -0.0918 -0.0201 558  THR B O   
12812 C CB  . THR B 560  ? 0.4099 0.2999 0.3278 -0.0451 -0.0836 -0.0087 558  THR B CB  
12813 O OG1 . THR B 560  ? 0.4091 0.3095 0.3298 -0.0521 -0.0819 -0.0047 558  THR B OG1 
12814 C CG2 . THR B 560  ? 0.3641 0.2620 0.2887 -0.0370 -0.0788 -0.0135 558  THR B CG2 
12815 N N   . LEU B 561  ? 0.3901 0.2464 0.2935 -0.0375 -0.0940 -0.0131 559  LEU B N   
12816 C CA  . LEU B 561  ? 0.4091 0.2564 0.3105 -0.0297 -0.0959 -0.0171 559  LEU B CA  
12817 C C   . LEU B 561  ? 0.4204 0.2507 0.3132 -0.0275 -0.1019 -0.0206 559  LEU B C   
12818 O O   . LEU B 561  ? 0.4597 0.2865 0.3527 -0.0194 -0.1019 -0.0259 559  LEU B O   
12819 C CB  . LEU B 561  ? 0.3986 0.2421 0.2980 -0.0307 -0.0976 -0.0140 559  LEU B CB  
12820 C CG  . LEU B 561  ? 0.4031 0.2627 0.3108 -0.0308 -0.0916 -0.0117 559  LEU B CG  
12821 C CD1 . LEU B 561  ? 0.3760 0.2308 0.2802 -0.0329 -0.0939 -0.0081 559  LEU B CD1 
12822 C CD2 . LEU B 561  ? 0.3416 0.2097 0.2568 -0.0223 -0.0870 -0.0165 559  LEU B CD2 
12823 N N   . ALA B 562  ? 0.4529 0.2725 0.3378 -0.0347 -0.1072 -0.0177 560  ALA B N   
12824 C CA  . ALA B 562  ? 0.4391 0.2411 0.3148 -0.0328 -0.1134 -0.0211 560  ALA B CA  
12825 C C   . ALA B 562  ? 0.4875 0.2930 0.3650 -0.0288 -0.1114 -0.0259 560  ALA B C   
12826 O O   . ALA B 562  ? 0.4539 0.2515 0.3284 -0.0212 -0.1130 -0.0314 560  ALA B O   
12827 C CB  . ALA B 562  ? 0.4644 0.2540 0.3311 -0.0423 -0.1198 -0.0165 560  ALA B CB  
12828 N N   . SER B 563  ? 0.4249 0.2428 0.3072 -0.0336 -0.1078 -0.0240 561  SER B N   
12829 C CA  . SER B 563  ? 0.4311 0.2524 0.3148 -0.0300 -0.1059 -0.0285 561  SER B CA  
12830 C C   . SER B 563  ? 0.4439 0.2758 0.3353 -0.0207 -0.1001 -0.0328 561  SER B C   
12831 O O   . SER B 563  ? 0.4630 0.2926 0.3532 -0.0147 -0.0998 -0.0379 561  SER B O   
12832 C CB  . SER B 563  ? 0.4987 0.3306 0.3856 -0.0374 -0.1038 -0.0252 561  SER B CB  
12833 O OG  . SER B 563  ? 0.5477 0.3980 0.4449 -0.0374 -0.0969 -0.0230 561  SER B OG  
12834 N N   . LEU B 564  ? 0.4278 0.2712 0.3269 -0.0196 -0.0955 -0.0308 562  LEU B N   
12835 C CA  . LEU B 564  ? 0.4208 0.2738 0.3273 -0.0113 -0.0904 -0.0346 562  LEU B CA  
12836 C C   . LEU B 564  ? 0.4447 0.2867 0.3473 -0.0034 -0.0934 -0.0390 562  LEU B C   
12837 O O   . LEU B 564  ? 0.4248 0.2702 0.3301 0.0039  -0.0910 -0.0437 562  LEU B O   
12838 C CB  . LEU B 564  ? 0.4064 0.2728 0.3211 -0.0125 -0.0855 -0.0312 562  LEU B CB  
12839 C CG  . LEU B 564  ? 0.4071 0.2852 0.3304 -0.0054 -0.0799 -0.0341 562  LEU B CG  
12840 C CD1 . LEU B 564  ? 0.4016 0.2892 0.3291 -0.0042 -0.0760 -0.0362 562  LEU B CD1 
12841 C CD2 . LEU B 564  ? 0.4374 0.3259 0.3669 -0.0074 -0.0764 -0.0305 562  LEU B CD2 
12842 N N   . THR B 565  ? 0.4204 0.2494 0.3166 -0.0047 -0.0986 -0.0374 563  THR B N   
12843 C CA  . THR B 565  ? 0.4662 0.2836 0.3579 0.0030  -0.1022 -0.0416 563  THR B CA  
12844 C C   . THR B 565  ? 0.4687 0.2780 0.3550 0.0074  -0.1045 -0.0469 563  THR B C   
12845 O O   . THR B 565  ? 0.4618 0.2718 0.3496 0.0162  -0.1033 -0.0519 563  THR B O   
12846 C CB  . THR B 565  ? 0.4860 0.2883 0.3697 -0.0002 -0.1086 -0.0387 563  THR B CB  
12847 O OG1 . THR B 565  ? 0.4583 0.2685 0.3469 -0.0031 -0.1063 -0.0343 563  THR B OG1 
12848 C CG2 . THR B 565  ? 0.4899 0.2789 0.3682 0.0082  -0.1130 -0.0433 563  THR B CG2 
12849 N N   . GLU B 566  ? 0.4810 0.2838 0.3613 0.0015  -0.1075 -0.0458 564  GLU B N   
12850 C CA  . GLU B 566  ? 0.5021 0.2963 0.3761 0.0055  -0.1100 -0.0509 564  GLU B CA  
12851 C C   . GLU B 566  ? 0.4732 0.2822 0.3546 0.0102  -0.1036 -0.0543 564  GLU B C   
12852 O O   . GLU B 566  ? 0.4692 0.2752 0.3485 0.0179  -0.1036 -0.0598 564  GLU B O   
12853 C CB  . GLU B 566  ? 0.5622 0.3451 0.4275 -0.0027 -0.1153 -0.0487 564  GLU B CB  
12854 C CG  . GLU B 566  ? 0.6341 0.3986 0.4899 -0.0063 -0.1229 -0.0463 564  GLU B CG  
12855 C CD  . GLU B 566  ? 0.7215 0.4743 0.5731 0.0028  -0.1261 -0.0505 564  GLU B CD  
12856 O OE1 . GLU B 566  ? 0.7818 0.5294 0.6301 0.0106  -0.1269 -0.0565 564  GLU B OE1 
12857 O OE2 . GLU B 566  ? 0.6943 0.4434 0.5457 0.0023  -0.1278 -0.0477 564  GLU B OE2 
12858 N N   . ALA B 567  ? 0.4414 0.2664 0.3311 0.0058  -0.0981 -0.0510 565  ALA B N   
12859 C CA  . ALA B 567  ? 0.4129 0.2522 0.3097 0.0097  -0.0919 -0.0536 565  ALA B CA  
12860 C C   . ALA B 567  ? 0.4224 0.2687 0.3254 0.0185  -0.0882 -0.0569 565  ALA B C   
12861 O O   . ALA B 567  ? 0.3893 0.2407 0.2941 0.0245  -0.0854 -0.0612 565  ALA B O   
12862 C CB  . ALA B 567  ? 0.3993 0.2535 0.3035 0.0031  -0.0873 -0.0490 565  ALA B CB  
12863 N N   . LEU B 568  ? 0.3841 0.2313 0.2902 0.0191  -0.0881 -0.0549 566  LEU B N   
12864 C CA  . LEU B 568  ? 0.3960 0.2498 0.3083 0.0269  -0.0851 -0.0576 566  LEU B CA  
12865 C C   . LEU B 568  ? 0.4177 0.2601 0.3239 0.0350  -0.0889 -0.0630 566  LEU B C   
12866 O O   . LEU B 568  ? 0.4224 0.2716 0.3324 0.0423  -0.0858 -0.0671 566  LEU B O   
12867 C CB  . LEU B 568  ? 0.4148 0.2713 0.3310 0.0250  -0.0848 -0.0539 566  LEU B CB  
12868 C CG  . LEU B 568  ? 0.3909 0.2603 0.3140 0.0184  -0.0805 -0.0490 566  LEU B CG  
12869 C CD1 . LEU B 568  ? 0.3889 0.2583 0.3138 0.0166  -0.0812 -0.0456 566  LEU B CD1 
12870 C CD2 . LEU B 568  ? 0.3444 0.2301 0.2767 0.0210  -0.0737 -0.0502 566  LEU B CD2 
12871 N N   . ARG B 569  ? 0.4148 0.2400 0.3113 0.0338  -0.0957 -0.0629 567  ARG B N   
12872 C CA  . ARG B 569  ? 0.4523 0.2647 0.3416 0.0415  -0.0999 -0.0682 567  ARG B CA  
12873 C C   . ARG B 569  ? 0.4543 0.2686 0.3416 0.0452  -0.0983 -0.0728 567  ARG B C   
12874 O O   . ARG B 569  ? 0.4778 0.2939 0.3658 0.0541  -0.0970 -0.0779 567  ARG B O   
12875 C CB  . ARG B 569  ? 0.4858 0.2779 0.3638 0.0381  -0.1080 -0.0669 567  ARG B CB  
12876 C CG  . ARG B 569  ? 0.5020 0.2892 0.3800 0.0372  -0.1107 -0.0637 567  ARG B CG  
12877 C CD  . ARG B 569  ? 0.5761 0.3418 0.4419 0.0339  -0.1190 -0.0625 567  ARG B CD  
12878 N NE  . ARG B 569  ? 0.6983 0.4590 0.5634 0.0321  -0.1218 -0.0587 567  ARG B NE  
12879 C CZ  . ARG B 569  ? 0.7530 0.4991 0.6097 0.0256  -0.1279 -0.0548 567  ARG B CZ  
12880 N NH1 . ARG B 569  ? 0.7135 0.4489 0.5620 0.0195  -0.1319 -0.0539 567  ARG B NH1 
12881 N NH2 . ARG B 569  ? 0.7642 0.5065 0.6204 0.0247  -0.1301 -0.0516 567  ARG B NH2 
12882 N N   . GLU B 570  ? 0.4575 0.2715 0.3419 0.0385  -0.0984 -0.0711 568  GLU B N   
12883 C CA  . GLU B 570  ? 0.4280 0.2437 0.3099 0.0415  -0.0969 -0.0753 568  GLU B CA  
12884 C C   . GLU B 570  ? 0.4032 0.2375 0.2953 0.0465  -0.0894 -0.0771 568  GLU B C   
12885 O O   . GLU B 570  ? 0.4339 0.2698 0.3247 0.0534  -0.0880 -0.0821 568  GLU B O   
12886 C CB  . GLU B 570  ? 0.4594 0.2731 0.3375 0.0327  -0.0983 -0.0724 568  GLU B CB  
12887 N N   . SER B 571  ? 0.3972 0.2456 0.2992 0.0432  -0.0845 -0.0731 569  SER B N   
12888 C CA  . SER B 571  ? 0.3871 0.2528 0.2987 0.0471  -0.0776 -0.0742 569  SER B CA  
12889 C C   . SER B 571  ? 0.4661 0.3337 0.3801 0.0567  -0.0767 -0.0785 569  SER B C   
12890 O O   . SER B 571  ? 0.4050 0.2828 0.3231 0.0618  -0.0724 -0.0815 569  SER B O   
12891 C CB  . SER B 571  ? 0.3545 0.2330 0.2755 0.0418  -0.0734 -0.0692 569  SER B CB  
12892 O OG  . SER B 571  ? 0.4151 0.2936 0.3396 0.0441  -0.0739 -0.0682 569  SER B OG  
12893 N N   . ALA B 572  ? 0.4482 0.3065 0.3598 0.0591  -0.0808 -0.0787 570  ALA B N   
12894 C CA  . ALA B 572  ? 0.4400 0.3002 0.3539 0.0685  -0.0804 -0.0827 570  ALA B CA  
12895 C C   . ALA B 572  ? 0.4764 0.3275 0.3823 0.0757  -0.0831 -0.0887 570  ALA B C   
12896 O O   . ALA B 572  ? 0.4738 0.3292 0.3823 0.0844  -0.0818 -0.0926 570  ALA B O   
12897 C CB  . ALA B 572  ? 0.4134 0.2664 0.3270 0.0690  -0.0842 -0.0809 570  ALA B CB  
12898 N N   . ALA B 573  ? 0.4621 0.3013 0.3584 0.0725  -0.0868 -0.0894 571  ALA B N   
12899 C CA  . ALA B 573  ? 0.4877 0.3175 0.3754 0.0794  -0.0895 -0.0954 571  ALA B CA  
12900 C C   . ALA B 573  ? 0.4367 0.2773 0.3260 0.0809  -0.0846 -0.0979 571  ALA B C   
12901 O O   . ALA B 573  ? 0.4377 0.2730 0.3206 0.0875  -0.0859 -0.1032 571  ALA B O   
12902 C CB  . ALA B 573  ? 0.4711 0.2797 0.3460 0.0758  -0.0973 -0.0954 571  ALA B CB  
12903 N N   . MET B 574  ? 0.4244 0.2796 0.3218 0.0754  -0.0792 -0.0942 572  MET B N   
12904 C CA  . MET B 574  ? 0.4493 0.3153 0.3485 0.0764  -0.0744 -0.0960 572  MET B CA  
12905 C C   . MET B 574  ? 0.4130 0.2933 0.3198 0.0845  -0.0690 -0.0990 572  MET B C   
12906 O O   . MET B 574  ? 0.3957 0.2827 0.3100 0.0868  -0.0673 -0.0978 572  MET B O   
12907 C CB  . MET B 574  ? 0.4187 0.2946 0.3234 0.0675  -0.0709 -0.0908 572  MET B CB  
12908 C CG  . MET B 574  ? 0.4525 0.3165 0.3503 0.0588  -0.0757 -0.0875 572  MET B CG  
12909 S SD  . MET B 574  ? 0.5032 0.3801 0.4099 0.0490  -0.0717 -0.0806 572  MET B SD  
12910 C CE  . MET B 574  ? 0.5172 0.3786 0.4146 0.0400  -0.0785 -0.0775 572  MET B CE  
12911 N N   . LYS B 575  ? 0.3633 0.2490 0.2682 0.0885  -0.0661 -0.1025 573  LYS B N   
12912 C CA  . LYS B 575  ? 0.4087 0.3101 0.3209 0.0953  -0.0603 -0.1050 573  LYS B CA  
12913 C C   . LYS B 575  ? 0.3706 0.2889 0.2928 0.0897  -0.0540 -0.1005 573  LYS B C   
12914 O O   . LYS B 575  ? 0.3787 0.3013 0.2996 0.0864  -0.0517 -0.0999 573  LYS B O   
12915 C CB  . LYS B 575  ? 0.3638 0.2631 0.2686 0.1022  -0.0601 -0.1108 573  LYS B CB  
12916 C CG  . LYS B 575  ? 0.4337 0.3507 0.3458 0.1085  -0.0536 -0.1130 573  LYS B CG  
12917 C CD  . LYS B 575  ? 0.5025 0.4163 0.4064 0.1168  -0.0540 -0.1195 573  LYS B CD  
12918 C CE  . LYS B 575  ? 0.5906 0.5232 0.5021 0.1231  -0.0473 -0.1214 573  LYS B CE  
12919 N NZ  . LYS B 575  ? 0.6304 0.5718 0.5518 0.1267  -0.0458 -0.1205 573  LYS B NZ  
12920 N N   . TRP B 576  ? 0.3389 0.2665 0.2710 0.0887  -0.0515 -0.0975 574  TRP B N   
12921 C CA  . TRP B 576  ? 0.3871 0.3299 0.3287 0.0838  -0.0459 -0.0933 574  TRP B CA  
12922 C C   . TRP B 576  ? 0.3979 0.3562 0.3462 0.0894  -0.0403 -0.0953 574  TRP B C   
12923 O O   . TRP B 576  ? 0.3558 0.3177 0.3076 0.0958  -0.0400 -0.0976 574  TRP B O   
12924 C CB  . TRP B 576  ? 0.3681 0.3124 0.3163 0.0793  -0.0463 -0.0888 574  TRP B CB  
12925 C CG  . TRP B 576  ? 0.3968 0.3283 0.3396 0.0729  -0.0511 -0.0859 574  TRP B CG  
12926 C CD1 . TRP B 576  ? 0.4011 0.3198 0.3394 0.0733  -0.0565 -0.0860 574  TRP B CD1 
12927 C CD2 . TRP B 576  ? 0.3688 0.2996 0.3103 0.0648  -0.0510 -0.0821 574  TRP B CD2 
12928 N NE1 . TRP B 576  ? 0.3659 0.2763 0.3003 0.0656  -0.0596 -0.0824 574  TRP B NE1 
12929 C CE2 . TRP B 576  ? 0.3864 0.3044 0.3228 0.0604  -0.0563 -0.0800 574  TRP B CE2 
12930 C CE3 . TRP B 576  ? 0.3615 0.3016 0.3058 0.0609  -0.0471 -0.0802 574  TRP B CE3 
12931 C CZ2 . TRP B 576  ? 0.3910 0.3062 0.3254 0.0522  -0.0575 -0.0761 574  TRP B CZ2 
12932 C CZ3 . TRP B 576  ? 0.3567 0.2936 0.2990 0.0532  -0.0484 -0.0765 574  TRP B CZ3 
12933 C CH2 . TRP B 576  ? 0.3671 0.2921 0.3046 0.0489  -0.0535 -0.0745 574  TRP B CH2 
12934 N N   . THR B 577  ? 0.3591 0.3272 0.3095 0.0869  -0.0359 -0.0942 575  THR B N   
12935 C CA  . THR B 577  ? 0.3411 0.3249 0.2979 0.0911  -0.0303 -0.0954 575  THR B CA  
12936 C C   . THR B 577  ? 0.3176 0.3136 0.2821 0.0849  -0.0256 -0.0905 575  THR B C   
12937 O O   . THR B 577  ? 0.3217 0.3141 0.2851 0.0779  -0.0264 -0.0870 575  THR B O   
12938 C CB  . THR B 577  ? 0.3639 0.3472 0.3134 0.0964  -0.0295 -0.1001 575  THR B CB  
12939 O OG1 . THR B 577  ? 0.3760 0.3547 0.3195 0.0910  -0.0301 -0.0988 575  THR B OG1 
12940 C CG2 . THR B 577  ? 0.4092 0.3799 0.3505 0.1034  -0.0343 -0.1053 575  THR B CG2 
12941 N N   . ALA B 578  ? 0.3080 0.3187 0.2803 0.0874  -0.0207 -0.0903 576  ALA B N   
12942 C CA  . ALA B 578  ? 0.2638 0.2868 0.2429 0.0826  -0.0158 -0.0864 576  ALA B CA  
12943 C C   . ALA B 578  ? 0.2600 0.2957 0.2414 0.0873  -0.0112 -0.0885 576  ALA B C   
12944 O O   . ALA B 578  ? 0.3151 0.3560 0.2995 0.0935  -0.0104 -0.0912 576  ALA B O   
12945 C CB  . ALA B 578  ? 0.2346 0.2633 0.2230 0.0788  -0.0147 -0.0823 576  ALA B CB  
12946 N N   . LEU B 579  ? 0.2871 0.3281 0.2669 0.0847  -0.0082 -0.0873 577  LEU B N   
12947 C CA  . LEU B 579  ? 0.2971 0.3502 0.2783 0.0887  -0.0036 -0.0890 577  LEU B CA  
12948 C C   . LEU B 579  ? 0.2664 0.3304 0.2531 0.0830  0.0008  -0.0843 577  LEU B C   
12949 O O   . LEU B 579  ? 0.2689 0.3291 0.2562 0.0766  -0.0002 -0.0806 577  LEU B O   
12950 C CB  . LEU B 579  ? 0.3414 0.3884 0.3120 0.0928  -0.0048 -0.0935 577  LEU B CB  
12951 C CG  . LEU B 579  ? 0.3853 0.4239 0.3509 0.1003  -0.0084 -0.0988 577  LEU B CG  
12952 C CD1 . LEU B 579  ? 0.4289 0.4492 0.3853 0.0985  -0.0144 -0.1001 577  LEU B CD1 
12953 C CD2 . LEU B 579  ? 0.4097 0.4548 0.3716 0.1077  -0.0057 -0.1034 577  LEU B CD2 
12954 N N   . PRO B 580  ? 0.2473 0.3251 0.2381 0.0852  0.0056  -0.0843 578  PRO B N   
12955 C CA  . PRO B 580  ? 0.2550 0.3417 0.2489 0.0800  0.0095  -0.0801 578  PRO B CA  
12956 C C   . PRO B 580  ? 0.2572 0.3374 0.2422 0.0779  0.0086  -0.0804 578  PRO B C   
12957 O O   . PRO B 580  ? 0.2959 0.3772 0.2746 0.0821  0.0095  -0.0839 578  PRO B O   
12958 C CB  . PRO B 580  ? 0.2760 0.3781 0.2746 0.0838  0.0144  -0.0809 578  PRO B CB  
12959 C CG  . PRO B 580  ? 0.3176 0.4202 0.3181 0.0906  0.0131  -0.0848 578  PRO B CG  
12960 C CD  . PRO B 580  ? 0.2746 0.3607 0.2670 0.0927  0.0076  -0.0881 578  PRO B CD  
12961 N N   . GLN B 581  ? 0.2930 0.3668 0.2772 0.0717  0.0066  -0.0771 579  GLN B N   
12962 C CA  . GLN B 581  ? 0.2609 0.3283 0.2370 0.0690  0.0052  -0.0769 579  GLN B CA  
12963 C C   . GLN B 581  ? 0.2566 0.3339 0.2357 0.0650  0.0092  -0.0729 579  GLN B C   
12964 O O   . GLN B 581  ? 0.2639 0.3418 0.2473 0.0595  0.0093  -0.0685 579  GLN B O   
12965 C CB  . GLN B 581  ? 0.2857 0.3407 0.2592 0.0648  0.0005  -0.0756 579  GLN B CB  
12966 C CG  . GLN B 581  ? 0.2956 0.3394 0.2650 0.0683  -0.0040 -0.0793 579  GLN B CG  
12967 C CD  . GLN B 581  ? 0.3342 0.3716 0.2937 0.0732  -0.0059 -0.0845 579  GLN B CD  
12968 O OE1 . GLN B 581  ? 0.3487 0.3886 0.3032 0.0733  -0.0043 -0.0852 579  GLN B OE1 
12969 N NE2 . GLN B 581  ? 0.3563 0.3847 0.3122 0.0777  -0.0094 -0.0883 579  GLN B NE2 
12970 N N   . LEU B 582  ? 0.2635 0.3485 0.2399 0.0679  0.0125  -0.0744 580  LEU B N   
12971 C CA  . LEU B 582  ? 0.2770 0.3707 0.2547 0.0643  0.0162  -0.0706 580  LEU B CA  
12972 C C   . LEU B 582  ? 0.3092 0.3959 0.2788 0.0614  0.0140  -0.0702 580  LEU B C   
12973 O O   . LEU B 582  ? 0.2897 0.3655 0.2520 0.0627  0.0101  -0.0734 580  LEU B O   
12974 C CB  . LEU B 582  ? 0.2602 0.3663 0.2387 0.0685  0.0208  -0.0721 580  LEU B CB  
12975 C CG  . LEU B 582  ? 0.3606 0.4787 0.3496 0.0685  0.0243  -0.0697 580  LEU B CG  
12976 C CD1 . LEU B 582  ? 0.3214 0.4355 0.3155 0.0705  0.0218  -0.0713 580  LEU B CD1 
12977 C CD2 . LEU B 582  ? 0.3791 0.5101 0.3684 0.0727  0.0289  -0.0713 580  LEU B CD2 
12978 N N   . ALA B 583  ? 0.2585 0.3511 0.2291 0.0573  0.0165  -0.0662 581  ALA B N   
12979 C CA  . ALA B 583  ? 0.3213 0.4086 0.2846 0.0545  0.0146  -0.0654 581  ALA B CA  
12980 C C   . ALA B 583  ? 0.4011 0.4851 0.3543 0.0589  0.0138  -0.0703 581  ALA B C   
12981 O O   . ALA B 583  ? 0.4267 0.5019 0.3724 0.0574  0.0103  -0.0714 581  ALA B O   
12982 C CB  . ALA B 583  ? 0.2728 0.3682 0.2389 0.0502  0.0177  -0.0604 581  ALA B CB  
12983 N N   . THR B 584  ? 0.2896 0.3808 0.2423 0.0643  0.0169  -0.0733 582  THR B N   
12984 C CA  . THR B 584  ? 0.3333 0.4224 0.2762 0.0693  0.0167  -0.0784 582  THR B CA  
12985 C C   . THR B 584  ? 0.3461 0.4251 0.2845 0.0745  0.0130  -0.0840 582  THR B C   
12986 O O   . THR B 584  ? 0.3114 0.3869 0.2409 0.0793  0.0121  -0.0888 582  THR B O   
12987 C CB  . THR B 584  ? 0.3570 0.4599 0.3010 0.0729  0.0223  -0.0788 582  THR B CB  
12988 O OG1 . THR B 584  ? 0.3793 0.4896 0.3323 0.0754  0.0245  -0.0789 582  THR B OG1 
12989 C CG2 . THR B 584  ? 0.4004 0.5118 0.3465 0.0677  0.0255  -0.0734 582  THR B CG2 
12990 N N   . GLY B 585  ? 0.3350 0.4090 0.2790 0.0739  0.0106  -0.0836 583  GLY B N   
12991 C CA  . GLY B 585  ? 0.2937 0.3577 0.2336 0.0786  0.0068  -0.0885 583  GLY B CA  
12992 C C   . GLY B 585  ? 0.3143 0.3837 0.2631 0.0816  0.0083  -0.0886 583  GLY B C   
12993 O O   . GLY B 585  ? 0.2992 0.3801 0.2570 0.0795  0.0122  -0.0849 583  GLY B O   
12994 N N   . PRO B 586  ? 0.2979 0.3587 0.2441 0.0862  0.0049  -0.0927 584  PRO B N   
12995 C CA  . PRO B 586  ? 0.3246 0.3902 0.2792 0.0891  0.0057  -0.0929 584  PRO B CA  
12996 C C   . PRO B 586  ? 0.3484 0.4278 0.3059 0.0953  0.0105  -0.0952 584  PRO B C   
12997 O O   . PRO B 586  ? 0.3338 0.4147 0.2841 0.0999  0.0118  -0.0989 584  PRO B O   
12998 C CB  . PRO B 586  ? 0.3326 0.3833 0.2815 0.0925  0.0001  -0.0969 584  PRO B CB  
12999 C CG  . PRO B 586  ? 0.3451 0.3869 0.2818 0.0947  -0.0023 -0.1009 584  PRO B CG  
13000 C CD  . PRO B 586  ? 0.3317 0.3775 0.2671 0.0887  -0.0004 -0.0972 584  PRO B CD  
13001 N N   . ALA B 587  ? 0.3653 0.4550 0.3333 0.0952  0.0133  -0.0928 585  ALA B N   
13002 C CA  . ALA B 587  ? 0.3665 0.4711 0.3391 0.1004  0.0179  -0.0943 585  ALA B CA  
13003 C C   . ALA B 587  ? 0.3240 0.4269 0.2988 0.1072  0.0160  -0.0983 585  ALA B C   
13004 O O   . ALA B 587  ? 0.3323 0.4242 0.3074 0.1066  0.0115  -0.0985 585  ALA B O   
13005 C CB  . ALA B 587  ? 0.3849 0.5038 0.3683 0.0954  0.0224  -0.0886 585  ALA B CB  
13006 N N   . ALA B 588  ? 0.3767 0.4912 0.3529 0.1140  0.0194  -0.1013 586  ALA B N   
13007 C CA  . ALA B 588  ? 0.3667 0.4823 0.3460 0.1212  0.0182  -0.1050 586  ALA B CA  
13008 C C   . ALA B 588  ? 0.3648 0.4919 0.3572 0.1186  0.0202  -0.1010 586  ALA B C   
13009 O O   . ALA B 588  ? 0.3885 0.5249 0.3875 0.1121  0.0235  -0.0958 586  ALA B O   
13010 C CB  . ALA B 588  ? 0.4382 0.5619 0.4133 0.1302  0.0210  -0.1103 586  ALA B CB  
13011 N N   . GLY B 589  ? 0.4534 0.5792 0.4494 0.1236  0.0179  -0.1035 587  GLY B N   
13012 C CA  . GLY B 589  ? 0.4019 0.5379 0.4100 0.1216  0.0192  -0.1001 587  GLY B CA  
13013 C C   . GLY B 589  ? 0.3795 0.5112 0.3892 0.1282  0.0157  -0.1037 587  GLY B C   
13014 O O   . GLY B 589  ? 0.3822 0.5037 0.3837 0.1347  0.0125  -0.1088 587  GLY B O   
13015 N N   . GLU B 590  ? 0.3959 0.5352 0.4162 0.1263  0.0160  -0.1008 588  GLU B N   
13016 C CA  . GLU B 590  ? 0.3891 0.5246 0.4120 0.1317  0.0123  -0.1034 588  GLU B CA  
13017 C C   . GLU B 590  ? 0.4004 0.5159 0.4177 0.1288  0.0062  -0.1032 588  GLU B C   
13018 O O   . GLU B 590  ? 0.3927 0.5036 0.4117 0.1207  0.0055  -0.0987 588  GLU B O   
13019 C CB  . GLU B 590  ? 0.3895 0.5398 0.4255 0.1301  0.0144  -0.1002 588  GLU B CB  
13020 N N   . THR B 591  ? 0.4218 0.5259 0.4328 0.1356  0.0019  -0.1079 589  THR B N   
13021 C CA  . THR B 591  ? 0.4361 0.5206 0.4405 0.1335  -0.0042 -0.1080 589  THR B CA  
13022 C C   . THR B 591  ? 0.4200 0.5024 0.4298 0.1359  -0.0076 -0.1080 589  THR B C   
13023 O O   . THR B 591  ? 0.4075 0.4977 0.4210 0.1435  -0.0072 -0.1110 589  THR B O   
13024 C CB  . THR B 591  ? 0.4607 0.5309 0.4523 0.1387  -0.0076 -0.1131 589  THR B CB  
13025 O OG1 . THR B 591  ? 0.4582 0.5312 0.4447 0.1368  -0.0043 -0.1133 589  THR B OG1 
13026 C CG2 . THR B 591  ? 0.4597 0.5094 0.4442 0.1350  -0.0139 -0.1125 589  THR B CG2 
13027 N N   . ARG B 592  ? 0.3994 0.4717 0.4096 0.1296  -0.0110 -0.1046 590  ARG B N   
13028 C CA  . ARG B 592  ? 0.3999 0.4671 0.4132 0.1315  -0.0151 -0.1045 590  ARG B CA  
13029 C C   . ARG B 592  ? 0.4020 0.4497 0.4076 0.1273  -0.0206 -0.1034 590  ARG B C   
13030 O O   . ARG B 592  ? 0.3716 0.4123 0.3721 0.1212  -0.0207 -0.1015 590  ARG B O   
13031 C CB  . ARG B 592  ? 0.4728 0.5535 0.4984 0.1276  -0.0127 -0.1004 590  ARG B CB  
13032 C CG  . ARG B 592  ? 0.4590 0.5439 0.4882 0.1182  -0.0097 -0.0952 590  ARG B CG  
13033 C CD  . ARG B 592  ? 0.5359 0.6396 0.5770 0.1164  -0.0053 -0.0925 590  ARG B CD  
13034 N NE  . ARG B 592  ? 0.5567 0.6618 0.6049 0.1153  -0.0075 -0.0906 590  ARG B NE  
13035 C CZ  . ARG B 592  ? 0.5789 0.6830 0.6311 0.1078  -0.0078 -0.0862 590  ARG B CZ  
13036 N NH1 . ARG B 592  ? 0.5040 0.6059 0.5542 0.1009  -0.0060 -0.0830 590  ARG B NH1 
13037 N NH2 . ARG B 592  ? 0.5624 0.6679 0.6205 0.1076  -0.0101 -0.0849 590  ARG B NH2 
13038 N N   . THR B 593  ? 0.3908 0.4302 0.3959 0.1304  -0.0253 -0.1044 591  THR B N   
13039 C CA  A THR B 593  ? 0.4092 0.4299 0.4066 0.1269  -0.0309 -0.1035 591  THR B CA  
13040 C CA  B THR B 593  ? 0.4083 0.4290 0.4058 0.1269  -0.0309 -0.1035 591  THR B CA  
13041 C C   . THR B 593  ? 0.3964 0.4177 0.3995 0.1185  -0.0310 -0.0980 591  THR B C   
13042 O O   . THR B 593  ? 0.3908 0.4238 0.4035 0.1178  -0.0289 -0.0959 591  THR B O   
13043 C CB  A THR B 593  ? 0.3950 0.4047 0.3877 0.1344  -0.0364 -0.1072 591  THR B CB  
13044 C CB  B THR B 593  ? 0.3951 0.4050 0.3880 0.1344  -0.0363 -0.1071 591  THR B CB  
13045 O OG1 A THR B 593  ? 0.4237 0.4424 0.4255 0.1370  -0.0364 -0.1064 591  THR B OG1 
13046 O OG1 B THR B 593  ? 0.3873 0.3804 0.3742 0.1299  -0.0417 -0.1051 591  THR B OG1 
13047 C CG2 A THR B 593  ? 0.3644 0.3735 0.3511 0.1434  -0.0362 -0.1130 591  THR B CG2 
13048 C CG2 B THR B 593  ? 0.4120 0.4342 0.4147 0.1392  -0.0355 -0.1074 591  THR B CG2 
13049 N N   . VAL B 594  ? 0.3814 0.3905 0.3783 0.1121  -0.0334 -0.0956 592  VAL B N   
13050 C CA  . VAL B 594  ? 0.3290 0.3367 0.3294 0.1042  -0.0338 -0.0906 592  VAL B CA  
13051 C C   . VAL B 594  ? 0.3514 0.3453 0.3475 0.1048  -0.0398 -0.0906 592  VAL B C   
13052 O O   . VAL B 594  ? 0.3290 0.3084 0.3155 0.1061  -0.0440 -0.0925 592  VAL B O   
13053 C CB  . VAL B 594  ? 0.3780 0.3825 0.3748 0.0967  -0.0325 -0.0878 592  VAL B CB  
13054 C CG1 . VAL B 594  ? 0.2548 0.2577 0.2548 0.0890  -0.0330 -0.0829 592  VAL B CG1 
13055 C CG2 . VAL B 594  ? 0.3627 0.3802 0.3629 0.0964  -0.0268 -0.0879 592  VAL B CG2 
13056 N N   . LEU B 595  ? 0.3639 0.3618 0.3665 0.1038  -0.0404 -0.0884 593  LEU B N   
13057 C CA  . LEU B 595  ? 0.3714 0.3576 0.3706 0.1054  -0.0459 -0.0884 593  LEU B CA  
13058 C C   . LEU B 595  ? 0.3323 0.3129 0.3311 0.0972  -0.0474 -0.0837 593  LEU B C   
13059 O O   . LEU B 595  ? 0.3581 0.3472 0.3624 0.0915  -0.0437 -0.0804 593  LEU B O   
13060 C CB  . LEU B 595  ? 0.3074 0.3020 0.3138 0.1116  -0.0463 -0.0899 593  LEU B CB  
13061 C CG  . LEU B 595  ? 0.3603 0.3615 0.3675 0.1206  -0.0450 -0.0948 593  LEU B CG  
13062 C CD1 . LEU B 595  ? 0.4091 0.4200 0.4246 0.1261  -0.0454 -0.0956 593  LEU B CD1 
13063 C CD2 . LEU B 595  ? 0.4072 0.3932 0.4032 0.1258  -0.0493 -0.0988 593  LEU B CD2 
13064 N N   . ASN B 596  ? 0.3399 0.3061 0.3319 0.0969  -0.0528 -0.0833 594  ASN B N   
13065 C CA  . ASN B 596  ? 0.3276 0.2883 0.3188 0.0899  -0.0546 -0.0790 594  ASN B CA  
13066 C C   . ASN B 596  ? 0.3304 0.2995 0.3299 0.0905  -0.0540 -0.0774 594  ASN B C   
13067 O O   . ASN B 596  ? 0.3013 0.2689 0.3015 0.0963  -0.0569 -0.0794 594  ASN B O   
13068 C CB  . ASN B 596  ? 0.3236 0.2661 0.3046 0.0898  -0.0608 -0.0791 594  ASN B CB  
13069 C CG  . ASN B 596  ? 0.3605 0.2968 0.3392 0.0821  -0.0626 -0.0745 594  ASN B CG  
13070 O OD1 . ASN B 596  ? 0.3209 0.2653 0.3060 0.0785  -0.0603 -0.0715 594  ASN B OD1 
13071 N ND2 . ASN B 596  ? 0.3407 0.2620 0.3098 0.0795  -0.0670 -0.0738 594  ASN B ND2 
13072 N N   . PRO B 597  ? 0.3188 0.2968 0.3245 0.0848  -0.0507 -0.0740 595  PRO B N   
13073 C CA  . PRO B 597  ? 0.3231 0.3085 0.3362 0.0852  -0.0506 -0.0727 595  PRO B CA  
13074 C C   . PRO B 597  ? 0.3327 0.3072 0.3416 0.0853  -0.0559 -0.0715 595  PRO B C   
13075 O O   . PRO B 597  ? 0.3412 0.3202 0.3551 0.0878  -0.0570 -0.0716 595  PRO B O   
13076 C CB  . PRO B 597  ? 0.2607 0.2545 0.2790 0.0785  -0.0464 -0.0692 595  PRO B CB  
13077 C CG  . PRO B 597  ? 0.3495 0.3371 0.3616 0.0737  -0.0455 -0.0679 595  PRO B CG  
13078 C CD  . PRO B 597  ? 0.3154 0.2972 0.3217 0.0784  -0.0469 -0.0715 595  PRO B CD  
13079 N N   . GLY B 598  ? 0.3433 0.3039 0.3432 0.0823  -0.0593 -0.0704 596  GLY B N   
13080 C CA  . GLY B 598  ? 0.3555 0.3049 0.3505 0.0825  -0.0647 -0.0692 596  GLY B CA  
13081 C C   . GLY B 598  ? 0.3812 0.3227 0.3722 0.0901  -0.0692 -0.0728 596  GLY B C   
13082 O O   . GLY B 598  ? 0.3842 0.3171 0.3717 0.0913  -0.0739 -0.0720 596  GLY B O   
13083 N N   . ASP B 599  ? 0.3385 0.2829 0.3296 0.0957  -0.0678 -0.0767 597  ASP B N   
13084 C CA  . ASP B 599  ? 0.3786 0.3148 0.3650 0.1037  -0.0721 -0.0805 597  ASP B CA  
13085 C C   . ASP B 599  ? 0.3882 0.3327 0.3770 0.1093  -0.0686 -0.0846 597  ASP B C   
13086 O O   . ASP B 599  ? 0.3976 0.3377 0.3811 0.1080  -0.0676 -0.0857 597  ASP B O   
13087 C CB  . ASP B 599  ? 0.3991 0.3158 0.3734 0.1016  -0.0775 -0.0800 597  ASP B CB  
13088 C CG  . ASP B 599  ? 0.4981 0.4035 0.4662 0.1098  -0.0830 -0.0836 597  ASP B CG  
13089 O OD1 . ASP B 599  ? 0.4570 0.3700 0.4296 0.1179  -0.0820 -0.0875 597  ASP B OD1 
13090 O OD2 . ASP B 599  ? 0.4334 0.3221 0.3920 0.1080  -0.0884 -0.0826 597  ASP B OD2 
13091 N N   . HIS B 600  ? 0.3623 0.3194 0.3592 0.1154  -0.0667 -0.0869 598  HIS B N   
13092 C CA  . HIS B 600  ? 0.3770 0.3447 0.3773 0.1205  -0.0627 -0.0904 598  HIS B CA  
13093 C C   . HIS B 600  ? 0.3575 0.3144 0.3492 0.1277  -0.0659 -0.0950 598  HIS B C   
13094 O O   . HIS B 600  ? 0.3848 0.3486 0.3772 0.1318  -0.0627 -0.0982 598  HIS B O   
13095 C CB  . HIS B 600  ? 0.3809 0.3661 0.3927 0.1246  -0.0597 -0.0911 598  HIS B CB  
13096 C CG  . HIS B 600  ? 0.3642 0.3621 0.3846 0.1176  -0.0553 -0.0872 598  HIS B CG  
13097 N ND1 . HIS B 600  ? 0.3816 0.3962 0.4129 0.1193  -0.0522 -0.0871 598  HIS B ND1 
13098 C CD2 . HIS B 600  ? 0.3262 0.3222 0.3458 0.1089  -0.0536 -0.0834 598  HIS B CD2 
13099 C CE1 . HIS B 600  ? 0.3634 0.3848 0.3997 0.1119  -0.0490 -0.0834 598  HIS B CE1 
13100 N NE2 . HIS B 600  ? 0.3598 0.3702 0.3891 0.1058  -0.0497 -0.0812 598  HIS B NE2 
13101 N N   . ARG B 601  ? 0.3751 0.3149 0.3581 0.1292  -0.0722 -0.0954 599  ARG B N   
13102 C CA  . ARG B 601  ? 0.3878 0.3142 0.3608 0.1351  -0.0760 -0.0996 599  ARG B CA  
13103 C C   . ARG B 601  ? 0.4184 0.3356 0.3832 0.1295  -0.0757 -0.0991 599  ARG B C   
13104 O O   . ARG B 601  ? 0.4300 0.3384 0.3869 0.1341  -0.0776 -0.1030 599  ARG B O   
13105 C CB  . ARG B 601  ? 0.4966 0.4066 0.4626 0.1382  -0.0833 -0.0999 599  ARG B CB  
13106 C CG  . ARG B 601  ? 0.4496 0.3673 0.4231 0.1433  -0.0845 -0.0999 599  ARG B CG  
13107 C CD  . ARG B 601  ? 0.5463 0.4465 0.5122 0.1441  -0.0920 -0.0988 599  ARG B CD  
13108 N NE  . ARG B 601  ? 0.5348 0.4262 0.4965 0.1338  -0.0934 -0.0936 599  ARG B NE  
13109 C CZ  . ARG B 601  ? 0.5952 0.4710 0.5496 0.1318  -0.0994 -0.0914 599  ARG B CZ  
13110 N NH1 . ARG B 601  ? 0.5347 0.4006 0.4846 0.1393  -0.1051 -0.0938 599  ARG B NH1 
13111 N NH2 . ARG B 601  ? 0.5782 0.4483 0.5295 0.1221  -0.0998 -0.0865 599  ARG B NH2 
13112 N N   . ASP B 602  ? 0.3930 0.3117 0.3592 0.1198  -0.0736 -0.0945 600  ASP B N   
13113 C CA  . ASP B 602  ? 0.4065 0.3174 0.3657 0.1134  -0.0735 -0.0932 600  ASP B CA  
13114 C C   . ASP B 602  ? 0.4132 0.3386 0.3777 0.1129  -0.0669 -0.0942 600  ASP B C   
13115 O O   . ASP B 602  ? 0.4051 0.3435 0.3778 0.1081  -0.0623 -0.0911 600  ASP B O   
13116 C CB  . ASP B 602  ? 0.4420 0.3479 0.4002 0.1037  -0.0746 -0.0877 600  ASP B CB  
13117 C CG  . ASP B 602  ? 0.4328 0.3323 0.3848 0.0967  -0.0743 -0.0860 600  ASP B CG  
13118 O OD1 . ASP B 602  ? 0.4681 0.3592 0.4126 0.0994  -0.0762 -0.0892 600  ASP B OD1 
13119 O OD2 . ASP B 602  ? 0.4634 0.3664 0.4179 0.0887  -0.0723 -0.0815 600  ASP B OD2 
13120 N N   . VAL B 603  ? 0.4200 0.3427 0.3792 0.1179  -0.0668 -0.0985 601  VAL B N   
13121 C CA  . VAL B 603  ? 0.4190 0.3545 0.3819 0.1179  -0.0610 -0.0997 601  VAL B CA  
13122 C C   . VAL B 603  ? 0.4177 0.3478 0.3756 0.1096  -0.0604 -0.0970 601  VAL B C   
13123 O O   . VAL B 603  ? 0.4175 0.3318 0.3654 0.1078  -0.0651 -0.0975 601  VAL B O   
13124 C CB  . VAL B 603  ? 0.4390 0.3747 0.3982 0.1276  -0.0610 -0.1057 601  VAL B CB  
13125 C CG1 . VAL B 603  ? 0.4195 0.3668 0.3807 0.1270  -0.0552 -0.1067 601  VAL B CG1 
13126 C CG2 . VAL B 603  ? 0.4477 0.3917 0.4134 0.1360  -0.0609 -0.1080 601  VAL B CG2 
13127 N N   . VAL B 604  ? 0.3510 0.2940 0.3160 0.1041  -0.0551 -0.0939 602  VAL B N   
13128 C CA  . VAL B 604  ? 0.3706 0.3106 0.3325 0.0957  -0.0543 -0.0907 602  VAL B CA  
13129 C C   . VAL B 604  ? 0.3507 0.2940 0.3095 0.0967  -0.0515 -0.0931 602  VAL B C   
13130 O O   . VAL B 604  ? 0.3560 0.2903 0.3074 0.0925  -0.0534 -0.0926 602  VAL B O   
13131 C CB  . VAL B 604  ? 0.3524 0.3031 0.3231 0.0890  -0.0507 -0.0857 602  VAL B CB  
13132 C CG1 . VAL B 604  ? 0.3364 0.2837 0.3039 0.0806  -0.0503 -0.0822 602  VAL B CG1 
13133 C CG2 . VAL B 604  ? 0.3560 0.3036 0.3294 0.0884  -0.0535 -0.0836 602  VAL B CG2 
13134 N N   . GLY B 605  ? 0.3210 0.2776 0.2853 0.1021  -0.0471 -0.0956 603  GLY B N   
13135 C CA  . GLY B 605  ? 0.3677 0.3290 0.3294 0.1033  -0.0440 -0.0978 603  GLY B CA  
13136 C C   . GLY B 605  ? 0.3954 0.3734 0.3648 0.1090  -0.0388 -0.0998 603  GLY B C   
13137 O O   . GLY B 605  ? 0.3726 0.3562 0.3478 0.1137  -0.0387 -0.1006 603  GLY B O   
13138 N N   . SER B 606  ? 0.3103 0.2969 0.2799 0.1085  -0.0345 -0.1003 604  SER B N   
13139 C CA  . SER B 606  ? 0.3672 0.3707 0.3442 0.1132  -0.0292 -0.1017 604  SER B CA  
13140 C C   . SER B 606  ? 0.3631 0.3782 0.3445 0.1073  -0.0239 -0.0984 604  SER B C   
13141 O O   . SER B 606  ? 0.3525 0.3619 0.3286 0.1021  -0.0242 -0.0969 604  SER B O   
13142 C CB  . SER B 606  ? 0.4369 0.4394 0.4080 0.1223  -0.0295 -0.1077 604  SER B CB  
13143 O OG  . SER B 606  ? 0.5079 0.5071 0.4714 0.1211  -0.0286 -0.1091 604  SER B OG  
13144 N N   . VAL B 607  ? 0.3190 0.3504 0.3102 0.1080  -0.0192 -0.0970 605  VAL B N   
13145 C CA  . VAL B 607  ? 0.2995 0.3426 0.2956 0.1027  -0.0141 -0.0936 605  VAL B CA  
13146 C C   . VAL B 607  ? 0.3725 0.4297 0.3713 0.1080  -0.0094 -0.0960 605  VAL B C   
13147 O O   . VAL B 607  ? 0.3291 0.3934 0.3321 0.1143  -0.0088 -0.0984 605  VAL B O   
13148 C CB  . VAL B 607  ? 0.3249 0.3747 0.3304 0.0968  -0.0127 -0.0886 605  VAL B CB  
13149 C CG1 . VAL B 607  ? 0.3254 0.3832 0.3389 0.1011  -0.0125 -0.0893 605  VAL B CG1 
13150 C CG2 . VAL B 607  ? 0.3162 0.3773 0.3262 0.0916  -0.0076 -0.0851 605  VAL B CG2 
13151 N N   . THR B 608  ? 0.3393 0.4008 0.3355 0.1055  -0.0062 -0.0953 606  THR B N   
13152 C CA  . THR B 608  ? 0.3008 0.3776 0.3002 0.1088  -0.0009 -0.0963 606  THR B CA  
13153 C C   . THR B 608  ? 0.2920 0.3806 0.2998 0.1019  0.0033  -0.0909 606  THR B C   
13154 O O   . THR B 608  ? 0.2912 0.3754 0.2971 0.0952  0.0032  -0.0876 606  THR B O   
13155 C CB  . THR B 608  ? 0.3179 0.3906 0.3074 0.1114  -0.0005 -0.0996 606  THR B CB  
13156 O OG1 . THR B 608  ? 0.3366 0.3973 0.3180 0.1181  -0.0048 -0.1049 606  THR B OG1 
13157 C CG2 . THR B 608  ? 0.2820 0.3713 0.2745 0.1145  0.0053  -0.1004 606  THR B CG2 
13158 N N   . GLU B 609  ? 0.2957 0.3989 0.3128 0.1033  0.0066  -0.0898 607  GLU B N   
13159 C CA  . GLU B 609  ? 0.3100 0.4231 0.3355 0.0966  0.0098  -0.0845 607  GLU B CA  
13160 C C   . GLU B 609  ? 0.3075 0.4328 0.3336 0.0956  0.0150  -0.0834 607  GLU B C   
13161 O O   . GLU B 609  ? 0.2921 0.4221 0.3144 0.1012  0.0169  -0.0869 607  GLU B O   
13162 C CB  . GLU B 609  ? 0.3368 0.4577 0.3722 0.0973  0.0097  -0.0833 607  GLU B CB  
13163 C CG  . GLU B 609  ? 0.3177 0.4255 0.3523 0.0955  0.0047  -0.0828 607  GLU B CG  
13164 C CD  . GLU B 609  ? 0.4254 0.5386 0.4686 0.0966  0.0036  -0.0820 607  GLU B CD  
13165 O OE1 . GLU B 609  ? 0.3856 0.5123 0.4353 0.1004  0.0062  -0.0829 607  GLU B OE1 
13166 O OE2 . GLU B 609  ? 0.3770 0.4811 0.4205 0.0935  0.0001  -0.0804 607  GLU B OE2 
13167 N N   . THR B 610  ? 0.2986 0.4284 0.3289 0.0884  0.0172  -0.0784 608  THR B N   
13168 C CA  . THR B 610  ? 0.3038 0.4424 0.3335 0.0858  0.0215  -0.0763 608  THR B CA  
13169 C C   . THR B 610  ? 0.3120 0.4684 0.3501 0.0869  0.0260  -0.0750 608  THR B C   
13170 O O   . THR B 610  ? 0.3192 0.4813 0.3660 0.0850  0.0260  -0.0728 608  THR B O   
13171 C CB  . THR B 610  ? 0.2869 0.4213 0.3169 0.0776  0.0214  -0.0713 608  THR B CB  
13172 O OG1 . THR B 610  ? 0.2838 0.4027 0.3080 0.0760  0.0169  -0.0719 608  THR B OG1 
13173 C CG2 . THR B 610  ? 0.3075 0.4473 0.3340 0.0752  0.0249  -0.0696 608  THR B CG2 
13174 N N   . SER B 611  ? 0.3033 0.4688 0.3388 0.0896  0.0297  -0.0763 609  SER B N   
13175 C CA  . SER B 611  ? 0.3610 0.5447 0.4045 0.0891  0.0345  -0.0740 609  SER B CA  
13176 C C   . SER B 611  ? 0.3740 0.5610 0.4212 0.0804  0.0364  -0.0678 609  SER B C   
13177 O O   . SER B 611  ? 0.3191 0.4965 0.3609 0.0761  0.0352  -0.0660 609  SER B O   
13178 C CB  . SER B 611  ? 0.3593 0.5523 0.3985 0.0947  0.0382  -0.0771 609  SER B CB  
13179 O OG  . SER B 611  ? 0.3807 0.5708 0.4126 0.0914  0.0397  -0.0757 609  SER B OG  
13180 N N   . GLU B 612  ? 0.3465 0.5471 0.4031 0.0778  0.0391  -0.0645 610  GLU B N   
13181 C CA  . GLU B 612  ? 0.3793 0.5828 0.4393 0.0696  0.0408  -0.0586 610  GLU B CA  
13182 C C   . GLU B 612  ? 0.3567 0.5629 0.4106 0.0678  0.0439  -0.0571 610  GLU B C   
13183 O O   . GLU B 612  ? 0.3764 0.5774 0.4284 0.0618  0.0436  -0.0533 610  GLU B O   
13184 C CB  . GLU B 612  ? 0.3749 0.5928 0.4459 0.0672  0.0429  -0.0555 610  GLU B CB  
13185 C CG  . GLU B 612  ? 0.4086 0.6220 0.4858 0.0668  0.0392  -0.0556 610  GLU B CG  
13186 C CD  . GLU B 612  ? 0.4737 0.7022 0.5617 0.0654  0.0410  -0.0533 610  GLU B CD  
13187 O OE1 . GLU B 612  ? 0.5137 0.7510 0.6057 0.0597  0.0438  -0.0487 610  GLU B OE1 
13188 O OE2 . GLU B 612  ? 0.4875 0.7189 0.5799 0.0700  0.0394  -0.0560 610  GLU B OE2 
13189 N N   . GLU B 613  ? 0.3245 0.5388 0.3748 0.0732  0.0468  -0.0602 611  GLU B N   
13190 C CA  . GLU B 613  ? 0.3324 0.5487 0.3758 0.0719  0.0496  -0.0592 611  GLU B CA  
13191 C C   . GLU B 613  ? 0.3508 0.5505 0.3845 0.0713  0.0462  -0.0606 611  GLU B C   
13192 O O   . GLU B 613  ? 0.3279 0.5252 0.3576 0.0667  0.0470  -0.0575 611  GLU B O   
13193 C CB  . GLU B 613  ? 0.3505 0.5785 0.3914 0.0786  0.0532  -0.0629 611  GLU B CB  
13194 N N   . ASP B 614  ? 0.3416 0.5298 0.3714 0.0757  0.0422  -0.0651 612  ASP B N   
13195 C CA  . ASP B 614  ? 0.3677 0.5401 0.3889 0.0745  0.0386  -0.0662 612  ASP B CA  
13196 C C   . ASP B 614  ? 0.3101 0.4750 0.3344 0.0673  0.0363  -0.0616 612  ASP B C   
13197 O O   . ASP B 614  ? 0.3049 0.4617 0.3237 0.0640  0.0350  -0.0602 612  ASP B O   
13198 C CB  . ASP B 614  ? 0.3304 0.4922 0.3466 0.0806  0.0347  -0.0719 612  ASP B CB  
13199 C CG  . ASP B 614  ? 0.3779 0.5422 0.3868 0.0877  0.0361  -0.0770 612  ASP B CG  
13200 O OD1 . ASP B 614  ? 0.4459 0.6155 0.4503 0.0869  0.0391  -0.0762 612  ASP B OD1 
13201 O OD2 . ASP B 614  ? 0.4504 0.6109 0.4574 0.0942  0.0340  -0.0819 612  ASP B OD2 
13202 N N   . ALA B 615  ? 0.3074 0.4750 0.3404 0.0652  0.0357  -0.0595 613  ALA B N   
13203 C CA  . ALA B 615  ? 0.2883 0.4502 0.3245 0.0586  0.0340  -0.0550 613  ALA B CA  
13204 C C   . ALA B 615  ? 0.3033 0.4700 0.3391 0.0533  0.0368  -0.0504 613  ALA B C   
13205 O O   . ALA B 615  ? 0.2596 0.4182 0.2919 0.0495  0.0352  -0.0482 613  ALA B O   
13206 C CB  . ALA B 615  ? 0.3238 0.4897 0.3695 0.0573  0.0334  -0.0535 613  ALA B CB  
13207 N N   . ARG B 616  ? 0.3252 0.5055 0.3643 0.0532  0.0410  -0.0488 614  ARG B N   
13208 C CA  . ARG B 616  ? 0.2759 0.4608 0.3141 0.0481  0.0436  -0.0441 614  ARG B CA  
13209 C C   . ARG B 616  ? 0.3036 0.4831 0.3319 0.0491  0.0435  -0.0454 614  ARG B C   
13210 O O   . ARG B 616  ? 0.3427 0.5181 0.3683 0.0445  0.0432  -0.0418 614  ARG B O   
13211 C CB  . ARG B 616  ? 0.3864 0.5877 0.4299 0.0478  0.0481  -0.0421 614  ARG B CB  
13212 C CG  . ARG B 616  ? 0.3990 0.6059 0.4526 0.0440  0.0481  -0.0388 614  ARG B CG  
13213 C CD  . ARG B 616  ? 0.4293 0.6527 0.4881 0.0423  0.0525  -0.0358 614  ARG B CD  
13214 N NE  . ARG B 616  ? 0.4717 0.7058 0.5326 0.0486  0.0546  -0.0399 614  ARG B NE  
13215 C CZ  . ARG B 616  ? 0.4801 0.7174 0.5477 0.0514  0.0534  -0.0419 614  ARG B CZ  
13216 N NH1 . ARG B 616  ? 0.4333 0.6640 0.5060 0.0482  0.0501  -0.0404 614  ARG B NH1 
13217 N NH2 . ARG B 616  ? 0.4542 0.7016 0.5232 0.0578  0.0554  -0.0457 614  ARG B NH2 
13218 N N   . ARG B 617  ? 0.3072 0.4860 0.3296 0.0551  0.0435  -0.0505 615  ARG B N   
13219 C CA  . ARG B 617  ? 0.3371 0.5105 0.3494 0.0561  0.0432  -0.0520 615  ARG B CA  
13220 C C   . ARG B 617  ? 0.3052 0.4640 0.3136 0.0533  0.0388  -0.0516 615  ARG B C   
13221 O O   . ARG B 617  ? 0.2818 0.4369 0.2848 0.0504  0.0385  -0.0496 615  ARG B O   
13222 C CB  . ARG B 617  ? 0.3288 0.5034 0.3354 0.0635  0.0437  -0.0580 615  ARG B CB  
13223 C CG  . ARG B 617  ? 0.3814 0.5480 0.3767 0.0648  0.0423  -0.0604 615  ARG B CG  
13224 C CD  . ARG B 617  ? 0.4668 0.6382 0.4558 0.0718  0.0443  -0.0655 615  ARG B CD  
13225 N NE  . ARG B 617  ? 0.5789 0.7456 0.5674 0.0782  0.0419  -0.0711 615  ARG B NE  
13226 C CZ  . ARG B 617  ? 0.6254 0.7794 0.6053 0.0817  0.0380  -0.0758 615  ARG B CZ  
13227 N NH1 . ARG B 617  ? 0.6044 0.7495 0.5760 0.0792  0.0360  -0.0756 615  ARG B NH1 
13228 N NH2 . ARG B 617  ? 0.5434 0.6934 0.5231 0.0877  0.0359  -0.0806 615  ARG B NH2 
13229 N N   . ALA B 618  ? 0.2626 0.4134 0.2738 0.0540  0.0354  -0.0532 616  ALA B N   
13230 C CA  . ALA B 618  ? 0.2915 0.4295 0.2996 0.0511  0.0314  -0.0524 616  ALA B CA  
13231 C C   . ALA B 618  ? 0.2430 0.3814 0.2542 0.0448  0.0318  -0.0467 616  ALA B C   
13232 O O   . ALA B 618  ? 0.2875 0.4193 0.2940 0.0422  0.0301  -0.0454 616  ALA B O   
13233 C CB  . ALA B 618  ? 0.2648 0.3957 0.2762 0.0526  0.0280  -0.0545 616  ALA B CB  
13234 N N   . VAL B 619  ? 0.2670 0.4131 0.2860 0.0422  0.0340  -0.0433 617  VAL B N   
13235 C CA  . VAL B 619  ? 0.2530 0.3987 0.2744 0.0365  0.0342  -0.0380 617  VAL B CA  
13236 C C   . VAL B 619  ? 0.3098 0.4586 0.3258 0.0348  0.0362  -0.0358 617  VAL B C   
13237 O O   . VAL B 619  ? 0.3043 0.4479 0.3179 0.0314  0.0349  -0.0329 617  VAL B O   
13238 C CB  . VAL B 619  ? 0.2534 0.4064 0.2838 0.0340  0.0359  -0.0350 617  VAL B CB  
13239 C CG1 . VAL B 619  ? 0.2484 0.3995 0.2806 0.0283  0.0356  -0.0297 617  VAL B CG1 
13240 C CG2 . VAL B 619  ? 0.2628 0.4122 0.2982 0.0356  0.0335  -0.0371 617  VAL B CG2 
13241 N N   . ARG B 620  ? 0.2891 0.4466 0.3026 0.0374  0.0394  -0.0372 618  ARG B N   
13242 C CA  . ARG B 620  ? 0.3366 0.4970 0.3441 0.0359  0.0413  -0.0352 618  ARG B CA  
13243 C C   . ARG B 620  ? 0.2858 0.4366 0.2846 0.0371  0.0385  -0.0376 618  ARG B C   
13244 O O   . ARG B 620  ? 0.2918 0.4406 0.2866 0.0342  0.0381  -0.0347 618  ARG B O   
13245 C CB  . ARG B 620  ? 0.3354 0.5080 0.3421 0.0387  0.0455  -0.0363 618  ARG B CB  
13246 C CG  . ARG B 620  ? 0.3670 0.5507 0.3824 0.0366  0.0485  -0.0332 618  ARG B CG  
13247 C CD  . ARG B 620  ? 0.4337 0.6309 0.4477 0.0380  0.0532  -0.0328 618  ARG B CD  
13248 N NE  . ARG B 620  ? 0.4432 0.6422 0.4524 0.0449  0.0539  -0.0388 618  ARG B NE  
13249 C CZ  . ARG B 620  ? 0.4331 0.6379 0.4467 0.0494  0.0548  -0.0423 618  ARG B CZ  
13250 N NH1 . ARG B 620  ? 0.3977 0.6083 0.4209 0.0476  0.0553  -0.0403 618  ARG B NH1 
13251 N NH2 . ARG B 620  ? 0.5030 0.7075 0.5110 0.0561  0.0549  -0.0481 618  ARG B NH2 
13252 N N   . LEU B 621  ? 0.2635 0.4084 0.2593 0.0414  0.0362  -0.0427 619  LEU B N   
13253 C CA  . LEU B 621  ? 0.3029 0.4376 0.2907 0.0420  0.0328  -0.0449 619  LEU B CA  
13254 C C   . LEU B 621  ? 0.3246 0.4511 0.3141 0.0376  0.0296  -0.0419 619  LEU B C   
13255 O O   . LEU B 621  ? 0.3005 0.4222 0.2847 0.0357  0.0278  -0.0409 619  LEU B O   
13256 C CB  . LEU B 621  ? 0.2925 0.4218 0.2770 0.0472  0.0306  -0.0509 619  LEU B CB  
13257 C CG  . LEU B 621  ? 0.3209 0.4563 0.3014 0.0529  0.0331  -0.0552 619  LEU B CG  
13258 C CD1 . LEU B 621  ? 0.3292 0.4581 0.3081 0.0580  0.0304  -0.0607 619  LEU B CD1 
13259 C CD2 . LEU B 621  ? 0.3679 0.5030 0.3388 0.0534  0.0336  -0.0560 619  LEU B CD2 
13260 N N   . ALA B 622  ? 0.2677 0.3930 0.2647 0.0360  0.0288  -0.0404 620  ALA B N   
13261 C CA  . ALA B 622  ? 0.3259 0.4447 0.3248 0.0322  0.0262  -0.0374 620  ALA B CA  
13262 C C   . ALA B 622  ? 0.2909 0.4131 0.2901 0.0282  0.0277  -0.0324 620  ALA B C   
13263 O O   . ALA B 622  ? 0.2611 0.3783 0.2577 0.0259  0.0256  -0.0305 620  ALA B O   
13264 C CB  . ALA B 622  ? 0.2523 0.3696 0.2588 0.0316  0.0252  -0.0369 620  ALA B CB  
13265 N N   . ALA B 623  ? 0.2800 0.4111 0.2821 0.0275  0.0312  -0.0301 621  ALA B N   
13266 C CA  . ALA B 623  ? 0.3257 0.4594 0.3276 0.0236  0.0324  -0.0250 621  ALA B CA  
13267 C C   . ALA B 623  ? 0.3126 0.4455 0.3062 0.0237  0.0322  -0.0250 621  ALA B C   
13268 O O   . ALA B 623  ? 0.3062 0.4360 0.2980 0.0209  0.0309  -0.0217 621  ALA B O   
13269 C CB  . ALA B 623  ? 0.2761 0.4196 0.2826 0.0224  0.0361  -0.0224 621  ALA B CB  
13270 N N   . ASP B 624  ? 0.2814 0.4168 0.2697 0.0272  0.0333  -0.0288 622  ASP B N   
13271 C CA  . ASP B 624  ? 0.3027 0.4370 0.2823 0.0275  0.0330  -0.0292 622  ASP B CA  
13272 C C   . ASP B 624  ? 0.3481 0.4727 0.3241 0.0267  0.0286  -0.0300 622  ASP B C   
13273 O O   . ASP B 624  ? 0.3806 0.5037 0.3517 0.0249  0.0276  -0.0280 622  ASP B O   
13274 C CB  . ASP B 624  ? 0.3714 0.5096 0.3457 0.0321  0.0347  -0.0338 622  ASP B CB  
13275 N N   . ALA B 625  ? 0.3406 0.4589 0.3190 0.0278  0.0260  -0.0326 623  ALA B N   
13276 C CA  . ALA B 625  ? 0.3537 0.4635 0.3290 0.0267  0.0219  -0.0333 623  ALA B CA  
13277 C C   . ALA B 625  ? 0.3434 0.4505 0.3241 0.0232  0.0203  -0.0293 623  ALA B C   
13278 O O   . ALA B 625  ? 0.3123 0.4136 0.2911 0.0219  0.0171  -0.0292 623  ALA B O   
13279 C CB  . ALA B 625  ? 0.4276 0.5313 0.4013 0.0296  0.0195  -0.0382 623  ALA B CB  
13280 N N   . ALA B 626  ? 0.3117 0.4229 0.2989 0.0217  0.0224  -0.0261 624  ALA B N   
13281 C CA  . ALA B 626  ? 0.2994 0.4075 0.2915 0.0190  0.0209  -0.0228 624  ALA B CA  
13282 C C   . ALA B 626  ? 0.3183 0.4242 0.3071 0.0169  0.0191  -0.0199 624  ALA B C   
13283 O O   . ALA B 626  ? 0.3384 0.4396 0.3286 0.0159  0.0164  -0.0193 624  ALA B O   
13284 C CB  . ALA B 626  ? 0.2823 0.3950 0.2809 0.0176  0.0234  -0.0198 624  ALA B CB  
13285 N N   . PRO B 627  ? 0.3202 0.4296 0.3048 0.0161  0.0204  -0.0177 625  PRO B N   
13286 C CA  . PRO B 627  ? 0.3164 0.4237 0.2982 0.0142  0.0183  -0.0148 625  PRO B CA  
13287 C C   . PRO B 627  ? 0.2984 0.4009 0.2758 0.0146  0.0148  -0.0174 625  PRO B C   
13288 O O   . PRO B 627  ? 0.3605 0.4604 0.3389 0.0131  0.0123  -0.0154 625  PRO B O   
13289 C CB  . PRO B 627  ? 0.3417 0.4539 0.3187 0.0136  0.0205  -0.0127 625  PRO B CB  
13290 C CG  . PRO B 627  ? 0.3573 0.4750 0.3377 0.0141  0.0241  -0.0126 625  PRO B CG  
13291 C CD  . PRO B 627  ? 0.3478 0.4639 0.3306 0.0166  0.0239  -0.0172 625  PRO B CD  
13292 N N   . ASP B 628  ? 0.2963 0.3977 0.2690 0.0166  0.0145  -0.0217 626  ASP B N   
13293 C CA  . ASP B 628  ? 0.3295 0.4256 0.2976 0.0165  0.0109  -0.0241 626  ASP B CA  
13294 C C   . ASP B 628  ? 0.3472 0.4388 0.3202 0.0156  0.0084  -0.0243 626  ASP B C   
13295 O O   . ASP B 628  ? 0.2878 0.3767 0.2598 0.0139  0.0054  -0.0235 626  ASP B O   
13296 C CB  . ASP B 628  ? 0.3442 0.4387 0.3062 0.0192  0.0108  -0.0291 626  ASP B CB  
13297 C CG  . ASP B 628  ? 0.4381 0.5367 0.3935 0.0202  0.0128  -0.0292 626  ASP B CG  
13298 O OD1 . ASP B 628  ? 0.4762 0.5765 0.4290 0.0183  0.0123  -0.0261 626  ASP B OD1 
13299 O OD2 . ASP B 628  ? 0.5104 0.6110 0.4633 0.0231  0.0148  -0.0325 626  ASP B OD2 
13300 N N   . TRP B 629  ? 0.2851 0.3765 0.2634 0.0167  0.0097  -0.0254 627  TRP B N   
13301 C CA  . TRP B 629  ? 0.2712 0.3584 0.2536 0.0160  0.0075  -0.0258 627  TRP B CA  
13302 C C   . TRP B 629  ? 0.2527 0.3410 0.2400 0.0139  0.0072  -0.0215 627  TRP B C   
13303 O O   . TRP B 629  ? 0.2587 0.3444 0.2471 0.0126  0.0046  -0.0209 627  TRP B O   
13304 C CB  . TRP B 629  ? 0.2324 0.3188 0.2185 0.0179  0.0087  -0.0283 627  TRP B CB  
13305 C CG  . TRP B 629  ? 0.2732 0.3555 0.2633 0.0172  0.0066  -0.0285 627  TRP B CG  
13306 C CD1 . TRP B 629  ? 0.2310 0.3139 0.2275 0.0169  0.0075  -0.0270 627  TRP B CD1 
13307 C CD2 . TRP B 629  ? 0.3000 0.3767 0.2873 0.0163  0.0031  -0.0300 627  TRP B CD2 
13308 N NE1 . TRP B 629  ? 0.2435 0.3219 0.2413 0.0161  0.0050  -0.0276 627  TRP B NE1 
13309 C CE2 . TRP B 629  ? 0.2495 0.3242 0.2420 0.0155  0.0023  -0.0293 627  TRP B CE2 
13310 C CE3 . TRP B 629  ? 0.2886 0.3616 0.2693 0.0157  0.0004  -0.0319 627  TRP B CE3 
13311 C CZ2 . TRP B 629  ? 0.2350 0.3048 0.2264 0.0142  -0.0009 -0.0301 627  TRP B CZ2 
13312 C CZ3 . TRP B 629  ? 0.2665 0.3342 0.2464 0.0141  -0.0031 -0.0327 627  TRP B CZ3 
13313 C CH2 . TRP B 629  ? 0.2922 0.3587 0.2775 0.0133  -0.0035 -0.0316 627  TRP B CH2 
13314 N N   . ALA B 630  ? 0.2749 0.3671 0.2649 0.0136  0.0097  -0.0186 628  ALA B N   
13315 C CA  . ALA B 630  ? 0.2820 0.3747 0.2756 0.0121  0.0092  -0.0146 628  ALA B CA  
13316 C C   . ALA B 630  ? 0.3074 0.3998 0.2977 0.0109  0.0068  -0.0130 628  ALA B C   
13317 O O   . ALA B 630  ? 0.3307 0.4226 0.3239 0.0101  0.0053  -0.0108 628  ALA B O   
13318 C CB  . ALA B 630  ? 0.3115 0.4077 0.3073 0.0118  0.0119  -0.0117 628  ALA B CB  
13319 N N   . ALA B 631  ? 0.3042 0.3972 0.2882 0.0109  0.0062  -0.0141 629  ALA B N   
13320 C CA  . ALA B 631  ? 0.2991 0.3923 0.2794 0.0097  0.0037  -0.0126 629  ALA B CA  
13321 C C   . ALA B 631  ? 0.3293 0.4194 0.3090 0.0087  0.0003  -0.0144 629  ALA B C   
13322 O O   . ALA B 631  ? 0.3028 0.3936 0.2808 0.0073  -0.0021 -0.0128 629  ALA B O   
13323 C CB  . ALA B 631  ? 0.3081 0.4030 0.2815 0.0099  0.0043  -0.0131 629  ALA B CB  
13324 N N   . VAL B 632  ? 0.3005 0.3873 0.2815 0.0092  0.0000  -0.0174 630  VAL B N   
13325 C CA  . VAL B 632  ? 0.2711 0.3547 0.2517 0.0078  -0.0033 -0.0186 630  VAL B CA  
13326 C C   . VAL B 632  ? 0.2553 0.3407 0.2419 0.0067  -0.0040 -0.0155 630  VAL B C   
13327 O O   . VAL B 632  ? 0.2990 0.3850 0.2907 0.0077  -0.0020 -0.0146 630  VAL B O   
13328 C CB  . VAL B 632  ? 0.2742 0.3533 0.2543 0.0087  -0.0037 -0.0224 630  VAL B CB  
13329 C CG1 . VAL B 632  ? 0.2558 0.3312 0.2355 0.0066  -0.0073 -0.0232 630  VAL B CG1 
13330 C CG2 . VAL B 632  ? 0.2907 0.3683 0.2647 0.0106  -0.0029 -0.0258 630  VAL B CG2 
13331 N N   . PRO B 633  ? 0.2515 0.3383 0.2376 0.0049  -0.0067 -0.0138 631  PRO B N   
13332 C CA  . PRO B 633  ? 0.2533 0.3428 0.2450 0.0044  -0.0071 -0.0109 631  PRO B CA  
13333 C C   . PRO B 633  ? 0.2665 0.3538 0.2625 0.0046  -0.0066 -0.0121 631  PRO B C   
13334 O O   . PRO B 633  ? 0.2531 0.3365 0.2471 0.0041  -0.0076 -0.0150 631  PRO B O   
13335 C CB  . PRO B 633  ? 0.2714 0.3626 0.2612 0.0020  -0.0105 -0.0100 631  PRO B CB  
13336 C CG  . PRO B 633  ? 0.2628 0.3536 0.2461 0.0017  -0.0113 -0.0108 631  PRO B CG  
13337 C CD  . PRO B 633  ? 0.2441 0.3309 0.2243 0.0033  -0.0093 -0.0142 631  PRO B CD  
13338 N N   . PRO B 634  ? 0.2855 0.3746 0.2867 0.0056  -0.0052 -0.0101 632  PRO B N   
13339 C CA  . PRO B 634  ? 0.2922 0.3792 0.2972 0.0060  -0.0047 -0.0113 632  PRO B CA  
13340 C C   . PRO B 634  ? 0.2216 0.3072 0.2261 0.0039  -0.0073 -0.0122 632  PRO B C   
13341 O O   . PRO B 634  ? 0.2442 0.3262 0.2489 0.0039  -0.0074 -0.0144 632  PRO B O   
13342 C CB  . PRO B 634  ? 0.2707 0.3604 0.2806 0.0073  -0.0035 -0.0085 632  PRO B CB  
13343 C CG  . PRO B 634  ? 0.3199 0.4115 0.3284 0.0081  -0.0025 -0.0065 632  PRO B CG  
13344 C CD  . PRO B 634  ? 0.2437 0.3362 0.2472 0.0068  -0.0041 -0.0069 632  PRO B CD  
13345 N N   . SER B 635  ? 0.2430 0.3318 0.2469 0.0020  -0.0095 -0.0105 633  SER B N   
13346 C CA  . SER B 635  ? 0.2413 0.3292 0.2447 -0.0006 -0.0121 -0.0110 633  SER B CA  
13347 C C   . SER B 635  ? 0.2349 0.3170 0.2327 -0.0020 -0.0139 -0.0141 633  SER B C   
13348 O O   . SER B 635  ? 0.2361 0.3147 0.2332 -0.0037 -0.0157 -0.0152 633  SER B O   
13349 C CB  . SER B 635  ? 0.3013 0.3950 0.3056 -0.0026 -0.0142 -0.0082 633  SER B CB  
13350 O OG  . SER B 635  ? 0.3592 0.4537 0.3595 -0.0031 -0.0154 -0.0080 633  SER B OG  
13351 N N   . GLU B 636  ? 0.2421 0.3227 0.2355 -0.0011 -0.0137 -0.0154 634  GLU B N   
13352 C CA  . GLU B 636  ? 0.2442 0.3187 0.2316 -0.0015 -0.0153 -0.0188 634  GLU B CA  
13353 C C   . GLU B 636  ? 0.2445 0.3148 0.2326 0.0009  -0.0133 -0.0215 634  GLU B C   
13354 O O   . GLU B 636  ? 0.2532 0.3176 0.2379 0.0006  -0.0151 -0.0242 634  GLU B O   
13355 C CB  . GLU B 636  ? 0.3016 0.3764 0.2836 -0.0010 -0.0155 -0.0196 634  GLU B CB  
13356 C CG  . GLU B 636  ? 0.3430 0.4208 0.3232 -0.0039 -0.0184 -0.0175 634  GLU B CG  
13357 C CD  . GLU B 636  ? 0.4940 0.5684 0.4725 -0.0074 -0.0223 -0.0182 634  GLU B CD  
13358 O OE1 . GLU B 636  ? 0.5143 0.5817 0.4879 -0.0075 -0.0238 -0.0215 634  GLU B OE1 
13359 O OE2 . GLU B 636  ? 0.5865 0.6654 0.5685 -0.0098 -0.0238 -0.0154 634  GLU B OE2 
13360 N N   . ARG B 637  ? 0.2010 0.2740 0.1931 0.0033  -0.0100 -0.0207 635  ARG B N   
13361 C CA  . ARG B 637  ? 0.2081 0.2780 0.2018 0.0054  -0.0083 -0.0229 635  ARG B CA  
13362 C C   . ARG B 637  ? 0.2396 0.3072 0.2362 0.0043  -0.0096 -0.0229 635  ARG B C   
13363 O O   . ARG B 637  ? 0.2320 0.2945 0.2272 0.0050  -0.0104 -0.0255 635  ARG B O   
13364 C CB  . ARG B 637  ? 0.2439 0.3176 0.2417 0.0076  -0.0048 -0.0217 635  ARG B CB  
13365 C CG  . ARG B 637  ? 0.2620 0.3386 0.2571 0.0084  -0.0033 -0.0211 635  ARG B CG  
13366 C CD  . ARG B 637  ? 0.2616 0.3408 0.2600 0.0102  0.0001  -0.0202 635  ARG B CD  
13367 N NE  . ARG B 637  ? 0.2570 0.3381 0.2609 0.0101  0.0010  -0.0174 635  ARG B NE  
13368 C CZ  . ARG B 637  ? 0.3234 0.4077 0.3286 0.0100  0.0019  -0.0144 635  ARG B CZ  
13369 N NH1 . ARG B 637  ? 0.3463 0.4326 0.3478 0.0097  0.0021  -0.0133 635  ARG B NH1 
13370 N NH2 . ARG B 637  ? 0.2396 0.3245 0.2494 0.0104  0.0026  -0.0124 635  ARG B NH2 
13371 N N   . ALA B 638  ? 0.2312 0.3024 0.2316 0.0029  -0.0098 -0.0200 636  ALA B N   
13372 C CA  . ALA B 638  ? 0.2117 0.2815 0.2144 0.0015  -0.0110 -0.0196 636  ALA B CA  
13373 C C   . ALA B 638  ? 0.2258 0.2909 0.2240 -0.0012 -0.0145 -0.0209 636  ALA B C   
13374 O O   . ALA B 638  ? 0.2224 0.2832 0.2205 -0.0018 -0.0156 -0.0220 636  ALA B O   
13375 C CB  . ALA B 638  ? 0.2175 0.2931 0.2246 0.0008  -0.0105 -0.0162 636  ALA B CB  
13376 N N   . ALA B 639  ? 0.2107 0.2762 0.2051 -0.0031 -0.0165 -0.0206 637  ALA B N   
13377 C CA  . ALA B 639  ? 0.2508 0.3108 0.2401 -0.0060 -0.0203 -0.0219 637  ALA B CA  
13378 C C   . ALA B 639  ? 0.2184 0.2703 0.2034 -0.0041 -0.0209 -0.0258 637  ALA B C   
13379 O O   . ALA B 639  ? 0.2368 0.2825 0.2188 -0.0060 -0.0239 -0.0270 637  ALA B O   
13380 C CB  . ALA B 639  ? 0.2004 0.2621 0.1859 -0.0081 -0.0225 -0.0213 637  ALA B CB  
13381 N N   . CYS B 640  ? 0.2103 0.2623 0.1950 -0.0004 -0.0183 -0.0278 638  CYS B N   
13382 C CA  . CYS B 640  ? 0.2193 0.2647 0.2005 0.0022  -0.0186 -0.0316 638  CYS B CA  
13383 C C   . CYS B 640  ? 0.2276 0.2705 0.2123 0.0027  -0.0184 -0.0318 638  CYS B C   
13384 O O   . CYS B 640  ? 0.1944 0.2301 0.1757 0.0029  -0.0207 -0.0341 638  CYS B O   
13385 C CB  . CYS B 640  ? 0.1980 0.2461 0.1793 0.0060  -0.0153 -0.0333 638  CYS B CB  
13386 S SG  . CYS B 640  ? 0.2675 0.3170 0.2428 0.0062  -0.0156 -0.0340 638  CYS B SG  
13387 N N   . LEU B 641  ? 0.1778 0.2260 0.1687 0.0032  -0.0158 -0.0295 639  LEU B N   
13388 C CA  . LEU B 641  ? 0.1899 0.2361 0.1840 0.0036  -0.0156 -0.0295 639  LEU B CA  
13389 C C   . LEU B 641  ? 0.2155 0.2580 0.2079 0.0000  -0.0189 -0.0285 639  LEU B C   
13390 O O   . LEU B 641  ? 0.2131 0.2500 0.2043 0.0002  -0.0204 -0.0298 639  LEU B O   
13391 C CB  . LEU B 641  ? 0.2081 0.2606 0.2088 0.0046  -0.0125 -0.0272 639  LEU B CB  
13392 C CG  . LEU B 641  ? 0.2302 0.2848 0.2340 0.0080  -0.0094 -0.0282 639  LEU B CG  
13393 C CD1 . LEU B 641  ? 0.2591 0.3153 0.2604 0.0095  -0.0081 -0.0294 639  LEU B CD1 
13394 C CD2 . LEU B 641  ? 0.2378 0.2973 0.2472 0.0081  -0.0072 -0.0256 639  LEU B CD2 
13395 N N   . ASP B 642  ? 0.2067 0.2528 0.1991 -0.0033 -0.0202 -0.0259 640  ASP B N   
13396 C CA  . ASP B 642  ? 0.2273 0.2711 0.2184 -0.0074 -0.0233 -0.0243 640  ASP B CA  
13397 C C   . ASP B 642  ? 0.1921 0.2266 0.1762 -0.0088 -0.0271 -0.0268 640  ASP B C   
13398 O O   . ASP B 642  ? 0.1991 0.2281 0.1814 -0.0109 -0.0296 -0.0267 640  ASP B O   
13399 C CB  . ASP B 642  ? 0.2294 0.2803 0.2223 -0.0107 -0.0237 -0.0209 640  ASP B CB  
13400 C CG  . ASP B 642  ? 0.2666 0.3255 0.2661 -0.0098 -0.0208 -0.0182 640  ASP B CG  
13401 O OD1 . ASP B 642  ? 0.2487 0.3069 0.2510 -0.0079 -0.0191 -0.0185 640  ASP B OD1 
13402 O OD2 . ASP B 642  ? 0.2438 0.3098 0.2457 -0.0107 -0.0203 -0.0158 640  ASP B OD2 
13403 N N   . ARG B 643  ? 0.2094 0.2416 0.1890 -0.0077 -0.0279 -0.0290 641  ARG B N   
13404 C CA  . ARG B 643  ? 0.2343 0.2566 0.2065 -0.0084 -0.0317 -0.0318 641  ARG B CA  
13405 C C   . ARG B 643  ? 0.2461 0.2617 0.2174 -0.0049 -0.0316 -0.0347 641  ARG B C   
13406 O O   . ARG B 643  ? 0.2620 0.2688 0.2287 -0.0062 -0.0351 -0.0360 641  ARG B O   
13407 C CB  . ARG B 643  ? 0.2477 0.2691 0.2150 -0.0073 -0.0323 -0.0339 641  ARG B CB  
13408 C CG  . ARG B 643  ? 0.3093 0.3347 0.2757 -0.0117 -0.0342 -0.0312 641  ARG B CG  
13409 C CD  . ARG B 643  ? 0.3244 0.3467 0.2840 -0.0111 -0.0358 -0.0337 641  ARG B CD  
13410 N NE  . ARG B 643  ? 0.3535 0.3808 0.3145 -0.0066 -0.0318 -0.0349 641  ARG B NE  
13411 C CZ  . ARG B 643  ? 0.3515 0.3871 0.3154 -0.0068 -0.0297 -0.0326 641  ARG B CZ  
13412 N NH1 . ARG B 643  ? 0.3066 0.3471 0.2727 -0.0108 -0.0311 -0.0291 641  ARG B NH1 
13413 N NH2 . ARG B 643  ? 0.3234 0.3626 0.2879 -0.0030 -0.0262 -0.0336 641  ARG B NH2 
13414 N N   . ALA B 644  ? 0.2362 0.2560 0.2117 -0.0006 -0.0277 -0.0357 642  ALA B N   
13415 C CA  . ALA B 644  ? 0.2248 0.2397 0.2003 0.0029  -0.0274 -0.0383 642  ALA B CA  
13416 C C   . ALA B 644  ? 0.2654 0.2776 0.2428 0.0009  -0.0288 -0.0366 642  ALA B C   
13417 O O   . ALA B 644  ? 0.2237 0.2279 0.1980 0.0020  -0.0311 -0.0385 642  ALA B O   
13418 C CB  . ALA B 644  ? 0.2129 0.2343 0.1935 0.0072  -0.0229 -0.0390 642  ALA B CB  
13419 N N   . ALA B 645  ? 0.2302 0.2491 0.2126 -0.0018 -0.0274 -0.0329 643  ALA B N   
13420 C CA  . ALA B 645  ? 0.2083 0.2255 0.1922 -0.0040 -0.0285 -0.0310 643  ALA B CA  
13421 C C   . ALA B 645  ? 0.2488 0.2582 0.2269 -0.0082 -0.0332 -0.0305 643  ALA B C   
13422 O O   . ALA B 645  ? 0.2534 0.2562 0.2295 -0.0086 -0.0354 -0.0309 643  ALA B O   
13423 C CB  . ALA B 645  ? 0.2232 0.2496 0.2131 -0.0057 -0.0260 -0.0273 643  ALA B CB  
13424 N N   . GLU B 646  ? 0.2293 0.2390 0.2043 -0.0114 -0.0352 -0.0297 644  GLU B N   
13425 C CA  . GLU B 646  ? 0.3244 0.3261 0.2933 -0.0158 -0.0401 -0.0293 644  GLU B CA  
13426 C C   . GLU B 646  ? 0.3040 0.2935 0.2665 -0.0132 -0.0430 -0.0333 644  GLU B C   
13427 O O   . GLU B 646  ? 0.3137 0.2948 0.2721 -0.0157 -0.0468 -0.0329 644  GLU B O   
13428 C CB  . GLU B 646  ? 0.2750 0.2787 0.2412 -0.0193 -0.0420 -0.0284 644  GLU B CB  
13429 C CG  . GLU B 646  ? 0.3266 0.3412 0.2982 -0.0228 -0.0404 -0.0242 644  GLU B CG  
13430 C CD  . GLU B 646  ? 0.4414 0.4565 0.4144 -0.0274 -0.0420 -0.0208 644  GLU B CD  
13431 O OE1 . GLU B 646  ? 0.5728 0.5786 0.5404 -0.0304 -0.0461 -0.0211 644  GLU B OE1 
13432 O OE2 . GLU B 646  ? 0.4947 0.5193 0.4738 -0.0278 -0.0391 -0.0179 644  GLU B OE2 
13433 N N   . LEU B 647  ? 0.2579 0.2466 0.2193 -0.0080 -0.0413 -0.0369 645  LEU B N   
13434 C CA  . LEU B 647  ? 0.2773 0.2552 0.2326 -0.0046 -0.0439 -0.0411 645  LEU B CA  
13435 C C   . LEU B 647  ? 0.2866 0.2613 0.2439 -0.0020 -0.0436 -0.0416 645  LEU B C   
13436 O O   . LEU B 647  ? 0.3008 0.2647 0.2527 -0.0018 -0.0474 -0.0432 645  LEU B O   
13437 C CB  . LEU B 647  ? 0.2918 0.2716 0.2458 0.0006  -0.0416 -0.0447 645  LEU B CB  
13438 C CG  . LEU B 647  ? 0.2954 0.2764 0.2455 -0.0011 -0.0424 -0.0451 645  LEU B CG  
13439 C CD1 . LEU B 647  ? 0.3315 0.3154 0.2808 0.0046  -0.0394 -0.0486 645  LEU B CD1 
13440 C CD2 . LEU B 647  ? 0.3841 0.3536 0.3255 -0.0045 -0.0483 -0.0462 645  LEU B CD2 
13441 N N   . MET B 648  ? 0.2611 0.2445 0.2258 0.0000  -0.0394 -0.0404 646  MET B N   
13442 C CA  . MET B 648  ? 0.2550 0.2360 0.2220 0.0023  -0.0391 -0.0407 646  MET B CA  
13443 C C   . MET B 648  ? 0.2863 0.2628 0.2517 -0.0025 -0.0422 -0.0377 646  MET B C   
13444 O O   . MET B 648  ? 0.3147 0.2837 0.2779 -0.0014 -0.0445 -0.0386 646  MET B O   
13445 C CB  . MET B 648  ? 0.2508 0.2420 0.2258 0.0048  -0.0342 -0.0398 646  MET B CB  
13446 C CG  . MET B 648  ? 0.3137 0.3088 0.2906 0.0100  -0.0312 -0.0427 646  MET B CG  
13447 S SD  . MET B 648  ? 0.2835 0.2879 0.2694 0.0125  -0.0266 -0.0415 646  MET B SD  
13448 C CE  . MET B 648  ? 0.2208 0.2308 0.2081 0.0169  -0.0233 -0.0442 646  MET B CE  
13449 N N   . GLN B 649  ? 0.2911 0.2729 0.2581 -0.0077 -0.0421 -0.0340 647  GLN B N   
13450 C CA  . GLN B 649  ? 0.2641 0.2429 0.2296 -0.0129 -0.0448 -0.0307 647  GLN B CA  
13451 C C   . GLN B 649  ? 0.2762 0.2419 0.2332 -0.0153 -0.0505 -0.0318 647  GLN B C   
13452 O O   . GLN B 649  ? 0.3050 0.2635 0.2592 -0.0167 -0.0532 -0.0310 647  GLN B O   
13453 C CB  . GLN B 649  ? 0.2946 0.2827 0.2634 -0.0178 -0.0436 -0.0267 647  GLN B CB  
13454 C CG  . GLN B 649  ? 0.2746 0.2615 0.2424 -0.0234 -0.0459 -0.0229 647  GLN B CG  
13455 C CD  . GLN B 649  ? 0.3002 0.2908 0.2723 -0.0218 -0.0434 -0.0216 647  GLN B CD  
13456 O OE1 . GLN B 649  ? 0.2810 0.2820 0.2592 -0.0212 -0.0396 -0.0199 647  GLN B OE1 
13457 N NE2 . GLN B 649  ? 0.2755 0.2571 0.2444 -0.0207 -0.0457 -0.0227 647  GLN B NE2 
13458 N N   . ALA B 650  ? 0.2928 0.2550 0.2452 -0.0159 -0.0525 -0.0336 648  ALA B N   
13459 C CA  . ALA B 650  ? 0.3234 0.2721 0.2669 -0.0182 -0.0582 -0.0349 648  ALA B CA  
13460 C C   . ALA B 650  ? 0.3915 0.3296 0.3308 -0.0127 -0.0600 -0.0390 648  ALA B C   
13461 O O   . ALA B 650  ? 0.3997 0.3257 0.3325 -0.0144 -0.0650 -0.0392 648  ALA B O   
13462 C CB  . ALA B 650  ? 0.3124 0.2601 0.2517 -0.0194 -0.0598 -0.0364 648  ALA B CB  
13463 N N   . ARG B 651  ? 0.3308 0.2733 0.2738 -0.0060 -0.0563 -0.0420 649  ARG B N   
13464 C CA  . ARG B 651  ? 0.3139 0.2482 0.2537 0.0001  -0.0576 -0.0462 649  ARG B CA  
13465 C C   . ARG B 651  ? 0.3245 0.2608 0.2691 0.0025  -0.0560 -0.0455 649  ARG B C   
13466 O O   . ARG B 651  ? 0.3494 0.2816 0.2932 0.0083  -0.0562 -0.0488 649  ARG B O   
13467 C CB  . ARG B 651  ? 0.3409 0.2792 0.2812 0.0059  -0.0547 -0.0503 649  ARG B CB  
13468 C CG  . ARG B 651  ? 0.3380 0.2728 0.2722 0.0035  -0.0571 -0.0513 649  ARG B CG  
13469 C CD  . ARG B 651  ? 0.3612 0.3000 0.2950 0.0088  -0.0543 -0.0550 649  ARG B CD  
13470 N NE  . ARG B 651  ? 0.3592 0.2958 0.2875 0.0058  -0.0563 -0.0554 649  ARG B NE  
13471 C CZ  . ARG B 651  ? 0.4127 0.3544 0.3405 0.0086  -0.0539 -0.0576 649  ARG B CZ  
13472 N NH1 . ARG B 651  ? 0.3535 0.3026 0.2857 0.0145  -0.0493 -0.0597 649  ARG B NH1 
13473 N NH2 . ARG B 651  ? 0.3849 0.3247 0.3077 0.0051  -0.0561 -0.0575 649  ARG B NH2 
13474 N N   . MET B 652  ? 0.3371 0.2796 0.2863 -0.0017 -0.0545 -0.0412 650  MET B N   
13475 C CA  . MET B 652  ? 0.2835 0.2283 0.2371 0.0003  -0.0530 -0.0403 650  MET B CA  
13476 C C   . MET B 652  ? 0.3343 0.2669 0.2828 0.0029  -0.0571 -0.0423 650  MET B C   
13477 O O   . MET B 652  ? 0.3461 0.2800 0.2977 0.0082  -0.0556 -0.0443 650  MET B O   
13478 C CB  . MET B 652  ? 0.2942 0.2454 0.2515 -0.0053 -0.0518 -0.0353 650  MET B CB  
13479 C CG  . MET B 652  ? 0.3070 0.2603 0.2682 -0.0037 -0.0505 -0.0342 650  MET B CG  
13480 S SD  . MET B 652  ? 0.3318 0.2939 0.2972 -0.0094 -0.0485 -0.0288 650  MET B SD  
13481 C CE  . MET B 652  ? 0.3052 0.2818 0.2789 -0.0071 -0.0424 -0.0288 650  MET B CE  
13482 N N   . PRO B 653  ? 0.3176 0.2380 0.2582 -0.0005 -0.0625 -0.0417 651  PRO B N   
13483 C CA  . PRO B 653  ? 0.3392 0.2476 0.2749 0.0024  -0.0666 -0.0434 651  PRO B CA  
13484 C C   . PRO B 653  ? 0.3390 0.2446 0.2740 0.0107  -0.0662 -0.0488 651  PRO B C   
13485 O O   . PRO B 653  ? 0.3704 0.2737 0.3066 0.0151  -0.0666 -0.0502 651  PRO B O   
13486 C CB  . PRO B 653  ? 0.3851 0.2805 0.3117 -0.0031 -0.0726 -0.0420 651  PRO B CB  
13487 C CG  . PRO B 653  ? 0.4235 0.3270 0.3525 -0.0104 -0.0712 -0.0378 651  PRO B CG  
13488 C CD  . PRO B 653  ? 0.3508 0.2675 0.2866 -0.0075 -0.0656 -0.0391 651  PRO B CD  
13489 N N   . THR B 654  ? 0.3618 0.2681 0.2949 0.0130  -0.0655 -0.0519 652  THR B N   
13490 C CA  . THR B 654  ? 0.3778 0.2832 0.3104 0.0211  -0.0646 -0.0571 652  THR B CA  
13491 C C   . THR B 654  ? 0.3907 0.3098 0.3330 0.0252  -0.0588 -0.0575 652  THR B C   
13492 O O   . THR B 654  ? 0.4142 0.3331 0.3581 0.0314  -0.0584 -0.0603 652  THR B O   
13493 C CB  . THR B 654  ? 0.3948 0.2981 0.3225 0.0222  -0.0650 -0.0601 652  THR B CB  
13494 O OG1 . THR B 654  ? 0.3944 0.2842 0.3129 0.0179  -0.0709 -0.0597 652  THR B OG1 
13495 C CG2 . THR B 654  ? 0.3488 0.2512 0.2753 0.0310  -0.0641 -0.0657 652  THR B CG2 
13496 N N   . LEU B 655  ? 0.3549 0.2860 0.3035 0.0218  -0.0544 -0.0545 653  LEU B N   
13497 C CA  . LEU B 655  ? 0.2971 0.2405 0.2546 0.0249  -0.0493 -0.0544 653  LEU B CA  
13498 C C   . LEU B 655  ? 0.3038 0.2460 0.2642 0.0261  -0.0500 -0.0534 653  LEU B C   
13499 O O   . LEU B 655  ? 0.3025 0.2492 0.2673 0.0313  -0.0481 -0.0555 653  LEU B O   
13500 C CB  . LEU B 655  ? 0.3323 0.2869 0.2954 0.0206  -0.0453 -0.0510 653  LEU B CB  
13501 C CG  . LEU B 655  ? 0.3449 0.3014 0.3055 0.0193  -0.0446 -0.0518 653  LEU B CG  
13502 C CD1 . LEU B 655  ? 0.3005 0.2691 0.2673 0.0162  -0.0403 -0.0486 653  LEU B CD1 
13503 C CD2 . LEU B 655  ? 0.3379 0.2942 0.2970 0.0257  -0.0436 -0.0564 653  LEU B CD2 
13504 N N   . LEU B 656  ? 0.3003 0.2370 0.2582 0.0212  -0.0529 -0.0502 654  LEU B N   
13505 C CA  . LEU B 656  ? 0.3088 0.2434 0.2683 0.0221  -0.0540 -0.0490 654  LEU B CA  
13506 C C   . LEU B 656  ? 0.3227 0.2503 0.2798 0.0286  -0.0565 -0.0529 654  LEU B C   
13507 O O   . LEU B 656  ? 0.3459 0.2778 0.3078 0.0324  -0.0552 -0.0536 654  LEU B O   
13508 C CB  . LEU B 656  ? 0.3274 0.2545 0.2821 0.0159  -0.0577 -0.0453 654  LEU B CB  
13509 C CG  . LEU B 656  ? 0.3598 0.2936 0.3165 0.0092  -0.0558 -0.0411 654  LEU B CG  
13510 C CD1 . LEU B 656  ? 0.3480 0.2744 0.2997 0.0034  -0.0597 -0.0374 654  LEU B CD1 
13511 C CD2 . LEU B 656  ? 0.3404 0.2872 0.3057 0.0100  -0.0506 -0.0398 654  LEU B CD2 
13512 N N   . GLY B 657  ? 0.3721 0.2885 0.3213 0.0301  -0.0606 -0.0554 655  GLY B N   
13513 C CA  . GLY B 657  ? 0.3792 0.2878 0.3253 0.0367  -0.0636 -0.0592 655  GLY B CA  
13514 C C   . GLY B 657  ? 0.3869 0.3053 0.3393 0.0436  -0.0596 -0.0627 655  GLY B C   
13515 O O   . GLY B 657  ? 0.3590 0.2774 0.3136 0.0488  -0.0602 -0.0644 655  GLY B O   
13516 N N   . LEU B 658  ? 0.3222 0.2497 0.2776 0.0437  -0.0555 -0.0635 656  LEU B N   
13517 C CA  . LEU B 658  ? 0.3593 0.2977 0.3211 0.0494  -0.0512 -0.0661 656  LEU B CA  
13518 C C   . LEU B 658  ? 0.3551 0.3041 0.3259 0.0489  -0.0479 -0.0638 656  LEU B C   
13519 O O   . LEU B 658  ? 0.3311 0.2848 0.3064 0.0541  -0.0468 -0.0658 656  LEU B O   
13520 C CB  . LEU B 658  ? 0.3537 0.2988 0.3159 0.0487  -0.0478 -0.0670 656  LEU B CB  
13521 C CG  . LEU B 658  ? 0.3658 0.3215 0.3332 0.0547  -0.0436 -0.0700 656  LEU B CG  
13522 C CD1 . LEU B 658  ? 0.3147 0.2651 0.2791 0.0623  -0.0460 -0.0745 656  LEU B CD1 
13523 C CD2 . LEU B 658  ? 0.3480 0.3090 0.3144 0.0536  -0.0407 -0.0705 656  LEU B CD2 
13524 N N   . ILE B 659  ? 0.3175 0.2703 0.2910 0.0428  -0.0464 -0.0596 657  ILE B N   
13525 C CA  . ILE B 659  ? 0.2714 0.2338 0.2530 0.0421  -0.0433 -0.0575 657  ILE B CA  
13526 C C   . ILE B 659  ? 0.3099 0.2672 0.2914 0.0441  -0.0463 -0.0575 657  ILE B C   
13527 O O   . ILE B 659  ? 0.2974 0.2616 0.2851 0.0468  -0.0446 -0.0579 657  ILE B O   
13528 C CB  . ILE B 659  ? 0.2864 0.2533 0.2700 0.0356  -0.0413 -0.0533 657  ILE B CB  
13529 C CG1 . ILE B 659  ? 0.2650 0.2391 0.2503 0.0343  -0.0378 -0.0533 657  ILE B CG1 
13530 C CG2 . ILE B 659  ? 0.2872 0.2616 0.2777 0.0349  -0.0390 -0.0512 657  ILE B CG2 
13531 C CD1 . ILE B 659  ? 0.3093 0.2847 0.2939 0.0279  -0.0372 -0.0495 657  ILE B CD1 
13532 N N   . ILE B 660  ? 0.2949 0.2400 0.2692 0.0424  -0.0511 -0.0568 658  ILE B N   
13533 C CA  . ILE B 660  ? 0.2798 0.2189 0.2530 0.0441  -0.0545 -0.0566 658  ILE B CA  
13534 C C   . ILE B 660  ? 0.2622 0.2019 0.2372 0.0519  -0.0551 -0.0607 658  ILE B C   
13535 O O   . ILE B 660  ? 0.3147 0.2581 0.2943 0.0545  -0.0551 -0.0607 658  ILE B O   
13536 C CB  . ILE B 660  ? 0.3089 0.2338 0.2731 0.0407  -0.0598 -0.0551 658  ILE B CB  
13537 C CG1 . ILE B 660  ? 0.3015 0.2281 0.2656 0.0330  -0.0591 -0.0503 658  ILE B CG1 
13538 C CG2 . ILE B 660  ? 0.3391 0.2552 0.3003 0.0442  -0.0643 -0.0559 658  ILE B CG2 
13539 C CD1 . ILE B 660  ? 0.3704 0.2847 0.3257 0.0282  -0.0637 -0.0483 658  ILE B CD1 
13540 N N   . ARG B 661  ? 0.2955 0.2319 0.2669 0.0559  -0.0558 -0.0643 659  ARG B N   
13541 C CA  . ARG B 661  ? 0.3410 0.2767 0.3129 0.0639  -0.0571 -0.0684 659  ARG B CA  
13542 C C   . ARG B 661  ? 0.3367 0.2873 0.3172 0.0678  -0.0519 -0.0702 659  ARG B C   
13543 O O   . ARG B 661  ? 0.3484 0.3033 0.3331 0.0731  -0.0519 -0.0721 659  ARG B O   
13544 C CB  . ARG B 661  ? 0.3293 0.2534 0.2923 0.0673  -0.0607 -0.0718 659  ARG B CB  
13545 C CG  . ARG B 661  ? 0.3647 0.2722 0.3188 0.0652  -0.0671 -0.0707 659  ARG B CG  
13546 C CD  . ARG B 661  ? 0.4202 0.3149 0.3646 0.0680  -0.0710 -0.0742 659  ARG B CD  
13547 N NE  . ARG B 661  ? 0.4235 0.3187 0.3679 0.0773  -0.0713 -0.0794 659  ARG B NE  
13548 C CZ  . ARG B 661  ? 0.4302 0.3271 0.3724 0.0810  -0.0697 -0.0831 659  ARG B CZ  
13549 N NH1 . ARG B 661  ? 0.3792 0.2772 0.3191 0.0762  -0.0679 -0.0822 659  ARG B NH1 
13550 N NH2 . ARG B 661  ? 0.4278 0.3254 0.3697 0.0899  -0.0701 -0.0879 659  ARG B NH2 
13551 N N   . GLU B 662  ? 0.2996 0.2584 0.2826 0.0652  -0.0477 -0.0696 660  GLU B N   
13552 C CA  . GLU B 662  ? 0.2852 0.2582 0.2762 0.0682  -0.0428 -0.0708 660  GLU B CA  
13553 C C   . GLU B 662  ? 0.2862 0.2687 0.2856 0.0655  -0.0402 -0.0678 660  GLU B C   
13554 O O   . GLU B 662  ? 0.3127 0.3049 0.3189 0.0689  -0.0380 -0.0688 660  GLU B O   
13555 C CB  . GLU B 662  ? 0.3228 0.3009 0.3132 0.0665  -0.0393 -0.0711 660  GLU B CB  
13556 C CG  . GLU B 662  ? 0.3158 0.3090 0.3144 0.0687  -0.0341 -0.0716 660  GLU B CG  
13557 C CD  . GLU B 662  ? 0.2984 0.2969 0.2964 0.0666  -0.0305 -0.0714 660  GLU B CD  
13558 O OE1 . GLU B 662  ? 0.3175 0.3126 0.3126 0.0611  -0.0307 -0.0689 660  GLU B OE1 
13559 O OE2 . GLU B 662  ? 0.3137 0.3202 0.3140 0.0707  -0.0277 -0.0737 660  GLU B OE2 
13560 N N   . ALA B 663  ? 0.2743 0.2547 0.2732 0.0593  -0.0404 -0.0641 661  ALA B N   
13561 C CA  . ALA B 663  ? 0.3028 0.2918 0.3089 0.0565  -0.0379 -0.0613 661  ALA B CA  
13562 C C   . ALA B 663  ? 0.2874 0.2713 0.2933 0.0560  -0.0411 -0.0600 661  ALA B C   
13563 O O   . ALA B 663  ? 0.2973 0.2878 0.3089 0.0544  -0.0396 -0.0582 661  ALA B O   
13564 C CB  . ALA B 663  ? 0.3084 0.3004 0.3150 0.0504  -0.0352 -0.0582 661  ALA B CB  
13565 N N   . GLY B 664  ? 0.3028 0.2750 0.3020 0.0573  -0.0458 -0.0607 662  GLY B N   
13566 C CA  . GLY B 664  ? 0.3313 0.2982 0.3294 0.0567  -0.0491 -0.0592 662  GLY B CA  
13567 C C   . GLY B 664  ? 0.3156 0.2808 0.3124 0.0501  -0.0490 -0.0551 662  GLY B C   
13568 O O   . GLY B 664  ? 0.3373 0.3029 0.3359 0.0492  -0.0501 -0.0535 662  GLY B O   
13569 N N   . LYS B 665  ? 0.2566 0.2203 0.2503 0.0455  -0.0479 -0.0534 663  LYS B N   
13570 C CA  . LYS B 665  ? 0.2878 0.2510 0.2802 0.0393  -0.0475 -0.0495 663  LYS B CA  
13571 C C   . LYS B 665  ? 0.2976 0.2487 0.2819 0.0366  -0.0521 -0.0479 663  LYS B C   
13572 O O   . LYS B 665  ? 0.2862 0.2284 0.2648 0.0382  -0.0553 -0.0496 663  LYS B O   
13573 C CB  . LYS B 665  ? 0.2837 0.2530 0.2776 0.0357  -0.0438 -0.0482 663  LYS B CB  
13574 C CG  . LYS B 665  ? 0.3878 0.3689 0.3895 0.0370  -0.0393 -0.0487 663  LYS B CG  
13575 C CD  . LYS B 665  ? 0.3555 0.3423 0.3587 0.0329  -0.0359 -0.0466 663  LYS B CD  
13576 C CE  . LYS B 665  ? 0.3630 0.3605 0.3738 0.0340  -0.0319 -0.0468 663  LYS B CE  
13577 N NZ  . LYS B 665  ? 0.3974 0.4000 0.4102 0.0299  -0.0291 -0.0440 663  LYS B NZ  
13578 N N   . SER B 666  ? 0.2988 0.2494 0.2824 0.0323  -0.0525 -0.0445 664  SER B N   
13579 C CA  . SER B 666  ? 0.3356 0.2760 0.3116 0.0282  -0.0563 -0.0420 664  SER B CA  
13580 C C   . SER B 666  ? 0.3269 0.2668 0.2999 0.0236  -0.0554 -0.0406 664  SER B C   
13581 O O   . SER B 666  ? 0.3385 0.2870 0.3158 0.0229  -0.0515 -0.0408 664  SER B O   
13582 C CB  . SER B 666  ? 0.4033 0.3448 0.3793 0.0248  -0.0565 -0.0386 664  SER B CB  
13583 O OG  . SER B 666  ? 0.3896 0.3404 0.3696 0.0212  -0.0522 -0.0365 664  SER B OG  
13584 N N   . ALA B 667  ? 0.2907 0.2202 0.2562 0.0202  -0.0595 -0.0390 665  ALA B N   
13585 C CA  . ALA B 667  ? 0.3520 0.2807 0.3144 0.0153  -0.0593 -0.0374 665  ALA B CA  
13586 C C   . ALA B 667  ? 0.3492 0.2887 0.3162 0.0109  -0.0550 -0.0343 665  ALA B C   
13587 O O   . ALA B 667  ? 0.3113 0.2565 0.2803 0.0095  -0.0524 -0.0343 665  ALA B O   
13588 C CB  . ALA B 667  ? 0.3927 0.3085 0.3463 0.0115  -0.0646 -0.0354 665  ALA B CB  
13589 N N   . LEU B 668  ? 0.3481 0.2905 0.3164 0.0089  -0.0544 -0.0316 666  LEU B N   
13590 C CA  . LEU B 668  ? 0.3562 0.3085 0.3283 0.0052  -0.0506 -0.0287 666  LEU B CA  
13591 C C   . LEU B 668  ? 0.3188 0.2816 0.2982 0.0083  -0.0459 -0.0307 666  LEU B C   
13592 O O   . LEU B 668  ? 0.3061 0.2758 0.2879 0.0060  -0.0430 -0.0295 666  LEU B O   
13593 C CB  . LEU B 668  ? 0.4089 0.3622 0.3808 0.0036  -0.0507 -0.0261 666  LEU B CB  
13594 C CG  . LEU B 668  ? 0.4591 0.4207 0.4328 -0.0009 -0.0477 -0.0227 666  LEU B CG  
13595 C CD1 . LEU B 668  ? 0.4438 0.4020 0.4124 -0.0068 -0.0498 -0.0196 666  LEU B CD1 
13596 C CD2 . LEU B 668  ? 0.5206 0.4841 0.4946 -0.0011 -0.0474 -0.0210 666  LEU B CD2 
13597 N N   . ASN B 669  ? 0.3292 0.2935 0.3124 0.0134  -0.0452 -0.0335 667  ASN B N   
13598 C CA  . ASN B 669  ? 0.2831 0.2569 0.2729 0.0160  -0.0410 -0.0351 667  ASN B CA  
13599 C C   . ASN B 669  ? 0.2704 0.2449 0.2601 0.0170  -0.0401 -0.0370 667  ASN B C   
13600 O O   . ASN B 669  ? 0.3064 0.2889 0.3003 0.0168  -0.0365 -0.0370 667  ASN B O   
13601 C CB  . ASN B 669  ? 0.3121 0.2878 0.3060 0.0208  -0.0408 -0.0374 667  ASN B CB  
13602 C CG  . ASN B 669  ? 0.3822 0.3591 0.3772 0.0198  -0.0409 -0.0356 667  ASN B CG  
13603 O OD1 . ASN B 669  ? 0.3929 0.3652 0.3865 0.0219  -0.0436 -0.0363 667  ASN B OD1 
13604 N ND2 . ASN B 669  ? 0.4431 0.4261 0.4401 0.0169  -0.0381 -0.0334 667  ASN B ND2 
13605 N N   . ALA B 670  ? 0.2413 0.2071 0.2257 0.0182  -0.0435 -0.0388 668  ALA B N   
13606 C CA  . ALA B 670  ? 0.2619 0.2277 0.2451 0.0190  -0.0430 -0.0407 668  ALA B CA  
13607 C C   . ALA B 670  ? 0.2967 0.2647 0.2783 0.0136  -0.0421 -0.0380 668  ALA B C   
13608 O O   . ALA B 670  ? 0.2459 0.2192 0.2294 0.0138  -0.0397 -0.0387 668  ALA B O   
13609 C CB  . ALA B 670  ? 0.2630 0.2179 0.2400 0.0216  -0.0472 -0.0433 668  ALA B CB  
13610 N N   . ILE B 671  ? 0.2251 0.1897 0.2033 0.0088  -0.0441 -0.0347 669  ILE B N   
13611 C CA  . ILE B 671  ? 0.2895 0.2579 0.2672 0.0036  -0.0431 -0.0318 669  ILE B CA  
13612 C C   . ILE B 671  ? 0.2613 0.2418 0.2459 0.0037  -0.0383 -0.0307 669  ILE B C   
13613 O O   . ILE B 671  ? 0.2432 0.2290 0.2293 0.0025  -0.0363 -0.0303 669  ILE B O   
13614 C CB  . ILE B 671  ? 0.2649 0.2285 0.2381 -0.0017 -0.0460 -0.0282 669  ILE B CB  
13615 C CG1 . ILE B 671  ? 0.2840 0.2347 0.2495 -0.0027 -0.0513 -0.0290 669  ILE B CG1 
13616 C CG2 . ILE B 671  ? 0.2795 0.2506 0.2541 -0.0070 -0.0441 -0.0247 669  ILE B CG2 
13617 C CD1 . ILE B 671  ? 0.3536 0.2974 0.3141 -0.0072 -0.0549 -0.0257 669  ILE B CD1 
13618 N N   . ALA B 672  ? 0.2256 0.2099 0.2140 0.0053  -0.0366 -0.0303 670  ALA B N   
13619 C CA  . ALA B 672  ? 0.2754 0.2698 0.2698 0.0058  -0.0323 -0.0295 670  ALA B CA  
13620 C C   . ALA B 672  ? 0.2416 0.2403 0.2395 0.0090  -0.0299 -0.0320 670  ALA B C   
13621 O O   . ALA B 672  ? 0.3102 0.3161 0.3113 0.0083  -0.0269 -0.0310 670  ALA B O   
13622 C CB  . ALA B 672  ? 0.2612 0.2572 0.2582 0.0075  -0.0316 -0.0294 670  ALA B CB  
13623 N N   . GLU B 673  ? 0.2499 0.2446 0.2471 0.0128  -0.0310 -0.0350 671  GLU B N   
13624 C CA  . GLU B 673  ? 0.2710 0.2702 0.2713 0.0159  -0.0286 -0.0373 671  GLU B CA  
13625 C C   . GLU B 673  ? 0.2397 0.2396 0.2376 0.0138  -0.0284 -0.0370 671  GLU B C   
13626 O O   . GLU B 673  ? 0.2663 0.2732 0.2675 0.0137  -0.0253 -0.0365 671  GLU B O   
13627 C CB  . GLU B 673  ? 0.2644 0.2593 0.2638 0.0204  -0.0302 -0.0407 671  GLU B CB  
13628 C CG  . GLU B 673  ? 0.3420 0.3418 0.3440 0.0236  -0.0278 -0.0431 671  GLU B CG  
13629 C CD  . GLU B 673  ? 0.3035 0.3095 0.3116 0.0269  -0.0255 -0.0442 671  GLU B CD  
13630 O OE1 . GLU B 673  ? 0.4265 0.4308 0.4359 0.0278  -0.0268 -0.0441 671  GLU B OE1 
13631 O OE2 . GLU B 673  ? 0.2520 0.2646 0.2636 0.0284  -0.0226 -0.0450 671  GLU B OE2 
13632 N N   . VAL B 674  ? 0.2275 0.2196 0.2193 0.0121  -0.0318 -0.0372 672  VAL B N   
13633 C CA  . VAL B 674  ? 0.2357 0.2278 0.2246 0.0099  -0.0321 -0.0370 672  VAL B CA  
13634 C C   . VAL B 674  ? 0.2086 0.2075 0.1998 0.0056  -0.0303 -0.0335 672  VAL B C   
13635 O O   . VAL B 674  ? 0.2232 0.2271 0.2155 0.0050  -0.0285 -0.0332 672  VAL B O   
13636 C CB  . VAL B 674  ? 0.2515 0.2326 0.2328 0.0084  -0.0368 -0.0379 672  VAL B CB  
13637 C CG1 . VAL B 674  ? 0.2613 0.2421 0.2393 0.0061  -0.0375 -0.0380 672  VAL B CG1 
13638 C CG2 . VAL B 674  ? 0.3062 0.2807 0.2853 0.0133  -0.0387 -0.0416 672  VAL B CG2 
13639 N N   . ARG B 675  ? 0.2167 0.2160 0.2083 0.0028  -0.0308 -0.0307 673  ARG B N   
13640 C CA  . ARG B 675  ? 0.2648 0.2715 0.2588 -0.0006 -0.0289 -0.0275 673  ARG B CA  
13641 C C   . ARG B 675  ? 0.2401 0.2556 0.2401 0.0018  -0.0247 -0.0276 673  ARG B C   
13642 O O   . ARG B 675  ? 0.2037 0.2252 0.2054 0.0003  -0.0231 -0.0261 673  ARG B O   
13643 C CB  . ARG B 675  ? 0.2359 0.2424 0.2294 -0.0034 -0.0298 -0.0247 673  ARG B CB  
13644 C CG  . ARG B 675  ? 0.2546 0.2538 0.2423 -0.0077 -0.0338 -0.0231 673  ARG B CG  
13645 C CD  . ARG B 675  ? 0.2493 0.2514 0.2373 -0.0109 -0.0337 -0.0197 673  ARG B CD  
13646 N NE  . ARG B 675  ? 0.2685 0.2807 0.2601 -0.0130 -0.0309 -0.0171 673  ARG B NE  
13647 C CZ  . ARG B 675  ? 0.2763 0.2944 0.2699 -0.0142 -0.0291 -0.0147 673  ARG B CZ  
13648 N NH1 . ARG B 675  ? 0.2582 0.2733 0.2507 -0.0136 -0.0297 -0.0144 673  ARG B NH1 
13649 N NH2 . ARG B 675  ? 0.2827 0.3101 0.2795 -0.0156 -0.0267 -0.0126 673  ARG B NH2 
13650 N N   . GLU B 676  ? 0.2155 0.2318 0.2186 0.0053  -0.0233 -0.0291 674  GLU B N   
13651 C CA  . GLU B 676  ? 0.2434 0.2670 0.2518 0.0074  -0.0197 -0.0292 674  GLU B CA  
13652 C C   . GLU B 676  ? 0.2302 0.2561 0.2389 0.0087  -0.0184 -0.0305 674  GLU B C   
13653 O O   . GLU B 676  ? 0.2064 0.2385 0.2179 0.0083  -0.0160 -0.0292 674  GLU B O   
13654 C CB  . GLU B 676  ? 0.2367 0.2603 0.2483 0.0106  -0.0189 -0.0307 674  GLU B CB  
13655 C CG  . GLU B 676  ? 0.2812 0.3116 0.2979 0.0122  -0.0155 -0.0304 674  GLU B CG  
13656 C CD  . GLU B 676  ? 0.4318 0.4625 0.4517 0.0144  -0.0150 -0.0313 674  GLU B CD  
13657 O OE1 . GLU B 676  ? 0.4099 0.4362 0.4287 0.0157  -0.0169 -0.0328 674  GLU B OE1 
13658 O OE2 . GLU B 676  ? 0.4944 0.5296 0.5178 0.0147  -0.0128 -0.0304 674  GLU B OE2 
13659 N N   . ALA B 677  ? 0.2194 0.2404 0.2251 0.0102  -0.0201 -0.0330 675  ALA B N   
13660 C CA  . ALA B 677  ? 0.2446 0.2676 0.2496 0.0113  -0.0190 -0.0343 675  ALA B CA  
13661 C C   . ALA B 677  ? 0.2225 0.2475 0.2256 0.0078  -0.0193 -0.0322 675  ALA B C   
13662 O O   . ALA B 677  ? 0.2247 0.2552 0.2296 0.0080  -0.0171 -0.0316 675  ALA B O   
13663 C CB  . ALA B 677  ? 0.2124 0.2291 0.2134 0.0138  -0.0210 -0.0376 675  ALA B CB  
13664 N N   . ILE B 678  ? 0.2495 0.2701 0.2488 0.0045  -0.0223 -0.0310 676  ILE B N   
13665 C CA  . ILE B 678  ? 0.1913 0.2146 0.1892 0.0006  -0.0230 -0.0286 676  ILE B CA  
13666 C C   . ILE B 678  ? 0.2026 0.2347 0.2055 -0.0001 -0.0200 -0.0259 676  ILE B C   
13667 O O   . ILE B 678  ? 0.2344 0.2715 0.2382 -0.0011 -0.0190 -0.0247 676  ILE B O   
13668 C CB  . ILE B 678  ? 0.2080 0.2253 0.2014 -0.0034 -0.0267 -0.0273 676  ILE B CB  
13669 C CG1 . ILE B 678  ? 0.2354 0.2430 0.2227 -0.0028 -0.0302 -0.0300 676  ILE B CG1 
13670 C CG2 . ILE B 678  ? 0.2004 0.2227 0.1938 -0.0079 -0.0271 -0.0240 676  ILE B CG2 
13671 C CD1 . ILE B 678  ? 0.2524 0.2521 0.2355 -0.0056 -0.0339 -0.0292 676  ILE B CD1 
13672 N N   . ASP B 679  ? 0.2310 0.2648 0.2370 0.0006  -0.0188 -0.0250 677  ASP B N   
13673 C CA  . ASP B 679  ? 0.2264 0.2678 0.2366 0.0004  -0.0162 -0.0227 677  ASP B CA  
13674 C C   . ASP B 679  ? 0.1890 0.2348 0.2026 0.0033  -0.0134 -0.0234 677  ASP B C   
13675 O O   . ASP B 679  ? 0.2186 0.2702 0.2342 0.0028  -0.0119 -0.0216 677  ASP B O   
13676 C CB  . ASP B 679  ? 0.2045 0.2461 0.2166 0.0010  -0.0157 -0.0220 677  ASP B CB  
13677 C CG  . ASP B 679  ? 0.2703 0.3093 0.2794 -0.0025 -0.0181 -0.0202 677  ASP B CG  
13678 O OD1 . ASP B 679  ? 0.2756 0.3153 0.2825 -0.0059 -0.0196 -0.0186 677  ASP B OD1 
13679 O OD2 . ASP B 679  ? 0.2951 0.3315 0.3039 -0.0020 -0.0185 -0.0203 677  ASP B OD2 
13680 N N   . PHE B 680  ? 0.1788 0.2224 0.1932 0.0062  -0.0126 -0.0258 678  PHE B N   
13681 C CA  . PHE B 680  ? 0.2012 0.2487 0.2183 0.0084  -0.0101 -0.0262 678  PHE B CA  
13682 C C   . PHE B 680  ? 0.1859 0.2354 0.2010 0.0074  -0.0102 -0.0258 678  PHE B C   
13683 O O   . PHE B 680  ? 0.1631 0.2177 0.1803 0.0075  -0.0084 -0.0243 678  PHE B O   
13684 C CB  . PHE B 680  ? 0.1792 0.2244 0.1969 0.0113  -0.0097 -0.0289 678  PHE B CB  
13685 C CG  . PHE B 680  ? 0.1805 0.2261 0.2019 0.0129  -0.0087 -0.0292 678  PHE B CG  
13686 C CD1 . PHE B 680  ? 0.1687 0.2185 0.1936 0.0130  -0.0067 -0.0275 678  PHE B CD1 
13687 C CD2 . PHE B 680  ? 0.2108 0.2525 0.2319 0.0144  -0.0099 -0.0312 678  PHE B CD2 
13688 C CE1 . PHE B 680  ? 0.1849 0.2346 0.2127 0.0143  -0.0061 -0.0278 678  PHE B CE1 
13689 C CE2 . PHE B 680  ? 0.2336 0.2758 0.2580 0.0157  -0.0092 -0.0314 678  PHE B CE2 
13690 C CZ  . PHE B 680  ? 0.1983 0.2445 0.2260 0.0155  -0.0074 -0.0297 678  PHE B CZ  
13691 N N   . LEU B 681  ? 0.2042 0.2493 0.2148 0.0064  -0.0124 -0.0272 679  LEU B N   
13692 C CA  . LEU B 681  ? 0.1676 0.2139 0.1755 0.0054  -0.0129 -0.0271 679  LEU B CA  
13693 C C   . LEU B 681  ? 0.2137 0.2650 0.2227 0.0027  -0.0129 -0.0240 679  LEU B C   
13694 O O   . LEU B 681  ? 0.2199 0.2757 0.2298 0.0029  -0.0116 -0.0230 679  LEU B O   
13695 C CB  . LEU B 681  ? 0.2339 0.2732 0.2361 0.0045  -0.0160 -0.0292 679  LEU B CB  
13696 C CG  . LEU B 681  ? 0.2419 0.2769 0.2424 0.0080  -0.0160 -0.0327 679  LEU B CG  
13697 C CD1 . LEU B 681  ? 0.2017 0.2280 0.1962 0.0074  -0.0198 -0.0348 679  LEU B CD1 
13698 C CD2 . LEU B 681  ? 0.1704 0.2093 0.1710 0.0101  -0.0138 -0.0337 679  LEU B CD2 
13699 N N   . ARG B 682  ? 0.1608 0.2116 0.1695 0.0001  -0.0145 -0.0224 680  ARG B N   
13700 C CA  . ARG B 682  ? 0.2152 0.2717 0.2252 -0.0025 -0.0147 -0.0194 680  ARG B CA  
13701 C C   . ARG B 682  ? 0.1978 0.2608 0.2127 -0.0006 -0.0118 -0.0177 680  ARG B C   
13702 O O   . ARG B 682  ? 0.1787 0.2475 0.1951 -0.0013 -0.0113 -0.0157 680  ARG B O   
13703 C CB  . ARG B 682  ? 0.1699 0.2248 0.1783 -0.0060 -0.0171 -0.0179 680  ARG B CB  
13704 C CG  . ARG B 682  ? 0.2170 0.2654 0.2199 -0.0088 -0.0206 -0.0190 680  ARG B CG  
13705 C CD  . ARG B 682  ? 0.2055 0.2514 0.2066 -0.0126 -0.0231 -0.0173 680  ARG B CD  
13706 N NE  . ARG B 682  ? 0.2342 0.2731 0.2295 -0.0156 -0.0270 -0.0181 680  ARG B NE  
13707 C CZ  . ARG B 682  ? 0.2560 0.2894 0.2481 -0.0189 -0.0299 -0.0173 680  ARG B CZ  
13708 N NH1 . ARG B 682  ? 0.2625 0.2971 0.2565 -0.0196 -0.0293 -0.0157 680  ARG B NH1 
13709 N NH2 . ARG B 682  ? 0.2778 0.3039 0.2642 -0.0216 -0.0338 -0.0182 680  ARG B NH2 
13710 N N   . TYR B 683  ? 0.1871 0.2490 0.2044 0.0017  -0.0102 -0.0185 681  TYR B N   
13711 C CA  . TYR B 683  ? 0.2035 0.2704 0.2248 0.0036  -0.0079 -0.0171 681  TYR B CA  
13712 C C   . TYR B 683  ? 0.1657 0.2349 0.1883 0.0056  -0.0061 -0.0172 681  TYR B C   
13713 O O   . TYR B 683  ? 0.2028 0.2768 0.2272 0.0061  -0.0052 -0.0153 681  TYR B O   
13714 C CB  . TYR B 683  ? 0.1664 0.2308 0.1894 0.0054  -0.0071 -0.0181 681  TYR B CB  
13715 C CG  . TYR B 683  ? 0.1950 0.2628 0.2214 0.0076  -0.0049 -0.0172 681  TYR B CG  
13716 C CD1 . TYR B 683  ? 0.1979 0.2700 0.2257 0.0075  -0.0045 -0.0153 681  TYR B CD1 
13717 C CD2 . TYR B 683  ? 0.1670 0.2339 0.1952 0.0100  -0.0034 -0.0182 681  TYR B CD2 
13718 C CE1 . TYR B 683  ? 0.1802 0.2547 0.2105 0.0100  -0.0027 -0.0147 681  TYR B CE1 
13719 C CE2 . TYR B 683  ? 0.1841 0.2529 0.2149 0.0118  -0.0019 -0.0174 681  TYR B CE2 
13720 C CZ  . TYR B 683  ? 0.1715 0.2436 0.2030 0.0120  -0.0016 -0.0158 681  TYR B CZ  
13721 O OH  . TYR B 683  ? 0.2029 0.2763 0.2364 0.0144  -0.0004 -0.0152 681  TYR B OH  
13722 N N   . TYR B 684  ? 0.1497 0.2156 0.1713 0.0068  -0.0058 -0.0193 682  TYR B N   
13723 C CA  . TYR B 684  ? 0.1975 0.2657 0.2199 0.0083  -0.0041 -0.0191 682  TYR B CA  
13724 C C   . TYR B 684  ? 0.1976 0.2683 0.2177 0.0068  -0.0049 -0.0179 682  TYR B C   
13725 O O   . TYR B 684  ? 0.2100 0.2841 0.2310 0.0076  -0.0038 -0.0166 682  TYR B O   
13726 C CB  . TYR B 684  ? 0.1797 0.2450 0.2015 0.0099  -0.0034 -0.0215 682  TYR B CB  
13727 C CG  . TYR B 684  ? 0.1535 0.2170 0.1782 0.0114  -0.0025 -0.0224 682  TYR B CG  
13728 C CD1 . TYR B 684  ? 0.1695 0.2349 0.1974 0.0121  -0.0013 -0.0210 682  TYR B CD1 
13729 C CD2 . TYR B 684  ? 0.1670 0.2269 0.1909 0.0123  -0.0031 -0.0249 682  TYR B CD2 
13730 C CE1 . TYR B 684  ? 0.1987 0.2622 0.2288 0.0133  -0.0009 -0.0219 682  TYR B CE1 
13731 C CE2 . TYR B 684  ? 0.1865 0.2453 0.2132 0.0136  -0.0026 -0.0257 682  TYR B CE2 
13732 C CZ  . TYR B 684  ? 0.1910 0.2516 0.2207 0.0139  -0.0015 -0.0241 682  TYR B CZ  
13733 O OH  . TYR B 684  ? 0.1871 0.2463 0.2193 0.0149  -0.0013 -0.0249 682  TYR B OH  
13734 N N   . ALA B 685  ? 0.1600 0.2289 0.1769 0.0046  -0.0073 -0.0184 683  ALA B N   
13735 C CA  . ALA B 685  ? 0.2065 0.2781 0.2213 0.0027  -0.0085 -0.0171 683  ALA B CA  
13736 C C   . ALA B 685  ? 0.2139 0.2918 0.2317 0.0022  -0.0082 -0.0141 683  ALA B C   
13737 O O   . ALA B 685  ? 0.2050 0.2868 0.2231 0.0025  -0.0077 -0.0126 683  ALA B O   
13738 C CB  . ALA B 685  ? 0.2029 0.2704 0.2134 -0.0001 -0.0116 -0.0181 683  ALA B CB  
13739 N N   . GLU B 686  ? 0.1739 0.2530 0.1938 0.0015  -0.0083 -0.0131 684  GLU B N   
13740 C CA  . GLU B 686  ? 0.2189 0.3047 0.2418 0.0016  -0.0078 -0.0104 684  GLU B CA  
13741 C C   . GLU B 686  ? 0.2295 0.3174 0.2553 0.0050  -0.0054 -0.0098 684  GLU B C   
13742 O O   . GLU B 686  ? 0.2064 0.2991 0.2335 0.0058  -0.0051 -0.0079 684  GLU B O   
13743 C CB  . GLU B 686  ? 0.2312 0.3182 0.2553 0.0003  -0.0083 -0.0097 684  GLU B CB  
13744 C CG  . GLU B 686  ? 0.2540 0.3487 0.2815 0.0012  -0.0072 -0.0072 684  GLU B CG  
13745 C CD  . GLU B 686  ? 0.3363 0.4375 0.3641 -0.0005 -0.0084 -0.0050 684  GLU B CD  
13746 O OE1 . GLU B 686  ? 0.3144 0.4140 0.3394 -0.0035 -0.0106 -0.0052 684  GLU B OE1 
13747 O OE2 . GLU B 686  ? 0.3474 0.4553 0.3783 0.0013  -0.0074 -0.0031 684  GLU B OE2 
13748 N N   . GLN B 687  ? 0.1767 0.2606 0.2033 0.0071  -0.0040 -0.0114 685  GLN B N   
13749 C CA  . GLN B 687  ? 0.1888 0.2735 0.2177 0.0099  -0.0022 -0.0107 685  GLN B CA  
13750 C C   . GLN B 687  ? 0.2587 0.3445 0.2865 0.0103  -0.0018 -0.0100 685  GLN B C   
13751 O O   . GLN B 687  ? 0.2132 0.3013 0.2424 0.0120  -0.0011 -0.0083 685  GLN B O   
13752 C CB  . GLN B 687  ? 0.2151 0.2953 0.2449 0.0113  -0.0011 -0.0125 685  GLN B CB  
13753 C CG  . GLN B 687  ? 0.1986 0.2780 0.2295 0.0114  -0.0013 -0.0129 685  GLN B CG  
13754 C CD  . GLN B 687  ? 0.2261 0.3097 0.2589 0.0129  -0.0007 -0.0111 685  GLN B CD  
13755 O OE1 . GLN B 687  ? 0.2392 0.3232 0.2733 0.0152  0.0003  -0.0105 685  GLN B OE1 
13756 N NE2 . GLN B 687  ? 0.2811 0.3680 0.3138 0.0115  -0.0015 -0.0103 685  GLN B NE2 
13757 N N   . THR B 688  ? 0.2016 0.2853 0.2265 0.0089  -0.0025 -0.0112 686  THR B N   
13758 C CA  . THR B 688  ? 0.2191 0.3042 0.2421 0.0089  -0.0024 -0.0105 686  THR B CA  
13759 C C   . THR B 688  ? 0.2188 0.3089 0.2417 0.0081  -0.0037 -0.0082 686  THR B C   
13760 O O   . THR B 688  ? 0.2325 0.3252 0.2559 0.0093  -0.0032 -0.0064 686  THR B O   
13761 C CB  . THR B 688  ? 0.1745 0.2565 0.1938 0.0078  -0.0030 -0.0127 686  THR B CB  
13762 O OG1 . THR B 688  ? 0.2249 0.3035 0.2448 0.0091  -0.0016 -0.0147 686  THR B OG1 
13763 C CG2 . THR B 688  ? 0.1883 0.2720 0.2047 0.0076  -0.0031 -0.0120 686  THR B CG2 
13764 N N   . ARG B 689  ? 0.1926 0.2843 0.2148 0.0058  -0.0055 -0.0081 687  ARG B N   
13765 C CA  . ARG B 689  ? 0.2337 0.3313 0.2564 0.0047  -0.0069 -0.0058 687  ARG B CA  
13766 C C   . ARG B 689  ? 0.2472 0.3494 0.2737 0.0072  -0.0058 -0.0036 687  ARG B C   
13767 O O   . ARG B 689  ? 0.2352 0.3425 0.2624 0.0077  -0.0064 -0.0016 687  ARG B O   
13768 C CB  . ARG B 689  ? 0.2243 0.3230 0.2460 0.0013  -0.0092 -0.0057 687  ARG B CB  
13769 C CG  . ARG B 689  ? 0.2453 0.3399 0.2623 -0.0014 -0.0112 -0.0074 687  ARG B CG  
13770 C CD  . ARG B 689  ? 0.2778 0.3735 0.2940 -0.0053 -0.0139 -0.0067 687  ARG B CD  
13771 N NE  . ARG B 689  ? 0.2763 0.3702 0.2939 -0.0057 -0.0136 -0.0071 687  ARG B NE  
13772 C CZ  . ARG B 689  ? 0.2906 0.3775 0.3054 -0.0068 -0.0145 -0.0093 687  ARG B CZ  
13773 N NH1 . ARG B 689  ? 0.2941 0.3752 0.3045 -0.0072 -0.0157 -0.0116 687  ARG B NH1 
13774 N NH2 . ARG B 689  ? 0.2606 0.3463 0.2768 -0.0073 -0.0143 -0.0093 687  ARG B NH2 
13775 N N   . ARG B 690  ? 0.1990 0.2995 0.2278 0.0091  -0.0043 -0.0042 688  ARG B N   
13776 C CA  . ARG B 690  ? 0.2070 0.3110 0.2388 0.0121  -0.0033 -0.0026 688  ARG B CA  
13777 C C   . ARG B 690  ? 0.2133 0.3151 0.2452 0.0148  -0.0022 -0.0021 688  ARG B C   
13778 O O   . ARG B 690  ? 0.2379 0.3423 0.2716 0.0175  -0.0019 -0.0005 688  ARG B O   
13779 C CB  . ARG B 690  ? 0.2014 0.3041 0.2351 0.0131  -0.0024 -0.0036 688  ARG B CB  
13780 C CG  . ARG B 690  ? 0.2504 0.3559 0.2842 0.0105  -0.0034 -0.0035 688  ARG B CG  
13781 C CD  . ARG B 690  ? 0.2720 0.3862 0.3081 0.0108  -0.0039 -0.0012 688  ARG B CD  
13782 N NE  . ARG B 690  ? 0.3019 0.4183 0.3404 0.0150  -0.0023 -0.0006 688  ARG B NE  
13783 C CZ  . ARG B 690  ? 0.3315 0.4513 0.3713 0.0179  -0.0022 0.0008  688  ARG B CZ  
13784 N NH1 . ARG B 690  ? 0.3063 0.4284 0.3454 0.0170  -0.0033 0.0021  688  ARG B NH1 
13785 N NH2 . ARG B 690  ? 0.2391 0.3594 0.2805 0.0220  -0.0010 0.0009  688  ARG B NH2 
13786 N N   . THR B 691  ? 0.2294 0.3263 0.2592 0.0143  -0.0016 -0.0032 689  THR B N   
13787 C CA  . THR B 691  ? 0.2294 0.3236 0.2596 0.0165  -0.0004 -0.0025 689  THR B CA  
13788 C C   . THR B 691  ? 0.2874 0.3806 0.3150 0.0158  -0.0003 -0.0018 689  THR B C   
13789 O O   . THR B 691  ? 0.2992 0.3923 0.3268 0.0174  -0.0001 0.0001  689  THR B O   
13790 C CB  . THR B 691  ? 0.2694 0.3586 0.3006 0.0171  0.0008  -0.0043 689  THR B CB  
13791 O OG1 . THR B 691  ? 0.2385 0.3253 0.2683 0.0150  0.0009  -0.0064 689  THR B OG1 
13792 C CG2 . THR B 691  ? 0.2384 0.3283 0.2718 0.0184  0.0008  -0.0048 689  THR B CG2 
13793 N N   . LEU B 692  ? 0.2297 0.3219 0.2549 0.0137  -0.0005 -0.0033 690  LEU B N   
13794 C CA  . LEU B 692  ? 0.2391 0.3296 0.2618 0.0134  0.0004  -0.0031 690  LEU B CA  
13795 C C   . LEU B 692  ? 0.2549 0.3486 0.2752 0.0131  -0.0007 -0.0011 690  LEU B C   
13796 O O   . LEU B 692  ? 0.2788 0.3753 0.2979 0.0118  -0.0023 -0.0010 690  LEU B O   
13797 C CB  . LEU B 692  ? 0.2421 0.3302 0.2629 0.0120  0.0009  -0.0058 690  LEU B CB  
13798 C CG  . LEU B 692  ? 0.2453 0.3301 0.2684 0.0126  0.0021  -0.0076 690  LEU B CG  
13799 C CD1 . LEU B 692  ? 0.2778 0.3609 0.2989 0.0119  0.0027  -0.0101 690  LEU B CD1 
13800 C CD2 . LEU B 692  ? 0.2931 0.3766 0.3183 0.0140  0.0034  -0.0061 690  LEU B CD2 
13801 N N   . GLY B 693  ? 0.2618 0.3547 0.2813 0.0140  0.0001  0.0008  691  GLY B N   
13802 C CA  . GLY B 693  ? 0.2667 0.3621 0.2835 0.0139  -0.0009 0.0030  691  GLY B CA  
13803 C C   . GLY B 693  ? 0.3377 0.4314 0.3513 0.0132  0.0004  0.0034  691  GLY B C   
13804 O O   . GLY B 693  ? 0.3223 0.4135 0.3362 0.0128  0.0021  0.0020  691  GLY B O   
13805 N N   . PRO B 694  ? 0.4070 0.5026 0.4175 0.0130  -0.0004 0.0055  692  PRO B N   
13806 C CA  . PRO B 694  ? 0.3760 0.4708 0.3830 0.0121  0.0009  0.0061  692  PRO B CA  
13807 C C   . PRO B 694  ? 0.4300 0.5217 0.4385 0.0126  0.0027  0.0076  692  PRO B C   
13808 O O   . PRO B 694  ? 0.4987 0.5900 0.5055 0.0115  0.0045  0.0073  692  PRO B O   
13809 C CB  . PRO B 694  ? 0.4070 0.5042 0.4106 0.0121  -0.0008 0.0087  692  PRO B CB  
13810 C CG  . PRO B 694  ? 0.4213 0.5215 0.4264 0.0122  -0.0031 0.0083  692  PRO B CG  
13811 C CD  . PRO B 694  ? 0.4055 0.5048 0.4156 0.0134  -0.0027 0.0073  692  PRO B CD  
13812 N N   . GLY B 695  ? 0.3771 0.4669 0.3887 0.0142  0.0021  0.0091  693  GLY B N   
13813 C CA  . GLY B 695  ? 0.3510 0.4371 0.3638 0.0143  0.0033  0.0105  693  GLY B CA  
13814 C C   . GLY B 695  ? 0.3949 0.4790 0.4106 0.0138  0.0048  0.0081  693  GLY B C   
13815 O O   . GLY B 695  ? 0.3522 0.4332 0.3690 0.0134  0.0056  0.0093  693  GLY B O   
13816 N N   . HIS B 696  ? 0.3508 0.4363 0.3677 0.0136  0.0049  0.0050  694  HIS B N   
13817 C CA  . HIS B 696  ? 0.3448 0.4285 0.3644 0.0133  0.0061  0.0026  694  HIS B CA  
13818 C C   . HIS B 696  ? 0.3576 0.4430 0.3754 0.0119  0.0076  0.0009  694  HIS B C   
13819 O O   . HIS B 696  ? 0.3557 0.4421 0.3729 0.0118  0.0075  -0.0019 694  HIS B O   
13820 C CB  . HIS B 696  ? 0.2936 0.3772 0.3155 0.0142  0.0050  0.0005  694  HIS B CB  
13821 C CG  . HIS B 696  ? 0.3004 0.3836 0.3238 0.0161  0.0037  0.0021  694  HIS B CG  
13822 N ND1 . HIS B 696  ? 0.2739 0.3603 0.2971 0.0167  0.0023  0.0024  694  HIS B ND1 
13823 C CD2 . HIS B 696  ? 0.2892 0.3693 0.3141 0.0176  0.0035  0.0036  694  HIS B CD2 
13824 C CE1 . HIS B 696  ? 0.2934 0.3795 0.3183 0.0189  0.0015  0.0038  694  HIS B CE1 
13825 N NE2 . HIS B 696  ? 0.3035 0.3852 0.3291 0.0197  0.0022  0.0044  694  HIS B NE2 
13826 N N   . GLY B 697  ? 0.3723 0.4580 0.3891 0.0109  0.0090  0.0027  695  GLY B N   
13827 C CA  . GLY B 697  ? 0.3544 0.4429 0.3690 0.0099  0.0108  0.0015  695  GLY B CA  
13828 C C   . GLY B 697  ? 0.2822 0.3709 0.2997 0.0100  0.0120  -0.0015 695  GLY B C   
13829 O O   . GLY B 697  ? 0.2840 0.3705 0.3052 0.0101  0.0120  -0.0017 695  GLY B O   
13830 N N   . PRO B 698  ? 0.3018 0.3930 0.3171 0.0102  0.0129  -0.0041 696  PRO B N   
13831 C CA  . PRO B 698  ? 0.2909 0.3824 0.3088 0.0107  0.0138  -0.0071 696  PRO B CA  
13832 C C   . PRO B 698  ? 0.2785 0.3724 0.2988 0.0098  0.0160  -0.0059 696  PRO B C   
13833 O O   . PRO B 698  ? 0.2890 0.3849 0.3080 0.0085  0.0171  -0.0030 696  PRO B O   
13834 C CB  . PRO B 698  ? 0.3196 0.4127 0.3334 0.0116  0.0139  -0.0100 696  PRO B CB  
13835 C CG  . PRO B 698  ? 0.3946 0.4875 0.4041 0.0112  0.0124  -0.0087 696  PRO B CG  
13836 C CD  . PRO B 698  ? 0.3237 0.4169 0.3339 0.0102  0.0126  -0.0046 696  PRO B CD  
13837 N N   . LEU B 699  ? 0.2720 0.3658 0.2961 0.0102  0.0164  -0.0079 697  LEU B N   
13838 C CA  . LEU B 699  ? 0.2854 0.3827 0.3125 0.0091  0.0185  -0.0071 697  LEU B CA  
13839 C C   . LEU B 699  ? 0.2766 0.3797 0.3013 0.0096  0.0207  -0.0082 697  LEU B C   
13840 O O   . LEU B 699  ? 0.2628 0.3701 0.2878 0.0080  0.0227  -0.0059 697  LEU B O   
13841 C CB  . LEU B 699  ? 0.2721 0.3681 0.3039 0.0097  0.0180  -0.0091 697  LEU B CB  
13842 C CG  . LEU B 699  ? 0.2737 0.3643 0.3079 0.0095  0.0160  -0.0084 697  LEU B CG  
13843 C CD1 . LEU B 699  ? 0.2989 0.3889 0.3372 0.0100  0.0157  -0.0106 697  LEU B CD1 
13844 C CD2 . LEU B 699  ? 0.3323 0.4212 0.3669 0.0076  0.0160  -0.0045 697  LEU B CD2 
13845 N N   . GLY B 700  ? 0.2419 0.3451 0.2641 0.0117  0.0203  -0.0118 698  GLY B N   
13846 C CA  . GLY B 700  ? 0.2551 0.3634 0.2751 0.0131  0.0223  -0.0139 698  GLY B CA  
13847 C C   . GLY B 700  ? 0.2731 0.3809 0.2948 0.0155  0.0219  -0.0181 698  GLY B C   
13848 O O   . GLY B 700  ? 0.2237 0.3264 0.2467 0.0161  0.0197  -0.0195 698  GLY B O   
13849 N N   . PRO B 701  ? 0.2650 0.3782 0.2866 0.0172  0.0240  -0.0201 699  PRO B N   
13850 C CA  . PRO B 701  ? 0.2597 0.3722 0.2826 0.0202  0.0234  -0.0243 699  PRO B CA  
13851 C C   . PRO B 701  ? 0.2453 0.3560 0.2744 0.0196  0.0223  -0.0242 699  PRO B C   
13852 O O   . PRO B 701  ? 0.2269 0.3411 0.2606 0.0177  0.0236  -0.0217 699  PRO B O   
13853 C CB  . PRO B 701  ? 0.2657 0.3864 0.2885 0.0220  0.0264  -0.0256 699  PRO B CB  
13854 C CG  . PRO B 701  ? 0.2526 0.3764 0.2709 0.0204  0.0280  -0.0231 699  PRO B CG  
13855 C CD  . PRO B 701  ? 0.2773 0.3979 0.2974 0.0168  0.0270  -0.0187 699  PRO B CD  
13856 N N   . ILE B 702  ? 0.2389 0.3437 0.2677 0.0210  0.0199  -0.0267 700  ILE B N   
13857 C CA  A ILE B 702  ? 0.2057 0.3081 0.2396 0.0207  0.0186  -0.0268 700  ILE B CA  
13858 C CA  B ILE B 702  ? 0.2061 0.3084 0.2399 0.0207  0.0185  -0.0268 700  ILE B CA  
13859 C C   . ILE B 702  ? 0.2273 0.3304 0.2623 0.0238  0.0182  -0.0306 700  ILE B C   
13860 O O   . ILE B 702  ? 0.2464 0.3462 0.2770 0.0262  0.0169  -0.0336 700  ILE B O   
13861 C CB  A ILE B 702  ? 0.2126 0.3078 0.2455 0.0195  0.0159  -0.0260 700  ILE B CB  
13862 C CB  B ILE B 702  ? 0.2126 0.3076 0.2454 0.0196  0.0158  -0.0261 700  ILE B CB  
13863 C CG1 A ILE B 702  ? 0.2372 0.3321 0.2702 0.0169  0.0162  -0.0221 700  ILE B CG1 
13864 C CG1 B ILE B 702  ? 0.2390 0.3334 0.2709 0.0171  0.0160  -0.0224 700  ILE B CG1 
13865 C CG2 A ILE B 702  ? 0.2087 0.3009 0.2455 0.0200  0.0143  -0.0271 700  ILE B CG2 
13866 C CG2 B ILE B 702  ? 0.2079 0.3003 0.2452 0.0196  0.0145  -0.0267 700  ILE B CG2 
13867 C CD1 A ILE B 702  ? 0.1918 0.2811 0.2249 0.0160  0.0140  -0.0212 700  ILE B CD1 
13868 C CD1 B ILE B 702  ? 0.2220 0.3193 0.2581 0.0150  0.0174  -0.0193 700  ILE B CD1 
13869 N N   . VAL B 703  ? 0.2074 0.3145 0.2480 0.0239  0.0190  -0.0304 701  VAL B N   
13870 C CA  . VAL B 703  ? 0.1938 0.3017 0.2365 0.0270  0.0183  -0.0338 701  VAL B CA  
13871 C C   . VAL B 703  ? 0.2261 0.3268 0.2699 0.0267  0.0154  -0.0343 701  VAL B C   
13872 O O   . VAL B 703  ? 0.2154 0.3150 0.2628 0.0242  0.0149  -0.0320 701  VAL B O   
13873 C CB  . VAL B 703  ? 0.2670 0.3838 0.3155 0.0270  0.0206  -0.0331 701  VAL B CB  
13874 C CG1 . VAL B 703  ? 0.1887 0.3061 0.2404 0.0301  0.0194  -0.0362 701  VAL B CG1 
13875 C CG2 . VAL B 703  ? 0.2193 0.3441 0.2661 0.0278  0.0237  -0.0329 701  VAL B CG2 
13876 N N   . CYS B 704  ? 0.1986 0.2940 0.2391 0.0292  0.0132  -0.0374 702  CYS B N   
13877 C CA  . CYS B 704  ? 0.2022 0.2907 0.2430 0.0290  0.0103  -0.0380 702  CYS B CA  
13878 C C   . CYS B 704  ? 0.1898 0.2786 0.2327 0.0322  0.0093  -0.0409 702  CYS B C   
13879 O O   . CYS B 704  ? 0.1924 0.2803 0.2320 0.0354  0.0088  -0.0439 702  CYS B O   
13880 C CB  . CYS B 704  ? 0.1951 0.2763 0.2298 0.0286  0.0082  -0.0386 702  CYS B CB  
13881 S SG  . CYS B 704  ? 0.2349 0.3153 0.2673 0.0251  0.0087  -0.0351 702  CYS B SG  
13882 N N   . ILE B 705  ? 0.1933 0.2833 0.2414 0.0314  0.0088  -0.0401 703  ILE B N   
13883 C CA  . ILE B 705  ? 0.1985 0.2897 0.2495 0.0344  0.0077  -0.0425 703  ILE B CA  
13884 C C   . ILE B 705  ? 0.2101 0.2934 0.2603 0.0339  0.0045  -0.0428 703  ILE B C   
13885 O O   . ILE B 705  ? 0.2154 0.2969 0.2674 0.0310  0.0041  -0.0405 703  ILE B O   
13886 C CB  . ILE B 705  ? 0.1946 0.2946 0.2526 0.0337  0.0096  -0.0412 703  ILE B CB  
13887 C CG1 . ILE B 705  ? 0.2161 0.3249 0.2747 0.0344  0.0129  -0.0410 703  ILE B CG1 
13888 C CG2 . ILE B 705  ? 0.2112 0.3123 0.2728 0.0365  0.0080  -0.0434 703  ILE B CG2 
13889 C CD1 . ILE B 705  ? 0.2558 0.3737 0.3213 0.0323  0.0149  -0.0387 703  ILE B CD1 
13890 N N   . SER B 706  ? 0.2149 0.2932 0.2619 0.0368  0.0023  -0.0455 704  SER B N   
13891 C CA  . SER B 706  ? 0.2129 0.2829 0.2576 0.0360  -0.0008 -0.0455 704  SER B CA  
13892 C C   . SER B 706  ? 0.2276 0.2965 0.2744 0.0388  -0.0029 -0.0476 704  SER B C   
13893 O O   . SER B 706  ? 0.2309 0.3043 0.2796 0.0423  -0.0024 -0.0497 704  SER B O   
13894 C CB  . SER B 706  ? 0.2243 0.2871 0.2620 0.0359  -0.0025 -0.0464 704  SER B CB  
13895 O OG  . SER B 706  ? 0.2352 0.2976 0.2699 0.0396  -0.0028 -0.0495 704  SER B OG  
13896 N N   . PRO B 707  ? 0.2464 0.3096 0.2927 0.0377  -0.0054 -0.0470 705  PRO B N   
13897 C CA  . PRO B 707  ? 0.2274 0.2895 0.2758 0.0402  -0.0077 -0.0485 705  PRO B CA  
13898 C C   . PRO B 707  ? 0.2795 0.3335 0.3224 0.0429  -0.0108 -0.0509 705  PRO B C   
13899 O O   . PRO B 707  ? 0.2496 0.2981 0.2868 0.0422  -0.0115 -0.0512 705  PRO B O   
13900 C CB  . PRO B 707  ? 0.2345 0.2946 0.2849 0.0371  -0.0086 -0.0463 705  PRO B CB  
13901 C CG  . PRO B 707  ? 0.2223 0.2778 0.2685 0.0341  -0.0085 -0.0445 705  PRO B CG  
13902 C CD  . PRO B 707  ? 0.2580 0.3169 0.3027 0.0340  -0.0060 -0.0445 705  PRO B CD  
13903 N N   . TRP B 708  ? 0.2312 0.2842 0.2757 0.0457  -0.0130 -0.0525 706  TRP B N   
13904 C CA  . TRP B 708  ? 0.2621 0.3068 0.3013 0.0487  -0.0164 -0.0548 706  TRP B CA  
13905 C C   . TRP B 708  ? 0.2675 0.3032 0.3028 0.0461  -0.0194 -0.0533 706  TRP B C   
13906 O O   . TRP B 708  ? 0.2617 0.2890 0.2915 0.0474  -0.0225 -0.0545 706  TRP B O   
13907 C CB  . TRP B 708  ? 0.2398 0.2877 0.2823 0.0537  -0.0175 -0.0573 706  TRP B CB  
13908 C CG  . TRP B 708  ? 0.2742 0.3276 0.3235 0.0527  -0.0174 -0.0559 706  TRP B CG  
13909 C CD1 . TRP B 708  ? 0.2958 0.3599 0.3522 0.0525  -0.0148 -0.0553 706  TRP B CD1 
13910 C CD2 . TRP B 708  ? 0.2341 0.2822 0.2831 0.0513  -0.0203 -0.0548 706  TRP B CD2 
13911 N NE1 . TRP B 708  ? 0.2705 0.3359 0.3310 0.0511  -0.0161 -0.0541 706  TRP B NE1 
13912 C CE2 . TRP B 708  ? 0.2858 0.3415 0.3417 0.0505  -0.0194 -0.0538 706  TRP B CE2 
13913 C CE3 . TRP B 708  ? 0.2854 0.3231 0.3285 0.0504  -0.0237 -0.0544 706  TRP B CE3 
13914 C CZ2 . TRP B 708  ? 0.2881 0.3411 0.3451 0.0492  -0.0218 -0.0528 706  TRP B CZ2 
13915 C CZ3 . TRP B 708  ? 0.2822 0.3177 0.3265 0.0491  -0.0258 -0.0532 706  TRP B CZ3 
13916 C CH2 . TRP B 708  ? 0.2682 0.3111 0.3192 0.0486  -0.0248 -0.0525 706  TRP B CH2 
13917 N N   . ASN B 709  ? 0.2297 0.2667 0.2674 0.0424  -0.0188 -0.0506 707  ASN B N   
13918 C CA  . ASN B 709  ? 0.2729 0.3027 0.3074 0.0402  -0.0214 -0.0492 707  ASN B CA  
13919 C C   . ASN B 709  ? 0.2862 0.3113 0.3156 0.0365  -0.0214 -0.0474 707  ASN B C   
13920 O O   . ASN B 709  ? 0.3060 0.3242 0.3311 0.0349  -0.0240 -0.0464 707  ASN B O   
13921 C CB  . ASN B 709  ? 0.2580 0.2914 0.2971 0.0385  -0.0210 -0.0475 707  ASN B CB  
13922 C CG  . ASN B 709  ? 0.3182 0.3572 0.3603 0.0354  -0.0177 -0.0455 707  ASN B CG  
13923 O OD1 . ASN B 709  ? 0.3424 0.3856 0.3855 0.0354  -0.0153 -0.0456 707  ASN B OD1 
13924 N ND2 . ASN B 709  ? 0.2922 0.3310 0.3355 0.0330  -0.0178 -0.0437 707  ASN B ND2 
13925 N N   . PHE B 710  ? 0.2744 0.3036 0.3043 0.0352  -0.0187 -0.0467 708  PHE B N   
13926 C CA  . PHE B 710  ? 0.2924 0.3180 0.3175 0.0322  -0.0188 -0.0453 708  PHE B CA  
13927 C C   . PHE B 710  ? 0.2812 0.3086 0.3048 0.0338  -0.0175 -0.0470 708  PHE B C   
13928 O O   . PHE B 710  ? 0.2696 0.3018 0.2944 0.0323  -0.0148 -0.0459 708  PHE B O   
13929 C CB  . PHE B 710  ? 0.3160 0.3452 0.3431 0.0286  -0.0167 -0.0424 708  PHE B CB  
13930 C CG  . PHE B 710  ? 0.3456 0.3724 0.3729 0.0271  -0.0181 -0.0409 708  PHE B CG  
13931 C CD1 . PHE B 710  ? 0.3888 0.4092 0.4112 0.0253  -0.0206 -0.0400 708  PHE B CD1 
13932 C CD2 . PHE B 710  ? 0.3707 0.4016 0.4028 0.0274  -0.0170 -0.0405 708  PHE B CD2 
13933 C CE1 . PHE B 710  ? 0.3818 0.4004 0.4039 0.0239  -0.0217 -0.0386 708  PHE B CE1 
13934 C CE2 . PHE B 710  ? 0.4213 0.4497 0.4528 0.0262  -0.0184 -0.0393 708  PHE B CE2 
13935 C CZ  . PHE B 710  ? 0.3857 0.4082 0.4122 0.0246  -0.0206 -0.0384 708  PHE B CZ  
13936 N N   . PRO B 711  ? 0.2496 0.2726 0.2699 0.0371  -0.0196 -0.0498 709  PRO B N   
13937 C CA  . PRO B 711  ? 0.2437 0.2693 0.2629 0.0397  -0.0182 -0.0520 709  PRO B CA  
13938 C C   . PRO B 711  ? 0.2349 0.2576 0.2489 0.0373  -0.0182 -0.0514 709  PRO B C   
13939 O O   . PRO B 711  ? 0.2487 0.2742 0.2617 0.0390  -0.0166 -0.0530 709  PRO B O   
13940 C CB  . PRO B 711  ? 0.2262 0.2466 0.2428 0.0443  -0.0210 -0.0553 709  PRO B CB  
13941 C CG  . PRO B 711  ? 0.2677 0.2788 0.2804 0.0425  -0.0248 -0.0542 709  PRO B CG  
13942 C CD  . PRO B 711  ? 0.2537 0.2690 0.2709 0.0389  -0.0234 -0.0510 709  PRO B CD  
13943 N N   . LEU B 712  ? 0.2569 0.2743 0.2676 0.0334  -0.0199 -0.0493 710  LEU B N   
13944 C CA  . LEU B 712  ? 0.2474 0.2640 0.2544 0.0304  -0.0197 -0.0481 710  LEU B CA  
13945 C C   . LEU B 712  ? 0.2250 0.2470 0.2354 0.0267  -0.0174 -0.0447 710  LEU B C   
13946 O O   . LEU B 712  ? 0.2349 0.2611 0.2454 0.0255  -0.0154 -0.0439 710  LEU B O   
13947 C CB  . LEU B 712  ? 0.2243 0.2310 0.2244 0.0285  -0.0237 -0.0482 710  LEU B CB  
13948 C CG  . LEU B 712  ? 0.2438 0.2495 0.2398 0.0253  -0.0240 -0.0472 710  LEU B CG  
13949 C CD1 . LEU B 712  ? 0.2490 0.2564 0.2431 0.0282  -0.0228 -0.0499 710  LEU B CD1 
13950 C CD2 . LEU B 712  ? 0.2978 0.2938 0.2875 0.0225  -0.0283 -0.0467 710  LEU B CD2 
13951 N N   . ALA B 713  ? 0.2442 0.2662 0.2569 0.0249  -0.0178 -0.0428 711  ALA B N   
13952 C CA  . ALA B 713  ? 0.2492 0.2752 0.2640 0.0216  -0.0161 -0.0397 711  ALA B CA  
13953 C C   . ALA B 713  ? 0.2319 0.2658 0.2519 0.0223  -0.0125 -0.0391 711  ALA B C   
13954 O O   . ALA B 713  ? 0.2020 0.2395 0.2224 0.0207  -0.0108 -0.0374 711  ALA B O   
13955 C CB  . ALA B 713  ? 0.2502 0.2740 0.2654 0.0198  -0.0174 -0.0379 711  ALA B CB  
13956 N N   . ILE B 714  ? 0.2299 0.2666 0.2541 0.0247  -0.0116 -0.0401 712  ILE B N   
13957 C CA  . ILE B 714  ? 0.2041 0.2478 0.2330 0.0248  -0.0084 -0.0392 712  ILE B CA  
13958 C C   . ILE B 714  ? 0.2291 0.2763 0.2574 0.0263  -0.0068 -0.0404 712  ILE B C   
13959 O O   . ILE B 714  ? 0.2336 0.2855 0.2634 0.0251  -0.0045 -0.0389 712  ILE B O   
13960 C CB  . ILE B 714  ? 0.2576 0.3036 0.2914 0.0262  -0.0082 -0.0396 712  ILE B CB  
13961 C CG1 . ILE B 714  ? 0.2475 0.2913 0.2817 0.0243  -0.0092 -0.0379 712  ILE B CG1 
13962 C CG2 . ILE B 714  ? 0.2362 0.2894 0.2747 0.0265  -0.0053 -0.0390 712  ILE B CG2 
13963 C CD1 . ILE B 714  ? 0.3633 0.4077 0.4012 0.0256  -0.0098 -0.0385 712  ILE B CD1 
13964 N N   . PHE B 715  ? 0.2365 0.2811 0.2622 0.0289  -0.0080 -0.0431 713  PHE B N   
13965 C CA  . PHE B 715  ? 0.2184 0.2652 0.2418 0.0304  -0.0068 -0.0446 713  PHE B CA  
13966 C C   . PHE B 715  ? 0.2162 0.2625 0.2363 0.0276  -0.0065 -0.0429 713  PHE B C   
13967 O O   . PHE B 715  ? 0.2129 0.2645 0.2340 0.0272  -0.0040 -0.0419 713  PHE B O   
13968 C CB  . PHE B 715  ? 0.2353 0.2767 0.2545 0.0336  -0.0092 -0.0480 713  PHE B CB  
13969 C CG  . PHE B 715  ? 0.2230 0.2658 0.2388 0.0357  -0.0081 -0.0501 713  PHE B CG  
13970 C CD1 . PHE B 715  ? 0.2227 0.2729 0.2418 0.0387  -0.0055 -0.0514 713  PHE B CD1 
13971 C CD2 . PHE B 715  ? 0.3026 0.3399 0.3119 0.0346  -0.0099 -0.0506 713  PHE B CD2 
13972 C CE1 . PHE B 715  ? 0.2967 0.3487 0.3123 0.0409  -0.0043 -0.0534 713  PHE B CE1 
13973 C CE2 . PHE B 715  ? 0.2387 0.2771 0.2442 0.0368  -0.0091 -0.0528 713  PHE B CE2 
13974 C CZ  . PHE B 715  ? 0.2503 0.2960 0.2588 0.0401  -0.0062 -0.0543 713  PHE B CZ  
13975 N N   . THR B 716  ? 0.2180 0.2585 0.2344 0.0253  -0.0090 -0.0421 714  THR B N   
13976 C CA  . THR B 716  ? 0.2271 0.2672 0.2402 0.0225  -0.0092 -0.0405 714  THR B CA  
13977 C C   . THR B 716  ? 0.2267 0.2723 0.2437 0.0203  -0.0070 -0.0373 714  THR B C   
13978 O O   . THR B 716  ? 0.2289 0.2779 0.2453 0.0194  -0.0056 -0.0362 714  THR B O   
13979 C CB  . THR B 716  ? 0.2202 0.2533 0.2289 0.0203  -0.0127 -0.0402 714  THR B CB  
13980 O OG1 . THR B 716  ? 0.2341 0.2609 0.2383 0.0225  -0.0151 -0.0433 714  THR B OG1 
13981 C CG2 . THR B 716  ? 0.2351 0.2686 0.2408 0.0171  -0.0132 -0.0384 714  THR B CG2 
13982 N N   . GLY B 717  ? 0.2142 0.2605 0.2348 0.0197  -0.0068 -0.0359 715  GLY B N   
13983 C CA  . GLY B 717  ? 0.2040 0.2544 0.2276 0.0180  -0.0051 -0.0331 715  GLY B CA  
13984 C C   . GLY B 717  ? 0.2174 0.2733 0.2437 0.0188  -0.0023 -0.0325 715  GLY B C   
13985 O O   . GLY B 717  ? 0.2214 0.2800 0.2475 0.0175  -0.0013 -0.0306 715  GLY B O   
13986 N N   . GLN B 718  ? 0.2022 0.2601 0.2312 0.0208  -0.0012 -0.0340 716  GLN B N   
13987 C CA  . GLN B 718  ? 0.2293 0.2927 0.2609 0.0211  0.0015  -0.0331 716  GLN B CA  
13988 C C   . GLN B 718  ? 0.2071 0.2722 0.2352 0.0211  0.0022  -0.0333 716  GLN B C   
13989 O O   . GLN B 718  ? 0.2254 0.2937 0.2537 0.0200  0.0038  -0.0312 716  GLN B O   
13990 C CB  . GLN B 718  ? 0.1934 0.2596 0.2286 0.0231  0.0024  -0.0346 716  GLN B CB  
13991 C CG  . GLN B 718  ? 0.2025 0.2676 0.2416 0.0229  0.0016  -0.0343 716  GLN B CG  
13992 C CD  . GLN B 718  ? 0.2377 0.3066 0.2810 0.0246  0.0024  -0.0356 716  GLN B CD  
13993 O OE1 . GLN B 718  ? 0.2993 0.3696 0.3465 0.0238  0.0025  -0.0345 716  GLN B OE1 
13994 N NE2 . GLN B 718  ? 0.2154 0.2861 0.2578 0.0270  0.0026  -0.0379 716  GLN B NE2 
13995 N N   . ILE B 719  ? 0.1933 0.2554 0.2174 0.0226  0.0009  -0.0359 717  ILE B N   
13996 C CA  . ILE B 719  ? 0.1619 0.2252 0.1819 0.0230  0.0015  -0.0367 717  ILE B CA  
13997 C C   . ILE B 719  ? 0.1860 0.2482 0.2032 0.0204  0.0006  -0.0346 717  ILE B C   
13998 O O   . ILE B 719  ? 0.1967 0.2623 0.2128 0.0198  0.0020  -0.0333 717  ILE B O   
13999 C CB  . ILE B 719  ? 0.2073 0.2665 0.2231 0.0255  -0.0003 -0.0403 717  ILE B CB  
14000 C CG1 . ILE B 719  ? 0.2047 0.2673 0.2236 0.0288  0.0012  -0.0424 717  ILE B CG1 
14001 C CG2 . ILE B 719  ? 0.2726 0.3308 0.2828 0.0255  -0.0007 -0.0412 717  ILE B CG2 
14002 C CD1 . ILE B 719  ? 0.2685 0.3261 0.2839 0.0319  -0.0009 -0.0460 717  ILE B CD1 
14003 N N   . ALA B 720  ? 0.1551 0.2131 0.1712 0.0187  -0.0018 -0.0340 718  ALA B N   
14004 C CA  . ALA B 720  ? 0.1853 0.2431 0.1992 0.0161  -0.0028 -0.0319 718  ALA B CA  
14005 C C   . ALA B 720  ? 0.1927 0.2555 0.2101 0.0152  -0.0008 -0.0288 718  ALA B C   
14006 O O   . ALA B 720  ? 0.1876 0.2527 0.2033 0.0141  -0.0005 -0.0273 718  ALA B O   
14007 C CB  . ALA B 720  ? 0.1954 0.2491 0.2085 0.0143  -0.0054 -0.0314 718  ALA B CB  
14008 N N   . ALA B 721  ? 0.2039 0.2681 0.2258 0.0156  0.0004  -0.0279 719  ALA B N   
14009 C CA  . ALA B 721  ? 0.2306 0.2983 0.2553 0.0150  0.0020  -0.0252 719  ALA B CA  
14010 C C   . ALA B 721  ? 0.1895 0.2608 0.2139 0.0154  0.0040  -0.0245 719  ALA B C   
14011 O O   . ALA B 721  ? 0.2115 0.2848 0.2351 0.0145  0.0044  -0.0223 719  ALA B O   
14012 C CB  . ALA B 721  ? 0.2105 0.2780 0.2396 0.0155  0.0026  -0.0248 719  ALA B CB  
14013 N N   . ALA B 722  ? 0.1948 0.2673 0.2197 0.0168  0.0052  -0.0264 720  ALA B N   
14014 C CA  . ALA B 722  ? 0.2159 0.2925 0.2404 0.0171  0.0073  -0.0257 720  ALA B CA  
14015 C C   . ALA B 722  ? 0.2220 0.2988 0.2413 0.0168  0.0068  -0.0258 720  ALA B C   
14016 O O   . ALA B 722  ? 0.2137 0.2933 0.2322 0.0159  0.0079  -0.0236 720  ALA B O   
14017 C CB  . ALA B 722  ? 0.1814 0.2602 0.2075 0.0189  0.0087  -0.0279 720  ALA B CB  
14018 N N   . LEU B 723  ? 0.1930 0.2663 0.2086 0.0173  0.0049  -0.0283 721  LEU B N   
14019 C CA  . LEU B 723  ? 0.1980 0.2708 0.2082 0.0167  0.0039  -0.0287 721  LEU B CA  
14020 C C   . LEU B 723  ? 0.2213 0.2947 0.2311 0.0145  0.0029  -0.0257 721  LEU B C   
14021 O O   . LEU B 723  ? 0.2601 0.3361 0.2677 0.0139  0.0035  -0.0243 721  LEU B O   
14022 C CB  . LEU B 723  ? 0.2068 0.2742 0.2128 0.0174  0.0013  -0.0318 721  LEU B CB  
14023 C CG  . LEU B 723  ? 0.2449 0.3113 0.2493 0.0203  0.0018  -0.0354 721  LEU B CG  
14024 C CD1 . LEU B 723  ? 0.2421 0.3015 0.2425 0.0207  -0.0014 -0.0381 721  LEU B CD1 
14025 C CD2 . LEU B 723  ? 0.2258 0.2961 0.2271 0.0217  0.0038  -0.0362 721  LEU B CD2 
14026 N N   . VAL B 724  ? 0.1929 0.2643 0.2046 0.0133  0.0013  -0.0248 722  VAL B N   
14027 C CA  . VAL B 724  ? 0.1897 0.2626 0.2012 0.0115  0.0002  -0.0222 722  VAL B CA  
14028 C C   . VAL B 724  ? 0.2327 0.3094 0.2468 0.0117  0.0021  -0.0193 722  VAL B C   
14029 O O   . VAL B 724  ? 0.2493 0.3281 0.2623 0.0108  0.0015  -0.0171 722  VAL B O   
14030 C CB  . VAL B 724  ? 0.2065 0.2774 0.2196 0.0103  -0.0016 -0.0217 722  VAL B CB  
14031 C CG1 . VAL B 724  ? 0.1893 0.2613 0.2075 0.0111  -0.0002 -0.0203 722  VAL B CG1 
14032 C CG2 . VAL B 724  ? 0.1870 0.2594 0.1982 0.0082  -0.0035 -0.0199 722  VAL B CG2 
14033 N N   . ALA B 725  ? 0.2126 0.2901 0.2300 0.0127  0.0041  -0.0190 723  ALA B N   
14034 C CA  . ALA B 725  ? 0.2308 0.3109 0.2501 0.0127  0.0057  -0.0162 723  ALA B CA  
14035 C C   . ALA B 725  ? 0.2465 0.3292 0.2626 0.0127  0.0069  -0.0157 723  ALA B C   
14036 O O   . ALA B 725  ? 0.2655 0.3501 0.2823 0.0124  0.0080  -0.0131 723  ALA B O   
14037 C CB  . ALA B 725  ? 0.2496 0.3293 0.2732 0.0133  0.0070  -0.0161 723  ALA B CB  
14038 N N   . GLY B 726  ? 0.2144 0.2967 0.2266 0.0130  0.0065  -0.0181 724  GLY B N   
14039 C CA  . GLY B 726  ? 0.2725 0.3575 0.2809 0.0131  0.0076  -0.0179 724  GLY B CA  
14040 C C   . GLY B 726  ? 0.2495 0.3368 0.2583 0.0143  0.0101  -0.0192 724  GLY B C   
14041 O O   . GLY B 726  ? 0.2497 0.3402 0.2559 0.0142  0.0116  -0.0183 724  GLY B O   
14042 N N   . ASN B 727  ? 0.1941 0.2805 0.2061 0.0153  0.0106  -0.0211 725  ASN B N   
14043 C CA  . ASN B 727  ? 0.2199 0.3097 0.2332 0.0166  0.0130  -0.0224 725  ASN B CA  
14044 C C   . ASN B 727  ? 0.2012 0.2899 0.2115 0.0188  0.0125  -0.0266 725  ASN B C   
14045 O O   . ASN B 727  ? 0.2354 0.3194 0.2452 0.0194  0.0103  -0.0286 725  ASN B O   
14046 C CB  . ASN B 727  ? 0.1656 0.2559 0.1850 0.0164  0.0137  -0.0217 725  ASN B CB  
14047 C CG  . ASN B 727  ? 0.2463 0.3363 0.2684 0.0146  0.0137  -0.0180 725  ASN B CG  
14048 O OD1 . ASN B 727  ? 0.2501 0.3430 0.2727 0.0135  0.0154  -0.0154 725  ASN B OD1 
14049 N ND2 . ASN B 727  ? 0.2285 0.3146 0.2522 0.0143  0.0118  -0.0176 725  ASN B ND2 
14050 N N   . PRO B 728  ? 0.2086 0.3011 0.2164 0.0204  0.0144  -0.0279 726  PRO B N   
14051 C CA  . PRO B 728  ? 0.2232 0.3147 0.2287 0.0233  0.0141  -0.0322 726  PRO B CA  
14052 C C   . PRO B 728  ? 0.2127 0.3055 0.2240 0.0246  0.0149  -0.0332 726  PRO B C   
14053 O O   . PRO B 728  ? 0.2382 0.3348 0.2547 0.0233  0.0166  -0.0307 726  PRO B O   
14054 C CB  . PRO B 728  ? 0.2584 0.3551 0.2600 0.0247  0.0166  -0.0329 726  PRO B CB  
14055 C CG  . PRO B 728  ? 0.2710 0.3733 0.2760 0.0223  0.0190  -0.0286 726  PRO B CG  
14056 C CD  . PRO B 728  ? 0.2799 0.3784 0.2874 0.0196  0.0172  -0.0255 726  PRO B CD  
14057 N N   . VAL B 729  ? 0.2035 0.2926 0.2136 0.0270  0.0133  -0.0368 727  VAL B N   
14058 C CA  . VAL B 729  ? 0.2395 0.3285 0.2549 0.0282  0.0131  -0.0379 727  VAL B CA  
14059 C C   . VAL B 729  ? 0.2118 0.3038 0.2267 0.0322  0.0142  -0.0415 727  VAL B C   
14060 O O   . VAL B 729  ? 0.2399 0.3295 0.2490 0.0347  0.0134  -0.0446 727  VAL B O   
14061 C CB  . VAL B 729  ? 0.1777 0.2589 0.1928 0.0275  0.0097  -0.0386 727  VAL B CB  
14062 C CG1 . VAL B 729  ? 0.1979 0.2782 0.2169 0.0296  0.0091  -0.0406 727  VAL B CG1 
14063 C CG2 . VAL B 729  ? 0.2180 0.2981 0.2351 0.0241  0.0092  -0.0349 727  VAL B CG2 
14064 N N   . LEU B 730  ? 0.2055 0.3027 0.2265 0.0330  0.0159  -0.0412 728  LEU B N   
14065 C CA  . LEU B 730  ? 0.2433 0.3434 0.2656 0.0370  0.0164  -0.0446 728  LEU B CA  
14066 C C   . LEU B 730  ? 0.2649 0.3599 0.2904 0.0375  0.0138  -0.0455 728  LEU B C   
14067 O O   . LEU B 730  ? 0.2177 0.3142 0.2488 0.0352  0.0140  -0.0431 728  LEU B O   
14068 C CB  . LEU B 730  ? 0.2085 0.3195 0.2358 0.0373  0.0201  -0.0433 728  LEU B CB  
14069 C CG  . LEU B 730  ? 0.2060 0.3236 0.2306 0.0366  0.0232  -0.0418 728  LEU B CG  
14070 C CD1 . LEU B 730  ? 0.2556 0.3701 0.2721 0.0394  0.0226  -0.0450 728  LEU B CD1 
14071 C CD2 . LEU B 730  ? 0.2604 0.3778 0.2857 0.0317  0.0237  -0.0371 728  LEU B CD2 
14072 N N   . ALA B 731  ? 0.2308 0.3190 0.2522 0.0402  0.0111  -0.0489 729  ALA B N   
14073 C CA  . ALA B 731  ? 0.2291 0.3113 0.2524 0.0404  0.0082  -0.0497 729  ALA B CA  
14074 C C   . ALA B 731  ? 0.2226 0.3081 0.2489 0.0447  0.0084  -0.0525 729  ALA B C   
14075 O O   . ALA B 731  ? 0.2549 0.3393 0.2773 0.0489  0.0080  -0.0560 729  ALA B O   
14076 C CB  . ALA B 731  ? 0.1955 0.2672 0.2121 0.0402  0.0046  -0.0511 729  ALA B CB  
14077 N N   . LYS B 732  ? 0.2565 0.3460 0.2897 0.0439  0.0090  -0.0510 730  LYS B N   
14078 C CA  . LYS B 732  ? 0.2745 0.3681 0.3118 0.0477  0.0090  -0.0533 730  LYS B CA  
14079 C C   . LYS B 732  ? 0.2691 0.3553 0.3072 0.0478  0.0055  -0.0538 730  LYS B C   
14080 O O   . LYS B 732  ? 0.2215 0.3085 0.2644 0.0449  0.0053  -0.0513 730  LYS B O   
14081 C CB  . LYS B 732  ? 0.2357 0.3406 0.2805 0.0465  0.0122  -0.0511 730  LYS B CB  
14082 C CG  . LYS B 732  ? 0.2825 0.3961 0.3301 0.0513  0.0138  -0.0537 730  LYS B CG  
14083 C CD  . LYS B 732  ? 0.2958 0.4061 0.3450 0.0550  0.0110  -0.0565 730  LYS B CD  
14084 C CE  . LYS B 732  ? 0.2493 0.3601 0.3049 0.0520  0.0098  -0.0541 730  LYS B CE  
14085 N NZ  . LYS B 732  ? 0.2902 0.4000 0.3482 0.0559  0.0074  -0.0566 730  LYS B NZ  
14086 N N   . PRO B 733  ? 0.2611 0.3397 0.2944 0.0510  0.0025  -0.0569 731  PRO B N   
14087 C CA  . PRO B 733  ? 0.2424 0.3135 0.2759 0.0508  -0.0009 -0.0571 731  PRO B CA  
14088 C C   . PRO B 733  ? 0.2345 0.3107 0.2740 0.0538  -0.0011 -0.0582 731  PRO B C   
14089 O O   . PRO B 733  ? 0.2314 0.3163 0.2740 0.0569  0.0012  -0.0596 731  PRO B O   
14090 C CB  . PRO B 733  ? 0.2781 0.3392 0.3036 0.0533  -0.0041 -0.0600 731  PRO B CB  
14091 C CG  . PRO B 733  ? 0.2487 0.3148 0.2725 0.0578  -0.0022 -0.0630 731  PRO B CG  
14092 C CD  . PRO B 733  ? 0.2890 0.3654 0.3163 0.0553  0.0021  -0.0606 731  PRO B CD  
14093 N N   . ALA B 734  ? 0.2398 0.3108 0.2806 0.0528  -0.0038 -0.0575 732  ALA B N   
14094 C CA  . ALA B 734  ? 0.2241 0.2987 0.2701 0.0556  -0.0047 -0.0586 732  ALA B CA  
14095 C C   . ALA B 734  ? 0.2975 0.3718 0.3412 0.0619  -0.0058 -0.0627 732  ALA B C   
14096 O O   . ALA B 734  ? 0.2578 0.3240 0.2943 0.0639  -0.0076 -0.0649 732  ALA B O   
14097 C CB  . ALA B 734  ? 0.2201 0.2871 0.2659 0.0538  -0.0081 -0.0575 732  ALA B CB  
14098 N N   . GLU B 735  ? 0.2475 0.3308 0.2974 0.0652  -0.0048 -0.0638 733  GLU B N   
14099 C CA  . GLU B 735  ? 0.2494 0.3341 0.2980 0.0720  -0.0055 -0.0678 733  GLU B CA  
14100 C C   . GLU B 735  ? 0.2302 0.3021 0.2731 0.0748  -0.0103 -0.0700 733  GLU B C   
14101 O O   . GLU B 735  ? 0.2497 0.3170 0.2871 0.0798  -0.0118 -0.0735 733  GLU B O   
14102 C CB  . GLU B 735  ? 0.3253 0.4229 0.3826 0.0746  -0.0037 -0.0681 733  GLU B CB  
14103 C CG  . GLU B 735  ? 0.4222 0.5239 0.4790 0.0822  -0.0037 -0.0723 733  GLU B CG  
14104 C CD  . GLU B 735  ? 0.4851 0.6001 0.5513 0.0849  -0.0025 -0.0724 733  GLU B CD  
14105 O OE1 . GLU B 735  ? 0.4493 0.5712 0.5224 0.0802  -0.0012 -0.0691 733  GLU B OE1 
14106 O OE2 . GLU B 735  ? 0.4549 0.5733 0.5214 0.0918  -0.0030 -0.0760 733  GLU B OE2 
14107 N N   . GLU B 736  ? 0.2580 0.3239 0.3016 0.0717  -0.0130 -0.0680 734  GLU B N   
14108 C CA  . GLU B 736  ? 0.2670 0.3211 0.3055 0.0739  -0.0178 -0.0696 734  GLU B CA  
14109 C C   . GLU B 736  ? 0.2841 0.3256 0.3133 0.0722  -0.0200 -0.0699 734  GLU B C   
14110 O O   . GLU B 736  ? 0.2701 0.3013 0.2936 0.0750  -0.0240 -0.0719 734  GLU B O   
14111 C CB  . GLU B 736  ? 0.2780 0.3303 0.3201 0.0708  -0.0198 -0.0670 734  GLU B CB  
14112 C CG  . GLU B 736  ? 0.3161 0.3796 0.3672 0.0723  -0.0185 -0.0668 734  GLU B CG  
14113 C CD  . GLU B 736  ? 0.3127 0.3864 0.3702 0.0676  -0.0146 -0.0638 734  GLU B CD  
14114 O OE1 . GLU B 736  ? 0.2525 0.3260 0.3078 0.0639  -0.0123 -0.0621 734  GLU B OE1 
14115 O OE2 . GLU B 736  ? 0.3557 0.4376 0.4204 0.0676  -0.0142 -0.0630 734  GLU B OE2 
14116 N N   . THR B 737  ? 0.2460 0.2876 0.2733 0.0675  -0.0179 -0.0678 735  THR B N   
14117 C CA  . THR B 737  ? 0.2671 0.2974 0.2864 0.0645  -0.0203 -0.0673 735  THR B CA  
14118 C C   . THR B 737  ? 0.2527 0.2846 0.2684 0.0638  -0.0180 -0.0678 735  THR B C   
14119 O O   . THR B 737  ? 0.2568 0.2868 0.2705 0.0588  -0.0174 -0.0653 735  THR B O   
14120 C CB  . THR B 737  ? 0.2524 0.2795 0.2726 0.0585  -0.0211 -0.0634 735  THR B CB  
14121 O OG1 . THR B 737  ? 0.2473 0.2840 0.2734 0.0551  -0.0172 -0.0607 735  THR B OG1 
14122 C CG2 . THR B 737  ? 0.2691 0.2928 0.2912 0.0592  -0.0240 -0.0630 735  THR B CG2 
14123 N N   . PRO B 738  ? 0.2628 0.2980 0.2770 0.0688  -0.0168 -0.0711 736  PRO B N   
14124 C CA  . PRO B 738  ? 0.2772 0.3142 0.2875 0.0681  -0.0146 -0.0716 736  PRO B CA  
14125 C C   . PRO B 738  ? 0.2867 0.3110 0.2874 0.0667  -0.0180 -0.0726 736  PRO B C   
14126 O O   . PRO B 738  ? 0.2437 0.2684 0.2411 0.0642  -0.0167 -0.0720 736  PRO B O   
14127 C CB  . PRO B 738  ? 0.2324 0.2772 0.2440 0.0745  -0.0124 -0.0752 736  PRO B CB  
14128 C CG  . PRO B 738  ? 0.2796 0.3187 0.2903 0.0796  -0.0159 -0.0780 736  PRO B CG  
14129 C CD  . PRO B 738  ? 0.2529 0.2903 0.2683 0.0758  -0.0176 -0.0748 736  PRO B CD  
14130 N N   . LEU B 739  ? 0.2385 0.2515 0.2345 0.0682  -0.0227 -0.0741 737  LEU B N   
14131 C CA  . LEU B 739  ? 0.2977 0.2983 0.2840 0.0676  -0.0263 -0.0756 737  LEU B CA  
14132 C C   . LEU B 739  ? 0.2766 0.2735 0.2610 0.0602  -0.0270 -0.0718 737  LEU B C   
14133 O O   . LEU B 739  ? 0.2811 0.2747 0.2600 0.0583  -0.0274 -0.0721 737  LEU B O   
14134 C CB  . LEU B 739  ? 0.2884 0.2771 0.2697 0.0711  -0.0314 -0.0780 737  LEU B CB  
14135 C CG  . LEU B 739  ? 0.3058 0.2973 0.2886 0.0792  -0.0314 -0.0821 737  LEU B CG  
14136 C CD1 . LEU B 739  ? 0.2851 0.2629 0.2618 0.0827  -0.0372 -0.0844 737  LEU B CD1 
14137 C CD2 . LEU B 739  ? 0.2859 0.2825 0.2662 0.0835  -0.0288 -0.0855 737  LEU B CD2 
14138 N N   . ILE B 740  ? 0.2440 0.2415 0.2327 0.0562  -0.0273 -0.0683 738  ILE B N   
14139 C CA  . ILE B 740  ? 0.2545 0.2497 0.2419 0.0495  -0.0276 -0.0646 738  ILE B CA  
14140 C C   . ILE B 740  ? 0.2571 0.2622 0.2479 0.0472  -0.0233 -0.0629 738  ILE B C   
14141 O O   . ILE B 740  ? 0.2751 0.2783 0.2625 0.0433  -0.0236 -0.0613 738  ILE B O   
14142 C CB  . ILE B 740  ? 0.3260 0.3199 0.3168 0.0462  -0.0288 -0.0615 738  ILE B CB  
14143 C CG1 . ILE B 740  ? 0.3171 0.3081 0.3057 0.0397  -0.0296 -0.0579 738  ILE B CG1 
14144 C CG2 . ILE B 740  ? 0.2971 0.3017 0.2968 0.0472  -0.0253 -0.0603 738  ILE B CG2 
14145 C CD1 . ILE B 740  ? 0.3096 0.2891 0.2895 0.0380  -0.0339 -0.0587 738  ILE B CD1 
14146 N N   . ALA B 741  ? 0.2443 0.2599 0.2414 0.0497  -0.0194 -0.0632 739  ALA B N   
14147 C CA  . ALA B 741  ? 0.2514 0.2760 0.2512 0.0478  -0.0154 -0.0616 739  ALA B CA  
14148 C C   . ALA B 741  ? 0.2448 0.2672 0.2379 0.0491  -0.0155 -0.0638 739  ALA B C   
14149 O O   . ALA B 741  ? 0.2672 0.2909 0.2587 0.0455  -0.0145 -0.0619 739  ALA B O   
14150 C CB  . ALA B 741  ? 0.2416 0.2775 0.2488 0.0503  -0.0116 -0.0616 739  ALA B CB  
14151 N N   . ALA B 742  ? 0.2641 0.2833 0.2532 0.0544  -0.0167 -0.0680 740  ALA B N   
14152 C CA  . ALA B 742  ? 0.2757 0.2914 0.2573 0.0560  -0.0174 -0.0706 740  ALA B CA  
14153 C C   . ALA B 742  ? 0.2811 0.2864 0.2560 0.0514  -0.0212 -0.0695 740  ALA B C   
14154 O O   . ALA B 742  ? 0.2672 0.2724 0.2379 0.0494  -0.0208 -0.0693 740  ALA B O   
14155 C CB  . ALA B 742  ? 0.2532 0.2652 0.2309 0.0630  -0.0188 -0.0757 740  ALA B CB  
14156 N N   . GLU B 743  ? 0.2608 0.2572 0.2341 0.0496  -0.0250 -0.0687 741  GLU B N   
14157 C CA  . GLU B 743  ? 0.2741 0.2616 0.2417 0.0445  -0.0286 -0.0671 741  GLU B CA  
14158 C C   . GLU B 743  ? 0.2675 0.2617 0.2390 0.0387  -0.0263 -0.0627 741  GLU B C   
14159 O O   . GLU B 743  ? 0.2800 0.2717 0.2472 0.0353  -0.0276 -0.0617 741  GLU B O   
14160 C CB  . GLU B 743  ? 0.3366 0.3142 0.3023 0.0435  -0.0330 -0.0666 741  GLU B CB  
14161 C CG  . GLU B 743  ? 0.3606 0.3295 0.3207 0.0376  -0.0368 -0.0644 741  GLU B CG  
14162 C CD  . GLU B 743  ? 0.3563 0.3155 0.3068 0.0384  -0.0403 -0.0674 741  GLU B CD  
14163 O OE1 . GLU B 743  ? 0.3284 0.2865 0.2758 0.0443  -0.0401 -0.0717 741  GLU B OE1 
14164 O OE2 . GLU B 743  ? 0.3747 0.3276 0.3207 0.0330  -0.0435 -0.0655 741  GLU B OE2 
14165 N N   . GLY B 744  ? 0.2483 0.2509 0.2279 0.0378  -0.0232 -0.0600 742  GLY B N   
14166 C CA  . GLY B 744  ? 0.2523 0.2621 0.2359 0.0334  -0.0206 -0.0562 742  GLY B CA  
14167 C C   . GLY B 744  ? 0.2274 0.2423 0.2093 0.0336  -0.0183 -0.0566 742  GLY B C   
14168 O O   . GLY B 744  ? 0.2776 0.2929 0.2578 0.0297  -0.0186 -0.0544 742  GLY B O   
14169 N N   . VAL B 745  ? 0.2438 0.2632 0.2261 0.0382  -0.0159 -0.0593 743  VAL B N   
14170 C CA  . VAL B 745  ? 0.2221 0.2466 0.2023 0.0386  -0.0136 -0.0597 743  VAL B CA  
14171 C C   . VAL B 745  ? 0.2660 0.2822 0.2371 0.0378  -0.0170 -0.0616 743  VAL B C   
14172 O O   . VAL B 745  ? 0.2470 0.2651 0.2160 0.0349  -0.0166 -0.0601 743  VAL B O   
14173 C CB  . VAL B 745  ? 0.2731 0.3049 0.2556 0.0438  -0.0102 -0.0622 743  VAL B CB  
14174 C CG1 . VAL B 745  ? 0.2159 0.2516 0.1942 0.0446  -0.0082 -0.0632 743  VAL B CG1 
14175 C CG2 . VAL B 745  ? 0.2700 0.3114 0.2617 0.0432  -0.0066 -0.0595 743  VAL B CG2 
14176 N N   . ARG B 746  ? 0.2525 0.2587 0.2180 0.0401  -0.0208 -0.0648 744  ARG B N   
14177 C CA  . ARG B 746  ? 0.2971 0.2942 0.2535 0.0389  -0.0246 -0.0666 744  ARG B CA  
14178 C C   . ARG B 746  ? 0.2506 0.2459 0.2065 0.0321  -0.0265 -0.0627 744  ARG B C   
14179 O O   . ARG B 746  ? 0.2409 0.2349 0.1919 0.0298  -0.0276 -0.0626 744  ARG B O   
14180 C CB  . ARG B 746  ? 0.3211 0.3061 0.2715 0.0418  -0.0291 -0.0701 744  ARG B CB  
14181 C CG  . ARG B 746  ? 0.3454 0.3308 0.2948 0.0492  -0.0281 -0.0747 744  ARG B CG  
14182 C CD  . ARG B 746  ? 0.3555 0.3273 0.2985 0.0518  -0.0333 -0.0778 744  ARG B CD  
14183 N NE  . ARG B 746  ? 0.3754 0.3487 0.3185 0.0595  -0.0321 -0.0821 744  ARG B NE  
14184 C CZ  . ARG B 746  ? 0.3356 0.3102 0.2838 0.0625  -0.0319 -0.0823 744  ARG B CZ  
14185 N NH1 . ARG B 746  ? 0.3105 0.2823 0.2622 0.0587  -0.0336 -0.0791 744  ARG B NH1 
14186 N NH2 . ARG B 746  ? 0.3082 0.2874 0.2577 0.0697  -0.0300 -0.0859 744  ARG B NH2 
14187 N N   . ILE B 747  ? 0.2622 0.2579 0.2231 0.0288  -0.0269 -0.0594 745  ILE B N   
14188 C CA  . ILE B 747  ? 0.2866 0.2811 0.2472 0.0226  -0.0289 -0.0558 745  ILE B CA  
14189 C C   . ILE B 747  ? 0.2497 0.2541 0.2142 0.0203  -0.0255 -0.0528 745  ILE B C   
14190 O O   . ILE B 747  ? 0.2549 0.2589 0.2164 0.0167  -0.0270 -0.0514 745  ILE B O   
14191 C CB  . ILE B 747  ? 0.2837 0.2760 0.2481 0.0203  -0.0302 -0.0533 745  ILE B CB  
14192 C CG1 . ILE B 747  ? 0.2680 0.2479 0.2261 0.0212  -0.0349 -0.0558 745  ILE B CG1 
14193 C CG2 . ILE B 747  ? 0.2495 0.2454 0.2164 0.0143  -0.0304 -0.0488 745  ILE B CG2 
14194 C CD1 . ILE B 747  ? 0.2896 0.2672 0.2509 0.0204  -0.0359 -0.0541 745  ILE B CD1 
14195 N N   . LEU B 748  ? 0.2294 0.2429 0.2007 0.0225  -0.0211 -0.0519 746  LEU B N   
14196 C CA  . LEU B 748  ? 0.2235 0.2459 0.1982 0.0208  -0.0180 -0.0492 746  LEU B CA  
14197 C C   . LEU B 748  ? 0.2532 0.2760 0.2222 0.0217  -0.0179 -0.0509 746  LEU B C   
14198 O O   . LEU B 748  ? 0.2463 0.2720 0.2145 0.0186  -0.0179 -0.0486 746  LEU B O   
14199 C CB  . LEU B 748  ? 0.2243 0.2549 0.2063 0.0230  -0.0137 -0.0482 746  LEU B CB  
14200 C CG  . LEU B 748  ? 0.3149 0.3471 0.3030 0.0209  -0.0133 -0.0453 746  LEU B CG  
14201 C CD1 . LEU B 748  ? 0.2734 0.3120 0.2682 0.0234  -0.0098 -0.0449 746  LEU B CD1 
14202 C CD2 . LEU B 748  ? 0.3157 0.3510 0.3052 0.0167  -0.0134 -0.0416 746  LEU B CD2 
14203 N N   . ARG B 749  ? 0.2251 0.2452 0.1899 0.0261  -0.0178 -0.0550 747  ARG B N   
14204 C CA  . ARG B 749  ? 0.2446 0.2646 0.2030 0.0273  -0.0178 -0.0570 747  ARG B CA  
14205 C C   . ARG B 749  ? 0.2516 0.2631 0.2027 0.0240  -0.0226 -0.0575 747  ARG B C   
14206 O O   . ARG B 749  ? 0.2509 0.2639 0.1984 0.0221  -0.0230 -0.0568 747  ARG B O   
14207 C CB  . ARG B 749  ? 0.2469 0.2663 0.2024 0.0333  -0.0166 -0.0616 747  ARG B CB  
14208 C CG  . ARG B 749  ? 0.2398 0.2699 0.2018 0.0362  -0.0114 -0.0609 747  ARG B CG  
14209 C CD  . ARG B 749  ? 0.2437 0.2742 0.2020 0.0421  -0.0103 -0.0655 747  ARG B CD  
14210 N NE  . ARG B 749  ? 0.2680 0.3096 0.2324 0.0446  -0.0053 -0.0648 747  ARG B NE  
14211 C CZ  . ARG B 749  ? 0.3080 0.3535 0.2704 0.0497  -0.0031 -0.0681 747  ARG B CZ  
14212 N NH1 . ARG B 749  ? 0.2682 0.3069 0.2223 0.0534  -0.0054 -0.0727 747  ARG B NH1 
14213 N NH2 . ARG B 749  ? 0.2739 0.3305 0.2427 0.0512  0.0014  -0.0669 747  ARG B NH2 
14214 N N   . GLU B 750  ? 0.2453 0.2473 0.1935 0.0231  -0.0266 -0.0586 748  GLU B N   
14215 C CA  . GLU B 750  ? 0.3074 0.3010 0.2489 0.0191  -0.0316 -0.0586 748  GLU B CA  
14216 C C   . GLU B 750  ? 0.2784 0.2774 0.2236 0.0132  -0.0316 -0.0538 748  GLU B C   
14217 O O   . GLU B 750  ? 0.2783 0.2751 0.2187 0.0099  -0.0343 -0.0532 748  GLU B O   
14218 C CB  . GLU B 750  ? 0.2767 0.2593 0.2151 0.0187  -0.0359 -0.0599 748  GLU B CB  
14219 C CG  . GLU B 750  ? 0.2740 0.2464 0.2043 0.0144  -0.0416 -0.0602 748  GLU B CG  
14220 C CD  . GLU B 750  ? 0.3511 0.3118 0.2779 0.0140  -0.0460 -0.0614 748  GLU B CD  
14221 O OE1 . GLU B 750  ? 0.3430 0.3022 0.2718 0.0185  -0.0448 -0.0633 748  GLU B OE1 
14222 O OE2 . GLU B 750  ? 0.3888 0.3420 0.3109 0.0089  -0.0507 -0.0601 748  GLU B OE2 
14223 N N   . ALA B 751  ? 0.2780 0.2842 0.2315 0.0121  -0.0288 -0.0503 749  ALA B N   
14224 C CA  . ALA B 751  ? 0.3045 0.3169 0.2623 0.0074  -0.0284 -0.0458 749  ALA B CA  
14225 C C   . ALA B 751  ? 0.2614 0.2818 0.2200 0.0074  -0.0258 -0.0445 749  ALA B C   
14226 O O   . ALA B 751  ? 0.2937 0.3189 0.2549 0.0038  -0.0260 -0.0410 749  ALA B O   
14227 C CB  . ALA B 751  ? 0.2631 0.2805 0.2291 0.0070  -0.0260 -0.0430 749  ALA B CB  
14228 N N   . GLY B 752  ? 0.2736 0.2959 0.2301 0.0115  -0.0234 -0.0470 750  GLY B N   
14229 C CA  . GLY B 752  ? 0.2528 0.2820 0.2091 0.0115  -0.0212 -0.0457 750  GLY B CA  
14230 C C   . GLY B 752  ? 0.2536 0.2909 0.2152 0.0146  -0.0161 -0.0450 750  GLY B C   
14231 O O   . GLY B 752  ? 0.2527 0.2957 0.2138 0.0146  -0.0142 -0.0437 750  GLY B O   
14232 N N   . ILE B 753  ? 0.2468 0.2854 0.2135 0.0169  -0.0140 -0.0454 751  ILE B N   
14233 C CA  . ILE B 753  ? 0.2474 0.2935 0.2186 0.0197  -0.0095 -0.0449 751  ILE B CA  
14234 C C   . ILE B 753  ? 0.2220 0.2681 0.1878 0.0235  -0.0083 -0.0486 751  ILE B C   
14235 O O   . ILE B 753  ? 0.2490 0.2894 0.2111 0.0264  -0.0098 -0.0524 751  ILE B O   
14236 C CB  . ILE B 753  ? 0.2058 0.2530 0.1835 0.0211  -0.0079 -0.0447 751  ILE B CB  
14237 C CG1 . ILE B 753  ? 0.2693 0.3161 0.2517 0.0177  -0.0091 -0.0415 751  ILE B CG1 
14238 C CG2 . ILE B 753  ? 0.2392 0.2942 0.2214 0.0234  -0.0035 -0.0441 751  ILE B CG2 
14239 C CD1 . ILE B 753  ? 0.2590 0.3123 0.2450 0.0153  -0.0074 -0.0374 751  ILE B CD1 
14240 N N   . PRO B 754  ? 0.2317 0.2839 0.1964 0.0239  -0.0058 -0.0476 752  PRO B N   
14241 C CA  . PRO B 754  ? 0.2792 0.3323 0.2384 0.0276  -0.0044 -0.0510 752  PRO B CA  
14242 C C   . PRO B 754  ? 0.2668 0.3225 0.2292 0.0319  -0.0018 -0.0533 752  PRO B C   
14243 O O   . PRO B 754  ? 0.2595 0.3194 0.2295 0.0316  0.0003  -0.0513 752  PRO B O   
14244 C CB  . PRO B 754  ? 0.2952 0.3557 0.2541 0.0264  -0.0018 -0.0483 752  PRO B CB  
14245 C CG  . PRO B 754  ? 0.3175 0.3792 0.2804 0.0221  -0.0028 -0.0438 752  PRO B CG  
14246 C CD  . PRO B 754  ? 0.2414 0.3004 0.2101 0.0212  -0.0038 -0.0431 752  PRO B CD  
14247 N N   . ALA B 755  ? 0.2796 0.3330 0.2361 0.0361  -0.0019 -0.0578 753  ALA B N   
14248 C CA  . ALA B 755  ? 0.2811 0.3381 0.2407 0.0407  0.0006  -0.0603 753  ALA B CA  
14249 C C   . ALA B 755  ? 0.2777 0.3462 0.2442 0.0406  0.0055  -0.0573 753  ALA B C   
14250 O O   . ALA B 755  ? 0.2926 0.3649 0.2656 0.0421  0.0074  -0.0571 753  ALA B O   
14251 C CB  . ALA B 755  ? 0.3328 0.3868 0.2842 0.0456  0.0001  -0.0655 753  ALA B CB  
14252 N N   . SER B 756  ? 0.2953 0.3691 0.2605 0.0385  0.0075  -0.0547 754  SER B N   
14253 C CA  . SER B 756  ? 0.2584 0.3425 0.2295 0.0381  0.0119  -0.0516 754  SER B CA  
14254 C C   . SER B 756  ? 0.2734 0.3588 0.2526 0.0345  0.0122  -0.0473 754  SER B C   
14255 O O   . SER B 756  ? 0.3339 0.4266 0.3190 0.0341  0.0154  -0.0449 754  SER B O   
14256 C CB  . SER B 756  ? 0.3372 0.4259 0.3038 0.0369  0.0137  -0.0499 754  SER B CB  
14257 O OG  . SER B 756  ? 0.3672 0.4523 0.3325 0.0328  0.0113  -0.0469 754  SER B OG  
14258 N N   . ALA B 757  ? 0.2617 0.3405 0.2411 0.0317  0.0089  -0.0462 755  ALA B N   
14259 C CA  . ALA B 757  ? 0.2215 0.3009 0.2079 0.0288  0.0088  -0.0426 755  ALA B CA  
14260 C C   . ALA B 757  ? 0.2457 0.3225 0.2367 0.0302  0.0080  -0.0441 755  ALA B C   
14261 O O   . ALA B 757  ? 0.2286 0.3069 0.2258 0.0284  0.0085  -0.0415 755  ALA B O   
14262 C CB  . ALA B 757  ? 0.2460 0.3208 0.2308 0.0253  0.0059  -0.0404 755  ALA B CB  
14263 N N   . LEU B 758  ? 0.2054 0.2780 0.1932 0.0334  0.0065  -0.0482 756  LEU B N   
14264 C CA  . LEU B 758  ? 0.2392 0.3087 0.2309 0.0348  0.0053  -0.0496 756  LEU B CA  
14265 C C   . LEU B 758  ? 0.2666 0.3366 0.2562 0.0399  0.0058  -0.0540 756  LEU B C   
14266 O O   . LEU B 758  ? 0.2690 0.3324 0.2518 0.0421  0.0034  -0.0574 756  LEU B O   
14267 C CB  . LEU B 758  ? 0.2112 0.2718 0.2008 0.0326  0.0012  -0.0496 756  LEU B CB  
14268 C CG  . LEU B 758  ? 0.2153 0.2714 0.2074 0.0342  -0.0006 -0.0512 756  LEU B CG  
14269 C CD1 . LEU B 758  ? 0.2176 0.2798 0.2180 0.0337  0.0019  -0.0488 756  LEU B CD1 
14270 C CD2 . LEU B 758  ? 0.2899 0.3375 0.2794 0.0314  -0.0046 -0.0506 756  LEU B CD2 
14271 N N   . GLN B 759  ? 0.2395 0.3171 0.2349 0.0418  0.0089  -0.0538 757  GLN B N   
14272 C CA  . GLN B 759  ? 0.1963 0.2764 0.1911 0.0471  0.0098  -0.0577 757  GLN B CA  
14273 C C   . GLN B 759  ? 0.2037 0.2827 0.2042 0.0484  0.0088  -0.0583 757  GLN B C   
14274 O O   . GLN B 759  ? 0.2280 0.3092 0.2348 0.0453  0.0093  -0.0550 757  GLN B O   
14275 C CB  . GLN B 759  ? 0.2372 0.3287 0.2340 0.0484  0.0144  -0.0571 757  GLN B CB  
14276 C CG  . GLN B 759  ? 0.2142 0.3067 0.2044 0.0475  0.0154  -0.0567 757  GLN B CG  
14277 C CD  . GLN B 759  ? 0.2379 0.3421 0.2301 0.0480  0.0200  -0.0552 757  GLN B CD  
14278 O OE1 . GLN B 759  ? 0.2526 0.3611 0.2418 0.0523  0.0217  -0.0584 757  GLN B OE1 
14279 N NE2 . GLN B 759  ? 0.2376 0.3468 0.2344 0.0438  0.0219  -0.0505 757  GLN B NE2 
14280 N N   . LEU B 760  ? 0.2342 0.3088 0.2319 0.0529  0.0069  -0.0624 758  LEU B N   
14281 C CA  . LEU B 760  ? 0.2249 0.2981 0.2272 0.0549  0.0055  -0.0635 758  LEU B CA  
14282 C C   . LEU B 760  ? 0.1976 0.2806 0.2041 0.0596  0.0085  -0.0654 758  LEU B C   
14283 O O   . LEU B 760  ? 0.2199 0.3047 0.2220 0.0641  0.0093  -0.0688 758  LEU B O   
14284 C CB  . LEU B 760  ? 0.2118 0.2728 0.2081 0.0569  0.0008  -0.0666 758  LEU B CB  
14285 C CG  . LEU B 760  ? 0.2462 0.3046 0.2466 0.0589  -0.0011 -0.0675 758  LEU B CG  
14286 C CD1 . LEU B 760  ? 0.2116 0.2686 0.2167 0.0536  -0.0019 -0.0634 758  LEU B CD1 
14287 C CD2 . LEU B 760  ? 0.2230 0.2700 0.2163 0.0625  -0.0054 -0.0715 758  LEU B CD2 
14288 N N   . LEU B 761  ? 0.2524 0.3416 0.2672 0.0587  0.0098  -0.0634 759  LEU B N   
14289 C CA  . LEU B 761  ? 0.2257 0.3256 0.2458 0.0627  0.0126  -0.0648 759  LEU B CA  
14290 C C   . LEU B 761  ? 0.2158 0.3141 0.2408 0.0646  0.0104  -0.0658 759  LEU B C   
14291 O O   . LEU B 761  ? 0.2722 0.3752 0.3045 0.0617  0.0111  -0.0628 759  LEU B O   
14292 C CB  . LEU B 761  ? 0.2249 0.3368 0.2511 0.0593  0.0168  -0.0609 759  LEU B CB  
14293 C CG  . LEU B 761  ? 0.2550 0.3701 0.2773 0.0568  0.0194  -0.0591 759  LEU B CG  
14294 C CD1 . LEU B 761  ? 0.2832 0.3980 0.2980 0.0616  0.0199  -0.0632 759  LEU B CD1 
14295 C CD2 . LEU B 761  ? 0.2268 0.3343 0.2466 0.0515  0.0176  -0.0560 759  LEU B CD2 
14296 N N   . PRO B 762  ? 0.1958 0.2873 0.2168 0.0695  0.0075  -0.0698 760  PRO B N   
14297 C CA  . PRO B 762  ? 0.1966 0.2869 0.2222 0.0719  0.0053  -0.0708 760  PRO B CA  
14298 C C   . PRO B 762  ? 0.2497 0.3538 0.2832 0.0747  0.0084  -0.0709 760  PRO B C   
14299 O O   . PRO B 762  ? 0.2498 0.3637 0.2838 0.0769  0.0119  -0.0718 760  PRO B O   
14300 C CB  . PRO B 762  ? 0.2589 0.3385 0.2769 0.0770  0.0015  -0.0753 760  PRO B CB  
14301 C CG  . PRO B 762  ? 0.2502 0.3233 0.2595 0.0760  0.0010  -0.0762 760  PRO B CG  
14302 C CD  . PRO B 762  ? 0.2489 0.3331 0.2606 0.0734  0.0058  -0.0738 760  PRO B CD  
14303 N N   . GLY B 763  ? 0.2832 0.3885 0.3230 0.0746  0.0070  -0.0701 761  GLY B N   
14304 C CA  . GLY B 763  ? 0.2278 0.3459 0.2756 0.0773  0.0091  -0.0704 761  GLY B CA  
14305 C C   . GLY B 763  ? 0.2477 0.3682 0.3031 0.0730  0.0084  -0.0670 761  GLY B C   
14306 O O   . GLY B 763  ? 0.2801 0.3916 0.3342 0.0688  0.0061  -0.0649 761  GLY B O   
14307 N N   . ASP B 764  ? 0.3238 0.4570 0.3873 0.0740  0.0106  -0.0663 762  ASP B N   
14308 C CA  . ASP B 764  ? 0.3529 0.4889 0.4239 0.0705  0.0096  -0.0636 762  ASP B CA  
14309 C C   . ASP B 764  ? 0.3342 0.4765 0.4092 0.0638  0.0125  -0.0590 762  ASP B C   
14310 O O   . ASP B 764  ? 0.2943 0.4355 0.3651 0.0614  0.0145  -0.0577 762  ASP B O   
14311 C CB  . ASP B 764  ? 0.3333 0.4791 0.4111 0.0753  0.0095  -0.0655 762  ASP B CB  
14312 C CG  . ASP B 764  ? 0.3867 0.5482 0.4686 0.0776  0.0139  -0.0658 762  ASP B CG  
14313 O OD1 . ASP B 764  ? 0.3465 0.5131 0.4281 0.0738  0.0173  -0.0634 762  ASP B OD1 
14314 O OD2 . ASP B 764  ? 0.4415 0.6107 0.5269 0.0834  0.0140  -0.0685 762  ASP B OD2 
14315 N N   . GLY B 765  ? 0.3012 0.4496 0.3839 0.0609  0.0125  -0.0565 763  GLY B N   
14316 C CA  . GLY B 765  ? 0.2999 0.4527 0.3861 0.0544  0.0146  -0.0522 763  GLY B CA  
14317 C C   . GLY B 765  ? 0.2683 0.4333 0.3565 0.0538  0.0190  -0.0509 763  GLY B C   
14318 O O   . GLY B 765  ? 0.3155 0.4820 0.4042 0.0484  0.0208  -0.0472 763  GLY B O   
14319 N N   . ARG B 766  ? 0.2690 0.4428 0.3582 0.0592  0.0208  -0.0537 764  ARG B N   
14320 C CA  . ARG B 766  ? 0.2572 0.4430 0.3475 0.0588  0.0253  -0.0525 764  ARG B CA  
14321 C C   . ARG B 766  ? 0.3206 0.4998 0.4024 0.0578  0.0265  -0.0524 764  ARG B C   
14322 O O   . ARG B 766  ? 0.2864 0.4720 0.3683 0.0543  0.0297  -0.0495 764  ARG B O   
14323 C CB  . ARG B 766  ? 0.3904 0.5871 0.4831 0.0656  0.0269  -0.0560 764  ARG B CB  
14324 N N   . VAL B 767  ? 0.2890 0.4553 0.3633 0.0604  0.0238  -0.0552 765  VAL B N   
14325 C CA  . VAL B 767  ? 0.2542 0.4135 0.3205 0.0590  0.0243  -0.0550 765  VAL B CA  
14326 C C   . VAL B 767  ? 0.2773 0.4314 0.3437 0.0520  0.0239  -0.0505 765  VAL B C   
14327 O O   . VAL B 767  ? 0.2551 0.4107 0.3188 0.0491  0.0261  -0.0482 765  VAL B O   
14328 C CB  . VAL B 767  ? 0.2560 0.4027 0.3144 0.0633  0.0211  -0.0591 765  VAL B CB  
14329 C CG1 . VAL B 767  ? 0.2303 0.3699 0.2804 0.0613  0.0213  -0.0587 765  VAL B CG1 
14330 C CG2 . VAL B 767  ? 0.2572 0.4084 0.3148 0.0708  0.0213  -0.0637 765  VAL B CG2 
14331 N N   . GLY B 768  ? 0.2316 0.3793 0.3007 0.0496  0.0210  -0.0494 766  GLY B N   
14332 C CA  . GLY B 768  ? 0.2769 0.4199 0.3462 0.0436  0.0206  -0.0454 766  GLY B CA  
14333 C C   . GLY B 768  ? 0.2803 0.4333 0.3547 0.0395  0.0236  -0.0415 766  GLY B C   
14334 O O   . GLY B 768  ? 0.2691 0.4203 0.3413 0.0355  0.0247  -0.0385 766  GLY B O   
14335 N N   . ALA B 769  ? 0.2942 0.4578 0.3756 0.0402  0.0248  -0.0414 767  ALA B N   
14336 C CA  . ALA B 769  ? 0.2989 0.4728 0.3856 0.0358  0.0276  -0.0375 767  ALA B CA  
14337 C C   . ALA B 769  ? 0.2751 0.4545 0.3579 0.0355  0.0312  -0.0364 767  ALA B C   
14338 O O   . ALA B 769  ? 0.2572 0.4379 0.3400 0.0305  0.0326  -0.0324 767  ALA B O   
14339 C CB  . ALA B 769  ? 0.2760 0.4618 0.3709 0.0373  0.0282  -0.0379 767  ALA B CB  
14340 N N   . ALA B 770  ? 0.2462 0.4283 0.3252 0.0409  0.0324  -0.0401 768  ALA B N   
14341 C CA  . ALA B 770  ? 0.2678 0.4551 0.3423 0.0411  0.0358  -0.0395 768  ALA B CA  
14342 C C   . ALA B 770  ? 0.3062 0.4829 0.3736 0.0381  0.0349  -0.0378 768  ALA B C   
14343 O O   . ALA B 770  ? 0.2750 0.4554 0.3402 0.0353  0.0373  -0.0350 768  ALA B O   
14344 C CB  . ALA B 770  ? 0.2428 0.4338 0.3138 0.0482  0.0369  -0.0444 768  ALA B CB  
14345 N N   . LEU B 771  ? 0.2286 0.3927 0.2925 0.0387  0.0314  -0.0394 769  LEU B N   
14346 C CA  . LEU B 771  ? 0.2679 0.4229 0.3257 0.0360  0.0304  -0.0378 769  LEU B CA  
14347 C C   . LEU B 771  ? 0.2688 0.4229 0.3298 0.0300  0.0304  -0.0328 769  LEU B C   
14348 O O   . LEU B 771  ? 0.2530 0.4066 0.3108 0.0271  0.0316  -0.0300 769  LEU B O   
14349 C CB  . LEU B 771  ? 0.2750 0.4176 0.3284 0.0380  0.0267  -0.0406 769  LEU B CB  
14350 C CG  . LEU B 771  ? 0.2269 0.3667 0.2748 0.0436  0.0259  -0.0455 769  LEU B CG  
14351 C CD1 . LEU B 771  ? 0.2206 0.3485 0.2658 0.0448  0.0218  -0.0476 769  LEU B CD1 
14352 C CD2 . LEU B 771  ? 0.2218 0.3614 0.2626 0.0439  0.0274  -0.0457 769  LEU B CD2 
14353 N N   . VAL B 772  ? 0.2513 0.4050 0.3183 0.0281  0.0288  -0.0318 770  VAL B N   
14354 C CA  . VAL B 772  ? 0.2795 0.4310 0.3490 0.0227  0.0283  -0.0274 770  VAL B CA  
14355 C C   . VAL B 772  ? 0.2866 0.4477 0.3585 0.0193  0.0315  -0.0237 770  VAL B C   
14356 O O   . VAL B 772  ? 0.2938 0.4521 0.3645 0.0151  0.0316  -0.0199 770  VAL B O   
14357 C CB  . VAL B 772  ? 0.2674 0.4165 0.3425 0.0218  0.0258  -0.0275 770  VAL B CB  
14358 C CG1 . VAL B 772  ? 0.2382 0.3871 0.3167 0.0162  0.0256  -0.0231 770  VAL B CG1 
14359 C CG2 . VAL B 772  ? 0.2498 0.3877 0.3216 0.0239  0.0225  -0.0301 770  VAL B CG2 
14360 N N   . ALA B 773  ? 0.2875 0.4603 0.3627 0.0211  0.0341  -0.0246 771  ALA B N   
14361 C CA  . ALA B 773  ? 0.2933 0.4768 0.3713 0.0177  0.0373  -0.0208 771  ALA B CA  
14362 C C   . ALA B 773  ? 0.3336 0.5196 0.4053 0.0180  0.0400  -0.0200 771  ALA B C   
14363 O O   . ALA B 773  ? 0.3245 0.5179 0.3973 0.0143  0.0425  -0.0162 771  ALA B O   
14364 C CB  . ALA B 773  ? 0.2926 0.4892 0.3773 0.0195  0.0391  -0.0220 771  ALA B CB  
14365 N N   . ALA B 774  ? 0.3123 0.4923 0.3773 0.0220  0.0394  -0.0234 772  ALA B N   
14366 C CA  . ALA B 774  ? 0.3043 0.4863 0.3627 0.0225  0.0416  -0.0230 772  ALA B CA  
14367 C C   . ALA B 774  ? 0.3077 0.4857 0.3637 0.0171  0.0416  -0.0181 772  ALA B C   
14368 O O   . ALA B 774  ? 0.3184 0.4870 0.3746 0.0147  0.0387  -0.0166 772  ALA B O   
14369 C CB  . ALA B 774  ? 0.3205 0.4947 0.3719 0.0273  0.0401  -0.0276 772  ALA B CB  
14370 N N   . ALA B 775  ? 0.3329 0.5182 0.3864 0.0156  0.0446  -0.0156 773  ALA B N   
14371 C CA  . ALA B 775  ? 0.3427 0.5256 0.3942 0.0103  0.0448  -0.0103 773  ALA B CA  
14372 C C   . ALA B 775  ? 0.3227 0.4934 0.3681 0.0103  0.0421  -0.0103 773  ALA B C   
14373 O O   . ALA B 775  ? 0.3409 0.5062 0.3861 0.0063  0.0407  -0.0064 773  ALA B O   
14374 C CB  . ALA B 775  ? 0.3633 0.5568 0.4124 0.0092  0.0487  -0.0079 773  ALA B CB  
14375 N N   . GLU B 776  ? 0.3113 0.4774 0.3515 0.0145  0.0411  -0.0145 774  GLU B N   
14376 C CA  . GLU B 776  ? 0.2787 0.4347 0.3132 0.0142  0.0386  -0.0142 774  GLU B CA  
14377 C C   . GLU B 776  ? 0.2648 0.4110 0.3013 0.0147  0.0350  -0.0157 774  GLU B C   
14378 O O   . GLU B 776  ? 0.2780 0.4164 0.3105 0.0144  0.0328  -0.0155 774  GLU B O   
14379 C CB  . GLU B 776  ? 0.3058 0.4615 0.3330 0.0179  0.0391  -0.0175 774  GLU B CB  
14380 C CG  . GLU B 776  ? 0.3315 0.4966 0.3553 0.0178  0.0427  -0.0163 774  GLU B CG  
14381 C CD  . GLU B 776  ? 0.4001 0.5753 0.4264 0.0212  0.0456  -0.0192 774  GLU B CD  
14382 O OE1 . GLU B 776  ? 0.4079 0.5832 0.4394 0.0232  0.0446  -0.0218 774  GLU B OE1 
14383 O OE2 . GLU B 776  ? 0.4439 0.6273 0.4669 0.0220  0.0487  -0.0190 774  GLU B OE2 
14384 N N   . THR B 777  ? 0.2637 0.4108 0.3061 0.0153  0.0343  -0.0172 775  THR B N   
14385 C CA  . THR B 777  ? 0.2975 0.4358 0.3415 0.0157  0.0310  -0.0185 775  THR B CA  
14386 C C   . THR B 777  ? 0.2788 0.4113 0.3236 0.0118  0.0295  -0.0146 775  THR B C   
14387 O O   . THR B 777  ? 0.2862 0.4219 0.3345 0.0085  0.0304  -0.0111 775  THR B O   
14388 C CB  . THR B 777  ? 0.2680 0.4094 0.3182 0.0171  0.0308  -0.0206 775  THR B CB  
14389 O OG1 . THR B 777  ? 0.2865 0.4314 0.3352 0.0217  0.0315  -0.0249 775  THR B OG1 
14390 C CG2 . THR B 777  ? 0.2655 0.3982 0.3177 0.0168  0.0275  -0.0213 775  THR B CG2 
14391 N N   . ALA B 778  ? 0.2445 0.3687 0.2859 0.0123  0.0271  -0.0150 776  ALA B N   
14392 C CA  . ALA B 778  ? 0.2508 0.3694 0.2918 0.0094  0.0257  -0.0115 776  ALA B CA  
14393 C C   . ALA B 778  ? 0.2687 0.3806 0.3125 0.0095  0.0230  -0.0122 776  ALA B C   
14394 O O   . ALA B 778  ? 0.2664 0.3734 0.3101 0.0077  0.0217  -0.0097 776  ALA B O   
14395 C CB  . ALA B 778  ? 0.2647 0.3800 0.2996 0.0097  0.0251  -0.0108 776  ALA B CB  
14396 N N   . GLY B 779  ? 0.2634 0.3750 0.3095 0.0117  0.0222  -0.0156 777  GLY B N   
14397 C CA  . GLY B 779  ? 0.2452 0.3509 0.2937 0.0118  0.0198  -0.0164 777  GLY B CA  
14398 C C   . GLY B 779  ? 0.2305 0.3370 0.2806 0.0145  0.0192  -0.0202 777  GLY B C   
14399 O O   . GLY B 779  ? 0.2101 0.3194 0.2580 0.0169  0.0201  -0.0227 777  GLY B O   
14400 N N   . VAL B 780  ? 0.2114 0.3149 0.2650 0.0143  0.0176  -0.0208 778  VAL B N   
14401 C CA  . VAL B 780  ? 0.2381 0.3416 0.2934 0.0169  0.0166  -0.0242 778  VAL B CA  
14402 C C   . VAL B 780  ? 0.1944 0.2903 0.2490 0.0172  0.0139  -0.0250 778  VAL B C   
14403 O O   . VAL B 780  ? 0.2091 0.3016 0.2649 0.0152  0.0129  -0.0230 778  VAL B O   
14404 C CB  . VAL B 780  ? 0.2047 0.3145 0.2660 0.0166  0.0174  -0.0242 778  VAL B CB  
14405 C CG1 . VAL B 780  ? 0.2027 0.3119 0.2654 0.0196  0.0159  -0.0277 778  VAL B CG1 
14406 C CG2 . VAL B 780  ? 0.1862 0.3051 0.2483 0.0163  0.0204  -0.0233 778  VAL B CG2 
14407 N N   . MET B 781  ? 0.1962 0.2890 0.2484 0.0197  0.0125  -0.0279 779  MET B N   
14408 C CA  . MET B 781  ? 0.2336 0.3200 0.2853 0.0200  0.0100  -0.0288 779  MET B CA  
14409 C C   . MET B 781  ? 0.2430 0.3302 0.2970 0.0222  0.0090  -0.0315 779  MET B C   
14410 O O   . MET B 781  ? 0.2215 0.3104 0.2741 0.0247  0.0093  -0.0339 779  MET B O   
14411 C CB  . MET B 781  ? 0.1834 0.2650 0.2298 0.0204  0.0088  -0.0294 779  MET B CB  
14412 C CG  . MET B 781  ? 0.2350 0.3168 0.2792 0.0187  0.0098  -0.0268 779  MET B CG  
14413 S SD  . MET B 781  ? 0.2617 0.3392 0.3001 0.0189  0.0082  -0.0275 779  MET B SD  
14414 C CE  . MET B 781  ? 0.2665 0.3391 0.3058 0.0180  0.0062  -0.0265 779  MET B CE  
14415 N N   . PHE B 782  ? 0.2353 0.3209 0.2926 0.0215  0.0077  -0.0312 780  PHE B N   
14416 C CA  . PHE B 782  ? 0.2410 0.3283 0.3013 0.0235  0.0067  -0.0334 780  PHE B CA  
14417 C C   . PHE B 782  ? 0.2510 0.3320 0.3109 0.0235  0.0040  -0.0340 780  PHE B C   
14418 O O   . PHE B 782  ? 0.2575 0.3358 0.3179 0.0215  0.0034  -0.0322 780  PHE B O   
14419 C CB  . PHE B 782  ? 0.2304 0.3250 0.2965 0.0225  0.0081  -0.0324 780  PHE B CB  
14420 C CG  . PHE B 782  ? 0.2404 0.3368 0.3104 0.0242  0.0066  -0.0342 780  PHE B CG  
14421 C CD1 . PHE B 782  ? 0.2060 0.3065 0.2767 0.0277  0.0069  -0.0368 780  PHE B CD1 
14422 C CD2 . PHE B 782  ? 0.2401 0.3342 0.3129 0.0226  0.0048  -0.0335 780  PHE B CD2 
14423 C CE1 . PHE B 782  ? 0.2440 0.3466 0.3184 0.0296  0.0054  -0.0385 780  PHE B CE1 
14424 C CE2 . PHE B 782  ? 0.2597 0.3558 0.3361 0.0242  0.0032  -0.0351 780  PHE B CE2 
14425 C CZ  . PHE B 782  ? 0.2593 0.3597 0.3367 0.0276  0.0035  -0.0375 780  PHE B CZ  
14426 N N   . THR B 783  ? 0.2358 0.3144 0.2945 0.0260  0.0023  -0.0365 781  THR B N   
14427 C CA  . THR B 783  ? 0.2733 0.3468 0.3319 0.0262  -0.0003 -0.0371 781  THR B CA  
14428 C C   . THR B 783  ? 0.2865 0.3625 0.3482 0.0287  -0.0014 -0.0392 781  THR B C   
14429 O O   . THR B 783  ? 0.2813 0.3585 0.3418 0.0315  -0.0014 -0.0413 781  THR B O   
14430 C CB  . THR B 783  ? 0.2726 0.3390 0.3256 0.0264  -0.0020 -0.0376 781  THR B CB  
14431 O OG1 . THR B 783  ? 0.2262 0.2917 0.2769 0.0243  -0.0008 -0.0355 781  THR B OG1 
14432 C CG2 . THR B 783  ? 0.3146 0.3760 0.3671 0.0261  -0.0044 -0.0377 781  THR B CG2 
14433 N N   . GLY B 784  ? 0.2580 0.3352 0.3238 0.0279  -0.0024 -0.0387 782  GLY B N   
14434 C CA  . GLY B 784  ? 0.2574 0.3382 0.3270 0.0302  -0.0036 -0.0405 782  GLY B CA  
14435 C C   . GLY B 784  ? 0.2373 0.3207 0.3119 0.0281  -0.0043 -0.0392 782  GLY B C   
14436 O O   . GLY B 784  ? 0.2864 0.3657 0.3600 0.0255  -0.0048 -0.0376 782  GLY B O   
14437 N N   . SER B 785  ? 0.2670 0.3572 0.3468 0.0294  -0.0043 -0.0400 783  SER B N   
14438 C CA  . SER B 785  ? 0.3007 0.3934 0.3854 0.0274  -0.0057 -0.0391 783  SER B CA  
14439 C C   . SER B 785  ? 0.3303 0.4253 0.4171 0.0232  -0.0040 -0.0363 783  SER B C   
14440 O O   . SER B 785  ? 0.2478 0.3463 0.3343 0.0223  -0.0014 -0.0351 783  SER B O   
14441 C CB  . SER B 785  ? 0.2982 0.3992 0.3887 0.0297  -0.0060 -0.0404 783  SER B CB  
14442 O OG  . SER B 785  ? 0.3324 0.4426 0.4262 0.0296  -0.0030 -0.0398 783  SER B OG  
14443 N N   . THR B 786  ? 0.3053 0.3978 0.3936 0.0207  -0.0059 -0.0352 784  THR B N   
14444 C CA  . THR B 786  ? 0.3363 0.4305 0.4269 0.0167  -0.0050 -0.0326 784  THR B CA  
14445 C C   . THR B 786  ? 0.3272 0.4321 0.4236 0.0157  -0.0031 -0.0316 784  THR B C   
14446 O O   . THR B 786  ? 0.3245 0.4319 0.4213 0.0130  -0.0010 -0.0293 784  THR B O   
14447 C CB  . THR B 786  ? 0.3748 0.4647 0.4663 0.0146  -0.0079 -0.0322 784  THR B CB  
14448 O OG1 . THR B 786  ? 0.3893 0.4701 0.4751 0.0155  -0.0094 -0.0329 784  THR B OG1 
14449 C CG2 . THR B 786  ? 0.4021 0.4930 0.4956 0.0103  -0.0075 -0.0295 784  THR B CG2 
14450 N N   . GLU B 787  ? 0.2762 0.3878 0.3772 0.0177  -0.0037 -0.0331 785  GLU B N   
14451 C CA  . GLU B 787  ? 0.2985 0.4217 0.4058 0.0167  -0.0019 -0.0321 785  GLU B CA  
14452 C C   . GLU B 787  ? 0.3462 0.4741 0.4520 0.0176  0.0018  -0.0316 785  GLU B C   
14453 O O   . GLU B 787  ? 0.2842 0.4185 0.3928 0.0145  0.0039  -0.0291 785  GLU B O   
14454 C CB  . GLU B 787  ? 0.4015 0.5314 0.5137 0.0199  -0.0033 -0.0343 785  GLU B CB  
14455 N N   . VAL B 788  ? 0.2774 0.4020 0.3785 0.0215  0.0024  -0.0339 786  VAL B N   
14456 C CA  . VAL B 788  ? 0.2879 0.4165 0.3869 0.0227  0.0057  -0.0338 786  VAL B CA  
14457 C C   . VAL B 788  ? 0.2713 0.3952 0.3665 0.0191  0.0069  -0.0311 786  VAL B C   
14458 O O   . VAL B 788  ? 0.2991 0.4285 0.3945 0.0179  0.0097  -0.0295 786  VAL B O   
14459 C CB  . VAL B 788  ? 0.3128 0.4380 0.4072 0.0278  0.0054  -0.0371 786  VAL B CB  
14460 C CG1 . VAL B 788  ? 0.2784 0.4062 0.3694 0.0288  0.0084  -0.0372 786  VAL B CG1 
14461 C CG2 . VAL B 788  ? 0.3217 0.4523 0.4200 0.0318  0.0042  -0.0397 786  VAL B CG2 
14462 N N   . ALA B 789  ? 0.2426 0.3568 0.3343 0.0177  0.0050  -0.0306 787  ALA B N   
14463 C CA  . ALA B 789  ? 0.2668 0.3766 0.3551 0.0148  0.0059  -0.0281 787  ALA B CA  
14464 C C   . ALA B 789  ? 0.2944 0.4091 0.3867 0.0105  0.0069  -0.0248 787  ALA B C   
14465 O O   . ALA B 789  ? 0.2333 0.3488 0.3238 0.0085  0.0089  -0.0226 787  ALA B O   
14466 C CB  . ALA B 789  ? 0.2709 0.3702 0.3552 0.0144  0.0036  -0.0282 787  ALA B CB  
14467 N N   . ARG B 790  ? 0.2746 0.3923 0.3720 0.0087  0.0053  -0.0244 788  ARG B N   
14468 C CA  . ARG B 790  ? 0.2845 0.4068 0.3858 0.0040  0.0058  -0.0211 788  ARG B CA  
14469 C C   . ARG B 790  ? 0.2495 0.3834 0.3540 0.0037  0.0091  -0.0201 788  ARG B C   
14470 O O   . ARG B 790  ? 0.3174 0.4543 0.4225 0.0000  0.0107  -0.0169 788  ARG B O   
14471 C CB  . ARG B 790  ? 0.2898 0.4127 0.3959 0.0019  0.0030  -0.0210 788  ARG B CB  
14472 C CG  . ARG B 790  ? 0.3337 0.4454 0.4363 0.0021  -0.0003 -0.0221 788  ARG B CG  
14473 C CD  . ARG B 790  ? 0.4190 0.5213 0.5161 0.0004  -0.0005 -0.0205 788  ARG B CD  
14474 N NE  . ARG B 790  ? 0.4649 0.5686 0.5636 -0.0043 0.0000  -0.0170 788  ARG B NE  
14475 C CZ  . ARG B 790  ? 0.4126 0.5116 0.5120 -0.0079 -0.0026 -0.0155 788  ARG B CZ  
14476 N NH1 . ARG B 790  ? 0.3777 0.4705 0.4763 -0.0072 -0.0057 -0.0173 788  ARG B NH1 
14477 N NH2 . ARG B 790  ? 0.4103 0.5102 0.5106 -0.0123 -0.0022 -0.0121 788  ARG B NH2 
14478 N N   . LEU B 791  ? 0.2170 0.3577 0.3234 0.0078  0.0101  -0.0228 789  LEU B N   
14479 C CA  . LEU B 791  ? 0.2423 0.3945 0.3512 0.0084  0.0135  -0.0222 789  LEU B CA  
14480 C C   . LEU B 791  ? 0.2631 0.4132 0.3662 0.0086  0.0160  -0.0213 789  LEU B C   
14481 O O   . LEU B 791  ? 0.2592 0.4159 0.3632 0.0060  0.0186  -0.0186 789  LEU B O   
14482 C CB  . LEU B 791  ? 0.2921 0.4509 0.4034 0.0137  0.0138  -0.0258 789  LEU B CB  
14483 C CG  . LEU B 791  ? 0.3125 0.4768 0.4305 0.0142  0.0118  -0.0268 789  LEU B CG  
14484 C CD1 . LEU B 791  ? 0.3355 0.5048 0.4543 0.0205  0.0121  -0.0306 789  LEU B CD1 
14485 C CD2 . LEU B 791  ? 0.2664 0.4420 0.3914 0.0095  0.0130  -0.0234 789  LEU B CD2 
14486 N N   . ILE B 792  ? 0.2294 0.3703 0.3264 0.0114  0.0152  -0.0233 790  ILE B N   
14487 C CA  . ILE B 792  ? 0.2337 0.3717 0.3250 0.0115  0.0171  -0.0224 790  ILE B CA  
14488 C C   . ILE B 792  ? 0.2447 0.3796 0.3351 0.0065  0.0172  -0.0183 790  ILE B C   
14489 O O   . ILE B 792  ? 0.2701 0.4084 0.3587 0.0049  0.0195  -0.0161 790  ILE B O   
14490 C CB  . ILE B 792  ? 0.1905 0.3189 0.2758 0.0147  0.0156  -0.0251 790  ILE B CB  
14491 C CG1 . ILE B 792  ? 0.2064 0.3374 0.2914 0.0198  0.0155  -0.0290 790  ILE B CG1 
14492 C CG2 . ILE B 792  ? 0.2103 0.3348 0.2897 0.0140  0.0169  -0.0237 790  ILE B CG2 
14493 C CD1 . ILE B 792  ? 0.2417 0.3626 0.3215 0.0223  0.0132  -0.0314 790  ILE B CD1 
14494 N N   . GLN B 793  ? 0.2588 0.3865 0.3498 0.0042  0.0145  -0.0174 791  GLN B N   
14495 C CA  . GLN B 793  ? 0.2808 0.4040 0.3705 -0.0001 0.0140  -0.0137 791  GLN B CA  
14496 C C   . GLN B 793  ? 0.2578 0.3897 0.3515 -0.0042 0.0157  -0.0103 791  GLN B C   
14497 O O   . GLN B 793  ? 0.2828 0.4140 0.3741 -0.0070 0.0169  -0.0072 791  GLN B O   
14498 C CB  . GLN B 793  ? 0.3074 0.4219 0.3972 -0.0013 0.0106  -0.0139 791  GLN B CB  
14499 C CG  . GLN B 793  ? 0.2881 0.3972 0.3768 -0.0056 0.0095  -0.0104 791  GLN B CG  
14500 C CD  . GLN B 793  ? 0.3429 0.4463 0.4334 -0.0074 0.0062  -0.0105 791  GLN B CD  
14501 O OE1 . GLN B 793  ? 0.3103 0.4181 0.4054 -0.0075 0.0051  -0.0118 791  GLN B OE1 
14502 N NE2 . GLN B 793  ? 0.3888 0.4823 0.4753 -0.0084 0.0043  -0.0095 791  GLN B NE2 
14503 N N   . ALA B 794  ? 0.2697 0.4102 0.3697 -0.0049 0.0158  -0.0107 792  ALA B N   
14504 C CA  . ALA B 794  ? 0.3170 0.4671 0.4214 -0.0092 0.0175  -0.0072 792  ALA B CA  
14505 C C   . ALA B 794  ? 0.3165 0.4751 0.4194 -0.0080 0.0215  -0.0066 792  ALA B C   
14506 O O   . ALA B 794  ? 0.3010 0.4634 0.4038 -0.0121 0.0231  -0.0027 792  ALA B O   
14507 C CB  . ALA B 794  ? 0.2706 0.4293 0.3825 -0.0098 0.0167  -0.0080 792  ALA B CB  
14508 N N   . GLN B 795  ? 0.2766 0.4379 0.3777 -0.0026 0.0229  -0.0103 793  GLN B N   
14509 C CA  . GLN B 795  ? 0.2977 0.4662 0.3964 -0.0010 0.0265  -0.0101 793  GLN B CA  
14510 C C   . GLN B 795  ? 0.3014 0.4630 0.3936 -0.0028 0.0270  -0.0077 793  GLN B C   
14511 O O   . GLN B 795  ? 0.2770 0.4445 0.3683 -0.0052 0.0296  -0.0048 793  GLN B O   
14512 C CB  . GLN B 795  ? 0.3168 0.4870 0.4138 0.0055  0.0271  -0.0150 793  GLN B CB  
14513 C CG  . GLN B 795  ? 0.3705 0.5473 0.4639 0.0079  0.0306  -0.0156 793  GLN B CG  
14514 C CD  . GLN B 795  ? 0.4081 0.6002 0.5068 0.0070  0.0338  -0.0142 793  GLN B CD  
14515 O OE1 . GLN B 795  ? 0.4935 0.6930 0.5980 0.0089  0.0337  -0.0160 793  GLN B OE1 
14516 N NE2 . GLN B 795  ? 0.4239 0.6212 0.5208 0.0040  0.0366  -0.0108 793  GLN B NE2 
14517 N N   . LEU B 796  ? 0.2532 0.4025 0.3409 -0.0018 0.0246  -0.0087 794  LEU B N   
14518 C CA  . LEU B 796  ? 0.2704 0.4130 0.3521 -0.0029 0.0247  -0.0066 794  LEU B CA  
14519 C C   . LEU B 796  ? 0.2994 0.4401 0.3816 -0.0085 0.0242  -0.0018 794  LEU B C   
14520 O O   . LEU B 796  ? 0.3414 0.4812 0.4197 -0.0101 0.0254  0.0010  794  LEU B O   
14521 C CB  . LEU B 796  ? 0.2762 0.4073 0.3538 -0.0004 0.0222  -0.0089 794  LEU B CB  
14522 C CG  . LEU B 796  ? 0.2642 0.3944 0.3393 0.0047  0.0222  -0.0132 794  LEU B CG  
14523 C CD1 . LEU B 796  ? 0.2378 0.3572 0.3094 0.0061  0.0195  -0.0146 794  LEU B CD1 
14524 C CD2 . LEU B 796  ? 0.2507 0.3855 0.3217 0.0063  0.0249  -0.0135 794  LEU B CD2 
14525 N N   . ALA B 797  ? 0.3051 0.4448 0.3919 -0.0116 0.0222  -0.0006 795  ALA B N   
14526 C CA  . ALA B 797  ? 0.3436 0.4794 0.4304 -0.0170 0.0210  0.0040  795  ALA B CA  
14527 C C   . ALA B 797  ? 0.3518 0.4972 0.4399 -0.0209 0.0238  0.0079  795  ALA B C   
14528 O O   . ALA B 797  ? 0.3692 0.5110 0.4559 -0.0256 0.0229  0.0122  795  ALA B O   
14529 C CB  . ALA B 797  ? 0.3289 0.4617 0.4202 -0.0195 0.0179  0.0041  795  ALA B CB  
14530 N N   . ASP B 798  ? 0.3154 0.4729 0.4059 -0.0190 0.0269  0.0066  796  ASP B N   
14531 C CA  . ASP B 798  ? 0.3671 0.5348 0.4583 -0.0223 0.0301  0.0103  796  ASP B CA  
14532 C C   . ASP B 798  ? 0.3614 0.5263 0.4456 -0.0218 0.0317  0.0119  796  ASP B C   
14533 O O   . ASP B 798  ? 0.4129 0.5826 0.4961 -0.0257 0.0335  0.0162  796  ASP B O   
14534 C CB  . ASP B 798  ? 0.3956 0.5778 0.4915 -0.0197 0.0331  0.0080  796  ASP B CB  
14535 C CG  . ASP B 798  ? 0.4054 0.6004 0.5055 -0.0246 0.0356  0.0123  796  ASP B CG  
14536 O OD1 . ASP B 798  ? 0.5337 0.7298 0.6388 -0.0297 0.0339  0.0152  796  ASP B OD1 
14537 O OD2 . ASP B 798  ? 0.4645 0.6685 0.5628 -0.0235 0.0393  0.0129  796  ASP B OD2 
14538 N N   . ARG B 799  ? 0.3481 0.5055 0.4272 -0.0172 0.0310  0.0087  797  ARG B N   
14539 C CA  . ARG B 799  ? 0.3412 0.4967 0.4136 -0.0160 0.0325  0.0095  797  ARG B CA  
14540 C C   . ARG B 799  ? 0.3479 0.4902 0.4156 -0.0168 0.0296  0.0110  797  ARG B C   
14541 O O   . ARG B 799  ? 0.3414 0.4754 0.4104 -0.0167 0.0266  0.0101  797  ARG B O   
14542 C CB  . ARG B 799  ? 0.3858 0.5438 0.4555 -0.0100 0.0339  0.0046  797  ARG B CB  
14543 C CG  . ARG B 799  ? 0.4205 0.5913 0.4942 -0.0078 0.0367  0.0024  797  ARG B CG  
14544 C CD  . ARG B 799  ? 0.4450 0.6182 0.5140 -0.0024 0.0385  -0.0016 797  ARG B CD  
14545 N NE  . ARG B 799  ? 0.4688 0.6361 0.5376 0.0023  0.0364  -0.0066 797  ARG B NE  
14546 C CZ  . ARG B 799  ? 0.4549 0.6118 0.5185 0.0043  0.0343  -0.0083 797  ARG B CZ  
14547 N NH1 . ARG B 799  ? 0.3830 0.5345 0.4417 0.0024  0.0339  -0.0056 797  ARG B NH1 
14548 N NH2 . ARG B 799  ? 0.4546 0.6071 0.5182 0.0082  0.0325  -0.0125 797  ARG B NH2 
14549 N N   . LEU B 800  ? 0.3675 0.5083 0.4296 -0.0173 0.0305  0.0133  798  LEU B N   
14550 C CA  . LEU B 800  ? 0.3289 0.4585 0.3859 -0.0167 0.0282  0.0143  798  LEU B CA  
14551 C C   . LEU B 800  ? 0.3726 0.5027 0.4243 -0.0128 0.0294  0.0120  798  LEU B C   
14552 O O   . LEU B 800  ? 0.3477 0.4865 0.3986 -0.0115 0.0323  0.0109  798  LEU B O   
14553 C CB  . LEU B 800  ? 0.3553 0.4812 0.4102 -0.0216 0.0274  0.0199  798  LEU B CB  
14554 C CG  . LEU B 800  ? 0.3157 0.4376 0.3744 -0.0259 0.0251  0.0225  798  LEU B CG  
14555 C CD1 . LEU B 800  ? 0.3579 0.4755 0.4132 -0.0306 0.0243  0.0282  798  LEU B CD1 
14556 C CD2 . LEU B 800  ? 0.2880 0.3998 0.3473 -0.0236 0.0218  0.0197  798  LEU B CD2 
14557 N N   . SER B 801  ? 0.3543 0.4753 0.4024 -0.0107 0.0271  0.0112  799  SER B N   
14558 C CA  . SER B 801  ? 0.3810 0.5012 0.4239 -0.0075 0.0275  0.0093  799  SER B CA  
14559 C C   . SER B 801  ? 0.4322 0.5554 0.4705 -0.0094 0.0292  0.0130  799  SER B C   
14560 O O   . SER B 801  ? 0.3990 0.5231 0.4379 -0.0134 0.0295  0.0173  799  SER B O   
14561 C CB  . SER B 801  ? 0.4135 0.5239 0.4543 -0.0055 0.0246  0.0082  799  SER B CB  
14562 O OG  . SER B 801  ? 0.3871 0.4917 0.4253 -0.0076 0.0231  0.0122  799  SER B OG  
14563 N N   . PRO B 802  ? 0.4672 0.5917 0.5005 -0.0069 0.0300  0.0114  800  PRO B N   
14564 C CA  . PRO B 802  ? 0.5069 0.6328 0.5349 -0.0086 0.0310  0.0151  800  PRO B CA  
14565 C C   . PRO B 802  ? 0.5054 0.6236 0.5319 -0.0113 0.0286  0.0196  800  PRO B C   
14566 O O   . PRO B 802  ? 0.5224 0.6422 0.5467 -0.0145 0.0295  0.0240  800  PRO B O   
14567 C CB  . PRO B 802  ? 0.4819 0.6072 0.5048 -0.0049 0.0308  0.0120  800  PRO B CB  
14568 C CG  . PRO B 802  ? 0.4933 0.6214 0.5190 -0.0017 0.0314  0.0068  800  PRO B CG  
14569 C CD  . PRO B 802  ? 0.4446 0.5700 0.4767 -0.0026 0.0301  0.0064  800  PRO B CD  
14570 N N   . ALA B 803  ? 0.4623 0.5721 0.4900 -0.0099 0.0257  0.0186  801  ALA B N   
14571 C CA  . ALA B 803  ? 0.4477 0.5493 0.4738 -0.0116 0.0231  0.0223  801  ALA B CA  
14572 C C   . ALA B 803  ? 0.4514 0.5503 0.4813 -0.0151 0.0222  0.0248  801  ALA B C   
14573 O O   . ALA B 803  ? 0.4665 0.5572 0.4951 -0.0162 0.0197  0.0275  801  ALA B O   
14574 C CB  . ALA B 803  ? 0.4372 0.5314 0.4625 -0.0081 0.0204  0.0200  801  ALA B CB  
14575 N N   . GLY B 804  ? 0.4231 0.5285 0.4577 -0.0168 0.0240  0.0239  802  GLY B N   
14576 C CA  . GLY B 804  ? 0.4107 0.5139 0.4491 -0.0207 0.0229  0.0263  802  GLY B CA  
14577 C C   . GLY B 804  ? 0.4135 0.5097 0.4553 -0.0194 0.0202  0.0238  802  GLY B C   
14578 O O   . GLY B 804  ? 0.3689 0.4590 0.4117 -0.0222 0.0180  0.0263  802  GLY B O   
14579 N N   . ARG B 805  ? 0.3472 0.4437 0.3902 -0.0152 0.0201  0.0191  803  ARG B N   
14580 C CA  . ARG B 805  ? 0.3667 0.4567 0.4122 -0.0136 0.0177  0.0165  803  ARG B CA  
14581 C C   . ARG B 805  ? 0.3097 0.4056 0.3602 -0.0125 0.0187  0.0128  803  ARG B C   
14582 O O   . ARG B 805  ? 0.3139 0.4181 0.3651 -0.0115 0.0213  0.0112  803  ARG B O   
14583 C CB  . ARG B 805  ? 0.3418 0.4257 0.3842 -0.0095 0.0161  0.0144  803  ARG B CB  
14584 C CG  . ARG B 805  ? 0.3905 0.4680 0.4283 -0.0097 0.0145  0.0176  803  ARG B CG  
14585 C CD  . ARG B 805  ? 0.4627 0.5349 0.4986 -0.0056 0.0128  0.0154  803  ARG B CD  
14586 N NE  . ARG B 805  ? 0.5392 0.6084 0.5705 -0.0049 0.0119  0.0180  803  ARG B NE  
14587 C CZ  . ARG B 805  ? 0.5393 0.6123 0.5677 -0.0033 0.0129  0.0176  803  ARG B CZ  
14588 N NH1 . ARG B 805  ? 0.4651 0.5443 0.4943 -0.0020 0.0147  0.0145  803  ARG B NH1 
14589 N NH2 . ARG B 805  ? 0.6212 0.6913 0.6454 -0.0028 0.0118  0.0204  803  ARG B NH2 
14590 N N   . PRO B 806  ? 0.3220 0.4134 0.3756 -0.0124 0.0167  0.0112  804  PRO B N   
14591 C CA  . PRO B 806  ? 0.3403 0.4364 0.3982 -0.0108 0.0172  0.0074  804  PRO B CA  
14592 C C   . PRO B 806  ? 0.2822 0.3804 0.3382 -0.0064 0.0182  0.0037  804  PRO B C   
14593 O O   . PRO B 806  ? 0.3182 0.4114 0.3704 -0.0042 0.0173  0.0031  804  PRO B O   
14594 C CB  . PRO B 806  ? 0.3298 0.4183 0.3895 -0.0109 0.0142  0.0064  804  PRO B CB  
14595 C CG  . PRO B 806  ? 0.2911 0.3732 0.3490 -0.0143 0.0125  0.0105  804  PRO B CG  
14596 C CD  . PRO B 806  ? 0.3308 0.4124 0.3838 -0.0136 0.0136  0.0126  804  PRO B CD  
14597 N N   . ILE B 807  ? 0.2775 0.3832 0.3362 -0.0052 0.0199  0.0012  805  ILE B N   
14598 C CA  . ILE B 807  ? 0.2822 0.3892 0.3393 -0.0011 0.0205  -0.0028 805  ILE B CA  
14599 C C   . ILE B 807  ? 0.2993 0.4000 0.3574 0.0010  0.0180  -0.0055 805  ILE B C   
14600 O O   . ILE B 807  ? 0.2789 0.3796 0.3411 0.0003  0.0170  -0.0063 805  ILE B O   
14601 C CB  . ILE B 807  ? 0.3113 0.4278 0.3710 0.0000  0.0228  -0.0047 805  ILE B CB  
14602 C CG1 . ILE B 807  ? 0.3454 0.4695 0.4046 -0.0024 0.0255  -0.0017 805  ILE B CG1 
14603 C CG2 . ILE B 807  ? 0.2594 0.3759 0.3163 0.0042  0.0230  -0.0088 805  ILE B CG2 
14604 C CD1 . ILE B 807  ? 0.3512 0.4743 0.4043 -0.0016 0.0265  -0.0009 805  ILE B CD1 
14605 N N   . PRO B 808  ? 0.2877 0.3831 0.3421 0.0032  0.0169  -0.0068 806  PRO B N   
14606 C CA  . PRO B 808  ? 0.2929 0.3828 0.3479 0.0050  0.0147  -0.0092 806  PRO B CA  
14607 C C   . PRO B 808  ? 0.2937 0.3868 0.3514 0.0068  0.0148  -0.0126 806  PRO B C   
14608 O O   . PRO B 808  ? 0.2790 0.3770 0.3361 0.0083  0.0163  -0.0142 806  PRO B O   
14609 C CB  . PRO B 808  ? 0.3233 0.4095 0.3738 0.0069  0.0141  -0.0096 806  PRO B CB  
14610 C CG  . PRO B 808  ? 0.3338 0.4209 0.3816 0.0055  0.0150  -0.0065 806  PRO B CG  
14611 C CD  . PRO B 808  ? 0.2986 0.3927 0.3482 0.0037  0.0173  -0.0055 806  PRO B CD  
14612 N N   . LEU B 809  ? 0.2617 0.3517 0.3221 0.0068  0.0130  -0.0136 807  LEU B N   
14613 C CA  . LEU B 809  ? 0.2356 0.3268 0.2980 0.0089  0.0124  -0.0169 807  LEU B CA  
14614 C C   . LEU B 809  ? 0.2674 0.3516 0.3282 0.0102  0.0101  -0.0182 807  LEU B C   
14615 O O   . LEU B 809  ? 0.2622 0.3420 0.3236 0.0090  0.0087  -0.0171 807  LEU B O   
14616 C CB  . LEU B 809  ? 0.2645 0.3603 0.3323 0.0075  0.0124  -0.0168 807  LEU B CB  
14617 C CG  . LEU B 809  ? 0.2798 0.3759 0.3502 0.0095  0.0110  -0.0198 807  LEU B CG  
14618 C CD1 . LEU B 809  ? 0.2302 0.3297 0.2994 0.0128  0.0120  -0.0226 807  LEU B CD1 
14619 C CD2 . LEU B 809  ? 0.2781 0.3790 0.3542 0.0074  0.0108  -0.0190 807  LEU B CD2 
14620 N N   . ILE B 810  ? 0.2447 0.3276 0.3031 0.0126  0.0096  -0.0206 808  ILE B N   
14621 C CA  . ILE B 810  ? 0.2451 0.3224 0.3021 0.0138  0.0076  -0.0220 808  ILE B CA  
14622 C C   . ILE B 810  ? 0.2831 0.3615 0.3423 0.0152  0.0067  -0.0246 808  ILE B C   
14623 O O   . ILE B 810  ? 0.2406 0.3218 0.2993 0.0169  0.0073  -0.0264 808  ILE B O   
14624 C CB  . ILE B 810  ? 0.2716 0.3465 0.3241 0.0149  0.0074  -0.0224 808  ILE B CB  
14625 C CG1 . ILE B 810  ? 0.2994 0.3738 0.3500 0.0137  0.0081  -0.0197 808  ILE B CG1 
14626 C CG2 . ILE B 810  ? 0.3148 0.3849 0.3661 0.0158  0.0054  -0.0236 808  ILE B CG2 
14627 C CD1 . ILE B 810  ? 0.3362 0.4092 0.3829 0.0146  0.0078  -0.0199 808  ILE B CD1 
14628 N N   . ALA B 811  ? 0.2710 0.3469 0.3324 0.0148  0.0051  -0.0249 809  ALA B N   
14629 C CA  . ALA B 811  ? 0.3052 0.3822 0.3691 0.0160  0.0039  -0.0270 809  ALA B CA  
14630 C C   . ALA B 811  ? 0.3228 0.3939 0.3852 0.0166  0.0017  -0.0280 809  ALA B C   
14631 O O   . ALA B 811  ? 0.3080 0.3756 0.3701 0.0154  0.0009  -0.0268 809  ALA B O   
14632 C CB  . ALA B 811  ? 0.3100 0.3919 0.3790 0.0145  0.0043  -0.0263 809  ALA B CB  
14633 N N   . GLU B 812  ? 0.3067 0.3761 0.3675 0.0186  0.0005  -0.0301 810  GLU B N   
14634 C CA  . GLU B 812  ? 0.3420 0.4066 0.4015 0.0191  -0.0017 -0.0310 810  GLU B CA  
14635 C C   . GLU B 812  ? 0.3080 0.3745 0.3707 0.0203  -0.0030 -0.0327 810  GLU B C   
14636 O O   . GLU B 812  ? 0.2739 0.3431 0.3371 0.0221  -0.0028 -0.0342 810  GLU B O   
14637 C CB  . GLU B 812  ? 0.3485 0.4092 0.4033 0.0201  -0.0024 -0.0316 810  GLU B CB  
14638 C CG  . GLU B 812  ? 0.4203 0.4760 0.4730 0.0201  -0.0044 -0.0319 810  GLU B CG  
14639 C CD  . GLU B 812  ? 0.4883 0.5418 0.5401 0.0216  -0.0064 -0.0338 810  GLU B CD  
14640 O OE1 . GLU B 812  ? 0.4804 0.5321 0.5290 0.0223  -0.0069 -0.0345 810  GLU B OE1 
14641 O OE2 . GLU B 812  ? 0.5006 0.5537 0.5546 0.0219  -0.0078 -0.0345 810  GLU B OE2 
14642 N N   . THR B 813  ? 0.3197 0.3848 0.3844 0.0195  -0.0045 -0.0326 811  THR B N   
14643 C CA  . THR B 813  ? 0.2907 0.3590 0.3595 0.0202  -0.0057 -0.0338 811  THR B CA  
14644 C C   . THR B 813  ? 0.3744 0.4382 0.4423 0.0207  -0.0085 -0.0349 811  THR B C   
14645 O O   . THR B 813  ? 0.3749 0.4406 0.4464 0.0203  -0.0099 -0.0352 811  THR B O   
14646 C CB  . THR B 813  ? 0.3490 0.4223 0.4227 0.0180  -0.0049 -0.0324 811  THR B CB  
14647 O OG1 . THR B 813  ? 0.3226 0.3918 0.3953 0.0157  -0.0054 -0.0308 811  THR B OG1 
14648 C CG2 . THR B 813  ? 0.3476 0.4266 0.4224 0.0176  -0.0020 -0.0314 811  THR B CG2 
14649 N N   . GLY B 814  ? 0.3316 0.3899 0.3948 0.0215  -0.0095 -0.0353 812  GLY B N   
14650 C CA  . GLY B 814  ? 0.4240 0.4786 0.4859 0.0225  -0.0122 -0.0364 812  GLY B CA  
14651 C C   . GLY B 814  ? 0.3885 0.4400 0.4502 0.0211  -0.0135 -0.0359 812  GLY B C   
14652 O O   . GLY B 814  ? 0.3472 0.3982 0.4088 0.0195  -0.0125 -0.0346 812  GLY B O   
14653 N N   . GLY B 815  ? 0.3573 0.4062 0.4182 0.0219  -0.0161 -0.0370 813  GLY B N   
14654 C CA  . GLY B 815  ? 0.3302 0.3753 0.3894 0.0209  -0.0176 -0.0367 813  GLY B CA  
14655 C C   . GLY B 815  ? 0.3623 0.4057 0.4216 0.0217  -0.0206 -0.0380 813  GLY B C   
14656 O O   . GLY B 815  ? 0.4185 0.4630 0.4786 0.0234  -0.0217 -0.0390 813  GLY B O   
14657 N N   . GLN B 816  ? 0.3075 0.3477 0.3654 0.0208  -0.0221 -0.0380 814  GLN B N   
14658 C CA  . GLN B 816  ? 0.3007 0.3385 0.3577 0.0214  -0.0252 -0.0390 814  GLN B CA  
14659 C C   . GLN B 816  ? 0.2818 0.3138 0.3323 0.0215  -0.0257 -0.0389 814  GLN B C   
14660 O O   . GLN B 816  ? 0.3219 0.3511 0.3705 0.0208  -0.0265 -0.0390 814  GLN B O   
14661 C CB  . GLN B 816  ? 0.3649 0.4044 0.4260 0.0199  -0.0269 -0.0392 814  GLN B CB  
14662 C CG  . GLN B 816  ? 0.3905 0.4288 0.4517 0.0205  -0.0304 -0.0404 814  GLN B CG  
14663 C CD  . GLN B 816  ? 0.4187 0.4610 0.4832 0.0224  -0.0314 -0.0411 814  GLN B CD  
14664 O OE1 . GLN B 816  ? 0.4216 0.4628 0.4837 0.0242  -0.0308 -0.0413 814  GLN B OE1 
14665 N NE2 . GLN B 816  ? 0.4815 0.5287 0.5518 0.0220  -0.0331 -0.0415 814  GLN B NE2 
14666 N N   . ASN B 817  ? 0.2808 0.3112 0.3276 0.0225  -0.0251 -0.0386 815  ASN B N   
14667 C CA  . ASN B 817  ? 0.2595 0.2864 0.3006 0.0223  -0.0243 -0.0378 815  ASN B CA  
14668 C C   . ASN B 817  ? 0.2327 0.2557 0.2695 0.0227  -0.0267 -0.0383 815  ASN B C   
14669 O O   . ASN B 817  ? 0.2541 0.2761 0.2907 0.0234  -0.0290 -0.0388 815  ASN B O   
14670 C CB  . ASN B 817  ? 0.2438 0.2712 0.2829 0.0225  -0.0227 -0.0370 815  ASN B CB  
14671 C CG  . ASN B 817  ? 0.2612 0.2925 0.3041 0.0224  -0.0206 -0.0367 815  ASN B CG  
14672 O OD1 . ASN B 817  ? 0.2279 0.2610 0.2727 0.0216  -0.0189 -0.0362 815  ASN B OD1 
14673 N ND2 . ASN B 817  ? 0.2417 0.2741 0.2857 0.0232  -0.0209 -0.0371 815  ASN B ND2 
14674 N N   . ALA B 818  ? 0.2548 0.2754 0.2878 0.0226  -0.0263 -0.0381 816  ALA B N   
14675 C CA  . ALA B 818  ? 0.2903 0.3073 0.3186 0.0230  -0.0283 -0.0386 816  ALA B CA  
14676 C C   . ALA B 818  ? 0.2551 0.2710 0.2777 0.0231  -0.0269 -0.0376 816  ALA B C   
14677 O O   . ALA B 818  ? 0.2496 0.2675 0.2720 0.0230  -0.0242 -0.0366 816  ALA B O   
14678 C CB  . ALA B 818  ? 0.2542 0.2693 0.2823 0.0228  -0.0293 -0.0397 816  ALA B CB  
14679 N N   . MET B 819  ? 0.1982 0.2114 0.2161 0.0234  -0.0287 -0.0376 817  MET B N   
14680 C CA  . MET B 819  ? 0.2250 0.2375 0.2369 0.0234  -0.0276 -0.0366 817  MET B CA  
14681 C C   . MET B 819  ? 0.2594 0.2689 0.2670 0.0242  -0.0294 -0.0377 817  MET B C   
14682 O O   . MET B 819  ? 0.2325 0.2396 0.2400 0.0242  -0.0324 -0.0385 817  MET B O   
14683 C CB  . MET B 819  ? 0.2605 0.2727 0.2698 0.0225  -0.0279 -0.0350 817  MET B CB  
14684 C CG  . MET B 819  ? 0.2527 0.2649 0.2556 0.0220  -0.0270 -0.0335 817  MET B CG  
14685 S SD  . MET B 819  ? 0.3034 0.3136 0.3027 0.0203  -0.0286 -0.0314 817  MET B SD  
14686 C CE  . MET B 819  ? 0.2611 0.2743 0.2641 0.0191  -0.0264 -0.0303 817  MET B CE  
14687 N N   . ILE B 820  ? 0.2700 0.2796 0.2739 0.0250  -0.0277 -0.0378 818  ILE B N   
14688 C CA  . ILE B 820  ? 0.2236 0.2303 0.2223 0.0261  -0.0291 -0.0390 818  ILE B CA  
14689 C C   . ILE B 820  ? 0.2579 0.2654 0.2503 0.0261  -0.0281 -0.0376 818  ILE B C   
14690 O O   . ILE B 820  ? 0.2529 0.2640 0.2447 0.0260  -0.0252 -0.0362 818  ILE B O   
14691 C CB  . ILE B 820  ? 0.2305 0.2361 0.2288 0.0275  -0.0281 -0.0406 818  ILE B CB  
14692 C CG1 . ILE B 820  ? 0.2522 0.2566 0.2565 0.0268  -0.0295 -0.0417 818  ILE B CG1 
14693 C CG2 . ILE B 820  ? 0.2471 0.2493 0.2388 0.0291  -0.0294 -0.0421 818  ILE B CG2 
14694 C CD1 . ILE B 820  ? 0.2694 0.2712 0.2728 0.0280  -0.0292 -0.0431 818  ILE B CD1 
14695 N N   . VAL B 821  ? 0.2373 0.2421 0.2253 0.0260  -0.0305 -0.0378 819  VAL B N   
14696 C CA  . VAL B 821  ? 0.2307 0.2361 0.2122 0.0256  -0.0300 -0.0362 819  VAL B CA  
14697 C C   . VAL B 821  ? 0.3098 0.3129 0.2853 0.0273  -0.0310 -0.0378 819  VAL B C   
14698 O O   . VAL B 821  ? 0.2905 0.2895 0.2656 0.0276  -0.0341 -0.0394 819  VAL B O   
14699 C CB  . VAL B 821  ? 0.2640 0.2676 0.2447 0.0238  -0.0324 -0.0345 819  VAL B CB  
14700 C CG1 . VAL B 821  ? 0.2514 0.2556 0.2249 0.0229  -0.0320 -0.0324 819  VAL B CG1 
14701 C CG2 . VAL B 821  ? 0.2413 0.2466 0.2274 0.0226  -0.0316 -0.0333 819  VAL B CG2 
14702 N N   . ASP B 822  ? 0.3068 0.3125 0.2773 0.0284  -0.0284 -0.0374 820  ASP B N   
14703 C CA  . ASP B 822  ? 0.2947 0.2982 0.2584 0.0302  -0.0292 -0.0391 820  ASP B CA  
14704 C C   . ASP B 822  ? 0.3043 0.3087 0.2614 0.0292  -0.0295 -0.0370 820  ASP B C   
14705 O O   . ASP B 822  ? 0.2972 0.3035 0.2551 0.0267  -0.0293 -0.0342 820  ASP B O   
14706 C CB  . ASP B 822  ? 0.3101 0.3153 0.2722 0.0331  -0.0266 -0.0407 820  ASP B CB  
14707 C CG  . ASP B 822  ? 0.3219 0.3338 0.2820 0.0336  -0.0225 -0.0387 820  ASP B CG  
14708 O OD1 . ASP B 822  ? 0.3194 0.3346 0.2782 0.0314  -0.0218 -0.0359 820  ASP B OD1 
14709 O OD2 . ASP B 822  ? 0.3576 0.3716 0.3175 0.0363  -0.0202 -0.0399 820  ASP B OD2 
14710 N N   . SER B 823  ? 0.3231 0.3258 0.2732 0.0308  -0.0302 -0.0384 821  SER B N   
14711 C CA  . SER B 823  ? 0.3436 0.3468 0.2868 0.0297  -0.0308 -0.0364 821  SER B CA  
14712 C C   . SER B 823  ? 0.3759 0.3860 0.3162 0.0291  -0.0268 -0.0337 821  SER B C   
14713 O O   . SER B 823  ? 0.3787 0.3900 0.3130 0.0278  -0.0269 -0.0316 821  SER B O   
14714 C CB  . SER B 823  ? 0.3464 0.3457 0.2824 0.0317  -0.0328 -0.0389 821  SER B CB  
14715 O OG  . SER B 823  ? 0.3625 0.3638 0.2958 0.0350  -0.0302 -0.0410 821  SER B OG  
14716 N N   . SER B 824  ? 0.3558 0.3710 0.3003 0.0298  -0.0234 -0.0335 822  SER B N   
14717 C CA  . SER B 824  ? 0.3508 0.3736 0.2935 0.0288  -0.0198 -0.0306 822  SER B CA  
14718 C C   . SER B 824  ? 0.3648 0.3898 0.3124 0.0251  -0.0196 -0.0273 822  SER B C   
14719 O O   . SER B 824  ? 0.3567 0.3879 0.3029 0.0233  -0.0171 -0.0243 822  SER B O   
14720 C CB  . SER B 824  ? 0.3860 0.4141 0.3297 0.0322  -0.0162 -0.0320 822  SER B CB  
14721 O OG  . SER B 824  ? 0.3070 0.3350 0.2583 0.0322  -0.0157 -0.0326 822  SER B OG  
14722 N N   . ALA B 825  ? 0.3055 0.3259 0.2586 0.0239  -0.0220 -0.0278 823  ALA B N   
14723 C CA  . ALA B 825  ? 0.3201 0.3416 0.2775 0.0207  -0.0219 -0.0252 823  ALA B CA  
14724 C C   . ALA B 825  ? 0.3587 0.3785 0.3114 0.0174  -0.0238 -0.0221 823  ALA B C   
14725 O O   . ALA B 825  ? 0.3387 0.3547 0.2861 0.0175  -0.0261 -0.0223 823  ALA B O   
14726 C CB  . ALA B 825  ? 0.2802 0.2971 0.2442 0.0209  -0.0241 -0.0269 823  ALA B CB  
14727 N N   . LEU B 826  ? 0.3670 0.3892 0.3213 0.0142  -0.0231 -0.0191 824  LEU B N   
14728 C CA  . LEU B 826  ? 0.3670 0.3866 0.3168 0.0106  -0.0253 -0.0157 824  LEU B CA  
14729 C C   . LEU B 826  ? 0.3892 0.4008 0.3414 0.0100  -0.0294 -0.0165 824  LEU B C   
14730 O O   . LEU B 826  ? 0.3580 0.3687 0.3157 0.0096  -0.0295 -0.0168 824  LEU B O   
14731 C CB  . LEU B 826  ? 0.4253 0.4505 0.3754 0.0070  -0.0231 -0.0121 824  LEU B CB  
14732 C CG  . LEU B 826  ? 0.3874 0.4094 0.3323 0.0026  -0.0255 -0.0082 824  LEU B CG  
14733 C CD1 . LEU B 826  ? 0.4860 0.5078 0.4233 0.0027  -0.0261 -0.0073 824  LEU B CD1 
14734 C CD2 . LEU B 826  ? 0.4797 0.5075 0.4253 -0.0014 -0.0236 -0.0045 824  LEU B CD2 
14735 N N   . ALA B 827  ? 0.3487 0.3547 0.2966 0.0103  -0.0327 -0.0167 825  ALA B N   
14736 C CA  . ALA B 827  ? 0.3534 0.3522 0.3036 0.0108  -0.0367 -0.0179 825  ALA B CA  
14737 C C   . ALA B 827  ? 0.3822 0.3787 0.3349 0.0083  -0.0379 -0.0159 825  ALA B C   
14738 O O   . ALA B 827  ? 0.3719 0.3659 0.3301 0.0096  -0.0390 -0.0178 825  ALA B O   
14739 C CB  . ALA B 827  ? 0.3880 0.3815 0.3319 0.0108  -0.0403 -0.0174 825  ALA B CB  
14740 N N   . GLU B 828  ? 0.3626 0.3598 0.3109 0.0046  -0.0375 -0.0122 826  GLU B N   
14741 C CA  . GLU B 828  ? 0.3576 0.3510 0.3070 0.0020  -0.0393 -0.0103 826  GLU B CA  
14742 C C   . GLU B 828  ? 0.3580 0.3552 0.3142 0.0025  -0.0369 -0.0116 826  GLU B C   
14743 O O   . GLU B 828  ? 0.3498 0.3429 0.3091 0.0025  -0.0387 -0.0122 826  GLU B O   
14744 C CB  . GLU B 828  ? 0.3913 0.3849 0.3344 -0.0026 -0.0395 -0.0058 826  GLU B CB  
14745 C CG  . GLU B 828  ? 0.4601 0.4476 0.3958 -0.0038 -0.0431 -0.0038 826  GLU B CG  
14746 C CD  . GLU B 828  ? 0.4912 0.4825 0.4226 -0.0025 -0.0416 -0.0042 826  GLU B CD  
14747 O OE1 . GLU B 828  ? 0.4211 0.4199 0.3548 -0.0006 -0.0377 -0.0058 826  GLU B OE1 
14748 O OE2 . GLU B 828  ? 0.5180 0.5044 0.4432 -0.0031 -0.0446 -0.0029 826  GLU B OE2 
14749 N N   . GLN B 829  ? 0.3338 0.3388 0.2923 0.0032  -0.0328 -0.0121 827  GLN B N   
14750 C CA  . GLN B 829  ? 0.3307 0.3394 0.2955 0.0038  -0.0305 -0.0132 827  GLN B CA  
14751 C C   . GLN B 829  ? 0.3134 0.3198 0.2838 0.0075  -0.0312 -0.0170 827  GLN B C   
14752 O O   . GLN B 829  ? 0.3261 0.3315 0.3010 0.0078  -0.0314 -0.0179 827  GLN B O   
14753 C CB  . GLN B 829  ? 0.3677 0.3853 0.3331 0.0039  -0.0262 -0.0125 827  GLN B CB  
14754 C CG  . GLN B 829  ? 0.4083 0.4302 0.3798 0.0044  -0.0239 -0.0133 827  GLN B CG  
14755 C CD  . GLN B 829  ? 0.4726 0.5035 0.4445 0.0049  -0.0199 -0.0125 827  GLN B CD  
14756 O OE1 . GLN B 829  ? 0.4985 0.5327 0.4662 0.0053  -0.0186 -0.0118 827  GLN B OE1 
14757 N NE2 . GLN B 829  ? 0.4877 0.5230 0.4645 0.0050  -0.0178 -0.0127 827  GLN B NE2 
14758 N N   . VAL B 830  ? 0.3086 0.3142 0.2784 0.0102  -0.0317 -0.0191 828  VAL B N   
14759 C CA  . VAL B 830  ? 0.2756 0.2791 0.2505 0.0131  -0.0328 -0.0224 828  VAL B CA  
14760 C C   . VAL B 830  ? 0.2889 0.2868 0.2655 0.0129  -0.0362 -0.0227 828  VAL B C   
14761 O O   . VAL B 830  ? 0.2796 0.2777 0.2618 0.0142  -0.0361 -0.0244 828  VAL B O   
14762 C CB  . VAL B 830  ? 0.3009 0.3033 0.2738 0.0153  -0.0337 -0.0243 828  VAL B CB  
14763 C CG1 . VAL B 830  ? 0.3086 0.3084 0.2867 0.0175  -0.0358 -0.0272 828  VAL B CG1 
14764 C CG2 . VAL B 830  ? 0.2911 0.2987 0.2631 0.0164  -0.0303 -0.0249 828  VAL B CG2 
14765 N N   . VAL B 831  ? 0.2793 0.2721 0.2507 0.0117  -0.0393 -0.0211 829  VAL B N   
14766 C CA  . VAL B 831  ? 0.2797 0.2665 0.2523 0.0125  -0.0430 -0.0217 829  VAL B CA  
14767 C C   . VAL B 831  ? 0.2811 0.2671 0.2560 0.0113  -0.0427 -0.0211 829  VAL B C   
14768 O O   . VAL B 831  ? 0.3067 0.2913 0.2862 0.0133  -0.0437 -0.0232 829  VAL B O   
14769 C CB  . VAL B 831  ? 0.3187 0.2996 0.2845 0.0115  -0.0467 -0.0199 829  VAL B CB  
14770 C CG1 . VAL B 831  ? 0.3284 0.3024 0.2940 0.0117  -0.0505 -0.0197 829  VAL B CG1 
14771 C CG2 . VAL B 831  ? 0.3413 0.3217 0.3064 0.0138  -0.0482 -0.0217 829  VAL B CG2 
14772 N N   . GLY B 832  ? 0.2731 0.2605 0.2449 0.0080  -0.0412 -0.0184 830  GLY B N   
14773 C CA  . GLY B 832  ? 0.2989 0.2857 0.2727 0.0067  -0.0409 -0.0178 830  GLY B CA  
14774 C C   . GLY B 832  ? 0.3190 0.3108 0.2998 0.0088  -0.0381 -0.0203 830  GLY B C   
14775 O O   . GLY B 832  ? 0.2946 0.2842 0.2784 0.0098  -0.0390 -0.0216 830  GLY B O   
14776 N N   . ASP B 833  ? 0.2822 0.2801 0.2652 0.0096  -0.0349 -0.0210 831  ASP B N   
14777 C CA  . ASP B 833  ? 0.2390 0.2414 0.2283 0.0114  -0.0323 -0.0230 831  ASP B CA  
14778 C C   . ASP B 833  ? 0.2760 0.2768 0.2697 0.0145  -0.0337 -0.0259 831  ASP B C   
14779 O O   . ASP B 833  ? 0.2546 0.2575 0.2534 0.0156  -0.0325 -0.0273 831  ASP B O   
14780 C CB  . ASP B 833  ? 0.2195 0.2282 0.2094 0.0116  -0.0288 -0.0227 831  ASP B CB  
14781 C CG  . ASP B 833  ? 0.3084 0.3210 0.2957 0.0087  -0.0269 -0.0199 831  ASP B CG  
14782 O OD1 . ASP B 833  ? 0.3222 0.3328 0.3085 0.0063  -0.0280 -0.0183 831  ASP B OD1 
14783 O OD2 . ASP B 833  ? 0.3055 0.3231 0.2916 0.0088  -0.0244 -0.0192 831  ASP B OD2 
14784 N N   . VAL B 834  ? 0.2231 0.2206 0.2151 0.0157  -0.0362 -0.0267 832  VAL B N   
14785 C CA  . VAL B 834  ? 0.2122 0.2089 0.2088 0.0184  -0.0379 -0.0292 832  VAL B CA  
14786 C C   . VAL B 834  ? 0.2479 0.2406 0.2453 0.0193  -0.0404 -0.0297 832  VAL B C   
14787 O O   . VAL B 834  ? 0.2917 0.2862 0.2945 0.0212  -0.0402 -0.0316 832  VAL B O   
14788 C CB  . VAL B 834  ? 0.2082 0.2032 0.2027 0.0194  -0.0400 -0.0299 832  VAL B CB  
14789 C CG1 . VAL B 834  ? 0.2521 0.2461 0.2510 0.0219  -0.0425 -0.0321 832  VAL B CG1 
14790 C CG2 . VAL B 834  ? 0.2445 0.2434 0.2391 0.0196  -0.0374 -0.0304 832  VAL B CG2 
14791 N N   . ILE B 835  ? 0.2281 0.2153 0.2201 0.0180  -0.0430 -0.0280 833  ILE B N   
14792 C CA  . ILE B 835  ? 0.2560 0.2381 0.2478 0.0192  -0.0459 -0.0286 833  ILE B CA  
14793 C C   . ILE B 835  ? 0.2627 0.2470 0.2578 0.0191  -0.0437 -0.0293 833  ILE B C   
14794 O O   . ILE B 835  ? 0.2909 0.2751 0.2898 0.0217  -0.0444 -0.0314 833  ILE B O   
14795 C CB  . ILE B 835  ? 0.2897 0.2646 0.2740 0.0170  -0.0490 -0.0261 833  ILE B CB  
14796 C CG1 . ILE B 835  ? 0.3225 0.2945 0.3035 0.0177  -0.0518 -0.0257 833  ILE B CG1 
14797 C CG2 . ILE B 835  ? 0.3257 0.2943 0.3089 0.0181  -0.0519 -0.0266 833  ILE B CG2 
14798 C CD1 . ILE B 835  ? 0.4169 0.3847 0.3993 0.0212  -0.0556 -0.0276 833  ILE B CD1 
14799 N N   . THR B 836  ? 0.2908 0.2779 0.2847 0.0163  -0.0410 -0.0276 834  THR B N   
14800 C CA  . THR B 836  ? 0.2661 0.2557 0.2628 0.0160  -0.0390 -0.0281 834  THR B CA  
14801 C C   . THR B 836  ? 0.2638 0.2593 0.2673 0.0184  -0.0364 -0.0303 834  THR B C   
14802 O O   . THR B 836  ? 0.2775 0.2735 0.2842 0.0202  -0.0364 -0.0321 834  THR B O   
14803 C CB  . THR B 836  ? 0.3183 0.3104 0.3123 0.0124  -0.0368 -0.0254 834  THR B CB  
14804 O OG1 . THR B 836  ? 0.3614 0.3477 0.3491 0.0097  -0.0395 -0.0231 834  THR B OG1 
14805 C CG2 . THR B 836  ? 0.3351 0.3304 0.3321 0.0120  -0.0346 -0.0259 834  THR B CG2 
14806 N N   . SER B 837  ? 0.2342 0.2343 0.2398 0.0185  -0.0344 -0.0304 835  SER B N   
14807 C CA  . SER B 837  ? 0.2294 0.2347 0.2411 0.0201  -0.0320 -0.0321 835  SER B CA  
14808 C C   . SER B 837  ? 0.2487 0.2539 0.2645 0.0229  -0.0337 -0.0344 835  SER B C   
14809 O O   . SER B 837  ? 0.2295 0.2383 0.2501 0.0241  -0.0322 -0.0357 835  SER B O   
14810 C CB  . SER B 837  ? 0.1900 0.1988 0.2022 0.0197  -0.0301 -0.0318 835  SER B CB  
14811 O OG  . SER B 837  ? 0.2118 0.2223 0.2210 0.0177  -0.0281 -0.0299 835  SER B OG  
14812 N N   . ALA B 838  ? 0.2098 0.2116 0.2240 0.0240  -0.0368 -0.0348 836  ALA B N   
14813 C CA  . ALA B 838  ? 0.2237 0.2267 0.2425 0.0267  -0.0385 -0.0369 836  ALA B CA  
14814 C C   . ALA B 838  ? 0.2095 0.2096 0.2283 0.0288  -0.0404 -0.0379 836  ALA B C   
14815 O O   . ALA B 838  ? 0.2516 0.2551 0.2756 0.0313  -0.0403 -0.0398 836  ALA B O   
14816 C CB  . ALA B 838  ? 0.2085 0.2095 0.2259 0.0273  -0.0412 -0.0370 836  ALA B CB  
14817 N N   . PHE B 839  ? 0.2528 0.2466 0.2658 0.0280  -0.0423 -0.0368 837  PHE B N   
14818 C CA  . PHE B 839  ? 0.2703 0.2596 0.2822 0.0305  -0.0451 -0.0380 837  PHE B CA  
14819 C C   . PHE B 839  ? 0.2647 0.2510 0.2739 0.0296  -0.0446 -0.0377 837  PHE B C   
14820 O O   . PHE B 839  ? 0.3385 0.3213 0.3470 0.0323  -0.0466 -0.0393 837  PHE B O   
14821 C CB  . PHE B 839  ? 0.2827 0.2649 0.2894 0.0307  -0.0493 -0.0371 837  PHE B CB  
14822 C CG  . PHE B 839  ? 0.3022 0.2869 0.3110 0.0315  -0.0503 -0.0374 837  PHE B CG  
14823 C CD1 . PHE B 839  ? 0.3430 0.3332 0.3586 0.0343  -0.0502 -0.0395 837  PHE B CD1 
14824 C CD2 . PHE B 839  ? 0.2967 0.2784 0.3005 0.0293  -0.0515 -0.0354 837  PHE B CD2 
14825 C CE1 . PHE B 839  ? 0.3025 0.2948 0.3199 0.0346  -0.0515 -0.0398 837  PHE B CE1 
14826 C CE2 . PHE B 839  ? 0.2996 0.2832 0.3048 0.0300  -0.0526 -0.0359 837  PHE B CE2 
14827 C CZ  . PHE B 839  ? 0.3322 0.3208 0.3442 0.0326  -0.0528 -0.0381 837  PHE B CZ  
14828 N N   . ASP B 840  ? 0.3018 0.2895 0.3092 0.0263  -0.0421 -0.0359 838  ASP B N   
14829 C CA  . ASP B 840  ? 0.2972 0.2831 0.3027 0.0254  -0.0415 -0.0359 838  ASP B CA  
14830 C C   . ASP B 840  ? 0.2796 0.2699 0.2904 0.0285  -0.0399 -0.0385 838  ASP B C   
14831 O O   . ASP B 840  ? 0.2565 0.2538 0.2729 0.0295  -0.0374 -0.0393 838  ASP B O   
14832 C CB  . ASP B 840  ? 0.3431 0.3321 0.3474 0.0214  -0.0387 -0.0336 838  ASP B CB  
14833 C CG  . ASP B 840  ? 0.3579 0.3456 0.3604 0.0201  -0.0381 -0.0335 838  ASP B CG  
14834 O OD1 . ASP B 840  ? 0.3807 0.3730 0.3872 0.0216  -0.0358 -0.0350 838  ASP B OD1 
14835 O OD2 . ASP B 840  ? 0.4313 0.4134 0.4283 0.0175  -0.0401 -0.0317 838  ASP B OD2 
14836 N N   . SER B 841  ? 0.2817 0.2676 0.2900 0.0300  -0.0414 -0.0398 839  SER B N   
14837 C CA  . SER B 841  ? 0.2909 0.2807 0.3033 0.0334  -0.0400 -0.0424 839  SER B CA  
14838 C C   . SER B 841  ? 0.2698 0.2640 0.2876 0.0371  -0.0404 -0.0443 839  SER B C   
14839 O O   . SER B 841  ? 0.2822 0.2837 0.3057 0.0389  -0.0379 -0.0458 839  SER B O   
14840 C CB  . SER B 841  ? 0.3014 0.2981 0.3169 0.0315  -0.0358 -0.0420 839  SER B CB  
14841 O OG  . SER B 841  ? 0.3676 0.3607 0.3782 0.0281  -0.0358 -0.0402 839  SER B OG  
14842 N N   . ALA B 842  ? 0.2344 0.2242 0.2505 0.0382  -0.0437 -0.0441 840  ALA B N   
14843 C CA  . ALA B 842  ? 0.2344 0.2280 0.2554 0.0415  -0.0448 -0.0457 840  ALA B CA  
14844 C C   . ALA B 842  ? 0.2106 0.2137 0.2384 0.0404  -0.0415 -0.0455 840  ALA B C   
14845 O O   . ALA B 842  ? 0.2826 0.2920 0.3163 0.0431  -0.0409 -0.0471 840  ALA B O   
14846 C CB  . ALA B 842  ? 0.2536 0.2471 0.2761 0.0466  -0.0462 -0.0485 840  ALA B CB  
14847 N N   . GLY B 843  ? 0.2491 0.2531 0.2757 0.0366  -0.0394 -0.0434 841  GLY B N   
14848 C CA  . GLY B 843  ? 0.2516 0.2629 0.2834 0.0352  -0.0366 -0.0430 841  GLY B CA  
14849 C C   . GLY B 843  ? 0.2910 0.3092 0.3279 0.0359  -0.0333 -0.0440 841  GLY B C   
14850 O O   . GLY B 843  ? 0.2748 0.2993 0.3170 0.0354  -0.0316 -0.0440 841  GLY B O   
14851 N N   . GLN B 844  ? 0.2534 0.2704 0.2885 0.0368  -0.0326 -0.0447 842  GLN B N   
14852 C CA  . GLN B 844  ? 0.2518 0.2754 0.2911 0.0377  -0.0296 -0.0457 842  GLN B CA  
14853 C C   . GLN B 844  ? 0.2878 0.3129 0.3261 0.0345  -0.0266 -0.0440 842  GLN B C   
14854 O O   . GLN B 844  ? 0.3325 0.3600 0.3711 0.0349  -0.0246 -0.0446 842  GLN B O   
14855 C CB  . GLN B 844  ? 0.2245 0.2464 0.2625 0.0413  -0.0307 -0.0479 842  GLN B CB  
14856 C CG  . GLN B 844  ? 0.2209 0.2429 0.2611 0.0454  -0.0336 -0.0498 842  GLN B CG  
14857 C CD  . GLN B 844  ? 0.2372 0.2570 0.2756 0.0497  -0.0348 -0.0523 842  GLN B CD  
14858 O OE1 . GLN B 844  ? 0.2394 0.2648 0.2824 0.0535  -0.0348 -0.0543 842  GLN B OE1 
14859 N NE2 . GLN B 844  ? 0.3180 0.3301 0.3498 0.0491  -0.0359 -0.0523 842  GLN B NE2 
14860 N N   . ARG B 845  ? 0.3033 0.3270 0.3400 0.0316  -0.0262 -0.0421 843  ARG B N   
14861 C CA  . ARG B 845  ? 0.2719 0.2981 0.3085 0.0289  -0.0234 -0.0405 843  ARG B CA  
14862 C C   . ARG B 845  ? 0.3144 0.3463 0.3562 0.0283  -0.0215 -0.0401 843  ARG B C   
14863 O O   . ARG B 845  ? 0.2990 0.3310 0.3426 0.0286  -0.0229 -0.0403 843  ARG B O   
14864 C CB  . ARG B 845  ? 0.2575 0.2794 0.2891 0.0264  -0.0240 -0.0386 843  ARG B CB  
14865 C CG  . ARG B 845  ? 0.3112 0.3271 0.3374 0.0260  -0.0260 -0.0384 843  ARG B CG  
14866 C CD  . ARG B 845  ? 0.3631 0.3766 0.3851 0.0229  -0.0262 -0.0360 843  ARG B CD  
14867 N NE  . ARG B 845  ? 0.3349 0.3424 0.3514 0.0216  -0.0284 -0.0354 843  ARG B NE  
14868 C CZ  . ARG B 845  ? 0.3716 0.3790 0.3859 0.0197  -0.0275 -0.0344 843  ARG B CZ  
14869 N NH1 . ARG B 845  ? 0.4010 0.4140 0.4180 0.0189  -0.0245 -0.0339 843  ARG B NH1 
14870 N NH2 . ARG B 845  ? 0.4199 0.4211 0.4290 0.0182  -0.0301 -0.0338 843  ARG B NH2 
14871 N N   . CYS B 846  ? 0.2676 0.3036 0.3114 0.0273  -0.0187 -0.0394 844  CYS B N   
14872 C CA  . CYS B 846  ? 0.2985 0.3385 0.3462 0.0262  -0.0171 -0.0387 844  CYS B CA  
14873 C C   . CYS B 846  ? 0.2786 0.3155 0.3237 0.0246  -0.0177 -0.0375 844  CYS B C   
14874 O O   . CYS B 846  ? 0.2984 0.3364 0.3459 0.0241  -0.0178 -0.0373 844  CYS B O   
14875 C CB  . CYS B 846  ? 0.3743 0.4184 0.4236 0.0253  -0.0142 -0.0379 844  CYS B CB  
14876 S SG  . CYS B 846  ? 0.5850 0.6338 0.6371 0.0274  -0.0131 -0.0395 844  CYS B SG  
14877 N N   . SER B 847  ? 0.2548 0.2880 0.2951 0.0237  -0.0181 -0.0366 845  SER B N   
14878 C CA  . SER B 847  ? 0.2326 0.2634 0.2698 0.0225  -0.0185 -0.0355 845  SER B CA  
14879 C C   . SER B 847  ? 0.2890 0.3161 0.3241 0.0231  -0.0213 -0.0360 845  SER B C   
14880 O O   . SER B 847  ? 0.2507 0.2759 0.2828 0.0222  -0.0216 -0.0351 845  SER B O   
14881 C CB  . SER B 847  ? 0.2721 0.3019 0.3053 0.0211  -0.0176 -0.0340 845  SER B CB  
14882 O OG  . SER B 847  ? 0.3402 0.3671 0.3708 0.0212  -0.0191 -0.0343 845  SER B OG  
14883 N N   . ALA B 848  ? 0.2323 0.2583 0.2686 0.0246  -0.0233 -0.0373 846  ALA B N   
14884 C CA  . ALA B 848  ? 0.2798 0.3015 0.3132 0.0252  -0.0264 -0.0376 846  ALA B CA  
14885 C C   . ALA B 848  ? 0.2391 0.2609 0.2731 0.0249  -0.0272 -0.0376 846  ALA B C   
14886 O O   . ALA B 848  ? 0.2602 0.2853 0.2983 0.0249  -0.0262 -0.0381 846  ALA B O   
14887 C CB  . ALA B 848  ? 0.2374 0.2586 0.2728 0.0276  -0.0285 -0.0392 846  ALA B CB  
14888 N N   . LEU B 849  ? 0.2573 0.2749 0.2867 0.0245  -0.0291 -0.0370 847  LEU B N   
14889 C CA  . LEU B 849  ? 0.2542 0.2710 0.2829 0.0244  -0.0303 -0.0372 847  LEU B CA  
14890 C C   . LEU B 849  ? 0.2370 0.2546 0.2696 0.0259  -0.0328 -0.0387 847  LEU B C   
14891 O O   . LEU B 849  ? 0.2452 0.2605 0.2769 0.0273  -0.0352 -0.0392 847  LEU B O   
14892 C CB  . LEU B 849  ? 0.2451 0.2577 0.2673 0.0235  -0.0316 -0.0360 847  LEU B CB  
14893 C CG  . LEU B 849  ? 0.2377 0.2486 0.2579 0.0237  -0.0333 -0.0364 847  LEU B CG  
14894 C CD1 . LEU B 849  ? 0.2582 0.2714 0.2795 0.0233  -0.0313 -0.0368 847  LEU B CD1 
14895 C CD2 . LEU B 849  ? 0.2776 0.2847 0.2910 0.0228  -0.0346 -0.0350 847  LEU B CD2 
14896 N N   . ARG B 850  ? 0.2353 0.2558 0.2718 0.0257  -0.0325 -0.0394 848  ARG B N   
14897 C CA  . ARG B 850  ? 0.2184 0.2410 0.2594 0.0267  -0.0348 -0.0407 848  ARG B CA  
14898 C C   . ARG B 850  ? 0.2661 0.2861 0.3050 0.0263  -0.0373 -0.0410 848  ARG B C   
14899 O O   . ARG B 850  ? 0.2797 0.2995 0.3199 0.0274  -0.0403 -0.0418 848  ARG B O   
14900 C CB  . ARG B 850  ? 0.2498 0.2782 0.2974 0.0263  -0.0330 -0.0411 848  ARG B CB  
14901 C CG  . ARG B 850  ? 0.2218 0.2533 0.2714 0.0266  -0.0302 -0.0408 848  ARG B CG  
14902 C CD  . ARG B 850  ? 0.2415 0.2722 0.2905 0.0288  -0.0315 -0.0415 848  ARG B CD  
14903 N NE  . ARG B 850  ? 0.2589 0.2927 0.3099 0.0295  -0.0291 -0.0417 848  ARG B NE  
14904 C CZ  . ARG B 850  ? 0.2969 0.3292 0.3464 0.0314  -0.0297 -0.0424 848  ARG B CZ  
14905 N NH1 . ARG B 850  ? 0.2265 0.2538 0.2724 0.0328  -0.0327 -0.0428 848  ARG B NH1 
14906 N NH2 . ARG B 850  ? 0.2570 0.2923 0.3080 0.0320  -0.0275 -0.0427 848  ARG B NH2 
14907 N N   . VAL B 851  ? 0.2884 0.3064 0.3238 0.0250  -0.0362 -0.0405 849  VAL B N   
14908 C CA  . VAL B 851  ? 0.2720 0.2873 0.3048 0.0247  -0.0385 -0.0411 849  VAL B CA  
14909 C C   . VAL B 851  ? 0.2646 0.2759 0.2899 0.0245  -0.0378 -0.0403 849  VAL B C   
14910 O O   . VAL B 851  ? 0.2437 0.2553 0.2673 0.0239  -0.0351 -0.0397 849  VAL B O   
14911 C CB  . VAL B 851  ? 0.2881 0.3050 0.3243 0.0236  -0.0382 -0.0418 849  VAL B CB  
14912 C CG1 . VAL B 851  ? 0.2980 0.3115 0.3311 0.0234  -0.0413 -0.0427 849  VAL B CG1 
14913 C CG2 . VAL B 851  ? 0.2732 0.2954 0.3171 0.0234  -0.0382 -0.0421 849  VAL B CG2 
14914 N N   . LEU B 852  ? 0.2755 0.2835 0.2964 0.0249  -0.0404 -0.0401 850  LEU B N   
14915 C CA  . LEU B 852  ? 0.2670 0.2719 0.2805 0.0245  -0.0400 -0.0392 850  LEU B CA  
14916 C C   . LEU B 852  ? 0.2595 0.2622 0.2702 0.0246  -0.0416 -0.0404 850  LEU B C   
14917 O O   . LEU B 852  ? 0.3188 0.3203 0.3304 0.0250  -0.0450 -0.0413 850  LEU B O   
14918 C CB  . LEU B 852  ? 0.2413 0.2432 0.2505 0.0246  -0.0418 -0.0380 850  LEU B CB  
14919 C CG  . LEU B 852  ? 0.2013 0.2007 0.2027 0.0238  -0.0414 -0.0367 850  LEU B CG  
14920 C CD1 . LEU B 852  ? 0.2473 0.2493 0.2473 0.0230  -0.0374 -0.0355 850  LEU B CD1 
14921 C CD2 . LEU B 852  ? 0.2062 0.2021 0.2037 0.0236  -0.0439 -0.0353 850  LEU B CD2 
14922 N N   . CYS B 853  ? 0.2674 0.2698 0.2749 0.0246  -0.0395 -0.0405 851  CYS B N   
14923 C CA  . CYS B 853  ? 0.2610 0.2607 0.2650 0.0250  -0.0409 -0.0419 851  CYS B CA  
14924 C C   . CYS B 853  ? 0.2407 0.2382 0.2364 0.0254  -0.0407 -0.0412 851  CYS B C   
14925 O O   . CYS B 853  ? 0.2682 0.2672 0.2611 0.0256  -0.0376 -0.0403 851  CYS B O   
14926 C CB  . CYS B 853  ? 0.2550 0.2553 0.2609 0.0250  -0.0389 -0.0428 851  CYS B CB  
14927 S SG  . CYS B 853  ? 0.3297 0.3334 0.3451 0.0240  -0.0387 -0.0430 851  CYS B SG  
14928 N N   . LEU B 854  ? 0.2507 0.2452 0.2424 0.0256  -0.0439 -0.0416 852  LEU B N   
14929 C CA  . LEU B 854  ? 0.2855 0.2783 0.2692 0.0258  -0.0439 -0.0407 852  LEU B CA  
14930 C C   . LEU B 854  ? 0.3178 0.3077 0.2963 0.0268  -0.0452 -0.0426 852  LEU B C   
14931 O O   . LEU B 854  ? 0.3222 0.3097 0.3020 0.0269  -0.0485 -0.0443 852  LEU B O   
14932 C CB  . LEU B 854  ? 0.2940 0.2846 0.2756 0.0252  -0.0469 -0.0394 852  LEU B CB  
14933 C CG  . LEU B 854  ? 0.2647 0.2567 0.2501 0.0245  -0.0466 -0.0377 852  LEU B CG  
14934 C CD1 . LEU B 854  ? 0.2490 0.2375 0.2313 0.0243  -0.0502 -0.0366 852  LEU B CD1 
14935 C CD2 . LEU B 854  ? 0.2869 0.2813 0.2706 0.0236  -0.0427 -0.0359 852  LEU B CD2 
14936 N N   . GLN B 855  ? 0.3098 0.3001 0.2822 0.0277  -0.0427 -0.0425 853  GLN B N   
14937 C CA  . GLN B 855  ? 0.3321 0.3193 0.2981 0.0291  -0.0439 -0.0444 853  GLN B CA  
14938 C C   . GLN B 855  ? 0.3379 0.3219 0.2996 0.0286  -0.0478 -0.0444 853  GLN B C   
14939 O O   . GLN B 855  ? 0.3448 0.3294 0.3047 0.0277  -0.0483 -0.0421 853  GLN B O   
14940 C CB  . GLN B 855  ? 0.2884 0.2777 0.2481 0.0305  -0.0403 -0.0440 853  GLN B CB  
14941 C CG  . GLN B 855  ? 0.3370 0.3228 0.2899 0.0326  -0.0413 -0.0467 853  GLN B CG  
14942 C CD  . GLN B 855  ? 0.3838 0.3726 0.3310 0.0347  -0.0376 -0.0466 853  GLN B CD  
14943 O OE1 . GLN B 855  ? 0.4074 0.4006 0.3577 0.0350  -0.0340 -0.0454 853  GLN B OE1 
14944 N NE2 . GLN B 855  ? 0.4074 0.3941 0.3461 0.0364  -0.0383 -0.0479 853  GLN B NE2 
14945 N N   . GLU B 856  ? 0.3446 0.3249 0.3047 0.0292  -0.0510 -0.0468 854  GLU B N   
14946 C CA  . GLU B 856  ? 0.3587 0.3359 0.3159 0.0288  -0.0555 -0.0470 854  GLU B CA  
14947 C C   . GLU B 856  ? 0.3820 0.3587 0.3307 0.0289  -0.0553 -0.0452 854  GLU B C   
14948 O O   . GLU B 856  ? 0.4427 0.4180 0.3903 0.0281  -0.0582 -0.0438 854  GLU B O   
14949 C CB  . GLU B 856  ? 0.3863 0.3595 0.3415 0.0294  -0.0586 -0.0500 854  GLU B CB  
14950 C CG  . GLU B 856  ? 0.5745 0.5449 0.5285 0.0288  -0.0638 -0.0505 854  GLU B CG  
14951 C CD  . GLU B 856  ? 0.6367 0.6092 0.6002 0.0275  -0.0661 -0.0499 854  GLU B CD  
14952 O OE1 . GLU B 856  ? 0.6708 0.6442 0.6408 0.0269  -0.0665 -0.0512 854  GLU B OE1 
14953 O OE2 . GLU B 856  ? 0.6702 0.6436 0.6346 0.0273  -0.0675 -0.0481 854  GLU B OE2 
14954 N N   . ASP B 857  ? 0.3618 0.3398 0.3044 0.0300  -0.0520 -0.0451 855  ASP B N   
14955 C CA  . ASP B 857  ? 0.3964 0.3746 0.3303 0.0299  -0.0515 -0.0433 855  ASP B CA  
14956 C C   . ASP B 857  ? 0.4707 0.4511 0.4060 0.0278  -0.0508 -0.0396 855  ASP B C   
14957 O O   . ASP B 857  ? 0.4247 0.4037 0.3538 0.0269  -0.0523 -0.0377 855  ASP B O   
14958 C CB  . ASP B 857  ? 0.4659 0.4468 0.3943 0.0317  -0.0474 -0.0439 855  ASP B CB  
14959 N N   . VAL B 858  ? 0.3826 0.3658 0.3251 0.0269  -0.0487 -0.0385 856  VAL B N   
14960 C CA  . VAL B 858  ? 0.3575 0.3420 0.3007 0.0249  -0.0482 -0.0351 856  VAL B CA  
14961 C C   . VAL B 858  ? 0.3407 0.3234 0.2909 0.0242  -0.0508 -0.0349 856  VAL B C   
14962 O O   . VAL B 858  ? 0.3674 0.3498 0.3180 0.0227  -0.0511 -0.0324 856  VAL B O   
14963 C CB  . VAL B 858  ? 0.3686 0.3583 0.3129 0.0242  -0.0433 -0.0335 856  VAL B CB  
14964 C CG1 . VAL B 858  ? 0.4266 0.4191 0.3633 0.0251  -0.0406 -0.0332 856  VAL B CG1 
14965 C CG2 . VAL B 858  ? 0.3206 0.3124 0.2727 0.0252  -0.0414 -0.0353 856  VAL B CG2 
14966 N N   . ALA B 859  ? 0.3425 0.3240 0.2981 0.0252  -0.0531 -0.0374 857  ALA B N   
14967 C CA  . ALA B 859  ? 0.3518 0.3332 0.3152 0.0250  -0.0550 -0.0375 857  ALA B CA  
14968 C C   . ALA B 859  ? 0.3324 0.3106 0.2936 0.0246  -0.0585 -0.0357 857  ALA B C   
14969 O O   . ALA B 859  ? 0.3584 0.3367 0.3231 0.0241  -0.0586 -0.0344 857  ALA B O   
14970 C CB  . ALA B 859  ? 0.3152 0.2965 0.2840 0.0260  -0.0570 -0.0403 857  ALA B CB  
14971 N N   . ASP B 860  ? 0.3785 0.3534 0.3334 0.0248  -0.0617 -0.0357 858  ASP B N   
14972 C CA  . ASP B 860  ? 0.4008 0.3719 0.3533 0.0246  -0.0657 -0.0339 858  ASP B CA  
14973 C C   . ASP B 860  ? 0.4027 0.3729 0.3514 0.0229  -0.0642 -0.0306 858  ASP B C   
14974 O O   . ASP B 860  ? 0.3933 0.3613 0.3444 0.0228  -0.0660 -0.0294 858  ASP B O   
14975 C CB  . ASP B 860  ? 0.4161 0.3838 0.3613 0.0250  -0.0692 -0.0343 858  ASP B CB  
14976 C CG  . ASP B 860  ? 0.5446 0.5125 0.4939 0.0263  -0.0720 -0.0374 858  ASP B CG  
14977 O OD1 . ASP B 860  ? 0.5408 0.5105 0.4987 0.0269  -0.0730 -0.0385 858  ASP B OD1 
14978 O OD2 . ASP B 860  ? 0.5798 0.5461 0.5235 0.0266  -0.0731 -0.0387 858  ASP B OD2 
14979 N N   . ARG B 861  ? 0.3967 0.3685 0.3394 0.0215  -0.0610 -0.0291 859  ARG B N   
14980 C CA  . ARG B 861  ? 0.3722 0.3433 0.3109 0.0192  -0.0598 -0.0255 859  ARG B CA  
14981 C C   . ARG B 861  ? 0.3603 0.3333 0.3058 0.0186  -0.0577 -0.0251 859  ARG B C   
14982 O O   . ARG B 861  ? 0.3547 0.3246 0.2994 0.0172  -0.0591 -0.0229 859  ARG B O   
14983 C CB  . ARG B 861  ? 0.4380 0.4122 0.3696 0.0179  -0.0564 -0.0240 859  ARG B CB  
14984 C CG  . ARG B 861  ? 0.4941 0.4683 0.4215 0.0147  -0.0553 -0.0199 859  ARG B CG  
14985 C CD  . ARG B 861  ? 0.6335 0.6117 0.5535 0.0133  -0.0522 -0.0180 859  ARG B CD  
14986 N NE  . ARG B 861  ? 0.6643 0.6437 0.5816 0.0098  -0.0508 -0.0138 859  ARG B NE  
14987 C CZ  . ARG B 861  ? 0.6172 0.6025 0.5373 0.0085  -0.0466 -0.0128 859  ARG B CZ  
14988 N NH1 . ARG B 861  ? 0.6133 0.6038 0.5383 0.0107  -0.0432 -0.0155 859  ARG B NH1 
14989 N NH2 . ARG B 861  ? 0.5974 0.5832 0.5152 0.0047  -0.0461 -0.0088 859  ARG B NH2 
14990 N N   . ILE B 862  ? 0.3292 0.3067 0.2809 0.0196  -0.0545 -0.0272 860  ILE B N   
14991 C CA  . ILE B 862  ? 0.3001 0.2796 0.2579 0.0190  -0.0525 -0.0269 860  ILE B CA  
14992 C C   . ILE B 862  ? 0.3105 0.2871 0.2736 0.0203  -0.0557 -0.0279 860  ILE B C   
14993 O O   . ILE B 862  ? 0.2840 0.2591 0.2486 0.0196  -0.0560 -0.0266 860  ILE B O   
14994 C CB  . ILE B 862  ? 0.3140 0.2989 0.2766 0.0199  -0.0484 -0.0287 860  ILE B CB  
14995 C CG1 . ILE B 862  ? 0.3713 0.3598 0.3288 0.0187  -0.0448 -0.0272 860  ILE B CG1 
14996 C CG2 . ILE B 862  ? 0.3015 0.2883 0.2713 0.0198  -0.0470 -0.0291 860  ILE B CG2 
14997 C CD1 . ILE B 862  ? 0.3353 0.3286 0.2962 0.0200  -0.0410 -0.0290 860  ILE B CD1 
14998 N N   . LEU B 863  ? 0.3378 0.3136 0.3036 0.0223  -0.0585 -0.0301 861  LEU B N   
14999 C CA  . LEU B 863  ? 0.3524 0.3265 0.3235 0.0240  -0.0617 -0.0311 861  LEU B CA  
15000 C C   . LEU B 863  ? 0.3370 0.3053 0.3031 0.0237  -0.0653 -0.0289 861  LEU B C   
15001 O O   . LEU B 863  ? 0.3097 0.2761 0.2789 0.0246  -0.0666 -0.0289 861  LEU B O   
15002 C CB  . LEU B 863  ? 0.3181 0.2932 0.2926 0.0258  -0.0643 -0.0337 861  LEU B CB  
15003 C CG  . LEU B 863  ? 0.3905 0.3706 0.3724 0.0264  -0.0621 -0.0361 861  LEU B CG  
15004 C CD1 . LEU B 863  ? 0.4552 0.4356 0.4388 0.0274  -0.0652 -0.0381 861  LEU B CD1 
15005 C CD2 . LEU B 863  ? 0.4263 0.4091 0.4159 0.0273  -0.0611 -0.0366 861  LEU B CD2 
15006 N N   . THR B 864  ? 0.3495 0.3143 0.3075 0.0226  -0.0670 -0.0272 862  THR B N   
15007 C CA  . THR B 864  ? 0.3583 0.3167 0.3107 0.0219  -0.0706 -0.0247 862  THR B CA  
15008 C C   . THR B 864  ? 0.3825 0.3394 0.3334 0.0196  -0.0687 -0.0223 862  THR B C   
15009 O O   . THR B 864  ? 0.3681 0.3200 0.3188 0.0200  -0.0715 -0.0214 862  THR B O   
15010 C CB  . THR B 864  ? 0.4049 0.3605 0.3484 0.0207  -0.0724 -0.0229 862  THR B CB  
15011 O OG1 . THR B 864  ? 0.3274 0.2840 0.2723 0.0228  -0.0745 -0.0254 862  THR B OG1 
15012 C CG2 . THR B 864  ? 0.4669 0.4150 0.4041 0.0199  -0.0766 -0.0200 862  THR B CG2 
15013 N N   . MET B 865  ? 0.3171 0.2785 0.2671 0.0174  -0.0642 -0.0213 863  MET B N   
15014 C CA  . MET B 865  ? 0.3658 0.3266 0.3147 0.0148  -0.0624 -0.0189 863  MET B CA  
15015 C C   . MET B 865  ? 0.3402 0.3015 0.2965 0.0163  -0.0620 -0.0208 863  MET B C   
15016 O O   . MET B 865  ? 0.3133 0.2701 0.2685 0.0155  -0.0635 -0.0195 863  MET B O   
15017 C CB  . MET B 865  ? 0.3179 0.2849 0.2652 0.0125  -0.0575 -0.0178 863  MET B CB  
15018 C CG  . MET B 865  ? 0.4188 0.3862 0.3643 0.0090  -0.0557 -0.0148 863  MET B CG  
15019 S SD  . MET B 865  ? 0.4612 0.4367 0.4034 0.0065  -0.0505 -0.0129 863  MET B SD  
15020 C CE  . MET B 865  ? 0.3564 0.3315 0.2932 0.0082  -0.0518 -0.0138 863  MET B CE  
15021 N N   . LEU B 866  ? 0.3020 0.2685 0.2655 0.0186  -0.0600 -0.0238 864  LEU B N   
15022 C CA  . LEU B 866  ? 0.3227 0.2907 0.2934 0.0203  -0.0593 -0.0257 864  LEU B CA  
15023 C C   . LEU B 866  ? 0.2997 0.2624 0.2714 0.0227  -0.0637 -0.0264 864  LEU B C   
15024 O O   . LEU B 866  ? 0.3285 0.2888 0.3014 0.0230  -0.0641 -0.0264 864  LEU B O   
15025 C CB  . LEU B 866  ? 0.2682 0.2427 0.2459 0.0220  -0.0567 -0.0285 864  LEU B CB  
15026 C CG  . LEU B 866  ? 0.3561 0.3337 0.3417 0.0237  -0.0554 -0.0305 864  LEU B CG  
15027 C CD1 . LEU B 866  ? 0.3378 0.3167 0.3232 0.0217  -0.0522 -0.0292 864  LEU B CD1 
15028 C CD2 . LEU B 866  ? 0.3685 0.3517 0.3601 0.0249  -0.0538 -0.0328 864  LEU B CD2 
15029 N N   . LYS B 867  ? 0.3018 0.2625 0.2726 0.0245  -0.0672 -0.0272 865  LYS B N   
15030 C CA  . LYS B 867  ? 0.3122 0.2681 0.2839 0.0274  -0.0717 -0.0279 865  LYS B CA  
15031 C C   . LYS B 867  ? 0.3496 0.2972 0.3140 0.0259  -0.0743 -0.0252 865  LYS B C   
15032 O O   . LYS B 867  ? 0.3565 0.2999 0.3220 0.0279  -0.0766 -0.0258 865  LYS B O   
15033 C CB  . LYS B 867  ? 0.3501 0.3059 0.3219 0.0294  -0.0751 -0.0290 865  LYS B CB  
15034 C CG  . LYS B 867  ? 0.3327 0.2961 0.3126 0.0310  -0.0734 -0.0318 865  LYS B CG  
15035 C CD  . LYS B 867  ? 0.4223 0.3857 0.4015 0.0321  -0.0767 -0.0326 865  LYS B CD  
15036 C CE  . LYS B 867  ? 0.4494 0.4200 0.4368 0.0332  -0.0755 -0.0353 865  LYS B CE  
15037 N NZ  . LYS B 867  ? 0.4943 0.4650 0.4806 0.0337  -0.0788 -0.0361 865  LYS B NZ  
15038 N N   . GLY B 868  ? 0.3574 0.3024 0.3142 0.0224  -0.0741 -0.0221 866  GLY B N   
15039 C CA  . GLY B 868  ? 0.3355 0.2724 0.2850 0.0201  -0.0767 -0.0190 866  GLY B CA  
15040 C C   . GLY B 868  ? 0.3270 0.2634 0.2778 0.0185  -0.0746 -0.0186 866  GLY B C   
15041 O O   . GLY B 868  ? 0.3647 0.2937 0.3127 0.0186  -0.0776 -0.0177 866  GLY B O   
15042 N N   . ALA B 869  ? 0.3170 0.2611 0.2720 0.0172  -0.0696 -0.0192 867  ALA B N   
15043 C CA  . ALA B 869  ? 0.3046 0.2490 0.2613 0.0156  -0.0675 -0.0189 867  ALA B CA  
15044 C C   . ALA B 869  ? 0.3450 0.2884 0.3075 0.0196  -0.0686 -0.0221 867  ALA B C   
15045 O O   . ALA B 869  ? 0.3437 0.2824 0.3049 0.0193  -0.0697 -0.0218 867  ALA B O   
15046 C CB  . ALA B 869  ? 0.3240 0.2772 0.2838 0.0137  -0.0621 -0.0189 867  ALA B CB  
15047 N N   . LEU B 870  ? 0.3404 0.2883 0.3091 0.0234  -0.0685 -0.0251 868  LEU B N   
15048 C CA  . LEU B 870  ? 0.3549 0.3034 0.3296 0.0275  -0.0694 -0.0281 868  LEU B CA  
15049 C C   . LEU B 870  ? 0.3929 0.3320 0.3635 0.0296  -0.0743 -0.0279 868  LEU B C   
15050 O O   . LEU B 870  ? 0.3918 0.3287 0.3640 0.0315  -0.0748 -0.0294 868  LEU B O   
15051 C CB  . LEU B 870  ? 0.3707 0.3258 0.3522 0.0307  -0.0691 -0.0307 868  LEU B CB  
15052 C CG  . LEU B 870  ? 0.4265 0.3857 0.4160 0.0349  -0.0689 -0.0339 868  LEU B CG  
15053 C CD1 . LEU B 870  ? 0.4327 0.4000 0.4282 0.0340  -0.0639 -0.0351 868  LEU B CD1 
15054 C CD2 . LEU B 870  ? 0.4744 0.4359 0.4676 0.0382  -0.0718 -0.0356 868  LEU B CD2 
15055 N N   . HIS B 871  ? 0.3493 0.2823 0.3141 0.0294  -0.0783 -0.0262 869  HIS B N   
15056 C CA  . HIS B 871  ? 0.3693 0.2928 0.3303 0.0320  -0.0835 -0.0262 869  HIS B CA  
15057 C C   . HIS B 871  ? 0.4053 0.3200 0.3592 0.0290  -0.0849 -0.0238 869  HIS B C   
15058 O O   . HIS B 871  ? 0.3884 0.2938 0.3385 0.0312  -0.0895 -0.0239 869  HIS B O   
15059 C CB  . HIS B 871  ? 0.4552 0.3749 0.4123 0.0330  -0.0877 -0.0251 869  HIS B CB  
15060 C CG  . HIS B 871  ? 0.4933 0.4202 0.4577 0.0370  -0.0879 -0.0280 869  HIS B CG  
15061 N ND1 . HIS B 871  ? 0.5339 0.4621 0.5042 0.0424  -0.0897 -0.0310 869  HIS B ND1 
15062 C CD2 . HIS B 871  ? 0.4405 0.3737 0.4072 0.0364  -0.0866 -0.0282 869  HIS B CD2 
15063 C CE1 . HIS B 871  ? 0.5023 0.4380 0.4786 0.0444  -0.0895 -0.0328 869  HIS B CE1 
15064 N NE2 . HIS B 871  ? 0.5226 0.4608 0.4966 0.0408  -0.0878 -0.0312 869  HIS B NE2 
15065 N N   . GLU B 872  ? 0.3749 0.2922 0.3272 0.0241  -0.0813 -0.0218 870  GLU B N   
15066 C CA  . GLU B 872  ? 0.3688 0.2788 0.3154 0.0206  -0.0824 -0.0196 870  GLU B CA  
15067 C C   . GLU B 872  ? 0.3753 0.2873 0.3263 0.0220  -0.0803 -0.0221 870  GLU B C   
15068 O O   . GLU B 872  ? 0.3895 0.2953 0.3361 0.0193  -0.0814 -0.0207 870  GLU B O   
15069 C CB  . GLU B 872  ? 0.3608 0.2731 0.3029 0.0142  -0.0799 -0.0156 870  GLU B CB  
15070 C CG  . GLU B 872  ? 0.3586 0.2689 0.2951 0.0124  -0.0819 -0.0128 870  GLU B CG  
15071 C CD  . GLU B 872  ? 0.4051 0.3026 0.3337 0.0124  -0.0881 -0.0108 870  GLU B CD  
15072 O OE1 . GLU B 872  ? 0.4605 0.3500 0.3859 0.0116  -0.0906 -0.0103 870  GLU B OE1 
15073 O OE2 . GLU B 872  ? 0.4482 0.3432 0.3734 0.0132  -0.0908 -0.0097 870  GLU B OE2 
15074 N N   . LEU B 873  ? 0.3809 0.3011 0.3403 0.0259  -0.0774 -0.0256 871  LEU B N   
15075 C CA  . LEU B 873  ? 0.3764 0.2993 0.3399 0.0273  -0.0751 -0.0280 871  LEU B CA  
15076 C C   . LEU B 873  ? 0.3783 0.2930 0.3402 0.0318  -0.0792 -0.0302 871  LEU B C   
15077 O O   . LEU B 873  ? 0.3863 0.2982 0.3485 0.0360  -0.0826 -0.0316 871  LEU B O   
15078 C CB  . LEU B 873  ? 0.3378 0.2725 0.3105 0.0296  -0.0707 -0.0306 871  LEU B CB  
15079 C CG  . LEU B 873  ? 0.3931 0.3361 0.3679 0.0260  -0.0664 -0.0290 871  LEU B CG  
15080 C CD1 . LEU B 873  ? 0.3729 0.3260 0.3565 0.0286  -0.0628 -0.0318 871  LEU B CD1 
15081 C CD2 . LEU B 873  ? 0.3731 0.3160 0.3445 0.0209  -0.0641 -0.0265 871  LEU B CD2 
15082 N N   . HIS B 874  ? 0.3476 0.2586 0.3077 0.0311  -0.0790 -0.0308 872  HIS B N   
15083 C CA  . HIS B 874  ? 0.3872 0.2905 0.3455 0.0358  -0.0825 -0.0336 872  HIS B CA  
15084 C C   . HIS B 874  ? 0.3798 0.2919 0.3461 0.0399  -0.0789 -0.0375 872  HIS B C   
15085 O O   . HIS B 874  ? 0.3357 0.2531 0.3041 0.0374  -0.0750 -0.0375 872  HIS B O   
15086 C CB  . HIS B 874  ? 0.3760 0.2679 0.3259 0.0323  -0.0854 -0.0318 872  HIS B CB  
15087 C CG  . HIS B 874  ? 0.3992 0.2816 0.3461 0.0373  -0.0894 -0.0347 872  HIS B CG  
15088 N ND1 . HIS B 874  ? 0.4356 0.3074 0.3753 0.0350  -0.0921 -0.0341 872  HIS B ND1 
15089 C CD2 . HIS B 874  ? 0.4998 0.3818 0.4497 0.0446  -0.0912 -0.0384 872  HIS B CD2 
15090 C CE1 . HIS B 874  ? 0.4827 0.3472 0.4207 0.0410  -0.0954 -0.0376 872  HIS B CE1 
15091 N NE2 . HIS B 874  ? 0.5057 0.3767 0.4499 0.0471  -0.0949 -0.0402 872  HIS B NE2 
15092 N N   . ILE B 875  ? 0.3358 0.2500 0.3063 0.0463  -0.0802 -0.0407 873  ILE B N   
15093 C CA  . ILE B 875  ? 0.3642 0.2875 0.3424 0.0506  -0.0769 -0.0443 873  ILE B CA  
15094 C C   . ILE B 875  ? 0.3850 0.3006 0.3601 0.0558  -0.0801 -0.0473 873  ILE B C   
15095 O O   . ILE B 875  ? 0.3806 0.2876 0.3516 0.0592  -0.0850 -0.0478 873  ILE B O   
15096 C CB  . ILE B 875  ? 0.3638 0.2973 0.3502 0.0540  -0.0756 -0.0457 873  ILE B CB  
15097 C CG1 . ILE B 875  ? 0.3816 0.3246 0.3724 0.0495  -0.0713 -0.0439 873  ILE B CG1 
15098 C CG2 . ILE B 875  ? 0.4247 0.3653 0.4177 0.0597  -0.0739 -0.0497 873  ILE B CG2 
15099 C CD1 . ILE B 875  ? 0.4587 0.3975 0.4441 0.0444  -0.0723 -0.0402 873  ILE B CD1 
15100 N N   . GLY B 876  ? 0.2977 0.2161 0.2743 0.0567  -0.0774 -0.0494 874  GLY B N   
15101 C CA  . GLY B 876  ? 0.3683 0.2792 0.3414 0.0619  -0.0803 -0.0526 874  GLY B CA  
15102 C C   . GLY B 876  ? 0.3528 0.2667 0.3265 0.0615  -0.0770 -0.0543 874  GLY B C   
15103 O O   . GLY B 876  ? 0.3165 0.2396 0.2946 0.0577  -0.0722 -0.0532 874  GLY B O   
15104 N N   . ARG B 877  ? 0.3508 0.2565 0.3198 0.0658  -0.0798 -0.0572 875  ARG B N   
15105 C CA  . ARG B 877  ? 0.3545 0.2613 0.3226 0.0659  -0.0774 -0.0592 875  ARG B CA  
15106 C C   . ARG B 877  ? 0.3817 0.2838 0.3447 0.0579  -0.0770 -0.0558 875  ARG B C   
15107 O O   . ARG B 877  ? 0.3752 0.2660 0.3309 0.0543  -0.0811 -0.0532 875  ARG B O   
15108 C CB  . ARG B 877  ? 0.4146 0.3117 0.3772 0.0724  -0.0813 -0.0632 875  ARG B CB  
15109 C CG  . ARG B 877  ? 0.4067 0.3076 0.3699 0.0748  -0.0784 -0.0664 875  ARG B CG  
15110 C CD  . ARG B 877  ? 0.4543 0.3453 0.4118 0.0823  -0.0825 -0.0707 875  ARG B CD  
15111 N NE  . ARG B 877  ? 0.4081 0.2822 0.3545 0.0794  -0.0873 -0.0701 875  ARG B NE  
15112 C CZ  . ARG B 877  ? 0.5758 0.4385 0.5150 0.0848  -0.0914 -0.0737 875  ARG B CZ  
15113 N NH1 . ARG B 877  ? 0.5326 0.3990 0.4745 0.0938  -0.0912 -0.0783 875  ARG B NH1 
15114 N NH2 . ARG B 877  ? 0.5788 0.4261 0.5078 0.0809  -0.0958 -0.0727 875  ARG B NH2 
15115 N N   . THR B 878  ? 0.3409 0.2518 0.3076 0.0552  -0.0722 -0.0557 876  THR B N   
15116 C CA  . THR B 878  ? 0.3515 0.2630 0.3164 0.0474  -0.0705 -0.0519 876  THR B CA  
15117 C C   . THR B 878  ? 0.3686 0.2692 0.3251 0.0443  -0.0732 -0.0516 876  THR B C   
15118 O O   . THR B 878  ? 0.3609 0.2631 0.3162 0.0379  -0.0717 -0.0487 876  THR B O   
15119 C CB  . THR B 878  ? 0.3419 0.2678 0.3147 0.0459  -0.0643 -0.0518 876  THR B CB  
15120 O OG1 . THR B 878  ? 0.3448 0.2751 0.3201 0.0507  -0.0623 -0.0556 876  THR B OG1 
15121 C CG2 . THR B 878  ? 0.3266 0.2619 0.3066 0.0465  -0.0620 -0.0508 876  THR B CG2 
15122 N N   . ASP B 879  ? 0.4190 0.3088 0.3695 0.0486  -0.0774 -0.0546 877  ASP B N   
15123 C CA  . ASP B 879  ? 0.4075 0.2850 0.3489 0.0453  -0.0810 -0.0542 877  ASP B CA  
15124 C C   . ASP B 879  ? 0.3999 0.2646 0.3337 0.0408  -0.0863 -0.0506 877  ASP B C   
15125 O O   . ASP B 879  ? 0.4064 0.2573 0.3315 0.0397  -0.0911 -0.0508 877  ASP B O   
15126 C CB  . ASP B 879  ? 0.3981 0.2689 0.3356 0.0521  -0.0832 -0.0592 877  ASP B CB  
15127 C CG  . ASP B 879  ? 0.4451 0.3080 0.3802 0.0590  -0.0875 -0.0617 877  ASP B CG  
15128 O OD1 . ASP B 879  ? 0.4709 0.3396 0.4114 0.0611  -0.0868 -0.0610 877  ASP B OD1 
15129 O OD2 . ASP B 879  ? 0.4658 0.3162 0.3933 0.0627  -0.0919 -0.0646 877  ASP B OD2 
15130 N N   . ARG B 880  ? 0.3925 0.2615 0.3292 0.0378  -0.0855 -0.0471 878  ARG B N   
15131 C CA  . ARG B 880  ? 0.3975 0.2573 0.3278 0.0322  -0.0894 -0.0427 878  ARG B CA  
15132 C C   . ARG B 880  ? 0.4065 0.2767 0.3409 0.0253  -0.0853 -0.0384 878  ARG B C   
15133 O O   . ARG B 880  ? 0.3595 0.2423 0.3019 0.0268  -0.0807 -0.0387 878  ARG B O   
15134 C CB  . ARG B 880  ? 0.3942 0.2482 0.3231 0.0363  -0.0931 -0.0429 878  ARG B CB  
15135 C CG  . ARG B 880  ? 0.5202 0.3615 0.4435 0.0429  -0.0984 -0.0466 878  ARG B CG  
15136 C CD  . ARG B 880  ? 0.6350 0.4705 0.5567 0.0465  -0.1024 -0.0461 878  ARG B CD  
15137 N NE  . ARG B 880  ? 0.7626 0.5891 0.6811 0.0548  -0.1065 -0.0506 878  ARG B NE  
15138 C CZ  . ARG B 880  ? 0.8225 0.6316 0.7310 0.0556  -0.1131 -0.0505 878  ARG B CZ  
15139 N NH1 . ARG B 880  ? 0.8499 0.6484 0.7506 0.0481  -0.1167 -0.0460 878  ARG B NH1 
15140 N NH2 . ARG B 880  ? 0.8701 0.6723 0.7764 0.0641  -0.1164 -0.0551 878  ARG B NH2 
15141 N N   . LEU B 881  ? 0.3710 0.2360 0.2998 0.0179  -0.0870 -0.0344 879  LEU B N   
15142 C CA  . LEU B 881  ? 0.3509 0.2259 0.2831 0.0116  -0.0832 -0.0303 879  LEU B CA  
15143 C C   . LEU B 881  ? 0.3842 0.2634 0.3190 0.0121  -0.0824 -0.0284 879  LEU B C   
15144 O O   . LEU B 881  ? 0.3521 0.2433 0.2928 0.0104  -0.0778 -0.0270 879  LEU B O   
15145 C CB  . LEU B 881  ? 0.4018 0.2700 0.3271 0.0035  -0.0858 -0.0261 879  LEU B CB  
15146 C CG  . LEU B 881  ? 0.3827 0.2611 0.3107 -0.0033 -0.0821 -0.0215 879  LEU B CG  
15147 C CD1 . LEU B 881  ? 0.4013 0.2929 0.3366 -0.0031 -0.0765 -0.0229 879  LEU B CD1 
15148 C CD2 . LEU B 881  ? 0.3784 0.2486 0.2986 -0.0113 -0.0859 -0.0170 879  LEU B CD2 
15149 N N   . SER B 882  ? 0.3637 0.2331 0.2941 0.0148  -0.0871 -0.0286 880  SER B N   
15150 C CA  . SER B 882  ? 0.3722 0.2447 0.3042 0.0151  -0.0869 -0.0267 880  SER B CA  
15151 C C   . SER B 882  ? 0.4043 0.2882 0.3453 0.0208  -0.0832 -0.0297 880  SER B C   
15152 O O   . SER B 882  ? 0.3821 0.2697 0.3248 0.0209  -0.0827 -0.0283 880  SER B O   
15153 C CB  . SER B 882  ? 0.4218 0.2800 0.3461 0.0164  -0.0934 -0.0259 880  SER B CB  
15154 O OG  . SER B 882  ? 0.4236 0.2757 0.3476 0.0238  -0.0961 -0.0304 880  SER B OG  
15155 N N   . VAL B 883  ? 0.3346 0.2238 0.2808 0.0255  -0.0807 -0.0337 881  VAL B N   
15156 C CA  . VAL B 883  ? 0.3361 0.2361 0.2909 0.0305  -0.0774 -0.0364 881  VAL B CA  
15157 C C   . VAL B 883  ? 0.3261 0.2389 0.2869 0.0269  -0.0718 -0.0347 881  VAL B C   
15158 O O   . VAL B 883  ? 0.3261 0.2430 0.2878 0.0237  -0.0689 -0.0341 881  VAL B O   
15159 C CB  . VAL B 883  ? 0.3268 0.2283 0.2849 0.0369  -0.0768 -0.0412 881  VAL B CB  
15160 C CG1 . VAL B 883  ? 0.3114 0.2269 0.2795 0.0403  -0.0721 -0.0432 881  VAL B CG1 
15161 C CG2 . VAL B 883  ? 0.3389 0.2292 0.2923 0.0423  -0.0823 -0.0434 881  VAL B CG2 
15162 N N   . ASP B 884  ? 0.3040 0.2231 0.2688 0.0276  -0.0704 -0.0341 882  ASP B N   
15163 C CA  . ASP B 884  ? 0.3402 0.2707 0.3104 0.0250  -0.0655 -0.0328 882  ASP B CA  
15164 C C   . ASP B 884  ? 0.3861 0.3266 0.3648 0.0290  -0.0617 -0.0360 882  ASP B C   
15165 O O   . ASP B 884  ? 0.4020 0.3503 0.3845 0.0271  -0.0575 -0.0358 882  ASP B O   
15166 C CB  . ASP B 884  ? 0.3345 0.2659 0.3038 0.0235  -0.0661 -0.0305 882  ASP B CB  
15167 C CG  . ASP B 884  ? 0.3763 0.2988 0.3371 0.0189  -0.0695 -0.0268 882  ASP B CG  
15168 O OD1 . ASP B 884  ? 0.3740 0.2962 0.3320 0.0139  -0.0684 -0.0244 882  ASP B OD1 
15169 O OD2 . ASP B 884  ? 0.3597 0.2756 0.3167 0.0200  -0.0734 -0.0260 882  ASP B OD2 
15170 N N   . VAL B 885  ? 0.3335 0.2741 0.3151 0.0345  -0.0633 -0.0388 883  VAL B N   
15171 C CA  . VAL B 885  ? 0.3499 0.3006 0.3399 0.0382  -0.0600 -0.0415 883  VAL B CA  
15172 C C   . VAL B 885  ? 0.3219 0.2701 0.3126 0.0438  -0.0618 -0.0450 883  VAL B C   
15173 O O   . VAL B 885  ? 0.3045 0.2450 0.2916 0.0470  -0.0661 -0.0459 883  VAL B O   
15174 C CB  . VAL B 885  ? 0.3610 0.3171 0.3553 0.0392  -0.0599 -0.0413 883  VAL B CB  
15175 C CG1 . VAL B 885  ? 0.3695 0.3354 0.3724 0.0431  -0.0574 -0.0440 883  VAL B CG1 
15176 C CG2 . VAL B 885  ? 0.3585 0.3180 0.3522 0.0342  -0.0575 -0.0383 883  VAL B CG2 
15177 N N   . GLY B 886  ? 0.3000 0.2544 0.2946 0.0452  -0.0585 -0.0470 884  GLY B N   
15178 C CA  . GLY B 886  ? 0.2740 0.2278 0.2696 0.0509  -0.0594 -0.0506 884  GLY B CA  
15179 C C   . GLY B 886  ? 0.2450 0.2092 0.2491 0.0553  -0.0575 -0.0528 884  GLY B C   
15180 O O   . GLY B 886  ? 0.2957 0.2653 0.3042 0.0545  -0.0569 -0.0517 884  GLY B O   
15181 N N   . PRO B 887  ? 0.2877 0.2550 0.2941 0.0600  -0.0566 -0.0560 885  PRO B N   
15182 C CA  . PRO B 887  ? 0.2648 0.2423 0.2792 0.0646  -0.0551 -0.0582 885  PRO B CA  
15183 C C   . PRO B 887  ? 0.3051 0.2949 0.3268 0.0619  -0.0499 -0.0574 885  PRO B C   
15184 O O   . PRO B 887  ? 0.2503 0.2408 0.2706 0.0576  -0.0472 -0.0558 885  PRO B O   
15185 C CB  . PRO B 887  ? 0.2687 0.2443 0.2815 0.0705  -0.0559 -0.0618 885  PRO B CB  
15186 C CG  . PRO B 887  ? 0.3229 0.2918 0.3292 0.0674  -0.0554 -0.0614 885  PRO B CG  
15187 C CD  . PRO B 887  ? 0.2699 0.2308 0.2709 0.0613  -0.0573 -0.0578 885  PRO B CD  
15188 N N   . VAL B 888  ? 0.2615 0.2612 0.2909 0.0647  -0.0486 -0.0585 886  VAL B N   
15189 C CA  . VAL B 888  ? 0.2816 0.2930 0.3179 0.0630  -0.0438 -0.0582 886  VAL B CA  
15190 C C   . VAL B 888  ? 0.2441 0.2596 0.2814 0.0669  -0.0418 -0.0609 886  VAL B C   
15191 O O   . VAL B 888  ? 0.2544 0.2647 0.2883 0.0717  -0.0444 -0.0633 886  VAL B O   
15192 C CB  . VAL B 888  ? 0.3101 0.3309 0.3543 0.0631  -0.0432 -0.0577 886  VAL B CB  
15193 C CG1 . VAL B 888  ? 0.2683 0.2853 0.3109 0.0587  -0.0447 -0.0550 886  VAL B CG1 
15194 C CG2 . VAL B 888  ? 0.2856 0.3095 0.3333 0.0692  -0.0457 -0.0602 886  VAL B CG2 
15195 N N   . ILE B 889  ? 0.2687 0.2932 0.3104 0.0651  -0.0374 -0.0605 887  ILE B N   
15196 C CA  . ILE B 889  ? 0.2654 0.2916 0.3055 0.0674  -0.0352 -0.0625 887  ILE B CA  
15197 C C   . ILE B 889  ? 0.2456 0.2781 0.2895 0.0741  -0.0353 -0.0658 887  ILE B C   
15198 O O   . ILE B 889  ? 0.2603 0.2897 0.3001 0.0781  -0.0357 -0.0684 887  ILE B O   
15199 C CB  . ILE B 889  ? 0.2483 0.2819 0.2914 0.0632  -0.0306 -0.0608 887  ILE B CB  
15200 C CG1 . ILE B 889  ? 0.2645 0.2988 0.3047 0.0649  -0.0285 -0.0626 887  ILE B CG1 
15201 C CG2 . ILE B 889  ? 0.2521 0.2978 0.3041 0.0624  -0.0280 -0.0598 887  ILE B CG2 
15202 C CD1 . ILE B 889  ? 0.2791 0.3010 0.3101 0.0644  -0.0310 -0.0631 887  ILE B CD1 
15203 N N   . THR B 890  ? 0.2619 0.3033 0.3133 0.0758  -0.0352 -0.0659 888  THR B N   
15204 C CA  . THR B 890  ? 0.2538 0.3038 0.3100 0.0821  -0.0347 -0.0688 888  THR B CA  
15205 C C   . THR B 890  ? 0.2273 0.2808 0.2886 0.0845  -0.0375 -0.0688 888  THR B C   
15206 O O   . THR B 890  ? 0.2452 0.2965 0.3075 0.0805  -0.0390 -0.0664 888  THR B O   
15207 C CB  . THR B 890  ? 0.2601 0.3244 0.3232 0.0814  -0.0296 -0.0685 888  THR B CB  
15208 O OG1 . THR B 890  ? 0.2927 0.3635 0.3619 0.0762  -0.0282 -0.0655 888  THR B OG1 
15209 C CG2 . THR B 890  ? 0.2245 0.2869 0.2830 0.0793  -0.0266 -0.0685 888  THR B CG2 
15210 N N   . SER B 891  ? 0.3202 0.3801 0.3852 0.0911  -0.0381 -0.0717 889  SER B N   
15211 C CA  . SER B 891  ? 0.2608 0.3272 0.3324 0.0937  -0.0403 -0.0718 889  SER B CA  
15212 C C   . SER B 891  ? 0.3010 0.3790 0.3810 0.0886  -0.0376 -0.0691 889  SER B C   
15213 O O   . SER B 891  ? 0.3163 0.3946 0.3992 0.0868  -0.0401 -0.0676 889  SER B O   
15214 C CB  . SER B 891  ? 0.3250 0.3992 0.4001 0.1019  -0.0404 -0.0753 889  SER B CB  
15215 O OG  . SER B 891  ? 0.4313 0.4935 0.4985 0.1074  -0.0442 -0.0781 889  SER B OG  
15216 N N   . GLU B 892  ? 0.2872 0.3746 0.3710 0.0862  -0.0329 -0.0684 890  GLU B N   
15217 C CA  . GLU B 892  ? 0.2994 0.3977 0.3911 0.0813  -0.0305 -0.0658 890  GLU B CA  
15218 C C   . GLU B 892  ? 0.2992 0.3896 0.3881 0.0747  -0.0315 -0.0629 890  GLU B C   
15219 O O   . GLU B 892  ? 0.3204 0.4149 0.4143 0.0718  -0.0324 -0.0612 890  GLU B O   
15220 C CB  . GLU B 892  ? 0.3321 0.4409 0.4274 0.0800  -0.0252 -0.0655 890  GLU B CB  
15221 N N   . ALA B 893  ? 0.3009 0.3803 0.3819 0.0723  -0.0313 -0.0623 891  ALA B N   
15222 C CA  . ALA B 893  ? 0.2963 0.3676 0.3737 0.0669  -0.0326 -0.0597 891  ALA B CA  
15223 C C   . ALA B 893  ? 0.3162 0.3821 0.3927 0.0682  -0.0372 -0.0597 891  ALA B C   
15224 O O   . ALA B 893  ? 0.3189 0.3859 0.3978 0.0647  -0.0382 -0.0579 891  ALA B O   
15225 C CB  . ALA B 893  ? 0.2764 0.3372 0.3453 0.0649  -0.0321 -0.0593 891  ALA B CB  
15226 N N   . LYS B 894  ? 0.2938 0.3536 0.3663 0.0732  -0.0404 -0.0618 892  LYS B N   
15227 C CA  . LYS B 894  ? 0.2701 0.3239 0.3410 0.0747  -0.0452 -0.0618 892  LYS B CA  
15228 C C   . LYS B 894  ? 0.3323 0.3969 0.4120 0.0752  -0.0459 -0.0615 892  LYS B C   
15229 O O   . LYS B 894  ? 0.3135 0.3759 0.3934 0.0721  -0.0481 -0.0598 892  LYS B O   
15230 C CB  . LYS B 894  ? 0.3046 0.3508 0.3703 0.0808  -0.0485 -0.0643 892  LYS B CB  
15231 C CG  . LYS B 894  ? 0.3124 0.3540 0.3773 0.0837  -0.0537 -0.0645 892  LYS B CG  
15232 C CD  . LYS B 894  ? 0.2865 0.3184 0.3449 0.0895  -0.0572 -0.0669 892  LYS B CD  
15233 C CE  . LYS B 894  ? 0.3939 0.4240 0.4531 0.0942  -0.0622 -0.0677 892  LYS B CE  
15234 N NZ  . LYS B 894  ? 0.4555 0.4729 0.5075 0.0913  -0.0662 -0.0656 892  LYS B NZ  
15235 N N   . ASP B 895  ? 0.2949 0.3715 0.3818 0.0787  -0.0441 -0.0631 893  ASP B N   
15236 C CA  . ASP B 895  ? 0.3326 0.4206 0.4285 0.0789  -0.0449 -0.0627 893  ASP B CA  
15237 C C   . ASP B 895  ? 0.3029 0.3947 0.4022 0.0719  -0.0432 -0.0599 893  ASP B C   
15238 O O   . ASP B 895  ? 0.3479 0.4419 0.4507 0.0702  -0.0457 -0.0589 893  ASP B O   
15239 C CB  . ASP B 895  ? 0.3240 0.4260 0.4274 0.0834  -0.0425 -0.0646 893  ASP B CB  
15240 C CG  . ASP B 895  ? 0.3699 0.4686 0.4701 0.0913  -0.0444 -0.0678 893  ASP B CG  
15241 O OD1 . ASP B 895  ? 0.4511 0.5381 0.5451 0.0935  -0.0487 -0.0684 893  ASP B OD1 
15242 O OD2 . ASP B 895  ? 0.4423 0.5501 0.5460 0.0952  -0.0416 -0.0697 893  ASP B OD2 
15243 N N   . ASN B 896  ? 0.2800 0.3725 0.3783 0.0680  -0.0391 -0.0587 894  ASN B N   
15244 C CA  . ASN B 896  ? 0.3260 0.4209 0.4267 0.0616  -0.0374 -0.0562 894  ASN B CA  
15245 C C   . ASN B 896  ? 0.3574 0.4415 0.4525 0.0584  -0.0404 -0.0548 894  ASN B C   
15246 O O   . ASN B 896  ? 0.3352 0.4216 0.4335 0.0551  -0.0416 -0.0535 894  ASN B O   
15247 C CB  . ASN B 896  ? 0.3507 0.4465 0.4499 0.0588  -0.0329 -0.0553 894  ASN B CB  
15248 C CG  . ASN B 896  ? 0.5003 0.5991 0.6022 0.0526  -0.0309 -0.0527 894  ASN B CG  
15249 O OD1 . ASN B 896  ? 0.5625 0.6559 0.6626 0.0493  -0.0330 -0.0514 894  ASN B OD1 
15250 N ND2 . ASN B 896  ? 0.5481 0.6552 0.6539 0.0509  -0.0271 -0.0519 894  ASN B ND2 
15251 N N   . ILE B 897  ? 0.3176 0.3900 0.4043 0.0593  -0.0417 -0.0551 895  ILE B N   
15252 C CA  . ILE B 897  ? 0.3250 0.3875 0.4058 0.0565  -0.0443 -0.0538 895  ILE B CA  
15253 C C   . ILE B 897  ? 0.3110 0.3732 0.3933 0.0586  -0.0489 -0.0542 895  ILE B C   
15254 O O   . ILE B 897  ? 0.3252 0.3859 0.4074 0.0555  -0.0505 -0.0530 895  ILE B O   
15255 C CB  . ILE B 897  ? 0.3261 0.3770 0.3977 0.0569  -0.0447 -0.0538 895  ILE B CB  
15256 C CG1 . ILE B 897  ? 0.2881 0.3392 0.3580 0.0542  -0.0405 -0.0531 895  ILE B CG1 
15257 C CG2 . ILE B 897  ? 0.2824 0.3239 0.3479 0.0545  -0.0477 -0.0523 895  ILE B CG2 
15258 C CD1 . ILE B 897  ? 0.2702 0.3130 0.3329 0.0558  -0.0407 -0.0538 895  ILE B CD1 
15259 N N   . GLU B 898  ? 0.3420 0.4051 0.4252 0.0641  -0.0511 -0.0561 896  GLU B N   
15260 C CA  . GLU B 898  ? 0.3661 0.4284 0.4503 0.0665  -0.0558 -0.0565 896  GLU B CA  
15261 C C   . GLU B 898  ? 0.3687 0.4426 0.4621 0.0652  -0.0561 -0.0561 896  GLU B C   
15262 O O   . GLU B 898  ? 0.4153 0.4879 0.5090 0.0644  -0.0597 -0.0555 896  GLU B O   
15263 C CB  . GLU B 898  ? 0.3608 0.4213 0.4439 0.0733  -0.0583 -0.0587 896  GLU B CB  
15264 C CG  . GLU B 898  ? 0.3876 0.4347 0.4607 0.0742  -0.0592 -0.0589 896  GLU B CG  
15265 C CD  . GLU B 898  ? 0.4588 0.5022 0.5298 0.0811  -0.0622 -0.0613 896  GLU B CD  
15266 O OE1 . GLU B 898  ? 0.4818 0.5349 0.5593 0.0859  -0.0616 -0.0633 896  GLU B OE1 
15267 O OE2 . GLU B 898  ? 0.5077 0.5384 0.5702 0.0819  -0.0653 -0.0610 896  GLU B OE2 
15268 N N   . LYS B 899  ? 0.3693 0.4547 0.4700 0.0645  -0.0525 -0.0562 897  LYS B N   
15269 C CA  . LYS B 899  ? 0.3431 0.4396 0.4525 0.0620  -0.0526 -0.0554 897  LYS B CA  
15270 C C   . LYS B 899  ? 0.3619 0.4537 0.4690 0.0558  -0.0532 -0.0534 897  LYS B C   
15271 O O   . LYS B 899  ? 0.3179 0.4128 0.4286 0.0542  -0.0561 -0.0528 897  LYS B O   
15272 C CB  . LYS B 899  ? 0.4054 0.5143 0.5219 0.0616  -0.0482 -0.0554 897  LYS B CB  
15273 C CG  . LYS B 899  ? 0.4194 0.5398 0.5448 0.0576  -0.0478 -0.0539 897  LYS B CG  
15274 C CD  . LYS B 899  ? 0.4744 0.6037 0.6041 0.0553  -0.0427 -0.0530 897  LYS B CD  
15275 C CE  . LYS B 899  ? 0.5073 0.6492 0.6464 0.0514  -0.0424 -0.0514 897  LYS B CE  
15276 N NZ  . LYS B 899  ? 0.5243 0.6724 0.6659 0.0479  -0.0376 -0.0499 897  LYS B NZ  
15277 N N   . HIS B 900  ? 0.2928 0.3771 0.3938 0.0526  -0.0507 -0.0524 898  HIS B N   
15278 C CA  . HIS B 900  ? 0.3147 0.3930 0.4121 0.0476  -0.0514 -0.0508 898  HIS B CA  
15279 C C   . HIS B 900  ? 0.3447 0.4145 0.4366 0.0484  -0.0559 -0.0509 898  HIS B C   
15280 O O   . HIS B 900  ? 0.3808 0.4499 0.4730 0.0457  -0.0582 -0.0502 898  HIS B O   
15281 C CB  . HIS B 900  ? 0.4022 0.4742 0.4938 0.0448  -0.0478 -0.0498 898  HIS B CB  
15282 C CG  . HIS B 900  ? 0.3994 0.4643 0.4862 0.0407  -0.0486 -0.0485 898  HIS B CG  
15283 N ND1 . HIS B 900  ? 0.4033 0.4717 0.4935 0.0367  -0.0482 -0.0476 898  HIS B ND1 
15284 C CD2 . HIS B 900  ? 0.3973 0.4520 0.4758 0.0400  -0.0497 -0.0481 898  HIS B CD2 
15285 C CE1 . HIS B 900  ? 0.4187 0.4791 0.5028 0.0342  -0.0490 -0.0469 898  HIS B CE1 
15286 N NE2 . HIS B 900  ? 0.3852 0.4378 0.4623 0.0362  -0.0498 -0.0471 898  HIS B NE2 
15287 N N   . ILE B 901  ? 0.3413 0.4039 0.4274 0.0520  -0.0573 -0.0517 899  ILE B N   
15288 C CA  . ILE B 901  ? 0.3202 0.3737 0.3999 0.0526  -0.0615 -0.0514 899  ILE B CA  
15289 C C   . ILE B 901  ? 0.3949 0.4537 0.4798 0.0545  -0.0657 -0.0519 899  ILE B C   
15290 O O   . ILE B 901  ? 0.4746 0.5296 0.5568 0.0526  -0.0687 -0.0513 899  ILE B O   
15291 C CB  . ILE B 901  ? 0.3665 0.4113 0.4393 0.0560  -0.0624 -0.0519 899  ILE B CB  
15292 C CG1 . ILE B 901  ? 0.3116 0.3506 0.3786 0.0533  -0.0588 -0.0510 899  ILE B CG1 
15293 C CG2 . ILE B 901  ? 0.3585 0.3950 0.4253 0.0572  -0.0673 -0.0515 899  ILE B CG2 
15294 C CD1 . ILE B 901  ? 0.3319 0.3620 0.3918 0.0557  -0.0599 -0.0512 899  ILE B CD1 
15295 N N   . GLU B 902  ? 0.4250 0.4932 0.5173 0.0582  -0.0658 -0.0532 900  GLU B N   
15296 C CA  . GLU B 902  ? 0.3877 0.4626 0.4859 0.0602  -0.0698 -0.0537 900  GLU B CA  
15297 C C   . GLU B 902  ? 0.3938 0.4752 0.4974 0.0553  -0.0699 -0.0527 900  GLU B C   
15298 O O   . GLU B 902  ? 0.4456 0.5272 0.5501 0.0548  -0.0741 -0.0525 900  GLU B O   
15299 C CB  . GLU B 902  ? 0.4129 0.4977 0.5183 0.0656  -0.0693 -0.0554 900  GLU B CB  
15300 C CG  . GLU B 902  ? 0.4501 0.5272 0.5498 0.0714  -0.0708 -0.0568 900  GLU B CG  
15301 C CD  . GLU B 902  ? 0.4951 0.5611 0.5875 0.0723  -0.0759 -0.0563 900  GLU B CD  
15302 O OE1 . GLU B 902  ? 0.5341 0.6036 0.6298 0.0733  -0.0799 -0.0563 900  GLU B OE1 
15303 O OE2 . GLU B 902  ? 0.5522 0.6060 0.6352 0.0717  -0.0760 -0.0558 900  GLU B OE2 
15304 N N   . ARG B 903  ? 0.3584 0.4449 0.4655 0.0516  -0.0658 -0.0519 901  ARG B N   
15305 C CA  . ARG B 903  ? 0.4085 0.4991 0.5194 0.0463  -0.0661 -0.0508 901  ARG B CA  
15306 C C   . ARG B 903  ? 0.4982 0.5777 0.6010 0.0432  -0.0684 -0.0501 901  ARG B C   
15307 O O   . ARG B 903  ? 0.5142 0.5948 0.6186 0.0410  -0.0717 -0.0498 901  ARG B O   
15308 C CB  . ARG B 903  ? 0.4024 0.4983 0.5169 0.0429  -0.0612 -0.0499 901  ARG B CB  
15309 C CG  . ARG B 903  ? 0.4787 0.5777 0.5965 0.0371  -0.0616 -0.0485 901  ARG B CG  
15310 C CD  . ARG B 903  ? 0.5651 0.6647 0.6830 0.0334  -0.0569 -0.0474 901  ARG B CD  
15311 N NE  . ARG B 903  ? 0.6670 0.7674 0.7869 0.0278  -0.0578 -0.0461 901  ARG B NE  
15312 C CZ  . ARG B 903  ? 0.7367 0.8476 0.8650 0.0248  -0.0572 -0.0450 901  ARG B CZ  
15313 N NH1 . ARG B 903  ? 0.7435 0.8663 0.8794 0.0270  -0.0553 -0.0450 901  ARG B NH1 
15314 N NH2 . ARG B 903  ? 0.6786 0.7881 0.8075 0.0194  -0.0586 -0.0438 901  ARG B NH2 
15315 N N   . MET B 904  ? 0.4561 0.5252 0.5501 0.0431  -0.0667 -0.0498 902  MET B N   
15316 C CA  . MET B 904  ? 0.4891 0.5482 0.5750 0.0407  -0.0687 -0.0493 902  MET B CA  
15317 C C   . MET B 904  ? 0.4826 0.5383 0.5659 0.0431  -0.0740 -0.0497 902  MET B C   
15318 O O   . MET B 904  ? 0.4876 0.5406 0.5687 0.0409  -0.0770 -0.0494 902  MET B O   
15319 C CB  . MET B 904  ? 0.4336 0.4836 0.5110 0.0403  -0.0658 -0.0487 902  MET B CB  
15320 C CG  . MET B 904  ? 0.4204 0.4724 0.4991 0.0374  -0.0610 -0.0481 902  MET B CG  
15321 S SD  . MET B 904  ? 0.5028 0.5564 0.5836 0.0322  -0.0610 -0.0475 902  MET B SD  
15322 C CE  . MET B 904  ? 0.5042 0.5706 0.5962 0.0313  -0.0586 -0.0473 902  MET B CE  
15323 N N   . ARG B 905  ? 0.4875 0.5427 0.5705 0.0479  -0.0754 -0.0503 903  ARG B N   
15324 C CA  . ARG B 905  ? 0.5082 0.5601 0.5887 0.0506  -0.0806 -0.0506 903  ARG B CA  
15325 C C   . ARG B 905  ? 0.5064 0.5675 0.5951 0.0504  -0.0839 -0.0510 903  ARG B C   
15326 O O   . ARG B 905  ? 0.5397 0.5978 0.6258 0.0498  -0.0883 -0.0508 903  ARG B O   
15327 C CB  . ARG B 905  ? 0.5413 0.5906 0.6202 0.0560  -0.0816 -0.0513 903  ARG B CB  
15328 C CG  . ARG B 905  ? 0.5776 0.6157 0.6472 0.0576  -0.0855 -0.0507 903  ARG B CG  
15329 C CD  . ARG B 905  ? 0.6303 0.6664 0.6993 0.0634  -0.0876 -0.0516 903  ARG B CD  
15330 N NE  . ARG B 905  ? 0.5583 0.5929 0.6262 0.0649  -0.0838 -0.0522 903  ARG B NE  
15331 C CZ  . ARG B 905  ? 0.5207 0.5446 0.5799 0.0649  -0.0835 -0.0515 903  ARG B CZ  
15332 N NH1 . ARG B 905  ? 0.5647 0.5787 0.6153 0.0633  -0.0862 -0.0500 903  ARG B NH1 
15333 N NH2 . ARG B 905  ? 0.5052 0.5285 0.5641 0.0664  -0.0804 -0.0522 903  ARG B NH2 
15334 N N   . GLY B 906  ? 0.5017 0.5747 0.6002 0.0507  -0.0820 -0.0514 904  GLY B N   
15335 C CA  . GLY B 906  ? 0.5334 0.6167 0.6406 0.0500  -0.0849 -0.0515 904  GLY B CA  
15336 C C   . GLY B 906  ? 0.5583 0.6403 0.6648 0.0440  -0.0858 -0.0507 904  GLY B C   
15337 O O   . GLY B 906  ? 0.5099 0.5961 0.6200 0.0428  -0.0899 -0.0506 904  GLY B O   
15338 N N   . LEU B 907  ? 0.5663 0.6425 0.6680 0.0403  -0.0822 -0.0500 905  LEU B N   
15339 C CA  . LEU B 907  ? 0.5570 0.6300 0.6565 0.0351  -0.0832 -0.0495 905  LEU B CA  
15340 C C   . LEU B 907  ? 0.5725 0.6346 0.6624 0.0348  -0.0868 -0.0496 905  LEU B C   
15341 O O   . LEU B 907  ? 0.6487 0.7075 0.7360 0.0310  -0.0883 -0.0496 905  LEU B O   
15342 C CB  . LEU B 907  ? 0.5299 0.6004 0.6275 0.0318  -0.0781 -0.0489 905  LEU B CB  
15343 N N   . GLY B 908  ? 0.5671 0.6232 0.6512 0.0387  -0.0882 -0.0498 906  GLY B N   
15344 C CA  . GLY B 908  ? 0.5116 0.5582 0.5866 0.0387  -0.0918 -0.0497 906  GLY B CA  
15345 C C   . GLY B 908  ? 0.5644 0.6003 0.6289 0.0383  -0.0892 -0.0491 906  GLY B C   
15346 O O   . GLY B 908  ? 0.4525 0.4806 0.5088 0.0385  -0.0919 -0.0488 906  GLY B O   
15347 N N   . ARG B 909  ? 0.4854 0.5211 0.5499 0.0375  -0.0841 -0.0489 907  ARG B N   
15348 C CA  . ARG B 909  ? 0.4245 0.4512 0.4796 0.0365  -0.0814 -0.0482 907  ARG B CA  
15349 C C   . ARG B 909  ? 0.5010 0.5216 0.5500 0.0397  -0.0826 -0.0476 907  ARG B C   
15350 O O   . ARG B 909  ? 0.5504 0.5737 0.6031 0.0431  -0.0838 -0.0479 907  ARG B O   
15351 C CB  . ARG B 909  ? 0.4699 0.4989 0.5274 0.0350  -0.0760 -0.0479 907  ARG B CB  
15352 N N   . LYS B 910  ? 0.4371 0.4492 0.4765 0.0385  -0.0824 -0.0467 908  LYS B N   
15353 C CA  . LYS B 910  ? 0.4329 0.4382 0.4655 0.0406  -0.0833 -0.0456 908  LYS B CA  
15354 C C   . LYS B 910  ? 0.5208 0.5264 0.5545 0.0414  -0.0793 -0.0453 908  LYS B C   
15355 O O   . LYS B 910  ? 0.5212 0.5279 0.5552 0.0392  -0.0751 -0.0452 908  LYS B O   
15356 C CB  . LYS B 910  ? 0.4196 0.4169 0.4417 0.0386  -0.0838 -0.0444 908  LYS B CB  
15357 N N   . VAL B 911  ? 0.5036 0.5075 0.5373 0.0448  -0.0810 -0.0453 909  VAL B N   
15358 C CA  . VAL B 911  ? 0.4374 0.4414 0.4724 0.0463  -0.0781 -0.0454 909  VAL B CA  
15359 C C   . VAL B 911  ? 0.4651 0.4600 0.4921 0.0478  -0.0803 -0.0443 909  VAL B C   
15360 O O   . VAL B 911  ? 0.5250 0.5175 0.5513 0.0509  -0.0847 -0.0445 909  VAL B O   
15361 C CB  . VAL B 911  ? 0.4836 0.4962 0.5283 0.0495  -0.0781 -0.0471 909  VAL B CB  
15362 C CG1 . VAL B 911  ? 0.4287 0.4406 0.4736 0.0515  -0.0755 -0.0475 909  VAL B CG1 
15363 C CG2 . VAL B 911  ? 0.4421 0.4639 0.4947 0.0473  -0.0760 -0.0478 909  VAL B CG2 
15364 N N   . GLU B 912  ? 0.4806 0.4702 0.5015 0.0455  -0.0776 -0.0429 910  GLU B N   
15365 C CA  . GLU B 912  ? 0.4313 0.4120 0.4445 0.0461  -0.0794 -0.0414 910  GLU B CA  
15366 C C   . GLU B 912  ? 0.4740 0.4546 0.4891 0.0477  -0.0772 -0.0421 910  GLU B C   
15367 O O   . GLU B 912  ? 0.3998 0.3847 0.4179 0.0460  -0.0728 -0.0424 910  GLU B O   
15368 C CB  . GLU B 912  ? 0.4728 0.4480 0.4775 0.0421  -0.0781 -0.0391 910  GLU B CB  
15369 C CG  . GLU B 912  ? 0.4499 0.4158 0.4461 0.0417  -0.0801 -0.0370 910  GLU B CG  
15370 C CD  . GLU B 912  ? 0.5366 0.4965 0.5269 0.0424  -0.0851 -0.0358 910  GLU B CD  
15371 O OE1 . GLU B 912  ? 0.4872 0.4501 0.4787 0.0423  -0.0864 -0.0363 910  GLU B OE1 
15372 O OE2 . GLU B 912  ? 0.5771 0.5290 0.5613 0.0430  -0.0880 -0.0343 910  GLU B OE2 
15373 N N   . GLN B 913  ? 0.4030 0.3782 0.4158 0.0510  -0.0805 -0.0423 911  GLN B N   
15374 C CA  . GLN B 913  ? 0.4491 0.4231 0.4626 0.0529  -0.0790 -0.0432 911  GLN B CA  
15375 C C   . GLN B 913  ? 0.4962 0.4587 0.5011 0.0535  -0.0822 -0.0419 911  GLN B C   
15376 O O   . GLN B 913  ? 0.5011 0.4576 0.5017 0.0549  -0.0868 -0.0410 911  GLN B O   
15377 C CB  . GLN B 913  ? 0.3985 0.3796 0.4205 0.0579  -0.0795 -0.0460 911  GLN B CB  
15378 C CG  . GLN B 913  ? 0.4430 0.4358 0.4739 0.0569  -0.0754 -0.0472 911  GLN B CG  
15379 C CD  . GLN B 913  ? 0.4136 0.4142 0.4527 0.0616  -0.0754 -0.0497 911  GLN B CD  
15380 O OE1 . GLN B 913  ? 0.4625 0.4639 0.5037 0.0656  -0.0792 -0.0506 911  GLN B OE1 
15381 N NE2 . GLN B 913  ? 0.3346 0.3414 0.3783 0.0614  -0.0711 -0.0507 911  GLN B NE2 
15382 N N   . ILE B 914  ? 0.4717 0.4310 0.4739 0.0522  -0.0799 -0.0415 912  ILE B N   
15383 C CA  . ILE B 914  ? 0.4677 0.4161 0.4625 0.0530  -0.0829 -0.0407 912  ILE B CA  
15384 C C   . ILE B 914  ? 0.5191 0.4659 0.5163 0.0594  -0.0865 -0.0432 912  ILE B C   
15385 O O   . ILE B 914  ? 0.5060 0.4611 0.5111 0.0629  -0.0846 -0.0459 912  ILE B O   
15386 C CB  . ILE B 914  ? 0.4816 0.4287 0.4745 0.0502  -0.0793 -0.0403 912  ILE B CB  
15387 C CG1 . ILE B 914  ? 0.4700 0.4161 0.4583 0.0441  -0.0770 -0.0372 912  ILE B CG1 
15388 C CG2 . ILE B 914  ? 0.5285 0.4661 0.5163 0.0524  -0.0823 -0.0407 912  ILE B CG2 
15389 C CD1 . ILE B 914  ? 0.4281 0.3742 0.4152 0.0413  -0.0735 -0.0367 912  ILE B CD1 
15390 N N   . GLY B 915  ? 0.6073 0.5434 0.5976 0.0611  -0.0916 -0.0422 913  GLY B N   
15391 C CA  . GLY B 915  ? 0.6120 0.5447 0.6031 0.0675  -0.0952 -0.0447 913  GLY B CA  
15392 C C   . GLY B 915  ? 0.6176 0.5450 0.6057 0.0684  -0.0942 -0.0458 913  GLY B C   
15393 O O   . GLY B 915  ? 0.7034 0.6217 0.6837 0.0643  -0.0947 -0.0435 913  GLY B O   
15394 N N   . LEU B 916  ? 0.5469 0.4802 0.5412 0.0735  -0.0929 -0.0492 914  LEU B N   
15395 C CA  . LEU B 916  ? 0.4950 0.4240 0.4868 0.0748  -0.0918 -0.0508 914  LEU B CA  
15396 C C   . LEU B 916  ? 0.5204 0.4375 0.5060 0.0801  -0.0974 -0.0521 914  LEU B C   
15397 O O   . LEU B 916  ? 0.5349 0.4516 0.5220 0.0852  -0.1012 -0.0532 914  LEU B O   
15398 C CB  . LEU B 916  ? 0.4635 0.4052 0.4645 0.0777  -0.0872 -0.0539 914  LEU B CB  
15399 C CG  . LEU B 916  ? 0.4914 0.4446 0.4987 0.0729  -0.0815 -0.0529 914  LEU B CG  
15400 C CD1 . LEU B 916  ? 0.4540 0.4178 0.4688 0.0757  -0.0774 -0.0558 914  LEU B CD1 
15401 C CD2 . LEU B 916  ? 0.4574 0.4055 0.4587 0.0659  -0.0795 -0.0499 914  LEU B CD2 
15402 N N   . ALA B 917  ? 0.4730 0.3798 0.4514 0.0788  -0.0982 -0.0519 915  ALA B N   
15403 C CA  . ALA B 917  ? 0.5338 0.4276 0.5052 0.0837  -0.1038 -0.0533 915  ALA B CA  
15404 C C   . ALA B 917  ? 0.5733 0.4730 0.5506 0.0922  -0.1035 -0.0581 915  ALA B C   
15405 O O   . ALA B 917  ? 0.4938 0.4065 0.4793 0.0931  -0.0984 -0.0601 915  ALA B O   
15406 C CB  . ALA B 917  ? 0.5461 0.4274 0.5082 0.0795  -0.1048 -0.0519 915  ALA B CB  
15407 N N   . SER B 918  ? 0.5301 0.4203 0.5031 0.0986  -0.1090 -0.0599 916  SER B N   
15408 C CA  . SER B 918  ? 0.5568 0.4525 0.5348 0.1075  -0.1090 -0.0646 916  SER B CA  
15409 C C   . SER B 918  ? 0.5479 0.4445 0.5254 0.1079  -0.1054 -0.0671 916  SER B C   
15410 O O   . SER B 918  ? 0.5012 0.4096 0.4862 0.1128  -0.1020 -0.0705 916  SER B O   
15411 C CB  . SER B 918  ? 0.6100 0.4931 0.5819 0.1144  -0.1161 -0.0660 916  SER B CB  
15412 O OG  . SER B 918  ? 0.6953 0.5602 0.6552 0.1123  -0.1199 -0.0649 916  SER B OG  
15413 N N   . GLU B 919  ? 0.5620 0.4469 0.5307 0.1026  -0.1060 -0.0654 917  GLU B N   
15414 C CA  . GLU B 919  ? 0.5605 0.4450 0.5277 0.1027  -0.1031 -0.0677 917  GLU B CA  
15415 C C   . GLU B 919  ? 0.5310 0.4326 0.5077 0.1003  -0.0958 -0.0682 917  GLU B C   
15416 O O   . GLU B 919  ? 0.5235 0.4282 0.5009 0.1023  -0.0930 -0.0709 917  GLU B O   
15417 C CB  . GLU B 919  ? 0.5709 0.4409 0.5275 0.0958  -0.1051 -0.0649 917  GLU B CB  
15418 C CG  . GLU B 919  ? 0.7002 0.5508 0.6457 0.0983  -0.1125 -0.0649 917  GLU B CG  
15419 C CD  . GLU B 919  ? 0.8003 0.6443 0.7426 0.0966  -0.1171 -0.0614 917  GLU B CD  
15420 O OE1 . GLU B 919  ? 0.6924 0.5472 0.6412 0.0939  -0.1145 -0.0593 917  GLU B OE1 
15421 O OE2 . GLU B 919  ? 0.8546 0.6821 0.7874 0.0980  -0.1234 -0.0609 917  GLU B OE2 
15422 N N   . THR B 920  ? 0.4653 0.3775 0.4486 0.0961  -0.0929 -0.0656 918  THR B N   
15423 C CA  . THR B 920  ? 0.4330 0.3610 0.4253 0.0939  -0.0864 -0.0659 918  THR B CA  
15424 C C   . THR B 920  ? 0.4617 0.4021 0.4626 0.1013  -0.0844 -0.0698 918  THR B C   
15425 O O   . THR B 920  ? 0.4205 0.3730 0.4278 0.1004  -0.0790 -0.0706 918  THR B O   
15426 C CB  . THR B 920  ? 0.4549 0.3901 0.4516 0.0878  -0.0842 -0.0624 918  THR B CB  
15427 O OG1 . THR B 920  ? 0.4352 0.3734 0.4356 0.0912  -0.0871 -0.0624 918  THR B OG1 
15428 C CG2 . THR B 920  ? 0.4289 0.3539 0.4176 0.0804  -0.0854 -0.0584 918  THR B CG2 
15429 N N   . GLY B 921  ? 0.4070 0.3454 0.4083 0.1086  -0.0885 -0.0720 919  GLY B N   
15430 C CA  . GLY B 921  ? 0.4522 0.4037 0.4621 0.1158  -0.0867 -0.0754 919  GLY B CA  
15431 C C   . GLY B 921  ? 0.4281 0.3843 0.4390 0.1193  -0.0831 -0.0788 919  GLY B C   
15432 O O   . GLY B 921  ? 0.4683 0.4394 0.4880 0.1231  -0.0796 -0.0809 919  GLY B O   
15433 N N   . VAL B 922  ? 0.4084 0.3525 0.4103 0.1178  -0.0839 -0.0794 920  VAL B N   
15434 C CA  . VAL B 922  ? 0.4307 0.3783 0.4324 0.1212  -0.0808 -0.0828 920  VAL B CA  
15435 C C   . VAL B 922  ? 0.4012 0.3589 0.4071 0.1148  -0.0744 -0.0812 920  VAL B C   
15436 O O   . VAL B 922  ? 0.4083 0.3709 0.4148 0.1170  -0.0712 -0.0837 920  VAL B O   
15437 C CB  . VAL B 922  ? 0.4312 0.3606 0.4207 0.1229  -0.0849 -0.0845 920  VAL B CB  
15438 C CG1 . VAL B 922  ? 0.4591 0.3795 0.4447 0.1313  -0.0909 -0.0871 920  VAL B CG1 
15439 C CG2 . VAL B 922  ? 0.4244 0.3414 0.4062 0.1139  -0.0867 -0.0802 920  VAL B CG2 
15440 N N   . GLY B 923  ? 0.3485 0.3092 0.3570 0.1072  -0.0727 -0.0771 921  GLY B N   
15441 C CA  . GLY B 923  ? 0.3338 0.3046 0.3470 0.1015  -0.0669 -0.0755 921  GLY B CA  
15442 C C   . GLY B 923  ? 0.3573 0.3414 0.3802 0.0990  -0.0643 -0.0735 921  GLY B C   
15443 O O   . GLY B 923  ? 0.3661 0.3532 0.3928 0.1026  -0.0668 -0.0739 921  GLY B O   
15444 N N   . THR B 924  ? 0.2976 0.2892 0.3242 0.0930  -0.0597 -0.0713 922  THR B N   
15445 C CA  . THR B 924  ? 0.3025 0.3059 0.3378 0.0899  -0.0572 -0.0693 922  THR B CA  
15446 C C   . THR B 924  ? 0.2841 0.2816 0.3161 0.0826  -0.0578 -0.0655 922  THR B C   
15447 O O   . THR B 924  ? 0.3069 0.3053 0.3380 0.0774  -0.0546 -0.0637 922  THR B O   
15448 C CB  . THR B 924  ? 0.2684 0.2855 0.3106 0.0890  -0.0515 -0.0697 922  THR B CB  
15449 O OG1 . THR B 924  ? 0.2898 0.3026 0.3269 0.0857  -0.0492 -0.0693 922  THR B OG1 
15450 C CG2 . THR B 924  ? 0.3260 0.3518 0.3730 0.0963  -0.0508 -0.0732 922  THR B CG2 
15451 N N   . PHE B 925  ? 0.3046 0.2969 0.3350 0.0825  -0.0617 -0.0642 923  PHE B N   
15452 C CA  . PHE B 925  ? 0.2825 0.2694 0.3093 0.0762  -0.0625 -0.0607 923  PHE B CA  
15453 C C   . PHE B 925  ? 0.3414 0.3365 0.3749 0.0748  -0.0622 -0.0595 923  PHE B C   
15454 O O   . PHE B 925  ? 0.3539 0.3539 0.3922 0.0793  -0.0642 -0.0609 923  PHE B O   
15455 C CB  . PHE B 925  ? 0.3074 0.2793 0.3249 0.0763  -0.0677 -0.0598 923  PHE B CB  
15456 C CG  . PHE B 925  ? 0.3022 0.2640 0.3119 0.0763  -0.0686 -0.0605 923  PHE B CG  
15457 C CD1 . PHE B 925  ? 0.3186 0.2770 0.3265 0.0826  -0.0705 -0.0638 923  PHE B CD1 
15458 C CD2 . PHE B 925  ? 0.3000 0.2558 0.3041 0.0700  -0.0678 -0.0578 923  PHE B CD2 
15459 C CE1 . PHE B 925  ? 0.3302 0.2781 0.3301 0.0824  -0.0718 -0.0646 923  PHE B CE1 
15460 C CE2 . PHE B 925  ? 0.2890 0.2354 0.2858 0.0694  -0.0689 -0.0583 923  PHE B CE2 
15461 C CZ  . PHE B 925  ? 0.3081 0.2500 0.3026 0.0755  -0.0711 -0.0618 923  PHE B CZ  
15462 N N   . VAL B 926  ? 0.2995 0.2962 0.3332 0.0688  -0.0600 -0.0568 924  VAL B N   
15463 C CA  . VAL B 926  ? 0.2770 0.2781 0.3144 0.0665  -0.0604 -0.0553 924  VAL B CA  
15464 C C   . VAL B 926  ? 0.2879 0.2789 0.3176 0.0624  -0.0627 -0.0526 924  VAL B C   
15465 O O   . VAL B 926  ? 0.2987 0.2855 0.3238 0.0585  -0.0609 -0.0511 924  VAL B O   
15466 C CB  . VAL B 926  ? 0.2353 0.2473 0.2795 0.0631  -0.0558 -0.0546 924  VAL B CB  
15467 C CG1 . VAL B 926  ? 0.2750 0.2894 0.3215 0.0602  -0.0568 -0.0529 924  VAL B CG1 
15468 C CG2 . VAL B 926  ? 0.2805 0.3035 0.3327 0.0668  -0.0536 -0.0568 924  VAL B CG2 
15469 N N   . PRO B 927  ? 0.2975 0.2849 0.3254 0.0630  -0.0666 -0.0518 925  PRO B N   
15470 C CA  . PRO B 927  ? 0.3214 0.2997 0.3416 0.0590  -0.0685 -0.0491 925  PRO B CA  
15471 C C   . PRO B 927  ? 0.3036 0.2865 0.3251 0.0537  -0.0651 -0.0472 925  PRO B C   
15472 O O   . PRO B 927  ? 0.2978 0.2900 0.3263 0.0535  -0.0630 -0.0478 925  PRO B O   
15473 C CB  . PRO B 927  ? 0.3874 0.3625 0.4066 0.0617  -0.0735 -0.0490 925  PRO B CB  
15474 C CG  . PRO B 927  ? 0.3564 0.3424 0.3850 0.0654  -0.0730 -0.0512 925  PRO B CG  
15475 C CD  . PRO B 927  ? 0.3026 0.2942 0.3354 0.0676  -0.0696 -0.0533 925  PRO B CD  
15476 N N   . PRO B 928  ? 0.3362 0.3131 0.3511 0.0495  -0.0644 -0.0449 926  PRO B N   
15477 C CA  . PRO B 928  ? 0.3334 0.3138 0.3486 0.0450  -0.0618 -0.0431 926  PRO B CA  
15478 C C   . PRO B 928  ? 0.3520 0.3348 0.3692 0.0454  -0.0638 -0.0430 926  PRO B C   
15479 O O   . PRO B 928  ? 0.3754 0.3530 0.3892 0.0469  -0.0680 -0.0426 926  PRO B O   
15480 C CB  . PRO B 928  ? 0.3801 0.3524 0.3867 0.0413  -0.0622 -0.0405 926  PRO B CB  
15481 C CG  . PRO B 928  ? 0.4053 0.3730 0.4097 0.0428  -0.0627 -0.0413 926  PRO B CG  
15482 C CD  . PRO B 928  ? 0.3984 0.3661 0.4060 0.0484  -0.0656 -0.0439 926  PRO B CD  
15483 N N   . THR B 929  ? 0.3117 0.3023 0.3343 0.0439  -0.0610 -0.0433 927  THR B N   
15484 C CA  . THR B 929  ? 0.3230 0.3175 0.3492 0.0444  -0.0629 -0.0438 927  THR B CA  
15485 C C   . THR B 929  ? 0.3297 0.3260 0.3549 0.0406  -0.0607 -0.0427 927  THR B C   
15486 O O   . THR B 929  ? 0.3184 0.3178 0.3450 0.0384  -0.0567 -0.0424 927  THR B O   
15487 C CB  . THR B 929  ? 0.3028 0.3062 0.3382 0.0473  -0.0623 -0.0460 927  THR B CB  
15488 O OG1 . THR B 929  ? 0.3208 0.3228 0.3568 0.0516  -0.0641 -0.0473 927  THR B OG1 
15489 C CG2 . THR B 929  ? 0.3317 0.3390 0.3708 0.0477  -0.0649 -0.0464 927  THR B CG2 
15490 N N   . ILE B 930  ? 0.3225 0.3166 0.3450 0.0399  -0.0634 -0.0421 928  ILE B N   
15491 C CA  . ILE B 930  ? 0.3893 0.3848 0.4105 0.0370  -0.0619 -0.0415 928  ILE B CA  
15492 C C   . ILE B 930  ? 0.4101 0.4101 0.4365 0.0379  -0.0642 -0.0428 928  ILE B C   
15493 O O   . ILE B 930  ? 0.4173 0.4156 0.4433 0.0399  -0.0683 -0.0431 928  ILE B O   
15494 C CB  . ILE B 930  ? 0.3480 0.3366 0.3601 0.0350  -0.0631 -0.0395 928  ILE B CB  
15495 C CG1 . ILE B 930  ? 0.4089 0.3933 0.4161 0.0337  -0.0614 -0.0379 928  ILE B CG1 
15496 C CG2 . ILE B 930  ? 0.3958 0.3861 0.4064 0.0326  -0.0614 -0.0393 928  ILE B CG2 
15497 C CD1 . ILE B 930  ? 0.3806 0.3588 0.3788 0.0315  -0.0627 -0.0355 928  ILE B CD1 
15498 N N   . ILE B 931  ? 0.3577 0.3634 0.3891 0.0364  -0.0618 -0.0435 929  ILE B N   
15499 C CA  . ILE B 931  ? 0.3657 0.3761 0.4024 0.0364  -0.0638 -0.0446 929  ILE B CA  
15500 C C   . ILE B 931  ? 0.4015 0.4102 0.4348 0.0335  -0.0631 -0.0443 929  ILE B C   
15501 O O   . ILE B 931  ? 0.3498 0.3586 0.3820 0.0317  -0.0595 -0.0439 929  ILE B O   
15502 C CB  . ILE B 931  ? 0.3601 0.3790 0.4062 0.0370  -0.0619 -0.0456 929  ILE B CB  
15503 C CG1 . ILE B 931  ? 0.3445 0.3653 0.3936 0.0405  -0.0624 -0.0463 929  ILE B CG1 
15504 C CG2 . ILE B 931  ? 0.3915 0.4157 0.4433 0.0362  -0.0641 -0.0464 929  ILE B CG2 
15505 C CD1 . ILE B 931  ? 0.3547 0.3849 0.4130 0.0415  -0.0607 -0.0473 929  ILE B CD1 
15506 N N   . GLU B 932  ? 0.3964 0.4032 0.4275 0.0333  -0.0667 -0.0446 930  GLU B N   
15507 C CA  . GLU B 932  ? 0.4276 0.4322 0.4547 0.0310  -0.0665 -0.0447 930  GLU B CA  
15508 C C   . GLU B 932  ? 0.4137 0.4234 0.4477 0.0298  -0.0672 -0.0459 930  GLU B C   
15509 O O   . GLU B 932  ? 0.4691 0.4825 0.5081 0.0307  -0.0704 -0.0466 930  GLU B O   
15510 C CB  . GLU B 932  ? 0.4492 0.4479 0.4685 0.0313  -0.0701 -0.0443 930  GLU B CB  
15511 C CG  . GLU B 932  ? 0.4845 0.4778 0.4961 0.0313  -0.0688 -0.0426 930  GLU B CG  
15512 C CD  . GLU B 932  ? 0.5849 0.5727 0.5890 0.0318  -0.0725 -0.0417 930  GLU B CD  
15513 O OE1 . GLU B 932  ? 0.5156 0.5018 0.5159 0.0308  -0.0740 -0.0422 930  GLU B OE1 
15514 O OE2 . GLU B 932  ? 0.5717 0.5563 0.5733 0.0330  -0.0742 -0.0405 930  GLU B OE2 
15515 N N   . LEU B 933  ? 0.3685 0.3789 0.4030 0.0278  -0.0642 -0.0460 931  LEU B N   
15516 C CA  . LEU B 933  ? 0.4726 0.4873 0.5133 0.0259  -0.0645 -0.0468 931  LEU B CA  
15517 C C   . LEU B 933  ? 0.5838 0.5941 0.6196 0.0243  -0.0667 -0.0476 931  LEU B C   
15518 O O   . LEU B 933  ? 0.5631 0.5676 0.5907 0.0244  -0.0663 -0.0476 931  LEU B O   
15519 C CB  . LEU B 933  ? 0.5050 0.5227 0.5493 0.0247  -0.0601 -0.0464 931  LEU B CB  
15520 C CG  . LEU B 933  ? 0.4617 0.4839 0.5105 0.0261  -0.0573 -0.0458 931  LEU B CG  
15521 C CD1 . LEU B 933  ? 0.5197 0.5444 0.5713 0.0244  -0.0533 -0.0454 931  LEU B CD1 
15522 C CD2 . LEU B 933  ? 0.4481 0.4767 0.5043 0.0275  -0.0594 -0.0463 931  LEU B CD2 
15523 N N   . GLU B 934  ? 0.6281 0.6414 0.6690 0.0226  -0.0691 -0.0484 932  GLU B N   
15524 C CA  . GLU B 934  ? 0.6540 0.6628 0.6908 0.0206  -0.0712 -0.0494 932  GLU B CA  
15525 C C   . GLU B 934  ? 0.6874 0.6942 0.7228 0.0191  -0.0678 -0.0494 932  GLU B C   
15526 O O   . GLU B 934  ? 0.7586 0.7593 0.7863 0.0193  -0.0670 -0.0500 932  GLU B O   
15527 C CB  . GLU B 934  ? 0.6844 0.6971 0.7272 0.0189  -0.0755 -0.0500 932  GLU B CB  
15528 N N   . LYS B 935  ? 0.7150 0.7270 0.7579 0.0177  -0.0656 -0.0488 933  LYS B N   
15529 C CA  . LYS B 935  ? 0.7248 0.7351 0.7670 0.0162  -0.0625 -0.0486 933  LYS B CA  
15530 C C   . LYS B 935  ? 0.6770 0.6921 0.7236 0.0170  -0.0581 -0.0473 933  LYS B C   
15531 O O   . LYS B 935  ? 0.6957 0.7167 0.7480 0.0178  -0.0580 -0.0468 933  LYS B O   
15532 C CB  . LYS B 935  ? 0.7618 0.7728 0.8082 0.0130  -0.0646 -0.0489 933  LYS B CB  
15533 N N   . LEU B 936  ? 0.6996 0.7119 0.7430 0.0169  -0.0547 -0.0469 934  LEU B N   
15534 C CA  . LEU B 936  ? 0.6719 0.6886 0.7191 0.0173  -0.0506 -0.0457 934  LEU B CA  
15535 C C   . LEU B 936  ? 0.7252 0.7486 0.7812 0.0153  -0.0504 -0.0450 934  LEU B C   
15536 O O   . LEU B 936  ? 0.6574 0.6860 0.7176 0.0159  -0.0477 -0.0441 934  LEU B O   
15537 C CB  . LEU B 936  ? 0.6621 0.6748 0.7045 0.0174  -0.0474 -0.0454 934  LEU B CB  
15538 N N   . SER B 937  ? 0.7219 0.7454 0.7805 0.0128  -0.0534 -0.0453 935  SER B N   
15539 C CA  . SER B 937  ? 0.7442 0.7750 0.8115 0.0104  -0.0535 -0.0444 935  SER B CA  
15540 C C   . SER B 937  ? 0.6639 0.7024 0.7374 0.0115  -0.0551 -0.0445 935  SER B C   
15541 O O   . SER B 937  ? 0.7065 0.7530 0.7879 0.0100  -0.0546 -0.0436 935  SER B O   
15542 C CB  . SER B 937  ? 0.7089 0.7369 0.7766 0.0067  -0.0565 -0.0446 935  SER B CB  
15543 N N   . ASP B 938  ? 0.6685 0.7051 0.7388 0.0143  -0.0569 -0.0454 936  ASP B N   
15544 C CA  . ASP B 938  ? 0.6630 0.7063 0.7386 0.0164  -0.0582 -0.0456 936  ASP B CA  
15545 C C   . ASP B 938  ? 0.6453 0.6940 0.7244 0.0184  -0.0544 -0.0450 936  ASP B C   
15546 O O   . ASP B 938  ? 0.6359 0.6919 0.7211 0.0200  -0.0549 -0.0451 936  ASP B O   
15547 C CB  . ASP B 938  ? 0.6368 0.6753 0.7068 0.0191  -0.0611 -0.0465 936  ASP B CB  
15548 C CG  . ASP B 938  ? 0.7539 0.7874 0.8200 0.0174  -0.0652 -0.0473 936  ASP B CG  
15549 O OD1 . ASP B 938  ? 0.7455 0.7789 0.8133 0.0142  -0.0662 -0.0473 936  ASP B OD1 
15550 O OD2 . ASP B 938  ? 0.7657 0.7948 0.8264 0.0193  -0.0677 -0.0479 936  ASP B OD2 
15551 N N   . LEU B 939  ? 0.6298 0.6749 0.7049 0.0186  -0.0507 -0.0445 937  LEU B N   
15552 C CA  . LEU B 939  ? 0.5859 0.6348 0.6630 0.0204  -0.0471 -0.0440 937  LEU B CA  
15553 C C   . LEU B 939  ? 0.5895 0.6440 0.6721 0.0178  -0.0445 -0.0429 937  LEU B C   
15554 O O   . LEU B 939  ? 0.6223 0.6731 0.7022 0.0158  -0.0428 -0.0422 937  LEU B O   
15555 C CB  . LEU B 939  ? 0.5100 0.5521 0.5795 0.0217  -0.0450 -0.0439 937  LEU B CB  
15556 C CG  . LEU B 939  ? 0.5348 0.5789 0.6045 0.0239  -0.0421 -0.0437 937  LEU B CG  
15557 C CD1 . LEU B 939  ? 0.5251 0.5726 0.5978 0.0269  -0.0441 -0.0446 937  LEU B CD1 
15558 C CD2 . LEU B 939  ? 0.4397 0.4766 0.5015 0.0245  -0.0409 -0.0433 937  LEU B CD2 
15559 N N   . GLN B 940  ? 0.6323 0.6961 0.7226 0.0181  -0.0442 -0.0427 938  GLN B N   
15560 C CA  . GLN B 940  ? 0.6105 0.6808 0.7067 0.0152  -0.0420 -0.0413 938  GLN B CA  
15561 C C   . GLN B 940  ? 0.6518 0.7268 0.7497 0.0168  -0.0379 -0.0409 938  GLN B C   
15562 O O   . GLN B 940  ? 0.6963 0.7779 0.7993 0.0146  -0.0358 -0.0396 938  GLN B O   
15563 C CB  . GLN B 940  ? 0.6151 0.6940 0.7192 0.0136  -0.0446 -0.0411 938  GLN B CB  
15564 N N   . ARG B 941  ? 0.5748 0.6466 0.6685 0.0203  -0.0367 -0.0418 939  ARG B N   
15565 C CA  . ARG B 941  ? 0.5840 0.6594 0.6785 0.0217  -0.0330 -0.0415 939  ARG B CA  
15566 C C   . ARG B 941  ? 0.5019 0.5703 0.5894 0.0245  -0.0323 -0.0423 939  ARG B C   
15567 O O   . ARG B 941  ? 0.4966 0.5591 0.5798 0.0258  -0.0348 -0.0431 939  ARG B O   
15568 C CB  . ARG B 941  ? 0.5575 0.6435 0.6592 0.0238  -0.0325 -0.0421 939  ARG B CB  
15569 C CG  . ARG B 941  ? 0.5691 0.6553 0.6710 0.0279  -0.0353 -0.0439 939  ARG B CG  
15570 C CD  . ARG B 941  ? 0.5688 0.6663 0.6780 0.0304  -0.0345 -0.0445 939  ARG B CD  
15571 N NE  . ARG B 941  ? 0.5660 0.6635 0.6751 0.0353  -0.0370 -0.0464 939  ARG B NE  
15572 C CZ  . ARG B 941  ? 0.5392 0.6344 0.6451 0.0394  -0.0361 -0.0478 939  ARG B CZ  
15573 N NH1 . ARG B 941  ? 0.5500 0.6428 0.6523 0.0393  -0.0328 -0.0476 939  ARG B NH1 
15574 N NH2 . ARG B 941  ? 0.4633 0.5584 0.5693 0.0439  -0.0389 -0.0495 939  ARG B NH2 
15575 N N   . GLU B 942  ? 0.5024 0.5716 0.5888 0.0250  -0.0289 -0.0419 940  GLU B N   
15576 C CA  . GLU B 942  ? 0.4940 0.5574 0.5743 0.0272  -0.0282 -0.0425 940  GLU B CA  
15577 C C   . GLU B 942  ? 0.4391 0.5042 0.5203 0.0311  -0.0297 -0.0441 940  GLU B C   
15578 O O   . GLU B 942  ? 0.4820 0.5546 0.5684 0.0328  -0.0288 -0.0448 940  GLU B O   
15579 C CB  . GLU B 942  ? 0.5423 0.6065 0.6213 0.0265  -0.0245 -0.0416 940  GLU B CB  
15580 C CG  . GLU B 942  ? 0.5287 0.5863 0.6010 0.0276  -0.0238 -0.0417 940  GLU B CG  
15581 C CD  . GLU B 942  ? 0.6153 0.6749 0.6870 0.0273  -0.0204 -0.0411 940  GLU B CD  
15582 O OE1 . GLU B 942  ? 0.6483 0.7148 0.7248 0.0272  -0.0186 -0.0409 940  GLU B OE1 
15583 O OE2 . GLU B 942  ? 0.5705 0.6252 0.6371 0.0269  -0.0196 -0.0405 940  GLU B OE2 
15584 N N   . VAL B 943  ? 0.4071 0.4652 0.4830 0.0327  -0.0321 -0.0448 941  VAL B N   
15585 C CA  . VAL B 943  ? 0.3971 0.4544 0.4723 0.0366  -0.0341 -0.0463 941  VAL B CA  
15586 C C   . VAL B 943  ? 0.3549 0.4057 0.4235 0.0375  -0.0331 -0.0463 941  VAL B C   
15587 O O   . VAL B 943  ? 0.3221 0.3655 0.3847 0.0362  -0.0340 -0.0455 941  VAL B O   
15588 C CB  . VAL B 943  ? 0.4119 0.4662 0.4863 0.0376  -0.0383 -0.0467 941  VAL B CB  
15589 C CG1 . VAL B 943  ? 0.3531 0.4068 0.4272 0.0420  -0.0405 -0.0483 941  VAL B CG1 
15590 C CG2 . VAL B 943  ? 0.4185 0.4791 0.4992 0.0358  -0.0393 -0.0465 941  VAL B CG2 
15591 N N   . PHE B 944  ? 0.3070 0.3608 0.3767 0.0395  -0.0312 -0.0471 942  PHE B N   
15592 C CA  . PHE B 944  ? 0.3107 0.3593 0.3748 0.0396  -0.0298 -0.0470 942  PHE B CA  
15593 C C   . PHE B 944  ? 0.3192 0.3613 0.3786 0.0427  -0.0328 -0.0482 942  PHE B C   
15594 O O   . PHE B 944  ? 0.3310 0.3731 0.3896 0.0457  -0.0326 -0.0497 942  PHE B O   
15595 C CB  . PHE B 944  ? 0.3020 0.3568 0.3690 0.0400  -0.0264 -0.0473 942  PHE B CB  
15596 C CG  . PHE B 944  ? 0.3260 0.3772 0.3884 0.0380  -0.0242 -0.0463 942  PHE B CG  
15597 C CD1 . PHE B 944  ? 0.3525 0.4033 0.4144 0.0344  -0.0225 -0.0444 942  PHE B CD1 
15598 C CD2 . PHE B 944  ? 0.3193 0.3672 0.3777 0.0399  -0.0240 -0.0473 942  PHE B CD2 
15599 C CE1 . PHE B 944  ? 0.3211 0.3693 0.3792 0.0328  -0.0205 -0.0433 942  PHE B CE1 
15600 C CE2 . PHE B 944  ? 0.2960 0.3410 0.3503 0.0378  -0.0221 -0.0462 942  PHE B CE2 
15601 C CZ  . PHE B 944  ? 0.3122 0.3579 0.3667 0.0343  -0.0204 -0.0441 942  PHE B CZ  
15602 N N   . GLY B 945  ? 0.2735 0.3093 0.3291 0.0420  -0.0356 -0.0476 943  GLY B N   
15603 C CA  . GLY B 945  ? 0.2952 0.3241 0.3461 0.0446  -0.0391 -0.0484 943  GLY B CA  
15604 C C   . GLY B 945  ? 0.2611 0.2824 0.3061 0.0423  -0.0412 -0.0468 943  GLY B C   
15605 O O   . GLY B 945  ? 0.2575 0.2792 0.3019 0.0390  -0.0399 -0.0453 943  GLY B O   
15606 N N   . PRO B 946  ? 0.2299 0.2442 0.2702 0.0441  -0.0447 -0.0470 944  PRO B N   
15607 C CA  . PRO B 946  ? 0.2394 0.2463 0.2731 0.0416  -0.0466 -0.0452 944  PRO B CA  
15608 C C   . PRO B 946  ? 0.2673 0.2753 0.3025 0.0413  -0.0487 -0.0449 944  PRO B C   
15609 O O   . PRO B 946  ? 0.2989 0.3019 0.3308 0.0426  -0.0524 -0.0448 944  PRO B O   
15610 C CB  . PRO B 946  ? 0.2168 0.2156 0.2449 0.0436  -0.0498 -0.0455 944  PRO B CB  
15611 C CG  . PRO B 946  ? 0.3034 0.3057 0.3362 0.0485  -0.0510 -0.0480 944  PRO B CG  
15612 C CD  . PRO B 946  ? 0.2451 0.2573 0.2849 0.0484  -0.0469 -0.0489 944  PRO B CD  
15613 N N   . VAL B 947  ? 0.2427 0.2569 0.2825 0.0395  -0.0466 -0.0447 945  VAL B N   
15614 C CA  . VAL B 947  ? 0.2699 0.2860 0.3119 0.0392  -0.0486 -0.0448 945  VAL B CA  
15615 C C   . VAL B 947  ? 0.2998 0.3152 0.3395 0.0357  -0.0469 -0.0435 945  VAL B C   
15616 O O   . VAL B 947  ? 0.3030 0.3231 0.3462 0.0341  -0.0439 -0.0434 945  VAL B O   
15617 C CB  . VAL B 947  ? 0.2609 0.2855 0.3115 0.0410  -0.0485 -0.0463 945  VAL B CB  
15618 C CG1 . VAL B 947  ? 0.2862 0.3120 0.3386 0.0406  -0.0515 -0.0464 945  VAL B CG1 
15619 C CG2 . VAL B 947  ? 0.2753 0.3014 0.3281 0.0452  -0.0497 -0.0478 945  VAL B CG2 
15620 N N   . LEU B 948  ? 0.2843 0.2940 0.3179 0.0346  -0.0489 -0.0424 946  LEU B N   
15621 C CA  . LEU B 948  ? 0.2729 0.2817 0.3035 0.0318  -0.0475 -0.0414 946  LEU B CA  
15622 C C   . LEU B 948  ? 0.3081 0.3183 0.3406 0.0318  -0.0498 -0.0421 946  LEU B C   
15623 O O   . LEU B 948  ? 0.3161 0.3239 0.3472 0.0331  -0.0535 -0.0424 946  LEU B O   
15624 C CB  . LEU B 948  ? 0.2797 0.2821 0.3020 0.0305  -0.0481 -0.0397 946  LEU B CB  
15625 C CG  . LEU B 948  ? 0.2933 0.2951 0.3118 0.0282  -0.0465 -0.0388 946  LEU B CG  
15626 C CD1 . LEU B 948  ? 0.2453 0.2509 0.2661 0.0269  -0.0424 -0.0386 946  LEU B CD1 
15627 C CD2 . LEU B 948  ? 0.2942 0.2906 0.3047 0.0271  -0.0475 -0.0370 946  LEU B CD2 
15628 N N   . HIS B 949  ? 0.2970 0.3104 0.3322 0.0301  -0.0480 -0.0424 947  HIS B N   
15629 C CA  . HIS B 949  ? 0.3414 0.3551 0.3773 0.0294  -0.0501 -0.0430 947  HIS B CA  
15630 C C   . HIS B 949  ? 0.3343 0.3434 0.3632 0.0279  -0.0497 -0.0424 947  HIS B C   
15631 O O   . HIS B 949  ? 0.3138 0.3222 0.3400 0.0269  -0.0466 -0.0416 947  HIS B O   
15632 C CB  . HIS B 949  ? 0.2999 0.3196 0.3430 0.0284  -0.0488 -0.0437 947  HIS B CB  
15633 C CG  . HIS B 949  ? 0.3675 0.3931 0.4177 0.0299  -0.0485 -0.0443 947  HIS B CG  
15634 N ND1 . HIS B 949  ? 0.3115 0.3396 0.3636 0.0304  -0.0453 -0.0440 947  HIS B ND1 
15635 C CD2 . HIS B 949  ? 0.3778 0.4079 0.4336 0.0314  -0.0510 -0.0452 947  HIS B CD2 
15636 C CE1 . HIS B 949  ? 0.3408 0.3746 0.3990 0.0321  -0.0456 -0.0448 947  HIS B CE1 
15637 N NE2 . HIS B 949  ? 0.3885 0.4238 0.4493 0.0329  -0.0490 -0.0455 947  HIS B NE2 
15638 N N   . VAL B 950  ? 0.3343 0.3404 0.3597 0.0280  -0.0529 -0.0427 948  VAL B N   
15639 C CA  . VAL B 950  ? 0.3253 0.3271 0.3433 0.0270  -0.0527 -0.0423 948  VAL B CA  
15640 C C   . VAL B 950  ? 0.3671 0.3689 0.3857 0.0263  -0.0545 -0.0436 948  VAL B C   
15641 O O   . VAL B 950  ? 0.3860 0.3886 0.4074 0.0267  -0.0580 -0.0444 948  VAL B O   
15642 C CB  . VAL B 950  ? 0.3687 0.3659 0.3798 0.0275  -0.0550 -0.0412 948  VAL B CB  
15643 C CG1 . VAL B 950  ? 0.3424 0.3364 0.3457 0.0265  -0.0541 -0.0406 948  VAL B CG1 
15644 C CG2 . VAL B 950  ? 0.3183 0.3146 0.3288 0.0279  -0.0539 -0.0398 948  VAL B CG2 
15645 N N   . ILE B 951  ? 0.3235 0.3241 0.3392 0.0253  -0.0524 -0.0439 949  ILE B N   
15646 C CA  . ILE B 951  ? 0.3324 0.3310 0.3465 0.0247  -0.0544 -0.0453 949  ILE B CA  
15647 C C   . ILE B 951  ? 0.3427 0.3370 0.3478 0.0250  -0.0535 -0.0452 949  ILE B C   
15648 O O   . ILE B 951  ? 0.3148 0.3091 0.3167 0.0252  -0.0504 -0.0441 949  ILE B O   
15649 C CB  . ILE B 951  ? 0.3894 0.3903 0.4089 0.0234  -0.0530 -0.0460 949  ILE B CB  
15650 C CG1 . ILE B 951  ? 0.4062 0.4079 0.4252 0.0234  -0.0486 -0.0452 949  ILE B CG1 
15651 C CG2 . ILE B 951  ? 0.5167 0.5228 0.5451 0.0229  -0.0543 -0.0461 949  ILE B CG2 
15652 C CD1 . ILE B 951  ? 0.4837 0.4875 0.5081 0.0221  -0.0472 -0.0456 949  ILE B CD1 
15653 N N   . ARG B 952  ? 0.3124 0.3034 0.3135 0.0249  -0.0564 -0.0465 950  ARG B N   
15654 C CA  . ARG B 952  ? 0.3086 0.2957 0.3007 0.0256  -0.0559 -0.0469 950  ARG B CA  
15655 C C   . ARG B 952  ? 0.3197 0.3047 0.3107 0.0255  -0.0556 -0.0487 950  ARG B C   
15656 O O   . ARG B 952  ? 0.3460 0.3309 0.3416 0.0245  -0.0577 -0.0499 950  ARG B O   
15657 C CB  . ARG B 952  ? 0.4006 0.3845 0.3873 0.0260  -0.0599 -0.0470 950  ARG B CB  
15658 C CG  . ARG B 952  ? 0.4227 0.4077 0.4111 0.0261  -0.0614 -0.0453 950  ARG B CG  
15659 C CD  . ARG B 952  ? 0.4949 0.4777 0.4818 0.0264  -0.0665 -0.0459 950  ARG B CD  
15660 N NE  . ARG B 952  ? 0.5698 0.5486 0.5470 0.0268  -0.0676 -0.0453 950  ARG B NE  
15661 C CZ  . ARG B 952  ? 0.5252 0.5024 0.4986 0.0270  -0.0688 -0.0434 950  ARG B CZ  
15662 N NH1 . ARG B 952  ? 0.5013 0.4799 0.4796 0.0273  -0.0694 -0.0422 950  ARG B NH1 
15663 N NH2 . ARG B 952  ? 0.5254 0.4993 0.4895 0.0271  -0.0696 -0.0428 950  ARG B NH2 
15664 N N   . TYR B 953  ? 0.3239 0.3073 0.3086 0.0266  -0.0529 -0.0489 951  TYR B N   
15665 C CA  . TYR B 953  ? 0.3139 0.2944 0.2968 0.0271  -0.0526 -0.0508 951  TYR B CA  
15666 C C   . TYR B 953  ? 0.3505 0.3274 0.3234 0.0290  -0.0524 -0.0519 951  TYR B C   
15667 O O   . TYR B 953  ? 0.3081 0.2865 0.2763 0.0297  -0.0508 -0.0506 951  TYR B O   
15668 C CB  . TYR B 953  ? 0.3189 0.3019 0.3059 0.0272  -0.0487 -0.0502 951  TYR B CB  
15669 C CG  . TYR B 953  ? 0.3311 0.3163 0.3143 0.0286  -0.0446 -0.0489 951  TYR B CG  
15670 C CD1 . TYR B 953  ? 0.3339 0.3232 0.3193 0.0280  -0.0428 -0.0466 951  TYR B CD1 
15671 C CD2 . TYR B 953  ? 0.2812 0.2647 0.2588 0.0306  -0.0427 -0.0500 951  TYR B CD2 
15672 C CE1 . TYR B 953  ? 0.2873 0.2793 0.2696 0.0287  -0.0393 -0.0452 951  TYR B CE1 
15673 C CE2 . TYR B 953  ? 0.3271 0.3140 0.3017 0.0319  -0.0389 -0.0486 951  TYR B CE2 
15674 C CZ  . TYR B 953  ? 0.3081 0.2994 0.2854 0.0306  -0.0372 -0.0461 951  TYR B CZ  
15675 O OH  . TYR B 953  ? 0.3162 0.3114 0.2908 0.0314  -0.0336 -0.0445 951  TYR B OH  
15676 N N   . ARG B 954  ? 0.3677 0.3400 0.3372 0.0296  -0.0543 -0.0544 952  ARG B N   
15677 C CA  . ARG B 954  ? 0.3859 0.3547 0.3457 0.0320  -0.0537 -0.0560 952  ARG B CA  
15678 C C   . ARG B 954  ? 0.3829 0.3529 0.3417 0.0339  -0.0494 -0.0561 952  ARG B C   
15679 O O   . ARG B 954  ? 0.3959 0.3660 0.3601 0.0334  -0.0484 -0.0562 952  ARG B O   
15680 C CB  . ARG B 954  ? 0.4389 0.4011 0.3947 0.0320  -0.0581 -0.0589 952  ARG B CB  
15681 N N   . ARG B 955  ? 0.4607 0.4321 0.4124 0.0362  -0.0467 -0.0559 953  ARG B N   
15682 C CA  . ARG B 955  ? 0.4737 0.4478 0.4246 0.0385  -0.0424 -0.0557 953  ARG B CA  
15683 C C   . ARG B 955  ? 0.4776 0.4468 0.4285 0.0400  -0.0430 -0.0582 953  ARG B C   
15684 O O   . ARG B 955  ? 0.4990 0.4702 0.4536 0.0407  -0.0403 -0.0576 953  ARG B O   
15685 C CB  . ARG B 955  ? 0.5376 0.5139 0.4800 0.0409  -0.0401 -0.0556 953  ARG B CB  
15686 C CG  . ARG B 955  ? 0.5947 0.5728 0.5340 0.0444  -0.0364 -0.0565 953  ARG B CG  
15687 C CD  . ARG B 955  ? 0.6463 0.6317 0.5912 0.0438  -0.0322 -0.0537 953  ARG B CD  
15688 N NE  . ARG B 955  ? 0.6744 0.6626 0.6165 0.0474  -0.0287 -0.0543 953  ARG B NE  
15689 C CZ  . ARG B 955  ? 0.7181 0.7060 0.6643 0.0486  -0.0273 -0.0549 953  ARG B CZ  
15690 N NH1 . ARG B 955  ? 0.6633 0.6482 0.6163 0.0463  -0.0291 -0.0547 953  ARG B NH1 
15691 N NH2 . ARG B 955  ? 0.7561 0.7472 0.6995 0.0524  -0.0241 -0.0554 953  ARG B NH2 
15692 N N   . ASP B 956  ? 0.4076 0.3699 0.3538 0.0405  -0.0468 -0.0610 954  ASP B N   
15693 C CA  . ASP B 956  ? 0.4689 0.4250 0.4144 0.0416  -0.0480 -0.0634 954  ASP B CA  
15694 C C   . ASP B 956  ? 0.4286 0.3844 0.3834 0.0384  -0.0492 -0.0624 954  ASP B C   
15695 O O   . ASP B 956  ? 0.5023 0.4534 0.4574 0.0389  -0.0499 -0.0637 954  ASP B O   
15696 C CB  . ASP B 956  ? 0.5025 0.4506 0.4405 0.0424  -0.0524 -0.0667 954  ASP B CB  
15697 C CG  . ASP B 956  ? 0.5502 0.4979 0.4778 0.0463  -0.0511 -0.0683 954  ASP B CG  
15698 O OD1 . ASP B 956  ? 0.5908 0.5433 0.5168 0.0490  -0.0466 -0.0675 954  ASP B OD1 
15699 O OD2 . ASP B 956  ? 0.6577 0.6008 0.5788 0.0465  -0.0545 -0.0702 954  ASP B OD2 
15700 N N   . ASP B 957  ? 0.3714 0.3319 0.3334 0.0352  -0.0497 -0.0601 955  ASP B N   
15701 C CA  . ASP B 957  ? 0.4199 0.3817 0.3910 0.0321  -0.0505 -0.0589 955  ASP B CA  
15702 C C   . ASP B 957  ? 0.3637 0.3317 0.3406 0.0320  -0.0461 -0.0564 955  ASP B C   
15703 O O   . ASP B 957  ? 0.3686 0.3393 0.3533 0.0295  -0.0462 -0.0549 955  ASP B O   
15704 C CB  . ASP B 957  ? 0.3980 0.3614 0.3739 0.0290  -0.0539 -0.0582 955  ASP B CB  
15705 C CG  . ASP B 957  ? 0.5114 0.4684 0.4840 0.0280  -0.0590 -0.0605 955  ASP B CG  
15706 O OD1 . ASP B 957  ? 0.5703 0.5208 0.5388 0.0287  -0.0603 -0.0626 955  ASP B OD1 
15707 O OD2 . ASP B 957  ? 0.5062 0.4645 0.4803 0.0264  -0.0620 -0.0602 955  ASP B OD2 
15708 N N   . LEU B 958  ? 0.3446 0.3156 0.3179 0.0347  -0.0424 -0.0558 956  LEU B N   
15709 C CA  . LEU B 958  ? 0.3084 0.2857 0.2869 0.0344  -0.0385 -0.0533 956  LEU B CA  
15710 C C   . LEU B 958  ? 0.3333 0.3096 0.3170 0.0337  -0.0379 -0.0530 956  LEU B C   
15711 O O   . LEU B 958  ? 0.3229 0.3033 0.3136 0.0316  -0.0367 -0.0511 956  LEU B O   
15712 C CB  . LEU B 958  ? 0.3904 0.3708 0.3637 0.0374  -0.0349 -0.0529 956  LEU B CB  
15713 C CG  . LEU B 958  ? 0.3161 0.3034 0.2943 0.0369  -0.0311 -0.0503 956  LEU B CG  
15714 C CD1 . LEU B 958  ? 0.2950 0.2857 0.2785 0.0339  -0.0317 -0.0483 956  LEU B CD1 
15715 C CD2 . LEU B 958  ? 0.3886 0.3799 0.3616 0.0395  -0.0278 -0.0497 956  LEU B CD2 
15716 N N   . ASP B 959  ? 0.3692 0.3395 0.3489 0.0355  -0.0387 -0.0550 957  ASP B N   
15717 C CA  . ASP B 959  ? 0.3491 0.3180 0.3330 0.0348  -0.0381 -0.0544 957  ASP B CA  
15718 C C   . ASP B 959  ? 0.3226 0.2911 0.3134 0.0306  -0.0408 -0.0536 957  ASP B C   
15719 O O   . ASP B 959  ? 0.3354 0.3070 0.3324 0.0288  -0.0393 -0.0517 957  ASP B O   
15720 C CB  . ASP B 959  ? 0.3394 0.3006 0.3170 0.0377  -0.0391 -0.0567 957  ASP B CB  
15721 C CG  . ASP B 959  ? 0.4088 0.3692 0.3896 0.0380  -0.0376 -0.0557 957  ASP B CG  
15722 O OD1 . ASP B 959  ? 0.3611 0.3281 0.3453 0.0385  -0.0340 -0.0536 957  ASP B OD1 
15723 O OD2 . ASP B 959  ? 0.4278 0.3806 0.4072 0.0375  -0.0403 -0.0569 957  ASP B OD2 
15724 N N   . ARG B 960  ? 0.3190 0.2842 0.3087 0.0289  -0.0447 -0.0549 958  ARG B N   
15725 C CA  . ARG B 960  ? 0.3256 0.2921 0.3224 0.0248  -0.0472 -0.0540 958  ARG B CA  
15726 C C   . ARG B 960  ? 0.3312 0.3062 0.3347 0.0234  -0.0453 -0.0517 958  ARG B C   
15727 O O   . ARG B 960  ? 0.3749 0.3535 0.3857 0.0208  -0.0453 -0.0502 958  ARG B O   
15728 C CB  . ARG B 960  ? 0.2922 0.2538 0.2860 0.0236  -0.0520 -0.0559 958  ARG B CB  
15729 N N   . LEU B 961  ? 0.3067 0.2848 0.3076 0.0252  -0.0439 -0.0515 959  LEU B N   
15730 C CA  . LEU B 961  ? 0.2946 0.2796 0.3010 0.0241  -0.0424 -0.0495 959  LEU B CA  
15731 C C   . LEU B 961  ? 0.3348 0.3239 0.3458 0.0239  -0.0387 -0.0477 959  LEU B C   
15732 O O   . LEU B 961  ? 0.3329 0.3266 0.3507 0.0221  -0.0383 -0.0464 959  LEU B O   
15733 C CB  . LEU B 961  ? 0.3135 0.3000 0.3153 0.0258  -0.0416 -0.0493 959  LEU B CB  
15734 C CG  . LEU B 961  ? 0.3162 0.3085 0.3221 0.0252  -0.0400 -0.0473 959  LEU B CG  
15735 C CD1 . LEU B 961  ? 0.3740 0.3682 0.3855 0.0234  -0.0428 -0.0472 959  LEU B CD1 
15736 C CD2 . LEU B 961  ? 0.3103 0.3031 0.3103 0.0267  -0.0389 -0.0467 959  LEU B CD2 
15737 N N   . VAL B 962  ? 0.3000 0.2878 0.3075 0.0260  -0.0362 -0.0477 960  VAL B N   
15738 C CA  . VAL B 962  ? 0.3043 0.2955 0.3156 0.0258  -0.0331 -0.0460 960  VAL B CA  
15739 C C   . VAL B 962  ? 0.3227 0.3133 0.3397 0.0232  -0.0342 -0.0455 960  VAL B C   
15740 O O   . VAL B 962  ? 0.3128 0.3083 0.3355 0.0217  -0.0325 -0.0438 960  VAL B O   
15741 C CB  . VAL B 962  ? 0.3310 0.3204 0.3373 0.0288  -0.0308 -0.0464 960  VAL B CB  
15742 C CG1 . VAL B 962  ? 0.3237 0.3157 0.3339 0.0285  -0.0282 -0.0448 960  VAL B CG1 
15743 C CG2 . VAL B 962  ? 0.3164 0.3087 0.3182 0.0308  -0.0289 -0.0462 960  VAL B CG2 
15744 N N   . ASP B 963  ? 0.3605 0.3451 0.3757 0.0224  -0.0372 -0.0469 961  ASP B N   
15745 C CA  . ASP B 963  ? 0.4003 0.3843 0.4207 0.0191  -0.0388 -0.0461 961  ASP B CA  
15746 C C   . ASP B 963  ? 0.3385 0.3291 0.3661 0.0166  -0.0394 -0.0449 961  ASP B C   
15747 O O   . ASP B 963  ? 0.3563 0.3512 0.3899 0.0145  -0.0382 -0.0433 961  ASP B O   
15748 C CB  . ASP B 963  ? 0.3950 0.3712 0.4119 0.0181  -0.0429 -0.0478 961  ASP B CB  
15749 C CG  . ASP B 963  ? 0.4601 0.4291 0.4712 0.0203  -0.0427 -0.0488 961  ASP B CG  
15750 O OD1 . ASP B 963  ? 0.4411 0.4119 0.4529 0.0216  -0.0395 -0.0475 961  ASP B OD1 
15751 O OD2 . ASP B 963  ? 0.4665 0.4277 0.4722 0.0207  -0.0459 -0.0509 961  ASP B OD2 
15752 N N   . ASP B 964  ? 0.3184 0.3101 0.3452 0.0169  -0.0412 -0.0459 962  ASP B N   
15753 C CA  . ASP B 964  ? 0.3704 0.3683 0.4038 0.0151  -0.0421 -0.0451 962  ASP B CA  
15754 C C   . ASP B 964  ? 0.3337 0.3381 0.3709 0.0158  -0.0385 -0.0435 962  ASP B C   
15755 O O   . ASP B 964  ? 0.3400 0.3500 0.3838 0.0142  -0.0382 -0.0425 962  ASP B O   
15756 C CB  . ASP B 964  ? 0.3782 0.3753 0.4090 0.0160  -0.0449 -0.0464 962  ASP B CB  
15757 C CG  . ASP B 964  ? 0.4291 0.4206 0.4572 0.0147  -0.0490 -0.0480 962  ASP B CG  
15758 O OD1 . ASP B 964  ? 0.4578 0.4460 0.4865 0.0129  -0.0500 -0.0480 962  ASP B OD1 
15759 O OD2 . ASP B 964  ? 0.4948 0.4849 0.5199 0.0155  -0.0516 -0.0492 962  ASP B OD2 
15760 N N   . VAL B 965  ? 0.3243 0.3282 0.3572 0.0182  -0.0360 -0.0434 963  VAL B N   
15761 C CA  . VAL B 965  ? 0.2879 0.2972 0.3237 0.0187  -0.0328 -0.0419 963  VAL B CA  
15762 C C   . VAL B 965  ? 0.3221 0.3334 0.3618 0.0174  -0.0307 -0.0406 963  VAL B C   
15763 O O   . VAL B 965  ? 0.3469 0.3636 0.3919 0.0165  -0.0294 -0.0395 963  VAL B O   
15764 C CB  . VAL B 965  ? 0.3441 0.3524 0.3743 0.0210  -0.0308 -0.0418 963  VAL B CB  
15765 C CG1 . VAL B 965  ? 0.3123 0.3253 0.3449 0.0213  -0.0277 -0.0403 963  VAL B CG1 
15766 C CG2 . VAL B 965  ? 0.3018 0.3087 0.3284 0.0219  -0.0328 -0.0426 963  VAL B CG2 
15767 N N   . ASN B 966  ? 0.3171 0.3239 0.3539 0.0176  -0.0305 -0.0407 964  ASN B N   
15768 C CA  . ASN B 966  ? 0.3267 0.3345 0.3664 0.0163  -0.0289 -0.0392 964  ASN B CA  
15769 C C   . ASN B 966  ? 0.3425 0.3527 0.3882 0.0130  -0.0304 -0.0384 964  ASN B C   
15770 O O   . ASN B 966  ? 0.3649 0.3785 0.4145 0.0115  -0.0287 -0.0368 964  ASN B O   
15771 C CB  . ASN B 966  ? 0.3361 0.3373 0.3708 0.0174  -0.0290 -0.0396 964  ASN B CB  
15772 C CG  . ASN B 966  ? 0.3587 0.3595 0.3885 0.0207  -0.0266 -0.0398 964  ASN B CG  
15773 O OD1 . ASN B 966  ? 0.3259 0.3317 0.3567 0.0214  -0.0243 -0.0390 964  ASN B OD1 
15774 N ND2 . ASN B 966  ? 0.2730 0.2679 0.2974 0.0227  -0.0272 -0.0409 964  ASN B ND2 
15775 N N   . ALA B 967  ? 0.3329 0.3419 0.3795 0.0116  -0.0337 -0.0395 965  ALA B N   
15776 C CA  . ALA B 967  ? 0.3387 0.3500 0.3910 0.0081  -0.0356 -0.0387 965  ALA B CA  
15777 C C   . ALA B 967  ? 0.3975 0.4181 0.4570 0.0072  -0.0341 -0.0375 965  ALA B C   
15778 O O   . ALA B 967  ? 0.4410 0.4654 0.5059 0.0041  -0.0349 -0.0363 965  ALA B O   
15779 C CB  . ALA B 967  ? 0.2728 0.2803 0.3238 0.0069  -0.0399 -0.0402 965  ALA B CB  
15780 N N   . THR B 968  ? 0.3238 0.3481 0.3833 0.0097  -0.0323 -0.0379 966  THR B N   
15781 C CA  . THR B 968  ? 0.3784 0.4111 0.4441 0.0094  -0.0307 -0.0370 966  THR B CA  
15782 C C   . THR B 968  ? 0.4132 0.4492 0.4814 0.0082  -0.0277 -0.0352 966  THR B C   
15783 O O   . THR B 968  ? 0.4350 0.4783 0.5087 0.0074  -0.0265 -0.0343 966  THR B O   
15784 C CB  . THR B 968  ? 0.3876 0.4219 0.4516 0.0125  -0.0298 -0.0379 966  THR B CB  
15785 O OG1 . THR B 968  ? 0.4060 0.4392 0.4668 0.0139  -0.0267 -0.0373 966  THR B OG1 
15786 C CG2 . THR B 968  ? 0.3811 0.4106 0.4406 0.0139  -0.0324 -0.0395 966  THR B CG2 
15787 N N   . GLY B 969  ? 0.4197 0.4508 0.4838 0.0084  -0.0264 -0.0345 967  GLY B N   
15788 C CA  . GLY B 969  ? 0.3782 0.4119 0.4438 0.0075  -0.0235 -0.0326 967  GLY B CA  
15789 C C   . GLY B 969  ? 0.4081 0.4449 0.4727 0.0099  -0.0205 -0.0325 967  GLY B C   
15790 O O   . GLY B 969  ? 0.3783 0.4164 0.4430 0.0096  -0.0181 -0.0310 967  GLY B O   
15791 N N   . TYR B 970  ? 0.3594 0.3972 0.4229 0.0121  -0.0207 -0.0339 968  TYR B N   
15792 C CA  . TYR B 970  ? 0.3716 0.4107 0.4329 0.0142  -0.0184 -0.0339 968  TYR B CA  
15793 C C   . TYR B 970  ? 0.3880 0.4217 0.4435 0.0156  -0.0180 -0.0339 968  TYR B C   
15794 O O   . TYR B 970  ? 0.3931 0.4218 0.4456 0.0157  -0.0196 -0.0346 968  TYR B O   
15795 C CB  . TYR B 970  ? 0.3917 0.4330 0.4536 0.0159  -0.0192 -0.0351 968  TYR B CB  
15796 C CG  . TYR B 970  ? 0.3935 0.4415 0.4614 0.0155  -0.0192 -0.0353 968  TYR B CG  
15797 C CD1 . TYR B 970  ? 0.4137 0.4665 0.4835 0.0160  -0.0167 -0.0347 968  TYR B CD1 
15798 C CD2 . TYR B 970  ? 0.4250 0.4748 0.4963 0.0150  -0.0217 -0.0361 968  TYR B CD2 
15799 C CE1 . TYR B 970  ? 0.4577 0.5173 0.5328 0.0162  -0.0164 -0.0350 968  TYR B CE1 
15800 C CE2 . TYR B 970  ? 0.4849 0.5419 0.5619 0.0151  -0.0216 -0.0362 968  TYR B CE2 
15801 C CZ  . TYR B 970  ? 0.4879 0.5499 0.5667 0.0159  -0.0188 -0.0357 968  TYR B CZ  
15802 O OH  . TYR B 970  ? 0.6656 0.7354 0.7501 0.0164  -0.0185 -0.0361 968  TYR B OH  
15803 N N   . GLY B 971  ? 0.3533 0.3883 0.4069 0.0168  -0.0157 -0.0333 969  GLY B N   
15804 C CA  . GLY B 971  ? 0.3135 0.3450 0.3620 0.0182  -0.0151 -0.0333 969  GLY B CA  
15805 C C   . GLY B 971  ? 0.2749 0.3090 0.3221 0.0191  -0.0131 -0.0327 969  GLY B C   
15806 O O   . GLY B 971  ? 0.2680 0.3027 0.3141 0.0194  -0.0113 -0.0316 969  GLY B O   
15807 N N   . LEU B 972  ? 0.3190 0.3543 0.3663 0.0196  -0.0138 -0.0334 970  LEU B N   
15808 C CA  . LEU B 972  ? 0.2625 0.2997 0.3084 0.0200  -0.0124 -0.0329 970  LEU B CA  
15809 C C   . LEU B 972  ? 0.2924 0.3272 0.3335 0.0207  -0.0127 -0.0328 970  LEU B C   
15810 O O   . LEU B 972  ? 0.2770 0.3119 0.3159 0.0210  -0.0114 -0.0319 970  LEU B O   
15811 C CB  . LEU B 972  ? 0.3028 0.3423 0.3511 0.0203  -0.0130 -0.0338 970  LEU B CB  
15812 C CG  . LEU B 972  ? 0.3132 0.3541 0.3602 0.0205  -0.0118 -0.0334 970  LEU B CG  
15813 C CD1 . LEU B 972  ? 0.2997 0.3428 0.3470 0.0199  -0.0094 -0.0320 970  LEU B CD1 
15814 C CD2 . LEU B 972  ? 0.3298 0.3728 0.3792 0.0213  -0.0123 -0.0345 970  LEU B CD2 
15815 N N   . THR B 973  ? 0.2516 0.2847 0.2910 0.0210  -0.0145 -0.0336 971  THR B N   
15816 C CA  . THR B 973  ? 0.2157 0.2468 0.2503 0.0213  -0.0148 -0.0332 971  THR B CA  
15817 C C   . THR B 973  ? 0.2518 0.2798 0.2843 0.0218  -0.0166 -0.0341 971  THR B C   
15818 O O   . THR B 973  ? 0.2575 0.2844 0.2921 0.0218  -0.0184 -0.0352 971  THR B O   
15819 C CB  . THR B 973  ? 0.2411 0.2719 0.2741 0.0209  -0.0156 -0.0329 971  THR B CB  
15820 O OG1 . THR B 973  ? 0.2484 0.2776 0.2827 0.0214  -0.0179 -0.0342 971  THR B OG1 
15821 C CG2 . THR B 973  ? 0.2631 0.2964 0.2975 0.0204  -0.0140 -0.0323 971  THR B CG2 
15822 N N   . PHE B 974  ? 0.2160 0.2431 0.2441 0.0222  -0.0162 -0.0336 972  PHE B N   
15823 C CA  . PHE B 974  ? 0.2655 0.2896 0.2903 0.0229  -0.0177 -0.0344 972  PHE B CA  
15824 C C   . PHE B 974  ? 0.2146 0.2389 0.2344 0.0230  -0.0172 -0.0335 972  PHE B C   
15825 O O   . PHE B 974  ? 0.2019 0.2291 0.2208 0.0230  -0.0151 -0.0322 972  PHE B O   
15826 C CB  . PHE B 974  ? 0.1989 0.2217 0.2237 0.0239  -0.0172 -0.0351 972  PHE B CB  
15827 C CG  . PHE B 974  ? 0.2309 0.2504 0.2512 0.0250  -0.0186 -0.0362 972  PHE B CG  
15828 C CD1 . PHE B 974  ? 0.2968 0.3132 0.3172 0.0247  -0.0213 -0.0376 972  PHE B CD1 
15829 C CD2 . PHE B 974  ? 0.2459 0.2659 0.2618 0.0264  -0.0171 -0.0359 972  PHE B CD2 
15830 C CE1 . PHE B 974  ? 0.2719 0.2849 0.2875 0.0258  -0.0228 -0.0387 972  PHE B CE1 
15831 C CE2 . PHE B 974  ? 0.2746 0.2918 0.2858 0.0277  -0.0183 -0.0371 972  PHE B CE2 
15832 C CZ  . PHE B 974  ? 0.2396 0.2529 0.2503 0.0273  -0.0212 -0.0386 972  PHE B CZ  
15833 N N   . GLY B 975  ? 0.1793 0.2010 0.1960 0.0230  -0.0192 -0.0339 973  GLY B N   
15834 C CA  . GLY B 975  ? 0.2312 0.2533 0.2429 0.0227  -0.0190 -0.0327 973  GLY B CA  
15835 C C   . GLY B 975  ? 0.2848 0.3048 0.2921 0.0240  -0.0196 -0.0337 973  GLY B C   
15836 O O   . GLY B 975  ? 0.2292 0.2461 0.2370 0.0247  -0.0216 -0.0354 973  GLY B O   
15837 N N   . LEU B 976  ? 0.2359 0.2582 0.2391 0.0243  -0.0180 -0.0326 974  LEU B N   
15838 C CA  . LEU B 976  ? 0.2456 0.2665 0.2437 0.0258  -0.0184 -0.0336 974  LEU B CA  
15839 C C   . LEU B 976  ? 0.2659 0.2893 0.2592 0.0248  -0.0177 -0.0316 974  LEU B C   
15840 O O   . LEU B 976  ? 0.2169 0.2450 0.2104 0.0242  -0.0154 -0.0298 974  LEU B O   
15841 C CB  . LEU B 976  ? 0.2352 0.2572 0.2331 0.0283  -0.0165 -0.0347 974  LEU B CB  
15842 C CG  . LEU B 976  ? 0.2719 0.2929 0.2637 0.0306  -0.0164 -0.0358 974  LEU B CG  
15843 C CD1 . LEU B 976  ? 0.2415 0.2566 0.2312 0.0309  -0.0195 -0.0380 974  LEU B CD1 
15844 C CD2 . LEU B 976  ? 0.2906 0.3130 0.2823 0.0333  -0.0143 -0.0367 974  LEU B CD2 
15845 N N   . HIS B 977  ? 0.2566 0.2770 0.2456 0.0245  -0.0197 -0.0318 975  HIS B N   
15846 C CA  . HIS B 977  ? 0.2418 0.2644 0.2254 0.0233  -0.0192 -0.0297 975  HIS B CA  
15847 C C   . HIS B 977  ? 0.2555 0.2782 0.2337 0.0256  -0.0187 -0.0309 975  HIS B C   
15848 O O   . HIS B 977  ? 0.2611 0.2790 0.2371 0.0266  -0.0211 -0.0328 975  HIS B O   
15849 C CB  . HIS B 977  ? 0.2349 0.2537 0.2168 0.0210  -0.0221 -0.0285 975  HIS B CB  
15850 C CG  . HIS B 977  ? 0.2576 0.2775 0.2419 0.0184  -0.0220 -0.0263 975  HIS B CG  
15851 N ND1 . HIS B 977  ? 0.3352 0.3545 0.3252 0.0184  -0.0222 -0.0270 975  HIS B ND1 
15852 C CD2 . HIS B 977  ? 0.2546 0.2755 0.2358 0.0157  -0.0221 -0.0235 975  HIS B CD2 
15853 C CE1 . HIS B 977  ? 0.3114 0.3310 0.3016 0.0160  -0.0224 -0.0250 975  HIS B CE1 
15854 N NE2 . HIS B 977  ? 0.2908 0.3111 0.2758 0.0142  -0.0225 -0.0228 975  HIS B NE2 
15855 N N   . THR B 978  ? 0.2522 0.2805 0.2280 0.0264  -0.0157 -0.0299 976  THR B N   
15856 C CA  . THR B 978  ? 0.2465 0.2759 0.2166 0.0291  -0.0147 -0.0311 976  THR B CA  
15857 C C   . THR B 978  ? 0.2991 0.3368 0.2676 0.0291  -0.0112 -0.0289 976  THR B C   
15858 O O   . THR B 978  ? 0.3121 0.3543 0.2850 0.0279  -0.0095 -0.0273 976  THR B O   
15859 C CB  . THR B 978  ? 0.2980 0.3243 0.2690 0.0327  -0.0148 -0.0344 976  THR B CB  
15860 O OG1 . THR B 978  ? 0.2977 0.3246 0.2624 0.0357  -0.0139 -0.0359 976  THR B OG1 
15861 C CG2 . THR B 978  ? 0.2784 0.3081 0.2545 0.0336  -0.0125 -0.0343 976  THR B CG2 
15862 N N   . ARG B 979  ? 0.3186 0.3590 0.2809 0.0305  -0.0102 -0.0288 977  ARG B N   
15863 C CA  . ARG B 979  ? 0.3272 0.3768 0.2880 0.0312  -0.0065 -0.0270 977  ARG B CA  
15864 C C   . ARG B 979  ? 0.3150 0.3666 0.2742 0.0364  -0.0045 -0.0298 977  ARG B C   
15865 O O   . ARG B 979  ? 0.3126 0.3726 0.2705 0.0380  -0.0013 -0.0288 977  ARG B O   
15866 C CB  . ARG B 979  ? 0.3754 0.4282 0.3299 0.0291  -0.0062 -0.0246 977  ARG B CB  
15867 C CG  . ARG B 979  ? 0.4573 0.5085 0.4124 0.0238  -0.0082 -0.0213 977  ARG B CG  
15868 C CD  . ARG B 979  ? 0.5221 0.5745 0.4699 0.0221  -0.0085 -0.0192 977  ARG B CD  
15869 N NE  . ARG B 979  ? 0.6072 0.6547 0.5541 0.0175  -0.0116 -0.0167 977  ARG B NE  
15870 C CZ  . ARG B 979  ? 0.6385 0.6854 0.5791 0.0151  -0.0127 -0.0144 977  ARG B CZ  
15871 N NH1 . ARG B 979  ? 0.6171 0.6689 0.5516 0.0166  -0.0106 -0.0141 977  ARG B NH1 
15872 N NH2 . ARG B 979  ? 0.6320 0.6730 0.5719 0.0113  -0.0159 -0.0123 977  ARG B NH2 
15873 N N   . LEU B 980  ? 0.2573 0.3015 0.2167 0.0392  -0.0063 -0.0333 978  LEU B N   
15874 C CA  . LEU B 980  ? 0.2681 0.3120 0.2245 0.0444  -0.0051 -0.0363 978  LEU B CA  
15875 C C   . LEU B 980  ? 0.2929 0.3368 0.2549 0.0464  -0.0042 -0.0373 978  LEU B C   
15876 O O   . LEU B 980  ? 0.2884 0.3264 0.2548 0.0450  -0.0064 -0.0380 978  LEU B O   
15877 C CB  . LEU B 980  ? 0.2511 0.2860 0.2028 0.0461  -0.0082 -0.0396 978  LEU B CB  
15878 C CG  . LEU B 980  ? 0.3397 0.3736 0.2857 0.0439  -0.0097 -0.0386 978  LEU B CG  
15879 C CD1 . LEU B 980  ? 0.3373 0.3620 0.2791 0.0454  -0.0132 -0.0420 978  LEU B CD1 
15880 C CD2 . LEU B 980  ? 0.3004 0.3426 0.2408 0.0453  -0.0065 -0.0373 978  LEU B CD2 
15881 N N   . ASP B 981  ? 0.2820 0.3329 0.2437 0.0497  -0.0011 -0.0372 979  ASP B N   
15882 C CA  . ASP B 981  ? 0.2727 0.3239 0.2393 0.0519  -0.0002 -0.0378 979  ASP B CA  
15883 C C   . ASP B 981  ? 0.2823 0.3234 0.2481 0.0547  -0.0027 -0.0414 979  ASP B C   
15884 O O   . ASP B 981  ? 0.2827 0.3206 0.2535 0.0541  -0.0035 -0.0415 979  ASP B O   
15885 C CB  . ASP B 981  ? 0.2876 0.3484 0.2533 0.0558  0.0034  -0.0374 979  ASP B CB  
15886 C CG  . ASP B 981  ? 0.3503 0.4219 0.3195 0.0524  0.0057  -0.0333 979  ASP B CG  
15887 O OD1 . ASP B 981  ? 0.3463 0.4169 0.3188 0.0472  0.0045  -0.0309 979  ASP B OD1 
15888 O OD2 . ASP B 981  ? 0.3519 0.4330 0.3202 0.0550  0.0088  -0.0324 979  ASP B OD2 
15889 N N   . GLU B 982  ? 0.2879 0.3238 0.2472 0.0574  -0.0040 -0.0443 980  GLU B N   
15890 C CA  . GLU B 982  ? 0.2864 0.3121 0.2447 0.0596  -0.0068 -0.0476 980  GLU B CA  
15891 C C   . GLU B 982  ? 0.2996 0.3189 0.2625 0.0550  -0.0099 -0.0471 980  GLU B C   
15892 O O   . GLU B 982  ? 0.2785 0.2921 0.2445 0.0551  -0.0115 -0.0482 980  GLU B O   
15893 C CB  . GLU B 982  ? 0.3339 0.3545 0.2837 0.0630  -0.0081 -0.0509 980  GLU B CB  
15894 C CG  . GLU B 982  ? 0.3532 0.3625 0.3015 0.0649  -0.0114 -0.0542 980  GLU B CG  
15895 C CD  . GLU B 982  ? 0.4752 0.4779 0.4151 0.0673  -0.0136 -0.0576 980  GLU B CD  
15896 O OE1 . GLU B 982  ? 0.5387 0.5441 0.4747 0.0662  -0.0135 -0.0571 980  GLU B OE1 
15897 O OE2 . GLU B 982  ? 0.4923 0.4866 0.4291 0.0704  -0.0157 -0.0608 980  GLU B OE2 
15898 N N   . THR B 983  ? 0.2749 0.2954 0.2384 0.0510  -0.0108 -0.0453 981  THR B N   
15899 C CA  . THR B 983  ? 0.2673 0.2829 0.2354 0.0470  -0.0137 -0.0449 981  THR B CA  
15900 C C   . THR B 983  ? 0.2775 0.2963 0.2531 0.0448  -0.0125 -0.0427 981  THR B C   
15901 O O   . THR B 983  ? 0.2964 0.3109 0.2765 0.0433  -0.0143 -0.0432 981  THR B O   
15902 C CB  . THR B 983  ? 0.2977 0.3137 0.2638 0.0440  -0.0150 -0.0437 981  THR B CB  
15903 O OG1 . THR B 983  ? 0.3040 0.3161 0.2629 0.0461  -0.0165 -0.0459 981  THR B OG1 
15904 C CG2 . THR B 983  ? 0.2956 0.3080 0.2671 0.0403  -0.0177 -0.0430 981  THR B CG2 
15905 N N   . ILE B 984  ? 0.2801 0.3068 0.2572 0.0444  -0.0096 -0.0403 982  ILE B N   
15906 C CA  . ILE B 984  ? 0.2498 0.2797 0.2335 0.0427  -0.0084 -0.0384 982  ILE B CA  
15907 C C   . ILE B 984  ? 0.2688 0.2956 0.2544 0.0454  -0.0083 -0.0399 982  ILE B C   
15908 O O   . ILE B 984  ? 0.2810 0.3049 0.2713 0.0436  -0.0094 -0.0397 982  ILE B O   
15909 C CB  . ILE B 984  ? 0.2865 0.3257 0.2709 0.0420  -0.0054 -0.0356 982  ILE B CB  
15910 C CG1 . ILE B 984  ? 0.3187 0.3596 0.3016 0.0383  -0.0061 -0.0336 982  ILE B CG1 
15911 C CG2 . ILE B 984  ? 0.2624 0.3047 0.2527 0.0409  -0.0043 -0.0340 982  ILE B CG2 
15912 C CD1 . ILE B 984  ? 0.3345 0.3843 0.3163 0.0373  -0.0035 -0.0309 982  ILE B CD1 
15913 N N   . ALA B 985  ? 0.2701 0.2971 0.2516 0.0498  -0.0072 -0.0415 983  ALA B N   
15914 C CA  . ALA B 985  ? 0.2950 0.3186 0.2776 0.0527  -0.0073 -0.0428 983  ALA B CA  
15915 C C   . ALA B 985  ? 0.3110 0.3246 0.2938 0.0517  -0.0107 -0.0447 983  ALA B C   
15916 O O   . ALA B 985  ? 0.3111 0.3219 0.2979 0.0508  -0.0114 -0.0443 983  ALA B O   
15917 C CB  . ALA B 985  ? 0.2720 0.2972 0.2494 0.0583  -0.0057 -0.0445 983  ALA B CB  
15918 N N   . HIS B 986  ? 0.2803 0.2889 0.2588 0.0516  -0.0129 -0.0467 984  HIS B N   
15919 C CA  . HIS B 986  ? 0.3049 0.3046 0.2837 0.0502  -0.0165 -0.0484 984  HIS B CA  
15920 C C   . HIS B 986  ? 0.2816 0.2819 0.2674 0.0455  -0.0174 -0.0465 984  HIS B C   
15921 O O   . HIS B 986  ? 0.3146 0.3113 0.3039 0.0444  -0.0185 -0.0464 984  HIS B O   
15922 C CB  . HIS B 986  ? 0.2795 0.2749 0.2523 0.0506  -0.0188 -0.0506 984  HIS B CB  
15923 C CG  . HIS B 986  ? 0.3539 0.3411 0.3274 0.0483  -0.0228 -0.0521 984  HIS B CG  
15924 N ND1 . HIS B 986  ? 0.3946 0.3773 0.3631 0.0483  -0.0255 -0.0540 984  HIS B ND1 
15925 C CD2 . HIS B 986  ? 0.3849 0.3682 0.3633 0.0458  -0.0246 -0.0518 984  HIS B CD2 
15926 C CE1 . HIS B 986  ? 0.4500 0.4266 0.4208 0.0458  -0.0290 -0.0549 984  HIS B CE1 
15927 N NE2 . HIS B 986  ? 0.3491 0.3261 0.3259 0.0441  -0.0284 -0.0535 984  HIS B NE2 
15928 N N   . VAL B 987  ? 0.2749 0.2799 0.2627 0.0427  -0.0170 -0.0448 985  VAL B N   
15929 C CA  . VAL B 987  ? 0.2893 0.2944 0.2830 0.0388  -0.0182 -0.0435 985  VAL B CA  
15930 C C   . VAL B 987  ? 0.2764 0.2851 0.2756 0.0379  -0.0162 -0.0416 985  VAL B C   
15931 O O   . VAL B 987  ? 0.2646 0.2712 0.2682 0.0359  -0.0174 -0.0414 985  VAL B O   
15932 C CB  . VAL B 987  ? 0.2737 0.2819 0.2671 0.0367  -0.0185 -0.0424 985  VAL B CB  
15933 C CG1 . VAL B 987  ? 0.2415 0.2511 0.2412 0.0334  -0.0192 -0.0410 985  VAL B CG1 
15934 C CG2 . VAL B 987  ? 0.2512 0.2548 0.2398 0.0370  -0.0212 -0.0443 985  VAL B CG2 
15935 N N   . THR B 988  ? 0.2679 0.2823 0.2669 0.0392  -0.0134 -0.0402 986  THR B N   
15936 C CA  . THR B 988  ? 0.3102 0.3281 0.3141 0.0383  -0.0117 -0.0384 986  THR B CA  
15937 C C   . THR B 988  ? 0.2992 0.3132 0.3036 0.0401  -0.0120 -0.0391 986  THR B C   
15938 O O   . THR B 988  ? 0.3486 0.3637 0.3574 0.0387  -0.0114 -0.0377 986  THR B O   
15939 C CB  . THR B 988  ? 0.3146 0.3402 0.3184 0.0389  -0.0089 -0.0365 986  THR B CB  
15940 O OG1 . THR B 988  ? 0.3258 0.3528 0.3255 0.0428  -0.0075 -0.0373 986  THR B OG1 
15941 C CG2 . THR B 988  ? 0.3302 0.3589 0.3332 0.0364  -0.0089 -0.0354 986  THR B CG2 
15942 N N   . SER B 989  ? 0.3475 0.3565 0.3473 0.0432  -0.0130 -0.0412 987  SER B N   
15943 C CA  . SER B 989  ? 0.3324 0.3357 0.3320 0.0447  -0.0140 -0.0420 987  SER B CA  
15944 C C   . SER B 989  ? 0.3784 0.3753 0.3802 0.0417  -0.0169 -0.0425 987  SER B C   
15945 O O   . SER B 989  ? 0.3778 0.3709 0.3812 0.0413  -0.0177 -0.0421 987  SER B O   
15946 C CB  . SER B 989  ? 0.2846 0.2841 0.2777 0.0495  -0.0142 -0.0443 987  SER B CB  
15947 O OG  . SER B 989  ? 0.3976 0.3915 0.3864 0.0497  -0.0167 -0.0466 987  SER B OG  
15948 N N   . ARG B 990  ? 0.2979 0.2938 0.2999 0.0393  -0.0188 -0.0432 988  ARG B N   
15949 C CA  . ARG B 990  ? 0.3265 0.3171 0.3307 0.0364  -0.0218 -0.0438 988  ARG B CA  
15950 C C   . ARG B 990  ? 0.3255 0.3206 0.3362 0.0325  -0.0217 -0.0420 988  ARG B C   
15951 O O   . ARG B 990  ? 0.3518 0.3445 0.3659 0.0299  -0.0234 -0.0417 988  ARG B O   
15952 C CB  . ARG B 990  ? 0.2914 0.2770 0.2910 0.0368  -0.0246 -0.0462 988  ARG B CB  
15953 C CG  . ARG B 990  ? 0.3825 0.3632 0.3748 0.0412  -0.0248 -0.0484 988  ARG B CG  
15954 C CD  . ARG B 990  ? 0.4133 0.3857 0.4042 0.0417  -0.0270 -0.0494 988  ARG B CD  
15955 N NE  . ARG B 990  ? 0.3791 0.3443 0.3681 0.0398  -0.0311 -0.0512 988  ARG B NE  
15956 C CZ  . ARG B 990  ? 0.3750 0.3313 0.3616 0.0397  -0.0340 -0.0524 988  ARG B CZ  
15957 N NH1 . ARG B 990  ? 0.4052 0.3583 0.3912 0.0414  -0.0334 -0.0519 988  ARG B NH1 
15958 N NH2 . ARG B 990  ? 0.3629 0.3132 0.3476 0.0377  -0.0378 -0.0541 988  ARG B NH2 
15959 N N   . ILE B 991  ? 0.3244 0.3258 0.3368 0.0320  -0.0198 -0.0409 989  ILE B N   
15960 C CA  . ILE B 991  ? 0.3146 0.3199 0.3327 0.0289  -0.0198 -0.0396 989  ILE B CA  
15961 C C   . ILE B 991  ? 0.3101 0.3179 0.3323 0.0279  -0.0181 -0.0378 989  ILE B C   
15962 O O   . ILE B 991  ? 0.3187 0.3274 0.3396 0.0297  -0.0162 -0.0370 989  ILE B O   
15963 C CB  . ILE B 991  ? 0.3112 0.3210 0.3288 0.0287  -0.0188 -0.0389 989  ILE B CB  
15964 C CG1 . ILE B 991  ? 0.2845 0.2968 0.3071 0.0261  -0.0197 -0.0383 989  ILE B CG1 
15965 C CG2 . ILE B 991  ? 0.3117 0.3261 0.3287 0.0299  -0.0158 -0.0375 989  ILE B CG2 
15966 C CD1 . ILE B 991  ? 0.2833 0.2925 0.3058 0.0251  -0.0229 -0.0398 989  ILE B CD1 
15967 N N   . LYS B 992  ? 0.2830 0.2921 0.3102 0.0252  -0.0187 -0.0371 990  LYS B N   
15968 C CA  . LYS B 992  ? 0.3099 0.3218 0.3411 0.0239  -0.0171 -0.0353 990  LYS B CA  
15969 C C   . LYS B 992  ? 0.2927 0.3106 0.3274 0.0227  -0.0158 -0.0344 990  LYS B C   
15970 O O   . LYS B 992  ? 0.4134 0.4330 0.4520 0.0207  -0.0168 -0.0344 990  LYS B O   
15971 C CB  . LYS B 992  ? 0.3690 0.3776 0.4027 0.0217  -0.0189 -0.0350 990  LYS B CB  
15972 N N   . ALA B 993  ? 0.2810 0.3022 0.3144 0.0238  -0.0138 -0.0336 991  ALA B N   
15973 C CA  . ALA B 993  ? 0.2299 0.2556 0.2657 0.0228  -0.0129 -0.0329 991  ALA B CA  
15974 C C   . ALA B 993  ? 0.2057 0.2348 0.2410 0.0234  -0.0105 -0.0315 991  ALA B C   
15975 O O   . ALA B 993  ? 0.2731 0.3017 0.3054 0.0251  -0.0096 -0.0312 991  ALA B O   
15976 C CB  . ALA B 993  ? 0.2594 0.2850 0.2934 0.0230  -0.0141 -0.0338 991  ALA B CB  
15977 N N   . GLY B 994  ? 0.2510 0.2836 0.2890 0.0222  -0.0095 -0.0307 992  GLY B N   
15978 C CA  . GLY B 994  ? 0.2370 0.2728 0.2747 0.0224  -0.0075 -0.0292 992  GLY B CA  
15979 C C   . GLY B 994  ? 0.2552 0.2929 0.2902 0.0228  -0.0070 -0.0289 992  GLY B C   
15980 O O   . GLY B 994  ? 0.2292 0.2695 0.2633 0.0232  -0.0056 -0.0277 992  GLY B O   
15981 N N   . ASN B 995  ? 0.2243 0.2610 0.2582 0.0223  -0.0083 -0.0297 993  ASN B N   
15982 C CA  . ASN B 995  ? 0.1886 0.2267 0.2198 0.0220  -0.0082 -0.0291 993  ASN B CA  
15983 C C   . ASN B 995  ? 0.2194 0.2550 0.2475 0.0225  -0.0096 -0.0299 993  ASN B C   
15984 O O   . ASN B 995  ? 0.2451 0.2781 0.2735 0.0222  -0.0114 -0.0310 993  ASN B O   
15985 C CB  . ASN B 995  ? 0.1731 0.2120 0.2055 0.0206  -0.0088 -0.0290 993  ASN B CB  
15986 C CG  . ASN B 995  ? 0.2117 0.2536 0.2455 0.0199  -0.0073 -0.0280 993  ASN B CG  
15987 O OD1 . ASN B 995  ? 0.2416 0.2843 0.2783 0.0199  -0.0067 -0.0282 993  ASN B OD1 
15988 N ND2 . ASN B 995  ? 0.2220 0.2659 0.2538 0.0192  -0.0067 -0.0268 993  ASN B ND2 
15989 N N   . LEU B 996  ? 0.2383 0.2751 0.2634 0.0235  -0.0087 -0.0293 994  LEU B N   
15990 C CA  . LEU B 996  ? 0.2166 0.2516 0.2378 0.0243  -0.0096 -0.0300 994  LEU B CA  
15991 C C   . LEU B 996  ? 0.2370 0.2744 0.2554 0.0231  -0.0093 -0.0285 994  LEU B C   
15992 O O   . LEU B 996  ? 0.2242 0.2658 0.2429 0.0223  -0.0079 -0.0269 994  LEU B O   
15993 C CB  . LEU B 996  ? 0.2418 0.2767 0.2610 0.0268  -0.0086 -0.0305 994  LEU B CB  
15994 C CG  . LEU B 996  ? 0.2868 0.3190 0.3082 0.0279  -0.0088 -0.0314 994  LEU B CG  
15995 C CD1 . LEU B 996  ? 0.3277 0.3586 0.3459 0.0308  -0.0083 -0.0322 994  LEU B CD1 
15996 C CD2 . LEU B 996  ? 0.3140 0.3421 0.3373 0.0268  -0.0110 -0.0327 994  LEU B CD2 
15997 N N   . TYR B 997  ? 0.1926 0.2275 0.2082 0.0226  -0.0110 -0.0289 995  TYR B N   
15998 C CA  . TYR B 997  ? 0.2433 0.2798 0.2558 0.0209  -0.0112 -0.0273 995  TYR B CA  
15999 C C   . TYR B 997  ? 0.2314 0.2669 0.2394 0.0217  -0.0116 -0.0276 995  TYR B C   
16000 O O   . TYR B 997  ? 0.2522 0.2835 0.2592 0.0226  -0.0134 -0.0292 995  TYR B O   
16001 C CB  . TYR B 997  ? 0.2263 0.2599 0.2393 0.0189  -0.0132 -0.0271 995  TYR B CB  
16002 C CG  . TYR B 997  ? 0.2555 0.2901 0.2723 0.0182  -0.0127 -0.0270 995  TYR B CG  
16003 C CD1 . TYR B 997  ? 0.2407 0.2783 0.2573 0.0166  -0.0117 -0.0253 995  TYR B CD1 
16004 C CD2 . TYR B 997  ? 0.2851 0.3179 0.3056 0.0191  -0.0133 -0.0286 995  TYR B CD2 
16005 C CE1 . TYR B 997  ? 0.2522 0.2905 0.2717 0.0161  -0.0113 -0.0254 995  TYR B CE1 
16006 C CE2 . TYR B 997  ? 0.2691 0.3032 0.2926 0.0187  -0.0127 -0.0285 995  TYR B CE2 
16007 C CZ  . TYR B 997  ? 0.2435 0.2800 0.2662 0.0173  -0.0117 -0.0270 995  TYR B CZ  
16008 O OH  . TYR B 997  ? 0.3288 0.3665 0.3539 0.0169  -0.0112 -0.0271 995  TYR B OH  
16009 N N   . ILE B 998  ? 0.2454 0.2852 0.2505 0.0215  -0.0101 -0.0260 996  ILE B N   
16010 C CA  . ILE B 998  ? 0.2393 0.2794 0.2396 0.0226  -0.0100 -0.0262 996  ILE B CA  
16011 C C   . ILE B 998  ? 0.2084 0.2497 0.2052 0.0197  -0.0106 -0.0238 996  ILE B C   
16012 O O   . ILE B 998  ? 0.2307 0.2770 0.2277 0.0179  -0.0092 -0.0216 996  ILE B O   
16013 C CB  . ILE B 998  ? 0.2599 0.3047 0.2592 0.0253  -0.0074 -0.0264 996  ILE B CB  
16014 C CG1 . ILE B 998  ? 0.2678 0.3103 0.2703 0.0279  -0.0072 -0.0284 996  ILE B CG1 
16015 C CG2 . ILE B 998  ? 0.2497 0.2947 0.2435 0.0269  -0.0073 -0.0269 996  ILE B CG2 
16016 C CD1 . ILE B 998  ? 0.2920 0.3279 0.2936 0.0291  -0.0093 -0.0308 996  ILE B CD1 
16017 N N   . ASN B 999  ? 0.2044 0.2410 0.1979 0.0192  -0.0129 -0.0243 997  ASN B N   
16018 C CA  . ASN B 999  ? 0.2380 0.2748 0.2271 0.0165  -0.0138 -0.0220 997  ASN B CA  
16019 C C   . ASN B 999  ? 0.2222 0.2582 0.2129 0.0132  -0.0149 -0.0200 997  ASN B C   
16020 O O   . ASN B 999  ? 0.2608 0.2994 0.2490 0.0103  -0.0147 -0.0173 997  ASN B O   
16021 C CB  . ASN B 999  ? 0.2461 0.2896 0.2317 0.0167  -0.0113 -0.0203 997  ASN B CB  
16022 C CG  . ASN B 999  ? 0.2115 0.2544 0.1937 0.0201  -0.0108 -0.0225 997  ASN B CG  
16023 O OD1 . ASN B 999  ? 0.2618 0.2986 0.2423 0.0208  -0.0132 -0.0242 997  ASN B OD1 
16024 N ND2 . ASN B 999  ? 0.2548 0.3040 0.2359 0.0223  -0.0080 -0.0224 997  ASN B ND2 
16025 N N   . ARG B 1000 ? 0.2015 0.2338 0.1961 0.0135  -0.0162 -0.0215 998  ARG B N   
16026 C CA  . ARG B 1000 ? 0.2279 0.2577 0.2235 0.0110  -0.0178 -0.0204 998  ARG B CA  
16027 C C   . ARG B 1000 ? 0.2246 0.2494 0.2235 0.0126  -0.0197 -0.0228 998  ARG B C   
16028 O O   . ARG B 1000 ? 0.2352 0.2589 0.2357 0.0150  -0.0199 -0.0249 998  ARG B O   
16029 C CB  . ARG B 1000 ? 0.2205 0.2555 0.2187 0.0098  -0.0157 -0.0191 998  ARG B CB  
16030 C CG  . ARG B 1000 ? 0.2179 0.2563 0.2204 0.0125  -0.0134 -0.0207 998  ARG B CG  
16031 C CD  . ARG B 1000 ? 0.2320 0.2729 0.2379 0.0113  -0.0125 -0.0200 998  ARG B CD  
16032 N NE  . ARG B 1000 ? 0.2080 0.2438 0.2153 0.0108  -0.0146 -0.0210 998  ARG B NE  
16033 C CZ  . ARG B 1000 ? 0.2526 0.2890 0.2621 0.0099  -0.0144 -0.0209 998  ARG B CZ  
16034 N NH1 . ARG B 1000 ? 0.2145 0.2564 0.2253 0.0091  -0.0124 -0.0195 998  ARG B NH1 
16035 N NH2 . ARG B 1000 ? 0.2704 0.3022 0.2807 0.0100  -0.0163 -0.0221 998  ARG B NH2 
16036 N N   . ASN B 1001 ? 0.2160 0.2379 0.2157 0.0113  -0.0213 -0.0226 999  ASN B N   
16037 C CA  . ASN B 1001 ? 0.2217 0.2401 0.2249 0.0131  -0.0228 -0.0249 999  ASN B CA  
16038 C C   . ASN B 1001 ? 0.2218 0.2439 0.2301 0.0147  -0.0205 -0.0262 999  ASN B C   
16039 O O   . ASN B 1001 ? 0.2286 0.2552 0.2376 0.0144  -0.0180 -0.0253 999  ASN B O   
16040 C CB  . ASN B 1001 ? 0.2000 0.2138 0.2020 0.0119  -0.0253 -0.0245 999  ASN B CB  
16041 C CG  . ASN B 1001 ? 0.2910 0.3067 0.2939 0.0102  -0.0242 -0.0235 999  ASN B CG  
16042 O OD1 . ASN B 1001 ? 0.2591 0.2789 0.2657 0.0111  -0.0219 -0.0242 999  ASN B OD1 
16043 N ND2 . ASN B 1001 ? 0.3087 0.3210 0.3078 0.0076  -0.0261 -0.0218 999  ASN B ND2 
16044 N N   . ILE B 1002 ? 0.2235 0.2441 0.2355 0.0163  -0.0213 -0.0282 1000 ILE B N   
16045 C CA  . ILE B 1002 ? 0.2209 0.2448 0.2375 0.0175  -0.0193 -0.0292 1000 ILE B CA  
16046 C C   . ILE B 1002 ? 0.2723 0.2967 0.2918 0.0175  -0.0191 -0.0297 1000 ILE B C   
16047 O O   . ILE B 1002 ? 0.2632 0.2899 0.2868 0.0185  -0.0178 -0.0306 1000 ILE B O   
16048 C CB  . ILE B 1002 ? 0.2425 0.2658 0.2615 0.0193  -0.0199 -0.0310 1000 ILE B CB  
16049 C CG1 . ILE B 1002 ? 0.2203 0.2407 0.2410 0.0201  -0.0225 -0.0324 1000 ILE B CG1 
16050 C CG2 . ILE B 1002 ? 0.2180 0.2405 0.2333 0.0196  -0.0200 -0.0308 1000 ILE B CG2 
16051 C CD1 . ILE B 1002 ? 0.1864 0.2071 0.2105 0.0214  -0.0231 -0.0340 1000 ILE B CD1 
16052 N N   . ILE B 1003 ? 0.2402 0.2623 0.2574 0.0162  -0.0204 -0.0290 1001 ILE B N   
16053 C CA  . ILE B 1003 ? 0.2576 0.2793 0.2766 0.0165  -0.0205 -0.0298 1001 ILE B CA  
16054 C C   . ILE B 1003 ? 0.3212 0.3442 0.3383 0.0144  -0.0196 -0.0282 1001 ILE B C   
16055 O O   . ILE B 1003 ? 0.3083 0.3329 0.3228 0.0125  -0.0189 -0.0262 1001 ILE B O   
16056 C CB  . ILE B 1003 ? 0.2741 0.2908 0.2919 0.0175  -0.0236 -0.0310 1001 ILE B CB  
16057 C CG1 . ILE B 1003 ? 0.3243 0.3362 0.3364 0.0155  -0.0258 -0.0294 1001 ILE B CG1 
16058 C CG2 . ILE B 1003 ? 0.2355 0.2517 0.2557 0.0196  -0.0247 -0.0326 1001 ILE B CG2 
16059 C CD1 . ILE B 1003 ? 0.3181 0.3239 0.3282 0.0167  -0.0291 -0.0306 1001 ILE B CD1 
16060 N N   . GLY B 1004 ? 0.2874 0.3101 0.3054 0.0146  -0.0196 -0.0290 1002 GLY B N   
16061 C CA  . GLY B 1004 ? 0.3264 0.3494 0.3423 0.0124  -0.0195 -0.0276 1002 GLY B CA  
16062 C C   . GLY B 1004 ? 0.3234 0.3523 0.3408 0.0114  -0.0167 -0.0261 1002 GLY B C   
16063 O O   . GLY B 1004 ? 0.3266 0.3569 0.3416 0.0090  -0.0167 -0.0241 1002 GLY B O   
16064 N N   . ALA B 1005 ? 0.3190 0.3515 0.3403 0.0132  -0.0146 -0.0269 1003 ALA B N   
16065 C CA  . ALA B 1005 ? 0.2280 0.2656 0.2507 0.0128  -0.0123 -0.0256 1003 ALA B CA  
16066 C C   . ALA B 1005 ? 0.2479 0.2869 0.2696 0.0111  -0.0121 -0.0247 1003 ALA B C   
16067 O O   . ALA B 1005 ? 0.3429 0.3796 0.3643 0.0113  -0.0130 -0.0258 1003 ALA B O   
16068 C CB  . ALA B 1005 ? 0.2704 0.3103 0.2971 0.0149  -0.0105 -0.0266 1003 ALA B CB  
16069 N N   . VAL B 1006 ? 0.2273 0.2703 0.2483 0.0096  -0.0111 -0.0226 1004 VAL B N   
16070 C CA  . VAL B 1006 ? 0.2202 0.2648 0.2398 0.0072  -0.0115 -0.0213 1004 VAL B CA  
16071 C C   . VAL B 1006 ? 0.2760 0.3254 0.2984 0.0082  -0.0094 -0.0210 1004 VAL B C   
16072 O O   . VAL B 1006 ? 0.2188 0.2720 0.2432 0.0095  -0.0076 -0.0203 1004 VAL B O   
16073 C CB  . VAL B 1006 ? 0.2349 0.2818 0.2521 0.0045  -0.0120 -0.0188 1004 VAL B CB  
16074 C CG1 . VAL B 1006 ? 0.2136 0.2637 0.2301 0.0018  -0.0122 -0.0171 1004 VAL B CG1 
16075 C CG2 . VAL B 1006 ? 0.2703 0.3114 0.2840 0.0030  -0.0145 -0.0188 1004 VAL B CG2 
16076 N N   . VAL B 1007 ? 0.2159 0.2645 0.2378 0.0076  -0.0099 -0.0215 1005 VAL B N   
16077 C CA  . VAL B 1007 ? 0.2301 0.2828 0.2541 0.0083  -0.0082 -0.0211 1005 VAL B CA  
16078 C C   . VAL B 1007 ? 0.1950 0.2536 0.2198 0.0075  -0.0070 -0.0188 1005 VAL B C   
16079 O O   . VAL B 1007 ? 0.2208 0.2810 0.2438 0.0051  -0.0080 -0.0172 1005 VAL B O   
16080 C CB  . VAL B 1007 ? 0.2178 0.2687 0.2400 0.0073  -0.0093 -0.0219 1005 VAL B CB  
16081 C CG1 . VAL B 1007 ? 0.1923 0.2478 0.2161 0.0077  -0.0076 -0.0211 1005 VAL B CG1 
16082 C CG2 . VAL B 1007 ? 0.2270 0.2733 0.2490 0.0091  -0.0099 -0.0245 1005 VAL B CG2 
16083 N N   . GLY B 1008 ? 0.2149 0.2767 0.2423 0.0097  -0.0051 -0.0185 1006 GLY B N   
16084 C CA  . GLY B 1008 ? 0.1923 0.2600 0.2208 0.0098  -0.0040 -0.0165 1006 GLY B CA  
16085 C C   . GLY B 1008 ? 0.2142 0.2841 0.2423 0.0100  -0.0037 -0.0156 1006 GLY B C   
16086 O O   . GLY B 1008 ? 0.2341 0.3097 0.2630 0.0103  -0.0027 -0.0139 1006 GLY B O   
16087 N N   . VAL B 1009 ? 0.2087 0.2744 0.2354 0.0101  -0.0044 -0.0167 1007 VAL B N   
16088 C CA  . VAL B 1009 ? 0.2400 0.3074 0.2656 0.0102  -0.0041 -0.0159 1007 VAL B CA  
16089 C C   . VAL B 1009 ? 0.2297 0.2934 0.2557 0.0128  -0.0038 -0.0177 1007 VAL B C   
16090 O O   . VAL B 1009 ? 0.1913 0.2572 0.2175 0.0149  -0.0026 -0.0177 1007 VAL B O   
16091 C CB  . VAL B 1009 ? 0.2439 0.3099 0.2667 0.0069  -0.0059 -0.0149 1007 VAL B CB  
16092 C CG1 . VAL B 1009 ? 0.2479 0.3163 0.2692 0.0070  -0.0054 -0.0140 1007 VAL B CG1 
16093 C CG2 . VAL B 1009 ? 0.2201 0.2895 0.2424 0.0037  -0.0067 -0.0130 1007 VAL B CG2 
16094 N N   . GLN B 1010 ? 0.2179 0.2760 0.2438 0.0129  -0.0050 -0.0195 1008 GLN B N   
16095 C CA  . GLN B 1010 ? 0.2067 0.2615 0.2338 0.0151  -0.0049 -0.0213 1008 GLN B CA  
16096 C C   . GLN B 1010 ? 0.1995 0.2529 0.2290 0.0156  -0.0047 -0.0223 1008 GLN B C   
16097 O O   . GLN B 1010 ? 0.2017 0.2518 0.2314 0.0154  -0.0058 -0.0237 1008 GLN B O   
16098 C CB  . GLN B 1010 ? 0.2353 0.2857 0.2606 0.0148  -0.0065 -0.0224 1008 GLN B CB  
16099 C CG  . GLN B 1010 ? 0.2319 0.2835 0.2544 0.0140  -0.0067 -0.0212 1008 GLN B CG  
16100 C CD  . GLN B 1010 ? 0.2309 0.2815 0.2508 0.0110  -0.0083 -0.0200 1008 GLN B CD  
16101 O OE1 . GLN B 1010 ? 0.2391 0.2857 0.2586 0.0101  -0.0099 -0.0208 1008 GLN B OE1 
16102 N NE2 . GLN B 1010 ? 0.2138 0.2680 0.2316 0.0095  -0.0079 -0.0180 1008 GLN B NE2 
16103 N N   . PRO B 1011 ? 0.2223 0.2786 0.2536 0.0165  -0.0033 -0.0216 1009 PRO B N   
16104 C CA  . PRO B 1011 ? 0.2047 0.2600 0.2381 0.0170  -0.0028 -0.0224 1009 PRO B CA  
16105 C C   . PRO B 1011 ? 0.2433 0.2951 0.2780 0.0179  -0.0034 -0.0241 1009 PRO B C   
16106 O O   . PRO B 1011 ? 0.2507 0.3010 0.2853 0.0189  -0.0036 -0.0245 1009 PRO B O   
16107 C CB  . PRO B 1011 ? 0.2168 0.2749 0.2514 0.0182  -0.0014 -0.0212 1009 PRO B CB  
16108 C CG  . PRO B 1011 ? 0.2693 0.3312 0.3025 0.0180  -0.0011 -0.0197 1009 PRO B CG  
16109 C CD  . PRO B 1011 ? 0.2179 0.2785 0.2492 0.0173  -0.0020 -0.0201 1009 PRO B CD  
16110 N N   . PHE B 1012 ? 0.2099 0.2605 0.2457 0.0175  -0.0038 -0.0251 1010 PHE B N   
16111 C CA  . PHE B 1012 ? 0.2522 0.3002 0.2893 0.0180  -0.0049 -0.0268 1010 PHE B CA  
16112 C C   . PHE B 1012 ? 0.2319 0.2807 0.2723 0.0185  -0.0041 -0.0272 1010 PHE B C   
16113 O O   . PHE B 1012 ? 0.2416 0.2926 0.2829 0.0182  -0.0031 -0.0268 1010 PHE B O   
16114 C CB  . PHE B 1012 ? 0.1831 0.2293 0.2189 0.0176  -0.0063 -0.0278 1010 PHE B CB  
16115 C CG  . PHE B 1012 ? 0.2248 0.2687 0.2618 0.0184  -0.0077 -0.0295 1010 PHE B CG  
16116 C CD1 . PHE B 1012 ? 0.2792 0.3204 0.3146 0.0185  -0.0091 -0.0297 1010 PHE B CD1 
16117 C CD2 . PHE B 1012 ? 0.2621 0.3071 0.3020 0.0192  -0.0075 -0.0307 1010 PHE B CD2 
16118 C CE1 . PHE B 1012 ? 0.2466 0.2858 0.2832 0.0194  -0.0107 -0.0311 1010 PHE B CE1 
16119 C CE2 . PHE B 1012 ? 0.3358 0.3795 0.3773 0.0201  -0.0089 -0.0321 1010 PHE B CE2 
16120 C CZ  . PHE B 1012 ? 0.3046 0.3452 0.3445 0.0202  -0.0106 -0.0323 1010 PHE B CZ  
16121 N N   . GLY B 1013 ? 0.2465 0.2936 0.2882 0.0190  -0.0047 -0.0278 1011 GLY B N   
16122 C CA  . GLY B 1013 ? 0.2646 0.3125 0.3096 0.0189  -0.0043 -0.0280 1011 GLY B CA  
16123 C C   . GLY B 1013 ? 0.3213 0.3667 0.3666 0.0192  -0.0050 -0.0280 1011 GLY B C   
16124 O O   . GLY B 1013 ? 0.2899 0.3337 0.3328 0.0199  -0.0050 -0.0275 1011 GLY B O   
16125 N N   . GLY B 1014 ? 0.3448 0.3900 0.3930 0.0187  -0.0057 -0.0286 1012 GLY B N   
16126 C CA  . GLY B 1014 ? 0.3136 0.3555 0.3617 0.0187  -0.0069 -0.0288 1012 GLY B CA  
16127 C C   . GLY B 1014 ? 0.3848 0.4268 0.4353 0.0175  -0.0065 -0.0278 1012 GLY B C   
16128 O O   . GLY B 1014 ? 0.3996 0.4441 0.4510 0.0169  -0.0049 -0.0264 1012 GLY B O   
16129 N N   . ARG B 1015 ? 0.3854 0.4243 0.4364 0.0169  -0.0081 -0.0282 1013 ARG B N   
16130 C CA  . ARG B 1015 ? 0.4358 0.4734 0.4887 0.0153  -0.0085 -0.0271 1013 ARG B CA  
16131 C C   . ARG B 1015 ? 0.4009 0.4396 0.4575 0.0136  -0.0101 -0.0278 1013 ARG B C   
16132 O O   . ARG B 1015 ? 0.3936 0.4337 0.4511 0.0141  -0.0110 -0.0292 1013 ARG B O   
16133 C CB  . ARG B 1015 ? 0.4211 0.4528 0.4704 0.0163  -0.0095 -0.0271 1013 ARG B CB  
16134 C CG  . ARG B 1015 ? 0.4188 0.4470 0.4653 0.0178  -0.0112 -0.0290 1013 ARG B CG  
16135 C CD  . ARG B 1015 ? 0.5265 0.5483 0.5706 0.0180  -0.0131 -0.0295 1013 ARG B CD  
16136 N NE  . ARG B 1015 ? 0.5789 0.5997 0.6262 0.0152  -0.0148 -0.0293 1013 ARG B NE  
16137 C CZ  . ARG B 1015 ? 0.5322 0.5530 0.5811 0.0141  -0.0168 -0.0305 1013 ARG B CZ  
16138 N NH1 . ARG B 1015 ? 0.4796 0.5006 0.5269 0.0157  -0.0174 -0.0321 1013 ARG B NH1 
16139 N NH2 . ARG B 1015 ? 0.5565 0.5773 0.6088 0.0112  -0.0183 -0.0299 1013 ARG B NH2 
16140 N N   . GLY B 1016 ? 0.3952 0.4330 0.4537 0.0113  -0.0106 -0.0266 1014 GLY B N   
16141 C CA  . GLY B 1016 ? 0.3856 0.4251 0.4480 0.0092  -0.0123 -0.0269 1014 GLY B CA  
16142 C C   . GLY B 1016 ? 0.3601 0.4073 0.4270 0.0089  -0.0110 -0.0270 1014 GLY B C   
16143 O O   . GLY B 1016 ? 0.3767 0.4281 0.4445 0.0088  -0.0087 -0.0258 1014 GLY B O   
16144 N N   . LEU B 1017 ? 0.3676 0.4168 0.4370 0.0091  -0.0127 -0.0284 1015 LEU B N   
16145 C CA  . LEU B 1017 ? 0.3636 0.4202 0.4372 0.0095  -0.0118 -0.0289 1015 LEU B CA  
16146 C C   . LEU B 1017 ? 0.3458 0.4035 0.4171 0.0123  -0.0103 -0.0300 1015 LEU B C   
16147 O O   . LEU B 1017 ? 0.3195 0.3826 0.3934 0.0132  -0.0094 -0.0306 1015 LEU B O   
16148 C CB  . LEU B 1017 ? 0.3602 0.4182 0.4369 0.0092  -0.0143 -0.0302 1015 LEU B CB  
16149 C CG  . LEU B 1017 ? 0.3795 0.4373 0.4592 0.0058  -0.0162 -0.0291 1015 LEU B CG  
16150 C CD1 . LEU B 1017 ? 0.4322 0.4904 0.5141 0.0057  -0.0193 -0.0306 1015 LEU B CD1 
16151 C CD2 . LEU B 1017 ? 0.3041 0.3694 0.3888 0.0033  -0.0143 -0.0271 1015 LEU B CD2 
16152 N N   . SER B 1018 ? 0.3047 0.3573 0.3709 0.0136  -0.0101 -0.0302 1016 SER B N   
16153 C CA  . SER B 1018 ? 0.3233 0.3760 0.3868 0.0157  -0.0091 -0.0310 1016 SER B CA  
16154 C C   . SER B 1018 ? 0.3281 0.3835 0.3910 0.0157  -0.0066 -0.0298 1016 SER B C   
16155 O O   . SER B 1018 ? 0.3409 0.3975 0.4023 0.0171  -0.0059 -0.0305 1016 SER B O   
16156 C CB  . SER B 1018 ? 0.3461 0.3931 0.4046 0.0168  -0.0101 -0.0314 1016 SER B CB  
16157 O OG  . SER B 1018 ? 0.3608 0.4055 0.4189 0.0174  -0.0125 -0.0328 1016 SER B OG  
16158 N N   . GLY B 1019 ? 0.3348 0.3909 0.3985 0.0141  -0.0054 -0.0280 1017 GLY B N   
16159 C CA  . GLY B 1019 ? 0.3049 0.3641 0.3681 0.0140  -0.0031 -0.0268 1017 GLY B CA  
16160 C C   . GLY B 1019 ? 0.3297 0.3872 0.3920 0.0125  -0.0024 -0.0246 1017 GLY B C   
16161 O O   . GLY B 1019 ? 0.3115 0.3647 0.3732 0.0117  -0.0037 -0.0241 1017 GLY B O   
16162 N N   . THR B 1020 ? 0.2552 0.3158 0.3170 0.0122  -0.0004 -0.0234 1018 THR B N   
16163 C CA  . THR B 1020 ? 0.3099 0.3690 0.3703 0.0111  0.0004  -0.0210 1018 THR B CA  
16164 C C   . THR B 1020 ? 0.2991 0.3547 0.3555 0.0127  0.0005  -0.0208 1018 THR B C   
16165 O O   . THR B 1020 ? 0.3151 0.3677 0.3699 0.0124  0.0004  -0.0191 1018 THR B O   
16166 C CB  . THR B 1020 ? 0.3001 0.3648 0.3618 0.0100  0.0026  -0.0196 1018 THR B CB  
16167 O OG1 . THR B 1020 ? 0.2841 0.3511 0.3439 0.0118  0.0036  -0.0208 1018 THR B OG1 
16168 C CG2 . THR B 1020 ? 0.3018 0.3716 0.3681 0.0084  0.0028  -0.0196 1018 THR B CG2 
16169 N N   . GLY B 1021 ? 0.2505 0.3064 0.3050 0.0143  0.0005  -0.0222 1019 GLY B N   
16170 C CA  . GLY B 1021 ? 0.2774 0.3323 0.3286 0.0155  0.0009  -0.0216 1019 GLY B CA  
16171 C C   . GLY B 1021 ? 0.2725 0.3308 0.3234 0.0149  0.0026  -0.0201 1019 GLY B C   
16172 O O   . GLY B 1021 ? 0.2448 0.3062 0.2976 0.0137  0.0035  -0.0196 1019 GLY B O   
16173 N N   . PRO B 1022 ? 0.2390 0.2971 0.2872 0.0157  0.0030  -0.0192 1020 PRO B N   
16174 C CA  . PRO B 1022 ? 0.2236 0.2798 0.2696 0.0171  0.0022  -0.0196 1020 PRO B CA  
16175 C C   . PRO B 1022 ? 0.2073 0.2640 0.2525 0.0174  0.0016  -0.0214 1020 PRO B C   
16176 O O   . PRO B 1022 ? 0.2485 0.3068 0.2946 0.0170  0.0017  -0.0225 1020 PRO B O   
16177 C CB  . PRO B 1022 ? 0.2242 0.2821 0.2684 0.0174  0.0030  -0.0178 1020 PRO B CB  
16178 C CG  . PRO B 1022 ? 0.2588 0.3200 0.3034 0.0162  0.0041  -0.0174 1020 PRO B CG  
16179 C CD  . PRO B 1022 ? 0.2770 0.3382 0.3243 0.0151  0.0043  -0.0178 1020 PRO B CD  
16180 N N   . LYS B 1023 ? 0.2273 0.2826 0.2708 0.0182  0.0008  -0.0217 1021 LYS B N   
16181 C CA  . LYS B 1023 ? 0.2259 0.2808 0.2683 0.0182  -0.0001 -0.0231 1021 LYS B CA  
16182 C C   . LYS B 1023 ? 0.1938 0.2508 0.2347 0.0175  0.0002  -0.0231 1021 LYS B C   
16183 O O   . LYS B 1023 ? 0.1634 0.2225 0.2033 0.0173  0.0008  -0.0217 1021 LYS B O   
16184 C CB  . LYS B 1023 ? 0.2426 0.2963 0.2831 0.0190  -0.0007 -0.0230 1021 LYS B CB  
16185 C CG  . LYS B 1023 ? 0.2079 0.2586 0.2488 0.0199  -0.0014 -0.0237 1021 LYS B CG  
16186 C CD  . LYS B 1023 ? 0.2422 0.2927 0.2806 0.0210  -0.0016 -0.0234 1021 LYS B CD  
16187 C CE  . LYS B 1023 ? 0.2746 0.3217 0.3124 0.0219  -0.0026 -0.0246 1021 LYS B CE  
16188 N NZ  . LYS B 1023 ? 0.2250 0.2711 0.2624 0.0211  -0.0038 -0.0258 1021 LYS B NZ  
16189 N N   . ALA B 1024 ? 0.2487 0.3049 0.2894 0.0174  -0.0006 -0.0247 1022 ALA B N   
16190 C CA  . ALA B 1024 ? 0.2408 0.2975 0.2792 0.0168  -0.0010 -0.0251 1022 ALA B CA  
16191 C C   . ALA B 1024 ? 0.2494 0.3057 0.2854 0.0160  -0.0019 -0.0242 1022 ALA B C   
16192 O O   . ALA B 1024 ? 0.2031 0.2582 0.2388 0.0162  -0.0025 -0.0241 1022 ALA B O   
16193 C CB  . ALA B 1024 ? 0.2084 0.2633 0.2468 0.0173  -0.0021 -0.0273 1022 ALA B CB  
16194 N N   . GLY B 1025 ? 0.1852 0.2429 0.2191 0.0150  -0.0020 -0.0235 1023 GLY B N   
16195 C CA  . GLY B 1025 ? 0.1492 0.2075 0.1812 0.0138  -0.0028 -0.0223 1023 GLY B CA  
16196 C C   . GLY B 1025 ? 0.1673 0.2283 0.2004 0.0144  -0.0019 -0.0207 1023 GLY B C   
16197 O O   . GLY B 1025 ? 0.1821 0.2441 0.2142 0.0139  -0.0023 -0.0198 1023 GLY B O   
16198 N N   . GLY B 1026 ? 0.1816 0.2439 0.2165 0.0156  -0.0006 -0.0201 1024 GLY B N   
16199 C CA  . GLY B 1026 ? 0.1665 0.2309 0.2022 0.0169  0.0002  -0.0186 1024 GLY B CA  
16200 C C   . GLY B 1026 ? 0.2028 0.2697 0.2389 0.0172  0.0010  -0.0172 1024 GLY B C   
16201 O O   . GLY B 1026 ? 0.1777 0.2448 0.2135 0.0163  0.0012  -0.0174 1024 GLY B O   
16202 N N   . PRO B 1027 ? 0.2440 0.3129 0.2805 0.0186  0.0015  -0.0158 1025 PRO B N   
16203 C CA  . PRO B 1027 ? 0.1873 0.2592 0.2238 0.0190  0.0020  -0.0141 1025 PRO B CA  
16204 C C   . PRO B 1027 ? 0.2025 0.2724 0.2397 0.0196  0.0026  -0.0136 1025 PRO B C   
16205 O O   . PRO B 1027 ? 0.1902 0.2621 0.2271 0.0197  0.0028  -0.0121 1025 PRO B O   
16206 C CB  . PRO B 1027 ? 0.1975 0.2724 0.2342 0.0208  0.0021  -0.0129 1025 PRO B CB  
16207 C CG  . PRO B 1027 ? 0.2475 0.3189 0.2844 0.0223  0.0021  -0.0142 1025 PRO B CG  
16208 C CD  . PRO B 1027 ? 0.2357 0.3045 0.2723 0.0203  0.0016  -0.0158 1025 PRO B CD  
16209 N N   . LEU B 1028 ? 0.2042 0.2703 0.2424 0.0199  0.0027  -0.0147 1026 LEU B N   
16210 C CA  . LEU B 1028 ? 0.2273 0.2916 0.2662 0.0198  0.0032  -0.0139 1026 LEU B CA  
16211 C C   . LEU B 1028 ? 0.1971 0.2621 0.2363 0.0180  0.0037  -0.0146 1026 LEU B C   
16212 O O   . LEU B 1028 ? 0.2258 0.2906 0.2655 0.0175  0.0044  -0.0137 1026 LEU B O   
16213 C CB  . LEU B 1028 ? 0.1746 0.2347 0.2145 0.0207  0.0029  -0.0145 1026 LEU B CB  
16214 C CG  . LEU B 1028 ? 0.2785 0.3371 0.3176 0.0231  0.0025  -0.0140 1026 LEU B CG  
16215 C CD1 . LEU B 1028 ? 0.2526 0.3059 0.2921 0.0236  0.0018  -0.0148 1026 LEU B CD1 
16216 C CD2 . LEU B 1028 ? 0.3101 0.3699 0.3484 0.0242  0.0026  -0.0118 1026 LEU B CD2 
16217 N N   . TYR B 1029 ? 0.1723 0.2381 0.2109 0.0172  0.0034  -0.0162 1027 TYR B N   
16218 C CA  . TYR B 1029 ? 0.2140 0.2801 0.2528 0.0163  0.0038  -0.0175 1027 TYR B CA  
16219 C C   . TYR B 1029 ? 0.2148 0.2835 0.2526 0.0157  0.0047  -0.0164 1027 TYR B C   
16220 O O   . TYR B 1029 ? 0.2149 0.2843 0.2536 0.0153  0.0057  -0.0162 1027 TYR B O   
16221 C CB  . TYR B 1029 ? 0.2084 0.2739 0.2460 0.0159  0.0028  -0.0193 1027 TYR B CB  
16222 C CG  . TYR B 1029 ? 0.2121 0.2768 0.2503 0.0159  0.0028  -0.0214 1027 TYR B CG  
16223 C CD1 . TYR B 1029 ? 0.2071 0.2704 0.2479 0.0164  0.0028  -0.0223 1027 TYR B CD1 
16224 C CD2 . TYR B 1029 ? 0.2282 0.2934 0.2644 0.0157  0.0026  -0.0226 1027 TYR B CD2 
16225 C CE1 . TYR B 1029 ? 0.2216 0.2849 0.2632 0.0168  0.0026  -0.0241 1027 TYR B CE1 
16226 C CE2 . TYR B 1029 ? 0.1972 0.2618 0.2338 0.0164  0.0025  -0.0247 1027 TYR B CE2 
16227 C CZ  . TYR B 1029 ? 0.2720 0.3361 0.3116 0.0170  0.0026  -0.0254 1027 TYR B CZ  
16228 O OH  . TYR B 1029 ? 0.2687 0.3330 0.3091 0.0180  0.0024  -0.0275 1027 TYR B OH  
16229 N N   . LEU B 1030 ? 0.2046 0.2750 0.2402 0.0154  0.0043  -0.0155 1028 LEU B N   
16230 C CA  . LEU B 1030 ? 0.2398 0.3125 0.2735 0.0148  0.0049  -0.0147 1028 LEU B CA  
16231 C C   . LEU B 1030 ? 0.2399 0.3131 0.2744 0.0149  0.0059  -0.0125 1028 LEU B C   
16232 O O   . LEU B 1030 ? 0.2264 0.3012 0.2598 0.0143  0.0069  -0.0119 1028 LEU B O   
16233 C CB  . LEU B 1030 ? 0.2244 0.2989 0.2558 0.0143  0.0038  -0.0139 1028 LEU B CB  
16234 C CG  . LEU B 1030 ? 0.2228 0.2965 0.2526 0.0135  0.0025  -0.0157 1028 LEU B CG  
16235 C CD1 . LEU B 1030 ? 0.2219 0.2981 0.2496 0.0124  0.0013  -0.0146 1028 LEU B CD1 
16236 C CD2 . LEU B 1030 ? 0.2365 0.3088 0.2651 0.0134  0.0027  -0.0181 1028 LEU B CD2 
16237 N N   . GLY B 1031 ? 0.2511 0.3226 0.2869 0.0158  0.0056  -0.0112 1029 GLY B N   
16238 C CA  . GLY B 1031 ? 0.2331 0.3038 0.2690 0.0158  0.0061  -0.0089 1029 GLY B CA  
16239 C C   . GLY B 1031 ? 0.2536 0.3237 0.2909 0.0146  0.0071  -0.0089 1029 GLY B C   
16240 O O   . GLY B 1031 ? 0.2534 0.3236 0.2902 0.0138  0.0077  -0.0067 1029 GLY B O   
16241 N N   . ARG B 1032 ? 0.2266 0.2965 0.2657 0.0143  0.0073  -0.0110 1030 ARG B N   
16242 C CA  . ARG B 1032 ? 0.2444 0.3152 0.2855 0.0130  0.0083  -0.0110 1030 ARG B CA  
16243 C C   . ARG B 1032 ? 0.2517 0.3266 0.2915 0.0123  0.0097  -0.0112 1030 ARG B C   
16244 O O   . ARG B 1032 ? 0.2874 0.3645 0.3286 0.0111  0.0110  -0.0105 1030 ARG B O   
16245 C CB  . ARG B 1032 ? 0.2627 0.3321 0.3063 0.0133  0.0078  -0.0133 1030 ARG B CB  
16246 C CG  . ARG B 1032 ? 0.3050 0.3755 0.3514 0.0119  0.0085  -0.0131 1030 ARG B CG  
16247 C CD  . ARG B 1032 ? 0.3518 0.4188 0.3992 0.0109  0.0077  -0.0110 1030 ARG B CD  
16248 N NE  . ARG B 1032 ? 0.3597 0.4278 0.4103 0.0093  0.0079  -0.0110 1030 ARG B NE  
16249 C CZ  . ARG B 1032 ? 0.4038 0.4738 0.4555 0.0070  0.0088  -0.0088 1030 ARG B CZ  
16250 N NH1 . ARG B 1032 ? 0.4035 0.4736 0.4529 0.0062  0.0094  -0.0062 1030 ARG B NH1 
16251 N NH2 . ARG B 1032 ? 0.3645 0.4366 0.4197 0.0053  0.0089  -0.0090 1030 ARG B NH2 
16252 N N   . LEU B 1033 ? 0.2159 0.2921 0.2530 0.0130  0.0095  -0.0121 1031 LEU B N   
16253 C CA  . LEU B 1033 ? 0.2549 0.3346 0.2900 0.0128  0.0106  -0.0131 1031 LEU B CA  
16254 C C   . LEU B 1033 ? 0.2466 0.3280 0.2786 0.0123  0.0111  -0.0108 1031 LEU B C   
16255 O O   . LEU B 1033 ? 0.2337 0.3176 0.2629 0.0124  0.0116  -0.0117 1031 LEU B O   
16256 C CB  . LEU B 1033 ? 0.2206 0.2995 0.2540 0.0138  0.0095  -0.0159 1031 LEU B CB  
16257 C CG  . LEU B 1033 ? 0.2390 0.3160 0.2752 0.0145  0.0089  -0.0180 1031 LEU B CG  
16258 C CD1 . LEU B 1033 ? 0.2619 0.3369 0.2961 0.0152  0.0074  -0.0204 1031 LEU B CD1 
16259 C CD2 . LEU B 1033 ? 0.3041 0.3838 0.3428 0.0146  0.0104  -0.0189 1031 LEU B CD2 
16260 N N   . VAL B 1034 ? 0.2273 0.3072 0.2593 0.0119  0.0106  -0.0080 1032 VAL B N   
16261 C CA  . VAL B 1034 ? 0.2556 0.3368 0.2847 0.0114  0.0109  -0.0054 1032 VAL B CA  
16262 C C   . VAL B 1034 ? 0.2946 0.3745 0.3250 0.0103  0.0113  -0.0025 1032 VAL B C   
16263 O O   . VAL B 1034 ? 0.2547 0.3319 0.2879 0.0101  0.0110  -0.0025 1032 VAL B O   
16264 C CB  . VAL B 1034 ? 0.2459 0.3264 0.2732 0.0123  0.0092  -0.0047 1032 VAL B CB  
16265 C CG1 . VAL B 1034 ? 0.2761 0.3580 0.3013 0.0125  0.0085  -0.0071 1032 VAL B CG1 
16266 C CG2 . VAL B 1034 ? 0.2316 0.3089 0.2613 0.0134  0.0080  -0.0044 1032 VAL B CG2 
16267 N N   . THR B 1035 ? 0.2842 0.3654 0.3120 0.0094  0.0119  0.0002  1033 THR B N   
16268 C CA  . THR B 1035 ? 0.3107 0.3899 0.3390 0.0079  0.0121  0.0033  1033 THR B CA  
16269 C C   . THR B 1035 ? 0.3491 0.4233 0.3774 0.0090  0.0101  0.0051  1033 THR B C   
16270 O O   . THR B 1035 ? 0.4030 0.4733 0.4323 0.0082  0.0095  0.0069  1033 THR B O   
16271 C CB  . THR B 1035 ? 0.3347 0.4172 0.3601 0.0062  0.0134  0.0058  1033 THR B CB  
16272 O OG1 . THR B 1035 ? 0.3569 0.4410 0.3785 0.0073  0.0129  0.0058  1033 THR B OG1 
16273 C CG2 . THR B 1035 ? 0.3773 0.4648 0.4037 0.0050  0.0157  0.0046  1033 THR B CG2 
16274 N N   . THR B 1036 ? 0.3053 0.3794 0.3321 0.0110  0.0088  0.0047  1034 THR B N   
16275 C CA  . THR B 1036 ? 0.3553 0.4255 0.3822 0.0129  0.0070  0.0058  1034 THR B CA  
16276 C C   . THR B 1036 ? 0.3016 0.3725 0.3301 0.0147  0.0063  0.0031  1034 THR B C   
16277 O O   . THR B 1036 ? 0.2759 0.3504 0.3034 0.0151  0.0062  0.0021  1034 THR B O   
16278 C CB  . THR B 1036 ? 0.3096 0.3804 0.3334 0.0137  0.0061  0.0086  1034 THR B CB  
16279 O OG1 . THR B 1036 ? 0.4231 0.4938 0.4448 0.0116  0.0068  0.0113  1034 THR B OG1 
16280 C CG2 . THR B 1036 ? 0.3744 0.4411 0.3985 0.0162  0.0042  0.0098  1034 THR B CG2 
16281 N N   . ALA B 1037 ? 0.2763 0.3439 0.3070 0.0157  0.0058  0.0020  1035 ALA B N   
16282 C CA  . ALA B 1037 ? 0.2855 0.3540 0.3176 0.0171  0.0053  -0.0005 1035 ALA B CA  
16283 C C   . ALA B 1037 ? 0.3159 0.3856 0.3472 0.0194  0.0041  0.0004  1035 ALA B C   
16284 O O   . ALA B 1037 ? 0.2707 0.3381 0.3010 0.0209  0.0033  0.0025  1035 ALA B O   
16285 C CB  . ALA B 1037 ? 0.2630 0.3277 0.2973 0.0175  0.0051  -0.0020 1035 ALA B CB  
16286 N N   . PRO B 1038 ? 0.2507 0.3241 0.2822 0.0197  0.0039  -0.0010 1036 PRO B N   
16287 C CA  . PRO B 1038 ? 0.2784 0.3542 0.3098 0.0217  0.0028  -0.0002 1036 PRO B CA  
16288 C C   . PRO B 1038 ? 0.2629 0.3368 0.2960 0.0240  0.0025  -0.0012 1036 PRO B C   
16289 O O   . PRO B 1038 ? 0.2312 0.3016 0.2653 0.0237  0.0029  -0.0027 1036 PRO B O   
16290 C CB  . PRO B 1038 ? 0.2519 0.3324 0.2829 0.0203  0.0027  -0.0013 1036 PRO B CB  
16291 C CG  . PRO B 1038 ? 0.2459 0.3248 0.2774 0.0186  0.0035  -0.0037 1036 PRO B CG  
16292 C CD  . PRO B 1038 ? 0.2765 0.3520 0.3080 0.0179  0.0044  -0.0033 1036 PRO B CD  
16293 N N   . VAL B 1039 ? 0.3134 0.3901 0.3468 0.0264  0.0017  -0.0003 1037 VAL B N   
16294 C CA  . VAL B 1039 ? 0.2607 0.3373 0.2953 0.0289  0.0015  -0.0014 1037 VAL B CA  
16295 C C   . VAL B 1039 ? 0.2296 0.3103 0.2652 0.0274  0.0018  -0.0030 1037 VAL B C   
16296 O O   . VAL B 1039 ? 0.2149 0.3011 0.2506 0.0265  0.0015  -0.0023 1037 VAL B O   
16297 C CB  . VAL B 1039 ? 0.2893 0.3681 0.3239 0.0325  0.0007  0.0002  1037 VAL B CB  
16298 C CG1 . VAL B 1039 ? 0.2678 0.3467 0.3033 0.0356  0.0008  -0.0011 1037 VAL B CG1 
16299 C CG2 . VAL B 1039 ? 0.2802 0.3538 0.3131 0.0337  0.0000  0.0021  1037 VAL B CG2 
16300 N N   . PRO B 1040 ? 0.2241 0.3022 0.2603 0.0269  0.0023  -0.0050 1038 PRO B N   
16301 C CA  . PRO B 1040 ? 0.2484 0.3297 0.2852 0.0253  0.0023  -0.0063 1038 PRO B CA  
16302 C C   . PRO B 1040 ? 0.2285 0.3155 0.2660 0.0269  0.0021  -0.0056 1038 PRO B C   
16303 O O   . PRO B 1040 ? 0.2591 0.3468 0.2970 0.0302  0.0021  -0.0048 1038 PRO B O   
16304 C CB  . PRO B 1040 ? 0.2078 0.2844 0.2448 0.0251  0.0026  -0.0084 1038 PRO B CB  
16305 C CG  . PRO B 1040 ? 0.2281 0.2995 0.2650 0.0255  0.0028  -0.0082 1038 PRO B CG  
16306 C CD  . PRO B 1040 ? 0.2369 0.3088 0.2732 0.0274  0.0024  -0.0061 1038 PRO B CD  
16307 N N   . PRO B 1041 ? 0.2429 0.3341 0.2807 0.0247  0.0018  -0.0058 1039 PRO B N   
16308 C CA  . PRO B 1041 ? 0.2243 0.3218 0.2632 0.0258  0.0018  -0.0050 1039 PRO B CA  
16309 C C   . PRO B 1041 ? 0.2449 0.3406 0.2841 0.0288  0.0025  -0.0062 1039 PRO B C   
16310 O O   . PRO B 1041 ? 0.2711 0.3613 0.3095 0.0282  0.0027  -0.0079 1039 PRO B O   
16311 C CB  . PRO B 1041 ? 0.2857 0.3858 0.3242 0.0220  0.0012  -0.0053 1039 PRO B CB  
16312 C CG  . PRO B 1041 ? 0.2467 0.3427 0.2836 0.0194  0.0007  -0.0059 1039 PRO B CG  
16313 C CD  . PRO B 1041 ? 0.2433 0.3332 0.2800 0.0211  0.0014  -0.0068 1039 PRO B CD  
16314 N N   . GLN B 1042 ? 0.2412 0.3415 0.2812 0.0321  0.0028  -0.0052 1040 GLN B N   
16315 C CA  . GLN B 1042 ? 0.2863 0.3861 0.3262 0.0354  0.0035  -0.0064 1040 GLN B CA  
16316 C C   . GLN B 1042 ? 0.2658 0.3566 0.3042 0.0376  0.0034  -0.0079 1040 GLN B C   
16317 O O   . GLN B 1042 ? 0.2485 0.3368 0.2860 0.0396  0.0037  -0.0094 1040 GLN B O   
16318 C CB  . GLN B 1042 ? 0.3153 0.4173 0.3550 0.0332  0.0039  -0.0072 1040 GLN B CB  
16319 C CG  . GLN B 1042 ? 0.2759 0.3874 0.3170 0.0312  0.0039  -0.0055 1040 GLN B CG  
16320 C CD  . GLN B 1042 ? 0.4190 0.5316 0.4593 0.0285  0.0041  -0.0060 1040 GLN B CD  
16321 O OE1 . GLN B 1042 ? 0.4481 0.5571 0.4875 0.0247  0.0033  -0.0065 1040 GLN B OE1 
16322 N NE2 . GLN B 1042 ? 0.4468 0.5644 0.4874 0.0308  0.0051  -0.0059 1040 GLN B NE2 
16323 N N   . HIS B 1043 ? 0.1979 0.2838 0.2358 0.0369  0.0029  -0.0074 1041 HIS B N   
16324 C CA  . HIS B 1043 ? 0.2361 0.3134 0.2728 0.0377  0.0025  -0.0085 1041 HIS B CA  
16325 C C   . HIS B 1043 ? 0.2674 0.3420 0.3031 0.0421  0.0019  -0.0079 1041 HIS B C   
16326 O O   . HIS B 1043 ? 0.2707 0.3436 0.3061 0.0422  0.0013  -0.0063 1041 HIS B O   
16327 C CB  . HIS B 1043 ? 0.2328 0.3067 0.2696 0.0342  0.0023  -0.0082 1041 HIS B CB  
16328 C CG  . HIS B 1043 ? 0.2261 0.2921 0.2621 0.0342  0.0019  -0.0089 1041 HIS B CG  
16329 N ND1 . HIS B 1043 ? 0.2495 0.3116 0.2855 0.0326  0.0019  -0.0107 1041 HIS B ND1 
16330 C CD2 . HIS B 1043 ? 0.2739 0.3350 0.3089 0.0353  0.0012  -0.0078 1041 HIS B CD2 
16331 C CE1 . HIS B 1043 ? 0.2862 0.3421 0.3218 0.0325  0.0013  -0.0107 1041 HIS B CE1 
16332 N NE2 . HIS B 1043 ? 0.2472 0.3019 0.2819 0.0340  0.0009  -0.0089 1041 HIS B NE2 
16333 N N   . SER B 1044 ? 0.2409 0.3147 0.2757 0.0458  0.0020  -0.0092 1042 SER B N   
16334 C CA  . SER B 1044 ? 0.2256 0.2958 0.2588 0.0506  0.0012  -0.0090 1042 SER B CA  
16335 C C   . SER B 1044 ? 0.2619 0.3292 0.2933 0.0539  0.0013  -0.0114 1042 SER B C   
16336 O O   . SER B 1044 ? 0.2435 0.3132 0.2751 0.0524  0.0022  -0.0127 1042 SER B O   
16337 C CB  . SER B 1044 ? 0.2273 0.3052 0.2617 0.0535  0.0013  -0.0072 1042 SER B CB  
16338 O OG  . SER B 1044 ? 0.2182 0.3043 0.2536 0.0553  0.0024  -0.0078 1042 SER B OG  
16339 N N   . SER B 1045 ? 0.2377 0.2994 0.2668 0.0584  0.0002  -0.0120 1043 SER B N   
16340 C CA  . SER B 1045 ? 0.2479 0.3063 0.2744 0.0623  0.0002  -0.0145 1043 SER B CA  
16341 C C   . SER B 1045 ? 0.2457 0.3017 0.2701 0.0687  -0.0008 -0.0146 1043 SER B C   
16342 O O   . SER B 1045 ? 0.2639 0.3150 0.2876 0.0693  -0.0022 -0.0131 1043 SER B O   
16343 C CB  . SER B 1045 ? 0.2694 0.3178 0.2940 0.0599  -0.0009 -0.0162 1043 SER B CB  
16344 O OG  . SER B 1045 ? 0.2704 0.3143 0.2918 0.0640  -0.0014 -0.0187 1043 SER B OG  
16345 N N   . VAL B 1046 ? 0.2146 0.2740 0.2376 0.0736  -0.0001 -0.0164 1044 VAL B N   
16346 C CA  . VAL B 1046 ? 0.2613 0.3179 0.2817 0.0806  -0.0011 -0.0171 1044 VAL B CA  
16347 C C   . VAL B 1046 ? 0.2728 0.3159 0.2883 0.0829  -0.0031 -0.0195 1044 VAL B C   
16348 O O   . VAL B 1046 ? 0.2872 0.3252 0.2997 0.0888  -0.0046 -0.0203 1044 VAL B O   
16349 C CB  . VAL B 1046 ? 0.2878 0.3555 0.3090 0.0857  0.0007  -0.0178 1044 VAL B CB  
16350 C CG1 . VAL B 1046 ? 0.3090 0.3900 0.3350 0.0834  0.0022  -0.0151 1044 VAL B CG1 
16351 C CG2 . VAL B 1046 ? 0.2518 0.3204 0.2714 0.0855  0.0019  -0.0203 1044 VAL B CG2 
16352 N N   . HIS B 1047 ? 0.2706 0.3075 0.2853 0.0785  -0.0035 -0.0207 1045 HIS B N   
16353 C CA  . HIS B 1047 ? 0.3046 0.3285 0.3148 0.0797  -0.0058 -0.0229 1045 HIS B CA  
16354 C C   . HIS B 1047 ? 0.2980 0.3119 0.3072 0.0775  -0.0082 -0.0211 1045 HIS B C   
16355 O O   . HIS B 1047 ? 0.3045 0.3204 0.3169 0.0723  -0.0078 -0.0186 1045 HIS B O   
16356 C CB  . HIS B 1047 ? 0.3009 0.3233 0.3110 0.0755  -0.0054 -0.0246 1045 HIS B CB  
16357 C CG  . HIS B 1047 ? 0.3764 0.3854 0.3829 0.0743  -0.0080 -0.0262 1045 HIS B CG  
16358 N ND1 . HIS B 1047 ? 0.3741 0.3750 0.3753 0.0792  -0.0097 -0.0291 1045 HIS B ND1 
16359 C CD2 . HIS B 1047 ? 0.3614 0.3642 0.3688 0.0686  -0.0094 -0.0254 1045 HIS B CD2 
16360 C CE1 . HIS B 1047 ? 0.3670 0.3568 0.3660 0.0761  -0.0122 -0.0298 1045 HIS B CE1 
16361 N NE2 . HIS B 1047 ? 0.3161 0.3074 0.3192 0.0697  -0.0120 -0.0275 1045 HIS B NE2 
16362 N N   . THR B 1048 ? 0.2543 0.2571 0.2588 0.0814  -0.0107 -0.0224 1046 THR B N   
16363 C CA  . THR B 1048 ? 0.2759 0.2674 0.2785 0.0791  -0.0135 -0.0208 1046 THR B CA  
16364 C C   . THR B 1048 ? 0.2817 0.2614 0.2806 0.0775  -0.0157 -0.0230 1046 THR B C   
16365 O O   . THR B 1048 ? 0.3134 0.2885 0.3082 0.0823  -0.0167 -0.0261 1046 THR B O   
16366 C CB  . THR B 1048 ? 0.3559 0.3428 0.3556 0.0848  -0.0153 -0.0199 1046 THR B CB  
16367 O OG1 . THR B 1048 ? 0.3208 0.3199 0.3241 0.0869  -0.0132 -0.0181 1046 THR B OG1 
16368 C CG2 . THR B 1048 ? 0.3455 0.3214 0.3435 0.0813  -0.0181 -0.0174 1046 THR B CG2 
16369 N N   . ASP B 1049 ? 0.2783 0.2538 0.2788 0.0708  -0.0166 -0.0216 1047 ASP B N   
16370 C CA  . ASP B 1049 ? 0.2457 0.2109 0.2433 0.0685  -0.0190 -0.0234 1047 ASP B CA  
16371 C C   . ASP B 1049 ? 0.2793 0.2308 0.2706 0.0728  -0.0226 -0.0244 1047 ASP B C   
16372 O O   . ASP B 1049 ? 0.3068 0.2535 0.2970 0.0733  -0.0241 -0.0220 1047 ASP B O   
16373 C CB  . ASP B 1049 ? 0.2956 0.2597 0.2965 0.0606  -0.0193 -0.0212 1047 ASP B CB  
16374 C CG  . ASP B 1049 ? 0.3110 0.2653 0.3095 0.0577  -0.0219 -0.0229 1047 ASP B CG  
16375 O OD1 . ASP B 1049 ? 0.3158 0.2583 0.3103 0.0578  -0.0252 -0.0225 1047 ASP B OD1 
16376 O OD2 . ASP B 1049 ? 0.3479 0.3059 0.3480 0.0557  -0.0210 -0.0247 1047 ASP B OD2 
16377 N N   . PRO B 1050 ? 0.2986 0.2428 0.2852 0.0760  -0.0242 -0.0280 1048 PRO B N   
16378 C CA  . PRO B 1050 ? 0.3682 0.2989 0.3479 0.0811  -0.0279 -0.0293 1048 PRO B CA  
16379 C C   . PRO B 1050 ? 0.3501 0.2674 0.3276 0.0761  -0.0317 -0.0275 1048 PRO B C   
16380 O O   . PRO B 1050 ? 0.3828 0.2894 0.3556 0.0791  -0.0347 -0.0269 1048 PRO B O   
16381 C CB  . PRO B 1050 ? 0.3750 0.3029 0.3502 0.0857  -0.0283 -0.0339 1048 PRO B CB  
16382 C CG  . PRO B 1050 ? 0.3432 0.2786 0.3225 0.0802  -0.0262 -0.0345 1048 PRO B CG  
16383 C CD  . PRO B 1050 ? 0.3212 0.2698 0.3077 0.0764  -0.0228 -0.0311 1048 PRO B CD  
16384 N N   . VAL B 1051 ? 0.3574 0.2749 0.3381 0.0685  -0.0318 -0.0265 1049 VAL B N   
16385 C CA  . VAL B 1051 ? 0.3640 0.2705 0.3433 0.0628  -0.0352 -0.0242 1049 VAL B CA  
16386 C C   . VAL B 1051 ? 0.3349 0.2441 0.3170 0.0603  -0.0346 -0.0196 1049 VAL B C   
16387 O O   . VAL B 1051 ? 0.3863 0.2845 0.3649 0.0592  -0.0378 -0.0175 1049 VAL B O   
16388 C CB  . VAL B 1051 ? 0.3829 0.2905 0.3654 0.0557  -0.0354 -0.0244 1049 VAL B CB  
16389 C CG1 . VAL B 1051 ? 0.3808 0.2778 0.3622 0.0496  -0.0390 -0.0218 1049 VAL B CG1 
16390 C CG2 . VAL B 1051 ? 0.3474 0.2521 0.3266 0.0585  -0.0362 -0.0289 1049 VAL B CG2 
16391 N N   . LEU B 1052 ? 0.3115 0.2348 0.2993 0.0594  -0.0306 -0.0180 1050 LEU B N   
16392 C CA  . LEU B 1052 ? 0.2998 0.2263 0.2894 0.0585  -0.0299 -0.0140 1050 LEU B CA  
16393 C C   . LEU B 1052 ? 0.3629 0.2815 0.3472 0.0652  -0.0322 -0.0139 1050 LEU B C   
16394 O O   . LEU B 1052 ? 0.3236 0.2348 0.3057 0.0638  -0.0345 -0.0108 1050 LEU B O   
16395 C CB  . LEU B 1052 ? 0.3136 0.2563 0.3092 0.0580  -0.0255 -0.0132 1050 LEU B CB  
16396 C CG  . LEU B 1052 ? 0.2974 0.2465 0.2955 0.0569  -0.0241 -0.0093 1050 LEU B CG  
16397 C CD1 . LEU B 1052 ? 0.2887 0.2378 0.2842 0.0641  -0.0246 -0.0092 1050 LEU B CD1 
16398 C CD2 . LEU B 1052 ? 0.2816 0.2246 0.2795 0.0506  -0.0258 -0.0056 1050 LEU B CD2 
16399 N N   . LEU B 1053 ? 0.3628 0.2833 0.3448 0.0728  -0.0316 -0.0172 1051 LEU B N   
16400 C CA  . LEU B 1053 ? 0.3966 0.3103 0.3737 0.0802  -0.0338 -0.0175 1051 LEU B CA  
16401 C C   . LEU B 1053 ? 0.3943 0.2893 0.3644 0.0802  -0.0389 -0.0177 1051 LEU B C   
16402 O O   . LEU B 1053 ? 0.4125 0.2994 0.3791 0.0826  -0.0415 -0.0157 1051 LEU B O   
16403 C CB  . LEU B 1053 ? 0.4066 0.3265 0.3826 0.0884  -0.0320 -0.0214 1051 LEU B CB  
16404 C CG  . LEU B 1053 ? 0.4097 0.3476 0.3917 0.0898  -0.0276 -0.0206 1051 LEU B CG  
16405 C CD1 . LEU B 1053 ? 0.4373 0.3819 0.4184 0.0967  -0.0257 -0.0245 1051 LEU B CD1 
16406 C CD2 . LEU B 1053 ? 0.3987 0.3399 0.3819 0.0918  -0.0276 -0.0173 1051 LEU B CD2 
16407 N N   . ASP B 1054 ? 0.4363 0.3239 0.4043 0.0774  -0.0406 -0.0201 1052 ASP B N   
16408 C CA  . ASP B 1054 ? 0.4796 0.3488 0.4408 0.0765  -0.0459 -0.0203 1052 ASP B CA  
16409 C C   . ASP B 1054 ? 0.4412 0.3055 0.4036 0.0689  -0.0476 -0.0152 1052 ASP B C   
16410 O O   . ASP B 1054 ? 0.4678 0.3182 0.4246 0.0696  -0.0518 -0.0136 1052 ASP B O   
16411 C CB  . ASP B 1054 ? 0.4271 0.2906 0.3862 0.0744  -0.0474 -0.0238 1052 ASP B CB  
16412 C CG  . ASP B 1054 ? 0.4823 0.3460 0.4374 0.0828  -0.0469 -0.0290 1052 ASP B CG  
16413 O OD1 . ASP B 1054 ? 0.4287 0.2949 0.3820 0.0906  -0.0460 -0.0299 1052 ASP B OD1 
16414 O OD2 . ASP B 1054 ? 0.5070 0.3689 0.4608 0.0816  -0.0473 -0.0322 1052 ASP B OD2 
16415 N N   . PHE B 1055 ? 0.3917 0.2673 0.3610 0.0618  -0.0445 -0.0126 1053 PHE B N   
16416 C CA  . PHE B 1055 ? 0.4038 0.2772 0.3748 0.0544  -0.0455 -0.0076 1053 PHE B CA  
16417 C C   . PHE B 1055 ? 0.4170 0.2903 0.3866 0.0574  -0.0457 -0.0043 1053 PHE B C   
16418 O O   . PHE B 1055 ? 0.3922 0.2551 0.3584 0.0544  -0.0489 -0.0008 1053 PHE B O   
16419 C CB  . PHE B 1055 ? 0.3457 0.2331 0.3244 0.0475  -0.0416 -0.0061 1053 PHE B CB  
16420 C CG  . PHE B 1055 ? 0.3688 0.2559 0.3497 0.0395  -0.0420 -0.0011 1053 PHE B CG  
16421 C CD1 . PHE B 1055 ? 0.4057 0.2799 0.3832 0.0345  -0.0461 0.0008  1053 PHE B CD1 
16422 C CD2 . PHE B 1055 ? 0.3696 0.2699 0.3560 0.0367  -0.0382 0.0017  1053 PHE B CD2 
16423 C CE1 . PHE B 1055 ? 0.4403 0.3155 0.4200 0.0268  -0.0462 0.0057  1053 PHE B CE1 
16424 C CE2 . PHE B 1055 ? 0.3482 0.2492 0.3365 0.0295  -0.0382 0.0062  1053 PHE B CE2 
16425 C CZ  . PHE B 1055 ? 0.3651 0.2539 0.3501 0.0245  -0.0421 0.0083  1053 PHE B CZ  
16426 N N   . ALA B 1056 ? 0.3972 0.2816 0.3692 0.0632  -0.0425 -0.0052 1054 ALA B N   
16427 C CA  . ALA B 1056 ? 0.4078 0.2928 0.3787 0.0666  -0.0429 -0.0022 1054 ALA B CA  
16428 C C   . ALA B 1056 ? 0.4421 0.3109 0.4050 0.0725  -0.0476 -0.0027 1054 ALA B C   
16429 O O   . ALA B 1056 ? 0.4755 0.3379 0.4357 0.0722  -0.0499 0.0010  1054 ALA B O   
16430 C CB  . ALA B 1056 ? 0.3986 0.2993 0.3739 0.0716  -0.0388 -0.0033 1054 ALA B CB  
16431 N N   . LYS B 1057 ? 0.4294 0.2914 0.3881 0.0784  -0.0493 -0.0073 1055 LYS B N   
16432 C CA  . LYS B 1057 ? 0.4966 0.3419 0.4470 0.0844  -0.0542 -0.0082 1055 LYS B CA  
16433 C C   . LYS B 1057 ? 0.5306 0.3593 0.4764 0.0778  -0.0590 -0.0055 1055 LYS B C   
16434 O O   . LYS B 1057 ? 0.5115 0.3279 0.4517 0.0795  -0.0629 -0.0031 1055 LYS B O   
16435 C CB  . LYS B 1057 ? 0.5272 0.3689 0.4736 0.0922  -0.0548 -0.0141 1055 LYS B CB  
16436 C CG  . LYS B 1057 ? 0.5151 0.3693 0.4636 0.1012  -0.0516 -0.0164 1055 LYS B CG  
16437 C CD  . LYS B 1057 ? 0.5163 0.3666 0.4602 0.1086  -0.0522 -0.0222 1055 LYS B CD  
16438 C CE  . LYS B 1057 ? 0.5049 0.3573 0.4507 0.1031  -0.0509 -0.0246 1055 LYS B CE  
16439 N NZ  . LYS B 1057 ? 0.5418 0.3935 0.4837 0.1105  -0.0506 -0.0302 1055 LYS B NZ  
16440 N N   . TRP B 1058 ? 0.5096 0.3376 0.4574 0.0702  -0.0589 -0.0058 1056 TRP B N   
16441 C CA  . TRP B 1058 ? 0.5273 0.3418 0.4719 0.0624  -0.0631 -0.0027 1056 TRP B CA  
16442 C C   . TRP B 1058 ? 0.5408 0.3573 0.4873 0.0572  -0.0629 0.0035  1056 TRP B C   
16443 O O   . TRP B 1058 ? 0.5347 0.3368 0.4756 0.0553  -0.0674 0.0066  1056 TRP B O   
16444 C CB  . TRP B 1058 ? 0.5493 0.3674 0.4978 0.0550  -0.0621 -0.0039 1056 TRP B CB  
16445 C CG  . TRP B 1058 ? 0.5837 0.3903 0.5302 0.0459  -0.0660 -0.0006 1056 TRP B CG  
16446 C CD1 . TRP B 1058 ? 0.5785 0.3666 0.5176 0.0452  -0.0718 -0.0017 1056 TRP B CD1 
16447 C CD2 . TRP B 1058 ? 0.5372 0.3506 0.4891 0.0362  -0.0645 0.0044  1056 TRP B CD2 
16448 N NE1 . TRP B 1058 ? 0.6026 0.3857 0.5425 0.0351  -0.0741 0.0025  1056 TRP B NE1 
16449 C CE2 . TRP B 1058 ? 0.5997 0.3987 0.5476 0.0295  -0.0695 0.0064  1056 TRP B CE2 
16450 C CE3 . TRP B 1058 ? 0.5350 0.3651 0.4944 0.0324  -0.0596 0.0073  1056 TRP B CE3 
16451 C CZ2 . TRP B 1058 ? 0.5376 0.3397 0.4894 0.0193  -0.0694 0.0114  1056 TRP B CZ2 
16452 C CZ3 . TRP B 1058 ? 0.5744 0.4071 0.5372 0.0227  -0.0594 0.0120  1056 TRP B CZ3 
16453 C CH2 . TRP B 1058 ? 0.4984 0.3177 0.4576 0.0163  -0.0641 0.0140  1056 TRP B CH2 
16454 N N   . LEU B 1059 ? 0.4895 0.3235 0.4433 0.0550  -0.0578 0.0053  1057 LEU B N   
16455 C CA  . LEU B 1059 ? 0.5080 0.3451 0.4634 0.0504  -0.0572 0.0111  1057 LEU B CA  
16456 C C   . LEU B 1059 ? 0.5711 0.4000 0.5209 0.0569  -0.0600 0.0128  1057 LEU B C   
16457 O O   . LEU B 1059 ? 0.5418 0.3628 0.4885 0.0532  -0.0626 0.0176  1057 LEU B O   
16458 C CB  . LEU B 1059 ? 0.4774 0.3345 0.4411 0.0481  -0.0514 0.0120  1057 LEU B CB  
16459 C CG  . LEU B 1059 ? 0.4686 0.3343 0.4382 0.0403  -0.0487 0.0117  1057 LEU B CG  
16460 C CD1 . LEU B 1059 ? 0.3949 0.2793 0.3716 0.0398  -0.0432 0.0118  1057 LEU B CD1 
16461 C CD2 . LEU B 1059 ? 0.4389 0.2980 0.4077 0.0311  -0.0509 0.0163  1057 LEU B CD2 
16462 N N   . ASP B 1060 ? 0.5094 0.3409 0.4581 0.0667  -0.0594 0.0091  1058 ASP B N   
16463 C CA  . ASP B 1060 ? 0.5748 0.3987 0.5182 0.0738  -0.0623 0.0104  1058 ASP B CA  
16464 C C   . ASP B 1060 ? 0.5622 0.3636 0.4964 0.0752  -0.0687 0.0103  1058 ASP B C   
16465 O O   . ASP B 1060 ? 0.6308 0.4222 0.5599 0.0770  -0.0722 0.0136  1058 ASP B O   
16466 C CB  . ASP B 1060 ? 0.5880 0.4213 0.5328 0.0842  -0.0599 0.0064  1058 ASP B CB  
16467 C CG  . ASP B 1060 ? 0.5900 0.4413 0.5413 0.0845  -0.0555 0.0086  1058 ASP B CG  
16468 O OD1 . ASP B 1060 ? 0.6626 0.5137 0.6138 0.0811  -0.0562 0.0135  1058 ASP B OD1 
16469 O OD2 . ASP B 1060 ? 0.5728 0.4382 0.5290 0.0880  -0.0516 0.0055  1058 ASP B OD2 
16470 N N   . GLY B 1061 ? 0.5935 0.3862 0.5249 0.0745  -0.0707 0.0066  1059 GLY B N   
16471 C CA  . GLY B 1061 ? 0.5872 0.3576 0.5096 0.0744  -0.0772 0.0067  1059 GLY B CA  
16472 C C   . GLY B 1061 ? 0.6686 0.4309 0.5897 0.0641  -0.0799 0.0129  1059 GLY B C   
16473 O O   . GLY B 1061 ? 0.7419 0.4859 0.6551 0.0642  -0.0856 0.0150  1059 GLY B O   
16474 N N   . LYS B 1062 ? 0.6576 0.4334 0.5862 0.0552  -0.0759 0.0159  1060 LYS B N   
16475 C CA  . LYS B 1062 ? 0.6731 0.4444 0.6015 0.0451  -0.0776 0.0221  1060 LYS B CA  
16476 C C   . LYS B 1062 ? 0.6762 0.4506 0.6042 0.0457  -0.0771 0.0272  1060 LYS B C   
16477 O O   . LYS B 1062 ? 0.7434 0.5111 0.6691 0.0384  -0.0794 0.0328  1060 LYS B O   
16478 C CB  . LYS B 1062 ? 0.6729 0.4585 0.6095 0.0359  -0.0733 0.0232  1060 LYS B CB  
16479 C CG  . LYS B 1062 ? 0.6648 0.4458 0.6016 0.0320  -0.0748 0.0200  1060 LYS B CG  
16480 C CD  . LYS B 1062 ? 0.6600 0.4571 0.6056 0.0236  -0.0701 0.0215  1060 LYS B CD  
16481 C CE  . LYS B 1062 ? 0.6435 0.4437 0.5909 0.0153  -0.0697 0.0283  1060 LYS B CE  
16482 N NZ  . LYS B 1062 ? 0.6601 0.4470 0.6040 0.0068  -0.0743 0.0316  1060 LYS B NZ  
16483 N N   . GLY B 1063 ? 0.6752 0.4600 0.6054 0.0537  -0.0742 0.0256  1061 GLY B N   
16484 C CA  . GLY B 1063 ? 0.5968 0.3881 0.5280 0.0535  -0.0729 0.0303  1061 GLY B CA  
16485 C C   . GLY B 1063 ? 0.6467 0.4563 0.5861 0.0462  -0.0674 0.0330  1061 GLY B C   
16486 O O   . GLY B 1063 ? 0.6807 0.4941 0.6203 0.0433  -0.0668 0.0379  1061 GLY B O   
16487 N N   . ALA B 1064 ? 0.5852 0.4059 0.5308 0.0432  -0.0636 0.0298  1062 ALA B N   
16488 C CA  . ALA B 1064 ? 0.5478 0.3867 0.5012 0.0376  -0.0581 0.0315  1062 ALA B CA  
16489 C C   . ALA B 1064 ? 0.5871 0.4404 0.5445 0.0448  -0.0543 0.0290  1062 ALA B C   
16490 O O   . ALA B 1064 ? 0.5317 0.3966 0.4944 0.0462  -0.0506 0.0252  1062 ALA B O   
16491 C CB  . ALA B 1064 ? 0.5387 0.3827 0.4968 0.0314  -0.0561 0.0295  1062 ALA B CB  
16492 N N   . ARG B 1065 ? 0.5974 0.4494 0.5519 0.0491  -0.0555 0.0316  1063 ARG B N   
16493 C CA  . ARG B 1065 ? 0.4829 0.3464 0.4402 0.0569  -0.0529 0.0293  1063 ARG B CA  
16494 C C   . ARG B 1065 ? 0.5192 0.4018 0.4841 0.0533  -0.0474 0.0295  1063 ARG B C   
16495 O O   . ARG B 1065 ? 0.5302 0.4240 0.4995 0.0574  -0.0443 0.0257  1063 ARG B O   
16496 C CB  . ARG B 1065 ? 0.5914 0.4492 0.5440 0.0618  -0.0559 0.0326  1063 ARG B CB  
16497 N N   . ALA B 1066 ? 0.5084 0.3949 0.4747 0.0455  -0.0461 0.0338  1064 ALA B N   
16498 C CA  . ALA B 1066 ? 0.4968 0.4005 0.4697 0.0420  -0.0410 0.0338  1064 ALA B CA  
16499 C C   . ALA B 1066 ? 0.5072 0.4175 0.4851 0.0403  -0.0382 0.0295  1064 ALA B C   
16500 O O   . ALA B 1066 ? 0.4780 0.4016 0.4609 0.0420  -0.0346 0.0270  1064 ALA B O   
16501 C CB  . ALA B 1066 ? 0.4793 0.3850 0.4522 0.0338  -0.0403 0.0390  1064 ALA B CB  
16502 N N   . GLU B 1067 ? 0.4632 0.3639 0.4395 0.0369  -0.0402 0.0286  1065 GLU B N   
16503 C CA  . GLU B 1067 ? 0.4697 0.3761 0.4505 0.0349  -0.0380 0.0248  1065 GLU B CA  
16504 C C   . GLU B 1067 ? 0.4412 0.3475 0.4218 0.0427  -0.0380 0.0195  1065 GLU B C   
16505 O O   . GLU B 1067 ? 0.4356 0.3526 0.4209 0.0433  -0.0347 0.0163  1065 GLU B O   
16506 C CB  . GLU B 1067 ? 0.4885 0.3853 0.4679 0.0283  -0.0403 0.0259  1065 GLU B CB  
16507 C CG  . GLU B 1067 ? 0.4048 0.3055 0.3860 0.0196  -0.0391 0.0306  1065 GLU B CG  
16508 C CD  . GLU B 1067 ? 0.5213 0.4125 0.4970 0.0179  -0.0422 0.0359  1065 GLU B CD  
16509 O OE1 . GLU B 1067 ? 0.5325 0.4126 0.5027 0.0236  -0.0457 0.0358  1065 GLU B OE1 
16510 O OE2 . GLU B 1067 ? 0.5548 0.4497 0.5315 0.0111  -0.0411 0.0402  1065 GLU B OE2 
16511 N N   . ALA B 1068 ? 0.4497 0.3440 0.4246 0.0488  -0.0418 0.0186  1066 ALA B N   
16512 C CA  . ALA B 1068 ? 0.4935 0.3889 0.4678 0.0571  -0.0416 0.0138  1066 ALA B CA  
16513 C C   . ALA B 1068 ? 0.4567 0.3682 0.4359 0.0609  -0.0377 0.0130  1066 ALA B C   
16514 O O   . ALA B 1068 ? 0.4328 0.3527 0.4152 0.0635  -0.0351 0.0092  1066 ALA B O   
16515 C CB  . ALA B 1068 ? 0.4410 0.3215 0.4081 0.0637  -0.0462 0.0134  1066 ALA B CB  
16516 N N   . GLU B 1069 ? 0.4625 0.3783 0.4419 0.0608  -0.0373 0.0166  1067 GLU B N   
16517 C CA  . GLU B 1069 ? 0.4697 0.4009 0.4537 0.0635  -0.0339 0.0163  1067 GLU B CA  
16518 C C   . GLU B 1069 ? 0.4684 0.4121 0.4584 0.0578  -0.0298 0.0153  1067 GLU B C   
16519 O O   . GLU B 1069 ? 0.4098 0.3645 0.4037 0.0604  -0.0270 0.0126  1067 GLU B O   
16520 C CB  . GLU B 1069 ? 0.4852 0.4177 0.4678 0.0637  -0.0348 0.0207  1067 GLU B CB  
16521 C CG  . GLU B 1069 ? 0.4985 0.4470 0.4859 0.0653  -0.0316 0.0208  1067 GLU B CG  
16522 C CD  . GLU B 1069 ? 0.5634 0.5163 0.5512 0.0742  -0.0318 0.0181  1067 GLU B CD  
16523 O OE1 . GLU B 1069 ? 0.6480 0.5951 0.6340 0.0789  -0.0329 0.0147  1067 GLU B OE1 
16524 O OE2 . GLU B 1069 ? 0.6742 0.6368 0.6641 0.0766  -0.0309 0.0195  1067 GLU B OE2 
16525 N N   . ALA B 1070 ? 0.4253 0.3677 0.4162 0.0501  -0.0293 0.0176  1068 ALA B N   
16526 C CA  . ALA B 1070 ? 0.4594 0.4125 0.4556 0.0451  -0.0257 0.0165  1068 ALA B CA  
16527 C C   . ALA B 1070 ? 0.3341 0.2881 0.3322 0.0467  -0.0248 0.0119  1068 ALA B C   
16528 O O   . ALA B 1070 ? 0.3480 0.3131 0.3505 0.0465  -0.0217 0.0098  1068 ALA B O   
16529 C CB  . ALA B 1070 ? 0.4206 0.3714 0.4172 0.0370  -0.0256 0.0197  1068 ALA B CB  
16530 N N   . ALA B 1071 ? 0.3654 0.3075 0.3598 0.0484  -0.0278 0.0103  1069 ALA B N   
16531 C CA  . ALA B 1071 ? 0.3446 0.2868 0.3400 0.0499  -0.0272 0.0059  1069 ALA B CA  
16532 C C   . ALA B 1071 ? 0.3777 0.3277 0.3742 0.0569  -0.0255 0.0029  1069 ALA B C   
16533 O O   . ALA B 1071 ? 0.3220 0.2805 0.3221 0.0565  -0.0229 0.0003  1069 ALA B O   
16534 C CB  . ALA B 1071 ? 0.3185 0.2453 0.3088 0.0504  -0.0312 0.0048  1069 ALA B CB  
16535 N N   . ARG B 1072 ? 0.3580 0.3055 0.3516 0.0632  -0.0270 0.0033  1070 ARG B N   
16536 C CA  A ARG B 1072 ? 0.3810 0.3373 0.3760 0.0699  -0.0253 0.0008  1070 ARG B CA  
16537 C CA  B ARG B 1072 ? 0.3809 0.3373 0.3760 0.0698  -0.0253 0.0008  1070 ARG B CA  
16538 C C   . ARG B 1072 ? 0.3855 0.3575 0.3863 0.0674  -0.0216 0.0015  1070 ARG B C   
16539 O O   . ARG B 1072 ? 0.3634 0.3443 0.3671 0.0693  -0.0193 -0.0011 1070 ARG B O   
16540 C CB  A ARG B 1072 ? 0.4065 0.3585 0.3979 0.0769  -0.0277 0.0018  1070 ARG B CB  
16541 C CB  B ARG B 1072 ? 0.4072 0.3587 0.3984 0.0770  -0.0277 0.0015  1070 ARG B CB  
16542 C CG  A ARG B 1072 ? 0.4429 0.3796 0.4279 0.0815  -0.0315 0.0001  1070 ARG B CG  
16543 C CG  B ARG B 1072 ? 0.4424 0.3775 0.4272 0.0804  -0.0317 0.0000  1070 ARG B CG  
16544 C CD  A ARG B 1072 ? 0.4412 0.3749 0.4229 0.0893  -0.0337 0.0008  1070 ARG B CD  
16545 C CD  B ARG B 1072 ? 0.4551 0.3861 0.4360 0.0894  -0.0339 -0.0006 1070 ARG B CD  
16546 N NE  A ARG B 1072 ? 0.4885 0.4178 0.4687 0.0867  -0.0356 0.0055  1070 ARG B NE  
16547 N NE  B ARG B 1072 ? 0.4693 0.3856 0.4440 0.0933  -0.0373 -0.0034 1070 ARG B NE  
16548 C CZ  A ARG B 1072 ? 0.4930 0.4067 0.4673 0.0862  -0.0397 0.0074  1070 ARG B CZ  
16549 C CZ  B ARG B 1072 ? 0.4736 0.3738 0.4425 0.0923  -0.0416 -0.0018 1070 ARG B CZ  
16550 N NH1 A ARG B 1072 ? 0.5073 0.4075 0.4766 0.0883  -0.0426 0.0048  1070 ARG B NH1 
16551 N NH1 B ARG B 1072 ? 0.5023 0.3991 0.4708 0.0876  -0.0429 0.0029  1070 ARG B NH1 
16552 N NH2 A ARG B 1072 ? 0.4549 0.3661 0.4280 0.0835  -0.0411 0.0120  1070 ARG B NH2 
16553 N NH2 B ARG B 1072 ? 0.4864 0.3732 0.4495 0.0958  -0.0447 -0.0049 1070 ARG B NH2 
16554 N N   . ASN B 1073 ? 0.3558 0.3310 0.3581 0.0631  -0.0211 0.0051  1071 ASN B N   
16555 C CA  . ASN B 1073 ? 0.3599 0.3488 0.3669 0.0604  -0.0179 0.0058  1071 ASN B CA  
16556 C C   . ASN B 1073 ? 0.3556 0.3491 0.3659 0.0557  -0.0156 0.0038  1071 ASN B C   
16557 O O   . ASN B 1073 ? 0.3479 0.3519 0.3618 0.0557  -0.0131 0.0024  1071 ASN B O   
16558 C CB  . ASN B 1073 ? 0.3608 0.3509 0.3676 0.0569  -0.0181 0.0099  1071 ASN B CB  
16559 C CG  . ASN B 1073 ? 0.4213 0.4101 0.4256 0.0622  -0.0200 0.0119  1071 ASN B CG  
16560 O OD1 . ASN B 1073 ? 0.5085 0.4978 0.5121 0.0687  -0.0207 0.0100  1071 ASN B OD1 
16561 N ND2 . ASN B 1073 ? 0.4511 0.4384 0.4539 0.0596  -0.0209 0.0157  1071 ASN B ND2 
16562 N N   . ALA B 1074 ? 0.3293 0.3151 0.3387 0.0514  -0.0165 0.0037  1072 ALA B N   
16563 C CA  . ALA B 1074 ? 0.3002 0.2898 0.3127 0.0476  -0.0147 0.0015  1072 ALA B CA  
16564 C C   . ALA B 1074 ? 0.3054 0.2967 0.3179 0.0520  -0.0142 -0.0023 1072 ALA B C   
16565 O O   . ALA B 1074 ? 0.2894 0.2890 0.3051 0.0508  -0.0119 -0.0040 1072 ALA B O   
16566 C CB  . ALA B 1074 ? 0.2800 0.2608 0.2913 0.0427  -0.0163 0.0022  1072 ALA B CB  
16567 N N   . GLY B 1075 ? 0.2625 0.2456 0.2711 0.0570  -0.0165 -0.0037 1073 GLY B N   
16568 C CA  . GLY B 1075 ? 0.3524 0.3370 0.3604 0.0616  -0.0159 -0.0074 1073 GLY B CA  
16569 C C   . GLY B 1075 ? 0.3426 0.3401 0.3536 0.0645  -0.0133 -0.0080 1073 GLY B C   
16570 O O   . GLY B 1075 ? 0.3354 0.3384 0.3479 0.0652  -0.0117 -0.0105 1073 GLY B O   
16571 N N   . SER B 1076 ? 0.2930 0.2958 0.3051 0.0659  -0.0130 -0.0055 1074 SER B N   
16572 C CA  . SER B 1076 ? 0.3278 0.3432 0.3429 0.0683  -0.0109 -0.0056 1074 SER B CA  
16573 C C   . SER B 1076 ? 0.3223 0.3468 0.3416 0.0625  -0.0085 -0.0050 1074 SER B C   
16574 O O   . SER B 1076 ? 0.3508 0.3839 0.3725 0.0628  -0.0066 -0.0064 1074 SER B O   
16575 C CB  . SER B 1076 ? 0.3520 0.3696 0.3666 0.0720  -0.0118 -0.0032 1074 SER B CB  
16576 O OG  . SER B 1076 ? 0.3838 0.3945 0.3946 0.0787  -0.0139 -0.0043 1074 SER B OG  
16577 N N   . SER B 1077 ? 0.2916 0.3143 0.3115 0.0573  -0.0086 -0.0029 1075 SER B N   
16578 C CA  . SER B 1077 ? 0.3344 0.3656 0.3577 0.0526  -0.0065 -0.0024 1075 SER B CA  
16579 C C   . SER B 1077 ? 0.2715 0.3025 0.2962 0.0494  -0.0054 -0.0047 1075 SER B C   
16580 O O   . SER B 1077 ? 0.3085 0.3467 0.3358 0.0467  -0.0037 -0.0051 1075 SER B O   
16581 C CB  . SER B 1077 ? 0.3721 0.4026 0.3954 0.0487  -0.0067 0.0006  1075 SER B CB  
16582 O OG  . SER B 1077 ? 0.4212 0.4426 0.4429 0.0459  -0.0079 0.0012  1075 SER B OG  
16583 N N   . SER B 1078 ? 0.2623 0.2846 0.2849 0.0498  -0.0067 -0.0062 1076 SER B N   
16584 C CA  . SER B 1078 ? 0.2593 0.2813 0.2831 0.0474  -0.0061 -0.0086 1076 SER B CA  
16585 C C   . SER B 1078 ? 0.2750 0.3051 0.3001 0.0493  -0.0044 -0.0104 1076 SER B C   
16586 O O   . SER B 1078 ? 0.2689 0.3017 0.2931 0.0540  -0.0043 -0.0109 1076 SER B O   
16587 C CB  . SER B 1078 ? 0.2192 0.2306 0.2398 0.0488  -0.0082 -0.0102 1076 SER B CB  
16588 O OG  . SER B 1078 ? 0.2385 0.2500 0.2599 0.0472  -0.0077 -0.0127 1076 SER B OG  
16589 N N   . ALA B 1079 ? 0.2387 0.2730 0.2661 0.0457  -0.0032 -0.0113 1077 ALA B N   
16590 C CA  . ALA B 1079 ? 0.2297 0.2708 0.2581 0.0467  -0.0018 -0.0128 1077 ALA B CA  
16591 C C   . ALA B 1079 ? 0.2652 0.3020 0.2923 0.0471  -0.0022 -0.0154 1077 ALA B C   
16592 O O   . ALA B 1079 ? 0.2301 0.2719 0.2579 0.0468  -0.0012 -0.0167 1077 ALA B O   
16593 C CB  . ALA B 1079 ? 0.2516 0.3001 0.2828 0.0428  -0.0004 -0.0120 1077 ALA B CB  
16594 N N   . LEU B 1080 ? 0.2710 0.2986 0.2959 0.0475  -0.0040 -0.0162 1078 LEU B N   
16595 C CA  . LEU B 1080 ? 0.2367 0.2596 0.2596 0.0484  -0.0048 -0.0189 1078 LEU B CA  
16596 C C   . LEU B 1080 ? 0.2297 0.2565 0.2508 0.0532  -0.0040 -0.0205 1078 LEU B C   
16597 O O   . LEU B 1080 ? 0.2518 0.2791 0.2714 0.0576  -0.0041 -0.0201 1078 LEU B O   
16598 C CB  . LEU B 1080 ? 0.2305 0.2424 0.2506 0.0489  -0.0073 -0.0192 1078 LEU B CB  
16599 C CG  . LEU B 1080 ? 0.2447 0.2504 0.2617 0.0506  -0.0086 -0.0222 1078 LEU B CG  
16600 C CD1 . LEU B 1080 ? 0.2279 0.2343 0.2469 0.0461  -0.0086 -0.0231 1078 LEU B CD1 
16601 C CD2 . LEU B 1080 ? 0.2225 0.2168 0.2358 0.0521  -0.0115 -0.0224 1078 LEU B CD2 
16602 N N   . GLY B 1081 ? 0.2228 0.2523 0.2439 0.0525  -0.0033 -0.0222 1079 GLY B N   
16603 C CA  . GLY B 1081 ? 0.2630 0.2973 0.2824 0.0565  -0.0022 -0.0236 1079 GLY B CA  
16604 C C   . GLY B 1081 ? 0.2723 0.3179 0.2944 0.0554  0.0000  -0.0222 1079 GLY B C   
16605 O O   . GLY B 1081 ? 0.2406 0.2917 0.2617 0.0581  0.0011  -0.0230 1079 GLY B O   
16606 N N   . LEU B 1082 ? 0.2556 0.3050 0.2809 0.0516  0.0005  -0.0201 1080 LEU B N   
16607 C CA  A LEU B 1082 ? 0.2508 0.3099 0.2785 0.0497  0.0020  -0.0189 1080 LEU B CA  
16608 C CA  B LEU B 1082 ? 0.2474 0.3065 0.2750 0.0497  0.0020  -0.0189 1080 LEU B CA  
16609 C C   . LEU B 1082 ? 0.2268 0.2878 0.2536 0.0485  0.0026  -0.0203 1080 LEU B C   
16610 O O   . LEU B 1082 ? 0.2357 0.2908 0.2614 0.0468  0.0017  -0.0217 1080 LEU B O   
16611 C CB  A LEU B 1082 ? 0.2315 0.2919 0.2618 0.0452  0.0020  -0.0171 1080 LEU B CB  
16612 C CB  B LEU B 1082 ? 0.2305 0.2908 0.2608 0.0452  0.0020  -0.0171 1080 LEU B CB  
16613 C CG  A LEU B 1082 ? 0.2454 0.3145 0.2777 0.0426  0.0031  -0.0157 1080 LEU B CG  
16614 C CG  B LEU B 1082 ? 0.2457 0.3143 0.2781 0.0423  0.0030  -0.0158 1080 LEU B CG  
16615 C CD1 A LEU B 1082 ? 0.2520 0.3288 0.2849 0.0457  0.0039  -0.0145 1080 LEU B CD1 
16616 C CD1 B LEU B 1082 ? 0.2249 0.2947 0.2590 0.0401  0.0028  -0.0139 1080 LEU B CD1 
16617 C CD2 A LEU B 1082 ? 0.2197 0.2888 0.2538 0.0388  0.0028  -0.0144 1080 LEU B CD2 
16618 C CD2 B LEU B 1082 ? 0.2048 0.2728 0.2372 0.0388  0.0030  -0.0168 1080 LEU B CD2 
16619 N N   . ASP B 1083 ? 0.2382 0.3078 0.2653 0.0493  0.0039  -0.0196 1081 ASP B N   
16620 C CA  . ASP B 1083 ? 0.2816 0.3535 0.3074 0.0484  0.0045  -0.0206 1081 ASP B CA  
16621 C C   . ASP B 1083 ? 0.2896 0.3718 0.3173 0.0463  0.0058  -0.0185 1081 ASP B C   
16622 O O   . ASP B 1083 ? 0.3254 0.4149 0.3533 0.0493  0.0070  -0.0178 1081 ASP B O   
16623 C CB  . ASP B 1083 ? 0.2905 0.3606 0.3128 0.0532  0.0047  -0.0226 1081 ASP B CB  
16624 C CG  . ASP B 1083 ? 0.3852 0.4569 0.4053 0.0523  0.0052  -0.0236 1081 ASP B CG  
16625 O OD1 . ASP B 1083 ? 0.4250 0.4971 0.4461 0.0478  0.0050  -0.0230 1081 ASP B OD1 
16626 O OD2 . ASP B 1083 ? 0.4611 0.5336 0.4782 0.0564  0.0058  -0.0251 1081 ASP B OD2 
16627 N N   . LEU B 1084 ? 0.2302 0.3128 0.2592 0.0414  0.0054  -0.0176 1082 LEU B N   
16628 C CA  . LEU B 1084 ? 0.2639 0.3550 0.2947 0.0385  0.0060  -0.0154 1082 LEU B CA  
16629 C C   . LEU B 1084 ? 0.2764 0.3681 0.3059 0.0351  0.0059  -0.0154 1082 LEU B C   
16630 O O   . LEU B 1084 ? 0.2606 0.3455 0.2888 0.0337  0.0049  -0.0169 1082 LEU B O   
16631 C CB  . LEU B 1084 ? 0.2687 0.3592 0.3017 0.0355  0.0053  -0.0141 1082 LEU B CB  
16632 C CG  . LEU B 1084 ? 0.3173 0.4078 0.3517 0.0380  0.0052  -0.0134 1082 LEU B CG  
16633 C CD1 . LEU B 1084 ? 0.2958 0.3853 0.3316 0.0344  0.0045  -0.0123 1082 LEU B CD1 
16634 C CD2 . LEU B 1084 ? 0.3745 0.4737 0.4099 0.0410  0.0062  -0.0121 1082 LEU B CD2 
16635 N N   . GLU B 1085 ? 0.2635 0.3637 0.2935 0.0336  0.0067  -0.0136 1083 GLU B N   
16636 C CA  . GLU B 1085 ? 0.2507 0.3515 0.2796 0.0292  0.0061  -0.0128 1083 GLU B CA  
16637 C C   . GLU B 1085 ? 0.3013 0.4034 0.3319 0.0248  0.0051  -0.0111 1083 GLU B C   
16638 O O   . GLU B 1085 ? 0.2985 0.4068 0.3313 0.0248  0.0054  -0.0095 1083 GLU B O   
16639 C CB  . GLU B 1085 ? 0.2608 0.3697 0.2885 0.0295  0.0074  -0.0116 1083 GLU B CB  
16640 C CG  . GLU B 1085 ? 0.3318 0.4401 0.3577 0.0245  0.0065  -0.0105 1083 GLU B CG  
16641 C CD  . GLU B 1085 ? 0.4334 0.5475 0.4570 0.0246  0.0077  -0.0096 1083 GLU B CD  
16642 O OE1 . GLU B 1085 ? 0.4521 0.5704 0.4751 0.0291  0.0094  -0.0104 1083 GLU B OE1 
16643 O OE2 . GLU B 1085 ? 0.4331 0.5475 0.4552 0.0201  0.0068  -0.0081 1083 GLU B OE2 
16644 N N   . LEU B 1086 ? 0.2832 0.3791 0.3127 0.0215  0.0036  -0.0117 1084 LEU B N   
16645 C CA  . LEU B 1086 ? 0.2409 0.3363 0.2711 0.0176  0.0024  -0.0107 1084 LEU B CA  
16646 C C   . LEU B 1086 ? 0.3016 0.4006 0.3304 0.0134  0.0016  -0.0088 1084 LEU B C   
16647 O O   . LEU B 1086 ? 0.2928 0.3904 0.3194 0.0128  0.0015  -0.0090 1084 LEU B O   
16648 C CB  . LEU B 1086 ? 0.2837 0.3703 0.3134 0.0168  0.0011  -0.0126 1084 LEU B CB  
16649 C CG  . LEU B 1086 ? 0.2784 0.3608 0.3094 0.0199  0.0015  -0.0142 1084 LEU B CG  
16650 C CD1 . LEU B 1086 ? 0.2569 0.3327 0.2879 0.0184  0.0004  -0.0156 1084 LEU B CD1 
16651 C CD2 . LEU B 1086 ? 0.3143 0.4013 0.3472 0.0214  0.0023  -0.0129 1084 LEU B CD2 
16652 N N   . PRO B 1087 ? 0.3252 0.4287 0.3551 0.0103  0.0009  -0.0068 1085 PRO B N   
16653 C CA  . PRO B 1087 ? 0.3080 0.4143 0.3363 0.0056  -0.0002 -0.0047 1085 PRO B CA  
16654 C C   . PRO B 1087 ? 0.2983 0.3954 0.3235 0.0030  -0.0022 -0.0058 1085 PRO B C   
16655 O O   . PRO B 1087 ? 0.3260 0.4161 0.3510 0.0033  -0.0033 -0.0076 1085 PRO B O   
16656 C CB  . PRO B 1087 ? 0.3131 0.4244 0.3431 0.0030  -0.0010 -0.0028 1085 PRO B CB  
16657 C CG  . PRO B 1087 ? 0.3704 0.4846 0.4032 0.0072  0.0004  -0.0034 1085 PRO B CG  
16658 C CD  . PRO B 1087 ? 0.3514 0.4576 0.3835 0.0108  0.0009  -0.0062 1085 PRO B CD  
16659 N N   . GLY B 1088 ? 0.3081 0.4055 0.3309 0.0005  -0.0028 -0.0046 1086 GLY B N   
16660 C CA  . GLY B 1088 ? 0.2898 0.3787 0.3094 -0.0020 -0.0050 -0.0053 1086 GLY B CA  
16661 C C   . GLY B 1088 ? 0.2477 0.3392 0.2646 -0.0061 -0.0059 -0.0026 1086 GLY B C   
16662 O O   . GLY B 1088 ? 0.2742 0.3745 0.2922 -0.0083 -0.0052 0.0001  1086 GLY B O   
16663 N N   . PRO B 1089 ? 0.2744 0.3589 0.2878 -0.0072 -0.0074 -0.0031 1087 PRO B N   
16664 C CA  . PRO B 1089 ? 0.2756 0.3618 0.2858 -0.0116 -0.0085 -0.0003 1087 PRO B CA  
16665 C C   . PRO B 1089 ? 0.2493 0.3438 0.2597 -0.0100 -0.0058 0.0010  1087 PRO B C   
16666 O O   . PRO B 1089 ? 0.2415 0.3377 0.2533 -0.0051 -0.0037 -0.0010 1087 PRO B O   
16667 C CB  . PRO B 1089 ? 0.2441 0.3191 0.2505 -0.0123 -0.0110 -0.0017 1087 PRO B CB  
16668 C CG  . PRO B 1089 ? 0.3187 0.3897 0.3268 -0.0068 -0.0099 -0.0053 1087 PRO B CG  
16669 C CD  . PRO B 1089 ? 0.2855 0.3608 0.2979 -0.0046 -0.0083 -0.0062 1087 PRO B CD  
16670 N N   . VAL B 1090 ? 0.2076 0.3071 0.2160 -0.0144 -0.0062 0.0044  1088 VAL B N   
16671 C CA  . VAL B 1090 ? 0.2035 0.3103 0.2109 -0.0133 -0.0039 0.0056  1088 VAL B CA  
16672 C C   . VAL B 1090 ? 0.2357 0.3342 0.2395 -0.0109 -0.0044 0.0034  1088 VAL B C   
16673 O O   . VAL B 1090 ? 0.2629 0.3507 0.2647 -0.0116 -0.0070 0.0019  1088 VAL B O   
16674 C CB  . VAL B 1090 ? 0.2742 0.3877 0.2798 -0.0193 -0.0044 0.0101  1088 VAL B CB  
16675 C CG1 . VAL B 1090 ? 0.2136 0.3356 0.2229 -0.0221 -0.0043 0.0124  1088 VAL B CG1 
16676 C CG2 . VAL B 1090 ? 0.2104 0.3138 0.2110 -0.0241 -0.0079 0.0112  1088 VAL B CG2 
16677 N N   . GLY B 1091 ? 0.2236 0.3273 0.2265 -0.0078 -0.0020 0.0032  1089 GLY B N   
16678 C CA  . GLY B 1091 ? 0.2094 0.3059 0.2086 -0.0056 -0.0025 0.0012  1089 GLY B CA  
16679 C C   . GLY B 1091 ? 0.2616 0.3500 0.2622 -0.0011 -0.0030 -0.0029 1089 GLY B C   
16680 O O   . GLY B 1091 ? 0.2440 0.3246 0.2419 -0.0001 -0.0045 -0.0045 1089 GLY B O   
16681 N N   . GLU B 1092 ? 0.2508 0.3411 0.2557 0.0016  -0.0019 -0.0043 1090 GLU B N   
16682 C CA  . GLU B 1092 ? 0.2385 0.3221 0.2451 0.0055  -0.0023 -0.0078 1090 GLU B CA  
16683 C C   . GLU B 1092 ? 0.2549 0.3444 0.2652 0.0092  0.0001  -0.0087 1090 GLU B C   
16684 O O   . GLU B 1092 ? 0.2278 0.3245 0.2403 0.0079  0.0010  -0.0067 1090 GLU B O   
16685 C CB  . GLU B 1092 ? 0.2735 0.3493 0.2810 0.0033  -0.0048 -0.0086 1090 GLU B CB  
16686 C CG  . GLU B 1092 ? 0.3031 0.3703 0.3109 0.0061  -0.0060 -0.0118 1090 GLU B CG  
16687 C CD  . GLU B 1092 ? 0.2983 0.3590 0.3068 0.0042  -0.0084 -0.0124 1090 GLU B CD  
16688 O OE1 . GLU B 1092 ? 0.2674 0.3299 0.2785 0.0037  -0.0080 -0.0123 1090 GLU B OE1 
16689 O OE2 . GLU B 1092 ? 0.3540 0.4079 0.3602 0.0033  -0.0106 -0.0131 1090 GLU B OE2 
16690 N N   . ARG B 1093 ? 0.2327 0.3190 0.2434 0.0137  0.0008  -0.0114 1091 ARG B N   
16691 C CA  . ARG B 1093 ? 0.2591 0.3487 0.2730 0.0175  0.0025  -0.0124 1091 ARG B CA  
16692 C C   . ARG B 1093 ? 0.2532 0.3349 0.2690 0.0187  0.0012  -0.0147 1091 ARG B C   
16693 O O   . ARG B 1093 ? 0.2366 0.3113 0.2510 0.0199  0.0001  -0.0168 1091 ARG B O   
16694 C CB  . ARG B 1093 ? 0.2911 0.3841 0.3034 0.0221  0.0044  -0.0136 1091 ARG B CB  
16695 C CG  . ARG B 1093 ? 0.4607 0.5650 0.4728 0.0220  0.0065  -0.0112 1091 ARG B CG  
16696 C CD  . ARG B 1093 ? 0.5163 0.6238 0.5266 0.0275  0.0085  -0.0129 1091 ARG B CD  
16697 N NE  . ARG B 1093 ? 0.5480 0.6507 0.5598 0.0320  0.0085  -0.0155 1091 ARG B NE  
16698 C CZ  . ARG B 1093 ? 0.6567 0.7595 0.6667 0.0374  0.0096  -0.0176 1091 ARG B CZ  
16699 N NH1 . ARG B 1093 ? 0.7195 0.8278 0.7263 0.0395  0.0112  -0.0176 1091 ARG B NH1 
16700 N NH2 . ARG B 1093 ? 0.6043 0.7015 0.6155 0.0408  0.0091  -0.0197 1091 ARG B NH2 
16701 N N   . ASN B 1094 ? 0.2162 0.2992 0.2351 0.0183  0.0013  -0.0143 1092 ASN B N   
16702 C CA  . ASN B 1094 ? 0.1963 0.2729 0.2171 0.0188  0.0003  -0.0160 1092 ASN B CA  
16703 C C   . ASN B 1094 ? 0.2661 0.3446 0.2892 0.0224  0.0017  -0.0166 1092 ASN B C   
16704 O O   . ASN B 1094 ? 0.2300 0.3145 0.2549 0.0225  0.0026  -0.0151 1092 ASN B O   
16705 C CB  . ASN B 1094 ? 0.2150 0.2904 0.2367 0.0151  -0.0010 -0.0150 1092 ASN B CB  
16706 C CG  . ASN B 1094 ? 0.2360 0.3069 0.2550 0.0122  -0.0029 -0.0148 1092 ASN B CG  
16707 O OD1 . ASN B 1094 ? 0.2324 0.2970 0.2507 0.0130  -0.0041 -0.0167 1092 ASN B OD1 
16708 N ND2 . ASN B 1094 ? 0.2376 0.3119 0.2551 0.0088  -0.0034 -0.0126 1092 ASN B ND2 
16709 N N   . LEU B 1095 ? 0.2078 0.2810 0.2306 0.0252  0.0015  -0.0187 1093 LEU B N   
16710 C CA  . LEU B 1095 ? 0.2274 0.3006 0.2514 0.0289  0.0024  -0.0195 1093 LEU B CA  
16711 C C   . LEU B 1095 ? 0.1972 0.2649 0.2232 0.0286  0.0015  -0.0204 1093 LEU B C   
16712 O O   . LEU B 1095 ? 0.2265 0.2893 0.2527 0.0267  0.0003  -0.0213 1093 LEU B O   
16713 C CB  . LEU B 1095 ? 0.2613 0.3322 0.2825 0.0324  0.0027  -0.0213 1093 LEU B CB  
16714 C CG  . LEU B 1095 ? 0.3052 0.3817 0.3238 0.0327  0.0037  -0.0205 1093 LEU B CG  
16715 C CD1 . LEU B 1095 ? 0.3792 0.4528 0.3943 0.0362  0.0038  -0.0226 1093 LEU B CD1 
16716 C CD2 . LEU B 1095 ? 0.2713 0.3576 0.2914 0.0333  0.0054  -0.0183 1093 LEU B CD2 
16717 N N   . TYR B 1096 ? 0.2030 0.2720 0.2306 0.0305  0.0022  -0.0199 1094 TYR B N   
16718 C CA  . TYR B 1096 ? 0.1778 0.2428 0.2074 0.0302  0.0017  -0.0202 1094 TYR B CA  
16719 C C   . TYR B 1096 ? 0.1990 0.2621 0.2282 0.0339  0.0020  -0.0206 1094 TYR B C   
16720 O O   . TYR B 1096 ? 0.2132 0.2810 0.2424 0.0362  0.0029  -0.0197 1094 TYR B O   
16721 C CB  . TYR B 1096 ? 0.1895 0.2583 0.2210 0.0278  0.0019  -0.0185 1094 TYR B CB  
16722 C CG  . TYR B 1096 ? 0.2101 0.2759 0.2434 0.0275  0.0017  -0.0184 1094 TYR B CG  
16723 C CD1 . TYR B 1096 ? 0.2285 0.2903 0.2625 0.0254  0.0009  -0.0193 1094 TYR B CD1 
16724 C CD2 . TYR B 1096 ? 0.2425 0.3101 0.2765 0.0293  0.0023  -0.0173 1094 TYR B CD2 
16725 C CE1 . TYR B 1096 ? 0.2346 0.2946 0.2701 0.0250  0.0010  -0.0191 1094 TYR B CE1 
16726 C CE2 . TYR B 1096 ? 0.2212 0.2863 0.2565 0.0287  0.0021  -0.0169 1094 TYR B CE2 
16727 C CZ  . TYR B 1096 ? 0.2486 0.3101 0.2845 0.0264  0.0016  -0.0177 1094 TYR B CZ  
16728 O OH  . TYR B 1096 ? 0.2556 0.3156 0.2927 0.0258  0.0017  -0.0171 1094 TYR B OH  
16729 N N   . THR B 1097 ? 0.1968 0.2530 0.2257 0.0345  0.0010  -0.0221 1095 THR B N   
16730 C CA  . THR B 1097 ? 0.1882 0.2405 0.2159 0.0379  0.0007  -0.0227 1095 THR B CA  
16731 C C   . THR B 1097 ? 0.2115 0.2583 0.2406 0.0366  -0.0003 -0.0226 1095 THR B C   
16732 O O   . THR B 1097 ? 0.2228 0.2677 0.2535 0.0336  -0.0009 -0.0229 1095 THR B O   
16733 C CB  . THR B 1097 ? 0.2227 0.2712 0.2472 0.0401  0.0001  -0.0248 1095 THR B CB  
16734 O OG1 . THR B 1097 ? 0.2910 0.3356 0.3157 0.0375  -0.0011 -0.0259 1095 THR B OG1 
16735 C CG2 . THR B 1097 ? 0.2687 0.3235 0.2914 0.0419  0.0013  -0.0247 1095 THR B CG2 
16736 N N   . LEU B 1098 ? 0.1863 0.2304 0.2148 0.0390  -0.0006 -0.0222 1096 LEU B N   
16737 C CA  . LEU B 1098 ? 0.1866 0.2253 0.2161 0.0376  -0.0016 -0.0217 1096 LEU B CA  
16738 C C   . LEU B 1098 ? 0.2216 0.2525 0.2485 0.0398  -0.0032 -0.0231 1096 LEU B C   
16739 O O   . LEU B 1098 ? 0.2245 0.2542 0.2488 0.0437  -0.0033 -0.0235 1096 LEU B O   
16740 C CB  . LEU B 1098 ? 0.2041 0.2452 0.2347 0.0378  -0.0010 -0.0195 1096 LEU B CB  
16741 C CG  . LEU B 1098 ? 0.2018 0.2499 0.2347 0.0353  0.0002  -0.0181 1096 LEU B CG  
16742 C CD1 . LEU B 1098 ? 0.2136 0.2638 0.2469 0.0361  0.0006  -0.0159 1096 LEU B CD1 
16743 C CD2 . LEU B 1098 ? 0.1970 0.2442 0.2317 0.0315  0.0001  -0.0184 1096 LEU B CD2 
16744 N N   . HIS B 1099 ? 0.2584 0.2841 0.2857 0.0373  -0.0046 -0.0239 1097 HIS B N   
16745 C CA  . HIS B 1099 ? 0.2628 0.2802 0.2875 0.0384  -0.0066 -0.0254 1097 HIS B CA  
16746 C C   . HIS B 1099 ? 0.2276 0.2401 0.2537 0.0358  -0.0079 -0.0240 1097 HIS B C   
16747 O O   . HIS B 1099 ? 0.2356 0.2516 0.2647 0.0331  -0.0070 -0.0221 1097 HIS B O   
16748 C CB  . HIS B 1099 ? 0.2540 0.2696 0.2781 0.0372  -0.0076 -0.0275 1097 HIS B CB  
16749 C CG  . HIS B 1099 ? 0.3142 0.3349 0.3370 0.0388  -0.0064 -0.0285 1097 HIS B CG  
16750 N ND1 . HIS B 1099 ? 0.2838 0.3022 0.3025 0.0422  -0.0068 -0.0303 1097 HIS B ND1 
16751 C CD2 . HIS B 1099 ? 0.2359 0.2635 0.2606 0.0373  -0.0049 -0.0277 1097 HIS B CD2 
16752 C CE1 . HIS B 1099 ? 0.3102 0.3347 0.3287 0.0425  -0.0054 -0.0305 1097 HIS B CE1 
16753 N NE2 . HIS B 1099 ? 0.3053 0.3350 0.3272 0.0394  -0.0044 -0.0288 1097 HIS B NE2 
16754 N N   . ALA B 1100 ? 0.2503 0.2544 0.2737 0.0365  -0.0102 -0.0250 1098 ALA B N   
16755 C CA  . ALA B 1100 ? 0.3251 0.3243 0.3499 0.0331  -0.0117 -0.0235 1098 ALA B CA  
16756 C C   . ALA B 1100 ? 0.2822 0.2847 0.3110 0.0286  -0.0116 -0.0235 1098 ALA B C   
16757 O O   . ALA B 1100 ? 0.2636 0.2684 0.2929 0.0285  -0.0115 -0.0252 1098 ALA B O   
16758 C CB  . ALA B 1100 ? 0.3390 0.3277 0.3597 0.0344  -0.0146 -0.0247 1098 ALA B CB  
16759 N N   . ARG B 1101 ? 0.2574 0.2605 0.2890 0.0250  -0.0116 -0.0213 1099 ARG B N   
16760 C CA  . ARG B 1101 ? 0.3041 0.3111 0.3398 0.0211  -0.0114 -0.0212 1099 ARG B CA  
16761 C C   . ARG B 1101 ? 0.2942 0.2954 0.3298 0.0191  -0.0141 -0.0223 1099 ARG B C   
16762 O O   . ARG B 1101 ? 0.3065 0.3105 0.3445 0.0175  -0.0144 -0.0235 1099 ARG B O   
16763 C CB  . ARG B 1101 ? 0.3206 0.3318 0.3595 0.0181  -0.0100 -0.0186 1099 ARG B CB  
16764 C CG  . ARG B 1101 ? 0.3459 0.3652 0.3866 0.0186  -0.0074 -0.0183 1099 ARG B CG  
16765 C CD  . ARG B 1101 ? 0.3423 0.3655 0.3854 0.0160  -0.0061 -0.0158 1099 ARG B CD  
16766 N NE  . ARG B 1101 ? 0.3829 0.4117 0.4299 0.0133  -0.0053 -0.0162 1099 ARG B NE  
16767 C CZ  . ARG B 1101 ? 0.4517 0.4865 0.5001 0.0139  -0.0036 -0.0170 1099 ARG B CZ  
16768 N NH1 . ARG B 1101 ? 0.4163 0.4526 0.4626 0.0164  -0.0027 -0.0175 1099 ARG B NH1 
16769 N NH2 . ARG B 1101 ? 0.4383 0.4779 0.4900 0.0118  -0.0029 -0.0172 1099 ARG B NH2 
16770 N N   . GLY B 1102 ? 0.2751 0.2681 0.3079 0.0190  -0.0163 -0.0218 1100 GLY B N   
16771 C CA  . GLY B 1102 ? 0.3233 0.3102 0.3558 0.0164  -0.0194 -0.0225 1100 GLY B CA  
16772 C C   . GLY B 1102 ? 0.3263 0.3070 0.3581 0.0136  -0.0212 -0.0201 1100 GLY B C   
16773 O O   . GLY B 1102 ? 0.3011 0.2764 0.3291 0.0160  -0.0216 -0.0193 1100 GLY B O   
16774 N N   . ARG B 1103 ? 0.2667 0.2485 0.3021 0.0085  -0.0223 -0.0187 1101 ARG B N   
16775 C CA  . ARG B 1103 ? 0.2838 0.2599 0.3187 0.0049  -0.0242 -0.0158 1101 ARG B CA  
16776 C C   . ARG B 1103 ? 0.2617 0.2462 0.3010 0.0019  -0.0215 -0.0126 1101 ARG B C   
16777 O O   . ARG B 1103 ? 0.2666 0.2598 0.3110 -0.0004 -0.0199 -0.0125 1101 ARG B O   
16778 C CB  . ARG B 1103 ? 0.3155 0.2865 0.3510 0.0008  -0.0277 -0.0161 1101 ARG B CB  
16779 C CG  . ARG B 1103 ? 0.3194 0.2824 0.3531 -0.0030 -0.0304 -0.0131 1101 ARG B CG  
16780 C CD  . ARG B 1103 ? 0.3540 0.3103 0.3874 -0.0069 -0.0345 -0.0137 1101 ARG B CD  
16781 N NE  . ARG B 1103 ? 0.4220 0.3698 0.4500 -0.0030 -0.0371 -0.0175 1101 ARG B NE  
16782 C CZ  . ARG B 1103 ? 0.4959 0.4309 0.5171 -0.0010 -0.0402 -0.0183 1101 ARG B CZ  
16783 N NH1 . ARG B 1103 ? 0.4004 0.3287 0.4190 -0.0022 -0.0414 -0.0155 1101 ARG B NH1 
16784 N NH2 . ARG B 1103 ? 0.4720 0.4005 0.4885 0.0025  -0.0423 -0.0221 1101 ARG B NH2 
16785 N N   . ILE B 1104 ? 0.2435 0.2251 0.2804 0.0023  -0.0211 -0.0101 1102 ILE B N   
16786 C CA  . ILE B 1104 ? 0.2314 0.2204 0.2714 -0.0001 -0.0185 -0.0070 1102 ILE B CA  
16787 C C   . ILE B 1104 ? 0.2665 0.2529 0.3078 -0.0059 -0.0202 -0.0037 1102 ILE B C   
16788 O O   . ILE B 1104 ? 0.2814 0.2573 0.3187 -0.0068 -0.0233 -0.0026 1102 ILE B O   
16789 C CB  . ILE B 1104 ? 0.2430 0.2308 0.2795 0.0036  -0.0171 -0.0060 1102 ILE B CB  
16790 C CG1 . ILE B 1104 ? 0.2553 0.2451 0.2904 0.0092  -0.0159 -0.0092 1102 ILE B CG1 
16791 C CG2 . ILE B 1104 ? 0.2764 0.2723 0.3156 0.0013  -0.0144 -0.0030 1102 ILE B CG2 
16792 C CD1 . ILE B 1104 ? 0.2865 0.2865 0.3257 0.0091  -0.0133 -0.0107 1102 ILE B CD1 
16793 N N   . LEU B 1105 ? 0.2257 0.2216 0.2723 -0.0099 -0.0183 -0.0019 1103 LEU B N   
16794 C CA  . LEU B 1105 ? 0.2286 0.2242 0.2768 -0.0159 -0.0193 0.0018  1103 LEU B CA  
16795 C C   . LEU B 1105 ? 0.2416 0.2357 0.2870 -0.0161 -0.0183 0.0053  1103 LEU B C   
16796 O O   . LEU B 1105 ? 0.2485 0.2500 0.2947 -0.0142 -0.0150 0.0056  1103 LEU B O   
16797 C CB  . LEU B 1105 ? 0.2274 0.2350 0.2824 -0.0196 -0.0172 0.0024  1103 LEU B CB  
16798 C CG  . LEU B 1105 ? 0.2729 0.2834 0.3306 -0.0262 -0.0175 0.0068  1103 LEU B CG  
16799 C CD1 . LEU B 1105 ? 0.2652 0.2658 0.3213 -0.0302 -0.0221 0.0078  1103 LEU B CD1 
16800 C CD2 . LEU B 1105 ? 0.2339 0.2585 0.2986 -0.0286 -0.0148 0.0069  1103 LEU B CD2 
16801 N N   . LEU B 1106 ? 0.2577 0.2415 0.2992 -0.0184 -0.0213 0.0078  1104 LEU B N   
16802 C CA  . LEU B 1106 ? 0.2559 0.2366 0.2941 -0.0190 -0.0210 0.0115  1104 LEU B CA  
16803 C C   . LEU B 1106 ? 0.2859 0.2692 0.3265 -0.0263 -0.0214 0.0159  1104 LEU B C   
16804 O O   . LEU B 1106 ? 0.2661 0.2443 0.3073 -0.0306 -0.0245 0.0167  1104 LEU B O   
16805 C CB  . LEU B 1106 ? 0.2736 0.2398 0.3050 -0.0159 -0.0246 0.0112  1104 LEU B CB  
16806 C CG  . LEU B 1106 ? 0.3331 0.2972 0.3608 -0.0086 -0.0237 0.0089  1104 LEU B CG  
16807 C CD1 . LEU B 1106 ? 0.2805 0.2537 0.3113 -0.0048 -0.0209 0.0050  1104 LEU B CD1 
16808 C CD2 . LEU B 1106 ? 0.2475 0.1970 0.2689 -0.0054 -0.0278 0.0077  1104 LEU B CD2 
16809 N N   . VAL B 1107 ? 0.2716 0.2632 0.3137 -0.0278 -0.0183 0.0188  1105 VAL B N   
16810 C CA  . VAL B 1107 ? 0.2387 0.2342 0.2830 -0.0347 -0.0180 0.0236  1105 VAL B CA  
16811 C C   . VAL B 1107 ? 0.3113 0.3020 0.3505 -0.0348 -0.0180 0.0274  1105 VAL B C   
16812 O O   . VAL B 1107 ? 0.2864 0.2861 0.3266 -0.0346 -0.0146 0.0290  1105 VAL B O   
16813 C CB  . VAL B 1107 ? 0.2620 0.2735 0.3129 -0.0367 -0.0139 0.0235  1105 VAL B CB  
16814 C CG1 . VAL B 1107 ? 0.2611 0.2774 0.3151 -0.0444 -0.0140 0.0280  1105 VAL B CG1 
16815 C CG2 . VAL B 1107 ? 0.2607 0.2770 0.3159 -0.0343 -0.0136 0.0188  1105 VAL B CG2 
16816 N N   . PRO B 1108 ? 0.2805 0.2571 0.3140 -0.0347 -0.0220 0.0288  1106 PRO B N   
16817 C CA  . PRO B 1108 ? 0.3179 0.2892 0.3463 -0.0345 -0.0224 0.0326  1106 PRO B CA  
16818 C C   . PRO B 1108 ? 0.3271 0.3003 0.3560 -0.0423 -0.0226 0.0384  1106 PRO B C   
16819 O O   . PRO B 1108 ? 0.3305 0.3062 0.3630 -0.0483 -0.0235 0.0398  1106 PRO B O   
16820 C CB  . PRO B 1108 ? 0.3022 0.2568 0.3242 -0.0313 -0.0271 0.0316  1106 PRO B CB  
16821 C CG  . PRO B 1108 ? 0.3450 0.2949 0.3687 -0.0342 -0.0300 0.0297  1106 PRO B CG  
16822 C CD  . PRO B 1108 ? 0.2977 0.2617 0.3284 -0.0339 -0.0265 0.0266  1106 PRO B CD  
16823 N N   . ALA B 1109 ? 0.2935 0.2657 0.3186 -0.0423 -0.0219 0.0421  1107 ALA B N   
16824 C CA  . ALA B 1109 ? 0.3810 0.3524 0.4048 -0.0495 -0.0226 0.0482  1107 ALA B CA  
16825 C C   . ALA B 1109 ? 0.4122 0.3668 0.4283 -0.0498 -0.0273 0.0514  1107 ALA B C   
16826 O O   . ALA B 1109 ? 0.4056 0.3544 0.4201 -0.0566 -0.0300 0.0559  1107 ALA B O   
16827 C CB  . ALA B 1109 ? 0.3610 0.3453 0.3860 -0.0501 -0.0180 0.0507  1107 ALA B CB  
16828 N N   . THR B 1110 ? 0.4033 0.3503 0.4147 -0.0426 -0.0284 0.0492  1108 THR B N   
16829 C CA  . THR B 1110 ? 0.3670 0.2983 0.3707 -0.0414 -0.0327 0.0518  1108 THR B CA  
16830 C C   . THR B 1110 ? 0.4228 0.3425 0.4233 -0.0346 -0.0360 0.0470  1108 THR B C   
16831 O O   . THR B 1110 ? 0.3561 0.2813 0.3599 -0.0300 -0.0341 0.0418  1108 THR B O   
16832 C CB  . THR B 1110 ? 0.3926 0.3269 0.3931 -0.0385 -0.0308 0.0543  1108 THR B CB  
16833 O OG1 . THR B 1110 ? 0.3856 0.3274 0.3880 -0.0310 -0.0279 0.0496  1108 THR B OG1 
16834 C CG2 . THR B 1110 ? 0.4047 0.3506 0.4076 -0.0449 -0.0275 0.0591  1108 THR B CG2 
16835 N N   . GLU B 1111 ? 0.3861 0.2892 0.3795 -0.0339 -0.0409 0.0488  1109 GLU B N   
16836 C CA  . GLU B 1111 ? 0.4107 0.3019 0.4000 -0.0269 -0.0442 0.0443  1109 GLU B CA  
16837 C C   . GLU B 1111 ? 0.4106 0.3080 0.4003 -0.0180 -0.0413 0.0407  1109 GLU B C   
16838 O O   . GLU B 1111 ? 0.3597 0.2579 0.3507 -0.0126 -0.0409 0.0354  1109 GLU B O   
16839 C CB  . GLU B 1111 ? 0.4210 0.2931 0.4021 -0.0272 -0.0500 0.0472  1109 GLU B CB  
16840 C CG  . GLU B 1111 ? 0.4606 0.3198 0.4367 -0.0193 -0.0535 0.0424  1109 GLU B CG  
16841 C CD  . GLU B 1111 ? 0.4987 0.3377 0.4660 -0.0194 -0.0598 0.0450  1109 GLU B CD  
16842 O OE1 . GLU B 1111 ? 0.5146 0.3490 0.4775 -0.0156 -0.0606 0.0472  1109 GLU B OE1 
16843 O OE2 . GLU B 1111 ? 0.5133 0.3407 0.4781 -0.0233 -0.0640 0.0449  1109 GLU B OE2 
16844 N N   . SER B 1112 ? 0.3762 0.2780 0.3645 -0.0166 -0.0395 0.0436  1110 SER B N   
16845 C CA  . SER B 1112 ? 0.4022 0.3107 0.3912 -0.0087 -0.0370 0.0405  1110 SER B CA  
16846 C C   . SER B 1112 ? 0.4096 0.3340 0.4057 -0.0083 -0.0321 0.0370  1110 SER B C   
16847 O O   . SER B 1112 ? 0.3682 0.2962 0.3655 -0.0020 -0.0308 0.0326  1110 SER B O   
16848 C CB  . SER B 1112 ? 0.4215 0.3316 0.4075 -0.0080 -0.0364 0.0447  1110 SER B CB  
16849 O OG  . SER B 1112 ? 0.4366 0.3553 0.4242 -0.0013 -0.0337 0.0419  1110 SER B OG  
16850 N N   . GLY B 1113 ? 0.3733 0.3076 0.3740 -0.0147 -0.0294 0.0389  1111 GLY B N   
16851 C CA  . GLY B 1113 ? 0.3282 0.2762 0.3354 -0.0144 -0.0253 0.0354  1111 GLY B CA  
16852 C C   . GLY B 1113 ? 0.3336 0.2782 0.3423 -0.0119 -0.0266 0.0305  1111 GLY B C   
16853 O O   . GLY B 1113 ? 0.3184 0.2701 0.3299 -0.0075 -0.0243 0.0263  1111 GLY B O   
16854 N N   . LEU B 1114 ? 0.3537 0.2871 0.3602 -0.0149 -0.0305 0.0310  1112 LEU B N   
16855 C CA  . LEU B 1114 ? 0.3470 0.2762 0.3542 -0.0129 -0.0321 0.0264  1112 LEU B CA  
16856 C C   . LEU B 1114 ? 0.3486 0.2724 0.3523 -0.0043 -0.0331 0.0225  1112 LEU B C   
16857 O O   . LEU B 1114 ? 0.2954 0.2231 0.3012 -0.0007 -0.0318 0.0180  1112 LEU B O   
16858 C CB  . LEU B 1114 ? 0.3371 0.2542 0.3418 -0.0180 -0.0367 0.0281  1112 LEU B CB  
16859 C CG  . LEU B 1114 ? 0.3789 0.2883 0.3825 -0.0160 -0.0395 0.0236  1112 LEU B CG  
16860 C CD1 . LEU B 1114 ? 0.3242 0.2461 0.3345 -0.0162 -0.0363 0.0199  1112 LEU B CD1 
16861 C CD2 . LEU B 1114 ? 0.3565 0.2530 0.3569 -0.0218 -0.0446 0.0258  1112 LEU B CD2 
16862 N N   . TYR B 1115 ? 0.3775 0.2923 0.3755 -0.0009 -0.0353 0.0243  1113 TYR B N   
16863 C CA  . TYR B 1115 ? 0.3682 0.2790 0.3629 0.0077  -0.0360 0.0208  1113 TYR B CA  
16864 C C   . TYR B 1115 ? 0.3216 0.2468 0.3206 0.0117  -0.0315 0.0186  1113 TYR B C   
16865 O O   . TYR B 1115 ? 0.3191 0.2461 0.3185 0.0171  -0.0308 0.0144  1113 TYR B O   
16866 C CB  . TYR B 1115 ? 0.3548 0.2543 0.3429 0.0106  -0.0392 0.0236  1113 TYR B CB  
16867 C CG  . TYR B 1115 ? 0.3632 0.2456 0.3457 0.0078  -0.0446 0.0254  1113 TYR B CG  
16868 C CD1 . TYR B 1115 ? 0.3926 0.2692 0.3753 0.0045  -0.0468 0.0234  1113 TYR B CD1 
16869 C CD2 . TYR B 1115 ? 0.4495 0.3210 0.4259 0.0085  -0.0478 0.0290  1113 TYR B CD2 
16870 C CE1 . TYR B 1115 ? 0.4357 0.2960 0.4127 0.0016  -0.0521 0.0250  1113 TYR B CE1 
16871 C CE2 . TYR B 1115 ? 0.4730 0.3277 0.4435 0.0059  -0.0531 0.0308  1113 TYR B CE2 
16872 C CZ  . TYR B 1115 ? 0.5000 0.3491 0.4709 0.0023  -0.0553 0.0287  1113 TYR B CZ  
16873 O OH  . TYR B 1115 ? 0.5355 0.3672 0.5001 -0.0008 -0.0610 0.0306  1113 TYR B OH  
16874 N N   . HIS B 1116 ? 0.3131 0.2483 0.3149 0.0090  -0.0285 0.0215  1114 HIS B N   
16875 C CA  . HIS B 1116 ? 0.3164 0.2648 0.3220 0.0122  -0.0245 0.0195  1114 HIS B CA  
16876 C C   . HIS B 1116 ? 0.3194 0.2755 0.3299 0.0111  -0.0222 0.0158  1114 HIS B C   
16877 O O   . HIS B 1116 ? 0.2840 0.2455 0.2960 0.0157  -0.0206 0.0124  1114 HIS B O   
16878 C CB  . HIS B 1116 ? 0.3302 0.2869 0.3371 0.0091  -0.0220 0.0232  1114 HIS B CB  
16879 C CG  . HIS B 1116 ? 0.3688 0.3209 0.3712 0.0120  -0.0235 0.0261  1114 HIS B CG  
16880 N ND1 . HIS B 1116 ? 0.4304 0.3719 0.4282 0.0094  -0.0267 0.0302  1114 HIS B ND1 
16881 C CD2 . HIS B 1116 ? 0.3888 0.3455 0.3905 0.0171  -0.0225 0.0258  1114 HIS B CD2 
16882 C CE1 . HIS B 1116 ? 0.4004 0.3399 0.3947 0.0131  -0.0276 0.0321  1114 HIS B CE1 
16883 N NE2 . HIS B 1116 ? 0.4245 0.3734 0.4213 0.0179  -0.0251 0.0295  1114 HIS B NE2 
16884 N N   . GLN B 1117 ? 0.3082 0.2654 0.3215 0.0051  -0.0222 0.0167  1115 GLN B N   
16885 C CA  . GLN B 1117 ? 0.2725 0.2367 0.2905 0.0040  -0.0204 0.0134  1115 GLN B CA  
16886 C C   . GLN B 1117 ? 0.2908 0.2483 0.3069 0.0081  -0.0225 0.0093  1115 GLN B C   
16887 O O   . GLN B 1117 ? 0.2972 0.2610 0.3158 0.0108  -0.0206 0.0058  1115 GLN B O   
16888 C CB  . GLN B 1117 ? 0.2886 0.2546 0.3097 -0.0032 -0.0206 0.0153  1115 GLN B CB  
16889 C CG  . GLN B 1117 ? 0.2893 0.2640 0.3128 -0.0076 -0.0180 0.0191  1115 GLN B CG  
16890 C CD  . GLN B 1117 ? 0.2994 0.2772 0.3266 -0.0147 -0.0180 0.0210  1115 GLN B CD  
16891 O OE1 . GLN B 1117 ? 0.2776 0.2484 0.3046 -0.0171 -0.0209 0.0206  1115 GLN B OE1 
16892 N NE2 . GLN B 1117 ? 0.2657 0.2545 0.2963 -0.0178 -0.0147 0.0231  1115 GLN B NE2 
16893 N N   . LEU B 1118 ? 0.2776 0.2220 0.2891 0.0084  -0.0264 0.0096  1116 LEU B N   
16894 C CA  . LEU B 1118 ? 0.3000 0.2372 0.3088 0.0127  -0.0285 0.0056  1116 LEU B CA  
16895 C C   . LEU B 1118 ? 0.3059 0.2458 0.3131 0.0203  -0.0272 0.0030  1116 LEU B C   
16896 O O   . LEU B 1118 ? 0.2956 0.2386 0.3037 0.0236  -0.0263 -0.0008 1116 LEU B O   
16897 C CB  . LEU B 1118 ? 0.3105 0.2321 0.3138 0.0116  -0.0334 0.0066  1116 LEU B CB  
16898 C CG  . LEU B 1118 ? 0.3953 0.3076 0.3951 0.0146  -0.0364 0.0025  1116 LEU B CG  
16899 C CD1 . LEU B 1118 ? 0.3889 0.3073 0.3932 0.0114  -0.0354 0.0002  1116 LEU B CD1 
16900 C CD2 . LEU B 1118 ? 0.4149 0.3106 0.4086 0.0128  -0.0416 0.0041  1116 LEU B CD2 
16901 N N   . ALA B 1119 ? 0.2800 0.2197 0.2851 0.0231  -0.0270 0.0052  1117 ALA B N   
16902 C CA  . ALA B 1119 ? 0.2858 0.2300 0.2902 0.0301  -0.0255 0.0032  1117 ALA B CA  
16903 C C   . ALA B 1119 ? 0.3115 0.2695 0.3212 0.0300  -0.0215 0.0013  1117 ALA B C   
16904 O O   . ALA B 1119 ? 0.2752 0.2365 0.2850 0.0346  -0.0206 -0.0019 1117 ALA B O   
16905 C CB  . ALA B 1119 ? 0.2661 0.2100 0.2684 0.0321  -0.0257 0.0064  1117 ALA B CB  
16906 N N   . ALA B 1120 ? 0.2774 0.2435 0.2911 0.0249  -0.0193 0.0033  1118 ALA B N   
16907 C CA  . ALA B 1120 ? 0.2898 0.2680 0.3079 0.0248  -0.0158 0.0016  1118 ALA B CA  
16908 C C   . ALA B 1120 ? 0.2865 0.2652 0.3062 0.0249  -0.0158 -0.0020 1118 ALA B C   
16909 O O   . ALA B 1120 ? 0.2623 0.2472 0.2834 0.0278  -0.0141 -0.0045 1118 ALA B O   
16910 C CB  . ALA B 1120 ? 0.2535 0.2391 0.2751 0.0195  -0.0137 0.0042  1118 ALA B CB  
16911 N N   . ALA B 1121 ? 0.2951 0.2669 0.3143 0.0217  -0.0180 -0.0022 1119 ALA B N   
16912 C CA  . ALA B 1121 ? 0.2380 0.2102 0.2587 0.0213  -0.0182 -0.0054 1119 ALA B CA  
16913 C C   . ALA B 1121 ? 0.2201 0.1862 0.2368 0.0269  -0.0198 -0.0087 1119 ALA B C   
16914 O O   . ALA B 1121 ? 0.2327 0.2031 0.2504 0.0289  -0.0186 -0.0116 1119 ALA B O   
16915 C CB  . ALA B 1121 ? 0.2438 0.2114 0.2656 0.0156  -0.0202 -0.0044 1119 ALA B CB  
16916 N N   . LEU B 1122 ? 0.2386 0.1943 0.2503 0.0295  -0.0225 -0.0081 1120 LEU B N   
16917 C CA  . LEU B 1122 ? 0.2714 0.2212 0.2787 0.0356  -0.0240 -0.0113 1120 LEU B CA  
16918 C C   . LEU B 1122 ? 0.2735 0.2320 0.2815 0.0409  -0.0212 -0.0125 1120 LEU B C   
16919 O O   . LEU B 1122 ? 0.2945 0.2547 0.3015 0.0446  -0.0207 -0.0157 1120 LEU B O   
16920 C CB  . LEU B 1122 ? 0.3077 0.2441 0.3092 0.0376  -0.0277 -0.0104 1120 LEU B CB  
16921 C CG  . LEU B 1122 ? 0.3152 0.2412 0.3150 0.0323  -0.0312 -0.0092 1120 LEU B CG  
16922 C CD1 . LEU B 1122 ? 0.3331 0.2456 0.3267 0.0344  -0.0349 -0.0078 1120 LEU B CD1 
16923 C CD2 . LEU B 1122 ? 0.2954 0.2181 0.2946 0.0316  -0.0326 -0.0127 1120 LEU B CD2 
16924 N N   . ALA B 1123 ? 0.2699 0.2345 0.2796 0.0411  -0.0195 -0.0099 1121 ALA B N   
16925 C CA  . ALA B 1123 ? 0.2948 0.2684 0.3056 0.0456  -0.0171 -0.0106 1121 ALA B CA  
16926 C C   . ALA B 1123 ? 0.2963 0.2797 0.3108 0.0445  -0.0144 -0.0126 1121 ALA B C   
16927 O O   . ALA B 1123 ? 0.2713 0.2608 0.2860 0.0485  -0.0129 -0.0141 1121 ALA B O   
16928 C CB  . ALA B 1123 ? 0.2602 0.2388 0.2725 0.0450  -0.0160 -0.0072 1121 ALA B CB  
16929 N N   . THR B 1124 ? 0.2207 0.2059 0.2382 0.0392  -0.0140 -0.0125 1122 THR B N   
16930 C CA  . THR B 1124 ? 0.2168 0.2100 0.2374 0.0380  -0.0119 -0.0143 1122 THR B CA  
16931 C C   . THR B 1124 ? 0.2088 0.1974 0.2281 0.0380  -0.0133 -0.0172 1122 THR B C   
16932 O O   . THR B 1124 ? 0.2456 0.2391 0.2675 0.0359  -0.0122 -0.0184 1122 THR B O   
16933 C CB  . THR B 1124 ? 0.2379 0.2376 0.2628 0.0329  -0.0102 -0.0124 1122 THR B CB  
16934 O OG1 . THR B 1124 ? 0.2588 0.2530 0.2839 0.0288  -0.0118 -0.0106 1122 THR B OG1 
16935 C CG2 . THR B 1124 ? 0.2371 0.2438 0.2631 0.0336  -0.0083 -0.0103 1122 THR B CG2 
16936 N N   . GLY B 1125 ? 0.2499 0.2287 0.2648 0.0406  -0.0158 -0.0184 1123 GLY B N   
16937 C CA  . GLY B 1125 ? 0.2462 0.2201 0.2588 0.0416  -0.0174 -0.0215 1123 GLY B CA  
16938 C C   . GLY B 1125 ? 0.2719 0.2411 0.2857 0.0363  -0.0193 -0.0215 1123 GLY B C   
16939 O O   . GLY B 1125 ? 0.2982 0.2638 0.3103 0.0365  -0.0208 -0.0241 1123 GLY B O   
16940 N N   . ASN B 1126 ? 0.2250 0.1944 0.2416 0.0315  -0.0195 -0.0186 1124 ASN B N   
16941 C CA  . ASN B 1126 ? 0.2450 0.2128 0.2641 0.0260  -0.0209 -0.0181 1124 ASN B CA  
16942 C C   . ASN B 1126 ? 0.2744 0.2300 0.2899 0.0244  -0.0248 -0.0178 1124 ASN B C   
16943 O O   . ASN B 1126 ? 0.2773 0.2253 0.2886 0.0268  -0.0264 -0.0169 1124 ASN B O   
16944 C CB  . ASN B 1126 ? 0.2394 0.2149 0.2636 0.0214  -0.0188 -0.0151 1124 ASN B CB  
16945 C CG  . ASN B 1126 ? 0.2403 0.2271 0.2678 0.0224  -0.0154 -0.0157 1124 ASN B CG  
16946 O OD1 . ASN B 1126 ? 0.2421 0.2327 0.2714 0.0222  -0.0148 -0.0177 1124 ASN B OD1 
16947 N ND2 . ASN B 1126 ? 0.2352 0.2266 0.2631 0.0236  -0.0135 -0.0138 1124 ASN B ND2 
16948 N N   . SER B 1127 ? 0.2982 0.2516 0.3151 0.0204  -0.0267 -0.0185 1125 SER B N   
16949 C CA  . SER B 1127 ? 0.2811 0.2248 0.2962 0.0164  -0.0303 -0.0171 1125 SER B CA  
16950 C C   . SER B 1127 ? 0.3211 0.2707 0.3415 0.0104  -0.0291 -0.0132 1125 SER B C   
16951 O O   . SER B 1127 ? 0.2953 0.2558 0.3201 0.0097  -0.0257 -0.0122 1125 SER B O   
16952 C CB  . SER B 1127 ? 0.2877 0.2264 0.3018 0.0149  -0.0332 -0.0197 1125 SER B CB  
16953 O OG  . SER B 1127 ? 0.3504 0.2988 0.3704 0.0114  -0.0316 -0.0198 1125 SER B OG  
16954 N N   . VAL B 1128 ? 0.2801 0.2223 0.2995 0.0058  -0.0321 -0.0108 1126 VAL B N   
16955 C CA  . VAL B 1128 ? 0.2697 0.2173 0.2935 -0.0001 -0.0311 -0.0068 1126 VAL B CA  
16956 C C   . VAL B 1128 ? 0.3108 0.2547 0.3362 -0.0065 -0.0342 -0.0056 1126 VAL B C   
16957 O O   . VAL B 1128 ? 0.3404 0.2741 0.3621 -0.0066 -0.0380 -0.0073 1126 VAL B O   
16958 C CB  . VAL B 1128 ? 0.2990 0.2427 0.3199 0.0002  -0.0311 -0.0033 1126 VAL B CB  
16959 C CG1 . VAL B 1128 ? 0.3011 0.2487 0.3205 0.0065  -0.0283 -0.0044 1126 VAL B CG1 
16960 C CG2 . VAL B 1128 ? 0.2880 0.2161 0.3027 -0.0003 -0.0358 -0.0026 1126 VAL B CG2 
16961 N N   . ALA B 1129 ? 0.2751 0.2281 0.3062 -0.0118 -0.0324 -0.0026 1127 ALA B N   
16962 C CA  . ALA B 1129 ? 0.3056 0.2566 0.3390 -0.0190 -0.0350 -0.0001 1127 ALA B CA  
16963 C C   . ALA B 1129 ? 0.3111 0.2653 0.3457 -0.0229 -0.0336 0.0048  1127 ALA B C   
16964 O O   . ALA B 1129 ? 0.2773 0.2432 0.3160 -0.0227 -0.0295 0.0059  1127 ALA B O   
16965 C CB  . ALA B 1129 ? 0.2958 0.2568 0.3358 -0.0219 -0.0342 -0.0013 1127 ALA B CB  
16966 N N   . ILE B 1130 ? 0.2695 0.2128 0.3000 -0.0261 -0.0371 0.0077  1128 ILE B N   
16967 C CA  . ILE B 1130 ? 0.2849 0.2293 0.3153 -0.0299 -0.0362 0.0127  1128 ILE B CA  
16968 C C   . ILE B 1130 ? 0.3047 0.2546 0.3402 -0.0383 -0.0368 0.0162  1128 ILE B C   
16969 O O   . ILE B 1130 ? 0.3328 0.2771 0.3685 -0.0421 -0.0406 0.0158  1128 ILE B O   
16970 C CB  . ILE B 1130 ? 0.3380 0.2669 0.3606 -0.0284 -0.0397 0.0143  1128 ILE B CB  
16971 C CG1 . ILE B 1130 ? 0.3069 0.2311 0.3248 -0.0196 -0.0392 0.0106  1128 ILE B CG1 
16972 C CG2 . ILE B 1130 ? 0.2959 0.2264 0.3180 -0.0319 -0.0386 0.0196  1128 ILE B CG2 
16973 C CD1 . ILE B 1130 ? 0.3490 0.2564 0.3587 -0.0172 -0.0436 0.0110  1128 ILE B CD1 
16974 N N   . ASP B 1131 ? 0.2871 0.2487 0.3269 -0.0411 -0.0331 0.0194  1129 ASP B N   
16975 C CA  . ASP B 1131 ? 0.2961 0.2651 0.3411 -0.0491 -0.0330 0.0232  1129 ASP B CA  
16976 C C   . ASP B 1131 ? 0.3193 0.2757 0.3602 -0.0550 -0.0378 0.0271  1129 ASP B C   
16977 O O   . ASP B 1131 ? 0.3489 0.2977 0.3846 -0.0550 -0.0386 0.0302  1129 ASP B O   
16978 C CB  . ASP B 1131 ? 0.3040 0.2864 0.3524 -0.0500 -0.0281 0.0261  1129 ASP B CB  
16979 C CG  . ASP B 1131 ? 0.3194 0.3119 0.3737 -0.0579 -0.0272 0.0301  1129 ASP B CG  
16980 O OD1 . ASP B 1131 ? 0.3028 0.2979 0.3614 -0.0612 -0.0289 0.0292  1129 ASP B OD1 
16981 O OD2 . ASP B 1131 ? 0.3066 0.3046 0.3611 -0.0607 -0.0249 0.0343  1129 ASP B OD2 
16982 N N   . ALA B 1132 ? 0.3305 0.2843 0.3735 -0.0601 -0.0413 0.0272  1130 ALA B N   
16983 C CA  . ALA B 1132 ? 0.3542 0.2945 0.3928 -0.0662 -0.0466 0.0307  1130 ALA B CA  
16984 C C   . ALA B 1132 ? 0.3793 0.3250 0.4197 -0.0735 -0.0455 0.0373  1130 ALA B C   
16985 O O   . ALA B 1132 ? 0.4220 0.3553 0.4569 -0.0772 -0.0491 0.0410  1130 ALA B O   
16986 C CB  . ALA B 1132 ? 0.3575 0.2947 0.3982 -0.0703 -0.0507 0.0291  1130 ALA B CB  
16987 N N   . ALA B 1133 ? 0.3383 0.3020 0.3860 -0.0755 -0.0405 0.0388  1131 ALA B N   
16988 C CA  . ALA B 1133 ? 0.4019 0.3724 0.4514 -0.0822 -0.0389 0.0451  1131 ALA B CA  
16989 C C   . ALA B 1133 ? 0.3818 0.3467 0.4250 -0.0793 -0.0376 0.0475  1131 ALA B C   
16990 O O   . ALA B 1133 ? 0.3898 0.3568 0.4324 -0.0849 -0.0371 0.0532  1131 ALA B O   
16991 C CB  . ALA B 1133 ? 0.4004 0.3923 0.4588 -0.0837 -0.0335 0.0455  1131 ALA B CB  
16992 N N   . SER B 1134 ? 0.3931 0.3515 0.4317 -0.0708 -0.0372 0.0435  1132 SER B N   
16993 C CA  . SER B 1134 ? 0.3905 0.3422 0.4228 -0.0677 -0.0368 0.0457  1132 SER B CA  
16994 C C   . SER B 1134 ? 0.3607 0.2954 0.3860 -0.0721 -0.0422 0.0498  1132 SER B C   
16995 O O   . SER B 1134 ? 0.4039 0.3347 0.4248 -0.0726 -0.0421 0.0537  1132 SER B O   
16996 C CB  . SER B 1134 ? 0.3986 0.3463 0.4276 -0.0578 -0.0358 0.0404  1132 SER B CB  
16997 O OG  . SER B 1134 ? 0.3394 0.2721 0.3637 -0.0550 -0.0405 0.0372  1132 SER B OG  
16998 N N   . GLY B 1135 ? 0.3821 0.3061 0.4060 -0.0752 -0.0472 0.0489  1133 GLY B N   
16999 C CA  . GLY B 1135 ? 0.4086 0.3148 0.4254 -0.0792 -0.0531 0.0524  1133 GLY B CA  
17000 C C   . GLY B 1135 ? 0.4947 0.3847 0.5025 -0.0718 -0.0557 0.0506  1133 GLY B C   
17001 O O   . GLY B 1135 ? 0.4427 0.3180 0.4437 -0.0744 -0.0600 0.0542  1133 GLY B O   
17002 N N   . LEU B 1136 ? 0.4541 0.3463 0.4616 -0.0625 -0.0533 0.0451  1134 LEU B N   
17003 C CA  . LEU B 1136 ? 0.4683 0.3481 0.4681 -0.0546 -0.0550 0.0432  1134 LEU B CA  
17004 C C   . LEU B 1136 ? 0.4518 0.3170 0.4467 -0.0500 -0.0596 0.0383  1134 LEU B C   
17005 O O   . LEU B 1136 ? 0.4559 0.3147 0.4461 -0.0415 -0.0599 0.0349  1134 LEU B O   
17006 C CB  . LEU B 1136 ? 0.4175 0.3096 0.4199 -0.0474 -0.0495 0.0408  1134 LEU B CB  
17007 C CG  . LEU B 1136 ? 0.4118 0.3159 0.4170 -0.0506 -0.0453 0.0456  1134 LEU B CG  
17008 C CD1 . LEU B 1136 ? 0.3862 0.3045 0.3953 -0.0445 -0.0397 0.0424  1134 LEU B CD1 
17009 C CD2 . LEU B 1136 ? 0.4438 0.3360 0.4416 -0.0512 -0.0481 0.0503  1134 LEU B CD2 
17010 N N   . GLN B 1137 ? 0.4780 0.3381 0.4737 -0.0554 -0.0632 0.0378  1135 GLN B N   
17011 C CA  . GLN B 1137 ? 0.4787 0.3259 0.4697 -0.0511 -0.0674 0.0326  1135 GLN B CA  
17012 C C   . GLN B 1137 ? 0.5453 0.3728 0.5261 -0.0462 -0.0720 0.0324  1135 GLN B C   
17013 O O   . GLN B 1137 ? 0.5953 0.4154 0.5717 -0.0381 -0.0732 0.0271  1135 GLN B O   
17014 C CB  . GLN B 1137 ? 0.4770 0.3212 0.4701 -0.0590 -0.0712 0.0331  1135 GLN B CB  
17015 C CG  . GLN B 1137 ? 0.4867 0.3487 0.4895 -0.0614 -0.0675 0.0311  1135 GLN B CG  
17016 C CD  . GLN B 1137 ? 0.4593 0.3381 0.4699 -0.0683 -0.0633 0.0362  1135 GLN B CD  
17017 O OE1 . GLN B 1137 ? 0.4864 0.3659 0.4955 -0.0700 -0.0620 0.0407  1135 GLN B OE1 
17018 N NE2 . GLN B 1137 ? 0.4232 0.3155 0.4419 -0.0720 -0.0614 0.0354  1135 GLN B NE2 
17019 N N   . ALA B 1138 ? 0.5218 0.3406 0.4983 -0.0508 -0.0746 0.0380  1136 ALA B N   
17020 C CA  . ALA B 1138 ? 0.5688 0.3676 0.5351 -0.0463 -0.0796 0.0380  1136 ALA B CA  
17021 C C   . ALA B 1138 ? 0.5793 0.3803 0.5433 -0.0362 -0.0766 0.0360  1136 ALA B C   
17022 O O   . ALA B 1138 ? 0.5825 0.3678 0.5382 -0.0306 -0.0804 0.0351  1136 ALA B O   
17023 C CB  . ALA B 1138 ? 0.4989 0.2878 0.4613 -0.0545 -0.0835 0.0451  1136 ALA B CB  
17024 N N   . SER B 1139 ? 0.5667 0.3864 0.5376 -0.0338 -0.0701 0.0354  1137 SER B N   
17025 C CA  . SER B 1139 ? 0.5389 0.3621 0.5083 -0.0247 -0.0672 0.0337  1137 SER B CA  
17026 C C   . SER B 1139 ? 0.5010 0.3221 0.4687 -0.0153 -0.0670 0.0268  1137 SER B C   
17027 O O   . SER B 1139 ? 0.5307 0.3520 0.4959 -0.0072 -0.0657 0.0251  1137 SER B O   
17028 C CB  . SER B 1139 ? 0.4915 0.3351 0.4685 -0.0259 -0.0606 0.0354  1137 SER B CB  
17029 O OG  . SER B 1139 ? 0.5192 0.3649 0.4967 -0.0330 -0.0603 0.0419  1137 SER B OG  
17030 N N   . LEU B 1140 ? 0.4944 0.3147 0.4636 -0.0163 -0.0682 0.0229  1138 LEU B N   
17031 C CA  . LEU B 1140 ? 0.5719 0.3906 0.5393 -0.0079 -0.0680 0.0164  1138 LEU B CA  
17032 C C   . LEU B 1140 ? 0.5262 0.3250 0.4853 -0.0065 -0.0745 0.0140  1138 LEU B C   
17033 O O   . LEU B 1140 ? 0.6102 0.4070 0.5686 -0.0042 -0.0755 0.0092  1138 LEU B O   
17034 C CB  . LEU B 1140 ? 0.5021 0.3363 0.4773 -0.0091 -0.0639 0.0134  1138 LEU B CB  
17035 C CG  . LEU B 1140 ? 0.5037 0.3570 0.4864 -0.0093 -0.0575 0.0149  1138 LEU B CG  
17036 C CD1 . LEU B 1140 ? 0.5068 0.3737 0.4961 -0.0086 -0.0539 0.0111  1138 LEU B CD1 
17037 C CD2 . LEU B 1140 ? 0.4839 0.3385 0.4640 -0.0017 -0.0556 0.0148  1138 LEU B CD2 
17038 N N   . LYS B 1141 ? 0.5784 0.3618 0.5307 -0.0081 -0.0792 0.0174  1139 LYS B N   
17039 C CA  . LYS B 1141 ? 0.6173 0.3795 0.5604 -0.0066 -0.0859 0.0153  1139 LYS B CA  
17040 C C   . LYS B 1141 ? 0.6537 0.4099 0.5911 0.0055  -0.0863 0.0096  1139 LYS B C   
17041 O O   . LYS B 1141 ? 0.6650 0.4248 0.6017 0.0120  -0.0839 0.0100  1139 LYS B O   
17042 C CB  . LYS B 1141 ? 0.6088 0.3558 0.5458 -0.0117 -0.0910 0.0209  1139 LYS B CB  
17043 N N   . ASN B 1142 ? 0.6687 0.4162 0.6020 0.0085  -0.0892 0.0044  1140 ASN B N   
17044 C CA  . ASN B 1142 ? 0.7019 0.4414 0.6284 0.0198  -0.0904 -0.0012 1140 ASN B CA  
17045 C C   . ASN B 1142 ? 0.6280 0.3855 0.5600 0.0273  -0.0837 -0.0039 1140 ASN B C   
17046 O O   . ASN B 1142 ? 0.6159 0.3719 0.5444 0.0363  -0.0830 -0.0057 1140 ASN B O   
17047 C CB  . ASN B 1142 ? 0.7185 0.4400 0.6357 0.0242  -0.0952 0.0004  1140 ASN B CB  
17048 N N   . LEU B 1143 ? 0.6289 0.4036 0.5697 0.0233  -0.0790 -0.0042 1141 LEU B N   
17049 C CA  . LEU B 1143 ? 0.6277 0.4190 0.5736 0.0295  -0.0730 -0.0072 1141 LEU B CA  
17050 C C   . LEU B 1143 ? 0.5892 0.3752 0.5298 0.0383  -0.0740 -0.0136 1141 LEU B C   
17051 O O   . LEU B 1143 ? 0.6302 0.4045 0.5659 0.0373  -0.0782 -0.0164 1141 LEU B O   
17052 C CB  . LEU B 1143 ? 0.5620 0.3704 0.5174 0.0231  -0.0687 -0.0064 1141 LEU B CB  
17053 C CG  . LEU B 1143 ? 0.5389 0.3629 0.5023 0.0185  -0.0639 -0.0019 1141 LEU B CG  
17054 C CD1 . LEU B 1143 ? 0.4997 0.3390 0.4711 0.0148  -0.0601 -0.0032 1141 LEU B CD1 
17055 C CD2 . LEU B 1143 ? 0.4888 0.3198 0.4526 0.0254  -0.0606 -0.0015 1141 LEU B CD2 
17056 N N   . PRO B 1144 ? 0.5869 0.3824 0.5286 0.0466  -0.0701 -0.0161 1142 PRO B N   
17057 C CA  . PRO B 1144 ? 0.5442 0.3392 0.4825 0.0543  -0.0697 -0.0221 1142 PRO B CA  
17058 C C   . PRO B 1144 ? 0.5550 0.3569 0.4973 0.0495  -0.0684 -0.0243 1142 PRO B C   
17059 O O   . PRO B 1144 ? 0.5649 0.3800 0.5154 0.0431  -0.0651 -0.0218 1142 PRO B O   
17060 C CB  . PRO B 1144 ? 0.5803 0.3894 0.5219 0.0617  -0.0645 -0.0229 1142 PRO B CB  
17061 C CG  . PRO B 1144 ? 0.5503 0.3599 0.4932 0.0603  -0.0644 -0.0178 1142 PRO B CG  
17062 C CD  . PRO B 1144 ? 0.5790 0.3861 0.5248 0.0494  -0.0659 -0.0133 1142 PRO B CD  
17063 N N   . GLN B 1145 ? 0.5647 0.3575 0.5011 0.0530  -0.0712 -0.0291 1143 GLN B N   
17064 C CA  . GLN B 1145 ? 0.5157 0.3137 0.4550 0.0489  -0.0707 -0.0314 1143 GLN B CA  
17065 C C   . GLN B 1145 ? 0.5139 0.3323 0.4615 0.0494  -0.0642 -0.0317 1143 GLN B C   
17066 O O   . GLN B 1145 ? 0.4777 0.3041 0.4310 0.0433  -0.0629 -0.0312 1143 GLN B O   
17067 C CB  . GLN B 1145 ? 0.6121 0.3980 0.5428 0.0543  -0.0742 -0.0371 1143 GLN B CB  
17068 N N   . THR B 1146 ? 0.5032 0.3300 0.4515 0.0566  -0.0605 -0.0325 1144 THR B N   
17069 C CA  . THR B 1146 ? 0.4822 0.3278 0.4380 0.0571  -0.0546 -0.0326 1144 THR B CA  
17070 C C   . THR B 1146 ? 0.4394 0.2954 0.4035 0.0493  -0.0521 -0.0277 1144 THR B C   
17071 O O   . THR B 1146 ? 0.4591 0.3275 0.4295 0.0460  -0.0488 -0.0277 1144 THR B O   
17072 C CB  . THR B 1146 ? 0.5067 0.3587 0.4614 0.0660  -0.0515 -0.0339 1144 THR B CB  
17073 O OG1 . THR B 1146 ? 0.4804 0.3263 0.4329 0.0678  -0.0530 -0.0310 1144 THR B OG1 
17074 C CG2 . THR B 1146 ? 0.5415 0.3877 0.4891 0.0740  -0.0527 -0.0393 1144 THR B CG2 
17075 N N   . VAL B 1147 ? 0.3904 0.2415 0.3543 0.0466  -0.0535 -0.0237 1145 VAL B N   
17076 C CA  . VAL B 1147 ? 0.4369 0.2977 0.4081 0.0393  -0.0512 -0.0191 1145 VAL B CA  
17077 C C   . VAL B 1147 ? 0.4279 0.2854 0.4012 0.0307  -0.0536 -0.0179 1145 VAL B C   
17078 O O   . VAL B 1147 ? 0.4277 0.2971 0.4082 0.0255  -0.0507 -0.0165 1145 VAL B O   
17079 C CB  . VAL B 1147 ? 0.4487 0.3065 0.4189 0.0394  -0.0516 -0.0149 1145 VAL B CB  
17080 C CG1 . VAL B 1147 ? 0.4278 0.2973 0.4054 0.0325  -0.0485 -0.0105 1145 VAL B CG1 
17081 C CG2 . VAL B 1147 ? 0.4160 0.2766 0.3840 0.0484  -0.0498 -0.0164 1145 VAL B CG2 
17082 N N   . GLY B 1148 ? 0.4413 0.2829 0.4084 0.0292  -0.0589 -0.0185 1146 GLY B N   
17083 C CA  . GLY B 1148 ? 0.4450 0.2835 0.4142 0.0207  -0.0617 -0.0172 1146 GLY B CA  
17084 C C   . GLY B 1148 ? 0.4500 0.2984 0.4239 0.0191  -0.0597 -0.0200 1146 GLY B C   
17085 O O   . GLY B 1148 ? 0.4484 0.3037 0.4284 0.0119  -0.0591 -0.0179 1146 GLY B O   
17086 N N   . LEU B 1149 ? 0.4022 0.2520 0.3733 0.0260  -0.0585 -0.0247 1147 LEU B N   
17087 C CA  . LEU B 1149 ? 0.4085 0.2666 0.3832 0.0248  -0.0570 -0.0274 1147 LEU B CA  
17088 C C   . LEU B 1149 ? 0.4193 0.2950 0.4031 0.0219  -0.0519 -0.0252 1147 LEU B C   
17089 O O   . LEU B 1149 ? 0.4075 0.2904 0.3957 0.0188  -0.0510 -0.0262 1147 LEU B O   
17090 C CB  . LEU B 1149 ? 0.4619 0.3183 0.4313 0.0330  -0.0565 -0.0325 1147 LEU B CB  
17091 N N   . ARG B 1150 ? 0.3600 0.2423 0.3466 0.0229  -0.0487 -0.0223 1148 ARG B N   
17092 C CA  . ARG B 1150 ? 0.3973 0.2954 0.3919 0.0202  -0.0441 -0.0203 1148 ARG B CA  
17093 C C   . ARG B 1150 ? 0.3746 0.2755 0.3740 0.0124  -0.0442 -0.0158 1148 ARG B C   
17094 O O   . ARG B 1150 ? 0.3470 0.2607 0.3530 0.0098  -0.0406 -0.0140 1148 ARG B O   
17095 C CB  . ARG B 1150 ? 0.3285 0.2336 0.3234 0.0258  -0.0404 -0.0198 1148 ARG B CB  
17096 C CG  . ARG B 1150 ? 0.3965 0.3050 0.3892 0.0327  -0.0385 -0.0239 1148 ARG B CG  
17097 C CD  . ARG B 1150 ? 0.3780 0.3007 0.3757 0.0344  -0.0337 -0.0229 1148 ARG B CD  
17098 N NE  . ARG B 1150 ? 0.3598 0.2859 0.3550 0.0414  -0.0319 -0.0258 1148 ARG B NE  
17099 C CZ  . ARG B 1150 ? 0.3884 0.3232 0.3855 0.0446  -0.0286 -0.0249 1148 ARG B CZ  
17100 N NH1 . ARG B 1150 ? 0.3110 0.2517 0.3121 0.0418  -0.0269 -0.0214 1148 ARG B NH1 
17101 N NH2 . ARG B 1150 ? 0.3531 0.2912 0.3479 0.0508  -0.0272 -0.0275 1148 ARG B NH2 
17102 N N   . VAL B 1151 ? 0.3667 0.2560 0.3628 0.0086  -0.0484 -0.0137 1149 VAL B N   
17103 C CA  . VAL B 1151 ? 0.3739 0.2654 0.3738 0.0013  -0.0486 -0.0088 1149 VAL B CA  
17104 C C   . VAL B 1151 ? 0.4117 0.3009 0.4138 -0.0057 -0.0517 -0.0084 1149 VAL B C   
17105 O O   . VAL B 1151 ? 0.3898 0.2666 0.3867 -0.0058 -0.0562 -0.0104 1149 VAL B O   
17106 C CB  . VAL B 1151 ? 0.4100 0.2903 0.4046 0.0015  -0.0511 -0.0058 1149 VAL B CB  
17107 C CG1 . VAL B 1151 ? 0.4238 0.3056 0.4218 -0.0071 -0.0518 -0.0005 1149 VAL B CG1 
17108 C CG2 . VAL B 1151 ? 0.3701 0.2546 0.3636 0.0081  -0.0479 -0.0057 1149 VAL B CG2 
17109 N N   . SER B 1152 ? 0.3638 0.2653 0.3736 -0.0113 -0.0492 -0.0060 1150 SER B N   
17110 C CA  . SER B 1152 ? 0.4201 0.3212 0.4331 -0.0189 -0.0520 -0.0045 1150 SER B CA  
17111 C C   . SER B 1152 ? 0.3979 0.3065 0.4160 -0.0254 -0.0503 0.0009  1150 SER B C   
17112 O O   . SER B 1152 ? 0.3576 0.2738 0.3775 -0.0237 -0.0464 0.0027  1150 SER B O   
17113 C CB  . SER B 1152 ? 0.3578 0.2681 0.3757 -0.0191 -0.0509 -0.0076 1150 SER B CB  
17114 O OG  . SER B 1152 ? 0.4011 0.3268 0.4253 -0.0179 -0.0456 -0.0073 1150 SER B OG  
17115 N N   . TRP B 1153 ? 0.3261 0.2324 0.3461 -0.0330 -0.0534 0.0034  1151 TRP B N   
17116 C CA  . TRP B 1153 ? 0.3419 0.2559 0.3670 -0.0400 -0.0520 0.0087  1151 TRP B CA  
17117 C C   . TRP B 1153 ? 0.3435 0.2704 0.3768 -0.0448 -0.0508 0.0087  1151 TRP B C   
17118 O O   . TRP B 1153 ? 0.3517 0.2753 0.3852 -0.0461 -0.0540 0.0062  1151 TRP B O   
17119 C CB  . TRP B 1153 ? 0.3509 0.2513 0.3711 -0.0456 -0.0568 0.0127  1151 TRP B CB  
17120 C CG  . TRP B 1153 ? 0.4518 0.3402 0.4642 -0.0408 -0.0579 0.0132  1151 TRP B CG  
17121 C CD1 . TRP B 1153 ? 0.4234 0.2975 0.4278 -0.0346 -0.0610 0.0096  1151 TRP B CD1 
17122 C CD2 . TRP B 1153 ? 0.4045 0.2947 0.4161 -0.0413 -0.0557 0.0175  1151 TRP B CD2 
17123 N NE1 . TRP B 1153 ? 0.4410 0.3081 0.4402 -0.0310 -0.0610 0.0114  1151 TRP B NE1 
17124 C CE2 . TRP B 1153 ? 0.4297 0.3061 0.4330 -0.0352 -0.0579 0.0163  1151 TRP B CE2 
17125 C CE3 . TRP B 1153 ? 0.4072 0.3093 0.4240 -0.0461 -0.0522 0.0221  1151 TRP B CE3 
17126 C CZ2 . TRP B 1153 ? 0.4510 0.3252 0.4514 -0.0340 -0.0569 0.0198  1151 TRP B CZ2 
17127 C CZ3 . TRP B 1153 ? 0.3694 0.2690 0.3828 -0.0451 -0.0512 0.0256  1151 TRP B CZ3 
17128 C CH2 . TRP B 1153 ? 0.4227 0.3084 0.4280 -0.0391 -0.0536 0.0244  1151 TRP B CH2 
17129 N N   . SER B 1154 ? 0.2952 0.2371 0.3352 -0.0472 -0.0464 0.0114  1152 SER B N   
17130 C CA  . SER B 1154 ? 0.3815 0.3375 0.4300 -0.0509 -0.0447 0.0114  1152 SER B CA  
17131 C C   . SER B 1154 ? 0.3251 0.2895 0.3786 -0.0586 -0.0437 0.0169  1152 SER B C   
17132 O O   . SER B 1154 ? 0.3415 0.3106 0.3951 -0.0585 -0.0404 0.0198  1152 SER B O   
17133 C CB  . SER B 1154 ? 0.3614 0.3299 0.4137 -0.0452 -0.0398 0.0083  1152 SER B CB  
17134 O OG  . SER B 1154 ? 0.3032 0.2844 0.3634 -0.0483 -0.0386 0.0081  1152 SER B OG  
17135 N N   . LYS B 1155 ? 0.3592 0.3263 0.4171 -0.0653 -0.0463 0.0184  1153 LYS B N   
17136 C CA  . LYS B 1155 ? 0.3357 0.3152 0.4004 -0.0726 -0.0447 0.0231  1153 LYS B CA  
17137 C C   . LYS B 1155 ? 0.3558 0.3534 0.4294 -0.0719 -0.0410 0.0215  1153 LYS B C   
17138 O O   . LYS B 1155 ? 0.4162 0.4268 0.4964 -0.0771 -0.0390 0.0249  1153 LYS B O   
17139 C CB  . LYS B 1155 ? 0.3399 0.3123 0.4045 -0.0812 -0.0501 0.0264  1153 LYS B CB  
17140 N N   . ASP B 1156 ? 0.3171 0.3159 0.3909 -0.0654 -0.0402 0.0163  1154 ASP B N   
17141 C CA  . ASP B 1156 ? 0.2948 0.3084 0.3763 -0.0645 -0.0378 0.0142  1154 ASP B CA  
17142 C C   . ASP B 1156 ? 0.2643 0.2786 0.3436 -0.0558 -0.0349 0.0095  1154 ASP B C   
17143 O O   . ASP B 1156 ? 0.2706 0.2781 0.3470 -0.0520 -0.0371 0.0056  1154 ASP B O   
17144 C CB  . ASP B 1156 ? 0.2881 0.3000 0.3723 -0.0683 -0.0424 0.0130  1154 ASP B CB  
17145 C CG  . ASP B 1156 ? 0.2354 0.2630 0.3281 -0.0675 -0.0404 0.0112  1154 ASP B CG  
17146 O OD1 . ASP B 1156 ? 0.2378 0.2752 0.3329 -0.0626 -0.0358 0.0097  1154 ASP B OD1 
17147 O OD2 . ASP B 1156 ? 0.2940 0.3238 0.3906 -0.0718 -0.0437 0.0113  1154 ASP B OD2 
17148 N N   . TRP B 1157 ? 0.2821 0.3046 0.3625 -0.0528 -0.0301 0.0102  1155 TRP B N   
17149 C CA  . TRP B 1157 ? 0.2998 0.3220 0.3773 -0.0451 -0.0275 0.0065  1155 TRP B CA  
17150 C C   . TRP B 1157 ? 0.3135 0.3425 0.3950 -0.0420 -0.0270 0.0025  1155 TRP B C   
17151 O O   . TRP B 1157 ? 0.2893 0.3130 0.3671 -0.0365 -0.0273 -0.0012 1155 TRP B O   
17152 C CB  . TRP B 1157 ? 0.2695 0.2998 0.3477 -0.0434 -0.0226 0.0082  1155 TRP B CB  
17153 C CG  . TRP B 1157 ? 0.2558 0.2809 0.3304 -0.0464 -0.0227 0.0125  1155 TRP B CG  
17154 C CD1 . TRP B 1157 ? 0.2476 0.2598 0.3173 -0.0495 -0.0266 0.0146  1155 TRP B CD1 
17155 C CD2 . TRP B 1157 ? 0.2594 0.2920 0.3344 -0.0464 -0.0187 0.0152  1155 TRP B CD2 
17156 N NE1 . TRP B 1157 ? 0.2529 0.2640 0.3201 -0.0515 -0.0253 0.0187  1155 TRP B NE1 
17157 C CE2 . TRP B 1157 ? 0.2566 0.2805 0.3270 -0.0498 -0.0204 0.0191  1155 TRP B CE2 
17158 C CE3 . TRP B 1157 ? 0.2500 0.2952 0.3283 -0.0438 -0.0141 0.0145  1155 TRP B CE3 
17159 C CZ2 . TRP B 1157 ? 0.2539 0.2819 0.3231 -0.0507 -0.0175 0.0225  1155 TRP B CZ2 
17160 C CZ3 . TRP B 1157 ? 0.2740 0.3232 0.3510 -0.0447 -0.0112 0.0176  1155 TRP B CZ3 
17161 C CH2 . TRP B 1157 ? 0.2585 0.2994 0.3311 -0.0481 -0.0128 0.0217  1155 TRP B CH2 
17162 N N   . ALA B 1158 ? 0.2903 0.3314 0.3793 -0.0452 -0.0263 0.0033  1156 ALA B N   
17163 C CA  . ALA B 1158 ? 0.3077 0.3558 0.4007 -0.0420 -0.0260 -0.0003 1156 ALA B CA  
17164 C C   . ALA B 1158 ? 0.2893 0.3277 0.3796 -0.0417 -0.0306 -0.0029 1156 ALA B C   
17165 O O   . ALA B 1158 ? 0.3367 0.3742 0.4258 -0.0369 -0.0307 -0.0067 1156 ALA B O   
17166 C CB  . ALA B 1158 ? 0.2563 0.3198 0.3580 -0.0454 -0.0244 0.0014  1156 ALA B CB  
17167 N N   . ALA B 1159 ? 0.2609 0.2917 0.3499 -0.0471 -0.0347 -0.0010 1157 ALA B N   
17168 C CA  . ALA B 1159 ? 0.3070 0.3280 0.3929 -0.0470 -0.0395 -0.0037 1157 ALA B CA  
17169 C C   . ALA B 1159 ? 0.3070 0.3135 0.3837 -0.0421 -0.0407 -0.0062 1157 ALA B C   
17170 O O   . ALA B 1159 ? 0.3073 0.3071 0.3807 -0.0397 -0.0435 -0.0095 1157 ALA B O   
17171 C CB  . ALA B 1159 ? 0.2919 0.3091 0.3792 -0.0547 -0.0440 -0.0008 1157 ALA B CB  
17172 N N   . ASP B 1160 ? 0.2725 0.2746 0.3450 -0.0403 -0.0386 -0.0047 1158 ASP B N   
17173 C CA  . ASP B 1160 ? 0.3145 0.3033 0.3785 -0.0357 -0.0398 -0.0068 1158 ASP B CA  
17174 C C   . ASP B 1160 ? 0.3266 0.3184 0.3888 -0.0286 -0.0361 -0.0096 1158 ASP B C   
17175 O O   . ASP B 1160 ? 0.3806 0.3632 0.4363 -0.0241 -0.0367 -0.0116 1158 ASP B O   
17176 C CB  . ASP B 1160 ? 0.3043 0.2851 0.3642 -0.0380 -0.0404 -0.0034 1158 ASP B CB  
17177 C CG  . ASP B 1160 ? 0.3553 0.3288 0.4147 -0.0449 -0.0452 -0.0009 1158 ASP B CG  
17178 O OD1 . ASP B 1160 ? 0.3988 0.3710 0.4596 -0.0470 -0.0485 -0.0026 1158 ASP B OD1 
17179 O OD2 . ASP B 1160 ? 0.3912 0.3603 0.4488 -0.0486 -0.0458 0.0029  1158 ASP B OD2 
17180 N N   . GLY B 1161 ? 0.3068 0.3114 0.3745 -0.0274 -0.0325 -0.0099 1159 GLY B N   
17181 C CA  . GLY B 1161 ? 0.2806 0.2881 0.3467 -0.0214 -0.0293 -0.0122 1159 GLY B CA  
17182 C C   . GLY B 1161 ? 0.3402 0.3458 0.4048 -0.0178 -0.0307 -0.0162 1159 GLY B C   
17183 O O   . GLY B 1161 ? 0.3072 0.3065 0.3702 -0.0192 -0.0345 -0.0175 1159 GLY B O   
17184 N N   . PRO B 1162 ? 0.3651 0.3759 0.4298 -0.0134 -0.0278 -0.0181 1160 PRO B N   
17185 C CA  . PRO B 1162 ? 0.3104 0.3285 0.3767 -0.0115 -0.0236 -0.0170 1160 PRO B CA  
17186 C C   . PRO B 1162 ? 0.2911 0.3026 0.3518 -0.0091 -0.0226 -0.0162 1160 PRO B C   
17187 O O   . PRO B 1162 ? 0.3229 0.3256 0.3781 -0.0063 -0.0243 -0.0179 1160 PRO B O   
17188 C CB  . PRO B 1162 ? 0.3490 0.3724 0.4163 -0.0077 -0.0222 -0.0198 1160 PRO B CB  
17189 C CG  . PRO B 1162 ? 0.3721 0.3872 0.4349 -0.0057 -0.0251 -0.0225 1160 PRO B CG  
17190 C CD  . PRO B 1162 ? 0.3659 0.3751 0.4287 -0.0098 -0.0289 -0.0216 1160 PRO B CD  
17191 N N   . PHE B 1163 ? 0.2731 0.2892 0.3351 -0.0098 -0.0199 -0.0137 1161 PHE B N   
17192 C CA  . PHE B 1163 ? 0.2620 0.2735 0.3193 -0.0071 -0.0187 -0.0129 1161 PHE B CA  
17193 C C   . PHE B 1163 ? 0.3023 0.3193 0.3592 -0.0028 -0.0156 -0.0146 1161 PHE B C   
17194 O O   . PHE B 1163 ? 0.2859 0.3099 0.3462 -0.0022 -0.0144 -0.0160 1161 PHE B O   
17195 C CB  . PHE B 1163 ? 0.2556 0.2679 0.3136 -0.0106 -0.0179 -0.0091 1161 PHE B CB  
17196 C CG  . PHE B 1163 ? 0.3133 0.3208 0.3721 -0.0158 -0.0211 -0.0071 1161 PHE B CG  
17197 C CD1 . PHE B 1163 ? 0.3134 0.3087 0.3672 -0.0156 -0.0247 -0.0076 1161 PHE B CD1 
17198 C CD2 . PHE B 1163 ? 0.2598 0.2753 0.3244 -0.0208 -0.0206 -0.0048 1161 PHE B CD2 
17199 C CE1 . PHE B 1163 ? 0.3013 0.2913 0.3553 -0.0208 -0.0281 -0.0057 1161 PHE B CE1 
17200 C CE2 . PHE B 1163 ? 0.2914 0.3027 0.3568 -0.0262 -0.0238 -0.0027 1161 PHE B CE2 
17201 C CZ  . PHE B 1163 ? 0.2885 0.2866 0.3485 -0.0263 -0.0276 -0.0031 1161 PHE B CZ  
17202 N N   . ALA B 1164 ? 0.2880 0.3015 0.3408 0.0002  -0.0147 -0.0143 1162 ALA B N   
17203 C CA  . ALA B 1164 ? 0.2983 0.3162 0.3503 0.0040  -0.0122 -0.0156 1162 ALA B CA  
17204 C C   . ALA B 1164 ? 0.3214 0.3435 0.3735 0.0039  -0.0097 -0.0133 1162 ALA B C   
17205 O O   . ALA B 1164 ? 0.3678 0.3927 0.4185 0.0068  -0.0079 -0.0140 1162 ALA B O   
17206 C CB  . ALA B 1164 ? 0.2707 0.2822 0.3177 0.0082  -0.0132 -0.0177 1162 ALA B CB  
17207 N N   . GLY B 1165 ? 0.2657 0.2883 0.3192 0.0004  -0.0096 -0.0104 1163 GLY B N   
17208 C CA  . GLY B 1165 ? 0.2416 0.2675 0.2946 0.0000  -0.0075 -0.0079 1163 GLY B CA  
17209 C C   . GLY B 1165 ? 0.2700 0.2926 0.3229 -0.0040 -0.0087 -0.0045 1163 GLY B C   
17210 O O   . GLY B 1165 ? 0.2585 0.2750 0.3111 -0.0062 -0.0114 -0.0042 1163 GLY B O   
17211 N N   . ALA B 1166 ? 0.2483 0.2748 0.3011 -0.0052 -0.0067 -0.0018 1164 ALA B N   
17212 C CA  . ALA B 1166 ? 0.2081 0.2319 0.2606 -0.0094 -0.0077 0.0020  1164 ALA B CA  
17213 C C   . ALA B 1166 ? 0.2561 0.2794 0.3053 -0.0084 -0.0064 0.0045  1164 ALA B C   
17214 O O   . ALA B 1166 ? 0.2605 0.2903 0.3099 -0.0063 -0.0038 0.0039  1164 ALA B O   
17215 C CB  . ALA B 1166 ? 0.2269 0.2591 0.2845 -0.0141 -0.0065 0.0035  1164 ALA B CB  
17216 N N   . LEU B 1167 ? 0.2387 0.2538 0.2845 -0.0100 -0.0085 0.0072  1165 LEU B N   
17217 C CA  . LEU B 1167 ? 0.2283 0.2420 0.2708 -0.0098 -0.0079 0.0104  1165 LEU B CA  
17218 C C   . LEU B 1167 ? 0.2860 0.2996 0.3292 -0.0157 -0.0085 0.0147  1165 LEU B C   
17219 O O   . LEU B 1167 ? 0.2407 0.2476 0.2836 -0.0189 -0.0113 0.0156  1165 LEU B O   
17220 C CB  . LEU B 1167 ? 0.2713 0.2743 0.3085 -0.0059 -0.0104 0.0100  1165 LEU B CB  
17221 C CG  . LEU B 1167 ? 0.2153 0.2183 0.2516 0.0000  -0.0101 0.0060  1165 LEU B CG  
17222 C CD1 . LEU B 1167 ? 0.2954 0.2884 0.3265 0.0039  -0.0125 0.0060  1165 LEU B CD1 
17223 C CD2 . LEU B 1167 ? 0.2682 0.2810 0.3059 0.0018  -0.0068 0.0055  1165 LEU B CD2 
17224 N N   . VAL B 1168 ? 0.2792 0.2999 0.3228 -0.0175 -0.0059 0.0173  1166 VAL B N   
17225 C CA  . VAL B 1168 ? 0.2587 0.2818 0.3035 -0.0235 -0.0057 0.0216  1166 VAL B CA  
17226 C C   . VAL B 1168 ? 0.2773 0.2981 0.3176 -0.0239 -0.0054 0.0254  1166 VAL B C   
17227 O O   . VAL B 1168 ? 0.2869 0.3112 0.3256 -0.0204 -0.0035 0.0248  1166 VAL B O   
17228 C CB  . VAL B 1168 ? 0.2712 0.3079 0.3217 -0.0259 -0.0024 0.0212  1166 VAL B CB  
17229 C CG1 . VAL B 1168 ? 0.2701 0.3105 0.3222 -0.0325 -0.0021 0.0259  1166 VAL B CG1 
17230 C CG2 . VAL B 1168 ? 0.2599 0.2991 0.3147 -0.0247 -0.0028 0.0171  1166 VAL B CG2 
17231 N N   . GLU B 1169 ? 0.2860 0.3002 0.3242 -0.0284 -0.0077 0.0296  1167 GLU B N   
17232 C CA  . GLU B 1169 ? 0.3189 0.3305 0.3527 -0.0298 -0.0077 0.0340  1167 GLU B CA  
17233 C C   . GLU B 1169 ? 0.3122 0.3303 0.3480 -0.0368 -0.0064 0.0385  1167 GLU B C   
17234 O O   . GLU B 1169 ? 0.3297 0.3466 0.3681 -0.0416 -0.0080 0.0398  1167 GLU B O   
17235 C CB  . GLU B 1169 ? 0.2912 0.2875 0.3192 -0.0287 -0.0121 0.0355  1167 GLU B CB  
17236 C CG  . GLU B 1169 ? 0.3336 0.3260 0.3566 -0.0300 -0.0127 0.0403  1167 GLU B CG  
17237 C CD  . GLU B 1169 ? 0.3485 0.3251 0.3661 -0.0305 -0.0175 0.0426  1167 GLU B CD  
17238 O OE1 . GLU B 1169 ? 0.3761 0.3450 0.3939 -0.0309 -0.0204 0.0407  1167 GLU B OE1 
17239 O OE2 . GLU B 1169 ? 0.3736 0.3449 0.3863 -0.0306 -0.0187 0.0463  1167 GLU B OE2 
17240 N N   . GLY B 1170 ? 0.3051 0.3306 0.3397 -0.0374 -0.0035 0.0410  1168 GLY B N   
17241 C CA  . GLY B 1170 ? 0.3493 0.3816 0.3853 -0.0439 -0.0019 0.0457  1168 GLY B CA  
17242 C C   . GLY B 1170 ? 0.3537 0.3972 0.3892 -0.0430 0.0022  0.0465  1168 GLY B C   
17243 O O   . GLY B 1170 ? 0.3361 0.3817 0.3702 -0.0375 0.0036  0.0435  1168 GLY B O   
17244 N N   . ASP B 1171 ? 0.3364 0.3875 0.3729 -0.0487 0.0041  0.0508  1169 ASP B N   
17245 C CA  . ASP B 1171 ? 0.3463 0.4094 0.3825 -0.0482 0.0084  0.0515  1169 ASP B CA  
17246 C C   . ASP B 1171 ? 0.3951 0.4710 0.4373 -0.0463 0.0119  0.0472  1169 ASP B C   
17247 O O   . ASP B 1171 ? 0.3366 0.4122 0.3833 -0.0455 0.0109  0.0439  1169 ASP B O   
17248 C CB  . ASP B 1171 ? 0.3779 0.4443 0.4121 -0.0548 0.0092  0.0580  1169 ASP B CB  
17249 C CG  . ASP B 1171 ? 0.4103 0.4816 0.4497 -0.0615 0.0092  0.0604  1169 ASP B CG  
17250 O OD1 . ASP B 1171 ? 0.3837 0.4600 0.4291 -0.0610 0.0097  0.0569  1169 ASP B OD1 
17251 O OD2 . ASP B 1171 ? 0.5189 0.5892 0.5564 -0.0678 0.0086  0.0663  1169 ASP B OD2 
17252 N N   . ALA B 1172 ? 0.3767 0.4636 0.4184 -0.0454 0.0158  0.0471  1170 ALA B N   
17253 C CA  . ALA B 1172 ? 0.3806 0.4793 0.4271 -0.0427 0.0190  0.0427  1170 ALA B CA  
17254 C C   . ALA B 1172 ? 0.3548 0.4600 0.4082 -0.0466 0.0193  0.0429  1170 ALA B C   
17255 O O   . ALA B 1172 ? 0.3570 0.4647 0.4149 -0.0439 0.0194  0.0384  1170 ALA B O   
17256 C CB  . ALA B 1172 ? 0.3434 0.4528 0.3877 -0.0419 0.0230  0.0433  1170 ALA B CB  
17257 N N   . GLU B 1173 ? 0.3498 0.4578 0.4041 -0.0532 0.0194  0.0482  1171 GLU B N   
17258 C CA  . GLU B 1173 ? 0.3283 0.4436 0.3896 -0.0574 0.0196  0.0487  1171 GLU B CA  
17259 C C   . GLU B 1173 ? 0.3068 0.4118 0.3704 -0.0573 0.0154  0.0465  1171 GLU B C   
17260 O O   . GLU B 1173 ? 0.3171 0.4275 0.3866 -0.0568 0.0155  0.0435  1171 GLU B O   
17261 C CB  . GLU B 1173 ? 0.4151 0.5350 0.4766 -0.0651 0.0202  0.0553  1171 GLU B CB  
17262 N N   . ARG B 1174 ? 0.3429 0.4329 0.4015 -0.0576 0.0115  0.0480  1172 ARG B N   
17263 C CA  . ARG B 1174 ? 0.3437 0.4231 0.4035 -0.0571 0.0074  0.0457  1172 ARG B CA  
17264 C C   . ARG B 1174 ? 0.2740 0.3538 0.3355 -0.0503 0.0078  0.0392  1172 ARG B C   
17265 O O   . ARG B 1174 ? 0.2732 0.3526 0.3389 -0.0501 0.0063  0.0365  1172 ARG B O   
17266 C CB  . ARG B 1174 ? 0.3319 0.3951 0.3851 -0.0578 0.0033  0.0483  1172 ARG B CB  
17267 C CG  . ARG B 1174 ? 0.3092 0.3602 0.3623 -0.0565 -0.0011 0.0456  1172 ARG B CG  
17268 C CD  . ARG B 1174 ? 0.3316 0.3843 0.3897 -0.0626 -0.0029 0.0470  1172 ARG B CD  
17269 N NE  . ARG B 1174 ? 0.3501 0.3903 0.4072 -0.0612 -0.0073 0.0443  1172 ARG B NE  
17270 C CZ  . ARG B 1174 ? 0.3668 0.4077 0.4284 -0.0643 -0.0094 0.0433  1172 ARG B CZ  
17271 N NH1 . ARG B 1174 ? 0.3182 0.3722 0.3864 -0.0689 -0.0074 0.0448  1172 ARG B NH1 
17272 N NH2 . ARG B 1174 ? 0.3501 0.3786 0.4096 -0.0625 -0.0134 0.0406  1172 ARG B NH2 
17273 N N   . ILE B 1175 ? 0.2921 0.3730 0.3505 -0.0449 0.0098  0.0369  1173 ILE B N   
17274 C CA  . ILE B 1175 ? 0.2916 0.3719 0.3508 -0.0386 0.0100  0.0312  1173 ILE B CA  
17275 C C   . ILE B 1175 ? 0.2891 0.3816 0.3547 -0.0380 0.0124  0.0282  1173 ILE B C   
17276 O O   . ILE B 1175 ? 0.2355 0.3265 0.3040 -0.0356 0.0112  0.0244  1173 ILE B O   
17277 C CB  . ILE B 1175 ? 0.3078 0.3871 0.3621 -0.0338 0.0114  0.0300  1173 ILE B CB  
17278 C CG1 . ILE B 1175 ? 0.2930 0.3593 0.3415 -0.0331 0.0084  0.0320  1173 ILE B CG1 
17279 C CG2 . ILE B 1175 ? 0.2834 0.3649 0.3390 -0.0281 0.0123  0.0244  1173 ILE B CG2 
17280 C CD1 . ILE B 1175 ? 0.3131 0.3795 0.3568 -0.0295 0.0096  0.0320  1173 ILE B CD1 
17281 N N   . ARG B 1176 ? 0.2865 0.3911 0.3540 -0.0399 0.0159  0.0299  1174 ARG B N   
17282 C CA  . ARG B 1176 ? 0.2871 0.4040 0.3606 -0.0388 0.0184  0.0271  1174 ARG B CA  
17283 C C   . ARG B 1176 ? 0.2754 0.3933 0.3548 -0.0425 0.0163  0.0275  1174 ARG B C   
17284 O O   . ARG B 1176 ? 0.2705 0.3917 0.3541 -0.0399 0.0161  0.0236  1174 ARG B O   
17285 C CB  . ARG B 1176 ? 0.3208 0.4507 0.3948 -0.0403 0.0226  0.0294  1174 ARG B CB  
17286 C CG  . ARG B 1176 ? 0.3369 0.4808 0.4170 -0.0390 0.0254  0.0268  1174 ARG B CG  
17287 C CD  . ARG B 1176 ? 0.4355 0.5928 0.5159 -0.0410 0.0296  0.0296  1174 ARG B CD  
17288 N NE  . ARG B 1176 ? 0.5078 0.6654 0.5823 -0.0368 0.0318  0.0283  1174 ARG B NE  
17289 C CZ  . ARG B 1176 ? 0.5820 0.7389 0.6512 -0.0390 0.0330  0.0321  1174 ARG B CZ  
17290 N NH1 . ARG B 1176 ? 0.6319 0.7879 0.7008 -0.0454 0.0323  0.0378  1174 ARG B NH1 
17291 N NH2 . ARG B 1176 ? 0.4844 0.6411 0.5481 -0.0348 0.0346  0.0303  1174 ARG B NH2 
17292 N N   . ALA B 1177 ? 0.2562 0.3704 0.3355 -0.0487 0.0143  0.0322  1175 ALA B N   
17293 C CA  . ALA B 1177 ? 0.2693 0.3841 0.3540 -0.0531 0.0119  0.0331  1175 ALA B CA  
17294 C C   . ALA B 1177 ? 0.2412 0.3444 0.3253 -0.0503 0.0080  0.0293  1175 ALA B C   
17295 O O   . ALA B 1177 ? 0.2585 0.3651 0.3477 -0.0502 0.0070  0.0269  1175 ALA B O   
17296 C CB  . ALA B 1177 ? 0.2664 0.3780 0.3499 -0.0607 0.0102  0.0393  1175 ALA B CB  
17297 N N   . VAL B 1178 ? 0.3010 0.3910 0.3788 -0.0477 0.0059  0.0288  1176 VAL B N   
17298 C CA  . VAL B 1178 ? 0.2823 0.3617 0.3589 -0.0445 0.0026  0.0251  1176 VAL B CA  
17299 C C   . VAL B 1178 ? 0.2837 0.3683 0.3623 -0.0384 0.0043  0.0198  1176 VAL B C   
17300 O O   . VAL B 1178 ? 0.2589 0.3421 0.3403 -0.0371 0.0025  0.0167  1176 VAL B O   
17301 C CB  . VAL B 1178 ? 0.2504 0.3156 0.3197 -0.0427 0.0002  0.0259  1176 VAL B CB  
17302 C CG1 . VAL B 1178 ? 0.2464 0.3020 0.3139 -0.0382 -0.0025 0.0216  1176 VAL B CG1 
17303 C CG2 . VAL B 1178 ? 0.2948 0.3526 0.3616 -0.0488 -0.0025 0.0311  1176 VAL B CG2 
17304 N N   . ASN B 1179 ? 0.2593 0.3496 0.3363 -0.0348 0.0076  0.0187  1177 ASN B N   
17305 C CA  . ASN B 1179 ? 0.2671 0.3619 0.3455 -0.0294 0.0092  0.0139  1177 ASN B CA  
17306 C C   . ASN B 1179 ? 0.2506 0.3554 0.3358 -0.0301 0.0099  0.0123  1177 ASN B C   
17307 O O   . ASN B 1179 ? 0.2654 0.3694 0.3524 -0.0268 0.0088  0.0084  1177 ASN B O   
17308 C CB  . ASN B 1179 ? 0.2802 0.3802 0.3556 -0.0264 0.0125  0.0136  1177 ASN B CB  
17309 C CG  . ASN B 1179 ? 0.3024 0.4015 0.3765 -0.0204 0.0130  0.0088  1177 ASN B CG  
17310 O OD1 . ASN B 1179 ? 0.2938 0.3852 0.3669 -0.0182 0.0106  0.0064  1177 ASN B OD1 
17311 N ND2 . ASN B 1179 ? 0.3050 0.4118 0.3785 -0.0179 0.0160  0.0076  1177 ASN B ND2 
17312 N N   . LYS B 1180 ? 0.3044 0.4193 0.3936 -0.0344 0.0116  0.0153  1178 LYS B N   
17313 C CA  . LYS B 1180 ? 0.2378 0.3635 0.3342 -0.0352 0.0123  0.0141  1178 LYS B CA  
17314 C C   . LYS B 1180 ? 0.2308 0.3506 0.3299 -0.0375 0.0083  0.0135  1178 LYS B C   
17315 O O   . LYS B 1180 ? 0.2299 0.3530 0.3329 -0.0351 0.0075  0.0102  1178 LYS B O   
17316 C CB  . LYS B 1180 ? 0.2412 0.3796 0.3412 -0.0397 0.0151  0.0180  1178 LYS B CB  
17317 N N   . ALA B 1181 ? 0.2670 0.3773 0.3637 -0.0420 0.0053  0.0167  1179 ALA B N   
17318 C CA  . ALA B 1181 ? 0.2434 0.3464 0.3416 -0.0441 0.0010  0.0159  1179 ALA B CA  
17319 C C   . ALA B 1181 ? 0.2605 0.3552 0.3560 -0.0384 -0.0007 0.0111  1179 ALA B C   
17320 O O   . ALA B 1181 ? 0.2399 0.3345 0.3386 -0.0379 -0.0029 0.0087  1179 ALA B O   
17321 C CB  . ALA B 1181 ? 0.2877 0.3800 0.3823 -0.0494 -0.0020 0.0200  1179 ALA B CB  
17322 N N   . ILE B 1182 ? 0.2245 0.3124 0.3142 -0.0341 0.0001  0.0098  1180 ILE B N   
17323 C CA  . ILE B 1182 ? 0.2224 0.3030 0.3093 -0.0289 -0.0013 0.0055  1180 ILE B CA  
17324 C C   . ILE B 1182 ? 0.2172 0.3066 0.3079 -0.0251 0.0004  0.0019  1180 ILE B C   
17325 O O   . ILE B 1182 ? 0.2636 0.3496 0.3547 -0.0226 -0.0015 -0.0013 1180 ILE B O   
17326 C CB  . ILE B 1182 ? 0.2463 0.3193 0.3265 -0.0254 -0.0006 0.0054  1180 ILE B CB  
17327 C CG1 . ILE B 1182 ? 0.2479 0.3091 0.3237 -0.0280 -0.0035 0.0080  1180 ILE B CG1 
17328 C CG2 . ILE B 1182 ? 0.2673 0.3370 0.3454 -0.0197 -0.0008 0.0010  1180 ILE B CG2 
17329 C CD1 . ILE B 1182 ? 0.2833 0.3383 0.3531 -0.0251 -0.0028 0.0087  1180 ILE B CD1 
17330 N N   . ALA B 1183 ? 0.2378 0.3383 0.3310 -0.0245 0.0039  0.0023  1181 ALA B N   
17331 C CA  . ALA B 1183 ? 0.2912 0.3998 0.3879 -0.0206 0.0053  -0.0012 1181 ALA B CA  
17332 C C   . ALA B 1183 ? 0.3261 0.4400 0.4291 -0.0224 0.0036  -0.0020 1181 ALA B C   
17333 O O   . ALA B 1183 ? 0.3460 0.4634 0.4512 -0.0187 0.0035  -0.0053 1181 ALA B O   
17334 C CB  . ALA B 1183 ? 0.3162 0.4354 0.4138 -0.0194 0.0094  -0.0007 1181 ALA B CB  
17335 N N   . ALA B 1184 ? 0.2838 0.3982 0.3896 -0.0281 0.0019  0.0012  1182 ALA B N   
17336 C CA  . ALA B 1184 ? 0.2516 0.3711 0.3636 -0.0303 -0.0002 0.0008  1182 ALA B CA  
17337 C C   . ALA B 1184 ? 0.2718 0.3798 0.3817 -0.0304 -0.0046 -0.0010 1182 ALA B C   
17338 O O   . ALA B 1184 ? 0.2639 0.3749 0.3785 -0.0322 -0.0070 -0.0015 1182 ALA B O   
17339 C CB  . ALA B 1184 ? 0.2831 0.4100 0.3997 -0.0371 -0.0001 0.0053  1182 ALA B CB  
17340 N N   . LEU B 1185 ? 0.2464 0.3419 0.3495 -0.0284 -0.0058 -0.0018 1183 LEU B N   
17341 C CA  . LEU B 1185 ? 0.2877 0.3723 0.3881 -0.0282 -0.0098 -0.0035 1183 LEU B CA  
17342 C C   . LEU B 1185 ? 0.3271 0.4132 0.4287 -0.0235 -0.0104 -0.0077 1183 LEU B C   
17343 O O   . LEU B 1185 ? 0.2825 0.3722 0.3833 -0.0191 -0.0078 -0.0097 1183 LEU B O   
17344 C CB  . LEU B 1185 ? 0.2956 0.3672 0.3884 -0.0266 -0.0107 -0.0034 1183 LEU B CB  
17345 C CG  . LEU B 1185 ? 0.2659 0.3323 0.3557 -0.0306 -0.0110 0.0006  1183 LEU B CG  
17346 C CD1 . LEU B 1185 ? 0.2451 0.2993 0.3275 -0.0274 -0.0118 -0.0002 1183 LEU B CD1 
17347 C CD2 . LEU B 1185 ? 0.2647 0.3288 0.3569 -0.0367 -0.0143 0.0030  1183 LEU B CD2 
17348 N N   . PRO B 1186 ? 0.2995 0.3824 0.4025 -0.0245 -0.0139 -0.0091 1184 PRO B N   
17349 C CA  . PRO B 1186 ? 0.3150 0.3984 0.4184 -0.0202 -0.0148 -0.0128 1184 PRO B CA  
17350 C C   . PRO B 1186 ? 0.2914 0.3646 0.3878 -0.0159 -0.0150 -0.0151 1184 PRO B C   
17351 O O   . PRO B 1186 ? 0.3710 0.4352 0.4622 -0.0164 -0.0156 -0.0142 1184 PRO B O   
17352 C CB  . PRO B 1186 ? 0.3593 0.4414 0.4656 -0.0233 -0.0188 -0.0130 1184 PRO B CB  
17353 C CG  . PRO B 1186 ? 0.3710 0.4444 0.4743 -0.0280 -0.0209 -0.0104 1184 PRO B CG  
17354 C CD  . PRO B 1186 ? 0.3029 0.3803 0.4063 -0.0297 -0.0176 -0.0072 1184 PRO B CD  
17355 N N   . GLY B 1187 ? 0.3089 0.3833 0.4049 -0.0116 -0.0148 -0.0182 1185 GLY B N   
17356 C CA  . GLY B 1187 ? 0.3350 0.4007 0.4247 -0.0078 -0.0153 -0.0203 1185 GLY B CA  
17357 C C   . GLY B 1187 ? 0.3051 0.3713 0.3917 -0.0050 -0.0120 -0.0202 1185 GLY B C   
17358 O O   . GLY B 1187 ? 0.3772 0.4514 0.4665 -0.0039 -0.0094 -0.0202 1185 GLY B O   
17359 N N   . PRO B 1188 ? 0.3249 0.3829 0.4058 -0.0037 -0.0120 -0.0202 1186 PRO B N   
17360 C CA  . PRO B 1188 ? 0.3448 0.4031 0.4225 -0.0009 -0.0093 -0.0203 1186 PRO B CA  
17361 C C   . PRO B 1188 ? 0.3566 0.4204 0.4359 -0.0026 -0.0067 -0.0178 1186 PRO B C   
17362 O O   . PRO B 1188 ? 0.3587 0.4227 0.4394 -0.0062 -0.0070 -0.0153 1186 PRO B O   
17363 C CB  . PRO B 1188 ? 0.3627 0.4113 0.4345 0.0005  -0.0104 -0.0205 1186 PRO B CB  
17364 C CG  . PRO B 1188 ? 0.3650 0.4086 0.4369 -0.0028 -0.0130 -0.0192 1186 PRO B CG  
17365 C CD  . PRO B 1188 ? 0.3458 0.3939 0.4227 -0.0048 -0.0146 -0.0199 1186 PRO B CD  
17366 N N   . LEU B 1189 ? 0.3281 0.3960 0.4066 -0.0001 -0.0042 -0.0185 1187 LEU B N   
17367 C CA  . LEU B 1189 ? 0.3561 0.4287 0.4347 -0.0009 -0.0014 -0.0164 1187 LEU B CA  
17368 C C   . LEU B 1189 ? 0.3780 0.4436 0.4516 -0.0009 -0.0014 -0.0148 1187 LEU B C   
17369 O O   . LEU B 1189 ? 0.3405 0.4021 0.4103 0.0020  -0.0013 -0.0161 1187 LEU B O   
17370 C CB  . LEU B 1189 ? 0.3319 0.4100 0.4105 0.0021  0.0007  -0.0182 1187 LEU B CB  
17371 C CG  . LEU B 1189 ? 0.4130 0.5006 0.4947 0.0015  0.0033  -0.0173 1187 LEU B CG  
17372 C CD1 . LEU B 1189 ? 0.3862 0.4779 0.4687 0.0051  0.0039  -0.0203 1187 LEU B CD1 
17373 C CD2 . LEU B 1189 ? 0.3666 0.4537 0.4448 0.0011  0.0054  -0.0153 1187 LEU B CD2 
17374 N N   . LEU B 1190 ? 0.3127 0.3770 0.3865 -0.0042 -0.0015 -0.0118 1188 LEU B N   
17375 C CA  . LEU B 1190 ? 0.2863 0.3432 0.3554 -0.0040 -0.0020 -0.0102 1188 LEU B CA  
17376 C C   . LEU B 1190 ? 0.3587 0.4185 0.4255 -0.0027 0.0006  -0.0092 1188 LEU B C   
17377 O O   . LEU B 1190 ? 0.2794 0.3465 0.3482 -0.0039 0.0027  -0.0080 1188 LEU B O   
17378 C CB  . LEU B 1190 ? 0.2998 0.3529 0.3691 -0.0081 -0.0036 -0.0072 1188 LEU B CB  
17379 C CG  . LEU B 1190 ? 0.2714 0.3197 0.3420 -0.0100 -0.0068 -0.0080 1188 LEU B CG  
17380 C CD1 . LEU B 1190 ? 0.3036 0.3454 0.3726 -0.0139 -0.0088 -0.0049 1188 LEU B CD1 
17381 C CD2 . LEU B 1190 ? 0.3149 0.3566 0.3823 -0.0063 -0.0085 -0.0111 1188 LEU B CD2 
17382 N N   . LEU B 1191 ? 0.2815 0.3359 0.3439 0.0000  0.0003  -0.0096 1189 LEU B N   
17383 C CA  . LEU B 1191 ? 0.2727 0.3286 0.3325 0.0011  0.0021  -0.0083 1189 LEU B CA  
17384 C C   . LEU B 1191 ? 0.2783 0.3308 0.3364 -0.0014 0.0017  -0.0047 1189 LEU B C   
17385 O O   . LEU B 1191 ? 0.3209 0.3656 0.3765 -0.0012 -0.0004 -0.0041 1189 LEU B O   
17386 C CB  . LEU B 1191 ? 0.2800 0.3323 0.3363 0.0048  0.0017  -0.0100 1189 LEU B CB  
17387 C CG  . LEU B 1191 ? 0.3502 0.4051 0.4040 0.0067  0.0034  -0.0098 1189 LEU B CG  
17388 C CD1 . LEU B 1191 ? 0.3267 0.3791 0.3783 0.0098  0.0027  -0.0118 1189 LEU B CD1 
17389 C CD2 . LEU B 1191 ? 0.2891 0.3420 0.3405 0.0058  0.0036  -0.0067 1189 LEU B CD2 
17390 N N   . VAL B 1192 ? 0.2845 0.3427 0.3437 -0.0037 0.0036  -0.0025 1190 VAL B N   
17391 C CA  . VAL B 1192 ? 0.2940 0.3499 0.3521 -0.0070 0.0032  0.0014  1190 VAL B CA  
17392 C C   . VAL B 1192 ? 0.3192 0.3740 0.3731 -0.0055 0.0042  0.0031  1190 VAL B C   
17393 O O   . VAL B 1192 ? 0.3093 0.3700 0.3628 -0.0040 0.0063  0.0023  1190 VAL B O   
17394 C CB  . VAL B 1192 ? 0.2933 0.3569 0.3553 -0.0109 0.0047  0.0033  1190 VAL B CB  
17395 C CG1 . VAL B 1192 ? 0.2680 0.3288 0.3287 -0.0150 0.0040  0.0077  1190 VAL B CG1 
17396 C CG2 . VAL B 1192 ? 0.2840 0.3499 0.3507 -0.0122 0.0036  0.0014  1190 VAL B CG2 
17397 N N   . GLN B 1193 ? 0.2748 0.3218 0.3254 -0.0058 0.0023  0.0053  1191 GLN B N   
17398 C CA  . GLN B 1193 ? 0.2542 0.3001 0.3010 -0.0047 0.0029  0.0075  1191 GLN B CA  
17399 C C   . GLN B 1193 ? 0.2738 0.3170 0.3193 -0.0087 0.0022  0.0118  1191 GLN B C   
17400 O O   . GLN B 1193 ? 0.2717 0.3082 0.3171 -0.0108 -0.0002 0.0129  1191 GLN B O   
17401 C CB  . GLN B 1193 ? 0.2742 0.3130 0.3175 -0.0007 0.0011  0.0064  1191 GLN B CB  
17402 C CG  . GLN B 1193 ? 0.2838 0.3251 0.3277 0.0030  0.0017  0.0027  1191 GLN B CG  
17403 C CD  . GLN B 1193 ? 0.3080 0.3446 0.3485 0.0068  0.0006  0.0024  1191 GLN B CD  
17404 O OE1 . GLN B 1193 ? 0.3162 0.3540 0.3544 0.0079  0.0011  0.0040  1191 GLN B OE1 
17405 N NE2 . GLN B 1193 ? 0.2611 0.2926 0.3012 0.0090  -0.0011 0.0003  1191 GLN B NE2 
17406 N N   . ALA B 1194 ? 0.2590 0.3069 0.3031 -0.0099 0.0041  0.0143  1192 ALA B N   
17407 C CA  . ALA B 1194 ? 0.2750 0.3216 0.3179 -0.0143 0.0038  0.0188  1192 ALA B CA  
17408 C C   . ALA B 1194 ? 0.2796 0.3239 0.3177 -0.0131 0.0038  0.0215  1192 ALA B C   
17409 O O   . ALA B 1194 ? 0.2857 0.3340 0.3225 -0.0100 0.0053  0.0200  1192 ALA B O   
17410 C CB  . ALA B 1194 ? 0.2863 0.3431 0.3329 -0.0180 0.0064  0.0200  1192 ALA B CB  
17411 N N   . ALA B 1195 ? 0.2377 0.2750 0.2729 -0.0158 0.0018  0.0254  1193 ALA B N   
17412 C CA  . ALA B 1195 ? 0.2627 0.2975 0.2932 -0.0151 0.0015  0.0285  1193 ALA B CA  
17413 C C   . ALA B 1195 ? 0.3168 0.3479 0.3455 -0.0204 0.0003  0.0337  1193 ALA B C   
17414 O O   . ALA B 1195 ? 0.2575 0.2843 0.2878 -0.0238 -0.0014 0.0345  1193 ALA B O   
17415 C CB  . ALA B 1195 ? 0.3026 0.3289 0.3298 -0.0102 -0.0010 0.0273  1193 ALA B CB  
17416 N N   . SER B 1196 ? 0.3006 0.3332 0.3257 -0.0214 0.0011  0.0372  1194 SER B N   
17417 C CA  . SER B 1196 ? 0.3291 0.3568 0.3514 -0.0264 -0.0003 0.0426  1194 SER B CA  
17418 C C   . SER B 1196 ? 0.3417 0.3553 0.3594 -0.0245 -0.0046 0.0440  1194 SER B C   
17419 O O   . SER B 1196 ? 0.3531 0.3627 0.3693 -0.0189 -0.0058 0.0412  1194 SER B O   
17420 C CB  . SER B 1196 ? 0.3049 0.3394 0.3245 -0.0283 0.0021  0.0461  1194 SER B CB  
17421 O OG  . SER B 1196 ? 0.3394 0.3712 0.3549 -0.0238 0.0014  0.0459  1194 SER B OG  
17422 N N   . SER B 1197 ? 0.3187 0.3249 0.3341 -0.0293 -0.0070 0.0484  1195 SER B N   
17423 C CA  . SER B 1197 ? 0.3879 0.3798 0.3979 -0.0274 -0.0113 0.0501  1195 SER B CA  
17424 C C   . SER B 1197 ? 0.4054 0.3969 0.4111 -0.0229 -0.0112 0.0510  1195 SER B C   
17425 O O   . SER B 1197 ? 0.4191 0.4025 0.4220 -0.0176 -0.0138 0.0495  1195 SER B O   
17426 C CB  . SER B 1197 ? 0.4181 0.4024 0.4254 -0.0340 -0.0139 0.0556  1195 SER B CB  
17427 O OG  . SER B 1197 ? 0.4282 0.4129 0.4397 -0.0385 -0.0144 0.0549  1195 SER B OG  
17428 N N   . GLY B 1198 ? 0.4219 0.4227 0.4271 -0.0246 -0.0083 0.0532  1196 GLY B N   
17429 C CA  . GLY B 1198 ? 0.4261 0.4274 0.4273 -0.0207 -0.0083 0.0541  1196 GLY B CA  
17430 C C   . GLY B 1198 ? 0.4301 0.4357 0.4333 -0.0143 -0.0072 0.0489  1196 GLY B C   
17431 O O   . GLY B 1198 ? 0.4233 0.4249 0.4235 -0.0095 -0.0089 0.0487  1196 GLY B O   
17432 N N   . GLU B 1199 ? 0.4052 0.4191 0.4135 -0.0140 -0.0045 0.0448  1197 GLU B N   
17433 C CA  . GLU B 1199 ? 0.3620 0.3799 0.3723 -0.0085 -0.0037 0.0401  1197 GLU B CA  
17434 C C   . GLU B 1199 ? 0.4416 0.4501 0.4514 -0.0042 -0.0067 0.0378  1197 GLU B C   
17435 O O   . GLU B 1199 ? 0.4025 0.4111 0.4116 0.0010  -0.0073 0.0358  1197 GLU B O   
17436 C CB  . GLU B 1199 ? 0.4051 0.4328 0.4206 -0.0094 -0.0005 0.0364  1197 GLU B CB  
17437 N N   . ILE B 1200 ? 0.3595 0.3602 0.3698 -0.0063 -0.0088 0.0380  1198 ILE B N   
17438 C CA  . ILE B 1200 ? 0.3647 0.3561 0.3740 -0.0021 -0.0117 0.0356  1198 ILE B CA  
17439 C C   . ILE B 1200 ? 0.4157 0.3990 0.4197 0.0016  -0.0146 0.0379  1198 ILE B C   
17440 O O   . ILE B 1200 ? 0.3491 0.3293 0.3523 0.0075  -0.0159 0.0352  1198 ILE B O   
17441 C CB  . ILE B 1200 ? 0.3713 0.3553 0.3814 -0.0057 -0.0137 0.0357  1198 ILE B CB  
17442 C CG1 . ILE B 1200 ? 0.3541 0.3469 0.3700 -0.0081 -0.0111 0.0328  1198 ILE B CG1 
17443 C CG2 . ILE B 1200 ? 0.3797 0.3522 0.3872 -0.0012 -0.0173 0.0336  1198 ILE B CG2 
17444 C CD1 . ILE B 1200 ? 0.3272 0.3144 0.3445 -0.0122 -0.0130 0.0329  1198 ILE B CD1 
17445 N N   . ALA B 1201 ? 0.4429 0.4231 0.4432 -0.0015 -0.0155 0.0428  1199 ALA B N   
17446 C CA  . ALA B 1201 ? 0.4427 0.4146 0.4376 0.0019  -0.0186 0.0454  1199 ALA B CA  
17447 C C   . ALA B 1201 ? 0.4821 0.4615 0.4766 0.0063  -0.0172 0.0448  1199 ALA B C   
17448 O O   . ALA B 1201 ? 0.5071 0.4816 0.4990 0.0116  -0.0196 0.0447  1199 ALA B O   
17449 C CB  . ALA B 1201 ? 0.4480 0.4136 0.4387 -0.0035 -0.0203 0.0512  1199 ALA B CB  
17450 N N   . ARG B 1202 ? 0.4473 0.4385 0.4443 0.0042  -0.0137 0.0445  1200 ARG B N   
17451 C CA  . ARG B 1202 ? 0.4498 0.4483 0.4460 0.0074  -0.0126 0.0444  1200 ARG B CA  
17452 C C   . ARG B 1202 ? 0.4857 0.4909 0.4858 0.0118  -0.0112 0.0394  1200 ARG B C   
17453 O O   . ARG B 1202 ? 0.5275 0.5351 0.5267 0.0162  -0.0119 0.0389  1200 ARG B O   
17454 C CB  . ARG B 1202 ? 0.4798 0.4870 0.4756 0.0029  -0.0098 0.0467  1200 ARG B CB  
17455 C CG  . ARG B 1202 ? 0.5703 0.5727 0.5618 -0.0019 -0.0108 0.0523  1200 ARG B CG  
17456 C CD  . ARG B 1202 ? 0.6045 0.6171 0.5956 -0.0056 -0.0075 0.0541  1200 ARG B CD  
17457 N NE  . ARG B 1202 ? 0.5425 0.5645 0.5386 -0.0072 -0.0040 0.0504  1200 ARG B NE  
17458 C CZ  . ARG B 1202 ? 0.5701 0.5955 0.5683 -0.0123 -0.0020 0.0513  1200 ARG B CZ  
17459 N NH1 . ARG B 1202 ? 0.5545 0.5752 0.5502 -0.0170 -0.0030 0.0561  1200 ARG B NH1 
17460 N NH2 . ARG B 1202 ? 0.5952 0.6290 0.5980 -0.0127 0.0009  0.0475  1200 ARG B NH2 
17461 N N   . ASN B 1203 ? 0.4122 0.4207 0.4165 0.0107  -0.0094 0.0359  1201 ASN B N   
17462 C CA  . ASN B 1203 ? 0.4446 0.4609 0.4525 0.0136  -0.0076 0.0316  1201 ASN B CA  
17463 C C   . ASN B 1203 ? 0.4325 0.4438 0.4422 0.0169  -0.0089 0.0282  1201 ASN B C   
17464 O O   . ASN B 1203 ? 0.4460 0.4545 0.4575 0.0145  -0.0087 0.0270  1201 ASN B O   
17465 C CB  . ASN B 1203 ? 0.4305 0.4557 0.4416 0.0099  -0.0043 0.0301  1201 ASN B CB  
17466 C CG  . ASN B 1203 ? 0.4881 0.5204 0.5025 0.0124  -0.0027 0.0257  1201 ASN B CG  
17467 O OD1 . ASN B 1203 ? 0.4734 0.5054 0.4881 0.0168  -0.0037 0.0240  1201 ASN B OD1 
17468 N ND2 . ASN B 1203 ? 0.4929 0.5320 0.5098 0.0098  -0.0001 0.0240  1201 ASN B ND2 
17469 N N   . PRO B 1204 ? 0.4706 0.4815 0.4800 0.0224  -0.0101 0.0267  1202 PRO B N   
17470 C CA  . PRO B 1204 ? 0.4024 0.4092 0.4130 0.0258  -0.0111 0.0233  1202 PRO B CA  
17471 C C   . PRO B 1204 ? 0.4522 0.4647 0.4671 0.0244  -0.0088 0.0196  1202 PRO B C   
17472 O O   . PRO B 1204 ? 0.4438 0.4520 0.4595 0.0256  -0.0096 0.0172  1202 PRO B O   
17473 C CB  . PRO B 1204 ? 0.4906 0.4994 0.5005 0.0319  -0.0121 0.0226  1202 PRO B CB  
17474 C CG  . PRO B 1204 ? 0.4862 0.5037 0.4963 0.0309  -0.0107 0.0243  1202 PRO B CG  
17475 C CD  . PRO B 1204 ? 0.4547 0.4702 0.4628 0.0256  -0.0104 0.0277  1202 PRO B CD  
17476 N N   . ASP B 1205 ? 0.4564 0.4780 0.4735 0.0219  -0.0062 0.0191  1203 ASP B N   
17477 C CA  . ASP B 1205 ? 0.4365 0.4633 0.4573 0.0206  -0.0043 0.0158  1203 ASP B CA  
17478 C C   . ASP B 1205 ? 0.4320 0.4603 0.4542 0.0153  -0.0028 0.0166  1203 ASP B C   
17479 O O   . ASP B 1205 ? 0.4320 0.4671 0.4567 0.0137  -0.0007 0.0148  1203 ASP B O   
17480 C CB  . ASP B 1205 ? 0.4860 0.5218 0.5083 0.0221  -0.0027 0.0141  1203 ASP B CB  
17481 C CG  . ASP B 1205 ? 0.4786 0.5147 0.5007 0.0272  -0.0038 0.0129  1203 ASP B CG  
17482 O OD1 . ASP B 1205 ? 0.5278 0.5592 0.5501 0.0297  -0.0049 0.0112  1203 ASP B OD1 
17483 O OD2 . ASP B 1205 ? 0.5990 0.6403 0.6206 0.0286  -0.0037 0.0138  1203 ASP B OD2 
17484 N N   . ALA B 1206 ? 0.3736 0.3955 0.3940 0.0127  -0.0041 0.0194  1204 ALA B N   
17485 C CA  . ALA B 1206 ? 0.3656 0.3894 0.3878 0.0075  -0.0028 0.0204  1204 ALA B CA  
17486 C C   . ALA B 1206 ? 0.3335 0.3593 0.3597 0.0070  -0.0020 0.0168  1204 ALA B C   
17487 O O   . ALA B 1206 ? 0.3112 0.3436 0.3401 0.0043  0.0001  0.0160  1204 ALA B O   
17488 C CB  . ALA B 1206 ? 0.3967 0.4122 0.4165 0.0045  -0.0049 0.0241  1204 ALA B CB  
17489 N N   . TYR B 1207 ? 0.3196 0.3397 0.3457 0.0099  -0.0038 0.0145  1205 TYR B N   
17490 C CA  . TYR B 1207 ? 0.2735 0.2950 0.3028 0.0101  -0.0033 0.0109  1205 TYR B CA  
17491 C C   . TYR B 1207 ? 0.3491 0.3735 0.3787 0.0146  -0.0029 0.0079  1205 TYR B C   
17492 O O   . TYR B 1207 ? 0.4016 0.4225 0.4289 0.0183  -0.0043 0.0080  1205 TYR B O   
17493 C CB  . TYR B 1207 ? 0.2862 0.2987 0.3149 0.0092  -0.0058 0.0106  1205 TYR B CB  
17494 C CG  . TYR B 1207 ? 0.3152 0.3251 0.3441 0.0039  -0.0065 0.0137  1205 TYR B CG  
17495 C CD1 . TYR B 1207 ? 0.2630 0.2804 0.2957 -0.0001 -0.0044 0.0140  1205 TYR B CD1 
17496 C CD2 . TYR B 1207 ? 0.3238 0.3241 0.3492 0.0030  -0.0092 0.0166  1205 TYR B CD2 
17497 C CE1 . TYR B 1207 ? 0.2790 0.2954 0.3122 -0.0053 -0.0048 0.0171  1205 TYR B CE1 
17498 C CE2 . TYR B 1207 ? 0.3453 0.3435 0.3708 -0.0025 -0.0099 0.0198  1205 TYR B CE2 
17499 C CZ  . TYR B 1207 ? 0.2744 0.2812 0.3040 -0.0068 -0.0076 0.0202  1205 TYR B CZ  
17500 O OH  . TYR B 1207 ? 0.2956 0.3015 0.3257 -0.0125 -0.0081 0.0237  1205 TYR B OH  
17501 N N   . CYS B 1208 ? 0.2871 0.3182 0.3196 0.0143  -0.0011 0.0054  1206 CYS B N   
17502 C CA  . CYS B 1208 ? 0.2899 0.3246 0.3227 0.0177  -0.0006 0.0029  1206 CYS B CA  
17503 C C   . CYS B 1208 ? 0.3217 0.3527 0.3552 0.0195  -0.0016 0.0001  1206 CYS B C   
17504 O O   . CYS B 1208 ? 0.2627 0.2930 0.2981 0.0175  -0.0016 -0.0012 1206 CYS B O   
17505 C CB  . CYS B 1208 ? 0.3551 0.3980 0.3899 0.0163  0.0016  0.0017  1206 CYS B CB  
17506 S SG  . CYS B 1208 ? 0.3746 0.4221 0.4097 0.0195  0.0020  -0.0008 1206 CYS B SG  
17507 N N   . LEU B 1209 ? 0.2875 0.3168 0.3193 0.0236  -0.0025 -0.0008 1207 LEU B N   
17508 C CA  . LEU B 1209 ? 0.2961 0.3219 0.3278 0.0258  -0.0034 -0.0034 1207 LEU B CA  
17509 C C   . LEU B 1209 ? 0.2762 0.3079 0.3102 0.0257  -0.0020 -0.0060 1207 LEU B C   
17510 O O   . LEU B 1209 ? 0.2791 0.3084 0.3130 0.0268  -0.0027 -0.0082 1207 LEU B O   
17511 C CB  . LEU B 1209 ? 0.2248 0.2473 0.2538 0.0306  -0.0046 -0.0036 1207 LEU B CB  
17512 C CG  . LEU B 1209 ? 0.2849 0.3004 0.3109 0.0316  -0.0065 -0.0012 1207 LEU B CG  
17513 C CD1 . LEU B 1209 ? 0.2832 0.2957 0.3067 0.0373  -0.0078 -0.0021 1207 LEU B CD1 
17514 C CD2 . LEU B 1209 ? 0.2449 0.2524 0.2702 0.0284  -0.0081 -0.0005 1207 LEU B CD2 
17515 N N   . ASN B 1210 ? 0.2405 0.2792 0.2757 0.0245  -0.0004 -0.0057 1208 ASN B N   
17516 C CA  . ASN B 1210 ? 0.2724 0.3157 0.3094 0.0240  0.0006  -0.0080 1208 ASN B CA  
17517 C C   . ASN B 1210 ? 0.2811 0.3223 0.3198 0.0219  0.0003  -0.0096 1208 ASN B C   
17518 O O   . ASN B 1210 ? 0.2472 0.2891 0.2865 0.0225  0.0002  -0.0117 1208 ASN B O   
17519 C CB  . ASN B 1210 ? 0.3259 0.3756 0.3636 0.0224  0.0020  -0.0074 1208 ASN B CB  
17520 C CG  . ASN B 1210 ? 0.3416 0.3946 0.3779 0.0242  0.0021  -0.0060 1208 ASN B CG  
17521 O OD1 . ASN B 1210 ? 0.3896 0.4403 0.4246 0.0268  0.0012  -0.0050 1208 ASN B OD1 
17522 N ND2 . ASN B 1210 ? 0.4055 0.4639 0.4420 0.0230  0.0029  -0.0059 1208 ASN B ND2 
17523 N N   . TRP B 1211 ? 0.2189 0.2581 0.2585 0.0192  0.0001  -0.0083 1209 TRP B N   
17524 C CA  . TRP B 1211 ? 0.2241 0.2630 0.2660 0.0168  0.0000  -0.0094 1209 TRP B CA  
17525 C C   . TRP B 1211 ? 0.2656 0.2976 0.3070 0.0168  -0.0020 -0.0101 1209 TRP B C   
17526 O O   . TRP B 1211 ? 0.2947 0.3264 0.3383 0.0147  -0.0025 -0.0110 1209 TRP B O   
17527 C CB  . TRP B 1211 ? 0.2384 0.2804 0.2820 0.0135  0.0011  -0.0076 1209 TRP B CB  
17528 C CG  . TRP B 1211 ? 0.2852 0.3326 0.3281 0.0137  0.0027  -0.0066 1209 TRP B CG  
17529 C CD1 . TRP B 1211 ? 0.3173 0.3659 0.3591 0.0125  0.0033  -0.0040 1209 TRP B CD1 
17530 C CD2 . TRP B 1211 ? 0.2979 0.3498 0.3407 0.0150  0.0036  -0.0083 1209 TRP B CD2 
17531 N NE1 . TRP B 1211 ? 0.3150 0.3686 0.3559 0.0132  0.0046  -0.0041 1209 TRP B NE1 
17532 C CE2 . TRP B 1211 ? 0.3596 0.4152 0.4011 0.0146  0.0047  -0.0067 1209 TRP B CE2 
17533 C CE3 . TRP B 1211 ? 0.3212 0.3741 0.3645 0.0162  0.0034  -0.0108 1209 TRP B CE3 
17534 C CZ2 . TRP B 1211 ? 0.3396 0.3994 0.3803 0.0153  0.0054  -0.0077 1209 TRP B CZ2 
17535 C CZ3 . TRP B 1211 ? 0.2945 0.3515 0.3371 0.0168  0.0041  -0.0115 1209 TRP B CZ3 
17536 C CH2 . TRP B 1211 ? 0.3210 0.3812 0.3623 0.0163  0.0050  -0.0101 1209 TRP B CH2 
17537 N N   . LEU B 1212 ? 0.2452 0.2717 0.2837 0.0194  -0.0033 -0.0097 1210 LEU B N   
17538 C CA  . LEU B 1212 ? 0.2091 0.2278 0.2460 0.0198  -0.0056 -0.0105 1210 LEU B CA  
17539 C C   . LEU B 1212 ? 0.2420 0.2592 0.2773 0.0232  -0.0061 -0.0133 1210 LEU B C   
17540 O O   . LEU B 1212 ? 0.2639 0.2741 0.2968 0.0245  -0.0081 -0.0144 1210 LEU B O   
17541 C CB  . LEU B 1212 ? 0.1955 0.2077 0.2296 0.0204  -0.0070 -0.0083 1210 LEU B CB  
17542 C CG  . LEU B 1212 ? 0.1905 0.2030 0.2258 0.0161  -0.0069 -0.0053 1210 LEU B CG  
17543 C CD1 . LEU B 1212 ? 0.2443 0.2509 0.2763 0.0170  -0.0082 -0.0027 1210 LEU B CD1 
17544 C CD2 . LEU B 1212 ? 0.2493 0.2596 0.2868 0.0122  -0.0080 -0.0055 1210 LEU B CD2 
17545 N N   . VAL B 1213 ? 0.2256 0.2490 0.2617 0.0246  -0.0046 -0.0145 1211 VAL B N   
17546 C CA  . VAL B 1213 ? 0.2518 0.2750 0.2865 0.0273  -0.0048 -0.0169 1211 VAL B CA  
17547 C C   . VAL B 1213 ? 0.2706 0.2981 0.3077 0.0253  -0.0041 -0.0183 1211 VAL B C   
17548 O O   . VAL B 1213 ? 0.2699 0.3015 0.3095 0.0228  -0.0031 -0.0175 1211 VAL B O   
17549 C CB  . VAL B 1213 ? 0.2459 0.2727 0.2790 0.0308  -0.0038 -0.0167 1211 VAL B CB  
17550 C CG1 . VAL B 1213 ? 0.1987 0.2204 0.2290 0.0338  -0.0049 -0.0158 1211 VAL B CG1 
17551 C CG2 . VAL B 1213 ? 0.2180 0.2520 0.2530 0.0295  -0.0020 -0.0151 1211 VAL B CG2 
17552 N N   . GLU B 1214 ? 0.2671 0.2934 0.3029 0.0268  -0.0047 -0.0204 1212 GLU B N   
17553 C CA  . GLU B 1214 ? 0.2927 0.3222 0.3302 0.0253  -0.0044 -0.0218 1212 GLU B CA  
17554 C C   . GLU B 1214 ? 0.2368 0.2705 0.2729 0.0272  -0.0034 -0.0224 1212 GLU B C   
17555 O O   . GLU B 1214 ? 0.2376 0.2702 0.2712 0.0300  -0.0035 -0.0230 1212 GLU B O   
17556 C CB  . GLU B 1214 ? 0.3133 0.3382 0.3505 0.0248  -0.0063 -0.0236 1212 GLU B CB  
17557 C CG  . GLU B 1214 ? 0.3909 0.4188 0.4293 0.0238  -0.0063 -0.0250 1212 GLU B CG  
17558 C CD  . GLU B 1214 ? 0.5541 0.5780 0.5927 0.0229  -0.0084 -0.0266 1212 GLU B CD  
17559 O OE1 . GLU B 1214 ? 0.5815 0.6012 0.6205 0.0217  -0.0098 -0.0263 1212 GLU B OE1 
17560 O OE2 . GLU B 1214 ? 0.6170 0.6420 0.6552 0.0231  -0.0088 -0.0280 1212 GLU B OE2 
17561 N N   . GLU B 1215 ? 0.2375 0.2761 0.2753 0.0256  -0.0024 -0.0222 1213 GLU B N   
17562 C CA  . GLU B 1215 ? 0.2015 0.2440 0.2381 0.0264  -0.0017 -0.0225 1213 GLU B CA  
17563 C C   . GLU B 1215 ? 0.2261 0.2670 0.2618 0.0263  -0.0027 -0.0242 1213 GLU B C   
17564 O O   . GLU B 1215 ? 0.2335 0.2727 0.2707 0.0247  -0.0036 -0.0251 1213 GLU B O   
17565 C CB  . GLU B 1215 ? 0.2443 0.2914 0.2824 0.0245  -0.0008 -0.0216 1213 GLU B CB  
17566 C CG  . GLU B 1215 ? 0.2446 0.2937 0.2834 0.0243  0.0001  -0.0198 1213 GLU B CG  
17567 C CD  . GLU B 1215 ? 0.2362 0.2888 0.2762 0.0222  0.0007  -0.0195 1213 GLU B CD  
17568 O OE1 . GLU B 1215 ? 0.2584 0.3104 0.3000 0.0208  0.0007  -0.0198 1213 GLU B OE1 
17569 O OE2 . GLU B 1215 ? 0.2516 0.3076 0.2906 0.0221  0.0011  -0.0189 1213 GLU B OE2 
17570 N N   . VAL B 1216 ? 0.2201 0.2620 0.2533 0.0281  -0.0025 -0.0247 1214 VAL B N   
17571 C CA  . VAL B 1216 ? 0.2165 0.2575 0.2481 0.0280  -0.0033 -0.0260 1214 VAL B CA  
17572 C C   . VAL B 1216 ? 0.2356 0.2815 0.2661 0.0277  -0.0024 -0.0252 1214 VAL B C   
17573 O O   . VAL B 1216 ? 0.2379 0.2875 0.2677 0.0291  -0.0012 -0.0241 1214 VAL B O   
17574 C CB  . VAL B 1216 ? 0.2304 0.2671 0.2592 0.0303  -0.0042 -0.0274 1214 VAL B CB  
17575 C CG1 . VAL B 1216 ? 0.2642 0.3003 0.2908 0.0301  -0.0050 -0.0287 1214 VAL B CG1 
17576 C CG2 . VAL B 1216 ? 0.2594 0.2908 0.2893 0.0299  -0.0055 -0.0280 1214 VAL B CG2 
17577 N N   . SER B 1217 ? 0.1997 0.2458 0.2301 0.0257  -0.0031 -0.0255 1215 SER B N   
17578 C CA  . SER B 1217 ? 0.1748 0.2246 0.2037 0.0248  -0.0027 -0.0246 1215 SER B CA  
17579 C C   . SER B 1217 ? 0.2119 0.2599 0.2380 0.0251  -0.0036 -0.0255 1215 SER B C   
17580 O O   . SER B 1217 ? 0.2372 0.2809 0.2632 0.0249  -0.0050 -0.0269 1215 SER B O   
17581 C CB  . SER B 1217 ? 0.2165 0.2670 0.2467 0.0222  -0.0032 -0.0242 1215 SER B CB  
17582 O OG  . SER B 1217 ? 0.2324 0.2841 0.2604 0.0207  -0.0037 -0.0236 1215 SER B OG  
17583 N N   . ALA B 1218 ? 0.2329 0.2846 0.2567 0.0257  -0.0027 -0.0246 1216 ALA B N   
17584 C CA  . ALA B 1218 ? 0.2186 0.2694 0.2390 0.0259  -0.0033 -0.0252 1216 ALA B CA  
17585 C C   . ALA B 1218 ? 0.2539 0.3092 0.2729 0.0238  -0.0029 -0.0233 1216 ALA B C   
17586 O O   . ALA B 1218 ? 0.2468 0.3079 0.2662 0.0239  -0.0014 -0.0217 1216 ALA B O   
17587 C CB  . ALA B 1218 ? 0.2115 0.2620 0.2296 0.0293  -0.0026 -0.0262 1216 ALA B CB  
17588 N N   . SER B 1219 ? 0.2282 0.2809 0.2453 0.0218  -0.0044 -0.0233 1217 SER B N   
17589 C CA  . SER B 1219 ? 0.2152 0.2710 0.2304 0.0190  -0.0046 -0.0212 1217 SER B CA  
17590 C C   . SER B 1219 ? 0.2181 0.2734 0.2292 0.0192  -0.0050 -0.0212 1217 SER B C   
17591 O O   . SER B 1219 ? 0.2443 0.2942 0.2540 0.0194  -0.0067 -0.0226 1217 SER B O   
17592 C CB  . SER B 1219 ? 0.2357 0.2881 0.2516 0.0162  -0.0064 -0.0210 1217 SER B CB  
17593 O OG  . SER B 1219 ? 0.2592 0.3136 0.2727 0.0132  -0.0069 -0.0188 1217 SER B OG  
17594 N N   . ILE B 1220 ? 0.2518 0.3133 0.2611 0.0193  -0.0034 -0.0196 1218 ILE B N   
17595 C CA  . ILE B 1220 ? 0.2440 0.3063 0.2490 0.0197  -0.0032 -0.0194 1218 ILE B CA  
17596 C C   . ILE B 1220 ? 0.2430 0.3086 0.2459 0.0158  -0.0035 -0.0165 1218 ILE B C   
17597 O O   . ILE B 1220 ? 0.2287 0.3009 0.2329 0.0142  -0.0022 -0.0143 1218 ILE B O   
17598 C CB  . ILE B 1220 ? 0.2748 0.3421 0.2789 0.0235  -0.0009 -0.0200 1218 ILE B CB  
17599 C CG1 . ILE B 1220 ? 0.3360 0.3988 0.3418 0.0272  -0.0010 -0.0227 1218 ILE B CG1 
17600 C CG2 . ILE B 1220 ? 0.2934 0.3613 0.2924 0.0242  -0.0007 -0.0200 1218 ILE B CG2 
17601 C CD1 . ILE B 1220 ? 0.3826 0.4485 0.3924 0.0283  0.0002  -0.0224 1218 ILE B CD1 
17602 N N   . ASN B 1221 ? 0.1996 0.2605 0.1991 0.0139  -0.0055 -0.0163 1219 ASN B N   
17603 C CA  . ASN B 1221 ? 0.2549 0.3179 0.2512 0.0100  -0.0062 -0.0133 1219 ASN B CA  
17604 C C   . ASN B 1221 ? 0.2620 0.3324 0.2554 0.0108  -0.0039 -0.0120 1219 ASN B C   
17605 O O   . ASN B 1221 ? 0.2815 0.3499 0.2713 0.0127  -0.0040 -0.0132 1219 ASN B O   
17606 C CB  . ASN B 1221 ? 0.2486 0.3034 0.2418 0.0083  -0.0092 -0.0136 1219 ASN B CB  
17607 C CG  . ASN B 1221 ? 0.2838 0.3391 0.2730 0.0038  -0.0104 -0.0103 1219 ASN B CG  
17608 O OD1 . ASN B 1221 ? 0.2859 0.3482 0.2752 0.0013  -0.0090 -0.0076 1219 ASN B OD1 
17609 N ND2 . ASN B 1221 ? 0.2365 0.2846 0.2222 0.0025  -0.0133 -0.0103 1219 ASN B ND2 
17610 N N   . THR B 1222 ? 0.2160 0.2952 0.2108 0.0095  -0.0019 -0.0096 1220 THR B N   
17611 C CA  . THR B 1222 ? 0.2469 0.3350 0.2394 0.0104  0.0006  -0.0082 1220 THR B CA  
17612 C C   . THR B 1222 ? 0.3318 0.4226 0.3206 0.0055  0.0000  -0.0046 1220 THR B C   
17613 O O   . THR B 1222 ? 0.3516 0.4513 0.3386 0.0054  0.0022  -0.0027 1220 THR B O   
17614 C CB  . THR B 1222 ? 0.3027 0.4003 0.2992 0.0122  0.0033  -0.0075 1220 THR B CB  
17615 O OG1 . THR B 1222 ? 0.2990 0.3991 0.2985 0.0080  0.0025  -0.0050 1220 THR B OG1 
17616 C CG2 . THR B 1222 ? 0.3190 0.4136 0.3183 0.0175  0.0039  -0.0109 1220 THR B CG2 
17617 N N   . ALA B 1223 ? 0.2927 0.3759 0.2799 0.0015  -0.0031 -0.0035 1221 ALA B N   
17618 C CA  . ALA B 1223 ? 0.3624 0.4462 0.3454 -0.0037 -0.0043 0.0000  1221 ALA B CA  
17619 C C   . ALA B 1223 ? 0.4120 0.4889 0.3896 -0.0031 -0.0060 -0.0008 1221 ALA B C   
17620 O O   . ALA B 1223 ? 0.5311 0.6091 0.5070 0.0010  -0.0046 -0.0028 1221 ALA B O   
17621 C CB  . ALA B 1223 ? 0.3218 0.4010 0.3057 -0.0085 -0.0071 0.0019  1221 ALA B CB  
# 
